data_7HFE
# 
_entry.id   7HFE 
# 
_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   7HFE         pdb_00007hfe 10.2210/pdb7hfe/pdb 
WWPDB D_1001407404 ?            ?                   
# 
_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                        7HFE 
_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 '2-[(1S,2R,5R)-3-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-3-azabicyclo[3.2.0]heptan-2-yl]propan-2-ol' 272.346   1   ? ? 
? ?                                                                                    
3 water       nat water                                                                                          18.015    418 ? ? 
? ?                                                                                    
# 
_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 '2-[(1S,2R,5R)-3-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-3-azabicyclo[3.2.0]heptan-2-yl]propan-2-ol' A1BA5 
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 
A1BA5 non-polymer         . '2-[(1S,2R,5R)-3-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-3-azabicyclo[3.2.0]heptan-2-yl]propan-2-ol' ? 
'C15 H20 N4 O'   272.346 
ALA   'L-peptide linking' y ALANINE                                                                                        ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                       ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                     ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                       ? 
'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                      ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                        ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                      ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                          ? 
'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                     ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                        ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                         ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                     ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                  ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                        ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                         ? 
'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                      ? 
'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                                                       ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                         ? 
'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1BA5 1   201 201  A1BA5 LA1 A . 
D 3 HOH   1   301 625  HOH   HOH A . 
D 3 HOH   2   302 109  HOH   HOH A . 
D 3 HOH   3   303 493  HOH   HOH A . 
D 3 HOH   4   304 105  HOH   HOH A . 
D 3 HOH   5   305 153  HOH   HOH A . 
D 3 HOH   6   306 292  HOH   HOH A . 
D 3 HOH   7   307 196  HOH   HOH A . 
D 3 HOH   8   308 662  HOH   HOH A . 
D 3 HOH   9   309 964  HOH   HOH A . 
D 3 HOH   10  310 2    HOH   HOH A . 
D 3 HOH   11  311 76   HOH   HOH A . 
D 3 HOH   12  312 1283 HOH   HOH A . 
D 3 HOH   13  313 209  HOH   HOH A . 
D 3 HOH   14  314 57   HOH   HOH A . 
D 3 HOH   15  315 192  HOH   HOH A . 
D 3 HOH   16  316 247  HOH   HOH A . 
D 3 HOH   17  317 49   HOH   HOH A . 
D 3 HOH   18  318 409  HOH   HOH A . 
D 3 HOH   19  319 1295 HOH   HOH A . 
D 3 HOH   20  320 92   HOH   HOH A . 
D 3 HOH   21  321 354  HOH   HOH A . 
D 3 HOH   22  322 93   HOH   HOH A . 
D 3 HOH   23  323 236  HOH   HOH A . 
D 3 HOH   24  324 26   HOH   HOH A . 
D 3 HOH   25  325 4    HOH   HOH A . 
D 3 HOH   26  326 1309 HOH   HOH A . 
D 3 HOH   27  327 1279 HOH   HOH A . 
D 3 HOH   28  328 140  HOH   HOH A . 
D 3 HOH   29  329 151  HOH   HOH A . 
D 3 HOH   30  330 225  HOH   HOH A . 
D 3 HOH   31  331 124  HOH   HOH A . 
D 3 HOH   32  332 229  HOH   HOH A . 
D 3 HOH   33  333 21   HOH   HOH A . 
D 3 HOH   34  334 136  HOH   HOH A . 
D 3 HOH   35  335 70   HOH   HOH A . 
D 3 HOH   36  336 164  HOH   HOH A . 
D 3 HOH   37  337 148  HOH   HOH A . 
D 3 HOH   38  338 1301 HOH   HOH A . 
D 3 HOH   39  339 68   HOH   HOH A . 
D 3 HOH   40  340 15   HOH   HOH A . 
D 3 HOH   41  341 139  HOH   HOH A . 
D 3 HOH   42  342 17   HOH   HOH A . 
D 3 HOH   43  343 630  HOH   HOH A . 
D 3 HOH   44  344 241  HOH   HOH A . 
D 3 HOH   45  345 661  HOH   HOH A . 
D 3 HOH   46  346 397  HOH   HOH A . 
D 3 HOH   47  347 405  HOH   HOH A . 
D 3 HOH   48  348 39   HOH   HOH A . 
D 3 HOH   49  349 6    HOH   HOH A . 
D 3 HOH   50  350 337  HOH   HOH A . 
D 3 HOH   51  351 320  HOH   HOH A . 
D 3 HOH   52  352 1300 HOH   HOH A . 
D 3 HOH   53  353 66   HOH   HOH A . 
D 3 HOH   54  354 33   HOH   HOH A . 
D 3 HOH   55  355 12   HOH   HOH A . 
D 3 HOH   56  356 42   HOH   HOH A . 
D 3 HOH   57  357 4    HOH   HOH A . 
D 3 HOH   58  358 396  HOH   HOH A . 
D 3 HOH   59  359 393  HOH   HOH A . 
D 3 HOH   60  360 1    HOH   HOH A . 
D 3 HOH   61  361 162  HOH   HOH A . 
D 3 HOH   62  362 159  HOH   HOH A . 
D 3 HOH   63  363 1308 HOH   HOH A . 
D 3 HOH   64  364 102  HOH   HOH A . 
D 3 HOH   65  365 165  HOH   HOH A . 
D 3 HOH   66  366 18   HOH   HOH A . 
D 3 HOH   67  367 2    HOH   HOH A . 
D 3 HOH   68  368 469  HOH   HOH A . 
D 3 HOH   69  369 169  HOH   HOH A . 
D 3 HOH   70  370 45   HOH   HOH A . 
D 3 HOH   71  371 19   HOH   HOH A . 
D 3 HOH   72  372 36   HOH   HOH A . 
D 3 HOH   73  373 186  HOH   HOH A . 
D 3 HOH   74  374 366  HOH   HOH A . 
D 3 HOH   75  375 86   HOH   HOH A . 
D 3 HOH   76  376 461  HOH   HOH A . 
D 3 HOH   77  377 24   HOH   HOH A . 
D 3 HOH   78  378 5    HOH   HOH A . 
D 3 HOH   79  379 27   HOH   HOH A . 
D 3 HOH   80  380 351  HOH   HOH A . 
D 3 HOH   81  381 3    HOH   HOH A . 
D 3 HOH   82  382 138  HOH   HOH A . 
D 3 HOH   83  383 6    HOH   HOH A . 
D 3 HOH   84  384 46   HOH   HOH A . 
D 3 HOH   85  385 116  HOH   HOH A . 
D 3 HOH   86  386 56   HOH   HOH A . 
D 3 HOH   87  387 303  HOH   HOH A . 
D 3 HOH   88  388 154  HOH   HOH A . 
D 3 HOH   89  389 155  HOH   HOH A . 
D 3 HOH   90  390 1315 HOH   HOH A . 
D 3 HOH   91  391 96   HOH   HOH A . 
D 3 HOH   92  392 939  HOH   HOH A . 
D 3 HOH   93  393 218  HOH   HOH A . 
D 3 HOH   94  394 134  HOH   HOH A . 
D 3 HOH   95  395 81   HOH   HOH A . 
D 3 HOH   96  396 35   HOH   HOH A . 
D 3 HOH   97  397 1094 HOH   HOH A . 
D 3 HOH   98  398 8    HOH   HOH A . 
D 3 HOH   99  399 74   HOH   HOH A . 
D 3 HOH   100 400 212  HOH   HOH A . 
D 3 HOH   101 401 132  HOH   HOH A . 
D 3 HOH   102 402 122  HOH   HOH A . 
D 3 HOH   103 403 78   HOH   HOH A . 
D 3 HOH   104 404 381  HOH   HOH A . 
D 3 HOH   105 405 51   HOH   HOH A . 
D 3 HOH   106 406 1222 HOH   HOH A . 
D 3 HOH   107 407 34   HOH   HOH A . 
D 3 HOH   108 408 67   HOH   HOH A . 
D 3 HOH   109 409 3    HOH   HOH A . 
D 3 HOH   110 410 58   HOH   HOH A . 
D 3 HOH   111 411 1189 HOH   HOH A . 
D 3 HOH   112 412 1290 HOH   HOH A . 
D 3 HOH   113 413 296  HOH   HOH A . 
D 3 HOH   114 414 121  HOH   HOH A . 
D 3 HOH   115 415 278  HOH   HOH A . 
D 3 HOH   116 416 83   HOH   HOH A . 
D 3 HOH   117 417 1286 HOH   HOH A . 
D 3 HOH   118 418 156  HOH   HOH A . 
D 3 HOH   119 419 582  HOH   HOH A . 
D 3 HOH   120 420 1275 HOH   HOH A . 
D 3 HOH   121 421 123  HOH   HOH A . 
D 3 HOH   122 422 71   HOH   HOH A . 
D 3 HOH   123 423 95   HOH   HOH A . 
D 3 HOH   124 424 85   HOH   HOH A . 
D 3 HOH   125 425 40   HOH   HOH A . 
D 3 HOH   126 426 199  HOH   HOH A . 
D 3 HOH   127 427 53   HOH   HOH A . 
D 3 HOH   128 428 16   HOH   HOH A . 
D 3 HOH   129 429 25   HOH   HOH A . 
D 3 HOH   130 430 115  HOH   HOH A . 
D 3 HOH   131 431 952  HOH   HOH A . 
D 3 HOH   132 432 1289 HOH   HOH A . 
D 3 HOH   133 433 1068 HOH   HOH A . 
D 3 HOH   134 434 125  HOH   HOH A . 
D 3 HOH   135 435 1313 HOH   HOH A . 
D 3 HOH   136 436 11   HOH   HOH A . 
D 3 HOH   137 437 195  HOH   HOH A . 
D 3 HOH   138 438 1296 HOH   HOH A . 
D 3 HOH   139 439 5    HOH   HOH A . 
D 3 HOH   140 440 7    HOH   HOH A . 
D 3 HOH   141 441 1310 HOH   HOH A . 
D 3 HOH   142 442 281  HOH   HOH A . 
D 3 HOH   143 443 944  HOH   HOH A . 
D 3 HOH   144 444 9    HOH   HOH A . 
D 3 HOH   145 445 80   HOH   HOH A . 
D 3 HOH   146 446 94   HOH   HOH A . 
D 3 HOH   147 447 333  HOH   HOH A . 
D 3 HOH   148 448 1238 HOH   HOH A . 
D 3 HOH   149 449 97   HOH   HOH A . 
D 3 HOH   150 450 8    HOH   HOH A . 
D 3 HOH   151 451 1276 HOH   HOH A . 
D 3 HOH   152 452 330  HOH   HOH A . 
D 3 HOH   153 453 104  HOH   HOH A . 
D 3 HOH   154 454 7    HOH   HOH A . 
D 3 HOH   155 455 73   HOH   HOH A . 
D 3 HOH   156 456 188  HOH   HOH A . 
D 3 HOH   157 457 79   HOH   HOH A . 
D 3 HOH   158 458 576  HOH   HOH A . 
D 3 HOH   159 459 1119 HOH   HOH A . 
D 3 HOH   160 460 726  HOH   HOH A . 
D 3 HOH   161 461 1134 HOH   HOH A . 
D 3 HOH   162 462 107  HOH   HOH A . 
D 3 HOH   163 463 163  HOH   HOH A . 
D 3 HOH   164 464 509  HOH   HOH A . 
D 3 HOH   165 465 408  HOH   HOH A . 
D 3 HOH   166 466 280  HOH   HOH A . 
D 3 HOH   167 467 756  HOH   HOH A . 
D 3 HOH   168 468 361  HOH   HOH A . 
D 3 HOH   169 469 801  HOH   HOH A . 
D 3 HOH   170 470 556  HOH   HOH A . 
D 3 HOH   171 471 319  HOH   HOH A . 
D 3 HOH   172 472 342  HOH   HOH A . 
D 3 HOH   173 473 63   HOH   HOH A . 
D 3 HOH   174 474 126  HOH   HOH A . 
D 3 HOH   175 475 1307 HOH   HOH A . 
D 3 HOH   176 476 250  HOH   HOH A . 
D 3 HOH   177 477 135  HOH   HOH A . 
D 3 HOH   178 478 224  HOH   HOH A . 
D 3 HOH   179 479 370  HOH   HOH A . 
D 3 HOH   180 480 202  HOH   HOH A . 
D 3 HOH   181 481 1306 HOH   HOH A . 
D 3 HOH   182 482 1287 HOH   HOH A . 
D 3 HOH   183 483 695  HOH   HOH A . 
D 3 HOH   184 484 326  HOH   HOH A . 
D 3 HOH   185 485 674  HOH   HOH A . 
D 3 HOH   186 486 267  HOH   HOH A . 
D 3 HOH   187 487 309  HOH   HOH A . 
D 3 HOH   188 488 919  HOH   HOH A . 
D 3 HOH   189 489 711  HOH   HOH A . 
D 3 HOH   190 490 941  HOH   HOH A . 
D 3 HOH   191 491 318  HOH   HOH A . 
D 3 HOH   192 492 521  HOH   HOH A . 
D 3 HOH   193 493 1314 HOH   HOH A . 
D 3 HOH   194 494 805  HOH   HOH A . 
D 3 HOH   195 495 1299 HOH   HOH A . 
D 3 HOH   196 496 10   HOH   HOH A . 
D 3 HOH   197 497 315  HOH   HOH A . 
D 3 HOH   198 498 263  HOH   HOH A . 
D 3 HOH   199 499 152  HOH   HOH A . 
D 3 HOH   200 500 208  HOH   HOH A . 
D 3 HOH   201 501 331  HOH   HOH A . 
D 3 HOH   202 502 1071 HOH   HOH A . 
D 3 HOH   203 503 356  HOH   HOH A . 
D 3 HOH   204 504 363  HOH   HOH A . 
D 3 HOH   205 505 350  HOH   HOH A . 
D 3 HOH   206 506 180  HOH   HOH A . 
D 3 HOH   207 507 371  HOH   HOH A . 
D 3 HOH   208 508 313  HOH   HOH A . 
D 3 HOH   209 509 376  HOH   HOH A . 
D 3 HOH   210 510 1284 HOH   HOH A . 
D 3 HOH   211 511 429  HOH   HOH A . 
D 3 HOH   212 512 772  HOH   HOH A . 
D 3 HOH   213 513 346  HOH   HOH A . 
D 3 HOH   214 514 1074 HOH   HOH A . 
D 3 HOH   215 515 1292 HOH   HOH A . 
D 3 HOH   216 516 1078 HOH   HOH A . 
E 3 HOH   1   201 64   HOH   HOH B . 
E 3 HOH   2   202 358  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   206 723  HOH   HOH B . 
E 3 HOH   7   207 240  HOH   HOH B . 
E 3 HOH   8   208 364  HOH   HOH B . 
E 3 HOH   9   209 549  HOH   HOH B . 
E 3 HOH   10  210 232  HOH   HOH B . 
E 3 HOH   11  211 264  HOH   HOH B . 
E 3 HOH   12  212 531  HOH   HOH B . 
E 3 HOH   13  213 120  HOH   HOH B . 
E 3 HOH   14  214 1249 HOH   HOH B . 
E 3 HOH   15  215 353  HOH   HOH B . 
E 3 HOH   16  216 743  HOH   HOH B . 
E 3 HOH   17  217 398  HOH   HOH B . 
E 3 HOH   18  218 332  HOH   HOH B . 
E 3 HOH   19  219 166  HOH   HOH B . 
E 3 HOH   20  220 1278 HOH   HOH B . 
E 3 HOH   21  221 272  HOH   HOH B . 
E 3 HOH   22  222 343  HOH   HOH B . 
E 3 HOH   23  223 50   HOH   HOH B . 
E 3 HOH   24  224 282  HOH   HOH B . 
E 3 HOH   25  225 444  HOH   HOH B . 
E 3 HOH   26  226 72   HOH   HOH B . 
E 3 HOH   27  227 276  HOH   HOH B . 
E 3 HOH   28  228 131  HOH   HOH B . 
E 3 HOH   29  229 54   HOH   HOH B . 
E 3 HOH   30  230 452  HOH   HOH B . 
E 3 HOH   31  231 1    HOH   HOH B . 
E 3 HOH   32  232 127  HOH   HOH B . 
E 3 HOH   33  233 128  HOH   HOH B . 
E 3 HOH   34  234 110  HOH   HOH B . 
E 3 HOH   35  235 252  HOH   HOH B . 
E 3 HOH   36  236 181  HOH   HOH B . 
E 3 HOH   37  237 75   HOH   HOH B . 
E 3 HOH   38  238 221  HOH   HOH B . 
E 3 HOH   39  239 1140 HOH   HOH B . 
E 3 HOH   40  240 205  HOH   HOH B . 
E 3 HOH   41  241 69   HOH   HOH B . 
E 3 HOH   42  242 300  HOH   HOH B . 
E 3 HOH   43  243 14   HOH   HOH B . 
E 3 HOH   44  244 60   HOH   HOH B . 
E 3 HOH   45  245 129  HOH   HOH B . 
E 3 HOH   46  246 9    HOH   HOH B . 
E 3 HOH   47  247 133  HOH   HOH B . 
E 3 HOH   48  248 31   HOH   HOH B . 
E 3 HOH   49  249 82   HOH   HOH B . 
E 3 HOH   50  250 47   HOH   HOH B . 
E 3 HOH   51  251 325  HOH   HOH B . 
E 3 HOH   52  252 59   HOH   HOH B . 
E 3 HOH   53  253 52   HOH   HOH B . 
E 3 HOH   54  254 635  HOH   HOH B . 
E 3 HOH   55  255 62   HOH   HOH B . 
E 3 HOH   56  256 143  HOH   HOH B . 
E 3 HOH   57  257 20   HOH   HOH B . 
E 3 HOH   58  258 231  HOH   HOH B . 
E 3 HOH   59  259 30   HOH   HOH B . 
E 3 HOH   60  260 150  HOH   HOH B . 
E 3 HOH   61  261 10   HOH   HOH B . 
E 3 HOH   62  262 103  HOH   HOH B . 
E 3 HOH   63  263 144  HOH   HOH B . 
E 3 HOH   64  264 41   HOH   HOH B . 
E 3 HOH   65  265 175  HOH   HOH B . 
E 3 HOH   66  266 391  HOH   HOH B . 
E 3 HOH   67  267 1106 HOH   HOH B . 
E 3 HOH   68  268 77   HOH   HOH B . 
E 3 HOH   69  269 362  HOH   HOH B . 
E 3 HOH   70  270 387  HOH   HOH B . 
E 3 HOH   71  271 1277 HOH   HOH B . 
E 3 HOH   72  272 84   HOH   HOH B . 
E 3 HOH   73  273 242  HOH   HOH B . 
E 3 HOH   74  274 114  HOH   HOH B . 
E 3 HOH   75  275 1126 HOH   HOH B . 
E 3 HOH   76  276 172  HOH   HOH B . 
E 3 HOH   77  277 347  HOH   HOH B . 
E 3 HOH   78  278 61   HOH   HOH B . 
E 3 HOH   79  279 302  HOH   HOH B . 
E 3 HOH   80  280 341  HOH   HOH B . 
E 3 HOH   81  281 100  HOH   HOH B . 
E 3 HOH   82  282 117  HOH   HOH B . 
E 3 HOH   83  283 11   HOH   HOH B . 
E 3 HOH   84  284 43   HOH   HOH B . 
E 3 HOH   85  285 1312 HOH   HOH B . 
E 3 HOH   86  286 287  HOH   HOH B . 
E 3 HOH   87  287 271  HOH   HOH B . 
E 3 HOH   88  288 297  HOH   HOH B . 
E 3 HOH   89  289 89   HOH   HOH B . 
E 3 HOH   90  290 22   HOH   HOH B . 
E 3 HOH   91  291 243  HOH   HOH B . 
E 3 HOH   92  292 311  HOH   HOH B . 
E 3 HOH   93  293 1066 HOH   HOH B . 
E 3 HOH   94  294 88   HOH   HOH B . 
E 3 HOH   95  295 13   HOH   HOH B . 
E 3 HOH   96  296 316  HOH   HOH B . 
E 3 HOH   97  297 235  HOH   HOH B . 
E 3 HOH   98  298 299  HOH   HOH B . 
E 3 HOH   99  299 704  HOH   HOH B . 
E 3 HOH   100 300 106  HOH   HOH B . 
E 3 HOH   101 301 339  HOH   HOH B . 
E 3 HOH   102 302 32   HOH   HOH B . 
E 3 HOH   103 303 137  HOH   HOH B . 
E 3 HOH   104 304 147  HOH   HOH B . 
E 3 HOH   105 305 118  HOH   HOH B . 
E 3 HOH   106 306 99   HOH   HOH B . 
E 3 HOH   107 307 38   HOH   HOH B . 
E 3 HOH   108 308 142  HOH   HOH B . 
E 3 HOH   109 309 216  HOH   HOH B . 
E 3 HOH   110 310 112  HOH   HOH B . 
E 3 HOH   111 311 37   HOH   HOH B . 
E 3 HOH   112 312 220  HOH   HOH B . 
E 3 HOH   113 313 1305 HOH   HOH B . 
E 3 HOH   114 314 101  HOH   HOH B . 
E 3 HOH   115 315 91   HOH   HOH B . 
E 3 HOH   116 316 48   HOH   HOH B . 
E 3 HOH   117 317 416  HOH   HOH B . 
E 3 HOH   118 318 215  HOH   HOH B . 
E 3 HOH   119 319 182  HOH   HOH B . 
E 3 HOH   120 320 23   HOH   HOH B . 
E 3 HOH   121 321 141  HOH   HOH B . 
E 3 HOH   122 322 170  HOH   HOH B . 
E 3 HOH   123 323 160  HOH   HOH B . 
E 3 HOH   124 324 334  HOH   HOH B . 
E 3 HOH   125 325 44   HOH   HOH B . 
E 3 HOH   126 326 28   HOH   HOH B . 
E 3 HOH   127 327 1291 HOH   HOH B . 
E 3 HOH   128 328 1285 HOH   HOH B . 
E 3 HOH   129 329 161  HOH   HOH B . 
E 3 HOH   130 330 1274 HOH   HOH B . 
E 3 HOH   131 331 717  HOH   HOH B . 
E 3 HOH   132 332 29   HOH   HOH B . 
E 3 HOH   133 333 177  HOH   HOH B . 
E 3 HOH   134 334 197  HOH   HOH B . 
E 3 HOH   135 335 98   HOH   HOH B . 
E 3 HOH   136 336 55   HOH   HOH B . 
E 3 HOH   137 337 207  HOH   HOH B . 
E 3 HOH   138 338 445  HOH   HOH B . 
E 3 HOH   139 339 960  HOH   HOH B . 
E 3 HOH   140 340 234  HOH   HOH B . 
E 3 HOH   141 341 65   HOH   HOH B . 
E 3 HOH   142 342 619  HOH   HOH B . 
E 3 HOH   143 343 1294 HOH   HOH B . 
E 3 HOH   144 344 1293 HOH   HOH B . 
E 3 HOH   145 345 203  HOH   HOH B . 
E 3 HOH   146 346 90   HOH   HOH B . 
E 3 HOH   147 347 1280 HOH   HOH B . 
E 3 HOH   148 348 463  HOH   HOH B . 
E 3 HOH   149 349 191  HOH   HOH B . 
E 3 HOH   150 350 304  HOH   HOH B . 
E 3 HOH   151 351 178  HOH   HOH B . 
E 3 HOH   152 352 335  HOH   HOH B . 
E 3 HOH   153 353 1046 HOH   HOH B . 
E 3 HOH   154 354 541  HOH   HOH B . 
E 3 HOH   155 355 623  HOH   HOH B . 
E 3 HOH   156 356 1304 HOH   HOH B . 
E 3 HOH   157 357 290  HOH   HOH B . 
E 3 HOH   158 358 1072 HOH   HOH B . 
E 3 HOH   159 359 283  HOH   HOH B . 
E 3 HOH   160 360 87   HOH   HOH B . 
E 3 HOH   161 361 718  HOH   HOH B . 
E 3 HOH   162 362 389  HOH   HOH B . 
E 3 HOH   163 363 1077 HOH   HOH B . 
E 3 HOH   164 364 479  HOH   HOH B . 
E 3 HOH   165 365 615  HOH   HOH B . 
E 3 HOH   166 366 291  HOH   HOH B . 
E 3 HOH   167 367 898  HOH   HOH B . 
E 3 HOH   168 368 667  HOH   HOH B . 
E 3 HOH   169 369 1316 HOH   HOH B . 
E 3 HOH   170 370 340  HOH   HOH B . 
E 3 HOH   171 371 310  HOH   HOH B . 
E 3 HOH   172 372 373  HOH   HOH B . 
E 3 HOH   173 373 190  HOH   HOH B . 
E 3 HOH   174 374 1173 HOH   HOH B . 
E 3 HOH   175 375 149  HOH   HOH B . 
E 3 HOH   176 376 1303 HOH   HOH B . 
E 3 HOH   177 377 431  HOH   HOH B . 
E 3 HOH   178 378 1163 HOH   HOH B . 
E 3 HOH   179 379 183  HOH   HOH B . 
E 3 HOH   180 380 418  HOH   HOH B . 
E 3 HOH   181 381 424  HOH   HOH B . 
E 3 HOH   182 382 470  HOH   HOH B . 
E 3 HOH   183 383 176  HOH   HOH B . 
E 3 HOH   184 384 1311 HOH   HOH B . 
E 3 HOH   185 385 1000 HOH   HOH B . 
E 3 HOH   186 386 248  HOH   HOH B . 
E 3 HOH   187 387 981  HOH   HOH B . 
E 3 HOH   188 388 265  HOH   HOH B . 
E 3 HOH   189 389 1298 HOH   HOH B . 
E 3 HOH   190 390 491  HOH   HOH B . 
E 3 HOH   191 391 184  HOH   HOH B . 
E 3 HOH   192 392 360  HOH   HOH B . 
E 3 HOH   193 393 410  HOH   HOH B . 
E 3 HOH   194 394 355  HOH   HOH B . 
E 3 HOH   195 395 566  HOH   HOH B . 
E 3 HOH   196 396 314  HOH   HOH B . 
E 3 HOH   197 397 274  HOH   HOH B . 
E 3 HOH   198 398 792  HOH   HOH B . 
E 3 HOH   199 399 185  HOH   HOH B . 
E 3 HOH   200 400 157  HOH   HOH B . 
E 3 HOH   201 401 321  HOH   HOH B . 
E 3 HOH   202 402 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HFE 
_cell.length_a           88.801 
_cell.length_b           88.801 
_cell.length_c           39.735 
_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                         7HFE 
_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          7HFE 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.16 
_exptl_crystal.density_percent_sol   43.02 
_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                     7HFE 
_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            0.990 
_reflns.number_obs                   171053 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.400 
_reflns.pdbx_Rmerge_I_obs            0.049 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.500 
_reflns.B_iso_Wilson_estimate        11.570 
_reflns.pdbx_redundancy              6.500 
_reflns.pdbx_Rrim_I_all              0.054 
_reflns.pdbx_Rpim_I_all              0.021 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1107449 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 0.990 1.010  ? 37802 7691 ? 2.179 ? ? ? 4.900 ? 0.600  ? ? ? ? ? ? 91.300 2.438 1.069 0.426 
1 2 5.420 44.400 ? 7970  1132 ? 0.032 ? ? ? 7.000 ? 61.300 ? ? ? ? ? ? 99.800 0.034 0.013 0.999 
# 
_refine.entry_id                                 7HFE 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9900 
_refine.ls_d_res_low                             39.7100 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.1900 
_refine.ls_number_reflns_obs                     170756 
_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                          0.1530 
_refine.ls_R_factor_R_work                       0.1524 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1667 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  8239 
_refine.ls_number_reflns_R_work                  162517 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.6845 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1200 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                62.340 
_refine.B_iso_min                                9.000 
_refine.pdbx_overall_phase_error                 21.1700 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       0.9900 
_refine_hist.d_res_low                        39.7100 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.number_atoms_solvent             418 
_refine_hist.number_atoms_total               3000 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           18.40 
_refine_hist.pdbx_B_iso_mean_solvent          29.97 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
0.9900 1.0000  30 87.0000  4650 . 0.4776 0.4555 . 245 0.0000 4895 . 'X-RAY DIFFRACTION' 
1.0000 1.0100  30 97.0000  5325 . 0.4031 0.3587 . 274 0.0000 5599 . 'X-RAY DIFFRACTION' 
1.0100 1.0300  30 100.0000 5349 . 0.3452 0.3420 . 241 0.0000 5590 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5466 . 0.3176 0.3049 . 271 0.0000 5737 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5430 . 0.2959 0.2960 . 278 0.0000 5708 . 'X-RAY DIFFRACTION' 
1.0500 1.0700  30 100.0000 5312 . 0.2751 0.2920 . 328 0.0000 5640 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 5536 . 0.2530 0.2745 . 277 0.0000 5813 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 5354 . 0.2340 0.2684 . 256 0.0000 5610 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 98.0000  5349 . 0.2225 0.2237 . 273 0.0000 5622 . 'X-RAY DIFFRACTION' 
1.1200 1.1300  30 100.0000 5467 . 0.1867 0.2178 . 244 0.0000 5711 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 5424 . 0.1712 0.1883 . 276 0.0000 5700 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 5423 . 0.1610 0.1912 . 276 0.0000 5699 . 'X-RAY DIFFRACTION' 
1.1700 1.2000  30 100.0000 5421 . 0.1542 0.2022 . 280 0.0000 5701 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 100.0000 5415 . 0.1428 0.1674 . 279 0.0000 5694 . 'X-RAY DIFFRACTION' 
1.2200 1.2500  30 100.0000 5468 . 0.1410 0.1582 . 268 0.0000 5736 . 'X-RAY DIFFRACTION' 
1.2500 1.2800  30 99.0000  5368 . 0.1466 0.1704 . 256 0.0000 5624 . 'X-RAY DIFFRACTION' 
1.2800 1.3100  30 99.0000  5427 . 0.1389 0.1657 . 277 0.0000 5704 . 'X-RAY DIFFRACTION' 
1.3100 1.3400  30 100.0000 5428 . 0.1376 0.1559 . 296 0.0000 5724 . 'X-RAY DIFFRACTION' 
1.3400 1.3800  30 100.0000 5423 . 0.1356 0.1768 . 295 0.0000 5718 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 5506 . 0.1285 0.1514 . 257 0.0000 5763 . 'X-RAY DIFFRACTION' 
1.4300 1.4800  30 100.0000 5485 . 0.1257 0.1360 . 272 0.0000 5757 . 'X-RAY DIFFRACTION' 
1.4800 1.5400  30 100.0000 5409 . 0.1182 0.1325 . 263 0.0000 5672 . 'X-RAY DIFFRACTION' 
1.5400 1.6100  30 100.0000 5432 . 0.1185 0.1303 . 305 0.0000 5737 . 'X-RAY DIFFRACTION' 
1.6100 1.6900  30 100.0000 5450 . 0.1250 0.1422 . 253 0.0000 5703 . 'X-RAY DIFFRACTION' 
1.6900 1.8000  30 100.0000 5554 . 0.1331 0.1513 . 269 0.0000 5823 . 'X-RAY DIFFRACTION' 
1.8000 1.9400  30 100.0000 5441 . 0.1360 0.1408 . 300 0.0000 5741 . 'X-RAY DIFFRACTION' 
1.9400 2.1300  30 100.0000 5512 . 0.1396 0.1592 . 270 0.0000 5782 . 'X-RAY DIFFRACTION' 
2.1300 2.4400  30 100.0000 5476 . 0.1402 0.1379 . 305 0.0000 5781 . 'X-RAY DIFFRACTION' 
2.4400 3.0800  30 100.0000 5532 . 0.1510 0.1718 . 286 0.0000 5818 . 'X-RAY DIFFRACTION' 
3.0800 39.7100 30 100.0000 5685 . 0.1508 0.1650 . 269 0.0000 5954 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HFE 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0004128' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HFE 
_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 7HFE A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HFE 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 7HFE SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HFE MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HFE SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HFE 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 LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HFE 
_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   B 
_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    301 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.57 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.89   -131.51 
2 1 HIS A 86  ? ? 55.89   -133.45 
3 1 ASP A 157 ? B -169.93 100.50  
4 1 HIS B 86  ? ? 57.44   -128.18 
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 515 ? 6.13 . 
2 1 O ? A HOH 516 ? 7.43 . 
3 1 O ? B HOH 402 ? 6.45 . 
# 
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 
A1BA5 N2   N Y N 1   
A1BA5 C3   C N R 2   
A1BA5 C6   C N N 3   
A1BA5 C9   C Y N 4   
A1BA5 C12  C Y N 5   
A1BA5 C14  C Y N 6   
A1BA5 C1   C N N 7   
A1BA5 C10  C Y N 8   
A1BA5 C11  C Y N 9   
A1BA5 C13  C Y N 10  
A1BA5 C15  C N N 11  
A1BA5 C2   C N N 12  
A1BA5 C4   C N S 13  
A1BA5 C5   C N N 14  
A1BA5 C7   C N R 15  
A1BA5 C8   C N N 16  
A1BA5 N1   N N N 17  
A1BA5 N3   N Y N 18  
A1BA5 N4   N Y N 19  
A1BA5 O1   O N N 20  
A1BA5 H16  H N N 21  
A1BA5 H1   H N N 22  
A1BA5 H10  H N N 23  
A1BA5 H11  H N N 24  
A1BA5 H15  H N N 25  
A1BA5 H17  H N N 26  
A1BA5 H4   H N N 27  
A1BA5 H5   H N N 28  
A1BA5 H6   H N N 29  
A1BA5 H14  H N N 30  
A1BA5 H20  H N N 31  
A1BA5 H19  H N N 32  
A1BA5 H18  H N N 33  
A1BA5 H2   H N N 34  
A1BA5 H8   H N N 35  
A1BA5 H9   H N N 36  
A1BA5 H3   H N N 37  
A1BA5 H13  H N N 38  
A1BA5 H12  H N N 39  
A1BA5 H7   H N N 40  
ALA   N    N N N 41  
ALA   CA   C N S 42  
ALA   C    C N N 43  
ALA   O    O N N 44  
ALA   CB   C N N 45  
ALA   OXT  O N N 46  
ALA   H    H N N 47  
ALA   H2   H N N 48  
ALA   HA   H N N 49  
ALA   HB1  H N N 50  
ALA   HB2  H N N 51  
ALA   HB3  H N N 52  
ALA   HXT  H N N 53  
ARG   N    N N N 54  
ARG   CA   C N S 55  
ARG   C    C N N 56  
ARG   O    O N N 57  
ARG   CB   C N N 58  
ARG   CG   C N N 59  
ARG   CD   C N N 60  
ARG   NE   N N N 61  
ARG   CZ   C N N 62  
ARG   NH1  N N N 63  
ARG   NH2  N N N 64  
ARG   OXT  O N N 65  
ARG   H    H N N 66  
ARG   H2   H N N 67  
ARG   HA   H N N 68  
ARG   HB2  H N N 69  
ARG   HB3  H N N 70  
ARG   HG2  H N N 71  
ARG   HG3  H N N 72  
ARG   HD2  H N N 73  
ARG   HD3  H N N 74  
ARG   HE   H N N 75  
ARG   HH11 H N N 76  
ARG   HH12 H N N 77  
ARG   HH21 H N N 78  
ARG   HH22 H N N 79  
ARG   HXT  H N N 80  
ASN   N    N N N 81  
ASN   CA   C N S 82  
ASN   C    C N N 83  
ASN   O    O N N 84  
ASN   CB   C N N 85  
ASN   CG   C N N 86  
ASN   OD1  O N N 87  
ASN   ND2  N N N 88  
ASN   OXT  O N N 89  
ASN   H    H N N 90  
ASN   H2   H N N 91  
ASN   HA   H N N 92  
ASN   HB2  H N N 93  
ASN   HB3  H N N 94  
ASN   HD21 H N N 95  
ASN   HD22 H N N 96  
ASN   HXT  H N N 97  
ASP   N    N N N 98  
ASP   CA   C N S 99  
ASP   C    C N N 100 
ASP   O    O N N 101 
ASP   CB   C N N 102 
ASP   CG   C N N 103 
ASP   OD1  O N N 104 
ASP   OD2  O N N 105 
ASP   OXT  O N N 106 
ASP   H    H N N 107 
ASP   H2   H N N 108 
ASP   HA   H N N 109 
ASP   HB2  H N N 110 
ASP   HB3  H N N 111 
ASP   HD2  H N N 112 
ASP   HXT  H N N 113 
CYS   N    N N N 114 
CYS   CA   C N R 115 
CYS   C    C N N 116 
CYS   O    O N N 117 
CYS   CB   C N N 118 
CYS   SG   S N N 119 
CYS   OXT  O N N 120 
CYS   H    H N N 121 
CYS   H2   H N N 122 
CYS   HA   H N N 123 
CYS   HB2  H N N 124 
CYS   HB3  H N N 125 
CYS   HG   H N N 126 
CYS   HXT  H N N 127 
GLN   N    N N N 128 
GLN   CA   C N S 129 
GLN   C    C N N 130 
GLN   O    O N N 131 
GLN   CB   C N N 132 
GLN   CG   C N N 133 
GLN   CD   C N N 134 
GLN   OE1  O N N 135 
GLN   NE2  N N N 136 
GLN   OXT  O N N 137 
GLN   H    H N N 138 
GLN   H2   H N N 139 
GLN   HA   H N N 140 
GLN   HB2  H N N 141 
GLN   HB3  H N N 142 
GLN   HG2  H N N 143 
GLN   HG3  H N N 144 
GLN   HE21 H N N 145 
GLN   HE22 H N N 146 
GLN   HXT  H N N 147 
GLU   N    N N N 148 
GLU   CA   C N S 149 
GLU   C    C N N 150 
GLU   O    O N N 151 
GLU   CB   C N N 152 
GLU   CG   C N N 153 
GLU   CD   C N N 154 
GLU   OE1  O N N 155 
GLU   OE2  O N N 156 
GLU   OXT  O N N 157 
GLU   H    H N N 158 
GLU   H2   H N N 159 
GLU   HA   H N N 160 
GLU   HB2  H N N 161 
GLU   HB3  H N N 162 
GLU   HG2  H N N 163 
GLU   HG3  H N N 164 
GLU   HE2  H N N 165 
GLU   HXT  H N N 166 
GLY   N    N N N 167 
GLY   CA   C N N 168 
GLY   C    C N N 169 
GLY   O    O N N 170 
GLY   OXT  O N N 171 
GLY   H    H N N 172 
GLY   H2   H N N 173 
GLY   HA2  H N N 174 
GLY   HA3  H N N 175 
GLY   HXT  H N N 176 
HIS   N    N N N 177 
HIS   CA   C N S 178 
HIS   C    C N N 179 
HIS   O    O N N 180 
HIS   CB   C N N 181 
HIS   CG   C Y N 182 
HIS   ND1  N Y N 183 
HIS   CD2  C Y N 184 
HIS   CE1  C Y N 185 
HIS   NE2  N Y N 186 
HIS   OXT  O N N 187 
HIS   H    H N N 188 
HIS   H2   H N N 189 
HIS   HA   H N N 190 
HIS   HB2  H N N 191 
HIS   HB3  H N N 192 
HIS   HD1  H N N 193 
HIS   HD2  H N N 194 
HIS   HE1  H N N 195 
HIS   HE2  H N N 196 
HIS   HXT  H N N 197 
HOH   O    O N N 198 
HOH   H1   H N N 199 
HOH   H2   H N N 200 
ILE   N    N N N 201 
ILE   CA   C N S 202 
ILE   C    C N N 203 
ILE   O    O N N 204 
ILE   CB   C N S 205 
ILE   CG1  C N N 206 
ILE   CG2  C N N 207 
ILE   CD1  C N N 208 
ILE   OXT  O N N 209 
ILE   H    H N N 210 
ILE   H2   H N N 211 
ILE   HA   H N N 212 
ILE   HB   H N N 213 
ILE   HG12 H N N 214 
ILE   HG13 H N N 215 
ILE   HG21 H N N 216 
ILE   HG22 H N N 217 
ILE   HG23 H N N 218 
ILE   HD11 H N N 219 
ILE   HD12 H N N 220 
ILE   HD13 H N N 221 
ILE   HXT  H N N 222 
LEU   N    N N N 223 
LEU   CA   C N S 224 
LEU   C    C N N 225 
LEU   O    O N N 226 
LEU   CB   C N N 227 
LEU   CG   C N N 228 
LEU   CD1  C N N 229 
LEU   CD2  C N N 230 
LEU   OXT  O N N 231 
LEU   H    H N N 232 
LEU   H2   H N N 233 
LEU   HA   H N N 234 
LEU   HB2  H N N 235 
LEU   HB3  H N N 236 
LEU   HG   H N N 237 
LEU   HD11 H N N 238 
LEU   HD12 H N N 239 
LEU   HD13 H N N 240 
LEU   HD21 H N N 241 
LEU   HD22 H N N 242 
LEU   HD23 H N N 243 
LEU   HXT  H N N 244 
LYS   N    N N N 245 
LYS   CA   C N S 246 
LYS   C    C N N 247 
LYS   O    O N N 248 
LYS   CB   C N N 249 
LYS   CG   C N N 250 
LYS   CD   C N N 251 
LYS   CE   C N N 252 
LYS   NZ   N N N 253 
LYS   OXT  O N N 254 
LYS   H    H N N 255 
LYS   H2   H N N 256 
LYS   HA   H N N 257 
LYS   HB2  H N N 258 
LYS   HB3  H N N 259 
LYS   HG2  H N N 260 
LYS   HG3  H N N 261 
LYS   HD2  H N N 262 
LYS   HD3  H N N 263 
LYS   HE2  H N N 264 
LYS   HE3  H N N 265 
LYS   HZ1  H N N 266 
LYS   HZ2  H N N 267 
LYS   HZ3  H N N 268 
LYS   HXT  H N N 269 
MET   N    N N N 270 
MET   CA   C N S 271 
MET   C    C N N 272 
MET   O    O N N 273 
MET   CB   C N N 274 
MET   CG   C N N 275 
MET   SD   S N N 276 
MET   CE   C N N 277 
MET   OXT  O N N 278 
MET   H    H N N 279 
MET   H2   H N N 280 
MET   HA   H N N 281 
MET   HB2  H N N 282 
MET   HB3  H N N 283 
MET   HG2  H N N 284 
MET   HG3  H N N 285 
MET   HE1  H N N 286 
MET   HE2  H N N 287 
MET   HE3  H N N 288 
MET   HXT  H N N 289 
PHE   N    N N N 290 
PHE   CA   C N S 291 
PHE   C    C N N 292 
PHE   O    O N N 293 
PHE   CB   C N N 294 
PHE   CG   C Y N 295 
PHE   CD1  C Y N 296 
PHE   CD2  C Y N 297 
PHE   CE1  C Y N 298 
PHE   CE2  C Y N 299 
PHE   CZ   C Y N 300 
PHE   OXT  O N N 301 
PHE   H    H N N 302 
PHE   H2   H N N 303 
PHE   HA   H N N 304 
PHE   HB2  H N N 305 
PHE   HB3  H N N 306 
PHE   HD1  H N N 307 
PHE   HD2  H N N 308 
PHE   HE1  H N N 309 
PHE   HE2  H N N 310 
PHE   HZ   H N N 311 
PHE   HXT  H N N 312 
PRO   N    N N N 313 
PRO   CA   C N S 314 
PRO   C    C N N 315 
PRO   O    O N N 316 
PRO   CB   C N N 317 
PRO   CG   C N N 318 
PRO   CD   C N N 319 
PRO   OXT  O N N 320 
PRO   H    H N N 321 
PRO   HA   H N N 322 
PRO   HB2  H N N 323 
PRO   HB3  H N N 324 
PRO   HG2  H N N 325 
PRO   HG3  H N N 326 
PRO   HD2  H N N 327 
PRO   HD3  H N N 328 
PRO   HXT  H N N 329 
SER   N    N N N 330 
SER   CA   C N S 331 
SER   C    C N N 332 
SER   O    O N N 333 
SER   CB   C N N 334 
SER   OG   O N N 335 
SER   OXT  O N N 336 
SER   H    H N N 337 
SER   H2   H N N 338 
SER   HA   H N N 339 
SER   HB2  H N N 340 
SER   HB3  H N N 341 
SER   HG   H N N 342 
SER   HXT  H N N 343 
THR   N    N N N 344 
THR   CA   C N S 345 
THR   C    C N N 346 
THR   O    O N N 347 
THR   CB   C N R 348 
THR   OG1  O N N 349 
THR   CG2  C N N 350 
THR   OXT  O N N 351 
THR   H    H N N 352 
THR   H2   H N N 353 
THR   HA   H N N 354 
THR   HB   H N N 355 
THR   HG1  H N N 356 
THR   HG21 H N N 357 
THR   HG22 H N N 358 
THR   HG23 H N N 359 
THR   HXT  H N N 360 
TYR   N    N N N 361 
TYR   CA   C N S 362 
TYR   C    C N N 363 
TYR   O    O N N 364 
TYR   CB   C N N 365 
TYR   CG   C Y N 366 
TYR   CD1  C Y N 367 
TYR   CD2  C Y N 368 
TYR   CE1  C Y N 369 
TYR   CE2  C Y N 370 
TYR   CZ   C Y N 371 
TYR   OH   O N N 372 
TYR   OXT  O N N 373 
TYR   H    H N N 374 
TYR   H2   H N N 375 
TYR   HA   H N N 376 
TYR   HB2  H N N 377 
TYR   HB3  H N N 378 
TYR   HD1  H N N 379 
TYR   HD2  H N N 380 
TYR   HE1  H N N 381 
TYR   HE2  H N N 382 
TYR   HH   H N N 383 
TYR   HXT  H N N 384 
VAL   N    N N N 385 
VAL   CA   C N S 386 
VAL   C    C N N 387 
VAL   O    O N N 388 
VAL   CB   C N N 389 
VAL   CG1  C N N 390 
VAL   CG2  C N N 391 
VAL   OXT  O N N 392 
VAL   H    H N N 393 
VAL   H2   H N N 394 
VAL   HA   H N N 395 
VAL   HB   H N N 396 
VAL   HG11 H N N 397 
VAL   HG12 H N N 398 
VAL   HG13 H N N 399 
VAL   HG21 H N N 400 
VAL   HG22 H N N 401 
VAL   HG23 H N N 402 
VAL   HXT  H N N 403 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1BA5 C6  C5   sing N N 1   
A1BA5 C6  C7   sing N N 2   
A1BA5 C5  C4   sing N N 3   
A1BA5 C4  C7   sing N N 4   
A1BA5 C4  C3   sing N N 5   
A1BA5 C7  C8   sing N N 6   
A1BA5 C1  C2   sing N N 7   
A1BA5 C3  C2   sing N N 8   
A1BA5 C3  N1   sing N N 9   
A1BA5 C8  N1   sing N N 10  
A1BA5 C2  C15  sing N N 11  
A1BA5 C2  O1   sing N N 12  
A1BA5 N1  C9   sing N N 13  
A1BA5 C9  N4   doub Y N 14  
A1BA5 C9  C10  sing Y N 15  
A1BA5 C11 C10  sing Y N 16  
A1BA5 C11 C12  doub Y N 17  
A1BA5 N4  C14  sing Y N 18  
A1BA5 C10 C13  doub Y N 19  
A1BA5 C12 N2   sing Y N 20  
A1BA5 C14 N3   doub Y N 21  
A1BA5 C13 N3   sing Y N 22  
A1BA5 C13 N2   sing Y N 23  
A1BA5 N2  H16  sing N N 24  
A1BA5 C3  H1   sing N N 25  
A1BA5 C6  H10  sing N N 26  
A1BA5 C6  H11  sing N N 27  
A1BA5 C12 H15  sing N N 28  
A1BA5 C14 H17  sing N N 29  
A1BA5 C1  H4   sing N N 30  
A1BA5 C1  H5   sing N N 31  
A1BA5 C1  H6   sing N N 32  
A1BA5 C11 H14  sing N N 33  
A1BA5 C15 H20  sing N N 34  
A1BA5 C15 H19  sing N N 35  
A1BA5 C15 H18  sing N N 36  
A1BA5 C4  H2   sing N N 37  
A1BA5 C5  H8   sing N N 38  
A1BA5 C5  H9   sing N N 39  
A1BA5 C7  H3   sing N N 40  
A1BA5 C8  H13  sing N N 41  
A1BA5 C8  H12  sing N N 42  
A1BA5 O1  H7   sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CYS   N   CA   sing N N 113 
CYS   N   H    sing N N 114 
CYS   N   H2   sing N N 115 
CYS   CA  C    sing N N 116 
CYS   CA  CB   sing N N 117 
CYS   CA  HA   sing N N 118 
CYS   C   O    doub N N 119 
CYS   C   OXT  sing N N 120 
CYS   CB  SG   sing N N 121 
CYS   CB  HB2  sing N N 122 
CYS   CB  HB3  sing N N 123 
CYS   SG  HG   sing N N 124 
CYS   OXT HXT  sing N N 125 
GLN   N   CA   sing N N 126 
GLN   N   H    sing N N 127 
GLN   N   H2   sing N N 128 
GLN   CA  C    sing N N 129 
GLN   CA  CB   sing N N 130 
GLN   CA  HA   sing N N 131 
GLN   C   O    doub N N 132 
GLN   C   OXT  sing N N 133 
GLN   CB  CG   sing N N 134 
GLN   CB  HB2  sing N N 135 
GLN   CB  HB3  sing N N 136 
GLN   CG  CD   sing N N 137 
GLN   CG  HG2  sing N N 138 
GLN   CG  HG3  sing N N 139 
GLN   CD  OE1  doub N N 140 
GLN   CD  NE2  sing N N 141 
GLN   NE2 HE21 sing N N 142 
GLN   NE2 HE22 sing N N 143 
GLN   OXT HXT  sing N N 144 
GLU   N   CA   sing N N 145 
GLU   N   H    sing N N 146 
GLU   N   H2   sing N N 147 
GLU   CA  C    sing N N 148 
GLU   CA  CB   sing N N 149 
GLU   CA  HA   sing N N 150 
GLU   C   O    doub N N 151 
GLU   C   OXT  sing N N 152 
GLU   CB  CG   sing N N 153 
GLU   CB  HB2  sing N N 154 
GLU   CB  HB3  sing N N 155 
GLU   CG  CD   sing N N 156 
GLU   CG  HG2  sing N N 157 
GLU   CG  HG3  sing N N 158 
GLU   CD  OE1  doub N N 159 
GLU   CD  OE2  sing N N 160 
GLU   OE2 HE2  sing N N 161 
GLU   OXT HXT  sing N N 162 
GLY   N   CA   sing N N 163 
GLY   N   H    sing N N 164 
GLY   N   H2   sing N N 165 
GLY   CA  C    sing N N 166 
GLY   CA  HA2  sing N N 167 
GLY   CA  HA3  sing N N 168 
GLY   C   O    doub N N 169 
GLY   C   OXT  sing N N 170 
GLY   OXT HXT  sing N N 171 
HIS   N   CA   sing N N 172 
HIS   N   H    sing N N 173 
HIS   N   H2   sing N N 174 
HIS   CA  C    sing N N 175 
HIS   CA  CB   sing N N 176 
HIS   CA  HA   sing N N 177 
HIS   C   O    doub N N 178 
HIS   C   OXT  sing N N 179 
HIS   CB  CG   sing N N 180 
HIS   CB  HB2  sing N N 181 
HIS   CB  HB3  sing N N 182 
HIS   CG  ND1  sing Y N 183 
HIS   CG  CD2  doub Y N 184 
HIS   ND1 CE1  doub Y N 185 
HIS   ND1 HD1  sing N N 186 
HIS   CD2 NE2  sing Y N 187 
HIS   CD2 HD2  sing N N 188 
HIS   CE1 NE2  sing Y N 189 
HIS   CE1 HE1  sing N N 190 
HIS   NE2 HE2  sing N N 191 
HIS   OXT HXT  sing N N 192 
HOH   O   H1   sing N N 193 
HOH   O   H2   sing N N 194 
ILE   N   CA   sing N N 195 
ILE   N   H    sing N N 196 
ILE   N   H2   sing N N 197 
ILE   CA  C    sing N N 198 
ILE   CA  CB   sing N N 199 
ILE   CA  HA   sing N N 200 
ILE   C   O    doub N N 201 
ILE   C   OXT  sing N N 202 
ILE   CB  CG1  sing N N 203 
ILE   CB  CG2  sing N N 204 
ILE   CB  HB   sing N N 205 
ILE   CG1 CD1  sing N N 206 
ILE   CG1 HG12 sing N N 207 
ILE   CG1 HG13 sing N N 208 
ILE   CG2 HG21 sing N N 209 
ILE   CG2 HG22 sing N N 210 
ILE   CG2 HG23 sing N N 211 
ILE   CD1 HD11 sing N N 212 
ILE   CD1 HD12 sing N N 213 
ILE   CD1 HD13 sing N N 214 
ILE   OXT HXT  sing N N 215 
LEU   N   CA   sing N N 216 
LEU   N   H    sing N N 217 
LEU   N   H2   sing N N 218 
LEU   CA  C    sing N N 219 
LEU   CA  CB   sing N N 220 
LEU   CA  HA   sing N N 221 
LEU   C   O    doub N N 222 
LEU   C   OXT  sing N N 223 
LEU   CB  CG   sing N N 224 
LEU   CB  HB2  sing N N 225 
LEU   CB  HB3  sing N N 226 
LEU   CG  CD1  sing N N 227 
LEU   CG  CD2  sing N N 228 
LEU   CG  HG   sing N N 229 
LEU   CD1 HD11 sing N N 230 
LEU   CD1 HD12 sing N N 231 
LEU   CD1 HD13 sing N N 232 
LEU   CD2 HD21 sing N N 233 
LEU   CD2 HD22 sing N N 234 
LEU   CD2 HD23 sing N N 235 
LEU   OXT HXT  sing N N 236 
LYS   N   CA   sing N N 237 
LYS   N   H    sing N N 238 
LYS   N   H2   sing N N 239 
LYS   CA  C    sing N N 240 
LYS   CA  CB   sing N N 241 
LYS   CA  HA   sing N N 242 
LYS   C   O    doub N N 243 
LYS   C   OXT  sing N N 244 
LYS   CB  CG   sing N N 245 
LYS   CB  HB2  sing N N 246 
LYS   CB  HB3  sing N N 247 
LYS   CG  CD   sing N N 248 
LYS   CG  HG2  sing N N 249 
LYS   CG  HG3  sing N N 250 
LYS   CD  CE   sing N N 251 
LYS   CD  HD2  sing N N 252 
LYS   CD  HD3  sing N N 253 
LYS   CE  NZ   sing N N 254 
LYS   CE  HE2  sing N N 255 
LYS   CE  HE3  sing N N 256 
LYS   NZ  HZ1  sing N N 257 
LYS   NZ  HZ2  sing N N 258 
LYS   NZ  HZ3  sing N N 259 
LYS   OXT HXT  sing N N 260 
MET   N   CA   sing N N 261 
MET   N   H    sing N N 262 
MET   N   H2   sing N N 263 
MET   CA  C    sing N N 264 
MET   CA  CB   sing N N 265 
MET   CA  HA   sing N N 266 
MET   C   O    doub N N 267 
MET   C   OXT  sing N N 268 
MET   CB  CG   sing N N 269 
MET   CB  HB2  sing N N 270 
MET   CB  HB3  sing N N 271 
MET   CG  SD   sing N N 272 
MET   CG  HG2  sing N N 273 
MET   CG  HG3  sing N N 274 
MET   SD  CE   sing N N 275 
MET   CE  HE1  sing N N 276 
MET   CE  HE2  sing N N 277 
MET   CE  HE3  sing N N 278 
MET   OXT HXT  sing N N 279 
PHE   N   CA   sing N N 280 
PHE   N   H    sing N N 281 
PHE   N   H2   sing N N 282 
PHE   CA  C    sing N N 283 
PHE   CA  CB   sing N N 284 
PHE   CA  HA   sing N N 285 
PHE   C   O    doub N N 286 
PHE   C   OXT  sing N N 287 
PHE   CB  CG   sing N N 288 
PHE   CB  HB2  sing N N 289 
PHE   CB  HB3  sing N N 290 
PHE   CG  CD1  doub Y N 291 
PHE   CG  CD2  sing Y N 292 
PHE   CD1 CE1  sing Y N 293 
PHE   CD1 HD1  sing N N 294 
PHE   CD2 CE2  doub Y N 295 
PHE   CD2 HD2  sing N N 296 
PHE   CE1 CZ   doub Y N 297 
PHE   CE1 HE1  sing N N 298 
PHE   CE2 CZ   sing Y N 299 
PHE   CE2 HE2  sing N N 300 
PHE   CZ  HZ   sing N N 301 
PHE   OXT HXT  sing N N 302 
PRO   N   CA   sing N N 303 
PRO   N   CD   sing N N 304 
PRO   N   H    sing N N 305 
PRO   CA  C    sing N N 306 
PRO   CA  CB   sing N N 307 
PRO   CA  HA   sing N N 308 
PRO   C   O    doub N N 309 
PRO   C   OXT  sing N N 310 
PRO   CB  CG   sing N N 311 
PRO   CB  HB2  sing N N 312 
PRO   CB  HB3  sing N N 313 
PRO   CG  CD   sing N N 314 
PRO   CG  HG2  sing N N 315 
PRO   CG  HG3  sing N N 316 
PRO   CD  HD2  sing N N 317 
PRO   CD  HD3  sing N N 318 
PRO   OXT HXT  sing N N 319 
SER   N   CA   sing N N 320 
SER   N   H    sing N N 321 
SER   N   H2   sing N N 322 
SER   CA  C    sing N N 323 
SER   CA  CB   sing N N 324 
SER   CA  HA   sing N N 325 
SER   C   O    doub N N 326 
SER   C   OXT  sing N N 327 
SER   CB  OG   sing N N 328 
SER   CB  HB2  sing N N 329 
SER   CB  HB3  sing N N 330 
SER   OG  HG   sing N N 331 
SER   OXT HXT  sing N N 332 
THR   N   CA   sing N N 333 
THR   N   H    sing N N 334 
THR   N   H2   sing N N 335 
THR   CA  C    sing N N 336 
THR   CA  CB   sing N N 337 
THR   CA  HA   sing N N 338 
THR   C   O    doub N N 339 
THR   C   OXT  sing N N 340 
THR   CB  OG1  sing N N 341 
THR   CB  CG2  sing N N 342 
THR   CB  HB   sing N N 343 
THR   OG1 HG1  sing N N 344 
THR   CG2 HG21 sing N N 345 
THR   CG2 HG22 sing N N 346 
THR   CG2 HG23 sing N N 347 
THR   OXT HXT  sing N N 348 
TYR   N   CA   sing N N 349 
TYR   N   H    sing N N 350 
TYR   N   H2   sing N N 351 
TYR   CA  C    sing N N 352 
TYR   CA  CB   sing N N 353 
TYR   CA  HA   sing N N 354 
TYR   C   O    doub N N 355 
TYR   C   OXT  sing N N 356 
TYR   CB  CG   sing N N 357 
TYR   CB  HB2  sing N N 358 
TYR   CB  HB3  sing N N 359 
TYR   CG  CD1  doub Y N 360 
TYR   CG  CD2  sing Y N 361 
TYR   CD1 CE1  sing Y N 362 
TYR   CD1 HD1  sing N N 363 
TYR   CD2 CE2  doub Y N 364 
TYR   CD2 HD2  sing N N 365 
TYR   CE1 CZ   doub Y N 366 
TYR   CE1 HE1  sing N N 367 
TYR   CE2 CZ   sing Y N 368 
TYR   CE2 HE2  sing N N 369 
TYR   CZ  OH   sing N N 370 
TYR   OH  HH   sing N N 371 
TYR   OXT HXT  sing N N 372 
VAL   N   CA   sing N N 373 
VAL   N   H    sing N N 374 
VAL   N   H2   sing N N 375 
VAL   CA  C    sing N N 376 
VAL   CA  CB   sing N N 377 
VAL   CA  HA   sing N N 378 
VAL   C   O    doub N N 379 
VAL   C   OXT  sing N N 380 
VAL   CB  CG1  sing N N 381 
VAL   CB  CG2  sing N N 382 
VAL   CB  HB   sing N N 383 
VAL   CG1 HG11 sing N N 384 
VAL   CG1 HG12 sing N N 385 
VAL   CG1 HG13 sing N N 386 
VAL   CG2 HG21 sing N N 387 
VAL   CG2 HG22 sing N N 388 
VAL   CG2 HG23 sing N N 389 
VAL   OXT HXT  sing N N 390 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171110 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         
'PanDDA analysis group deposition of SARS-CoV-2 NSP3 macrodomain ligand screen - FrankenROCS hits and analogues of AVI-313' 
_pdbx_deposit_group.group_description   
'SARS-CoV-2 NSP3 macrodomain in complex with ligands identified by X-ray diffraction using ALS 8.3.1,  SSRL 9-2, and SSRL 12-2' 
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002304 
# 
_atom_sites.entry_id                    7HFE 
_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]   0.025167 
_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   ? 19.839 -16.414 22.364  0.40 47.22 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.746 -16.388 22.449  0.60 47.78 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.861 -15.345 22.524  0.40 46.92 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.803 -15.292 22.638  0.60 47.40 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.507 -13.994 22.245  0.40 45.68 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.468 -13.959 22.318  0.60 45.98 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.629 -13.731 22.678  0.40 45.98 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.572 -13.681 22.785  0.60 46.33 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.210 -15.386 23.923  0.40 47.62 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.213 -15.300 24.064  0.60 48.16 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.175 -14.280 24.066  0.40 47.85 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.225 -14.155 24.241  0.60 48.41 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.575 -16.746 24.170  0.40 47.84 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.544 -16.634 24.351  0.60 48.39 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.156 -15.467 21.874  0.40 56.36 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 18.066 -15.405 22.023  0.60 56.94 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.893 -15.246 24.598  0.40 57.20 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.929 -15.178 24.707  0.60 57.85 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.668 -14.428 24.880  0.40 57.48 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.731 -14.290 25.065  0.60 58.14 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.628 -13.424 24.112  0.40 57.48 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.712 -13.317 24.282  0.60 58.14 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.582 -14.302 23.300  0.40 57.48 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.613 -14.148 23.488  0.60 58.14 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 17.113 -16.728 25.023  0.40 57.47 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.120 -16.594 25.222  0.60 58.12 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.944 -16.932 23.457  0.40 57.47 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.879 -16.806 23.666  0.60 58.12 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.269 -17.422 24.183  0.40 57.47 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.216 -17.333 24.343  0.60 58.12 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.795 -13.141 21.511  1.00 43.80 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.256 -11.794 21.196  1.00 39.54 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 18.123 -10.810 21.443  1.00 36.09 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.997 -11.192 21.778  1.00 35.62 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.785 -11.667 19.760  1.00 38.55 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.756 -12.045 18.720  1.00 37.62 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.678 -11.454 18.656  1.00 37.24 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 19.094 -13.017 17.878  1.00 37.35 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 18.019 -13.324 21.183  0.40 52.62 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 18.051 -13.349 21.127  0.60 52.62 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.977 -11.561 21.797  1.00 47.50 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 20.040 -10.742 19.601  1.00 46.32 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.551 -12.245 19.655  1.00 46.32 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.546 -13.267 17.264  1.00 44.88 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.860 -13.402 17.951  1.00 44.88 ?  4   ASN   A HD22 1 
ATOM   46   N N    . SER   A 1 5   ? 18.428 -9.528  21.257  1.00 32.96 ?  5   SER   A N    1 
ATOM   47   C CA   . SER   A 1 5   ? 17.517 -8.462  21.647  1.00 30.05 ?  5   SER   A CA   1 
ATOM   48   C C    . SER   A 1 5   ? 16.597 -7.995  20.523  1.00 26.23 ?  5   SER   A C    1 
ATOM   49   O O    . SER   A 1 5   ? 15.814 -7.064  20.736  1.00 26.60 ?  5   SER   A O    1 
ATOM   50   C CB   . SER   A 1 5   ? 18.303 -7.285  22.230  1.00 30.87 ?  5   SER   A CB   1 
ATOM   51   O OG   . SER   A 1 5   ? 19.261 -6.820  21.300  1.00 31.30 ?  5   SER   A OG   1 
ATOM   52   H H    . SER   A 1 5   ? 19.170 -9.252  20.903  1.00 39.61 ?  5   SER   A H    1 
ATOM   53   H HA   . SER   A 1 5   ? 16.951 -8.795  22.346  1.00 36.12 ?  5   SER   A HA   1 
ATOM   54   H HB2  . SER   A 1 5   ? 17.692 -6.563  22.440  1.00 37.11 ?  5   SER   A HB2  1 
ATOM   55   H HB3  . SER   A 1 5   ? 18.755 -7.577  23.044  1.00 37.11 ?  5   SER   A HB3  1 
ATOM   56   H HG   . SER   A 1 5   ? 19.842 -7.409  21.156  1.00 37.62 ?  5   SER   A HG   1 
ATOM   57   N N    A PHE   A 1 6   ? 16.647 -8.621  19.350  0.40 23.88 ?  6   PHE   A N    1 
ATOM   58   N N    B PHE   A 1 6   ? 16.667 -8.609  19.343  0.60 24.48 ?  6   PHE   A N    1 
ATOM   59   C CA   A PHE   A 1 6   ? 15.725 -8.262  18.280  0.40 21.44 ?  6   PHE   A CA   1 
ATOM   60   C CA   B PHE   A 1 6   ? 15.795 -8.217  18.243  0.60 22.65 ?  6   PHE   A CA   1 
ATOM   61   C C    A PHE   A 1 6   ? 14.303 -8.638  18.678  0.40 20.44 ?  6   PHE   A C    1 
ATOM   62   C C    B PHE   A 1 6   ? 14.344 -8.485  18.617  0.60 23.28 ?  6   PHE   A C    1 
ATOM   63   O O    A PHE   A 1 6   ? 14.073 -9.674  19.310  0.40 20.56 ?  6   PHE   A O    1 
ATOM   64   O O    B PHE   A 1 6   ? 13.943 -9.642  18.785  0.60 23.69 ?  6   PHE   A O    1 
ATOM   65   C CB   A PHE   A 1 6   ? 16.112 -8.978  16.986  0.40 20.26 ?  6   PHE   A CB   1 
ATOM   66   C CB   B PHE   A 1 6   ? 16.182 -8.945  16.955  0.60 20.89 ?  6   PHE   A CB   1 
ATOM   67   C CG   A PHE   A 1 6   ? 17.394 -8.479  16.372  0.40 19.47 ?  6   PHE   A CG   1 
ATOM   68   C CG   B PHE   A 1 6   ? 17.442 -8.417  16.323  0.60 19.71 ?  6   PHE   A CG   1 
ATOM   69   C CD1  A PHE   A 1 6   ? 17.430 -7.282  15.675  0.40 19.14 ?  6   PHE   A CD1  1 
ATOM   70   C CD1  B PHE   A 1 6   ? 17.430 -7.230  15.610  0.60 19.28 ?  6   PHE   A CD1  1 
ATOM   71   C CD2  A PHE   A 1 6   ? 18.560 -9.219  16.480  0.40 19.39 ?  6   PHE   A CD2  1 
ATOM   72   C CD2  B PHE   A 1 6   ? 18.638 -9.107  16.447  0.60 19.66 ?  6   PHE   A CD2  1 
ATOM   73   C CE1  A PHE   A 1 6   ? 18.609 -6.827  15.107  0.40 19.00 ?  6   PHE   A CE1  1 
ATOM   74   C CE1  B PHE   A 1 6   ? 18.588 -6.741  15.033  0.60 19.22 ?  6   PHE   A CE1  1 
ATOM   75   C CE2  A PHE   A 1 6   ? 19.740 -8.772  15.913  0.40 19.24 ?  6   PHE   A CE2  1 
ATOM   76   C CE2  B PHE   A 1 6   ? 19.796 -8.624  15.871  0.60 19.67 ?  6   PHE   A CE2  1 
ATOM   77   C CZ   A PHE   A 1 6   ? 19.765 -7.576  15.225  0.40 18.97 ?  6   PHE   A CZ   1 
ATOM   78   C CZ   B PHE   A 1 6   ? 19.772 -7.442  15.162  0.60 19.35 ?  6   PHE   A CZ   1 
ATOM   79   H H    A PHE   A 1 6   ? 17.190 -9.258  19.156  0.40 28.71 ?  6   PHE   A H    1 
ATOM   80   H H    B PHE   A 1 6   ? 17.201 -9.256  19.159  0.60 29.43 ?  6   PHE   A H    1 
ATOM   81   H HA   A PHE   A 1 6   ? 15.758 -7.306  18.128  0.40 25.79 ?  6   PHE   A HA   1 
ATOM   82   H HA   B PHE   A 1 6   ? 15.887 -7.269  18.089  0.60 27.23 ?  6   PHE   A HA   1 
ATOM   83   H HB2  A PHE   A 1 6   ? 16.221 -9.925  17.173  0.40 24.36 ?  6   PHE   A HB2  1 
ATOM   84   H HB2  B PHE   A 1 6   ? 16.317 -9.887  17.156  0.60 25.13 ?  6   PHE   A HB2  1 
ATOM   85   H HB3  A PHE   A 1 6   ? 15.403 -8.853  16.336  0.40 24.36 ?  6   PHE   A HB3  1 
ATOM   86   H HB3  B PHE   A 1 6   ? 15.461 -8.851  16.312  0.60 25.13 ?  6   PHE   A HB3  1 
ATOM   87   H HD1  A PHE   A 1 6   ? 16.654 -6.775  15.592  0.40 23.02 ?  6   PHE   A HD1  1 
ATOM   88   H HD1  B PHE   A 1 6   ? 16.632 -6.758  15.521  0.60 23.19 ?  6   PHE   A HD1  1 
ATOM   89   H HD2  A PHE   A 1 6   ? 18.549 -10.026 16.942  0.40 23.33 ?  6   PHE   A HD2  1 
ATOM   90   H HD2  B PHE   A 1 6   ? 18.657 -9.906  16.925  0.60 23.65 ?  6   PHE   A HD2  1 
ATOM   91   H HE1  A PHE   A 1 6   ? 18.623 -6.021  14.642  0.40 22.86 ?  6   PHE   A HE1  1 
ATOM   92   H HE1  B PHE   A 1 6   ? 18.568 -5.943  14.555  0.60 23.12 ?  6   PHE   A HE1  1 
ATOM   93   H HE2  A PHE   A 1 6   ? 20.517 -9.276  15.994  0.40 23.14 ?  6   PHE   A HE2  1 
ATOM   94   H HE2  B PHE   A 1 6   ? 20.592 -9.094  15.961  0.60 23.66 ?  6   PHE   A HE2  1 
ATOM   95   H HZ   A PHE   A 1 6   ? 20.558 -7.272  14.843  0.40 22.82 ?  6   PHE   A HZ   1 
ATOM   96   H HZ   B PHE   A 1 6   ? 20.550 -7.111  14.775  0.60 23.28 ?  6   PHE   A HZ   1 
ATOM   97   N N    A SER   A 1 7   ? 13.340 -7.789  18.311  0.40 19.14 ?  7   SER   A N    1 
ATOM   98   N N    B SER   A 1 7   ? 13.558 -7.419  18.753  0.60 23.60 ?  7   SER   A N    1 
ATOM   99   C CA   A SER   A 1 7   ? 11.972 -7.932  18.793  0.40 18.45 ?  7   SER   A CA   1 
ATOM   100  C CA   B SER   A 1 7   ? 12.209 -7.489  19.298  0.60 24.20 ?  7   SER   A CA   1 
ATOM   101  C C    A SER   A 1 7   ? 10.970 -7.630  17.688  0.40 17.25 ?  7   SER   A C    1 
ATOM   102  C C    B SER   A 1 7   ? 11.189 -7.398  18.172  0.60 23.52 ?  7   SER   A C    1 
ATOM   103  O O    A SER   A 1 7   ? 11.178 -6.726  16.876  0.40 17.18 ?  7   SER   A O    1 
ATOM   104  O O    B SER   A 1 7   ? 11.288 -6.524  17.306  0.60 23.64 ?  7   SER   A O    1 
ATOM   105  C CB   A SER   A 1 7   ? 11.715 -6.995  19.981  0.40 19.41 ?  7   SER   A CB   1 
ATOM   106  C CB   B SER   A 1 7   ? 11.990 -6.346  20.294  0.60 25.17 ?  7   SER   A CB   1 
ATOM   107  O OG   A SER   A 1 7   ? 10.377 -7.091  20.435  0.40 20.54 ?  7   SER   A OG   1 
ATOM   108  O OG   B SER   A 1 7   ? 10.630 -6.245  20.677  0.60 26.12 ?  7   SER   A OG   1 
ATOM   109  H H    A SER   A 1 7   ? 13.457 -7.122  17.781  0.40 23.02 ?  7   SER   A H    1 
ATOM   110  H H    B SER   A 1 7   ? 13.788 -6.619  18.526  0.60 28.38 ?  7   SER   A H    1 
ATOM   111  H HA   A SER   A 1 7   ? 11.826 -8.842  19.089  0.40 22.20 ?  7   SER   A HA   1 
ATOM   112  H HA   B SER   A 1 7   ? 12.084 -8.328  19.764  0.60 29.10 ?  7   SER   A HA   1 
ATOM   113  H HB2  A SER   A 1 7   ? 12.306 -7.242  20.709  0.40 23.35 ?  7   SER   A HB2  1 
ATOM   114  H HB2  B SER   A 1 7   ? 12.522 -6.512  21.089  0.60 30.26 ?  7   SER   A HB2  1 
ATOM   115  H HB3  A SER   A 1 7   ? 11.893 -6.081  19.706  0.40 23.35 ?  7   SER   A HB3  1 
ATOM   116  H HB3  B SER   A 1 7   ? 12.261 -5.510  19.884  0.60 30.26 ?  7   SER   A HB3  1 
ATOM   117  H HG   A SER   A 1 7   ? 10.253 -6.565  21.079  0.40 24.70 ?  7   SER   A HG   1 
ATOM   118  H HG   B SER   A 1 7   ? 10.528 -5.610  21.223  0.60 31.40 ?  7   SER   A HG   1 
ATOM   119  N N    A GLY   A 1 8   ? 9.877  -8.394  17.667  0.40 16.80 ?  8   GLY   A N    1 
ATOM   120  N N    B GLY   A 1 8   ? 10.218 -8.309  18.182  0.60 23.36 ?  8   GLY   A N    1 
ATOM   121  C CA   A GLY   A 1 8   ? 8.779  -8.129  16.761  0.40 16.55 ?  8   GLY   A CA   1 
ATOM   122  C CA   B GLY   A 1 8   ? 9.089  -8.200  17.283  0.60 22.93 ?  8   GLY   A CA   1 
ATOM   123  C C    A GLY   A 1 8   ? 8.967  -8.615  15.344  0.40 16.13 ?  8   GLY   A C    1 
ATOM   124  C C    B GLY   A 1 8   ? 9.317  -8.675  15.869  0.60 22.35 ?  8   GLY   A C    1 
ATOM   125  O O    A GLY   A 1 8   ? 8.194  -8.212  14.465  0.40 16.54 ?  8   GLY   A O    1 
ATOM   126  O O    B GLY   A 1 8   ? 8.579  -8.260  14.970  0.60 23.37 ?  8   GLY   A O    1 
ATOM   127  H H    A GLY   A 1 8   ? 9.755  -9.080  18.175  0.40 20.22 ?  8   GLY   A H    1 
ATOM   128  H H    B GLY   A 1 8   ? 10.198 -8.999  18.695  0.60 28.09 ?  8   GLY   A H    1 
ATOM   129  H HA2  A GLY   A 1 8   ? 7.974  -8.545  17.116  0.40 19.91 ?  8   GLY   A HA2  1 
ATOM   130  H HA2  B GLY   A 1 8   ? 8.349  -8.706  17.648  0.60 27.57 ?  8   GLY   A HA2  1 
ATOM   131  H HA3  A GLY   A 1 8   ? 8.627  -7.174  16.724  0.40 19.91 ?  8   GLY   A HA3  1 
ATOM   132  H HA3  B GLY   A 1 8   ? 8.822  -7.271  17.229  0.60 27.57 ?  8   GLY   A HA3  1 
ATOM   133  N N    A TYR   A 1 9   ? 9.954  -9.470  15.089  0.40 14.53 ?  9   TYR   A N    1 
ATOM   134  N N    B TYR   A 1 9   ? 10.306 -9.535  15.635  0.60 21.01 ?  9   TYR   A N    1 
ATOM   135  C CA   A TYR   A 1 9   ? 10.186 -9.983  13.750  0.40 13.26 ?  9   TYR   A CA   1 
ATOM   136  C CA   B TYR   A 1 9   ? 10.575 -10.042 14.297  0.60 19.69 ?  9   TYR   A CA   1 
ATOM   137  C C    A TYR   A 1 9   ? 9.304  -11.190 13.471  0.40 13.20 ?  9   TYR   A C    1 
ATOM   138  C C    B TYR   A 1 9   ? 9.759  -11.294 14.004  0.60 19.02 ?  9   TYR   A C    1 
ATOM   139  O O    A TYR   A 1 9   ? 8.968  -11.970 14.371  0.40 14.13 ?  9   TYR   A O    1 
ATOM   140  O O    B TYR   A 1 9   ? 9.621  -12.183 14.850  0.60 19.72 ?  9   TYR   A O    1 
ATOM   141  C CB   A TYR   A 1 9   ? 11.646 -10.396 13.566  0.40 12.90 ?  9   TYR   A CB   1 
ATOM   142  C CB   B TYR   A 1 9   ? 12.066 -10.338 14.118  0.60 19.11 ?  9   TYR   A CB   1 
ATOM   143  C CG   A TYR   A 1 9   ? 12.581 -9.232  13.414  0.40 13.07 ?  9   TYR   A CG   1 
ATOM   144  C CG   B TYR   A 1 9   ? 12.881 -9.098  13.853  0.60 18.11 ?  9   TYR   A CG   1 
ATOM   145  C CD1  A TYR   A 1 9   ? 12.924 -8.458  14.510  0.40 13.59 ?  9   TYR   A CD1  1 
ATOM   146  C CD1  B TYR   A 1 9   ? 13.180 -8.216  14.878  0.60 18.04 ?  9   TYR   A CD1  1 
ATOM   147  C CD2  A TYR   A 1 9   ? 13.107 -8.896  12.175  0.40 13.06 ?  9   TYR   A CD2  1 
ATOM   148  C CD2  B TYR   A 1 9   ? 13.338 -8.802  12.575  0.60 17.72 ?  9   TYR   A CD2  1 
ATOM   149  C CE1  A TYR   A 1 9   ? 13.768 -7.381  14.382  0.40 13.84 ?  9   TYR   A CE1  1 
ATOM   150  C CE1  B TYR   A 1 9   ? 13.911 -7.072  14.644  0.60 17.80 ?  9   TYR   A CE1  1 
ATOM   151  C CE2  A TYR   A 1 9   ? 13.959 -7.817  12.035  0.40 13.39 ?  9   TYR   A CE2  1 
ATOM   152  C CE2  B TYR   A 1 9   ? 14.075 -7.658  12.328  0.60 17.25 ?  9   TYR   A CE2  1 
ATOM   153  C CZ   A TYR   A 1 9   ? 14.283 -7.062  13.141  0.40 13.75 ?  9   TYR   A CZ   1 
ATOM   154  C CZ   B TYR   A 1 9   ? 14.356 -6.799  13.366  0.60 17.55 ?  9   TYR   A CZ   1 
ATOM   155  O OH   A TYR   A 1 9   ? 15.126 -5.986  13.014  0.40 14.64 ?  9   TYR   A OH   1 
ATOM   156  O OH   B TYR   A 1 9   ? 15.086 -5.661  13.120  0.60 18.27 ?  9   TYR   A OH   1 
ATOM   157  H H    A TYR   A 1 9   ? 10.492 -9.786  15.684  0.40 17.49 ?  9   TYR   A H    1 
ATOM   158  H H    B TYR   A 1 9   ? 10.840 -9.842  16.238  0.60 25.27 ?  9   TYR   A H    1 
ATOM   159  H HA   A TYR   A 1 9   ? 9.971  -9.294  13.103  0.40 15.97 ?  9   TYR   A HA   1 
ATOM   160  H HA   B TYR   A 1 9   ? 10.332 -9.369  13.645  0.60 23.68 ?  9   TYR   A HA   1 
ATOM   161  H HB2  A TYR   A 1 9   ? 11.922 -10.914 14.339  0.40 15.53 ?  9   TYR   A HB2  1 
ATOM   162  H HB2  B TYR   A 1 9   ? 12.412 -10.760 14.919  0.60 22.99 ?  9   TYR   A HB2  1 
ATOM   163  H HB3  A TYR   A 1 9   ? 11.701 -10.940 12.766  0.40 15.53 ?  9   TYR   A HB3  1 
ATOM   164  H HB3  B TYR   A 1 9   ? 12.174 -10.930 13.359  0.60 22.99 ?  9   TYR   A HB3  1 
ATOM   165  H HD1  A TYR   A 1 9   ? 12.568 -8.672  15.346  0.40 16.37 ?  9   TYR   A HD1  1 
ATOM   166  H HD1  B TYR   A 1 9   ? 12.876 -8.397  15.740  0.60 21.70 ?  9   TYR   A HD1  1 
ATOM   167  H HD2  A TYR   A 1 9   ? 12.876 -9.408  11.428  0.40 15.73 ?  9   TYR   A HD2  1 
ATOM   168  H HD2  B TYR   A 1 9   ? 13.146 -9.384  11.875  0.60 21.32 ?  9   TYR   A HD2  1 
ATOM   169  H HE1  A TYR   A 1 9   ? 13.989 -6.877  15.128  0.40 16.66 ?  9   TYR   A HE1  1 
ATOM   170  H HE1  B TYR   A 1 9   ? 14.104 -6.490  15.341  0.60 21.42 ?  9   TYR   A HE1  1 
ATOM   171  H HE2  A TYR   A 1 9   ? 14.303 -7.608  11.200  0.40 16.12 ?  9   TYR   A HE2  1 
ATOM   172  H HE2  B TYR   A 1 9   ? 14.378 -7.474  11.467  0.60 20.76 ?  9   TYR   A HE2  1 
ATOM   173  H HH   A TYR   A 1 9   ? 15.238 -5.630  13.765  0.40 17.62 ?  9   TYR   A HH   1 
ATOM   174  H HH   B TYR   A 1 9   ? 15.231 -5.255  13.838  0.60 21.98 ?  9   TYR   A HH   1 
ATOM   175  N N    A LEU   A 1 10  ? 8.936  -11.333 12.201  0.40 12.78 ?  10  LEU   A N    1 
ATOM   176  N N    B LEU   A 1 10  ? 9.215  -11.347 12.794  0.60 17.97 ?  10  LEU   A N    1 
ATOM   177  C CA   A LEU   A 1 10  ? 8.315  -12.545 11.698  0.40 12.86 ?  10  LEU   A CA   1 
ATOM   178  C CA   B LEU   A 1 10  ? 8.597  -12.557 12.277  0.60 17.72 ?  10  LEU   A CA   1 
ATOM   179  C C    A LEU   A 1 10  ? 9.412  -13.483 11.204  0.40 12.38 ?  10  LEU   A C    1 
ATOM   180  C C    B LEU   A 1 10  ? 9.682  -13.501 11.772  0.60 15.71 ?  10  LEU   A C    1 
ATOM   181  O O    A LEU   A 1 10  ? 10.344 -13.067 10.507  0.40 12.54 ?  10  LEU   A O    1 
ATOM   182  O O    B LEU   A 1 10  ? 10.624 -13.083 11.095  0.60 14.62 ?  10  LEU   A O    1 
ATOM   183  C CB   A LEU   A 1 10  ? 7.362  -12.208 10.549  0.40 14.04 ?  10  LEU   A CB   1 
ATOM   184  C CB   B LEU   A 1 10  ? 7.657  -12.186 11.129  0.60 19.89 ?  10  LEU   A CB   1 
ATOM   185  C CG   A LEU   A 1 10  ? 6.716  -13.433 9.893   0.40 15.95 ?  10  LEU   A CG   1 
ATOM   186  C CG   B LEU   A 1 10  ? 7.072  -13.349 10.328  0.60 22.53 ?  10  LEU   A CG   1 
ATOM   187  C CD1  A LEU   A 1 10  ? 5.641  -14.037 10.790  0.40 16.91 ?  10  LEU   A CD1  1 
ATOM   188  C CD1  B LEU   A 1 10  ? 5.980  -14.036 11.118  0.60 23.52 ?  10  LEU   A CD1  1 
ATOM   189  C CD2  A LEU   A 1 10  ? 6.152  -13.087 8.539   0.40 16.70 ?  10  LEU   A CD2  1 
ATOM   190  C CD2  B LEU   A 1 10  ? 6.554  -12.855 8.992   0.60 23.26 ?  10  LEU   A CD2  1 
ATOM   191  H H    A LEU   A 1 10  ? 9.043  -10.731 11.594  0.40 15.39 ?  10  LEU   A H    1 
ATOM   192  H H    B LEU   A 1 10  ? 9.197  -10.688 12.246  0.60 21.62 ?  10  LEU   A H    1 
ATOM   193  H HA   A LEU   A 1 10  ? 7.800  -12.980 12.404  0.40 15.49 ?  10  LEU   A HA   1 
ATOM   194  H HA   B LEU   A 1 10  ? 8.084  -12.999 12.971  0.60 21.32 ?  10  LEU   A HA   1 
ATOM   195  H HB2  A LEU   A 1 10  ? 6.640  -11.642 10.884  0.40 16.90 ?  10  LEU   A HB2  1 
ATOM   196  H HB2  B LEU   A 1 10  ? 6.908  -11.683 11.499  0.60 23.93 ?  10  LEU   A HB2  1 
ATOM   197  H HB3  A LEU   A 1 10  ? 7.851  -11.732 9.862   0.40 16.90 ?  10  LEU   A HB3  1 
ATOM   198  H HB3  B LEU   A 1 10  ? 8.141  -11.619 10.508  0.60 23.93 ?  10  LEU   A HB3  1 
ATOM   199  H HG   A LEU   A 1 10  ? 7.391  -14.114 9.758   0.40 19.20 ?  10  LEU   A HG   1 
ATOM   200  H HG   B LEU   A 1 10  ? 7.764  -14.003 10.150  0.60 27.10 ?  10  LEU   A HG   1 
ATOM   201  H HD11 A LEU   A 1 10  ? 5.313  -14.855 10.382  0.40 20.35 ?  10  LEU   A HD11 1 
ATOM   202  H HD11 B LEU   A 1 10  ? 5.636  -14.781 10.600  0.60 28.28 ?  10  LEU   A HD11 1 
ATOM   203  H HD12 A LEU   A 1 10  ? 6.026  -14.237 11.660  0.40 20.35 ?  10  LEU   A HD12 1 
ATOM   204  H HD12 B LEU   A 1 10  ? 6.342  -14.353 11.959  0.60 28.28 ?  10  LEU   A HD12 1 
ATOM   205  H HD13 A LEU   A 1 10  ? 4.916  -13.403 10.889  0.40 20.35 ?  10  LEU   A HD13 1 
ATOM   206  H HD13 B LEU   A 1 10  ? 5.270  -13.397 11.288  0.60 28.28 ?  10  LEU   A HD13 1 
ATOM   207  H HD21 A LEU   A 1 10  ? 5.751  -13.883 8.162   0.40 20.10 ?  10  LEU   A HD21 1 
ATOM   208  H HD21 B LEU   A 1 10  ? 6.177  -13.605 8.507   0.60 27.96 ?  10  LEU   A HD21 1 
ATOM   209  H HD22 A LEU   A 1 10  ? 5.490  -12.393 8.648   0.40 20.10 ?  10  LEU   A HD22 1 
ATOM   210  H HD22 B LEU   A 1 10  ? 5.873  -12.183 9.148   0.60 27.96 ?  10  LEU   A HD22 1 
ATOM   211  H HD23 A LEU   A 1 10  ? 6.878  -12.778 7.977   0.40 20.10 ?  10  LEU   A HD23 1 
ATOM   212  H HD23 B LEU   A 1 10  ? 7.291  -12.472 8.492   0.60 27.96 ?  10  LEU   A HD23 1 
ATOM   213  N N    A LYS   A 1 11  ? 9.293  -14.751 11.571  0.40 11.75 ?  11  LYS   A N    1 
ATOM   214  N N    B LYS   A 1 11  ? 9.555  -14.778 12.109  0.60 15.58 ?  11  LYS   A N    1 
ATOM   215  C CA   A LYS   A 1 11  ? 10.260 -15.769 11.188  0.40 11.78 ?  11  LYS   A CA   1 
ATOM   216  C CA   B LYS   A 1 11  ? 10.522 -15.787 11.695  0.60 15.17 ?  11  LYS   A CA   1 
ATOM   217  C C    A LYS   A 1 11  ? 9.893  -16.314 9.812   0.40 11.60 ?  11  LYS   A C    1 
ATOM   218  C C    B LYS   A 1 11  ? 10.100 -16.327 10.334  0.60 14.52 ?  11  LYS   A C    1 
ATOM   219  O O    A LYS   A 1 11  ? 8.748  -16.706 9.588   0.40 12.10 ?  11  LYS   A O    1 
ATOM   220  O O    B LYS   A 1 11  ? 9.052  -16.968 10.215  0.60 14.58 ?  11  LYS   A O    1 
ATOM   221  C CB   A LYS   A 1 11  ? 10.226 -16.876 12.241  0.40 12.08 ?  11  LYS   A CB   1 
ATOM   222  C CB   B LYS   A 1 11  ? 10.576 -16.901 12.734  0.60 15.43 ?  11  LYS   A CB   1 
ATOM   223  C CG   A LYS   A 1 11  ? 11.344 -17.892 12.179  0.40 13.01 ?  11  LYS   A CG   1 
ATOM   224  C CG   B LYS   A 1 11  ? 11.531 -18.025 12.386  0.60 16.40 ?  11  LYS   A CG   1 
ATOM   225  C CD   A LYS   A 1 11  ? 11.428 -18.637 13.510  0.40 13.27 ?  11  LYS   A CD   1 
ATOM   226  C CD   B LYS   A 1 11  ? 11.630 -19.008 13.541  0.60 16.98 ?  11  LYS   A CD   1 
ATOM   227  C CE   A LYS   A 1 11  ? 12.391 -19.812 13.458  0.40 13.24 ?  11  LYS   A CE   1 
ATOM   228  C CE   B LYS   A 1 11  ? 12.659 -20.092 13.279  0.60 17.35 ?  11  LYS   A CE   1 
ATOM   229  N NZ   A LYS   A 1 11  ? 13.775 -19.392 13.114  0.40 13.05 ?  11  LYS   A NZ   1 
ATOM   230  N NZ   B LYS   A 1 11  ? 14.018 -19.530 13.071  0.60 17.50 ?  11  LYS   A NZ   1 
ATOM   231  H H    A LYS   A 1 11  ? 8.644  -15.052 12.064  0.40 14.16 ?  11  LYS   A H    1 
ATOM   232  H H    B LYS   A 1 11  ? 8.910  -15.097 12.583  0.60 18.75 ?  11  LYS   A H    1 
ATOM   233  H HA   A LYS   A 1 11  ? 11.144 -15.381 11.152  0.40 14.19 ?  11  LYS   A HA   1 
ATOM   234  H HA   B LYS   A 1 11  ? 11.403 -15.383 11.615  0.60 18.27 ?  11  LYS   A HA   1 
ATOM   235  H HB2  A LYS   A 1 11  ? 10.257 -16.463 13.118  0.40 14.56 ?  11  LYS   A HB2  1 
ATOM   236  H HB2  B LYS   A 1 11  ? 10.865 -16.522 13.580  0.60 18.58 ?  11  LYS   A HB2  1 
ATOM   237  H HB3  A LYS   A 1 11  ? 9.388  -17.360 12.145  0.40 14.56 ?  11  LYS   A HB3  1 
ATOM   238  H HB3  B LYS   A 1 11  ? 9.691  -17.281 12.829  0.60 18.58 ?  11  LYS   A HB3  1 
ATOM   239  H HG2  A LYS   A 1 11  ? 11.159 -18.534 11.475  0.40 15.67 ?  11  LYS   A HG2  1 
ATOM   240  H HG2  B LYS   A 1 11  ? 11.199 -18.499 11.604  0.60 19.74 ?  11  LYS   A HG2  1 
ATOM   241  H HG3  A LYS   A 1 11  ? 12.185 -17.439 12.020  0.40 15.67 ?  11  LYS   A HG3  1 
ATOM   242  H HG3  B LYS   A 1 11  ? 12.411 -17.658 12.209  0.60 19.74 ?  11  LYS   A HG3  1 
ATOM   243  H HD2  A LYS   A 1 11  ? 11.734 -18.021 14.196  0.40 15.98 ?  11  LYS   A HD2  1 
ATOM   244  H HD2  B LYS   A 1 11  ? 11.891 -18.529 14.341  0.60 20.44 ?  11  LYS   A HD2  1 
ATOM   245  H HD3  A LYS   A 1 11  ? 10.547 -18.975 13.739  0.40 15.98 ?  11  LYS   A HD3  1 
ATOM   246  H HD3  B LYS   A 1 11  ? 10.768 -19.433 13.670  0.60 20.44 ?  11  LYS   A HD3  1 
ATOM   247  H HE2  A LYS   A 1 11  ? 12.414 -20.239 14.328  0.40 15.94 ?  11  LYS   A HE2  1 
ATOM   248  H HE2  B LYS   A 1 11  ? 12.692 -20.695 14.039  0.60 20.88 ?  11  LYS   A HE2  1 
ATOM   249  H HE3  A LYS   A 1 11  ? 12.090 -20.439 12.785  0.40 15.94 ?  11  LYS   A HE3  1 
ATOM   250  H HE3  B LYS   A 1 11  ? 12.409 -20.575 12.478  0.60 20.88 ?  11  LYS   A HE3  1 
ATOM   251  H HZ1  A LYS   A 1 11  ? 14.292 -20.108 13.011  0.40 15.71 ?  11  LYS   A HZ1  1 
ATOM   252  H HZ1  B LYS   A 1 11  ? 14.610 -20.189 12.978  0.60 21.06 ?  11  LYS   A HZ1  1 
ATOM   253  H HZ2  A LYS   A 1 11  ? 13.772 -18.925 12.356  0.40 15.71 ?  11  LYS   A HZ2  1 
ATOM   254  H HZ2  B LYS   A 1 11  ? 14.031 -19.027 12.336  0.60 21.06 ?  11  LYS   A HZ2  1 
ATOM   255  H HZ3  A LYS   A 1 11  ? 14.111 -18.884 13.763  0.40 15.71 ?  11  LYS   A HZ3  1 
ATOM   256  H HZ3  B LYS   A 1 11  ? 14.251 -19.030 13.768  0.60 21.06 ?  11  LYS   A HZ3  1 
ATOM   257  N N    A LEU   A 1 12  ? 10.852 -16.317 8.885   0.40 11.26 ?  12  LEU   A N    1 
ATOM   258  N N    B LEU   A 1 12  ? 10.906 -16.070 9.305   0.60 14.43 ?  12  LEU   A N    1 
ATOM   259  C CA   A LEU   A 1 12  ? 10.645 -16.902 7.560   0.40 11.42 ?  12  LEU   A CA   1 
ATOM   260  C CA   B LEU   A 1 12  ? 10.588 -16.598 7.984   0.60 14.51 ?  12  LEU   A CA   1 
ATOM   261  C C    A LEU   A 1 12  ? 11.272 -18.279 7.401   0.40 11.92 ?  12  LEU   A C    1 
ATOM   262  C C    B LEU   A 1 12  ? 11.145 -18.001 7.774   0.60 13.80 ?  12  LEU   A C    1 
ATOM   263  O O    A LEU   A 1 12  ? 10.655 -19.164 6.800   0.40 12.38 ?  12  LEU   A O    1 
ATOM   264  O O    B LEU   A 1 12  ? 10.472 -18.855 7.186   0.60 13.73 ?  12  LEU   A O    1 
ATOM   265  C CB   A LEU   A 1 12  ? 11.202 -15.993 6.463   0.40 11.63 ?  12  LEU   A CB   1 
ATOM   266  C CB   B LEU   A 1 12  ? 11.111 -15.660 6.895   0.60 15.03 ?  12  LEU   A CB   1 
ATOM   267  C CG   A LEU   A 1 12  ? 10.554 -14.628 6.245   0.40 12.45 ?  12  LEU   A CG   1 
ATOM   268  C CG   B LEU   A 1 12  ? 10.443 -14.289 6.793   0.60 15.18 ?  12  LEU   A CG   1 
ATOM   269  C CD1  A LEU   A 1 12  ? 11.257 -13.921 5.101   0.40 13.01 ?  12  LEU   A CD1  1 
ATOM   270  C CD1  B LEU   A 1 12  ? 11.071 -13.467 5.675   0.60 15.32 ?  12  LEU   A CD1  1 
ATOM   271  C CD2  A LEU   A 1 12  ? 9.058  -14.756 5.966   0.40 12.63 ?  12  LEU   A CD2  1 
ATOM   272  C CD2  B LEU   A 1 12  ? 8.950  -14.456 6.567   0.60 15.90 ?  12  LEU   A CD2  1 
ATOM   273  H H    A LEU   A 1 12  ? 11.628 -15.979 9.004   0.40 13.57 ?  12  LEU   A H    1 
ATOM   274  H H    B LEU   A 1 12  ? 11.627 -15.591 9.342   0.60 17.37 ?  12  LEU   A H    1 
ATOM   275  H HA   A LEU   A 1 12  ? 9.693  -17.003 7.413   0.40 13.76 ?  12  LEU   A HA   1 
ATOM   276  H HA   B LEU   A 1 12  ? 9.622  -16.646 7.898   0.60 17.47 ?  12  LEU   A HA   1 
ATOM   277  H HB2  A LEU   A 1 12  ? 12.136 -15.838 6.663   0.40 14.01 ?  12  LEU   A HB2  1 
ATOM   278  H HB2  B LEU   A 1 12  ? 12.053 -15.505 7.054   0.60 18.09 ?  12  LEU   A HB2  1 
ATOM   279  H HB3  A LEU   A 1 12  ? 11.133 -16.479 5.627   0.40 14.01 ?  12  LEU   A HB3  1 
ATOM   280  H HB3  B LEU   A 1 12  ? 10.994 -16.096 6.039   0.60 18.09 ?  12  LEU   A HB3  1 
ATOM   281  H HG   A LEU   A 1 12  ? 10.670 -14.095 7.045   0.40 15.00 ?  12  LEU   A HG   1 
ATOM   282  H HG   B LEU   A 1 12  ? 10.570 -13.805 7.625   0.60 18.28 ?  12  LEU   A HG   1 
ATOM   283  H HD11 A LEU   A 1 12  ? 10.845 -13.056 4.967   0.40 15.67 ?  12  LEU   A HD11 1 
ATOM   284  H HD11 B LEU   A 1 12  ? 10.631 -12.601 5.632   0.60 18.44 ?  12  LEU   A HD11 1 
ATOM   285  H HD12 A LEU   A 1 12  ? 12.195 -13.812 5.326   0.40 15.67 ?  12  LEU   A HD12 1 
ATOM   286  H HD12 B LEU   A 1 12  ? 12.015 -13.348 5.861   0.60 18.44 ?  12  LEU   A HD12 1 
ATOM   287  H HD13 A LEU   A 1 12  ? 11.171 -14.459 4.297   0.40 15.67 ?  12  LEU   A HD13 1 
ATOM   288  H HD13 B LEU   A 1 12  ? 10.955 -13.937 4.834   0.60 18.44 ?  12  LEU   A HD13 1 
ATOM   289  H HD21 A LEU   A 1 12  ? 8.698  -13.880 5.767   0.40 15.22 ?  12  LEU   A HD21 1 
ATOM   290  H HD21 B LEU   A 1 12  ? 8.573  -13.609 6.286   0.60 19.13 ?  12  LEU   A HD21 1 
ATOM   291  H HD22 A LEU   A 1 12  ? 8.925  -15.347 5.208   0.40 15.22 ?  12  LEU   A HD22 1 
ATOM   292  H HD22 B LEU   A 1 12  ? 8.810  -15.127 5.880   0.60 19.13 ?  12  LEU   A HD22 1 
ATOM   293  H HD23 A LEU   A 1 12  ? 8.618  -15.125 6.750   0.40 15.22 ?  12  LEU   A HD23 1 
ATOM   294  H HD23 B LEU   A 1 12  ? 8.537  -14.743 7.397   0.60 19.13 ?  12  LEU   A HD23 1 
ATOM   295  N N    A THR   A 1 13  ? 12.498 -18.466 7.888   0.40 12.33 ?  13  THR   A N    1 
ATOM   296  N N    B THR   A 1 13  ? 12.369 -18.246 8.232   0.60 13.81 ?  13  THR   A N    1 
ATOM   297  C CA   A THR   A 1 13  ? 13.192 -19.750 7.851   0.40 12.88 ?  13  THR   A CA   1 
ATOM   298  C CA   B THR   A 1 13  ? 13.031 -19.532 8.069   0.60 14.02 ?  13  THR   A CA   1 
ATOM   299  C C    A THR   A 1 13  ? 13.928 -19.926 9.174   0.40 12.99 ?  13  THR   A C    1 
ATOM   300  C C    B THR   A 1 13  ? 13.860 -19.807 9.317   0.60 14.77 ?  13  THR   A C    1 
ATOM   301  O O    A THR   A 1 13  ? 13.765 -19.140 10.113  0.40 13.32 ?  13  THR   A O    1 
ATOM   302  O O    B THR   A 1 13  ? 13.830 -19.057 10.297  0.60 14.92 ?  13  THR   A O    1 
ATOM   303  C CB   A THR   A 1 13  ? 14.190 -19.832 6.685   0.40 13.64 ?  13  THR   A CB   1 
ATOM   304  C CB   B THR   A 1 13  ? 13.950 -19.548 6.840   0.60 14.12 ?  13  THR   A CB   1 
ATOM   305  O OG1  A THR   A 1 13  ? 15.285 -18.939 6.925   0.40 13.77 ?  13  THR   A OG1  1 
ATOM   306  O OG1  B THR   A 1 13  ? 15.011 -18.613 7.039   0.60 14.16 ?  13  THR   A OG1  1 
ATOM   307  C CG2  A THR   A 1 13  ? 13.540 -19.468 5.370   0.40 14.30 ?  13  THR   A CG2  1 
ATOM   308  C CG2  B THR   A 1 13  ? 13.198 -19.216 5.561   0.60 15.03 ?  13  THR   A CG2  1 
ATOM   309  H H    A THR   A 1 13  ? 12.964 -17.849 8.258   0.40 14.85 ?  13  THR   A H    1 
ATOM   310  H H    B THR   A 1 13  ? 12.846 -17.663 8.647   0.60 16.63 ?  13  THR   A H    1 
ATOM   311  H HA   A THR   A 1 13  ? 12.550 -20.474 7.758   0.40 15.51 ?  13  THR   A HA   1 
ATOM   312  H HA   B THR   A 1 13  ? 12.365 -20.230 7.969   0.60 16.88 ?  13  THR   A HA   1 
ATOM   313  H HB   A THR   A 1 13  ? 14.520 -20.747 6.614   0.40 16.43 ?  13  THR   A HB   1 
ATOM   314  H HB   B THR   A 1 13  ? 14.330 -20.433 6.739   0.60 17.00 ?  13  THR   A HB   1 
ATOM   315  H HG1  A THR   A 1 13  ? 15.850 -19.004 6.300   0.40 16.58 ?  13  THR   A HG1  1 
ATOM   316  H HG1  B THR   A 1 13  ? 15.700 -19.007 7.301   0.60 17.05 ?  13  THR   A HG1  1 
ATOM   317  H HG21 A THR   A 1 13  ? 14.148 -19.662 4.639   0.40 17.22 ?  13  THR   A HG21 1 
ATOM   318  H HG21 B THR   A 1 13  ? 13.795 -19.297 4.797   0.60 18.09 ?  13  THR   A HG21 1 
ATOM   319  H HG22 A THR   A 1 13  ? 12.729 -19.983 5.251   0.40 17.22 ?  13  THR   A HG22 1 
ATOM   320  H HG22 B THR   A 1 13  ? 12.458 -19.834 5.444   0.60 18.09 ?  13  THR   A HG22 1 
ATOM   321  H HG23 A THR   A 1 13  ? 13.324 -18.525 5.362   0.40 17.22 ?  13  THR   A HG23 1 
ATOM   322  H HG23 B THR   A 1 13  ? 12.856 -18.313 5.599   0.60 18.09 ?  13  THR   A HG23 1 
ATOM   323  N N    A ASP   A 1 14  ? 14.767 -20.959 9.238   0.40 13.01 ?  14  ASP   A N    1 
ATOM   324  N N    B ASP   A 1 14  ? 14.636 -20.886 9.255   0.60 15.81 ?  14  ASP   A N    1 
ATOM   325  C CA   A ASP   A 1 14  ? 15.566 -21.197 10.433  0.40 12.70 ?  14  ASP   A CA   1 
ATOM   326  C CA   B ASP   A 1 14  ? 15.534 -21.219 10.352  0.60 16.95 ?  14  ASP   A CA   1 
ATOM   327  C C    A ASP   A 1 14  ? 16.336 -19.950 10.873  0.40 12.30 ?  14  ASP   A C    1 
ATOM   328  C C    B ASP   A 1 14  ? 16.454 -20.055 10.705  0.60 15.50 ?  14  ASP   A C    1 
ATOM   329  O O    A ASP   A 1 14  ? 16.469 -19.688 12.074  0.40 12.75 ?  14  ASP   A O    1 
ATOM   330  O O    B ASP   A 1 14  ? 16.798 -19.874 11.878  0.60 15.68 ?  14  ASP   A O    1 
ATOM   331  C CB   A ASP   A 1 14  ? 16.533 -22.348 10.163  0.40 13.56 ?  14  ASP   A CB   1 
ATOM   332  C CB   B ASP   A 1 14  ? 16.379 -22.436 9.969   0.60 20.09 ?  14  ASP   A CB   1 
ATOM   333  C CG   A ASP   A 1 14  ? 17.411 -22.641 11.344  0.40 15.70 ?  14  ASP   A CG   1 
ATOM   334  C CG   B ASP   A 1 14  ? 17.095 -23.050 11.158  0.60 23.24 ?  14  ASP   A CG   1 
ATOM   335  O OD1  A ASP   A 1 14  ? 16.875 -23.123 12.363  0.40 16.02 ?  14  ASP   A OD1  1 
ATOM   336  O OD1  B ASP   A 1 14  ? 16.412 -23.596 12.048  0.60 24.52 ?  14  ASP   A OD1  1 
ATOM   337  O OD2  A ASP   A 1 14  ? 18.628 -22.382 11.254  0.40 17.57 -1 14  ASP   A OD2  1 
ATOM   338  O OD2  B ASP   A 1 14  ? 18.342 -22.998 11.196  0.60 24.61 -1 14  ASP   A OD2  1 
ATOM   339  H H    A ASP   A 1 14  ? 14.900 -21.533 8.609   0.40 15.67 ?  14  ASP   A H    1 
ATOM   340  H H    B ASP   A 1 14  ? 14.671 -21.420 8.583   0.60 19.03 ?  14  ASP   A H    1 
ATOM   341  H HA   A ASP   A 1 14  ? 14.987 -21.460 11.162  0.40 15.29 ?  14  ASP   A HA   1 
ATOM   342  H HA   B ASP   A 1 14  ? 15.001 -21.451 11.129  0.60 20.40 ?  14  ASP   A HA   1 
ATOM   343  H HB2  A ASP   A 1 14  ? 16.021 -23.153 9.963   0.40 16.32 ?  14  ASP   A HB2  1 
ATOM   344  H HB2  B ASP   A 1 14  ? 15.803 -23.103 9.554   0.60 24.17 ?  14  ASP   A HB2  1 
ATOM   345  H HB3  A ASP   A 1 14  ? 17.099 -22.126 9.407   0.40 16.32 ?  14  ASP   A HB3  1 
ATOM   346  H HB3  B ASP   A 1 14  ? 17.066 -22.159 9.348   0.60 24.17 ?  14  ASP   A HB3  1 
ATOM   347  N N    A ASN   A 1 15  ? 16.841 -19.161 9.922   0.40 12.13 ?  15  ASN   A N    1 
ATOM   348  N N    B ASN   A 1 15  ? 16.861 -19.252 9.714   0.60 14.25 ?  15  ASN   A N    1 
ATOM   349  C CA   A ASN   A 1 15  ? 17.786 -18.093 10.236  0.40 12.31 ?  15  ASN   A CA   1 
ATOM   350  C CA   B ASN   A 1 15  ? 17.876 -18.225 9.937   0.60 13.61 ?  15  ASN   A CA   1 
ATOM   351  C C    A ASN   A 1 15  ? 17.395 -16.716 9.718   0.40 12.23 ?  15  ASN   A C    1 
ATOM   352  C C    B ASN   A 1 15  ? 17.507 -16.824 9.459   0.60 13.88 ?  15  ASN   A C    1 
ATOM   353  O O    A ASN   A 1 15  ? 18.066 -15.741 10.078  0.40 12.20 ?  15  ASN   A O    1 
ATOM   354  O O    B ASN   A 1 15  ? 18.338 -15.916 9.585   0.60 14.02 ?  15  ASN   A O    1 
ATOM   355  C CB   A ASN   A 1 15  ? 19.180 -18.428 9.680   0.40 12.32 ?  15  ASN   A CB   1 
ATOM   356  C CB   B ASN   A 1 15  ? 19.223 -18.631 9.304   0.60 12.83 ?  15  ASN   A CB   1 
ATOM   357  C CG   A ASN   A 1 15  ? 19.180 -18.576 8.172   0.40 11.84 ?  15  ASN   A CG   1 
ATOM   358  C CG   B ASN   A 1 15  ? 19.167 -18.687 7.788   0.60 12.83 ?  15  ASN   A CG   1 
ATOM   359  O OD1  A ASN   A 1 15  ? 18.553 -19.490 7.631   0.40 11.86 ?  15  ASN   A OD1  1 
ATOM   360  O OD1  B ASN   A 1 15  ? 18.351 -19.411 7.217   0.60 13.14 ?  15  ASN   A OD1  1 
ATOM   361  N ND2  A ASN   A 1 15  ? 19.872 -17.669 7.480   0.40 11.81 ?  15  ASN   A ND2  1 
ATOM   362  N ND2  B ASN   A 1 15  ? 20.022 -17.915 7.128   0.60 13.00 ?  15  ASN   A ND2  1 
ATOM   363  H H    A ASN   A 1 15  ? 16.651 -19.218 9.092   0.40 14.61 ?  15  ASN   A H    1 
ATOM   364  H H    B ASN   A 1 15  ? 16.566 -19.294 8.914   0.60 17.15 ?  15  ASN   A H    1 
ATOM   365  H HA   A ASN   A 1 15  ? 17.875 -18.024 11.203  0.40 14.82 ?  15  ASN   A HA   1 
ATOM   366  H HA   B ASN   A 1 15  ? 18.024 -18.160 10.892  0.60 16.39 ?  15  ASN   A HA   1 
ATOM   367  H HB2  A ASN   A 1 15  ? 19.796 -17.710 9.914   0.40 14.84 ?  15  ASN   A HB2  1 
ATOM   368  H HB2  B ASN   A 1 15  ? 19.895 -17.976 9.562   0.60 15.46 ?  15  ASN   A HB2  1 
ATOM   369  H HB3  A ASN   A 1 15  ? 19.483 -19.262 10.064  0.40 14.84 ?  15  ASN   A HB3  1 
ATOM   370  H HB3  B ASN   A 1 15  ? 19.476 -19.507 9.635   0.60 15.46 ?  15  ASN   A HB3  1 
ATOM   371  H HD21 A ASN   A 1 15  ? 19.899 -17.709 6.618   0.40 14.23 ?  15  ASN   A HD21 1 
ATOM   372  H HD21 B ASN   A 1 15  ? 20.024 -17.919 6.268   0.60 15.65 ?  15  ASN   A HD21 1 
ATOM   373  H HD22 A ASN   A 1 15  ? 20.298 -17.042 7.889   0.40 14.23 ?  15  ASN   A HD22 1 
ATOM   374  H HD22 B ASN   A 1 15  ? 20.582 -17.421 7.556   0.60 15.65 ?  15  ASN   A HD22 1 
ATOM   375  N N    A VAL   A 1 16  ? 16.357 -16.600 8.889   0.40 12.48 ?  16  VAL   A N    1 
ATOM   376  N N    B VAL   A 1 16  ? 16.305 -16.607 8.934   0.60 14.11 ?  16  VAL   A N    1 
ATOM   377  C CA   A VAL   A 1 16  ? 15.954 -15.340 8.269   0.40 12.36 ?  16  VAL   A CA   1 
ATOM   378  C CA   B VAL   A 1 16  ? 15.905 -15.304 8.413   0.60 13.59 ?  16  VAL   A CA   1 
ATOM   379  C C    A VAL   A 1 16  ? 14.659 -14.843 8.900   0.40 12.10 ?  16  VAL   A C    1 
ATOM   380  C C    B VAL   A 1 16  ? 14.687 -14.803 9.184   0.60 13.35 ?  16  VAL   A C    1 
ATOM   381  O O    A VAL   A 1 16  ? 13.643 -15.555 8.924   0.40 11.86 ?  16  VAL   A O    1 
ATOM   382  O O    B VAL   A 1 16  ? 13.690 -15.526 9.340   0.60 13.52 ?  16  VAL   A O    1 
ATOM   383  C CB   A VAL   A 1 16  ? 15.804 -15.467 6.745   0.40 13.02 ?  16  VAL   A CB   1 
ATOM   384  C CB   B VAL   A 1 16  ? 15.651 -15.343 6.894   0.60 13.65 ?  16  VAL   A CB   1 
ATOM   385  C CG1  A VAL   A 1 16  ? 15.382 -14.126 6.146   0.40 13.39 ?  16  VAL   A CG1  1 
ATOM   386  C CG1  B VAL   A 1 16  ? 15.207 -13.972 6.384   0.60 13.91 ?  16  VAL   A CG1  1 
ATOM   387  C CG2  A VAL   A 1 16  ? 17.100 -15.952 6.123   0.40 13.65 ?  16  VAL   A CG2  1 
ATOM   388  C CG2  B VAL   A 1 16  ? 16.900 -15.807 6.150   0.60 14.36 ?  16  VAL   A CG2  1 
ATOM   389  H H    A VAL   A 1 16  ? 15.861 -17.262 8.670   0.40 15.04 ?  16  VAL   A H    1 
ATOM   390  H H    B VAL   A 1 16  ? 15.688 -17.206 8.878   0.60 16.98 ?  16  VAL   A H    1 
ATOM   391  H HA   A VAL   A 1 16  ? 16.640 -14.676 8.441   0.40 14.88 ?  16  VAL   A HA   1 
ATOM   392  H HA   B VAL   A 1 16  ? 16.628 -14.676 8.566   0.60 16.37 ?  16  VAL   A HA   1 
ATOM   393  H HB   A VAL   A 1 16  ? 15.114 -16.121 6.548   0.40 15.68 ?  16  VAL   A HB   1 
ATOM   394  H HB   B VAL   A 1 16  ? 14.943 -15.977 6.709   0.60 16.43 ?  16  VAL   A HB   1 
ATOM   395  H HG11 A VAL   A 1 16  ? 15.498 -14.162 5.185   0.40 16.13 ?  16  VAL   A HG11 1 
ATOM   396  H HG11 B VAL   A 1 16  ? 15.228 -13.978 5.412   0.60 16.75 ?  16  VAL   A HG11 1 
ATOM   397  H HG12 A VAL   A 1 16  ? 14.449 -13.963 6.359   0.40 16.13 ?  16  VAL   A HG12 1 
ATOM   398  H HG12 B VAL   A 1 16  ? 14.305 -13.797 6.691   0.60 16.75 ?  16  VAL   A HG12 1 
ATOM   399  H HG13 A VAL   A 1 16  ? 15.936 -13.425 6.521   0.40 16.13 ?  16  VAL   A HG13 1 
ATOM   400  H HG13 B VAL   A 1 16  ? 15.813 -13.296 6.722   0.60 16.75 ?  16  VAL   A HG13 1 
ATOM   401  H HG21 A VAL   A 1 16  ? 17.004 -15.954 5.158   0.40 16.44 ?  16  VAL   A HG21 1 
ATOM   402  H HG21 B VAL   A 1 16  ? 16.729 -15.778 5.195   0.60 17.29 ?  16  VAL   A HG21 1 
ATOM   403  H HG22 A VAL   A 1 16  ? 17.817 -15.351 6.382   0.40 16.44 ?  16  VAL   A HG22 1 
ATOM   404  H HG22 B VAL   A 1 16  ? 17.639 -15.216 6.370   0.60 17.29 ?  16  VAL   A HG22 1 
ATOM   405  H HG23 A VAL   A 1 16  ? 17.289 -16.848 6.440   0.40 16.44 ?  16  VAL   A HG23 1 
ATOM   406  H HG23 B VAL   A 1 16  ? 17.113 -16.714 6.420   0.60 17.29 ?  16  VAL   A HG23 1 
ATOM   407  N N    A TYR   A 1 17  ? 14.693 -13.589 9.350   0.40 12.22 ?  17  TYR   A N    1 
ATOM   408  N N    B TYR   A 1 17  ? 14.772 -13.545 9.633   0.60 13.44 ?  17  TYR   A N    1 
ATOM   409  C CA   A TYR   A 1 17  ? 13.578 -12.908 9.982   0.40 12.05 ?  17  TYR   A CA   1 
ATOM   410  C CA   B TYR   A 1 17  ? 13.746 -12.876 10.418  0.60 13.12 ?  17  TYR   A CA   1 
ATOM   411  C C    A TYR   A 1 17  ? 13.321 -11.600 9.240   0.40 11.36 ?  17  TYR   A C    1 
ATOM   412  C C    B TYR   A 1 17  ? 13.450 -11.527 9.781   0.60 12.81 ?  17  TYR   A C    1 
ATOM   413  O O    A TYR   A 1 17  ? 14.208 -11.057 8.572   0.40 11.09 ?  17  TYR   A O    1 
ATOM   414  O O    B TYR   A 1 17  ? 14.328 -10.925 9.158   0.60 12.40 ?  17  TYR   A O    1 
ATOM   415  C CB   A TYR   A 1 17  ? 13.903 -12.620 11.456  0.40 12.27 ?  17  TYR   A CB   1 
ATOM   416  C CB   B TYR   A 1 17  ? 14.232 -12.656 11.851  0.60 13.05 ?  17  TYR   A CB   1 
ATOM   417  C CG   A TYR   A 1 17  ? 14.076 -13.869 12.289  0.40 13.07 ?  17  TYR   A CG   1 
ATOM   418  C CG   B TYR   A 1 17  ? 14.422 -13.937 12.634  0.60 13.38 ?  17  TYR   A CG   1 
ATOM   419  C CD1  A TYR   A 1 17  ? 15.253 -14.606 12.248  0.40 13.95 ?  17  TYR   A CD1  1 
ATOM   420  C CD1  B TYR   A 1 17  ? 15.585 -14.692 12.512  0.60 14.41 ?  17  TYR   A CD1  1 
ATOM   421  C CD2  A TYR   A 1 17  ? 13.054 -14.321 13.109  0.40 13.12 ?  17  TYR   A CD2  1 
ATOM   422  C CD2  B TYR   A 1 17  ? 13.433 -14.398 13.491  0.60 13.61 ?  17  TYR   A CD2  1 
ATOM   423  C CE1  A TYR   A 1 17  ? 15.406 -15.761 13.006  0.40 14.14 ?  17  TYR   A CE1  1 
ATOM   424  C CE1  B TYR   A 1 17  ? 15.753 -15.873 13.226  0.60 15.13 ?  17  TYR   A CE1  1 
ATOM   425  C CE2  A TYR   A 1 17  ? 13.195 -15.475 13.868  0.40 13.61 ?  17  TYR   A CE2  1 
ATOM   426  C CE2  B TYR   A 1 17  ? 13.592 -15.573 14.209  0.60 14.18 ?  17  TYR   A CE2  1 
ATOM   427  C CZ   A TYR   A 1 17  ? 14.374 -16.190 13.816  0.40 14.26 ?  17  TYR   A CZ   1 
ATOM   428  C CZ   B TYR   A 1 17  ? 14.751 -16.306 14.075  0.60 14.73 ?  17  TYR   A CZ   1 
ATOM   429  O OH   A TYR   A 1 17  ? 14.510 -17.334 14.574  0.40 14.90 ?  17  TYR   A OH   1 
ATOM   430  O OH   B TYR   A 1 17  ? 14.904 -17.472 14.792  0.60 15.23 ?  17  TYR   A OH   1 
ATOM   431  H H    A TYR   A 1 17  ? 15.394 -13.094 9.294   0.40 14.72 ?  17  TYR   A H    1 
ATOM   432  H H    B TYR   A 1 17  ? 15.453 -13.026 9.468   0.60 16.18 ?  17  TYR   A H    1 
ATOM   433  H HA   A TYR   A 1 17  ? 12.784 -13.467 9.940   0.40 14.52 ?  17  TYR   A HA   1 
ATOM   434  H HA   B TYR   A 1 17  ? 12.938 -13.401 10.422  0.60 15.80 ?  17  TYR   A HA   1 
ATOM   435  H HB2  A TYR   A 1 17  ? 14.725 -12.114 11.505  0.40 14.79 ?  17  TYR   A HB2  1 
ATOM   436  H HB2  B TYR   A 1 17  ? 15.088 -12.197 11.821  0.60 15.72 ?  17  TYR   A HB2  1 
ATOM   437  H HB3  A TYR   A 1 17  ? 13.175 -12.109 11.839  0.40 14.79 ?  17  TYR   A HB3  1 
ATOM   438  H HB3  B TYR   A 1 17  ? 13.586 -12.114 12.321  0.60 15.72 ?  17  TYR   A HB3  1 
ATOM   439  H HD1  A TYR   A 1 17  ? 15.950 -14.322 11.706  0.40 16.80 ?  17  TYR   A HD1  1 
ATOM   440  H HD1  B TYR   A 1 17  ? 16.261 -14.405 11.937  0.60 17.35 ?  17  TYR   A HD1  1 
ATOM   441  H HD2  A TYR   A 1 17  ? 12.253 -13.851 13.151  0.40 15.80 ?  17  TYR   A HD2  1 
ATOM   442  H HD2  B TYR   A 1 17  ? 12.648 -13.911 13.584  0.60 16.39 ?  17  TYR   A HD2  1 
ATOM   443  H HE1  A TYR   A 1 17  ? 16.205 -16.241 12.970  0.40 17.02 ?  17  TYR   A HE1  1 
ATOM   444  H HE1  B TYR   A 1 17  ? 16.537 -16.368 13.131  0.60 18.21 ?  17  TYR   A HE1  1 
ATOM   445  H HE2  A TYR   A 1 17  ? 12.500 -15.766 14.416  0.40 16.39 ?  17  TYR   A HE2  1 
ATOM   446  H HE2  B TYR   A 1 17  ? 12.920 -15.867 14.776  0.60 17.07 ?  17  TYR   A HE2  1 
ATOM   447  H HH   A TYR   A 1 17  ? 13.804 -17.481 15.001  0.40 17.93 ?  17  TYR   A HH   1 
ATOM   448  H HH   B TYR   A 1 17  ? 15.643 -17.828 14.605  0.60 18.33 ?  17  TYR   A HH   1 
ATOM   449  N N    A ILE   A 1 18  ? 12.100 -11.075 9.374   0.40 10.74 ?  18  ILE   A N    1 
ATOM   450  N N    B ILE   A 1 18  ? 12.219 -11.029 9.941   0.60 12.72 ?  18  ILE   A N    1 
ATOM   451  C CA   A ILE   A 1 18  ? 11.702 -9.895  8.611   0.40 10.82 ?  18  ILE   A CA   1 
ATOM   452  C CA   B ILE   A 1 18  ? 11.812 -9.807  9.251   0.60 12.55 ?  18  ILE   A CA   1 
ATOM   453  C C    A ILE   A 1 18  ? 10.739 -9.046  9.431   0.40 10.95 ?  18  ILE   A C    1 
ATOM   454  C C    B ILE   A 1 18  ? 10.892 -8.965  10.127  0.60 12.54 ?  18  ILE   A C    1 
ATOM   455  O O    A ILE   A 1 18  ? 9.917  -9.567  10.187  0.40 11.02 ?  18  ILE   A O    1 
ATOM   456  O O    B ILE   A 1 18  ? 10.081 -9.488  10.899  0.60 13.04 ?  18  ILE   A O    1 
ATOM   457  C CB   A ILE   A 1 18  ? 11.129 -10.306 7.232   0.40 11.37 ?  18  ILE   A CB   1 
ATOM   458  C CB   B ILE   A 1 18  ? 11.174 -10.129 7.878   0.60 12.48 ?  18  ILE   A CB   1 
ATOM   459  C CG1  A ILE   A 1 18  ? 11.016 -9.095  6.309   0.40 11.55 ?  18  ILE   A CG1  1 
ATOM   460  C CG1  B ILE   A 1 18  ? 11.062 -8.876  7.007   0.60 12.73 ?  18  ILE   A CG1  1 
ATOM   461  C CG2  A ILE   A 1 18  ? 9.797  -11.043 7.386   0.40 11.53 ?  18  ILE   A CG2  1 
ATOM   462  C CG2  B ILE   A 1 18  ? 9.821  -10.821 8.051   0.60 12.35 ?  18  ILE   A CG2  1 
ATOM   463  C CD1  A ILE   A 1 18  ? 10.726 -9.469  4.872   0.40 12.67 ?  18  ILE   A CD1  1 
ATOM   464  C CD1  B ILE   A 1 18  ? 10.806 -9.214  5.565   0.60 13.96 ?  18  ILE   A CD1  1 
ATOM   465  H H    A ILE   A 1 18  ? 11.496 -11.385 9.910   0.40 12.95 ?  18  ILE   A H    1 
ATOM   466  H H    B ILE   A 1 18  ? 11.606 -11.375 10.437  0.60 15.32 ?  18  ILE   A H    1 
ATOM   467  H HA   A ILE   A 1 18  ? 12.487 -9.361  8.454   0.40 13.04 ?  18  ILE   A HA   1 
ATOM   468  H HA   B ILE   A 1 18  ? 12.605 -9.277  9.071   0.60 15.12 ?  18  ILE   A HA   1 
ATOM   469  H HB   A ILE   A 1 18  ? 11.756 -10.925 6.834   0.40 13.70 ?  18  ILE   A HB   1 
ATOM   470  H HB   B ILE   A 1 18  ? 11.760 -10.743 7.416   0.60 15.03 ?  18  ILE   A HB   1 
ATOM   471  H HG12 A ILE   A 1 18  ? 10.296 -8.527  6.621   0.40 13.92 ?  18  ILE   A HG12 1 
ATOM   472  H HG12 B ILE   A 1 18  ? 10.326 -8.327  7.320   0.60 15.34 ?  18  ILE   A HG12 1 
ATOM   473  H HG13 A ILE   A 1 18  ? 11.855 -8.611  6.327   0.40 13.92 ?  18  ILE   A HG13 1 
ATOM   474  H HG13 B ILE   A 1 18  ? 11.893 -8.376  7.052   0.60 15.34 ?  18  ILE   A HG13 1 
ATOM   475  H HG21 A ILE   A 1 18  ? 9.542  -11.416 6.526   0.40 13.90 ?  18  ILE   A HG21 1 
ATOM   476  H HG21 B ILE   A 1 18  ? 9.527  -11.160 7.187   0.60 14.88 ?  18  ILE   A HG21 1 
ATOM   477  H HG22 A ILE   A 1 18  ? 9.901  -11.760 8.034   0.40 13.90 ?  18  ILE   A HG22 1 
ATOM   478  H HG22 B ILE   A 1 18  ? 9.923  -11.554 8.674   0.60 14.88 ?  18  ILE   A HG22 1 
ATOM   479  H HG23 A ILE   A 1 18  ? 9.118  -10.421 7.690   0.40 13.90 ?  18  ILE   A HG23 1 
ATOM   480  H HG23 B ILE   A 1 18  ? 9.175  -10.182 8.389   0.60 14.88 ?  18  ILE   A HG23 1 
ATOM   481  H HD11 A ILE   A 1 18  ? 10.735 -8.664  4.331   0.40 15.27 ?  18  ILE   A HD11 1 
ATOM   482  H HD11 B ILE   A 1 18  ? 10.803 -8.398  5.043   0.60 16.81 ?  18  ILE   A HD11 1 
ATOM   483  H HD12 A ILE   A 1 18  ? 11.406 -10.086 4.562   0.40 15.27 ?  18  ILE   A HD12 1 
ATOM   484  H HD12 B ILE   A 1 18  ? 11.509 -9.805  5.252   0.60 16.81 ?  18  ILE   A HD12 1 
ATOM   485  H HD13 A ILE   A 1 18  ? 9.852  -9.889  4.824   0.40 15.27 ?  18  ILE   A HD13 1 
ATOM   486  H HD13 B ILE   A 1 18  ? 9.946  -9.657  5.494   0.60 16.81 ?  18  ILE   A HD13 1 
ATOM   487  N N    A LYS   A 1 19  ? 10.834 -7.725  9.263   0.40 11.07 ?  19  LYS   A N    1 
ATOM   488  N N    B LYS   A 1 19  ? 11.017 -7.641  9.987   0.60 12.58 ?  19  LYS   A N    1 
ATOM   489  C CA   A LYS   A 1 19  ? 10.026 -6.781  10.026  0.40 11.77 ?  19  LYS   A CA   1 
ATOM   490  C CA   B LYS   A 1 19  ? 10.232 -6.697  10.774  0.60 13.37 ?  19  LYS   A CA   1 
ATOM   491  C C    A LYS   A 1 19  ? 9.804  -5.519  9.200   0.40 11.79 ?  19  LYS   A C    1 
ATOM   492  C C    B LYS   A 1 19  ? 9.980  -5.444  9.951   0.60 13.49 ?  19  LYS   A C    1 
ATOM   493  O O    A LYS   A 1 19  ? 10.677 -5.102  8.431   0.40 11.77 ?  19  LYS   A O    1 
ATOM   494  O O    B LYS   A 1 19  ? 10.848 -5.015  9.190   0.60 13.73 ?  19  LYS   A O    1 
ATOM   495  C CB   A LYS   A 1 19  ? 10.725 -6.438  11.353  0.40 12.41 ?  19  LYS   A CB   1 
ATOM   496  C CB   B LYS   A 1 19  ? 10.972 -6.328  12.067  0.60 14.08 ?  19  LYS   A CB   1 
ATOM   497  C CG   A LYS   A 1 19  ? 9.966  -5.531  12.317  0.40 13.49 ?  19  LYS   A CG   1 
ATOM   498  C CG   B LYS   A 1 19  ? 10.263 -5.357  12.995  0.60 14.86 ?  19  LYS   A CG   1 
ATOM   499  C CD   A LYS   A 1 19  ? 10.801 -5.301  13.580  0.40 14.37 ?  19  LYS   A CD   1 
ATOM   500  C CD   B LYS   A 1 19  ? 11.185 -4.987  14.156  0.60 15.67 ?  19  LYS   A CD   1 
ATOM   501  C CE   A LYS   A 1 19  ? 10.136 -4.340  14.556  0.40 14.63 ?  19  LYS   A CE   1 
ATOM   502  C CE   B LYS   A 1 19  ? 10.499 -4.117  15.197  0.60 16.20 ?  19  LYS   A CE   1 
ATOM   503  N NZ   A LYS   A 1 19  ? 10.996 -4.074  15.748  0.40 14.77 ?  19  LYS   A NZ   1 
ATOM   504  N NZ   B LYS   A 1 19  ? 11.364 -3.932  16.402  0.60 16.65 ?  19  LYS   A NZ   1 
ATOM   505  H H    A LYS   A 1 19  ? 11.368 -7.353  8.712   0.40 13.34 ?  19  LYS   A H    1 
ATOM   506  H H    B LYS   A 1 19  ? 11.568 -7.251  9.435   0.60 15.15 ?  19  LYS   A H    1 
ATOM   507  H HA   A LYS   A 1 19  ? 9.162  -7.180  10.232  0.40 14.18 ?  19  LYS   A HA   1 
ATOM   508  H HA   B LYS   A 1 19  ? 9.380  -7.092  11.001  0.60 16.10 ?  19  LYS   A HA   1 
ATOM   509  H HB2  A LYS   A 1 19  ? 10.901 -7.265  11.829  0.40 14.94 ?  19  LYS   A HB2  1 
ATOM   510  H HB2  B LYS   A 1 19  ? 11.126 -7.141  12.569  0.60 16.96 ?  19  LYS   A HB2  1 
ATOM   511  H HB3  A LYS   A 1 19  ? 11.564 -5.999  11.152  0.40 14.94 ?  19  LYS   A HB3  1 
ATOM   512  H HB3  B LYS   A 1 19  ? 11.824 -5.928  11.830  0.60 16.96 ?  19  LYS   A HB3  1 
ATOM   513  H HG2  A LYS   A 1 19  ? 9.802  -4.672  11.900  0.40 16.25 ?  19  LYS   A HG2  1 
ATOM   514  H HG2  B LYS   A 1 19  ? 10.037 -4.546  12.514  0.60 17.89 ?  19  LYS   A HG2  1 
ATOM   515  H HG3  A LYS   A 1 19  ? 9.131  -5.951  12.577  0.40 16.25 ?  19  LYS   A HG3  1 
ATOM   516  H HG3  B LYS   A 1 19  ? 9.466  -5.774  13.356  0.60 17.89 ?  19  LYS   A HG3  1 
ATOM   517  H HD2  A LYS   A 1 19  ? 10.930 -6.148  14.037  0.40 17.30 ?  19  LYS   A HD2  1 
ATOM   518  H HD2  B LYS   A 1 19  ? 11.479 -5.800  14.594  0.60 18.86 ?  19  LYS   A HD2  1 
ATOM   519  H HD3  A LYS   A 1 19  ? 11.660 -4.925  13.330  0.40 17.30 ?  19  LYS   A HD3  1 
ATOM   520  H HD3  B LYS   A 1 19  ? 11.951 -4.500  13.810  0.60 18.86 ?  19  LYS   A HD3  1 
ATOM   521  H HE2  A LYS   A 1 19  ? 9.969  -3.495  14.111  0.40 17.61 ?  19  LYS   A HE2  1 
ATOM   522  H HE2  B LYS   A 1 19  ? 10.318 -3.243  14.816  0.60 19.50 ?  19  LYS   A HE2  1 
ATOM   523  H HE3  A LYS   A 1 19  ? 9.301  -4.725  14.867  0.40 17.61 ?  19  LYS   A HE3  1 
ATOM   524  H HE3  B LYS   A 1 19  ? 9.674  -4.540  15.477  0.60 19.50 ?  19  LYS   A HE3  1 
ATOM   525  H HZ1  A LYS   A 1 19  ? 10.586 -3.511  16.302  0.40 17.78 ?  19  LYS   A HZ1  1 
ATOM   526  H HZ1  B LYS   A 1 19  ? 10.944 -3.430  17.005  0.60 20.04 ?  19  LYS   A HZ1  1 
ATOM   527  H HZ2  A LYS   A 1 19  ? 11.162 -4.835  16.180  0.40 17.78 ?  19  LYS   A HZ2  1 
ATOM   528  H HZ2  B LYS   A 1 19  ? 11.553 -4.723  16.764  0.60 20.04 ?  19  LYS   A HZ2  1 
ATOM   529  H HZ3  A LYS   A 1 19  ? 11.769 -3.714  15.492  0.40 17.78 ?  19  LYS   A HZ3  1 
ATOM   530  H HZ3  B LYS   A 1 19  ? 12.125 -3.531  16.172  0.60 20.04 ?  19  LYS   A HZ3  1 
ATOM   531  N N    A ASN   A 1 20  ? 8.620  -4.921  9.353   0.40 12.56 ?  20  ASN   A N    1 
ATOM   532  N N    B ASN   A 1 20  ? 8.797  -4.858  10.107  0.60 14.50 ?  20  ASN   A N    1 
ATOM   533  C CA   A ASN   A 1 20  ? 8.335  -3.604  8.780   0.40 13.76 ?  20  ASN   A CA   1 
ATOM   534  C CA   B ASN   A 1 20  ? 8.515  -3.550  9.522   0.60 15.56 ?  20  ASN   A CA   1 
ATOM   535  C C    A ASN   A 1 20  ? 8.898  -2.553  9.728   0.40 14.63 ?  20  ASN   A C    1 
ATOM   536  C C    B ASN   A 1 20  ? 9.146  -2.521  10.449  0.60 15.56 ?  20  ASN   A C    1 
ATOM   537  O O    A ASN   A 1 20  ? 8.292  -2.240  10.754  0.40 15.28 ?  20  ASN   A O    1 
ATOM   538  O O    B ASN   A 1 20  ? 8.635  -2.250  11.536  0.60 16.09 ?  20  ASN   A O    1 
ATOM   539  C CB   A ASN   A 1 20  ? 6.833  -3.420  8.582   0.40 14.31 ?  20  ASN   A CB   1 
ATOM   540  C CB   B ASN   A 1 20  ? 7.009  -3.346  9.379   0.60 16.77 ?  20  ASN   A CB   1 
ATOM   541  C CG   A ASN   A 1 20  ? 6.459  -1.996  8.199   0.40 15.32 ?  20  ASN   A CG   1 
ATOM   542  C CG   B ASN   A 1 20  ? 6.633  -1.908  9.068   0.60 17.99 ?  20  ASN   A CG   1 
ATOM   543  O OD1  A ASN   A 1 20  ? 5.493  -1.436  8.724   0.40 16.10 ?  20  ASN   A OD1  1 
ATOM   544  O OD1  B ASN   A 1 20  ? 5.773  -1.320  9.737   0.60 19.29 ?  20  ASN   A OD1  1 
ATOM   545  N ND2  A ASN   A 1 20  ? 7.225  -1.403  7.285   0.40 16.03 ?  20  ASN   A ND2  1 
ATOM   546  N ND2  B ASN   A 1 20  ? 7.266  -1.335  8.046   0.60 18.41 ?  20  ASN   A ND2  1 
ATOM   547  H H    A ASN   A 1 20  ? 7.956  -5.266  9.785   0.40 15.13 ?  20  ASN   A H    1 
ATOM   548  H H    B ASN   A 1 20  ? 8.147  -5.191  10.549  0.60 17.46 ?  20  ASN   A H    1 
ATOM   549  H HA   A ASN   A 1 20  ? 8.777  -3.523  7.927   0.40 16.56 ?  20  ASN   A HA   1 
ATOM   550  H HA   B ASN   A 1 20  ? 8.929  -3.481  8.644   0.60 18.72 ?  20  ASN   A HA   1 
ATOM   551  H HB2  A ASN   A 1 20  ? 6.534  -4.003  7.874   0.40 17.23 ?  20  ASN   A HB2  1 
ATOM   552  H HB2  B ASN   A 1 20  ? 6.686  -3.902  8.655   0.60 20.18 ?  20  ASN   A HB2  1 
ATOM   553  H HB3  A ASN   A 1 20  ? 6.376  -3.639  9.412   0.40 17.23 ?  20  ASN   A HB3  1 
ATOM   554  H HB3  B ASN   A 1 20  ? 6.581  -3.592  10.209  0.60 20.18 ?  20  ASN   A HB3  1 
ATOM   555  H HD21 A ASN   A 1 20  ? 7.060  -0.594  7.044   0.40 19.29 ?  20  ASN   A HD21 1 
ATOM   556  H HD21 B ASN   A 1 20  ? 7.088  -0.523  7.827   0.60 22.15 ?  20  ASN   A HD21 1 
ATOM   557  H HD22 A ASN   A 1 20  ? 7.886  -1.828  6.938   0.40 19.29 ?  20  ASN   A HD22 1 
ATOM   558  H HD22 B ASN   A 1 20  ? 7.855  -1.779  7.597   0.60 22.15 ?  20  ASN   A HD22 1 
ATOM   559  N N    A ALA   A 1 21  ? 10.063 -2.001  9.394   0.40 14.73 ?  21  ALA   A N    1 
ATOM   560  N N    B ALA   A 1 21  ? 10.293 -1.981  10.046  0.60 15.80 ?  21  ALA   A N    1 
ATOM   561  C CA   A ALA   A 1 21  ? 10.750 -1.107  10.316  0.40 15.13 ?  21  ALA   A CA   1 
ATOM   562  C CA   B ALA   A 1 21  ? 10.989 -1.015  10.880  0.60 16.09 ?  21  ALA   A CA   1 
ATOM   563  C C    A ALA   A 1 21  ? 11.736 -0.229  9.558   0.40 15.11 ?  21  ALA   A C    1 
ATOM   564  C C    B ALA   A 1 21  ? 12.012 -0.280  10.033  0.60 15.76 ?  21  ALA   A C    1 
ATOM   565  O O    A ALA   A 1 21  ? 12.174 -0.560  8.452   0.40 15.31 ?  21  ALA   A O    1 
ATOM   566  O O    B ALA   A 1 21  ? 12.442 -0.767  8.983   0.60 15.99 ?  21  ALA   A O    1 
ATOM   567  C CB   A ALA   A 1 21  ? 11.481 -1.893  11.410  0.40 15.70 ?  21  ALA   A CB   1 
ATOM   568  C CB   B ALA   A 1 21  ? 11.669 -1.687  12.079  0.60 17.60 ?  21  ALA   A CB   1 
ATOM   569  H H    A ALA   A 1 21  ? 10.464 -2.127  8.649   0.40 17.73 ?  21  ALA   A H    1 
ATOM   570  H H    B ALA   A 1 21  ? 10.693 -2.163  9.303   0.60 19.02 ?  21  ALA   A H    1 
ATOM   571  H HA   A ALA   A 1 21  ? 10.094 -0.533  10.747  0.40 18.21 ?  21  ALA   A HA   1 
ATOM   572  H HA   B ALA   A 1 21  ? 10.356 -0.364  11.213  0.60 19.37 ?  21  ALA   A HA   1 
ATOM   573  H HB1  A ALA   A 1 21  ? 11.923 -1.267  12.005  0.40 18.90 ?  21  ALA   A HB1  1 
ATOM   574  H HB1  B ALA   A 1 21  ? 12.118 -1.009  12.608  0.60 21.17 ?  21  ALA   A HB1  1 
ATOM   575  H HB2  A ALA   A 1 21  ? 10.833 -2.419  11.909  0.40 18.90 ?  21  ALA   A HB2  1 
ATOM   576  H HB2  B ALA   A 1 21  ? 10.990 -2.128  12.616  0.60 21.17 ?  21  ALA   A HB2  1 
ATOM   577  H HB3  A ALA   A 1 21  ? 12.133 -2.477  10.997  0.40 18.90 ?  21  ALA   A HB3  1 
ATOM   578  H HB3  B ALA   A 1 21  ? 12.310 -2.338  11.757  0.60 21.17 ?  21  ALA   A HB3  1 
ATOM   579  N N    A ASP   A 1 22  ? 12.063 0.905   10.182  0.40 15.50 ?  22  ASP   A N    1 
ATOM   580  N N    B ASP   A 1 22  ? 12.379 0.907   10.507  0.60 16.21 ?  22  ASP   A N    1 
ATOM   581  C CA   A ASP   A 1 22  ? 13.099 1.821   9.722   0.40 15.43 ?  22  ASP   A CA   1 
ATOM   582  C CA   B ASP   A 1 22  ? 13.491 1.661   9.956   0.60 16.62 ?  22  ASP   A CA   1 
ATOM   583  C C    A ASP   A 1 22  ? 14.433 1.344   10.280  0.40 14.76 ?  22  ASP   A C    1 
ATOM   584  C C    B ASP   A 1 22  ? 14.777 1.041   10.481  0.60 15.18 ?  22  ASP   A C    1 
ATOM   585  O O    A ASP   A 1 22  ? 14.640 1.359   11.497  0.40 14.79 ?  22  ASP   A O    1 
ATOM   586  O O    B ASP   A 1 22  ? 14.950 0.901   11.695  0.60 15.75 ?  22  ASP   A O    1 
ATOM   587  C CB   A ASP   A 1 22  ? 12.781 3.226   10.238  0.40 16.43 ?  22  ASP   A CB   1 
ATOM   588  C CB   B ASP   A 1 22  ? 13.387 3.113   10.430  0.60 18.30 ?  22  ASP   A CB   1 
ATOM   589  C CG   A ASP   A 1 22  ? 13.847 4.256   9.882   0.40 17.36 ?  22  ASP   A CG   1 
ATOM   590  C CG   B ASP   A 1 22  ? 14.327 4.060   9.689   0.60 19.88 ?  22  ASP   A CG   1 
ATOM   591  O OD1  A ASP   A 1 22  ? 14.864 3.909   9.246   0.40 17.54 ?  22  ASP   A OD1  1 
ATOM   592  O OD1  B ASP   A 1 22  ? 15.416 3.621   9.266   0.60 19.75 ?  22  ASP   A OD1  1 
ATOM   593  O OD2  A ASP   A 1 22  ? 13.671 5.432   10.268  0.40 17.95 -1 22  ASP   A OD2  1 
ATOM   594  O OD2  B ASP   A 1 22  ? 13.981 5.253   9.536   0.60 22.00 -1 22  ASP   A OD2  1 
ATOM   595  H H    A ASP   A 1 22  ? 11.673 1.170   10.903  0.40 18.66 ?  22  ASP   A H    1 
ATOM   596  H H    B ASP   A 1 22  ? 11.988 1.300   11.164  0.60 19.51 ?  22  ASP   A H    1 
ATOM   597  H HA   A ASP   A 1 22  ? 13.133 1.829   8.751   0.40 18.57 ?  22  ASP   A HA   1 
ATOM   598  H HA   B ASP   A 1 22  ? 13.481 1.623   8.987   0.60 20.00 ?  22  ASP   A HA   1 
ATOM   599  H HB2  A ASP   A 1 22  ? 11.920 3.507   9.880   0.40 19.78 ?  22  ASP   A HB2  1 
ATOM   600  H HB2  B ASP   A 1 22  ? 12.476 3.413   10.304  0.60 22.02 ?  22  ASP   A HB2  1 
ATOM   601  H HB3  A ASP   A 1 22  ? 12.741 3.204   11.205  0.40 19.78 ?  22  ASP   A HB3  1 
ATOM   602  H HB3  B ASP   A 1 22  ? 13.623 3.148   11.371  0.60 22.02 ?  22  ASP   A HB3  1 
ATOM   603  N N    A ILE   A 1 23  ? 15.337 0.934   9.389   0.40 14.58 ?  23  ILE   A N    1 
ATOM   604  N N    B ILE   A 1 23  ? 15.676 0.659   9.567   0.60 14.56 ?  23  ILE   A N    1 
ATOM   605  C CA   A ILE   A 1 23  ? 16.607 0.360   9.823   0.40 13.96 ?  23  ILE   A CA   1 
ATOM   606  C CA   B ILE   A 1 23  ? 16.929 0.034   9.979   0.60 14.15 ?  23  ILE   A CA   1 
ATOM   607  C C    A ILE   A 1 23  ? 17.388 1.336   10.694  0.40 13.97 ?  23  ILE   A C    1 
ATOM   608  C C    B ILE   A 1 23  ? 17.693 0.938   10.939  0.60 14.00 ?  23  ILE   A C    1 
ATOM   609  O O    A ILE   A 1 23  ? 18.133 0.920   11.589  0.40 13.90 ?  23  ILE   A O    1 
ATOM   610  O O    B ILE   A 1 23  ? 18.375 0.457   11.853  0.60 14.59 ?  23  ILE   A O    1 
ATOM   611  C CB   A ILE   A 1 23  ? 17.415 -0.127  8.603   0.40 13.65 ?  23  ILE   A CB   1 
ATOM   612  C CB   B ILE   A 1 23  ? 17.767 -0.391  8.747   0.60 13.36 ?  23  ILE   A CB   1 
ATOM   613  C CG1  A ILE   A 1 23  ? 18.604 -0.974  9.057   0.40 13.94 ?  23  ILE   A CG1  1 
ATOM   614  C CG1  B ILE   A 1 23  ? 18.837 -1.407  9.159   0.60 13.44 ?  23  ILE   A CG1  1 
ATOM   615  C CG2  A ILE   A 1 23  ? 17.863 1.054   7.738   0.40 13.51 ?  23  ILE   A CG2  1 
ATOM   616  C CG2  B ILE   A 1 23  ? 18.395 0.816   8.048   0.60 13.41 ?  23  ILE   A CG2  1 
ATOM   617  C CD1  A ILE   A 1 23  ? 19.321 -1.666  7.919   0.40 14.08 ?  23  ILE   A CD1  1 
ATOM   618  C CD1  B ILE   A 1 23  ? 19.615 -2.004  7.992   0.60 13.50 ?  23  ILE   A CD1  1 
ATOM   619  H H    A ILE   A 1 23  ? 15.234 0.977   8.541   0.40 17.55 ?  23  ILE   A H    1 
ATOM   620  H H    B ILE   A 1 23  ? 15.588 0.753   8.722   0.60 17.53 ?  23  ILE   A H    1 
ATOM   621  H HA   A ILE   A 1 23  ? 16.418 -0.418  10.368  0.40 16.81 ?  23  ILE   A HA   1 
ATOM   622  H HA   B ILE   A 1 23  ? 16.718 -0.778  10.457  0.60 17.04 ?  23  ILE   A HA   1 
ATOM   623  H HB   A ILE   A 1 23  ? 16.836 -0.688  8.066   0.40 16.44 ?  23  ILE   A HB   1 
ATOM   624  H HB   B ILE   A 1 23  ? 17.178 -0.830  8.110   0.60 16.09 ?  23  ILE   A HB   1 
ATOM   625  H HG12 A ILE   A 1 23  ? 19.245 -0.404  9.507   0.40 16.79 ?  23  ILE   A HG12 1 
ATOM   626  H HG12 B ILE   A 1 23  ? 19.477 -0.971  9.741   0.60 16.19 ?  23  ILE   A HG12 1 
ATOM   627  H HG13 A ILE   A 1 23  ? 18.286 -1.660  9.666   0.40 16.79 ?  23  ILE   A HG13 1 
ATOM   628  H HG13 B ILE   A 1 23  ? 18.411 -2.140  9.627   0.60 16.19 ?  23  ILE   A HG13 1 
ATOM   629  H HG21 A ILE   A 1 23  ? 18.228 0.714   6.904   0.40 16.27 ?  23  ILE   A HG21 1 
ATOM   630  H HG21 B ILE   A 1 23  ? 18.738 0.536   7.179   0.60 16.15 ?  23  ILE   A HG21 1 
ATOM   631  H HG22 A ILE   A 1 23  ? 17.095 1.618   7.553   0.40 16.27 ?  23  ILE   A HG22 1 
ATOM   632  H HG22 B ILE   A 1 23  ? 17.716 1.494   7.928   0.60 16.15 ?  23  ILE   A HG22 1 
ATOM   633  H HG23 A ILE   A 1 23  ? 18.538 1.560   8.213   0.40 16.27 ?  23  ILE   A HG23 1 
ATOM   634  H HG23 B ILE   A 1 23  ? 19.119 1.156   8.592   0.60 16.15 ?  23  ILE   A HG23 1 
ATOM   635  H HD11 A ILE   A 1 23  ? 20.009 -2.243  8.284   0.40 16.96 ?  23  ILE   A HD11 1 
ATOM   636  H HD11 B ILE   A 1 23  ? 20.217 -2.688  8.329   0.60 16.26 ?  23  ILE   A HD11 1 
ATOM   637  H HD12 A ILE   A 1 23  ? 18.679 -2.193  7.417   0.40 16.96 ?  23  ILE   A HD12 1 
ATOM   638  H HD12 B ILE   A 1 23  ? 18.991 -2.396  7.362   0.60 16.26 ?  23  ILE   A HD12 1 
ATOM   639  H HD13 A ILE   A 1 23  ? 19.721 -0.996  7.344   0.40 16.96 ?  23  ILE   A HD13 1 
ATOM   640  H HD13 B ILE   A 1 23  ? 20.126 -1.302  7.558   0.60 16.26 ?  23  ILE   A HD13 1 
ATOM   641  N N    A VAL   A 1 24  ? 17.223 2.640   10.467  0.40 14.45 ?  24  VAL   A N    1 
ATOM   642  N N    B VAL   A 1 24  ? 17.568 2.255   10.773  0.60 14.74 ?  24  VAL   A N    1 
ATOM   643  C CA   A VAL   A 1 24  ? 17.911 3.631   11.291  0.40 15.18 ?  24  VAL   A CA   1 
ATOM   644  C CA   B VAL   A 1 24  ? 18.258 3.189   11.660  0.60 16.02 ?  24  VAL   A CA   1 
ATOM   645  C C    A VAL   A 1 24  ? 17.430 3.548   12.732  0.40 15.99 ?  24  VAL   A C    1 
ATOM   646  C C    B VAL   A 1 24  ? 17.717 3.070   13.079  0.60 16.53 ?  24  VAL   A C    1 
ATOM   647  O O    A VAL   A 1 24  ? 18.230 3.522   13.673  0.40 15.73 ?  24  VAL   A O    1 
ATOM   648  O O    B VAL   A 1 24  ? 18.471 3.104   14.059  0.60 16.83 ?  24  VAL   A O    1 
ATOM   649  C CB   A VAL   A 1 24  ? 17.721 5.043   10.710  0.40 15.28 ?  24  VAL   A CB   1 
ATOM   650  C CB   B VAL   A 1 24  ? 18.117 4.620   11.111  0.60 16.51 ?  24  VAL   A CB   1 
ATOM   651  C CG1  A VAL   A 1 24  ? 18.238 6.096   11.687  0.40 15.26 ?  24  VAL   A CG1  1 
ATOM   652  C CG1  B VAL   A 1 24  ? 18.675 5.629   12.100  0.60 17.11 ?  24  VAL   A CG1  1 
ATOM   653  C CG2  A VAL   A 1 24  ? 18.423 5.159   9.368   0.40 15.52 ?  24  VAL   A CG2  1 
ATOM   654  C CG2  B VAL   A 1 24  ? 18.812 4.737   9.761   0.60 17.00 ?  24  VAL   A CG2  1 
ATOM   655  H H    A VAL   A 1 24  ? 16.727 2.973   9.852   0.40 17.39 ?  24  VAL   A H    1 
ATOM   656  H H    B VAL   A 1 24  ? 17.100 2.624   10.157  0.60 17.75 ?  24  VAL   A H    1 
ATOM   657  H HA   A VAL   A 1 24  ? 18.860 3.438   11.289  0.40 18.27 ?  24  VAL   A HA   1 
ATOM   658  H HA   B VAL   A 1 24  ? 19.207 2.970   11.672  0.60 19.28 ?  24  VAL   A HA   1 
ATOM   659  H HB   A VAL   A 1 24  ? 16.774 5.204   10.572  0.40 18.39 ?  24  VAL   A HB   1 
ATOM   660  H HB   B VAL   A 1 24  ? 17.178 4.816   10.979  0.60 19.86 ?  24  VAL   A HB   1 
ATOM   661  H HG11 A VAL   A 1 24  ? 18.366 6.929   11.209  0.40 18.37 ?  24  VAL   A HG11 1 
ATOM   662  H HG11 B VAL   A 1 24  ? 18.861 6.456   11.631  0.60 20.59 ?  24  VAL   A HG11 1 
ATOM   663  H HG12 A VAL   A 1 24  ? 17.589 6.219   12.397  0.40 18.37 ?  24  VAL   A HG12 1 
ATOM   664  H HG12 B VAL   A 1 24  ? 18.016 5.781   12.791  0.60 20.59 ?  24  VAL   A HG12 1 
ATOM   665  H HG13 A VAL   A 1 24  ? 19.083 5.794   12.056  0.40 18.37 ?  24  VAL   A HG13 1 
ATOM   666  H HG13 B VAL   A 1 24  ? 19.492 5.274   12.484  0.60 20.59 ?  24  VAL   A HG13 1 
ATOM   667  H HG21 A VAL   A 1 24  ? 18.154 5.987   8.944   0.40 18.69 ?  24  VAL   A HG21 1 
ATOM   668  H HG21 B VAL   A 1 24  ? 18.611 5.604   9.377   0.60 20.46 ?  24  VAL   A HG21 1 
ATOM   669  H HG22 A VAL   A 1 24  ? 19.381 5.159   9.516   0.40 18.69 ?  24  VAL   A HG22 1 
ATOM   670  H HG22 B VAL   A 1 24  ? 19.768 4.647   9.889   0.60 20.46 ?  24  VAL   A HG22 1 
ATOM   671  H HG23 A VAL   A 1 24  ? 18.171 4.404   8.814   0.40 18.69 ?  24  VAL   A HG23 1 
ATOM   672  H HG23 B VAL   A 1 24  ? 18.489 4.035   9.172   0.60 20.46 ?  24  VAL   A HG23 1 
ATOM   673  N N    A GLU   A 1 25  ? 16.111 3.514   12.928  0.40 17.28 ?  25  GLU   A N    1 
ATOM   674  N N    B GLU   A 1 25  ? 16.399 2.917   13.211  0.60 17.52 ?  25  GLU   A N    1 
ATOM   675  C CA   A GLU   A 1 25  ? 15.574 3.442   14.282  0.40 18.34 ?  25  GLU   A CA   1 
ATOM   676  C CA   B GLU   A 1 25  ? 15.788 2.789   14.529  0.60 18.98 ?  25  GLU   A CA   1 
ATOM   677  C C    A GLU   A 1 25  ? 15.808 2.075   14.907  0.40 17.54 ?  25  GLU   A C    1 
ATOM   678  C C    B GLU   A 1 25  ? 16.091 1.434   15.155  0.60 18.53 ?  25  GLU   A C    1 
ATOM   679  O O    A GLU   A 1 25  ? 16.048 1.985   16.115  0.40 17.87 ?  25  GLU   A O    1 
ATOM   680  O O    B GLU   A 1 25  ? 16.357 1.350   16.360  0.60 19.26 ?  25  GLU   A O    1 
ATOM   681  C CB   A GLU   A 1 25  ? 14.088 3.805   14.283  0.40 20.20 ?  25  GLU   A CB   1 
ATOM   682  C CB   B GLU   A 1 25  ? 14.282 3.028   14.425  0.60 20.65 ?  25  GLU   A CB   1 
ATOM   683  C CG   A GLU   A 1 25  ? 13.823 5.246   13.875  0.40 22.14 ?  25  GLU   A CG   1 
ATOM   684  C CG   B GLU   A 1 25  ? 13.928 4.447   14.012  0.60 22.28 ?  25  GLU   A CG   1 
ATOM   685  C CD   A GLU   A 1 25  ? 14.620 6.243   14.690  0.40 23.70 ?  25  GLU   A CD   1 
ATOM   686  C CD   B GLU   A 1 25  ? 14.447 5.487   14.994  0.60 24.04 ?  25  GLU   A CD   1 
ATOM   687  O OE1  A GLU   A 1 25  ? 14.694 6.075   15.926  0.40 24.08 ?  25  GLU   A OE1  1 
ATOM   688  O OE1  B GLU   A 1 25  ? 14.275 5.294   16.215  0.60 24.77 ?  25  GLU   A OE1  1 
ATOM   689  O OE2  A GLU   A 1 25  ? 15.189 7.182   14.092  0.40 24.45 -1 25  GLU   A OE2  1 
ATOM   690  O OE2  B GLU   A 1 25  ? 15.047 6.490   14.548  0.60 25.31 -1 25  GLU   A OE2  1 
ATOM   691  H H    A GLU   A 1 25  ? 15.518 3.534   12.308  0.40 20.79 ?  25  GLU   A H    1 
ATOM   692  H H    B GLU   A 1 25  ? 15.850 2.887   12.555  0.60 21.09 ?  25  GLU   A H    1 
ATOM   693  H HA   A GLU   A 1 25  ? 16.039 4.084   14.838  0.40 22.07 ?  25  GLU   A HA   1 
ATOM   694  H HA   B GLU   A 1 25  ? 16.161 3.463   15.111  0.60 22.84 ?  25  GLU   A HA   1 
ATOM   695  H HB2  A GLU   A 1 25  ? 13.620 3.231   13.655  0.40 24.30 ?  25  GLU   A HB2  1 
ATOM   696  H HB2  B GLU   A 1 25  ? 13.913 2.422   13.761  0.60 24.84 ?  25  GLU   A HB2  1 
ATOM   697  H HB3  A GLU   A 1 25  ? 13.728 3.679   15.175  0.40 24.30 ?  25  GLU   A HB3  1 
ATOM   698  H HB3  B GLU   A 1 25  ? 13.878 2.857   15.288  0.60 24.84 ?  25  GLU   A HB3  1 
ATOM   699  H HG2  A GLU   A 1 25  ? 14.067 5.360   12.945  0.40 26.62 ?  25  GLU   A HG2  1 
ATOM   700  H HG2  B GLU   A 1 25  ? 14.333 4.637   13.153  0.60 26.79 ?  25  GLU   A HG2  1 
ATOM   701  H HG3  A GLU   A 1 25  ? 12.883 5.443   14.003  0.40 26.62 ?  25  GLU   A HG3  1 
ATOM   702  H HG3  B GLU   A 1 25  ? 12.959 4.519   13.944  0.60 26.79 ?  25  GLU   A HG3  1 
ATOM   703  N N    A GLU   A 1 26  ? 15.761 1.007   14.107  0.40 17.09 ?  26  GLU   A N    1 
ATOM   704  N N    B GLU   A 1 26  ? 16.068 0.362   14.358  0.60 18.04 ?  26  GLU   A N    1 
ATOM   705  C CA   A GLU   A 1 26  ? 16.096 -0.316  14.622  0.40 17.23 ?  26  GLU   A CA   1 
ATOM   706  C CA   B GLU   A 1 26  ? 16.484 -0.937  14.878  0.60 17.93 ?  26  GLU   A CA   1 
ATOM   707  C C    A GLU   A 1 26  ? 17.533 -0.348  15.121  0.40 16.38 ?  26  GLU   A C    1 
ATOM   708  C C    B GLU   A 1 26  ? 17.913 -0.879  15.397  0.60 17.70 ?  26  GLU   A C    1 
ATOM   709  O O    A GLU   A 1 26  ? 17.819 -0.860  16.209  0.40 16.02 ?  26  GLU   A O    1 
ATOM   710  O O    B GLU   A 1 26  ? 18.215 -1.407  16.473  0.60 18.22 ?  26  GLU   A O    1 
ATOM   711  C CB   A GLU   A 1 26  ? 15.903 -1.362  13.525  0.40 17.95 ?  26  GLU   A CB   1 
ATOM   712  C CB   B GLU   A 1 26  ? 16.361 -2.009  13.794  0.60 18.47 ?  26  GLU   A CB   1 
ATOM   713  C CG   A GLU   A 1 26  ? 14.477 -1.824  13.340  0.40 19.09 ?  26  GLU   A CG   1 
ATOM   714  C CG   B GLU   A 1 26  ? 14.941 -2.413  13.497  0.60 19.03 ?  26  GLU   A CG   1 
ATOM   715  C CD   A GLU   A 1 26  ? 13.992 -2.675  14.490  0.40 20.28 ?  26  GLU   A CD   1 
ATOM   716  C CD   B GLU   A 1 26  ? 14.248 -3.013  14.706  0.60 18.89 ?  26  GLU   A CD   1 
ATOM   717  O OE1  A GLU   A 1 26  ? 14.434 -3.839  14.604  0.40 21.05 ?  26  GLU   A OE1  1 
ATOM   718  O OE1  B GLU   A 1 26  ? 14.703 -4.070  15.213  0.60 18.45 ?  26  GLU   A OE1  1 
ATOM   719  O OE2  A GLU   A 1 26  ? 13.175 -2.166  15.285  0.40 20.93 -1 26  GLU   A OE2  1 
ATOM   720  O OE2  B GLU   A 1 26  ? 13.253 -2.412  15.150  0.60 19.55 -1 26  GLU   A OE2  1 
ATOM   721  H H    A GLU   A 1 26  ? 15.544 1.025   13.276  0.40 20.56 ?  26  GLU   A H    1 
ATOM   722  H H    B GLU   A 1 26  ? 15.824 0.357   13.534  0.60 21.71 ?  26  GLU   A H    1 
ATOM   723  H HA   A GLU   A 1 26  ? 15.507 -0.537  15.363  0.40 20.73 ?  26  GLU   A HA   1 
ATOM   724  H HA   B GLU   A 1 26  ? 15.911 -1.188  15.617  0.60 21.57 ?  26  GLU   A HA   1 
ATOM   725  H HB2  A GLU   A 1 26  ? 16.198 -0.985  12.682  0.40 21.60 ?  26  GLU   A HB2  1 
ATOM   726  H HB2  B GLU   A 1 26  ? 16.751 -1.673  12.970  0.60 22.22 ?  26  GLU   A HB2  1 
ATOM   727  H HB3  A GLU   A 1 26  ? 16.439 -2.141  13.741  0.40 21.60 ?  26  GLU   A HB3  1 
ATOM   728  H HB3  B GLU   A 1 26  ? 16.840 -2.806  14.078  0.60 22.22 ?  26  GLU   A HB3  1 
ATOM   729  H HG2  A GLU   A 1 26  ? 13.895 -1.052  13.291  0.40 22.96 ?  26  GLU   A HG2  1 
ATOM   730  H HG2  B GLU   A 1 26  ? 14.444 -1.630  13.214  0.60 22.89 ?  26  GLU   A HG2  1 
ATOM   731  H HG3  A GLU   A 1 26  ? 14.414 -2.343  12.522  0.40 22.96 ?  26  GLU   A HG3  1 
ATOM   732  H HG3  B GLU   A 1 26  ? 14.940 -3.080  12.792  0.60 22.89 ?  26  GLU   A HG3  1 
ATOM   733  N N    A ALA   A 1 27  ? 18.455 0.212   14.337  0.40 16.14 ?  27  ALA   A N    1 
ATOM   734  N N    B ALA   A 1 27  ? 18.806 -0.228  14.650  0.60 17.49 ?  27  ALA   A N    1 
ATOM   735  C CA   A ALA   A 1 27  ? 19.861 0.194   14.722  0.40 16.48 ?  27  ALA   A CA   1 
ATOM   736  C CA   B ALA   A 1 27  ? 20.201 -0.151  15.070  0.60 17.65 ?  27  ALA   A CA   1 
ATOM   737  C C    A ALA   A 1 27  ? 20.076 0.941   16.032  0.40 17.68 ?  27  ALA   A C    1 
ATOM   738  C C    B ALA   A 1 27  ? 20.343 0.680   16.338  0.60 19.19 ?  27  ALA   A C    1 
ATOM   739  O O    A ALA   A 1 27  ? 20.748 0.442   16.942  0.40 17.27 ?  27  ALA   A O    1 
ATOM   740  O O    B ALA   A 1 27  ? 21.031 0.276   17.283  0.60 19.11 ?  27  ALA   A O    1 
ATOM   741  C CB   A ALA   A 1 27  ? 20.716 0.792   13.602  0.40 15.98 ?  27  ALA   A CB   1 
ATOM   742  C CB   B ALA   A 1 27  ? 21.061 0.420   13.941  0.60 17.09 ?  27  ALA   A CB   1 
ATOM   743  H H    A ALA   A 1 27  ? 18.287 0.615   13.596  0.40 19.42 ?  27  ALA   A H    1 
ATOM   744  H H    B ALA   A 1 27  ? 18.633 0.169   13.911  0.60 21.05 ?  27  ALA   A H    1 
ATOM   745  H HA   A ALA   A 1 27  ? 20.136 -0.723  14.852  0.40 19.83 ?  27  ALA   A HA   1 
ATOM   746  H HA   B ALA   A 1 27  ? 20.525 -1.044  15.265  0.60 21.24 ?  27  ALA   A HA   1 
ATOM   747  H HB1  A ALA   A 1 27  ? 21.646 0.771   13.870  0.40 19.23 ?  27  ALA   A HB1  1 
ATOM   748  H HB1  B ALA   A 1 27  ? 21.987 0.458   14.236  0.60 20.56 ?  27  ALA   A HB1  1 
ATOM   749  H HB2  A ALA   A 1 27  ? 20.590 0.267   12.795  0.40 19.23 ?  27  ALA   A HB2  1 
ATOM   750  H HB2  B ALA   A 1 27  ? 20.989 -0.161  13.166  0.60 20.56 ?  27  ALA   A HB2  1 
ATOM   751  H HB3  A ALA   A 1 27  ? 20.436 1.709   13.445  0.40 19.23 ?  27  ALA   A HB3  1 
ATOM   752  H HB3  B ALA   A 1 27  ? 20.747 1.308   13.721  0.60 20.56 ?  27  ALA   A HB3  1 
ATOM   753  N N    A LYS   A 1 28  ? 19.491 2.137   16.156  0.40 19.90 ?  28  LYS   A N    1 
ATOM   754  N N    B LYS   A 1 28  ? 19.684 1.843   16.384  0.60 21.37 ?  28  LYS   A N    1 
ATOM   755  C CA   A LYS   A 1 28  ? 19.685 2.932   17.366  0.40 22.75 ?  28  LYS   A CA   1 
ATOM   756  C CA   B LYS   A 1 28  ? 19.735 2.670   17.585  0.60 24.10 ?  28  LYS   A CA   1 
ATOM   757  C C    A LYS   A 1 28  ? 19.098 2.252   18.597  0.40 24.12 ?  28  LYS   A C    1 
ATOM   758  C C    B LYS   A 1 28  ? 19.241 1.896   18.803  0.60 24.99 ?  28  LYS   A C    1 
ATOM   759  O O    A LYS   A 1 28  ? 19.592 2.459   19.711  0.40 24.84 ?  28  LYS   A O    1 
ATOM   760  O O    B LYS   A 1 28  ? 19.794 2.030   19.901  0.60 26.04 ?  28  LYS   A O    1 
ATOM   761  C CB   A LYS   A 1 28  ? 19.083 4.326   17.187  0.40 24.17 ?  28  LYS   A CB   1 
ATOM   762  C CB   B LYS   A 1 28  ? 18.922 3.953   17.377  0.60 25.65 ?  28  LYS   A CB   1 
ATOM   763  C CG   A LYS   A 1 28  ? 19.866 5.197   16.222  0.40 25.44 ?  28  LYS   A CG   1 
ATOM   764  C CG   B LYS   A 1 28  ? 19.712 5.090   16.735  0.60 27.21 ?  28  LYS   A CG   1 
ATOM   765  C CD   A LYS   A 1 28  ? 19.421 6.648   16.273  0.40 26.80 ?  28  LYS   A CD   1 
ATOM   766  C CD   B LYS   A 1 28  ? 18.962 6.417   16.794  0.60 28.96 ?  28  LYS   A CD   1 
ATOM   767  C CE   A LYS   A 1 28  ? 18.076 6.844   15.604  0.40 27.75 ?  28  LYS   A CE   1 
ATOM   768  C CE   B LYS   A 1 28  ? 17.825 6.467   15.790  0.60 30.20 ?  28  LYS   A CE   1 
ATOM   769  N NZ   A LYS   A 1 28  ? 17.701 8.283   15.545  0.40 28.30 ?  28  LYS   A NZ   1 
ATOM   770  N NZ   B LYS   A 1 28  ? 17.194 7.818   15.734  0.60 30.88 ?  28  LYS   A NZ   1 
ATOM   771  H H    A LYS   A 1 28  ? 18.990 2.505   15.561  0.40 23.93 ?  28  LYS   A H    1 
ATOM   772  H H    B LYS   A 1 28  ? 19.204 2.160   15.748  0.60 25.70 ?  28  LYS   A H    1 
ATOM   773  H HA   A LYS   A 1 28  ? 20.634 3.039   17.517  0.40 27.35 ?  28  LYS   A HA   1 
ATOM   774  H HA   B LYS   A 1 28  ? 20.652 2.929   17.754  0.60 28.98 ?  28  LYS   A HA   1 
ATOM   775  H HB2  A LYS   A 1 28  ? 18.180 4.237   16.846  0.40 29.06 ?  28  LYS   A HB2  1 
ATOM   776  H HB2  B LYS   A 1 28  ? 18.171 3.761   16.793  0.60 30.84 ?  28  LYS   A HB2  1 
ATOM   777  H HB3  A LYS   A 1 28  ? 19.068 4.773   18.049  0.40 29.06 ?  28  LYS   A HB3  1 
ATOM   778  H HB3  B LYS   A 1 28  ? 18.601 4.270   18.233  0.60 30.84 ?  28  LYS   A HB3  1 
ATOM   779  H HG2  A LYS   A 1 28  ? 20.807 5.160   16.454  0.40 30.59 ?  28  LYS   A HG2  1 
ATOM   780  H HG2  B LYS   A 1 28  ? 20.552 5.202   17.207  0.60 32.71 ?  28  LYS   A HG2  1 
ATOM   781  H HG3  A LYS   A 1 28  ? 19.731 4.870   15.319  0.40 30.59 ?  28  LYS   A HG3  1 
ATOM   782  H HG3  B LYS   A 1 28  ? 19.878 4.882   15.803  0.60 32.71 ?  28  LYS   A HG3  1 
ATOM   783  H HD2  A LYS   A 1 28  ? 19.342 6.927   17.200  0.40 32.22 ?  28  LYS   A HD2  1 
ATOM   784  H HD2  B LYS   A 1 28  ? 18.586 6.534   17.682  0.60 34.80 ?  28  LYS   A HD2  1 
ATOM   785  H HD3  A LYS   A 1 28  ? 20.073 7.198   15.812  0.40 32.22 ?  28  LYS   A HD3  1 
ATOM   786  H HD3  B LYS   A 1 28  ? 19.575 7.143   16.594  0.60 34.80 ?  28  LYS   A HD3  1 
ATOM   787  H HE2  A LYS   A 1 28  ? 18.117 6.503   14.696  0.40 33.36 ?  28  LYS   A HE2  1 
ATOM   788  H HE2  B LYS   A 1 28  ? 18.171 6.260   14.909  0.60 36.30 ?  28  LYS   A HE2  1 
ATOM   789  H HE3  A LYS   A 1 28  ? 17.394 6.372   16.108  0.40 33.36 ?  28  LYS   A HE3  1 
ATOM   790  H HE3  B LYS   A 1 28  ? 17.144 5.825   16.043  0.60 36.30 ?  28  LYS   A HE3  1 
ATOM   791  H HZ1  A LYS   A 1 28  ? 16.910 8.376   15.148  0.40 34.01 ?  28  LYS   A HZ1  1 
ATOM   792  H HZ1  B LYS   A 1 28  ? 16.532 7.822   15.139  0.60 37.12 ?  28  LYS   A HZ1  1 
ATOM   793  H HZ2  A LYS   A 1 28  ? 17.653 8.618   16.368  0.40 34.01 ?  28  LYS   A HZ2  1 
ATOM   794  H HZ2  B LYS   A 1 28  ? 16.866 8.034   16.533  0.60 37.12 ?  28  LYS   A HZ2  1 
ATOM   795  H HZ3  A LYS   A 1 28  ? 18.311 8.737   15.083  0.40 34.01 ?  28  LYS   A HZ3  1 
ATOM   796  H HZ3  B LYS   A 1 28  ? 17.799 8.427   15.497  0.60 37.12 ?  28  LYS   A HZ3  1 
ATOM   797  N N    A LYS   A 1 29  ? 18.047 1.450   18.424  0.40 25.18 ?  29  LYS   A N    1 
ATOM   798  N N    B LYS   A 1 29  ? 18.219 1.060   18.620  0.60 25.50 ?  29  LYS   A N    1 
ATOM   799  C CA   A LYS   A 1 29  ? 17.444 0.752   19.554  0.40 26.69 ?  29  LYS   A CA   1 
ATOM   800  C CA   B LYS   A 1 29  ? 17.636 0.320   19.736  0.60 26.41 ?  29  LYS   A CA   1 
ATOM   801  C C    A LYS   A 1 29  ? 18.252 -0.483  19.937  0.40 25.82 ?  29  LYS   A C    1 
ATOM   802  C C    B LYS   A 1 29  ? 18.493 -0.882  20.123  0.60 24.71 ?  29  LYS   A C    1 
ATOM   803  O O    A LYS   A 1 29  ? 18.575 -0.686  21.112  0.40 26.24 ?  29  LYS   A O    1 
ATOM   804  O O    B LYS   A 1 29  ? 18.763 -1.106  21.309  0.60 24.93 ?  29  LYS   A O    1 
ATOM   805  C CB   A LYS   A 1 29  ? 16.004 0.360   19.209  0.40 29.08 ?  29  LYS   A CB   1 
ATOM   806  C CB   B LYS   A 1 29  ? 16.229 -0.143  19.357  0.60 29.31 ?  29  LYS   A CB   1 
ATOM   807  C CG   A LYS   A 1 29  ? 15.268 -0.383  20.315  0.40 31.46 ?  29  LYS   A CG   1 
ATOM   808  C CG   B LYS   A 1 29  ? 15.439 -0.779  20.490  0.60 32.23 ?  29  LYS   A CG   1 
ATOM   809  C CD   A LYS   A 1 29  ? 14.911 0.544   21.462  0.40 33.64 ?  29  LYS   A CD   1 
ATOM   810  C CD   B LYS   A 1 29  ? 14.998 0.250   21.516  0.60 34.84 ?  29  LYS   A CD   1 
ATOM   811  C CE   A LYS   A 1 29  ? 14.050 -0.161  22.497  0.40 35.25 ?  29  LYS   A CE   1 
ATOM   812  C CE   B LYS   A 1 29  ? 14.079 -0.370  22.557  0.60 36.74 ?  29  LYS   A CE   1 
ATOM   813  N NZ   A LYS   A 1 29  ? 13.581 0.776   23.553  0.40 36.20 ?  29  LYS   A NZ   1 
ATOM   814  N NZ   B LYS   A 1 29  ? 13.584 0.642   23.528  0.60 37.88 ?  29  LYS   A NZ   1 
ATOM   815  H H    A LYS   A 1 29  ? 17.665 1.298   17.670  0.40 30.27 ?  29  LYS   A H    1 
ATOM   816  H H    B LYS   A 1 29  ? 17.844 0.909   17.861  0.60 30.65 ?  29  LYS   A H    1 
ATOM   817  H HA   A LYS   A 1 29  ? 17.418 1.343   20.321  0.40 32.09 ?  29  LYS   A HA   1 
ATOM   818  H HA   B LYS   A 1 29  ? 17.568 0.906   20.505  0.60 31.75 ?  29  LYS   A HA   1 
ATOM   819  H HB2  A LYS   A 1 29  ? 15.500 1.166   19.015  0.40 34.95 ?  29  LYS   A HB2  1 
ATOM   820  H HB2  B LYS   A 1 29  ? 15.727 0.622   19.042  0.60 35.23 ?  29  LYS   A HB2  1 
ATOM   821  H HB3  A LYS   A 1 29  ? 16.015 -0.214  18.428  0.40 34.95 ?  29  LYS   A HB3  1 
ATOM   822  H HB3  B LYS   A 1 29  ? 16.303 -0.801  18.648  0.60 35.23 ?  29  LYS   A HB3  1 
ATOM   823  H HG2  A LYS   A 1 29  ? 14.446 -0.751  19.957  0.40 37.80 ?  29  LYS   A HG2  1 
ATOM   824  H HG2  B LYS   A 1 29  ? 14.644 -1.201  20.126  0.60 38.73 ?  29  LYS   A HG2  1 
ATOM   825  H HG3  A LYS   A 1 29  ? 15.826 -1.098  20.663  0.40 37.80 ?  29  LYS   A HG3  1 
ATOM   826  H HG3  B LYS   A 1 29  ? 15.989 -1.438  20.941  0.60 38.73 ?  29  LYS   A HG3  1 
ATOM   827  H HD2  A LYS   A 1 29  ? 15.724 0.846   21.896  0.40 40.42 ?  29  LYS   A HD2  1 
ATOM   828  H HD2  B LYS   A 1 29  ? 15.777 0.607   21.972  0.60 41.86 ?  29  LYS   A HD2  1 
ATOM   829  H HD3  A LYS   A 1 29  ? 14.413 1.301   21.116  0.40 40.42 ?  29  LYS   A HD3  1 
ATOM   830  H HD3  B LYS   A 1 29  ? 14.514 0.964   21.070  0.60 41.86 ?  29  LYS   A HD3  1 
ATOM   831  H HE2  A LYS   A 1 29  ? 13.271 -0.541  22.059  0.40 42.36 ?  29  LYS   A HE2  1 
ATOM   832  H HE2  B LYS   A 1 29  ? 13.311 -0.764  22.112  0.60 44.15 ?  29  LYS   A HE2  1 
ATOM   833  H HE3  A LYS   A 1 29  ? 14.570 -0.862  22.921  0.40 42.36 ?  29  LYS   A HE3  1 
ATOM   834  H HE3  B LYS   A 1 29  ? 14.565 -1.050  23.049  0.60 44.15 ?  29  LYS   A HE3  1 
ATOM   835  H HZ1  A LYS   A 1 29  ? 13.080 0.340   24.146  0.40 43.49 ?  29  LYS   A HZ1  1 
ATOM   836  H HZ1  B LYS   A 1 29  ? 13.050 0.255   24.125  0.60 45.51 ?  29  LYS   A HZ1  1 
ATOM   837  H HZ2  A LYS   A 1 29  ? 14.279 1.135   23.972  0.40 43.49 ?  29  LYS   A HZ2  1 
ATOM   838  H HZ2  B LYS   A 1 29  ? 14.271 1.016   23.953  0.60 45.51 ?  29  LYS   A HZ2  1 
ATOM   839  H HZ3  A LYS   A 1 29  ? 13.097 1.427   23.188  0.40 43.49 ?  29  LYS   A HZ3  1 
ATOM   840  H HZ3  B LYS   A 1 29  ? 13.129 1.276   23.100  0.60 45.51 ?  29  LYS   A HZ3  1 
ATOM   841  N N    A VAL   A 1 30  ? 18.588 -1.317  18.953  0.40 24.77 ?  30  VAL   A N    1 
ATOM   842  N N    B VAL   A 1 30  ? 18.918 -1.669  19.139  0.60 23.15 ?  30  VAL   A N    1 
ATOM   843  C CA   A VAL   A 1 30  ? 19.233 -2.594  19.238  0.40 24.18 ?  30  VAL   A CA   1 
ATOM   844  C CA   B VAL   A 1 30  ? 19.597 -2.929  19.425  0.60 22.95 ?  30  VAL   A CA   1 
ATOM   845  C C    A VAL   A 1 30  ? 20.731 -2.420  19.462  0.40 23.48 ?  30  VAL   A C    1 
ATOM   846  C C    B VAL   A 1 30  ? 21.109 -2.759  19.586  0.60 21.60 ?  30  VAL   A C    1 
ATOM   847  O O    A VAL   A 1 30  ? 21.324 -3.095  20.311  0.40 23.28 ?  30  VAL   A O    1 
ATOM   848  O O    B VAL   A 1 30  ? 21.741 -3.520  20.326  0.60 21.78 ?  30  VAL   A O    1 
ATOM   849  C CB   A VAL   A 1 30  ? 18.929 -3.592  18.105  0.40 24.44 ?  30  VAL   A CB   1 
ATOM   850  C CB   B VAL   A 1 30  ? 19.264 -3.953  18.326  0.60 24.03 ?  30  VAL   A CB   1 
ATOM   851  C CG1  A VAL   A 1 30  ? 19.674 -4.900  18.323  0.40 24.48 ?  30  VAL   A CG1  1 
ATOM   852  C CG1  B VAL   A 1 30  ? 20.058 -5.236  18.517  0.60 24.43 ?  30  VAL   A CG1  1 
ATOM   853  C CG2  A VAL   A 1 30  ? 17.431 -3.840  18.005  0.40 24.67 ?  30  VAL   A CG2  1 
ATOM   854  C CG2  B VAL   A 1 30  ? 17.771 -4.238  18.305  0.60 24.53 ?  30  VAL   A CG2  1 
ATOM   855  H H    A VAL   A 1 30  ? 18.452 -1.166  18.118  0.40 29.78 ?  30  VAL   A H    1 
ATOM   856  H H    B VAL   A 1 30  ? 18.836 -1.495  18.296  0.60 27.84 ?  30  VAL   A H    1 
ATOM   857  H HA   A VAL   A 1 30  ? 18.853 -2.958  20.052  0.40 29.07 ?  30  VAL   A HA   1 
ATOM   858  H HA   B VAL   A 1 30  ? 19.238 -3.275  20.257  0.60 27.60 ?  30  VAL   A HA   1 
ATOM   859  H HB   A VAL   A 1 30  ? 19.224 -3.216  17.261  0.40 29.38 ?  30  VAL   A HB   1 
ATOM   860  H HB   B VAL   A 1 30  ? 19.507 -3.583  17.465  0.60 28.90 ?  30  VAL   A HB   1 
ATOM   861  H HG11 A VAL   A 1 30  ? 19.303 -5.576  17.733  0.40 29.43 ?  30  VAL   A HG11 1 
ATOM   862  H HG11 B VAL   A 1 30  ? 19.654 -5.939  17.984  0.60 29.37 ?  30  VAL   A HG11 1 
ATOM   863  H HG12 A VAL   A 1 30  ? 20.613 -4.768  18.122  0.40 29.43 ?  30  VAL   A HG12 1 
ATOM   864  H HG12 B VAL   A 1 30  ? 20.972 -5.088  18.230  0.60 29.37 ?  30  VAL   A HG12 1 
ATOM   865  H HG13 A VAL   A 1 30  ? 19.565 -5.174  19.246  0.40 29.43 ?  30  VAL   A HG13 1 
ATOM   866  H HG13 B VAL   A 1 30  ? 20.038 -5.481  19.455  0.60 29.37 ?  30  VAL   A HG13 1 
ATOM   867  H HG21 A VAL   A 1 30  ? 17.266 -4.508  17.321  0.40 29.66 ?  30  VAL   A HG21 1 
ATOM   868  H HG21 B VAL   A 1 30  ? 17.588 -4.915  17.636  0.60 29.50 ?  30  VAL   A HG21 1 
ATOM   869  H HG22 A VAL   A 1 30  ? 17.107 -4.159  18.862  0.40 29.66 ?  30  VAL   A HG22 1 
ATOM   870  H HG22 B VAL   A 1 30  ? 17.498 -4.553  19.180  0.60 29.50 ?  30  VAL   A HG22 1 
ATOM   871  H HG23 A VAL   A 1 30  ? 16.988 -3.011  17.771  0.40 29.66 ?  30  VAL   A HG23 1 
ATOM   872  H HG23 B VAL   A 1 30  ? 17.300 -3.419  18.086  0.60 29.50 ?  30  VAL   A HG23 1 
ATOM   873  N N    A LYS   A 1 31  ? 21.361 -1.509  18.727  0.40 23.32 ?  31  LYS   A N    1 
ATOM   874  N N    B LYS   A 1 31  ? 21.702 -1.777  18.916  0.60 20.61 ?  31  LYS   A N    1 
ATOM   875  C CA   A LYS   A 1 31  ? 22.815 -1.403  18.668  0.40 23.70 ?  31  LYS   A CA   1 
ATOM   876  C CA   B LYS   A 1 31  ? 23.151 -1.647  18.816  0.60 20.89 ?  31  LYS   A CA   1 
ATOM   877  C C    A LYS   A 1 31  ? 23.434 -2.762  18.328  0.40 21.73 ?  31  LYS   A C    1 
ATOM   878  C C    B LYS   A 1 31  ? 23.770 -2.982  18.391  0.60 19.01 ?  31  LYS   A C    1 
ATOM   879  O O    A LYS   A 1 31  ? 24.187 -3.325  19.128  0.40 21.97 ?  31  LYS   A O    1 
ATOM   880  O O    B LYS   A 1 31  ? 24.591 -3.553  19.115  0.60 19.60 ?  31  LYS   A O    1 
ATOM   881  C CB   A LYS   A 1 31  ? 23.400 -0.849  19.960  0.40 26.45 ?  31  LYS   A CB   1 
ATOM   882  C CB   B LYS   A 1 31  ? 23.778 -1.137  20.107  0.60 24.75 ?  31  LYS   A CB   1 
ATOM   883  C CG   A LYS   A 1 31  ? 22.686 0.379   20.494  0.40 29.25 ?  31  LYS   A CG   1 
ATOM   884  C CG   B LYS   A 1 31  ? 23.103 0.109   20.674  0.60 29.05 ?  31  LYS   A CG   1 
ATOM   885  C CD   A LYS   A 1 31  ? 23.675 1.442   20.943  0.40 31.49 ?  31  LYS   A CD   1 
ATOM   886  C CD   B LYS   A 1 31  ? 24.079 1.271   20.811  0.60 32.52 ?  31  LYS   A CD   1 
ATOM   887  C CE   A LYS   A 1 31  ? 23.014 2.466   21.853  0.40 33.01 ?  31  LYS   A CE   1 
ATOM   888  C CE   B LYS   A 1 31  ? 23.525 2.376   21.705  0.60 34.78 ?  31  LYS   A CE   1 
ATOM   889  N NZ   A LYS   A 1 31  ? 21.820 3.099   21.230  0.40 33.81 ?  31  LYS   A NZ   1 
ATOM   890  N NZ   B LYS   A 1 31  ? 22.238 2.939   21.209  0.60 35.96 ?  31  LYS   A NZ   1 
ATOM   891  H H    A LYS   A 1 31  ? 20.956 -0.924  18.248  0.40 28.04 ?  31  LYS   A H    1 
ATOM   892  H H    B LYS   A 1 31  ? 21.274 -1.169  18.492  0.60 24.79 ?  31  LYS   A H    1 
ATOM   893  H HA   A LYS   A 1 31  ? 23.044 -0.787  17.959  0.40 28.49 ?  31  LYS   A HA   1 
ATOM   894  H HA   B LYS   A 1 31  ? 23.346 -1.004  18.127  0.60 25.12 ?  31  LYS   A HA   1 
ATOM   895  H HB2  A LYS   A 1 31  ? 23.360 -1.535  20.643  0.40 31.79 ?  31  LYS   A HB2  1 
ATOM   896  H HB2  B LYS   A 1 31  ? 23.735 -1.832  20.779  0.60 29.76 ?  31  LYS   A HB2  1 
ATOM   897  H HB3  A LYS   A 1 31  ? 24.327 -0.604  19.798  0.40 31.79 ?  31  LYS   A HB3  1 
ATOM   898  H HB3  B LYS   A 1 31  ? 24.709 -0.913  19.928  0.60 29.76 ?  31  LYS   A HB3  1 
ATOM   899  H HG2  A LYS   A 1 31  ? 22.130 0.757   19.795  0.40 35.16 ?  31  LYS   A HG2  1 
ATOM   900  H HG2  B LYS   A 1 31  ? 22.388 0.387   20.079  0.60 34.92 ?  31  LYS   A HG2  1 
ATOM   901  H HG3  A LYS   A 1 31  ? 22.143 0.127   21.257  0.40 35.16 ?  31  LYS   A HG3  1 
ATOM   902  H HG3  B LYS   A 1 31  ? 22.746 -0.093  21.553  0.60 34.92 ?  31  LYS   A HG3  1 
ATOM   903  H HD2  A LYS   A 1 31  ? 24.399 1.020   21.433  0.40 37.85 ?  31  LYS   A HD2  1 
ATOM   904  H HD2  B LYS   A 1 31  ? 24.904 0.951   21.206  0.60 39.08 ?  31  LYS   A HD2  1 
ATOM   905  H HD3  A LYS   A 1 31  ? 24.023 1.904   20.164  0.40 37.85 ?  31  LYS   A HD3  1 
ATOM   906  H HD3  B LYS   A 1 31  ? 24.250 1.650   19.935  0.60 39.08 ?  31  LYS   A HD3  1 
ATOM   907  H HE2  A LYS   A 1 31  ? 22.731 2.026   22.669  0.40 39.67 ?  31  LYS   A HE2  1 
ATOM   908  H HE2  B LYS   A 1 31  ? 23.371 2.017   22.593  0.60 41.80 ?  31  LYS   A HE2  1 
ATOM   909  H HE3  A LYS   A 1 31  ? 23.654 3.165   22.057  0.40 39.67 ?  31  LYS   A HE3  1 
ATOM   910  H HE3  B LYS   A 1 31  ? 24.170 3.100   21.749  0.60 41.80 ?  31  LYS   A HE3  1 
ATOM   911  H HZ1  A LYS   A 1 31  ? 21.475 3.706   21.783  0.40 40.63 ?  31  LYS   A HZ1  1 
ATOM   912  H HZ1  B LYS   A 1 31  ? 21.954 3.580   21.757  0.60 43.21 ?  31  LYS   A HZ1  1 
ATOM   913  H HZ2  A LYS   A 1 31  ? 22.050 3.499   20.469  0.40 40.63 ?  31  LYS   A HZ2  1 
ATOM   914  H HZ2  B LYS   A 1 31  ? 22.350 3.283   20.396  0.60 43.21 ?  31  LYS   A HZ2  1 
ATOM   915  H HZ3  A LYS   A 1 31  ? 21.203 2.481   21.057  0.40 40.63 ?  31  LYS   A HZ3  1 
ATOM   916  H HZ3  B LYS   A 1 31  ? 21.621 2.298   21.170  0.60 43.21 ?  31  LYS   A HZ3  1 
ATOM   917  N N    A PRO   A 1 32  ? 23.133 -3.311  17.154  0.40 19.89 ?  32  PRO   A N    1 
ATOM   918  N N    B PRO   A 1 32  ? 23.383 -3.505  17.232  0.60 16.88 ?  32  PRO   A N    1 
ATOM   919  C CA   A PRO   A 1 32  ? 23.618 -4.653  16.821  0.40 19.19 ?  32  PRO   A CA   1 
ATOM   920  C CA   B PRO   A 1 32  ? 23.854 -4.830  16.826  0.60 17.11 ?  32  PRO   A CA   1 
ATOM   921  C C    A PRO   A 1 32  ? 25.124 -4.658  16.610  0.40 18.49 ?  32  PRO   A C    1 
ATOM   922  C C    B PRO   A 1 32  ? 25.349 -4.828  16.566  0.60 17.25 ?  32  PRO   A C    1 
ATOM   923  O O    A PRO   A 1 32  ? 25.776 -3.618  16.494  0.40 18.38 ?  32  PRO   A O    1 
ATOM   924  O O    B PRO   A 1 32  ? 25.970 -3.790  16.324  0.60 16.68 ?  32  PRO   A O    1 
ATOM   925  C CB   A PRO   A 1 32  ? 22.871 -4.977  15.524  0.40 19.38 ?  32  PRO   A CB   1 
ATOM   926  C CB   B PRO   A 1 32  ? 23.083 -5.085  15.528  0.60 17.31 ?  32  PRO   A CB   1 
ATOM   927  C CG   A PRO   A 1 32  ? 22.663 -3.641  14.887  0.40 19.26 ?  32  PRO   A CG   1 
ATOM   928  C CG   B PRO   A 1 32  ? 22.902 -3.711  14.953  0.60 16.39 ?  32  PRO   A CG   1 
ATOM   929  C CD   A PRO   A 1 32  ? 22.400 -2.697  16.032  0.40 19.46 ?  32  PRO   A CD   1 
ATOM   930  C CD   B PRO   A 1 32  ? 22.639 -2.834  16.152  0.60 16.41 ?  32  PRO   A CD   1 
ATOM   931  H HA   A PRO   A 1 32  ? 23.379 -5.292  17.508  0.40 23.09 ?  32  PRO   A HA   1 
ATOM   932  H HA   B PRO   A 1 32  ? 23.629 -5.503  17.486  0.60 20.58 ?  32  PRO   A HA   1 
ATOM   933  H HB2  A PRO   A 1 32  ? 23.412 -5.551  14.960  0.40 23.31 ?  32  PRO   A HB2  1 
ATOM   934  H HB2  B PRO   A 1 32  ? 23.606 -5.647  14.933  0.60 20.83 ?  32  PRO   A HB2  1 
ATOM   935  H HB3  A PRO   A 1 32  ? 22.018 -5.398  15.729  0.40 23.31 ?  32  PRO   A HB3  1 
ATOM   936  H HB3  B PRO   A 1 32  ? 22.225 -5.495  15.725  0.60 20.83 ?  32  PRO   A HB3  1 
ATOM   937  H HG2  A PRO   A 1 32  ? 23.464 -3.384  14.404  0.40 23.17 ?  32  PRO   A HG2  1 
ATOM   938  H HG2  B PRO   A 1 32  ? 23.713 -3.444  14.493  0.60 19.72 ?  32  PRO   A HG2  1 
ATOM   939  H HG3  A PRO   A 1 32  ? 21.900 -3.680  14.288  0.40 23.17 ?  32  PRO   A HG3  1 
ATOM   940  H HG3  B PRO   A 1 32  ? 22.145 -3.710  14.345  0.60 19.72 ?  32  PRO   A HG3  1 
ATOM   941  H HD2  A PRO   A 1 32  ? 22.758 -1.819  15.828  0.40 23.40 ?  32  PRO   A HD2  1 
ATOM   942  H HD2  B PRO   A 1 32  ? 22.994 -1.944  15.991  0.60 19.74 ?  32  PRO   A HD2  1 
ATOM   943  H HD3  A PRO   A 1 32  ? 21.451 -2.660  16.224  0.40 23.40 ?  32  PRO   A HD3  1 
ATOM   944  H HD3  B PRO   A 1 32  ? 21.693 -2.813  16.347  0.60 19.74 ?  32  PRO   A HD3  1 
ATOM   945  N N    A THR   A 1 33  ? 25.680 -5.869  16.568  0.40 18.17 ?  33  THR   A N    1 
ATOM   946  N N    B THR   A 1 33  ? 25.928 -6.027  16.600  0.60 17.64 ?  33  THR   A N    1 
ATOM   947  C CA   A THR   A 1 33  ? 27.101 -6.020  16.273  0.40 17.61 ?  33  THR   A CA   1 
ATOM   948  C CA   B THR   A 1 33  ? 27.326 -6.164  16.219  0.60 18.09 ?  33  THR   A CA   1 
ATOM   949  C C    A THR   A 1 33  ? 27.416 -5.549  14.858  0.40 16.23 ?  33  THR   A C    1 
ATOM   950  C C    B THR   A 1 33  ? 27.547 -5.688  14.789  0.60 16.58 ?  33  THR   A C    1 
ATOM   951  O O    A THR   A 1 33  ? 28.395 -4.827  14.633  0.40 16.11 ?  33  THR   A O    1 
ATOM   952  O O    B THR   A 1 33  ? 28.573 -5.063  14.491  0.60 16.61 ?  33  THR   A O    1 
ATOM   953  C CB   A THR   A 1 33  ? 27.507 -7.483  16.463  0.40 18.46 ?  33  THR   A CB   1 
ATOM   954  C CB   B THR   A 1 33  ? 27.775 -7.615  16.392  0.60 19.67 ?  33  THR   A CB   1 
ATOM   955  O OG1  A THR   A 1 33  ? 27.189 -7.894  17.798  0.40 19.29 ?  33  THR   A OG1  1 
ATOM   956  O OG1  B THR   A 1 33  ? 27.567 -8.018  17.750  0.60 21.00 ?  33  THR   A OG1  1 
ATOM   957  C CG2  A THR   A 1 33  ? 29.001 -7.670  16.211  0.40 18.81 ?  33  THR   A CG2  1 
ATOM   958  C CG2  B THR   A 1 33  ? 29.252 -7.770  16.048  0.60 20.16 ?  33  THR   A CG2  1 
ATOM   959  H H    A THR   A 1 33  ? 25.264 -6.610  16.713  0.40 21.86 ?  33  THR   A H    1 
ATOM   960  H H    B THR   A 1 33  ? 25.541 -6.760  16.828  0.60 21.23 ?  33  THR   A H    1 
ATOM   961  H HA   A THR   A 1 33  ? 27.614 -5.482  16.894  0.40 21.19 ?  33  THR   A HA   1 
ATOM   962  H HA   B THR   A 1 33  ? 27.868 -5.613  16.805  0.60 21.77 ?  33  THR   A HA   1 
ATOM   963  H HB   A THR   A 1 33  ? 27.023 -8.040  15.832  0.40 22.21 ?  33  THR   A HB   1 
ATOM   964  H HB   B THR   A 1 33  ? 27.260 -8.189  15.801  0.60 23.67 ?  33  THR   A HB   1 
ATOM   965  H HG1  A THR   A 1 33  ? 27.616 -7.425  18.351  0.40 23.20 ?  33  THR   A HG1  1 
ATOM   966  H HG1  B THR   A 1 33  ? 28.014 -7.528  18.266  0.60 25.25 ?  33  THR   A HG1  1 
ATOM   967  H HG21 A THR   A 1 33  ? 29.278 -8.555  16.494  0.40 22.63 ?  33  THR   A HG21 1 
ATOM   968  H HG21 B THR   A 1 33  ? 29.564 -8.648  16.314  0.60 24.25 ?  33  THR   A HG21 1 
ATOM   969  H HG22 A THR   A 1 33  ? 29.196 -7.570  15.264  0.40 22.63 ?  33  THR   A HG22 1 
ATOM   970  H HG22 B THR   A 1 33  ? 29.386 -7.665  15.093  0.60 24.25 ?  33  THR   A HG22 1 
ATOM   971  H HG23 A THR   A 1 33  ? 29.507 -7.008  16.707  0.40 22.63 ?  33  THR   A HG23 1 
ATOM   972  H HG23 B THR   A 1 33  ? 29.772 -7.097  16.516  0.60 24.25 ?  33  THR   A HG23 1 
ATOM   973  N N    . VAL   A 1 34  ? 26.593 -5.954  13.893  1.00 15.22 ?  34  VAL   A N    1 
ATOM   974  C CA   . VAL   A 1 34  ? 26.740 -5.592  12.489  1.00 14.00 ?  34  VAL   A CA   1 
ATOM   975  C C    . VAL   A 1 34  ? 25.420 -5.037  11.961  1.00 13.22 ?  34  VAL   A C    1 
ATOM   976  O O    . VAL   A 1 34  ? 24.381 -5.710  12.027  1.00 14.06 ?  34  VAL   A O    1 
ATOM   977  C CB   . VAL   A 1 34  ? 27.194 -6.782  11.621  1.00 14.20 ?  34  VAL   A CB   1 
ATOM   978  C CG1  . VAL   A 1 34  ? 27.351 -6.352  10.169  1.00 14.06 ?  34  VAL   A CG1  1 
ATOM   979  C CG2  . VAL   A 1 34  ? 28.494 -7.393  12.145  1.00 14.76 ?  34  VAL   A CG2  1 
ATOM   980  H H    A VAL   A 1 34  ? 25.918 -6.467  14.033  0.40 18.32 ?  34  VAL   A H    1 
ATOM   981  H H    B VAL   A 1 34  ? 25.856 -6.354  14.074  0.60 18.32 ?  34  VAL   A H    1 
ATOM   982  H HA   . VAL   A 1 34  ? 27.413 -4.895  12.405  1.00 16.85 ?  34  VAL   A HA   1 
ATOM   983  H HB   . VAL   A 1 34  ? 26.516 -7.469  11.648  1.00 17.10 ?  34  VAL   A HB   1 
ATOM   984  H HG11 . VAL   A 1 34  ? 27.833 -7.041  9.682   1.00 16.93 ?  34  VAL   A HG11 1 
ATOM   985  H HG12 . VAL   A 1 34  ? 26.476 -6.223  9.775   1.00 16.93 ?  34  VAL   A HG12 1 
ATOM   986  H HG13 . VAL   A 1 34  ? 27.856 -5.520  10.136  1.00 16.93 ?  34  VAL   A HG13 1 
ATOM   987  H HG21 . VAL   A 1 34  ? 28.783 -8.097  11.540  1.00 17.77 ?  34  VAL   A HG21 1 
ATOM   988  H HG22 . VAL   A 1 34  ? 29.176 -6.702  12.191  1.00 17.77 ?  34  VAL   A HG22 1 
ATOM   989  H HG23 . VAL   A 1 34  ? 28.338 -7.761  13.027  1.00 17.77 ?  34  VAL   A HG23 1 
ATOM   990  N N    . VAL   A 1 35  ? 25.465 -3.818  11.421  1.00 12.21 ?  35  VAL   A N    1 
ATOM   991  C CA   . VAL   A 1 35  ? 24.403 -3.292  10.568  1.00 11.97 ?  35  VAL   A CA   1 
ATOM   992  C C    . VAL   A 1 35  ? 24.925 -3.274  9.142   1.00 11.23 ?  35  VAL   A C    1 
ATOM   993  O O    . VAL   A 1 35  ? 26.065 -2.861  8.900   1.00 11.71 ?  35  VAL   A O    1 
ATOM   994  C CB   . VAL   A 1 35  ? 23.891 -1.908  11.018  1.00 12.68 ?  35  VAL   A CB   1 
ATOM   995  C CG1  . VAL   A 1 35  ? 24.958 -0.812  10.884  1.00 13.24 ?  35  VAL   A CG1  1 
ATOM   996  C CG2  . VAL   A 1 35  ? 22.622 -1.532  10.235  1.00 12.91 ?  35  VAL   A CG2  1 
ATOM   997  H H    . VAL   A 1 35  ? 26.116 -3.266  11.532  1.00 14.71 ?  35  VAL   A H    1 
ATOM   998  H HA   . VAL   A 1 35  ? 23.648 -3.903  10.598  1.00 14.43 ?  35  VAL   A HA   1 
ATOM   999  H HB   . VAL   A 1 35  ? 23.644 -1.959  11.951  1.00 15.27 ?  35  VAL   A HB   1 
ATOM   1000 H HG11 . VAL   A 1 35  ? 24.621 0.014   11.275  1.00 15.95 ?  35  VAL   A HG11 1 
ATOM   1001 H HG12 . VAL   A 1 35  ? 25.761 -1.089  11.356  1.00 15.95 ?  35  VAL   A HG12 1 
ATOM   1002 H HG13 . VAL   A 1 35  ? 25.163 -0.667  9.946   1.00 15.95 ?  35  VAL   A HG13 1 
ATOM   1003 H HG21 . VAL   A 1 35  ? 22.285 -0.682  10.563  1.00 15.55 ?  35  VAL   A HG21 1 
ATOM   1004 H HG22 . VAL   A 1 35  ? 22.838 -1.455  9.290   1.00 15.55 ?  35  VAL   A HG22 1 
ATOM   1005 H HG23 . VAL   A 1 35  ? 21.952 -2.222  10.363  1.00 15.55 ?  35  VAL   A HG23 1 
ATOM   1006 N N    . VAL   A 1 36  ? 24.109 -3.739  8.205   1.00 10.92 ?  36  VAL   A N    1 
ATOM   1007 C CA   . VAL   A 1 36  ? 24.463 -3.735  6.793   1.00 10.67 ?  36  VAL   A CA   1 
ATOM   1008 C C    . VAL   A 1 36  ? 23.991 -2.439  6.152   1.00 10.76 ?  36  VAL   A C    1 
ATOM   1009 O O    . VAL   A 1 36  ? 22.836 -2.031  6.330   1.00 11.69 ?  36  VAL   A O    1 
ATOM   1010 C CB   . VAL   A 1 36  ? 23.849 -4.944  6.077   1.00 10.73 ?  36  VAL   A CB   1 
ATOM   1011 C CG1  . VAL   A 1 36  ? 24.100 -4.867  4.598   1.00 11.40 ?  36  VAL   A CG1  1 
ATOM   1012 C CG2  . VAL   A 1 36  ? 24.398 -6.245  6.644   1.00 11.78 ?  36  VAL   A CG2  1 
ATOM   1013 H H    . VAL   A 1 36  ? 23.323 -4.059  8.364   1.00 13.16 ?  36  VAL   A H    1 
ATOM   1014 H HA   . VAL   A 1 36  ? 25.429 -3.792  6.709   1.00 12.86 ?  36  VAL   A HA   1 
ATOM   1015 H HB   . VAL   A 1 36  ? 22.889 -4.938  6.220   1.00 12.93 ?  36  VAL   A HB   1 
ATOM   1016 H HG11 . VAL   A 1 36  ? 23.960 -5.747  4.210   1.00 13.74 ?  36  VAL   A HG11 1 
ATOM   1017 H HG12 . VAL   A 1 36  ? 23.486 -4.232  4.202   1.00 13.74 ?  36  VAL   A HG12 1 
ATOM   1018 H HG13 . VAL   A 1 36  ? 25.017 -4.587  4.448   1.00 13.74 ?  36  VAL   A HG13 1 
ATOM   1019 H HG21 . VAL   A 1 36  ? 23.989 -6.993  6.172   1.00 14.20 ?  36  VAL   A HG21 1 
ATOM   1020 H HG22 . VAL   A 1 36  ? 25.356 -6.266  6.530   1.00 14.20 ?  36  VAL   A HG22 1 
ATOM   1021 H HG23 . VAL   A 1 36  ? 24.173 -6.302  7.590   1.00 14.20 ?  36  VAL   A HG23 1 
ATOM   1022 N N    . ASN   A 1 37  ? 24.877 -1.812  5.384   1.00 10.42 ?  37  ASN   A N    1 
ATOM   1023 C CA   . ASN   A 1 37  ? 24.525 -0.694  4.527   1.00 10.51 ?  37  ASN   A CA   1 
ATOM   1024 C C    . ASN   A 1 37  ? 24.377 -1.157  3.084   1.00 10.17 ?  37  ASN   A C    1 
ATOM   1025 O O    . ASN   A 1 37  ? 25.160 -1.977  2.594   1.00 10.56 ?  37  ASN   A O    1 
ATOM   1026 C CB   . ASN   A 1 37  ? 25.601 0.396   4.595   1.00 10.71 ?  37  ASN   A CB   1 
ATOM   1027 C CG   . ASN   A 1 37  ? 25.252 1.603   3.754   1.00 10.89 ?  37  ASN   A CG   1 
ATOM   1028 O OD1  . ASN   A 1 37  ? 24.075 1.922   3.579   1.00 11.31 ?  37  ASN   A OD1  1 
ATOM   1029 N ND2  . ASN   A 1 37  ? 26.266 2.275   3.231   1.00 11.11 ?  37  ASN   A ND2  1 
ATOM   1030 H H    . ASN   A 1 37  ? 25.715 -2.025  5.344   1.00 12.56 ?  37  ASN   A H    1 
ATOM   1031 H HA   . ASN   A 1 37  ? 23.687 -0.313  4.821   1.00 12.66 ?  37  ASN   A HA   1 
ATOM   1032 H HB2  . ASN   A 1 37  ? 25.699 0.683   5.518   1.00 12.91 ?  37  ASN   A HB2  1 
ATOM   1033 H HB3  . ASN   A 1 37  ? 26.445 0.028   4.275   1.00 12.91 ?  37  ASN   A HB3  1 
ATOM   1034 H HD21 . ASN   A 1 37  ? 26.114 2.965   2.745   1.00 13.39 ?  37  ASN   A HD21 1 
ATOM   1035 H HD22 . ASN   A 1 37  ? 27.070 2.020   3.369   1.00 13.39 ?  37  ASN   A HD22 1 
ATOM   1036 N N    A ALA   A 1 38  ? 23.367 -0.593  2.412   0.40 10.19 ?  38  ALA   A N    1 
ATOM   1037 N N    B ALA   A 1 38  ? 23.346 -0.648  2.407   0.60 10.98 ?  38  ALA   A N    1 
ATOM   1038 C CA   A ALA   A 1 38  ? 23.168 -0.699  0.965   0.40 10.12 ?  38  ALA   A CA   1 
ATOM   1039 C CA   B ALA   A 1 38  ? 23.155 -0.885  0.974   0.60 11.75 ?  38  ALA   A CA   1 
ATOM   1040 C C    A ALA   A 1 38  ? 24.086 0.319   0.290   0.40 9.81  ?  38  ALA   A C    1 
ATOM   1041 C C    B ALA   A 1 38  ? 23.993 0.140   0.207   0.60 11.11 ?  38  ALA   A C    1 
ATOM   1042 O O    A ALA   A 1 38  ? 23.686 1.433   -0.058  0.40 10.09 ?  38  ALA   A O    1 
ATOM   1043 O O    B ALA   A 1 38  ? 23.518 1.195   -0.230  0.60 11.06 ?  38  ALA   A O    1 
ATOM   1044 C CB   A ALA   A 1 38  ? 21.706 -0.439  0.617   0.40 10.61 ?  38  ALA   A CB   1 
ATOM   1045 C CB   B ALA   A 1 38  ? 21.678 -0.808  0.611   0.60 12.79 ?  38  ALA   A CB   1 
ATOM   1046 H H    A ALA   A 1 38  ? 22.765 -0.111  2.791   0.40 12.28 ?  38  ALA   A H    1 
ATOM   1047 H H    B ALA   A 1 38  ? 22.736 -0.153  2.762   0.60 13.24 ?  38  ALA   A H    1 
ATOM   1048 H HA   A ALA   A 1 38  ? 23.411 -1.584  0.661   0.40 12.21 ?  38  ALA   A HA   1 
ATOM   1049 H HA   B ALA   A 1 38  ? 23.481 -1.779  0.755   0.60 14.16 ?  38  ALA   A HA   1 
ATOM   1050 H HB1  A ALA   A 1 38  ? 21.587 -0.532  -0.341  0.40 12.79 ?  38  ALA   A HB1  1 
ATOM   1051 H HB1  B ALA   A 1 38  ? 21.591 -0.895  -0.349  0.60 15.41 ?  38  ALA   A HB1  1 
ATOM   1052 H HB2  A ALA   A 1 38  ? 21.154 -1.084  1.085   0.40 12.79 ?  38  ALA   A HB2  1 
ATOM   1053 H HB2  B ALA   A 1 38  ? 21.203 -1.530  1.055   0.60 15.41 ?  38  ALA   A HB2  1 
ATOM   1054 H HB3  A ALA   A 1 38  ? 21.470 0.461   0.894   0.40 12.79 ?  38  ALA   A HB3  1 
ATOM   1055 H HB3  B ALA   A 1 38  ? 21.331 0.047   0.900   0.60 15.41 ?  38  ALA   A HB3  1 
ATOM   1056 N N    A ALA   A 1 39  ? 25.346 -0.070  0.114   0.40 9.74  ?  39  ALA   A N    1 
ATOM   1057 N N    B ALA   A 1 39  ? 25.272 -0.188  0.041   0.60 11.33 ?  39  ALA   A N    1 
ATOM   1058 C CA   A ALA   A 1 39  ? 26.390 0.823   -0.363  0.40 10.47 ?  39  ALA   A CA   1 
ATOM   1059 C CA   B ALA   A 1 39  ? 26.270 0.744   -0.448  0.60 10.99 ?  39  ALA   A CA   1 
ATOM   1060 C C    A ALA   A 1 39  ? 26.562 0.729   -1.876  0.40 10.50 ?  39  ALA   A C    1 
ATOM   1061 C C    B ALA   A 1 39  ? 26.357 0.720   -1.970  0.60 10.51 ?  39  ALA   A C    1 
ATOM   1062 O O    A ALA   A 1 39  ? 26.131 -0.233  -2.517  0.40 10.38 ?  39  ALA   A O    1 
ATOM   1063 O O    B ALA   A 1 39  ? 25.839 -0.178  -2.640  0.60 10.71 ?  39  ALA   A O    1 
ATOM   1064 C CB   A ALA   A 1 39  ? 27.714 0.471   0.320   0.40 10.75 ?  39  ALA   A CB   1 
ATOM   1065 C CB   B ALA   A 1 39  ? 27.628 0.382   0.155   0.60 11.44 ?  39  ALA   A CB   1 
ATOM   1066 H H    A ALA   A 1 39  ? 25.627 -0.867  0.271   0.40 11.74 ?  39  ALA   A H    1 
ATOM   1067 H H    B ALA   A 1 39  ? 25.587 -0.976  0.203   0.60 13.65 ?  39  ALA   A H    1 
ATOM   1068 H HA   A ALA   A 1 39  ? 26.164 1.739   -0.139  0.40 12.62 ?  39  ALA   A HA   1 
ATOM   1069 H HA   B ALA   A 1 39  ? 26.027 1.644   -0.160  0.60 13.24 ?  39  ALA   A HA   1 
ATOM   1070 H HB1  A ALA   A 1 39  ? 28.405 1.071   -0.001  0.40 12.95 ?  39  ALA   A HB1  1 
ATOM   1071 H HB1  B ALA   A 1 39  ? 28.284 1.013   -0.170  0.60 13.79 ?  39  ALA   A HB1  1 
ATOM   1072 H HB2  A ALA   A 1 39  ? 27.607 0.572   1.280   0.40 12.95 ?  39  ALA   A HB2  1 
ATOM   1073 H HB2  B ALA   A 1 39  ? 27.562 0.435   1.122   0.60 13.79 ?  39  ALA   A HB2  1 
ATOM   1074 H HB3  A ALA   A 1 39  ? 27.944 -0.446  0.107   0.40 12.95 ?  39  ALA   A HB3  1 
ATOM   1075 H HB3  B ALA   A 1 39  ? 27.855 -0.516  -0.117  0.60 13.79 ?  39  ALA   A HB3  1 
ATOM   1076 N N    A ASN   A 1 40  ? 27.218 1.747   -2.440  0.40 10.63 ?  40  ASN   A N    1 
ATOM   1077 N N    B ASN   A 1 40  ? 27.025 1.735   -2.517  0.60 10.72 ?  40  ASN   A N    1 
ATOM   1078 C CA   A ASN   A 1 40  ? 27.775 1.693   -3.785  0.40 10.71 ?  40  ASN   A CA   1 
ATOM   1079 C CA   B ASN   A 1 40  ? 27.502 1.711   -3.890  0.60 11.22 ?  40  ASN   A CA   1 
ATOM   1080 C C    A ASN   A 1 40  ? 29.298 1.609   -3.706  0.40 10.11 ?  40  ASN   A C    1 
ATOM   1081 C C    B ASN   A 1 40  ? 29.026 1.608   -3.889  0.60 10.69 ?  40  ASN   A C    1 
ATOM   1082 O O    A ASN   A 1 40  ? 29.894 1.719   -2.631  0.40 10.35 ?  40  ASN   A O    1 
ATOM   1083 O O    B ASN   A 1 40  ? 29.670 1.686   -2.843  0.60 10.59 ?  40  ASN   A O    1 
ATOM   1084 C CB   A ASN   A 1 40  ? 27.299 2.867   -4.660  0.40 11.20 ?  40  ASN   A CB   1 
ATOM   1085 C CB   B ASN   A 1 40  ? 27.000 2.929   -4.677  0.60 11.77 ?  40  ASN   A CB   1 
ATOM   1086 C CG   A ASN   A 1 40  ? 27.682 4.223   -4.104  0.40 12.08 ?  40  ASN   A CG   1 
ATOM   1087 C CG   B ASN   A 1 40  ? 27.347 4.248   -4.013  0.60 12.50 ?  40  ASN   A CG   1 
ATOM   1088 O OD1  A ASN   A 1 40  ? 28.862 4.531   -3.964  0.40 12.24 ?  40  ASN   A OD1  1 
ATOM   1089 O OD1  B ASN   A 1 40  ? 28.493 4.485   -3.619  0.60 13.79 ?  40  ASN   A OD1  1 
ATOM   1090 N ND2  A ASN   A 1 40  ? 26.685 5.055   -3.819  0.40 12.96 ?  40  ASN   A ND2  1 
ATOM   1091 N ND2  B ASN   A 1 40  ? 26.349 5.115   -3.886  0.60 13.13 ?  40  ASN   A ND2  1 
ATOM   1092 H H    A ASN   A 1 40  ? 27.361 2.498   -2.047  0.40 12.81 ?  40  ASN   A H    1 
ATOM   1093 H H    B ASN   A 1 40  ? 27.206 2.464   -2.097  0.60 12.92 ?  40  ASN   A H    1 
ATOM   1094 H HA   A ASN   A 1 40  ? 27.473 0.882   -4.212  0.40 12.91 ?  40  ASN   A HA   1 
ATOM   1095 H HA   B ASN   A 1 40  ? 27.145 0.917   -4.323  0.60 13.52 ?  40  ASN   A HA   1 
ATOM   1096 H HB2  A ASN   A 1 40  ? 27.693 2.784   -5.546  0.40 13.50 ?  40  ASN   A HB2  1 
ATOM   1097 H HB2  B ASN   A 1 40  ? 27.401 2.918   -5.559  0.60 14.18 ?  40  ASN   A HB2  1 
ATOM   1098 H HB3  A ASN   A 1 40  ? 26.334 2.836   -4.727  0.40 13.50 ?  40  ASN   A HB3  1 
ATOM   1099 H HB3  B ASN   A 1 40  ? 26.031 2.876   -4.758  0.60 14.18 ?  40  ASN   A HB3  1 
ATOM   1100 H HD21 A ASN   A 1 40  ? 26.855 5.844   -3.511  0.40 15.61 ?  40  ASN   A HD21 1 
ATOM   1101 H HD21 B ASN   A 1 40  ? 26.489 5.883   -3.523  0.60 15.81 ?  40  ASN   A HD21 1 
ATOM   1102 H HD22 A ASN   A 1 40  ? 25.873 4.810   -3.939  0.40 15.61 ?  40  ASN   A HD22 1 
ATOM   1103 H HD22 B ASN   A 1 40  ? 25.564 4.913   -4.173  0.60 15.81 ?  40  ASN   A HD22 1 
ATOM   1104 N N    A VAL   A 1 41  ? 29.926 1.378   -4.864  0.40 9.56  ?  41  VAL   A N    1 
ATOM   1105 N N    B VAL   A 1 41  ? 29.599 1.392   -5.075  0.60 10.79 ?  41  VAL   A N    1 
ATOM   1106 C CA   A VAL   A 1 41  ? 31.354 1.069   -4.876  0.40 9.85  ?  41  VAL   A CA   1 
ATOM   1107 C CA   B VAL   A 1 41  ? 31.028 1.088   -5.167  0.60 11.38 ?  41  VAL   A CA   1 
ATOM   1108 C C    A VAL   A 1 41  ? 32.182 2.221   -4.333  0.40 9.79  ?  41  VAL   A C    1 
ATOM   1109 C C    B VAL   A 1 41  ? 31.911 2.235   -4.706  0.60 10.95 ?  41  VAL   A C    1 
ATOM   1110 O O    A VAL   A 1 41  ? 33.269 2.001   -3.787  0.40 9.30  ?  41  VAL   A O    1 
ATOM   1111 O O    B VAL   A 1 41  ? 33.087 2.014   -4.378  0.60 10.08 ?  41  VAL   A O    1 
ATOM   1112 C CB   A VAL   A 1 41  ? 31.843 0.584   -6.263  0.40 9.45  ?  41  VAL   A CB   1 
ATOM   1113 C CB   B VAL   A 1 41  ? 31.444 0.658   -6.589  0.60 12.31 ?  41  VAL   A CB   1 
ATOM   1114 C CG1  A VAL   A 1 41  ? 31.143 -0.715  -6.658  0.40 9.67  ?  41  VAL   A CG1  1 
ATOM   1115 C CG1  B VAL   A 1 41  ? 30.765 -0.645  -6.977  0.60 13.10 ?  41  VAL   A CG1  1 
ATOM   1116 C CG2  A VAL   A 1 41  ? 31.668 1.653   -7.343  0.40 9.27  ?  41  VAL   A CG2  1 
ATOM   1117 C CG2  B VAL   A 1 41  ? 31.157 1.767   -7.609  0.60 13.28 ?  41  VAL   A CG2  1 
ATOM   1118 H H    A VAL   A 1 41  ? 29.560 1.391   -5.640  0.40 11.53 ?  41  VAL   A H    1 
ATOM   1119 H H    B VAL   A 1 41  ? 29.180 1.404   -5.825  0.60 13.01 ?  41  VAL   A H    1 
ATOM   1120 H HA   A VAL   A 1 41  ? 31.510 0.338   -4.273  0.40 11.88 ?  41  VAL   A HA   1 
ATOM   1121 H HA   B VAL   A 1 41  ? 31.206 0.343   -4.573  0.60 13.71 ?  41  VAL   A HA   1 
ATOM   1122 H HB   A VAL   A 1 41  ? 32.795 0.387   -6.214  0.40 11.40 ?  41  VAL   A HB   1 
ATOM   1123 H HB   B VAL   A 1 41  ? 32.403 0.506   -6.579  0.60 14.83 ?  41  VAL   A HB   1 
ATOM   1124 H HG11 A VAL   A 1 41  ? 31.477 -1.013  -7.520  0.40 11.66 ?  41  VAL   A HG11 1 
ATOM   1125 H HG11 B VAL   A 1 41  ? 31.049 -0.890  -7.869  0.60 15.78 ?  41  VAL   A HG11 1 
ATOM   1126 H HG12 A VAL   A 1 41  ? 31.325 -1.388  -5.983  0.40 11.66 ?  41  VAL   A HG12 1 
ATOM   1127 H HG12 B VAL   A 1 41  ? 31.021 -1.337  -6.344  0.60 15.78 ?  41  VAL   A HG12 1 
ATOM   1128 H HG13 A VAL   A 1 41  ? 30.187 -0.554  -6.714  0.40 11.66 ?  41  VAL   A HG13 1 
ATOM   1129 H HG13 B VAL   A 1 41  ? 29.804 -0.520  -6.955  0.60 15.78 ?  41  VAL   A HG13 1 
ATOM   1130 H HG21 A VAL   A 1 41  ? 31.933 1.283   -8.204  0.40 11.19 ?  41  VAL   A HG21 1 
ATOM   1131 H HG21 B VAL   A 1 41  ? 31.393 1.442   -8.492  0.60 15.99 ?  41  VAL   A HG21 1 
ATOM   1132 H HG22 A VAL   A 1 41  ? 30.735 1.915   -7.375  0.40 11.19 ?  41  VAL   A HG22 1 
ATOM   1133 H HG22 B VAL   A 1 41  ? 30.213 1.988   -7.580  0.60 15.99 ?  41  VAL   A HG22 1 
ATOM   1134 H HG23 A VAL   A 1 41  ? 32.222 2.415   -7.127  0.40 11.19 ?  41  VAL   A HG23 1 
ATOM   1135 H HG23 B VAL   A 1 41  ? 31.687 2.550   -7.393  0.60 15.99 ?  41  VAL   A HG23 1 
ATOM   1136 N N    A TYR   A 1 42  ? 31.696 3.456   -4.458  0.40 10.28 ?  42  TYR   A N    1 
ATOM   1137 N N    B TYR   A 1 42  ? 31.389 3.463   -4.709  0.60 11.04 ?  42  TYR   A N    1 
ATOM   1138 C CA   A TYR   A 1 42  ? 32.437 4.629   -4.006  0.40 10.86 ?  42  TYR   A CA   1 
ATOM   1139 C CA   B TYR   A 1 42  ? 32.131 4.651   -4.308  0.60 11.17 ?  42  TYR   A CA   1 
ATOM   1140 C C    A TYR   A 1 42  ? 32.117 4.996   -2.564  0.40 10.84 ?  42  TYR   A C    1 
ATOM   1141 C C    B TYR   A 1 42  ? 31.914 5.013   -2.851  0.60 10.94 ?  42  TYR   A C    1 
ATOM   1142 O O    A TYR   A 1 42  ? 32.687 5.961   -2.040  0.40 11.10 ?  42  TYR   A O    1 
ATOM   1143 O O    B TYR   A 1 42  ? 32.479 6.013   -2.388  0.60 11.22 ?  42  TYR   A O    1 
ATOM   1144 C CB   A TYR   A 1 42  ? 32.174 5.832   -4.933  0.40 11.76 ?  42  TYR   A CB   1 
ATOM   1145 C CB   B TYR   A 1 42  ? 31.754 5.840   -5.211  0.60 11.80 ?  42  TYR   A CB   1 
ATOM   1146 C CG   A TYR   A 1 42  ? 32.294 5.517   -6.414  0.40 13.03 ?  42  TYR   A CG   1 
ATOM   1147 C CG   B TYR   A 1 42  ? 31.973 5.545   -6.675  0.60 13.43 ?  42  TYR   A CG   1 
ATOM   1148 C CD1  A TYR   A 1 42  ? 33.533 5.333   -7.016  0.40 13.95 ?  42  TYR   A CD1  1 
ATOM   1149 C CD1  B TYR   A 1 42  ? 33.248 5.367   -7.171  0.60 14.09 ?  42  TYR   A CD1  1 
ATOM   1150 C CD2  A TYR   A 1 42  ? 31.163 5.401   -7.211  0.40 14.07 ?  42  TYR   A CD2  1 
ATOM   1151 C CD2  B TYR   A 1 42  ? 30.905 5.414   -7.555  0.60 14.93 ?  42  TYR   A CD2  1 
ATOM   1152 C CE1  A TYR   A 1 42  ? 33.639 5.039   -8.370  0.40 14.62 ?  42  TYR   A CE1  1 
ATOM   1153 C CE1  B TYR   A 1 42  ? 33.466 5.080   -8.500  0.60 15.04 ?  42  TYR   A CE1  1 
ATOM   1154 C CE2  A TYR   A 1 42  ? 31.260 5.114   -8.561  0.40 14.91 ?  42  TYR   A CE2  1 
ATOM   1155 C CE2  B TYR   A 1 42  ? 31.115 5.131   -8.898  0.60 16.10 ?  42  TYR   A CE2  1 
ATOM   1156 C CZ   A TYR   A 1 42  ? 32.500 4.936   -9.135  0.40 15.32 ?  42  TYR   A CZ   1 
ATOM   1157 C CZ   B TYR   A 1 42  ? 32.402 4.964   -9.362  0.60 16.22 ?  42  TYR   A CZ   1 
ATOM   1158 O OH   A TYR   A 1 42  ? 32.591 4.645   -10.477 0.40 16.65 ?  42  TYR   A OH   1 
ATOM   1159 O OH   B TYR   A 1 42  ? 32.637 4.676   -10.688 0.60 17.96 ?  42  TYR   A OH   1 
ATOM   1160 H H    A TYR   A 1 42  ? 30.934 3.640   -4.799  0.40 12.39 ?  42  TYR   A H    1 
ATOM   1161 H H    B TYR   A 1 42  ? 30.581 3.643   -4.953  0.60 13.31 ?  42  TYR   A H    1 
ATOM   1162 H HA   A TYR   A 1 42  ? 33.391 4.434   -4.067  0.40 13.08 ?  42  TYR   A HA   1 
ATOM   1163 H HA   B TYR   A 1 42  ? 33.073 4.489   -4.427  0.60 13.46 ?  42  TYR   A HA   1 
ATOM   1164 H HB2  A TYR   A 1 42  ? 31.278 6.159   -4.777  0.40 14.17 ?  42  TYR   A HB2  1 
ATOM   1165 H HB2  B TYR   A 1 42  ? 30.813 6.057   -5.086  0.60 14.22 ?  42  TYR   A HB2  1 
ATOM   1166 H HB3  A TYR   A 1 42  ? 32.819 6.533   -4.732  0.40 14.17 ?  42  TYR   A HB3  1 
ATOM   1167 H HB3  B TYR   A 1 42  ? 32.299 6.610   -4.978  0.60 14.22 ?  42  TYR   A HB3  1 
ATOM   1168 H HD1  A TYR   A 1 42  ? 34.310 5.405   -6.510  0.40 16.80 ?  42  TYR   A HD1  1 
ATOM   1169 H HD1  B TYR   A 1 42  ? 33.973 5.446   -6.593  0.60 16.96 ?  42  TYR   A HD1  1 
ATOM   1170 H HD2  A TYR   A 1 42  ? 30.325 5.522   -6.831  0.40 16.94 ?  42  TYR   A HD2  1 
ATOM   1171 H HD2  B TYR   A 1 42  ? 30.033 5.531   -7.242  0.60 17.97 ?  42  TYR   A HD2  1 
ATOM   1172 H HE1  A TYR   A 1 42  ? 34.475 4.917   -8.766  0.40 17.60 ?  42  TYR   A HE1  1 
ATOM   1173 H HE1  B TYR   A 1 42  ? 34.334 4.967   -8.808  0.60 18.11 ?  42  TYR   A HE1  1 
ATOM   1174 H HE2  A TYR   A 1 42  ? 30.487 5.037   -9.079  0.40 17.94 ?  42  TYR   A HE2  1 
ATOM   1175 H HE2  B TYR   A 1 42  ? 30.392 5.048   -9.478  0.60 19.38 ?  42  TYR   A HE2  1 
ATOM   1176 H HH   A TYR   A 1 42  ? 33.395 4.552   -10.703 0.40 20.04 ?  42  TYR   A HH   1 
ATOM   1177 H HH   B TYR   A 1 42  ? 33.466 4.591   -10.813 0.60 21.61 ?  42  TYR   A HH   1 
ATOM   1178 N N    A LEU   A 1 43  ? 31.220 4.253   -1.916  0.40 10.65 ?  43  LEU   A N    1 
ATOM   1179 N N    B LEU   A 1 43  ? 31.102 4.235   -2.130  0.60 10.94 ?  43  LEU   A N    1 
ATOM   1180 C CA   A LEU   A 1 43  ? 30.784 4.554   -0.556  0.40 10.36 ?  43  LEU   A CA   1 
ATOM   1181 C CA   B LEU   A 1 43  ? 30.683 4.564   -0.770  0.60 10.93 ?  43  LEU   A CA   1 
ATOM   1182 C C    A LEU   A 1 43  ? 30.265 5.985   -0.437  0.40 10.75 ?  43  LEU   A C    1 
ATOM   1183 C C    B LEU   A 1 43  ? 30.225 6.016   -0.660  0.60 11.25 ?  43  LEU   A C    1 
ATOM   1184 O O    A LEU   A 1 43  ? 30.450 6.653   0.583   0.40 11.17 ?  43  LEU   A O    1 
ATOM   1185 O O    B LEU   A 1 43  ? 30.571 6.725   0.285   0.60 11.81 ?  43  LEU   A O    1 
ATOM   1186 C CB   A LEU   A 1 43  ? 31.868 4.254   0.480   0.40 10.59 ?  43  LEU   A CB   1 
ATOM   1187 C CB   B LEU   A 1 43  ? 31.753 4.249   0.272   0.60 10.97 ?  43  LEU   A CB   1 
ATOM   1188 C CG   A LEU   A 1 43  ? 32.391 2.812   0.532   0.40 11.04 ?  43  LEU   A CG   1 
ATOM   1189 C CG   B LEU   A 1 43  ? 32.237 2.800   0.374   0.60 11.33 ?  43  LEU   A CG   1 
ATOM   1190 C CD1  A LEU   A 1 43  ? 33.507 2.702   1.563   0.40 11.69 ?  43  LEU   A CD1  1 
ATOM   1191 C CD1  B LEU   A 1 43  ? 33.280 2.696   1.481   0.60 12.44 ?  43  LEU   A CD1  1 
ATOM   1192 C CD2  A LEU   A 1 43  ? 31.280 1.819   0.836   0.40 11.15 ?  43  LEU   A CD2  1 
ATOM   1193 C CD2  B LEU   A 1 43  ? 31.085 1.832   0.613   0.60 11.47 ?  43  LEU   A CD2  1 
ATOM   1194 H H    A LEU   A 1 43  ? 30.850 3.551   -2.254  0.40 12.83 ?  43  LEU   A H    1 
ATOM   1195 H H    B LEU   A 1 43  ? 30.771 3.495   -2.418  0.60 13.19 ?  43  LEU   A H    1 
ATOM   1196 H HA   A LEU   A 1 43  ? 30.039 3.979   -0.359  0.40 12.49 ?  43  LEU   A HA   1 
ATOM   1197 H HA   B LEU   A 1 43  ? 29.914 4.003   -0.559  0.60 13.18 ?  43  LEU   A HA   1 
ATOM   1198 H HB2  A LEU   A 1 43  ? 32.630 4.831   0.309   0.40 12.76 ?  43  LEU   A HB2  1 
ATOM   1199 H HB2  B LEU   A 1 43  ? 32.525 4.798   0.072   0.60 13.22 ?  43  LEU   A HB2  1 
ATOM   1200 H HB3  A LEU   A 1 43  ? 31.501 4.450   1.352   0.40 12.76 ?  43  LEU   A HB3  1 
ATOM   1201 H HB3  B LEU   A 1 43  ? 31.401 4.496   1.141   0.60 13.22 ?  43  LEU   A HB3  1 
ATOM   1202 H HG   A LEU   A 1 43  ? 32.767 2.583   -0.333  0.40 13.30 ?  43  LEU   A HG   1 
ATOM   1203 H HG   B LEU   A 1 43  ? 32.665 2.555   -0.460  0.60 13.66 ?  43  LEU   A HG   1 
ATOM   1204 H HD11 A LEU   A 1 43  ? 33.828 1.788   1.584   0.40 14.08 ?  43  LEU   A HD11 1 
ATOM   1205 H HD11 B LEU   A 1 43  ? 33.585 1.780   1.543   0.60 14.98 ?  43  LEU   A HD11 1 
ATOM   1206 H HD12 A LEU   A 1 43  ? 34.228 3.301   1.313   0.40 14.08 ?  43  LEU   A HD12 1 
ATOM   1207 H HD12 B LEU   A 1 43  ? 34.027 3.281   1.268   0.60 14.98 ?  43  LEU   A HD12 1 
ATOM   1208 H HD13 A LEU   A 1 43  ? 33.157 2.951   2.433   0.40 14.08 ?  43  LEU   A HD13 1 
ATOM   1209 H HD13 B LEU   A 1 43  ? 32.879 2.971   2.322   0.60 14.98 ?  43  LEU   A HD13 1 
ATOM   1210 H HD21 A LEU   A 1 43  ? 31.669 0.940   0.950   0.40 13.44 ?  43  LEU   A HD21 1 
ATOM   1211 H HD21 B LEU   A 1 43  ? 31.447 0.950   0.775   0.60 13.83 ?  43  LEU   A HD21 1 
ATOM   1212 H HD22 A LEU   A 1 43  ? 30.831 2.094   1.651   0.40 13.44 ?  43  LEU   A HD22 1 
ATOM   1213 H HD22 B LEU   A 1 43  ? 30.579 2.132   1.385   0.60 13.83 ?  43  LEU   A HD22 1 
ATOM   1214 H HD23 A LEU   A 1 43  ? 30.654 1.815   0.097   0.40 13.44 ?  43  LEU   A HD23 1 
ATOM   1215 H HD23 B LEU   A 1 43  ? 30.517 1.822   -0.172  0.60 13.83 ?  43  LEU   A HD23 1 
ATOM   1216 N N    A LYS   A 1 44  ? 29.588 6.447   -1.490  0.40 10.79 ?  44  LYS   A N    1 
ATOM   1217 N N    B LYS   A 1 44  ? 29.438 6.459   -1.642  0.60 11.40 ?  44  LYS   A N    1 
ATOM   1218 C CA   A LYS   A 1 44  ? 28.946 7.762   -1.498  0.40 11.61 ?  44  LYS   A CA   1 
ATOM   1219 C CA   B LYS   A 1 44  ? 28.779 7.765   -1.616  0.60 12.07 ?  44  LYS   A CA   1 
ATOM   1220 C C    A LYS   A 1 44  ? 27.514 7.572   -1.021  0.40 11.42 ?  44  LYS   A C    1 
ATOM   1221 C C    B LYS   A 1 44  ? 27.374 7.537   -1.064  0.60 11.41 ?  44  LYS   A C    1 
ATOM   1222 O O    A LYS   A 1 44  ? 26.648 7.097   -1.762  0.40 12.16 ?  44  LYS   A O    1 
ATOM   1223 O O    B LYS   A 1 44  ? 26.499 7.008   -1.754  0.60 12.27 ?  44  LYS   A O    1 
ATOM   1224 C CB   A LYS   A 1 44  ? 29.005 8.396   -2.883  0.40 13.11 ?  44  LYS   A CB   1 
ATOM   1225 C CB   B LYS   A 1 44  ? 28.726 8.367   -3.016  0.60 14.23 ?  44  LYS   A CB   1 
ATOM   1226 C CG   A LYS   A 1 44  ? 30.401 8.829   -3.317  0.40 15.33 ?  44  LYS   A CG   1 
ATOM   1227 C CG   B LYS   A 1 44  ? 30.051 8.880   -3.549  0.60 17.50 ?  44  LYS   A CG   1 
ATOM   1228 C CD   A LYS   A 1 44  ? 31.087 9.710   -2.282  0.40 18.68 ?  44  LYS   A CD   1 
ATOM   1229 C CD   B LYS   A 1 44  ? 30.689 9.906   -2.627  0.60 21.61 ?  44  LYS   A CD   1 
ATOM   1230 C CE   A LYS   A 1 44  ? 32.424 10.217  -2.790  0.40 20.74 ?  44  LYS   A CE   1 
ATOM   1231 C CE   B LYS   A 1 44  ? 31.861 10.586  -3.313  0.60 24.18 ?  44  LYS   A CE   1 
ATOM   1232 N NZ   A LYS   A 1 44  ? 33.182 10.924  -1.727  0.40 21.88 ?  44  LYS   A NZ   1 
ATOM   1233 N NZ   B LYS   A 1 44  ? 32.845 11.138  -2.346  0.60 26.03 ?  44  LYS   A NZ   1 
ATOM   1234 H H    A LYS   A 1 44  ? 29.481 6.007   -2.226  0.40 13.00 ?  44  LYS   A H    1 
ATOM   1235 H H    B LYS   A 1 44  ? 29.268 6.012   -2.359  0.60 13.74 ?  44  LYS   A H    1 
ATOM   1236 H HA   A LYS   A 1 44  ? 29.390 8.343   -0.864  0.40 13.99 ?  44  LYS   A HA   1 
ATOM   1237 H HA   B LYS   A 1 44  ? 29.253 8.368   -1.022  0.60 14.54 ?  44  LYS   A HA   1 
ATOM   1238 H HB2  A LYS   A 1 44  ? 28.679 7.757   -3.535  0.40 15.79 ?  44  LYS   A HB2  1 
ATOM   1239 H HB2  B LYS   A 1 44  ? 28.406 7.688   -3.631  0.60 17.13 ?  44  LYS   A HB2  1 
ATOM   1240 H HB3  A LYS   A 1 44  ? 28.438 9.185   -2.889  0.40 15.79 ?  44  LYS   A HB3  1 
ATOM   1241 H HB3  B LYS   A 1 44  ? 28.106 9.115   -3.010  0.60 17.13 ?  44  LYS   A HB3  1 
ATOM   1242 H HG2  A LYS   A 1 44  ? 30.948 8.041   -3.453  0.40 18.45 ?  44  LYS   A HG2  1 
ATOM   1243 H HG2  B LYS   A 1 44  ? 30.662 8.134   -3.646  0.60 21.05 ?  44  LYS   A HG2  1 
ATOM   1244 H HG3  A LYS   A 1 44  ? 30.333 9.333   -4.145  0.40 18.45 ?  44  LYS   A HG3  1 
ATOM   1245 H HG3  B LYS   A 1 44  ? 29.903 9.302   -4.412  0.60 21.05 ?  44  LYS   A HG3  1 
ATOM   1246 H HD2  A LYS   A 1 44  ? 30.516 10.472  -2.085  0.40 22.47 ?  44  LYS   A HD2  1 
ATOM   1247 H HD2  B LYS   A 1 44  ? 30.033 10.577  -2.388  0.60 25.99 ?  44  LYS   A HD2  1 
ATOM   1248 H HD3  A LYS   A 1 44  ? 31.249 9.194   -1.478  0.40 22.47 ?  44  LYS   A HD3  1 
ATOM   1249 H HD3  B LYS   A 1 44  ? 31.019 9.456   -1.830  0.60 25.99 ?  44  LYS   A HD3  1 
ATOM   1250 H HE2  A LYS   A 1 44  ? 32.953 9.462   -3.091  0.40 24.95 ?  44  LYS   A HE2  1 
ATOM   1251 H HE2  B LYS   A 1 44  ? 32.318 9.938   -3.873  0.60 29.07 ?  44  LYS   A HE2  1 
ATOM   1252 H HE3  A LYS   A 1 44  ? 32.271 10.834  -3.522  0.40 24.95 ?  44  LYS   A HE3  1 
ATOM   1253 H HE3  B LYS   A 1 44  ? 31.526 11.316  -3.855  0.60 29.07 ?  44  LYS   A HE3  1 
ATOM   1254 H HZ1  A LYS   A 1 44  ? 33.958 11.210  -2.050  0.40 26.32 ?  44  LYS   A HZ1  1 
ATOM   1255 H HZ1  B LYS   A 1 44  ? 33.516 11.528  -2.784  0.60 31.29 ?  44  LYS   A HZ1  1 
ATOM   1256 H HZ2  A LYS   A 1 44  ? 32.713 11.627  -1.438  0.40 26.32 ?  44  LYS   A HZ2  1 
ATOM   1257 H HZ2  B LYS   A 1 44  ? 32.454 11.741  -1.822  0.60 31.29 ?  44  LYS   A HZ2  1 
ATOM   1258 H HZ3  A LYS   A 1 44  ? 33.332 10.377  -1.044  0.40 26.32 ?  44  LYS   A HZ3  1 
ATOM   1259 H HZ3  B LYS   A 1 44  ? 33.176 10.484  -1.839  0.60 31.29 ?  44  LYS   A HZ3  1 
ATOM   1260 N N    A HIS   A 1 45  ? 27.271 7.942   0.231   0.40 11.15 ?  45  HIS   A N    1 
ATOM   1261 N N    B HIS   A 1 45  ? 27.162 7.921   0.191   0.60 11.04 ?  45  HIS   A N    1 
ATOM   1262 C CA   A HIS   A 1 45  ? 26.025 7.623   0.919   0.40 11.24 ?  45  HIS   A CA   1 
ATOM   1263 C CA   B HIS   A 1 45  ? 25.936 7.566   0.910   0.60 11.28 ?  45  HIS   A CA   1 
ATOM   1264 C C    A HIS   A 1 45  ? 25.073 8.808   0.789   0.40 11.74 ?  45  HIS   A C    1 
ATOM   1265 C C    B HIS   A 1 45  ? 24.869 8.648   0.732   0.60 11.34 ?  45  HIS   A C    1 
ATOM   1266 O O    A HIS   A 1 45  ? 24.862 9.584   1.720   0.40 12.46 ?  45  HIS   A O    1 
ATOM   1267 O O    B HIS   A 1 45  ? 24.510 9.373   1.659   0.60 12.10 ?  45  HIS   A O    1 
ATOM   1268 C CB   A HIS   A 1 45  ? 26.326 7.275   2.365   0.40 10.76 ?  45  HIS   A CB   1 
ATOM   1269 C CB   B HIS   A 1 45  ? 26.246 7.350   2.383   0.60 11.22 ?  45  HIS   A CB   1 
ATOM   1270 C CG   A HIS   A 1 45  ? 27.450 6.301   2.517   0.40 10.35 ?  45  HIS   A CG   1 
ATOM   1271 C CG   B HIS   A 1 45  ? 27.378 6.408   2.632   0.60 10.91 ?  45  HIS   A CG   1 
ATOM   1272 N ND1  A HIS   A 1 45  ? 27.407 5.023   1.997   0.40 10.05 ?  45  HIS   A ND1  1 
ATOM   1273 N ND1  B HIS   A 1 45  ? 27.397 5.111   2.161   0.60 11.34 ?  45  HIS   A ND1  1 
ATOM   1274 C CD2  A HIS   A 1 45  ? 28.660 6.429   3.113   0.40 10.77 ?  45  HIS   A CD2  1 
ATOM   1275 C CD2  B HIS   A 1 45  ? 28.541 6.589   3.302   0.60 10.56 ?  45  HIS   A CD2  1 
ATOM   1276 C CE1  A HIS   A 1 45  ? 28.540 4.404   2.280   0.40 10.11 ?  45  HIS   A CE1  1 
ATOM   1277 C CE1  B HIS   A 1 45  ? 28.527 4.538   2.534   0.60 10.29 ?  45  HIS   A CE1  1 
ATOM   1278 N NE2  A HIS   A 1 45  ? 29.316 5.233   2.958   0.40 10.67 ?  45  HIS   A NE2  1 
ATOM   1279 N NE2  B HIS   A 1 45  ? 29.237 5.409   3.231   0.60 10.19 ?  45  HIS   A NE2  1 
ATOM   1280 H H    A HIS   A 1 45  ? 27.829 8.389   0.709   0.40 13.43 ?  45  HIS   A H    1 
ATOM   1281 H H    B HIS   A 1 45  ? 27.709 8.394   0.655   0.60 13.30 ?  45  HIS   A H    1 
ATOM   1282 H HA   A HIS   A 1 45  ? 25.616 6.858   0.496   0.40 13.55 ?  45  HIS   A HA   1 
ATOM   1283 H HA   B HIS   A 1 45  ? 25.584 6.734   0.549   0.60 13.59 ?  45  HIS   A HA   1 
ATOM   1284 H HB2  A HIS   A 1 45  ? 26.565 8.083   2.844   0.40 12.97 ?  45  HIS   A HB2  1 
ATOM   1285 H HB2  B HIS   A 1 45  ? 26.467 8.206   2.780   0.60 13.52 ?  45  HIS   A HB2  1 
ATOM   1286 H HB3  A HIS   A 1 45  ? 25.535 6.877   2.761   0.40 12.97 ?  45  HIS   A HB3  1 
ATOM   1287 H HB3  B HIS   A 1 45  ? 25.455 6.984   2.815   0.60 13.52 ?  45  HIS   A HB3  1 
ATOM   1288 H HD2  A HIS   A 1 45  ? 28.988 7.183   3.551   0.40 12.98 ?  45  HIS   A HD2  1 
ATOM   1289 H HD2  B HIS   A 1 45  ? 28.817 7.373   3.730   0.60 12.73 ?  45  HIS   A HD2  1 
ATOM   1290 H HE1  A HIS   A 1 45  ? 28.757 3.526   2.053   0.40 12.19 ?  45  HIS   A HE1  1 
ATOM   1291 H HE1  B HIS   A 1 45  ? 28.775 3.666   2.346   0.60 12.41 ?  45  HIS   A HE1  1 
ATOM   1292 H HE2  A HIS   A 1 45  ? 30.108 5.051   3.253   0.40 12.86 ?  45  HIS   A HE2  1 
ATOM   1293 H HE2  B HIS   A 1 45  ? 30.008 5.265   3.576   0.60 12.28 ?  45  HIS   A HE2  1 
ATOM   1294 N N    A GLY   A 1 46  ? 24.494 8.939   -0.401  0.40 11.83 ?  46  GLY   A N    1 
ATOM   1295 N N    B GLY   A 1 46  ? 24.322 8.713   -0.477  0.60 11.97 ?  46  GLY   A N    1 
ATOM   1296 C CA   A GLY   A 1 46  ? 23.707 10.111  -0.736  0.40 11.68 ?  46  GLY   A CA   1 
ATOM   1297 C CA   B GLY   A 1 46  ? 23.466 9.829   -0.843  0.60 12.55 ?  46  GLY   A CA   1 
ATOM   1298 C C    A GLY   A 1 46  ? 22.202 9.974   -0.591  0.40 11.34 ?  46  GLY   A C    1 
ATOM   1299 C C    B GLY   A 1 46  ? 22.013 9.741   -0.402  0.60 12.68 ?  46  GLY   A C    1 
ATOM   1300 O O    A GLY   A 1 46  ? 21.502 10.980  -0.444  0.40 11.68 ?  46  GLY   A O    1 
ATOM   1301 O O    B GLY   A 1 46  ? 21.418 10.744  0.017   0.60 12.97 ?  46  GLY   A O    1 
ATOM   1302 H H    A GLY   A 1 46  ? 24.552 8.360   -1.033  0.40 14.26 ?  46  GLY   A H    1 
ATOM   1303 H H    B GLY   A 1 46  ? 24.420 8.123   -1.094  0.60 14.42 ?  46  GLY   A H    1 
ATOM   1304 H HA2  A GLY   A 1 46  ? 24.011 10.854  -0.187  0.40 14.07 ?  46  GLY   A HA2  1 
ATOM   1305 H HA2  B GLY   A 1 46  ? 23.822 10.635  -0.451  0.60 15.12 ?  46  GLY   A HA2  1 
ATOM   1306 H HA3  A GLY   A 1 46  ? 23.878 10.341  -1.662  0.40 14.07 ?  46  GLY   A HA3  1 
ATOM   1307 H HA3  B GLY   A 1 46  ? 23.488 9.929   -1.808  0.60 15.12 ?  46  GLY   A HA3  1 
ATOM   1308 N N    A GLY   A 1 47  ? 21.681 8.754   -0.661  0.40 11.03 ?  47  GLY   A N    1 
ATOM   1309 N N    B GLY   A 1 47  ? 21.413 8.563   -0.511  0.60 13.06 ?  47  GLY   A N    1 
ATOM   1310 C CA   A GLY   A 1 47  ? 20.244 8.544   -0.641  0.40 11.09 ?  47  GLY   A CA   1 
ATOM   1311 C CA   B GLY   A 1 47  ? 19.991 8.427   -0.276  0.60 12.57 ?  47  GLY   A CA   1 
ATOM   1312 C C    A GLY   A 1 47  ? 19.925 7.087   -0.378  0.40 10.25 ?  47  GLY   A C    1 
ATOM   1313 C C    B GLY   A 1 47  ? 19.652 7.010   0.128   0.60 11.30 ?  47  GLY   A C    1 
ATOM   1314 O O    A GLY   A 1 47  ? 20.815 6.249   -0.227  0.40 10.45 ?  47  GLY   A O    1 
ATOM   1315 O O    B GLY   A 1 47  ? 20.537 6.167   0.311   0.60 10.74 ?  47  GLY   A O    1 
ATOM   1316 H H    A GLY   A 1 47  ? 22.143 8.038   -0.719  0.40 13.29 ?  47  GLY   A H    1 
ATOM   1317 H H    B GLY   A 1 47  ? 21.807 7.817   -0.708  0.60 15.72 ?  47  GLY   A H    1 
ATOM   1318 H HA2  A GLY   A 1 47  ? 19.837 9.101   0.048   0.40 13.36 ?  47  GLY   A HA2  1 
ATOM   1319 H HA2  B GLY   A 1 47  ? 19.716 9.017   0.439   0.60 15.14 ?  47  GLY   A HA2  1 
ATOM   1320 H HA3  A GLY   A 1 47  ? 19.872 8.789   -1.500  0.40 13.36 ?  47  GLY   A HA3  1 
ATOM   1321 H HA3  B GLY   A 1 47  ? 19.494 8.665   -1.083  0.60 15.14 ?  47  GLY   A HA3  1 
ATOM   1322 N N    A GLY   A 1 48  ? 18.633 6.779   -0.349  0.40 9.95  ?  48  GLY   A N    1 
ATOM   1323 N N    B GLY   A 1 48  ? 18.351 6.752   0.267   0.60 11.26 ?  48  GLY   A N    1 
ATOM   1324 C CA   A GLY   A 1 48  ? 18.193 5.442   -0.003  0.40 9.52  ?  48  GLY   A CA   1 
ATOM   1325 C CA   B GLY   A 1 48  ? 17.919 5.430   0.677   0.60 10.54 ?  48  GLY   A CA   1 
ATOM   1326 C C    A GLY   A 1 48  ? 18.618 5.078   1.406   0.40 9.14  ?  48  GLY   A C    1 
ATOM   1327 C C    B GLY   A 1 48  ? 18.509 5.050   2.026   0.60 10.48 ?  48  GLY   A C    1 
ATOM   1328 O O    A GLY   A 1 48  ? 18.784 5.936   2.280   0.40 9.63  ?  48  GLY   A O    1 
ATOM   1329 O O    B GLY   A 1 48  ? 18.708 5.882   2.922   0.60 10.62 ?  48  GLY   A O    1 
ATOM   1330 H H    A GLY   A 1 48  ? 18.010 7.321   -0.524  0.40 12.00 ?  48  GLY   A H    1 
ATOM   1331 H H    B GLY   A 1 48  ? 17.705 7.322   0.131   0.60 13.57 ?  48  GLY   A H    1 
ATOM   1332 H HA2  A GLY   A 1 48  ? 17.230 5.390   -0.063  0.40 11.48 ?  48  GLY   A HA2  1 
ATOM   1333 H HA2  B GLY   A 1 48  ? 16.943 5.406   0.735   0.60 12.71 ?  48  GLY   A HA2  1 
ATOM   1334 H HA3  A GLY   A 1 48  ? 18.584 4.793   -0.608  0.40 11.48 ?  48  GLY   A HA3  1 
ATOM   1335 H HA3  B GLY   A 1 48  ? 18.192 4.775   0.013   0.60 12.71 ?  48  GLY   A HA3  1 
ATOM   1336 N N    A VAL   A 1 49  ? 18.822 3.775   1.626   0.40 10.08 ?  49  VAL   A N    1 
ATOM   1337 N N    B VAL   A 1 49  ? 18.790 3.754   2.172   0.60 9.90  ?  49  VAL   A N    1 
ATOM   1338 C CA   A VAL   A 1 49  ? 19.280 3.306   2.932   0.40 10.11 ?  49  VAL   A CA   1 
ATOM   1339 C CA   B VAL   A 1 49  ? 19.355 3.241   3.416   0.60 10.50 ?  49  VAL   A CA   1 
ATOM   1340 C C    A VAL   A 1 49  ? 20.609 3.954   3.302   0.40 9.54  ?  49  VAL   A C    1 
ATOM   1341 C C    B VAL   A 1 49  ? 20.662 3.953   3.752   0.60 10.28 ?  49  VAL   A C    1 
ATOM   1342 O O    A VAL   A 1 49  ? 20.822 4.344   4.454   0.40 9.77  ?  49  VAL   A O    1 
ATOM   1343 O O    B VAL   A 1 49  ? 20.889 4.370   4.896   0.60 10.56 ?  49  VAL   A O    1 
ATOM   1344 C CB   A VAL   A 1 49  ? 19.375 1.769   2.959   0.40 11.20 ?  49  VAL   A CB   1 
ATOM   1345 C CB   B VAL   A 1 49  ? 19.559 1.721   3.306   0.60 11.26 ?  49  VAL   A CB   1 
ATOM   1346 C CG1  A VAL   A 1 49  ? 20.046 1.297   4.248   0.40 11.72 ?  49  VAL   A CG1  1 
ATOM   1347 C CG1  B VAL   A 1 49  ? 20.449 1.227   4.427   0.60 11.43 ?  49  VAL   A CG1  1 
ATOM   1348 C CG2  A VAL   A 1 49  ? 17.995 1.150   2.831   0.40 11.93 ?  49  VAL   A CG2  1 
ATOM   1349 C CG2  B VAL   A 1 49  ? 18.213 0.995   3.310   0.60 12.23 ?  49  VAL   A CG2  1 
ATOM   1350 H H    A VAL   A 1 49  ? 18.710 3.148   1.050   0.40 12.16 ?  49  VAL   A H    1 
ATOM   1351 H H    B VAL   A 1 49  ? 18.663 3.158   1.562   0.60 11.94 ?  49  VAL   A H    1 
ATOM   1352 H HA   A VAL   A 1 49  ? 18.632 3.559   3.608   0.40 12.19 ?  49  VAL   A HA   1 
ATOM   1353 H HA   B VAL   A 1 49  ? 18.728 3.407   4.134   0.60 12.65 ?  49  VAL   A HA   1 
ATOM   1354 H HB   A VAL   A 1 49  ? 19.916 1.459   2.216   0.40 13.50 ?  49  VAL   A HB   1 
ATOM   1355 H HB   B VAL   A 1 49  ? 19.997 1.520   2.461   0.60 13.56 ?  49  VAL   A HB   1 
ATOM   1356 H HG11 A VAL   A 1 49  ? 19.858 0.350   4.378   0.40 14.12 ?  49  VAL   A HG11 1 
ATOM   1357 H HG11 B VAL   A 1 49  ? 20.328 0.268   4.520   0.60 13.77 ?  49  VAL   A HG11 1 
ATOM   1358 H HG12 A VAL   A 1 49  ? 21.004 1.431   4.183   0.40 14.12 ?  49  VAL   A HG12 1 
ATOM   1359 H HG12 B VAL   A 1 49  ? 21.371 1.422   4.208   0.60 13.77 ?  49  VAL   A HG12 1 
ATOM   1360 H HG13 A VAL   A 1 49  ? 19.688 1.803   4.996   0.40 14.12 ?  49  VAL   A HG13 1 
ATOM   1361 H HG13 B VAL   A 1 49  ? 20.193 1.672   5.247   0.60 13.77 ?  49  VAL   A HG13 1 
ATOM   1362 H HG21 A VAL   A 1 49  ? 18.074 0.182   2.858   0.40 14.38 ?  49  VAL   A HG21 1 
ATOM   1363 H HG21 B VAL   A 1 49  ? 18.366 0.038   3.365   0.60 14.73 ?  49  VAL   A HG21 1 
ATOM   1364 H HG22 A VAL   A 1 49  ? 17.444 1.453   3.572   0.40 14.38 ?  49  VAL   A HG22 1 
ATOM   1365 H HG22 B VAL   A 1 49  ? 17.694 1.292   4.072   0.60 14.73 ?  49  VAL   A HG22 1 
ATOM   1366 H HG23 A VAL   A 1 49  ? 17.605 1.427   1.991   0.40 14.38 ?  49  VAL   A HG23 1 
ATOM   1367 H HG23 B VAL   A 1 49  ? 17.737 1.202   2.487   0.60 14.73 ?  49  VAL   A HG23 1 
ATOM   1368 N N    A ALA   A 1 50  ? 21.530 4.058   2.342   0.40 9.36  ?  50  ALA   A N    1 
ATOM   1369 N N    B ALA   A 1 50  ? 21.553 4.073   2.765   0.60 9.71  ?  50  ALA   A N    1 
ATOM   1370 C CA   A ALA   A 1 50  ? 22.853 4.605   2.635   0.40 9.28  ?  50  ALA   A CA   1 
ATOM   1371 C CA   B ALA   A 1 50  ? 22.871 4.639   3.027   0.60 9.72  ?  50  ALA   A CA   1 
ATOM   1372 C C    A ALA   A 1 50  ? 22.773 6.065   3.061   0.40 9.11  ?  50  ALA   A C    1 
ATOM   1373 C C    B ALA   A 1 50  ? 22.763 6.081   3.499   0.60 9.91  ?  50  ALA   A C    1 
ATOM   1374 O O    A ALA   A 1 50  ? 23.447 6.484   4.008   0.40 9.47  ?  50  ALA   A O    1 
ATOM   1375 O O    B ALA   A 1 50  ? 23.410 6.483   4.477   0.60 10.06 ?  50  ALA   A O    1 
ATOM   1376 C CB   A ALA   A 1 50  ? 23.761 4.464   1.416   0.40 10.00 ?  50  ALA   A CB   1 
ATOM   1377 C CB   B ALA   A 1 50  ? 23.738 4.539   1.772   0.60 9.70  ?  50  ALA   A CB   1 
ATOM   1378 H H    A ALA   A 1 50  ? 21.419 3.806   1.535   0.40 11.29 ?  50  ALA   A H    1 
ATOM   1379 H H    B ALA   A 1 50  ? 21.410 3.851   1.940   0.60 11.70 ?  50  ALA   A H    1 
ATOM   1380 H HA   A ALA   A 1 50  ? 23.248 4.108   3.369   0.40 11.20 ?  50  ALA   A HA   1 
ATOM   1381 H HA   B ALA   A 1 50  ? 23.294 4.136   3.729   0.60 11.72 ?  50  ALA   A HA   1 
ATOM   1382 H HB1  A ALA   A 1 50  ? 24.627 4.846   1.627   0.40 12.06 ?  50  ALA   A HB1  1 
ATOM   1383 H HB1  B ALA   A 1 50  ? 24.610 4.915   1.957   0.60 11.70 ?  50  ALA   A HB1  1 
ATOM   1384 H HB2  A ALA   A 1 50  ? 23.852 3.525   1.204   0.40 12.06 ?  50  ALA   A HB2  1 
ATOM   1385 H HB2  B ALA   A 1 50  ? 23.826 3.604   1.523   0.60 11.70 ?  50  ALA   A HB2  1 
ATOM   1386 H HB3  A ALA   A 1 50  ? 23.360 4.939   0.673   0.40 12.06 ?  50  ALA   A HB3  1 
ATOM   1387 H HB3  B ALA   A 1 50  ? 23.313 5.030   1.048   0.60 11.70 ?  50  ALA   A HB3  1 
ATOM   1388 N N    A GLY   A 1 51  ? 21.988 6.872   2.350   0.40 9.30  ?  51  GLY   A N    1 
ATOM   1389 N N    B GLY   A 1 51  ? 21.954 6.886   2.806   0.60 10.34 ?  51  GLY   A N    1 
ATOM   1390 C CA   A GLY   A 1 51  ? 21.861 8.271   2.730   0.40 9.61  ?  51  GLY   A CA   1 
ATOM   1391 C CA   B GLY   A 1 51  ? 21.771 8.266   3.224   0.60 10.49 ?  51  GLY   A CA   1 
ATOM   1392 C C    A GLY   A 1 51  ? 21.268 8.445   4.114   0.40 9.31  ?  51  GLY   A C    1 
ATOM   1393 C C    B GLY   A 1 51  ? 21.196 8.361   4.624   0.60 10.74 ?  51  GLY   A C    1 
ATOM   1394 O O    A GLY   A 1 51  ? 21.654 9.354   4.854   0.40 9.00  ?  51  GLY   A O    1 
ATOM   1395 O O    B GLY   A 1 51  ? 21.599 9.218   5.420   0.60 11.23 ?  51  GLY   A O    1 
ATOM   1396 H H    A GLY   A 1 51  ? 21.541 6.648   1.659   0.40 11.22 ?  51  GLY   A H    1 
ATOM   1397 H H    B GLY   A 1 51  ? 21.507 6.657   2.097   0.60 12.46 ?  51  GLY   A H    1 
ATOM   1398 H HA2  A GLY   A 1 51  ? 22.735 8.696   2.727   0.40 11.58 ?  51  GLY   A HA2  1 
ATOM   1399 H HA2  B GLY   A 1 51  ? 22.628 8.725   3.200   0.60 12.64 ?  51  GLY   A HA2  1 
ATOM   1400 H HA3  A GLY   A 1 51  ? 21.291 8.735   2.101   0.40 11.58 ?  51  GLY   A HA3  1 
ATOM   1401 H HA3  B GLY   A 1 51  ? 21.173 8.716   2.595   0.60 12.64 ?  51  GLY   A HA3  1 
ATOM   1402 N N    A ALA   A 1 52  ? 20.317 7.581   4.481   0.40 9.80  ?  52  ALA   A N    1 
ATOM   1403 N N    B ALA   A 1 52  ? 20.246 7.475   4.941   0.60 11.28 ?  52  ALA   A N    1 
ATOM   1404 C CA   A ALA   A 1 52  ? 19.669 7.683   5.786   0.40 10.25 ?  52  ALA   A CA   1 
ATOM   1405 C CA   B ALA   A 1 52  ? 19.632 7.472   6.263   0.60 11.41 ?  52  ALA   A CA   1 
ATOM   1406 C C    A ALA   A 1 52  ? 20.604 7.257   6.912   0.40 10.52 ?  52  ALA   A C    1 
ATOM   1407 C C    B ALA   A 1 52  ? 20.632 7.055   7.337   0.60 11.06 ?  52  ALA   A C    1 
ATOM   1408 O O    A ALA   A 1 52  ? 20.681 7.927   7.947   0.40 10.56 ?  52  ALA   A O    1 
ATOM   1409 O O    B ALA   A 1 52  ? 20.718 7.684   8.400   0.60 11.55 ?  52  ALA   A O    1 
ATOM   1410 C CB   A ALA   A 1 52  ? 18.396 6.834   5.801   0.40 11.08 ?  52  ALA   A CB   1 
ATOM   1411 C CB   B ALA   A 1 52  ? 18.422 6.536   6.262   0.60 12.44 ?  52  ALA   A CB   1 
ATOM   1412 H H    A ALA   A 1 52  ? 20.041 6.927   4.006   0.40 11.82 ?  52  ALA   A H    1 
ATOM   1413 H H    B ALA   A 1 52  ? 19.957 6.858   4.402   0.60 13.60 ?  52  ALA   A H    1 
ATOM   1414 H HA   A ALA   A 1 52  ? 19.407 8.603   5.948   0.40 12.36 ?  52  ALA   A HA   1 
ATOM   1415 H HA   B ALA   A 1 52  ? 19.329 8.365   6.459   0.60 13.75 ?  52  ALA   A HA   1 
ATOM   1416 H HB1  A ALA   A 1 52  ? 17.968 6.908   6.673   0.40 13.35 ?  52  ALA   A HB1  1 
ATOM   1417 H HB1  B ALA   A 1 52  ? 18.022 6.547   7.143   0.60 14.98 ?  52  ALA   A HB1  1 
ATOM   1418 H HB2  A ALA   A 1 52  ? 17.791 7.156   5.114   0.40 13.35 ?  52  ALA   A HB2  1 
ATOM   1419 H HB2  B ALA   A 1 52  ? 17.780 6.852   5.603   0.60 14.98 ?  52  ALA   A HB2  1 
ATOM   1420 H HB3  A ALA   A 1 52  ? 18.627 5.907   5.630   0.40 13.35 ?  52  ALA   A HB3  1 
ATOM   1421 H HB3  B ALA   A 1 52  ? 18.710 5.640   6.036   0.60 14.98 ?  52  ALA   A HB3  1 
ATOM   1422 N N    A LEU   A 1 53  ? 21.312 6.141   6.739   0.40 10.54 ?  53  LEU   A N    1 
ATOM   1423 N N    B LEU   A 1 53  ? 21.382 5.981   7.085   0.60 11.18 ?  53  LEU   A N    1 
ATOM   1424 C CA   A LEU   A 1 53  ? 22.230 5.689   7.780   0.40 11.11 ?  53  LEU   A CA   1 
ATOM   1425 C CA   B LEU   A 1 53  ? 22.435 5.595   8.017   0.60 11.08 ?  53  LEU   A CA   1 
ATOM   1426 C C    A LEU   A 1 53  ? 23.311 6.725   8.030   0.40 11.21 ?  53  LEU   A C    1 
ATOM   1427 C C    B LEU   A 1 53  ? 23.447 6.720   8.178   0.60 11.33 ?  53  LEU   A C    1 
ATOM   1428 O O    A LEU   A 1 53  ? 23.660 7.005   9.181   0.40 12.09 ?  53  LEU   A O    1 
ATOM   1429 O O    B LEU   A 1 53  ? 23.805 7.097   9.300   0.60 12.33 ?  53  LEU   A O    1 
ATOM   1430 C CB   A LEU   A 1 53  ? 22.862 4.353   7.385   0.40 11.97 ?  53  LEU   A CB   1 
ATOM   1431 C CB   B LEU   A 1 53  ? 23.126 4.316   7.535   0.60 10.91 ?  53  LEU   A CB   1 
ATOM   1432 C CG   A LEU   A 1 53  ? 21.971 3.114   7.489   0.40 12.56 ?  53  LEU   A CG   1 
ATOM   1433 C CG   B LEU   A 1 53  ? 22.327 3.012   7.617   0.60 11.39 ?  53  LEU   A CG   1 
ATOM   1434 C CD1  A LEU   A 1 53  ? 22.701 1.892   6.952   0.40 12.30 ?  53  LEU   A CD1  1 
ATOM   1435 C CD1  B LEU   A 1 53  ? 23.081 1.885   6.920   0.60 11.80 ?  53  LEU   A CD1  1 
ATOM   1436 C CD2  A LEU   A 1 53  ? 21.530 2.877   8.925   0.40 13.49 ?  53  LEU   A CD2  1 
ATOM   1437 C CD2  B LEU   A 1 53  ? 22.033 2.632   9.057   0.60 12.07 ?  53  LEU   A CD2  1 
ATOM   1438 H H    A LEU   A 1 53  ? 21.283 5.647   6.046   0.40 12.71 ?  53  LEU   A H    1 
ATOM   1439 H H    B LEU   A 1 53  ? 21.298 5.461   6.394   0.60 13.47 ?  53  LEU   A H    1 
ATOM   1440 H HA   A LEU   A 1 53  ? 21.746 5.566   8.612   0.40 13.39 ?  53  LEU   A HA   1 
ATOM   1441 H HA   B LEU   A 1 53  ? 22.039 5.414   8.879   0.60 13.35 ?  53  LEU   A HA   1 
ATOM   1442 H HB2  A LEU   A 1 53  ? 23.151 4.420   6.461   0.40 14.42 ?  53  LEU   A HB2  1 
ATOM   1443 H HB2  B LEU   A 1 53  ? 23.378 4.435   6.604   0.60 13.14 ?  53  LEU   A HB2  1 
ATOM   1444 H HB3  A LEU   A 1 53  ? 23.632 4.199   7.951   0.40 14.42 ?  53  LEU   A HB3  1 
ATOM   1445 H HB3  B LEU   A 1 53  ? 23.928 4.186   8.066   0.60 13.14 ?  53  LEU   A HB3  1 
ATOM   1446 H HG   A LEU   A 1 53  ? 21.176 3.249   6.948   0.40 15.13 ?  53  LEU   A HG   1 
ATOM   1447 H HG   B LEU   A 1 53  ? 21.481 3.127   7.154   0.60 13.72 ?  53  LEU   A HG   1 
ATOM   1448 H HD11 A LEU   A 1 53  ? 22.120 1.119   7.025   0.40 14.82 ?  53  LEU   A HD11 1 
ATOM   1449 H HD11 B LEU   A 1 53  ? 22.560 1.068   6.982   0.60 14.22 ?  53  LEU   A HD11 1 
ATOM   1450 H HD12 A LEU   A 1 53  ? 22.934 2.045   6.023   0.40 14.82 ?  53  LEU   A HD12 1 
ATOM   1451 H HD12 B LEU   A 1 53  ? 23.216 2.120   5.988   0.60 14.22 ?  53  LEU   A HD12 1 
ATOM   1452 H HD13 A LEU   A 1 53  ? 23.507 1.752   7.475   0.40 14.82 ?  53  LEU   A HD13 1 
ATOM   1453 H HD13 B LEU   A 1 53  ? 23.939 1.762   7.356   0.60 14.22 ?  53  LEU   A HD13 1 
ATOM   1454 H HD21 A LEU   A 1 53  ? 21.072 2.026   8.978   0.40 16.24 ?  53  LEU   A HD21 1 
ATOM   1455 H HD21 B LEU   A 1 53  ? 21.563 1.786   9.074   0.60 14.54 ?  53  LEU   A HD21 1 
ATOM   1456 H HD22 A LEU   A 1 53  ? 22.315 2.868   9.495   0.40 16.24 ?  53  LEU   A HD22 1 
ATOM   1457 H HD22 B LEU   A 1 53  ? 22.870 2.559   9.540   0.60 14.54 ?  53  LEU   A HD22 1 
ATOM   1458 H HD23 A LEU   A 1 53  ? 20.934 3.592   9.197   0.40 16.24 ?  53  LEU   A HD23 1 
ATOM   1459 H HD23 B LEU   A 1 53  ? 21.481 3.325   9.456   0.60 14.54 ?  53  LEU   A HD23 1 
ATOM   1460 N N    A ASN   A 1 54  ? 23.842 7.316   6.964   0.40 10.84 ?  54  ASN   A N    1 
ATOM   1461 N N    B ASN   A 1 54  ? 23.914 7.277   7.061   0.60 11.20 ?  54  ASN   A N    1 
ATOM   1462 C CA   A ASN   A 1 54  ? 24.914 8.286   7.139   0.40 10.94 ?  54  ASN   A CA   1 
ATOM   1463 C CA   B ASN   A 1 54  ? 24.941 8.308   7.154   0.60 11.30 ?  54  ASN   A CA   1 
ATOM   1464 C C    A ASN   A 1 54  ? 24.421 9.530   7.870   0.40 11.47 ?  54  ASN   A C    1 
ATOM   1465 C C    B ASN   A 1 54  ? 24.419 9.535   7.893   0.60 11.76 ?  54  ASN   A C    1 
ATOM   1466 O O    A ASN   A 1 54  ? 25.134 10.085  8.715   0.40 11.86 ?  54  ASN   A O    1 
ATOM   1467 O O    B ASN   A 1 54  ? 25.098 10.081  8.773   0.60 12.40 ?  54  ASN   A O    1 
ATOM   1468 C CB   A ASN   A 1 54  ? 25.498 8.658   5.787   0.40 10.78 ?  54  ASN   A CB   1 
ATOM   1469 C CB   B ASN   A 1 54  ? 25.451 8.689   5.771   0.60 11.44 ?  54  ASN   A CB   1 
ATOM   1470 C CG   A ASN   A 1 54  ? 26.524 9.745   5.907   0.40 10.81 ?  54  ASN   A CG   1 
ATOM   1471 C CG   B ASN   A 1 54  ? 26.454 9.806   5.842   0.60 11.84 ?  54  ASN   A CG   1 
ATOM   1472 O OD1  A ASN   A 1 54  ? 27.491 9.615   6.662   0.40 10.30 ?  54  ASN   A OD1  1 
ATOM   1473 O OD1  B ASN   A 1 54  ? 27.515 9.643   6.445   0.60 12.41 ?  54  ASN   A OD1  1 
ATOM   1474 N ND2  A ASN   A 1 54  ? 26.318 10.840  5.190   0.40 11.28 ?  54  ASN   A ND2  1 
ATOM   1475 N ND2  B ASN   A 1 54  ? 26.125 10.958  5.267   0.60 11.85 ?  54  ASN   A ND2  1 
ATOM   1476 H H    A ASN   A 1 54  ? 23.599 7.182   6.151   0.40 13.07 ?  54  ASN   A H    1 
ATOM   1477 H H    B ASN   A 1 54  ? 23.661 7.078   6.260   0.60 13.49 ?  54  ASN   A H    1 
ATOM   1478 H HA   A ASN   A 1 54  ? 25.617 7.885   7.669   0.40 13.18 ?  54  ASN   A HA   1 
ATOM   1479 H HA   B ASN   A 1 54  ? 25.686 7.953   7.659   0.60 13.62 ?  54  ASN   A HA   1 
ATOM   1480 H HB2  A ASN   A 1 54  ? 25.919 7.873   5.395   0.40 12.99 ?  54  ASN   A HB2  1 
ATOM   1481 H HB2  B ASN   A 1 54  ? 25.883 7.918   5.368   0.60 13.78 ?  54  ASN   A HB2  1 
ATOM   1482 H HB3  A ASN   A 1 54  ? 24.784 8.972   5.206   0.40 12.99 ?  54  ASN   A HB3  1 
ATOM   1483 H HB3  B ASN   A 1 54  ? 24.707 8.980   5.223   0.60 13.78 ?  54  ASN   A HB3  1 
ATOM   1484 H HD21 A ASN   A 1 54  ? 26.883 11.483  5.227   0.40 13.59 ?  54  ASN   A HD21 1 
ATOM   1485 H HD21 B ASN   A 1 54  ? 26.669 11.624  5.291   0.60 14.27 ?  54  ASN   A HD21 1 
ATOM   1486 H HD22 A ASN   A 1 54  ? 25.625 10.899  4.684   0.40 13.59 ?  54  ASN   A HD22 1 
ATOM   1487 H HD22 B ASN   A 1 54  ? 25.372 11.034  4.858   0.60 14.27 ?  54  ASN   A HD22 1 
ATOM   1488 N N    . LYS   A 1 55  ? 23.204 9.981   7.554   1.00 12.04 ?  55  LYS   A N    1 
ATOM   1489 C CA   . LYS   A 1 55  ? 22.626 11.130  8.240   1.00 12.41 ?  55  LYS   A CA   1 
ATOM   1490 C C    . LYS   A 1 55  ? 22.550 10.878  9.739   1.00 12.93 ?  55  LYS   A C    1 
ATOM   1491 O O    . LYS   A 1 55  ? 22.834 11.772  10.546  1.00 13.59 ?  55  LYS   A O    1 
ATOM   1492 C CB   . LYS   A 1 55  ? 21.249 11.440  7.640   1.00 13.57 ?  55  LYS   A CB   1 
ATOM   1493 C CG   . LYS   A 1 55  ? 20.499 12.586  8.294   1.00 14.60 ?  55  LYS   A CG   1 
ATOM   1494 C CD   . LYS   A 1 55  ? 19.188 12.883  7.546   1.00 15.69 ?  55  LYS   A CD   1 
ATOM   1495 C CE   . LYS   A 1 55  ? 18.404 14.006  8.204   1.00 17.03 ?  55  LYS   A CE   1 
ATOM   1496 N NZ   . LYS   A 1 55  ? 17.098 14.253  7.522   1.00 17.68 ?  55  LYS   A NZ   1 
ATOM   1497 H H    A LYS   A 1 55  ? 22.696 9.638   6.946   0.40 14.50 ?  55  LYS   A H    1 
ATOM   1498 H H    B LYS   A 1 55  ? 22.699 9.634   6.946   0.60 14.50 ?  55  LYS   A H    1 
ATOM   1499 H HA   . LYS   A 1 55  ? 23.194 11.902  8.095   1.00 14.94 ?  55  LYS   A HA   1 
ATOM   1500 H HB2  . LYS   A 1 55  ? 21.364 11.669  6.704   1.00 16.34 ?  55  LYS   A HB2  1 
ATOM   1501 H HB3  . LYS   A 1 55  ? 20.695 10.648  7.714   1.00 16.34 ?  55  LYS   A HB3  1 
ATOM   1502 H HG2  . LYS   A 1 55  ? 20.277 12.337  9.208   1.00 17.57 ?  55  LYS   A HG2  1 
ATOM   1503 H HG3  . LYS   A 1 55  ? 21.050 13.377  8.282   1.00 17.57 ?  55  LYS   A HG3  1 
ATOM   1504 H HD2  . LYS   A 1 55  ? 19.401 13.149  6.638   1.00 18.89 ?  55  LYS   A HD2  1 
ATOM   1505 H HD3  . LYS   A 1 55  ? 18.638 12.084  7.540   1.00 18.89 ?  55  LYS   A HD3  1 
ATOM   1506 H HE2  . LYS   A 1 55  ? 18.224 13.765  9.127   1.00 20.49 ?  55  LYS   A HE2  1 
ATOM   1507 H HE3  . LYS   A 1 55  ? 18.927 14.821  8.168   1.00 20.49 ?  55  LYS   A HE3  1 
ATOM   1508 H HZ1  . LYS   A 1 55  ? 16.585 14.769  8.032   1.00 21.27 ?  55  LYS   A HZ1  1 
ATOM   1509 H HZ2  . LYS   A 1 55  ? 17.237 14.660  6.743   1.00 21.27 ?  55  LYS   A HZ2  1 
ATOM   1510 H HZ3  . LYS   A 1 55  ? 16.680 13.481  7.377   1.00 21.27 ?  55  LYS   A HZ3  1 
ATOM   1511 N N    . ALA   A 1 56  ? 22.189 9.654   10.132  1.00 13.54 ?  56  ALA   A N    1 
ATOM   1512 C CA   . ALA   A 1 56  ? 22.085 9.320   11.545  1.00 14.36 ?  56  ALA   A CA   1 
ATOM   1513 C C    . ALA   A 1 56  ? 23.433 9.348   12.262  1.00 14.15 ?  56  ALA   A C    1 
ATOM   1514 O O    . ALA   A 1 56  ? 23.458 9.517   13.485  1.00 15.85 ?  56  ALA   A O    1 
ATOM   1515 C CB   . ALA   A 1 56  ? 21.401 7.960   11.713  1.00 14.91 ?  56  ALA   A CB   1 
ATOM   1516 H H    . ALA   A 1 56  ? 22.008 9.006   9.598   1.00 16.30 ?  56  ALA   A H    1 
ATOM   1517 H HA   . ALA   A 1 56  ? 21.522 9.983   11.970  1.00 17.29 ?  56  ALA   A HA   1 
ATOM   1518 H HB1  . ALA   A 1 56  ? 21.333 7.758   12.659  1.00 17.95 ?  56  ALA   A HB1  1 
ATOM   1519 H HB2  . ALA   A 1 56  ? 20.513 8.007   11.321  1.00 17.95 ?  56  ALA   A HB2  1 
ATOM   1520 H HB3  . ALA   A 1 56  ? 21.926 7.283   11.263  1.00 17.95 ?  56  ALA   A HB3  1 
ATOM   1521 N N    . THR   A 1 57  ? 24.549 9.195   11.537  1.00 12.93 ?  57  THR   A N    1 
ATOM   1522 C CA   . THR   A 1 57  ? 25.891 9.329   12.104  1.00 13.05 ?  57  THR   A CA   1 
ATOM   1523 C C    . THR   A 1 57  ? 26.421 10.755  12.027  1.00 13.41 ?  57  THR   A C    1 
ATOM   1524 O O    . THR   A 1 57  ? 27.601 10.981  12.319  1.00 13.87 ?  57  THR   A O    1 
ATOM   1525 C CB   . THR   A 1 57  ? 26.901 8.389   11.421  1.00 12.92 ?  57  THR   A CB   1 
ATOM   1526 O OG1  . THR   A 1 57  ? 27.257 8.889   10.121  1.00 12.50 ?  57  THR   A OG1  1 
ATOM   1527 C CG2  . THR   A 1 57  ? 26.367 6.972   11.309  1.00 12.70 ?  57  THR   A CG2  1 
ATOM   1528 H H    . THR   A 1 57  ? 24.550 8.991   10.696  1.00 15.57 ?  57  THR   A H    1 
ATOM   1529 H HA   . THR   A 1 57  ? 25.853 9.074   13.042  1.00 15.72 ?  57  THR   A HA   1 
ATOM   1530 H HB   . THR   A 1 57  ? 27.704 8.346   11.969  1.00 15.56 ?  57  THR   A HB   1 
ATOM   1531 H HG1  . THR   A 1 57  ? 26.569 8.943   9.645   1.00 15.05 ?  57  THR   A HG1  1 
ATOM   1532 H HG21 . THR   A 1 57  ? 27.094 6.346   11.172  1.00 15.30 ?  57  THR   A HG21 1 
ATOM   1533 H HG22 . THR   A 1 57  ? 25.890 6.727   12.119  1.00 15.30 ?  57  THR   A HG22 1 
ATOM   1534 H HG23 . THR   A 1 57  ? 25.754 6.907   10.558  1.00 15.30 ?  57  THR   A HG23 1 
ATOM   1535 N N    . ASN   A 1 58  ? 25.589 11.714  11.619  1.00 13.80 ?  58  ASN   A N    1 
ATOM   1536 C CA   . ASN   A 1 58  ? 26.014 13.105  11.496  1.00 14.91 ?  58  ASN   A CA   1 
ATOM   1537 C C    . ASN   A 1 58  ? 27.165 13.247  10.493  1.00 13.78 ?  58  ASN   A C    1 
ATOM   1538 O O    . ASN   A 1 58  ? 28.069 14.067  10.663  1.00 14.29 ?  58  ASN   A O    1 
ATOM   1539 C CB   . ASN   A 1 58  ? 26.360 13.686  12.874  1.00 17.82 ?  58  ASN   A CB   1 
ATOM   1540 C CG   . ASN   A 1 58  ? 26.643 15.176  12.838  1.00 21.84 ?  58  ASN   A CG   1 
ATOM   1541 O OD1  . ASN   A 1 58  ? 25.985 15.925  12.124  1.00 23.26 ?  58  ASN   A OD1  1 
ATOM   1542 N ND2  . ASN   A 1 58  ? 27.626 15.613  13.615  1.00 23.63 ?  58  ASN   A ND2  1 
ATOM   1543 H H    . ASN   A 1 58  ? 24.769 11.572  11.398  1.00 16.61 ?  58  ASN   A H    1 
ATOM   1544 H HA   . ASN   A 1 58  ? 25.267 13.608  11.149  1.00 17.95 ?  58  ASN   A HA   1 
ATOM   1545 H HB2  . ASN   A 1 58  ? 25.606 13.534  13.475  1.00 21.44 ?  58  ASN   A HB2  1 
ATOM   1546 H HB3  . ASN   A 1 58  ? 27.146 13.246  13.220  1.00 21.44 ?  58  ASN   A HB3  1 
ATOM   1547 H HD21 . ASN   A 1 58  ? 27.809 16.454  13.634  1.00 28.41 ?  58  ASN   A HD21 1 
ATOM   1548 H HD22 . ASN   A 1 58  ? 28.054 15.064  14.107  1.00 28.41 ?  58  ASN   A HD22 1 
ATOM   1549 N N    . ASN   A 1 59  ? 27.140 12.432  9.436   1.00 12.44 ?  59  ASN   A N    1 
ATOM   1550 C CA   . ASN   A 1 59  ? 28.112 12.418  8.332   1.00 12.33 ?  59  ASN   A CA   1 
ATOM   1551 C C    . ASN   A 1 59  ? 29.441 11.752  8.706   1.00 11.91 ?  59  ASN   A C    1 
ATOM   1552 O O    . ASN   A 1 59  ? 30.354 11.723  7.871   1.00 12.06 ?  59  ASN   A O    1 
ATOM   1553 C CB   . ASN   A 1 59  ? 28.390 13.813  7.740   1.00 12.43 ?  59  ASN   A CB   1 
ATOM   1554 C CG   . ASN   A 1 59  ? 28.726 13.767  6.267   1.00 12.76 ?  59  ASN   A CG   1 
ATOM   1555 O OD1  . ASN   A 1 59  ? 28.024 13.141  5.477   1.00 12.81 ?  59  ASN   A OD1  1 
ATOM   1556 N ND2  . ASN   A 1 59  ? 29.805 14.438  5.887   1.00 13.18 ?  59  ASN   A ND2  1 
ATOM   1557 H H    . ASN   A 1 59  ? 26.529 11.843  9.322   1.00 14.99 ?  59  ASN   A H    1 
ATOM   1558 H HA   . ASN   A 1 59  ? 27.731 11.893  7.616   1.00 14.85 ?  59  ASN   A HA   1 
ATOM   1559 H HB2  . ASN   A 1 59  ? 27.605 14.371  7.839   1.00 14.98 ?  59  ASN   A HB2  1 
ATOM   1560 H HB3  . ASN   A 1 59  ? 29.146 14.216  8.196   1.00 14.98 ?  59  ASN   A HB3  1 
ATOM   1561 H HD21 . ASN   A 1 59  ? 30.046 14.444  5.056   1.00 15.88 ?  59  ASN   A HD21 1 
ATOM   1562 H HD22 . ASN   A 1 59  ? 30.281 14.865  6.466   1.00 15.88 ?  59  ASN   A HD22 1 
ATOM   1563 N N    . ALA   A 1 60  ? 29.586 11.211  9.912   1.00 11.40 ?  60  ALA   A N    1 
ATOM   1564 C CA   . ALA   A 1 60  ? 30.833 10.530  10.250  1.00 12.00 ?  60  ALA   A CA   1 
ATOM   1565 C C    . ALA   A 1 60  ? 31.060 9.301   9.370   1.00 11.68 ?  60  ALA   A C    1 
ATOM   1566 O O    . ALA   A 1 60  ? 32.204 8.982   9.024   1.00 12.48 ?  60  ALA   A O    1 
ATOM   1567 C CB   . ALA   A 1 60  ? 30.841 10.137  11.724  1.00 12.72 ?  60  ALA   A CB   1 
ATOM   1568 H H    . ALA   A 1 60  ? 28.995 11.221  10.533  1.00 13.73 ?  60  ALA   A H    1 
ATOM   1569 H HA   . ALA   A 1 60  ? 31.572 11.141  10.099  1.00 14.46 ?  60  ALA   A HA   1 
ATOM   1570 H HB1  . ALA   A 1 60  ? 31.673 9.688   11.927  1.00 15.32 ?  60  ALA   A HB1  1 
ATOM   1571 H HB2  . ALA   A 1 60  ? 30.752 10.938  12.263  1.00 15.32 ?  60  ALA   A HB2  1 
ATOM   1572 H HB3  . ALA   A 1 60  ? 30.092 9.541   11.893  1.00 15.32 ?  60  ALA   A HB3  1 
ATOM   1573 N N    . MET   A 1 61  ? 29.988 8.590   9.006   1.00 11.39 ?  61  MET   A N    1 
ATOM   1574 C CA   . MET   A 1 61  ? 30.129 7.457   8.100   1.00 11.38 ?  61  MET   A CA   1 
ATOM   1575 C C    . MET   A 1 61  ? 30.734 7.892   6.769   1.00 10.90 ?  61  MET   A C    1 
ATOM   1576 O O    . MET   A 1 61  ? 31.623 7.221   6.236   1.00 11.34 ?  61  MET   A O    1 
ATOM   1577 C CB   . MET   A 1 61  ? 28.770 6.783   7.902   1.00 11.22 ?  61  MET   A CB   1 
ATOM   1578 C CG   . MET   A 1 61  ? 28.782 5.621   6.912   1.00 11.65 ?  61  MET   A CG   1 
ATOM   1579 S SD   . MET   A 1 61  ? 27.158 4.855   6.739   1.00 12.54 ?  61  MET   A SD   1 
ATOM   1580 C CE   . MET   A 1 61  ? 27.061 3.954   8.285   1.00 14.01 ?  61  MET   A CE   1 
ATOM   1581 H H    . MET   A 1 61  ? 29.181 8.748   9.257   1.00 13.72 ?  61  MET   A H    1 
ATOM   1582 H HA   . MET   A 1 61  ? 30.725 6.808   8.507   1.00 13.72 ?  61  MET   A HA   1 
ATOM   1583 H HB2  . MET   A 1 61  ? 28.473 6.431   8.754   1.00 13.52 ?  61  MET   A HB2  1 
ATOM   1584 H HB3  . MET   A 1 61  ? 28.139 7.436   7.575   1.00 13.52 ?  61  MET   A HB3  1 
ATOM   1585 H HG2  . MET   A 1 61  ? 29.049 5.940   6.035   1.00 14.04 ?  61  MET   A HG2  1 
ATOM   1586 H HG3  . MET   A 1 61  ? 29.396 4.936   7.218   1.00 14.04 ?  61  MET   A HG3  1 
ATOM   1587 H HE1  . MET   A 1 61  ? 26.223 3.461   8.313   1.00 16.87 ?  61  MET   A HE1  1 
ATOM   1588 H HE2  . MET   A 1 61  ? 27.807 3.337   8.337   1.00 16.87 ?  61  MET   A HE2  1 
ATOM   1589 H HE3  . MET   A 1 61  ? 27.097 4.582   9.023   1.00 16.87 ?  61  MET   A HE3  1 
ATOM   1590 N N    . GLN   A 1 62  ? 30.272 9.021   6.222   1.00 11.41 ?  62  GLN   A N    1 
ATOM   1591 C CA   . GLN   A 1 62  ? 30.817 9.506   4.956   1.00 11.78 ?  62  GLN   A CA   1 
ATOM   1592 C C    . GLN   A 1 62  ? 32.286 9.892   5.083   1.00 11.42 ?  62  GLN   A C    1 
ATOM   1593 O O    . GLN   A 1 62  ? 33.087 9.585   4.195   1.00 11.82 ?  62  GLN   A O    1 
ATOM   1594 C CB   . GLN   A 1 62  ? 30.003 10.690  4.432   1.00 11.44 ?  62  GLN   A CB   1 
ATOM   1595 C CG   . GLN   A 1 62  ? 30.354 11.049  3.008   1.00 11.42 ?  62  GLN   A CG   1 
ATOM   1596 C CD   . GLN   A 1 62  ? 30.013 9.919   2.065   1.00 11.87 ?  62  GLN   A CD   1 
ATOM   1597 O OE1  . GLN   A 1 62  ? 28.832 9.607   1.873   1.00 12.59 ?  62  GLN   A OE1  1 
ATOM   1598 N NE2  . GLN   A 1 62  ? 31.028 9.253   1.516   1.00 12.43 ?  62  GLN   A NE2  1 
ATOM   1599 H H    . GLN   A 1 62  ? 29.661 9.518   6.564   1.00 13.75 ?  62  GLN   A H    1 
ATOM   1600 H HA   . GLN   A 1 62  ? 30.758 8.790   4.305   1.00 14.20 ?  62  GLN   A HA   1 
ATOM   1601 H HB2  . GLN   A 1 62  ? 29.063 10.469  4.463   1.00 13.78 ?  62  GLN   A HB2  1 
ATOM   1602 H HB3  . GLN   A 1 62  ? 30.184 11.468  4.984   1.00 13.78 ?  62  GLN   A HB3  1 
ATOM   1603 H HG2  . GLN   A 1 62  ? 29.845 11.826  2.736   1.00 13.76 ?  62  GLN   A HG2  1 
ATOM   1604 H HG3  . GLN   A 1 62  ? 31.305 11.225  2.937   1.00 13.76 ?  62  GLN   A HG3  1 
ATOM   1605 H HE21 . GLN   A 1 62  ? 31.837 9.491   1.680   1.00 14.97 ?  62  GLN   A HE21 1 
ATOM   1606 H HE22 . GLN   A 1 62  ? 30.874 8.597   0.978   1.00 14.97 ?  62  GLN   A HE22 1 
ATOM   1607 N N    . VAL   A 1 63  ? 32.654 10.584  6.163   1.00 11.97 ?  63  VAL   A N    1 
ATOM   1608 C CA   . VAL   A 1 63  ? 34.045 10.984  6.360   1.00 12.68 ?  63  VAL   A CA   1 
ATOM   1609 C C    . VAL   A 1 63  ? 34.949 9.755   6.404   1.00 12.03 ?  63  VAL   A C    1 
ATOM   1610 O O    . VAL   A 1 63  ? 35.994 9.700   5.739   1.00 12.39 ?  63  VAL   A O    1 
ATOM   1611 C CB   . VAL   A 1 63  ? 34.166 11.850  7.628   1.00 14.21 ?  63  VAL   A CB   1 
ATOM   1612 C CG1  . VAL   A 1 63  ? 35.610 12.107  7.973   1.00 15.43 ?  63  VAL   A CG1  1 
ATOM   1613 C CG2  . VAL   A 1 63  ? 33.413 13.171  7.437   1.00 14.44 ?  63  VAL   A CG2  1 
ATOM   1614 H H    . VAL   A 1 63  ? 32.118 10.827  6.789   1.00 14.43 ?  63  VAL   A H    1 
ATOM   1615 H HA   . VAL   A 1 63  ? 34.322 11.525  5.606   1.00 15.27 ?  63  VAL   A HA   1 
ATOM   1616 H HB   . VAL   A 1 63  ? 33.756 11.377  8.372   1.00 17.11 ?  63  VAL   A HB   1 
ATOM   1617 H HG11 . VAL   A 1 63  ? 35.652 12.839  8.608   1.00 18.57 ?  63  VAL   A HG11 1 
ATOM   1618 H HG12 . VAL   A 1 63  ? 35.990 11.307  8.363   1.00 18.57 ?  63  VAL   A HG12 1 
ATOM   1619 H HG13 . VAL   A 1 63  ? 36.086 12.346  7.163   1.00 18.57 ?  63  VAL   A HG13 1 
ATOM   1620 H HG21 . VAL   A 1 63  ? 33.503 13.704  8.242   1.00 17.39 ?  63  VAL   A HG21 1 
ATOM   1621 H HG22 . VAL   A 1 63  ? 33.789 13.643  6.681   1.00 17.39 ?  63  VAL   A HG22 1 
ATOM   1622 H HG23 . VAL   A 1 63  ? 32.473 12.979  7.274   1.00 17.39 ?  63  VAL   A HG23 1 
ATOM   1623 N N    . GLU   A 1 64  ? 34.551 8.743   7.182   1.00 12.02 ?  64  GLU   A N    1 
ATOM   1624 C CA   . GLU   A 1 64  ? 35.318 7.505   7.267   1.00 11.89 ?  64  GLU   A CA   1 
ATOM   1625 C C    . GLU   A 1 64  ? 35.400 6.825   5.909   1.00 11.31 ?  64  GLU   A C    1 
ATOM   1626 O O    . GLU   A 1 64  ? 36.450 6.287   5.523   1.00 12.02 ?  64  GLU   A O    1 
ATOM   1627 C CB   . GLU   A 1 64  ? 34.641 6.585   8.281   1.00 12.57 ?  64  GLU   A CB   1 
ATOM   1628 C CG   . GLU   A 1 64  ? 35.306 5.234   8.430   1.00 12.76 ?  64  GLU   A CG   1 
ATOM   1629 C CD   . GLU   A 1 64  ? 34.441 4.230   9.157   1.00 13.16 ?  64  GLU   A CD   1 
ATOM   1630 O OE1  . GLU   A 1 64  ? 33.200 4.318   9.031   1.00 13.58 ?  64  GLU   A OE1  1 
ATOM   1631 O OE2  . GLU   A 1 64  ? 35.009 3.339   9.831   1.00 13.78 -1 64  GLU   A OE2  1 
ATOM   1632 H H    . GLU   A 1 64  ? 33.833 8.748   7.657   1.00 14.48 ?  64  GLU   A H    1 
ATOM   1633 H HA   . GLU   A 1 64  ? 36.217 7.703   7.576   1.00 14.33 ?  64  GLU   A HA   1 
ATOM   1634 H HB2  . GLU   A 1 64  ? 34.651 7.023   9.151   1.00 15.14 ?  64  GLU   A HB2  1 
ATOM   1635 H HB3  . GLU   A 1 64  ? 33.721 6.445   8.001   1.00 15.14 ?  64  GLU   A HB3  1 
ATOM   1636 H HG2  . GLU   A 1 64  ? 35.509 4.872   7.549   1.00 15.37 ?  64  GLU   A HG2  1 
ATOM   1637 H HG3  . GLU   A 1 64  ? 36.128 5.344   8.933   1.00 15.37 ?  64  GLU   A HG3  1 
ATOM   1638 N N    . SER   A 1 65  ? 34.273 6.810   5.188   1.00 11.39 ?  65  SER   A N    1 
ATOM   1639 C CA   . SER   A 1 65  ? 34.212 6.154   3.889   1.00 11.15 ?  65  SER   A CA   1 
ATOM   1640 C C    . SER   A 1 65  ? 35.117 6.835   2.875   1.00 11.52 ?  65  SER   A C    1 
ATOM   1641 O O    . SER   A 1 65  ? 35.750 6.164   2.053   1.00 12.12 ?  65  SER   A O    1 
ATOM   1642 C CB   . SER   A 1 65  ? 32.769 6.153   3.380   1.00 11.15 ?  65  SER   A CB   1 
ATOM   1643 O OG   . SER   A 1 65  ? 31.922 5.320   4.164   1.00 11.61 ?  65  SER   A OG   1 
ATOM   1644 H H    . SER   A 1 65  ? 33.535 7.170   5.436   1.00 13.72 ?  65  SER   A H    1 
ATOM   1645 H HA   . SER   A 1 65  ? 34.502 5.233   3.979   1.00 13.43 ?  65  SER   A HA   1 
ATOM   1646 H HB2  . SER   A 1 65  ? 32.425 7.059   3.412   1.00 13.43 ?  65  SER   A HB2  1 
ATOM   1647 H HB3  . SER   A 1 65  ? 32.762 5.833   2.467   1.00 13.43 ?  65  SER   A HB3  1 
ATOM   1648 H HG   . SER   A 1 65  ? 31.915 5.591   4.965   1.00 13.99 ?  65  SER   A HG   1 
ATOM   1649 N N    . ASP   A 1 66  ? 35.165 8.169   2.889   1.00 11.54 ?  66  ASP   A N    1 
ATOM   1650 C CA   . ASP   A 1 66  ? 36.017 8.877   1.937   1.00 12.29 ?  66  ASP   A CA   1 
ATOM   1651 C C    . ASP   A 1 66  ? 37.486 8.522   2.151   1.00 12.54 ?  66  ASP   A C    1 
ATOM   1652 O O    . ASP   A 1 66  ? 38.246 8.356   1.186   1.00 13.25 ?  66  ASP   A O    1 
ATOM   1653 C CB   . ASP   A 1 66  ? 35.806 10.384  2.050   1.00 13.57 ?  66  ASP   A CB   1 
ATOM   1654 C CG   . ASP   A 1 66  ? 34.455 10.849  1.490   1.00 15.06 ?  66  ASP   A CG   1 
ATOM   1655 O OD1  . ASP   A 1 66  ? 33.740 10.052  0.845   1.00 15.29 ?  66  ASP   A OD1  1 
ATOM   1656 O OD2  . ASP   A 1 66  ? 34.137 12.039  1.686   1.00 18.02 -1 66  ASP   A OD2  1 
ATOM   1657 H H    . ASP   A 1 66  ? 34.719 8.677   3.427   1.00 13.91 ?  66  ASP   A H    1 
ATOM   1658 H HA   . ASP   A 1 66  ? 35.770 8.606   1.039   1.00 14.80 ?  66  ASP   A HA   1 
ATOM   1659 H HB2  . ASP   A 1 66  ? 35.847 10.638  2.984   1.00 16.34 ?  66  ASP   A HB2  1 
ATOM   1660 H HB3  . ASP   A 1 66  ? 36.506 10.834  1.551   1.00 16.34 ?  66  ASP   A HB3  1 
ATOM   1661 N N    A ASP   A 1 67  ? 37.904 8.414   3.417   0.40 11.98 ?  67  ASP   A N    1 
ATOM   1662 N N    B ASP   A 1 67  ? 37.905 8.370   3.403   0.60 12.47 ?  67  ASP   A N    1 
ATOM   1663 C CA   A ASP   A 1 67  ? 39.269 8.003   3.734   0.40 12.38 ?  67  ASP   A CA   1 
ATOM   1664 C CA   B ASP   A 1 67  ? 39.264 7.905   3.644   0.60 13.39 ?  67  ASP   A CA   1 
ATOM   1665 C C    A ASP   A 1 67  ? 39.521 6.560   3.314   0.40 12.16 ?  67  ASP   A C    1 
ATOM   1666 C C    B ASP   A 1 67  ? 39.455 6.478   3.132   0.60 13.02 ?  67  ASP   A C    1 
ATOM   1667 O O    A ASP   A 1 67  ? 40.611 6.229   2.834   0.40 12.80 ?  67  ASP   A O    1 
ATOM   1668 O O    B ASP   A 1 67  ? 40.491 6.161   2.535   0.60 13.17 ?  67  ASP   A O    1 
ATOM   1669 C CB   A ASP   A 1 67  ? 39.512 8.165   5.234   0.40 12.90 ?  67  ASP   A CB   1 
ATOM   1670 C CB   B ASP   A 1 67  ? 39.597 8.024   5.128   0.60 14.13 ?  67  ASP   A CB   1 
ATOM   1671 C CG   A ASP   A 1 67  ? 40.788 7.483   5.698   0.40 13.18 ?  67  ASP   A CG   1 
ATOM   1672 C CG   B ASP   A 1 67  ? 40.907 7.369   5.485   0.60 14.36 ?  67  ASP   A CG   1 
ATOM   1673 O OD1  A ASP   A 1 67  ? 40.759 6.242   5.885   0.40 13.75 ?  67  ASP   A OD1  1 
ATOM   1674 O OD1  B ASP   A 1 67  ? 41.971 7.932   5.117   0.60 14.59 ?  67  ASP   A OD1  1 
ATOM   1675 O OD2  A ASP   A 1 67  ? 41.819 8.182   5.863   0.40 13.25 -1 67  ASP   A OD2  1 
ATOM   1676 O OD2  B ASP   A 1 67  ? 40.864 6.294   6.137   0.60 14.67 -1 67  ASP   A OD2  1 
ATOM   1677 H H    A ASP   A 1 67  ? 37.419 8.578   4.104   0.40 14.43 ?  67  ASP   A H    1 
ATOM   1678 H H    B ASP   A 1 67  ? 37.439 8.527   4.106   0.60 15.02 ?  67  ASP   A H    1 
ATOM   1679 H HA   A ASP   A 1 67  ? 39.898 8.581   3.264   0.40 14.91 ?  67  ASP   A HA   1 
ATOM   1680 H HA   B ASP   A 1 67  ? 39.877 8.474   3.155   0.60 16.13 ?  67  ASP   A HA   1 
ATOM   1681 H HB2  A ASP   A 1 67  ? 39.580 9.105   5.445   0.40 15.54 ?  67  ASP   A HB2  1 
ATOM   1682 H HB2  B ASP   A 1 67  ? 39.673 8.962   5.358   0.60 17.02 ?  67  ASP   A HB2  1 
ATOM   1683 H HB3  A ASP   A 1 67  ? 38.770 7.765   5.717   0.40 15.54 ?  67  ASP   A HB3  1 
ATOM   1684 H HB3  B ASP   A 1 67  ? 38.897 7.604   5.645   0.60 17.02 ?  67  ASP   A HB3  1 
ATOM   1685 N N    A TYR   A 1 68  ? 38.539 5.679   3.512   0.40 11.21 ?  68  TYR   A N    1 
ATOM   1686 N N    B TYR   A 1 68  ? 38.464 5.602   3.341   0.60 12.38 ?  68  TYR   A N    1 
ATOM   1687 C CA   A TYR   A 1 68  ? 38.703 4.293   3.085   0.40 11.08 ?  68  TYR   A CA   1 
ATOM   1688 C CA   B TYR   A 1 68  ? 38.567 4.233   2.835   0.60 12.62 ?  68  TYR   A CA   1 
ATOM   1689 C C    A TYR   A 1 68  ? 38.907 4.204   1.578   0.40 11.09 ?  68  TYR   A C    1 
ATOM   1690 C C    B TYR   A 1 68  ? 38.810 4.222   1.327   0.60 12.52 ?  68  TYR   A C    1 
ATOM   1691 O O    A TYR   A 1 68  ? 39.765 3.448   1.105   0.40 11.39 ?  68  TYR   A O    1 
ATOM   1692 O O    B TYR   A 1 68  ? 39.687 3.500   0.830   0.60 12.65 ?  68  TYR   A O    1 
ATOM   1693 C CB   A TYR   A 1 68  ? 37.491 3.454   3.507   0.40 10.94 ?  68  TYR   A CB   1 
ATOM   1694 C CB   B TYR   A 1 68  ? 37.304 3.420   3.183   0.60 12.49 ?  68  TYR   A CB   1 
ATOM   1695 C CG   A TYR   A 1 68  ? 37.551 2.044   2.961   0.40 11.67 ?  68  TYR   A CG   1 
ATOM   1696 C CG   B TYR   A 1 68  ? 37.327 2.060   2.512   0.60 12.50 ?  68  TYR   A CG   1 
ATOM   1697 C CD1  A TYR   A 1 68  ? 37.049 1.746   1.700   0.40 12.29 ?  68  TYR   A CD1  1 
ATOM   1698 C CD1  B TYR   A 1 68  ? 36.884 1.906   1.202   0.60 12.85 ?  68  TYR   A CD1  1 
ATOM   1699 C CD2  A TYR   A 1 68  ? 38.158 1.023   3.682   0.40 12.74 ?  68  TYR   A CD2  1 
ATOM   1700 C CD2  B TYR   A 1 68  ? 37.860 0.951   3.157   0.60 13.25 ?  68  TYR   A CD2  1 
ATOM   1701 C CE1  A TYR   A 1 68  ? 37.133 0.471   1.179   0.40 13.35 ?  68  TYR   A CE1  1 
ATOM   1702 C CE1  B TYR   A 1 68  ? 36.957 0.696   0.563   0.60 12.71 ?  68  TYR   A CE1  1 
ATOM   1703 C CE2  A TYR   A 1 68  ? 38.238 -0.262  3.170   0.40 13.53 ?  68  TYR   A CE2  1 
ATOM   1704 C CE2  B TYR   A 1 68  ? 37.923 -0.282  2.526   0.60 12.71 ?  68  TYR   A CE2  1 
ATOM   1705 C CZ   A TYR   A 1 68  ? 37.728 -0.525  1.921   0.40 13.83 ?  68  TYR   A CZ   1 
ATOM   1706 C CZ   B TYR   A 1 68  ? 37.479 -0.392  1.230   0.60 12.30 ?  68  TYR   A CZ   1 
ATOM   1707 O OH   A TYR   A 1 68  ? 37.826 -1.794  1.410   0.40 15.98 ?  68  TYR   A OH   1 
ATOM   1708 O OH   B TYR   A 1 68  ? 37.565 -1.606  0.604   0.60 12.87 ?  68  TYR   A OH   1 
ATOM   1709 H H    A TYR   A 1 68  ? 37.791 5.861   3.884   0.40 13.51 ?  68  TYR   A H    1 
ATOM   1710 H H    B TYR   A 1 68  ? 37.734 5.777   3.759   0.60 14.91 ?  68  TYR   A H    1 
ATOM   1711 H HA   A TYR   A 1 68  ? 39.492 3.931   3.510   0.40 13.35 ?  68  TYR   A HA   1 
ATOM   1712 H HA   B TYR   A 1 68  ? 39.322 3.799   3.257   0.60 15.21 ?  68  TYR   A HA   1 
ATOM   1713 H HB2  A TYR   A 1 68  ? 37.471 3.405   4.471   0.40 13.19 ?  68  TYR   A HB2  1 
ATOM   1714 H HB2  B TYR   A 1 68  ? 37.262 3.288   4.143   0.60 15.04 ?  68  TYR   A HB2  1 
ATOM   1715 H HB3  A TYR   A 1 68  ? 36.687 3.876   3.170   0.40 13.19 ?  68  TYR   A HB3  1 
ATOM   1716 H HB3  B TYR   A 1 68  ? 36.518 3.901   2.876   0.60 15.04 ?  68  TYR   A HB3  1 
ATOM   1717 H HD1  A TYR   A 1 68  ? 36.656 2.422   1.192   0.40 14.81 ?  68  TYR   A HD1  1 
ATOM   1718 H HD1  B TYR   A 1 68  ? 36.536 2.642   0.748   0.60 15.48 ?  68  TYR   A HD1  1 
ATOM   1719 H HD2  A TYR   A 1 68  ? 38.514 1.202   4.518   0.40 15.34 ?  68  TYR   A HD2  1 
ATOM   1720 H HD2  B TYR   A 1 68  ? 38.176 1.038   4.028   0.60 15.96 ?  68  TYR   A HD2  1 
ATOM   1721 H HE1  A TYR   A 1 68  ? 36.784 0.288   0.331   0.40 16.08 ?  68  TYR   A HE1  1 
ATOM   1722 H HE1  B TYR   A 1 68  ? 36.643 0.602   -0.309  0.60 15.31 ?  68  TYR   A HE1  1 
ATOM   1723 H HE2  A TYR   A 1 68  ? 38.643 -0.942  3.656   0.40 16.29 ?  68  TYR   A HE2  1 
ATOM   1724 H HE2  B TYR   A 1 68  ? 38.283 -1.015  2.968   0.60 15.31 ?  68  TYR   A HE2  1 
ATOM   1725 H HH   A TYR   A 1 68  ? 38.195 -2.308  1.959   0.40 19.23 ?  68  TYR   A HH   1 
ATOM   1726 H HH   B TYR   A 1 68  ? 37.892 -2.177  1.132   0.60 15.51 ?  68  TYR   A HH   1 
ATOM   1727 N N    A ILE   A 1 69  ? 38.118 4.957   0.806   0.40 10.78 ?  69  ILE   A N    1 
ATOM   1728 N N    B ILE   A 1 69  ? 38.021 4.999   0.579   0.60 12.02 ?  69  ILE   A N    1 
ATOM   1729 C CA   A ILE   A 1 69  ? 38.246 4.922   -0.647  0.40 11.16 ?  69  ILE   A CA   1 
ATOM   1730 C CA   B ILE   A 1 69  ? 38.134 5.003   -0.877  0.60 12.28 ?  69  ILE   A CA   1 
ATOM   1731 C C    A ILE   A 1 69  ? 39.573 5.531   -1.091  0.40 11.16 ?  69  ILE   A C    1 
ATOM   1732 C C    B ILE   A 1 69  ? 39.458 5.614   -1.315  0.60 12.00 ?  69  ILE   A C    1 
ATOM   1733 O O    A ILE   A 1 69  ? 40.228 5.020   -2.007  0.40 11.12 ?  69  ILE   A O    1 
ATOM   1734 O O    B ILE   A 1 69  ? 40.084 5.152   -2.275  0.60 12.38 ?  69  ILE   A O    1 
ATOM   1735 C CB   A ILE   A 1 69  ? 37.029 5.597   -1.312  0.40 12.33 ?  69  ILE   A CB   1 
ATOM   1736 C CB   B ILE   A 1 69  ? 36.939 5.746   -1.503  0.60 12.79 ?  69  ILE   A CB   1 
ATOM   1737 C CG1  A ILE   A 1 69  ? 35.741 4.815   -1.010  0.40 12.84 ?  69  ILE   A CG1  1 
ATOM   1738 C CG1  B ILE   A 1 69  ? 35.621 5.010   -1.235  0.60 12.40 ?  69  ILE   A CG1  1 
ATOM   1739 C CG2  A ILE   A 1 69  ? 37.247 5.752   -2.816  0.40 13.48 ?  69  ILE   A CG2  1 
ATOM   1740 C CG2  B ILE   A 1 69  ? 37.168 5.969   -2.998  0.60 14.45 ?  69  ILE   A CG2  1 
ATOM   1741 C CD1  A ILE   A 1 69  ? 35.632 3.475   -1.722  0.40 12.87 ?  69  ILE   A CD1  1 
ATOM   1742 C CD1  B ILE   A 1 69  ? 35.449 3.715   -2.011  0.60 12.46 ?  69  ILE   A CD1  1 
ATOM   1743 H H    A ILE   A 1 69  ? 37.510 5.491   1.093   0.40 13.00 ?  69  ILE   A H    1 
ATOM   1744 H H    B ILE   A 1 69  ? 37.420 5.532   0.892   0.60 14.48 ?  69  ILE   A H    1 
ATOM   1745 H HA   A ILE   A 1 69  ? 38.257 3.998   -0.935  0.40 13.45 ?  69  ILE   A HA   1 
ATOM   1746 H HA   B ILE   A 1 69  ? 38.112 4.084   -1.191  0.60 14.80 ?  69  ILE   A HA   1 
ATOM   1747 H HB   A ILE   A 1 69  ? 36.931 6.481   -0.937  0.40 14.85 ?  69  ILE   A HB   1 
ATOM   1748 H HB   B ILE   A 1 69  ? 36.879 6.613   -1.076  0.60 15.40 ?  69  ILE   A HB   1 
ATOM   1749 H HG12 A ILE   A 1 69  ? 35.702 4.643   -0.055  0.40 15.47 ?  69  ILE   A HG12 1 
ATOM   1750 H HG12 B ILE   A 1 69  ? 35.573 4.795   -0.288  0.60 14.94 ?  69  ILE   A HG12 1 
ATOM   1751 H HG13 A ILE   A 1 69  ? 34.981 5.351   -1.276  0.40 15.47 ?  69  ILE   A HG13 1 
ATOM   1752 H HG13 B ILE   A 1 69  ? 34.887 5.597   -1.471  0.60 14.94 ?  69  ILE   A HG13 1 
ATOM   1753 H HG21 A ILE   A 1 69  ? 36.392 5.928   -3.244  0.40 16.23 ?  69  ILE   A HG21 1 
ATOM   1754 H HG21 B ILE   A 1 69  ? 36.322 6.194   -3.413  0.60 17.39 ?  69  ILE   A HG21 1 
ATOM   1755 H HG22 A ILE   A 1 69  ? 37.848 6.499   -2.975  0.40 16.23 ?  69  ILE   A HG22 1 
ATOM   1756 H HG22 B ILE   A 1 69  ? 37.798 6.696   -3.117  0.60 17.39 ?  69  ILE   A HG22 1 
ATOM   1757 H HG23 A ILE   A 1 69  ? 37.629 4.937   -3.171  0.40 16.23 ?  69  ILE   A HG23 1 
ATOM   1758 H HG23 B ILE   A 1 69  ? 37.520 5.154   -3.387  0.60 17.39 ?  69  ILE   A HG23 1 
ATOM   1759 H HD11 A ILE   A 1 69  ? 34.826 3.026   -1.424  0.40 15.50 ?  69  ILE   A HD11 1 
ATOM   1760 H HD11 B ILE   A 1 69  ? 34.626 3.287   -1.729  0.60 15.01 ?  69  ILE   A HD11 1 
ATOM   1761 H HD12 A ILE   A 1 69  ? 35.589 3.628   -2.679  0.40 15.50 ?  69  ILE   A HD12 1 
ATOM   1762 H HD12 B ILE   A 1 69  ? 35.408 3.916   -2.959  0.60 15.01 ?  69  ILE   A HD12 1 
ATOM   1763 H HD13 A ILE   A 1 69  ? 36.408 2.934   -1.507  0.40 15.50 ?  69  ILE   A HD13 1 
ATOM   1764 H HD13 B ILE   A 1 69  ? 36.203 3.132   -1.828  0.60 15.01 ?  69  ILE   A HD13 1 
ATOM   1765 N N    A ALA   A 1 70  ? 39.996 6.623   -0.453  0.40 11.72 ?  70  ALA   A N    1 
ATOM   1766 N N    B ALA   A 1 70  ? 39.885 6.685   -0.648  0.60 12.45 ?  70  ALA   A N    1 
ATOM   1767 C CA   A ALA   A 1 70  ? 41.270 7.234   -0.817  0.40 12.61 ?  70  ALA   A CA   1 
ATOM   1768 C CA   B ALA   A 1 70  ? 41.157 7.297   -1.002  0.60 13.07 ?  70  ALA   A CA   1 
ATOM   1769 C C    A ALA   A 1 70  ? 42.432 6.275   -0.606  0.40 12.25 ?  70  ALA   A C    1 
ATOM   1770 C C    B ALA   A 1 70  ? 42.293 6.286   -0.890  0.60 12.85 ?  70  ALA   A C    1 
ATOM   1771 O O    A ALA   A 1 70  ? 43.445 6.366   -1.305  0.40 12.81 ?  70  ALA   A O    1 
ATOM   1772 O O    B ALA   A 1 70  ? 43.211 6.273   -1.717  0.60 13.78 ?  70  ALA   A O    1 
ATOM   1773 C CB   A ALA   A 1 70  ? 41.498 8.499   0.006   0.40 13.10 ?  70  ALA   A CB   1 
ATOM   1774 C CB   B ALA   A 1 70  ? 41.410 8.522   -0.119  0.60 13.45 ?  70  ALA   A CB   1 
ATOM   1775 H H    A ALA   A 1 70  ? 39.573 7.020   0.174   0.40 14.12 ?  70  ALA   A H    1 
ATOM   1776 H H    B ALA   A 1 70  ? 39.460 7.067   -0.004  0.60 15.00 ?  70  ALA   A H    1 
ATOM   1777 H HA   A ALA   A 1 70  ? 41.250 7.488   -1.756  0.40 15.19 ?  70  ALA   A HA   1 
ATOM   1778 H HA   B ALA   A 1 70  ? 41.115 7.604   -1.920  0.60 15.74 ?  70  ALA   A HA   1 
ATOM   1779 H HB1  A ALA   A 1 70  ? 42.358 8.882   -0.238  0.40 15.78 ?  70  ALA   A HB1  1 
ATOM   1780 H HB1  B ALA   A 1 70  ? 42.260 8.922   -0.364  0.60 16.20 ?  70  ALA   A HB1  1 
ATOM   1781 H HB2  A ALA   A 1 70  ? 40.790 9.129   -0.180  0.40 15.78 ?  70  ALA   A HB2  1 
ATOM   1782 H HB2  B ALA   A 1 70  ? 40.694 9.165   -0.249  0.60 16.20 ?  70  ALA   A HB2  1 
ATOM   1783 H HB3  A ALA   A 1 70  ? 41.500 8.263   0.947   0.40 15.78 ?  70  ALA   A HB3  1 
ATOM   1784 H HB3  B ALA   A 1 70  ? 41.434 8.244   0.812   0.60 16.20 ?  70  ALA   A HB3  1 
ATOM   1785 N N    A THR   A 1 71  ? 42.319 5.367   0.358   0.40 11.75 ?  71  THR   A N    1 
ATOM   1786 N N    B THR   A 1 71  ? 42.229 5.406   0.108   0.60 12.68 ?  71  THR   A N    1 
ATOM   1787 C CA   A THR   A 1 71  ? 43.379 4.411   0.645   0.40 12.42 ?  71  THR   A CA   1 
ATOM   1788 C CA   B THR   A 1 71  ? 43.289 4.421   0.301   0.60 13.42 ?  71  THR   A CA   1 
ATOM   1789 C C    A THR   A 1 71  ? 43.284 3.159   -0.210  0.40 11.83 ?  71  THR   A C    1 
ATOM   1790 C C    B THR   A 1 71  ? 43.140 3.227   -0.637  0.60 13.18 ?  71  THR   A C    1 
ATOM   1791 O O    A THR   A 1 71  ? 44.313 2.631   -0.648  0.40 12.09 ?  71  THR   A O    1 
ATOM   1792 O O    B THR   A 1 71  ? 44.126 2.780   -1.239  0.60 13.79 ?  71  THR   A O    1 
ATOM   1793 C CB   A THR   A 1 71  ? 43.293 3.984   2.109   0.40 14.35 ?  71  THR   A CB   1 
ATOM   1794 C CB   B THR   A 1 71  ? 43.287 3.954   1.758   0.60 14.93 ?  71  THR   A CB   1 
ATOM   1795 O OG1  A THR   A 1 71  ? 43.520 5.120   2.949   0.40 15.96 ?  71  THR   A OG1  1 
ATOM   1796 O OG1  B THR   A 1 71  ? 43.571 5.072   2.606   0.60 15.99 ?  71  THR   A OG1  1 
ATOM   1797 C CG2  A THR   A 1 71  ? 44.305 2.880   2.422   0.40 14.75 ?  71  THR   A CG2  1 
ATOM   1798 C CG2  B THR   A 1 71  ? 44.323 2.854   1.999   0.60 15.82 ?  71  THR   A CG2  1 
ATOM   1799 H H    A THR   A 1 71  ? 41.636 5.287   0.864   0.40 14.16 ?  71  THR   A H    1 
ATOM   1800 H H    B THR   A 1 71  ? 41.585 5.357   0.678   0.60 15.28 ?  71  THR   A H    1 
ATOM   1801 H HA   A THR   A 1 71  ? 44.245 4.825   0.482   0.40 14.96 ?  71  THR   A HA   1 
ATOM   1802 H HA   B THR   A 1 71  ? 44.147 4.838   0.126   0.60 16.16 ?  71  THR   A HA   1 
ATOM   1803 H HB   A THR   A 1 71  ? 42.407 3.631   2.273   0.40 17.28 ?  71  THR   A HB   1 
ATOM   1804 H HB   B THR   A 1 71  ? 42.415 3.595   1.982   0.60 17.98 ?  71  THR   A HB   1 
ATOM   1805 H HG1  A THR   A 1 71  ? 43.484 4.885   3.748   0.40 19.21 ?  71  THR   A HG1  1 
ATOM   1806 H HG1  B THR   A 1 71  ? 42.976 5.658   2.523   0.60 19.24 ?  71  THR   A HG1  1 
ATOM   1807 H HG21 A THR   A 1 71  ? 44.432 2.817   3.380   0.40 17.76 ?  71  THR   A HG21 1 
ATOM   1808 H HG21 B THR   A 1 71  ? 44.471 2.741   2.955   0.60 19.04 ?  71  THR   A HG21 1 
ATOM   1809 H HG22 A THR   A 1 71  ? 43.989 2.023   2.091   0.40 17.76 ?  71  THR   A HG22 1 
ATOM   1810 H HG22 B THR   A 1 71  ? 44.013 2.015   1.631   0.60 19.04 ?  71  THR   A HG22 1 
ATOM   1811 H HG23 A THR   A 1 71  ? 45.160 3.081   2.005   0.40 17.76 ?  71  THR   A HG23 1 
ATOM   1812 H HG23 B THR   A 1 71  ? 45.166 3.095   1.583   0.60 19.04 ?  71  THR   A HG23 1 
ATOM   1813 N N    A ASN   A 1 72  ? 42.070 2.659   -0.441  0.40 11.30 ?  72  ASN   A N    1 
ATOM   1814 N N    B ASN   A 1 72  ? 41.917 2.709   -0.781  0.60 12.70 ?  72  ASN   A N    1 
ATOM   1815 C CA   A ASN   A 1 72  ? 41.876 1.334   -1.009  0.40 11.88 ?  72  ASN   A CA   1 
ATOM   1816 C CA   B ASN   A 1 72  ? 41.685 1.388   -1.354  0.60 12.87 ?  72  ASN   A CA   1 
ATOM   1817 C C    A ASN   A 1 72  ? 41.225 1.326   -2.380  0.40 11.54 ?  72  ASN   A C    1 
ATOM   1818 C C    B ASN   A 1 72  ? 41.047 1.397   -2.734  0.60 13.15 ?  72  ASN   A C    1 
ATOM   1819 O O    A ASN   A 1 72  ? 41.166 0.258   -3.003  0.40 12.18 ?  72  ASN   A O    1 
ATOM   1820 O O    B ASN   A 1 72  ? 41.109 0.374   -3.430  0.60 14.45 ?  72  ASN   A O    1 
ATOM   1821 C CB   A ASN   A 1 72  ? 41.019 0.485   -0.065  0.40 12.68 ?  72  ASN   A CB   1 
ATOM   1822 C CB   B ASN   A 1 72  ? 40.804 0.563   -0.405  0.60 13.22 ?  72  ASN   A CB   1 
ATOM   1823 C CG   A ASN   A 1 72  ? 41.629 0.372   1.316   0.40 13.97 ?  72  ASN   A CG   1 
ATOM   1824 C CG   B ASN   A 1 72  ? 41.435 0.391   0.958   0.60 13.95 ?  72  ASN   A CG   1 
ATOM   1825 O OD1  A ASN   A 1 72  ? 41.137 0.953   2.283   0.40 15.29 ?  72  ASN   A OD1  1 
ATOM   1826 O OD1  B ASN   A 1 72  ? 40.984 0.980   1.936   0.60 15.31 ?  72  ASN   A OD1  1 
ATOM   1827 N ND2  A ASN   A 1 72  ? 42.722 -0.358  1.409   0.40 14.71 ?  72  ASN   A ND2  1 
ATOM   1828 N ND2  B ASN   A 1 72  ? 42.486 -0.406  1.029   0.60 13.77 ?  72  ASN   A ND2  1 
ATOM   1829 H H    A ASN   A 1 72  ? 41.338 3.074   -0.269  0.40 13.62 ?  72  ASN   A H    1 
ATOM   1830 H H    B ASN   A 1 72  ? 41.195 3.119   -0.551  0.60 15.30 ?  72  ASN   A H    1 
ATOM   1831 H HA   A ASN   A 1 72  ? 42.743 0.906   -1.098  0.40 14.32 ?  72  ASN   A HA   1 
ATOM   1832 H HA   B ASN   A 1 72  ? 42.532 0.931   -1.427  0.60 15.50 ?  72  ASN   A HA   1 
ATOM   1833 H HB2  A ASN   A 1 72  ? 40.144 0.893   0.006   0.40 15.27 ?  72  ASN   A HB2  1 
ATOM   1834 H HB2  B ASN   A 1 72  ? 39.950 1.008   -0.275  0.60 15.92 ?  72  ASN   A HB2  1 
ATOM   1835 H HB3  A ASN   A 1 72  ? 40.941 -0.407  -0.443  0.40 15.27 ?  72  ASN   A HB3  1 
ATOM   1836 H HB3  B ASN   A 1 72  ? 40.664 -0.322  -0.775  0.60 15.92 ?  72  ASN   A HB3  1 
ATOM   1837 H HD21 A ASN   A 1 72  ? 43.104 -0.447  2.170   0.40 17.71 ?  72  ASN   A HD21 1 
ATOM   1838 H HD21 B ASN   A 1 72  ? 42.882 -0.540  1.786   0.60 16.58 ?  72  ASN   A HD21 1 
ATOM   1839 H HD22 A ASN   A 1 72  ? 43.044 -0.745  0.712   0.40 17.71 ?  72  ASN   A HD22 1 
ATOM   1840 H HD22 B ASN   A 1 72  ? 42.779 -0.790  0.321   0.60 16.58 ?  72  ASN   A HD22 1 
ATOM   1841 N N    A GLY   A 1 73  ? 40.723 2.461   -2.862  0.40 11.29 ?  73  GLY   A N    1 
ATOM   1842 N N    B GLY   A 1 73  ? 40.432 2.503   -3.144  0.60 12.87 ?  73  GLY   A N    1 
ATOM   1843 C CA   A GLY   A 1 73  ? 39.984 2.484   -4.100  0.40 11.03 ?  73  GLY   A CA   1 
ATOM   1844 C CA   B GLY   A 1 73  ? 39.677 2.536   -4.372  0.60 12.67 ?  73  GLY   A CA   1 
ATOM   1845 C C    A GLY   A 1 73  ? 38.586 1.923   -3.919  0.40 10.85 ?  73  GLY   A C    1 
ATOM   1846 C C    B GLY   A 1 73  ? 38.304 1.913   -4.217  0.60 11.87 ?  73  GLY   A C    1 
ATOM   1847 O O    A GLY   A 1 73  ? 38.190 1.509   -2.823  0.40 10.94 ?  73  GLY   A O    1 
ATOM   1848 O O    B GLY   A 1 73  ? 37.949 1.387   -3.159  0.60 12.62 ?  73  GLY   A O    1 
ATOM   1849 H H    A GLY   A 1 73  ? 40.795 3.235   -2.485  0.40 13.61 ?  73  GLY   A H    1 
ATOM   1850 H H    B GLY   A 1 73  ? 40.448 3.257   -2.721  0.60 15.51 ?  73  GLY   A H    1 
ATOM   1851 H HA2  A GLY   A 1 73  ? 39.910 3.400   -4.423  0.40 13.30 ?  73  GLY   A HA2  1 
ATOM   1852 H HA2  B GLY   A 1 73  ? 39.562 3.458   -4.653  0.60 15.26 ?  73  GLY   A HA2  1 
ATOM   1853 H HA3  A GLY   A 1 73  ? 40.447 1.960   -4.773  0.40 13.30 ?  73  GLY   A HA3  1 
ATOM   1854 H HA3  B GLY   A 1 73  ? 40.154 2.055   -5.060  0.60 15.26 ?  73  GLY   A HA3  1 
ATOM   1855 N N    A PRO   A 1 74  ? 37.816 1.890   -5.003  0.40 11.46 ?  74  PRO   A N    1 
ATOM   1856 N N    B PRO   A 1 74  ? 37.508 1.962   -5.288  0.60 12.08 ?  74  PRO   A N    1 
ATOM   1857 C CA   A PRO   A 1 74  ? 36.416 1.463   -4.906  0.40 11.48 ?  74  PRO   A CA   1 
ATOM   1858 C CA   B PRO   A 1 74  ? 36.117 1.504   -5.200  0.60 12.32 ?  74  PRO   A CA   1 
ATOM   1859 C C    A PRO   A 1 74  ? 36.271 -0.024  -4.620  0.40 10.63 ?  74  PRO   A C    1 
ATOM   1860 C C    B PRO   A 1 74  ? 36.001 0.019   -4.880  0.60 11.98 ?  74  PRO   A C    1 
ATOM   1861 O O    A PRO   A 1 74  ? 37.174 -0.838  -4.832  0.40 10.91 ?  74  PRO   A O    1 
ATOM   1862 O O    B PRO   A 1 74  ? 36.849 -0.806  -5.247  0.60 12.02 ?  74  PRO   A O    1 
ATOM   1863 C CB   A PRO   A 1 74  ? 35.841 1.802   -6.287  0.40 12.85 ?  74  PRO   A CB   1 
ATOM   1864 C CB   B PRO   A 1 74  ? 35.551 1.810   -6.595  0.60 14.10 ?  74  PRO   A CB   1 
ATOM   1865 C CG   A PRO   A 1 74  ? 36.812 2.766   -6.897  0.40 14.40 ?  74  PRO   A CG   1 
ATOM   1866 C CG   B PRO   A 1 74  ? 36.456 2.855   -7.164  0.60 15.43 ?  74  PRO   A CG   1 
ATOM   1867 C CD   A PRO   A 1 74  ? 38.148 2.384   -6.350  0.40 12.90 ?  74  PRO   A CD   1 
ATOM   1868 C CD   B PRO   A 1 74  ? 37.818 2.530   -6.609  0.60 14.10 ?  74  PRO   A CD   1 
ATOM   1869 H HA   A PRO   A 1 74  ? 35.952 1.973   -4.227  0.40 13.83 ?  74  PRO   A HA   1 
ATOM   1870 H HA   B PRO   A 1 74  ? 35.622 2.017   -4.536  0.60 14.84 ?  74  PRO   A HA   1 
ATOM   1871 H HB2  A PRO   A 1 74  ? 35.779 0.995   -6.823  0.40 15.47 ?  74  PRO   A HB2  1 
ATOM   1872 H HB2  B PRO   A 1 74  ? 35.566 1.009   -7.141  0.60 16.98 ?  74  PRO   A HB2  1 
ATOM   1873 H HB3  A PRO   A 1 74  ? 34.967 2.212   -6.186  0.40 15.47 ?  74  PRO   A HB3  1 
ATOM   1874 H HB3  B PRO   A 1 74  ? 34.644 2.154   -6.518  0.60 16.98 ?  74  PRO   A HB3  1 
ATOM   1875 H HG2  A PRO   A 1 74  ? 36.793 2.678   -7.864  0.40 17.34 ?  74  PRO   A HG2  1 
ATOM   1876 H HG2  B PRO   A 1 74  ? 36.465 2.797   -8.130  0.60 18.57 ?  74  PRO   A HG2  1 
ATOM   1877 H HG3  A PRO   A 1 74  ? 36.576 3.671   -6.634  0.40 17.34 ?  74  PRO   A HG3  1 
ATOM   1878 H HG3  B PRO   A 1 74  ? 36.174 3.734   -6.871  0.60 18.57 ?  74  PRO   A HG3  1 
ATOM   1879 H HD2  A PRO   A 1 74  ? 38.547 1.682   -6.889  0.40 15.54 ?  74  PRO   A HD2  1 
ATOM   1880 H HD2  B PRO   A 1 74  ? 38.266 1.866   -7.157  0.60 16.97 ?  74  PRO   A HD2  1 
ATOM   1881 H HD3  A PRO   A 1 74  ? 38.722 3.167   -6.306  0.40 15.54 ?  74  PRO   A HD3  1 
ATOM   1882 H HD3  B PRO   A 1 74  ? 38.350 3.336   -6.519  0.60 16.97 ?  74  PRO   A HD3  1 
ATOM   1883 N N    A LEU   A 1 75  ? 35.086 -0.372  -4.135  0.40 10.88 ?  75  LEU   A N    1 
ATOM   1884 N N    B LEU   A 1 75  ? 34.908 -0.313  -4.192  0.60 11.76 ?  75  LEU   A N    1 
ATOM   1885 C CA   A LEU   A 1 75  ? 34.705 -1.766  -4.002  0.40 11.44 ?  75  LEU   A CA   1 
ATOM   1886 C CA   B LEU   A 1 75  ? 34.530 -1.704  -4.009  0.60 11.49 ?  75  LEU   A CA   1 
ATOM   1887 C C    A LEU   A 1 75  ? 34.326 -2.337  -5.367  0.40 11.52 ?  75  LEU   A C    1 
ATOM   1888 C C    B LEU   A 1 75  ? 34.115 -2.309  -5.345  0.60 12.04 ?  75  LEU   A C    1 
ATOM   1889 O O    A LEU   A 1 75  ? 34.281 -1.636  -6.383  0.40 11.73 ?  75  LEU   A O    1 
ATOM   1890 O O    B LEU   A 1 75  ? 33.842 -1.604  -6.323  0.60 12.97 ?  75  LEU   A O    1 
ATOM   1891 C CB   A LEU   A 1 75  ? 33.513 -1.907  -3.059  0.40 12.21 ?  75  LEU   A CB   1 
ATOM   1892 C CB   B LEU   A 1 75  ? 33.352 -1.830  -3.042  0.60 11.72 ?  75  LEU   A CB   1 
ATOM   1893 C CG   A LEU   A 1 75  ? 33.666 -1.399  -1.627  0.40 13.36 ?  75  LEU   A CG   1 
ATOM   1894 C CG   B LEU   A 1 75  ? 33.616 -1.484  -1.579  0.60 13.19 ?  75  LEU   A CG   1 
ATOM   1895 C CD1  A LEU   A 1 75  ? 32.342 -1.512  -0.873  0.40 14.09 ?  75  LEU   A CD1  1 
ATOM   1896 C CD1  B LEU   A 1 75  ? 32.403 -1.820  -0.719  0.60 14.58 ?  75  LEU   A CD1  1 
ATOM   1897 C CD2  A LEU   A 1 75  ? 34.766 -2.125  -0.887  0.40 14.95 ?  75  LEU   A CD2  1 
ATOM   1898 C CD2  B LEU   A 1 75  ? 34.838 -2.185  -1.053  0.60 16.36 ?  75  LEU   A CD2  1 
ATOM   1899 H H    A LEU   A 1 75  ? 34.489 0.183   -3.874  0.40 13.11 ?  75  LEU   A H    1 
ATOM   1900 H H    B LEU   A 1 75  ? 34.360 0.248   -3.832  0.60 14.17 ?  75  LEU   A H    1 
ATOM   1901 H HA   A LEU   A 1 75  ? 35.457 -2.276  -3.650  0.40 13.79 ?  75  LEU   A HA   1 
ATOM   1902 H HA   B LEU   A 1 75  ? 35.280 -2.206  -3.668  0.60 13.85 ?  75  LEU   A HA   1 
ATOM   1903 H HB2  A LEU   A 1 75  ? 32.771 -1.432  -3.458  0.40 14.71 ?  75  LEU   A HB2  1 
ATOM   1904 H HB2  B LEU   A 1 75  ? 32.639 -1.247  -3.351  0.60 14.12 ?  75  LEU   A HB2  1 
ATOM   1905 H HB3  A LEU   A 1 75  ? 33.295 -2.851  -3.007  0.40 14.71 ?  75  LEU   A HB3  1 
ATOM   1906 H HB3  B LEU   A 1 75  ? 33.036 -2.751  -3.066  0.60 14.12 ?  75  LEU   A HB3  1 
ATOM   1907 H HG   A LEU   A 1 75  ? 33.903 -0.460  -1.657  0.40 16.09 ?  75  LEU   A HG   1 
ATOM   1908 H HG   B LEU   A 1 75  ? 33.769 -0.530  -1.511  0.60 15.89 ?  75  LEU   A HG   1 
ATOM   1909 H HD11 A LEU   A 1 75  ? 32.465 -1.186  0.032   0.40 16.96 ?  75  LEU   A HD11 1 
ATOM   1910 H HD11 B LEU   A 1 75  ? 32.592 -1.578  0.202   0.60 17.56 ?  75  LEU   A HD11 1 
ATOM   1911 H HD12 A LEU   A 1 75  ? 31.670 -0.984  -1.329  0.40 16.96 ?  75  LEU   A HD12 1 
ATOM   1912 H HD12 B LEU   A 1 75  ? 31.638 -1.314  -1.040  0.60 17.56 ?  75  LEU   A HD12 1 
ATOM   1913 H HD13 A LEU   A 1 75  ? 32.069 -2.446  -0.852  0.40 16.96 ?  75  LEU   A HD13 1 
ATOM   1914 H HD13 B LEU   A 1 75  ? 32.221 -2.769  -0.782  0.60 17.56 ?  75  LEU   A HD13 1 
ATOM   1915 H HD21 A LEU   A 1 75  ? 34.814 -1.787  0.020   0.40 18.00 ?  75  LEU   A HD21 1 
ATOM   1916 H HD21 B LEU   A 1 75  ? 34.874 -2.075  -0.091  0.60 19.69 ?  75  LEU   A HD21 1 
ATOM   1917 H HD22 A LEU   A 1 75  ? 34.569 -3.075  -0.878  0.40 18.00 ?  75  LEU   A HD22 1 
ATOM   1918 H HD22 B LEU   A 1 75  ? 34.784 -3.125  -1.280  0.60 19.69 ?  75  LEU   A HD22 1 
ATOM   1919 H HD23 A LEU   A 1 75  ? 35.610 -1.969  -1.343  0.40 18.00 ?  75  LEU   A HD23 1 
ATOM   1920 H HD23 B LEU   A 1 75  ? 35.626 -1.790  -1.460  0.60 19.69 ?  75  LEU   A HD23 1 
ATOM   1921 N N    . LYS   A 1 76  ? 34.056 -3.639  -5.372  1.00 12.44 ?  76  LYS   A N    1 
ATOM   1922 C CA   . LYS   A 1 76  ? 33.465 -4.362  -6.490  1.00 13.18 ?  76  LYS   A CA   1 
ATOM   1923 C C    . LYS   A 1 76  ? 31.954 -4.450  -6.286  1.00 11.96 ?  76  LYS   A C    1 
ATOM   1924 O O    . LYS   A 1 76  ? 31.478 -4.573  -5.158  1.00 11.99 ?  76  LYS   A O    1 
ATOM   1925 C CB   . LYS   A 1 76  ? 34.017 -5.799  -6.539  1.00 14.74 ?  76  LYS   A CB   1 
ATOM   1926 C CG   . LYS   A 1 76  ? 35.535 -5.900  -6.711  1.00 15.97 ?  76  LYS   A CG   1 
ATOM   1927 C CD   . LYS   A 1 76  ? 36.047 -7.318  -6.568  1.00 17.04 ?  76  LYS   A CD   1 
ATOM   1928 C CE   . LYS   A 1 76  ? 37.540 -7.382  -6.786  1.00 19.37 ?  76  LYS   A CE   1 
ATOM   1929 N NZ   . LYS   A 1 76  ? 38.067 -8.744  -6.592  1.00 20.11 ?  76  LYS   A NZ   1 
ATOM   1930 H H    A LYS   A 1 76  ? 34.216 -4.150  -4.695  0.40 14.99 ?  76  LYS   A H    1 
ATOM   1931 H H    B LYS   A 1 76  ? 34.355 -4.149  -4.743  0.60 14.99 ?  76  LYS   A H    1 
ATOM   1932 H HA   . LYS   A 1 76  ? 33.661 -3.913  -7.327  1.00 15.88 ?  76  LYS   A HA   1 
ATOM   1933 H HB2  . LYS   A 1 76  ? 33.790 -6.249  -5.712  1.00 17.75 ?  76  LYS   A HB2  1 
ATOM   1934 H HB3  . LYS   A 1 76  ? 33.612 -6.261  -7.288  1.00 17.75 ?  76  LYS   A HB3  1 
ATOM   1935 H HG2  . LYS   A 1 76  ? 35.781 -5.581  -7.595  1.00 19.22 ?  76  LYS   A HG2  1 
ATOM   1936 H HG3  . LYS   A 1 76  ? 35.972 -5.357  -6.033  1.00 19.22 ?  76  LYS   A HG3  1 
ATOM   1937 H HD2  . LYS   A 1 76  ? 35.852 -7.644  -5.675  1.00 20.50 ?  76  LYS   A HD2  1 
ATOM   1938 H HD3  . LYS   A 1 76  ? 35.617 -7.883  -7.233  1.00 20.50 ?  76  LYS   A HD3  1 
ATOM   1939 H HE2  . LYS   A 1 76  ? 37.746 -7.107  -7.692  1.00 23.31 ?  76  LYS   A HE2  1 
ATOM   1940 H HE3  . LYS   A 1 76  ? 37.982 -6.800  -6.149  1.00 23.31 ?  76  LYS   A HE3  1 
ATOM   1941 H HZ1  . LYS   A 1 76  ? 38.946 -8.764  -6.725  1.00 24.19 ?  76  LYS   A HZ1  1 
ATOM   1942 H HZ2  . LYS   A 1 76  ? 37.895 -9.031  -5.764  1.00 24.19 ?  76  LYS   A HZ2  1 
ATOM   1943 H HZ3  . LYS   A 1 76  ? 37.680 -9.311  -7.169  1.00 24.19 ?  76  LYS   A HZ3  1 
ATOM   1944 N N    . VAL   A 1 77  ? 31.200 -4.422  -7.388  1.00 12.20 ?  77  VAL   A N    1 
ATOM   1945 C CA   . VAL   A 1 77  ? 29.794 -4.807  -7.301  1.00 12.37 ?  77  VAL   A CA   1 
ATOM   1946 C C    . VAL   A 1 77  ? 29.739 -6.263  -6.857  1.00 11.73 ?  77  VAL   A C    1 
ATOM   1947 O O    . VAL   A 1 77  ? 30.406 -7.131  -7.436  1.00 12.27 ?  77  VAL   A O    1 
ATOM   1948 C CB   . VAL   A 1 77  ? 29.077 -4.599  -8.643  1.00 13.51 ?  77  VAL   A CB   1 
ATOM   1949 C CG1  . VAL   A 1 77  ? 27.619 -5.030  -8.547  1.00 14.06 ?  77  VAL   A CG1  1 
ATOM   1950 C CG2  . VAL   A 1 77  ? 29.172 -3.146  -9.064  1.00 14.90 ?  77  VAL   A CG2  1 
ATOM   1951 H H    . VAL   A 1 77  ? 31.477 -4.187  -8.166  1.00 14.70 ?  77  VAL   A H    1 
ATOM   1952 H HA   . VAL   A 1 77  ? 29.360 -4.264  -6.625  1.00 14.90 ?  77  VAL   A HA   1 
ATOM   1953 H HB   . VAL   A 1 77  ? 29.514 -5.135  -9.319  1.00 16.27 ?  77  VAL   A HB   1 
ATOM   1954 H HG11 . VAL   A 1 77  ? 27.158 -4.749  -9.350  1.00 16.92 ?  77  VAL   A HG11 1 
ATOM   1955 H HG12 . VAL   A 1 77  ? 27.580 -5.994  -8.460  1.00 16.92 ?  77  VAL   A HG12 1 
ATOM   1956 H HG13 . VAL   A 1 77  ? 27.217 -4.610  -7.769  1.00 16.92 ?  77  VAL   A HG13 1 
ATOM   1957 H HG21 . VAL   A 1 77  ? 28.656 -3.020  -9.874  1.00 17.94 ?  77  VAL   A HG21 1 
ATOM   1958 H HG22 . VAL   A 1 77  ? 28.814 -2.586  -8.354  1.00 17.94 ?  77  VAL   A HG22 1 
ATOM   1959 H HG23 . VAL   A 1 77  ? 30.101 -2.918  -9.223  1.00 17.94 ?  77  VAL   A HG23 1 
ATOM   1960 N N    . GLY   A 1 78  ? 28.958 -6.536  -5.809  1.00 11.53 ?  78  GLY   A N    1 
ATOM   1961 C CA   . GLY   A 1 78  ? 28.942 -7.829  -5.155  1.00 11.56 ?  78  GLY   A CA   1 
ATOM   1962 C C    . GLY   A 1 78  ? 29.866 -7.929  -3.964  1.00 11.12 ?  78  GLY   A C    1 
ATOM   1963 O O    . GLY   A 1 78  ? 29.816 -8.937  -3.243  1.00 11.81 ?  78  GLY   A O    1 
ATOM   1964 H H    . GLY   A 1 78  ? 28.407 -5.966  -5.465  1.00 13.89 ?  78  GLY   A H    1 
ATOM   1965 H HA2  . GLY   A 1 78  ? 28.042 -8.020  -4.855  1.00 13.92 ?  78  GLY   A HA2  1 
ATOM   1966 H HA3  . GLY   A 1 78  ? 29.200 -8.509  -5.797  1.00 13.92 ?  78  GLY   A HA3  1 
ATOM   1967 N N    . GLY   A 1 79  ? 30.719 -6.924  -3.746  1.00 11.13 ?  79  GLY   A N    1 
ATOM   1968 C CA   . GLY   A 1 79  ? 31.689 -6.938  -2.678  1.00 11.34 ?  79  GLY   A CA   1 
ATOM   1969 C C    . GLY   A 1 79  ? 31.242 -6.142  -1.462  1.00 11.07 ?  79  GLY   A C    1 
ATOM   1970 O O    . GLY   A 1 79  ? 30.121 -5.644  -1.372  1.00 11.83 ?  79  GLY   A O    1 
ATOM   1971 H H    . GLY   A 1 79  ? 30.761 -6.210  -4.229  1.00 13.41 ?  79  GLY   A H    1 
ATOM   1972 H HA2  . GLY   A 1 79  ? 31.847 -7.862  -2.402  1.00 13.67 ?  79  GLY   A HA2  1 
ATOM   1973 H HA3  . GLY   A 1 79  ? 32.530 -6.574  -2.994  1.00 13.67 ?  79  GLY   A HA3  1 
ATOM   1974 N N    . SER   A 1 80  ? 32.154 -6.048  -0.496  1.00 11.71 ?  80  SER   A N    1 
ATOM   1975 C CA   . SER   A 1 80  ? 31.847 -5.423  0.780   1.00 11.06 ?  80  SER   A CA   1 
ATOM   1976 C C    . SER   A 1 80  ? 33.121 -4.975  1.475   1.00 11.26 ?  80  SER   A C    1 
ATOM   1977 O O    . SER   A 1 80  ? 34.236 -5.399  1.133   1.00 12.34 ?  80  SER   A O    1 
ATOM   1978 C CB   . SER   A 1 80  ? 31.104 -6.389  1.706   1.00 11.53 ?  80  SER   A CB   1 
ATOM   1979 O OG   . SER   A 1 80  ? 31.941 -7.436  2.167   1.00 13.44 ?  80  SER   A OG   1 
ATOM   1980 H H    . SER   A 1 80  ? 32.964 -6.327  -0.562  1.00 14.11 ?  80  SER   A H    1 
ATOM   1981 H HA   . SER   A 1 80  ? 31.287 -4.649  0.617   1.00 13.33 ?  80  SER   A HA   1 
ATOM   1982 H HB2  . SER   A 1 80  ? 30.766 -5.898  2.468   1.00 13.89 ?  80  SER   A HB2  1 
ATOM   1983 H HB3  . SER   A 1 80  ? 30.362 -6.784  1.214   1.00 13.89 ?  80  SER   A HB3  1 
ATOM   1984 H HG   . SER   A 1 80  ? 32.246 -7.868  1.512   1.00 16.18 ?  80  SER   A HG   1 
ATOM   1985 N N    . CYS   A 1 81  ? 32.936 -4.121  2.479   1.00 10.56 ?  81  CYS   A N    1 
ATOM   1986 C CA   . CYS   A 1 81  ? 33.999 -3.838  3.430   1.00 10.91 ?  81  CYS   A CA   1 
ATOM   1987 C C    . CYS   A 1 81  ? 33.371 -3.610  4.795   1.00 10.81 ?  81  CYS   A C    1 
ATOM   1988 O O    . CYS   A 1 81  ? 32.205 -3.219  4.901   1.00 11.93 ?  81  CYS   A O    1 
ATOM   1989 C CB   . CYS   A 1 81  ? 34.854 -2.642  2.997   1.00 12.16 ?  81  CYS   A CB   1 
ATOM   1990 S SG   . CYS   A 1 81  ? 33.948 -1.066  3.035   1.00 11.75 ?  81  CYS   A SG   1 
ATOM   1991 H H    . CYS   A 1 81  ? 32.207 -3.686  2.631   1.00 12.73 ?  81  CYS   A H    1 
ATOM   1992 H HA   . CYS   A 1 81  ? 34.587 -4.609  3.486   1.00 13.15 ?  81  CYS   A HA   1 
ATOM   1993 H HB2  . CYS   A 1 81  ? 35.616 -2.564  3.593   1.00 14.65 ?  81  CYS   A HB2  1 
ATOM   1994 H HB3  . CYS   A 1 81  ? 35.164 -2.788  2.087   1.00 14.65 ?  81  CYS   A HB3  1 
ATOM   1995 H HG   . CYS   A 1 81  ? 34.679 -0.178  2.684   1.00 14.16 ?  81  CYS   A HG   1 
ATOM   1996 N N    . VAL   A 1 82  ? 34.151 -3.879  5.838   1.00 11.48 ?  82  VAL   A N    1 
ATOM   1997 C CA   . VAL   A 1 82  ? 33.739 -3.645  7.213   1.00 11.59 ?  82  VAL   A CA   1 
ATOM   1998 C C    . VAL   A 1 82  ? 34.334 -2.322  7.676   1.00 12.17 ?  82  VAL   A C    1 
ATOM   1999 O O    . VAL   A 1 82  ? 35.559 -2.136  7.646   1.00 13.21 ?  82  VAL   A O    1 
ATOM   2000 C CB   . VAL   A 1 82  ? 34.182 -4.786  8.142   1.00 13.25 ?  82  VAL   A CB   1 
ATOM   2001 C CG1  . VAL   A 1 82  ? 33.734 -4.495  9.561   1.00 14.72 ?  82  VAL   A CG1  1 
ATOM   2002 C CG2  . VAL   A 1 82  ? 33.649 -6.133  7.666   1.00 14.33 ?  82  VAL   A CG2  1 
ATOM   2003 H H    . VAL   A 1 82  ? 34.943 -4.223  5.768   1.00 13.83 ?  82  VAL   A H    1 
ATOM   2004 H HA   . VAL   A 1 82  ? 32.771 -3.581  7.248   1.00 13.96 ?  82  VAL   A HA   1 
ATOM   2005 H HB   . VAL   A 1 82  ? 35.151 -4.829  8.142   1.00 15.95 ?  82  VAL   A HB   1 
ATOM   2006 H HG11 . VAL   A 1 82  ? 33.830 -5.298  10.094  1.00 17.72 ?  82  VAL   A HG11 1 
ATOM   2007 H HG12 . VAL   A 1 82  ? 34.286 -3.786  9.933   1.00 17.72 ?  82  VAL   A HG12 1 
ATOM   2008 H HG13 . VAL   A 1 82  ? 32.804 -4.215  9.550   1.00 17.72 ?  82  VAL   A HG13 1 
ATOM   2009 H HG21 . VAL   A 1 82  ? 33.920 -6.817  8.301   1.00 17.26 ?  82  VAL   A HG21 1 
ATOM   2010 H HG22 . VAL   A 1 82  ? 32.685 -6.091  7.615   1.00 17.26 ?  82  VAL   A HG22 1 
ATOM   2011 H HG23 . VAL   A 1 82  ? 34.025 -6.328  6.794   1.00 17.26 ?  82  VAL   A HG23 1 
ATOM   2012 N N    . LEU   A 1 83  ? 33.473 -1.409  8.114   1.00 11.70 ?  83  LEU   A N    1 
ATOM   2013 C CA   . LEU   A 1 83  ? 33.886 -0.139  8.692   1.00 11.81 ?  83  LEU   A CA   1 
ATOM   2014 C C    . LEU   A 1 83  ? 33.193 0.023   10.040  1.00 12.14 ?  83  LEU   A C    1 
ATOM   2015 O O    . LEU   A 1 83  ? 32.491 -0.877  10.512  1.00 12.61 ?  83  LEU   A O    1 
ATOM   2016 C CB   . LEU   A 1 83  ? 33.613 1.026   7.724   1.00 12.02 ?  83  LEU   A CB   1 
ATOM   2017 C CG   . LEU   A 1 83  ? 34.506 1.037   6.473   1.00 13.11 ?  83  LEU   A CG   1 
ATOM   2018 C CD1  . LEU   A 1 83  ? 34.037 2.074   5.473   1.00 13.32 ?  83  LEU   A CD1  1 
ATOM   2019 C CD2  . LEU   A 1 83  ? 35.974 1.286   6.829   1.00 13.95 ?  83  LEU   A CD2  1 
ATOM   2020 H H    . LEU   A 1 83  ? 32.618 -1.507  8.074   1.00 14.10 ?  83  LEU   A H    1 
ATOM   2021 H HA   . LEU   A 1 83  ? 34.841 -0.163  8.848   1.00 14.23 ?  83  LEU   A HA   1 
ATOM   2022 H HB2  . LEU   A 1 83  ? 32.692 0.982   7.422   1.00 14.48 ?  83  LEU   A HB2  1 
ATOM   2023 H HB3  . LEU   A 1 83  ? 33.759 1.866   8.191   1.00 14.48 ?  83  LEU   A HB3  1 
ATOM   2024 H HG   . LEU   A 1 83  ? 34.452 0.170   6.046   1.00 15.79 ?  83  LEU   A HG   1 
ATOM   2025 H HD11 . LEU   A 1 83  ? 34.619 2.045   4.693   1.00 16.04 ?  83  LEU   A HD11 1 
ATOM   2026 H HD12 . LEU   A 1 83  ? 33.127 1.868   5.209   1.00 16.04 ?  83  LEU   A HD12 1 
ATOM   2027 H HD13 . LEU   A 1 83  ? 34.077 2.951   5.881   1.00 16.04 ?  83  LEU   A HD13 1 
ATOM   2028 H HD21 . LEU   A 1 83  ? 36.480 1.431   6.011   1.00 16.80 ?  83  LEU   A HD21 1 
ATOM   2029 H HD22 . LEU   A 1 83  ? 36.035 2.075   7.393   1.00 16.80 ?  83  LEU   A HD22 1 
ATOM   2030 H HD23 . LEU   A 1 83  ? 36.324 0.516   7.299   1.00 16.80 ?  83  LEU   A HD23 1 
ATOM   2031 N N    . SER   A 1 84  ? 33.404 1.175   10.673  1.00 12.70 ?  84  SER   A N    1 
ATOM   2032 C CA   . SER   A 1 84  ? 32.774 1.419   11.961  1.00 13.05 ?  84  SER   A CA   1 
ATOM   2033 C C    . SER   A 1 84  ? 31.254 1.503   11.828  1.00 12.81 ?  84  SER   A C    1 
ATOM   2034 O O    . SER   A 1 84  ? 30.714 1.960   10.822  1.00 12.82 ?  84  SER   A O    1 
ATOM   2035 C CB   . SER   A 1 84  ? 33.281 2.728   12.554  1.00 13.67 ?  84  SER   A CB   1 
ATOM   2036 O OG   . SER   A 1 84  ? 32.644 3.000   13.788  1.00 15.09 ?  84  SER   A OG   1 
ATOM   2037 H H    . SER   A 1 84  ? 33.898 1.821   10.377  1.00 15.30 ?  84  SER   A H    1 
ATOM   2038 H HA   . SER   A 1 84  ? 32.997 0.697   12.565  1.00 15.72 ?  84  SER   A HA   1 
ATOM   2039 H HB2  . SER   A 1 84  ? 34.240 2.658   12.704  1.00 16.46 ?  84  SER   A HB2  1 
ATOM   2040 H HB3  . SER   A 1 84  ? 33.101 3.451   11.931  1.00 16.46 ?  84  SER   A HB3  1 
ATOM   2041 H HG   . SER   A 1 84  ? 32.928 3.728   14.104  1.00 18.16 ?  84  SER   A HG   1 
ATOM   2042 N N    . GLY   A 1 85  ? 30.563 1.072   12.880  1.00 13.43 ?  85  GLY   A N    1 
ATOM   2043 C CA   . GLY   A 1 85  ? 29.143 1.308   12.990  1.00 14.19 ?  85  GLY   A CA   1 
ATOM   2044 C C    . GLY   A 1 85  ? 28.784 2.608   13.668  1.00 14.32 ?  85  GLY   A C    1 
ATOM   2045 O O    . GLY   A 1 85  ? 27.596 2.913   13.808  1.00 14.84 ?  85  GLY   A O    1 
ATOM   2046 H H    . GLY   A 1 85  ? 30.906 0.637   13.538  1.00 16.17 ?  85  GLY   A H    1 
ATOM   2047 H HA2  . GLY   A 1 85  ? 28.757 1.308   12.100  1.00 17.08 ?  85  GLY   A HA2  1 
ATOM   2048 H HA3  . GLY   A 1 85  ? 28.745 0.588   13.493  1.00 17.08 ?  85  GLY   A HA3  1 
ATOM   2049 N N    . HIS   A 1 86  ? 29.774 3.385   14.101  1.00 14.13 ?  86  HIS   A N    1 
ATOM   2050 C CA   . HIS   A 1 86  ? 29.554 4.719   14.679  1.00 14.28 ?  86  HIS   A CA   1 
ATOM   2051 C C    . HIS   A 1 86  ? 28.590 4.590   15.851  1.00 15.56 ?  86  HIS   A C    1 
ATOM   2052 O O    . HIS   A 1 86  ? 28.792 3.710   16.704  1.00 16.13 ?  86  HIS   A O    1 
ATOM   2053 C CB   . HIS   A 1 86  ? 29.151 5.707   13.593  1.00 14.12 ?  86  HIS   A CB   1 
ATOM   2054 C CG   . HIS   A 1 86  ? 30.177 5.815   12.528  1.00 14.02 ?  86  HIS   A CG   1 
ATOM   2055 N ND1  . HIS   A 1 86  ? 31.252 6.674   12.620  1.00 14.88 ?  86  HIS   A ND1  1 
ATOM   2056 C CD2  . HIS   A 1 86  ? 30.342 5.115   11.385  1.00 13.56 ?  86  HIS   A CD2  1 
ATOM   2057 C CE1  . HIS   A 1 86  ? 32.023 6.507   11.562  1.00 14.40 ?  86  HIS   A CE1  1 
ATOM   2058 N NE2  . HIS   A 1 86  ? 31.496 5.566   10.799  1.00 13.71 ?  86  HIS   A NE2  1 
ATOM   2059 H H    . HIS   A 1 86  ? 30.603 3.160   14.079  1.00 17.02 ?  86  HIS   A H    1 
ATOM   2060 H HA   . HIS   A 1 86  ? 30.398 5.032   15.041  1.00 17.19 ?  86  HIS   A HA   1 
ATOM   2061 H HB2  . HIS   A 1 86  ? 28.318 5.417   13.188  1.00 17.00 ?  86  HIS   A HB2  1 
ATOM   2062 H HB3  . HIS   A 1 86  ? 29.035 6.589   13.987  1.00 17.00 ?  86  HIS   A HB3  1 
ATOM   2063 H HD2  . HIS   A 1 86  ? 29.782 4.440   11.058  1.00 16.33 ?  86  HIS   A HD2  1 
ATOM   2064 H HE1  . HIS   A 1 86  ? 32.803 6.979   11.369  1.00 17.34 ?  86  HIS   A HE1  1 
ATOM   2065 H HE2  . HIS   A 1 86  ? 31.819 5.284   10.046  1.00 16.51 ?  86  HIS   A HE2  1 
ATOM   2066 N N    A ASN   A 1 87  ? 27.551 5.419   15.928  0.40 16.04 ?  87  ASN   A N    1 
ATOM   2067 N N    B ASN   A 1 87  ? 27.576 5.437   15.954  0.60 15.96 ?  87  ASN   A N    1 
ATOM   2068 C CA   A ASN   A 1 87  ? 26.549 5.396   16.982  0.40 16.93 ?  87  ASN   A CA   1 
ATOM   2069 C CA   B ASN   A 1 87  ? 26.640 5.395   17.065  0.60 16.96 ?  87  ASN   A CA   1 
ATOM   2070 C C    A ASN   A 1 87  ? 25.393 4.451   16.676  0.40 17.44 ?  87  ASN   A C    1 
ATOM   2071 C C    B ASN   A 1 87  ? 25.569 4.327   16.895  0.60 17.21 ?  87  ASN   A C    1 
ATOM   2072 O O    A ASN   A 1 87  ? 24.362 4.515   17.354  0.40 18.17 ?  87  ASN   A O    1 
ATOM   2073 O O    B ASN   A 1 87  ? 24.774 4.122   17.818  0.60 17.71 ?  87  ASN   A O    1 
ATOM   2074 C CB   A ASN   A 1 87  ? 25.982 6.805   17.175  0.40 17.53 ?  87  ASN   A CB   1 
ATOM   2075 C CB   B ASN   A 1 87  ? 25.990 6.774   17.247  0.60 17.89 ?  87  ASN   A CB   1 
ATOM   2076 C CG   A ASN   A 1 87  ? 25.403 7.381   15.891  0.40 18.24 ?  87  ASN   A CG   1 
ATOM   2077 C CG   B ASN   A 1 87  ? 25.484 7.365   15.940  0.60 18.68 ?  87  ASN   A CG   1 
ATOM   2078 O OD1  A ASN   A 1 87  ? 25.980 7.237   14.814  0.40 18.40 ?  87  ASN   A OD1  1 
ATOM   2079 O OD1  B ASN   A 1 87  ? 26.140 7.274   14.903  0.60 18.92 ?  87  ASN   A OD1  1 
ATOM   2080 N ND2  A ASN   A 1 87  ? 24.255 8.031   16.001  0.40 18.95 ?  87  ASN   A ND2  1 
ATOM   2081 N ND2  B ASN   A 1 87  ? 24.316 7.988   15.991  0.60 19.45 ?  87  ASN   A ND2  1 
ATOM   2082 H H    A ASN   A 1 87  ? 27.402 6.032   15.347  0.40 19.31 ?  87  ASN   A H    1 
ATOM   2083 H H    B ASN   A 1 87  ? 27.408 6.052   15.381  0.60 19.21 ?  87  ASN   A H    1 
ATOM   2084 H HA   A ASN   A 1 87  ? 26.970 5.124   17.816  0.40 20.37 ?  87  ASN   A HA   1 
ATOM   2085 H HA   B ASN   A 1 87  ? 27.123 5.186   17.878  0.60 20.40 ?  87  ASN   A HA   1 
ATOM   2086 H HB2  A ASN   A 1 87  ? 25.271 6.770   17.839  0.40 21.09 ?  87  ASN   A HB2  1 
ATOM   2087 H HB2  B ASN   A 1 87  ? 25.236 6.690   17.854  0.60 21.52 ?  87  ASN   A HB2  1 
ATOM   2088 H HB3  A ASN   A 1 87  ? 26.689 7.393   17.480  0.40 21.09 ?  87  ASN   A HB3  1 
ATOM   2089 H HB3  B ASN   A 1 87  ? 26.646 7.384   17.618  0.60 21.52 ?  87  ASN   A HB3  1 
ATOM   2090 H HD21 A ASN   A 1 87  ? 23.889 8.371   15.302  0.40 22.80 ?  87  ASN   A HD21 1 
ATOM   2091 H HD21 B ASN   A 1 87  ? 23.985 8.341   15.282  0.60 23.40 ?  87  ASN   A HD21 1 
ATOM   2092 H HD22 A ASN   A 1 87  ? 23.877 8.113   16.769  0.40 22.80 ?  87  ASN   A HD22 1 
ATOM   2093 H HD22 B ASN   A 1 87  ? 23.887 8.044   16.738  0.60 23.40 ?  87  ASN   A HD22 1 
ATOM   2094 N N    A LEU   A 1 88  ? 25.526 3.597   15.660  0.40 17.22 ?  88  LEU   A N    1 
ATOM   2095 N N    B LEU   A 1 88  ? 25.555 3.620   15.765  0.60 16.92 ?  88  LEU   A N    1 
ATOM   2096 C CA   A LEU   A 1 88  ? 24.440 2.718   15.246  0.40 16.96 ?  88  LEU   A CA   1 
ATOM   2097 C CA   B LEU   A 1 88  ? 24.445 2.745   15.402  0.60 16.74 ?  88  LEU   A CA   1 
ATOM   2098 C C    A LEU   A 1 88  ? 24.689 1.244   15.526  0.40 16.66 ?  88  LEU   A C    1 
ATOM   2099 C C    B LEU   A 1 88  ? 24.694 1.273   15.703  0.60 16.74 ?  88  LEU   A C    1 
ATOM   2100 O O    A LEU   A 1 88  ? 23.722 0.480   15.618  0.40 16.88 ?  88  LEU   A O    1 
ATOM   2101 O O    B LEU   A 1 88  ? 23.743 0.543   16.007  0.60 17.40 ?  88  LEU   A O    1 
ATOM   2102 C CB   A LEU   A 1 88  ? 24.191 2.865   13.739  0.40 17.68 ?  88  LEU   A CB   1 
ATOM   2103 C CB   B LEU   A 1 88  ? 24.133 2.907   13.910  0.60 17.60 ?  88  LEU   A CB   1 
ATOM   2104 C CG   A LEU   A 1 88  ? 23.862 4.265   13.226  0.40 18.67 ?  88  LEU   A CG   1 
ATOM   2105 C CG   B LEU   A 1 88  ? 23.793 4.328   13.453  0.60 18.59 ?  88  LEU   A CG   1 
ATOM   2106 C CD1  A LEU   A 1 88  ? 23.670 4.239   11.720  0.40 19.08 ?  88  LEU   A CD1  1 
ATOM   2107 C CD1  B LEU   A 1 88  ? 23.556 4.366   11.952  0.60 18.58 ?  88  LEU   A CD1  1 
ATOM   2108 C CD2  A LEU   A 1 88  ? 22.626 4.815   13.921  0.40 19.42 ?  88  LEU   A CD2  1 
ATOM   2109 C CD2  B LEU   A 1 88  ? 22.578 4.860   14.203  0.60 19.79 ?  88  LEU   A CD2  1 
ATOM   2110 H H    A LEU   A 1 88  ? 26.240 3.522   15.187  0.40 20.72 ?  88  LEU   A H    1 
ATOM   2111 H H    B LEU   A 1 88  ? 26.193 3.629   15.184  0.60 20.36 ?  88  LEU   A H    1 
ATOM   2112 H HA   A LEU   A 1 88  ? 23.631 2.981   15.711  0.40 20.41 ?  88  LEU   A HA   1 
ATOM   2113 H HA   B LEU   A 1 88  ? 23.661 3.014   15.895  0.60 20.15 ?  88  LEU   A HA   1 
ATOM   2114 H HB2  A LEU   A 1 88  ? 24.986 2.566   13.274  0.40 21.27 ?  88  LEU   A HB2  1 
ATOM   2115 H HB2  B LEU   A 1 88  ? 24.902 2.619   13.395  0.60 21.18 ?  88  LEU   A HB2  1 
ATOM   2116 H HB3  A LEU   A 1 88  ? 23.447 2.289   13.506  0.40 21.27 ?  88  LEU   A HB3  1 
ATOM   2117 H HB3  B LEU   A 1 88  ? 23.370 2.350   13.691  0.60 21.18 ?  88  LEU   A HB3  1 
ATOM   2118 H HG   A LEU   A 1 88  ? 24.605 4.855   13.423  0.40 22.46 ?  88  LEU   A HG   1 
ATOM   2119 H HG   B LEU   A 1 88  ? 24.544 4.911   13.644  0.60 22.36 ?  88  LEU   A HG   1 
ATOM   2120 H HD11 A LEU   A 1 88  ? 23.500 5.142   11.408  0.40 22.95 ?  88  LEU   A HD11 1 
ATOM   2121 H HD11 B LEU   A 1 88  ? 23.344 5.276   11.685  0.60 22.35 ?  88  LEU   A HD11 1 
ATOM   2122 H HD12 A LEU   A 1 88  ? 24.475 3.891   11.304  0.40 22.95 ?  88  LEU   A HD12 1 
ATOM   2123 H HD12 B LEU   A 1 88  ? 24.358 4.068   11.494  0.60 22.35 ?  88  LEU   A HD12 1 
ATOM   2124 H HD13 A LEU   A 1 88  ? 22.915 3.668   11.509  0.40 22.95 ?  88  LEU   A HD13 1 
ATOM   2125 H HD13 B LEU   A 1 88  ? 22.814 3.779   11.732  0.60 22.35 ?  88  LEU   A HD13 1 
ATOM   2126 H HD21 A LEU   A 1 88  ? 22.376 5.651   13.500  0.40 23.36 ?  88  LEU   A HD21 1 
ATOM   2127 H HD21 B LEU   A 1 88  ? 22.303 5.700   13.803  0.60 23.81 ?  88  LEU   A HD21 1 
ATOM   2128 H HD22 A LEU   A 1 88  ? 21.905 4.172   13.837  0.40 23.36 ?  88  LEU   A HD22 1 
ATOM   2129 H HD22 B LEU   A 1 88  ? 21.862 4.211   14.140  0.60 23.81 ?  88  LEU   A HD22 1 
ATOM   2130 H HD23 A LEU   A 1 88  ? 22.830 4.962   14.858  0.40 23.36 ?  88  LEU   A HD23 1 
ATOM   2131 H HD23 B LEU   A 1 88  ? 22.821 4.999   15.131  0.60 23.81 ?  88  LEU   A HD23 1 
ATOM   2132 N N    . ALA   A 1 89  ? 25.944 0.827   15.636  1.00 16.10 ?  89  ALA   A N    1 
ATOM   2133 C CA   . ALA   A 1 89  ? 26.294 -0.583  15.730  1.00 16.01 ?  89  ALA   A CA   1 
ATOM   2134 C C    . ALA   A 1 89  ? 27.789 -0.628  15.987  1.00 16.66 ?  89  ALA   A C    1 
ATOM   2135 O O    . ALA   A 1 89  ? 28.482 0.380   15.852  1.00 17.01 ?  89  ALA   A O    1 
ATOM   2136 C CB   . ALA   A 1 89  ? 25.983 -1.289  14.411  1.00 15.38 ?  89  ALA   A CB   1 
ATOM   2137 H H    A ALA   A 1 89  ? 26.627 1.353   15.631  0.40 19.38 ?  89  ALA   A H    1 
ATOM   2138 H H    B ALA   A 1 89  ? 26.629 1.342   15.539  0.60 19.38 ?  89  ALA   A H    1 
ATOM   2139 H HA   . ALA   A 1 89  ? 25.817 -1.007  16.457  1.00 19.27 ?  89  ALA   A HA   1 
ATOM   2140 H HB1  . ALA   A 1 89  ? 26.260 -2.218  14.478  1.00 18.52 ?  89  ALA   A HB1  1 
ATOM   2141 H HB2  . ALA   A 1 89  ? 25.030 -1.240  14.240  1.00 18.52 ?  89  ALA   A HB2  1 
ATOM   2142 H HB3  . ALA   A 1 89  ? 26.472 -0.854  13.695  1.00 18.52 ?  89  ALA   A HB3  1 
ATOM   2143 N N    A LYS   A 1 90  ? 28.285 -1.809  16.354  0.40 17.07 ?  90  LYS   A N    1 
ATOM   2144 N N    B LYS   A 1 90  ? 28.293 -1.805  16.351  0.60 16.66 ?  90  LYS   A N    1 
ATOM   2145 C CA   A LYS   A 1 90  ? 29.728 -1.969  16.502  0.40 17.83 ?  90  LYS   A CA   1 
ATOM   2146 C CA   B LYS   A 1 90  ? 29.742 -1.944  16.454  0.60 17.05 ?  90  LYS   A CA   1 
ATOM   2147 C C    A LYS   A 1 90  ? 30.429 -1.825  15.159  0.40 16.72 ?  90  LYS   A C    1 
ATOM   2148 C C    B LYS   A 1 90  ? 30.391 -1.735  15.091  0.60 15.61 ?  90  LYS   A C    1 
ATOM   2149 O O    A LYS   A 1 90  ? 31.459 -1.146  15.057  0.40 17.31 ?  90  LYS   A O    1 
ATOM   2150 O O    B LYS   A 1 90  ? 31.272 -0.879  14.925  0.60 16.17 ?  90  LYS   A O    1 
ATOM   2151 C CB   A LYS   A 1 90  ? 30.046 -3.327  17.125  0.40 20.32 ?  90  LYS   A CB   1 
ATOM   2152 C CB   B LYS   A 1 90  ? 30.109 -3.309  17.042  0.60 19.82 ?  90  LYS   A CB   1 
ATOM   2153 C CG   A LYS   A 1 90  ? 31.512 -3.511  17.479  0.40 23.13 ?  90  LYS   A CG   1 
ATOM   2154 C CG   B LYS   A 1 90  ? 31.594 -3.457  17.339  0.60 23.03 ?  90  LYS   A CG   1 
ATOM   2155 C CD   A LYS   A 1 90  ? 31.706 -4.714  18.387  0.40 25.61 ?  90  LYS   A CD   1 
ATOM   2156 C CD   B LYS   A 1 90  ? 31.882 -4.721  18.134  0.60 26.02 ?  90  LYS   A CD   1 
ATOM   2157 C CE   A LYS   A 1 90  ? 33.125 -4.785  18.927  0.40 27.40 ?  90  LYS   A CE   1 
ATOM   2158 C CE   B LYS   A 1 90  ? 33.283 -4.705  18.733  0.60 28.25 ?  90  LYS   A CE   1 
ATOM   2159 N NZ   A LYS   A 1 90  ? 34.117 -5.088  17.862  0.40 28.45 ?  90  LYS   A NZ   1 
ATOM   2160 N NZ   B LYS   A 1 90  ? 34.359 -4.828  17.709  0.60 29.63 ?  90  LYS   A NZ   1 
ATOM   2161 H H    A LYS   A 1 90  ? 27.824 -2.511  16.517  0.40 20.54 ?  90  LYS   A H    1 
ATOM   2162 H H    B LYS   A 1 90  ? 27.839 -2.508  16.531  0.60 20.05 ?  90  LYS   A H    1 
ATOM   2163 H HA   A LYS   A 1 90  ? 30.069 -1.277  17.087  0.40 21.46 ?  90  LYS   A HA   1 
ATOM   2164 H HA   B LYS   A 1 90  ? 30.084 -1.263  17.052  0.60 20.52 ?  90  LYS   A HA   1 
ATOM   2165 H HB2  A LYS   A 1 90  ? 29.529 -3.422  17.938  0.40 24.44 ?  90  LYS   A HB2  1 
ATOM   2166 H HB2  B LYS   A 1 90  ? 29.625 -3.433  17.877  0.60 23.84 ?  90  LYS   A HB2  1 
ATOM   2167 H HB3  A LYS   A 1 90  ? 29.803 -4.024  16.496  0.40 24.44 ?  90  LYS   A HB3  1 
ATOM   2168 H HB3  B LYS   A 1 90  ? 29.859 -4.004  16.413  0.60 23.84 ?  90  LYS   A HB3  1 
ATOM   2169 H HG2  A LYS   A 1 90  ? 32.024 -3.656  16.667  0.40 27.81 ?  90  LYS   A HG2  1 
ATOM   2170 H HG2  B LYS   A 1 90  ? 32.084 -3.507  16.504  0.60 27.70 ?  90  LYS   A HG2  1 
ATOM   2171 H HG3  A LYS   A 1 90  ? 31.832 -2.723  17.943  0.40 27.81 ?  90  LYS   A HG3  1 
ATOM   2172 H HG3  B LYS   A 1 90  ? 31.894 -2.697  17.861  0.60 27.70 ?  90  LYS   A HG3  1 
ATOM   2173 H HD2  A LYS   A 1 90  ? 31.098 -4.648  19.140  0.40 30.79 ?  90  LYS   A HD2  1 
ATOM   2174 H HD2  B LYS   A 1 90  ? 31.242 -4.796  18.860  0.60 31.28 ?  90  LYS   A HD2  1 
ATOM   2175 H HD3  A LYS   A 1 90  ? 31.532 -5.526  17.885  0.40 30.79 ?  90  LYS   A HD3  1 
ATOM   2176 H HD3  B LYS   A 1 90  ? 31.812 -5.491  17.547  0.60 31.28 ?  90  LYS   A HD3  1 
ATOM   2177 H HE2  A LYS   A 1 90  ? 33.357 -3.929  19.322  0.40 32.94 ?  90  LYS   A HE2  1 
ATOM   2178 H HE2  B LYS   A 1 90  ? 33.414 -3.866  19.204  0.60 33.95 ?  90  LYS   A HE2  1 
ATOM   2179 H HE3  A LYS   A 1 90  ? 33.176 -5.485  19.596  0.40 32.94 ?  90  LYS   A HE3  1 
ATOM   2180 H HE3  B LYS   A 1 90  ? 33.371 -5.447  19.351  0.60 33.95 ?  90  LYS   A HE3  1 
ATOM   2181 H HZ1  A LYS   A 1 90  ? 34.933 -5.146  18.214  0.40 34.20 ?  90  LYS   A HZ1  1 
ATOM   2182 H HZ1  B LYS   A 1 90  ? 35.157 -4.814  18.104  0.60 35.61 ?  90  LYS   A HZ1  1 
ATOM   2183 H HZ2  A LYS   A 1 90  ? 33.916 -5.860  17.469  0.40 34.20 ?  90  LYS   A HZ2  1 
ATOM   2184 H HZ2  B LYS   A 1 90  ? 34.270 -5.596  17.267  0.60 35.61 ?  90  LYS   A HZ2  1 
ATOM   2185 H HZ3  A LYS   A 1 90  ? 34.113 -4.441  17.250  0.40 34.20 ?  90  LYS   A HZ3  1 
ATOM   2186 H HZ3  B LYS   A 1 90  ? 34.309 -4.154  17.132  0.60 35.61 ?  90  LYS   A HZ3  1 
ATOM   2187 N N    A HIS   A 1 91  ? 29.879 -2.453  14.122  0.40 15.26 ?  91  HIS   A N    1 
ATOM   2188 N N    B HIS   A 1 91  ? 29.933 -2.485  14.094  0.60 14.10 ?  91  HIS   A N    1 
ATOM   2189 C CA   A HIS   A 1 91  ? 30.433 -2.411  12.782  0.40 14.52 ?  91  HIS   A CA   1 
ATOM   2190 C CA   B HIS   A 1 91  ? 30.468 -2.442  12.748  0.60 13.73 ?  91  HIS   A CA   1 
ATOM   2191 C C    A HIS   A 1 91  ? 29.326 -2.124  11.783  0.40 12.82 ?  91  HIS   A C    1 
ATOM   2192 C C    B HIS   A 1 91  ? 29.349 -2.181  11.756  0.60 12.21 ?  91  HIS   A C    1 
ATOM   2193 O O    A HIS   A 1 91  ? 28.150 -2.420  12.025  0.40 13.47 ?  91  HIS   A O    1 
ATOM   2194 O O    B HIS   A 1 91  ? 28.195 -2.578  11.965  0.60 12.78 ?  91  HIS   A O    1 
ATOM   2195 C CB   A HIS   A 1 91  ? 31.069 -3.756  12.394  0.40 16.23 ?  91  HIS   A CB   1 
ATOM   2196 C CB   B HIS   A 1 91  ? 31.089 -3.787  12.345  0.60 15.73 ?  91  HIS   A CB   1 
ATOM   2197 C CG   A HIS   A 1 91  ? 32.008 -4.304  13.422  0.40 18.92 ?  91  HIS   A CG   1 
ATOM   2198 C CG   B HIS   A 1 91  ? 32.127 -4.290  13.298  0.60 19.34 ?  91  HIS   A CG   1 
ATOM   2199 N ND1  A HIS   A 1 91  ? 33.276 -3.799  13.617  0.40 20.18 ?  91  HIS   A ND1  1 
ATOM   2200 N ND1  B HIS   A 1 91  ? 33.398 -3.763  13.360  0.60 21.10 ?  91  HIS   A ND1  1 
ATOM   2201 C CD2  A HIS   A 1 91  ? 31.868 -5.319  14.306  0.40 20.11 ?  91  HIS   A CD2  1 
ATOM   2202 C CD2  B HIS   A 1 91  ? 32.088 -5.285  14.216  0.60 20.91 ?  91  HIS   A CD2  1 
ATOM   2203 C CE1  A HIS   A 1 91  ? 33.874 -4.478  14.580  0.40 20.80 ?  91  HIS   A CE1  1 
ATOM   2204 C CE1  B HIS   A 1 91  ? 34.096 -4.405  14.280  0.60 21.88 ?  91  HIS   A CE1  1 
ATOM   2205 N NE2  A HIS   A 1 91  ? 33.040 -5.406  15.016  0.40 20.91 ?  91  HIS   A NE2  1 
ATOM   2206 N NE2  B HIS   A 1 91  ? 33.323 -5.334  14.815  0.60 22.14 ?  91  HIS   A NE2  1 
ATOM   2207 H H    A HIS   A 1 91  ? 29.165 -2.935  14.176  0.40 18.37 ?  91  HIS   A H    1 
ATOM   2208 H H    B HIS   A 1 91  ? 29.288 -3.056  14.181  0.60 16.97 ?  91  HIS   A H    1 
ATOM   2209 H HA   A HIS   A 1 91  ? 31.103 -1.719  12.714  0.40 17.48 ?  91  HIS   A HA   1 
ATOM   2210 H HA   B HIS   A 1 91  ? 31.139 -1.750  12.669  0.60 16.53 ?  91  HIS   A HA   1 
ATOM   2211 H HB2  A HIS   A 1 91  ? 30.366 -4.412  12.261  0.40 19.53 ?  91  HIS   A HB2  1 
ATOM   2212 H HB2  B HIS   A 1 91  ? 30.390 -4.457  12.296  0.60 18.93 ?  91  HIS   A HB2  1 
ATOM   2213 H HB3  A HIS   A 1 91  ? 31.570 -3.642  11.570  0.40 19.53 ?  91  HIS   A HB3  1 
ATOM   2214 H HB3  B HIS   A 1 91  ? 31.513 -3.691  11.477  0.60 18.93 ?  91  HIS   A HB3  1 
ATOM   2215 H HD1  A HIS   A 1 91  ? 33.625 -3.144  13.179  0.40 24.28 ?  91  HIS   A HD1  1 
ATOM   2216 H HD1  B HIS   A 1 91  ? 33.694 -3.119  12.878  0.60 25.37 ?  91  HIS   A HD1  1 
ATOM   2217 H HD2  A HIS   A 1 91  ? 31.121 -5.857  14.416  0.40 24.19 ?  91  HIS   A HD2  1 
ATOM   2218 H HD2  B HIS   A 1 91  ? 31.359 -5.830  14.409  0.60 25.15 ?  91  HIS   A HD2  1 
ATOM   2219 H HE1  A HIS   A 1 91  ? 34.739 -4.326  14.896  0.40 25.02 ?  91  HIS   A HE1  1 
ATOM   2220 H HE1  B HIS   A 1 91  ? 34.980 -4.236  14.517  0.60 26.32 ?  91  HIS   A HE1  1 
ATOM   2221 N N    . CYS   A 1 92  ? 29.719 -1.556  10.647  1.00 12.07 ?  92  CYS   A N    1 
ATOM   2222 C CA   . CYS   A 1 92  ? 28.856 -1.467  9.478   1.00 11.78 ?  92  CYS   A CA   1 
ATOM   2223 C C    . CYS   A 1 92  ? 29.497 -2.276  8.361   1.00 11.03 ?  92  CYS   A C    1 
ATOM   2224 O O    . CYS   A 1 92  ? 30.646 -2.010  7.985   1.00 11.92 ?  92  CYS   A O    1 
ATOM   2225 C CB   . CYS   A 1 92  ? 28.630 -0.023  9.030   1.00 12.21 ?  92  CYS   A CB   1 
ATOM   2226 S SG   . CYS   A 1 92  ? 27.593 0.082   7.534   1.00 11.60 ?  92  CYS   A SG   1 
ATOM   2227 H H    A CYS   A 1 92  ? 30.494 -1.206  10.530  0.40 14.54 ?  92  CYS   A H    1 
ATOM   2228 H H    B CYS   A 1 92  ? 30.476 -1.166  10.545  0.60 14.54 ?  92  CYS   A H    1 
ATOM   2229 H HA   . CYS   A 1 92  ? 27.994 -1.859  9.684   1.00 14.19 ?  92  CYS   A HA   1 
ATOM   2230 H HB2  . CYS   A 1 92  ? 28.185 0.464   9.743   1.00 14.70 ?  92  CYS   A HB2  1 
ATOM   2231 H HB3  . CYS   A 1 92  ? 29.486 0.385   8.831   1.00 14.70 ?  92  CYS   A HB3  1 
ATOM   2232 H HG   . CYS   A 1 92  ? 27.434 1.237   7.246   1.00 13.97 ?  92  CYS   A HG   1 
ATOM   2233 N N    . LEU   A 1 93  ? 28.763 -3.265  7.856   1.00 10.88 ?  93  LEU   A N    1 
ATOM   2234 C CA   . LEU   A 1 93  ? 29.168 -4.025  6.678   1.00 10.88 ?  93  LEU   A CA   1 
ATOM   2235 C C    . LEU   A 1 93  ? 28.551 -3.333  5.469   1.00 10.48 ?  93  LEU   A C    1 
ATOM   2236 O O    . LEU   A 1 93  ? 27.331 -3.390  5.268   1.00 10.60 ?  93  LEU   A O    1 
ATOM   2237 C CB   . LEU   A 1 93  ? 28.684 -5.473  6.778   1.00 11.06 ?  93  LEU   A CB   1 
ATOM   2238 C CG   . LEU   A 1 93  ? 29.062 -6.364  5.592   1.00 11.25 ?  93  LEU   A CG   1 
ATOM   2239 C CD1  . LEU   A 1 93  ? 30.577 -6.604  5.532   1.00 11.95 ?  93  LEU   A CD1  1 
ATOM   2240 C CD2  . LEU   A 1 93  ? 28.309 -7.687  5.634   1.00 12.14 ?  93  LEU   A CD2  1 
ATOM   2241 H H    . LEU   A 1 93  ? 28.008 -3.519  8.193   1.00 13.11 ?  93  LEU   A H    1 
ATOM   2242 H HA   . LEU   A 1 93  ? 30.132 -4.015  6.600   1.00 13.11 ?  93  LEU   A HA   1 
ATOM   2243 H HB2  . LEU   A 1 93  ? 29.066 -5.873  7.578   1.00 13.33 ?  93  LEU   A HB2  1 
ATOM   2244 H HB3  . LEU   A 1 93  ? 27.717 -5.474  6.848   1.00 13.33 ?  93  LEU   A HB3  1 
ATOM   2245 H HG   . LEU   A 1 93  ? 28.809 -5.920  4.774   1.00 13.56 ?  93  LEU   A HG   1 
ATOM   2246 H HD11 . LEU   A 1 93  ? 30.780 -7.211  4.800   1.00 14.40 ?  93  LEU   A HD11 1 
ATOM   2247 H HD12 . LEU   A 1 93  ? 31.029 -5.756  5.387   1.00 14.40 ?  93  LEU   A HD12 1 
ATOM   2248 H HD13 . LEU   A 1 93  ? 30.877 -6.994  6.371   1.00 14.40 ?  93  LEU   A HD13 1 
ATOM   2249 H HD21 . LEU   A 1 93  ? 28.579 -8.229  4.869   1.00 14.63 ?  93  LEU   A HD21 1 
ATOM   2250 H HD22 . LEU   A 1 93  ? 28.531 -8.155  6.456   1.00 14.63 ?  93  LEU   A HD22 1 
ATOM   2251 H HD23 . LEU   A 1 93  ? 27.359 -7.514  5.595   1.00 14.63 ?  93  LEU   A HD23 1 
ATOM   2252 N N    . HIS   A 1 94  ? 29.381 -2.630  4.697   1.00 10.15 ?  94  HIS   A N    1 
ATOM   2253 C CA   . HIS   A 1 94  ? 28.938 -1.952  3.483   1.00 10.21 ?  94  HIS   A CA   1 
ATOM   2254 C C    . HIS   A 1 94  ? 28.941 -2.976  2.365   1.00 10.02 ?  94  HIS   A C    1 
ATOM   2255 O O    . HIS   A 1 94  ? 30.007 -3.479  2.006   1.00 11.26 ?  94  HIS   A O    1 
ATOM   2256 C CB   . HIS   A 1 94  ? 29.872 -0.791  3.142   1.00 10.42 ?  94  HIS   A CB   1 
ATOM   2257 C CG   . HIS   A 1 94  ? 29.862 0.294   4.164   1.00 10.39 ?  94  HIS   A CG   1 
ATOM   2258 N ND1  . HIS   A 1 94  ? 28.979 1.352   4.125   1.00 10.49 ?  94  HIS   A ND1  1 
ATOM   2259 C CD2  . HIS   A 1 94  ? 30.616 0.462   5.273   1.00 11.12 ?  94  HIS   A CD2  1 
ATOM   2260 C CE1  . HIS   A 1 94  ? 29.195 2.125   5.173   1.00 10.59 ?  94  HIS   A CE1  1 
ATOM   2261 N NE2  . HIS   A 1 94  ? 30.184 1.610   5.882   1.00 10.83 ?  94  HIS   A NE2  1 
ATOM   2262 H H    . HIS   A 1 94  ? 30.228 -2.539  4.856   1.00 12.24 ?  94  HIS   A H    1 
ATOM   2263 H HA   . HIS   A 1 94  ? 28.033 -1.619  3.606   1.00 12.31 ?  94  HIS   A HA   1 
ATOM   2264 H HB2  . HIS   A 1 94  ? 30.773 -1.133  3.070   1.00 12.56 ?  94  HIS   A HB2  1 
ATOM   2265 H HB3  . HIS   A 1 94  ? 29.588 -0.412  2.295   1.00 12.56 ?  94  HIS   A HB3  1 
ATOM   2266 H HD2  . HIS   A 1 94  ? 31.301 -0.092  5.565   1.00 13.40 ?  94  HIS   A HD2  1 
ATOM   2267 H HE1  . HIS   A 1 94  ? 28.730 2.905   5.375   1.00 12.77 ?  94  HIS   A HE1  1 
ATOM   2268 H HE2  . HIS   A 1 94  ? 30.509 1.950   6.602   1.00 13.06 ?  94  HIS   A HE2  1 
ATOM   2269 N N    . VAL   A 1 95  ? 27.770 -3.297  1.821   1.00 9.72  ?  95  VAL   A N    1 
ATOM   2270 C CA   . VAL   A 1 95  ? 27.630 -4.333  0.803   1.00 9.75  ?  95  VAL   A CA   1 
ATOM   2271 C C    . VAL   A 1 95  ? 27.071 -3.697  -0.456  1.00 9.91  ?  95  VAL   A C    1 
ATOM   2272 O O    . VAL   A 1 95  ? 26.062 -2.985  -0.397  1.00 10.82 ?  95  VAL   A O    1 
ATOM   2273 C CB   . VAL   A 1 95  ? 26.709 -5.476  1.262   1.00 10.44 ?  95  VAL   A CB   1 
ATOM   2274 C CG1  . VAL   A 1 95  ? 26.610 -6.535  0.169   1.00 10.99 ?  95  VAL   A CG1  1 
ATOM   2275 C CG2  . VAL   A 1 95  ? 27.222 -6.086  2.540   1.00 10.92 ?  95  VAL   A CG2  1 
ATOM   2276 H H    . VAL   A 1 95  ? 27.021 -2.931  2.040   1.00 11.72 ?  95  VAL   A H    1 
ATOM   2277 H HA   . VAL   A 1 95  ? 28.499 -4.706  0.593   1.00 11.76 ?  95  VAL   A HA   1 
ATOM   2278 H HB   . VAL   A 1 95  ? 25.824 -5.129  1.426   1.00 12.58 ?  95  VAL   A HB   1 
ATOM   2279 H HG11 . VAL   A 1 95  ? 26.203 -7.340  0.539   1.00 13.24 ?  95  VAL   A HG11 1 
ATOM   2280 H HG12 . VAL   A 1 95  ? 26.058 -6.201  -0.558  1.00 13.24 ?  95  VAL   A HG12 1 
ATOM   2281 H HG13 . VAL   A 1 95  ? 27.498 -6.747  -0.162  1.00 13.24 ?  95  VAL   A HG13 1 
ATOM   2282 H HG21 . VAL   A 1 95  ? 26.670 -6.853  2.766   1.00 13.16 ?  95  VAL   A HG21 1 
ATOM   2283 H HG22 . VAL   A 1 95  ? 28.140 -6.366  2.414   1.00 13.16 ?  95  VAL   A HG22 1 
ATOM   2284 H HG23 . VAL   A 1 95  ? 27.169 -5.424  3.246   1.00 13.16 ?  95  VAL   A HG23 1 
ATOM   2285 N N    . VAL   A 1 96  ? 27.684 -3.989  -1.599  1.00 10.10 ?  96  VAL   A N    1 
ATOM   2286 C CA   . VAL   A 1 96  ? 27.266 -3.431  -2.876  1.00 10.50 ?  96  VAL   A CA   1 
ATOM   2287 C C    . VAL   A 1 96  ? 26.464 -4.478  -3.638  1.00 10.80 ?  96  VAL   A C    1 
ATOM   2288 O O    . VAL   A 1 96  ? 27.026 -5.416  -4.212  1.00 11.77 ?  96  VAL   A O    1 
ATOM   2289 C CB   . VAL   A 1 96  ? 28.453 -2.943  -3.704  1.00 11.11 ?  96  VAL   A CB   1 
ATOM   2290 C CG1  . VAL   A 1 96  ? 27.942 -2.291  -4.981  1.00 11.46 ?  96  VAL   A CG1  1 
ATOM   2291 C CG2  . VAL   A 1 96  ? 29.306 -1.974  -2.894  1.00 11.79 ?  96  VAL   A CG2  1 
ATOM   2292 H H    . VAL   A 1 96  ? 28.355 -4.524  -1.659  1.00 12.18 ?  96  VAL   A H    1 
ATOM   2293 H HA   . VAL   A 1 96  ? 26.682 -2.672  -2.712  1.00 12.66 ?  96  VAL   A HA   1 
ATOM   2294 H HB   . VAL   A 1 96  ? 29.002 -3.700  -3.949  1.00 13.39 ?  96  VAL   A HB   1 
ATOM   2295 H HG11 . VAL   A 1 96  ? 28.682 -1.821  -5.405  1.00 13.80 ?  96  VAL   A HG11 1 
ATOM   2296 H HG12 . VAL   A 1 96  ? 27.601 -2.971  -5.575  1.00 13.80 ?  96  VAL   A HG12 1 
ATOM   2297 H HG13 . VAL   A 1 96  ? 27.243 -1.657  -4.755  1.00 13.80 ?  96  VAL   A HG13 1 
ATOM   2298 H HG21 . VAL   A 1 96  ? 29.999 -1.611  -3.459  1.00 14.21 ?  96  VAL   A HG21 1 
ATOM   2299 H HG22 . VAL   A 1 96  ? 28.739 -1.256  -2.559  1.00 14.21 ?  96  VAL   A HG22 1 
ATOM   2300 H HG23 . VAL   A 1 96  ? 29.701 -2.450  -2.144  1.00 14.21 ?  96  VAL   A HG23 1 
ATOM   2301 N N    A GLY   A 1 97  ? 25.141 -4.338  -3.616  0.40 10.47 ?  97  GLY   A N    1 
ATOM   2302 N N    B GLY   A 1 97  ? 25.142 -4.317  -3.688  0.60 10.31 ?  97  GLY   A N    1 
ATOM   2303 C CA   A GLY   A 1 97  ? 24.294 -5.086  -4.505  0.40 11.05 ?  97  GLY   A CA   1 
ATOM   2304 C CA   B GLY   A 1 97  ? 24.339 -5.084  -4.609  0.60 11.01 ?  97  GLY   A CA   1 
ATOM   2305 C C    A GLY   A 1 97  ? 24.240 -4.400  -5.850  0.40 11.25 ?  97  GLY   A C    1 
ATOM   2306 C C    B GLY   A 1 97  ? 24.383 -4.467  -5.996  0.60 11.06 ?  97  GLY   A C    1 
ATOM   2307 O O    A GLY   A 1 97  ? 24.466 -3.191  -5.955  0.40 11.47 ?  97  GLY   A O    1 
ATOM   2308 O O    B GLY   A 1 97  ? 24.710 -3.286  -6.157  0.60 11.72 ?  97  GLY   A O    1 
ATOM   2309 H H    A GLY   A 1 97  ? 24.710 -3.804  -3.091  0.40 12.62 ?  97  GLY   A H    1 
ATOM   2310 H H    B GLY   A 1 97  ? 24.688 -3.771  -3.193  0.60 12.43 ?  97  GLY   A H    1 
ATOM   2311 H HA2  A GLY   A 1 97  ? 24.647 -5.977  -4.620  0.40 13.31 ?  97  GLY   A HA2  1 
ATOM   2312 H HA2  B GLY   A 1 97  ? 24.679 -5.992  -4.653  0.60 13.27 ?  97  GLY   A HA2  1 
ATOM   2313 H HA3  A GLY   A 1 97  ? 23.394 -5.138  -4.151  0.40 13.31 ?  97  GLY   A HA3  1 
ATOM   2314 H HA3  B GLY   A 1 97  ? 23.417 -5.114  -4.303  0.60 13.27 ?  97  GLY   A HA3  1 
ATOM   2315 N N    A PRO   A 1 98  ? 23.930 -5.148  -6.906  0.40 11.30 ?  98  PRO   A N    1 
ATOM   2316 N N    B PRO   A 1 98  ? 24.043 -5.244  -7.024  0.60 11.32 ?  98  PRO   A N    1 
ATOM   2317 C CA   A PRO   A 1 98  ? 23.820 -4.529  -8.230  0.40 11.69 ?  98  PRO   A CA   1 
ATOM   2318 C CA   B PRO   A 1 98  ? 23.970 -4.681  -8.377  0.60 12.56 ?  98  PRO   A CA   1 
ATOM   2319 C C    A PRO   A 1 98  ? 22.719 -3.482  -8.256  0.40 11.65 ?  98  PRO   A C    1 
ATOM   2320 C C    B PRO   A 1 98  ? 22.852 -3.657  -8.494  0.60 13.15 ?  98  PRO   A C    1 
ATOM   2321 O O    A PRO   A 1 98  ? 21.647 -3.662  -7.674  0.40 11.72 ?  98  PRO   A O    1 
ATOM   2322 O O    B PRO   A 1 98  ? 21.778 -3.801  -7.905  0.60 13.39 ?  98  PRO   A O    1 
ATOM   2323 C CB   A PRO   A 1 98  ? 23.497 -5.713  -9.150  0.40 12.02 ?  98  PRO   A CB   1 
ATOM   2324 C CB   B PRO   A 1 98  ? 23.687 -5.906  -9.255  0.60 12.70 ?  98  PRO   A CB   1 
ATOM   2325 C CG   A PRO   A 1 98  ? 22.870 -6.732  -8.252  0.40 12.50 ?  98  PRO   A CG   1 
ATOM   2326 C CG   B PRO   A 1 98  ? 23.027 -6.885  -8.333  0.60 13.41 ?  98  PRO   A CG   1 
ATOM   2327 C CD   A PRO   A 1 98  ? 23.557 -6.572  -6.925  0.40 11.78 ?  98  PRO   A CD   1 
ATOM   2328 C CD   B PRO   A 1 98  ? 23.699 -6.676  -7.002  0.60 12.08 ?  98  PRO   A CD   1 
ATOM   2329 H HA   A PRO   A 1 98  ? 24.658 -4.125  -8.494  0.40 14.08 ?  98  PRO   A HA   1 
ATOM   2330 H HA   B PRO   A 1 98  ? 24.819 -4.281  -8.626  0.60 15.13 ?  98  PRO   A HA   1 
ATOM   2331 H HB2  A PRO   A 1 98  ? 22.874 -5.436  -9.843  0.40 14.48 ?  98  PRO   A HB2  1 
ATOM   2332 H HB2  B PRO   A 1 98  ? 23.089 -5.654  -9.978  0.60 15.29 ?  98  PRO   A HB2  1 
ATOM   2333 H HB3  A PRO   A 1 98  ? 24.316 -6.054  -9.543  0.40 14.48 ?  98  PRO   A HB3  1 
ATOM   2334 H HB3  B PRO   A 1 98  ? 24.518 -6.261  -9.602  0.60 15.29 ?  98  PRO   A HB3  1 
ATOM   2335 H HG2  A PRO   A 1 98  ? 21.921 -6.557  -8.172  0.40 15.06 ?  98  PRO   A HG2  1 
ATOM   2336 H HG2  B PRO   A 1 98  ? 22.078 -6.689  -8.275  0.60 16.15 ?  98  PRO   A HG2  1 
ATOM   2337 H HG3  A PRO   A 1 98  ? 23.027 -7.620  -8.611  0.40 15.06 ?  98  PRO   A HG3  1 
ATOM   2338 H HG3  B PRO   A 1 98  ? 23.174 -7.786  -8.657  0.60 16.15 ?  98  PRO   A HG3  1 
ATOM   2339 H HD2  A PRO   A 1 98  ? 22.942 -6.775  -6.200  0.40 14.19 ?  98  PRO   A HD2  1 
ATOM   2340 H HD2  B PRO   A 1 98  ? 23.079 -6.869  -6.277  0.60 14.55 ?  98  PRO   A HD2  1 
ATOM   2341 H HD3  A PRO   A 1 98  ? 24.354 -7.119  -6.882  0.40 14.19 ?  98  PRO   A HD3  1 
ATOM   2342 H HD3  B PRO   A 1 98  ? 24.500 -7.220  -6.936  0.60 14.55 ?  98  PRO   A HD3  1 
ATOM   2343 N N    A ASN   A 1 99  ? 23.004 -2.370  -8.927  0.40 12.06 ?  99  ASN   A N    1 
ATOM   2344 N N    B ASN   A 1 99  ? 23.108 -2.620  -9.277  0.60 14.17 ?  99  ASN   A N    1 
ATOM   2345 C CA   A ASN   A 1 99  ? 22.031 -1.313  -9.160  0.40 12.90 ?  99  ASN   A CA   1 
ATOM   2346 C CA   B ASN   A 1 99  ? 22.131 -1.572  -9.541  0.60 15.65 ?  99  ASN   A CA   1 
ATOM   2347 C C    A ASN   A 1 99  ? 21.510 -1.466  -10.584 0.40 13.92 ?  99  ASN   A C    1 
ATOM   2348 C C    B ASN   A 1 99  ? 21.493 -1.865  -10.892 0.60 17.07 ?  99  ASN   A C    1 
ATOM   2349 O O    A ASN   A 1 99  ? 22.213 -1.142  -11.550 0.40 13.97 ?  99  ASN   A O    1 
ATOM   2350 O O    B ASN   A 1 99  ? 22.151 -1.771  -11.933 0.60 17.31 ?  99  ASN   A O    1 
ATOM   2351 C CB   A ASN   A 1 99  ? 22.670 0.058   -8.959  0.40 12.62 ?  99  ASN   A CB   1 
ATOM   2352 C CB   B ASN   A 1 99  ? 22.805 -0.205  -9.538  0.60 16.71 ?  99  ASN   A CB   1 
ATOM   2353 C CG   A ASN   A 1 99  ? 21.648 1.183   -8.938  0.40 12.93 ?  99  ASN   A CG   1 
ATOM   2354 C CG   B ASN   A 1 99  ? 21.812 0.938   -9.639  0.60 18.18 ?  99  ASN   A CG   1 
ATOM   2355 O OD1  A ASN   A 1 99  ? 20.624 1.116   -9.614  0.40 13.83 ?  99  ASN   A OD1  1 
ATOM   2356 O OD1  B ASN   A 1 99  ? 20.787 0.826   -10.309 0.60 18.90 ?  99  ASN   A OD1  1 
ATOM   2357 N ND2  A ASN   A 1 99  ? 21.925 2.223   -8.159  0.40 13.15 ?  99  ASN   A ND2  1 
ATOM   2358 N ND2  B ASN   A 1 99  ? 22.118 2.049   -8.973  0.60 18.97 ?  99  ASN   A ND2  1 
ATOM   2359 H H    A ASN   A 1 99  ? 23.777 -2.196  -9.260  0.40 14.52 ?  99  ASN   A H    1 
ATOM   2360 H H    B ASN   A 1 99  ? 23.861 -2.495  -9.671  0.60 17.06 ?  99  ASN   A H    1 
ATOM   2361 H HA   A ASN   A 1 99  ? 21.286 -1.401  -8.543  0.40 15.54 ?  99  ASN   A HA   1 
ATOM   2362 H HA   B ASN   A 1 99  ? 21.440 -1.583  -8.856  0.60 18.83 ?  99  ASN   A HA   1 
ATOM   2363 H HB2  A ASN   A 1 99  ? 23.141 0.071   -8.115  0.40 15.20 ?  99  ASN   A HB2  1 
ATOM   2364 H HB2  B ASN   A 1 99  ? 23.309 -0.096  -8.718  0.60 20.11 ?  99  ASN   A HB2  1 
ATOM   2365 H HB3  A ASN   A 1 99  ? 23.287 0.231   -9.690  0.40 15.20 ?  99  ASN   A HB3  1 
ATOM   2366 H HB3  B ASN   A 1 99  ? 23.390 -0.150  -10.305 0.60 20.11 ?  99  ASN   A HB3  1 
ATOM   2367 H HD21 A ASN   A 1 99  ? 21.378 2.888   -8.116  0.40 15.83 ?  99  ASN   A HD21 1 
ATOM   2368 H HD21 B ASN   A 1 99  ? 21.589 2.726   -8.988  0.60 22.82 ?  99  ASN   A HD21 1 
ATOM   2369 H HD22 A ASN   A 1 99  ? 22.651 2.235   -7.702  0.40 15.83 ?  99  ASN   A HD22 1 
ATOM   2370 H HD22 B ASN   A 1 99  ? 22.850 2.086   -8.517  0.60 22.82 ?  99  ASN   A HD22 1 
ATOM   2371 N N    A VAL   A 1 100 ? 20.273 -1.961  -10.705 0.40 15.38 ?  100 VAL   A N    1 
ATOM   2372 N N    B VAL   A 1 100 ? 20.208 -2.222  -10.865 0.60 19.31 ?  100 VAL   A N    1 
ATOM   2373 C CA   A VAL   A 1 100 ? 19.663 -2.179  -12.015 0.40 17.32 ?  100 VAL   A CA   1 
ATOM   2374 C CA   B VAL   A 1 100 ? 19.506 -2.608  -12.084 0.60 22.19 ?  100 VAL   A CA   1 
ATOM   2375 C C    A VAL   A 1 100 ? 19.579 -0.877  -12.800 0.40 17.55 ?  100 VAL   A C    1 
ATOM   2376 C C    B VAL   A 1 100 ? 19.402 -1.432  -13.046 0.60 23.56 ?  100 VAL   A C    1 
ATOM   2377 O O    A VAL   A 1 100 ? 19.666 -0.877  -14.034 0.40 18.25 ?  100 VAL   A O    1 
ATOM   2378 O O    B VAL   A 1 100 ? 19.463 -1.607  -14.269 0.60 23.77 ?  100 VAL   A O    1 
ATOM   2379 C CB   A VAL   A 1 100 ? 18.280 -2.847  -11.847 0.40 19.41 ?  100 VAL   A CB   1 
ATOM   2380 C CB   B VAL   A 1 100 ? 18.126 -3.191  -11.733 0.60 23.82 ?  100 VAL   A CB   1 
ATOM   2381 C CG1  A VAL   A 1 100 ? 17.628 -3.094  -13.200 0.40 20.23 ?  100 VAL   A CG1  1 
ATOM   2382 C CG1  B VAL   A 1 100 ? 17.217 -3.193  -12.950 0.60 24.74 ?  100 VAL   A CG1  1 
ATOM   2383 C CG2  A VAL   A 1 100 ? 18.409 -4.152  -11.071 0.40 19.97 ?  100 VAL   A CG2  1 
ATOM   2384 C CG2  B VAL   A 1 100 ? 18.281 -4.594  -11.170 0.60 24.21 ?  100 VAL   A CG2  1 
ATOM   2385 H H    A VAL   A 1 100 ? 19.767 -2.181  -10.038 0.40 18.51 ?  100 VAL   A H    1 
ATOM   2386 H H    B VAL   A 1 100 ? 19.724 -2.250  -10.151 0.60 23.23 ?  100 VAL   A H    1 
ATOM   2387 H HA   A VAL   A 1 100 ? 20.219 -2.796  -12.514 0.40 20.84 ?  100 VAL   A HA   1 
ATOM   2388 H HA   B VAL   A 1 100 ? 20.015 -3.305  -12.524 0.60 26.69 ?  100 VAL   A HA   1 
ATOM   2389 H HB   A VAL   A 1 100 ? 17.701 -2.258  -11.340 0.40 23.35 ?  100 VAL   A HB   1 
ATOM   2390 H HB   B VAL   A 1 100 ? 17.715 -2.637  -11.051 0.60 28.64 ?  100 VAL   A HB   1 
ATOM   2391 H HG11 A VAL   A 1 100 ? 16.841 -3.650  -13.074 0.40 24.33 ?  100 VAL   A HG11 1 
ATOM   2392 H HG11 B VAL   A 1 100 ? 16.474 -3.793  -12.782 0.60 29.74 ?  100 VAL   A HG11 1 
ATOM   2393 H HG12 A VAL   A 1 100 ? 17.371 -2.245  -13.588 0.40 24.33 ?  100 VAL   A HG12 1 
ATOM   2394 H HG12 B VAL   A 1 100 ? 16.884 -2.294  -13.102 0.60 29.74 ?  100 VAL   A HG12 1 
ATOM   2395 H HG13 A VAL   A 1 100 ? 18.261 -3.548  -13.777 0.40 24.33 ?  100 VAL   A HG13 1 
ATOM   2396 H HG13 B VAL   A 1 100 ? 17.720 -3.498  -13.720 0.60 29.74 ?  100 VAL   A HG13 1 
ATOM   2397 H HG21 A VAL   A 1 100 ? 17.556 -4.616  -11.087 0.40 24.02 ?  100 VAL   A HG21 1 
ATOM   2398 H HG21 B VAL   A 1 100 ? 17.405 -4.939  -10.942 0.60 29.10 ?  100 VAL   A HG21 1 
ATOM   2399 H HG22 A VAL   A 1 100 ? 19.090 -4.702  -11.489 0.40 24.02 ?  100 VAL   A HG22 1 
ATOM   2400 H HG22 B VAL   A 1 100 ? 18.696 -5.157  -11.842 0.60 29.10 ?  100 VAL   A HG22 1 
ATOM   2401 H HG23 A VAL   A 1 100 ? 18.659 -3.954  -10.155 0.40 24.02 ?  100 VAL   A HG23 1 
ATOM   2402 H HG23 B VAL   A 1 100 ? 18.841 -4.555  -10.379 0.60 29.10 ?  100 VAL   A HG23 1 
ATOM   2403 N N    A ASN   A 1 101 ? 19.400 0.247   -12.111 0.40 17.33 ?  101 ASN   A N    1 
ATOM   2404 N N    B ASN   A 1 101 ? 19.227 -0.219  -12.516 0.60 24.79 ?  101 ASN   A N    1 
ATOM   2405 C CA   A ASN   A 1 101 ? 19.340 1.533   -12.794 0.40 17.98 ?  101 ASN   A CA   1 
ATOM   2406 C CA   B ASN   A 1 101 ? 19.125 0.949   -13.385 0.60 26.08 ?  101 ASN   A CA   1 
ATOM   2407 C C    A ASN   A 1 101 ? 20.691 1.964   -13.360 0.40 19.53 ?  101 ASN   A C    1 
ATOM   2408 C C    B ASN   A 1 101 ? 20.434 1.222   -14.115 0.60 27.17 ?  101 ASN   A C    1 
ATOM   2409 O O    A ASN   A 1 101 ? 20.751 2.981   -14.063 0.40 20.09 ?  101 ASN   A O    1 
ATOM   2410 O O    B ASN   A 1 101 ? 20.419 1.750   -15.233 0.60 27.60 ?  101 ASN   A O    1 
ATOM   2411 C CB   A ASN   A 1 101 ? 18.756 2.586   -11.853 0.40 17.25 ?  101 ASN   A CB   1 
ATOM   2412 C CB   B ASN   A 1 101 ? 18.688 2.172   -12.580 0.60 26.31 ?  101 ASN   A CB   1 
ATOM   2413 C CG   A ASN   A 1 101 ? 17.417 2.158   -11.260 0.40 16.71 ?  101 ASN   A CG   1 
ATOM   2414 C CG   B ASN   A 1 101 ? 17.344 1.975   -11.909 0.60 26.54 ?  101 ASN   A CG   1 
ATOM   2415 O OD1  A ASN   A 1 101 ? 16.568 1.576   -11.943 0.40 17.14 ?  101 ASN   A OD1  1 
ATOM   2416 O OD1  B ASN   A 1 101 ? 16.335 1.761   -12.577 0.60 26.49 ?  101 ASN   A OD1  1 
ATOM   2417 N ND2  A ASN   A 1 101 ? 17.231 2.432   -9.976  0.40 16.66 ?  101 ASN   A ND2  1 
ATOM   2418 N ND2  B ASN   A 1 101 ? 17.323 2.053   -10.584 0.60 26.66 ?  101 ASN   A ND2  1 
ATOM   2419 H H    A ASN   A 1 101 ? 19.300 0.286   -11.260 0.40 20.85 ?  101 ASN   A H    1 
ATOM   2420 H H    B ASN   A 1 101 ? 19.156 -0.052  -11.674 0.60 29.80 ?  101 ASN   A H    1 
ATOM   2421 H HA   A ASN   A 1 101 ? 18.734 1.450   -13.543 0.40 21.63 ?  101 ASN   A HA   1 
ATOM   2422 H HA   B ASN   A 1 101 ? 18.442 0.777   -14.052 0.60 31.35 ?  101 ASN   A HA   1 
ATOM   2423 H HB2  A ASN   A 1 101 ? 19.375 2.742   -11.122 0.40 20.76 ?  101 ASN   A HB2  1 
ATOM   2424 H HB2  B ASN   A 1 101 ? 19.340 2.352   -11.889 0.60 31.63 ?  101 ASN   A HB2  1 
ATOM   2425 H HB3  A ASN   A 1 101 ? 18.620 3.412   -12.350 0.40 20.76 ?  101 ASN   A HB3  1 
ATOM   2426 H HB3  B ASN   A 1 101 ? 18.613 2.935   -13.177 0.60 31.63 ?  101 ASN   A HB3  1 
ATOM   2427 H HD21 A ASN   A 1 101 ? 16.491 2.218   -9.599  0.40 20.05 ?  101 ASN   A HD21 1 
ATOM   2428 H HD21 B ASN   A 1 101 ? 16.582 1.950   -10.157 0.60 32.05 ?  101 ASN   A HD21 1 
ATOM   2429 H HD22 A ASN   A 1 101 ? 17.843 2.838   -9.528  0.40 20.05 ?  101 ASN   A HD22 1 
ATOM   2430 H HD22 B ASN   A 1 101 ? 18.049 2.204   -10.152 0.60 32.05 ?  101 ASN   A HD22 1 
ATOM   2431 N N    A LYS   A 1 102 ? 21.760 1.213   -13.086 0.40 21.00 ?  102 LYS   A N    1 
ATOM   2432 N N    B LYS   A 1 102 ? 21.569 0.886   -13.501 0.60 28.00 ?  102 LYS   A N    1 
ATOM   2433 C CA   A LYS   A 1 102 ? 23.048 1.399   -13.741 0.40 22.26 ?  102 LYS   A CA   1 
ATOM   2434 C CA   B LYS   A 1 102 ? 22.859 0.955   -14.175 0.60 28.18 ?  102 LYS   A CA   1 
ATOM   2435 C C    A LYS   A 1 102 ? 23.354 0.309   -14.759 0.40 22.93 ?  102 LYS   A C    1 
ATOM   2436 C C    B LYS   A 1 102 ? 23.100 -0.231  -15.099 0.60 27.10 ?  102 LYS   A C    1 
ATOM   2437 O O    A LYS   A 1 102 ? 24.447 0.313   -15.336 0.40 23.49 ?  102 LYS   A O    1 
ATOM   2438 O O    B LYS   A 1 102 ? 24.182 -0.327  -15.688 0.60 27.12 ?  102 LYS   A O    1 
ATOM   2439 C CB   A LYS   A 1 102 ? 24.179 1.451   -12.705 0.40 23.10 ?  102 LYS   A CB   1 
ATOM   2440 C CB   B LYS   A 1 102 ? 23.998 0.996   -13.152 0.60 29.74 ?  102 LYS   A CB   1 
ATOM   2441 C CG   A LYS   A 1 102 ? 24.056 2.571   -11.686 0.40 23.94 ?  102 LYS   A CG   1 
ATOM   2442 C CG   B LYS   A 1 102 ? 24.003 2.206   -12.234 0.60 31.15 ?  102 LYS   A CG   1 
ATOM   2443 C CD   A LYS   A 1 102 ? 25.222 2.545   -10.708 0.40 24.80 ?  102 LYS   A CD   1 
ATOM   2444 C CD   B LYS   A 1 102 ? 25.080 2.069   -11.163 0.60 32.62 ?  102 LYS   A CD   1 
ATOM   2445 C CE   A LYS   A 1 102 ? 25.132 3.674   -9.690  0.40 25.44 ?  102 LYS   A CE   1 
ATOM   2446 C CE   B LYS   A 1 102 ? 24.978 3.168   -10.118 0.60 33.75 ?  102 LYS   A CE   1 
ATOM   2447 N NZ   A LYS   A 1 102 ? 26.254 3.619   -8.708  0.40 25.69 ?  102 LYS   A NZ   1 
ATOM   2448 N NZ   B LYS   A 1 102 ? 25.511 2.727   -8.794  0.60 34.36 ?  102 LYS   A NZ   1 
ATOM   2449 H H    A LYS   A 1 102 ? 21.761 0.572   -12.512 0.40 25.26 ?  102 LYS   A H    1 
ATOM   2450 H H    B LYS   A 1 102 ? 21.613 0.619   -12.684 0.60 33.66 ?  102 LYS   A H    1 
ATOM   2451 H HA   A LYS   A 1 102 ? 23.041 2.241   -14.215 0.40 26.77 ?  102 LYS   A HA   1 
ATOM   2452 H HA   B LYS   A 1 102 ? 22.892 1.777   -14.695 0.60 33.87 ?  102 LYS   A HA   1 
ATOM   2453 H HB2  A LYS   A 1 102 ? 24.194 0.611   -12.219 0.40 27.78 ?  102 LYS   A HB2  1 
ATOM   2454 H HB2  B LYS   A 1 102 ? 23.936 0.205   -12.594 0.60 35.74 ?  102 LYS   A HB2  1 
ATOM   2455 H HB3  A LYS   A 1 102 ? 25.020 1.570   -13.173 0.40 27.78 ?  102 LYS   A HB3  1 
ATOM   2456 H HB3  B LYS   A 1 102 ? 24.840 0.990   -13.633 0.60 35.74 ?  102 LYS   A HB3  1 
ATOM   2457 H HG2  A LYS   A 1 102 ? 24.061 3.426   -12.144 0.40 28.79 ?  102 LYS   A HG2  1 
ATOM   2458 H HG2  B LYS   A 1 102 ? 24.188 3.004   -12.753 0.60 37.44 ?  102 LYS   A HG2  1 
ATOM   2459 H HG3  A LYS   A 1 102 ? 23.233 2.461   -11.184 0.40 28.79 ?  102 LYS   A HG3  1 
ATOM   2460 H HG3  B LYS   A 1 102 ? 23.142 2.281   -11.794 0.60 37.44 ?  102 LYS   A HG3  1 
ATOM   2461 H HD2  A LYS   A 1 102 ? 25.217 1.701   -10.228 0.40 29.82 ?  102 LYS   A HD2  1 
ATOM   2462 H HD2  B LYS   A 1 102 ? 24.988 1.213   -10.717 0.60 39.20 ?  102 LYS   A HD2  1 
ATOM   2463 H HD3  A LYS   A 1 102 ? 26.053 2.645   -11.200 0.40 29.82 ?  102 LYS   A HD3  1 
ATOM   2464 H HD3  B LYS   A 1 102 ? 25.952 2.131   -11.583 0.60 39.20 ?  102 LYS   A HD3  1 
ATOM   2465 H HE2  A LYS   A 1 102 ? 25.173 4.526   -10.153 0.40 30.58 ?  102 LYS   A HE2  1 
ATOM   2466 H HE2  B LYS   A 1 102 ? 25.495 3.934   -10.413 0.60 40.55 ?  102 LYS   A HE2  1 
ATOM   2467 H HE3  A LYS   A 1 102 ? 24.295 3.598   -9.203  0.40 30.58 ?  102 LYS   A HE3  1 
ATOM   2468 H HE3  B LYS   A 1 102 ? 24.048 3.417   -10.005 0.60 40.55 ?  102 LYS   A HE3  1 
ATOM   2469 H HZ1  A LYS   A 1 102 ? 26.180 4.286   -8.125  0.40 30.89 ?  102 LYS   A HZ1  1 
ATOM   2470 H HZ1  B LYS   A 1 102 ? 25.440 3.388   -8.202  0.60 41.28 ?  102 LYS   A HZ1  1 
ATOM   2471 H HZ2  A LYS   A 1 102 ? 26.233 2.845   -8.269  0.40 30.89 ?  102 LYS   A HZ2  1 
ATOM   2472 H HZ2  B LYS   A 1 102 ? 25.051 2.024   -8.500  0.60 41.28 ?  102 LYS   A HZ2  1 
ATOM   2473 H HZ3  A LYS   A 1 102 ? 27.032 3.689   -9.134  0.40 30.89 ?  102 LYS   A HZ3  1 
ATOM   2474 H HZ3  B LYS   A 1 102 ? 26.368 2.499   -8.872  0.60 41.28 ?  102 LYS   A HZ3  1 
ATOM   2475 N N    A GLY   A 1 103 ? 22.429 -0.620  -14.995 0.40 23.36 ?  103 GLY   A N    1 
ATOM   2476 N N    B GLY   A 1 103 ? 22.145 -1.151  -15.215 0.60 26.14 ?  103 GLY   A N    1 
ATOM   2477 C CA   A GLY   A 1 103 ? 22.684 -1.711  -15.916 0.40 23.55 ?  103 GLY   A CA   1 
ATOM   2478 C CA   B GLY   A 1 103 ? 22.327 -2.320  -16.050 0.60 25.13 ?  103 GLY   A CA   1 
ATOM   2479 C C    A GLY   A 1 103 ? 23.581 -2.798  -15.371 0.40 23.96 ?  103 GLY   A C    1 
ATOM   2480 C C    B GLY   A 1 103 ? 23.196 -3.404  -15.450 0.60 24.35 ?  103 GLY   A C    1 
ATOM   2481 O O    A GLY   A 1 103 ? 24.274 -3.463  -16.148 0.40 24.33 ?  103 GLY   A O    1 
ATOM   2482 O O    B GLY   A 1 103 ? 23.610 -4.318  -16.174 0.60 24.96 ?  103 GLY   A O    1 
ATOM   2483 H H    A GLY   A 1 103 ? 21.647 -0.643  -14.637 0.40 28.09 ?  103 GLY   A H    1 
ATOM   2484 H H    B GLY   A 1 103 ? 21.384 -1.121  -14.809 0.60 31.42 ?  103 GLY   A H    1 
ATOM   2485 H HA2  A GLY   A 1 103 ? 21.837 -2.107  -16.184 0.40 28.31 ?  103 GLY   A HA2  1 
ATOM   2486 H HA2  B GLY   A 1 103 ? 21.458 -2.698  -16.249 0.60 30.22 ?  103 GLY   A HA2  1 
ATOM   2487 H HA3  A GLY   A 1 103 ? 23.116 -1.365  -16.710 0.40 28.31 ?  103 GLY   A HA3  1 
ATOM   2488 H HA3  B GLY   A 1 103 ? 22.729 -2.039  -16.890 0.60 30.22 ?  103 GLY   A HA3  1 
ATOM   2489 N N    A GLU   A 1 104 ? 23.594 -3.001  -14.057 0.40 23.52 ?  104 GLU   A N    1 
ATOM   2490 N N    B GLU   A 1 104 ? 23.491 -3.336  -14.156 0.60 22.80 ?  104 GLU   A N    1 
ATOM   2491 C CA   A GLU   A 1 104 ? 24.464 -3.990  -13.440 0.40 23.08 ?  104 GLU   A CA   1 
ATOM   2492 C CA   B GLU   A 1 104 ? 24.386 -4.310  -13.548 0.60 21.46 ?  104 GLU   A CA   1 
ATOM   2493 C C    A GLU   A 1 104 ? 23.770 -5.346  -13.325 0.40 23.83 ?  104 GLU   A C    1 
ATOM   2494 C C    B GLU   A 1 104 ? 23.692 -5.661  -13.373 0.60 21.58 ?  104 GLU   A C    1 
ATOM   2495 O O    A GLU   A 1 104 ? 22.553 -5.434  -13.136 0.40 24.14 ?  104 GLU   A O    1 
ATOM   2496 O O    B GLU   A 1 104 ? 22.476 -5.746  -13.178 0.60 22.15 ?  104 GLU   A O    1 
ATOM   2497 C CB   A GLU   A 1 104 ? 24.945 -3.490  -12.075 0.40 21.99 ?  104 GLU   A CB   1 
ATOM   2498 C CB   B GLU   A 1 104 ? 24.930 -3.770  -12.220 0.60 20.33 ?  104 GLU   A CB   1 
ATOM   2499 C CG   A GLU   A 1 104 ? 25.864 -2.272  -12.201 0.40 21.28 ?  104 GLU   A CG   1 
ATOM   2500 C CG   B GLU   A 1 104 ? 25.788 -2.516  -12.417 0.60 19.76 ?  104 GLU   A CG   1 
ATOM   2501 C CD   A GLU   A 1 104 ? 26.164 -1.579  -10.878 0.40 20.64 ?  104 GLU   A CD   1 
ATOM   2502 C CD   B GLU   A 1 104 ? 26.233 -1.817  -11.144 0.60 18.73 ?  104 GLU   A CD   1 
ATOM   2503 O OE1  A GLU   A 1 104 ? 25.514 -1.898  -9.862  0.40 19.74 ?  104 GLU   A OE1  1 
ATOM   2504 O OE1  B GLU   A 1 104 ? 25.734 -2.132  -10.046 0.60 17.83 ?  104 GLU   A OE1  1 
ATOM   2505 O OE2  A GLU   A 1 104 ? 27.057 -0.703  -10.860 0.40 21.27 -1 104 GLU   A OE2  1 
ATOM   2506 O OE2  B GLU   A 1 104 ? 27.091 -0.913  -11.267 0.60 19.07 -1 104 GLU   A OE2  1 
ATOM   2507 H H    A GLU   A 1 104 ? 23.111 -2.565  -13.492 0.40 28.28 ?  104 GLU   A H    1 
ATOM   2508 H H    B GLU   A 1 104 ? 23.196 -2.730  -13.621 0.60 27.42 ?  104 GLU   A H    1 
ATOM   2509 H HA   A GLU   A 1 104 ? 25.243 -4.109  -14.001 0.40 27.75 ?  104 GLU   A HA   1 
ATOM   2510 H HA   B GLU   A 1 104 ? 25.141 -4.439  -14.145 0.60 25.80 ?  104 GLU   A HA   1 
ATOM   2511 H HB2  A GLU   A 1 104 ? 24.175 -3.235  -11.542 0.40 26.45 ?  104 GLU   A HB2  1 
ATOM   2512 H HB2  B GLU   A 1 104 ? 24.186 -3.543  -11.646 0.60 24.46 ?  104 GLU   A HB2  1 
ATOM   2513 H HB3  A GLU   A 1 104 ? 25.438 -4.198  -11.633 0.40 26.45 ?  104 GLU   A HB3  1 
ATOM   2514 H HB3  B GLU   A 1 104 ? 25.479 -4.454  -11.811 0.60 24.46 ?  104 GLU   A HB3  1 
ATOM   2515 H HG2  A GLU   A 1 104 ? 26.709 -2.561  -12.579 0.40 25.60 ?  104 GLU   A HG2  1 
ATOM   2516 H HG2  B GLU   A 1 104 ? 26.586 -2.761  -12.907 0.60 23.77 ?  104 GLU   A HG2  1 
ATOM   2517 H HG3  A GLU   A 1 104 ? 25.445 -1.629  -12.799 0.40 25.60 ?  104 GLU   A HG3  1 
ATOM   2518 H HG3  B GLU   A 1 104 ? 25.276 -1.865  -12.918 0.60 23.77 ?  104 GLU   A HG3  1 
ATOM   2519 N N    A ASP   A 1 105 ? 24.571 -6.404  -13.442 0.40 24.62 ?  105 ASP   A N    1 
ATOM   2520 N N    B ASP   A 1 105 ? 24.492 -6.723  -13.446 0.60 21.61 ?  105 ASP   A N    1 
ATOM   2521 C CA   A ASP   A 1 105 ? 24.058 -7.763  -13.568 0.40 25.52 ?  105 ASP   A CA   1 
ATOM   2522 C CA   B ASP   A 1 105 ? 23.982 -8.088  -13.531 0.60 22.20 ?  105 ASP   A CA   1 
ATOM   2523 C C    A ASP   A 1 105 ? 23.368 -8.206  -12.281 0.40 24.66 ?  105 ASP   A C    1 
ATOM   2524 C C    B ASP   A 1 105 ? 23.314 -8.493  -12.221 0.60 20.24 ?  105 ASP   A C    1 
ATOM   2525 O O    A ASP   A 1 105 ? 23.966 -8.171  -11.202 0.40 24.00 ?  105 ASP   A O    1 
ATOM   2526 O O    B ASP   A 1 105 ? 23.978 -8.601  -11.188 0.60 18.09 ?  105 ASP   A O    1 
ATOM   2527 C CB   A ASP   A 1 105 ? 25.222 -8.703  -13.883 0.40 27.22 ?  105 ASP   A CB   1 
ATOM   2528 C CB   B ASP   A 1 105 ? 25.148 -9.022  -13.849 0.60 24.91 ?  105 ASP   A CB   1 
ATOM   2529 C CG   A ASP   A 1 105 ? 24.762 -10.098 -14.243 0.40 28.66 ?  105 ASP   A CG   1 
ATOM   2530 C CG   B ASP   A 1 105 ? 24.772 -10.492 -13.776 0.60 27.18 ?  105 ASP   A CG   1 
ATOM   2531 O OD1  A ASP   A 1 105 ? 23.538 -10.297 -14.391 0.40 29.10 ?  105 ASP   A OD1  1 
ATOM   2532 O OD1  B ASP   A 1 105 ? 23.569 -10.822 -13.872 0.60 27.38 ?  105 ASP   A OD1  1 
ATOM   2533 O OD2  A ASP   A 1 105 ? 25.624 -10.991 -14.388 0.40 29.38 -1 105 ASP   A OD2  1 
ATOM   2534 O OD2  B ASP   A 1 105 ? 25.695 -11.321 -13.611 0.60 28.83 -1 105 ASP   A OD2  1 
ATOM   2535 H H    A ASP   A 1 105 ? 25.427 -6.360  -13.449 0.40 29.60 ?  105 ASP   A H    1 
ATOM   2536 H H    B ASP   A 1 105 ? 25.349 -6.667  -13.441 0.60 25.99 ?  105 ASP   A H    1 
ATOM   2537 H HA   A ASP   A 1 105 ? 23.421 -7.816  -14.297 0.40 30.68 ?  105 ASP   A HA   1 
ATOM   2538 H HA   B ASP   A 1 105 ? 23.329 -8.146  -14.241 0.60 26.70 ?  105 ASP   A HA   1 
ATOM   2539 H HB2  A ASP   A 1 105 ? 25.712 -8.361  -14.648 0.40 32.72 ?  105 ASP   A HB2  1 
ATOM   2540 H HB2  B ASP   A 1 105 ? 25.463 -8.830  -14.748 0.60 29.95 ?  105 ASP   A HB2  1 
ATOM   2541 H HB3  A ASP   A 1 105 ? 25.813 -8.749  -13.110 0.40 32.72 ?  105 ASP   A HB3  1 
ATOM   2542 H HB3  B ASP   A 1 105 ? 25.863 -8.860  -13.211 0.60 29.95 ?  105 ASP   A HB3  1 
ATOM   2543 N N    A ILE   A 1 106 ? 22.110 -8.644  -12.400 0.40 24.35 ?  106 ILE   A N    1 
ATOM   2544 N N    B ILE   A 1 106 ? 22.000 -8.730  -12.265 0.60 20.62 ?  106 ILE   A N    1 
ATOM   2545 C CA   A ILE   A 1 106 ? 21.348 -9.056  -11.225 0.40 23.72 ?  106 ILE   A CA   1 
ATOM   2546 C CA   B ILE   A 1 106 ? 21.269 -9.101  -11.059 0.60 20.44 ?  106 ILE   A CA   1 
ATOM   2547 C C    A ILE   A 1 106 ? 21.885 -10.350 -10.626 0.40 22.72 ?  106 ILE   A C    1 
ATOM   2548 C C    B ILE   A 1 106 ? 21.814 -10.379 -10.444 0.60 19.33 ?  106 ILE   A C    1 
ATOM   2549 O O    A ILE   A 1 106 ? 21.643 -10.628 -9.446  0.40 21.90 ?  106 ILE   A O    1 
ATOM   2550 O O    B ILE   A 1 106 ? 21.639 -10.608 -9.244  0.60 18.47 ?  106 ILE   A O    1 
ATOM   2551 C CB   A ILE   A 1 106 ? 19.841 -9.152  -11.548 0.40 24.36 ?  106 ILE   A CB   1 
ATOM   2552 C CB   B ILE   A 1 106 ? 19.749 -9.184  -11.341 0.60 21.78 ?  106 ILE   A CB   1 
ATOM   2553 C CG1  A ILE   A 1 106 ? 19.008 -9.204  -10.263 0.40 24.66 ?  106 ILE   A CG1  1 
ATOM   2554 C CG1  B ILE   A 1 106 ? 18.954 -9.250  -10.033 0.60 22.61 ?  106 ILE   A CG1  1 
ATOM   2555 C CG2  A ILE   A 1 106 ? 19.549 -10.373 -12.406 0.40 24.68 ?  106 ILE   A CG2  1 
ATOM   2556 C CG2  B ILE   A 1 106 ? 19.428 -10.389 -12.207 0.60 22.45 ?  106 ILE   A CG2  1 
ATOM   2557 C CD1  A ILE   A 1 106 ? 19.131 -7.961  -9.403  0.40 24.69 ?  106 ILE   A CD1  1 
ATOM   2558 C CD1  B ILE   A 1 106 ? 19.131 -8.037  -9.143  0.60 22.91 ?  106 ILE   A CD1  1 
ATOM   2559 H H    A ILE   A 1 106 ? 21.680 -8.709  -13.140 0.40 29.28 ?  106 ILE   A H    1 
ATOM   2560 H H    B ILE   A 1 106 ? 21.522 -8.671  -12.970 0.60 24.80 ?  106 ILE   A H    1 
ATOM   2561 H HA   A ILE   A 1 106 ? 21.454 -8.372  -10.551 0.40 28.52 ?  106 ILE   A HA   1 
ATOM   2562 H HA   B ILE   A 1 106 ? 21.405 -8.406  -10.403 0.60 24.59 ?  106 ILE   A HA   1 
ATOM   2563 H HB   A ILE   A 1 106 ? 19.583 -8.361  -12.045 0.40 29.28 ?  106 ILE   A HB   1 
ATOM   2564 H HB   B ILE   A 1 106 ? 19.484 -8.382  -11.819 0.60 26.19 ?  106 ILE   A HB   1 
ATOM   2565 H HG12 A ILE   A 1 106 ? 18.072 -9.305  -10.500 0.40 29.65 ?  106 ILE   A HG12 1 
ATOM   2566 H HG12 B ILE   A 1 106 ? 18.011 -9.323  -10.244 0.60 27.19 ?  106 ILE   A HG12 1 
ATOM   2567 H HG13 A ILE   A 1 106 ? 19.294 -9.962  -9.731  0.40 29.65 ?  106 ILE   A HG13 1 
ATOM   2568 H HG13 B ILE   A 1 106 ? 19.239 -10.029 -9.531  0.60 27.19 ?  106 ILE   A HG13 1 
ATOM   2569 H HG21 A ILE   A 1 106 ? 18.653 -10.294 -12.771 0.40 29.68 ?  106 ILE   A HG21 1 
ATOM   2570 H HG21 B ILE   A 1 106 ? 18.516 -10.310 -12.527 0.60 27.00 ?  106 ILE   A HG21 1 
ATOM   2571 H HG22 A ILE   A 1 106 ? 20.198 -10.412 -13.124 0.40 29.68 ?  106 ILE   A HG22 1 
ATOM   2572 H HG22 B ILE   A 1 106 ? 20.042 -10.407 -12.957 0.60 27.00 ?  106 ILE   A HG22 1 
ATOM   2573 H HG23 A ILE   A 1 106 ? 19.612 -11.169 -11.856 0.40 29.68 ?  106 ILE   A HG23 1 
ATOM   2574 H HG23 B ILE   A 1 106 ? 19.526 -11.194 -11.677 0.60 27.00 ?  106 ILE   A HG23 1 
ATOM   2575 H HD11 A ILE   A 1 106 ? 18.399 -7.944  -8.768  0.40 29.68 ?  106 ILE   A HD11 1 
ATOM   2576 H HD11 B ILE   A 1 106 ? 18.425 -8.029  -8.479  0.60 27.55 ?  106 ILE   A HD11 1 
ATOM   2577 H HD12 A ILE   A 1 106 ? 19.978 -7.985  -8.929  0.40 29.68 ?  106 ILE   A HD12 1 
ATOM   2578 H HD12 B ILE   A 1 106 ? 19.995 -8.088  -8.704  0.60 27.55 ?  106 ILE   A HD12 1 
ATOM   2579 H HD13 A ILE   A 1 106 ? 19.091 -7.177  -9.973  0.40 29.68 ?  106 ILE   A HD13 1 
ATOM   2580 H HD13 B ILE   A 1 106 ? 19.082 -7.236  -9.688  0.60 27.55 ?  106 ILE   A HD13 1 
ATOM   2581 N N    A GLN   A 1 107 ? 22.612 -11.152 -11.407 0.40 22.75 ?  107 GLN   A N    1 
ATOM   2582 N N    B GLN   A 1 107 ? 22.489 -11.220 -11.233 0.60 20.25 ?  107 GLN   A N    1 
ATOM   2583 C CA   A GLN   A 1 107 ? 23.220 -12.365 -10.871 0.40 23.31 ?  107 GLN   A CA   1 
ATOM   2584 C CA   B GLN   A 1 107 ? 23.108 -12.410 -10.667 0.60 22.07 ?  107 GLN   A CA   1 
ATOM   2585 C C    A GLN   A 1 107 ? 24.176 -12.057 -9.726  0.40 20.72 ?  107 GLN   A C    1 
ATOM   2586 C C    B GLN   A 1 107 ? 24.161 -12.052 -9.625  0.60 20.16 ?  107 GLN   A C    1 
ATOM   2587 O O    A GLN   A 1 107 ? 24.393 -12.913 -8.861  0.40 21.51 ?  107 GLN   A O    1 
ATOM   2588 O O    B GLN   A 1 107 ? 24.429 -12.858 -8.725  0.60 20.76 ?  107 GLN   A O    1 
ATOM   2589 C CB   A GLN   A 1 107 ? 23.952 -13.113 -11.990 0.40 26.25 ?  107 GLN   A CB   1 
ATOM   2590 C CB   B GLN   A 1 107 ? 23.687 -13.287 -11.783 0.60 25.77 ?  107 GLN   A CB   1 
ATOM   2591 C CG   A GLN   A 1 107 ? 23.107 -13.339 -13.240 0.40 29.21 ?  107 GLN   A CG   1 
ATOM   2592 C CG   B GLN   A 1 107 ? 22.645 -13.762 -12.793 0.60 29.34 ?  107 GLN   A CG   1 
ATOM   2593 C CD   A GLN   A 1 107 ? 21.832 -14.107 -12.952 0.40 31.64 ?  107 GLN   A CD   1 
ATOM   2594 C CD   B GLN   A 1 107 ? 21.569 -14.628 -12.163 0.60 32.38 ?  107 GLN   A CD   1 
ATOM   2595 O OE1  A GLN   A 1 107 ? 21.863 -15.177 -12.345 0.40 32.66 ?  107 GLN   A OE1  1 
ATOM   2596 O OE1  B GLN   A 1 107 ? 21.828 -15.360 -11.206 0.60 33.45 ?  107 GLN   A OE1  1 
ATOM   2597 N NE2  A GLN   A 1 107 ? 20.701 -13.559 -13.382 0.40 32.34 ?  107 GLN   A NE2  1 
ATOM   2598 N NE2  B GLN   A 1 107 ? 20.352 -14.546 -12.694 0.60 33.48 ?  107 GLN   A NE2  1 
ATOM   2599 H H    A GLN   A 1 107 ? 22.764 -11.012 -12.240 0.40 27.36 ?  107 GLN   A H    1 
ATOM   2600 H H    B GLN   A 1 107 ? 22.601 -11.122 -12.081 0.60 24.36 ?  107 GLN   A H    1 
ATOM   2601 H HA   A GLN   A 1 107 ? 22.526 -12.946 -10.529 0.40 28.03 ?  107 GLN   A HA   1 
ATOM   2602 H HA   B GLN   A 1 107 ? 22.428 -12.931 -10.218 0.60 26.54 ?  107 GLN   A HA   1 
ATOM   2603 H HB2  A GLN   A 1 107 ? 24.733 -12.603 -12.254 0.40 31.56 ?  107 GLN   A HB2  1 
ATOM   2604 H HB2  B GLN   A 1 107 ? 24.356 -12.785 -12.271 0.60 30.99 ?  107 GLN   A HB2  1 
ATOM   2605 H HB3  A GLN   A 1 107 ? 24.223 -13.985 -11.662 0.40 31.56 ?  107 GLN   A HB3  1 
ATOM   2606 H HB3  B GLN   A 1 107 ? 24.089 -14.077 -11.390 0.60 30.99 ?  107 GLN   A HB3  1 
ATOM   2607 H HG2  A GLN   A 1 107 ? 22.861 -12.482 -13.622 0.40 35.11 ?  107 GLN   A HG2  1 
ATOM   2608 H HG2  B GLN   A 1 107 ? 22.211 -12.990 -13.191 0.60 35.27 ?  107 GLN   A HG2  1 
ATOM   2609 H HG3  A GLN   A 1 107 ? 23.624 -13.848 -13.882 0.40 35.11 ?  107 GLN   A HG3  1 
ATOM   2610 H HG3  B GLN   A 1 107 ? 23.082 -14.286 -13.483 0.60 35.27 ?  107 GLN   A HG3  1 
ATOM   2611 H HE21 A GLN   A 1 107 ? 20.718 -12.809 -13.801 0.40 38.87 ?  107 GLN   A HE21 1 
ATOM   2612 H HE21 B GLN   A 1 107 ? 20.208 -14.021 -13.362 0.60 40.23 ?  107 GLN   A HE21 1 
ATOM   2613 H HE22 A GLN   A 1 107 ? 19.951 -13.957 -13.241 0.40 38.87 ?  107 GLN   A HE22 1 
ATOM   2614 H HE22 B GLN   A 1 107 ? 19.707 -15.016 -12.373 0.60 40.23 ?  107 GLN   A HE22 1 
ATOM   2615 N N    . LEU   A 1 108 ? 24.726 -10.842 -9.689  1.00 17.57 ?  108 LEU   A N    1 
ATOM   2616 C CA   . LEU   A 1 108 ? 25.658 -10.428 -8.651  1.00 14.97 ?  108 LEU   A CA   1 
ATOM   2617 C C    . LEU   A 1 108 ? 24.979 -10.257 -7.302  1.00 13.46 ?  108 LEU   A C    1 
ATOM   2618 O O    . LEU   A 1 108 ? 25.674 -10.092 -6.294  1.00 14.00 ?  108 LEU   A O    1 
ATOM   2619 C CB   . LEU   A 1 108 ? 26.369 -9.139  -9.065  1.00 14.92 ?  108 LEU   A CB   1 
ATOM   2620 C CG   . LEU   A 1 108 ? 27.371 -9.333  -10.204 1.00 16.25 ?  108 LEU   A CG   1 
ATOM   2621 C CD1  . LEU   A 1 108 ? 27.836 -8.000  -10.771 1.00 17.18 ?  108 LEU   A CD1  1 
ATOM   2622 C CD2  . LEU   A 1 108 ? 28.565 -10.141 -9.726  1.00 18.18 ?  108 LEU   A CD2  1 
ATOM   2623 H H    A LEU   A 1 108 ? 24.568 -10.235 -10.273 0.40 21.14 ?  108 LEU   A H    1 
ATOM   2624 H H    B LEU   A 1 108 ? 24.585 -10.264 -10.307 0.60 21.14 ?  108 LEU   A H    1 
ATOM   2625 H HA   . LEU   A 1 108 ? 26.330 -11.115 -8.545  1.00 18.02 ?  108 LEU   A HA   1 
ATOM   2626 H HB2  . LEU   A 1 108 ? 25.707 -8.494  -9.364  1.00 17.96 ?  108 LEU   A HB2  1 
ATOM   2627 H HB3  . LEU   A 1 108 ? 26.852 -8.785  -8.304  1.00 17.96 ?  108 LEU   A HB3  1 
ATOM   2628 H HG   . LEU   A 1 108 ? 26.945 -9.828  -10.923 1.00 19.56 ?  108 LEU   A HG   1 
ATOM   2629 H HD11 . LEU   A 1 108 ? 28.440 -8.161  -11.515 1.00 20.67 ?  108 LEU   A HD11 1 
ATOM   2630 H HD12 . LEU   A 1 108 ? 27.063 -7.498  -11.079 1.00 20.67 ?  108 LEU   A HD12 1 
ATOM   2631 H HD13 . LEU   A 1 108 ? 28.296 -7.502  -10.077 1.00 20.67 ?  108 LEU   A HD13 1 
ATOM   2632 H HD21 . LEU   A 1 108 ? 29.267 -10.090 -10.390 1.00 21.87 ?  108 LEU   A HD21 1 
ATOM   2633 H HD22 . LEU   A 1 108 ? 28.874 -9.771  -8.884  1.00 21.87 ?  108 LEU   A HD22 1 
ATOM   2634 H HD23 . LEU   A 1 108 ? 28.290 -11.062 -9.601  1.00 21.87 ?  108 LEU   A HD23 1 
ATOM   2635 N N    . LEU   A 1 109 ? 23.644 -10.297 -7.258  1.00 13.03 ?  109 LEU   A N    1 
ATOM   2636 C CA   . LEU   A 1 109 ? 22.952 -10.181 -5.981  1.00 12.70 ?  109 LEU   A CA   1 
ATOM   2637 C C    . LEU   A 1 109 ? 23.307 -11.340 -5.060  1.00 11.97 ?  109 LEU   A C    1 
ATOM   2638 O O    . LEU   A 1 109 ? 23.440 -11.158 -3.847  1.00 12.15 ?  109 LEU   A O    1 
ATOM   2639 C CB   . LEU   A 1 109 ? 21.439 -10.085 -6.209  1.00 13.24 ?  109 LEU   A CB   1 
ATOM   2640 C CG   . LEU   A 1 109 ? 20.568 -9.828  -4.983  1.00 13.67 ?  109 LEU   A CG   1 
ATOM   2641 C CD1  . LEU   A 1 109 ? 21.021 -8.580  -4.250  1.00 13.98 ?  109 LEU   A CD1  1 
ATOM   2642 C CD2  . LEU   A 1 109 ? 19.102 -9.711  -5.397  1.00 14.77 ?  109 LEU   A CD2  1 
ATOM   2643 H H    . LEU   A 1 109 ? 23.124 -10.389 -7.944  1.00 15.70 ?  109 LEU   A H    1 
ATOM   2644 H HA   . LEU   A 1 109 ? 23.242 -9.363  -5.554  1.00 15.30 ?  109 LEU   A HA   1 
ATOM   2645 H HB2  . LEU   A 1 109 ? 21.272 -9.357  -6.829  1.00 15.95 ?  109 LEU   A HB2  1 
ATOM   2646 H HB3  . LEU   A 1 109 ? 21.138 -10.916 -6.604  1.00 15.95 ?  109 LEU   A HB3  1 
ATOM   2647 H HG   . LEU   A 1 109 ? 20.643 -10.583 -4.377  1.00 16.46 ?  109 LEU   A HG   1 
ATOM   2648 H HD11 . LEU   A 1 109 ? 20.361 -8.347  -3.585  1.00 16.83 ?  109 LEU   A HD11 1 
ATOM   2649 H HD12 . LEU   A 1 109 ? 21.876 -8.760  -3.827  1.00 16.83 ?  109 LEU   A HD12 1 
ATOM   2650 H HD13 . LEU   A 1 109 ? 21.116 -7.859  -4.894  1.00 16.83 ?  109 LEU   A HD13 1 
ATOM   2651 H HD21 . LEU   A 1 109 ? 18.583 -9.395  -4.639  1.00 17.78 ?  109 LEU   A HD21 1 
ATOM   2652 H HD22 . LEU   A 1 109 ? 19.028 -9.082  -6.131  1.00 17.78 ?  109 LEU   A HD22 1 
ATOM   2653 H HD23 . LEU   A 1 109 ? 18.776 -10.583 -5.677  1.00 17.78 ?  109 LEU   A HD23 1 
ATOM   2654 N N    . LYS   A 1 110 ? 23.462 -12.547 -5.612  1.00 11.95 ?  110 LYS   A N    1 
ATOM   2655 C CA   . LYS   A 1 110 ? 23.851 -13.677 -4.769  1.00 11.63 ?  110 LYS   A CA   1 
ATOM   2656 C C    . LYS   A 1 110 ? 25.236 -13.452 -4.170  1.00 11.28 ?  110 LYS   A C    1 
ATOM   2657 O O    . LYS   A 1 110 ? 25.442 -13.654 -2.971  1.00 11.50 ?  110 LYS   A O    1 
ATOM   2658 C CB   . LYS   A 1 110 ? 23.772 -14.996 -5.543  1.00 12.72 ?  110 LYS   A CB   1 
ATOM   2659 C CG   . LYS   A 1 110 ? 23.966 -16.216 -4.641  1.00 12.62 ?  110 LYS   A CG   1 
ATOM   2660 C CD   . LYS   A 1 110 ? 23.735 -17.527 -5.368  1.00 12.80 ?  110 LYS   A CD   1 
ATOM   2661 C CE   . LYS   A 1 110 ? 23.834 -18.721 -4.432  1.00 13.55 ?  110 LYS   A CE   1 
ATOM   2662 N NZ   . LYS   A 1 110 ? 22.657 -18.837 -3.537  1.00 14.04 ?  110 LYS   A NZ   1 
ATOM   2663 H H    . LYS   A 1 110 ? 23.355 -12.736 -6.448  1.00 14.40 ?  110 LYS   A H    1 
ATOM   2664 H HA   . LYS   A 1 110 ? 23.221 -13.737 -4.036  1.00 14.01 ?  110 LYS   A HA   1 
ATOM   2665 H HB2  . LYS   A 1 110 ? 22.898 -15.065 -5.960  1.00 15.32 ?  110 LYS   A HB2  1 
ATOM   2666 H HB3  . LYS   A 1 110 ? 24.465 -15.006 -6.220  1.00 15.32 ?  110 LYS   A HB3  1 
ATOM   2667 H HG2  . LYS   A 1 110 ? 24.875 -16.218 -4.303  1.00 15.20 ?  110 LYS   A HG2  1 
ATOM   2668 H HG3  . LYS   A 1 110 ? 23.338 -16.167 -3.904  1.00 15.20 ?  110 LYS   A HG3  1 
ATOM   2669 H HD2  . LYS   A 1 110 ? 22.847 -17.522 -5.760  1.00 15.41 ?  110 LYS   A HD2  1 
ATOM   2670 H HD3  . LYS   A 1 110 ? 24.406 -17.629 -6.062  1.00 15.41 ?  110 LYS   A HD3  1 
ATOM   2671 H HE2  . LYS   A 1 110 ? 23.895 -19.534 -4.958  1.00 16.31 ?  110 LYS   A HE2  1 
ATOM   2672 H HE3  . LYS   A 1 110 ? 24.625 -18.624 -3.877  1.00 16.31 ?  110 LYS   A HE3  1 
ATOM   2673 H HZ1  . LYS   A 1 110 ? 22.745 -19.543 -3.006  1.00 16.90 ?  110 LYS   A HZ1  1 
ATOM   2674 H HZ2  . LYS   A 1 110 ? 22.580 -18.104 -3.039  1.00 16.90 ?  110 LYS   A HZ2  1 
ATOM   2675 H HZ3  . LYS   A 1 110 ? 21.915 -18.932 -4.024  1.00 16.90 ?  110 LYS   A HZ3  1 
ATOM   2676 N N    . SER   A 1 111 ? 26.192 -12.999 -4.988  1.00 11.06 ?  111 SER   A N    1 
ATOM   2677 C CA   . SER   A 1 111 ? 27.524 -12.694 -4.476  1.00 11.46 ?  111 SER   A CA   1 
ATOM   2678 C C    . SER   A 1 111 ? 27.455 -11.661 -3.359  1.00 10.94 ?  111 SER   A C    1 
ATOM   2679 O O    . SER   A 1 111 ? 28.158 -11.770 -2.351  1.00 11.49 ?  111 SER   A O    1 
ATOM   2680 C CB   . SER   A 1 111 ? 28.407 -12.195 -5.619  1.00 12.72 ?  111 SER   A CB   1 
ATOM   2681 O OG   . SER   A 1 111 ? 28.476 -13.176 -6.648  1.00 15.22 ?  111 SER   A OG   1 
ATOM   2682 H H    . SER   A 1 111 ? 26.088 -12.861 -5.831  1.00 13.33 ?  111 SER   A H    1 
ATOM   2683 H HA   . SER   A 1 111 ? 27.918 -13.503 -4.116  1.00 13.81 ?  111 SER   A HA   1 
ATOM   2684 H HB2  . SER   A 1 111 ? 28.021 -11.388 -5.991  1.00 15.32 ?  111 SER   A HB2  1 
ATOM   2685 H HB3  . SER   A 1 111 ? 29.296 -12.009 -5.271  1.00 15.32 ?  111 SER   A HB3  1 
ATOM   2686 H HG   . SER   A 1 111 ? 28.994 -12.901 -7.263  1.00 18.33 ?  111 SER   A HG   1 
ATOM   2687 N N    . ALA   A 1 112 ? 26.611 -10.642 -3.531  1.00 11.06 ?  112 ALA   A N    1 
ATOM   2688 C CA   . ALA   A 1 112 ? 26.463 -9.610  -2.504  1.00 10.74 ?  112 ALA   A CA   1 
ATOM   2689 C C    . ALA   A 1 112 ? 26.001 -10.220 -1.182  1.00 10.57 ?  112 ALA   A C    1 
ATOM   2690 O O    . ALA   A 1 112 ? 26.564 -9.940  -0.116  1.00 10.98 ?  112 ALA   A O    1 
ATOM   2691 C CB   . ALA   A 1 112 ? 25.498 -8.526  -2.984  1.00 11.33 ?  112 ALA   A CB   1 
ATOM   2692 H H    . ALA   A 1 112 ? 26.121 -10.520 -4.228  1.00 13.33 ?  112 ALA   A H    1 
ATOM   2693 H HA   . ALA   A 1 112 ? 27.320 -9.190  -2.350  1.00 12.95 ?  112 ALA   A HA   1 
ATOM   2694 H HB1  . ALA   A 1 112 ? 25.427 -7.837  -2.299  1.00 13.65 ?  112 ALA   A HB1  1 
ATOM   2695 H HB2  . ALA   A 1 112 ? 25.836 -8.137  -3.804  1.00 13.65 ?  112 ALA   A HB2  1 
ATOM   2696 H HB3  . ALA   A 1 112 ? 24.624 -8.920  -3.140  1.00 13.65 ?  112 ALA   A HB3  1 
ATOM   2697 N N    . TYR   A 1 113 ? 24.965 -11.064 -1.231  1.00 11.04 ?  113 TYR   A N    1 
ATOM   2698 C CA   . TYR   A 1 113 ? 24.462 -11.677 -0.005  1.00 10.62 ?  113 TYR   A CA   1 
ATOM   2699 C C    . TYR   A 1 113 ? 25.472 -12.632 0.631   1.00 10.69 ?  113 TYR   A C    1 
ATOM   2700 O O    . TYR   A 1 113 ? 25.445 -12.824 1.850   1.00 10.93 ?  113 TYR   A O    1 
ATOM   2701 C CB   . TYR   A 1 113 ? 23.139 -12.402 -0.269  1.00 11.19 ?  113 TYR   A CB   1 
ATOM   2702 C CG   . TYR   A 1 113 ? 21.925 -11.510 -0.173  1.00 11.39 ?  113 TYR   A CG   1 
ATOM   2703 C CD1  . TYR   A 1 113 ? 21.580 -10.897 1.030   1.00 11.72 ?  113 TYR   A CD1  1 
ATOM   2704 C CD2  . TYR   A 1 113 ? 21.107 -11.300 -1.275  1.00 11.74 ?  113 TYR   A CD2  1 
ATOM   2705 C CE1  . TYR   A 1 113 ? 20.454 -10.094 1.129   1.00 12.15 ?  113 TYR   A CE1  1 
ATOM   2706 C CE2  . TYR   A 1 113 ? 19.968 -10.495 -1.188  1.00 12.00 ?  113 TYR   A CE2  1 
ATOM   2707 C CZ   . TYR   A 1 113 ? 19.651 -9.903  0.017   1.00 11.96 ?  113 TYR   A CZ   1 
ATOM   2708 O OH   . TYR   A 1 113 ? 18.532 -9.107  0.135   1.00 13.59 ?  113 TYR   A OH   1 
ATOM   2709 H H    . TYR   A 1 113 ? 24.548 -11.295 -1.950  1.00 13.31 ?  113 TYR   A H    1 
ATOM   2710 H HA   . TYR   A 1 113 ? 24.291 -10.974 0.635   1.00 12.80 ?  113 TYR   A HA   1 
ATOM   2711 H HB2  . TYR   A 1 113 ? 23.160 -12.772 -1.162  1.00 13.48 ?  113 TYR   A HB2  1 
ATOM   2712 H HB3  . TYR   A 1 113 ? 23.042 -13.109 0.384   1.00 13.48 ?  113 TYR   A HB3  1 
ATOM   2713 H HD1  . TYR   A 1 113 ? 22.122 -11.034 1.781   1.00 14.12 ?  113 TYR   A HD1  1 
ATOM   2714 H HD2  . TYR   A 1 113 ? 21.322 -11.708 -2.079  1.00 14.15 ?  113 TYR   A HD2  1 
ATOM   2715 H HE1  . TYR   A 1 113 ? 20.241 -9.698  1.940   1.00 14.64 ?  113 TYR   A HE1  1 
ATOM   2716 H HE2  . TYR   A 1 113 ? 19.429 -10.369 -1.933  1.00 14.45 ?  113 TYR   A HE2  1 
ATOM   2717 H HH   . TYR   A 1 113 ? 18.044 -9.212  -0.544  1.00 16.37 ?  113 TYR   A HH   1 
ATOM   2718 N N    . GLU   A 1 114 ? 26.367 -13.237 -0.163  1.00 10.60 ?  114 GLU   A N    1 
ATOM   2719 C CA   . GLU   A 1 114 ? 27.363 -14.134 0.424   1.00 10.69 ?  114 GLU   A CA   1 
ATOM   2720 C C    . GLU   A 1 114 ? 28.225 -13.429 1.466   1.00 10.69 ?  114 GLU   A C    1 
ATOM   2721 O O    . GLU   A 1 114 ? 28.722 -14.067 2.403   1.00 11.17 ?  114 GLU   A O    1 
ATOM   2722 C CB   . GLU   A 1 114 ? 28.227 -14.771 -0.674  1.00 11.14 ?  114 GLU   A CB   1 
ATOM   2723 C CG   . GLU   A 1 114 ? 27.452 -15.807 -1.462  1.00 11.54 ?  114 GLU   A CG   1 
ATOM   2724 C CD   . GLU   A 1 114 ? 28.157 -16.335 -2.709  1.00 11.68 ?  114 GLU   A CD   1 
ATOM   2725 O OE1  . GLU   A 1 114 ? 29.112 -15.701 -3.206  1.00 11.83 ?  114 GLU   A OE1  1 
ATOM   2726 O OE2  . GLU   A 1 114 ? 27.708 -17.397 -3.208  1.00 12.67 -1 114 GLU   A OE2  1 
ATOM   2727 H H    . GLU   A 1 114 ? 26.412 -13.147 -1.023  1.00 12.77 ?  114 GLU   A H    1 
ATOM   2728 H HA   . GLU   A 1 114 ? 26.893 -14.852 0.872   1.00 12.89 ?  114 GLU   A HA   1 
ATOM   2729 H HB2  . GLU   A 1 114 ? 28.522 -14.084 -1.293  1.00 13.42 ?  114 GLU   A HB2  1 
ATOM   2730 H HB3  . GLU   A 1 114 ? 28.987 -15.210 -0.269  1.00 13.42 ?  114 GLU   A HB3  1 
ATOM   2731 H HG2  . GLU   A 1 114 ? 27.280 -16.567 -0.887  1.00 13.90 ?  114 GLU   A HG2  1 
ATOM   2732 H HG3  . GLU   A 1 114 ? 26.610 -15.416 -1.746  1.00 13.90 ?  114 GLU   A HG3  1 
ATOM   2733 N N    . ASN   A 1 115 ? 28.399 -12.110 1.340   1.00 10.41 ?  115 ASN   A N    1 
ATOM   2734 C CA   . ASN   A 1 115 ? 29.167 -11.384 2.344   1.00 10.77 ?  115 ASN   A CA   1 
ATOM   2735 C C    . ASN   A 1 115 ? 28.559 -11.525 3.734   1.00 10.82 ?  115 ASN   A C    1 
ATOM   2736 O O    . ASN   A 1 115 ? 29.276 -11.456 4.737   1.00 11.16 ?  115 ASN   A O    1 
ATOM   2737 C CB   . ASN   A 1 115 ? 29.267 -9.907  1.968   1.00 10.92 ?  115 ASN   A CB   1 
ATOM   2738 C CG   . ASN   A 1 115 ? 30.063 -9.683  0.707   1.00 11.61 ?  115 ASN   A CG   1 
ATOM   2739 O OD1  . ASN   A 1 115 ? 31.282 -9.774  0.719   1.00 14.77 ?  115 ASN   A OD1  1 
ATOM   2740 N ND2  . ASN   A 1 115 ? 29.385 -9.378  -0.383  1.00 11.25 ?  115 ASN   A ND2  1 
ATOM   2741 H H    . ASN   A 1 115 ? 28.079 -11.617 0.703   1.00 12.55 ?  115 ASN   A H    1 
ATOM   2742 H HA   . ASN   A 1 115 ? 30.062 -11.750 2.374   1.00 12.98 ?  115 ASN   A HA   1 
ATOM   2743 H HB2  . ASN   A 1 115 ? 28.376 -9.553  1.836   1.00 13.16 ?  115 ASN   A HB2  1 
ATOM   2744 H HB3  . ASN   A 1 115 ? 29.708 -9.431  2.693   1.00 13.16 ?  115 ASN   A HB3  1 
ATOM   2745 H HD21 . ASN   A 1 115 ? 29.799 -9.236  -1.122  1.00 13.55 ?  115 ASN   A HD21 1 
ATOM   2746 H HD22 . ASN   A 1 115 ? 28.526 -9.331  -0.355  1.00 13.55 ?  115 ASN   A HD22 1 
ATOM   2747 N N    . PHE   A 1 116 ? 27.236 -11.693 3.821   1.00 10.92 ?  116 PHE   A N    1 
ATOM   2748 C CA   . PHE   A 1 116 ? 26.596 -11.796 5.130   1.00 10.87 ?  116 PHE   A CA   1 
ATOM   2749 C C    . PHE   A 1 116 ? 27.074 -13.032 5.892   1.00 11.29 ?  116 PHE   A C    1 
ATOM   2750 O O    . PHE   A 1 116 ? 27.002 -13.061 7.121   1.00 11.97 ?  116 PHE   A O    1 
ATOM   2751 C CB   . PHE   A 1 116 ? 25.065 -11.920 5.013   1.00 11.07 ?  116 PHE   A CB   1 
ATOM   2752 C CG   . PHE   A 1 116 ? 24.310 -10.676 4.552   1.00 10.96 ?  116 PHE   A CG   1 
ATOM   2753 C CD1  . PHE   A 1 116 ? 24.876 -9.658  3.799   1.00 11.57 ?  116 PHE   A CD1  1 
ATOM   2754 C CD2  . PHE   A 1 116 ? 22.960 -10.569 4.883   1.00 11.73 ?  116 PHE   A CD2  1 
ATOM   2755 C CE1  . PHE   A 1 116 ? 24.103 -8.577  3.386   1.00 11.56 ?  116 PHE   A CE1  1 
ATOM   2756 C CE2  . PHE   A 1 116 ? 22.188 -9.496  4.478   1.00 11.65 ?  116 PHE   A CE2  1 
ATOM   2757 C CZ   . PHE   A 1 116 ? 22.756 -8.491  3.735   1.00 11.62 ?  116 PHE   A CZ   1 
ATOM   2758 H H    . PHE   A 1 116 ? 26.694 -11.747 3.150   1.00 13.16 ?  116 PHE   A H    1 
ATOM   2759 H HA   . PHE   A 1 116 ? 26.800 -11.009 5.657   1.00 13.10 ?  116 PHE   A HA   1 
ATOM   2760 H HB2  . PHE   A 1 116 ? 24.866 -12.630 4.383   1.00 13.35 ?  116 PHE   A HB2  1 
ATOM   2761 H HB3  . PHE   A 1 116 ? 24.715 -12.167 5.888   1.00 13.35 ?  116 PHE   A HB3  1 
ATOM   2762 H HD1  . PHE   A 1 116 ? 25.771 -9.712  3.561   1.00 13.94 ?  116 PHE   A HD1  1 
ATOM   2763 H HD2  . PHE   A 1 116 ? 22.561 -11.254 5.382   1.00 14.13 ?  116 PHE   A HD2  1 
ATOM   2764 H HE1  . PHE   A 1 116 ? 24.496 -7.900  2.890   1.00 13.93 ?  116 PHE   A HE1  1 
ATOM   2765 H HE2  . PHE   A 1 116 ? 21.285 -9.459  4.720   1.00 14.04 ?  116 PHE   A HE2  1 
ATOM   2766 H HZ   . PHE   A 1 116 ? 22.245 -7.763  3.467   1.00 14.00 ?  116 PHE   A HZ   1 
ATOM   2767 N N    . ASN   A 1 117 ? 27.511 -14.075 5.181   1.00 11.32 ?  117 ASN   A N    1 
ATOM   2768 C CA   . ASN   A 1 117 ? 27.891 -15.328 5.830   1.00 11.50 ?  117 ASN   A CA   1 
ATOM   2769 C C    . ASN   A 1 117 ? 29.161 -15.209 6.652   1.00 12.14 ?  117 ASN   A C    1 
ATOM   2770 O O    . ASN   A 1 117 ? 29.471 -16.131 7.416   1.00 13.12 ?  117 ASN   A O    1 
ATOM   2771 C CB   . ASN   A 1 117 ? 27.997 -16.442 4.790   1.00 11.38 ?  117 ASN   A CB   1 
ATOM   2772 C CG   . ASN   A 1 117 ? 26.638 -16.827 4.267   1.00 11.54 ?  117 ASN   A CG   1 
ATOM   2773 O OD1  . ASN   A 1 117 ? 25.673 -16.873 5.035   1.00 12.33 ?  117 ASN   A OD1  1 
ATOM   2774 N ND2  . ASN   A 1 117 ? 26.538 -17.085 2.975   1.00 11.57 ?  117 ASN   A ND2  1 
ATOM   2775 H H    . ASN   A 1 117 ? 27.583 -14.078 4.325   1.00 13.64 ?  117 ASN   A H    1 
ATOM   2776 H HA   . ASN   A 1 117 ? 27.176 -15.570 6.439   1.00 13.85 ?  117 ASN   A HA   1 
ATOM   2777 H HB2  . ASN   A 1 117 ? 28.541 -16.132 4.046   1.00 13.71 ?  117 ASN   A HB2  1 
ATOM   2778 H HB3  . ASN   A 1 117 ? 28.400 -17.219 5.200   1.00 13.71 ?  117 ASN   A HB3  1 
ATOM   2779 H HD21 . ASN   A 1 117 ? 25.784 -17.302 2.635   1.00 13.95 ?  117 ASN   A HD21 1 
ATOM   2780 H HD22 . ASN   A 1 117 ? 27.238 -17.023 2.468   1.00 13.95 ?  117 ASN   A HD22 1 
ATOM   2781 N N    . GLN   A 1 118 ? 29.886 -14.098 6.532   1.00 11.94 ?  118 GLN   A N    1 
ATOM   2782 C CA   . GLN   A 1 118 ? 31.071 -13.867 7.346   1.00 12.52 ?  118 GLN   A CA   1 
ATOM   2783 C C    . GLN   A 1 118 ? 30.741 -13.295 8.718   1.00 12.76 ?  118 GLN   A C    1 
ATOM   2784 O O    . GLN   A 1 118 ? 31.667 -12.997 9.483   1.00 14.09 ?  118 GLN   A O    1 
ATOM   2785 C CB   . GLN   A 1 118 ? 32.045 -12.954 6.601   1.00 12.39 ?  118 GLN   A CB   1 
ATOM   2786 C CG   . GLN   A 1 118 ? 32.510 -13.534 5.271   1.00 12.48 ?  118 GLN   A CG   1 
ATOM   2787 C CD   . GLN   A 1 118 ? 33.340 -14.795 5.442   1.00 12.36 ?  118 GLN   A CD   1 
ATOM   2788 O OE1  . GLN   A 1 118 ? 34.212 -14.861 6.315   1.00 13.52 ?  118 GLN   A OE1  1 
ATOM   2789 N NE2  . GLN   A 1 118 ? 33.078 -15.801 4.605   1.00 12.55 ?  118 GLN   A NE2  1 
ATOM   2790 H H    . GLN   A 1 118 ? 29.709 -13.458 5.978   1.00 14.38 ?  118 GLN   A H    1 
ATOM   2791 H HA   . GLN   A 1 118 ? 31.513 -14.721 7.482   1.00 15.08 ?  118 GLN   A HA   1 
ATOM   2792 H HB2  . GLN   A 1 118 ? 31.609 -12.108 6.423   1.00 14.93 ?  118 GLN   A HB2  1 
ATOM   2793 H HB3  . GLN   A 1 118 ? 32.829 -12.816 7.155   1.00 14.93 ?  118 GLN   A HB3  1 
ATOM   2794 H HG2  . GLN   A 1 118 ? 31.732 -13.752 4.729   1.00 15.03 ?  118 GLN   A HG2  1 
ATOM   2795 H HG3  . GLN   A 1 118 ? 33.056 -12.877 4.811   1.00 15.03 ?  118 GLN   A HG3  1 
ATOM   2796 H HE21 . GLN   A 1 118 ? 32.453 -15.722 4.010   1.00 15.12 ?  118 GLN   A HE21 1 
ATOM   2797 H HE22 . GLN   A 1 118 ? 33.515 -16.541 4.659   1.00 15.12 ?  118 GLN   A HE22 1 
ATOM   2798 N N    . HIS   A 1 119 ? 29.452 -13.149 9.045   1.00 12.51 ?  119 HIS   A N    1 
ATOM   2799 C CA   . HIS   A 1 119 ? 29.004 -12.557 10.301  1.00 13.22 ?  119 HIS   A CA   1 
ATOM   2800 C C    . HIS   A 1 119 ? 27.879 -13.398 10.878  1.00 13.65 ?  119 HIS   A C    1 
ATOM   2801 O O    . HIS   A 1 119 ? 26.920 -13.722 10.172  1.00 13.97 ?  119 HIS   A O    1 
ATOM   2802 C CB   . HIS   A 1 119 ? 28.545 -11.124 10.047  1.00 13.52 ?  119 HIS   A CB   1 
ATOM   2803 C CG   . HIS   A 1 119 ? 29.614 -10.310 9.414   1.00 14.25 ?  119 HIS   A CG   1 
ATOM   2804 N ND1  . HIS   A 1 119 ? 30.603 -9.707  10.152  1.00 15.91 ?  119 HIS   A ND1  1 
ATOM   2805 C CD2  . HIS   A 1 119 ? 29.929 -10.108 8.115   1.00 15.12 ?  119 HIS   A CD2  1 
ATOM   2806 C CE1  . HIS   A 1 119 ? 31.452 -9.114  9.333   1.00 16.34 ?  119 HIS   A CE1  1 
ATOM   2807 N NE2  . HIS   A 1 119 ? 31.079 -9.357  8.091   1.00 16.42 ?  119 HIS   A NE2  1 
ATOM   2808 H H    . HIS   A 1 119 ? 28.798 -13.408 8.543   1.00 15.06 ?  119 HIS   A H    1 
ATOM   2809 H HA   . HIS   A 1 119 ? 29.738 -12.550 10.935  1.00 15.92 ?  119 HIS   A HA   1 
ATOM   2810 H HB2  . HIS   A 1 119 ? 27.775 -11.142 9.458   1.00 16.28 ?  119 HIS   A HB2  1 
ATOM   2811 H HB3  . HIS   A 1 119 ? 28.308 -10.720 10.897  1.00 16.28 ?  119 HIS   A HB3  1 
ATOM   2812 H HD1  . HIS   A 1 119 ? 30.646 -9.695  11.011  1.00 19.14 ?  119 HIS   A HD1  1 
ATOM   2813 H HD2  . HIS   A 1 119 ? 29.445 -10.418 7.379   1.00 18.20 ?  119 HIS   A HD2  1 
ATOM   2814 H HE1  . HIS   A 1 119 ? 32.189 -8.612  9.584   1.00 19.67 ?  119 HIS   A HE1  1 
ATOM   2815 N N    A GLU   A 1 120 ? 27.995 -13.743 12.163  0.40 14.71 ?  120 GLU   A N    1 
ATOM   2816 N N    B GLU   A 1 120 ? 27.989 -13.740 12.164  0.60 13.90 ?  120 GLU   A N    1 
ATOM   2817 C CA   A GLU   A 1 120 ? 27.045 -14.678 12.760  0.40 16.59 ?  120 GLU   A CA   1 
ATOM   2818 C CA   B GLU   A 1 120 ? 27.044 -14.689 12.751  0.60 15.48 ?  120 GLU   A CA   1 
ATOM   2819 C C    A GLU   A 1 120 ? 25.632 -14.104 12.792  0.40 15.28 ?  120 GLU   A C    1 
ATOM   2820 C C    B GLU   A 1 120 ? 25.632 -14.122 12.873  0.60 14.58 ?  120 GLU   A C    1 
ATOM   2821 O O    A GLU   A 1 120 ? 24.656 -14.826 12.549  0.40 15.09 ?  120 GLU   A O    1 
ATOM   2822 O O    B GLU   A 1 120 ? 24.657 -14.886 12.824  0.60 14.18 ?  120 GLU   A O    1 
ATOM   2823 C CB   A GLU   A 1 120 ? 27.507 -15.076 14.164  0.40 20.64 ?  120 GLU   A CB   1 
ATOM   2824 C CB   B GLU   A 1 120 ? 27.527 -15.151 14.125  0.60 19.37 ?  120 GLU   A CB   1 
ATOM   2825 C CG   A GLU   A 1 120 ? 28.673 -16.051 14.184  0.40 25.30 ?  120 GLU   A CG   1 
ATOM   2826 C CG   B GLU   A 1 120 ? 28.745 -16.056 14.083  0.60 24.74 ?  120 GLU   A CG   1 
ATOM   2827 C CD   A GLU   A 1 120 ? 28.808 -16.756 15.518  0.40 29.09 ?  120 GLU   A CD   1 
ATOM   2828 C CD   B GLU   A 1 120 ? 28.967 -16.795 15.386  0.60 29.45 ?  120 GLU   A CD   1 
ATOM   2829 O OE1  A GLU   A 1 120 ? 28.312 -16.214 16.530  0.40 30.48 ?  120 GLU   A OE1  1 
ATOM   2830 O OE1  B GLU   A 1 120 ? 28.501 -16.304 16.437  0.60 31.23 ?  120 GLU   A OE1  1 
ATOM   2831 O OE2  A GLU   A 1 120 ? 29.396 -17.857 15.553  0.40 30.67 -1 120 GLU   A OE2  1 
ATOM   2832 O OE2  B GLU   A 1 120 ? 29.601 -17.871 15.356  0.60 31.44 -1 120 GLU   A OE2  1 
ATOM   2833 H H    A GLU   A 1 120 ? 28.598 -13.451 12.701  0.40 17.71 ?  120 GLU   A H    1 
ATOM   2834 H H    B GLU   A 1 120 ? 28.591 -13.451 12.705  0.60 16.73 ?  120 GLU   A H    1 
ATOM   2835 H HA   A GLU   A 1 120 ? 27.020 -15.484 12.225  0.40 19.96 ?  120 GLU   A HA   1 
ATOM   2836 H HA   B GLU   A 1 120 ? 26.997 -15.471 12.180  0.60 18.63 ?  120 GLU   A HA   1 
ATOM   2837 H HB2  A GLU   A 1 120 ? 27.788 -14.281 14.643  0.40 24.83 ?  120 GLU   A HB2  1 
ATOM   2838 H HB2  B GLU   A 1 120 ? 27.754 -14.372 14.654  0.60 23.30 ?  120 GLU   A HB2  1 
ATOM   2839 H HB3  A GLU   A 1 120 ? 26.771 -15.498 14.633  0.40 24.83 ?  120 GLU   A HB3  1 
ATOM   2840 H HB3  B GLU   A 1 120 ? 26.808 -15.642 14.558  0.60 23.30 ?  120 GLU   A HB3  1 
ATOM   2841 H HG2  A GLU   A 1 120 ? 28.539 -16.726 13.501  0.40 30.42 ?  120 GLU   A HG2  1 
ATOM   2842 H HG2  B GLU   A 1 120 ? 28.627 -16.715 13.382  0.60 29.74 ?  120 GLU   A HG2  1 
ATOM   2843 H HG3  A GLU   A 1 120 ? 29.498 -15.567 14.016  0.40 30.42 ?  120 GLU   A HG3  1 
ATOM   2844 H HG3  B GLU   A 1 120 ? 29.532 -15.519 13.910  0.60 29.74 ?  120 GLU   A HG3  1 
ATOM   2845 N N    . VAL   A 1 121 ? 25.504 -12.811 13.078  1.00 14.79 ?  121 VAL   A N    1 
ATOM   2846 C CA   . VAL   A 1 121 ? 24.212 -12.144 13.224  1.00 14.99 ?  121 VAL   A CA   1 
ATOM   2847 C C    . VAL   A 1 121 ? 24.324 -10.763 12.591  1.00 13.50 ?  121 VAL   A C    1 
ATOM   2848 O O    . VAL   A 1 121 ? 25.304 -10.050 12.826  1.00 14.56 ?  121 VAL   A O    1 
ATOM   2849 C CB   . VAL   A 1 121 ? 23.818 -11.984 14.712  1.00 17.61 ?  121 VAL   A CB   1 
ATOM   2850 C CG1  . VAL   A 1 121 ? 22.433 -11.345 14.840  1.00 17.92 ?  121 VAL   A CG1  1 
ATOM   2851 C CG2  . VAL   A 1 121 ? 23.851 -13.306 15.463  1.00 19.54 ?  121 VAL   A CG2  1 
ATOM   2852 H H    A VAL   A 1 121 ? 26.172 -12.277 13.174  0.40 17.81 ?  121 VAL   A H    1 
ATOM   2853 H H    B VAL   A 1 121 ? 26.172 -12.274 13.154  0.60 17.81 ?  121 VAL   A H    1 
ATOM   2854 H HA   . VAL   A 1 121 ? 23.522 -12.656 12.772  1.00 18.04 ?  121 VAL   A HA   1 
ATOM   2855 H HB   . VAL   A 1 121 ? 24.452 -11.386 15.139  1.00 21.19 ?  121 VAL   A HB   1 
ATOM   2856 H HG11 . VAL   A 1 121 ? 22.150 -11.384 15.769  1.00 21.56 ?  121 VAL   A HG11 1 
ATOM   2857 H HG12 . VAL   A 1 121 ? 22.479 -10.419 14.551  1.00 21.56 ?  121 VAL   A HG12 1 
ATOM   2858 H HG13 . VAL   A 1 121 ? 21.805 -11.833 14.285  1.00 21.56 ?  121 VAL   A HG13 1 
ATOM   2859 H HG21 . VAL   A 1 121 ? 23.536 -13.159 16.377  1.00 23.51 ?  121 VAL   A HG21 1 
ATOM   2860 H HG22 . VAL   A 1 121 ? 23.266 -13.940 15.020  1.00 23.51 ?  121 VAL   A HG22 1 
ATOM   2861 H HG23 . VAL   A 1 121 ? 24.756 -13.641 15.482  1.00 23.51 ?  121 VAL   A HG23 1 
ATOM   2862 N N    . LEU   A 1 122 ? 23.306 -10.364 11.821  1.00 13.30 ?  122 LEU   A N    1 
ATOM   2863 C CA   . LEU   A 1 122 ? 23.304 -9.058  11.166  1.00 13.08 ?  122 LEU   A CA   1 
ATOM   2864 C C    . LEU   A 1 122 ? 21.909 -8.465  11.128  1.00 12.71 ?  122 LEU   A C    1 
ATOM   2865 O O    . LEU   A 1 122 ? 20.918 -9.190  11.007  1.00 13.54 ?  122 LEU   A O    1 
ATOM   2866 C CB   . LEU   A 1 122 ? 23.712 -9.145  9.692   1.00 14.67 ?  122 LEU   A CB   1 
ATOM   2867 C CG   . LEU   A 1 122 ? 24.909 -9.987  9.295   1.00 14.59 ?  122 LEU   A CG   1 
ATOM   2868 C CD1  . LEU   A 1 122 ? 24.492 -11.429 9.062   1.00 15.30 ?  122 LEU   A CD1  1 
ATOM   2869 C CD2  . LEU   A 1 122 ? 25.550 -9.398  8.045   1.00 14.07 ?  122 LEU   A CD2  1 
ATOM   2870 H H    . LEU   A 1 122 ? 22.599 -10.836 11.669  1.00 16.02 ?  122 LEU   A H    1 
ATOM   2871 H HA   . LEU   A 1 122 ? 23.899 -8.451  11.628  1.00 15.76 ?  122 LEU   A HA   1 
ATOM   2872 H HB2  . LEU   A 1 122 ? 22.962 -9.501  9.197   1.00 17.66 ?  122 LEU   A HB2  1 
ATOM   2873 H HB3  . LEU   A 1 122 ? 23.897 -8.247  9.385   1.00 17.66 ?  122 LEU   A HB3  1 
ATOM   2874 H HG   . LEU   A 1 122 ? 25.579 -9.968  10.002  1.00 17.56 ?  122 LEU   A HG   1 
ATOM   2875 H HD11 . LEU   A 1 122 ? 25.265 -11.943 8.778   1.00 18.42 ?  122 LEU   A HD11 1 
ATOM   2876 H HD12 . LEU   A 1 122 ? 24.143 -11.790 9.890   1.00 18.42 ?  122 LEU   A HD12 1 
ATOM   2877 H HD13 . LEU   A 1 122 ? 23.811 -11.451 8.374   1.00 18.42 ?  122 LEU   A HD13 1 
ATOM   2878 H HD21 . LEU   A 1 122 ? 26.288 -9.964  7.761   1.00 16.94 ?  122 LEU   A HD21 1 
ATOM   2879 H HD22 . LEU   A 1 122 ? 24.884 -9.351  7.340   1.00 16.94 ?  122 LEU   A HD22 1 
ATOM   2880 H HD23 . LEU   A 1 122 ? 25.881 -8.506  8.243   1.00 16.94 ?  122 LEU   A HD23 1 
ATOM   2881 N N    A LEU   A 1 123 ? 21.847 -7.133  11.171  0.40 12.49 ?  123 LEU   A N    1 
ATOM   2882 N N    B LEU   A 1 123 ? 21.858 -7.139  11.264  0.60 12.30 ?  123 LEU   A N    1 
ATOM   2883 C CA   A LEU   A 1 123 ? 20.664 -6.366  10.792  0.40 12.21 ?  123 LEU   A CA   1 
ATOM   2884 C CA   B LEU   A 1 123 ? 20.682 -6.328  10.973  0.60 11.91 ?  123 LEU   A CA   1 
ATOM   2885 C C    A LEU   A 1 123 ? 20.888 -5.833  9.382   0.40 11.74 ?  123 LEU   A C    1 
ATOM   2886 C C    B LEU   A 1 123 ? 20.888 -5.756  9.582   0.60 11.55 ?  123 LEU   A C    1 
ATOM   2887 O O    A LEU   A 1 123 ? 21.975 -5.337  9.073   0.40 11.94 ?  123 LEU   A O    1 
ATOM   2888 O O    B LEU   A 1 123 ? 21.898 -5.090  9.341   0.60 11.96 ?  123 LEU   A O    1 
ATOM   2889 C CB   A LEU   A 1 123 ? 20.468 -5.193  11.760  0.40 12.99 ?  123 LEU   A CB   1 
ATOM   2890 C CB   B LEU   A 1 123 ? 20.588 -5.180  11.978  0.60 12.23 ?  123 LEU   A CB   1 
ATOM   2891 C CG   A LEU   A 1 123 ? 19.416 -4.133  11.414  0.40 13.32 ?  123 LEU   A CG   1 
ATOM   2892 C CG   B LEU   A 1 123 ? 19.556 -4.090  11.679  0.60 12.57 ?  123 LEU   A CG   1 
ATOM   2893 C CD1  A LEU   A 1 123 ? 18.015 -4.725  11.349  0.40 13.44 ?  123 LEU   A CD1  1 
ATOM   2894 C CD1  B LEU   A 1 123 ? 18.136 -4.633  11.748  0.60 13.14 ?  123 LEU   A CD1  1 
ATOM   2895 C CD2  A LEU   A 1 123 ? 19.465 -2.987  12.419  0.40 13.64 ?  123 LEU   A CD2  1 
ATOM   2896 C CD2  B LEU   A 1 123 ? 19.740 -2.929  12.640  0.60 13.40 ?  123 LEU   A CD2  1 
ATOM   2897 H H    A LEU   A 1 123 ? 22.505 -6.634  11.419  0.40 15.05 ?  123 LEU   A H    1 
ATOM   2898 H H    B LEU   A 1 123 ? 22.533 -6.666  11.518  0.60 14.81 ?  123 LEU   A H    1 
ATOM   2899 H HA   A LEU   A 1 123 ? 19.872 -6.933  10.809  0.40 14.71 ?  123 LEU   A HA   1 
ATOM   2900 H HA   B LEU   A 1 123 ? 19.876 -6.869  10.988  0.60 14.34 ?  123 LEU   A HA   1 
ATOM   2901 H HB2  A LEU   A 1 123 ? 20.220 -5.558  12.626  0.40 15.65 ?  123 LEU   A HB2  1 
ATOM   2902 H HB2  B LEU   A 1 123 ? 20.361 -5.558  12.838  0.60 14.73 ?  123 LEU   A HB2  1 
ATOM   2903 H HB3  A LEU   A 1 123 ? 21.313 -4.732  11.842  0.40 15.65 ?  123 LEU   A HB3  1 
ATOM   2904 H HB3  B LEU   A 1 123 ? 21.453 -4.751  12.026  0.60 14.73 ?  123 LEU   A HB3  1 
ATOM   2905 H HG   A LEU   A 1 123 ? 19.619 -3.760  10.544  0.40 16.05 ?  123 LEU   A HG   1 
ATOM   2906 H HG   B LEU   A 1 123 ? 19.697 -3.747  10.778  0.60 15.14 ?  123 LEU   A HG   1 
ATOM   2907 H HD11 A LEU   A 1 123 ? 17.374 -4.006  11.226  0.40 16.19 ?  123 LEU   A HD11 1 
ATOM   2908 H HD11 B LEU   A 1 123 ? 17.512 -3.913  11.564  0.60 15.82 ?  123 LEU   A HD11 1 
ATOM   2909 H HD12 A LEU   A 1 123 ? 17.968 -5.340  10.603  0.40 16.19 ?  123 LEU   A HD12 1 
ATOM   2910 H HD12 B LEU   A 1 123 ? 18.034 -5.336  11.087  0.60 15.82 ?  123 LEU   A HD12 1 
ATOM   2911 H HD13 A LEU   A 1 123 ? 17.829 -5.192  12.179  0.40 16.19 ?  123 LEU   A HD13 1 
ATOM   2912 H HD13 B LEU   A 1 123 ? 17.980 -4.988  12.636  0.60 15.82 ?  123 LEU   A HD13 1 
ATOM   2913 H HD21 A LEU   A 1 123 ? 18.794 -2.328  12.182  0.40 16.43 ?  123 LEU   A HD21 1 
ATOM   2914 H HD21 B LEU   A 1 123 ? 19.080 -2.248  12.442  0.60 16.14 ?  123 LEU   A HD21 1 
ATOM   2915 H HD22 A LEU   A 1 123 ? 19.285 -3.337  13.307  0.40 16.43 ?  123 LEU   A HD22 1 
ATOM   2916 H HD22 B LEU   A 1 123 ? 19.620 -3.256  13.546  0.60 16.14 ?  123 LEU   A HD22 1 
ATOM   2917 H HD23 A LEU   A 1 123 ? 20.347 -2.585  12.397  0.40 16.43 ?  123 LEU   A HD23 1 
ATOM   2918 H HD23 B LEU   A 1 123 ? 20.633 -2.571  12.531  0.60 16.14 ?  123 LEU   A HD23 1 
ATOM   2919 N N    A ALA   A 1 124 ? 19.877 -5.943  8.519   0.40 11.31 ?  124 ALA   A N    1 
ATOM   2920 N N    B ALA   A 1 124 ? 19.944 -5.989  8.673   0.60 11.63 ?  124 ALA   A N    1 
ATOM   2921 C CA   A ALA   A 1 124 ? 20.119 -5.634  7.116   0.40 10.88 ?  124 ALA   A CA   1 
ATOM   2922 C CA   B ALA   A 1 124 ? 20.225 -5.723  7.272   0.60 12.01 ?  124 ALA   A CA   1 
ATOM   2923 C C    A ALA   A 1 124 ? 18.857 -5.175  6.404   0.40 11.06 ?  124 ALA   A C    1 
ATOM   2924 C C    B ALA   A 1 124 ? 18.983 -5.242  6.539   0.60 11.68 ?  124 ALA   A C    1 
ATOM   2925 O O    A ALA   A 1 124 ? 17.744 -5.554  6.792   0.40 11.61 ?  124 ALA   A O    1 
ATOM   2926 O O    B ALA   A 1 124 ? 17.854 -5.555  6.944   0.60 12.36 ?  124 ALA   A O    1 
ATOM   2927 C CB   A ALA   A 1 124 ? 20.688 -6.850  6.374   0.40 10.53 ?  124 ALA   A CB   1 
ATOM   2928 C CB   B ALA   A 1 124 ? 20.775 -6.976  6.570   0.60 12.50 ?  124 ALA   A CB   1 
ATOM   2929 H H    A ALA   A 1 124 ? 19.070 -6.188  8.711   0.40 13.63 ?  124 ALA   A H    1 
ATOM   2930 H H    B ALA   A 1 124 ? 19.152 -6.279  8.827   0.60 14.01 ?  124 ALA   A H    1 
ATOM   2931 H HA   A ALA   A 1 124 ? 20.776 -4.928  7.070   0.40 13.11 ?  124 ALA   A HA   1 
ATOM   2932 H HA   B ALA   A 1 124 ? 20.916 -5.038  7.212   0.60 14.47 ?  124 ALA   A HA   1 
ATOM   2933 H HB1  A ALA   A 1 124 ? 20.840 -6.615  5.445   0.40 12.70 ?  124 ALA   A HB1  1 
ATOM   2934 H HB1  B ALA   A 1 124 ? 20.963 -6.777  5.637   0.60 15.05 ?  124 ALA   A HB1  1 
ATOM   2935 H HB2  A ALA   A 1 124 ? 21.526 -7.114  6.789   0.40 12.70 ?  124 ALA   A HB2  1 
ATOM   2936 H HB2  B ALA   A 1 124 ? 21.594 -7.265  7.011   0.60 15.05 ?  124 ALA   A HB2  1 
ATOM   2937 H HB3  A ALA   A 1 124 ? 20.052 -7.583  6.427   0.40 12.70 ?  124 ALA   A HB3  1 
ATOM   2938 H HB3  B ALA   A 1 124 ? 20.113 -7.688  6.622   0.60 15.05 ?  124 ALA   A HB3  1 
ATOM   2939 N N    A PRO   A 1 125 ? 19.001 -4.377  5.351   0.40 11.55 ?  125 PRO   A N    1 
ATOM   2940 N N    B PRO   A 1 125 ? 19.162 -4.494  5.455   0.60 11.27 ?  125 PRO   A N    1 
ATOM   2941 C CA   A PRO   A 1 125 ? 17.911 -4.163  4.401   0.40 11.77 ?  125 PRO   A CA   1 
ATOM   2942 C CA   B PRO   A 1 125 ? 18.079 -4.236  4.509   0.60 11.44 ?  125 PRO   A CA   1 
ATOM   2943 C C    A PRO   A 1 125 ? 17.998 -5.204  3.291   0.40 11.84 ?  125 PRO   A C    1 
ATOM   2944 C C    B PRO   A 1 125 ? 18.120 -5.291  3.411   0.60 11.75 ?  125 PRO   A C    1 
ATOM   2945 O O    A PRO   A 1 125 ? 18.971 -5.953  3.181   0.40 12.11 ?  125 PRO   A O    1 
ATOM   2946 O O    B PRO   A 1 125 ? 19.109 -6.006  3.239   0.60 12.21 ?  125 PRO   A O    1 
ATOM   2947 C CB   A PRO   A 1 125 ? 18.254 -2.782  3.836   0.40 11.98 ?  125 PRO   A CB   1 
ATOM   2948 C CB   B PRO   A 1 125 ? 18.508 -2.886  3.926   0.60 11.52 ?  125 PRO   A CB   1 
ATOM   2949 C CG   A PRO   A 1 125 ? 19.748 -2.819  3.759   0.40 12.38 ?  125 PRO   A CG   1 
ATOM   2950 C CG   B PRO   A 1 125 ? 20.006 -3.046  3.791   0.60 11.48 ?  125 PRO   A CG   1 
ATOM   2951 C CD   A PRO   A 1 125 ? 20.196 -3.593  4.985   0.40 11.87 ?  125 PRO   A CD   1 
ATOM   2952 C CD   B PRO   A 1 125 ? 20.427 -3.883  4.997   0.60 10.91 ?  125 PRO   A CD   1 
ATOM   2953 H HA   A PRO   A 1 125 ? 17.037 -4.168  4.830   0.40 14.18 ?  125 PRO   A HA   1 
ATOM   2954 H HA   B PRO   A 1 125 ? 17.205 -4.188  4.938   0.60 13.79 ?  125 PRO   A HA   1 
ATOM   2955 H HB2  A PRO   A 1 125 ? 17.858 -2.675  2.957   0.40 14.43 ?  125 PRO   A HB2  1 
ATOM   2956 H HB2  B PRO   A 1 125 ? 18.087 -2.749  3.064   0.60 13.88 ?  125 PRO   A HB2  1 
ATOM   2957 H HB3  A PRO   A 1 125 ? 17.951 -2.091  4.445   0.40 14.43 ?  125 PRO   A HB3  1 
ATOM   2958 H HB3  B PRO   A 1 125 ? 18.285 -2.172  4.544   0.60 13.88 ?  125 PRO   A HB3  1 
ATOM   2959 H HG2  A PRO   A 1 125 ? 20.018 -3.277  2.947   0.40 14.92 ?  125 PRO   A HG2  1 
ATOM   2960 H HG2  B PRO   A 1 125 ? 20.211 -3.504  2.958   0.60 13.83 ?  125 PRO   A HG2  1 
ATOM   2961 H HG3  A PRO   A 1 125 ? 20.094 -1.915  3.776   0.40 14.92 ?  125 PRO   A HG3  1 
ATOM   2962 H HG3  B PRO   A 1 125 ? 20.427 -2.170  3.808   0.60 13.83 ?  125 PRO   A HG3  1 
ATOM   2963 H HD2  A PRO   A 1 125 ? 20.934 -4.182  4.766   0.40 14.30 ?  125 PRO   A HD2  1 
ATOM   2964 H HD2  B PRO   A 1 125 ? 21.061 -4.567  4.725   0.60 13.15 ?  125 PRO   A HD2  1 
ATOM   2965 H HD3  A PRO   A 1 125 ? 20.428 -2.984  5.705   0.40 14.30 ?  125 PRO   A HD3  1 
ATOM   2966 H HD3  B PRO   A 1 125 ? 20.799 -3.311  5.687   0.60 13.15 ?  125 PRO   A HD3  1 
ATOM   2967 N N    A LEU   A 1 126 ? 16.966 -5.224  2.451   0.40 12.02 ?  126 LEU   A N    1 
ATOM   2968 N N    B LEU   A 1 126 ? 17.037 -5.356  2.645   0.60 12.06 ?  126 LEU   A N    1 
ATOM   2969 C CA   A LEU   A 1 126 ? 16.995 -6.082  1.273   0.40 11.94 ?  126 LEU   A CA   1 
ATOM   2970 C CA   B LEU   A 1 126 ? 17.082 -6.098  1.394   0.60 12.42 ?  126 LEU   A CA   1 
ATOM   2971 C C    A LEU   A 1 126 ? 17.923 -5.475  0.230   0.40 11.19 ?  126 LEU   A C    1 
ATOM   2972 C C    B LEU   A 1 126 ? 18.012 -5.389  0.416   0.60 12.64 ?  126 LEU   A C    1 
ATOM   2973 O O    A LEU   A 1 126 ? 17.654 -4.395  -0.313  0.40 10.29 ?  126 LEU   A O    1 
ATOM   2974 O O    B LEU   A 1 126 ? 17.926 -4.172  0.238   0.60 14.05 ?  126 LEU   A O    1 
ATOM   2975 C CB   A LEU   A 1 126 ? 15.592 -6.289  0.715   0.40 12.64 ?  126 LEU   A CB   1 
ATOM   2976 C CB   B LEU   A 1 126 ? 15.687 -6.187  0.792   0.60 13.14 ?  126 LEU   A CB   1 
ATOM   2977 C CG   A LEU   A 1 126 ? 14.761 -7.355  1.438   0.40 13.14 ?  126 LEU   A CG   1 
ATOM   2978 C CG   B LEU   A 1 126 ? 14.666 -7.013  1.562   0.60 13.77 ?  126 LEU   A CG   1 
ATOM   2979 C CD1  A LEU   A 1 126 ? 13.312 -7.253  1.034   0.40 13.65 ?  126 LEU   A CD1  1 
ATOM   2980 C CD1  B LEU   A 1 126 ? 13.308 -6.862  0.908   0.60 15.03 ?  126 LEU   A CD1  1 
ATOM   2981 C CD2  A LEU   A 1 126 ? 15.282 -8.766  1.160   0.40 12.55 ?  126 LEU   A CD2  1 
ATOM   2982 C CD2  B LEU   A 1 126 ? 15.077 -8.481  1.605   0.60 13.68 ?  126 LEU   A CD2  1 
ATOM   2983 H H    A LEU   A 1 126 ? 16.247 -4.759  2.535   0.40 14.48 ?  126 LEU   A H    1 
ATOM   2984 H H    B LEU   A 1 126 ? 16.281 -4.985  2.818   0.60 14.53 ?  126 LEU   A H    1 
ATOM   2985 H HA   A LEU   A 1 126 ? 17.356 -6.946  1.519   0.40 14.39 ?  126 LEU   A HA   1 
ATOM   2986 H HA   B LEU   A 1 126 ? 17.418 -6.993  1.557   0.60 14.96 ?  126 LEU   A HA   1 
ATOM   2987 H HB2  A LEU   A 1 126 ? 15.109 -5.452  0.777   0.40 15.22 ?  126 LEU   A HB2  1 
ATOM   2988 H HB2  B LEU   A 1 126 ? 15.333 -5.286  0.720   0.60 15.83 ?  126 LEU   A HB2  1 
ATOM   2989 H HB3  A LEU   A 1 126 ? 15.667 -6.555  -0.215  0.40 15.22 ?  126 LEU   A HB3  1 
ATOM   2990 H HB3  B LEU   A 1 126 ? 15.764 -6.575  -0.090  0.60 15.83 ?  126 LEU   A HB3  1 
ATOM   2991 H HG   A LEU   A 1 126 ? 14.819 -7.207  2.394   0.40 15.82 ?  126 LEU   A HG   1 
ATOM   2992 H HG   B LEU   A 1 126 ? 14.602 -6.684  2.474   0.60 16.58 ?  126 LEU   A HG   1 
ATOM   2993 H HD11 A LEU   A 1 126 ? 12.806 -7.938  1.497   0.40 16.44 ?  126 LEU   A HD11 1 
ATOM   2994 H HD11 B LEU   A 1 126 ? 12.661 -7.393  1.397   0.60 18.09 ?  126 LEU   A HD11 1 
ATOM   2995 H HD12 A LEU   A 1 126 ? 12.983 -6.374  1.277   0.40 16.44 ?  126 LEU   A HD12 1 
ATOM   2996 H HD12 B LEU   A 1 126 ? 13.051 -5.928  0.923   0.60 18.09 ?  126 LEU   A HD12 1 
ATOM   2997 H HD13 A LEU   A 1 126 ? 13.244 -7.380  0.075   0.40 16.44 ?  126 LEU   A HD13 1 
ATOM   2998 H HD13 B LEU   A 1 126 ? 13.365 -7.175  -0.010  0.60 18.09 ?  126 LEU   A HD13 1 
ATOM   2999 H HD21 A LEU   A 1 126 ? 14.676 -9.412  1.557   0.40 15.12 ?  126 LEU   A HD21 1 
ATOM   3000 H HD21 B LEU   A 1 126 ? 14.361 -8.997  2.001   0.60 16.47 ?  126 LEU   A HD21 1 
ATOM   3001 H HD22 A LEU   A 1 126 ? 15.328 -8.903  0.201   0.40 15.12 ?  126 LEU   A HD22 1 
ATOM   3002 H HD22 B LEU   A 1 126 ? 15.247 -8.784  0.700   0.60 16.47 ?  126 LEU   A HD22 1 
ATOM   3003 H HD23 A LEU   A 1 126 ? 16.166 -8.863  1.549   0.40 15.12 ?  126 LEU   A HD23 1 
ATOM   3004 H HD23 B LEU   A 1 126 ? 15.883 -8.565  2.139   0.60 16.47 ?  126 LEU   A HD23 1 
ATOM   3005 N N    A LEU   A 1 127 ? 19.016 -6.180  -0.045  0.40 11.61 ?  127 LEU   A N    1 
ATOM   3006 N N    B LEU   A 1 127 ? 18.896 -6.151  -0.225  0.60 12.25 ?  127 LEU   A N    1 
ATOM   3007 C CA   A LEU   A 1 127 ? 19.995 -5.713  -1.009  0.40 11.64 ?  127 LEU   A CA   1 
ATOM   3008 C CA   B LEU   A 1 127 ? 19.861 -5.585  -1.154  0.60 12.42 ?  127 LEU   A CA   1 
ATOM   3009 C C    A LEU   A 1 127 ? 19.331 -5.475  -2.353  0.40 11.19 ?  127 LEU   A C    1 
ATOM   3010 C C    B LEU   A 1 127 ? 19.271 -5.482  -2.556  0.60 12.26 ?  127 LEU   A C    1 
ATOM   3011 O O    A LEU   A 1 127 ? 18.466 -6.239  -2.792  0.40 12.07 ?  127 LEU   A O    1 
ATOM   3012 O O    B LEU   A 1 127 ? 18.426 -6.282  -2.971  0.60 12.89 ?  127 LEU   A O    1 
ATOM   3013 C CB   A LEU   A 1 127 ? 21.105 -6.751  -1.166  0.40 11.99 ?  127 LEU   A CB   1 
ATOM   3014 C CB   B LEU   A 1 127 ? 21.140 -6.424  -1.184  0.60 12.95 ?  127 LEU   A CB   1 
ATOM   3015 C CG   A LEU   A 1 127 ? 21.944 -7.026  0.080   0.40 11.50 ?  127 LEU   A CG   1 
ATOM   3016 C CG   B LEU   A 1 127 ? 21.937 -6.505  0.121   0.60 13.53 ?  127 LEU   A CG   1 
ATOM   3017 C CD1  A LEU   A 1 127 ? 23.053 -8.003  -0.250  0.40 11.29 ?  127 LEU   A CD1  1 
ATOM   3018 C CD1  B LEU   A 1 127 ? 23.099 -7.469  -0.035  0.60 14.13 ?  127 LEU   A CD1  1 
ATOM   3019 C CD2  A LEU   A 1 127 ? 22.528 -5.737  0.636   0.40 11.37 ?  127 LEU   A CD2  1 
ATOM   3020 C CD2  B LEU   A 1 127 ? 22.448 -5.134  0.526   0.60 14.40 ?  127 LEU   A CD2  1 
ATOM   3021 H H    A LEU   A 1 127 ? 19.208 -6.935  0.312   0.40 13.99 ?  127 LEU   A H    1 
ATOM   3022 H H    B LEU   A 1 127 ? 18.954 -7.009  -0.126  0.60 14.76 ?  127 LEU   A H    1 
ATOM   3023 H HA   A LEU   A 1 127 ? 20.386 -4.882  -0.711  0.40 14.03 ?  127 LEU   A HA   1 
ATOM   3024 H HA   B LEU   A 1 127 ? 20.098 -4.699  -0.852  0.60 14.96 ?  127 LEU   A HA   1 
ATOM   3025 H HB2  A LEU   A 1 127 ? 20.701 -7.594  -1.434  0.40 14.45 ?  127 LEU   A HB2  1 
ATOM   3026 H HB2  B LEU   A 1 127 ? 20.904 -7.335  -1.430  0.60 15.60 ?  127 LEU   A HB2  1 
ATOM   3027 H HB3  A LEU   A 1 127 ? 21.711 -6.453  -1.862  0.40 14.45 ?  127 LEU   A HB3  1 
ATOM   3028 H HB3  B LEU   A 1 127 ? 21.729 -6.054  -1.857  0.60 15.60 ?  127 LEU   A HB3  1 
ATOM   3029 H HG   A LEU   A 1 127 ? 21.380 -7.426  0.764   0.40 13.85 ?  127 LEU   A HG   1 
ATOM   3030 H HG   B LEU   A 1 127 ? 21.365 -6.839  0.831   0.60 16.30 ?  127 LEU   A HG   1 
ATOM   3031 H HD11 A LEU   A 1 127 ? 23.535 -8.221  0.564   0.40 13.61 ?  127 LEU   A HD11 1 
ATOM   3032 H HD11 B LEU   A 1 127 ? 23.607 -7.493  0.794   0.60 17.02 ?  127 LEU   A HD11 1 
ATOM   3033 H HD12 A LEU   A 1 127 ? 22.665 -8.807  -0.629  0.40 13.61 ?  127 LEU   A HD12 1 
ATOM   3034 H HD12 B LEU   A 1 127 ? 22.757 -8.353  -0.235  0.60 17.02 ?  127 LEU   A HD12 1 
ATOM   3035 H HD13 A LEU   A 1 127 ? 23.653 -7.592  -0.890  0.40 13.61 ?  127 LEU   A HD13 1 
ATOM   3036 H HD13 B LEU   A 1 127 ? 23.670 -7.163  -0.759  0.60 17.02 ?  127 LEU   A HD13 1 
ATOM   3037 H HD21 A LEU   A 1 127 ? 23.191 -5.955  1.308   0.40 13.71 ?  127 LEU   A HD21 1 
ATOM   3038 H HD21 B LEU   A 1 127 ? 23.043 -5.230  1.286   0.60 17.34 ?  127 LEU   A HD21 1 
ATOM   3039 H HD22 A LEU   A 1 127 ? 22.944 -5.244  -0.091  0.40 13.71 ?  127 LEU   A HD22 1 
ATOM   3040 H HD22 B LEU   A 1 127 ? 22.928 -4.745  -0.223  0.60 17.34 ?  127 LEU   A HD22 1 
ATOM   3041 H HD23 A LEU   A 1 127 ? 21.817 -5.209  1.028   0.40 13.71 ?  127 LEU   A HD23 1 
ATOM   3042 H HD23 B LEU   A 1 127 ? 21.694 -4.575  0.763   0.60 17.34 ?  127 LEU   A HD23 1 
ATOM   3043 N N    A SER   A 1 128 ? 19.740 -4.391  -2.996  0.40 10.98 ?  128 SER   A N    1 
ATOM   3044 N N    B SER   A 1 128 ? 19.743 -4.476  -3.283  0.60 12.69 ?  128 SER   A N    1 
ATOM   3045 C CA   A SER   A 1 128 ? 19.324 -3.992  -4.328  0.40 10.78 ?  128 SER   A CA   1 
ATOM   3046 C CA   B SER   A 1 128 ? 19.360 -4.137  -4.647  0.60 13.23 ?  128 SER   A CA   1 
ATOM   3047 C C    A SER   A 1 128 ? 17.868 -3.568  -4.389  0.40 11.00 ?  128 SER   A C    1 
ATOM   3048 C C    B SER   A 1 128 ? 17.928 -3.627  -4.768  0.60 14.46 ?  128 SER   A C    1 
ATOM   3049 O O    A SER   A 1 128 ? 17.388 -3.245  -5.473  0.40 11.58 ?  128 SER   A O    1 
ATOM   3050 O O    B SER   A 1 128 ? 17.474 -3.363  -5.888  0.60 15.35 ?  128 SER   A O    1 
ATOM   3051 C CB   A SER   A 1 128 ? 19.665 -5.026  -5.410  0.40 10.76 ?  128 SER   A CB   1 
ATOM   3052 C CB   B SER   A 1 128 ? 19.685 -5.234  -5.672  0.60 12.90 ?  128 SER   A CB   1 
ATOM   3053 O OG   A SER   A 1 128 ? 21.079 -5.181  -5.518  0.40 10.64 ?  128 SER   A OG   1 
ATOM   3054 O OG   B SER   A 1 128 ? 21.091 -5.454  -5.752  0.60 12.91 ?  128 SER   A OG   1 
ATOM   3055 H H    A SER   A 1 128 ? 20.294 -3.828  -2.652  0.40 13.23 ?  128 SER   A H    1 
ATOM   3056 H H    B SER   A 1 128 ? 20.347 -3.945  -2.976  0.60 15.28 ?  128 SER   A H    1 
ATOM   3057 H HA   A SER   A 1 128 ? 19.826 -3.204  -4.552  0.40 13.00 ?  128 SER   A HA   1 
ATOM   3058 H HA   B SER   A 1 128 ? 19.913 -3.386  -4.889  0.60 15.93 ?  128 SER   A HA   1 
ATOM   3059 H HB2  A SER   A 1 128 ? 19.260 -5.874  -5.174  0.40 12.97 ?  128 SER   A HB2  1 
ATOM   3060 H HB2  B SER   A 1 128 ? 19.241 -6.055  -5.414  0.60 15.54 ?  128 SER   A HB2  1 
ATOM   3061 H HB3  A SER   A 1 128 ? 19.315 -4.715  -6.262  0.40 12.97 ?  128 SER   A HB3  1 
ATOM   3062 H HB3  B SER   A 1 128 ? 19.374 -4.944  -6.546  0.60 15.54 ?  128 SER   A HB3  1 
ATOM   3063 H HG   A SER   A 1 128 ? 21.423 -4.431  -5.690  0.40 12.83 ?  128 SER   A HG   1 
ATOM   3064 H HG   B SER   A 1 128 ? 21.481 -4.731  -5.930  0.60 15.55 ?  128 SER   A HG   1 
ATOM   3065 N N    A ALA   A 1 129 ? 17.162 -3.522  -3.261  0.40 11.34 ?  129 ALA   A N    1 
ATOM   3066 N N    B ALA   A 1 129 ? 17.223 -3.442  -3.650  0.60 15.41 ?  129 ALA   A N    1 
ATOM   3067 C CA   A ALA   A 1 129 ? 15.806 -3.005  -3.240  0.40 10.93 ?  129 ALA   A CA   1 
ATOM   3068 C CA   B ALA   A 1 129 ? 15.898 -2.843  -3.669  0.60 16.47 ?  129 ALA   A CA   1 
ATOM   3069 C C    A ALA   A 1 129 ? 15.844 -1.474  -3.225  0.40 10.76 ?  129 ALA   A C    1 
ATOM   3070 C C    B ALA   A 1 129 ? 16.022 -1.318  -3.735  0.60 16.92 ?  129 ALA   A C    1 
ATOM   3071 O O    A ALA   A 1 129 ? 16.908 -0.844  -3.295  0.40 11.48 ?  129 ALA   A O    1 
ATOM   3072 O O    B ALA   A 1 129 ? 17.117 -0.759  -3.842  0.60 16.86 ?  129 ALA   A O    1 
ATOM   3073 C CB   A ALA   A 1 129 ? 15.031 -3.596  -2.058  0.40 11.80 ?  129 ALA   A CB   1 
ATOM   3074 C CB   B ALA   A 1 129 ? 15.088 -3.310  -2.458  0.60 17.67 ?  129 ALA   A CB   1 
ATOM   3075 H H    A ALA   A 1 129 ? 17.447 -3.785  -2.492  0.40 13.66 ?  129 ALA   A H    1 
ATOM   3076 H H    B ALA   A 1 129 ? 17.491 -3.656  -2.851  0.60 18.55 ?  129 ALA   A H    1 
ATOM   3077 H HA   A ALA   A 1 129 ? 15.348 -3.285  -4.049  0.40 13.17 ?  129 ALA   A HA   1 
ATOM   3078 H HA   B ALA   A 1 129 ? 15.432 -3.138  -4.463  0.60 19.82 ?  129 ALA   A HA   1 
ATOM   3079 H HB1  A ALA   A 1 129 ? 14.122 -3.244  -2.065  0.40 14.21 ?  129 ALA   A HB1  1 
ATOM   3080 H HB1  B ALA   A 1 129 ? 14.203 -2.909  -2.490  0.60 21.26 ?  129 ALA   A HB1  1 
ATOM   3081 H HB2  A ALA   A 1 129 ? 15.006 -4.562  -2.144  0.40 14.21 ?  129 ALA   A HB2  1 
ATOM   3082 H HB2  B ALA   A 1 129 ? 15.007 -4.280  -2.481  0.60 21.26 ?  129 ALA   A HB2  1 
ATOM   3083 H HB3  A ALA   A 1 129 ? 15.471 -3.347  -1.232  0.40 14.21 ?  129 ALA   A HB3  1 
ATOM   3084 H HB3  B ALA   A 1 129 ? 15.541 -3.040  -1.643  0.60 21.26 ?  129 ALA   A HB3  1 
ATOM   3085 N N    A GLY   A 1 130 ? 14.663 -0.865  -3.157  0.40 11.63 ?  130 GLY   A N    1 
ATOM   3086 N N    B GLY   A 1 130 ? 14.889 -0.624  -3.692  0.60 18.03 ?  130 GLY   A N    1 
ATOM   3087 C CA   A GLY   A 1 130 ? 14.600 0.587   -3.112  0.40 12.54 ?  130 GLY   A CA   1 
ATOM   3088 C CA   B GLY   A 1 130 ? 14.955 0.828   -3.702  0.60 19.43 ?  130 GLY   A CA   1 
ATOM   3089 C C    A GLY   A 1 130 ? 15.194 1.205   -4.368  0.40 12.07 ?  130 GLY   A C    1 
ATOM   3090 C C    B GLY   A 1 130 ? 15.517 1.348   -5.010  0.60 20.05 ?  130 GLY   A C    1 
ATOM   3091 O O    A GLY   A 1 130 ? 14.915 0.770   -5.490  0.40 11.28 ?  130 GLY   A O    1 
ATOM   3092 O O    B GLY   A 1 130 ? 15.218 0.831   -6.093  0.60 20.12 ?  130 GLY   A O    1 
ATOM   3093 H H    A GLY   A 1 130 ? 13.889 -1.264  -3.147  0.40 14.01 ?  130 GLY   A H    1 
ATOM   3094 H H    B GLY   A 1 130 ? 14.094 -0.958  -3.663  0.60 21.70 ?  130 GLY   A H    1 
ATOM   3095 H HA2  A GLY   A 1 130 ? 13.672 0.868   -3.014  0.40 15.11 ?  130 GLY   A HA2  1 
ATOM   3096 H HA2  B GLY   A 1 130 ? 14.071 1.198   -3.584  0.60 23.38 ?  130 GLY   A HA2  1 
ATOM   3097 H HA3  A GLY   A 1 130 ? 15.099 0.902   -2.347  0.40 15.11 ?  130 GLY   A HA3  1 
ATOM   3098 H HA3  B GLY   A 1 130 ? 15.524 1.132   -2.975  0.60 23.38 ?  130 GLY   A HA3  1 
ATOM   3099 N N    A ILE   A 1 131 ? 16.035 2.227   -4.183  0.40 12.12 ?  131 ILE   A N    1 
ATOM   3100 N N    B ILE   A 1 131 ? 16.361 2.381   -4.911  0.60 20.83 ?  131 ILE   A N    1 
ATOM   3101 C CA   A ILE   A 1 131 ? 16.570 2.979   -5.317  0.40 11.43 ?  131 ILE   A CA   1 
ATOM   3102 C CA   B ILE   A 1 131 ? 16.924 3.007   -6.101  0.60 20.96 ?  131 ILE   A CA   1 
ATOM   3103 C C    A ILE   A 1 131 ? 17.581 2.199   -6.144  0.40 10.52 ?  131 ILE   A C    1 
ATOM   3104 C C    B ILE   A 1 131 ? 17.849 2.085   -6.875  0.60 19.80 ?  131 ILE   A C    1 
ATOM   3105 O O    A ILE   A 1 131 ? 18.027 2.707   -7.181  0.40 11.29 ?  131 ILE   A O    1 
ATOM   3106 O O    B ILE   A 1 131 ? 18.196 2.400   -8.018  0.60 19.70 ?  131 ILE   A O    1 
ATOM   3107 C CB   A ILE   A 1 131 ? 17.138 4.348   -4.881  0.40 12.30 ?  131 ILE   A CB   1 
ATOM   3108 C CB   B ILE   A 1 131 ? 17.589 4.372   -5.803  0.60 22.79 ?  131 ILE   A CB   1 
ATOM   3109 C CG1  A ILE   A 1 131 ? 18.392 4.182   -4.020  0.40 13.66 ?  131 ILE   A CG1  1 
ATOM   3110 C CG1  B ILE   A 1 131 ? 18.750 4.251   -4.813  0.60 24.22 ?  131 ILE   A CG1  1 
ATOM   3111 C CG2  A ILE   A 1 131 ? 16.071 5.146   -4.139  0.40 12.56 ?  131 ILE   A CG2  1 
ATOM   3112 C CG2  B ILE   A 1 131 ? 16.565 5.354   -5.275  0.60 23.39 ?  131 ILE   A CG2  1 
ATOM   3113 C CD1  A ILE   A 1 131 ? 19.022 5.500   -3.603  0.40 14.57 ?  131 ILE   A CD1  1 
ATOM   3114 C CD1  B ILE   A 1 131 ? 19.414 5.596   -4.529  0.60 24.99 ?  131 ILE   A CD1  1 
ATOM   3115 H H    A ILE   A 1 131 ? 16.292 2.493   -3.412  0.40 14.60 ?  131 ILE   A H    1 
ATOM   3116 H H    B ILE   A 1 131 ? 16.621 2.733   -4.176  0.60 25.05 ?  131 ILE   A H    1 
ATOM   3117 H HA   A ILE   A 1 131 ? 15.818 3.171   -5.900  0.40 13.78 ?  131 ILE   A HA   1 
ATOM   3118 H HA   B ILE   A 1 131 ? 16.195 3.188   -6.703  0.60 25.21 ?  131 ILE   A HA   1 
ATOM   3119 H HB   A ILE   A 1 131 ? 17.373 4.836   -5.680  0.40 14.81 ?  131 ILE   A HB   1 
ATOM   3120 H HB   B ILE   A 1 131 ? 17.941 4.725   -6.632  0.60 27.41 ?  131 ILE   A HB   1 
ATOM   3121 H HG12 A ILE   A 1 131 ? 18.157 3.693   -3.216  0.40 16.45 ?  131 ILE   A HG12 1 
ATOM   3122 H HG12 B ILE   A 1 131 ? 18.420 3.900   -3.971  0.60 29.12 ?  131 ILE   A HG12 1 
ATOM   3123 H HG13 A ILE   A 1 131 ? 19.053 3.686   -4.526  0.40 16.45 ?  131 ILE   A HG13 1 
ATOM   3124 H HG13 B ILE   A 1 131 ? 19.424 3.660   -5.180  0.60 29.12 ?  131 ILE   A HG13 1 
ATOM   3125 H HG21 A ILE   A 1 131 ? 16.375 6.062   -4.035  0.40 15.13 ?  131 ILE   A HG21 1 
ATOM   3126 H HG21 B ILE   A 1 131 ? 16.935 6.251   -5.316  0.60 28.12 ?  131 ILE   A HG21 1 
ATOM   3127 H HG22 A ILE   A 1 131 ? 15.247 5.132   -4.655  0.40 15.13 ?  131 ILE   A HG22 1 
ATOM   3128 H HG22 B ILE   A 1 131 ? 15.771 5.301   -5.825  0.60 28.12 ?  131 ILE   A HG22 1 
ATOM   3129 H HG23 A ILE   A 1 131 ? 15.919 4.747   -3.269  0.40 15.13 ?  131 ILE   A HG23 1 
ATOM   3130 H HG23 B ILE   A 1 131 ? 16.352 5.124   -4.359  0.60 28.12 ?  131 ILE   A HG23 1 
ATOM   3131 H HD11 A ILE   A 1 131 ? 19.876 5.319   -3.184  0.40 17.54 ?  131 ILE   A HD11 1 
ATOM   3132 H HD11 B ILE   A 1 131 ? 20.268 5.448   -4.099  0.60 30.04 ?  131 ILE   A HD11 1 
ATOM   3133 H HD12 A ILE   A 1 131 ? 19.147 6.052   -4.390  0.40 17.54 ?  131 ILE   A HD12 1 
ATOM   3134 H HD12 B ILE   A 1 131 ? 19.543 6.067   -5.370  0.60 30.04 ?  131 ILE   A HD12 1 
ATOM   3135 H HD13 A ILE   A 1 131 ? 18.432 5.947   -2.975  0.40 17.54 ?  131 ILE   A HD13 1 
ATOM   3136 H HD13 B ILE   A 1 131 ? 18.836 6.121   -3.949  0.60 30.04 ?  131 ILE   A HD13 1 
ATOM   3137 N N    A PHE   A 1 132 ? 17.953 0.986   -5.720  0.40 9.93  ?  132 PHE   A N    1 
ATOM   3138 N N    B PHE   A 1 132 ? 18.247 0.950   -6.298  0.60 19.01 ?  132 PHE   A N    1 
ATOM   3139 C CA   A PHE   A 1 132 ? 18.782 0.125   -6.551  0.40 10.31 ?  132 PHE   A CA   1 
ATOM   3140 C CA   B PHE   A 1 132 ? 19.056 0.002   -7.051  0.60 19.17 ?  132 PHE   A CA   1 
ATOM   3141 C C    A PHE   A 1 132 ? 17.977 -0.615  -7.616  0.40 10.73 ?  132 PHE   A C    1 
ATOM   3142 C C    B PHE   A 1 132 ? 18.249 -0.760  -8.096  0.60 19.05 ?  132 PHE   A C    1 
ATOM   3143 O O    A PHE   A 1 132 ? 18.577 -1.240  -8.495  0.40 11.54 ?  132 PHE   A O    1 
ATOM   3144 O O    B PHE   A 1 132 ? 18.844 -1.443  -8.937  0.60 19.88 ?  132 PHE   A O    1 
ATOM   3145 C CB   A PHE   A 1 132 ? 19.568 -0.860  -5.684  0.40 9.88  ?  132 PHE   A CB   1 
ATOM   3146 C CB   B PHE   A 1 132 ? 19.793 -0.947  -6.104  0.60 19.58 ?  132 PHE   A CB   1 
ATOM   3147 C CG   A PHE   A 1 132 ? 20.784 -0.263  -5.020  0.40 9.26  ?  132 PHE   A CG   1 
ATOM   3148 C CG   B PHE   A 1 132 ? 21.071 -0.376  -5.544  0.60 20.86 ?  132 PHE   A CG   1 
ATOM   3149 C CD1  A PHE   A 1 132 ? 20.646 0.696   -4.035  0.40 9.67  ?  132 PHE   A CD1  1 
ATOM   3150 C CD1  B PHE   A 1 132 ? 21.066 0.794   -4.800  0.60 22.11 ?  132 PHE   A CD1  1 
ATOM   3151 C CD2  A PHE   A 1 132 ? 22.060 -0.690  -5.357  0.40 9.52  ?  132 PHE   A CD2  1 
ATOM   3152 C CD2  B PHE   A 1 132 ? 22.281 -1.021  -5.755  0.60 21.54 ?  132 PHE   A CD2  1 
ATOM   3153 C CE1  A PHE   A 1 132 ? 21.753 1.236   -3.416  0.40 9.60  ?  132 PHE   A CE1  1 
ATOM   3154 C CE1  B PHE   A 1 132 ? 22.245 1.312   -4.289  0.60 22.70 ?  132 PHE   A CE1  1 
ATOM   3155 C CE2  A PHE   A 1 132 ? 23.168 -0.157  -4.740  0.40 9.57  ?  132 PHE   A CE2  1 
ATOM   3156 C CE2  B PHE   A 1 132 ? 23.456 -0.508  -5.246  0.60 22.41 ?  132 PHE   A CE2  1 
ATOM   3157 C CZ   A PHE   A 1 132 ? 23.015 0.811   -3.769  0.40 9.25  ?  132 PHE   A CZ   1 
ATOM   3158 C CZ   B PHE   A 1 132 ? 23.439 0.656   -4.513  0.60 22.78 ?  132 PHE   A CZ   1 
ATOM   3159 H H    A PHE   A 1 132 ? 17.723 0.645   -4.958  0.40 11.98 ?  132 PHE   A H    1 
ATOM   3160 H H    B PHE   A 1 132 ? 18.072 0.718   -5.486  0.60 22.87 ?  132 PHE   A H    1 
ATOM   3161 H HA   A PHE   A 1 132 ? 19.414 0.684   -7.009  0.40 12.43 ?  132 PHE   A HA   1 
ATOM   3162 H HA   B PHE   A 1 132 ? 19.735 0.505   -7.523  0.60 23.06 ?  132 PHE   A HA   1 
ATOM   3163 H HB2  A PHE   A 1 132 ? 18.973 -1.186  -4.984  0.40 11.92 ?  132 PHE   A HB2  1 
ATOM   3164 H HB2  B PHE   A 1 132 ? 19.216 -1.161  -5.356  0.60 23.55 ?  132 PHE   A HB2  1 
ATOM   3165 H HB3  A PHE   A 1 132 ? 19.854 -1.597  -6.239  0.40 11.92 ?  132 PHE   A HB3  1 
ATOM   3166 H HB3  B PHE   A 1 132 ? 20.021 -1.756  -6.588  0.60 23.55 ?  132 PHE   A HB3  1 
ATOM   3167 H HD1  A PHE   A 1 132 ? 19.794 0.993   -3.791  0.40 11.67 ?  132 PHE   A HD1  1 
ATOM   3168 H HD1  B PHE   A 1 132 ? 20.267 1.244   -4.648  0.60 26.59 ?  132 PHE   A HD1  1 
ATOM   3169 H HD2  A PHE   A 1 132 ? 22.155 -1.340  -6.016  0.40 11.48 ?  132 PHE   A HD2  1 
ATOM   3170 H HD2  B PHE   A 1 132 ? 22.301 -1.808  -6.251  0.60 25.90 ?  132 PHE   A HD2  1 
ATOM   3171 H HE1  A PHE   A 1 132 ? 21.649 1.891   -2.761  0.40 11.57 ?  132 PHE   A HE1  1 
ATOM   3172 H HE1  B PHE   A 1 132 ? 22.237 2.099   -3.795  0.60 27.30 ?  132 PHE   A HE1  1 
ATOM   3173 H HE2  A PHE   A 1 132 ? 24.012 -0.444  -4.988  0.40 11.54 ?  132 PHE   A HE2  1 
ATOM   3174 H HE2  B PHE   A 1 132 ? 24.260 -0.950  -5.398  0.60 26.95 ?  132 PHE   A HE2  1 
ATOM   3175 H HZ   A PHE   A 1 132 ? 23.763 1.176   -3.358  0.40 11.15 ?  132 PHE   A HZ   1 
ATOM   3176 H HZ   B PHE   A 1 132 ? 24.233 0.999   -4.172  0.60 27.39 ?  132 PHE   A HZ   1 
ATOM   3177 N N    A GLY   A 1 133 ? 16.644 -0.581  -7.548  0.40 10.82 ?  133 GLY   A N    1 
ATOM   3178 N N    B GLY   A 1 133 ? 16.919 -0.662  -8.071  0.60 18.58 ?  133 GLY   A N    1 
ATOM   3179 C CA   A GLY   A 1 133 ? 15.798 -0.950  -8.668  0.40 11.85 ?  133 GLY   A CA   1 
ATOM   3180 C CA   B GLY   A 1 133 ? 16.095 -1.065  -9.186  0.60 18.56 ?  133 GLY   A CA   1 
ATOM   3181 C C    A GLY   A 1 133 ? 15.558 -2.424  -8.898  0.40 13.19 ?  133 GLY   A C    1 
ATOM   3182 C C    B GLY   A 1 133 ? 15.497 -2.458  -9.109  0.60 18.62 ?  133 GLY   A C    1 
ATOM   3183 O O    A GLY   A 1 133 ? 15.044 -2.779  -9.965  0.40 14.89 ?  133 GLY   A O    1 
ATOM   3184 O O    B GLY   A 1 133 ? 14.539 -2.732  -9.838  0.60 19.39 ?  133 GLY   A O    1 
ATOM   3185 H H    A GLY   A 1 133 ? 16.195 -0.350  -6.853  0.40 13.04 ?  133 GLY   A H    1 
ATOM   3186 H H    B GLY   A 1 133 ? 16.474 -0.342  -7.404  0.60 22.35 ?  133 GLY   A H    1 
ATOM   3187 H HA2  A GLY   A 1 133 ? 14.926 -0.531  -8.560  0.40 14.28 ?  133 GLY   A HA2  1 
ATOM   3188 H HA2  B GLY   A 1 133 ? 15.369 -0.433  -9.279  0.60 22.33 ?  133 GLY   A HA2  1 
ATOM   3189 H HA3  A GLY   A 1 133 ? 16.186 -0.609  -9.486  0.40 14.28 ?  133 GLY   A HA3  1 
ATOM   3190 H HA3  B GLY   A 1 133 ? 16.628 -1.026  -9.995  0.60 22.33 ?  133 GLY   A HA3  1 
ATOM   3191 N N    A ALA   A 1 134 ? 15.902 -3.298  -7.956  0.40 13.21 ?  134 ALA   A N    1 
ATOM   3192 N N    B ALA   A 1 134 ? 16.028 -3.349  -8.274  0.60 17.92 ?  134 ALA   A N    1 
ATOM   3193 C CA   A ALA   A 1 134 ? 15.642 -4.718  -8.142  0.40 14.30 ?  134 ALA   A CA   1 
ATOM   3194 C CA   B ALA   A 1 134 ? 15.565 -4.729  -8.316  0.60 17.79 ?  134 ALA   A CA   1 
ATOM   3195 C C    A ALA   A 1 134 ? 14.277 -5.090  -7.571  0.40 15.19 ?  134 ALA   A C    1 
ATOM   3196 C C    B ALA   A 1 134 ? 14.257 -4.893  -7.541  0.60 18.05 ?  134 ALA   A C    1 
ATOM   3197 O O    A ALA   A 1 134 ? 13.696 -4.369  -6.755  0.40 15.86 ?  134 ALA   A O    1 
ATOM   3198 O O    B ALA   A 1 134 ? 13.829 -4.019  -6.782  0.60 18.63 ?  134 ALA   A O    1 
ATOM   3199 C CB   A ALA   A 1 134 ? 16.738 -5.565  -7.492  0.40 14.69 ?  134 ALA   A CB   1 
ATOM   3200 C CB   B ALA   A 1 134 ? 16.634 -5.683  -7.783  0.60 17.75 ?  134 ALA   A CB   1 
ATOM   3201 H H    A ALA   A 1 134 ? 16.285 -3.095  -7.209  0.40 15.91 ?  134 ALA   A H    1 
ATOM   3202 H H    B ALA   A 1 134 ? 16.639 -3.183  -7.690  0.60 21.57 ?  134 ALA   A H    1 
ATOM   3203 H HA   A ALA   A 1 134 ? 15.636 -4.917  -9.090  0.40 17.22 ?  134 ALA   A HA   1 
ATOM   3204 H HA   B ALA   A 1 134 ? 15.391 -4.966  -9.238  0.60 21.40 ?  134 ALA   A HA   1 
ATOM   3205 H HB1  A ALA   A 1 134 ? 16.547 -6.503  -7.651  0.40 17.69 ?  134 ALA   A HB1  1 
ATOM   3206 H HB1  B ALA   A 1 134 ? 16.310 -6.595  -7.863  0.60 21.36 ?  134 ALA   A HB1  1 
ATOM   3207 H HB2  A ALA   A 1 134 ? 17.594 -5.331  -7.887  0.40 17.69 ?  134 ALA   A HB2  1 
ATOM   3208 H HB2  B ALA   A 1 134 ? 17.442 -5.574  -8.309  0.60 21.36 ?  134 ALA   A HB2  1 
ATOM   3209 H HB3  A ALA   A 1 134 ? 16.754 -5.386  -6.540  0.40 17.69 ?  134 ALA   A HB3  1 
ATOM   3210 H HB3  B ALA   A 1 134 ? 16.812 -5.475  -6.854  0.60 21.36 ?  134 ALA   A HB3  1 
ATOM   3211 N N    A ASP   A 1 135 ? 13.766 -6.230  -8.025  0.40 15.46 ?  135 ASP   A N    1 
ATOM   3212 N N    B ASP   A 1 135 ? 13.621 -6.043  -7.745  0.60 18.28 ?  135 ASP   A N    1 
ATOM   3213 C CA   A ASP   A 1 135 ? 12.514 -6.758  -7.497  0.40 15.49 ?  135 ASP   A CA   1 
ATOM   3214 C CA   B ASP   A 1 135 ? 12.356 -6.334  -7.086  0.60 18.28 ?  135 ASP   A CA   1 
ATOM   3215 C C    A ASP   A 1 135 ? 12.740 -7.198  -6.060  0.40 14.56 ?  135 ASP   A C    1 
ATOM   3216 C C    B ASP   A 1 135 ? 12.612 -6.872  -5.681  0.60 17.00 ?  135 ASP   A C    1 
ATOM   3217 O O    A ASP   A 1 135 ? 13.561 -8.094  -5.818  0.40 14.31 ?  135 ASP   A O    1 
ATOM   3218 O O    B ASP   A 1 135 ? 13.319 -7.879  -5.532  0.60 16.82 ?  135 ASP   A O    1 
ATOM   3219 C CB   A ASP   A 1 135 ? 12.041 -7.945  -8.329  0.40 16.78 ?  135 ASP   A CB   1 
ATOM   3220 C CB   B ASP   A 1 135 ? 11.559 -7.347  -7.890  0.60 19.75 ?  135 ASP   A CB   1 
ATOM   3221 C CG   A ASP   A 1 135 ? 10.672 -8.459  -7.903  0.40 18.27 ?  135 ASP   A CG   1 
ATOM   3222 C CG   B ASP   A 1 135 ? 10.586 -8.115  -7.030  0.60 21.83 ?  135 ASP   A CG   1 
ATOM   3223 O OD1  A ASP   A 1 135 ? 10.151 -8.012  -6.860  0.40 18.59 ?  135 ASP   A OD1  1 
ATOM   3224 O OD1  B ASP   A 1 135 ? 9.856  -7.475  -6.239  0.60 21.90 ?  135 ASP   A OD1  1 
ATOM   3225 O OD2  A ASP   A 1 135 ? 10.107 -9.310  -8.618  0.40 19.91 -1 135 ASP   A OD2  1 
ATOM   3226 O OD2  B ASP   A 1 135 ? 10.574 -9.359  -7.129  0.60 23.52 -1 135 ASP   A OD2  1 
ATOM   3227 H H    A ASP   A 1 135 ? 14.123 -6.720  -8.634  0.40 18.61 ?  135 ASP   A H    1 
ATOM   3228 H H    B ASP   A 1 135 ? 13.900 -6.676  -8.259  0.60 21.99 ?  135 ASP   A H    1 
ATOM   3229 H HA   A ASP   A 1 135 ? 11.836 -6.070  -7.525  0.40 18.65 ?  135 ASP   A HA   1 
ATOM   3230 H HA   B ASP   A 1 135 ? 11.832 -5.521  -7.037  0.60 22.00 ?  135 ASP   A HA   1 
ATOM   3231 H HB2  A ASP   A 1 135 ? 11.968 -7.674  -9.252  0.40 20.19 ?  135 ASP   A HB2  1 
ATOM   3232 H HB2  B ASP   A 1 135 ? 11.075 -6.881  -8.600  0.60 23.76 ?  135 ASP   A HB2  1 
ATOM   3233 H HB3  A ASP   A 1 135 ? 12.678 -8.671  -8.239  0.40 20.19 ?  135 ASP   A HB3  1 
ATOM   3234 H HB3  B ASP   A 1 135 ? 12.161 -7.997  -8.279  0.60 23.76 ?  135 ASP   A HB3  1 
ATOM   3235 N N    A PRO   A 1 136 ? 12.056 -6.606  -5.081  0.40 14.70 ?  136 PRO   A N    1 
ATOM   3236 N N    B PRO   A 1 136 ? 12.072 -6.241  -4.633  0.60 16.35 ?  136 PRO   A N    1 
ATOM   3237 C CA   A PRO   A 1 136 ? 12.282 -7.019  -3.688  0.40 14.58 ?  136 PRO   A CA   1 
ATOM   3238 C CA   B PRO   A 1 136 ? 12.352 -6.713  -3.266  0.60 15.77 ?  136 PRO   A CA   1 
ATOM   3239 C C    A PRO   A 1 136 ? 11.901 -8.463  -3.415  0.40 14.12 ?  136 PRO   A C    1 
ATOM   3240 C C    B PRO   A 1 136 ? 11.903 -8.142  -2.983  0.60 14.79 ?  136 PRO   A C    1 
ATOM   3241 O O    A PRO   A 1 136 ? 12.528 -9.104  -2.566  0.40 14.15 ?  136 PRO   A O    1 
ATOM   3242 O O    B PRO   A 1 136 ? 12.506 -8.807  -2.132  0.60 13.85 ?  136 PRO   A O    1 
ATOM   3243 C CB   A PRO   A 1 136 ? 11.432 -6.025  -2.880  0.40 15.19 ?  136 PRO   A CB   1 
ATOM   3244 C CB   B PRO   A 1 136 ? 11.634 -5.680  -2.379  0.60 16.30 ?  136 PRO   A CB   1 
ATOM   3245 C CG   A PRO   A 1 136 ? 10.403 -5.533  -3.842  0.40 15.70 ?  136 PRO   A CG   1 
ATOM   3246 C CG   B PRO   A 1 136 ? 10.644 -5.004  -3.283  0.60 16.97 ?  136 PRO   A CG   1 
ATOM   3247 C CD   A PRO   A 1 136 ? 11.045 -5.540  -5.190  0.40 15.07 ?  136 PRO   A CD   1 
ATOM   3248 C CD   B PRO   A 1 136 ? 11.282 -4.999  -4.632  0.60 15.90 ?  136 PRO   A CD   1 
ATOM   3249 H HA   A PRO   A 1 136 ? 13.216 -6.896  -3.444  0.40 17.56 ?  136 PRO   A HA   1 
ATOM   3250 H HA   B PRO   A 1 136 ? 13.304 -6.651  -3.089  0.60 18.99 ?  136 PRO   A HA   1 
ATOM   3251 H HB2  A PRO   A 1 136 ? 11.014 -6.481  -2.130  0.40 18.29 ?  136 PRO   A HB2  1 
ATOM   3252 H HB2  B PRO   A 1 136 ? 11.179 -6.125  -1.649  0.60 19.62 ?  136 PRO   A HB2  1 
ATOM   3253 H HB3  A PRO   A 1 136 ? 11.991 -5.296  -2.565  0.40 18.29 ?  136 PRO   A HB3  1 
ATOM   3254 H HB3  B PRO   A 1 136 ? 12.275 -5.031  -2.038  0.60 19.62 ?  136 PRO   A HB3  1 
ATOM   3255 H HG2  A PRO   A 1 136 ? 9.641  -6.128  -3.829  0.40 18.90 ?  136 PRO   A HG2  1 
ATOM   3256 H HG2  B PRO   A 1 136 ? 9.815  -5.512  -3.302  0.60 20.42 ?  136 PRO   A HG2  1 
ATOM   3257 H HG3  A PRO   A 1 136 ? 10.141 -4.633  -3.600  0.40 18.90 ?  136 PRO   A HG3  1 
ATOM   3258 H HG3  B PRO   A 1 136 ? 10.478 -4.096  -2.979  0.60 20.42 ?  136 PRO   A HG3  1 
ATOM   3259 H HD2  A PRO   A 1 136 ? 10.393 -5.766  -5.871  0.40 18.15 ?  136 PRO   A HD2  1 
ATOM   3260 H HD2  B PRO   A 1 136 ? 10.602 -5.026  -5.327  0.60 19.14 ?  136 PRO   A HD2  1 
ATOM   3261 H HD3  A PRO   A 1 136 ? 11.471 -4.688  -5.371  0.40 18.15 ?  136 PRO   A HD3  1 
ATOM   3262 H HD3  B PRO   A 1 136 ? 11.863 -4.227  -4.736  0.60 19.14 ?  136 PRO   A HD3  1 
ATOM   3263 N N    A ILE   A 1 137 ? 10.885 -8.997  -4.098  0.40 14.14 ?  137 ILE   A N    1 
ATOM   3264 N N    B ILE   A 1 137 ? 10.853 -8.635  -3.645  0.60 14.82 ?  137 ILE   A N    1 
ATOM   3265 C CA   A ILE   A 1 137 ? 10.545 -10.409 -3.928  0.40 14.15 ?  137 ILE   A CA   1 
ATOM   3266 C CA   B ILE   A 1 137 ? 10.460 -10.031 -3.451  0.60 15.19 ?  137 ILE   A CA   1 
ATOM   3267 C C    A ILE   A 1 137 ? 11.716 -11.291 -4.346  0.40 13.36 ?  137 ILE   A C    1 
ATOM   3268 C C    B ILE   A 1 137 ? 11.589 -10.960 -3.890  0.60 14.67 ?  137 ILE   A C    1 
ATOM   3269 O O    A ILE   A 1 137 ? 12.062 -12.257 -3.656  0.40 13.44 ?  137 ILE   A O    1 
ATOM   3270 O O    B ILE   A 1 137 ? 11.908 -11.948 -3.212  0.60 14.89 ?  137 ILE   A O    1 
ATOM   3271 C CB   A ILE   A 1 137 ? 9.257  -10.758 -4.699  0.40 15.06 ?  137 ILE   A CB   1 
ATOM   3272 C CB   B ILE   A 1 137 ? 9.133  -10.326 -4.181  0.60 16.35 ?  137 ILE   A CB   1 
ATOM   3273 C CG1  A ILE   A 1 137 ? 8.069  -9.945  -4.169  0.40 16.44 ?  137 ILE   A CG1  1 
ATOM   3274 C CG1  B ILE   A 1 137 ? 7.993  -9.459  -3.618  0.60 18.18 ?  137 ILE   A CG1  1 
ATOM   3275 C CG2  A ILE   A 1 137 ? 8.973  -12.253 -4.597  0.40 15.11 ?  137 ILE   A CG2  1 
ATOM   3276 C CG2  B ILE   A 1 137 ? 8.778  -11.797 -4.060  0.60 16.72 ?  137 ILE   A CG2  1 
ATOM   3277 C CD1  A ILE   A 1 137 ? 6.805  -10.097 -4.990  0.40 17.64 ?  137 ILE   A CD1  1 
ATOM   3278 C CD1  B ILE   A 1 137 ? 6.651  -9.658  -4.297  0.60 19.58 ?  137 ILE   A CD1  1 
ATOM   3279 H H    A ILE   A 1 137 ? 10.385 -8.570  -4.644  0.40 17.03 ?  137 ILE   A H    1 
ATOM   3280 H H    B ILE   A 1 137 ? 10.363 -8.187  -4.197  0.60 17.84 ?  137 ILE   A H    1 
ATOM   3281 H HA   A ILE   A 1 137 ? 10.377 -10.579 -2.987  0.40 17.04 ?  137 ILE   A HA   1 
ATOM   3282 H HA   B ILE   A 1 137 ? 10.308 -10.176 -2.506  0.60 18.29 ?  137 ILE   A HA   1 
ATOM   3283 H HB   A ILE   A 1 137 ? 9.389  -10.535 -5.631  0.40 18.12 ?  137 ILE   A HB   1 
ATOM   3284 H HB   B ILE   A 1 137 ? 9.239  -10.110 -5.118  0.60 19.68 ?  137 ILE   A HB   1 
ATOM   3285 H HG12 A ILE   A 1 137 ? 7.876  -10.232 -3.262  0.40 19.79 ?  137 ILE   A HG12 1 
ATOM   3286 H HG12 B ILE   A 1 137 ? 7.876  -9.670  -2.679  0.60 21.87 ?  137 ILE   A HG12 1 
ATOM   3287 H HG13 A ILE   A 1 137 ? 8.312  -9.004  -4.168  0.40 19.79 ?  137 ILE   A HG13 1 
ATOM   3288 H HG13 B ILE   A 1 137 ? 8.235  -8.521  -3.712  0.60 21.87 ?  137 ILE   A HG13 1 
ATOM   3289 H HG21 A ILE   A 1 137 ? 8.071  -12.433 -4.909  0.40 18.19 ?  137 ILE   A HG21 1 
ATOM   3290 H HG21 B ILE   A 1 137 ? 8.013  -11.988 -4.621  0.60 20.12 ?  137 ILE   A HG21 1 
ATOM   3291 H HG22 A ILE   A 1 137 ? 9.608  -12.736 -5.144  0.40 18.19 ?  137 ILE   A HG22 1 
ATOM   3292 H HG22 B ILE   A 1 137 ? 9.525  -12.336 -4.353  0.60 20.12 ?  137 ILE   A HG22 1 
ATOM   3293 H HG23 A ILE   A 1 137 ? 9.055  -12.527 -3.669  0.40 18.19 ?  137 ILE   A HG23 1 
ATOM   3294 H HG23 B ILE   A 1 137 ? 8.569  -11.994 -3.134  0.60 20.12 ?  137 ILE   A HG23 1 
ATOM   3295 H HD11 A ILE   A 1 137 ? 6.097  -10.428 -4.416  0.40 21.23 ?  137 ILE   A HD11 1 
ATOM   3296 H HD11 B ILE   A 1 137 ? 5.971  -9.252  -3.742  0.60 23.56 ?  137 ILE   A HD11 1 
ATOM   3297 H HD12 A ILE   A 1 137 ? 6.566  -9.230  -5.350  0.40 21.23 ?  137 ILE   A HD12 1 
ATOM   3298 H HD12 B ILE   A 1 137 ? 6.667  -9.237  -5.171  0.60 23.56 ?  137 ILE   A HD12 1 
ATOM   3299 H HD13 A ILE   A 1 137 ? 6.968  -10.720 -5.713  0.40 21.23 ?  137 ILE   A HD13 1 
ATOM   3300 H HD13 B ILE   A 1 137 ? 6.460  -10.605 -4.389  0.60 23.56 ?  137 ILE   A HD13 1 
ATOM   3301 N N    A HIS   A 1 138 ? 12.348 -10.972 -5.477  0.40 13.39 ?  138 HIS   A N    1 
ATOM   3302 N N    B HIS   A 1 138 ? 12.214 -10.655 -5.030  0.60 14.75 ?  138 HIS   A N    1 
ATOM   3303 C CA   A HIS   A 1 138 ? 13.511 -11.740 -5.910  0.40 13.39 ?  138 HIS   A CA   1 
ATOM   3304 C CA   B HIS   A 1 138 ? 13.359 -11.436 -5.488  0.60 14.39 ?  138 HIS   A CA   1 
ATOM   3305 C C    A HIS   A 1 138 ? 14.657 -11.612 -4.917  0.40 12.86 ?  138 HIS   A C    1 
ATOM   3306 C C    B HIS   A 1 138 ? 14.534 -11.306 -4.528  0.60 13.35 ?  138 HIS   A C    1 
ATOM   3307 O O    A HIS   A 1 138 ? 15.364 -12.590 -4.644  0.40 13.25 ?  138 HIS   A O    1 
ATOM   3308 O O    B HIS   A 1 138 ? 15.196 -12.301 -4.204  0.60 13.11 ?  138 HIS   A O    1 
ATOM   3309 C CB   A HIS   A 1 138 ? 13.968 -11.275 -7.289  0.40 14.35 ?  138 HIS   A CB   1 
ATOM   3310 C CB   B HIS   A 1 138 ? 13.752 -10.998 -6.901  0.60 15.07 ?  138 HIS   A CB   1 
ATOM   3311 C CG   A HIS   A 1 138 ? 15.254 -11.899 -7.729  0.40 15.22 ?  138 HIS   A CG   1 
ATOM   3312 C CG   B HIS   A 1 138 ? 15.007 -11.639 -7.402  0.60 16.11 ?  138 HIS   A CG   1 
ATOM   3313 N ND1  A HIS   A 1 138 ? 15.399 -13.259 -7.907  0.40 15.95 ?  138 HIS   A ND1  1 
ATOM   3314 N ND1  B HIS   A 1 138 ? 15.080 -12.972 -7.746  0.60 17.20 ?  138 HIS   A ND1  1 
ATOM   3315 C CD2  A HIS   A 1 138 ? 16.459 -11.351 -8.011  0.40 15.53 ?  138 HIS   A CD2  1 
ATOM   3316 C CD2  B HIS   A 1 138 ? 16.244 -11.127 -7.612  0.60 16.23 ?  138 HIS   A CD2  1 
ATOM   3317 C CE1  A HIS   A 1 138 ? 16.637 -13.520 -8.286  0.40 16.05 ?  138 HIS   A CE1  1 
ATOM   3318 C CE1  B HIS   A 1 138 ? 16.307 -13.253 -8.147  0.60 17.29 ?  138 HIS   A CE1  1 
ATOM   3319 N NE2  A HIS   A 1 138 ? 17.300 -12.380 -8.358  0.40 15.73 ?  138 HIS   A NE2  1 
ATOM   3320 N NE2  B HIS   A 1 138 ? 17.033 -12.151 -8.077  0.60 16.89 ?  138 HIS   A NE2  1 
ATOM   3321 H H    A HIS   A 1 138 ? 12.132 -10.321 -5.995  0.40 16.13 ?  138 HIS   A H    1 
ATOM   3322 H H    B HIS   A 1 138 ? 11.989 -10.002 -5.550  0.60 17.75 ?  138 HIS   A H    1 
ATOM   3323 H HA   A HIS   A 1 138 ? 13.266 -12.674 -5.969  0.40 16.13 ?  138 HIS   A HA   1 
ATOM   3324 H HA   B HIS   A 1 138 ? 13.100 -12.366 -5.526  0.60 17.33 ?  138 HIS   A HA   1 
ATOM   3325 H HB2  A HIS   A 1 138 ? 13.286 -11.507 -7.936  0.40 17.27 ?  138 HIS   A HB2  1 
ATOM   3326 H HB2  B HIS   A 1 138 ? 13.032 -11.235 -7.514  0.60 18.14 ?  138 HIS   A HB2  1 
ATOM   3327 H HB3  A HIS   A 1 138 ? 14.092 -10.313 -7.269  0.40 17.27 ?  138 HIS   A HB3  1 
ATOM   3328 H HB3  B HIS   A 1 138 ? 13.882 -10.037 -6.911  0.60 18.14 ?  138 HIS   A HB3  1 
ATOM   3329 H HD1  B HIS   A 1 138 ? 14.429 -13.532 -7.708  0.60 20.70 ?  138 HIS   A HD1  1 
ATOM   3330 H HD2  A HIS   A 1 138 ? 16.675 -10.447 -7.978  0.40 18.69 ?  138 HIS   A HD2  1 
ATOM   3331 H HD2  B HIS   A 1 138 ? 16.507 -10.248 -7.470  0.60 19.54 ?  138 HIS   A HD2  1 
ATOM   3332 H HE1  A HIS   A 1 138 ? 16.978 -14.363 -8.470  0.40 19.32 ?  138 HIS   A HE1  1 
ATOM   3333 H HE1  B HIS   A 1 138 ? 16.609 -14.086 -8.435  0.60 20.80 ?  138 HIS   A HE1  1 
ATOM   3334 H HE2  A HIS   A 1 138 ? 18.124 -12.296 -8.584  0.40 18.94 ?  138 HIS   A HE2  1 
ATOM   3335 N N    A SER   A 1 139 ? 14.862 -10.413 -4.373  0.40 12.40 ?  139 SER   A N    1 
ATOM   3336 N N    B SER   A 1 139 ? 14.802 -10.089 -4.052  0.60 12.94 ?  139 SER   A N    1 
ATOM   3337 C CA   A SER   A 1 139 ? 15.962 -10.210 -3.441  0.40 11.70 ?  139 SER   A CA   1 
ATOM   3338 C CA   B SER   A 1 139 ? 15.891 -9.898  -3.104  0.60 12.67 ?  139 SER   A CA   1 
ATOM   3339 C C    A SER   A 1 139 ? 15.758 -11.007 -2.159  0.40 11.87 ?  139 SER   A C    1 
ATOM   3340 C C    B SER   A 1 139 ? 15.700 -10.770 -1.872  0.60 12.64 ?  139 SER   A C    1 
ATOM   3341 O O    A SER   A 1 139 ? 16.716 -11.574 -1.619  0.40 12.10 ?  139 SER   A O    1 
ATOM   3342 O O    B SER   A 1 139 ? 16.657 -11.377 -1.377  0.60 12.62 ?  139 SER   A O    1 
ATOM   3343 C CB   A SER   A 1 139 ? 16.119 -8.721  -3.136  0.40 11.11 ?  139 SER   A CB   1 
ATOM   3344 C CB   B SER   A 1 139 ? 15.995 -8.421  -2.721  0.60 12.24 ?  139 SER   A CB   1 
ATOM   3345 O OG   A SER   A 1 139 ? 17.223 -8.515  -2.281  0.40 10.63 ?  139 SER   A OG   1 
ATOM   3346 O OG   B SER   A 1 139 ? 17.049 -8.246  -1.791  0.60 12.25 ?  139 SER   A OG   1 
ATOM   3347 H H    A SER   A 1 139 ? 14.387 -9.716  -4.523  0.40 14.94 ?  139 SER   A H    1 
ATOM   3348 H H    B SER   A 1 139 ? 14.375 -9.367  -4.256  0.60 15.59 ?  139 SER   A H    1 
ATOM   3349 H HA   A SER   A 1 139 ? 16.784 -10.516 -3.853  0.40 14.10 ?  139 SER   A HA   1 
ATOM   3350 H HA   B SER   A 1 139 ? 16.727 -10.146 -3.521  0.60 15.26 ?  139 SER   A HA   1 
ATOM   3351 H HB2  A SER   A 1 139 ? 16.286 -8.243  -3.959  0.40 13.39 ?  139 SER   A HB2  1 
ATOM   3352 H HB2  B SER   A 1 139 ? 16.177 -7.887  -3.518  0.60 14.74 ?  139 SER   A HB2  1 
ATOM   3353 H HB3  A SER   A 1 139 ? 15.314 -8.395  -2.710  0.40 13.39 ?  139 SER   A HB3  1 
ATOM   3354 H HB3  B SER   A 1 139 ? 15.161 -8.125  -2.318  0.60 14.74 ?  139 SER   A HB3  1 
ATOM   3355 H HG   A SER   A 1 139 ? 17.305 -7.703  -2.090  0.40 12.81 ?  139 SER   A HG   1 
ATOM   3356 H HG   B SER   A 1 139 ? 17.793 -8.301  -2.174  0.60 14.76 ?  139 SER   A HG   1 
ATOM   3357 N N    A LEU   A 1 140 ? 14.524 -11.060 -1.650  0.40 12.38 ?  140 LEU   A N    1 
ATOM   3358 N N    B LEU   A 1 140 ? 14.471 -10.839 -1.357  0.60 13.08 ?  140 LEU   A N    1 
ATOM   3359 C CA   A LEU   A 1 140 ? 14.259 -11.858 -0.457  0.40 12.41 ?  140 LEU   A CA   1 
ATOM   3360 C CA   B LEU   A 1 140 ? 14.217 -11.689 -0.200  0.60 13.25 ?  140 LEU   A CA   1 
ATOM   3361 C C    A LEU   A 1 140 ? 14.517 -13.333 -0.726  0.40 12.16 ?  140 LEU   A C    1 
ATOM   3362 C C    B LEU   A 1 140 ? 14.485 -13.157 -0.525  0.60 13.22 ?  140 LEU   A C    1 
ATOM   3363 O O    A LEU   A 1 140 ? 15.106 -14.032 0.106   0.40 12.23 ?  140 LEU   A O    1 
ATOM   3364 O O    B LEU   A 1 140 ? 15.045 -13.893 0.296   0.60 13.69 ?  140 LEU   A O    1 
ATOM   3365 C CB   A LEU   A 1 140 ? 12.819 -11.643 0.015   0.40 13.17 ?  140 LEU   A CB   1 
ATOM   3366 C CB   B LEU   A 1 140 ? 12.781 -11.489 0.279   0.60 14.18 ?  140 LEU   A CB   1 
ATOM   3367 C CG   A LEU   A 1 140 ? 12.357 -12.455 1.232   0.40 13.65 ?  140 LEU   A CG   1 
ATOM   3368 C CG   B LEU   A 1 140 ? 12.363 -12.422 1.412   0.60 14.81 ?  140 LEU   A CG   1 
ATOM   3369 C CD1  A LEU   A 1 140 ? 13.304 -12.273 2.408   0.40 13.73 ?  140 LEU   A CD1  1 
ATOM   3370 C CD1  B LEU   A 1 140 ? 13.230 -12.187 2.640   0.60 14.82 ?  140 LEU   A CD1  1 
ATOM   3371 C CD2  A LEU   A 1 140 ? 10.929 -12.080 1.639   0.40 13.93 ?  140 LEU   A CD2  1 
ATOM   3372 C CD2  B LEU   A 1 140 ? 10.890 -12.234 1.734   0.60 15.43 ?  140 LEU   A CD2  1 
ATOM   3373 H H    A LEU   A 1 140 ? 13.843 -10.655 -1.966  0.40 14.91 ?  140 LEU   A H    1 
ATOM   3374 H H    B LEU   A 1 140 ? 13.785 -10.410 -1.653  0.60 15.75 ?  140 LEU   A H    1 
ATOM   3375 H HA   A LEU   A 1 140 ? 14.859 -11.582 0.254   0.40 14.95 ?  140 LEU   A HA   1 
ATOM   3376 H HA   B LEU   A 1 140 ? 14.812 -11.423 0.521   0.60 15.96 ?  140 LEU   A HA   1 
ATOM   3377 H HB2  A LEU   A 1 140 ? 12.719 -10.711 0.242   0.40 15.86 ?  140 LEU   A HB2  1 
ATOM   3378 H HB2  B LEU   A 1 140 ? 12.683 -10.577 0.599   0.60 17.07 ?  140 LEU   A HB2  1 
ATOM   3379 H HB3  A LEU   A 1 140 ? 12.228 -11.869 -0.716  0.40 15.86 ?  140 LEU   A HB3  1 
ATOM   3380 H HB3  B LEU   A 1 140 ? 12.182 -11.640 -0.466  0.60 17.07 ?  140 LEU   A HB3  1 
ATOM   3381 H HG   A LEU   A 1 140 ? 12.355 -13.399 1.002   0.40 16.43 ?  140 LEU   A HG   1 
ATOM   3382 H HG   B LEU   A 1 140 ? 12.485 -13.343 1.130   0.60 17.83 ?  140 LEU   A HG   1 
ATOM   3383 H HD11 A LEU   A 1 140 ? 12.926 -12.709 3.189   0.40 16.53 ?  140 LEU   A HD11 1 
ATOM   3384 H HD11 B LEU   A 1 140 ? 12.867 -12.692 3.381   0.60 17.84 ?  140 LEU   A HD11 1 
ATOM   3385 H HD12 A LEU   A 1 140 ? 14.160 -12.671 2.190   0.40 16.53 ?  140 LEU   A HD12 1 
ATOM   3386 H HD12 B LEU   A 1 140 ? 14.135 -12.482 2.450   0.60 17.84 ?  140 LEU   A HD12 1 
ATOM   3387 H HD13 A LEU   A 1 140 ? 13.412 -11.325 2.581   0.40 16.53 ?  140 LEU   A HD13 1 
ATOM   3388 H HD13 B LEU   A 1 140 ? 13.228 -11.240 2.849   0.60 17.84 ?  140 LEU   A HD13 1 
ATOM   3389 H HD21 A LEU   A 1 140 ? 10.667 -12.612 2.410   0.40 16.77 ?  140 LEU   A HD21 1 
ATOM   3390 H HD21 B LEU   A 1 140 ? 10.647 -12.839 2.452   0.60 18.57 ?  140 LEU   A HD21 1 
ATOM   3391 H HD22 A LEU   A 1 140 ? 10.901 -11.138 1.866   0.40 16.77 ?  140 LEU   A HD22 1 
ATOM   3392 H HD22 B LEU   A 1 140 ? 10.743 -11.316 2.007   0.60 18.57 ?  140 LEU   A HD22 1 
ATOM   3393 H HD23 A LEU   A 1 140 ? 10.330 -12.260 0.898   0.40 16.77 ?  140 LEU   A HD23 1 
ATOM   3394 H HD23 B LEU   A 1 140 ? 10.366 -12.433 0.942   0.60 18.57 ?  140 LEU   A HD23 1 
ATOM   3395 N N    A ARG   A 1 141 ? 14.089 -13.823 -1.890  0.40 12.53 ?  141 ARG   A N    1 
ATOM   3396 N N    B ARG   A 1 141 ? 14.096 -13.598 -1.724  0.60 13.96 ?  141 ARG   A N    1 
ATOM   3397 C CA   A ARG   A 1 141 ? 14.366 -15.203 -2.271  0.40 13.26 ?  141 ARG   A CA   1 
ATOM   3398 C CA   B ARG   A 1 141 ? 14.315 -14.986 -2.125  0.60 15.04 ?  141 ARG   A CA   1 
ATOM   3399 C C    A ARG   A 1 141 ? 15.865 -15.475 -2.262  0.40 12.86 ?  141 ARG   A C    1 
ATOM   3400 C C    B ARG   A 1 141 ? 15.806 -15.313 -2.171  0.60 14.11 ?  141 ARG   A C    1 
ATOM   3401 O O    A ARG   A 1 141 ? 16.324 -16.485 -1.715  0.40 12.83 ?  141 ARG   A O    1 
ATOM   3402 O O    B ARG   A 1 141 ? 16.251 -16.326 -1.617  0.60 13.92 ?  141 ARG   A O    1 
ATOM   3403 C CB   A ARG   A 1 141 ? 13.789 -15.452 -3.663  0.40 14.39 ?  141 ARG   A CB   1 
ATOM   3404 C CB   B ARG   A 1 141 ? 13.649 -15.213 -3.487  0.60 17.09 ?  141 ARG   A CB   1 
ATOM   3405 C CG   A ARG   A 1 141 ? 13.672 -16.906 -4.044  0.40 15.61 ?  141 ARG   A CG   1 
ATOM   3406 C CG   B ARG   A 1 141 ? 13.939 -16.541 -4.167  0.60 19.42 ?  141 ARG   A CG   1 
ATOM   3407 C CD   A ARG   A 1 141 ? 12.643 -17.599 -3.184  0.40 17.13 ?  141 ARG   A CD   1 
ATOM   3408 C CD   B ARG   A 1 141 ? 12.957 -17.589 -3.741  0.60 20.99 ?  141 ARG   A CD   1 
ATOM   3409 N NE   A ARG   A 1 141 ? 13.267 -18.401 -2.143  0.40 18.18 ?  141 ARG   A NE   1 
ATOM   3410 N NE   B ARG   A 1 141 ? 13.460 -18.359 -2.616  0.60 21.30 ?  141 ARG   A NE   1 
ATOM   3411 C CZ   A ARG   A 1 141 ? 12.601 -18.991 -1.160  0.40 19.05 ?  141 ARG   A CZ   1 
ATOM   3412 C CZ   B ARG   A 1 141 ? 12.694 -18.918 -1.691  0.60 22.01 ?  141 ARG   A CZ   1 
ATOM   3413 N NH1  A ARG   A 1 141 ? 11.300 -18.814 -1.004  0.40 19.21 ?  141 ARG   A NH1  1 
ATOM   3414 N NH1  B ARG   A 1 141 ? 11.389 -18.710 -1.658  0.60 22.47 ?  141 ARG   A NH1  1 
ATOM   3415 N NH2  A ARG   A 1 141 ? 13.258 -19.768 -0.304  0.40 19.70 ?  141 ARG   A NH2  1 
ATOM   3416 N NH2  B ARG   A 1 141 ? 13.253 -19.692 -0.766  0.60 21.95 ?  141 ARG   A NH2  1 
ATOM   3417 H H    A ARG   A 1 141 ? 13.646 -13.383 -2.471  0.40 15.10 ?  141 ARG   A H    1 
ATOM   3418 H H    B ARG   A 1 141 ? 13.710 -13.115 -2.318  0.60 16.81 ?  141 ARG   A H    1 
ATOM   3419 H HA   A ARG   A 1 141 ? 13.944 -15.812 -1.644  0.40 15.97 ?  141 ARG   A HA   1 
ATOM   3420 H HA   B ARG   A 1 141 ? 13.900 -15.578 -1.483  0.60 18.11 ?  141 ARG   A HA   1 
ATOM   3421 H HB2  A ARG   A 1 141 ? 12.904 -15.062 -3.703  0.40 17.32 ?  141 ARG   A HB2  1 
ATOM   3422 H HB2  B ARG   A 1 141 ? 12.686 -15.140 -3.372  0.60 20.56 ?  141 ARG   A HB2  1 
ATOM   3423 H HB3  A ARG   A 1 141 ? 14.366 -15.020 -4.316  0.40 17.32 ?  141 ARG   A HB3  1 
ATOM   3424 H HB3  B ARG   A 1 141 ? 13.947 -14.517 -4.090  0.60 20.56 ?  141 ARG   A HB3  1 
ATOM   3425 H HG2  A ARG   A 1 141 ? 13.400 -16.971 -4.974  0.40 18.79 ?  141 ARG   A HG2  1 
ATOM   3426 H HG2  B ARG   A 1 141 ? 13.864 -16.429 -5.126  0.60 23.36 ?  141 ARG   A HG2  1 
ATOM   3427 H HG3  A ARG   A 1 141 ? 14.532 -17.341 -3.916  0.40 18.79 ?  141 ARG   A HG3  1 
ATOM   3428 H HG3  B ARG   A 1 141 ? 14.831 -16.853 -3.940  0.60 23.36 ?  141 ARG   A HG3  1 
ATOM   3429 H HD2  A ARG   A 1 141 ? 12.091 -16.931 -2.750  0.40 20.62 ?  141 ARG   A HD2  1 
ATOM   3430 H HD2  B ARG   A 1 141 ? 12.123 -17.163 -3.479  0.60 25.25 ?  141 ARG   A HD2  1 
ATOM   3431 H HD3  A ARG   A 1 141 ? 12.098 -18.172 -3.746  0.40 20.62 ?  141 ARG   A HD3  1 
ATOM   3432 H HD3  B ARG   A 1 141 ? 12.797 -18.196 -4.479  0.60 25.25 ?  141 ARG   A HD3  1 
ATOM   3433 H HE   A ARG   A 1 141 ? 14.107 -18.567 -2.212  0.40 21.87 ?  141 ARG   A HE   1 
ATOM   3434 H HE   B ARG   A 1 141 ? 14.306 -18.498 -2.571  0.60 25.61 ?  141 ARG   A HE   1 
ATOM   3435 H HH11 A ARG   A 1 141 ? 10.858 -18.328 -1.562  0.40 23.11 ?  141 ARG   A HH11 1 
ATOM   3436 H HH11 B ARG   A 1 141 ? 11.004 -18.220 -2.250  0.60 27.02 ?  141 ARG   A HH11 1 
ATOM   3437 H HH12 A ARG   A 1 141 ? 10.884 -19.207 -0.361  0.40 23.11 ?  141 ARG   A HH12 1 
ATOM   3438 H HH12 B ARG   A 1 141 ? 10.920 -19.081 -1.045  0.60 27.02 ?  141 ARG   A HH12 1 
ATOM   3439 H HH21 A ARG   A 1 141 ? 14.103 -19.889 -0.396  0.40 23.70 ?  141 ARG   A HH21 1 
ATOM   3440 H HH21 B ARG   A 1 141 ? 14.101 -19.831 -0.776  0.60 26.40 ?  141 ARG   A HH21 1 
ATOM   3441 H HH22 A ARG   A 1 141 ? 12.836 -20.148 0.342   0.40 23.70 ?  141 ARG   A HH22 1 
ATOM   3442 H HH22 B ARG   A 1 141 ? 12.766 -20.053 -0.154  0.60 26.40 ?  141 ARG   A HH22 1 
ATOM   3443 N N    A VAL   A 1 142 ? 16.647 -14.580 -2.868  0.40 12.50 ?  142 VAL   A N    1 
ATOM   3444 N N    B VAL   A 1 142 ? 16.599 -14.464 -2.834  0.60 13.17 ?  142 VAL   A N    1 
ATOM   3445 C CA   A VAL   A 1 142 ? 18.095 -14.761 -2.889  0.40 12.62 ?  142 VAL   A CA   1 
ATOM   3446 C CA   B VAL   A 1 142 ? 18.040 -14.705 -2.896  0.60 12.98 ?  142 VAL   A CA   1 
ATOM   3447 C C    A VAL   A 1 142 ? 18.665 -14.709 -1.477  0.40 12.25 ?  142 VAL   A C    1 
ATOM   3448 C C    B VAL   A 1 142 ? 18.638 -14.698 -1.497  0.60 12.33 ?  142 VAL   A C    1 
ATOM   3449 O O    A VAL   A 1 142 ? 19.539 -15.508 -1.120  0.40 12.50 ?  142 VAL   A O    1 
ATOM   3450 O O    B VAL   A 1 142 ? 19.505 -15.517 -1.173  0.60 12.73 ?  142 VAL   A O    1 
ATOM   3451 C CB   A VAL   A 1 142 ? 18.765 -13.743 -3.829  0.40 13.03 ?  142 VAL   A CB   1 
ATOM   3452 C CB   B VAL   A 1 142 ? 18.735 -13.689 -3.821  0.60 13.31 ?  142 VAL   A CB   1 
ATOM   3453 C CG1  A VAL   A 1 142 ? 20.275 -13.897 -3.774  0.40 12.89 ?  142 VAL   A CG1  1 
ATOM   3454 C CG1  B VAL   A 1 142 ? 20.239 -13.938 -3.836  0.60 12.95 ?  142 VAL   A CG1  1 
ATOM   3455 C CG2  A VAL   A 1 142 ? 18.271 -13.932 -5.256  0.40 13.68 ?  142 VAL   A CG2  1 
ATOM   3456 C CG2  B VAL   A 1 142 ? 18.181 -13.779 -5.229  0.60 14.06 ?  142 VAL   A CG2  1 
ATOM   3457 H H    A VAL   A 1 142 ? 16.368 -13.879 -3.278  0.40 15.05 ?  142 VAL   A H    1 
ATOM   3458 H H    B VAL   A 1 142 ? 16.336 -13.755 -3.248  0.60 15.86 ?  142 VAL   A H    1 
ATOM   3459 H HA   A VAL   A 1 142 ? 18.291 -15.642 -3.246  0.40 15.20 ?  142 VAL   A HA   1 
ATOM   3460 H HA   B VAL   A 1 142 ? 18.192 -15.584 -3.275  0.60 15.63 ?  142 VAL   A HA   1 
ATOM   3461 H HB   A VAL   A 1 142 ? 18.545 -12.842 -3.546  0.40 15.70 ?  142 VAL   A HB   1 
ATOM   3462 H HB   B VAL   A 1 142 ? 18.587 -12.789 -3.490  0.60 16.03 ?  142 VAL   A HB   1 
ATOM   3463 H HG11 A VAL   A 1 142 ? 20.672 -13.404 -4.510  0.40 15.53 ?  142 VAL   A HG11 1 
ATOM   3464 H HG11 B VAL   A 1 142 ? 20.639 -13.443 -4.571  0.60 15.59 ?  142 VAL   A HG11 1 
ATOM   3465 H HG12 A VAL   A 1 142 ? 20.604 -13.546 -2.931  0.40 15.53 ?  142 VAL   A HG12 1 
ATOM   3466 H HG12 B VAL   A 1 142 ? 20.626 -13.639 -2.996  0.60 15.59 ?  142 VAL   A HG12 1 
ATOM   3467 H HG13 A VAL   A 1 142 ? 20.501 -14.838 -3.852  0.40 15.53 ?  142 VAL   A HG13 1 
ATOM   3468 H HG13 B VAL   A 1 142 ? 20.405 -14.887 -3.955  0.60 15.59 ?  142 VAL   A HG13 1 
ATOM   3469 H HG21 A VAL   A 1 142 ? 18.669 -13.251 -5.822  0.40 16.47 ?  142 VAL   A HG21 1 
ATOM   3470 H HG21 B VAL   A 1 142 ? 18.671 -13.165 -5.801  0.60 16.93 ?  142 VAL   A HG21 1 
ATOM   3471 H HG22 A VAL   A 1 142 ? 18.536 -14.813 -5.566  0.40 16.47 ?  142 VAL   A HG22 1 
ATOM   3472 H HG22 B VAL   A 1 142 ? 18.294 -14.688 -5.551  0.60 16.93 ?  142 VAL   A HG22 1 
ATOM   3473 H HG23 A VAL   A 1 142 ? 17.307 -13.852 -5.270  0.40 16.47 ?  142 VAL   A HG23 1 
ATOM   3474 H HG23 B VAL   A 1 142 ? 17.245 -13.545 -5.211  0.60 16.93 ?  142 VAL   A HG23 1 
ATOM   3475 N N    . CYS   A 1 143 ? 18.185 -13.778 -0.649  1.00 12.46 ?  143 CYS   A N    1 
ATOM   3476 C CA   . CYS   A 1 143 ? 18.656 -13.725 0.729   1.00 12.42 ?  143 CYS   A CA   1 
ATOM   3477 C C    . CYS   A 1 143 ? 18.437 -15.066 1.422   1.00 12.41 ?  143 CYS   A C    1 
ATOM   3478 O O    . CYS   A 1 143 ? 19.365 -15.658 1.982   1.00 12.68 ?  143 CYS   A O    1 
ATOM   3479 C CB   . CYS   A 1 143 ? 17.925 -12.614 1.475   1.00 13.11 ?  143 CYS   A CB   1 
ATOM   3480 S SG   . CYS   A 1 143 ? 18.426 -12.448 3.199   1.00 13.46 ?  143 CYS   A SG   1 
ATOM   3481 H H    A CYS   A 1 143 ? 17.602 -13.186 -0.859  0.40 15.01 ?  143 CYS   A H    1 
ATOM   3482 H H    B CYS   A 1 143 ? 17.606 -13.180 -0.849  0.60 15.01 ?  143 CYS   A H    1 
ATOM   3483 H HA   . CYS   A 1 143 ? 19.606 -13.532 0.738   1.00 14.96 ?  143 CYS   A HA   1 
ATOM   3484 H HB2  . CYS   A 1 143 ? 18.094 -11.769 1.026   1.00 15.78 ?  143 CYS   A HB2  1 
ATOM   3485 H HB3  . CYS   A 1 143 ? 16.975 -12.801 1.461   1.00 15.78 ?  143 CYS   A HB3  1 
ATOM   3486 H HG   . CYS   A 1 143 ? 17.860 -11.502 3.669   1.00 16.21 ?  143 CYS   A HG   1 
ATOM   3487 N N    . VAL   A 1 144 ? 17.208 -15.571 1.377   1.00 12.93 ?  144 VAL   A N    1 
ATOM   3488 C CA   . VAL   A 1 144 ? 16.883 -16.812 2.073   1.00 13.92 ?  144 VAL   A CA   1 
ATOM   3489 C C    . VAL   A 1 144 ? 17.704 -17.976 1.533   1.00 13.45 ?  144 VAL   A C    1 
ATOM   3490 O O    . VAL   A 1 144 ? 18.087 -18.882 2.284   1.00 13.95 ?  144 VAL   A O    1 
ATOM   3491 C CB   . VAL   A 1 144 ? 15.368 -17.067 1.966   1.00 15.94 ?  144 VAL   A CB   1 
ATOM   3492 C CG1  . VAL   A 1 144 ? 15.016 -18.521 2.266   1.00 17.35 ?  144 VAL   A CG1  1 
ATOM   3493 C CG2  . VAL   A 1 144 ? 14.620 -16.100 2.883   1.00 16.23 ?  144 VAL   A CG2  1 
ATOM   3494 H H    . VAL   A 1 144 ? 16.546 -15.215 0.958   1.00 15.57 ?  144 VAL   A H    1 
ATOM   3495 H HA   . VAL   A 1 144 ? 17.093 -16.717 3.011   1.00 16.76 ?  144 VAL   A HA   1 
ATOM   3496 H HB   . VAL   A 1 144 ? 15.081 -16.882 1.054   1.00 19.19 ?  144 VAL   A HB   1 
ATOM   3497 H HG11 . VAL   A 1 144 ? 14.064 -18.585 2.460   1.00 20.87 ?  144 VAL   A HG11 1 
ATOM   3498 H HG12 . VAL   A 1 144 ? 15.224 -19.068 1.490   1.00 20.87 ?  144 VAL   A HG12 1 
ATOM   3499 H HG13 . VAL   A 1 144 ? 15.527 -18.820 3.031   1.00 20.87 ?  144 VAL   A HG13 1 
ATOM   3500 H HG21 . VAL   A 1 144 ? 13.664 -16.265 2.813   1.00 19.53 ?  144 VAL   A HG21 1 
ATOM   3501 H HG22 . VAL   A 1 144 ? 14.911 -16.241 3.797   1.00 19.53 ?  144 VAL   A HG22 1 
ATOM   3502 H HG23 . VAL   A 1 144 ? 14.816 -15.189 2.611   1.00 19.53 ?  144 VAL   A HG23 1 
ATOM   3503 N N    . ASP   A 1 145 ? 17.953 -17.993 0.227   1.00 13.12 ?  145 ASP   A N    1 
ATOM   3504 C CA   . ASP   A 1 145 ? 18.661 -19.090 -0.425  1.00 14.10 ?  145 ASP   A CA   1 
ATOM   3505 C C    . ASP   A 1 145 ? 20.182 -18.941 -0.399  1.00 13.73 ?  145 ASP   A C    1 
ATOM   3506 O O    . ASP   A 1 145 ? 20.886 -19.825 -0.901  1.00 15.64 ?  145 ASP   A O    1 
ATOM   3507 C CB   . ASP   A 1 145 ? 18.194 -19.212 -1.877  1.00 15.42 ?  145 ASP   A CB   1 
ATOM   3508 C CG   . ASP   A 1 145 ? 16.754 -19.677 -1.995  1.00 17.03 ?  145 ASP   A CG   1 
ATOM   3509 O OD1  . ASP   A 1 145 ? 16.212 -20.233 -1.014  1.00 17.51 ?  145 ASP   A OD1  1 
ATOM   3510 O OD2  . ASP   A 1 145 ? 16.173 -19.468 -3.077  1.00 18.84 -1 145 ASP   A OD2  1 
ATOM   3511 H H    . ASP   A 1 145 ? 17.700 -17.371 -0.318  1.00 15.80 ?  145 ASP   A H    1 
ATOM   3512 H HA   . ASP   A 1 145 ? 18.429 -19.915 0.029   1.00 16.98 ?  145 ASP   A HA   1 
ATOM   3513 H HB2  . ASP   A 1 145 ? 18.273 -18.344 -2.306  1.00 18.57 ?  145 ASP   A HB2  1 
ATOM   3514 H HB3  . ASP   A 1 145 ? 18.754 -19.859 -2.330  1.00 18.57 ?  145 ASP   A HB3  1 
ATOM   3515 N N    . THR   A 1 146 ? 20.706 -17.858 0.164   1.00 12.26 ?  146 THR   A N    1 
ATOM   3516 C CA   . THR   A 1 146 ? 22.141 -17.601 0.177   1.00 11.85 ?  146 THR   A CA   1 
ATOM   3517 C C    . THR   A 1 146 ? 22.703 -17.415 1.573   1.00 11.79 ?  146 THR   A C    1 
ATOM   3518 O O    . THR   A 1 146 ? 23.782 -17.943 1.879   1.00 12.93 ?  146 THR   A O    1 
ATOM   3519 C CB   . THR   A 1 146 ? 22.460 -16.348 -0.664  1.00 11.69 ?  146 THR   A CB   1 
ATOM   3520 O OG1  . THR   A 1 146 ? 21.916 -16.505 -1.980  1.00 12.49 ?  146 THR   A OG1  1 
ATOM   3521 C CG2  . THR   A 1 146 ? 23.963 -16.104 -0.745  1.00 12.12 ?  146 THR   A CG2  1 
ATOM   3522 H H    . THR   A 1 146 ? 20.240 -17.244 0.556   1.00 14.77 ?  146 THR   A H    1 
ATOM   3523 H HA   . THR   A 1 146 ? 22.600 -18.349 -0.224  1.00 14.28 ?  146 THR   A HA   1 
ATOM   3524 H HB   . THR   A 1 146 ? 22.059 -15.568 -0.245  1.00 14.09 ?  146 THR   A HB   1 
ATOM   3525 H HG1  . THR   A 1 146 ? 21.087 -16.586 -1.935  1.00 15.05 ?  146 THR   A HG1  1 
ATOM   3526 H HG21 . THR   A 1 146 ? 24.155 -15.432 -1.420  1.00 14.60 ?  146 THR   A HG21 1 
ATOM   3527 H HG22 . THR   A 1 146 ? 24.302 -15.789 0.111   1.00 14.60 ?  146 THR   A HG22 1 
ATOM   3528 H HG23 . THR   A 1 146 ? 24.422 -16.925 -0.981  1.00 14.60 ?  146 THR   A HG23 1 
ATOM   3529 N N    . VAL   A 1 147 ? 22.022 -16.648 2.414   1.00 12.07 ?  147 VAL   A N    1 
ATOM   3530 C CA   . VAL   A 1 147 ? 22.515 -16.358 3.751   1.00 12.00 ?  147 VAL   A CA   1 
ATOM   3531 C C    . VAL   A 1 147 ? 22.200 -17.535 4.660   1.00 12.20 ?  147 VAL   A C    1 
ATOM   3532 O O    . VAL   A 1 147 ? 21.055 -18.005 4.717   1.00 13.26 ?  147 VAL   A O    1 
ATOM   3533 C CB   . VAL   A 1 147 ? 21.890 -15.062 4.286   1.00 12.39 ?  147 VAL   A CB   1 
ATOM   3534 C CG1  . VAL   A 1 147 ? 22.426 -14.759 5.659   1.00 13.65 ?  147 VAL   A CG1  1 
ATOM   3535 C CG2  . VAL   A 1 147 ? 22.134 -13.905 3.327   1.00 12.29 ?  147 VAL   A CG2  1 
ATOM   3536 H H    . VAL   A 1 147 ? 21.257 -16.285 2.238   1.00 14.54 ?  147 VAL   A H    1 
ATOM   3537 H HA   . VAL   A 1 147 ? 23.477 -16.240 3.717   1.00 14.45 ?  147 VAL   A HA   1 
ATOM   3538 H HB   . VAL   A 1 147 ? 20.931 -15.188 4.366   1.00 14.93 ?  147 VAL   A HB   1 
ATOM   3539 H HG11 . VAL   A 1 147 ? 22.180 -13.856 5.903   1.00 16.44 ?  147 VAL   A HG11 1 
ATOM   3540 H HG12 . VAL   A 1 147 ? 22.039 -15.387 6.297   1.00 16.44 ?  147 VAL   A HG12 1 
ATOM   3541 H HG13 . VAL   A 1 147 ? 23.390 -14.852 5.651   1.00 16.44 ?  147 VAL   A HG13 1 
ATOM   3542 H HG21 . VAL   A 1 147 ? 21.799 -13.088 3.730   1.00 14.81 ?  147 VAL   A HG21 1 
ATOM   3543 H HG22 . VAL   A 1 147 ? 23.082 -13.830 3.158   1.00 14.81 ?  147 VAL   A HG22 1 
ATOM   3544 H HG23 . VAL   A 1 147 ? 21.659 -14.080 2.498   1.00 14.81 ?  147 VAL   A HG23 1 
ATOM   3545 N N    . ARG   A 1 148 ? 23.228 -18.012 5.365   1.00 12.45 ?  148 ARG   A N    1 
ATOM   3546 C CA   . ARG   A 1 148 ? 23.092 -19.098 6.321   1.00 12.68 ?  148 ARG   A CA   1 
ATOM   3547 C C    . ARG   A 1 148 ? 23.246 -18.643 7.759   1.00 13.17 ?  148 ARG   A C    1 
ATOM   3548 O O    . ARG   A 1 148 ? 22.852 -19.375 8.675   1.00 14.51 ?  148 ARG   A O    1 
ATOM   3549 C CB   . ARG   A 1 148 ? 24.107 -20.207 6.017   1.00 13.49 ?  148 ARG   A CB   1 
ATOM   3550 C CG   . ARG   A 1 148 ? 23.923 -20.821 4.642   1.00 13.97 ?  148 ARG   A CG   1 
ATOM   3551 C CD   . ARG   A 1 148 ? 24.993 -21.864 4.321   1.00 14.65 ?  148 ARG   A CD   1 
ATOM   3552 N NE   . ARG   A 1 148 ? 26.334 -21.287 4.337   1.00 14.77 ?  148 ARG   A NE   1 
ATOM   3553 C CZ   . ARG   A 1 148 ? 26.844 -20.548 3.361   1.00 13.95 ?  148 ARG   A CZ   1 
ATOM   3554 N NH1  . ARG   A 1 148 ? 26.158 -20.294 2.260   1.00 14.31 ?  148 ARG   A NH1  1 
ATOM   3555 N NH2  . ARG   A 1 148 ? 28.072 -20.044 3.499   1.00 14.57 ?  148 ARG   A NH2  1 
ATOM   3556 H H    . ARG   A 1 148 ? 24.037 -17.716 5.286   1.00 15.00 ?  148 ARG   A H    1 
ATOM   3557 H HA   . ARG   A 1 148 ? 22.207 -19.475 6.226   1.00 15.27 ?  148 ARG   A HA   1 
ATOM   3558 H HB2  . ARG   A 1 148 ? 25.001 -19.844 6.066   1.00 16.24 ?  148 ARG   A HB2  1 
ATOM   3559 H HB3  . ARG   A 1 148 ? 23.997 -20.915 6.674   1.00 16.24 ?  148 ARG   A HB3  1 
ATOM   3560 H HG2  . ARG   A 1 148 ? 23.056 -21.256 4.602   1.00 16.83 ?  148 ARG   A HG2  1 
ATOM   3561 H HG3  . ARG   A 1 148 ? 23.975 -20.120 3.974   1.00 16.83 ?  148 ARG   A HG3  1 
ATOM   3562 H HD2  . ARG   A 1 148 ? 24.961 -22.573 4.984   1.00 17.63 ?  148 ARG   A HD2  1 
ATOM   3563 H HD3  . ARG   A 1 148 ? 24.828 -22.232 3.436   1.00 17.63 ?  148 ARG   A HD3  1 
ATOM   3564 H HE   . ARG   A 1 148 ? 26.832 -21.446 5.019   1.00 17.78 ?  148 ARG   A HE   1 
ATOM   3565 H HH11 . ARG   A 1 148 ? 25.369 -20.608 2.157   1.00 17.22 ?  148 ARG   A HH11 1 
ATOM   3566 H HH12 . ARG   A 1 148 ? 26.510 -19.804 1.640   1.00 17.22 ?  148 ARG   A HH12 1 
ATOM   3567 H HH21 . ARG   A 1 148 ? 28.524 -20.201 4.211   1.00 17.54 ?  148 ARG   A HH21 1 
ATOM   3568 H HH22 . ARG   A 1 148 ? 28.411 -19.557 2.873   1.00 17.54 ?  148 ARG   A HH22 1 
ATOM   3569 N N    . THR   A 1 149 ? 23.810 -17.458 7.973   1.00 13.36 ?  149 THR   A N    1 
ATOM   3570 C CA   . THR   A 1 149 ? 23.897 -16.875 9.295   1.00 13.40 ?  149 THR   A CA   1 
ATOM   3571 C C    . THR   A 1 149 ? 22.572 -16.185 9.624   1.00 12.99 ?  149 THR   A C    1 
ATOM   3572 O O    . THR   A 1 149 ? 21.626 -16.177 8.825   1.00 13.54 ?  149 THR   A O    1 
ATOM   3573 C CB   . THR   A 1 149 ? 25.097 -15.941 9.352   1.00 13.77 ?  149 THR   A CB   1 
ATOM   3574 O OG1  . THR   A 1 149 ? 24.956 -14.983 8.299   1.00 13.85 ?  149 THR   A OG1  1 
ATOM   3575 C CG2  . THR   A 1 149 ? 26.396 -16.735 9.169   1.00 14.58 ?  149 THR   A CG2  1 
ATOM   3576 H H    . THR   A 1 149 ? 24.158 -16.964 7.351   1.00 16.09 ?  149 THR   A H    1 
ATOM   3577 H HA   . THR   A 1 149 ? 24.033 -17.590 9.936   1.00 16.14 ?  149 THR   A HA   1 
ATOM   3578 H HB   . THR   A 1 149 ? 25.118 -15.498 10.214  1.00 16.59 ?  149 THR   A HB   1 
ATOM   3579 H HG1  . THR   A 1 149 ? 25.605 -14.453 8.312   1.00 16.68 ?  149 THR   A HG1  1 
ATOM   3580 H HG21 . THR   A 1 149 ? 27.161 -16.146 9.245   1.00 17.55 ?  149 THR   A HG21 1 
ATOM   3581 H HG22 . THR   A 1 149 ? 26.466 -17.431 9.845   1.00 17.55 ?  149 THR   A HG22 1 
ATOM   3582 H HG23 . THR   A 1 149 ? 26.410 -17.156 8.291   1.00 17.55 ?  149 THR   A HG23 1 
ATOM   3583 N N    . ASN   A 1 150 ? 22.470 -15.645 10.831  1.00 13.20 ?  150 ASN   A N    1 
ATOM   3584 C CA   . ASN   A 1 150 ? 21.194 -15.141 11.340  1.00 14.05 ?  150 ASN   A CA   1 
ATOM   3585 C C    . ASN   A 1 150 ? 21.012 -13.699 10.892  1.00 13.09 ?  150 ASN   A C    1 
ATOM   3586 O O    . ASN   A 1 150 ? 21.748 -12.808 11.325  1.00 15.03 ?  150 ASN   A O    1 
ATOM   3587 C CB   . ASN   A 1 150 ? 21.155 -15.255 12.859  1.00 16.35 ?  150 ASN   A CB   1 
ATOM   3588 C CG   . ASN   A 1 150 ? 21.054 -16.683 13.320  1.00 20.25 ?  150 ASN   A CG   1 
ATOM   3589 O OD1  . ASN   A 1 150 ? 20.435 -17.509 12.651  1.00 21.44 ?  150 ASN   A OD1  1 
ATOM   3590 N ND2  . ASN   A 1 150 ? 21.681 -16.994 14.451  1.00 22.58 ?  150 ASN   A ND2  1 
ATOM   3591 H H    . ASN   A 1 150 ? 23.128 -15.558 11.374  1.00 15.89 ?  150 ASN   A H    1 
ATOM   3592 H HA   . ASN   A 1 150 ? 20.470 -15.675 10.976  1.00 16.91 ?  150 ASN   A HA   1 
ATOM   3593 H HB2  . ASN   A 1 150 ? 21.968 -14.878 13.229  1.00 19.67 ?  150 ASN   A HB2  1 
ATOM   3594 H HB3  . ASN   A 1 150 ? 20.381 -14.778 13.193  1.00 19.67 ?  150 ASN   A HB3  1 
ATOM   3595 H HD21 . ASN   A 1 150 ? 21.652 -17.801 14.759  1.00 27.16 ?  150 ASN   A HD21 1 
ATOM   3596 H HD22 . ASN   A 1 150 ? 22.111 -16.390 14.888  1.00 27.16 ?  150 ASN   A HD22 1 
ATOM   3597 N N    . VAL   A 1 151 ? 20.016 -13.461 10.045  1.00 12.88 ?  151 VAL   A N    1 
ATOM   3598 C CA   . VAL   A 1 151 ? 19.802 -12.145 9.468   1.00 13.48 ?  151 VAL   A CA   1 
ATOM   3599 C C    . VAL   A 1 151 ? 18.418 -11.635 9.844   1.00 13.19 ?  151 VAL   A C    1 
ATOM   3600 O O    . VAL   A 1 151 ? 17.410 -12.349 9.707   1.00 13.99 ?  151 VAL   A O    1 
ATOM   3601 C CB   . VAL   A 1 151 ? 20.082 -12.117 7.951   1.00 14.34 ?  151 VAL   A CB   1 
ATOM   3602 C CG1  . VAL   A 1 151 ? 19.235 -13.120 7.194   1.00 15.04 ?  151 VAL   A CG1  1 
ATOM   3603 C CG2  . VAL   A 1 151 ? 19.901 -10.716 7.398   1.00 14.58 ?  151 VAL   A CG2  1 
ATOM   3604 H H    . VAL   A 1 151 ? 19.452 -14.055 9.783   1.00 15.51 ?  151 VAL   A H    1 
ATOM   3605 H HA   . VAL   A 1 151 ? 20.445 -11.538 9.872   1.00 16.23 ?  151 VAL   A HA   1 
ATOM   3606 H HB   . VAL   A 1 151 ? 21.015 -12.359 7.806   1.00 17.26 ?  151 VAL   A HB   1 
ATOM   3607 H HG11 . VAL   A 1 151 ? 19.437 -13.057 6.245   1.00 18.10 ?  151 VAL   A HG11 1 
ATOM   3608 H HG12 . VAL   A 1 151 ? 19.440 -14.014 7.514   1.00 18.10 ?  151 VAL   A HG12 1 
ATOM   3609 H HG13 . VAL   A 1 151 ? 18.298 -12.922 7.345   1.00 18.10 ?  151 VAL   A HG13 1 
ATOM   3610 H HG21 . VAL   A 1 151 ? 20.220 -10.694 6.480   1.00 17.55 ?  151 VAL   A HG21 1 
ATOM   3611 H HG22 . VAL   A 1 151 ? 18.962 -10.482 7.426   1.00 17.55 ?  151 VAL   A HG22 1 
ATOM   3612 H HG23 . VAL   A 1 151 ? 20.415 -10.092 7.937   1.00 17.55 ?  151 VAL   A HG23 1 
ATOM   3613 N N    . TYR   A 1 152 ? 18.405 -10.385 10.327  1.00 13.10 ?  152 TYR   A N    1 
ATOM   3614 C CA   . TYR   A 1 152 ? 17.217 -9.656  10.739  1.00 13.00 ?  152 TYR   A CA   1 
ATOM   3615 C C    . TYR   A 1 152 ? 17.008 -8.545  9.721   1.00 12.58 ?  152 TYR   A C    1 
ATOM   3616 O O    . TYR   A 1 152 ? 17.773 -7.573  9.686   1.00 13.09 ?  152 TYR   A O    1 
ATOM   3617 C CB   . TYR   A 1 152 ? 17.413 -9.126  12.159  1.00 13.47 ?  152 TYR   A CB   1 
ATOM   3618 C CG   . TYR   A 1 152 ? 17.379 -10.263 13.154  1.00 14.44 ?  152 TYR   A CG   1 
ATOM   3619 C CD1  . TYR   A 1 152 ? 18.504 -11.042 13.404  1.00 15.66 ?  152 TYR   A CD1  1 
ATOM   3620 C CD2  . TYR   A 1 152 ? 16.197 -10.605 13.797  1.00 14.67 ?  152 TYR   A CD2  1 
ATOM   3621 C CE1  . TYR   A 1 152 ? 18.463 -12.110 14.285  1.00 16.72 ?  152 TYR   A CE1  1 
ATOM   3622 C CE2  . TYR   A 1 152 ? 16.142 -11.674 14.681  1.00 15.79 ?  152 TYR   A CE2  1 
ATOM   3623 C CZ   . TYR   A 1 152 ? 17.279 -12.420 14.922  1.00 16.60 ?  152 TYR   A CZ   1 
ATOM   3624 O OH   . TYR   A 1 152 ? 17.218 -13.488 15.796  1.00 18.08 ?  152 TYR   A OH   1 
ATOM   3625 H H    . TYR   A 1 152 ? 19.126 -9.916  10.420  1.00 15.78 ?  152 TYR   A H    1 
ATOM   3626 H HA   . TYR   A 1 152 ? 16.451 -10.251 10.725  1.00 15.66 ?  152 TYR   A HA   1 
ATOM   3627 H HB2  . TYR   A 1 152 ? 18.274 -8.691  12.226  1.00 16.23 ?  152 TYR   A HB2  1 
ATOM   3628 H HB3  . TYR   A 1 152 ? 16.699 -8.508  12.373  1.00 16.23 ?  152 TYR   A HB3  1 
ATOM   3629 H HD1  . TYR   A 1 152 ? 19.299 -10.835 12.971  1.00 18.85 ?  152 TYR   A HD1  1 
ATOM   3630 H HD2  . TYR   A 1 152 ? 15.425 -10.106 13.638  1.00 17.66 ?  152 TYR   A HD2  1 
ATOM   3631 H HE1  . TYR   A 1 152 ? 19.228 -12.611 14.448  1.00 20.12 ?  152 TYR   A HE1  1 
ATOM   3632 H HE2  . TYR   A 1 152 ? 15.345 -11.882 15.117  1.00 19.00 ?  152 TYR   A HE2  1 
ATOM   3633 H HH   . TYR   A 1 152 ? 16.441 -13.550 16.117  1.00 21.75 ?  152 TYR   A HH   1 
ATOM   3634 N N    A LEU   A 1 153 ? 15.979 -8.709  8.880   0.40 12.41 ?  153 LEU   A N    1 
ATOM   3635 N N    B LEU   A 1 153 ? 15.980 -8.694  8.901   0.60 12.84 ?  153 LEU   A N    1 
ATOM   3636 C CA   A LEU   A 1 153 ? 15.733 -7.858  7.716   0.40 12.02 ?  153 LEU   A CA   1 
ATOM   3637 C CA   B LEU   A 1 153 ? 15.680 -7.717  7.872   0.60 12.61 ?  153 LEU   A CA   1 
ATOM   3638 C C    A LEU   A 1 153 ? 14.703 -6.780  8.037   0.40 11.73 ?  153 LEU   A C    1 
ATOM   3639 C C    B LEU   A 1 153 ? 14.727 -6.662  8.415   0.60 13.17 ?  153 LEU   A C    1 
ATOM   3640 O O    A LEU   A 1 153 ? 13.604 -7.086  8.511   0.40 12.35 ?  153 LEU   A O    1 
ATOM   3641 O O    B LEU   A 1 153 ? 13.662 -6.987  8.956   0.60 13.88 ?  153 LEU   A O    1 
ATOM   3642 C CB   A LEU   A 1 153 ? 15.221 -8.692  6.537   0.40 12.01 ?  153 LEU   A CB   1 
ATOM   3643 C CB   B LEU   A 1 153 ? 15.062 -8.408  6.660   0.60 12.10 ?  153 LEU   A CB   1 
ATOM   3644 C CG   A LEU   A 1 153 ? 16.177 -9.701  5.896   0.40 12.15 ?  153 LEU   A CG   1 
ATOM   3645 C CG   B LEU   A 1 153 ? 15.963 -9.442  5.981   0.60 11.60 ?  153 LEU   A CG   1 
ATOM   3646 C CD1  A LEU   A 1 153 ? 15.424 -10.613 4.932   0.40 12.65 ?  153 LEU   A CD1  1 
ATOM   3647 C CD1  B LEU   A 1 153 ? 15.145 -10.290 5.033   0.60 11.92 ?  153 LEU   A CD1  1 
ATOM   3648 C CD2  A LEU   A 1 153 ? 17.322 -8.991  5.178   0.40 12.63 ?  153 LEU   A CD2  1 
ATOM   3649 C CD2  B LEU   A 1 153 ? 17.107 -8.749  5.242   0.60 12.52 ?  153 LEU   A CD2  1 
ATOM   3650 H H    A LEU   A 1 153 ? 15.387 -9.334  8.970   0.40 14.95 ?  153 LEU   A H    1 
ATOM   3651 H H    B LEU   A 1 153 ? 15.432 -9.361  8.922   0.60 15.46 ?  153 LEU   A H    1 
ATOM   3652 H HA   A LEU   A 1 153 ? 16.558 -7.431  7.452   0.40 14.49 ?  153 LEU   A HA   1 
ATOM   3653 H HA   B LEU   A 1 153 ? 16.502 -7.282  7.601   0.60 15.19 ?  153 LEU   A HA   1 
ATOM   3654 H HB2  A LEU   A 1 153 ? 14.451 -9.195  6.834   0.40 14.46 ?  153 LEU   A HB2  1 
ATOM   3655 H HB2  B LEU   A 1 153 ? 14.256 -8.857  6.945   0.60 14.58 ?  153 LEU   A HB2  1 
ATOM   3656 H HB3  A LEU   A 1 153 ? 14.953 -8.084  5.831   0.40 14.46 ?  153 LEU   A HB3  1 
ATOM   3657 H HB3  B LEU   A 1 153 ? 14.845 -7.725  6.004   0.60 14.58 ?  153 LEU   A HB3  1 
ATOM   3658 H HG   A LEU   A 1 153 ? 16.564 -10.258 6.590   0.40 14.64 ?  153 LEU   A HG   1 
ATOM   3659 H HG   B LEU   A 1 153 ? 16.351 -10.016 6.660   0.60 13.98 ?  153 LEU   A HG   1 
ATOM   3660 H HD11 A LEU   A 1 153 ? 15.957 -11.408 4.767   0.40 15.24 ?  153 LEU   A HD11 1 
ATOM   3661 H HD11 B LEU   A 1 153 ? 15.734 -10.933 4.608   0.60 14.36 ?  153 LEU   A HD11 1 
ATOM   3662 H HD12 A LEU   A 1 153 ? 14.579 -10.863 5.332   0.40 15.24 ?  153 LEU   A HD12 1 
ATOM   3663 H HD12 B LEU   A 1 153 ? 14.460 -10.749 5.539   0.60 14.36 ?  153 LEU   A HD12 1 
ATOM   3664 H HD13 A LEU   A 1 153 ? 15.272 -10.138 4.101   0.40 15.24 ?  153 LEU   A HD13 1 
ATOM   3665 H HD13 B LEU   A 1 153 ? 14.743 -9.715  4.366   0.60 14.36 ?  153 LEU   A HD13 1 
ATOM   3666 H HD21 A LEU   A 1 153 ? 17.965 -9.651  4.876   0.40 15.22 ?  153 LEU   A HD21 1 
ATOM   3667 H HD21 B LEU   A 1 153 ? 17.636 -9.424  4.785   0.60 15.08 ?  153 LEU   A HD21 1 
ATOM   3668 H HD22 A LEU   A 1 153 ? 16.965 -8.505  4.419   0.40 15.22 ?  153 LEU   A HD22 1 
ATOM   3669 H HD22 B LEU   A 1 153 ? 16.738 -8.127  4.598   0.60 15.08 ?  153 LEU   A HD22 1 
ATOM   3670 H HD23 A LEU   A 1 153 ? 17.748 -8.377  5.795   0.40 15.22 ?  153 LEU   A HD23 1 
ATOM   3671 H HD23 B LEU   A 1 153 ? 17.662 -8.274  5.881   0.60 15.08 ?  153 LEU   A HD23 1 
ATOM   3672 N N    A ALA   A 1 154 ? 15.045 -5.528  7.735   0.40 10.67 ?  154 ALA   A N    1 
ATOM   3673 N N    B ALA   A 1 154 ? 15.118 -5.398  8.265   0.60 12.53 ?  154 ALA   A N    1 
ATOM   3674 C CA   A ALA   A 1 154 ? 14.180 -4.379  7.983   0.40 11.01 ?  154 ALA   A CA   1 
ATOM   3675 C CA   B ALA   A 1 154 ? 14.270 -4.256  8.571   0.60 12.60 ?  154 ALA   A CA   1 
ATOM   3676 C C    A ALA   A 1 154 ? 13.658 -3.825  6.662   0.40 11.25 ?  154 ALA   A C    1 
ATOM   3677 C C    B ALA   A 1 154 ? 13.761 -3.696  7.250   0.60 12.42 ?  154 ALA   A C    1 
ATOM   3678 O O    A ALA   A 1 154 ? 14.442 -3.393  5.807   0.40 11.59 ?  154 ALA   A O    1 
ATOM   3679 O O    B ALA   A 1 154 ? 14.557 -3.255  6.414   0.60 12.22 ?  154 ALA   A O    1 
ATOM   3680 C CB   A ALA   A 1 154 ? 14.932 -3.287  8.743   0.40 11.49 ?  154 ALA   A CB   1 
ATOM   3681 C CB   B ALA   A 1 154 ? 15.056 -3.191  9.336   0.60 13.09 ?  154 ALA   A CB   1 
ATOM   3682 H H    A ALA   A 1 154 ? 15.801 -5.320  7.390   0.40 12.86 ?  154 ALA   A H    1 
ATOM   3683 H H    B ALA   A 1 154 ? 15.898 -5.164  7.974   0.60 15.09 ?  154 ALA   A H    1 
ATOM   3684 H HA   A ALA   A 1 154 ? 13.423 -4.659  8.523   0.40 13.27 ?  154 ALA   A HA   1 
ATOM   3685 H HA   B ALA   A 1 154 ? 13.513 -4.530  9.109   0.60 15.18 ?  154 ALA   A HA   1 
ATOM   3686 H HB1  A ALA   A 1 154 ? 14.333 -2.541  8.893   0.40 13.85 ?  154 ALA   A HB1  1 
ATOM   3687 H HB1  B ALA   A 1 154 ? 14.476 -2.437  9.528   0.60 15.76 ?  154 ALA   A HB1  1 
ATOM   3688 H HB2  A ALA   A 1 154 ? 15.237 -3.643  9.594   0.40 13.85 ?  154 ALA   A HB2  1 
ATOM   3689 H HB2  B ALA   A 1 154 ? 15.386 -3.573  10.165  0.60 15.76 ?  154 ALA   A HB2  1 
ATOM   3690 H HB3  A ALA   A 1 154 ? 15.693 -3.002  8.214   0.40 13.85 ?  154 ALA   A HB3  1 
ATOM   3691 H HB3  B ALA   A 1 154 ? 15.807 -2.895  8.791   0.60 15.76 ?  154 ALA   A HB3  1 
ATOM   3692 N N    A VAL   A 1 155 ? 12.336 -3.833  6.509   0.40 12.15 ?  155 VAL   A N    1 
ATOM   3693 N N    B VAL   A 1 155 ? 12.445 -3.728  7.057   0.60 13.72 ?  155 VAL   A N    1 
ATOM   3694 C CA   A VAL   A 1 155 ? 11.656 -3.322  5.325   0.40 13.14 ?  155 VAL   A CA   1 
ATOM   3695 C CA   B VAL   A 1 155 ? 11.802 -3.277  5.827   0.60 15.27 ?  155 VAL   A CA   1 
ATOM   3696 C C    A VAL   A 1 155 ? 10.914 -2.054  5.726   0.40 14.38 ?  155 VAL   A C    1 
ATOM   3697 C C    B VAL   A 1 155 ? 10.949 -2.069  6.187   0.60 17.21 ?  155 VAL   A C    1 
ATOM   3698 O O    A VAL   A 1 155 ? 9.996  -2.098  6.553   0.40 15.28 ?  155 VAL   A O    1 
ATOM   3699 O O    B VAL   A 1 155 ? 9.915  -2.209  6.855   0.60 18.43 ?  155 VAL   A O    1 
ATOM   3700 C CB   A VAL   A 1 155 ? 10.687 -4.362  4.743   0.40 13.27 ?  155 VAL   A CB   1 
ATOM   3701 C CB   B VAL   A 1 155 ? 10.950 -4.381  5.184   0.60 16.03 ?  155 VAL   A CB   1 
ATOM   3702 C CG1  A VAL   A 1 155 ? 10.001 -3.802  3.506   0.40 13.94 ?  155 VAL   A CG1  1 
ATOM   3703 C CG1  B VAL   A 1 155 ? 10.180 -3.828  3.989   0.60 16.99 ?  155 VAL   A CG1  1 
ATOM   3704 C CG2  A VAL   A 1 155 ? 11.424 -5.652  4.422   0.40 13.61 ?  155 VAL   A CG2  1 
ATOM   3705 C CG2  B VAL   A 1 155 ? 11.834 -5.550  4.761   0.60 16.31 ?  155 VAL   A CG2  1 
ATOM   3706 H H    A VAL   A 1 155 ? 11.799 -4.156  7.099   0.40 14.64 ?  155 VAL   A H    1 
ATOM   3707 H H    B VAL   A 1 155 ? 11.888 -4.010  7.645   0.60 16.52 ?  155 VAL   A H    1 
ATOM   3708 H HA   A VAL   A 1 155 ? 12.313 -3.096  4.649   0.40 15.82 ?  155 VAL   A HA   1 
ATOM   3709 H HA   B VAL   A 1 155 ? 12.476 -2.993  5.188   0.60 18.39 ?  155 VAL   A HA   1 
ATOM   3710 H HB   A VAL   A 1 155 ? 10.004 -4.559  5.406   0.40 15.98 ?  155 VAL   A HB   1 
ATOM   3711 H HB   B VAL   A 1 155 ? 10.308 -4.701  5.835   0.60 19.29 ?  155 VAL   A HB   1 
ATOM   3712 H HG11 A VAL   A 1 155 ? 9.518  -4.516  3.067   0.40 16.78 ?  155 VAL   A HG11 1 
ATOM   3713 H HG11 B VAL   A 1 155 ? 9.838  -4.568  3.465   0.60 20.44 ?  155 VAL   A HG11 1 
ATOM   3714 H HG12 A VAL   A 1 155 ? 9.382  -3.102  3.776   0.40 16.78 ?  155 VAL   A HG12 1 
ATOM   3715 H HG12 B VAL   A 1 155 ? 9.440  -3.282  4.307   0.60 20.44 ?  155 VAL   A HG12 1 
ATOM   3716 H HG13 A VAL   A 1 155 ? 10.673 -3.438  2.911   0.40 16.78 ?  155 VAL   A HG13 1 
ATOM   3717 H HG13 B VAL   A 1 155 ? 10.777 -3.288  3.447   0.60 20.44 ?  155 VAL   A HG13 1 
ATOM   3718 H HG21 A VAL   A 1 155 ? 10.810 -6.260  3.986   0.40 16.39 ?  155 VAL   A HG21 1 
ATOM   3719 H HG21 B VAL   A 1 155 ? 11.280 -6.222  4.337   0.60 19.63 ?  155 VAL   A HG21 1 
ATOM   3720 H HG22 A VAL   A 1 155 ? 12.167 -5.448  3.835   0.40 16.39 ?  155 VAL   A HG22 1 
ATOM   3721 H HG22 B VAL   A 1 155 ? 12.502 -5.227  4.136   0.60 19.63 ?  155 VAL   A HG22 1 
ATOM   3722 H HG23 A VAL   A 1 155 ? 11.750 -6.042  5.248   0.40 16.39 ?  155 VAL   A HG23 1 
ATOM   3723 H HG23 B VAL   A 1 155 ? 12.264 -5.918  5.547   0.60 19.63 ?  155 VAL   A HG23 1 
ATOM   3724 N N    A PHE   A 1 156 ? 11.291 -0.929  5.116   0.40 15.18 ?  156 PHE   A N    1 
ATOM   3725 N N    B PHE   A 1 156 ? 11.375 -0.885  5.745   0.60 17.87 ?  156 PHE   A N    1 
ATOM   3726 C CA   A PHE   A 1 156 ? 10.775 0.371   5.546   0.40 16.57 ?  156 PHE   A CA   1 
ATOM   3727 C CA   B PHE   A 1 156 ? 10.723 0.366   6.135   0.60 19.64 ?  156 PHE   A CA   1 
ATOM   3728 C C    A PHE   A 1 156 ? 9.318  0.566   5.142   0.40 16.67 ?  156 PHE   A C    1 
ATOM   3729 C C    B PHE   A 1 156 ? 9.626  0.758   5.142   0.60 20.53 ?  156 PHE   A C    1 
ATOM   3730 O O    A PHE   A 1 156 ? 8.547  1.203   5.869   0.40 17.87 ?  156 PHE   A O    1 
ATOM   3731 O O    B PHE   A 1 156 ? 9.646  1.817   4.510   0.60 20.76 ?  156 PHE   A O    1 
ATOM   3732 C CB   A PHE   A 1 156 ? 11.652 1.479   4.954   0.40 17.78 ?  156 PHE   A CB   1 
ATOM   3733 C CB   B PHE   A 1 156 ? 11.764 1.470   6.280   0.60 21.08 ?  156 PHE   A CB   1 
ATOM   3734 C CG   A PHE   A 1 156 ? 11.185 2.877   5.272   0.40 19.26 ?  156 PHE   A CG   1 
ATOM   3735 C CG   B PHE   A 1 156 ? 11.288 2.653   7.067   0.60 22.56 ?  156 PHE   A CG   1 
ATOM   3736 C CD1  A PHE   A 1 156 ? 11.140 3.327   6.581   0.40 19.76 ?  156 PHE   A CD1  1 
ATOM   3737 C CD1  B PHE   A 1 156 ? 10.186 2.558   7.908   0.60 23.31 ?  156 PHE   A CD1  1 
ATOM   3738 C CD2  A PHE   A 1 156 ? 10.823 3.752   4.255   0.40 20.15 ?  156 PHE   A CD2  1 
ATOM   3739 C CD2  B PHE   A 1 156 ? 11.939 3.866   6.962   0.60 22.88 ?  156 PHE   A CD2  1 
ATOM   3740 C CE1  A PHE   A 1 156 ? 10.722 4.614   6.874   0.40 20.38 ?  156 PHE   A CE1  1 
ATOM   3741 C CE1  B PHE   A 1 156 ? 9.752  3.645   8.629   0.60 23.85 ?  156 PHE   A CE1  1 
ATOM   3742 C CE2  A PHE   A 1 156 ? 10.403 5.039   4.542   0.40 20.64 ?  156 PHE   A CE2  1 
ATOM   3743 C CE2  B PHE   A 1 156 ? 11.505 4.961   7.682   0.60 23.48 ?  156 PHE   A CE2  1 
ATOM   3744 C CZ   A PHE   A 1 156 ? 10.356 5.471   5.853   0.40 20.62 ?  156 PHE   A CZ   1 
ATOM   3745 C CZ   B PHE   A 1 156 ? 10.410 4.848   8.516   0.60 23.77 ?  156 PHE   A CZ   1 
ATOM   3746 H H    A PHE   A 1 156 ? 11.836 -0.894  4.454   0.40 18.28 ?  156 PHE   A H    1 
ATOM   3747 H H    B PHE   A 1 156 ? 12.059 -0.769  5.231   0.60 21.51 ?  156 PHE   A H    1 
ATOM   3748 H HA   A PHE   A 1 156 ? 10.831 0.431   6.512   0.40 19.94 ?  156 PHE   A HA   1 
ATOM   3749 H HA   B PHE   A 1 156 ? 10.309 0.210   6.993   0.60 23.62 ?  156 PHE   A HA   1 
ATOM   3750 H HB2  A PHE   A 1 156 ? 12.553 1.384   5.301   0.40 21.39 ?  156 PHE   A HB2  1 
ATOM   3751 H HB2  B PHE   A 1 156 ? 12.544 1.116   6.735   0.60 25.36 ?  156 PHE   A HB2  1 
ATOM   3752 H HB3  A PHE   A 1 156 ? 11.664 1.386   3.988   0.40 21.39 ?  156 PHE   A HB3  1 
ATOM   3753 H HB3  B PHE   A 1 156 ? 12.018 1.790   5.398   0.60 25.36 ?  156 PHE   A HB3  1 
ATOM   3754 H HD1  A PHE   A 1 156 ? 11.385 2.753   7.271   0.40 23.77 ?  156 PHE   A HD1  1 
ATOM   3755 H HD1  B PHE   A 1 156 ? 9.738  1.746   7.992   0.60 28.02 ?  156 PHE   A HD1  1 
ATOM   3756 H HD2  A PHE   A 1 156 ? 10.854 3.464   3.371   0.40 24.23 ?  156 PHE   A HD2  1 
ATOM   3757 H HD2  B PHE   A 1 156 ? 12.676 3.950   6.403   0.60 27.51 ?  156 PHE   A HD2  1 
ATOM   3758 H HE1  A PHE   A 1 156 ? 10.691 4.902   7.757   0.40 24.52 ?  156 PHE   A HE1  1 
ATOM   3759 H HE1  B PHE   A 1 156 ? 9.013  3.562   9.189   0.60 28.68 ?  156 PHE   A HE1  1 
ATOM   3760 H HE2  A PHE   A 1 156 ? 10.160 5.612   3.853   0.40 24.83 ?  156 PHE   A HE2  1 
ATOM   3761 H HE2  B PHE   A 1 156 ? 11.948 5.777   7.606   0.60 28.23 ?  156 PHE   A HE2  1 
ATOM   3762 H HZ   A PHE   A 1 156 ? 10.076 6.334   6.049   0.40 24.81 ?  156 PHE   A HZ   1 
ATOM   3763 H HZ   B PHE   A 1 156 ? 10.114 5.585   9.002   0.60 28.58 ?  156 PHE   A HZ   1 
ATOM   3764 N N    A ASP   A 1 157 ? 8.929  0.040   3.985   0.40 16.23 ?  157 ASP   A N    1 
ATOM   3765 N N    B ASP   A 1 157 ? 8.632  -0.118  5.052   0.60 20.95 ?  157 ASP   A N    1 
ATOM   3766 C CA   A ASP   A 1 157 ? 7.618  0.293   3.403   0.40 16.42 ?  157 ASP   A CA   1 
ATOM   3767 C CA   B ASP   A 1 157 ? 7.521  0.027   4.122   0.60 22.17 ?  157 ASP   A CA   1 
ATOM   3768 C C    A ASP   A 1 157 ? 6.635  -0.762  3.899   0.40 16.41 ?  157 ASP   A C    1 
ATOM   3769 C C    B ASP   A 1 157 ? 6.483  -1.022  4.495   0.60 22.56 ?  157 ASP   A C    1 
ATOM   3770 O O    A ASP   A 1 157 ? 6.841  -1.963  3.677   0.40 15.81 ?  157 ASP   A O    1 
ATOM   3771 O O    B ASP   A 1 157 ? 6.650  -2.201  4.165   0.60 22.25 ?  157 ASP   A O    1 
ATOM   3772 C CB   A ASP   A 1 157 ? 7.736  0.247   1.882   0.40 16.98 ?  157 ASP   A CB   1 
ATOM   3773 C CB   B ASP   A 1 157 ? 8.031  -0.180  2.691   0.60 22.50 ?  157 ASP   A CB   1 
ATOM   3774 C CG   A ASP   A 1 157 ? 6.497  0.752   1.184   0.40 17.92 ?  157 ASP   A CG   1 
ATOM   3775 C CG   B ASP   A 1 157 ? 6.979  0.089   1.631   0.60 22.55 ?  157 ASP   A CG   1 
ATOM   3776 O OD1  A ASP   A 1 157 ? 6.291  1.982   1.159   0.40 19.55 ?  157 ASP   A OD1  1 
ATOM   3777 O OD1  B ASP   A 1 157 ? 5.771  0.076   1.944   0.60 22.03 ?  157 ASP   A OD1  1 
ATOM   3778 O OD2  A ASP   A 1 157 ? 5.739  -0.084  0.650   0.40 17.86 -1 157 ASP   A OD2  1 
ATOM   3779 O OD2  B ASP   A 1 157 ? 7.373  0.295   0.463   0.60 23.15 -1 157 ASP   A OD2  1 
ATOM   3780 H H    A ASP   A 1 157 ? 9.423  -0.478  3.505   0.40 19.53 ?  157 ASP   A H    1 
ATOM   3781 H H    B ASP   A 1 157 ? 8.581  -0.823  5.539   0.60 25.20 ?  157 ASP   A H    1 
ATOM   3782 H HA   A ASP   A 1 157 ? 7.303  1.170   3.673   0.40 19.76 ?  157 ASP   A HA   1 
ATOM   3783 H HA   B ASP   A 1 157 ? 7.129  0.911   4.203   0.60 26.67 ?  157 ASP   A HA   1 
ATOM   3784 H HB2  A ASP   A 1 157 ? 8.484  0.802   1.609   0.40 20.43 ?  157 ASP   A HB2  1 
ATOM   3785 H HB2  B ASP   A 1 157 ? 8.770  0.420   2.531   0.60 27.06 ?  157 ASP   A HB2  1 
ATOM   3786 H HB3  A ASP   A 1 157 ? 7.882  -0.667  1.604   0.40 20.43 ?  157 ASP   A HB3  1 
ATOM   3787 H HB3  B ASP   A 1 157 ? 8.322  -1.097  2.592   0.60 27.06 ?  157 ASP   A HB3  1 
ATOM   3788 N N    A LYS   A 1 158 ? 5.572  -0.313  4.579   0.40 17.24 ?  158 LYS   A N    1 
ATOM   3789 N N    B LYS   A 1 158 ? 5.428  -0.618  5.210   0.60 23.43 ?  158 LYS   A N    1 
ATOM   3790 C CA   A LYS   A 1 158 ? 4.599  -1.249  5.136   0.40 17.70 ?  158 LYS   A CA   1 
ATOM   3791 C CA   B LYS   A 1 158 ? 4.481  -1.598  5.737   0.60 24.17 ?  158 LYS   A CA   1 
ATOM   3792 C C    A LYS   A 1 158 ? 3.911  -2.051  4.034   0.40 17.61 ?  158 LYS   A C    1 
ATOM   3793 C C    B LYS   A 1 158 ? 3.789  -2.356  4.611   0.60 23.78 ?  158 LYS   A C    1 
ATOM   3794 O O    A LYS   A 1 158 ? 3.712  -3.265  4.169   0.40 17.72 ?  158 LYS   A O    1 
ATOM   3795 O O    B LYS   A 1 158 ? 3.603  -3.575  4.697   0.60 23.57 ?  158 LYS   A O    1 
ATOM   3796 C CB   A LYS   A 1 158 ? 3.587  -0.487  6.000   0.40 18.62 ?  158 LYS   A CB   1 
ATOM   3797 C CB   B LYS   A 1 158 ? 3.466  -0.914  6.656   0.60 25.45 ?  158 LYS   A CB   1 
ATOM   3798 C CG   A LYS   A 1 158 ? 2.391  -1.309  6.476   0.40 20.36 ?  158 LYS   A CG   1 
ATOM   3799 C CG   B LYS   A 1 158 ? 2.354  -1.822  7.185   0.60 26.47 ?  158 LYS   A CG   1 
ATOM   3800 C CD   A LYS   A 1 158 ? 2.805  -2.510  7.315   0.40 21.86 ?  158 LYS   A CD   1 
ATOM   3801 C CD   B LYS   A 1 158 ? 2.886  -2.996  8.007   0.60 27.12 ?  158 LYS   A CD   1 
ATOM   3802 C CE   A LYS   A 1 158 ? 1.584  -3.231  7.873   0.40 22.90 ?  158 LYS   A CE   1 
ATOM   3803 C CE   B LYS   A 1 158 ? 1.748  -3.722  8.722   0.60 27.30 ?  158 LYS   A CE   1 
ATOM   3804 N NZ   A LYS   A 1 158 ? 1.926  -4.538  8.500   0.40 23.27 ?  158 LYS   A NZ   1 
ATOM   3805 N NZ   B LYS   A 1 158 ? 2.127  -5.093  9.166   0.60 27.60 ?  158 LYS   A NZ   1 
ATOM   3806 H H    A LYS   A 1 158 ? 5.406  0.517   4.739   0.40 20.75 ?  158 LYS   A H    1 
ATOM   3807 H H    B LYS   A 1 158 ? 5.247  0.199   5.398   0.60 28.17 ?  158 LYS   A H    1 
ATOM   3808 H HA   A LYS   A 1 158 ? 5.061  -1.872  5.718   0.40 21.29 ?  158 LYS   A HA   1 
ATOM   3809 H HA   B LYS   A 1 158 ? 4.969  -2.246  6.267   0.60 29.06 ?  158 LYS   A HA   1 
ATOM   3810 H HB2  A LYS   A 1 158 ? 4.040  -0.152  6.795   0.40 22.40 ?  158 LYS   A HB2  1 
ATOM   3811 H HB2  B LYS   A 1 158 ? 3.942  -0.557  7.424   0.60 30.59 ?  158 LYS   A HB2  1 
ATOM   3812 H HB3  A LYS   A 1 158 ? 3.240  0.262   5.492   0.40 22.40 ?  158 LYS   A HB3  1 
ATOM   3813 H HB3  B LYS   A 1 158 ? 3.047  -0.189  6.169   0.60 30.59 ?  158 LYS   A HB3  1 
ATOM   3814 H HG2  A LYS   A 1 158 ? 1.820  -0.748  7.025   0.40 24.49 ?  158 LYS   A HG2  1 
ATOM   3815 H HG2  B LYS   A 1 158 ? 1.770  -1.300  7.755   0.60 31.82 ?  158 LYS   A HG2  1 
ATOM   3816 H HG3  A LYS   A 1 158 ? 1.895  -1.632  5.709   0.40 24.49 ?  158 LYS   A HG3  1 
ATOM   3817 H HG3  B LYS   A 1 158 ? 1.852  -2.181  6.437   0.60 31.82 ?  158 LYS   A HG3  1 
ATOM   3818 H HD2  A LYS   A 1 158 ? 3.304  -3.133  6.764   0.40 26.28 ?  158 LYS   A HD2  1 
ATOM   3819 H HD2  B LYS   A 1 158 ? 3.331  -3.626  7.419   0.60 32.60 ?  158 LYS   A HD2  1 
ATOM   3820 H HD3  A LYS   A 1 158 ? 3.348  -2.210  8.062   0.40 26.28 ?  158 LYS   A HD3  1 
ATOM   3821 H HD3  B LYS   A 1 158 ? 3.508  -2.664  8.676   0.60 32.60 ?  158 LYS   A HD3  1 
ATOM   3822 H HE2  A LYS   A 1 158 ? 1.166  -2.674  8.549   0.40 27.54 ?  158 LYS   A HE2  1 
ATOM   3823 H HE2  B LYS   A 1 158 ? 1.493  -3.211  9.507   0.60 32.82 ?  158 LYS   A HE2  1 
ATOM   3824 H HE3  A LYS   A 1 158 ? 0.959  -3.400  7.151   0.40 27.54 ?  158 LYS   A HE3  1 
ATOM   3825 H HE3  B LYS   A 1 158 ? 0.994  -3.798  8.117   0.60 32.82 ?  158 LYS   A HE3  1 
ATOM   3826 H HZ1  A LYS   A 1 158 ? 1.190  -4.929  8.813   0.40 27.98 ?  158 LYS   A HZ1  1 
ATOM   3827 H HZ1  B LYS   A 1 158 ? 1.440  -5.478  9.581   0.60 33.18 ?  158 LYS   A HZ1  1 
ATOM   3828 H HZ2  A LYS   A 1 158 ? 2.303  -5.075  7.898   0.40 27.98 ?  158 LYS   A HZ2  1 
ATOM   3829 H HZ2  B LYS   A 1 158 ? 2.355  -5.587  8.462   0.60 33.18 ?  158 LYS   A HZ2  1 
ATOM   3830 H HZ3  A LYS   A 1 158 ? 2.495  -4.414  9.173   0.40 27.98 ?  158 LYS   A HZ3  1 
ATOM   3831 H HZ3  B LYS   A 1 158 ? 2.817  -5.050  9.726   0.60 33.18 ?  158 LYS   A HZ3  1 
ATOM   3832 N N    A ASN   A 1 159 ? 3.556  -1.396  2.927   0.40 18.14 ?  159 ASN   A N    1 
ATOM   3833 N N    B ASN   A 1 159 ? 3.410  -1.654  3.542   0.60 23.42 ?  159 ASN   A N    1 
ATOM   3834 C CA   A ASN   A 1 159 ? 2.867  -2.097  1.849   0.40 18.49 ?  159 ASN   A CA   1 
ATOM   3835 C CA   B ASN   A 1 159 ? 2.811  -2.320  2.390   0.60 23.26 ?  159 ASN   A CA   1 
ATOM   3836 C C    A ASN   A 1 159 ? 3.759  -3.162  1.207   0.40 17.43 ?  159 ASN   A C    1 
ATOM   3837 C C    B ASN   A 1 159 ? 3.761  -3.362  1.814   0.60 21.23 ?  159 ASN   A C    1 
ATOM   3838 O O    A ASN   A 1 159 ? 3.288  -4.255  0.867   0.40 17.65 ?  159 ASN   A O    1 
ATOM   3839 O O    B ASN   A 1 159 ? 3.360  -4.498  1.530   0.60 20.55 ?  159 ASN   A O    1 
ATOM   3840 C CB   A ASN   A 1 159 ? 2.354  -1.083  0.823   0.40 20.04 ?  159 ASN   A CB   1 
ATOM   3841 C CB   B ASN   A 1 159 ? 2.426  -1.281  1.335   0.60 25.04 ?  159 ASN   A CB   1 
ATOM   3842 C CG   A ASN   A 1 159 ? 1.199  -0.250  1.358   0.40 21.61 ?  159 ASN   A CG   1 
ATOM   3843 C CG   B ASN   A 1 159 ? 1.930  -1.912  0.046   0.60 26.49 ?  159 ASN   A CG   1 
ATOM   3844 O OD1  A ASN   A 1 159 ? 0.370  -0.750  2.114   0.40 22.07 ?  159 ASN   A OD1  1 
ATOM   3845 O OD1  B ASN   A 1 159 ? 2.664  -2.005  -0.938  0.60 27.37 ?  159 ASN   A OD1  1 
ATOM   3846 N ND2  A ASN   A 1 159 ? 1.142  1.024   0.970   0.40 22.28 ?  159 ASN   A ND2  1 
ATOM   3847 N ND2  B ASN   A 1 159 ? 0.680  -2.348  0.045   0.60 27.11 ?  159 ASN   A ND2  1 
ATOM   3848 H H    A ASN   A 1 159 ? 3.712  -0.561  2.783   0.40 21.83 ?  159 ASN   A H    1 
ATOM   3849 H H    B ASN   A 1 159 ? 3.493  -0.803  3.458   0.60 28.16 ?  159 ASN   A H    1 
ATOM   3850 H HA   A ASN   A 1 159 ? 2.095  -2.545  2.228   0.40 22.24 ?  159 ASN   A HA   1 
ATOM   3851 H HA   B ASN   A 1 159 ? 2.007  -2.778  2.668   0.60 27.97 ?  159 ASN   A HA   1 
ATOM   3852 H HB2  A ASN   A 1 159 ? 3.067  -0.475  0.585   0.40 24.10 ?  159 ASN   A HB2  1 
ATOM   3853 H HB2  B ASN   A 1 159 ? 1.712  -0.725  1.689   0.60 30.10 ?  159 ASN   A HB2  1 
ATOM   3854 H HB3  A ASN   A 1 159 ? 2.036  -1.556  0.042   0.40 24.10 ?  159 ASN   A HB3  1 
ATOM   3855 H HB3  B ASN   A 1 159 ? 3.200  -0.735  1.128   0.60 30.10 ?  159 ASN   A HB3  1 
ATOM   3856 H HD21 A ASN   A 1 159 ? 0.505  1.537   1.247   0.40 26.80 ?  159 ASN   A HD21 1 
ATOM   3857 H HD21 B ASN   A 1 159 ? 0.358  -2.714  -0.661  0.60 32.59 ?  159 ASN   A HD21 1 
ATOM   3858 H HD22 A ASN   A 1 159 ? 1.742  1.337   0.443   0.40 26.80 ?  159 ASN   A HD22 1 
ATOM   3859 H HD22 B ASN   A 1 159 ? 0.196  -2.264  0.750   0.60 32.59 ?  159 ASN   A HD22 1 
ATOM   3860 N N    A LEU   A 1 160 ? 5.050  -2.870  1.044   0.40 16.32 ?  160 LEU   A N    1 
ATOM   3861 N N    B LEU   A 1 160 ? 5.035  -2.996  1.651   0.60 20.07 ?  160 LEU   A N    1 
ATOM   3862 C CA   A LEU   A 1 160 ? 5.967  -3.858  0.481   0.40 15.11 ?  160 LEU   A CA   1 
ATOM   3863 C CA   B LEU   A 1 160 ? 6.017  -3.958  1.167   0.60 18.68 ?  160 LEU   A CA   1 
ATOM   3864 C C    A LEU   A 1 160 ? 6.179  -5.025  1.439   0.40 13.90 ?  160 LEU   A C    1 
ATOM   3865 C C    B LEU   A 1 160 ? 6.222  -5.082  2.175   0.60 17.47 ?  160 LEU   A C    1 
ATOM   3866 O O    A LEU   A 1 160 ? 6.242  -6.185  1.011   0.40 14.20 ?  160 LEU   A O    1 
ATOM   3867 O O    B LEU   A 1 160 ? 6.246  -6.262  1.805   0.60 17.40 ?  160 LEU   A O    1 
ATOM   3868 C CB   A LEU   A 1 160 ? 7.301  -3.194  0.152   0.40 15.20 ?  160 LEU   A CB   1 
ATOM   3869 C CB   B LEU   A 1 160 ? 7.342  -3.254  0.871   0.60 18.84 ?  160 LEU   A CB   1 
ATOM   3870 C CG   A LEU   A 1 160 ? 8.419  -4.155  -0.239  0.40 15.29 ?  160 LEU   A CG   1 
ATOM   3871 C CG   B LEU   A 1 160 ? 8.444  -4.184  0.365   0.60 18.27 ?  160 LEU   A CG   1 
ATOM   3872 C CD1  A LEU   A 1 160 ? 7.994  -4.943  -1.456  0.40 15.86 ?  160 LEU   A CD1  1 
ATOM   3873 C CD1  B LEU   A 1 160 ? 8.023  -4.837  -0.937  0.60 18.90 ?  160 LEU   A CD1  1 
ATOM   3874 C CD2  A LEU   A 1 160 ? 9.712  -3.403  -0.496  0.40 15.23 ?  160 LEU   A CD2  1 
ATOM   3875 C CD2  B LEU   A 1 160 ? 9.737  -3.417  0.187   0.60 17.56 ?  160 LEU   A CD2  1 
ATOM   3876 H H    A LEU   A 1 160 ? 5.413  -2.119  1.259   0.40 19.64 ?  160 LEU   A H    1 
ATOM   3877 H H    B LEU   A 1 160 ? 5.353  -2.211  1.815   0.60 24.15 ?  160 LEU   A H    1 
ATOM   3878 H HA   A LEU   A 1 160 ? 5.585  -4.206  -0.337  0.40 18.19 ?  160 LEU   A HA   1 
ATOM   3879 H HA   B LEU   A 1 160 ? 5.699  -4.344  0.338   0.60 22.47 ?  160 LEU   A HA   1 
ATOM   3880 H HB2  A LEU   A 1 160 ? 7.164  -2.579  -0.584  0.40 18.30 ?  160 LEU   A HB2  1 
ATOM   3881 H HB2  B LEU   A 1 160 ? 7.201  -2.565  0.194   0.60 22.66 ?  160 LEU   A HB2  1 
ATOM   3882 H HB3  A LEU   A 1 160 ? 7.596  -2.705  0.936   0.40 18.30 ?  160 LEU   A HB3  1 
ATOM   3883 H HB3  B LEU   A 1 160 ? 7.664  -2.845  1.686   0.60 22.66 ?  160 LEU   A HB3  1 
ATOM   3884 H HG   A LEU   A 1 160 ? 8.578  -4.777  0.490   0.40 18.40 ?  160 LEU   A HG   1 
ATOM   3885 H HG   B LEU   A 1 160 ? 8.600  -4.884  1.018   0.60 21.98 ?  160 LEU   A HG   1 
ATOM   3886 H HD11 A LEU   A 1 160 ? 8.732  -5.495  -1.739  0.40 19.09 ?  160 LEU   A HD11 1 
ATOM   3887 H HD11 B LEU   A 1 160 ? 8.774  -5.323  -1.302  0.60 22.74 ?  160 LEU   A HD11 1 
ATOM   3888 H HD12 A LEU   A 1 160 ? 7.233  -5.500  -1.223  0.40 19.09 ?  160 LEU   A HD12 1 
ATOM   3889 H HD12 B LEU   A 1 160 ? 7.288  -5.448  -0.764  0.60 22.74 ?  160 LEU   A HD12 1 
ATOM   3890 H HD13 A LEU   A 1 160 ? 7.747  -4.322  -2.158  0.40 19.09 ?  160 LEU   A HD13 1 
ATOM   3891 H HD13 B LEU   A 1 160 ? 7.739  -4.146  -1.559  0.60 22.74 ?  160 LEU   A HD13 1 
ATOM   3892 H HD21 A LEU   A 1 160 ? 10.402 -4.039  -0.738  0.40 18.33 ?  160 LEU   A HD21 1 
ATOM   3893 H HD21 B LEU   A 1 160 ? 10.431 -4.031  -0.097  0.60 21.13 ?  160 LEU   A HD21 1 
ATOM   3894 H HD22 A LEU   A 1 160 ? 9.571  -2.772  -1.218  0.40 18.33 ?  160 LEU   A HD22 1 
ATOM   3895 H HD22 B LEU   A 1 160 ? 9.605  -2.730  -0.485  0.60 21.13 ?  160 LEU   A HD22 1 
ATOM   3896 H HD23 A LEU   A 1 160 ? 9.969  -2.928  0.312   0.40 18.33 ?  160 LEU   A HD23 1 
ATOM   3897 H HD23 B LEU   A 1 160 ? 9.978  -3.010  1.034   0.60 21.13 ?  160 LEU   A HD23 1 
ATOM   3898 N N    A TYR   A 1 161 ? 6.297  -4.733  2.735   0.40 14.01 ?  161 TYR   A N    1 
ATOM   3899 N N    B TYR   A 1 161 ? 6.356  -4.735  3.458   0.60 17.56 ?  161 TYR   A N    1 
ATOM   3900 C CA   A TYR   A 1 161 ? 6.453  -5.788  3.729   0.40 14.02 ?  161 TYR   A CA   1 
ATOM   3901 C CA   B TYR   A 1 161 ? 6.520  -5.754  4.489   0.60 17.38 ?  161 TYR   A CA   1 
ATOM   3902 C C    A TYR   A 1 161 ? 5.304  -6.785  3.654   0.40 14.27 ?  161 TYR   A C    1 
ATOM   3903 C C    B TYR   A 1 161 ? 5.393  -6.778  4.426   0.60 17.77 ?  161 TYR   A C    1 
ATOM   3904 O O    A TYR   A 1 161 ? 5.518  -8.004  3.641   0.40 13.92 ?  161 TYR   A O    1 
ATOM   3905 O O    B TYR   A 1 161 ? 5.632  -7.992  4.433   0.60 17.48 ?  161 TYR   A O    1 
ATOM   3906 C CB   A TYR   A 1 161 ? 6.536  -5.167  5.125   0.40 14.36 ?  161 TYR   A CB   1 
ATOM   3907 C CB   B TYR   A 1 161 ? 6.579  -5.101  5.873   0.60 17.61 ?  161 TYR   A CB   1 
ATOM   3908 C CG   A TYR   A 1 161 ? 6.465  -6.188  6.231   0.40 14.55 ?  161 TYR   A CG   1 
ATOM   3909 C CG   B TYR   A 1 161 ? 6.505  -6.095  7.014   0.60 18.04 ?  161 TYR   A CG   1 
ATOM   3910 C CD1  A TYR   A 1 161 ? 7.602  -6.863  6.647   0.40 14.50 ?  161 TYR   A CD1  1 
ATOM   3911 C CD1  B TYR   A 1 161 ? 7.648  -6.714  7.501   0.60 18.02 ?  161 TYR   A CD1  1 
ATOM   3912 C CD2  A TYR   A 1 161 ? 5.258  -6.484  6.855   0.40 15.00 ?  161 TYR   A CD2  1 
ATOM   3913 C CD2  B TYR   A 1 161 ? 5.284  -6.415  7.601   0.60 19.01 ?  161 TYR   A CD2  1 
ATOM   3914 C CE1  A TYR   A 1 161 ? 7.544  -7.805  7.650   0.40 14.75 ?  161 TYR   A CE1  1 
ATOM   3915 C CE1  B TYR   A 1 161 ? 7.581  -7.623  8.540   0.60 19.16 ?  161 TYR   A CE1  1 
ATOM   3916 C CE2  A TYR   A 1 161 ? 5.189  -7.422  7.862   0.40 14.93 ?  161 TYR   A CE2  1 
ATOM   3917 C CE2  B TYR   A 1 161 ? 5.205  -7.320  8.637   0.60 19.79 ?  161 TYR   A CE2  1 
ATOM   3918 C CZ   A TYR   A 1 161 ? 6.336  -8.081  8.254   0.40 15.25 ?  161 TYR   A CZ   1 
ATOM   3919 C CZ   B TYR   A 1 161 ? 6.354  -7.924  9.106   0.60 20.42 ?  161 TYR   A CZ   1 
ATOM   3920 O OH   A TYR   A 1 161 ? 6.279  -9.025  9.256   0.40 15.79 ?  161 TYR   A OH   1 
ATOM   3921 O OH   B TYR   A 1 161 ? 6.272  -8.827  10.142  0.60 21.80 ?  161 TYR   A OH   1 
ATOM   3922 H H    A TYR   A 1 161 ? 6.284  -3.937  3.065   0.40 16.87 ?  161 TYR   A H    1 
ATOM   3923 H H    B TYR   A 1 161 ? 6.347  -3.922  3.748   0.60 21.13 ?  161 TYR   A H    1 
ATOM   3924 H HA   A TYR   A 1 161 ? 7.274  -6.267  3.565   0.40 16.88 ?  161 TYR   A HA   1 
ATOM   3925 H HA   B TYR   A 1 161 ? 7.357  -6.215  4.340   0.60 20.91 ?  161 TYR   A HA   1 
ATOM   3926 H HB2  A TYR   A 1 161 ? 7.378  -4.695  5.211   0.40 17.29 ?  161 TYR   A HB2  1 
ATOM   3927 H HB2  B TYR   A 1 161 ? 7.415  -4.612  5.952   0.60 21.19 ?  161 TYR   A HB2  1 
ATOM   3928 H HB3  A TYR   A 1 161 ? 5.797  -4.549  5.245   0.40 17.29 ?  161 TYR   A HB3  1 
ATOM   3929 H HB3  B TYR   A 1 161 ? 5.832  -4.486  5.961   0.60 21.19 ?  161 TYR   A HB3  1 
ATOM   3930 H HD1  A TYR   A 1 161 ? 8.415  -6.682  6.241   0.40 17.46 ?  161 TYR   A HD1  1 
ATOM   3931 H HD1  B TYR   A 1 161 ? 8.475  -6.512  7.121   0.60 21.68 ?  161 TYR   A HD1  1 
ATOM   3932 H HD2  A TYR   A 1 161 ? 4.484  -6.042  6.594   0.40 18.06 ?  161 TYR   A HD2  1 
ATOM   3933 H HD2  B TYR   A 1 161 ? 4.507  -6.009  7.288   0.60 22.87 ?  161 TYR   A HD2  1 
ATOM   3934 H HE1  A TYR   A 1 161 ? 8.314  -8.253  7.920   0.40 17.76 ?  161 TYR   A HE1  1 
ATOM   3935 H HE1  B TYR   A 1 161 ? 8.357  -8.028  8.856   0.60 23.06 ?  161 TYR   A HE1  1 
ATOM   3936 H HE2  A TYR   A 1 161 ? 4.373  -7.613  8.275   0.40 17.97 ?  161 TYR   A HE2  1 
ATOM   3937 H HE2  B TYR   A 1 161 ? 4.382  -7.521  9.019   0.60 23.81 ?  161 TYR   A HE2  1 
ATOM   3938 H HH   A TYR   A 1 161 ? 7.039  -9.354  9.399   0.40 19.01 ?  161 TYR   A HH   1 
ATOM   3939 H HH   B TYR   A 1 161 ? 7.037  -9.117  10.331  0.60 26.22 ?  161 TYR   A HH   1 
ATOM   3940 N N    A ASP   A 1 162 ? 4.070  -6.278  3.612   0.40 14.86 ?  162 ASP   A N    1 
ATOM   3941 N N    B ASP   A 1 162 ? 4.149  -6.304  4.351   0.60 18.78 ?  162 ASP   A N    1 
ATOM   3942 C CA   A ASP   A 1 162 ? 2.907  -7.158  3.553   0.40 15.67 ?  162 ASP   A CA   1 
ATOM   3943 C CA   B ASP   A 1 162 ? 3.019  -7.226  4.304   0.60 19.92 ?  162 ASP   A CA   1 
ATOM   3944 C C    A ASP   A 1 162 ? 2.946  -8.026  2.300   0.40 15.84 ?  162 ASP   A C    1 
ATOM   3945 C C    B ASP   A 1 162 ? 3.031  -8.045  3.019   0.60 20.43 ?  162 ASP   A C    1 
ATOM   3946 O O    A ASP   A 1 162 ? 2.584  -9.209  2.338   0.40 16.21 ?  162 ASP   A O    1 
ATOM   3947 O O    B ASP   A 1 162 ? 2.683  -9.233  3.030   0.60 20.78 ?  162 ASP   A O    1 
ATOM   3948 C CB   A ASP   A 1 162 ? 1.620  -6.326  3.605   0.40 16.55 ?  162 ASP   A CB   1 
ATOM   3949 C CB   B ASP   A 1 162 ? 1.696  -6.467  4.459   0.60 20.99 ?  162 ASP   A CB   1 
ATOM   3950 C CG   A ASP   A 1 162 ? 1.360  -5.706  4.966   0.40 17.50 ?  162 ASP   A CG   1 
ATOM   3951 C CG   B ASP   A 1 162 ? 1.469  -5.959  5.870   0.60 22.54 ?  162 ASP   A CG   1 
ATOM   3952 O OD1  A ASP   A 1 162 ? 2.046  -6.062  5.942   0.40 18.31 ?  162 ASP   A OD1  1 
ATOM   3953 O OD1  B ASP   A 1 162 ? 2.105  -6.489  6.804   0.60 23.21 ?  162 ASP   A OD1  1 
ATOM   3954 O OD2  A ASP   A 1 162 ? 0.432  -4.867  5.059   0.40 18.42 -1 162 ASP   A OD2  1 
ATOM   3955 O OD2  B ASP   A 1 162 ? 0.627  -5.047  6.045   0.60 23.59 -1 162 ASP   A OD2  1 
ATOM   3956 H H    A ASP   A 1 162 ? 3.880  -5.440  3.614   0.40 17.89 ?  162 ASP   A H    1 
ATOM   3957 H H    B ASP   A 1 162 ? 3.935  -5.472  4.314   0.60 22.59 ?  162 ASP   A H    1 
ATOM   3958 H HA   A ASP   A 1 162 ? 2.911  -7.748  4.319   0.40 18.86 ?  162 ASP   A HA   1 
ATOM   3959 H HA   B ASP   A 1 162 ? 3.092  -7.848  5.039   0.60 23.96 ?  162 ASP   A HA   1 
ATOM   3960 H HB2  A ASP   A 1 162 ? 1.676  -5.600  2.972   0.40 19.92 ?  162 ASP   A HB2  1 
ATOM   3961 H HB2  B ASP   A 1 162 ? 1.698  -5.699  3.873   0.60 25.25 ?  162 ASP   A HB2  1 
ATOM   3962 H HB3  A ASP   A 1 162 ? 0.860  -6.890  3.413   0.40 19.92 ?  162 ASP   A HB3  1 
ATOM   3963 H HB3  B ASP   A 1 162 ? 0.961  -7.060  4.239   0.60 25.25 ?  162 ASP   A HB3  1 
ATOM   3964 N N    A LYS   A 1 163 ? 3.388  -7.455  1.177   0.40 16.52 ?  163 LYS   A N    1 
ATOM   3965 N N    B LYS   A 1 163 ? 3.444  -7.432  1.906   0.60 21.18 ?  163 LYS   A N    1 
ATOM   3966 C CA   A LYS   A 1 163 ? 3.532  -8.238  -0.045  0.40 16.80 ?  163 LYS   A CA   1 
ATOM   3967 C CA   B LYS   A 1 163 ? 3.464  -8.138  0.628   0.60 22.29 ?  163 LYS   A CA   1 
ATOM   3968 C C    A LYS   A 1 163 ? 4.628  -9.289  0.088   0.40 16.00 ?  163 LYS   A C    1 
ATOM   3969 C C    B LYS   A 1 163 ? 4.540  -9.219  0.602   0.60 21.87 ?  163 LYS   A C    1 
ATOM   3970 O O    A LYS   A 1 163 ? 4.513  -10.378 -0.491  0.40 16.62 ?  163 LYS   A O    1 
ATOM   3971 O O    B LYS   A 1 163 ? 4.288  -10.343 0.149   0.60 21.88 ?  163 LYS   A O    1 
ATOM   3972 C CB   A LYS   A 1 163 ? 3.830  -7.302  -1.213  0.40 19.02 ?  163 LYS   A CB   1 
ATOM   3973 C CB   B LYS   A 1 163 ? 3.672  -7.138  -0.509  0.60 24.27 ?  163 LYS   A CB   1 
ATOM   3974 C CG   A LYS   A 1 163 ? 3.753  -7.958  -2.573  0.40 21.56 ?  163 LYS   A CG   1 
ATOM   3975 C CG   B LYS   A 1 163 ? 3.756  -7.760  -1.889  0.60 26.51 ?  163 LYS   A CG   1 
ATOM   3976 C CD   A LYS   A 1 163 ? 4.172  -6.992  -3.661  0.40 23.88 ?  163 LYS   A CD   1 
ATOM   3977 C CD   B LYS   A 1 163 ? 4.041  -6.701  -2.939  0.60 28.55 ?  163 LYS   A CD   1 
ATOM   3978 C CE   A LYS   A 1 163 ? 4.093  -7.636  -5.030  0.40 25.52 ?  163 LYS   A CE   1 
ATOM   3979 C CE   B LYS   A 1 163 ? 3.891  -7.251  -4.351  0.60 30.06 ?  163 LYS   A CE   1 
ATOM   3980 N NZ   A LYS   A 1 163 ? 4.750  -6.797  -6.067  0.40 26.31 ?  163 LYS   A NZ   1 
ATOM   3981 N NZ   B LYS   A 1 163 ? 4.185  -6.220  -5.386  0.60 30.84 ?  163 LYS   A NZ   1 
ATOM   3982 H H    A LYS   A 1 163 ? 3.593  -6.622  1.095   0.40 19.89 ?  163 LYS   A H    1 
ATOM   3983 H H    B LYS   A 1 163 ? 3.720  -6.617  1.866   0.60 25.48 ?  163 LYS   A H    1 
ATOM   3984 H HA   A LYS   A 1 163 ? 2.697  -8.696  -0.231  0.40 20.21 ?  163 LYS   A HA   1 
ATOM   3985 H HA   B LYS   A 1 163 ? 2.607  -8.567  0.488   0.60 26.80 ?  163 LYS   A HA   1 
ATOM   3986 H HB2  A LYS   A 1 163 ? 3.187  -6.575  -1.200  0.40 22.88 ?  163 LYS   A HB2  1 
ATOM   3987 H HB2  B LYS   A 1 163 ? 2.925  -6.514  -0.518  0.60 29.18 ?  163 LYS   A HB2  1 
ATOM   3988 H HB3  A LYS   A 1 163 ? 4.726  -6.948  -1.107  0.40 22.88 ?  163 LYS   A HB3  1 
ATOM   3989 H HB3  B LYS   A 1 163 ? 4.497  -6.653  -0.357  0.60 29.18 ?  163 LYS   A HB3  1 
ATOM   3990 H HG2  A LYS   A 1 163 ? 4.349  -8.722  -2.597  0.40 25.93 ?  163 LYS   A HG2  1 
ATOM   3991 H HG2  B LYS   A 1 163 ? 4.477  -8.408  -1.911  0.60 31.87 ?  163 LYS   A HG2  1 
ATOM   3992 H HG3  A LYS   A 1 163 ? 2.839  -8.236  -2.744  0.40 25.93 ?  163 LYS   A HG3  1 
ATOM   3993 H HG3  B LYS   A 1 163 ? 2.911  -8.187  -2.102  0.60 31.87 ?  163 LYS   A HG3  1 
ATOM   3994 H HD2  A LYS   A 1 163 ? 3.578  -6.224  -3.649  0.40 28.71 ?  163 LYS   A HD2  1 
ATOM   3995 H HD2  B LYS   A 1 163 ? 3.414  -5.970  -2.831  0.60 34.32 ?  163 LYS   A HD2  1 
ATOM   3996 H HD3  A LYS   A 1 163 ? 5.086  -6.713  -3.504  0.40 28.71 ?  163 LYS   A HD3  1 
ATOM   3997 H HD3  B LYS   A 1 163 ? 4.951  -6.382  -2.830  0.60 34.32 ?  163 LYS   A HD3  1 
ATOM   3998 H HE2  A LYS   A 1 163 ? 4.536  -8.497  -5.002  0.40 30.68 ?  163 LYS   A HE2  1 
ATOM   3999 H HE2  B LYS   A 1 163 ? 4.507  -7.988  -4.478  0.60 36.13 ?  163 LYS   A HE2  1 
ATOM   4000 H HE3  A LYS   A 1 163 ? 3.161  -7.747  -5.273  0.40 30.68 ?  163 LYS   A HE3  1 
ATOM   4001 H HE3  B LYS   A 1 163 ? 2.981  -7.556  -4.475  0.60 36.13 ?  163 LYS   A HE3  1 
ATOM   4002 H HZ1  A LYS   A 1 163 ? 4.691  -7.194  -6.860  0.40 31.64 ?  163 LYS   A HZ1  1 
ATOM   4003 H HZ1  B LYS   A 1 163 ? 4.092  -6.571  -6.199  0.60 37.07 ?  163 LYS   A HZ1  1 
ATOM   4004 H HZ2  A LYS   A 1 163 ? 4.350  -6.002  -6.111  0.40 31.64 ?  163 LYS   A HZ2  1 
ATOM   4005 H HZ2  B LYS   A 1 163 ? 3.624  -5.535  -5.300  0.60 37.07 ?  163 LYS   A HZ2  1 
ATOM   4006 H HZ3  A LYS   A 1 163 ? 5.608  -6.678  -5.864  0.40 31.64 ?  163 LYS   A HZ3  1 
ATOM   4007 H HZ3  B LYS   A 1 163 ? 5.020  -5.923  -5.294  0.60 37.07 ?  163 LYS   A HZ3  1 
ATOM   4008 N N    A LEU   A 1 164 ? 5.693  -8.975  0.838   0.40 15.50 ?  164 LEU   A N    1 
ATOM   4009 N N    B LEU   A 1 164 ? 5.747  -8.899  1.080   0.60 21.60 ?  164 LEU   A N    1 
ATOM   4010 C CA   A LEU   A 1 164 ? 6.791  -9.920  1.032   0.40 14.93 ?  164 LEU   A CA   1 
ATOM   4011 C CA   B LEU   A 1 164 ? 6.834  -9.874  1.070   0.60 21.42 ?  164 LEU   A CA   1 
ATOM   4012 C C    A LEU   A 1 164 ? 6.393  -11.054 1.975   0.40 14.82 ?  164 LEU   A C    1 
ATOM   4013 C C    B LEU   A 1 164 ? 6.402  -11.172 1.730   0.60 22.19 ?  164 LEU   A C    1 
ATOM   4014 O O    A LEU   A 1 164 ? 6.726  -12.221 1.731   0.40 15.48 ?  164 LEU   A O    1 
ATOM   4015 O O    B LEU   A 1 164 ? 6.720  -12.266 1.248   0.60 22.84 ?  164 LEU   A O    1 
ATOM   4016 C CB   A LEU   A 1 164 ? 8.014  -9.178  1.575   0.40 14.77 ?  164 LEU   A CB   1 
ATOM   4017 C CB   B LEU   A 1 164 ? 8.054  -9.294  1.789   0.60 20.79 ?  164 LEU   A CB   1 
ATOM   4018 C CG   A LEU   A 1 164 ? 8.733  -8.214  0.625   0.40 14.62 ?  164 LEU   A CG   1 
ATOM   4019 C CG   B LEU   A 1 164 ? 8.768  -8.167  1.044   0.60 20.15 ?  164 LEU   A CG   1 
ATOM   4020 C CD1  A LEU   A 1 164 ? 9.652  -7.271  1.397   0.40 14.03 ?  164 LEU   A CD1  1 
ATOM   4021 C CD1  B LEU   A 1 164 ? 9.775  -7.442  1.931   0.60 19.71 ?  164 LEU   A CD1  1 
ATOM   4022 C CD2  A LEU   A 1 164 ? 9.521  -8.981  -0.427  0.40 15.30 ?  164 LEU   A CD2  1 
ATOM   4023 C CD2  B LEU   A 1 164 ? 9.442  -8.736  -0.190  0.60 20.33 ?  164 LEU   A CD2  1 
ATOM   4024 H H    A LEU   A 1 164 ? 5.798  -8.221  1.244   0.40 18.66 ?  164 LEU   A H    1 
ATOM   4025 H H    B LEU   A 1 164 ? 5.952  -8.143  1.430   0.60 25.98 ?  164 LEU   A H    1 
ATOM   4026 H HA   A LEU   A 1 164 ? 7.025  -10.307 0.179   0.40 17.97 ?  164 LEU   A HA   1 
ATOM   4027 H HA   B LEU   A 1 164 ? 7.077  -10.079 0.158   0.60 25.76 ?  164 LEU   A HA   1 
ATOM   4028 H HB2  A LEU   A 1 164 ? 7.735  -8.656  2.343   0.40 17.79 ?  164 LEU   A HB2  1 
ATOM   4029 H HB2  B LEU   A 1 164 ? 7.770  -8.943  2.645   0.60 25.00 ?  164 LEU   A HB2  1 
ATOM   4030 H HB3  A LEU   A 1 164 ? 8.665  -9.836  1.853   0.40 17.79 ?  164 LEU   A HB3  1 
ATOM   4031 H HB3  B LEU   A 1 164 ? 8.700  -10.006 1.927   0.60 25.00 ?  164 LEU   A HB3  1 
ATOM   4032 H HG   A LEU   A 1 164 ? 8.075  -7.672  0.164   0.40 17.60 ?  164 LEU   A HG   1 
ATOM   4033 H HG   B LEU   A 1 164 ? 8.109  -7.520  0.750   0.60 24.23 ?  164 LEU   A HG   1 
ATOM   4034 H HD11 A LEU   A 1 164 ? 10.097 -6.676  0.771   0.40 16.90 ?  164 LEU   A HD11 1 
ATOM   4035 H HD11 B LEU   A 1 164 ? 10.200 -6.736  1.415   0.60 23.70 ?  164 LEU   A HD11 1 
ATOM   4036 H HD12 A LEU   A 1 164 ? 9.118  -6.750  2.020   0.40 16.90 ?  164 LEU   A HD12 1 
ATOM   4037 H HD12 B LEU   A 1 164 ? 9.311  -7.059  2.692   0.60 23.70 ?  164 LEU   A HD12 1 
ATOM   4038 H HD13 A LEU   A 1 164 ? 10.309 -7.793  1.882   0.40 16.90 ?  164 LEU   A HD13 1 
ATOM   4039 H HD13 B LEU   A 1 164 ? 10.445 -8.074  2.236   0.60 23.70 ?  164 LEU   A HD13 1 
ATOM   4040 H HD21 A LEU   A 1 164 ? 9.980  -8.349  -1.002  0.40 18.42 ?  164 LEU   A HD21 1 
ATOM   4041 H HD21 B LEU   A 1 164 ? 10.008 -8.056  -0.582  0.60 24.45 ?  164 LEU   A HD21 1 
ATOM   4042 H HD22 A LEU   A 1 164 ? 10.164 -9.555  0.017   0.40 18.42 ?  164 LEU   A HD22 1 
ATOM   4043 H HD22 B LEU   A 1 164 ? 9.972  -9.506  0.066   0.60 24.45 ?  164 LEU   A HD22 1 
ATOM   4044 H HD23 A LEU   A 1 164 ? 8.904  -9.517  -0.950  0.40 18.42 ?  164 LEU   A HD23 1 
ATOM   4045 H HD23 B LEU   A 1 164 ? 8.758  -9.003  -0.824  0.60 24.45 ?  164 LEU   A HD23 1 
ATOM   4046 N N    A VAL   A 1 165 ? 5.708  -10.730 3.073   0.40 14.52 ?  165 VAL   A N    1 
ATOM   4047 N N    B VAL   A 1 165 ? 5.672  -11.066 2.838   0.60 22.74 ?  165 VAL   A N    1 
ATOM   4048 C CA   A VAL   A 1 165 ? 5.240  -11.778 3.978   0.40 14.11 ?  165 VAL   A CA   1 
ATOM   4049 C CA   B VAL   A 1 165 ? 5.184  -12.255 3.525   0.60 23.14 ?  165 VAL   A CA   1 
ATOM   4050 C C    A VAL   A 1 165 ? 4.203  -12.651 3.289   0.40 13.95 ?  165 VAL   A C    1 
ATOM   4051 C C    B VAL   A 1 165 ? 4.196  -13.017 2.649   0.60 22.92 ?  165 VAL   A C    1 
ATOM   4052 O O    A VAL   A 1 165 ? 4.301  -13.885 3.285   0.40 14.07 ?  165 VAL   A O    1 
ATOM   4053 O O    B VAL   A 1 165 ? 4.265  -14.245 2.536   0.60 22.13 ?  165 VAL   A O    1 
ATOM   4054 C CB   A VAL   A 1 165 ? 4.687  -11.162 5.275   0.40 14.48 ?  165 VAL   A CB   1 
ATOM   4055 C CB   B VAL   A 1 165 ? 4.571  -11.867 4.885   0.60 24.36 ?  165 VAL   A CB   1 
ATOM   4056 C CG1  A VAL   A 1 165 ? 3.918  -12.213 6.070   0.40 14.62 ?  165 VAL   A CG1  1 
ATOM   4057 C CG1  B VAL   A 1 165 ? 4.127  -13.108 5.632   0.60 24.67 ?  165 VAL   A CG1  1 
ATOM   4058 C CG2  A VAL   A 1 165 ? 5.823  -10.566 6.096   0.40 15.08 ?  165 VAL   A CG2  1 
ATOM   4059 C CG2  B VAL   A 1 165 ? 5.563  -11.075 5.717   0.60 24.85 ?  165 VAL   A CG2  1 
ATOM   4060 H H    A VAL   A 1 165 ? 5.501  -9.922  3.312   0.40 17.49 ?  165 VAL   A H    1 
ATOM   4061 H H    B VAL   A 1 165 ? 5.450  -10.328 3.212   0.60 27.34 ?  165 VAL   A H    1 
ATOM   4062 H HA   A VAL   A 1 165 ? 5.990  -12.335 4.216   0.40 16.99 ?  165 VAL   A HA   1 
ATOM   4063 H HA   B VAL   A 1 165 ? 5.933  -12.847 3.706   0.60 27.83 ?  165 VAL   A HA   1 
ATOM   4064 H HB   A VAL   A 1 165 ? 4.076  -10.438 5.055   0.40 17.44 ?  165 VAL   A HB   1 
ATOM   4065 H HB   B VAL   A 1 165 ? 3.790  -11.313 4.738   0.60 29.29 ?  165 VAL   A HB   1 
ATOM   4066 H HG11 A VAL   A 1 165 ? 3.836  -11.913 6.987   0.40 17.60 ?  165 VAL   A HG11 1 
ATOM   4067 H HG11 B VAL   A 1 165 ? 3.904  -12.866 6.544   0.60 29.66 ?  165 VAL   A HG11 1 
ATOM   4068 H HG12 A VAL   A 1 165 ? 3.036  -12.316 5.678   0.40 17.60 ?  165 VAL   A HG12 1 
ATOM   4069 H HG12 B VAL   A 1 165 ? 3.350  -13.485 5.191   0.60 29.66 ?  165 VAL   A HG12 1 
ATOM   4070 H HG13 A VAL   A 1 165 ? 4.404  -13.047 6.034   0.40 17.60 ?  165 VAL   A HG13 1 
ATOM   4071 H HG13 B VAL   A 1 165 ? 4.854  -13.752 5.631   0.60 29.66 ?  165 VAL   A HG13 1 
ATOM   4072 H HG21 A VAL   A 1 165 ? 5.490  -10.334 6.974   0.40 18.15 ?  165 VAL   A HG21 1 
ATOM   4073 H HG21 B VAL   A 1 165 ? 5.186  -10.925 6.599   0.60 29.88 ?  165 VAL   A HG21 1 
ATOM   4074 H HG22 A VAL   A 1 165 ? 6.533  -11.221 6.171   0.40 18.15 ?  165 VAL   A HG22 1 
ATOM   4075 H HG22 B VAL   A 1 165 ? 6.386  -11.583 5.792   0.60 29.88 ?  165 VAL   A HG22 1 
ATOM   4076 H HG23 A VAL   A 1 165 ? 6.156  -9.771  5.645   0.40 18.15 ?  165 VAL   A HG23 1 
ATOM   4077 H HG23 B VAL   A 1 165 ? 5.734  -10.227 5.283   0.60 29.88 ?  165 VAL   A HG23 1 
ATOM   4078 N N    A SER   A 1 166 ? 3.191  -12.018 2.696   0.40 14.17 ?  166 SER   A N    1 
ATOM   4079 N N    B SER   A 1 166 ? 3.278  -12.302 1.993   0.60 23.94 ?  166 SER   A N    1 
ATOM   4080 C CA   A SER   A 1 166 ? 2.073  -12.780 2.152   0.40 14.93 ?  166 SER   A CA   1 
ATOM   4081 C CA   B SER   A 1 166 ? 2.149  -12.953 1.334   0.60 25.00 ?  166 SER   A CA   1 
ATOM   4082 C C    A SER   A 1 166 ? 2.486  -13.640 0.967   0.40 15.19 ?  166 SER   A C    1 
ATOM   4083 C C    B SER   A 1 166 ? 2.552  -13.765 0.111   0.60 25.41 ?  166 SER   A C    1 
ATOM   4084 O O    A SER   A 1 166 ? 1.874  -14.692 0.729   0.40 16.21 ?  166 SER   A O    1 
ATOM   4085 O O    B SER   A 1 166 ? 1.818  -14.685 -0.268  0.60 25.06 ?  166 SER   A O    1 
ATOM   4086 C CB   A SER   A 1 166 ? 0.933  -11.843 1.750   0.40 16.72 ?  166 SER   A CB   1 
ATOM   4087 C CB   B SER   A 1 166 ? 1.105  -11.910 0.932   0.60 26.11 ?  166 SER   A CB   1 
ATOM   4088 O OG   A SER   A 1 166 ? 0.348  -11.222 2.882   0.40 18.47 ?  166 SER   A OG   1 
ATOM   4089 O OG   B SER   A 1 166 ? 0.759  -11.094 2.034   0.60 27.40 ?  166 SER   A OG   1 
ATOM   4090 H H    A SER   A 1 166 ? 3.117  -11.162 2.613   0.40 17.07 ?  166 SER   A H    1 
ATOM   4091 H H    B SER   A 1 166 ? 3.289  -11.449 1.916   0.60 28.79 ?  166 SER   A H    1 
ATOM   4092 H HA   A SER   A 1 166 ? 1.730  -13.372 2.837   0.40 17.98 ?  166 SER   A HA   1 
ATOM   4093 H HA   B SER   A 1 166 ? 1.730  -13.563 1.958   0.60 30.06 ?  166 SER   A HA   1 
ATOM   4094 H HB2  A SER   A 1 166 ? 1.276  -11.150 1.167   0.40 20.12 ?  166 SER   A HB2  1 
ATOM   4095 H HB2  B SER   A 1 166 ? 1.469  -11.351 0.229   0.60 31.39 ?  166 SER   A HB2  1 
ATOM   4096 H HB3  A SER   A 1 166 ? 0.246  -12.353 1.289   0.40 20.12 ?  166 SER   A HB3  1 
ATOM   4097 H HB3  B SER   A 1 166 ? 0.308  -12.366 0.614   0.60 31.39 ?  166 SER   A HB3  1 
ATOM   4098 H HG   A SER   A 1 166 ? 0.926  -10.780 3.302   0.40 22.22 ?  166 SER   A HG   1 
ATOM   4099 H HG   B SER   A 1 166 ? 1.435  -10.677 2.307   0.60 32.94 ?  166 SER   A HG   1 
ATOM   4100 N N    A SER   A 1 167 ? 3.510  -13.219 0.218   0.40 15.03 ?  167 SER   A N    1 
ATOM   4101 N N    B SER   A 1 167 ? 3.688  -13.455 -0.515  0.60 26.43 ?  167 SER   A N    1 
ATOM   4102 C CA   A SER   A 1 167 ? 3.946  -13.944 -0.967  0.40 15.28 ?  167 SER   A CA   1 
ATOM   4103 C CA   B SER   A 1 167 ? 4.117  -14.133 -1.731  0.60 27.68 ?  167 SER   A CA   1 
ATOM   4104 C C    A SER   A 1 167 ? 5.112  -14.882 -0.694  0.40 15.49 ?  167 SER   A C    1 
ATOM   4105 C C    B SER   A 1 167 ? 5.357  -14.993 -1.521  0.60 28.57 ?  167 SER   A C    1 
ATOM   4106 O O    A SER   A 1 167 ? 5.601  -15.527 -1.625  0.40 16.56 ?  167 SER   A O    1 
ATOM   4107 O O    B SER   A 1 167 ? 5.910  -15.514 -2.495  0.60 28.65 ?  167 SER   A O    1 
ATOM   4108 C CB   A SER   A 1 167 ? 4.349  -12.967 -2.075  0.40 15.89 ?  167 SER   A CB   1 
ATOM   4109 C CB   B SER   A 1 167 ? 4.362  -13.117 -2.850  0.60 28.01 ?  167 SER   A CB   1 
ATOM   4110 O OG   A SER   A 1 167 ? 5.463  -12.186 -1.664  0.40 16.18 ?  167 SER   A OG   1 
ATOM   4111 O OG   B SER   A 1 167 ? 5.404  -12.225 -2.502  0.60 28.13 ?  167 SER   A OG   1 
ATOM   4112 H H    A SER   A 1 167 ? 3.957  -12.493 0.372   0.40 18.10 ?  167 SER   A H    1 
ATOM   4113 H H    B SER   A 1 167 ? 4.234  -12.847 -0.247  0.60 31.77 ?  167 SER   A H    1 
ATOM   4114 H HA   A SER   A 1 167 ? 3.196  -14.467 -1.298  0.40 18.39 ?  167 SER   A HA   1 
ATOM   4115 H HA   B SER   A 1 167 ? 3.408  -14.720 -2.028  0.60 33.27 ?  167 SER   A HA   1 
ATOM   4116 H HB2  A SER   A 1 167 ? 4.595  -13.476 -2.867  0.40 19.12 ?  167 SER   A HB2  1 
ATOM   4117 H HB2  B SER   A 1 167 ? 4.608  -13.591 -3.661  0.60 33.67 ?  167 SER   A HB2  1 
ATOM   4118 H HB3  A SER   A 1 167 ? 3.593  -12.389 -2.284  0.40 19.12 ?  167 SER   A HB3  1 
ATOM   4119 H HB3  B SER   A 1 167 ? 3.547  -12.609 -3.001  0.60 33.67 ?  167 SER   A HB3  1 
ATOM   4120 H HG   A SER   A 1 167 ? 5.270  -11.785 -0.949  0.40 19.47 ?  167 SER   A HG   1 
ATOM   4121 H HG   B SER   A 1 167 ? 5.201  -11.806 -1.803  0.60 33.81 ?  167 SER   A HG   1 
ATOM   4122 N N    A PHE   A 1 168 ? 5.577  -14.967 0.545   0.40 14.86 ?  168 PHE   A N    1 
ATOM   4123 N N    B PHE   A 1 168 ? 5.798  -15.165 -0.278  0.60 29.28 ?  168 PHE   A N    1 
ATOM   4124 C CA   A PHE   A 1 168 ? 6.759  -15.769 0.827   0.40 15.16 ?  168 PHE   A CA   1 
ATOM   4125 C CA   B PHE   A 1 168 ? 7.039  -15.882 -0.018  0.60 30.12 ?  168 PHE   A CA   1 
ATOM   4126 C C    A PHE   A 1 168 ? 6.437  -17.251 0.713   0.40 16.65 ?  168 PHE   A C    1 
ATOM   4127 C C    B PHE   A 1 168 ? 6.838  -17.381 -0.203  0.60 33.28 ?  168 PHE   A C    1 
ATOM   4128 O O    A PHE   A 1 168 ? 5.484  -17.744 1.329   0.40 17.28 ?  168 PHE   A O    1 
ATOM   4129 O O    B PHE   A 1 168 ? 5.951  -17.981 0.412   0.60 33.37 ?  168 PHE   A O    1 
ATOM   4130 C CB   A PHE   A 1 168 ? 7.290  -15.469 2.221   0.40 14.76 ?  168 PHE   A CB   1 
ATOM   4131 C CB   B PHE   A 1 168 ? 7.528  -15.592 1.400   0.60 27.90 ?  168 PHE   A CB   1 
ATOM   4132 C CG   A PHE   A 1 168 ? 8.567  -16.190 2.529   0.40 14.07 ?  168 PHE   A CG   1 
ATOM   4133 C CG   B PHE   A 1 168 ? 8.762  -16.365 1.786   0.60 25.68 ?  168 PHE   A CG   1 
ATOM   4134 C CD1  A PHE   A 1 168 ? 9.749  -15.787 1.941   0.40 14.15 ?  168 PHE   A CD1  1 
ATOM   4135 C CD1  B PHE   A 1 168 ? 9.931  -16.247 1.048   0.60 24.82 ?  168 PHE   A CD1  1 
ATOM   4136 C CD2  A PHE   A 1 168 ? 8.585  -17.285 3.378   0.40 13.68 ?  168 PHE   A CD2  1 
ATOM   4137 C CD2  B PHE   A 1 168 ? 8.754  -17.203 2.891   0.60 24.78 ?  168 PHE   A CD2  1 
ATOM   4138 C CE1  A PHE   A 1 168 ? 10.926 -16.448 2.203   0.40 14.00 ?  168 PHE   A CE1  1 
ATOM   4139 C CE1  B PHE   A 1 168 ? 11.064 -16.958 1.401   0.60 24.24 ?  168 PHE   A CE1  1 
ATOM   4140 C CE2  A PHE   A 1 168 ? 9.769  -17.947 3.649   0.40 13.65 ?  168 PHE   A CE2  1 
ATOM   4141 C CE2  B PHE   A 1 168 ? 9.886  -17.915 3.250   0.60 24.14 ?  168 PHE   A CE2  1 
ATOM   4142 C CZ   A PHE   A 1 168 ? 10.940 -17.527 3.058   0.40 13.74 ?  168 PHE   A CZ   1 
ATOM   4143 C CZ   B PHE   A 1 168 ? 11.042 -17.791 2.504   0.60 23.95 ?  168 PHE   A CZ   1 
ATOM   4144 H H    A PHE   A 1 168 ? 5.238  -14.569 1.228   0.40 17.89 ?  168 PHE   A H    1 
ATOM   4145 H H    B PHE   A 1 168 ? 5.398  -14.878 0.423   0.60 35.19 ?  168 PHE   A H    1 
ATOM   4146 H HA   A PHE   A 1 168 ? 7.449  -15.552 0.179   0.40 18.26 ?  168 PHE   A HA   1 
ATOM   4147 H HA   B PHE   A 1 168 ? 7.718  -15.585 -0.642  0.60 36.21 ?  168 PHE   A HA   1 
ATOM   4148 H HB2  A PHE   A 1 168 ? 7.459  -14.515 2.294   0.40 17.76 ?  168 PHE   A HB2  1 
ATOM   4149 H HB2  B PHE   A 1 168 ? 7.736  -14.648 1.473   0.60 33.53 ?  168 PHE   A HB2  1 
ATOM   4150 H HB3  A PHE   A 1 168 ? 6.627  -15.737 2.874   0.40 17.76 ?  168 PHE   A HB3  1 
ATOM   4151 H HB3  B PHE   A 1 168 ? 6.825  -15.824 2.027   0.60 33.53 ?  168 PHE   A HB3  1 
ATOM   4152 H HD1  A PHE   A 1 168 ? 9.753  -15.057 1.364   0.40 17.04 ?  168 PHE   A HD1  1 
ATOM   4153 H HD1  B PHE   A 1 168 ? 9.951  -15.691 0.303   0.60 29.84 ?  168 PHE   A HD1  1 
ATOM   4154 H HD2  A PHE   A 1 168 ? 7.793  -17.569 3.777   0.40 16.47 ?  168 PHE   A HD2  1 
ATOM   4155 H HD2  B PHE   A 1 168 ? 7.977  -17.290 3.395   0.60 29.80 ?  168 PHE   A HD2  1 
ATOM   4156 H HE1  A PHE   A 1 168 ? 11.720 -16.161 1.808   0.40 16.85 ?  168 PHE   A HE1  1 
ATOM   4157 H HE1  B PHE   A 1 168 ? 11.842 -16.873 0.896   0.60 29.15 ?  168 PHE   A HE1  1 
ATOM   4158 H HE2  A PHE   A 1 168 ? 9.766  -18.679 4.225   0.40 16.44 ?  168 PHE   A HE2  1 
ATOM   4159 H HE2  B PHE   A 1 168 ? 9.867  -18.477 3.995   0.60 29.03 ?  168 PHE   A HE2  1 
ATOM   4160 H HZ   A PHE   A 1 168 ? 11.735 -17.972 3.238   0.40 16.54 ?  168 PHE   A HZ   1 
ATOM   4161 H HZ   B PHE   A 1 168 ? 11.804 -18.269 2.744   0.60 28.80 ?  168 PHE   A HZ   1 
ATOM   4162 N N    A LEU   A 1 169 ? 7.235  -17.959 -0.081  0.40 18.89 ?  169 LEU   A N    1 
ATOM   4163 N N    B LEU   A 1 169 ? 7.668  -17.982 -1.051  0.60 36.03 ?  169 LEU   A N    1 
ATOM   4164 C CA   A LEU   A 1 169 ? 7.060  -19.391 -0.242  0.40 22.16 ?  169 LEU   A CA   1 
ATOM   4165 C CA   B LEU   A 1 169 ? 7.585  -19.412 -1.320  0.60 38.46 ?  169 LEU   A CA   1 
ATOM   4166 C C    A LEU   A 1 169 ? 7.930  -20.123 0.769   0.40 22.37 ?  169 LEU   A C    1 
ATOM   4167 C C    B LEU   A 1 169 ? 8.685  -20.164 -0.579  0.60 39.47 ?  169 LEU   A C    1 
ATOM   4168 O O    A LEU   A 1 169 ? 7.419  -20.627 1.767   0.40 22.26 ?  169 LEU   A O    1 
ATOM   4169 O O    B LEU   A 1 169 ? 8.506  -21.308 -0.161  0.60 39.84 ?  169 LEU   A O    1 
ATOM   4170 C CB   A LEU   A 1 169 ? 7.401  -19.815 -1.675  0.40 25.01 ?  169 LEU   A CB   1 
ATOM   4171 C CB   B LEU   A 1 169 ? 7.687  -19.679 -2.824  0.60 39.64 ?  169 LEU   A CB   1 
ATOM   4172 C CG   A LEU   A 1 169 ? 7.092  -21.267 -2.050  0.40 27.22 ?  169 LEU   A CG   1 
ATOM   4173 C CG   B LEU   A 1 169 ? 7.103  -21.008 -3.309  0.60 40.50 ?  169 LEU   A CG   1 
ATOM   4174 C CD1  A LEU   A 1 169 ? 5.657  -21.620 -1.694  0.40 27.99 ?  169 LEU   A CD1  1 
ATOM   4175 C CD1  B LEU   A 1 169 ? 5.599  -21.034 -3.085  0.60 40.84 ?  169 LEU   A CD1  1 
ATOM   4176 C CD2  A LEU   A 1 169 ? 7.345  -21.498 -3.534  0.40 27.96 ?  169 LEU   A CD2  1 
ATOM   4177 C CD2  B LEU   A 1 169 ? 7.432  -21.244 -4.776  0.60 40.75 ?  169 LEU   A CD2  1 
ATOM   4178 O OXT  A LEU   A 1 169 ? 9.151  -20.209 0.628   0.40 22.37 -1 169 LEU   A OXT  1 
ATOM   4179 O OXT  B LEU   A 1 169 ? 9.779  -19.643 -0.374  0.60 39.82 -1 169 LEU   A OXT  1 
ATOM   4180 H H    A LEU   A 1 169 ? 7.878  -17.627 -0.549  0.40 22.72 ?  169 LEU   A H    1 
ATOM   4181 H H    B LEU   A 1 169 ? 8.292  -17.577 -1.488  0.60 43.29 ?  169 LEU   A H    1 
ATOM   4182 H HA   A LEU   A 1 169 ? 6.138  -19.621 -0.062  0.40 26.65 ?  169 LEU   A HA   1 
ATOM   4183 H HA   B LEU   A 1 169 ? 6.736  -19.747 -1.005  0.60 46.21 ?  169 LEU   A HA   1 
ATOM   4184 H HB2  A LEU   A 1 169 ? 6.902  -19.251 -2.287  0.40 30.07 ?  169 LEU   A HB2  1 
ATOM   4185 H HB2  B LEU   A 1 169 ? 7.219  -18.971 -3.293  0.60 47.62 ?  169 LEU   A HB2  1 
ATOM   4186 H HB3  A LEU   A 1 169 ? 8.350  -19.680 -1.816  0.40 30.07 ?  169 LEU   A HB3  1 
ATOM   4187 H HB3  B LEU   A 1 169 ? 8.623  -19.668 -3.074  0.60 47.62 ?  169 LEU   A HB3  1 
ATOM   4188 H HG   A LEU   A 1 169 ? 7.680  -21.856 -1.553  0.40 32.72 ?  169 LEU   A HG   1 
ATOM   4189 H HG   B LEU   A 1 169 ? 7.494  -21.732 -2.796  0.60 48.66 ?  169 LEU   A HG   1 
ATOM   4190 H HD11 A LEU   A 1 169 ? 5.422  -22.456 -2.124  0.40 33.65 ?  169 LEU   A HD11 1 
ATOM   4191 H HD11 B LEU   A 1 169 ? 5.216  -21.756 -3.605  0.60 49.07 ?  169 LEU   A HD11 1 
ATOM   4192 H HD12 A LEU   A 1 169 ? 5.585  -21.711 -0.731  0.40 33.65 ?  169 LEU   A HD12 1 
ATOM   4193 H HD12 B LEU   A 1 169 ? 5.423  -21.175 -2.142  0.60 49.07 ?  169 LEU   A HD12 1 
ATOM   4194 H HD13 A LEU   A 1 169 ? 5.072  -20.911 -2.006  0.40 33.65 ?  169 LEU   A HD13 1 
ATOM   4195 H HD13 B LEU   A 1 169 ? 5.224  -20.186 -3.371  0.60 49.07 ?  169 LEU   A HD13 1 
ATOM   4196 H HD21 A LEU   A 1 169 ? 7.148  -22.424 -3.747  0.40 33.60 ?  169 LEU   A HD21 1 
ATOM   4197 H HD21 B LEU   A 1 169 ? 7.056  -22.095 -5.051  0.60 48.96 ?  169 LEU   A HD21 1 
ATOM   4198 H HD22 A LEU   A 1 169 ? 6.767  -20.911 -4.047  0.40 33.60 ?  169 LEU   A HD22 1 
ATOM   4199 H HD22 B LEU   A 1 169 ? 7.049  -20.526 -5.304  0.60 48.96 ?  169 LEU   A HD22 1 
ATOM   4200 H HD23 A LEU   A 1 169 ? 8.274  -21.302 -3.730  0.40 33.60 ?  169 LEU   A HD23 1 
ATOM   4201 H HD23 B LEU   A 1 169 ? 8.396  -21.257 -4.885  0.60 48.96 ?  169 LEU   A HD23 1 
ATOM   4202 N N    A SER   B 1 1   ? 50.659 -9.118  -23.709 0.40 29.46 ?  1   SER   B N    1 
ATOM   4203 N N    B SER   B 1 1   ? 50.918 -9.383  -24.009 0.60 28.39 ?  1   SER   B N    1 
ATOM   4204 C CA   A SER   B 1 1   ? 51.230 -10.221 -22.911 0.40 28.72 ?  1   SER   B CA   1 
ATOM   4205 C CA   B SER   B 1 1   ? 51.279 -10.304 -22.908 0.60 28.28 ?  1   SER   B CA   1 
ATOM   4206 C C    A SER   B 1 1   ? 50.190 -11.306 -22.682 0.40 27.27 ?  1   SER   B C    1 
ATOM   4207 C C    B SER   B 1 1   ? 50.158 -11.297 -22.629 0.60 27.75 ?  1   SER   B C    1 
ATOM   4208 O O    A SER   B 1 1   ? 49.005 -11.138 -22.993 0.40 27.00 ?  1   SER   B O    1 
ATOM   4209 O O    B SER   B 1 1   ? 49.004 -11.102 -23.028 0.60 27.10 ?  1   SER   B O    1 
ATOM   4210 C CB   A SER   B 1 1   ? 51.737 -9.701  -21.570 0.40 29.22 ?  1   SER   B CB   1 
ATOM   4211 C CB   B SER   B 1 1   ? 51.622 -9.530  -21.640 0.60 28.45 ?  1   SER   B CB   1 
ATOM   4212 O OG   A SER   B 1 1   ? 50.659 -9.258  -20.767 0.40 30.01 ?  1   SER   B OG   1 
ATOM   4213 O OG   B SER   B 1 1   ? 50.694 -9.810  -20.609 0.60 29.11 ?  1   SER   B OG   1 
ATOM   4214 H H1   A SER   B 1 1   ? 50.382 -9.440  -24.488 0.40 35.41 ?  1   SER   B H1   1 
ATOM   4215 H H1   B SER   B 1 1   ? 51.588 -8.814  -24.140 0.60 34.13 ?  1   SER   B H1   1 
ATOM   4216 H H2   A SER   B 1 1   ? 49.977 -8.764  -23.267 0.40 35.41 ?  1   SER   B H2   1 
ATOM   4217 H H2   B SER   B 1 1   ? 50.776 -9.856  -24.747 0.60 34.13 ?  1   SER   B H2   1 
ATOM   4218 H H3   A SER   B 1 1   ? 51.287 -8.505  -23.841 0.40 35.41 ?  1   SER   B H3   1 
ATOM   4219 H H3   B SER   B 1 1   ? 50.184 -8.940  -23.787 0.60 34.13 ?  1   SER   B H3   1 
ATOM   4220 H HA   A SER   B 1 1   ? 51.972 -10.602 -23.398 0.40 34.52 ?  1   SER   B HA   1 
ATOM   4221 H HA   B SER   B 1 1   ? 52.063 -10.796 -23.183 0.60 33.99 ?  1   SER   B HA   1 
ATOM   4222 H HB2  A SER   B 1 1   ? 52.206 -10.420 -21.118 0.40 35.13 ?  1   SER   B HB2  1 
ATOM   4223 H HB2  B SER   B 1 1   ? 52.506 -9.795  -21.345 0.60 34.20 ?  1   SER   B HB2  1 
ATOM   4224 H HB3  A SER   B 1 1   ? 52.338 -8.957  -21.725 0.40 35.13 ?  1   SER   B HB3  1 
ATOM   4225 H HB3  B SER   B 1 1   ? 51.609 -8.580  -21.837 0.60 34.20 ?  1   SER   B HB3  1 
ATOM   4226 H HG   A SER   B 1 1   ? 50.928 -8.674  -20.230 0.40 36.06 ?  1   SER   B HG   1 
ATOM   4227 H HG   B SER   B 1 1   ? 50.703 -9.186  -20.046 0.60 34.99 ?  1   SER   B HG   1 
ATOM   4228 N N    A MET   B 1 2   ? 50.650 -12.418 -22.125 0.40 25.95 ?  2   MET   B N    1 
ATOM   4229 N N    B MET   B 1 2   ? 50.518 -12.359 -21.918 0.60 27.72 ?  2   MET   B N    1 
ATOM   4230 C CA   A MET   B 1 2   ? 49.834 -13.606 -21.925 0.40 25.19 ?  2   MET   B CA   1 
ATOM   4231 C CA   B MET   B 1 2   ? 49.705 -13.566 -21.806 0.60 27.93 ?  2   MET   B CA   1 
ATOM   4232 C C    A MET   B 1 2   ? 49.619 -13.795 -20.431 0.40 21.93 ?  2   MET   B C    1 
ATOM   4233 C C    B MET   B 1 2   ? 49.453 -13.861 -20.332 0.60 25.53 ?  2   MET   B C    1 
ATOM   4234 O O    A MET   B 1 2   ? 50.580 -13.997 -19.680 0.40 20.85 ?  2   MET   B O    1 
ATOM   4235 O O    B MET   B 1 2   ? 50.303 -14.451 -19.657 0.60 25.87 ?  2   MET   B O    1 
ATOM   4236 C CB   A MET   B 1 2   ? 50.536 -14.817 -22.534 0.40 28.20 ?  2   MET   B CB   1 
ATOM   4237 C CB   B MET   B 1 2   ? 50.455 -14.708 -22.468 0.60 30.93 ?  2   MET   B CB   1 
ATOM   4238 C CG   A MET   B 1 2   ? 49.650 -16.035 -22.731 0.40 30.96 ?  2   MET   B CG   1 
ATOM   4239 C CG   B MET   B 1 2   ? 49.635 -15.946 -22.769 0.60 33.74 ?  2   MET   B CG   1 
ATOM   4240 S SD   A MET   B 1 2   ? 50.465 -17.313 -23.706 0.40 33.42 ?  2   MET   B SD   1 
ATOM   4241 S SD   B MET   B 1 2   ? 50.549 -17.076 -23.836 0.60 36.28 ?  2   MET   B SD   1 
ATOM   4242 C CE   A MET   B 1 2   ? 51.070 -16.315 -25.065 0.40 33.56 ?  2   MET   B CE   1 
ATOM   4243 C CE   B MET   B 1 2   ? 51.254 -15.916 -25.001 0.60 36.46 ?  2   MET   B CE   1 
ATOM   4244 H H    A MET   B 1 2   ? 51.457 -12.513 -21.844 0.40 31.19 ?  2   MET   B H    1 
ATOM   4245 H H    B MET   B 1 2   ? 51.261 -12.412 -21.493 0.60 33.32 ?  2   MET   B H    1 
ATOM   4246 H HA   A MET   B 1 2   ? 48.978 -13.501 -22.369 0.40 30.28 ?  2   MET   B HA   1 
ATOM   4247 H HA   B MET   B 1 2   ? 48.861 -13.442 -22.271 0.60 33.57 ?  2   MET   B HA   1 
ATOM   4248 H HB2  A MET   B 1 2   ? 50.882 -14.540 -23.394 0.40 33.90 ?  2   MET   B HB2  1 
ATOM   4249 H HB2  B MET   B 1 2   ? 50.807 -14.345 -23.290 0.60 37.17 ?  2   MET   B HB2  1 
ATOM   4250 H HB3  A MET   B 1 2   ? 51.266 -15.086 -21.960 0.40 33.90 ?  2   MET   B HB3  1 
ATOM   4251 H HB3  B MET   B 1 2   ? 51.189 -14.987 -21.899 0.60 37.17 ?  2   MET   B HB3  1 
ATOM   4252 H HG2  A MET   B 1 2   ? 49.431 -16.404 -21.861 0.40 37.21 ?  2   MET   B HG2  1 
ATOM   4253 H HG2  B MET   B 1 2   ? 49.429 -16.402 -21.935 0.60 40.54 ?  2   MET   B HG2  1 
ATOM   4254 H HG3  A MET   B 1 2   ? 48.842 -15.777 -23.199 0.40 37.21 ?  2   MET   B HG3  1 
ATOM   4255 H HG3  B MET   B 1 2   ? 48.819 -15.700 -23.225 0.60 40.54 ?  2   MET   B HG3  1 
ATOM   4256 H HE1  A MET   B 1 2   ? 51.226 -16.887 -25.823 0.40 40.32 ?  2   MET   B HE1  1 
ATOM   4257 H HE1  B MET   B 1 2   ? 51.506 -16.396 -25.790 0.60 43.81 ?  2   MET   B HE1  1 
ATOM   4258 H HE2  A MET   B 1 2   ? 50.399 -15.645 -25.281 0.40 40.32 ?  2   MET   B HE2  1 
ATOM   4259 H HE2  B MET   B 1 2   ? 50.584 -15.243 -25.215 0.60 43.81 ?  2   MET   B HE2  1 
ATOM   4260 H HE3  A MET   B 1 2   ? 51.897 -15.873 -24.803 0.40 40.32 ?  2   MET   B HE3  1 
ATOM   4261 H HE3  B MET   B 1 2   ? 52.035 -15.490 -24.602 0.60 43.81 ?  2   MET   B HE3  1 
ATOM   4262 N N    A VAL   B 1 3   ? 48.361 -13.700 -20.003 0.40 19.75 ?  3   VAL   B N    1 
ATOM   4263 N N    B VAL   B 1 3   ? 48.287 -13.456 -19.836 0.60 22.88 ?  3   VAL   B N    1 
ATOM   4264 C CA   A VAL   B 1 3   ? 47.965 -13.933 -18.623 0.40 18.50 ?  3   VAL   B CA   1 
ATOM   4265 C CA   B VAL   B 1 3   ? 47.864 -13.762 -18.476 0.60 20.81 ?  3   VAL   B CA   1 
ATOM   4266 C C    A VAL   B 1 3   ? 46.734 -14.829 -18.639 0.40 17.19 ?  3   VAL   B C    1 
ATOM   4267 C C    B VAL   B 1 3   ? 46.633 -14.655 -18.535 0.60 18.50 ?  3   VAL   B C    1 
ATOM   4268 O O    A VAL   B 1 3   ? 46.033 -14.944 -19.647 0.40 17.19 ?  3   VAL   B O    1 
ATOM   4269 O O    B VAL   B 1 3   ? 45.844 -14.610 -19.484 0.60 18.88 ?  3   VAL   B O    1 
ATOM   4270 C CB   A VAL   B 1 3   ? 47.681 -12.615 -17.866 0.40 19.24 ?  3   VAL   B CB   1 
ATOM   4271 C CB   B VAL   B 1 3   ? 47.594 -12.497 -17.631 0.60 21.43 ?  3   VAL   B CB   1 
ATOM   4272 C CG1  A VAL   B 1 3   ? 48.945 -11.759 -17.786 0.40 19.45 ?  3   VAL   B CG1  1 
ATOM   4273 C CG1  B VAL   B 1 3   ? 48.873 -11.681 -17.457 0.60 21.59 ?  3   VAL   B CG1  1 
ATOM   4274 C CG2  A VAL   B 1 3   ? 46.548 -11.849 -18.536 0.40 19.60 ?  3   VAL   B CG2  1 
ATOM   4275 C CG2  B VAL   B 1 3   ? 46.488 -11.659 -18.255 0.60 21.77 ?  3   VAL   B CG2  1 
ATOM   4276 H H    A VAL   B 1 3   ? 47.702 -13.485 -20.513 0.40 23.76 ?  3   VAL   B H    1 
ATOM   4277 H H    B VAL   B 1 3   ? 47.716 -12.989 -20.283 0.60 27.51 ?  3   VAL   B H    1 
ATOM   4278 H HA   A VAL   B 1 3   ? 48.678 -14.399 -18.158 0.40 22.26 ?  3   VAL   B HA   1 
ATOM   4279 H HA   B VAL   B 1 3   ? 48.568 -14.261 -18.038 0.60 25.03 ?  3   VAL   B HA   1 
ATOM   4280 H HB   A VAL   B 1 3   ? 47.406 -12.825 -16.958 0.40 23.15 ?  3   VAL   B HB   1 
ATOM   4281 H HB   B VAL   B 1 3   ? 47.297 -12.770 -16.749 0.60 25.77 ?  3   VAL   B HB   1 
ATOM   4282 H HG11 A VAL   B 1 3   ? 48.746 -10.947 -17.294 0.40 23.40 ?  3   VAL   B HG11 1 
ATOM   4283 H HG11 B VAL   B 1 3   ? 48.678 -10.899 -16.916 0.60 25.96 ?  3   VAL   B HG11 1 
ATOM   4284 H HG12 A VAL   B 1 3   ? 49.637 -12.261 -17.327 0.40 23.40 ?  3   VAL   B HG12 1 
ATOM   4285 H HG12 B VAL   B 1 3   ? 49.540 -12.231 -17.016 0.60 25.96 ?  3   VAL   B HG12 1 
ATOM   4286 H HG13 A VAL   B 1 3   ? 49.234 -11.540 -18.684 0.40 23.40 ?  3   VAL   B HG13 1 
ATOM   4287 H HG13 B VAL   B 1 3   ? 49.194 -11.408 -18.331 0.60 25.96 ?  3   VAL   B HG13 1 
ATOM   4288 H HG21 A VAL   B 1 3   ? 46.479 -10.973 -18.128 0.40 23.58 ?  3   VAL   B HG21 1 
ATOM   4289 H HG21 B VAL   B 1 3   ? 46.408 -10.828 -17.762 0.60 26.18 ?  3   VAL   B HG21 1 
ATOM   4290 H HG22 A VAL   B 1 3   ? 46.745 -11.761 -19.481 0.40 23.58 ?  3   VAL   B HG22 1 
ATOM   4291 H HG22 B VAL   B 1 3   ? 46.716 -11.474 -19.179 0.60 26.18 ?  3   VAL   B HG22 1 
ATOM   4292 H HG23 A VAL   B 1 3   ? 45.720 -12.338 -18.413 0.40 23.58 ?  3   VAL   B HG23 1 
ATOM   4293 H HG23 B VAL   B 1 3   ? 45.654 -12.152 -18.211 0.60 26.18 ?  3   VAL   B HG23 1 
ATOM   4294 N N    . ASN   B 1 4   ? 46.479 -15.479 -17.505 1.00 16.65 ?  4   ASN   B N    1 
ATOM   4295 C CA   . ASN   B 1 4   ? 45.355 -16.409 -17.397 1.00 15.67 ?  4   ASN   B CA   1 
ATOM   4296 C C    . ASN   B 1 4   ? 45.306 -17.371 -18.585 1.00 16.26 ?  4   ASN   B C    1 
ATOM   4297 O O    . ASN   B 1 4   ? 44.242 -17.644 -19.144 1.00 17.29 ?  4   ASN   B O    1 
ATOM   4298 C CB   . ASN   B 1 4   ? 44.024 -15.670 -17.233 1.00 15.39 ?  4   ASN   B CB   1 
ATOM   4299 C CG   . ASN   B 1 4   ? 43.971 -14.852 -15.967 1.00 14.56 ?  4   ASN   B CG   1 
ATOM   4300 O OD1  . ASN   B 1 4   ? 44.258 -15.356 -14.891 1.00 14.04 ?  4   ASN   B OD1  1 
ATOM   4301 N ND2  . ASN   B 1 4   ? 43.621 -13.576 -16.094 1.00 15.59 ?  4   ASN   B ND2  1 
ATOM   4302 H H    A ASN   B 1 4   ? 46.944 -15.400 -16.787 0.40 20.04 ?  4   ASN   B H    1 
ATOM   4303 H H    B ASN   B 1 4   ? 47.029 -15.524 -16.847 0.60 20.04 ?  4   ASN   B H    1 
ATOM   4304 H HA   . ASN   B 1 4   ? 45.489 -16.941 -16.595 1.00 18.86 ?  4   ASN   B HA   1 
ATOM   4305 H HB2  . ASN   B 1 4   ? 43.899 -15.073 -17.983 1.00 18.52 ?  4   ASN   B HB2  1 
ATOM   4306 H HB3  . ASN   B 1 4   ? 43.306 -16.322 -17.200 1.00 18.52 ?  4   ASN   B HB3  1 
ATOM   4307 H HD21 . ASN   B 1 4   ? 43.575 -13.068 -15.400 1.00 18.77 ?  4   ASN   B HD21 1 
ATOM   4308 H HD22 . ASN   B 1 4   ? 43.426 -13.258 -16.870 1.00 18.77 ?  4   ASN   B HD22 1 
ATOM   4309 N N    . SER   B 1 5   ? 46.469 -17.889 -18.981 1.00 17.96 ?  5   SER   B N    1 
ATOM   4310 C CA   . SER   B 1 5   ? 46.562 -18.809 -20.116 1.00 20.47 ?  5   SER   B CA   1 
ATOM   4311 C C    . SER   B 1 5   ? 46.568 -20.233 -19.575 1.00 21.28 ?  5   SER   B C    1 
ATOM   4312 O O    . SER   B 1 5   ? 47.595 -20.907 -19.514 1.00 23.24 ?  5   SER   B O    1 
ATOM   4313 C CB   . SER   B 1 5   ? 47.799 -18.513 -20.957 1.00 22.64 ?  5   SER   B CB   1 
ATOM   4314 O OG   . SER   B 1 5   ? 48.988 -18.816 -20.246 1.00 25.31 ?  5   SER   B OG   1 
ATOM   4315 H H    . SER   B 1 5   ? 47.232 -17.711 -18.612 1.00 21.60 ?  5   SER   B H    1 
ATOM   4316 H HA   . SER   B 1 5   ? 45.781 -18.702 -20.676 1.00 24.62 ?  5   SER   B HA   1 
ATOM   4317 H HB2  . SER   B 1 5   ? 47.763 -19.047 -21.766 1.00 27.22 ?  5   SER   B HB2  1 
ATOM   4318 H HB3  . SER   B 1 5   ? 47.789 -17.571 -21.182 1.00 27.22 ?  5   SER   B HB3  1 
ATOM   4319 H HG   . SER   B 1 5   ? 49.028 -19.643 -20.103 1.00 30.43 ?  5   SER   B HG   1 
ATOM   4320 N N    . PHE   B 1 6   ? 45.388 -20.689 -19.175 1.00 20.49 ?  6   PHE   B N    1 
ATOM   4321 C CA   . PHE   B 1 6   ? 45.225 -22.036 -18.652 1.00 19.46 ?  6   PHE   B CA   1 
ATOM   4322 C C    . PHE   B 1 6   ? 45.181 -23.027 -19.806 1.00 22.14 ?  6   PHE   B C    1 
ATOM   4323 O O    . PHE   B 1 6   ? 44.545 -22.774 -20.832 1.00 24.56 ?  6   PHE   B O    1 
ATOM   4324 C CB   . PHE   B 1 6   ? 43.933 -22.118 -17.839 1.00 17.95 ?  6   PHE   B CB   1 
ATOM   4325 C CG   . PHE   B 1 6   ? 43.924 -21.231 -16.621 1.00 16.10 ?  6   PHE   B CG   1 
ATOM   4326 C CD1  . PHE   B 1 6   ? 44.426 -21.693 -15.425 1.00 15.11 ?  6   PHE   B CD1  1 
ATOM   4327 C CD2  . PHE   B 1 6   ? 43.406 -19.942 -16.673 1.00 15.58 ?  6   PHE   B CD2  1 
ATOM   4328 C CE1  . PHE   B 1 6   ? 44.413 -20.897 -14.294 1.00 14.95 ?  6   PHE   B CE1  1 
ATOM   4329 C CE2  . PHE   B 1 6   ? 43.403 -19.131 -15.548 1.00 16.07 ?  6   PHE   B CE2  1 
ATOM   4330 C CZ   . PHE   B 1 6   ? 43.909 -19.603 -14.360 1.00 15.49 ?  6   PHE   B CZ   1 
ATOM   4331 H H    . PHE   B 1 6   ? 44.657 -20.234 -19.205 1.00 24.65 ?  6   PHE   B H    1 
ATOM   4332 H HA   . PHE   B 1 6   ? 45.971 -22.259 -18.076 1.00 23.40 ?  6   PHE   B HA   1 
ATOM   4333 H HB2  . PHE   B 1 6   ? 43.191 -21.854 -18.404 1.00 21.60 ?  6   PHE   B HB2  1 
ATOM   4334 H HB3  . PHE   B 1 6   ? 43.810 -23.032 -17.540 1.00 21.60 ?  6   PHE   B HB3  1 
ATOM   4335 H HD1  . PHE   B 1 6   ? 44.778 -22.553 -15.373 1.00 18.18 ?  6   PHE   B HD1  1 
ATOM   4336 H HD2  . PHE   B 1 6   ? 43.064 -19.620 -17.477 1.00 18.76 ?  6   PHE   B HD2  1 
ATOM   4337 H HE1  . PHE   B 1 6   ? 44.770 -21.211 -13.495 1.00 17.99 ?  6   PHE   B HE1  1 
ATOM   4338 H HE2  . PHE   B 1 6   ? 43.052 -18.269 -15.599 1.00 19.34 ?  6   PHE   B HE2  1 
ATOM   4339 H HZ   . PHE   B 1 6   ? 43.905 -19.063 -13.605 1.00 18.64 ?  6   PHE   B HZ   1 
ATOM   4340 N N    A SER   B 1 7   ? 45.857 -24.162 -19.640 0.40 22.30 ?  7   SER   B N    1 
ATOM   4341 N N    B SER   B 1 7   ? 45.883 -24.148 -19.632 0.60 22.27 ?  7   SER   B N    1 
ATOM   4342 C CA   A SER   B 1 7   ? 45.913 -25.163 -20.695 0.40 22.94 ?  7   SER   B CA   1 
ATOM   4343 C CA   B SER   B 1 7   ? 46.064 -25.146 -20.677 0.60 23.17 ?  7   SER   B CA   1 
ATOM   4344 C C    A SER   B 1 7   ? 45.895 -26.562 -20.095 0.40 22.10 ?  7   SER   B C    1 
ATOM   4345 C C    B SER   B 1 7   ? 46.002 -26.541 -20.069 0.60 22.26 ?  7   SER   B C    1 
ATOM   4346 O O    A SER   B 1 7   ? 46.438 -26.801 -19.012 0.40 22.54 ?  7   SER   B O    1 
ATOM   4347 O O    B SER   B 1 7   ? 46.563 -26.788 -18.997 0.60 23.00 ?  7   SER   B O    1 
ATOM   4348 C CB   A SER   B 1 7   ? 47.162 -24.977 -21.569 0.40 24.44 ?  7   SER   B CB   1 
ATOM   4349 C CB   B SER   B 1 7   ? 47.420 -24.953 -21.373 0.60 24.89 ?  7   SER   B CB   1 
ATOM   4350 O OG   A SER   B 1 7   ? 47.084 -25.762 -22.746 0.40 25.79 ?  7   SER   B OG   1 
ATOM   4351 O OG   B SER   B 1 7   ? 47.652 -25.954 -22.348 0.60 26.54 ?  7   SER   B OG   1 
ATOM   4352 H H    A SER   B 1 7   ? 46.295 -24.371 -18.928 0.40 26.82 ?  7   SER   B H    1 
ATOM   4353 H H    B SER   B 1 7   ? 46.274 -24.354 -18.894 0.60 26.79 ?  7   SER   B H    1 
ATOM   4354 H HA   A SER   B 1 7   ? 45.134 -25.068 -21.264 0.40 27.58 ?  7   SER   B HA   1 
ATOM   4355 H HA   B SER   B 1 7   ? 45.360 -25.063 -21.338 0.60 27.86 ?  7   SER   B HA   1 
ATOM   4356 H HB2  A SER   B 1 7   ? 47.235 -24.041 -21.822 0.40 29.38 ?  7   SER   B HB2  1 
ATOM   4357 H HB2  B SER   B 1 7   ? 47.432 -24.078 -21.798 0.60 29.92 ?  7   SER   B HB2  1 
ATOM   4358 H HB3  A SER   B 1 7   ? 47.945 -25.241 -21.060 0.40 29.38 ?  7   SER   B HB3  1 
ATOM   4359 H HB3  B SER   B 1 7   ? 48.125 -25.004 -20.710 0.60 29.92 ?  7   SER   B HB3  1 
ATOM   4360 H HG   A SER   B 1 7   ? 47.778 -25.653 -23.209 0.40 31.00 ?  7   SER   B HG   1 
ATOM   4361 H HG   B SER   B 1 7   ? 48.388 -25.818 -22.730 0.60 31.90 ?  7   SER   B HG   1 
ATOM   4362 N N    A GLY   B 1 8   ? 45.260 -27.488 -20.812 0.40 21.70 ?  8   GLY   B N    1 
ATOM   4363 N N    B GLY   B 1 8   ? 45.318 -27.451 -20.758 0.60 21.98 ?  8   GLY   B N    1 
ATOM   4364 C CA   A GLY   B 1 8   ? 45.227 -28.878 -20.405 0.40 21.17 ?  8   GLY   B CA   1 
ATOM   4365 C CA   B GLY   B 1 8   ? 45.284 -28.836 -20.336 0.60 21.32 ?  8   GLY   B CA   1 
ATOM   4366 C C    A GLY   B 1 8   ? 44.219 -29.218 -19.332 0.40 20.30 ?  8   GLY   B C    1 
ATOM   4367 C C    B GLY   B 1 8   ? 44.321 -29.144 -19.215 0.60 20.25 ?  8   GLY   B C    1 
ATOM   4368 O O    A GLY   B 1 8   ? 44.259 -30.335 -18.802 0.40 20.65 ?  8   GLY   B O    1 
ATOM   4369 O O    B GLY   B 1 8   ? 44.491 -30.160 -18.530 0.60 20.67 ?  8   GLY   B O    1 
ATOM   4370 H H    A GLY   B 1 8   ? 44.841 -27.329 -21.548 0.40 26.10 ?  8   GLY   B H    1 
ATOM   4371 H H    B GLY   B 1 8   ? 44.866 -27.286 -21.470 0.60 26.43 ?  8   GLY   B H    1 
ATOM   4372 H HA2  A GLY   B 1 8   ? 45.033 -29.426 -21.181 0.40 25.46 ?  8   GLY   B HA2  1 
ATOM   4373 H HA2  B GLY   B 1 8   ? 45.050 -29.388 -21.100 0.60 25.64 ?  8   GLY   B HA2  1 
ATOM   4374 H HA3  A GLY   B 1 8   ? 46.103 -29.127 -20.074 0.40 25.46 ?  8   GLY   B HA3  1 
ATOM   4375 H HA3  B GLY   B 1 8   ? 46.169 -29.095 -20.040 0.60 25.64 ?  8   GLY   B HA3  1 
ATOM   4376 N N    . TYR   B 1 9   ? 43.308 -28.306 -19.004 1.00 19.49 ?  9   TYR   B N    1 
ATOM   4377 C CA   . TYR   B 1 9   ? 42.319 -28.562 -17.969 1.00 17.47 ?  9   TYR   B CA   1 
ATOM   4378 C C    . TYR   B 1 9   ? 41.129 -29.338 -18.507 1.00 17.16 ?  9   TYR   B C    1 
ATOM   4379 O O    . TYR   B 1 9   ? 40.728 -29.193 -19.665 1.00 19.52 ?  9   TYR   B O    1 
ATOM   4380 C CB   . TYR   B 1 9   ? 41.817 -27.259 -17.348 1.00 17.22 ?  9   TYR   B CB   1 
ATOM   4381 C CG   . TYR   B 1 9   ? 42.820 -26.640 -16.411 1.00 17.01 ?  9   TYR   B CG   1 
ATOM   4382 C CD1  . TYR   B 1 9   ? 43.943 -25.997 -16.906 1.00 17.53 ?  9   TYR   B CD1  1 
ATOM   4383 C CD2  . TYR   B 1 9   ? 42.660 -26.720 -15.040 1.00 16.43 ?  9   TYR   B CD2  1 
ATOM   4384 C CE1  . TYR   B 1 9   ? 44.879 -25.450 -16.060 1.00 17.72 ?  9   TYR   B CE1  1 
ATOM   4385 C CE2  . TYR   B 1 9   ? 43.587 -26.166 -14.182 1.00 16.73 ?  9   TYR   B CE2  1 
ATOM   4386 C CZ   . TYR   B 1 9   ? 44.698 -25.536 -14.701 1.00 17.75 ?  9   TYR   B CZ   1 
ATOM   4387 O OH   . TYR   B 1 9   ? 45.627 -24.990 -13.853 1.00 18.63 ?  9   TYR   B OH   1 
ATOM   4388 H H    A TYR   B 1 9   ? 43.234 -27.536 -19.377 0.40 23.45 ?  9   TYR   B H    1 
ATOM   4389 H H    B TYR   B 1 9   ? 43.168 -27.586 -19.453 0.60 23.45 ?  9   TYR   B H    1 
ATOM   4390 H HA   . TYR   B 1 9   ? 42.723 -29.089 -17.266 1.00 21.02 ?  9   TYR   B HA   1 
ATOM   4391 H HB2  . TYR   B 1 9   ? 41.624 -26.618 -18.051 1.00 20.72 ?  9   TYR   B HB2  1 
ATOM   4392 H HB3  . TYR   B 1 9   ? 41.014 -27.449 -16.841 1.00 20.72 ?  9   TYR   B HB3  1 
ATOM   4393 H HD1  . TYR   B 1 9   ? 44.070 -25.946 -17.826 1.00 21.10 ?  9   TYR   B HD1  1 
ATOM   4394 H HD2  . TYR   B 1 9   ? 41.909 -27.151 -14.689 1.00 19.77 ?  9   TYR   B HD2  1 
ATOM   4395 H HE1  . TYR   B 1 9   ? 45.627 -25.023 -16.404 1.00 21.32 ?  9   TYR   B HE1  1 
ATOM   4396 H HE2  . TYR   B 1 9   ? 43.461 -26.230 -13.260 1.00 20.14 ?  9   TYR   B HE2  1 
ATOM   4397 H HH   . TYR   B 1 9   ? 46.242 -24.639 -14.297 1.00 22.42 ?  9   TYR   B HH   1 
ATOM   4398 N N    A LEU   B 1 10  ? 40.566 -30.175 -17.644 0.40 16.27 ?  10  LEU   B N    1 
ATOM   4399 N N    B LEU   B 1 10  ? 40.560 -30.164 -17.639 0.60 15.76 ?  10  LEU   B N    1 
ATOM   4400 C CA   A LEU   B 1 10  ? 39.358 -30.927 -17.941 0.40 16.13 ?  10  LEU   B CA   1 
ATOM   4401 C CA   B LEU   B 1 10  ? 39.359 -30.927 -17.934 0.60 15.40 ?  10  LEU   B CA   1 
ATOM   4402 C C    A LEU   B 1 10  ? 38.166 -30.161 -17.384 0.40 15.61 ?  10  LEU   B C    1 
ATOM   4403 C C    B LEU   B 1 10  ? 38.162 -30.165 -17.380 0.60 14.94 ?  10  LEU   B C    1 
ATOM   4404 O O    A LEU   B 1 10  ? 38.177 -29.748 -16.221 0.40 15.35 ?  10  LEU   B O    1 
ATOM   4405 O O    B LEU   B 1 10  ? 38.163 -29.763 -16.215 0.60 14.53 ?  10  LEU   B O    1 
ATOM   4406 C CB   A LEU   B 1 10  ? 39.434 -32.316 -17.306 0.40 17.09 ?  10  LEU   B CB   1 
ATOM   4407 C CB   B LEU   B 1 10  ? 39.454 -32.304 -17.279 0.60 16.33 ?  10  LEU   B CB   1 
ATOM   4408 C CG   A LEU   B 1 10  ? 38.209 -33.195 -17.544 0.40 18.01 ?  10  LEU   B CG   1 
ATOM   4409 C CG   B LEU   B 1 10  ? 38.365 -33.293 -17.674 0.60 17.16 ?  10  LEU   B CG   1 
ATOM   4410 C CD1  A LEU   B 1 10  ? 38.144 -33.638 -18.998 0.40 18.50 ?  10  LEU   B CD1  1 
ATOM   4411 C CD1  B LEU   B 1 10  ? 38.633 -33.856 -19.062 0.60 17.69 ?  10  LEU   B CD1  1 
ATOM   4412 C CD2  A LEU   B 1 10  ? 38.219 -34.386 -16.611 0.40 18.78 ?  10  LEU   B CD2  1 
ATOM   4413 C CD2  B LEU   B 1 10  ? 38.264 -34.402 -16.645 0.60 18.36 ?  10  LEU   B CD2  1 
ATOM   4414 H H    A LEU   B 1 10  ? 40.872 -30.325 -16.854 0.40 19.59 ?  10  LEU   B H    1 
ATOM   4415 H H    B LEU   B 1 10  ? 40.859 -30.299 -16.841 0.60 18.97 ?  10  LEU   B H    1 
ATOM   4416 H HA   A LEU   B 1 10  ? 39.252 -31.027 -18.898 0.40 19.42 ?  10  LEU   B HA   1 
ATOM   4417 H HA   B LEU   B 1 10  ? 39.253 -31.036 -18.889 0.60 18.54 ?  10  LEU   B HA   1 
ATOM   4418 H HB2  A LEU   B 1 10  ? 40.205 -32.783 -17.670 0.40 20.57 ?  10  LEU   B HB2  1 
ATOM   4419 H HB2  B LEU   B 1 10  ? 40.308 -32.701 -17.519 0.60 19.65 ?  10  LEU   B HB2  1 
ATOM   4420 H HB3  A LEU   B 1 10  ? 39.541 -32.215 -16.346 0.40 20.57 ?  10  LEU   B HB3  1 
ATOM   4421 H HB3  B LEU   B 1 10  ? 39.411 -32.193 -16.316 0.60 19.65 ?  10  LEU   B HB3  1 
ATOM   4422 H HG   A LEU   B 1 10  ? 37.408 -32.683 -17.355 0.40 21.67 ?  10  LEU   B HG   1 
ATOM   4423 H HG   B LEU   B 1 10  ? 37.514 -32.830 -17.698 0.60 20.65 ?  10  LEU   B HG   1 
ATOM   4424 H HD11 A LEU   B 1 10  ? 37.391 -34.238 -19.110 0.40 22.26 ?  10  LEU   B HD11 1 
ATOM   4425 H HD11 B LEU   B 1 10  ? 37.934 -34.489 -19.285 0.60 21.28 ?  10  LEU   B HD11 1 
ATOM   4426 H HD12 A LEU   B 1 10  ? 38.033 -32.857 -19.563 0.40 22.26 ?  10  LEU   B HD12 1 
ATOM   4427 H HD12 B LEU   B 1 10  ? 38.636 -33.126 -19.702 0.60 21.28 ?  10  LEU   B HD12 1 
ATOM   4428 H HD13 A LEU   B 1 10  ? 38.969 -34.096 -19.225 0.40 22.26 ?  10  LEU   B HD13 1 
ATOM   4429 H HD13 B LEU   B 1 10  ? 39.495 -34.299 -19.062 0.60 21.28 ?  10  LEU   B HD13 1 
ATOM   4430 H HD21 A LEU   B 1 10  ? 37.434 -34.926 -16.786 0.40 22.59 ?  10  LEU   B HD21 1 
ATOM   4431 H HD21 B LEU   B 1 10  ? 37.578 -35.026 -16.923 0.60 22.09 ?  10  LEU   B HD21 1 
ATOM   4432 H HD22 A LEU   B 1 10  ? 39.023 -34.902 -16.771 0.40 22.59 ?  10  LEU   B HD22 1 
ATOM   4433 H HD22 B LEU   B 1 10  ? 39.120 -34.851 -16.583 0.60 22.09 ?  10  LEU   B HD22 1 
ATOM   4434 H HD23 A LEU   B 1 10  ? 38.205 -34.065 -15.696 0.40 22.59 ?  10  LEU   B HD23 1 
ATOM   4435 H HD23 B LEU   B 1 10  ? 38.031 -34.012 -15.787 0.60 22.09 ?  10  LEU   B HD23 1 
ATOM   4436 N N    . LYS   B 1 11  ? 37.145 -29.975 -18.211 1.00 16.14 ?  11  LYS   B N    1 
ATOM   4437 C CA   . LYS   B 1 11  ? 35.950 -29.255 -17.796 1.00 17.87 ?  11  LYS   B CA   1 
ATOM   4438 C C    . LYS   B 1 11  ? 35.041 -30.179 -16.991 1.00 17.52 ?  11  LYS   B C    1 
ATOM   4439 O O    . LYS   B 1 11  ? 34.629 -31.232 -17.483 1.00 19.11 ?  11  LYS   B O    1 
ATOM   4440 C CB   . LYS   B 1 11  ? 35.229 -28.738 -19.038 1.00 21.33 ?  11  LYS   B CB   1 
ATOM   4441 C CG   . LYS   B 1 11  ? 34.030 -27.856 -18.760 1.00 24.52 ?  11  LYS   B CG   1 
ATOM   4442 C CD   . LYS   B 1 11  ? 33.212 -27.650 -20.029 1.00 27.48 ?  11  LYS   B CD   1 
ATOM   4443 C CE   . LYS   B 1 11  ? 32.192 -26.540 -19.860 1.00 29.54 ?  11  LYS   B CE   1 
ATOM   4444 N NZ   . LYS   B 1 11  ? 32.847 -25.213 -19.715 1.00 30.81 ?  11  LYS   B NZ   1 
ATOM   4445 H H    A LYS   B 1 11  ? 37.119 -30.261 -19.021 0.40 19.42 ?  11  LYS   B H    1 
ATOM   4446 H H    B LYS   B 1 11  ? 37.122 -30.259 -19.022 0.60 19.42 ?  11  LYS   B H    1 
ATOM   4447 H HA   . LYS   B 1 11  ? 36.201 -28.503 -17.238 1.00 21.50 ?  11  LYS   B HA   1 
ATOM   4448 H HB2  . LYS   B 1 11  ? 35.860 -28.219 -19.564 1.00 25.66 ?  11  LYS   B HB2  1 
ATOM   4449 H HB3  . LYS   B 1 11  ? 34.924 -29.498 -19.556 1.00 25.66 ?  11  LYS   B HB3  1 
ATOM   4450 H HG2  . LYS   B 1 11  ? 33.463 -28.280 -18.098 1.00 29.48 ?  11  LYS   B HG2  1 
ATOM   4451 H HG3  . LYS   B 1 11  ? 34.333 -26.992 -18.445 1.00 29.48 ?  11  LYS   B HG3  1 
ATOM   4452 H HD2  . LYS   B 1 11  ? 33.808 -27.411 -20.757 1.00 33.03 ?  11  LYS   B HD2  1 
ATOM   4453 H HD3  . LYS   B 1 11  ? 32.740 -28.471 -20.241 1.00 33.03 ?  11  LYS   B HD3  1 
ATOM   4454 H HE2  . LYS   B 1 11  ? 31.619 -26.513 -20.641 1.00 35.50 ?  11  LYS   B HE2  1 
ATOM   4455 H HE3  . LYS   B 1 11  ? 31.667 -26.710 -19.063 1.00 35.50 ?  11  LYS   B HE3  1 
ATOM   4456 H HZ1  . LYS   B 1 11  ? 32.230 -24.573 -19.665 1.00 37.03 ?  11  LYS   B HZ1  1 
ATOM   4457 H HZ2  . LYS   B 1 11  ? 33.342 -25.195 -18.975 1.00 37.03 ?  11  LYS   B HZ2  1 
ATOM   4458 H HZ3  . LYS   B 1 11  ? 33.372 -25.053 -20.417 1.00 37.03 ?  11  LYS   B HZ3  1 
ATOM   4459 N N    . LEU   B 1 12  ? 34.715 -29.781 -15.761 1.00 16.19 ?  12  LEU   B N    1 
ATOM   4460 C CA   . LEU   B 1 12  ? 33.748 -30.494 -14.930 1.00 15.88 ?  12  LEU   B CA   1 
ATOM   4461 C C    . LEU   B 1 12  ? 32.353 -29.890 -15.016 1.00 16.09 ?  12  LEU   B C    1 
ATOM   4462 O O    . LEU   B 1 12  ? 31.364 -30.610 -15.172 1.00 16.98 ?  12  LEU   B O    1 
ATOM   4463 C CB   . LEU   B 1 12  ? 34.201 -30.516 -13.466 1.00 15.54 ?  12  LEU   B CB   1 
ATOM   4464 C CG   . LEU   B 1 12  ? 35.539 -31.190 -13.173 1.00 15.64 ?  12  LEU   B CG   1 
ATOM   4465 C CD1  . LEU   B 1 12  ? 35.858 -31.135 -11.687 1.00 15.97 ?  12  LEU   B CD1  1 
ATOM   4466 C CD2  . LEU   B 1 12  ? 35.535 -32.625 -13.664 1.00 16.45 ?  12  LEU   B CD2  1 
ATOM   4467 H H    . LEU   B 1 12  ? 35.041 -29.085 -15.386 1.00 19.49 ?  12  LEU   B H    1 
ATOM   4468 H HA   . LEU   B 1 12  ? 33.687 -31.414 -15.242 1.00 19.11 ?  12  LEU   B HA   1 
ATOM   4469 H HB2  . LEU   B 1 12  ? 34.264 -29.601 -13.158 1.00 18.70 ?  12  LEU   B HB2  1 
ATOM   4470 H HB3  . LEU   B 1 12  ? 33.524 -30.984 -12.950 1.00 18.70 ?  12  LEU   B HB3  1 
ATOM   4471 H HG   . LEU   B 1 12  ? 36.240 -30.716 -13.644 1.00 18.83 ?  12  LEU   B HG   1 
ATOM   4472 H HD11 . LEU   B 1 12  ? 36.715 -31.567 -11.528 1.00 19.22 ?  12  LEU   B HD11 1 
ATOM   4473 H HD12 . LEU   B 1 12  ? 35.903 -30.207 -11.404 1.00 19.22 ?  12  LEU   B HD12 1 
ATOM   4474 H HD13 . LEU   B 1 12  ? 35.162 -31.596 -11.192 1.00 19.22 ?  12  LEU   B HD13 1 
ATOM   4475 H HD21 . LEU   B 1 12  ? 36.336 -33.073 -13.344 1.00 19.80 ?  12  LEU   B HD21 1 
ATOM   4476 H HD22 . LEU   B 1 12  ? 34.747 -33.077 -13.323 1.00 19.80 ?  12  LEU   B HD22 1 
ATOM   4477 H HD23 . LEU   B 1 12  ? 35.523 -32.630 -14.635 1.00 19.80 ?  12  LEU   B HD23 1 
ATOM   4478 N N    . THR   B 1 13  ? 32.264 -28.569 -14.895 1.00 16.13 ?  13  THR   B N    1 
ATOM   4479 C CA   . THR   B 1 13  ? 31.032 -27.819 -15.083 1.00 15.85 ?  13  THR   B CA   1 
ATOM   4480 C C    . THR   B 1 13  ? 31.351 -26.608 -15.956 1.00 17.57 ?  13  THR   B C    1 
ATOM   4481 O O    . THR   B 1 13  ? 32.490 -26.406 -16.389 1.00 18.58 ?  13  THR   B O    1 
ATOM   4482 C CB   . THR   B 1 13  ? 30.433 -27.373 -13.744 1.00 16.08 ?  13  THR   B CB   1 
ATOM   4483 O OG1  . THR   B 1 13  ? 31.262 -26.346 -13.191 1.00 15.86 ?  13  THR   B OG1  1 
ATOM   4484 C CG2  . THR   B 1 13  ? 30.340 -28.535 -12.760 1.00 16.77 ?  13  THR   B CG2  1 
ATOM   4485 H H    . THR   B 1 13  ? 32.933 -28.067 -14.692 1.00 19.41 ?  13  THR   B H    1 
ATOM   4486 H HA   . THR   B 1 13  ? 30.378 -28.374 -15.536 1.00 19.08 ?  13  THR   B HA   1 
ATOM   4487 H HB   . THR   B 1 13  ? 29.538 -27.021 -13.887 1.00 19.36 ?  13  THR   B HB   1 
ATOM   4488 H HG1  . THR   B 1 13  ? 30.945 -25.583 -13.382 1.00 19.09 ?  13  THR   B HG1  1 
ATOM   4489 H HG21 . THR   B 1 13  ? 29.835 -28.269 -11.974 1.00 20.18 ?  13  THR   B HG21 1 
ATOM   4490 H HG22 . THR   B 1 13  ? 29.895 -29.288 -13.177 1.00 20.18 ?  13  THR   B HG22 1 
ATOM   4491 H HG23 . THR   B 1 13  ? 31.229 -28.810 -12.482 1.00 20.18 ?  13  THR   B HG23 1 
ATOM   4492 N N    A ASP   B 1 14  ? 30.329 -25.784 -16.197 0.40 18.44 ?  14  ASP   B N    1 
ATOM   4493 N N    B ASP   B 1 14  ? 30.332 -25.791 -16.220 0.60 18.54 ?  14  ASP   B N    1 
ATOM   4494 C CA   A ASP   B 1 14  ? 30.514 -24.609 -17.041 0.40 19.73 ?  14  ASP   B CA   1 
ATOM   4495 C CA   B ASP   B 1 14  ? 30.537 -24.616 -17.059 0.60 20.09 ?  14  ASP   B CA   1 
ATOM   4496 C C    A ASP   B 1 14  ? 31.602 -23.688 -16.506 0.40 18.46 ?  14  ASP   B C    1 
ATOM   4497 C C    B ASP   B 1 14  ? 31.595 -23.675 -16.502 0.60 18.79 ?  14  ASP   B C    1 
ATOM   4498 O O    A ASP   B 1 14  ? 32.213 -22.945 -17.281 0.40 19.46 ?  14  ASP   B O    1 
ATOM   4499 O O    B ASP   B 1 14  ? 32.168 -22.896 -17.270 0.60 20.18 ?  14  ASP   B O    1 
ATOM   4500 C CB   A ASP   B 1 14  ? 29.196 -23.842 -17.174 0.40 22.18 ?  14  ASP   B CB   1 
ATOM   4501 C CB   B ASP   B 1 14  ? 29.223 -23.855 -17.242 0.60 22.88 ?  14  ASP   B CB   1 
ATOM   4502 C CG   A ASP   B 1 14  ? 28.206 -24.523 -18.099 0.40 24.61 ?  14  ASP   B CG   1 
ATOM   4503 C CG   B ASP   B 1 14  ? 28.323 -24.491 -18.284 0.60 25.86 ?  14  ASP   B CG   1 
ATOM   4504 O OD1  A ASP   B 1 14  ? 28.511 -25.616 -18.626 0.40 25.04 ?  14  ASP   B OD1  1 
ATOM   4505 O OD1  B ASP   B 1 14  ? 28.851 -25.155 -19.201 0.60 26.50 ?  14  ASP   B OD1  1 
ATOM   4506 O OD2  A ASP   B 1 14  ? 27.113 -23.951 -18.299 0.40 25.99 -1 14  ASP   B OD2  1 
ATOM   4507 O OD2  B ASP   B 1 14  ? 27.090 -24.325 -18.191 0.60 27.60 -1 14  ASP   B OD2  1 
ATOM   4508 H H    A ASP   B 1 14  ? 29.532 -25.879 -15.886 0.40 22.18 ?  14  ASP   B H    1 
ATOM   4509 H H    B ASP   B 1 14  ? 29.528 -25.894 -15.934 0.60 22.30 ?  14  ASP   B H    1 
ATOM   4510 H HA   A ASP   B 1 14  ? 30.785 -24.892 -17.925 0.40 23.73 ?  14  ASP   B HA   1 
ATOM   4511 H HA   B ASP   B 1 14  ? 30.834 -24.905 -17.935 0.60 24.17 ?  14  ASP   B HA   1 
ATOM   4512 H HB2  A ASP   B 1 14  ? 28.774 -23.779 -16.306 0.40 26.67 ?  14  ASP   B HB2  1 
ATOM   4513 H HB2  B ASP   B 1 14  ? 28.748 -23.837 -16.396 0.60 27.51 ?  14  ASP   B HB2  1 
ATOM   4514 H HB3  A ASP   B 1 14  ? 29.378 -22.956 -17.524 0.40 26.67 ?  14  ASP   B HB3  1 
ATOM   4515 H HB3  B ASP   B 1 14  ? 29.422 -22.948 -17.527 0.60 27.51 ?  14  ASP   B HB3  1 
ATOM   4516 N N    . ASN   B 1 15  ? 31.860 -23.716 -15.196 1.00 16.49 ?  15  ASN   B N    1 
ATOM   4517 C CA   . ASN   B 1 15  ? 32.818 -22.797 -14.590 1.00 14.30 ?  15  ASN   B CA   1 
ATOM   4518 C C    . ASN   B 1 15  ? 33.911 -23.449 -13.753 1.00 13.37 ?  15  ASN   B C    1 
ATOM   4519 O O    . ASN   B 1 15  ? 34.746 -22.717 -13.208 1.00 13.97 ?  15  ASN   B O    1 
ATOM   4520 C CB   . ASN   B 1 15  ? 32.099 -21.742 -13.732 1.00 14.11 ?  15  ASN   B CB   1 
ATOM   4521 C CG   . ASN   B 1 15  ? 31.468 -22.343 -12.495 1.00 14.15 ?  15  ASN   B CG   1 
ATOM   4522 O OD1  . ASN   B 1 15  ? 30.535 -23.151 -12.590 1.00 15.81 ?  15  ASN   B OD1  1 
ATOM   4523 N ND2  . ASN   B 1 15  ? 31.976 -21.983 -11.332 1.00 13.90 ?  15  ASN   B ND2  1 
ATOM   4524 H H    A ASN   B 1 15  ? 31.488 -24.259 -14.640 0.40 19.85 ?  15  ASN   B H    1 
ATOM   4525 H H    B ASN   B 1 15  ? 31.489 -24.260 -14.640 0.60 19.85 ?  15  ASN   B H    1 
ATOM   4526 H HA   . ASN   B 1 15  ? 33.268 -22.320 -15.298 1.00 17.22 ?  15  ASN   B HA   1 
ATOM   4527 H HB2  . ASN   B 1 15  ? 32.745 -21.072 -13.453 1.00 16.99 ?  15  ASN   B HB2  1 
ATOM   4528 H HB3  . ASN   B 1 15  ? 31.398 -21.326 -14.261 1.00 16.99 ?  15  ASN   B HB3  1 
ATOM   4529 H HD21 . ASN   B 1 15  ? 31.652 -22.295 -10.598 1.00 16.73 ?  15  ASN   B HD21 1 
ATOM   4530 H HD22 . ASN   B 1 15  ? 32.634 -21.420 -11.297 1.00 16.73 ?  15  ASN   B HD22 1 
ATOM   4531 N N    . VAL   B 1 16  ? 33.938 -24.775 -13.627 1.00 13.38 ?  16  VAL   B N    1 
ATOM   4532 C CA   . VAL   B 1 16  ? 34.936 -25.465 -12.816 1.00 12.75 ?  16  VAL   B CA   1 
ATOM   4533 C C    . VAL   B 1 16  ? 35.731 -26.404 -13.710 1.00 12.83 ?  16  VAL   B C    1 
ATOM   4534 O O    . VAL   B 1 16  ? 35.152 -27.271 -14.382 1.00 14.15 ?  16  VAL   B O    1 
ATOM   4535 C CB   . VAL   B 1 16  ? 34.307 -26.230 -11.638 1.00 13.05 ?  16  VAL   B CB   1 
ATOM   4536 C CG1  . VAL   B 1 16  ? 35.383 -26.949 -10.836 1.00 13.65 ?  16  VAL   B CG1  1 
ATOM   4537 C CG2  . VAL   B 1 16  ? 33.503 -25.280 -10.756 1.00 13.74 ?  16  VAL   B CG2  1 
ATOM   4538 H H    . VAL   B 1 16  ? 33.379 -25.314 -14.006 1.00 16.12 ?  16  VAL   B H    1 
ATOM   4539 H HA   . VAL   B 1 16  ? 35.551 -24.809 -12.443 1.00 15.36 ?  16  VAL   B HA   1 
ATOM   4540 H HB   . VAL   B 1 16  ? 33.700 -26.901 -11.987 1.00 15.72 ?  16  VAL   B HB   1 
ATOM   4541 H HG11 . VAL   B 1 16  ? 34.999 -27.245 -9.995  1.00 16.44 ?  16  VAL   B HG11 1 
ATOM   4542 H HG12 . VAL   B 1 16  ? 35.704 -27.707 -11.340 1.00 16.44 ?  16  VAL   B HG12 1 
ATOM   4543 H HG13 . VAL   B 1 16  ? 36.110 -26.327 -10.662 1.00 16.44 ?  16  VAL   B HG13 1 
ATOM   4544 H HG21 . VAL   B 1 16  ? 33.163 -25.769 -9.990  1.00 16.54 ?  16  VAL   B HG21 1 
ATOM   4545 H HG22 . VAL   B 1 16  ? 34.080 -24.559 -10.458 1.00 16.54 ?  16  VAL   B HG22 1 
ATOM   4546 H HG23 . VAL   B 1 16  ? 32.764 -24.919 -11.271 1.00 16.54 ?  16  VAL   B HG23 1 
ATOM   4547 N N    . TYR   B 1 17  ? 37.060 -26.241 -13.681 1.00 13.02 ?  17  TYR   B N    1 
ATOM   4548 C CA   . TYR   B 1 17  ? 38.014 -26.986 -14.488 1.00 13.22 ?  17  TYR   B CA   1 
ATOM   4549 C C    . TYR   B 1 17  ? 39.057 -27.601 -13.568 1.00 12.71 ?  17  TYR   B C    1 
ATOM   4550 O O    . TYR   B 1 17  ? 39.325 -27.073 -12.486 1.00 13.33 ?  17  TYR   B O    1 
ATOM   4551 C CB   . TYR   B 1 17  ? 38.727 -26.050 -15.471 1.00 15.08 ?  17  TYR   B CB   1 
ATOM   4552 C CG   . TYR   B 1 17  ? 37.807 -25.285 -16.385 1.00 17.49 ?  17  TYR   B CG   1 
ATOM   4553 C CD1  . TYR   B 1 17  ? 37.186 -24.110 -15.966 1.00 18.44 ?  17  TYR   B CD1  1 
ATOM   4554 C CD2  . TYR   B 1 17  ? 37.553 -25.737 -17.669 1.00 19.20 ?  17  TYR   B CD2  1 
ATOM   4555 C CE1  . TYR   B 1 17  ? 36.337 -23.412 -16.806 1.00 19.93 ?  17  TYR   B CE1  1 
ATOM   4556 C CE2  . TYR   B 1 17  ? 36.711 -25.047 -18.516 1.00 20.49 ?  17  TYR   B CE2  1 
ATOM   4557 C CZ   . TYR   B 1 17  ? 36.106 -23.888 -18.079 1.00 20.89 ?  17  TYR   B CZ   1 
ATOM   4558 O OH   . TYR   B 1 17  ? 35.267 -23.200 -18.923 1.00 22.41 ?  17  TYR   B OH   1 
ATOM   4559 H H    . TYR   B 1 17  ? 37.454 -25.669 -13.160 1.00 15.68 ?  17  TYR   B H    1 
ATOM   4560 H HA   . TYR   B 1 17  ? 37.559 -27.693 -14.978 1.00 15.92 ?  17  TYR   B HA   1 
ATOM   4561 H HB2  . TYR   B 1 17  ? 39.250 -25.410 -14.965 1.00 18.15 ?  17  TYR   B HB2  1 
ATOM   4562 H HB3  . TYR   B 1 17  ? 39.311 -26.585 -16.028 1.00 18.15 ?  17  TYR   B HB3  1 
ATOM   4563 H HD1  . TYR   B 1 17  ? 37.342 -23.791 -15.107 1.00 22.18 ?  17  TYR   B HD1  1 
ATOM   4564 H HD2  . TYR   B 1 17  ? 37.954 -26.520 -17.968 1.00 23.09 ?  17  TYR   B HD2  1 
ATOM   4565 H HE1  . TYR   B 1 17  ? 35.929 -22.627 -16.517 1.00 23.97 ?  17  TYR   B HE1  1 
ATOM   4566 H HE2  . TYR   B 1 17  ? 36.547 -25.365 -19.376 1.00 24.64 ?  17  TYR   B HE2  1 
ATOM   4567 H HH   . TYR   B 1 17  ? 35.208 -23.592 -19.664 1.00 26.95 ?  17  TYR   B HH   1 
ATOM   4568 N N    . ILE   B 1 18  ? 39.676 -28.700 -14.004 1.00 12.58 ?  18  ILE   B N    1 
ATOM   4569 C CA   . ILE   B 1 18  ? 40.609 -29.422 -13.146 1.00 12.73 ?  18  ILE   B CA   1 
ATOM   4570 C C    . ILE   B 1 18  ? 41.781 -29.965 -13.959 1.00 13.06 ?  18  ILE   B C    1 
ATOM   4571 O O    . ILE   B 1 18  ? 41.628 -30.374 -15.114 1.00 14.41 ?  18  ILE   B O    1 
ATOM   4572 C CB   . ILE   B 1 18  ? 39.857 -30.526 -12.357 1.00 12.89 ?  18  ILE   B CB   1 
ATOM   4573 C CG1  . ILE   B 1 18  ? 40.689 -31.055 -11.189 1.00 13.80 ?  18  ILE   B CG1  1 
ATOM   4574 C CG2  . ILE   B 1 18  ? 39.379 -31.644 -13.289 1.00 13.95 ?  18  ILE   B CG2  1 
ATOM   4575 C CD1  . ILE   B 1 18  ? 39.860 -31.876 -10.205 1.00 15.70 ?  18  ILE   B CD1  1 
ATOM   4576 H H    . ILE   B 1 18  ? 39.581 -29.046 -14.787 1.00 15.15 ?  18  ILE   B H    1 
ATOM   4577 H HA   . ILE   B 1 18  ? 40.971 -28.809 -12.489 1.00 15.33 ?  18  ILE   B HA   1 
ATOM   4578 H HB   . ILE   B 1 18  ? 39.062 -30.122 -11.977 1.00 15.53 ?  18  ILE   B HB   1 
ATOM   4579 H HG12 . ILE   B 1 18  ? 41.396 -31.617 -11.525 1.00 16.62 ?  18  ILE   B HG12 1 
ATOM   4580 H HG13 . ILE   B 1 18  ? 41.059 -30.300 -10.701 1.00 16.62 ?  18  ILE   B HG13 1 
ATOM   4581 H HG21 . ILE   B 1 18  ? 38.777 -32.231 -12.797 1.00 16.80 ?  18  ILE   B HG21 1 
ATOM   4582 H HG22 . ILE   B 1 18  ? 38.909 -31.249 -14.037 1.00 16.80 ?  18  ILE   B HG22 1 
ATOM   4583 H HG23 . ILE   B 1 18  ? 40.144 -32.147 -13.602 1.00 16.80 ?  18  ILE   B HG23 1 
ATOM   4584 H HD11 . ILE   B 1 18  ? 40.416 -32.135 -9.454  1.00 18.90 ?  18  ILE   B HD11 1 
ATOM   4585 H HD12 . ILE   B 1 18  ? 39.111 -31.341 -9.890  1.00 18.90 ?  18  ILE   B HD12 1 
ATOM   4586 H HD13 . ILE   B 1 18  ? 39.525 -32.670 -10.656 1.00 18.90 ?  18  ILE   B HD13 1 
ATOM   4587 N N    . LYS   B 1 19  ? 42.960 -29.995 -13.332 1.00 13.44 ?  19  LYS   B N    1 
ATOM   4588 C CA   . LYS   B 1 19  ? 44.171 -30.484 -13.979 1.00 13.81 ?  19  LYS   B CA   1 
ATOM   4589 C C    . LYS   B 1 19  ? 45.065 -31.153 -12.946 1.00 13.51 ?  19  LYS   B C    1 
ATOM   4590 O O    . LYS   B 1 19  ? 45.147 -30.710 -11.801 1.00 13.62 ?  19  LYS   B O    1 
ATOM   4591 C CB   . LYS   B 1 19  ? 44.936 -29.323 -14.632 1.00 15.10 ?  19  LYS   B CB   1 
ATOM   4592 C CG   . LYS   B 1 19  ? 46.187 -29.718 -15.404 1.00 16.53 ?  19  LYS   B CG   1 
ATOM   4593 C CD   . LYS   B 1 19  ? 46.871 -28.478 -15.973 1.00 17.90 ?  19  LYS   B CD   1 
ATOM   4594 C CE   . LYS   B 1 19  ? 48.076 -28.835 -16.824 1.00 19.71 ?  19  LYS   B CE   1 
ATOM   4595 N NZ   . LYS   B 1 19  ? 48.788 -27.623 -17.314 1.00 20.94 ?  19  LYS   B NZ   1 
ATOM   4596 H H    . LYS   B 1 19  ? 43.077 -29.732 -12.519 1.00 16.18 ?  19  LYS   B H    1 
ATOM   4597 H HA   . LYS   B 1 19  ? 43.933 -31.133 -14.662 1.00 16.63 ?  19  LYS   B HA   1 
ATOM   4598 H HB2  . LYS   B 1 19  ? 44.337 -28.878 -15.253 1.00 18.17 ?  19  LYS   B HB2  1 
ATOM   4599 H HB3  . LYS   B 1 19  ? 45.199 -28.704 -13.935 1.00 18.17 ?  19  LYS   B HB3  1 
ATOM   4600 H HG2  . LYS   B 1 19  ? 46.804 -30.168 -14.809 1.00 19.89 ?  19  LYS   B HG2  1 
ATOM   4601 H HG3  . LYS   B 1 19  ? 45.938 -30.300 -16.140 1.00 19.89 ?  19  LYS   B HG3  1 
ATOM   4602 H HD2  . LYS   B 1 19  ? 46.241 -27.991 -16.527 1.00 21.53 ?  19  LYS   B HD2  1 
ATOM   4603 H HD3  . LYS   B 1 19  ? 47.173 -27.918 -15.240 1.00 21.53 ?  19  LYS   B HD3  1 
ATOM   4604 H HE2  . LYS   B 1 19  ? 48.695 -29.361 -16.294 1.00 23.70 ?  19  LYS   B HE2  1 
ATOM   4605 H HE3  . LYS   B 1 19  ? 47.779 -29.348 -17.594 1.00 23.70 ?  19  LYS   B HE3  1 
ATOM   4606 H HZ1  . LYS   B 1 19  ? 49.442 -27.859 -17.871 1.00 25.19 ?  19  LYS   B HZ1  1 
ATOM   4607 H HZ2  . LYS   B 1 19  ? 48.220 -27.090 -17.745 1.00 25.19 ?  19  LYS   B HZ2  1 
ATOM   4608 H HZ3  . LYS   B 1 19  ? 49.138 -27.178 -16.629 1.00 25.19 ?  19  LYS   B HZ3  1 
ATOM   4609 N N    . ASN   B 1 20  ? 45.750 -32.213 -13.368 1.00 14.23 ?  20  ASN   B N    1 
ATOM   4610 C CA   . ASN   B 1 20  ? 46.787 -32.841 -12.553 1.00 15.10 ?  20  ASN   B CA   1 
ATOM   4611 C C    . ASN   B 1 20  ? 48.053 -32.015 -12.743 1.00 15.82 ?  20  ASN   B C    1 
ATOM   4612 O O    . ASN   B 1 20  ? 48.701 -32.084 -13.793 1.00 17.93 ?  20  ASN   B O    1 
ATOM   4613 C CB   . ASN   B 1 20  ? 46.971 -34.287 -12.999 1.00 15.86 ?  20  ASN   B CB   1 
ATOM   4614 C CG   . ASN   B 1 20  ? 48.114 -34.995 -12.300 1.00 17.38 ?  20  ASN   B CG   1 
ATOM   4615 O OD1  . ASN   B 1 20  ? 48.760 -35.862 -12.890 1.00 19.87 ?  20  ASN   B OD1  1 
ATOM   4616 N ND2  . ASN   B 1 20  ? 48.360 -34.654 -11.046 1.00 17.33 ?  20  ASN   B ND2  1 
ATOM   4617 H H    . ASN   B 1 20  ? 45.626 -32.594 -14.127 1.00 17.13 ?  20  ASN   B H    1 
ATOM   4618 H HA   . ASN   B 1 20  ? 46.514 -32.829 -11.617 1.00 18.18 ?  20  ASN   B HA   1 
ATOM   4619 H HB2  . ASN   B 1 20  ? 46.160 -34.783 -12.811 1.00 19.09 ?  20  ASN   B HB2  1 
ATOM   4620 H HB3  . ASN   B 1 20  ? 47.152 -34.295 -13.951 1.00 19.09 ?  20  ASN   B HB3  1 
ATOM   4621 H HD21 . ASN   B 1 20  ? 49.004 -35.021 -10.617 1.00 20.85 ?  20  ASN   B HD21 1 
ATOM   4622 H HD22 . ASN   B 1 20  ? 47.882 -34.044 -10.658 1.00 20.85 ?  20  ASN   B HD22 1 
ATOM   4623 N N    . ALA   B 1 21  ? 48.403 -31.213 -11.735 1.00 15.17 ?  21  ALA   B N    1 
ATOM   4624 C CA   . ALA   B 1 21  ? 49.498 -30.269 -11.888 1.00 16.19 ?  21  ALA   B CA   1 
ATOM   4625 C C    . ALA   B 1 21  ? 49.957 -29.790 -10.521 1.00 15.42 ?  21  ALA   B C    1 
ATOM   4626 O O    . ALA   B 1 21  ? 49.210 -29.824 -9.538  1.00 15.55 ?  21  ALA   B O    1 
ATOM   4627 C CB   . ALA   B 1 21  ? 49.084 -29.086 -12.765 1.00 17.36 ?  21  ALA   B CB   1 
ATOM   4628 H H    . ALA   B 1 21  ? 48.026 -31.207 -10.951 1.00 18.26 ?  21  ALA   B H    1 
ATOM   4629 H HA   . ALA   B 1 21  ? 50.240 -30.723 -12.313 1.00 19.48 ?  21  ALA   B HA   1 
ATOM   4630 H HB1  . ALA   B 1 21  ? 49.859 -28.540 -12.926 1.00 20.89 ?  21  ALA   B HB1  1 
ATOM   4631 H HB2  . ALA   B 1 21  ? 48.737 -29.433 -13.604 1.00 20.89 ?  21  ALA   B HB2  1 
ATOM   4632 H HB3  . ALA   B 1 21  ? 48.394 -28.582 -12.307 1.00 20.89 ?  21  ALA   B HB3  1 
ATOM   4633 N N    . ASP   B 1 22  ? 51.217 -29.353 -10.494 1.00 14.69 ?  22  ASP   B N    1 
ATOM   4634 C CA   . ASP   B 1 22  ? 51.828 -28.647 -9.373  1.00 14.45 ?  22  ASP   B CA   1 
ATOM   4635 C C    . ASP   B 1 22  ? 51.414 -27.178 -9.465  1.00 13.55 ?  22  ASP   B C    1 
ATOM   4636 O O    . ASP   B 1 22  ? 51.732 -26.503 -10.448 1.00 14.12 ?  22  ASP   B O    1 
ATOM   4637 C CB   . ASP   B 1 22  ? 53.345 -28.810 -9.533  1.00 15.91 ?  22  ASP   B CB   1 
ATOM   4638 C CG   . ASP   B 1 22  ? 54.171 -28.066 -8.487  1.00 17.29 ?  22  ASP   B CG   1 
ATOM   4639 O OD1  . ASP   B 1 22  ? 53.818 -26.941 -8.094  1.00 17.78 ?  22  ASP   B OD1  1 
ATOM   4640 O OD2  . ASP   B 1 22  ? 55.228 -28.608 -8.082  1.00 19.48 -1 22  ASP   B OD2  1 
ATOM   4641 H H    . ASP   B 1 22  ? 51.765 -29.460 -11.154 1.00 17.68 ?  22  ASP   B H    1 
ATOM   4642 H HA   . ASP   B 1 22  ? 51.542 -29.029 -8.527  1.00 17.39 ?  22  ASP   B HA   1 
ATOM   4643 H HB2  . ASP   B 1 22  ? 53.573 -29.742 -9.474  1.00 19.15 ?  22  ASP   B HB2  1 
ATOM   4644 H HB3  . ASP   B 1 22  ? 53.603 -28.453 -10.400 1.00 19.15 ?  22  ASP   B HB3  1 
ATOM   4645 N N    . ILE   B 1 23  ? 50.701 -26.683 -8.446  1.00 13.29 ?  23  ILE   B N    1 
ATOM   4646 C CA   . ILE   B 1 23  ? 50.102 -25.347 -8.522  1.00 13.16 ?  23  ILE   B CA   1 
ATOM   4647 C C    . ILE   B 1 23  ? 51.155 -24.254 -8.658  1.00 13.00 ?  23  ILE   B C    1 
ATOM   4648 O O    . ILE   B 1 23  ? 50.879 -23.202 -9.248  1.00 12.78 ?  23  ILE   B O    1 
ATOM   4649 C CB   . ILE   B 1 23  ? 49.159 -25.109 -7.326  1.00 13.65 ?  23  ILE   B CB   1 
ATOM   4650 C CG1  . ILE   B 1 23  ? 48.339 -23.836 -7.527  1.00 14.31 ?  23  ILE   B CG1  1 
ATOM   4651 C CG2  . ILE   B 1 23  ? 49.933 -25.072 -6.023  1.00 14.80 ?  23  ILE   B CG2  1 
ATOM   4652 C CD1  . ILE   B 1 23  ? 47.198 -23.685 -6.537  1.00 15.06 ?  23  ILE   B CD1  1 
ATOM   4653 H H    . ILE   B 1 23  ? 50.554 -27.099 -7.707  1.00 16.01 ?  23  ILE   B H    1 
ATOM   4654 H HA   . ILE   B 1 23  ? 49.557 -25.314 -9.324  1.00 15.85 ?  23  ILE   B HA   1 
ATOM   4655 H HB   . ILE   B 1 23  ? 48.537 -25.855 -7.286  1.00 16.44 ?  23  ILE   B HB   1 
ATOM   4656 H HG12 . ILE   B 1 23  ? 48.929 -23.067 -7.422  1.00 17.23 ?  23  ILE   B HG12 1 
ATOM   4657 H HG13 . ILE   B 1 23  ? 47.965 -23.837 -8.422  1.00 17.23 ?  23  ILE   B HG13 1 
ATOM   4658 H HG21 . ILE   B 1 23  ? 49.307 -25.066 -5.284  1.00 17.81 ?  23  ILE   B HG21 1 
ATOM   4659 H HG22 . ILE   B 1 23  ? 50.502 -25.855 -5.970  1.00 17.81 ?  23  ILE   B HG22 1 
ATOM   4660 H HG23 . ILE   B 1 23  ? 50.477 -24.268 -6.003  1.00 17.81 ?  23  ILE   B HG23 1 
ATOM   4661 H HD11 . ILE   B 1 23  ? 46.687 -22.892 -6.762  1.00 18.13 ?  23  ILE   B HD11 1 
ATOM   4662 H HD12 . ILE   B 1 23  ? 46.630 -24.471 -6.594  1.00 18.13 ?  23  ILE   B HD12 1 
ATOM   4663 H HD13 . ILE   B 1 23  ? 47.561 -23.604 -5.643  1.00 18.13 ?  23  ILE   B HD13 1 
ATOM   4664 N N    . VAL   B 1 24  ? 52.350 -24.460 -8.097  1.00 13.01 ?  24  VAL   B N    1 
ATOM   4665 C CA   . VAL   B 1 24  ? 53.434 -23.488 -8.266  1.00 13.82 ?  24  VAL   B CA   1 
ATOM   4666 C C    . VAL   B 1 24  ? 53.881 -23.439 -9.722  1.00 13.75 ?  24  VAL   B C    1 
ATOM   4667 O O    . VAL   B 1 24  ? 54.015 -22.359 -10.317 1.00 14.13 ?  24  VAL   B O    1 
ATOM   4668 C CB   . VAL   B 1 24  ? 54.615 -23.812 -7.328  1.00 14.64 ?  24  VAL   B CB   1 
ATOM   4669 C CG1  . VAL   B 1 24  ? 55.819 -22.928 -7.652  1.00 14.91 ?  24  VAL   B CG1  1 
ATOM   4670 C CG2  . VAL   B 1 24  ? 54.200 -23.646 -5.879  1.00 15.91 ?  24  VAL   B CG2  1 
ATOM   4671 H H    . VAL   B 1 24  ? 52.552 -25.139 -7.616  1.00 15.67 ?  24  VAL   B H    1 
ATOM   4672 H HA   . VAL   B 1 24  ? 53.105 -22.607 -8.026  1.00 16.64 ?  24  VAL   B HA   1 
ATOM   4673 H HB   . VAL   B 1 24  ? 54.874 -24.740 -7.456  1.00 17.63 ?  24  VAL   B HB   1 
ATOM   4674 H HG11 . VAL   B 1 24  ? 56.401 -22.901 -6.877  1.00 17.95 ?  24  VAL   B HG11 1 
ATOM   4675 H HG12 . VAL   B 1 24  ? 56.291 -23.316 -8.405  1.00 17.95 ?  24  VAL   B HG12 1 
ATOM   4676 H HG13 . VAL   B 1 24  ? 55.507 -22.040 -7.868  1.00 17.95 ?  24  VAL   B HG13 1 
ATOM   4677 H HG21 . VAL   B 1 24  ? 54.929 -23.929 -5.306  1.00 19.15 ?  24  VAL   B HG21 1 
ATOM   4678 H HG22 . VAL   B 1 24  ? 53.994 -22.712 -5.717  1.00 19.15 ?  24  VAL   B HG22 1 
ATOM   4679 H HG23 . VAL   B 1 24  ? 53.414 -24.191 -5.707  1.00 19.15 ?  24  VAL   B HG23 1 
ATOM   4680 N N    . GLU   B 1 25  ? 54.146 -24.611 -10.310 1.00 15.08 ?  25  GLU   B N    1 
ATOM   4681 C CA   . GLU   B 1 25  ? 54.528 -24.656 -11.715 1.00 16.28 ?  25  GLU   B CA   1 
ATOM   4682 C C    . GLU   B 1 25  ? 53.421 -24.103 -12.599 1.00 15.08 ?  25  GLU   B C    1 
ATOM   4683 O O    . GLU   B 1 25  ? 53.689 -23.382 -13.567 1.00 15.67 ?  25  GLU   B O    1 
ATOM   4684 C CB   . GLU   B 1 25  ? 54.901 -26.085 -12.105 1.00 19.95 ?  25  GLU   B CB   1 
ATOM   4685 C CG   . GLU   B 1 25  ? 56.183 -26.553 -11.435 1.00 25.41 ?  25  GLU   B CG   1 
ATOM   4686 C CD   . GLU   B 1 25  ? 57.309 -25.528 -11.521 1.00 30.75 ?  25  GLU   B CD   1 
ATOM   4687 O OE1  . GLU   B 1 25  ? 57.647 -25.096 -12.647 1.00 32.50 ?  25  GLU   B OE1  1 
ATOM   4688 O OE2  . GLU   B 1 25  ? 57.844 -25.134 -10.459 1.00 32.66 -1 25  GLU   B OE2  1 
ATOM   4689 H H    . GLU   B 1 25  ? 54.111 -25.375 -9.916  1.00 18.15 ?  25  GLU   B H    1 
ATOM   4690 H HA   . GLU   B 1 25  ? 55.291 -24.081 -11.847 1.00 19.59 ?  25  GLU   B HA   1 
ATOM   4691 H HB2  . GLU   B 1 25  ? 54.188 -26.688 -11.833 1.00 23.99 ?  25  GLU   B HB2  1 
ATOM   4692 H HB3  . GLU   B 1 25  ? 55.027 -26.132 -13.064 1.00 23.99 ?  25  GLU   B HB3  1 
ATOM   4693 H HG2  . GLU   B 1 25  ? 56.011 -26.710 -10.498 1.00 30.54 ?  25  GLU   B HG2  1 
ATOM   4694 H HG3  . GLU   B 1 25  ? 56.484 -27.366 -11.868 1.00 30.54 ?  25  GLU   B HG3  1 
ATOM   4695 N N    . GLU   B 1 26  ? 52.169 -24.406 -12.263 1.00 13.84 ?  26  GLU   B N    1 
ATOM   4696 C CA   . GLU   B 1 26  ? 51.043 -23.868 -13.016 1.00 14.50 ?  26  GLU   B CA   1 
ATOM   4697 C C    . GLU   B 1 26  ? 51.003 -22.350 -12.931 1.00 14.14 ?  26  GLU   B C    1 
ATOM   4698 O O    . GLU   B 1 26  ? 50.810 -21.670 -13.941 1.00 15.31 ?  26  GLU   B O    1 
ATOM   4699 C CB   . GLU   B 1 26  ? 49.733 -24.450 -12.483 1.00 16.55 ?  26  GLU   B CB   1 
ATOM   4700 C CG   . GLU   B 1 26  ? 49.287 -25.738 -13.140 1.00 19.42 ?  26  GLU   B CG   1 
ATOM   4701 C CD   . GLU   B 1 26  ? 49.068 -25.610 -14.633 1.00 20.85 ?  26  GLU   B CD   1 
ATOM   4702 O OE1  . GLU   B 1 26  ? 48.109 -24.938 -15.067 1.00 21.10 ?  26  GLU   B OE1  1 
ATOM   4703 O OE2  . GLU   B 1 26  ? 49.853 -26.216 -15.373 1.00 22.70 -1 26  GLU   B OE2  1 
ATOM   4704 H H    . GLU   B 1 26  ? 51.944 -24.916 -11.600 1.00 16.66 ?  26  GLU   B H    1 
ATOM   4705 H HA   . GLU   B 1 26  ? 51.134 -24.120 -13.945 1.00 17.45 ?  26  GLU   B HA   1 
ATOM   4706 H HB2  . GLU   B 1 26  ? 49.836 -24.637 -11.533 1.00 19.91 ?  26  GLU   B HB2  1 
ATOM   4707 H HB3  . GLU   B 1 26  ? 49.027 -23.796 -12.605 1.00 19.91 ?  26  GLU   B HB3  1 
ATOM   4708 H HG2  . GLU   B 1 26  ? 49.973 -26.399 -13.022 1.00 23.36 ?  26  GLU   B HG2  1 
ATOM   4709 H HG3  . GLU   B 1 26  ? 48.454 -26.029 -12.736 1.00 23.36 ?  26  GLU   B HG3  1 
ATOM   4710 N N    . ALA   B 1 27  ? 51.152 -21.802 -11.723 1.00 13.52 ?  27  ALA   B N    1 
ATOM   4711 C CA   . ALA   B 1 27  ? 51.116 -20.351 -11.571 1.00 14.27 ?  27  ALA   B CA   1 
ATOM   4712 C C    . ALA   B 1 27  ? 52.185 -19.683 -12.425 1.00 15.10 ?  27  ALA   B C    1 
ATOM   4713 O O    . ALA   B 1 27  ? 51.924 -18.667 -13.081 1.00 15.79 ?  27  ALA   B O    1 
ATOM   4714 C CB   . ALA   B 1 27  ? 51.270 -19.970 -10.100 1.00 14.32 ?  27  ALA   B CB   1 
ATOM   4715 H H    . ALA   B 1 27  ? 51.273 -22.243 -10.989 1.00 16.28 ?  27  ALA   B H    1 
ATOM   4716 H HA   . ALA   B 1 27  ? 50.256 -20.029 -11.869 1.00 17.18 ?  27  ALA   B HA   1 
ATOM   4717 H HB1  . ALA   B 1 27  ? 51.238 -19.004 -10.019 1.00 17.24 ?  27  ALA   B HB1  1 
ATOM   4718 H HB2  . ALA   B 1 27  ? 50.540 -20.367 -9.594  1.00 17.24 ?  27  ALA   B HB2  1 
ATOM   4719 H HB3  . ALA   B 1 27  ? 52.118 -20.303 -9.770  1.00 17.24 ?  27  ALA   B HB3  1 
ATOM   4720 N N    A LYS   B 1 28  ? 53.390 -20.252 -12.458 0.40 16.75 ?  28  LYS   B N    1 
ATOM   4721 N N    B LYS   B 1 28  ? 53.400 -20.230 -12.420 0.60 15.49 ?  28  LYS   B N    1 
ATOM   4722 C CA   A LYS   B 1 28  ? 54.461 -19.630 -13.227 0.40 19.05 ?  28  LYS   B CA   1 
ATOM   4723 C CA   B LYS   B 1 28  ? 54.479 -19.604 -13.175 0.60 17.17 ?  28  LYS   B CA   1 
ATOM   4724 C C    A LYS   B 1 28  ? 54.203 -19.712 -14.730 0.40 19.88 ?  28  LYS   B C    1 
ATOM   4725 C C    B LYS   B 1 28  ? 54.230 -19.686 -14.674 0.60 17.87 ?  28  LYS   B C    1 
ATOM   4726 O O    A LYS   B 1 28  ? 54.596 -18.806 -15.473 0.40 20.26 ?  28  LYS   B O    1 
ATOM   4727 O O    B LYS   B 1 28  ? 54.643 -18.790 -15.419 0.60 18.62 ?  28  LYS   B O    1 
ATOM   4728 C CB   A LYS   B 1 28  ? 55.814 -20.233 -12.835 0.40 21.01 ?  28  LYS   B CB   1 
ATOM   4729 C CB   B LYS   B 1 28  ? 55.824 -20.221 -12.785 0.60 19.22 ?  28  LYS   B CB   1 
ATOM   4730 C CG   A LYS   B 1 28  ? 56.235 -19.869 -11.414 0.40 23.11 ?  28  LYS   B CG   1 
ATOM   4731 C CG   B LYS   B 1 28  ? 56.222 -19.905 -11.344 0.60 21.63 ?  28  LYS   B CG   1 
ATOM   4732 C CD   A LYS   B 1 28  ? 57.649 -20.320 -11.093 0.40 25.18 ?  28  LYS   B CD   1 
ATOM   4733 C CD   B LYS   B 1 28  ? 57.662 -20.281 -11.024 0.60 24.40 ?  28  LYS   B CD   1 
ATOM   4734 C CE   A LYS   B 1 28  ? 57.717 -21.815 -10.869 0.40 26.82 ?  28  LYS   B CE   1 
ATOM   4735 C CE   B LYS   B 1 28  ? 57.780 -21.716 -10.557 0.60 26.58 ?  28  LYS   B CE   1 
ATOM   4736 N NZ   A LYS   B 1 28  ? 59.067 -22.236 -10.402 0.40 27.69 ?  28  LYS   B NZ   1 
ATOM   4737 N NZ   B LYS   B 1 28  ? 59.130 -22.003 -9.993  0.60 27.68 ?  28  LYS   B NZ   1 
ATOM   4738 H H    A LYS   B 1 28  ? 53.607 -20.981 -12.054 0.40 20.16 ?  28  LYS   B H    1 
ATOM   4739 H H    B LYS   B 1 28  ? 53.624 -20.942 -11.998 0.60 18.64 ?  28  LYS   B H    1 
ATOM   4740 H HA   A LYS   B 1 28  ? 54.495 -18.691 -12.994 0.40 22.92 ?  28  LYS   B HA   1 
ATOM   4741 H HA   B LYS   B 1 28  ? 54.514 -18.664 -12.940 0.60 20.66 ?  28  LYS   B HA   1 
ATOM   4742 H HB2  A LYS   B 1 28  ? 55.763 -21.199 -12.889 0.40 25.27 ?  28  LYS   B HB2  1 
ATOM   4743 H HB2  B LYS   B 1 28  ? 55.769 -21.183 -12.874 0.60 23.13 ?  28  LYS   B HB2  1 
ATOM   4744 H HB3  A LYS   B 1 28  ? 56.497 -19.901 -13.438 0.40 25.27 ?  28  LYS   B HB3  1 
ATOM   4745 H HB3  B LYS   B 1 28  ? 56.514 -19.870 -13.370 0.60 23.13 ?  28  LYS   B HB3  1 
ATOM   4746 H HG2  A LYS   B 1 28  ? 56.195 -18.905 -11.308 0.40 27.79 ?  28  LYS   B HG2  1 
ATOM   4747 H HG2  B LYS   B 1 28  ? 56.120 -18.949 -11.195 0.60 26.01 ?  28  LYS   B HG2  1 
ATOM   4748 H HG3  A LYS   B 1 28  ? 55.633 -20.297 -10.785 0.40 27.79 ?  28  LYS   B HG3  1 
ATOM   4749 H HG3  B LYS   B 1 28  ? 55.640 -20.394 -10.744 0.60 26.01 ?  28  LYS   B HG3  1 
ATOM   4750 H HD2  A LYS   B 1 28  ? 58.232 -20.095 -11.835 0.40 30.28 ?  28  LYS   B HD2  1 
ATOM   4751 H HD2  B LYS   B 1 28  ? 58.204 -20.174 -11.822 0.60 29.34 ?  28  LYS   B HD2  1 
ATOM   4752 H HD3  A LYS   B 1 28  ? 57.951 -19.876 -10.284 0.40 30.28 ?  28  LYS   B HD3  1 
ATOM   4753 H HD3  B LYS   B 1 28  ? 57.991 -19.702 -10.318 0.60 29.34 ?  28  LYS   B HD3  1 
ATOM   4754 H HE2  A LYS   B 1 28  ? 57.068 -22.067 -10.193 0.40 32.25 ?  28  LYS   B HE2  1 
ATOM   4755 H HE2  B LYS   B 1 28  ? 57.120 -21.881 -9.865  0.60 31.96 ?  28  LYS   B HE2  1 
ATOM   4756 H HE3  A LYS   B 1 28  ? 57.527 -22.273 -11.703 0.40 32.25 ?  28  LYS   B HE3  1 
ATOM   4757 H HE3  B LYS   B 1 28  ? 57.630 -22.312 -11.309 0.60 31.96 ?  28  LYS   B HE3  1 
ATOM   4758 H HZ1  A LYS   B 1 28  ? 59.085 -23.116 -10.276 0.40 33.29 ?  28  LYS   B HZ1  1 
ATOM   4759 H HZ1  B LYS   B 1 28  ? 59.176 -22.851 -9.725  0.60 33.27 ?  28  LYS   B HZ1  1 
ATOM   4760 H HZ2  A LYS   B 1 28  ? 59.680 -22.017 -11.008 0.40 33.29 ?  28  LYS   B HZ2  1 
ATOM   4761 H HZ2  B LYS   B 1 28  ? 59.755 -21.861 -10.611 0.60 33.27 ?  28  LYS   B HZ2  1 
ATOM   4762 H HZ3  A LYS   B 1 28  ? 59.262 -21.830 -9.633  0.40 33.29 ?  28  LYS   B HZ3  1 
ATOM   4763 H HZ3  B LYS   B 1 28  ? 59.288 -21.472 -9.296  0.60 33.27 ?  28  LYS   B HZ3  1 
ATOM   4764 N N    A LYS   B 1 29  ? 53.523 -20.765 -15.191 0.40 20.93 ?  29  LYS   B N    1 
ATOM   4765 N N    B LYS   B 1 29  ? 53.525 -20.722 -15.129 0.60 19.06 ?  29  LYS   B N    1 
ATOM   4766 C CA   A LYS   B 1 29  ? 53.218 -20.902 -16.614 0.40 22.41 ?  29  LYS   B CA   1 
ATOM   4767 C CA   B LYS   B 1 29  ? 53.235 -20.859 -16.552 0.60 21.26 ?  29  LYS   B CA   1 
ATOM   4768 C C    A LYS   B 1 29  ? 51.960 -20.139 -17.020 0.40 21.15 ?  29  LYS   B C    1 
ATOM   4769 C C    B LYS   B 1 29  ? 52.007 -20.048 -16.958 0.60 20.56 ?  29  LYS   B C    1 
ATOM   4770 O O    A LYS   B 1 29  ? 51.910 -19.570 -18.116 0.40 21.63 ?  29  LYS   B O    1 
ATOM   4771 O O    B LYS   B 1 29  ? 52.031 -19.342 -17.972 0.60 21.38 ?  29  LYS   B O    1 
ATOM   4772 C CB   A LYS   B 1 29  ? 53.070 -22.379 -16.984 0.40 25.53 ?  29  LYS   B CB   1 
ATOM   4773 C CB   B LYS   B 1 29  ? 53.048 -22.338 -16.895 0.60 24.91 ?  29  LYS   B CB   1 
ATOM   4774 C CG   A LYS   B 1 29  ? 52.832 -22.613 -18.471 0.40 28.22 ?  29  LYS   B CG   1 
ATOM   4775 C CG   B LYS   B 1 29  ? 52.934 -22.625 -18.383 0.60 28.06 ?  29  LYS   B CG   1 
ATOM   4776 C CD   A LYS   B 1 29  ? 53.003 -24.074 -18.856 0.40 30.31 ?  29  LYS   B CD   1 
ATOM   4777 C CD   B LYS   B 1 29  ? 53.281 -24.075 -18.706 0.60 30.52 ?  29  LYS   B CD   1 
ATOM   4778 C CE   A LYS   B 1 29  ? 51.923 -24.949 -18.244 0.40 31.76 ?  29  LYS   B CE   1 
ATOM   4779 C CE   B LYS   B 1 29  ? 52.317 -25.054 -18.052 0.60 32.24 ?  29  LYS   B CE   1 
ATOM   4780 N NZ   A LYS   B 1 29  ? 52.077 -26.373 -18.651 0.40 32.62 ?  29  LYS   B NZ   1 
ATOM   4781 N NZ   B LYS   B 1 29  ? 52.641 -26.467 -18.400 0.60 33.30 ?  29  LYS   B NZ   1 
ATOM   4782 H H    A LYS   B 1 29  ? 53.254 -21.415 -14.704 0.40 25.17 ?  29  LYS   B H    1 
ATOM   4783 H H    B LYS   B 1 29  ? 53.205 -21.351 -14.636 0.60 22.93 ?  29  LYS   B H    1 
ATOM   4784 H HA   A LYS   B 1 29  ? 53.951 -20.541 -17.128 0.40 26.95 ?  29  LYS   B HA   1 
ATOM   4785 H HA   B LYS   B 1 29  ? 53.990 -20.528 -17.057 0.60 25.57 ?  29  LYS   B HA   1 
ATOM   4786 H HB2  A LYS   B 1 29  ? 53.883 -22.846 -16.736 0.40 30.69 ?  29  LYS   B HB2  1 
ATOM   4787 H HB2  B LYS   B 1 29  ? 53.813 -22.831 -16.557 0.60 29.95 ?  29  LYS   B HB2  1 
ATOM   4788 H HB3  A LYS   B 1 29  ? 52.316 -22.751 -16.500 0.40 30.69 ?  29  LYS   B HB3  1 
ATOM   4789 H HB3  B LYS   B 1 29  ? 52.239 -22.657 -16.468 0.60 29.95 ?  29  LYS   B HB3  1 
ATOM   4790 H HG2  A LYS   B 1 29  ? 51.926 -22.350 -18.696 0.40 33.92 ?  29  LYS   B HG2  1 
ATOM   4791 H HG2  B LYS   B 1 29  ? 52.022 -22.460 -18.670 0.60 33.73 ?  29  LYS   B HG2  1 
ATOM   4792 H HG3  A LYS   B 1 29  ? 53.469 -22.091 -18.983 0.40 33.92 ?  29  LYS   B HG3  1 
ATOM   4793 H HG3  B LYS   B 1 29  ? 53.548 -22.051 -18.868 0.60 33.73 ?  29  LYS   B HG3  1 
ATOM   4794 H HD2  A LYS   B 1 29  ? 52.951 -24.158 -19.822 0.40 36.42 ?  29  LYS   B HD2  1 
ATOM   4795 H HD2  B LYS   B 1 29  ? 53.239 -24.208 -19.666 0.60 36.68 ?  29  LYS   B HD2  1 
ATOM   4796 H HD3  A LYS   B 1 29  ? 53.865 -24.389 -18.540 0.40 36.42 ?  29  LYS   B HD3  1 
ATOM   4797 H HD3  B LYS   B 1 29  ? 54.174 -24.271 -18.381 0.60 36.68 ?  29  LYS   B HD3  1 
ATOM   4798 H HE2  A LYS   B 1 29  ? 51.982 -24.902 -17.277 0.40 38.17 ?  29  LYS   B HE2  1 
ATOM   4799 H HE2  B LYS   B 1 29  ? 52.369 -24.962 -17.088 0.60 38.74 ?  29  LYS   B HE2  1 
ATOM   4800 H HE3  A LYS   B 1 29  ? 51.053 -24.639 -18.543 0.40 38.17 ?  29  LYS   B HE3  1 
ATOM   4801 H HE3  B LYS   B 1 29  ? 51.415 -24.865 -18.357 0.60 38.74 ?  29  LYS   B HE3  1 
ATOM   4802 H HZ1  A LYS   B 1 29  ? 51.436 -26.866 -18.282 0.40 39.20 ?  29  LYS   B HZ1  1 
ATOM   4803 H HZ1  B LYS   B 1 29  ? 52.062 -27.018 -18.006 0.60 40.02 ?  29  LYS   B HZ1  1 
ATOM   4804 H HZ2  A LYS   B 1 29  ? 52.024 -26.444 -19.537 0.40 39.20 ?  29  LYS   B HZ2  1 
ATOM   4805 H HZ2  B LYS   B 1 29  ? 52.593 -26.582 -19.281 0.60 40.02 ?  29  LYS   B HZ2  1 
ATOM   4806 H HZ3  A LYS   B 1 29  ? 52.869 -26.681 -18.384 0.40 39.20 ?  29  LYS   B HZ3  1 
ATOM   4807 H HZ3  B LYS   B 1 29  ? 53.463 -26.668 -18.126 0.60 40.02 ?  29  LYS   B HZ3  1 
ATOM   4808 N N    . VAL   B 1 30  ? 50.931 -20.135 -16.169 1.00 19.81 ?  30  VAL   B N    1 
ATOM   4809 C CA   . VAL   B 1 30  ? 49.643 -19.536 -16.538 1.00 19.86 ?  30  VAL   B CA   1 
ATOM   4810 C C    . VAL   B 1 30  ? 49.638 -18.023 -16.366 1.00 18.85 ?  30  VAL   B C    1 
ATOM   4811 O O    . VAL   B 1 30  ? 48.906 -17.310 -17.070 1.00 19.78 ?  30  VAL   B O    1 
ATOM   4812 C CB   . VAL   B 1 30  ? 48.532 -20.179 -15.685 1.00 20.90 ?  30  VAL   B CB   1 
ATOM   4813 C CG1  . VAL   B 1 30  ? 47.233 -19.378 -15.772 1.00 21.33 ?  30  VAL   B CG1  1 
ATOM   4814 C CG2  . VAL   B 1 30  ? 48.310 -21.628 -16.102 1.00 21.75 ?  30  VAL   B CG2  1 
ATOM   4815 H H    A VAL   B 1 30  ? 50.948 -20.476 -15.374 0.40 23.83 ?  30  VAL   B H    1 
ATOM   4816 H H    B VAL   B 1 30  ? 50.916 -20.552 -15.411 0.60 23.83 ?  30  VAL   B H    1 
ATOM   4817 H HA   . VAL   B 1 30  ? 49.456 -19.750 -17.467 1.00 23.89 ?  30  VAL   B HA   1 
ATOM   4818 H HB   . VAL   B 1 30  ? 48.809 -20.192 -14.755 1.00 25.13 ?  30  VAL   B HB   1 
ATOM   4819 H HG11 . VAL   B 1 30  ? 46.491 -19.966 -15.559 1.00 25.65 ?  30  VAL   B HG11 1 
ATOM   4820 H HG12 . VAL   B 1 30  ? 47.265 -18.650 -15.135 1.00 25.65 ?  30  VAL   B HG12 1 
ATOM   4821 H HG13 . VAL   B 1 30  ? 47.128 -19.041 -16.671 1.00 25.65 ?  30  VAL   B HG13 1 
ATOM   4822 H HG21 . VAL   B 1 30  ? 47.610 -22.017 -15.550 1.00 26.16 ?  30  VAL   B HG21 1 
ATOM   4823 H HG22 . VAL   B 1 30  ? 48.040 -21.650 -17.035 1.00 26.16 ?  30  VAL   B HG22 1 
ATOM   4824 H HG23 . VAL   B 1 30  ? 49.135 -22.122 -15.985 1.00 26.16 ?  30  VAL   B HG23 1 
ATOM   4825 N N    . LYS   B 1 31  ? 50.410 -17.523 -15.414 1.00 18.21 ?  31  LYS   B N    1 
ATOM   4826 C CA   . LYS   B 1 31  ? 50.429 -16.114 -15.049 1.00 19.08 ?  31  LYS   B CA   1 
ATOM   4827 C C    . LYS   B 1 31  ? 49.019 -15.663 -14.674 1.00 16.82 ?  31  LYS   B C    1 
ATOM   4828 O O    . LYS   B 1 31  ? 48.468 -14.747 -15.298 1.00 17.86 ?  31  LYS   B O    1 
ATOM   4829 C CB   . LYS   B 1 31  ? 51.050 -15.280 -16.177 1.00 22.25 ?  31  LYS   B CB   1 
ATOM   4830 C CG   . LYS   B 1 31  ? 52.447 -15.759 -16.585 1.00 25.70 ?  31  LYS   B CG   1 
ATOM   4831 C CD   . LYS   B 1 31  ? 53.007 -14.947 -17.740 1.00 28.98 ?  31  LYS   B CD   1 
ATOM   4832 C CE   . LYS   B 1 31  ? 54.471 -15.266 -17.979 1.00 31.43 ?  31  LYS   B CE   1 
ATOM   4833 N NZ   . LYS   B 1 31  ? 55.308 -14.924 -16.793 1.00 33.73 ?  31  LYS   B NZ   1 
ATOM   4834 H H    . LYS   B 1 31  ? 50.942 -18.005 -14.949 1.00 21.91 ?  31  LYS   B H    1 
ATOM   4835 H HA   . LYS   B 1 31  ? 50.982 -16.019 -14.270 1.00 22.96 ?  31  LYS   B HA   1 
ATOM   4836 H HB2  . LYS   B 1 31  ? 50.479 -15.324 -16.960 1.00 26.75 ?  31  LYS   B HB2  1 
ATOM   4837 H HB3  . LYS   B 1 31  ? 51.127 -14.362 -15.875 1.00 26.75 ?  31  LYS   B HB3  1 
ATOM   4838 H HG2  . LYS   B 1 31  ? 53.045 -15.672 -15.828 1.00 30.90 ?  31  LYS   B HG2  1 
ATOM   4839 H HG3  . LYS   B 1 31  ? 52.397 -16.689 -16.865 1.00 30.90 ?  31  LYS   B HG3  1 
ATOM   4840 H HD2  . LYS   B 1 31  ? 52.512 -15.160 -18.548 1.00 34.83 ?  31  LYS   B HD2  1 
ATOM   4841 H HD3  . LYS   B 1 31  ? 52.927 -14.004 -17.535 1.00 34.83 ?  31  LYS   B HD3  1 
ATOM   4842 H HE2  . LYS   B 1 31  ? 54.568 -16.216 -18.155 1.00 37.77 ?  31  LYS   B HE2  1 
ATOM   4843 H HE3  . LYS   B 1 31  ? 54.791 -14.751 -18.736 1.00 37.77 ?  31  LYS   B HE3  1 
ATOM   4844 H HZ1  . LYS   B 1 31  ? 56.170 -15.022 -16.990 1.00 40.53 ?  31  LYS   B HZ1  1 
ATOM   4845 H HZ2  . LYS   B 1 31  ? 55.161 -14.080 -16.550 1.00 40.53 ?  31  LYS   B HZ2  1 
ATOM   4846 H HZ3  . LYS   B 1 31  ? 55.105 -15.459 -16.111 1.00 40.53 ?  31  LYS   B HZ3  1 
ATOM   4847 N N    . PRO   B 1 32  ? 48.404 -16.281 -13.661 1.00 14.61 ?  32  PRO   B N    1 
ATOM   4848 C CA   . PRO   B 1 32  ? 47.020 -15.930 -13.319 1.00 13.80 ?  32  PRO   B CA   1 
ATOM   4849 C C    . PRO   B 1 32  ? 46.928 -14.585 -12.623 1.00 13.68 ?  32  PRO   B C    1 
ATOM   4850 O O    . PRO   B 1 32  ? 47.851 -14.155 -11.923 1.00 15.00 ?  32  PRO   B O    1 
ATOM   4851 C CB   . PRO   B 1 32  ? 46.609 -17.048 -12.355 1.00 14.07 ?  32  PRO   B CB   1 
ATOM   4852 C CG   . PRO   B 1 32  ? 47.898 -17.382 -11.661 1.00 14.53 ?  32  PRO   B CG   1 
ATOM   4853 C CD   . PRO   B 1 32  ? 48.964 -17.270 -12.720 1.00 14.68 ?  32  PRO   B CD   1 
ATOM   4854 H HA   . PRO   B 1 32  ? 46.444 -15.946 -14.102 1.00 16.62 ?  32  PRO   B HA   1 
ATOM   4855 H HB2  . PRO   B 1 32  ? 45.948 -16.721 -11.720 1.00 16.94 ?  32  PRO   B HB2  1 
ATOM   4856 H HB3  . PRO   B 1 32  ? 46.271 -17.812 -12.846 1.00 16.94 ?  32  PRO   B HB3  1 
ATOM   4857 H HG2  . PRO   B 1 32  ? 48.057 -16.748 -10.942 1.00 17.50 ?  32  PRO   B HG2  1 
ATOM   4858 H HG3  . PRO   B 1 32  ? 47.856 -18.288 -11.309 1.00 17.50 ?  32  PRO   B HG3  1 
ATOM   4859 H HD2  . PRO   B 1 32  ? 49.785 -16.937 -12.331 1.00 17.67 ?  32  PRO   B HD2  1 
ATOM   4860 H HD3  . PRO   B 1 32  ? 49.089 -18.123 -13.157 1.00 17.67 ?  32  PRO   B HD3  1 
ATOM   4861 N N    . THR   B 1 33  ? 45.773 -13.935 -12.795 1.00 13.45 ?  33  THR   B N    1 
ATOM   4862 C CA   . THR   B 1 33  ? 45.468 -12.757 -11.989 1.00 13.77 ?  33  THR   B CA   1 
ATOM   4863 C C    . THR   B 1 33  ? 45.414 -13.109 -10.509 1.00 13.44 ?  33  THR   B C    1 
ATOM   4864 O O    . THR   B 1 33  ? 45.871 -12.324 -9.665  1.00 14.22 ?  33  THR   B O    1 
ATOM   4865 C CB   . THR   B 1 33  ? 44.148 -12.130 -12.447 1.00 14.47 ?  33  THR   B CB   1 
ATOM   4866 O OG1  . THR   B 1 33  ? 44.209 -11.882 -13.853 1.00 14.48 ?  33  THR   B OG1  1 
ATOM   4867 C CG2  . THR   B 1 33  ? 43.886 -10.819 -11.715 1.00 15.50 ?  33  THR   B CG2  1 
ATOM   4868 H H    . THR   B 1 33  ? 45.157 -14.158 -13.353 1.00 16.19 ?  33  THR   B H    1 
ATOM   4869 H HA   . THR   B 1 33  ? 46.166 -12.104 -12.108 1.00 16.58 ?  33  THR   B HA   1 
ATOM   4870 H HB   . THR   B 1 33  ? 43.414 -12.738 -12.251 1.00 17.42 ?  33  THR   B HB   1 
ATOM   4871 H HG1  . THR   B 1 33  ? 43.488 -11.527 -14.112 1.00 17.43 ?  33  THR   B HG1  1 
ATOM   4872 H HG21 . THR   B 1 33  ? 43.121 -10.373 -12.102 1.00 18.66 ?  33  THR   B HG21 1 
ATOM   4873 H HG22 . THR   B 1 33  ? 43.713 -10.990 -10.775 1.00 18.66 ?  33  THR   B HG22 1 
ATOM   4874 H HG23 . THR   B 1 33  ? 44.663 -10.241 -11.791 1.00 18.66 ?  33  THR   B HG23 1 
ATOM   4875 N N    . VAL   B 1 34  ? 44.880 -14.287 -10.172 1.00 12.68 ?  34  VAL   B N    1 
ATOM   4876 C CA   . VAL   B 1 34  ? 44.681 -14.684 -8.782  1.00 12.14 ?  34  VAL   B CA   1 
ATOM   4877 C C    . VAL   B 1 34  ? 45.123 -16.130 -8.624  1.00 11.25 ?  34  VAL   B C    1 
ATOM   4878 O O    . VAL   B 1 34  ? 44.604 -17.020 -9.312  1.00 11.99 ?  34  VAL   B O    1 
ATOM   4879 C CB   . VAL   B 1 34  ? 43.211 -14.555 -8.340  1.00 13.15 ?  34  VAL   B CB   1 
ATOM   4880 C CG1  . VAL   B 1 34  ? 43.057 -14.973 -6.885  1.00 13.77 ?  34  VAL   B CG1  1 
ATOM   4881 C CG2  . VAL   B 1 34  ? 42.687 -13.139 -8.558  1.00 13.99 ?  34  VAL   B CG2  1 
ATOM   4882 H H    . VAL   B 1 34  ? 44.638 -14.889 -10.735 1.00 15.27 ?  34  VAL   B H    1 
ATOM   4883 H HA   . VAL   B 1 34  ? 45.219 -14.127 -8.195  1.00 14.63 ?  34  VAL   B HA   1 
ATOM   4884 H HB   . VAL   B 1 34  ? 42.664 -15.155 -8.877  1.00 15.84 ?  34  VAL   B HB   1 
ATOM   4885 H HG11 . VAL   B 1 34  ? 42.187 -14.674 -6.560  1.00 16.58 ?  34  VAL   B HG11 1 
ATOM   4886 H HG12 . VAL   B 1 34  ? 43.114 -15.936 -6.819  1.00 16.58 ?  34  VAL   B HG12 1 
ATOM   4887 H HG13 . VAL   B 1 34  ? 43.758 -14.556 -6.362  1.00 16.58 ?  34  VAL   B HG13 1 
ATOM   4888 H HG21 . VAL   B 1 34  ? 41.764 -13.091 -8.248  1.00 16.84 ?  34  VAL   B HG21 1 
ATOM   4889 H HG22 . VAL   B 1 34  ? 43.235 -12.519 -8.064  1.00 16.84 ?  34  VAL   B HG22 1 
ATOM   4890 H HG23 . VAL   B 1 34  ? 42.720 -12.935 -9.508  1.00 16.84 ?  34  VAL   B HG23 1 
ATOM   4891 N N    . VAL   B 1 35  ? 46.041 -16.375 -7.691  1.00 11.06 ?  35  VAL   B N    1 
ATOM   4892 C CA   . VAL   B 1 35  ? 46.282 -17.717 -7.173  1.00 11.07 ?  35  VAL   B CA   1 
ATOM   4893 C C    . VAL   B 1 35  ? 45.737 -17.774 -5.755  1.00 10.41 ?  35  VAL   B C    1 
ATOM   4894 O O    . VAL   B 1 35  ? 45.953 -16.848 -4.962  1.00 10.90 ?  35  VAL   B O    1 
ATOM   4895 C CB   . VAL   B 1 35  ? 47.768 -18.131 -7.254  1.00 11.85 ?  35  VAL   B CB   1 
ATOM   4896 C CG1  . VAL   B 1 35  ? 48.656 -17.295 -6.339  1.00 12.46 ?  35  VAL   B CG1  1 
ATOM   4897 C CG2  . VAL   B 1 35  ? 47.924 -19.631 -6.951  1.00 12.10 ?  35  VAL   B CG2  1 
ATOM   4898 H H    . VAL   B 1 35  ? 46.541 -15.771 -7.335  1.00 13.33 ?  35  VAL   B H    1 
ATOM   4899 H HA   . VAL   B 1 35  ? 45.773 -18.351 -7.705  1.00 13.34 ?  35  VAL   B HA   1 
ATOM   4900 H HB   . VAL   B 1 35  ? 48.074 -17.992 -8.165  1.00 14.28 ?  35  VAL   B HB   1 
ATOM   4901 H HG11 . VAL   B 1 35  ? 49.583 -17.520 -6.516  1.00 15.01 ?  35  VAL   B HG11 1 
ATOM   4902 H HG12 . VAL   B 1 35  ? 48.498 -16.360 -6.522  1.00 15.01 ?  35  VAL   B HG12 1 
ATOM   4903 H HG13 . VAL   B 1 35  ? 48.436 -17.500 -5.417  1.00 15.01 ?  35  VAL   B HG13 1 
ATOM   4904 H HG21 . VAL   B 1 35  ? 48.854 -19.880 -7.045  1.00 14.58 ?  35  VAL   B HG21 1 
ATOM   4905 H HG22 . VAL   B 1 35  ? 47.624 -19.804 -6.043  1.00 14.58 ?  35  VAL   B HG22 1 
ATOM   4906 H HG23 . VAL   B 1 35  ? 47.380 -20.140 -7.577  1.00 14.58 ?  35  VAL   B HG23 1 
ATOM   4907 N N    . VAL   B 1 36  ? 45.022 -18.856 -5.438  1.00 10.66 ?  36  VAL   B N    1 
ATOM   4908 C CA   . VAL   B 1 36  ? 44.480 -19.065 -4.106  1.00 10.25 ?  36  VAL   B CA   1 
ATOM   4909 C C    . VAL   B 1 36  ? 45.489 -19.823 -3.255  1.00 9.83  ?  36  VAL   B C    1 
ATOM   4910 O O    . VAL   B 1 36  ? 46.028 -20.858 -3.675  1.00 10.97 ?  36  VAL   B O    1 
ATOM   4911 C CB   . VAL   B 1 36  ? 43.142 -19.821 -4.180  1.00 10.66 ?  36  VAL   B CB   1 
ATOM   4912 C CG1  . VAL   B 1 36  ? 42.641 -20.178 -2.784  1.00 11.35 ?  36  VAL   B CG1  1 
ATOM   4913 C CG2  . VAL   B 1 36  ? 42.113 -18.993 -4.940  1.00 10.99 ?  36  VAL   B CG2  1 
ATOM   4914 H H    . VAL   B 1 36  ? 44.849 -19.496 -5.986  1.00 12.85 ?  36  VAL   B H    1 
ATOM   4915 H HA   . VAL   B 1 36  ? 44.320 -18.204 -3.688  1.00 12.35 ?  36  VAL   B HA   1 
ATOM   4916 H HB   . VAL   B 1 36  ? 43.278 -20.645 -4.667  1.00 12.85 ?  36  VAL   B HB   1 
ATOM   4917 H HG11 . VAL   B 1 36  ? 41.703 -20.412 -2.836  1.00 13.68 ?  36  VAL   B HG11 1 
ATOM   4918 H HG12 . VAL   B 1 36  ? 43.153 -20.925 -2.442  1.00 13.68 ?  36  VAL   B HG12 1 
ATOM   4919 H HG13 . VAL   B 1 36  ? 42.754 -19.405 -2.201  1.00 13.68 ?  36  VAL   B HG13 1 
ATOM   4920 H HG21 . VAL   B 1 36  ? 41.271 -19.471 -4.954  1.00 13.25 ?  36  VAL   B HG21 1 
ATOM   4921 H HG22 . VAL   B 1 36  ? 42.004 -18.137 -4.500  1.00 13.25 ?  36  VAL   B HG22 1 
ATOM   4922 H HG23 . VAL   B 1 36  ? 42.428 -18.856 -5.852  1.00 13.25 ?  36  VAL   B HG23 1 
ATOM   4923 N N    . ASN   B 1 37  ? 45.712 -19.331 -2.039  1.00 10.35 ?  37  ASN   B N    1 
ATOM   4924 C CA   . ASN   B 1 37  ? 46.468 -20.060 -1.031  1.00 10.68 ?  37  ASN   B CA   1 
ATOM   4925 C C    . ASN   B 1 37  ? 45.519 -20.738 -0.047  1.00 10.73 ?  37  ASN   B C    1 
ATOM   4926 O O    . ASN   B 1 37  ? 44.508 -20.158 0.369   1.00 10.92 ?  37  ASN   B O    1 
ATOM   4927 C CB   . ASN   B 1 37  ? 47.391 -19.111 -0.267  1.00 10.64 ?  37  ASN   B CB   1 
ATOM   4928 C CG   . ASN   B 1 37  ? 48.247 -19.832 0.741   1.00 10.93 ?  37  ASN   B CG   1 
ATOM   4929 O OD1  . ASN   B 1 37  ? 48.588 -21.006 0.556   1.00 11.70 ?  37  ASN   B OD1  1 
ATOM   4930 N ND2  . ASN   B 1 37  ? 48.598 -19.141 1.817   1.00 11.17 ?  37  ASN   B ND2  1 
ATOM   4931 H H    . ASN   B 1 37  ? 45.431 -18.566 -1.769  1.00 12.47 ?  37  ASN   B H    1 
ATOM   4932 H HA   . ASN   B 1 37  ? 47.009 -20.745 -1.456  1.00 12.87 ?  37  ASN   B HA   1 
ATOM   4933 H HB2  . ASN   B 1 37  ? 47.983 -18.674 -0.895  1.00 12.82 ?  37  ASN   B HB2  1 
ATOM   4934 H HB3  . ASN   B 1 37  ? 46.858 -18.460 0.208   1.00 12.82 ?  37  ASN   B HB3  1 
ATOM   4935 H HD21 . ASN   B 1 37  ? 49.083 -19.513 2.427   1.00 13.47 ?  37  ASN   B HD21 1 
ATOM   4936 H HD22 . ASN   B 1 37  ? 48.340 -18.335 1.916   1.00 13.47 ?  37  ASN   B HD22 1 
ATOM   4937 N N    . ALA   B 1 38  ? 45.871 -21.970 0.331   1.00 10.56 ?  38  ALA   B N    1 
ATOM   4938 C CA   . ALA   B 1 38  ? 45.223 -22.717 1.411   1.00 10.96 ?  38  ALA   B CA   1 
ATOM   4939 C C    . ALA   B 1 38  ? 45.806 -22.233 2.737   1.00 10.96 ?  38  ALA   B C    1 
ATOM   4940 O O    . ALA   B 1 38  ? 46.710 -22.841 3.324   1.00 11.85 ?  38  ALA   B O    1 
ATOM   4941 C CB   . ALA   B 1 38  ? 45.438 -24.213 1.219   1.00 11.87 ?  38  ALA   B CB   1 
ATOM   4942 H H    . ALA   B 1 38  ? 46.518 -22.409 -0.031  1.00 12.73 ?  38  ALA   B H    1 
ATOM   4943 H HA   . ALA   B 1 38  ? 44.267 -22.534 1.405   1.00 13.21 ?  38  ALA   B HA   1 
ATOM   4944 H HB1  . ALA   B 1 38  ? 44.994 -24.690 1.945   1.00 14.30 ?  38  ALA   B HB1  1 
ATOM   4945 H HB2  . ALA   B 1 38  ? 45.053 -24.482 0.371   1.00 14.30 ?  38  ALA   B HB2  1 
ATOM   4946 H HB3  . ALA   B 1 38  ? 46.385 -24.402 1.233   1.00 14.30 ?  38  ALA   B HB3  1 
ATOM   4947 N N    . ALA   B 1 39  ? 45.285 -21.094 3.199   1.00 10.88 ?  39  ALA   B N    1 
ATOM   4948 C CA   . ALA   B 1 39  ? 45.837 -20.363 4.326   1.00 11.38 ?  39  ALA   B CA   1 
ATOM   4949 C C    . ALA   B 1 39  ? 45.220 -20.814 5.647   1.00 11.03 ?  39  ALA   B C    1 
ATOM   4950 O O    . ALA   B 1 39  ? 44.193 -21.492 5.690   1.00 11.96 ?  39  ALA   B O    1 
ATOM   4951 C CB   . ALA   B 1 39  ? 45.591 -18.864 4.137   1.00 11.99 ?  39  ALA   B CB   1 
ATOM   4952 H H    . ALA   B 1 39  ? 44.587 -20.717 2.858   1.00 13.11 ?  39  ALA   B H    1 
ATOM   4953 H HA   . ALA   B 1 39  ? 46.794 -20.511 4.366   1.00 13.72 ?  39  ALA   B HA   1 
ATOM   4954 H HB1  . ALA   B 1 39  ? 45.969 -18.385 4.894   1.00 14.44 ?  39  ALA   B HB1  1 
ATOM   4955 H HB2  . ALA   B 1 39  ? 46.024 -18.571 3.317   1.00 14.44 ?  39  ALA   B HB2  1 
ATOM   4956 H HB3  . ALA   B 1 39  ? 44.639 -18.701 4.085   1.00 14.44 ?  39  ALA   B HB3  1 
ATOM   4957 N N    . ASN   B 1 40  ? 45.854 -20.386 6.737   1.00 12.03 ?  40  ASN   B N    1 
ATOM   4958 C CA   . ASN   B 1 40  ? 45.291 -20.440 8.075   1.00 12.67 ?  40  ASN   B CA   1 
ATOM   4959 C C    . ASN   B 1 40  ? 45.123 -19.016 8.608   1.00 12.58 ?  40  ASN   B C    1 
ATOM   4960 O O    . ASN   B 1 40  ? 45.541 -18.036 7.980   1.00 12.78 ?  40  ASN   B O    1 
ATOM   4961 C CB   . ASN   B 1 40  ? 46.137 -21.319 9.014   1.00 13.48 ?  40  ASN   B CB   1 
ATOM   4962 C CG   . ASN   B 1 40  ? 47.596 -20.927 9.031   1.00 14.55 ?  40  ASN   B CG   1 
ATOM   4963 O OD1  . ASN   B 1 40  ? 47.929 -19.744 9.084   1.00 16.10 ?  40  ASN   B OD1  1 
ATOM   4964 N ND2  . ASN   B 1 40  ? 48.479 -21.919 8.996   1.00 14.70 ?  40  ASN   B ND2  1 
ATOM   4965 H H    . ASN   B 1 40  ? 46.648 -20.048 6.716   1.00 14.50 ?  40  ASN   B H    1 
ATOM   4966 H HA   . ASN   B 1 40  ? 44.408 -20.835 8.024   1.00 15.27 ?  40  ASN   B HA   1 
ATOM   4967 H HB2  . ASN   B 1 40  ? 45.792 -21.238 9.917   1.00 16.23 ?  40  ASN   B HB2  1 
ATOM   4968 H HB3  . ASN   B 1 40  ? 46.075 -22.242 8.718   1.00 16.23 ?  40  ASN   B HB3  1 
ATOM   4969 H HD21 . ASN   B 1 40  ? 49.321 -21.749 9.003   1.00 17.70 ?  40  ASN   B HD21 1 
ATOM   4970 H HD22 . ASN   B 1 40  ? 48.208 -22.737 8.957   1.00 17.70 ?  40  ASN   B HD22 1 
ATOM   4971 N N    . VAL   B 1 41  ? 44.474 -18.895 9.770   1.00 12.93 ?  41  VAL   B N    1 
ATOM   4972 C CA   . VAL   B 1 41  ? 44.016 -17.575 10.218  1.00 13.74 ?  41  VAL   B CA   1 
ATOM   4973 C C    . VAL   B 1 41  ? 45.169 -16.627 10.529  1.00 13.70 ?  41  VAL   B C    1 
ATOM   4974 O O    . VAL   B 1 41  ? 44.990 -15.406 10.462  1.00 13.81 ?  41  VAL   B O    1 
ATOM   4975 C CB   . VAL   B 1 41  ? 43.029 -17.653 11.400  1.00 14.75 ?  41  VAL   B CB   1 
ATOM   4976 C CG1  . VAL   B 1 41  ? 41.724 -18.309 10.973  1.00 15.14 ?  41  VAL   B CG1  1 
ATOM   4977 C CG2  . VAL   B 1 41  ? 43.651 -18.358 12.595  1.00 15.72 ?  41  VAL   B CG2  1 
ATOM   4978 H H    . VAL   B 1 41  ? 44.292 -19.540 10.299  1.00 15.58 ?  41  VAL   B H    1 
ATOM   4979 H HA   . VAL   B 1 41  ? 43.528 -17.174 9.487   1.00 16.55 ?  41  VAL   B HA   1 
ATOM   4980 H HB   . VAL   B 1 41  ? 42.815 -16.750 11.682  1.00 17.75 ?  41  VAL   B HB   1 
ATOM   4981 H HG11 . VAL   B 1 41  ? 41.105 -18.301 11.721  1.00 18.22 ?  41  VAL   B HG11 1 
ATOM   4982 H HG12 . VAL   B 1 41  ? 41.350 -17.811 10.229  1.00 18.22 ?  41  VAL   B HG12 1 
ATOM   4983 H HG13 . VAL   B 1 41  ? 41.904 -19.223 10.703  1.00 18.22 ?  41  VAL   B HG13 1 
ATOM   4984 H HG21 . VAL   B 1 41  ? 43.007 -18.378 13.322  1.00 18.92 ?  41  VAL   B HG21 1 
ATOM   4985 H HG22 . VAL   B 1 41  ? 43.886 -19.266 12.341  1.00 18.92 ?  41  VAL   B HG22 1 
ATOM   4986 H HG23 . VAL   B 1 41  ? 44.444 -17.876 12.871  1.00 18.92 ?  41  VAL   B HG23 1 
ATOM   4987 N N    . TYR   B 1 42  ? 46.342 -17.140 10.906  1.00 14.13 ?  42  TYR   B N    1 
ATOM   4988 C CA   . TYR   B 1 42  ? 47.492 -16.283 11.171  1.00 14.85 ?  42  TYR   B CA   1 
ATOM   4989 C C    . TYR   B 1 42  ? 48.453 -16.210 9.989   1.00 13.72 ?  42  TYR   B C    1 
ATOM   4990 O O    . TYR   B 1 42  ? 49.542 -15.644 10.124  1.00 14.93 ?  42  TYR   B O    1 
ATOM   4991 C CB   . TYR   B 1 42  ? 48.201 -16.679 12.473  1.00 16.90 ?  42  TYR   B CB   1 
ATOM   4992 C CG   . TYR   B 1 42  ? 47.584 -16.025 13.701  1.00 17.70 ?  42  TYR   B CG   1 
ATOM   4993 C CD1  . TYR   B 1 42  ? 47.815 -14.682 13.992  1.00 17.02 ?  42  TYR   B CD1  1 
ATOM   4994 C CD2  . TYR   B 1 42  ? 46.769 -16.743 14.561  1.00 19.74 ?  42  TYR   B CD2  1 
ATOM   4995 C CE1  . TYR   B 1 42  ? 47.252 -14.079 15.106  1.00 18.46 ?  42  TYR   B CE1  1 
ATOM   4996 C CE2  . TYR   B 1 42  ? 46.206 -16.153 15.674  1.00 20.14 ?  42  TYR   B CE2  1 
ATOM   4997 C CZ   . TYR   B 1 42  ? 46.446 -14.820 15.943  1.00 20.22 ?  42  TYR   B CZ   1 
ATOM   4998 O OH   . TYR   B 1 42  ? 45.880 -14.236 17.055  1.00 23.00 ?  42  TYR   B OH   1 
ATOM   4999 H H    . TYR   B 1 42  ? 46.494 -17.984 11.007  1.00 17.01 ?  42  TYR   B H    1 
ATOM   5000 H HA   . TYR   B 1 42  ? 47.156 -15.383 11.304  1.00 17.88 ?  42  TYR   B HA   1 
ATOM   5001 H HB2  . TYR   B 1 42  ? 48.143 -17.637 12.583  1.00 20.34 ?  42  TYR   B HB2  1 
ATOM   5002 H HB3  . TYR   B 1 42  ? 49.128 -16.401 12.418  1.00 20.34 ?  42  TYR   B HB3  1 
ATOM   5003 H HD1  . TYR   B 1 42  ? 48.361 -14.177 13.425  1.00 20.48 ?  42  TYR   B HD1  1 
ATOM   5004 H HD2  . TYR   B 1 42  ? 46.600 -17.640 14.381  1.00 23.74 ?  42  TYR   B HD2  1 
ATOM   5005 H HE1  . TYR   B 1 42  ? 47.422 -13.182 15.287  1.00 22.21 ?  42  TYR   B HE1  1 
ATOM   5006 H HE2  . TYR   B 1 42  ? 45.663 -16.651 16.238  1.00 24.23 ?  42  TYR   B HE2  1 
ATOM   5007 H HH   . TYR   B 1 42  ? 46.112 -13.434 17.101  1.00 27.66 ?  42  TYR   B HH   1 
ATOM   5008 N N    . LEU   B 1 43  ? 48.056 -16.728 8.829   1.00 12.87 ?  43  LEU   B N    1 
ATOM   5009 C CA   . LEU   B 1 43  ? 48.868 -16.657 7.616   1.00 12.76 ?  43  LEU   B CA   1 
ATOM   5010 C C    . LEU   B 1 43  ? 50.281 -17.162 7.873   1.00 13.15 ?  43  LEU   B C    1 
ATOM   5011 O O    . LEU   B 1 43  ? 51.262 -16.563 7.436   1.00 13.73 ?  43  LEU   B O    1 
ATOM   5012 C CB   . LEU   B 1 43  ? 48.884 -15.250 7.005   1.00 12.71 ?  43  LEU   B CB   1 
ATOM   5013 C CG   . LEU   B 1 43  ? 47.525 -14.642 6.629   1.00 12.84 ?  43  LEU   B CG   1 
ATOM   5014 C CD1  . LEU   B 1 43  ? 47.731 -13.247 6.058   1.00 14.15 ?  43  LEU   B CD1  1 
ATOM   5015 C CD2  . LEU   B 1 43  ? 46.769 -15.533 5.653   1.00 13.03 ?  43  LEU   B CD2  1 
ATOM   5016 H H    . LEU   B 1 43  ? 47.312 -17.145 8.717   1.00 15.50 ?  43  LEU   B H    1 
ATOM   5017 H HA   . LEU   B 1 43  ? 48.469 -17.245 6.953   1.00 15.36 ?  43  LEU   B HA   1 
ATOM   5018 H HB2  . LEU   B 1 43  ? 49.300 -14.645 7.637   1.00 15.31 ?  43  LEU   B HB2  1 
ATOM   5019 H HB3  . LEU   B 1 43  ? 49.417 -15.279 6.192   1.00 15.31 ?  43  LEU   B HB3  1 
ATOM   5020 H HG   . LEU   B 1 43  ? 46.989 -14.560 7.426   1.00 15.47 ?  43  LEU   B HG   1 
ATOM   5021 H HD11 . LEU   B 1 43  ? 46.865 -12.871 5.819   1.00 17.04 ?  43  LEU   B HD11 1 
ATOM   5022 H HD12 . LEU   B 1 43  ? 48.156 -12.690 6.727   1.00 17.04 ?  43  LEU   B HD12 1 
ATOM   5023 H HD13 . LEU   B 1 43  ? 48.291 -13.302 5.267   1.00 17.04 ?  43  LEU   B HD13 1 
ATOM   5024 H HD21 . LEU   B 1 43  ? 45.965 -15.073 5.359   1.00 15.69 ?  43  LEU   B HD21 1 
ATOM   5025 H HD22 . LEU   B 1 43  ? 47.334 -15.727 4.888   1.00 15.69 ?  43  LEU   B HD22 1 
ATOM   5026 H HD23 . LEU   B 1 43  ? 46.526 -16.361 6.101   1.00 15.69 ?  43  LEU   B HD23 1 
ATOM   5027 N N    . LYS   B 1 44  ? 50.381 -18.290 8.580   1.00 12.88 ?  44  LYS   B N    1 
ATOM   5028 C CA   . LYS   B 1 44  ? 51.650 -18.966 8.816   1.00 13.34 ?  44  LYS   B CA   1 
ATOM   5029 C C    . LYS   B 1 44  ? 51.762 -20.079 7.782   1.00 12.71 ?  44  LYS   B C    1 
ATOM   5030 O O    . LYS   B 1 44  ? 51.059 -21.092 7.863   1.00 13.66 ?  44  LYS   B O    1 
ATOM   5031 C CB   . LYS   B 1 44  ? 51.720 -19.490 10.248  1.00 14.88 ?  44  LYS   B CB   1 
ATOM   5032 C CG   . LYS   B 1 44  ? 51.893 -18.387 11.285  1.00 18.00 ?  44  LYS   B CG   1 
ATOM   5033 C CD   . LYS   B 1 44  ? 53.103 -17.518 10.949  1.00 20.37 ?  44  LYS   B CD   1 
ATOM   5034 C CE   . LYS   B 1 44  ? 53.436 -16.547 12.053  1.00 22.66 ?  44  LYS   B CE   1 
ATOM   5035 N NZ   . LYS   B 1 44  ? 54.680 -15.781 11.770  1.00 24.01 ?  44  LYS   B NZ   1 
ATOM   5036 H H    . LYS   B 1 44  ? 49.708 -18.685 8.944   1.00 15.51 ?  44  LYS   B H    1 
ATOM   5037 H HA   . LYS   B 1 44  ? 52.379 -18.349 8.657   1.00 16.07 ?  44  LYS   B HA   1 
ATOM   5038 H HB2  . LYS   B 1 44  ? 50.891 -19.961 10.448  1.00 17.91 ?  44  LYS   B HB2  1 
ATOM   5039 H HB3  . LYS   B 1 44  ? 52.469 -20.098 10.323  1.00 17.91 ?  44  LYS   B HB3  1 
ATOM   5040 H HG2  . LYS   B 1 44  ? 51.106 -17.826 11.298  1.00 21.66 ?  44  LYS   B HG2  1 
ATOM   5041 H HG3  . LYS   B 1 44  ? 52.040 -18.790 12.158  1.00 21.66 ?  44  LYS   B HG3  1 
ATOM   5042 H HD2  . LYS   B 1 44  ? 53.873 -18.097 10.792  1.00 24.50 ?  44  LYS   B HD2  1 
ATOM   5043 H HD3  . LYS   B 1 44  ? 52.911 -17.002 10.150  1.00 24.50 ?  44  LYS   B HD3  1 
ATOM   5044 H HE2  . LYS   B 1 44  ? 52.708 -15.915 12.138  1.00 27.24 ?  44  LYS   B HE2  1 
ATOM   5045 H HE3  . LYS   B 1 44  ? 53.560 -17.036 12.878  1.00 27.24 ?  44  LYS   B HE3  1 
ATOM   5046 H HZ1  . LYS   B 1 44  ? 54.845 -15.216 12.438  1.00 28.86 ?  44  LYS   B HZ1  1 
ATOM   5047 H HZ2  . LYS   B 1 44  ? 55.369 -16.337 11.683  1.00 28.86 ?  44  LYS   B HZ2  1 
ATOM   5048 H HZ3  . LYS   B 1 44  ? 54.588 -15.316 11.015  1.00 28.86 ?  44  LYS   B HZ3  1 
ATOM   5049 N N    . HIS   B 1 45  ? 52.606 -19.859 6.777   1.00 12.18 ?  45  HIS   B N    1 
ATOM   5050 C CA   . HIS   B 1 45  ? 52.621 -20.695 5.580   1.00 12.80 ?  45  HIS   B CA   1 
ATOM   5051 C C    . HIS   B 1 45  ? 53.638 -21.821 5.745   1.00 14.67 ?  45  HIS   B C    1 
ATOM   5052 O O    . HIS   B 1 45  ? 54.706 -21.833 5.143   1.00 17.02 ?  45  HIS   B O    1 
ATOM   5053 C CB   . HIS   B 1 45  ? 52.934 -19.844 4.362   1.00 12.55 ?  45  HIS   B CB   1 
ATOM   5054 C CG   . HIS   B 1 45  ? 52.069 -18.633 4.256   1.00 12.59 ?  45  HIS   B CG   1 
ATOM   5055 N ND1  . HIS   B 1 45  ? 50.690 -18.700 4.218   1.00 12.57 ?  45  HIS   B ND1  1 
ATOM   5056 C CD2  . HIS   B 1 45  ? 52.393 -17.321 4.193   1.00 13.26 ?  45  HIS   B CD2  1 
ATOM   5057 C CE1  . HIS   B 1 45  ? 50.210 -17.475 4.122   1.00 12.31 ?  45  HIS   B CE1  1 
ATOM   5058 N NE2  . HIS   B 1 45  ? 51.219 -16.621 4.102   1.00 12.97 ?  45  HIS   B NE2  1 
ATOM   5059 H H    . HIS   B 1 45  ? 53.175 -19.214 6.758   1.00 14.68 ?  45  HIS   B H    1 
ATOM   5060 H HA   . HIS   B 1 45  ? 51.743 -21.092 5.456   1.00 15.42 ?  45  HIS   B HA   1 
ATOM   5061 H HB2  . HIS   B 1 45  ? 53.855 -19.558 4.405   1.00 15.11 ?  45  HIS   B HB2  1 
ATOM   5062 H HB3  . HIS   B 1 45  ? 52.796 -20.388 3.561   1.00 15.11 ?  45  HIS   B HB3  1 
ATOM   5063 H HD2  . HIS   B 1 45  ? 53.251 -16.966 4.200   1.00 15.97 ?  45  HIS   B HD2  1 
ATOM   5064 H HE1  . HIS   B 1 45  ? 49.309 -17.256 4.065   1.00 14.83 ?  45  HIS   B HE1  1 
ATOM   5065 H HE2  . HIS   B 1 45  ? 51.146 -15.769 4.049   1.00 15.62 ?  45  HIS   B HE2  1 
ATOM   5066 N N    A GLY   B 1 46  ? 53.269 -22.794 6.574   0.40 15.36 ?  46  GLY   B N    1 
ATOM   5067 N N    B GLY   B 1 46  ? 53.276 -22.784 6.585   0.60 15.36 ?  46  GLY   B N    1 
ATOM   5068 C CA   A GLY   B 1 46  ? 54.196 -23.847 6.944   0.40 16.53 ?  46  GLY   B CA   1 
ATOM   5069 C CA   B GLY   B 1 46  ? 54.199 -23.847 6.927   0.60 16.62 ?  46  GLY   B CA   1 
ATOM   5070 C C    A GLY   B 1 46  ? 54.239 -25.056 6.027   0.40 17.85 ?  46  GLY   B C    1 
ATOM   5071 C C    B GLY   B 1 46  ? 54.229 -25.009 5.952   0.60 18.09 ?  46  GLY   B C    1 
ATOM   5072 O O    A GLY   B 1 46  ? 55.317 -25.468 5.585   0.40 19.70 ?  46  GLY   B O    1 
ATOM   5073 O O    B GLY   B 1 46  ? 55.276 -25.331 5.381   0.60 20.34 ?  46  GLY   B O    1 
ATOM   5074 H H    A GLY   B 1 46  ? 52.491 -22.857 6.944   0.40 18.49 ?  46  GLY   B H    1 
ATOM   5075 H H    B GLY   B 1 46  ? 52.508 -22.836 6.976   0.60 18.49 ?  46  GLY   B H    1 
ATOM   5076 H HA2  A GLY   B 1 46  ? 55.090 -23.473 6.982   0.40 19.89 ?  46  GLY   B HA2  1 
ATOM   5077 H HA2  B GLY   B 1 46  ? 55.095 -23.478 6.983   0.60 20.00 ?  46  GLY   B HA2  1 
ATOM   5078 H HA3  A GLY   B 1 46  ? 53.970 -24.164 7.832   0.40 19.89 ?  46  GLY   B HA3  1 
ATOM   5079 H HA3  B GLY   B 1 46  ? 53.967 -24.194 7.805   0.60 20.00 ?  46  GLY   B HA3  1 
ATOM   5080 N N    . GLY   B 1 47  ? 53.081 -25.649 5.743   1.00 17.77 ?  47  GLY   B N    1 
ATOM   5081 C CA   . GLY   B 1 47  ? 53.019 -26.920 5.051   1.00 15.47 ?  47  GLY   B CA   1 
ATOM   5082 C C    . GLY   B 1 47  ? 52.115 -26.898 3.833   1.00 13.77 ?  47  GLY   B C    1 
ATOM   5083 O O    . GLY   B 1 47  ? 51.478 -25.892 3.526   1.00 14.09 ?  47  GLY   B O    1 
ATOM   5084 H H    A GLY   B 1 47  ? 52.312 -25.334 5.962   0.40 21.38 ?  47  GLY   B H    1 
ATOM   5085 H H    B GLY   B 1 47  ? 52.315 -25.361 6.007   0.60 21.38 ?  47  GLY   B H    1 
ATOM   5086 H HA2  . GLY   B 1 47  ? 53.907 -27.181 4.763   1.00 18.62 ?  47  GLY   B HA2  1 
ATOM   5087 H HA3  . GLY   B 1 47  ? 52.690 -27.600 5.663   1.00 18.62 ?  47  GLY   B HA3  1 
ATOM   5088 N N    . GLY   B 1 48  ? 52.072 -28.039 3.147   1.00 12.89 ?  48  GLY   B N    1 
ATOM   5089 C CA   . GLY   B 1 48  ? 51.158 -28.189 2.029   1.00 12.62 ?  48  GLY   B CA   1 
ATOM   5090 C C    . GLY   B 1 48  ? 51.292 -27.076 1.012   1.00 12.08 ?  48  GLY   B C    1 
ATOM   5091 O O    . GLY   B 1 48  ? 52.396 -26.606 0.700   1.00 12.93 ?  48  GLY   B O    1 
ATOM   5092 H H    . GLY   B 1 48  ? 52.559 -28.722 3.302   1.00 15.52 ?  48  GLY   B H    1 
ATOM   5093 H HA2  . GLY   B 1 48  ? 51.327 -29.033 1.583   1.00 15.20 ?  48  GLY   B HA2  1 
ATOM   5094 H HA3  . GLY   B 1 48  ? 50.242 -28.193 2.354   1.00 15.20 ?  48  GLY   B HA3  1 
ATOM   5095 N N    . VAL   B 1 49  ? 50.142 -26.629 0.496   1.00 12.27 ?  49  VAL   B N    1 
ATOM   5096 C CA   . VAL   B 1 49  ? 50.124 -25.601 -0.544  1.00 12.50 ?  49  VAL   B CA   1 
ATOM   5097 C C    . VAL   B 1 49  ? 50.784 -24.316 -0.054  1.00 11.95 ?  49  VAL   B C    1 
ATOM   5098 O O    . VAL   B 1 49  ? 51.572 -23.693 -0.775  1.00 12.31 ?  49  VAL   B O    1 
ATOM   5099 C CB   . VAL   B 1 49  ? 48.680 -25.345 -1.021  1.00 13.56 ?  49  VAL   B CB   1 
ATOM   5100 C CG1  . VAL   B 1 49  ? 48.615 -24.090 -1.888  1.00 13.74 ?  49  VAL   B CG1  1 
ATOM   5101 C CG2  . VAL   B 1 49  ? 48.129 -26.549 -1.772  1.00 14.83 ?  49  VAL   B CG2  1 
ATOM   5102 H H    . VAL   B 1 49  ? 49.359 -26.900 0.730   1.00 14.78 ?  49  VAL   B H    1 
ATOM   5103 H HA   . VAL   B 1 49  ? 50.630 -25.912 -1.306  1.00 15.06 ?  49  VAL   B HA   1 
ATOM   5104 H HB   . VAL   B 1 49  ? 48.116 -25.194 -0.248  1.00 16.33 ?  49  VAL   B HB   1 
ATOM   5105 H HG11 . VAL   B 1 49  ? 47.792 -24.098 -2.400  1.00 16.54 ?  49  VAL   B HG11 1 
ATOM   5106 H HG12 . VAL   B 1 49  ? 48.636 -23.302 -1.317  1.00 16.54 ?  49  VAL   B HG12 1 
ATOM   5107 H HG13 . VAL   B 1 49  ? 49.376 -24.078 -2.492  1.00 16.54 ?  49  VAL   B HG13 1 
ATOM   5108 H HG21 . VAL   B 1 49  ? 47.219 -26.357 -2.048  1.00 17.86 ?  49  VAL   B HG21 1 
ATOM   5109 H HG22 . VAL   B 1 49  ? 48.684 -26.712 -2.551  1.00 17.86 ?  49  VAL   B HG22 1 
ATOM   5110 H HG23 . VAL   B 1 49  ? 48.145 -27.316 -1.183  1.00 17.86 ?  49  VAL   B HG23 1 
ATOM   5111 N N    . ALA   B 1 50  ? 50.449 -23.879 1.160   1.00 11.89 ?  50  ALA   B N    1 
ATOM   5112 C CA   . ALA   B 1 50  ? 50.964 -22.596 1.639   1.00 11.53 ?  50  ALA   B CA   1 
ATOM   5113 C C    . ALA   B 1 50  ? 52.484 -22.625 1.741   1.00 11.87 ?  50  ALA   B C    1 
ATOM   5114 O O    . ALA   B 1 50  ? 53.167 -21.655 1.379   1.00 12.28 ?  50  ALA   B O    1 
ATOM   5115 C CB   . ALA   B 1 50  ? 50.337 -22.247 2.989   1.00 11.90 ?  50  ALA   B CB   1 
ATOM   5116 H H    . ALA   B 1 50  ? 49.944 -24.296 1.718   1.00 14.32 ?  50  ALA   B H    1 
ATOM   5117 H HA   . ALA   B 1 50  ? 50.729 -21.902 1.015   1.00 13.89 ?  50  ALA   B HA   1 
ATOM   5118 H HB1  . ALA   B 1 50  ? 50.688 -21.393 3.295   1.00 14.34 ?  50  ALA   B HB1  1 
ATOM   5119 H HB2  . ALA   B 1 50  ? 49.375 -22.189 2.888   1.00 14.34 ?  50  ALA   B HB2  1 
ATOM   5120 H HB3  . ALA   B 1 50  ? 50.559 -22.939 3.636   1.00 14.34 ?  50  ALA   B HB3  1 
ATOM   5121 N N    . GLY   B 1 51  ? 53.034 -23.722 2.254   1.00 12.47 ?  51  GLY   B N    1 
ATOM   5122 C CA   . GLY   B 1 51  ? 54.478 -23.823 2.329   1.00 12.92 ?  51  GLY   B CA   1 
ATOM   5123 C C    . GLY   B 1 51  ? 55.128 -23.765 0.961   1.00 12.76 ?  51  GLY   B C    1 
ATOM   5124 O O    . GLY   B 1 51  ? 56.169 -23.127 0.784   1.00 13.72 ?  51  GLY   B O    1 
ATOM   5125 H H    . GLY   B 1 51  ? 52.608 -24.408 2.555   1.00 15.02 ?  51  GLY   B H    1 
ATOM   5126 H HA2  . GLY   B 1 51  ? 54.830 -23.094 2.867   1.00 15.56 ?  51  GLY   B HA2  1 
ATOM   5127 H HA3  . GLY   B 1 51  ? 54.727 -24.662 2.755   1.00 15.56 ?  51  GLY   B HA3  1 
ATOM   5128 N N    . ALA   B 1 52  ? 54.526 -24.431 -0.025  1.00 12.73 ?  52  ALA   B N    1 
ATOM   5129 C CA   . ALA   B 1 52  ? 55.087 -24.432 -1.369  1.00 12.99 ?  52  ALA   B CA   1 
ATOM   5130 C C    . ALA   B 1 52  ? 55.002 -23.054 -2.018  1.00 12.66 ?  52  ALA   B C    1 
ATOM   5131 O O    . ALA   B 1 52  ? 55.969 -22.601 -2.648  1.00 13.12 ?  52  ALA   B O    1 
ATOM   5132 C CB   . ALA   B 1 52  ? 54.381 -25.474 -2.226  1.00 13.82 ?  52  ALA   B CB   1 
ATOM   5133 H H    . ALA   B 1 52  ? 53.790 -24.876 0.062   1.00 15.33 ?  52  ALA   B H    1 
ATOM   5134 H HA   . ALA   B 1 52  ? 56.022 -24.679 -1.308  1.00 15.65 ?  52  ALA   B HA   1 
ATOM   5135 H HB1  . ALA   B 1 52  ? 54.771 -25.463 -3.114  1.00 16.64 ?  52  ALA   B HB1  1 
ATOM   5136 H HB2  . ALA   B 1 52  ? 54.503 -26.348 -1.822  1.00 16.64 ?  52  ALA   B HB2  1 
ATOM   5137 H HB3  . ALA   B 1 52  ? 53.439 -25.258 -2.273  1.00 16.64 ?  52  ALA   B HB3  1 
ATOM   5138 N N    . LEU   B 1 53  ? 53.855 -22.380 -1.900  1.00 12.07 ?  53  LEU   B N    1 
ATOM   5139 C CA   . LEU   B 1 53  ? 53.741 -21.038 -2.464  1.00 12.27 ?  53  LEU   B CA   1 
ATOM   5140 C C    . LEU   B 1 53  ? 54.745 -20.097 -1.811  1.00 11.99 ?  53  LEU   B C    1 
ATOM   5141 O O    . LEU   B 1 53  ? 55.447 -19.341 -2.494  1.00 12.95 ?  53  LEU   B O    1 
ATOM   5142 C CB   . LEU   B 1 53  ? 52.314 -20.510 -2.293  1.00 12.61 ?  53  LEU   B CB   1 
ATOM   5143 C CG   . LEU   B 1 53  ? 51.188 -21.231 -3.042  1.00 13.00 ?  53  LEU   B CG   1 
ATOM   5144 C CD1  . LEU   B 1 53  ? 49.850 -20.606 -2.703  1.00 14.43 ?  53  LEU   B CD1  1 
ATOM   5145 C CD2  . LEU   B 1 53  ? 51.406 -21.224 -4.542  1.00 14.60 ?  53  LEU   B CD2  1 
ATOM   5146 H H    . LEU   B 1 53  ? 53.152 -22.673 -1.504  1.00 14.54 ?  53  LEU   B H    1 
ATOM   5147 H HA   . LEU   B 1 53  ? 53.941 -21.083 -3.414  1.00 14.78 ?  53  LEU   B HA   1 
ATOM   5148 H HB2  . LEU   B 1 53  ? 52.096 -20.554 -1.351  1.00 15.19 ?  53  LEU   B HB2  1 
ATOM   5149 H HB3  . LEU   B 1 53  ? 52.304 -19.592 -2.586  1.00 15.19 ?  53  LEU   B HB3  1 
ATOM   5150 H HG   . LEU   B 1 53  ? 51.157 -22.157 -2.753  1.00 15.66 ?  53  LEU   B HG   1 
ATOM   5151 H HD11 . LEU   B 1 53  ? 49.149 -21.071 -3.184  1.00 17.38 ?  53  LEU   B HD11 1 
ATOM   5152 H HD12 . LEU   B 1 53  ? 49.700 -20.679 -1.746  1.00 17.38 ?  53  LEU   B HD12 1 
ATOM   5153 H HD13 . LEU   B 1 53  ? 49.864 -19.670 -2.963  1.00 17.38 ?  53  LEU   B HD13 1 
ATOM   5154 H HD21 . LEU   B 1 53  ? 50.665 -21.680 -4.973  1.00 17.58 ?  53  LEU   B HD21 1 
ATOM   5155 H HD22 . LEU   B 1 53  ? 51.452 -20.307 -4.851  1.00 17.58 ?  53  LEU   B HD22 1 
ATOM   5156 H HD23 . LEU   B 1 53  ? 52.236 -21.685 -4.744  1.00 17.58 ?  53  LEU   B HD23 1 
ATOM   5157 N N    . ASN   B 1 54  ? 54.831 -20.128 -0.485  1.00 12.15 ?  54  ASN   B N    1 
ATOM   5158 C CA   . ASN   B 1 54  ? 55.748 -19.219 0.189   1.00 12.93 ?  54  ASN   B CA   1 
ATOM   5159 C C    . ASN   B 1 54  ? 57.190 -19.492 -0.215  1.00 13.00 ?  54  ASN   B C    1 
ATOM   5160 O O    . ASN   B 1 54  ? 57.964 -18.556 -0.462  1.00 13.45 ?  54  ASN   B O    1 
ATOM   5161 C CB   . ASN   B 1 54  ? 55.587 -19.304 1.700   1.00 13.34 ?  54  ASN   B CB   1 
ATOM   5162 C CG   . ASN   B 1 54  ? 56.563 -18.398 2.416   1.00 13.56 ?  54  ASN   B CG   1 
ATOM   5163 O OD1  . ASN   B 1 54  ? 56.579 -17.185 2.175   1.00 13.70 ?  54  ASN   B OD1  1 
ATOM   5164 N ND2  . ASN   B 1 54  ? 57.409 -18.976 3.262   1.00 15.28 ?  54  ASN   B ND2  1 
ATOM   5165 H H    . ASN   B 1 54  ? 54.380 -20.651 0.032   1.00 14.63 ?  54  ASN   B H    1 
ATOM   5166 H HA   . ASN   B 1 54  ? 55.531 -18.316 -0.080  1.00 15.57 ?  54  ASN   B HA   1 
ATOM   5167 H HB2  . ASN   B 1 54  ? 54.684 -19.025 1.939   1.00 16.07 ?  54  ASN   B HB2  1 
ATOM   5168 H HB3  . ASN   B 1 54  ? 55.742 -20.212 1.991   1.00 16.07 ?  54  ASN   B HB3  1 
ATOM   5169 H HD21 . ASN   B 1 54  ? 57.987 -18.503 3.684   1.00 18.40 ?  54  ASN   B HD21 1 
ATOM   5170 H HD22 . ASN   B 1 54  ? 57.370 -19.827 3.393   1.00 18.40 ?  54  ASN   B HD22 1 
ATOM   5171 N N    A LYS   B 1 55  ? 57.572 -20.769 -0.289  0.40 13.47 ?  55  LYS   B N    1 
ATOM   5172 N N    B LYS   B 1 55  ? 57.571 -20.769 -0.282  0.60 13.58 ?  55  LYS   B N    1 
ATOM   5173 C CA   A LYS   B 1 55  ? 58.932 -21.101 -0.696  0.40 14.23 ?  55  LYS   B CA   1 
ATOM   5174 C CA   B LYS   B 1 55  ? 58.925 -21.111 -0.697  0.60 14.45 ?  55  LYS   B CA   1 
ATOM   5175 C C    A LYS   B 1 55  ? 59.230 -20.572 -2.094  0.40 14.05 ?  55  LYS   B C    1 
ATOM   5176 C C    B LYS   B 1 55  ? 59.223 -20.563 -2.087  0.60 14.24 ?  55  LYS   B C    1 
ATOM   5177 O O    A LYS   B 1 55  ? 60.333 -20.082 -2.356  0.40 14.57 ?  55  LYS   B O    1 
ATOM   5178 O O    B LYS   B 1 55  ? 60.315 -20.040 -2.333  0.60 14.99 ?  55  LYS   B O    1 
ATOM   5179 C CB   A LYS   B 1 55  ? 59.151 -22.613 -0.617  0.40 15.55 ?  55  LYS   B CB   1 
ATOM   5180 C CB   B LYS   B 1 55  ? 59.115 -22.628 -0.647  0.60 15.90 ?  55  LYS   B CB   1 
ATOM   5181 C CG   A LYS   B 1 55  ? 60.516 -23.065 -1.115  0.40 18.03 ?  55  LYS   B CG   1 
ATOM   5182 C CG   B LYS   B 1 55  ? 60.521 -23.089 -0.990  0.60 19.02 ?  55  LYS   B CG   1 
ATOM   5183 C CD   A LYS   B 1 55  ? 60.711 -24.563 -0.960  0.40 20.10 ?  55  LYS   B CD   1 
ATOM   5184 C CD   B LYS   B 1 55  ? 60.664 -24.600 -0.885  0.60 21.67 ?  55  LYS   B CD   1 
ATOM   5185 C CE   A LYS   B 1 55  ? 60.787 -24.970 0.505   0.40 21.62 ?  55  LYS   B CE   1 
ATOM   5186 C CE   B LYS   B 1 55  ? 60.390 -25.096 0.530   0.60 23.59 ?  55  LYS   B CE   1 
ATOM   5187 N NZ   A LYS   B 1 55  ? 61.090 -26.413 0.668   0.40 22.64 ?  55  LYS   B NZ   1 
ATOM   5188 N NZ   B LYS   B 1 55  ? 61.032 -26.406 0.810   0.60 24.94 ?  55  LYS   B NZ   1 
ATOM   5189 H H    A LYS   B 1 55  ? 57.074 -21.447 -0.110  0.40 16.22 ?  55  LYS   B H    1 
ATOM   5190 H H    B LYS   B 1 55  ? 57.073 -21.444 -0.094  0.60 16.35 ?  55  LYS   B H    1 
ATOM   5191 H HA   A LYS   B 1 55  ? 59.555 -20.681 -0.082  0.40 17.14 ?  55  LYS   B HA   1 
ATOM   5192 H HA   B LYS   B 1 55  ? 59.557 -20.710 -0.078  0.60 17.40 ?  55  LYS   B HA   1 
ATOM   5193 H HB2  A LYS   B 1 55  ? 59.065 -22.886 0.311   0.40 18.72 ?  55  LYS   B HB2  1 
ATOM   5194 H HB2  B LYS   B 1 55  ? 58.913 -22.931 0.252   0.60 19.14 ?  55  LYS   B HB2  1 
ATOM   5195 H HB3  A LYS   B 1 55  ? 58.479 -23.057 -1.153  0.40 18.72 ?  55  LYS   B HB3  1 
ATOM   5196 H HB3  B LYS   B 1 55  ? 58.508 -23.040 -1.278  0.60 19.14 ?  55  LYS   B HB3  1 
ATOM   5197 H HG2  A LYS   B 1 55  ? 60.603 -22.848 -2.056  0.40 21.69 ?  55  LYS   B HG2  1 
ATOM   5198 H HG2  B LYS   B 1 55  ? 60.728 -22.828 -1.902  0.60 22.88 ?  55  LYS   B HG2  1 
ATOM   5199 H HG3  A LYS   B 1 55  ? 61.208 -22.615 -0.604  0.40 21.69 ?  55  LYS   B HG3  1 
ATOM   5200 H HG3  B LYS   B 1 55  ? 61.150 -22.679 -0.376  0.60 22.88 ?  55  LYS   B HG3  1 
ATOM   5201 H HD2  A LYS   B 1 55  ? 59.963 -25.027 -1.368  0.40 24.18 ?  55  LYS   B HD2  1 
ATOM   5202 H HD2  B LYS   B 1 55  ? 60.031 -25.024 -1.485  0.60 26.06 ?  55  LYS   B HD2  1 
ATOM   5203 H HD3  A LYS   B 1 55  ? 61.542 -24.824 -1.391  0.40 24.18 ?  55  LYS   B HD3  1 
ATOM   5204 H HD3  B LYS   B 1 55  ? 61.571 -24.853 -1.123  0.60 26.06 ?  55  LYS   B HD3  1 
ATOM   5205 H HE2  A LYS   B 1 55  ? 61.487 -24.456 0.939   0.40 26.00 ?  55  LYS   B HE2  1 
ATOM   5206 H HE2  B LYS   B 1 55  ? 60.734 -24.443 1.163   0.60 28.37 ?  55  LYS   B HE2  1 
ATOM   5207 H HE3  A LYS   B 1 55  ? 59.931 -24.790 0.928   0.40 26.00 ?  55  LYS   B HE3  1 
ATOM   5208 H HE3  B LYS   B 1 55  ? 59.430 -25.193 0.647   0.60 28.37 ?  55  LYS   B HE3  1 
ATOM   5209 H HZ1  A LYS   B 1 55  ? 61.122 -26.618 1.532   0.40 27.22 ?  55  LYS   B HZ1  1 
ATOM   5210 H HZ1  B LYS   B 1 55  ? 60.832 -26.670 1.636   0.60 29.98 ?  55  LYS   B HZ1  1 
ATOM   5211 H HZ2  A LYS   B 1 55  ? 60.455 -26.900 0.277   0.40 27.22 ?  55  LYS   B HZ2  1 
ATOM   5212 H HZ2  B LYS   B 1 55  ? 60.740 -27.015 0.232   0.60 29.98 ?  55  LYS   B HZ2  1 
ATOM   5213 H HZ3  A LYS   B 1 55  ? 61.873 -26.602 0.293   0.40 27.22 ?  55  LYS   B HZ3  1 
ATOM   5214 H HZ3  B LYS   B 1 55  ? 61.915 -26.332 0.734   0.60 29.98 ?  55  LYS   B HZ3  1 
ATOM   5215 N N    . ALA   B 1 56  ? 58.253 -20.646 -3.002  1.00 13.95 ?  56  ALA   B N    1 
ATOM   5216 C CA   . ALA   B 1 56  ? 58.473 -20.140 -4.353  1.00 14.36 ?  56  ALA   B CA   1 
ATOM   5217 C C    . ALA   B 1 56  ? 58.746 -18.641 -4.352  1.00 13.98 ?  56  ALA   B C    1 
ATOM   5218 O O    . ALA   B 1 56  ? 59.474 -18.139 -5.220  1.00 15.38 ?  56  ALA   B O    1 
ATOM   5219 C CB   . ALA   B 1 56  ? 57.279 -20.478 -5.245  1.00 15.32 ?  56  ALA   B CB   1 
ATOM   5220 H H    A ALA   B 1 56  ? 57.471 -20.977 -2.863  0.40 16.80 ?  56  ALA   B H    1 
ATOM   5221 H H    B ALA   B 1 56  ? 57.474 -20.984 -2.866  0.60 16.80 ?  56  ALA   B H    1 
ATOM   5222 H HA   . ALA   B 1 56  ? 59.254 -20.577 -4.724  1.00 17.29 ?  56  ALA   B HA   1 
ATOM   5223 H HB1  . ALA   B 1 56  ? 57.451 -20.140 -6.140  1.00 18.44 ?  56  ALA   B HB1  1 
ATOM   5224 H HB2  . ALA   B 1 56  ? 57.171 -21.441 -5.273  1.00 18.44 ?  56  ALA   B HB2  1 
ATOM   5225 H HB3  . ALA   B 1 56  ? 56.484 -20.063 -4.881  1.00 18.44 ?  56  ALA   B HB3  1 
ATOM   5226 N N    . THR   B 1 57  ? 58.175 -17.914 -3.389  1.00 14.07 ?  57  THR   B N    1 
ATOM   5227 C CA   . THR   B 1 57  ? 58.413 -16.479 -3.260  1.00 14.36 ?  57  THR   B CA   1 
ATOM   5228 C C    . THR   B 1 57  ? 59.667 -16.156 -2.453  1.00 15.14 ?  57  THR   B C    1 
ATOM   5229 O O    . THR   B 1 57  ? 59.903 -14.985 -2.141  1.00 15.36 ?  57  THR   B O    1 
ATOM   5230 C CB   . THR   B 1 57  ? 57.209 -15.757 -2.625  1.00 14.19 ?  57  THR   B CB   1 
ATOM   5231 O OG1  . THR   B 1 57  ? 57.187 -15.969 -1.208  1.00 13.88 ?  57  THR   B OG1  1 
ATOM   5232 C CG2  . THR   B 1 57  ? 55.889 -16.183 -3.258  1.00 13.79 ?  57  THR   B CG2  1 
ATOM   5233 H H    . THR   B 1 57  ? 57.629 -18.230 -2.803  1.00 16.94 ?  57  THR   B H    1 
ATOM   5234 H HA   . THR   B 1 57  ? 58.530 -16.110 -4.151  1.00 17.29 ?  57  THR   B HA   1 
ATOM   5235 H HB   . THR   B 1 57  ? 57.306 -14.808 -2.791  1.00 17.09 ?  57  THR   B HB   1 
ATOM   5236 H HG1  . THR   B 1 57  ? 57.125 -16.791 -1.043  1.00 16.72 ?  57  THR   B HG1  1 
ATOM   5237 H HG21 . THR   B 1 57  ? 55.163 -15.646 -2.907  1.00 16.60 ?  57  THR   B HG21 1 
ATOM   5238 H HG22 . THR   B 1 57  ? 55.928 -16.073 -4.220  1.00 16.60 ?  57  THR   B HG22 1 
ATOM   5239 H HG23 . THR   B 1 57  ? 55.711 -17.117 -3.059  1.00 16.60 ?  57  THR   B HG23 1 
ATOM   5240 N N    . ASN   B 1 58  ? 60.464 -17.158 -2.096  1.00 15.64 ?  58  ASN   B N    1 
ATOM   5241 C CA   . ASN   B 1 58  ? 61.669 -16.931 -1.305  1.00 18.60 ?  58  ASN   B CA   1 
ATOM   5242 C C    . ASN   B 1 58  ? 61.335 -16.239 0.017   1.00 16.32 ?  58  ASN   B C    1 
ATOM   5243 O O    . ASN   B 1 58  ? 62.068 -15.367 0.488   1.00 16.78 ?  58  ASN   B O    1 
ATOM   5244 C CB   . ASN   B 1 58  ? 62.724 -16.150 -2.095  1.00 26.18 ?  58  ASN   B CB   1 
ATOM   5245 C CG   . ASN   B 1 58  ? 64.107 -16.249 -1.482  1.00 33.76 ?  58  ASN   B CG   1 
ATOM   5246 O OD1  . ASN   B 1 58  ? 64.432 -17.228 -0.808  1.00 37.01 ?  58  ASN   B OD1  1 
ATOM   5247 N ND2  . ASN   B 1 58  ? 64.933 -15.233 -1.716  1.00 38.93 ?  58  ASN   B ND2  1 
ATOM   5248 H H    . ASN   B 1 58  ? 60.331 -17.981 -2.300  1.00 18.82 ?  58  ASN   B H    1 
ATOM   5249 H HA   . ASN   B 1 58  ? 62.057 -17.792 -1.093  1.00 22.37 ?  58  ASN   B HA   1 
ATOM   5250 H HB2  . ASN   B 1 58  ? 62.772 -16.503 -3.000  1.00 31.47 ?  58  ASN   B HB2  1 
ATOM   5251 H HB3  . ASN   B 1 58  ? 62.478 -15.212 -2.121  1.00 31.47 ?  58  ASN   B HB3  1 
ATOM   5252 H HD21 . ASN   B 1 58  ? 65.731 -15.242 -1.393  1.00 46.77 ?  58  ASN   B HD21 1 
ATOM   5253 H HD22 . ASN   B 1 58  ? 64.671 -14.565 -2.190  1.00 46.77 ?  58  ASN   B HD22 1 
ATOM   5254 N N    . ASN   B 1 59  ? 60.214 -16.634 0.618   1.00 15.48 ?  59  ASN   B N    1 
ATOM   5255 C CA   . ASN   B 1 59  ? 59.730 -16.172 1.916   1.00 15.27 ?  59  ASN   B CA   1 
ATOM   5256 C C    . ASN   B 1 59  ? 59.139 -14.765 1.866   1.00 14.53 ?  59  ASN   B C    1 
ATOM   5257 O O    . ASN   B 1 59  ? 58.722 -14.259 2.920   1.00 14.41 ?  59  ASN   B O    1 
ATOM   5258 C CB   . ASN   B 1 59  ? 60.797 -16.233 3.024   1.00 16.25 ?  59  ASN   B CB   1 
ATOM   5259 C CG   . ASN   B 1 59  ? 60.206 -16.413 4.401   1.00 17.24 ?  59  ASN   B CG   1 
ATOM   5260 O OD1  . ASN   B 1 59  ? 59.373 -17.292 4.617   1.00 17.87 ?  59  ASN   B OD1  1 
ATOM   5261 N ND2  . ASN   B 1 59  ? 60.635 -15.583 5.345   1.00 18.02 ?  59  ASN   B ND2  1 
ATOM   5262 H H    . ASN   B 1 59  ? 59.684 -17.217 0.270   1.00 18.63 ?  59  ASN   B H    1 
ATOM   5263 H HA   . ASN   B 1 59  ? 59.018 -16.769 2.191   1.00 18.38 ?  59  ASN   B HA   1 
ATOM   5264 H HB2  . ASN   B 1 59  ? 61.385 -16.987 2.865   1.00 19.56 ?  59  ASN   B HB2  1 
ATOM   5265 H HB3  . ASN   B 1 59  ? 61.303 -15.409 3.031   1.00 19.56 ?  59  ASN   B HB3  1 
ATOM   5266 H HD21 . ASN   B 1 59  ? 60.326 -15.642 6.149   1.00 21.68 ?  59  ASN   B HD21 1 
ATOM   5267 H HD22 . ASN   B 1 59  ? 61.222 -14.985 5.156   1.00 21.68 ?  59  ASN   B HD22 1 
ATOM   5268 N N    . ALA   B 1 60  ? 59.065 -14.119 0.697   1.00 14.15 ?  60  ALA   B N    1 
ATOM   5269 C CA   . ALA   B 1 60  ? 58.479 -12.782 0.634   1.00 14.69 ?  60  ALA   B CA   1 
ATOM   5270 C C    . ALA   B 1 60  ? 57.013 -12.801 1.045   1.00 13.68 ?  60  ALA   B C    1 
ATOM   5271 O O    . ALA   B 1 60  ? 56.519 -11.845 1.660   1.00 13.86 ?  60  ALA   B O    1 
ATOM   5272 C CB   . ALA   B 1 60  ? 58.634 -12.197 -0.770  1.00 15.62 ?  60  ALA   B CB   1 
ATOM   5273 H H    . ALA   B 1 60  ? 59.349 -14.432 -0.052  1.00 17.04 ?  60  ALA   B H    1 
ATOM   5274 H HA   . ALA   B 1 60  ? 58.955 -12.206 1.250   1.00 17.68 ?  60  ALA   B HA   1 
ATOM   5275 H HB1  . ALA   B 1 60  ? 58.239 -11.313 -0.786  1.00 18.80 ?  60  ALA   B HB1  1 
ATOM   5276 H HB2  . ALA   B 1 60  ? 59.579 -12.143 -0.989  1.00 18.80 ?  60  ALA   B HB2  1 
ATOM   5277 H HB3  . ALA   B 1 60  ? 58.181 -12.775 -1.405  1.00 18.80 ?  60  ALA   B HB3  1 
ATOM   5278 N N    . MET   B 1 61  ? 56.297 -13.870 0.693   1.00 13.11 ?  61  MET   B N    1 
ATOM   5279 C CA   . MET   B 1 61  ? 54.902 -13.994 1.091   1.00 12.87 ?  61  MET   B CA   1 
ATOM   5280 C C    . MET   B 1 61  ? 54.770 -14.010 2.610   1.00 12.95 ?  61  MET   B C    1 
ATOM   5281 O O    . MET   B 1 61  ? 53.870 -13.367 3.168   1.00 13.06 ?  61  MET   B O    1 
ATOM   5282 C CB   . MET   B 1 61  ? 54.316 -15.257 0.458   1.00 12.77 ?  61  MET   B CB   1 
ATOM   5283 C CG   . MET   B 1 61  ? 52.876 -15.555 0.875   1.00 12.89 ?  61  MET   B CG   1 
ATOM   5284 S SD   . MET   B 1 61  ? 52.242 -17.058 0.113   1.00 13.13 ?  61  MET   B SD   1 
ATOM   5285 C CE   . MET   B 1 61  ? 51.987 -16.493 -1.561  1.00 14.72 ?  61  MET   B CE   1 
ATOM   5286 H H    . MET   B 1 61  ? 56.595 -14.527 0.223   1.00 15.79 ?  61  MET   B H    1 
ATOM   5287 H HA   . MET   B 1 61  ? 54.409 -13.235 0.743   1.00 15.50 ?  61  MET   B HA   1 
ATOM   5288 H HB2  . MET   B 1 61  ? 54.325 -15.155 -0.509  1.00 15.38 ?  61  MET   B HB2  1 
ATOM   5289 H HB3  . MET   B 1 61  ? 54.861 -16.017 0.709   1.00 15.38 ?  61  MET   B HB3  1 
ATOM   5290 H HG2  . MET   B 1 61  ? 52.841 -15.675 1.837   1.00 15.53 ?  61  MET   B HG2  1 
ATOM   5291 H HG3  . MET   B 1 61  ? 52.307 -14.820 0.607   1.00 15.53 ?  61  MET   B HG3  1 
ATOM   5292 H HE1  . MET   B 1 61  ? 51.609 -17.221 -2.082  1.00 17.72 ?  61  MET   B HE1  1 
ATOM   5293 H HE2  . MET   B 1 61  ? 51.375 -15.743 -1.548  1.00 17.72 ?  61  MET   B HE2  1 
ATOM   5294 H HE3  . MET   B 1 61  ? 52.838 -16.225 -1.935  1.00 17.72 ?  61  MET   B HE3  1 
ATOM   5295 N N    . GLN   B 1 62  ? 55.659 -14.725 3.304   1.00 13.12 ?  62  GLN   B N    1 
ATOM   5296 C CA   . GLN   B 1 62  ? 55.557 -14.792 4.759   1.00 13.49 ?  62  GLN   B CA   1 
ATOM   5297 C C    . GLN   B 1 62  ? 55.848 -13.444 5.404   1.00 13.70 ?  62  GLN   B C    1 
ATOM   5298 O O    . GLN   B 1 62  ? 55.167 -13.045 6.356   1.00 14.17 ?  62  GLN   B O    1 
ATOM   5299 C CB   . GLN   B 1 62  ? 56.499 -15.854 5.318   1.00 13.58 ?  62  GLN   B CB   1 
ATOM   5300 C CG   . GLN   B 1 62  ? 56.284 -16.119 6.796   1.00 14.01 ?  62  GLN   B CG   1 
ATOM   5301 C CD   . GLN   B 1 62  ? 54.917 -16.715 7.050   1.00 13.56 ?  62  GLN   B CD   1 
ATOM   5302 O OE1  . GLN   B 1 62  ? 54.657 -17.859 6.684   1.00 13.69 ?  62  GLN   B OE1  1 
ATOM   5303 N NE2  . GLN   B 1 62  ? 54.018 -15.931 7.631   1.00 13.94 ?  62  GLN   B NE2  1 
ATOM   5304 H H    . GLN   B 1 62  ? 56.310 -15.170 2.960   1.00 15.80 ?  62  GLN   B H    1 
ATOM   5305 H HA   . GLN   B 1 62  ? 54.652 -15.042 4.992   1.00 16.25 ?  62  GLN   B HA   1 
ATOM   5306 H HB2  . GLN   B 1 62  ? 56.362 -16.687 4.838   1.00 16.35 ?  62  GLN   B HB2  1 
ATOM   5307 H HB3  . GLN   B 1 62  ? 57.418 -15.556 5.200   1.00 16.35 ?  62  GLN   B HB3  1 
ATOM   5308 H HG2  . GLN   B 1 62  ? 56.952 -16.753 7.106   1.00 16.87 ?  62  GLN   B HG2  1 
ATOM   5309 H HG3  . GLN   B 1 62  ? 56.350 -15.292 7.289   1.00 16.87 ?  62  GLN   B HG3  1 
ATOM   5310 H HE21 . GLN   B 1 62  ? 54.231 -15.135 7.862   1.00 16.79 ?  62  GLN   B HE21 1 
ATOM   5311 H HE22 . GLN   B 1 62  ? 53.226 -16.231 7.791   1.00 16.79 ?  62  GLN   B HE22 1 
ATOM   5312 N N    . VAL   B 1 63  ? 56.865 -12.733 4.914   1.00 14.18 ?  63  VAL   B N    1 
ATOM   5313 C CA   . VAL   B 1 63  ? 57.178 -11.417 5.471   1.00 14.91 ?  63  VAL   B CA   1 
ATOM   5314 C C    . VAL   B 1 63  ? 55.988 -10.483 5.298   1.00 14.27 ?  63  VAL   B C    1 
ATOM   5315 O O    . VAL   B 1 63  ? 55.578 -9.787  6.235   1.00 15.11 ?  63  VAL   B O    1 
ATOM   5316 C CB   . VAL   B 1 63  ? 58.459 -10.853 4.836   1.00 16.63 ?  63  VAL   B CB   1 
ATOM   5317 C CG1  . VAL   B 1 63  ? 58.675 -9.409  5.273   1.00 17.17 ?  63  VAL   B CG1  1 
ATOM   5318 C CG2  . VAL   B 1 63  ? 59.645 -11.719 5.217   1.00 17.33 ?  63  VAL   B CG2  1 
ATOM   5319 H H    . VAL   B 1 63  ? 57.381 -12.982 4.269   1.00 17.07 ?  63  VAL   B H    1 
ATOM   5320 H HA   . VAL   B 1 63  ? 57.340 -11.517 6.421   1.00 17.95 ?  63  VAL   B HA   1 
ATOM   5321 H HB   . VAL   B 1 63  ? 58.372 -10.867 3.871   1.00 20.02 ?  63  VAL   B HB   1 
ATOM   5322 H HG11 . VAL   B 1 63  ? 59.590 -9.155  5.085   1.00 20.67 ?  63  VAL   B HG11 1 
ATOM   5323 H HG12 . VAL   B 1 63  ? 58.065 -8.833  4.785   1.00 20.67 ?  63  VAL   B HG12 1 
ATOM   5324 H HG13 . VAL   B 1 63  ? 58.502 -9.339  6.227   1.00 20.67 ?  63  VAL   B HG13 1 
ATOM   5325 H HG21 . VAL   B 1 63  ? 60.453 -11.338 4.831   1.00 20.85 ?  63  VAL   B HG21 1 
ATOM   5326 H HG22 . VAL   B 1 63  ? 59.726 -11.739 6.186   1.00 20.85 ?  63  VAL   B HG22 1 
ATOM   5327 H HG23 . VAL   B 1 63  ? 59.509 -12.616 4.879   1.00 20.85 ?  63  VAL   B HG23 1 
ATOM   5328 N N    . GLU   B 1 64  ? 55.414 -10.462 4.091   1.00 13.94 ?  64  GLU   B N    1 
ATOM   5329 C CA   . GLU   B 1 64  ? 54.243 -9.631  3.820   1.00 13.80 ?  64  GLU   B CA   1 
ATOM   5330 C C    . GLU   B 1 64  ? 53.068 -10.030 4.707   1.00 13.42 ?  64  GLU   B C    1 
ATOM   5331 O O    . GLU   B 1 64  ? 52.324 -9.167  5.205   1.00 14.07 ?  64  GLU   B O    1 
ATOM   5332 C CB   . GLU   B 1 64  ? 53.869 -9.778  2.344   1.00 14.00 ?  64  GLU   B CB   1 
ATOM   5333 C CG   . GLU   B 1 64  ? 52.605 -9.039  1.921   1.00 13.95 ?  64  GLU   B CG   1 
ATOM   5334 C CD   . GLU   B 1 64  ? 52.045 -9.536  0.594   1.00 14.52 ?  64  GLU   B CD   1 
ATOM   5335 O OE1  . GLU   B 1 64  ? 52.214 -10.742 0.276   1.00 15.42 ?  64  GLU   B OE1  1 
ATOM   5336 O OE2  . GLU   B 1 64  ? 51.418 -8.717  -0.124  1.00 15.23 -1 64  GLU   B OE2  1 
ATOM   5337 H H    . GLU   B 1 64  ? 55.692 -10.916 3.413   1.00 16.79 ?  64  GLU   B H    1 
ATOM   5338 H HA   . GLU   B 1 64  ? 54.459 -8.702  3.994   1.00 16.62 ?  64  GLU   B HA   1 
ATOM   5339 H HB2  . GLU   B 1 64  ? 54.600 -9.431  1.803   1.00 16.86 ?  64  GLU   B HB2  1 
ATOM   5340 H HB3  . GLU   B 1 64  ? 53.742 -10.717 2.150   1.00 16.86 ?  64  GLU   B HB3  1 
ATOM   5341 H HG2  . GLU   B 1 64  ? 51.915 -9.160  2.595   1.00 16.80 ?  64  GLU   B HG2  1 
ATOM   5342 H HG3  . GLU   B 1 64  ? 52.808 -8.096  1.826   1.00 16.80 ?  64  GLU   B HG3  1 
ATOM   5343 N N    . SER   B 1 65  ? 52.891 -11.339 4.908   1.00 13.33 ?  65  SER   B N    1 
ATOM   5344 C CA   . SER   B 1 65  ? 51.779 -11.842 5.703   1.00 13.38 ?  65  SER   B CA   1 
ATOM   5345 C C    . SER   B 1 65  ? 51.916 -11.454 7.169   1.00 13.38 ?  65  SER   B C    1 
ATOM   5346 O O    . SER   B 1 65  ? 50.920 -11.081 7.805   1.00 13.80 ?  65  SER   B O    1 
ATOM   5347 C CB   . SER   B 1 65  ? 51.677 -13.360 5.557   1.00 13.42 ?  65  SER   B CB   1 
ATOM   5348 O OG   . SER   B 1 65  ? 51.339 -13.746 4.232   1.00 13.38 ?  65  SER   B OG   1 
ATOM   5349 H H    . SER   B 1 65  ? 53.414 -11.959 4.601   1.00 16.05 ?  65  SER   B H    1 
ATOM   5350 H HA   . SER   B 1 65  ? 50.958 -11.456 5.368   1.00 16.12 ?  65  SER   B HA   1 
ATOM   5351 H HB2  . SER   B 1 65  ? 52.527 -13.760 5.794   1.00 16.16 ?  65  SER   B HB2  1 
ATOM   5352 H HB3  . SER   B 1 65  ? 50.985 -13.684 6.159   1.00 16.16 ?  65  SER   B HB3  1 
ATOM   5353 H HG   . SER   B 1 65  ? 51.934 -13.474 3.697   1.00 16.12 ?  65  SER   B HG   1 
ATOM   5354 N N    . ASP   B 1 66  ? 53.122 -11.565 7.734   1.00 13.97 ?  66  ASP   B N    1 
ATOM   5355 C CA   . ASP   B 1 66  ? 53.308 -11.182 9.131   1.00 14.62 ?  66  ASP   B CA   1 
ATOM   5356 C C    . ASP   B 1 66  ? 52.991 -9.705  9.335   1.00 14.76 ?  66  ASP   B C    1 
ATOM   5357 O O    . ASP   B 1 66  ? 52.407 -9.321  10.353  1.00 15.05 ?  66  ASP   B O    1 
ATOM   5358 C CB   . ASP   B 1 66  ? 54.744 -11.477 9.570   1.00 15.99 ?  66  ASP   B CB   1 
ATOM   5359 C CG   . ASP   B 1 66  ? 55.038 -12.959 9.703   1.00 17.19 ?  66  ASP   B CG   1 
ATOM   5360 O OD1  . ASP   B 1 66  ? 54.098 -13.785 9.629   1.00 17.42 ?  66  ASP   B OD1  1 
ATOM   5361 O OD2  . ASP   B 1 66  ? 56.233 -13.297 9.892   1.00 19.73 -1 66  ASP   B OD2  1 
ATOM   5362 H H    . ASP   B 1 66  ? 53.828 -11.868 7.343   1.00 16.82 ?  66  ASP   B H    1 
ATOM   5363 H HA   . ASP   B 1 66  ? 52.710 -11.700 9.692   1.00 17.60 ?  66  ASP   B HA   1 
ATOM   5364 H HB2  . ASP   B 1 66  ? 55.358 -11.113 8.914   1.00 19.24 ?  66  ASP   B HB2  1 
ATOM   5365 H HB3  . ASP   B 1 66  ? 54.901 -11.069 10.436  1.00 19.24 ?  66  ASP   B HB3  1 
ATOM   5366 N N    . ASP   B 1 67  ? 53.374 -8.857  8.380   1.00 14.12 ?  67  ASP   B N    1 
ATOM   5367 C CA   . ASP   B 1 67  ? 53.024 -7.446  8.479   1.00 14.91 ?  67  ASP   B CA   1 
ATOM   5368 C C    . ASP   B 1 67  ? 51.512 -7.239  8.389   1.00 14.79 ?  67  ASP   B C    1 
ATOM   5369 O O    . ASP   B 1 67  ? 50.944 -6.430  9.133   1.00 15.30 ?  67  ASP   B O    1 
ATOM   5370 C CB   . ASP   B 1 67  ? 53.752 -6.659  7.396   1.00 16.12 ?  67  ASP   B CB   1 
ATOM   5371 C CG   . ASP   B 1 67  ? 53.341 -5.213  7.374   1.00 17.55 ?  67  ASP   B CG   1 
ATOM   5372 O OD1  . ASP   B 1 67  ? 53.851 -4.425  8.202   1.00 18.36 ?  67  ASP   B OD1  1 
ATOM   5373 O OD2  . ASP   B 1 67  ? 52.483 -4.880  6.538   1.00 18.57 -1 67  ASP   B OD2  1 
ATOM   5374 H H    . ASP   B 1 67  ? 53.834 -9.071  7.683   1.00 17.00 ?  67  ASP   B H    1 
ATOM   5375 H HA   . ASP   B 1 67  ? 53.322 -7.109  9.338   1.00 17.95 ?  67  ASP   B HA   1 
ATOM   5376 H HB2  . ASP   B 1 67  ? 54.709 -6.691  7.562   1.00 19.40 ?  67  ASP   B HB2  1 
ATOM   5377 H HB3  . ASP   B 1 67  ? 53.554 -7.046  6.529   1.00 19.40 ?  67  ASP   B HB3  1 
ATOM   5378 N N    . TYR   B 1 68  ? 50.838 -7.972  7.497   1.00 14.35 ?  68  TYR   B N    1 
ATOM   5379 C CA   . TYR   B 1 68  ? 49.381 -7.881  7.417   1.00 15.11 ?  68  TYR   B CA   1 
ATOM   5380 C C    . TYR   B 1 68  ? 48.741 -8.222  8.759   1.00 14.36 ?  68  TYR   B C    1 
ATOM   5381 O O    . TYR   B 1 68  ? 47.810 -7.547  9.211   1.00 15.10 ?  68  TYR   B O    1 
ATOM   5382 C CB   . TYR   B 1 68  ? 48.845 -8.811  6.324   1.00 15.68 ?  68  TYR   B CB   1 
ATOM   5383 C CG   . TYR   B 1 68  ? 47.334 -8.955  6.386   1.00 16.90 ?  68  TYR   B CG   1 
ATOM   5384 C CD1  . TYR   B 1 68  ? 46.738 -9.907  7.209   1.00 17.47 ?  68  TYR   B CD1  1 
ATOM   5385 C CD2  . TYR   B 1 68  ? 46.507 -8.121  5.656   1.00 17.77 ?  68  TYR   B CD2  1 
ATOM   5386 C CE1  . TYR   B 1 68  ? 45.371 -10.028 7.294   1.00 18.34 ?  68  TYR   B CE1  1 
ATOM   5387 C CE2  . TYR   B 1 68  ? 45.123 -8.243  5.729   1.00 17.95 ?  68  TYR   B CE2  1 
ATOM   5388 C CZ   . TYR   B 1 68  ? 44.572 -9.194  6.556   1.00 18.18 ?  68  TYR   B CZ   1 
ATOM   5389 O OH   . TYR   B 1 68  ? 43.204 -9.318  6.653   1.00 19.14 ?  68  TYR   B OH   1 
ATOM   5390 H H    . TYR   B 1 68  ? 51.198 -8.529  6.945   1.00 17.28 ?  68  TYR   B H    1 
ATOM   5391 H HA   . TYR   B 1 68  ? 49.139 -6.975  7.192   1.00 18.19 ?  68  TYR   B HA   1 
ATOM   5392 H HB2  . TYR   B 1 68  ? 49.074 -8.446  5.458   1.00 18.88 ?  68  TYR   B HB2  1 
ATOM   5393 H HB3  . TYR   B 1 68  ? 49.236 -9.692  6.432   1.00 18.88 ?  68  TYR   B HB3  1 
ATOM   5394 H HD1  . TYR   B 1 68  ? 47.273 -10.479 7.716   1.00 21.02 ?  68  TYR   B HD1  1 
ATOM   5395 H HD2  . TYR   B 1 68  ? 46.883 -7.477  5.106   1.00 21.38 ?  68  TYR   B HD2  1 
ATOM   5396 H HE1  . TYR   B 1 68  ? 44.986 -10.679 7.842   1.00 22.06 ?  68  TYR   B HE1  1 
ATOM   5397 H HE2  . TYR   B 1 68  ? 44.575 -7.681  5.234   1.00 21.60 ?  68  TYR   B HE2  1 
ATOM   5398 H HH   . TYR   B 1 68  ? 42.820 -8.767  6.141   1.00 23.03 ?  68  TYR   B HH   1 
ATOM   5399 N N    . ILE   B 1 69  ? 49.211 -9.297  9.397   1.00 14.60 ?  69  ILE   B N    1 
ATOM   5400 C CA   . ILE   B 1 69  ? 48.650 -9.725  10.677  1.00 15.34 ?  69  ILE   B CA   1 
ATOM   5401 C C    . ILE   B 1 69  ? 48.911 -8.687  11.763  1.00 14.76 ?  69  ILE   B C    1 
ATOM   5402 O O    . ILE   B 1 69  ? 48.042 -8.418  12.598  1.00 15.39 ?  69  ILE   B O    1 
ATOM   5403 C CB   . ILE   B 1 69  ? 49.208 -11.110 11.055  1.00 16.18 ?  69  ILE   B CB   1 
ATOM   5404 C CG1  . ILE   B 1 69  ? 48.689 -12.196 10.101  1.00 16.61 ?  69  ILE   B CG1  1 
ATOM   5405 C CG2  . ILE   B 1 69  ? 48.911 -11.445 12.506  1.00 17.17 ?  69  ILE   B CG2  1 
ATOM   5406 C CD1  . ILE   B 1 69  ? 47.209 -12.516 10.238  1.00 16.45 ?  69  ILE   B CD1  1 
ATOM   5407 H H    . ILE   B 1 69  ? 49.849 -9.794  9.113   1.00 17.57 ?  69  ILE   B H    1 
ATOM   5408 H HA   . ILE   B 1 69  ? 47.687 -9.814  10.579  1.00 18.47 ?  69  ILE   B HA   1 
ATOM   5409 H HB   . ILE   B 1 69  ? 50.173 -11.072 10.956  1.00 19.47 ?  69  ILE   B HB   1 
ATOM   5410 H HG12 . ILE   B 1 69  ? 48.843 -11.901 9.189   1.00 19.99 ?  69  ILE   B HG12 1 
ATOM   5411 H HG13 . ILE   B 1 69  ? 49.185 -13.012 10.266  1.00 19.99 ?  69  ILE   B HG13 1 
ATOM   5412 H HG21 . ILE   B 1 69  ? 49.050 -12.397 12.640  1.00 20.67 ?  69  ILE   B HG21 1 
ATOM   5413 H HG22 . ILE   B 1 69  ? 49.511 -10.944 13.080  1.00 20.67 ?  69  ILE   B HG22 1 
ATOM   5414 H HG23 . ILE   B 1 69  ? 47.990 -11.217 12.702  1.00 20.67 ?  69  ILE   B HG23 1 
ATOM   5415 H HD11 . ILE   B 1 69  ? 46.980 -13.211 9.602   1.00 19.80 ?  69  ILE   B HD11 1 
ATOM   5416 H HD12 . ILE   B 1 69  ? 47.034 -12.828 11.141  1.00 19.80 ?  69  ILE   B HD12 1 
ATOM   5417 H HD13 . ILE   B 1 69  ? 46.691 -11.718 10.056  1.00 19.80 ?  69  ILE   B HD13 1 
ATOM   5418 N N    . ALA   B 1 70  ? 50.113 -8.115  11.797  1.00 14.69 ?  70  ALA   B N    1 
ATOM   5419 C CA   . ALA   B 1 70  ? 50.394 -7.081  12.787  1.00 14.59 ?  70  ALA   B CA   1 
ATOM   5420 C C    . ALA   B 1 70  ? 49.406 -5.927  12.671  1.00 14.42 ?  70  ALA   B C    1 
ATOM   5421 O O    . ALA   B 1 70  ? 48.965 -5.376  13.684  1.00 14.83 ?  70  ALA   B O    1 
ATOM   5422 C CB   . ALA   B 1 70  ? 51.828 -6.589  12.624  1.00 14.96 ?  70  ALA   B CB   1 
ATOM   5423 H H    . ALA   B 1 70  ? 50.761 -8.308  11.272  1.00 17.68 ?  70  ALA   B H    1 
ATOM   5424 H HA   . ALA   B 1 70  ? 50.310 -7.464  13.676  1.00 17.56 ?  70  ALA   B HA   1 
ATOM   5425 H HB1  . ALA   B 1 70  ? 52.019 -5.934  13.312  1.00 18.01 ?  70  ALA   B HB1  1 
ATOM   5426 H HB2  . ALA   B 1 70  ? 52.436 -7.343  12.710  1.00 18.01 ?  70  ALA   B HB2  1 
ATOM   5427 H HB3  . ALA   B 1 70  ? 51.928 -6.188  11.746  1.00 18.01 ?  70  ALA   B HB3  1 
ATOM   5428 N N    . THR   B 1 71  ? 49.043 -5.557  11.443  1.00 14.84 ?  71  THR   B N    1 
ATOM   5429 C CA   . THR   B 1 71  ? 48.158 -4.416  11.229  1.00 15.84 ?  71  THR   B CA   1 
ATOM   5430 C C    . THR   B 1 71  ? 46.687 -4.774  11.422  1.00 16.54 ?  71  THR   B C    1 
ATOM   5431 O O    . THR   B 1 71  ? 45.910 -3.950  11.922  1.00 18.08 ?  71  THR   B O    1 
ATOM   5432 C CB   . THR   B 1 71  ? 48.389 -3.851  9.827   1.00 17.57 ?  71  THR   B CB   1 
ATOM   5433 O OG1  . THR   B 1 71  ? 49.722 -3.336  9.738   1.00 19.36 ?  71  THR   B OG1  1 
ATOM   5434 C CG2  . THR   B 1 71  ? 47.389 -2.748  9.503   1.00 18.42 ?  71  THR   B CG2  1 
ATOM   5435 H H    . THR   B 1 71  ? 49.310 -5.942  10.721  1.00 17.86 ?  71  THR   B H    1 
ATOM   5436 H HA   . THR   B 1 71  ? 48.384 -3.722  11.870  1.00 19.06 ?  71  THR   B HA   1 
ATOM   5437 H HB   . THR   B 1 71  ? 48.284 -4.562  9.175   1.00 21.14 ?  71  THR   B HB   1 
ATOM   5438 H HG1  . THR   B 1 71  ? 49.862 -3.019  8.970   1.00 23.29 ?  71  THR   B HG1  1 
ATOM   5439 H HG21 . THR   B 1 71  ? 47.704 -2.234  8.743   1.00 22.16 ?  71  THR   B HG21 1 
ATOM   5440 H HG22 . THR   B 1 71  ? 46.528 -3.132  9.290   1.00 22.16 ?  71  THR   B HG22 1 
ATOM   5441 H HG23 . THR   B 1 71  ? 47.297 -2.154  10.265  1.00 22.16 ?  71  THR   B HG23 1 
ATOM   5442 N N    . ASN   B 1 72  ? 46.284 -5.990  11.034  1.00 16.18 ?  72  ASN   B N    1 
ATOM   5443 C CA   . ASN   B 1 72  ? 44.876 -6.338  10.913  1.00 16.44 ?  72  ASN   B CA   1 
ATOM   5444 C C    . ASN   B 1 72  ? 44.402 -7.440  11.846  1.00 16.64 ?  72  ASN   B C    1 
ATOM   5445 O O    . ASN   B 1 72  ? 43.184 -7.601  12.006  1.00 17.51 ?  72  ASN   B O    1 
ATOM   5446 C CB   . ASN   B 1 72  ? 44.555 -6.749  9.467   1.00 17.04 ?  72  ASN   B CB   1 
ATOM   5447 C CG   . ASN   B 1 72  ? 44.830 -5.638  8.481   1.00 18.39 ?  72  ASN   B CG   1 
ATOM   5448 O OD1  . ASN   B 1 72  ? 45.842 -5.633  7.780   1.00 19.35 ?  72  ASN   B OD1  1 
ATOM   5449 N ND2  . ASN   B 1 72  ? 43.940 -4.669  8.444   1.00 19.52 ?  72  ASN   B ND2  1 
ATOM   5450 H H    . ASN   B 1 72  ? 46.824 -6.637  10.827  1.00 19.47 ?  72  ASN   B H    1 
ATOM   5451 H HA   . ASN   B 1 72  ? 44.354 -5.550  11.111  1.00 19.78 ?  72  ASN   B HA   1 
ATOM   5452 H HB2  . ASN   B 1 72  ? 45.104 -7.515  9.225   1.00 20.50 ?  72  ASN   B HB2  1 
ATOM   5453 H HB3  . ASN   B 1 72  ? 43.616 -6.984  9.408   1.00 20.50 ?  72  ASN   B HB3  1 
ATOM   5454 H HD21 . ASN   B 1 72  ? 44.040 -4.010  7.899   1.00 23.48 ?  72  ASN   B HD21 1 
ATOM   5455 H HD22 . ASN   B 1 72  ? 43.240 -4.704  8.947   1.00 23.48 ?  72  ASN   B HD22 1 
ATOM   5456 N N    . GLY   B 1 73  ? 45.305 -8.201  12.458  1.00 16.48 ?  73  GLY   B N    1 
ATOM   5457 C CA   . GLY   B 1 73  ? 44.909 -9.347  13.243  1.00 15.92 ?  73  GLY   B CA   1 
ATOM   5458 C C    . GLY   B 1 73  ? 44.536 -10.524 12.370  1.00 15.05 ?  73  GLY   B C    1 
ATOM   5459 O O    . GLY   B 1 73  ? 44.525 -10.439 11.139  1.00 15.15 ?  73  GLY   B O    1 
ATOM   5460 H H    . GLY   B 1 73  ? 46.160 -8.077  12.424  1.00 19.84 ?  73  GLY   B H    1 
ATOM   5461 H HA2  . GLY   B 1 73  ? 45.642 -9.607  13.830  1.00 19.17 ?  73  GLY   B HA2  1 
ATOM   5462 H HA3  . GLY   B 1 73  ? 44.146 -9.113  13.794  1.00 19.17 ?  73  GLY   B HA3  1 
ATOM   5463 N N    . PRO   B 1 74  ? 44.227 -11.650 13.004  1.00 15.10 ?  74  PRO   B N    1 
ATOM   5464 C CA   . PRO   B 1 74  ? 43.976 -12.881 12.256  1.00 14.34 ?  74  PRO   B CA   1 
ATOM   5465 C C    . PRO   B 1 74  ? 42.672 -12.827 11.473  1.00 14.12 ?  74  PRO   B C    1 
ATOM   5466 O O    . PRO   B 1 74  ? 41.728 -12.093 11.796  1.00 14.94 ?  74  PRO   B O    1 
ATOM   5467 C CB   . PRO   B 1 74  ? 43.909 -13.948 13.355  1.00 15.57 ?  74  PRO   B CB   1 
ATOM   5468 C CG   . PRO   B 1 74  ? 43.435 -13.204 14.557  1.00 17.20 ?  74  PRO   B CG   1 
ATOM   5469 C CD   . PRO   B 1 74  ? 44.103 -11.858 14.457  1.00 16.48 ?  74  PRO   B CD   1 
ATOM   5470 H HA   . PRO   B 1 74  ? 44.718 -13.072 11.656  1.00 17.26 ?  74  PRO   B HA   1 
ATOM   5471 H HB2  . PRO   B 1 74  ? 43.278 -14.638 13.100  1.00 18.74 ?  74  PRO   B HB2  1 
ATOM   5472 H HB3  . PRO   B 1 74  ? 44.792 -14.322 13.503  1.00 18.74 ?  74  PRO   B HB3  1 
ATOM   5473 H HG2  . PRO   B 1 74  ? 42.469 -13.112 14.528  1.00 20.70 ?  74  PRO   B HG2  1 
ATOM   5474 H HG3  . PRO   B 1 74  ? 43.712 -13.669 15.362  1.00 20.70 ?  74  PRO   B HG3  1 
ATOM   5475 H HD2  . PRO   B 1 74  ? 43.538 -11.173 14.857  1.00 19.84 ?  74  PRO   B HD2  1 
ATOM   5476 H HD3  . PRO   B 1 74  ? 44.977 -11.884 14.876  1.00 19.84 ?  74  PRO   B HD3  1 
ATOM   5477 N N    . LEU   B 1 75  ? 42.641 -13.646 10.424  1.00 13.07 ?  75  LEU   B N    1 
ATOM   5478 C CA   . LEU   B 1 75  ? 41.425 -13.870 9.665   1.00 12.88 ?  75  LEU   B CA   1 
ATOM   5479 C C    . LEU   B 1 75  ? 40.460 -14.731 10.478  1.00 13.15 ?  75  LEU   B C    1 
ATOM   5480 O O    . LEU   B 1 75  ? 40.800 -15.267 11.534  1.00 14.35 ?  75  LEU   B O    1 
ATOM   5481 C CB   . LEU   B 1 75  ? 41.748 -14.587 8.355   1.00 13.16 ?  75  LEU   B CB   1 
ATOM   5482 C CG   . LEU   B 1 75  ? 42.587 -13.832 7.323   1.00 15.13 ?  75  LEU   B CG   1 
ATOM   5483 C CD1  . LEU   B 1 75  ? 42.772 -14.671 6.065   1.00 16.43 ?  75  LEU   B CD1  1 
ATOM   5484 C CD2  . LEU   B 1 75  ? 42.001 -12.488 6.983   1.00 18.28 ?  75  LEU   B CD2  1 
ATOM   5485 H H    . LEU   B 1 75  ? 43.317 -14.097 10.132  1.00 15.74 ?  75  LEU   B H    1 
ATOM   5486 H HA   . LEU   B 1 75  ? 40.997 -13.023 9.463   1.00 15.52 ?  75  LEU   B HA   1 
ATOM   5487 H HB2  . LEU   B 1 75  ? 42.230 -15.405 8.570   1.00 15.84 ?  75  LEU   B HB2  1 
ATOM   5488 H HB3  . LEU   B 1 75  ? 40.911 -14.824 7.921   1.00 15.84 ?  75  LEU   B HB3  1 
ATOM   5489 H HG   . LEU   B 1 75  ? 43.468 -13.679 7.700   1.00 18.22 ?  75  LEU   B HG   1 
ATOM   5490 H HD11 . LEU   B 1 75  ? 43.314 -14.174 5.430   1.00 19.77 ?  75  LEU   B HD11 1 
ATOM   5491 H HD12 . LEU   B 1 75  ? 43.225 -15.500 6.300   1.00 19.77 ?  75  LEU   B HD12 1 
ATOM   5492 H HD13 . LEU   B 1 75  ? 41.906 -14.866 5.681   1.00 19.77 ?  75  LEU   B HD13 1 
ATOM   5493 H HD21 . LEU   B 1 75  ? 42.505 -12.098 6.255   1.00 21.99 ?  75  LEU   B HD21 1 
ATOM   5494 H HD22 . LEU   B 1 75  ? 41.074 -12.609 6.718   1.00 21.99 ?  75  LEU   B HD22 1 
ATOM   5495 H HD23 . LEU   B 1 75  ? 42.047 -11.917 7.765   1.00 21.99 ?  75  LEU   B HD23 1 
ATOM   5496 N N    . LYS   B 1 76  ? 39.236 -14.862 9.959   1.00 14.71 ?  76  LYS   B N    1 
ATOM   5497 C CA   . LYS   B 1 76  ? 38.260 -15.834 10.438  1.00 15.82 ?  76  LYS   B CA   1 
ATOM   5498 C C    . LYS   B 1 76  ? 38.340 -17.096 9.581   1.00 14.44 ?  76  LYS   B C    1 
ATOM   5499 O O    . LYS   B 1 76  ? 38.600 -17.024 8.380   1.00 14.07 ?  76  LYS   B O    1 
ATOM   5500 C CB   . LYS   B 1 76  ? 36.832 -15.274 10.295  1.00 18.59 ?  76  LYS   B CB   1 
ATOM   5501 C CG   . LYS   B 1 76  ? 36.580 -13.854 10.846  1.00 20.73 ?  76  LYS   B CG   1 
ATOM   5502 C CD   . LYS   B 1 76  ? 35.159 -13.342 10.517  1.00 22.60 ?  76  LYS   B CD   1 
ATOM   5503 C CE   . LYS   B 1 76  ? 34.908 -11.954 11.096  1.00 24.64 ?  76  LYS   B CE   1 
ATOM   5504 N NZ   . LYS   B 1 76  ? 33.608 -11.364 10.665  1.00 25.48 ?  76  LYS   B NZ   1 
ATOM   5505 H H    . LYS   B 1 76  ? 38.936 -14.381 9.313   1.00 17.71 ?  76  LYS   B H    1 
ATOM   5506 H HA   . LYS   B 1 76  ? 38.427 -16.065 11.367  1.00 19.04 ?  76  LYS   B HA   1 
ATOM   5507 H HB2  . LYS   B 1 76  ? 36.610 -15.259 9.350   1.00 22.36 ?  76  LYS   B HB2  1 
ATOM   5508 H HB3  . LYS   B 1 76  ? 36.224 -15.873 10.756  1.00 22.36 ?  76  LYS   B HB3  1 
ATOM   5509 H HG2  . LYS   B 1 76  ? 36.683 -13.867 11.810  1.00 24.93 ?  76  LYS   B HG2  1 
ATOM   5510 H HG3  . LYS   B 1 76  ? 37.222 -13.243 10.450  1.00 24.93 ?  76  LYS   B HG3  1 
ATOM   5511 H HD2  . LYS   B 1 76  ? 35.055 -13.292 9.554   1.00 27.17 ?  76  LYS   B HD2  1 
ATOM   5512 H HD3  . LYS   B 1 76  ? 34.507 -13.951 10.895  1.00 27.17 ?  76  LYS   B HD3  1 
ATOM   5513 H HE2  . LYS   B 1 76  ? 34.902 -12.015 12.063  1.00 29.63 ?  76  LYS   B HE2  1 
ATOM   5514 H HE3  . LYS   B 1 76  ? 35.617 -11.360 10.805  1.00 29.63 ?  76  LYS   B HE3  1 
ATOM   5515 H HZ1  . LYS   B 1 76  ? 33.506 -10.555 11.026  1.00 30.63 ?  76  LYS   B HZ1  1 
ATOM   5516 H HZ2  . LYS   B 1 76  ? 33.587 -11.286 9.778   1.00 30.63 ?  76  LYS   B HZ2  1 
ATOM   5517 H HZ3  . LYS   B 1 76  ? 32.934 -11.883 10.925  1.00 30.63 ?  76  LYS   B HZ3  1 
ATOM   5518 N N    . VAL   B 1 77  ? 38.087 -18.259 10.198  1.00 14.02 ?  77  VAL   B N    1 
ATOM   5519 C CA   . VAL   B 1 77  ? 37.866 -19.461 9.397   1.00 13.69 ?  77  VAL   B CA   1 
ATOM   5520 C C    . VAL   B 1 77  ? 36.671 -19.209 8.486   1.00 13.23 ?  77  VAL   B C    1 
ATOM   5521 O O    . VAL   B 1 77  ? 35.608 -18.753 8.935   1.00 13.60 ?  77  VAL   B O    1 
ATOM   5522 C CB   . VAL   B 1 77  ? 37.675 -20.704 10.286  1.00 14.72 ?  77  VAL   B CB   1 
ATOM   5523 C CG1  . VAL   B 1 77  ? 37.379 -21.928 9.419   1.00 15.25 ?  77  VAL   B CG1  1 
ATOM   5524 C CG2  . VAL   B 1 77  ? 38.925 -20.960 11.128  1.00 16.47 ?  77  VAL   B CG2  1 
ATOM   5525 H H    . VAL   B 1 77  ? 38.051 -18.374 11.048  1.00 16.88 ?  77  VAL   B H    1 
ATOM   5526 H HA   . VAL   B 1 77  ? 38.641 -19.615 8.836   1.00 16.49 ?  77  VAL   B HA   1 
ATOM   5527 H HB   . VAL   B 1 77  ? 36.926 -20.563 10.884  1.00 17.72 ?  77  VAL   B HB   1 
ATOM   5528 H HG11 . VAL   B 1 77  ? 37.436 -22.723 9.971   1.00 18.35 ?  77  VAL   B HG11 1 
ATOM   5529 H HG12 . VAL   B 1 77  ? 36.485 -21.846 9.050   1.00 18.35 ?  77  VAL   B HG12 1 
ATOM   5530 H HG13 . VAL   B 1 77  ? 38.031 -21.973 8.704   1.00 18.35 ?  77  VAL   B HG13 1 
ATOM   5531 H HG21 . VAL   B 1 77  ? 38.787 -21.761 11.656  1.00 19.82 ?  77  VAL   B HG21 1 
ATOM   5532 H HG22 . VAL   B 1 77  ? 39.683 -21.075 10.536  1.00 19.82 ?  77  VAL   B HG22 1 
ATOM   5533 H HG23 . VAL   B 1 77  ? 39.070 -20.199 11.711  1.00 19.82 ?  77  VAL   B HG23 1 
ATOM   5534 N N    . GLY   B 1 78  ? 36.850 -19.480 7.197   1.00 12.97 ?  78  GLY   B N    1 
ATOM   5535 C CA   . GLY   B 1 78  ? 35.874 -19.155 6.183   1.00 12.20 ?  78  GLY   B CA   1 
ATOM   5536 C C    . GLY   B 1 78  ? 36.126 -17.839 5.477   1.00 11.83 ?  78  GLY   B C    1 
ATOM   5537 O O    . GLY   B 1 78  ? 35.448 -17.548 4.489   1.00 12.51 ?  78  GLY   B O    1 
ATOM   5538 H H    . GLY   B 1 78  ? 37.552 -19.868 6.884   1.00 15.62 ?  78  GLY   B H    1 
ATOM   5539 H HA2  . GLY   B 1 78  ? 35.864 -19.858 5.515   1.00 14.70 ?  78  GLY   B HA2  1 
ATOM   5540 H HA3  . GLY   B 1 78  ? 34.994 -19.114 6.589   1.00 14.70 ?  78  GLY   B HA3  1 
ATOM   5541 N N    . GLY   B 1 79  ? 37.075 -17.037 5.960   1.00 12.55 ?  79  GLY   B N    1 
ATOM   5542 C CA   . GLY   B 1 79  ? 37.369 -15.741 5.386   1.00 12.20 ?  79  GLY   B CA   1 
ATOM   5543 C C    . GLY   B 1 79  ? 38.605 -15.748 4.504   1.00 12.00 ?  79  GLY   B C    1 
ATOM   5544 O O    . GLY   B 1 79  ? 39.222 -16.784 4.246   1.00 12.56 ?  79  GLY   B O    1 
ATOM   5545 H H    . GLY   B 1 79  ? 37.575 -17.228 6.630   1.00 15.12 ?  79  GLY   B H    1 
ATOM   5546 H HA2  . GLY   B 1 79  ? 36.615 -15.447 4.844   1.00 14.69 ?  79  GLY   B HA2  1 
ATOM   5547 H HA3  . GLY   B 1 79  ? 37.503 -15.095 6.092   1.00 14.69 ?  79  GLY   B HA3  1 
ATOM   5548 N N    . SER   B 1 80  ? 38.972 -14.549 4.043   1.00 12.01 ?  80  SER   B N    1 
ATOM   5549 C CA   . SER   B 1 80  ? 40.077 -14.407 3.105   1.00 12.22 ?  80  SER   B CA   1 
ATOM   5550 C C    . SER   B 1 80  ? 40.655 -13.000 3.179   1.00 11.85 ?  80  SER   B C    1 
ATOM   5551 O O    . SER   B 1 80  ? 40.038 -12.072 3.716   1.00 13.16 ?  80  SER   B O    1 
ATOM   5552 C CB   . SER   B 1 80  ? 39.626 -14.689 1.669   1.00 12.34 ?  80  SER   B CB   1 
ATOM   5553 O OG   . SER   B 1 80  ? 38.784 -13.664 1.177   1.00 13.23 ?  80  SER   B OG   1 
ATOM   5554 H H    . SER   B 1 80  ? 38.602 -13.805 4.263   1.00 14.47 ?  80  SER   B H    1 
ATOM   5555 H HA   . SER   B 1 80  ? 40.770 -15.035 3.343   1.00 14.72 ?  80  SER   B HA   1 
ATOM   5556 H HB2  . SER   B 1 80  ? 40.405 -14.752 1.094   1.00 14.87 ?  80  SER   B HB2  1 
ATOM   5557 H HB3  . SER   B 1 80  ? 39.138 -15.532 1.650   1.00 14.87 ?  80  SER   B HB3  1 
ATOM   5558 H HG   . SER   B 1 80  ? 38.093 -13.607 1.653   1.00 15.93 ?  80  SER   B HG   1 
ATOM   5559 N N    . CYS   B 1 81  ? 41.837 -12.847 2.583   1.00 11.88 ?  81  CYS   B N    1 
ATOM   5560 C CA   . CYS   B 1 81  ? 42.375 -11.530 2.284   1.00 12.09 ?  81  CYS   B CA   1 
ATOM   5561 C C    . CYS   B 1 81  ? 43.148 -11.606 0.976   1.00 11.52 ?  81  CYS   B C    1 
ATOM   5562 O O    . CYS   B 1 81  ? 43.666 -12.665 0.599   1.00 12.44 ?  81  CYS   B O    1 
ATOM   5563 C CB   . CYS   B 1 81  ? 43.262 -10.983 3.412   1.00 13.26 ?  81  CYS   B CB   1 
ATOM   5564 S SG   . CYS   B 1 81  ? 44.786 -11.918 3.665   1.00 12.87 ?  81  CYS   B SG   1 
ATOM   5565 H H    . CYS   B 1 81  ? 42.348 -13.496 2.342   1.00 14.31 ?  81  CYS   B H    1 
ATOM   5566 H HA   . CYS   B 1 81  ? 41.638 -10.909 2.163   1.00 14.57 ?  81  CYS   B HA   1 
ATOM   5567 H HB2  . CYS   B 1 81  ? 43.510 -10.070 3.204   1.00 15.96 ?  81  CYS   B HB2  1 
ATOM   5568 H HB3  . CYS   B 1 81  ? 42.759 -11.002 4.246   1.00 15.96 ?  81  CYS   B HB3  1 
ATOM   5569 H HG   . CYS   B 1 81  ? 45.412 -11.422 4.572   1.00 15.50 ?  81  CYS   B HG   1 
ATOM   5570 N N    . VAL   B 1 82  ? 43.242 -10.463 0.304   1.00 11.68 ?  82  VAL   B N    1 
ATOM   5571 C CA   . VAL   B 1 82  ? 44.002 -10.334 -0.935  1.00 11.92 ?  82  VAL   B CA   1 
ATOM   5572 C C    . VAL   B 1 82  ? 45.339 -9.689  -0.613  1.00 12.31 ?  82  VAL   B C    1 
ATOM   5573 O O    . VAL   B 1 82  ? 45.385 -8.573  -0.075  1.00 13.03 ?  82  VAL   B O    1 
ATOM   5574 C CB   . VAL   B 1 82  ? 43.251 -9.497  -1.980  1.00 13.48 ?  82  VAL   B CB   1 
ATOM   5575 C CG1  . VAL   B 1 82  ? 44.095 -9.346  -3.243  1.00 14.75 ?  82  VAL   B CG1  1 
ATOM   5576 C CG2  . VAL   B 1 82  ? 41.907 -10.120 -2.301  1.00 14.19 ?  82  VAL   B CG2  1 
ATOM   5577 H H    . VAL   B 1 82  ? 42.858 -9.731  0.549   1.00 14.08 ?  82  VAL   B H    1 
ATOM   5578 H HA   . VAL   B 1 82  ? 44.160 -11.214 -1.307  1.00 14.36 ?  82  VAL   B HA   1 
ATOM   5579 H HB   . VAL   B 1 82  ? 43.086 -8.610  -1.619  1.00 16.23 ?  82  VAL   B HB   1 
ATOM   5580 H HG11 . VAL   B 1 82  ? 43.531 -9.027  -3.963  1.00 17.75 ?  82  VAL   B HG11 1 
ATOM   5581 H HG12 . VAL   B 1 82  ? 44.807 -8.709  -3.073  1.00 17.75 ?  82  VAL   B HG12 1 
ATOM   5582 H HG13 . VAL   B 1 82  ? 44.469 -10.210 -3.473  1.00 17.75 ?  82  VAL   B HG13 1 
ATOM   5583 H HG21 . VAL   B 1 82  ? 41.469 -9.595  -2.989  1.00 17.09 ?  82  VAL   B HG21 1 
ATOM   5584 H HG22 . VAL   B 1 82  ? 42.049 -11.027 -2.619  1.00 17.09 ?  82  VAL   B HG22 1 
ATOM   5585 H HG23 . VAL   B 1 82  ? 41.362 -10.135 -1.499  1.00 17.09 ?  82  VAL   B HG23 1 
ATOM   5586 N N    . LEU   B 1 83  ? 46.424 -10.370 -0.975  1.00 12.08 ?  83  LEU   B N    1 
ATOM   5587 C CA   . LEU   B 1 83  ? 47.774 -9.846  -0.849  1.00 11.99 ?  83  LEU   B CA   1 
ATOM   5588 C C    . LEU   B 1 83  ? 48.479 -9.985  -2.195  1.00 12.03 ?  83  LEU   B C    1 
ATOM   5589 O O    . LEU   B 1 83  ? 47.878 -10.394 -3.191  1.00 11.99 ?  83  LEU   B O    1 
ATOM   5590 C CB   . LEU   B 1 83  ? 48.522 -10.535 0.295   1.00 12.59 ?  83  LEU   B CB   1 
ATOM   5591 C CG   . LEU   B 1 83  ? 48.013 -10.188 1.696   1.00 13.82 ?  83  LEU   B CG   1 
ATOM   5592 C CD1  . LEU   B 1 83  ? 48.679 -11.042 2.749   1.00 14.19 ?  83  LEU   B CD1  1 
ATOM   5593 C CD2  . LEU   B 1 83  ? 48.198 -8.701  2.017   1.00 15.19 ?  83  LEU   B CD2  1 
ATOM   5594 H H    . LEU   B 1 83  ? 46.392 -11.168 -1.303  1.00 14.56 ?  83  LEU   B H    1 
ATOM   5595 H HA   . LEU   B 1 83  ? 47.714 -8.900  -0.642  1.00 14.45 ?  83  LEU   B HA   1 
ATOM   5596 H HB2  . LEU   B 1 83  ? 48.447 -11.494 0.180   1.00 15.17 ?  83  LEU   B HB2  1 
ATOM   5597 H HB3  . LEU   B 1 83  ? 49.457 -10.273 0.247   1.00 15.17 ?  83  LEU   B HB3  1 
ATOM   5598 H HG   . LEU   B 1 83  ? 47.063 -10.375 1.727   1.00 16.64 ?  83  LEU   B HG   1 
ATOM   5599 H HD11 . LEU   B 1 83  ? 48.327 -10.804 3.619   1.00 17.08 ?  83  LEU   B HD11 1 
ATOM   5600 H HD12 . LEU   B 1 83  ? 48.492 -11.977 2.560   1.00 17.08 ?  83  LEU   B HD12 1 
ATOM   5601 H HD13 . LEU   B 1 83  ? 49.637 -10.887 2.723   1.00 17.08 ?  83  LEU   B HD13 1 
ATOM   5602 H HD21 . LEU   B 1 83  ? 48.020 -8.560  2.958   1.00 18.28 ?  83  LEU   B HD21 1 
ATOM   5603 H HD22 . LEU   B 1 83  ? 49.107 -8.444  1.806   1.00 18.28 ?  83  LEU   B HD22 1 
ATOM   5604 H HD23 . LEU   B 1 83  ? 47.574 -8.184  1.481   1.00 18.28 ?  83  LEU   B HD23 1 
ATOM   5605 N N    . SER   B 1 84  ? 49.757 -9.615  -2.244  1.00 12.98 ?  84  SER   B N    1 
ATOM   5606 C CA   . SER   B 1 84  ? 50.492 -9.716  -3.496  1.00 13.39 ?  84  SER   B CA   1 
ATOM   5607 C C    . SER   B 1 84  ? 50.645 -11.172 -3.926  1.00 12.63 ?  84  SER   B C    1 
ATOM   5608 O O    . SER   B 1 84  ? 50.767 -12.082 -3.105  1.00 12.35 ?  84  SER   B O    1 
ATOM   5609 C CB   . SER   B 1 84  ? 51.887 -9.113  -3.341  1.00 15.08 ?  84  SER   B CB   1 
ATOM   5610 O OG   . SER   B 1 84  ? 52.638 -9.327  -4.520  1.00 17.02 ?  84  SER   B OG   1 
ATOM   5611 H H    . SER   B 1 84  ? 50.205 -9.297  -1.579  1.00 15.63 ?  84  SER   B H    1 
ATOM   5612 H HA   . SER   B 1 84  ? 50.018 -9.235  -4.190  1.00 16.12 ?  84  SER   B HA   1 
ATOM   5613 H HB2  . SER   B 1 84  ? 51.803 -8.156  -3.172  1.00 18.15 ?  84  SER   B HB2  1 
ATOM   5614 H HB3  . SER   B 1 84  ? 52.342 -9.540  -2.601  1.00 18.15 ?  84  SER   B HB3  1 
ATOM   5615 H HG   . SER   B 1 84  ? 53.401 -8.974  -4.444  1.00 20.48 ?  84  SER   B HG   1 
ATOM   5616 N N    . GLY   B 1 85  ? 50.703 -11.380 -5.234  1.00 13.53 ?  85  GLY   B N    1 
ATOM   5617 C CA   . GLY   B 1 85  ? 51.057 -12.668 -5.779  1.00 13.90 ?  85  GLY   B CA   1 
ATOM   5618 C C    . GLY   B 1 85  ? 52.524 -12.852 -6.087  1.00 13.23 ?  85  GLY   B C    1 
ATOM   5619 O O    . GLY   B 1 85  ? 52.891 -13.928 -6.563  1.00 13.73 ?  85  GLY   B O    1 
ATOM   5620 H H    . GLY   B 1 85  ? 50.536 -10.784 -5.823  1.00 16.29 ?  85  GLY   B H    1 
ATOM   5621 H HA2  . GLY   B 1 85  ? 50.798 -13.360 -5.148  1.00 16.73 ?  85  GLY   B HA2  1 
ATOM   5622 H HA3  . GLY   B 1 85  ? 50.565 -12.807 -6.596  1.00 16.73 ?  85  GLY   B HA3  1 
ATOM   5623 N N    . HIS   B 1 86  ? 53.375 -11.854 -5.856  1.00 13.31 ?  86  HIS   B N    1 
ATOM   5624 C CA   . HIS   B 1 86  ? 54.836 -12.027 -5.935  1.00 13.16 ?  86  HIS   B CA   1 
ATOM   5625 C C    . HIS   B 1 86  ? 55.204 -12.536 -7.327  1.00 13.47 ?  86  HIS   B C    1 
ATOM   5626 O O    . HIS   B 1 86  ? 54.817 -11.913 -8.327  1.00 13.99 ?  86  HIS   B O    1 
ATOM   5627 C CB   . HIS   B 1 86  ? 55.325 -12.882 -4.763  1.00 13.70 ?  86  HIS   B CB   1 
ATOM   5628 C CG   . HIS   B 1 86  ? 55.018 -12.284 -3.432  1.00 13.33 ?  86  HIS   B CG   1 
ATOM   5629 N ND1  . HIS   B 1 86  ? 55.842 -11.364 -2.817  1.00 15.05 ?  86  HIS   B ND1  1 
ATOM   5630 C CD2  . HIS   B 1 86  ? 53.940 -12.430 -2.625  1.00 14.00 ?  86  HIS   B CD2  1 
ATOM   5631 C CE1  . HIS   B 1 86  ? 55.285 -10.980 -1.683  1.00 14.76 ?  86  HIS   B CE1  1 
ATOM   5632 N NE2  . HIS   B 1 86  ? 54.132 -11.611 -1.542  1.00 13.97 ?  86  HIS   B NE2  1 
ATOM   5633 H H    . HIS   B 1 86  ? 53.138 -11.054 -5.660  1.00 16.03 ?  86  HIS   B H    1 
ATOM   5634 H HA   . HIS   B 1 86  ? 55.252 -11.156 -5.834  1.00 15.85 ?  86  HIS   B HA   1 
ATOM   5635 H HB2  . HIS   B 1 86  ? 54.898 -13.753 -4.809  1.00 16.50 ?  86  HIS   B HB2  1 
ATOM   5636 H HB3  . HIS   B 1 86  ? 56.289 -12.987 -4.826  1.00 16.50 ?  86  HIS   B HB3  1 
ATOM   5637 H HD2  . HIS   B 1 86  ? 53.204 -12.982 -2.778  1.00 16.85 ?  86  HIS   B HD2  1 
ATOM   5638 H HE1  . HIS   B 1 86  ? 55.655 -10.383 -1.074  1.00 17.77 ?  86  HIS   B HE1  1 
ATOM   5639 H HE2  . HIS   B 1 86  ? 53.598 -11.536 -0.870  1.00 16.83 ?  86  HIS   B HE2  1 
ATOM   5640 N N    . ASN   B 1 87  ? 55.968 -13.620 -7.442  1.00 13.84 ?  87  ASN   B N    1 
ATOM   5641 C CA   . ASN   B 1 87  ? 56.372 -14.183 -8.722  1.00 14.57 ?  87  ASN   B CA   1 
ATOM   5642 C C    . ASN   B 1 87  ? 55.396 -15.227 -9.232  1.00 14.18 ?  87  ASN   B C    1 
ATOM   5643 O O    . ASN   B 1 87  ? 55.718 -15.940 -10.185 1.00 15.91 ?  87  ASN   B O    1 
ATOM   5644 C CB   . ASN   B 1 87  ? 57.774 -14.801 -8.611  1.00 16.14 ?  87  ASN   B CB   1 
ATOM   5645 C CG   . ASN   B 1 87  ? 57.843 -15.921 -7.579  1.00 17.43 ?  87  ASN   B CG   1 
ATOM   5646 O OD1  . ASN   B 1 87  ? 57.209 -15.852 -6.520  1.00 16.30 ?  87  ASN   B OD1  1 
ATOM   5647 N ND2  . ASN   B 1 87  ? 58.594 -16.978 -7.901  1.00 19.50 ?  87  ASN   B ND2  1 
ATOM   5648 H H    . ASN   B 1 87  ? 56.275 -14.062 -6.769  1.00 16.67 ?  87  ASN   B H    1 
ATOM   5649 H HA   . ASN   B 1 87  ? 56.415 -13.473 -9.377  1.00 17.54 ?  87  ASN   B HA   1 
ATOM   5650 H HB2  . ASN   B 1 87  ? 58.024 -15.172 -9.477  1.00 19.43 ?  87  ASN   B HB2  1 
ATOM   5651 H HB3  . ASN   B 1 87  ? 58.404 -14.116 -8.352  1.00 19.43 ?  87  ASN   B HB3  1 
ATOM   5652 H HD21 . ASN   B 1 87  ? 58.668 -17.633 -7.353  1.00 23.45 ?  87  ASN   B HD21 1 
ATOM   5653 H HD22 . ASN   B 1 87  ? 59.019 -16.994 -8.652  1.00 23.45 ?  87  ASN   B HD22 1 
ATOM   5654 N N    . LEU   B 1 88  ? 54.217 -15.328 -8.623  1.00 13.32 ?  88  LEU   B N    1 
ATOM   5655 C CA   . LEU   B 1 88  ? 53.246 -16.365 -8.949  1.00 13.14 ?  88  LEU   B CA   1 
ATOM   5656 C C    . LEU   B 1 88  ? 52.008 -15.854 -9.667  1.00 12.94 ?  88  LEU   B C    1 
ATOM   5657 O O    . LEU   B 1 88  ? 51.402 -16.610 -10.440 1.00 14.75 ?  88  LEU   B O    1 
ATOM   5658 C CB   . LEU   B 1 88  ? 52.779 -17.057 -7.665  1.00 14.21 ?  88  LEU   B CB   1 
ATOM   5659 C CG   . LEU   B 1 88  ? 53.882 -17.684 -6.827  1.00 16.23 ?  88  LEU   B CG   1 
ATOM   5660 C CD1  . LEU   B 1 88  ? 53.353 -18.017 -5.441  1.00 17.68 ?  88  LEU   B CD1  1 
ATOM   5661 C CD2  . LEU   B 1 88  ? 54.408 -18.925 -7.518  1.00 18.94 ?  88  LEU   B CD2  1 
ATOM   5662 H H    . LEU   B 1 88  ? 53.956 -14.803 -7.993  1.00 16.05 ?  88  LEU   B H    1 
ATOM   5663 H HA   . LEU   B 1 88  ? 53.663 -17.027 -9.514  1.00 15.83 ?  88  LEU   B HA   1 
ATOM   5664 H HB2  . LEU   B 1 88  ? 52.323 -16.404 -7.110  1.00 17.11 ?  88  LEU   B HB2  1 
ATOM   5665 H HB3  . LEU   B 1 88  ? 52.159 -17.764 -7.907  1.00 17.11 ?  88  LEU   B HB3  1 
ATOM   5666 H HG   . LEU   B 1 88  ? 54.612 -17.052 -6.728  1.00 19.53 ?  88  LEU   B HG   1 
ATOM   5667 H HD11 . LEU   B 1 88  ? 53.998 -18.576 -4.983  1.00 21.27 ?  88  LEU   B HD11 1 
ATOM   5668 H HD12 . LEU   B 1 88  ? 53.217 -17.193 -4.947  1.00 21.27 ?  88  LEU   B HD12 1 
ATOM   5669 H HD13 . LEU   B 1 88  ? 52.511 -18.490 -5.533  1.00 21.27 ?  88  LEU   B HD13 1 
ATOM   5670 H HD21 . LEU   B 1 88  ? 55.085 -19.335 -6.955  1.00 22.79 ?  88  LEU   B HD21 1 
ATOM   5671 H HD22 . LEU   B 1 88  ? 53.675 -19.542 -7.658  1.00 22.79 ?  88  LEU   B HD22 1 
ATOM   5672 H HD23 . LEU   B 1 88  ? 54.797 -18.670 -8.369  1.00 22.79 ?  88  LEU   B HD23 1 
ATOM   5673 N N    . ALA   B 1 89  ? 51.601 -14.615 -9.404  1.00 12.73 ?  89  ALA   B N    1 
ATOM   5674 C CA   . ALA   B 1 89  ? 50.302 -14.131 -9.848  1.00 12.22 ?  89  ALA   B CA   1 
ATOM   5675 C C    . ALA   B 1 89  ? 50.262 -12.638 -9.575  1.00 12.40 ?  89  ALA   B C    1 
ATOM   5676 O O    . ALA   B 1 89  ? 51.095 -12.111 -8.840  1.00 13.22 ?  89  ALA   B O    1 
ATOM   5677 C CB   . ALA   B 1 89  ? 49.179 -14.809 -9.073  1.00 12.04 ?  89  ALA   B CB   1 
ATOM   5678 H H    . ALA   B 1 89  ? 52.049 -14.031 -8.951  1.00 15.33 ?  89  ALA   B H    1 
ATOM   5679 H HA   . ALA   B 1 89  ? 50.183 -14.294 -10.795 1.00 14.72 ?  89  ALA   B HA   1 
ATOM   5680 H HB1  . ALA   B 1 89  ? 48.325 -14.481 -9.398  1.00 14.50 ?  89  ALA   B HB1  1 
ATOM   5681 H HB2  . ALA   B 1 89  ? 49.237 -15.768 -9.209  1.00 14.50 ?  89  ALA   B HB2  1 
ATOM   5682 H HB3  . ALA   B 1 89  ? 49.276 -14.603 -8.130  1.00 14.50 ?  89  ALA   B HB3  1 
ATOM   5683 N N    . LYS   B 1 90  ? 49.255 -11.961 -10.126 1.00 13.24 ?  90  LYS   B N    1 
ATOM   5684 C CA   . LYS   B 1 90  ? 49.055 -10.576 -9.723  1.00 13.88 ?  90  LYS   B CA   1 
ATOM   5685 C C    . LYS   B 1 90  ? 48.747 -10.500 -8.232  1.00 13.55 ?  90  LYS   B C    1 
ATOM   5686 O O    . LYS   B 1 90  ? 49.380 -9.735  -7.486  1.00 14.71 ?  90  LYS   B O    1 
ATOM   5687 C CB   . LYS   B 1 90  ? 47.964 -9.921  -10.575 1.00 14.81 ?  90  LYS   B CB   1 
ATOM   5688 C CG   . LYS   B 1 90  ? 47.673 -8.477  -10.218 1.00 15.88 ?  90  LYS   B CG   1 
ATOM   5689 C CD   . LYS   B 1 90  ? 48.868 -7.569  -10.340 1.00 19.06 ?  90  LYS   B CD   1 
ATOM   5690 C CE   . LYS   B 1 90  ? 48.426 -6.133  -10.135 1.00 21.26 ?  90  LYS   B CE   1 
ATOM   5691 N NZ   . LYS   B 1 90  ? 49.585 -5.214  -10.042 1.00 21.45 ?  90  LYS   B NZ   1 
ATOM   5692 H H    . LYS   B 1 90  ? 48.694 -12.270 -10.704 1.00 15.95 ?  90  LYS   B H    1 
ATOM   5693 H HA   . LYS   B 1 90  ? 49.875 -10.091 -9.876  1.00 16.71 ?  90  LYS   B HA   1 
ATOM   5694 H HB2  . LYS   B 1 90  ? 48.244 -9.943  -11.504 1.00 17.83 ?  90  LYS   B HB2  1 
ATOM   5695 H HB3  . LYS   B 1 90  ? 47.141 -10.424 -10.472 1.00 17.83 ?  90  LYS   B HB3  1 
ATOM   5696 H HG2  . LYS   B 1 90  ? 46.983 -8.144  -10.815 1.00 19.11 ?  90  LYS   B HG2  1 
ATOM   5697 H HG3  . LYS   B 1 90  ? 47.356 -8.438  -9.301  1.00 19.11 ?  90  LYS   B HG3  1 
ATOM   5698 H HD2  . LYS   B 1 90  ? 49.520 -7.793  -9.658  1.00 22.93 ?  90  LYS   B HD2  1 
ATOM   5699 H HD3  . LYS   B 1 90  ? 49.253 -7.654  -11.226 1.00 22.93 ?  90  LYS   B HD3  1 
ATOM   5700 H HE2  . LYS   B 1 90  ? 47.880 -5.852  -10.888 1.00 25.56 ?  90  LYS   B HE2  1 
ATOM   5701 H HE3  . LYS   B 1 90  ? 47.921 -6.063  -9.311  1.00 25.56 ?  90  LYS   B HE3  1 
ATOM   5702 H HZ1  . LYS   B 1 90  ? 49.306 -4.375  -9.924  1.00 25.80 ?  90  LYS   B HZ1  1 
ATOM   5703 H HZ2  . LYS   B 1 90  ? 50.104 -5.443  -9.356  1.00 25.80 ?  90  LYS   B HZ2  1 
ATOM   5704 H HZ3  . LYS   B 1 90  ? 50.068 -5.251  -10.792 1.00 25.80 ?  90  LYS   B HZ3  1 
ATOM   5705 N N    . HIS   B 1 91  ? 47.792 -11.317 -7.778  1.00 12.10 ?  91  HIS   B N    1 
ATOM   5706 C CA   . HIS   B 1 91  ? 47.335 -11.337 -6.401  1.00 12.07 ?  91  HIS   B CA   1 
ATOM   5707 C C    . HIS   B 1 91  ? 47.338 -12.765 -5.885  1.00 11.27 ?  91  HIS   B C    1 
ATOM   5708 O O    . HIS   B 1 91  ? 47.108 -13.721 -6.638  1.00 11.89 ?  91  HIS   B O    1 
ATOM   5709 C CB   . HIS   B 1 91  ? 45.881 -10.858 -6.273  1.00 13.65 ?  91  HIS   B CB   1 
ATOM   5710 C CG   . HIS   B 1 91  ? 45.655 -9.468  -6.751  1.00 16.71 ?  91  HIS   B CG   1 
ATOM   5711 N ND1  . HIS   B 1 91  ? 46.232 -8.369  -6.152  1.00 18.89 ?  91  HIS   B ND1  1 
ATOM   5712 C CD2  . HIS   B 1 91  ? 44.887 -8.991  -7.755  1.00 18.68 ?  91  HIS   B CD2  1 
ATOM   5713 C CE1  . HIS   B 1 91  ? 45.844 -7.272  -6.779  1.00 19.63 ?  91  HIS   B CE1  1 
ATOM   5714 N NE2  . HIS   B 1 91  ? 45.020 -7.623  -7.751  1.00 19.78 ?  91  HIS   B NE2  1 
ATOM   5715 H H    . HIS   B 1 91  ? 47.376 -11.887 -8.272  1.00 14.57 ?  91  HIS   B H    1 
ATOM   5716 H HA   . HIS   B 1 91  ? 47.909 -10.781 -5.840  1.00 14.54 ?  91  HIS   B HA   1 
ATOM   5717 H HB2  . HIS   B 1 91  ? 45.312 -11.443 -6.791  1.00 16.44 ?  91  HIS   B HB2  1 
ATOM   5718 H HB3  . HIS   B 1 91  ? 45.620 -10.893 -5.335  1.00 16.44 ?  91  HIS   B HB3  1 
ATOM   5719 H HD1  . HIS   B 1 91  ? 46.768 -8.389  -5.477  1.00 22.73 ?  91  HIS   B HD1  1 
ATOM   5720 H HD2  . HIS   B 1 91  ? 44.370 -9.485  -8.341  1.00 22.48 ?  91  HIS   B HD2  1 
ATOM   5721 H HE1  . HIS   B 1 91  ? 46.101 -6.399  -6.565  1.00 23.62 ?  91  HIS   B HE1  1 
ATOM   5722 N N    . CYS   B 1 92  ? 47.538 -12.899 -4.584  1.00 11.23 ?  92  CYS   B N    1 
ATOM   5723 C CA   . CYS   B 1 92  ? 47.250 -14.136 -3.875  1.00 11.00 ?  92  CYS   B CA   1 
ATOM   5724 C C    . CYS   B 1 92  ? 46.032 -13.905 -2.988  1.00 10.78 ?  92  CYS   B C    1 
ATOM   5725 O O    . CYS   B 1 92  ? 46.029 -13.005 -2.134  1.00 11.57 ?  92  CYS   B O    1 
ATOM   5726 C CB   . CYS   B 1 92  ? 48.432 -14.602 -3.031  1.00 11.60 ?  92  CYS   B CB   1 
ATOM   5727 S SG   . CYS   B 1 92  ? 48.078 -16.133 -2.139  1.00 11.38 ?  92  CYS   B SG   1 
ATOM   5728 H H    . CYS   B 1 92  ? 47.863 -12.277 -4.077  1.00 13.54 ?  92  CYS   B H    1 
ATOM   5729 H HA   . CYS   B 1 92  ? 47.048 -14.831 -4.520  1.00 13.26 ?  92  CYS   B HA   1 
ATOM   5730 H HB2  . CYS   B 1 92  ? 49.194 -14.755 -3.607  1.00 13.98 ?  92  CYS   B HB2  1 
ATOM   5731 H HB3  . CYS   B 1 92  ? 48.640 -13.915 -2.377  1.00 13.98 ?  92  CYS   B HB3  1 
ATOM   5732 H HG   . CYS   B 1 92  ? 49.063 -16.452 -1.523  1.00 13.71 ?  92  CYS   B HG   1 
ATOM   5733 N N    . LEU   B 1 93  ? 44.997 -14.707 -3.214  1.00 10.70 ?  93  LEU   B N    1 
ATOM   5734 C CA   . LEU   B 1 93  ? 43.826 -14.739 -2.348  1.00 10.55 ?  93  LEU   B CA   1 
ATOM   5735 C C    . LEU   B 1 93  ? 44.059 -15.808 -1.283  1.00 10.09 ?  93  LEU   B C    1 
ATOM   5736 O O    . LEU   B 1 93  ? 44.006 -17.011 -1.573  1.00 11.11 ?  93  LEU   B O    1 
ATOM   5737 C CB   . LEU   B 1 93  ? 42.564 -15.033 -3.159  1.00 11.11 ?  93  LEU   B CB   1 
ATOM   5738 C CG   . LEU   B 1 93  ? 41.260 -15.059 -2.365  1.00 11.63 ?  93  LEU   B CG   1 
ATOM   5739 C CD1  . LEU   B 1 93  ? 40.894 -13.675 -1.854  1.00 12.33 ?  93  LEU   B CD1  1 
ATOM   5740 C CD2  . LEU   B 1 93  ? 40.139 -15.646 -3.206  1.00 11.96 ?  93  LEU   B CD2  1 
ATOM   5741 H H    . LEU   B 1 93  ? 44.952 -15.267 -3.878  1.00 12.90 ?  93  LEU   B H    1 
ATOM   5742 H HA   . LEU   B 1 93  ? 43.724 -13.880 -1.914  1.00 12.71 ?  93  LEU   B HA   1 
ATOM   5743 H HB2  . LEU   B 1 93  ? 42.477 -14.350 -3.843  1.00 13.39 ?  93  LEU   B HB2  1 
ATOM   5744 H HB3  . LEU   B 1 93  ? 42.665 -15.900 -3.578  1.00 13.39 ?  93  LEU   B HB3  1 
ATOM   5745 H HG   . LEU   B 1 93  ? 41.377 -15.627 -1.594  1.00 14.02 ?  93  LEU   B HG   1 
ATOM   5746 H HD11 . LEU   B 1 93  ? 40.039 -13.717 -1.395  1.00 14.85 ?  93  LEU   B HD11 1 
ATOM   5747 H HD12 . LEU   B 1 93  ? 41.580 -13.364 -1.242  1.00 14.85 ?  93  LEU   B HD12 1 
ATOM   5748 H HD13 . LEU   B 1 93  ? 40.827 -13.059 -2.607  1.00 14.85 ?  93  LEU   B HD13 1 
ATOM   5749 H HD21 . LEU   B 1 93  ? 39.320 -15.647 -2.688  1.00 14.40 ?  93  LEU   B HD21 1 
ATOM   5750 H HD22 . LEU   B 1 93  ? 40.025 -15.110 -4.007  1.00 14.40 ?  93  LEU   B HD22 1 
ATOM   5751 H HD23 . LEU   B 1 93  ? 40.375 -16.557 -3.452  1.00 14.40 ?  93  LEU   B HD23 1 
ATOM   5752 N N    . HIS   B 1 94  ? 44.344 -15.376 -0.061  1.00 10.65 ?  94  HIS   B N    1 
ATOM   5753 C CA   . HIS   B 1 94  ? 44.559 -16.288 1.058   1.00 10.38 ?  94  HIS   B CA   1 
ATOM   5754 C C    . HIS   B 1 94  ? 43.195 -16.644 1.638   1.00 10.84 ?  94  HIS   B C    1 
ATOM   5755 O O    . HIS   B 1 94  ? 42.518 -15.774 2.195   1.00 12.29 ?  94  HIS   B O    1 
ATOM   5756 C CB   . HIS   B 1 94  ? 45.432 -15.618 2.116   1.00 10.68 ?  94  HIS   B CB   1 
ATOM   5757 C CG   . HIS   B 1 94  ? 46.813 -15.314 1.644   1.00 10.78 ?  94  HIS   B CG   1 
ATOM   5758 N ND1  . HIS   B 1 94  ? 47.845 -16.226 1.713   1.00 11.05 ?  94  HIS   B ND1  1 
ATOM   5759 C CD2  . HIS   B 1 94  ? 47.310 -14.203 1.053   1.00 11.13 ?  94  HIS   B CD2  1 
ATOM   5760 C CE1  . HIS   B 1 94  ? 48.927 -15.670 1.198   1.00 11.15 ?  94  HIS   B CE1  1 
ATOM   5761 N NE2  . HIS   B 1 94  ? 48.634 -14.442 0.797   1.00 11.19 ?  94  HIS   B NE2  1 
ATOM   5762 H H    . HIS   B 1 94  ? 44.416 -14.542 0.152   1.00 12.84 ?  94  HIS   B H    1 
ATOM   5763 H HA   . HIS   B 1 94  ? 44.998 -17.098 0.747   1.00 12.51 ?  94  HIS   B HA   1 
ATOM   5764 H HB2  . HIS   B 1 94  ? 45.020 -14.784 2.380   1.00 12.87 ?  94  HIS   B HB2  1 
ATOM   5765 H HB3  . HIS   B 1 94  ? 45.506 -16.210 2.880   1.00 12.87 ?  94  HIS   B HB3  1 
ATOM   5766 H HD2  . HIS   B 1 94  ? 46.850 -13.417 0.870   1.00 13.41 ?  94  HIS   B HD2  1 
ATOM   5767 H HE1  . HIS   B 1 94  ? 49.764 -16.079 1.126   1.00 13.44 ?  94  HIS   B HE1  1 
ATOM   5768 H HE2  . HIS   B 1 94  ? 49.184 -13.896 0.426   1.00 13.48 ?  94  HIS   B HE2  1 
ATOM   5769 N N    . VAL   B 1 95  ? 42.774 -17.902 1.486   1.00 10.77 ?  95  VAL   B N    1 
ATOM   5770 C CA   . VAL   B 1 95  ? 41.448 -18.348 1.919   1.00 10.73 ?  95  VAL   B CA   1 
ATOM   5771 C C    . VAL   B 1 95  ? 41.615 -19.390 3.012   1.00 10.73 ?  95  VAL   B C    1 
ATOM   5772 O O    . VAL   B 1 95  ? 42.381 -20.346 2.847   1.00 11.36 ?  95  VAL   B O    1 
ATOM   5773 C CB   . VAL   B 1 95  ? 40.624 -18.946 0.763   1.00 10.95 ?  95  VAL   B CB   1 
ATOM   5774 C CG1  . VAL   B 1 95  ? 39.255 -19.408 1.264   1.00 11.80 ?  95  VAL   B CG1  1 
ATOM   5775 C CG2  . VAL   B 1 95  ? 40.491 -17.954 -0.377  1.00 11.38 ?  95  VAL   B CG2  1 
ATOM   5776 H H    . VAL   B 1 95  ? 43.240 -18.525 1.119   1.00 12.98 ?  95  VAL   B H    1 
ATOM   5777 H HA   . VAL   B 1 95  ? 40.953 -17.597 2.286   1.00 12.93 ?  95  VAL   B HA   1 
ATOM   5778 H HB   . VAL   B 1 95  ? 41.086 -19.726 0.422   1.00 13.19 ?  95  VAL   B HB   1 
ATOM   5779 H HG11 . VAL   B 1 95  ? 38.679 -19.584 0.499   1.00 14.22 ?  95  VAL   B HG11 1 
ATOM   5780 H HG12 . VAL   B 1 95  ? 39.360 -20.226 1.782   1.00 14.22 ?  95  VAL   B HG12 1 
ATOM   5781 H HG13 . VAL   B 1 95  ? 38.863 -18.716 1.816   1.00 14.22 ?  95  VAL   B HG13 1 
ATOM   5782 H HG21 . VAL   B 1 95  ? 39.913 -18.332 -1.060  1.00 13.71 ?  95  VAL   B HG21 1 
ATOM   5783 H HG22 . VAL   B 1 95  ? 40.101 -17.132 -0.035  1.00 13.71 ?  95  VAL   B HG22 1 
ATOM   5784 H HG23 . VAL   B 1 95  ? 41.368 -17.778 -0.744  1.00 13.71 ?  95  VAL   B HG23 1 
ATOM   5785 N N    . VAL   B 1 96  ? 40.886 -19.223 4.112   1.00 11.44 ?  96  VAL   B N    1 
ATOM   5786 C CA   . VAL   B 1 96  ? 40.967 -20.143 5.247   1.00 11.62 ?  96  VAL   B CA   1 
ATOM   5787 C C    . VAL   B 1 96  ? 39.777 -21.099 5.198   1.00 11.74 ?  96  VAL   B C    1 
ATOM   5788 O O    . VAL   B 1 96  ? 38.654 -20.740 5.569   1.00 12.26 ?  96  VAL   B O    1 
ATOM   5789 C CB   . VAL   B 1 96  ? 41.024 -19.397 6.582   1.00 12.45 ?  96  VAL   B CB   1 
ATOM   5790 C CG1  . VAL   B 1 96  ? 41.200 -20.381 7.733   1.00 12.86 ?  96  VAL   B CG1  1 
ATOM   5791 C CG2  . VAL   B 1 96  ? 42.130 -18.351 6.575   1.00 13.28 ?  96  VAL   B CG2  1 
ATOM   5792 H H    . VAL   B 1 96  ? 40.327 -18.580 4.227   1.00 13.79 ?  96  VAL   B H    1 
ATOM   5793 H HA   . VAL   B 1 96  ? 41.779 -20.671 5.169   1.00 14.00 ?  96  VAL   B HA   1 
ATOM   5794 H HB   . VAL   B 1 96  ? 40.184 -18.933 6.716   1.00 15.00 ?  96  VAL   B HB   1 
ATOM   5795 H HG11 . VAL   B 1 96  ? 41.378 -19.881 8.550   1.00 15.49 ?  96  VAL   B HG11 1 
ATOM   5796 H HG12 . VAL   B 1 96  ? 40.390 -20.899 7.838   1.00 15.49 ?  96  VAL   B HG12 1 
ATOM   5797 H HG13 . VAL   B 1 96  ? 41.950 -20.965 7.541   1.00 15.49 ?  96  VAL   B HG13 1 
ATOM   5798 H HG21 . VAL   B 1 96  ? 42.197 -17.949 7.458   1.00 15.99 ?  96  VAL   B HG21 1 
ATOM   5799 H HG22 . VAL   B 1 96  ? 42.971 -18.772 6.341   1.00 15.99 ?  96  VAL   B HG22 1 
ATOM   5800 H HG23 . VAL   B 1 96  ? 41.915 -17.662 5.921   1.00 15.99 ?  96  VAL   B HG23 1 
ATOM   5801 N N    . GLY   B 1 97  ? 40.014 -22.336 4.768   1.00 12.06 ?  97  GLY   B N    1 
ATOM   5802 C CA   . GLY   B 1 97  ? 39.034 -23.388 4.927   1.00 12.12 ?  97  GLY   B CA   1 
ATOM   5803 C C    . GLY   B 1 97  ? 39.149 -23.996 6.305   1.00 12.80 ?  97  GLY   B C    1 
ATOM   5804 O O    . GLY   B 1 97  ? 40.187 -23.876 6.965   1.00 13.26 ?  97  GLY   B O    1 
ATOM   5805 H H    . GLY   B 1 97  ? 40.743 -22.589 4.381   1.00 14.53 ?  97  GLY   B H    1 
ATOM   5806 H HA2  . GLY   B 1 97  ? 38.145 -23.018 4.809   1.00 14.61 ?  97  GLY   B HA2  1 
ATOM   5807 H HA3  . GLY   B 1 97  ? 39.179 -24.077 4.261   1.00 14.61 ?  97  GLY   B HA3  1 
ATOM   5808 N N    . PRO   B 1 98  ? 38.096 -24.673 6.763   1.00 13.07 ?  98  PRO   B N    1 
ATOM   5809 C CA   . PRO   B 1 98  ? 38.177 -25.364 8.053   1.00 14.04 ?  98  PRO   B CA   1 
ATOM   5810 C C    . PRO   B 1 98  ? 39.202 -26.484 8.011   1.00 13.31 ?  98  PRO   B C    1 
ATOM   5811 O O    . PRO   B 1 98  ? 39.308 -27.213 7.026   1.00 13.34 ?  98  PRO   B O    1 
ATOM   5812 C CB   . PRO   B 1 98  ? 36.761 -25.920 8.244   1.00 13.89 ?  98  PRO   B CB   1 
ATOM   5813 C CG   . PRO   B 1 98  ? 36.218 -26.048 6.861   1.00 13.17 ?  98  PRO   B CG   1 
ATOM   5814 C CD   . PRO   B 1 98  ? 36.785 -24.870 6.118   1.00 12.75 ?  98  PRO   B CD   1 
ATOM   5815 H HA   . PRO   B 1 98  ? 38.388 -24.744 8.768   1.00 16.91 ?  98  PRO   B HA   1 
ATOM   5816 H HB2  . PRO   B 1 98  ? 36.805 -26.790 8.674   1.00 16.72 ?  98  PRO   B HB2  1 
ATOM   5817 H HB3  . PRO   B 1 98  ? 36.231 -25.302 8.766   1.00 16.72 ?  98  PRO   B HB3  1 
ATOM   5818 H HG2  . PRO   B 1 98  ? 36.517 -26.879 6.465   1.00 15.86 ?  98  PRO   B HG2  1 
ATOM   5819 H HG3  . PRO   B 1 98  ? 35.250 -26.003 6.885   1.00 15.86 ?  98  PRO   B HG3  1 
ATOM   5820 H HD2  . PRO   B 1 98  ? 36.896 -25.086 5.175   1.00 15.36 ?  98  PRO   B HD2  1 
ATOM   5821 H HD3  . PRO   B 1 98  ? 36.225 -24.087 6.237   1.00 15.36 ?  98  PRO   B HD3  1 
ATOM   5822 N N    A ASN   B 1 99  ? 39.973 -26.599 9.090   0.40 13.84 ?  99  ASN   B N    1 
ATOM   5823 N N    B ASN   B 1 99  ? 39.921 -26.640 9.113   0.60 13.93 ?  99  ASN   B N    1 
ATOM   5824 C CA   A ASN   B 1 99  ? 40.982 -27.644 9.240   0.40 14.39 ?  99  ASN   B CA   1 
ATOM   5825 C CA   B ASN   B 1 99  ? 40.881 -27.722 9.279   0.60 14.32 ?  99  ASN   B CA   1 
ATOM   5826 C C    A ASN   B 1 99  ? 40.402 -28.718 10.152  0.40 15.49 ?  99  ASN   B C    1 
ATOM   5827 C C    B ASN   B 1 99  ? 40.205 -28.809 10.109  0.60 15.22 ?  99  ASN   B C    1 
ATOM   5828 O O    A ASN   B 1 99  ? 40.397 -28.570 11.376  0.40 16.07 ?  99  ASN   B O    1 
ATOM   5829 O O    B ASN   B 1 99  ? 40.019 -28.656 11.318  0.60 15.94 ?  99  ASN   B O    1 
ATOM   5830 C CB   A ASN   B 1 99  ? 42.265 -27.061 9.819   0.40 14.62 ?  99  ASN   B CB   1 
ATOM   5831 C CB   B ASN   B 1 99  ? 42.141 -27.192 9.949   0.60 14.90 ?  99  ASN   B CB   1 
ATOM   5832 C CG   A ASN   B 1 99  ? 43.416 -28.047 9.797   0.40 15.73 ?  99  ASN   B CG   1 
ATOM   5833 C CG   B ASN   B 1 99  ? 43.255 -28.205 9.960   0.60 15.71 ?  99  ASN   B CG   1 
ATOM   5834 O OD1  A ASN   B 1 99  ? 43.217 -29.251 9.946   0.40 16.46 ?  99  ASN   B OD1  1 
ATOM   5835 O OD1  B ASN   B 1 99  ? 43.009 -29.402 10.105  0.60 16.53 ?  99  ASN   B OD1  1 
ATOM   5836 N ND2  A ASN   B 1 99  ? 44.628 -27.540 9.605   0.40 16.04 ?  99  ASN   B ND2  1 
ATOM   5837 N ND2  B ASN   B 1 99  ? 44.487 -27.737 9.792   0.60 16.00 ?  99  ASN   B ND2  1 
ATOM   5838 H H    A ASN   B 1 99  ? 39.928 -26.066 9.764   0.40 16.67 ?  99  ASN   B H    1 
ATOM   5839 H H    B ASN   B 1 99  ? 39.867 -26.120 9.797   0.60 16.77 ?  99  ASN   B H    1 
ATOM   5840 H HA   A ASN   B 1 99  ? 41.176 -28.042 8.378   0.40 17.32 ?  99  ASN   B HA   1 
ATOM   5841 H HA   B ASN   B 1 99  ? 41.113 -28.091 8.412   0.60 17.24 ?  99  ASN   B HA   1 
ATOM   5842 H HB2  A ASN   B 1 99  ? 42.522 -26.288 9.302   0.40 17.60 ?  99  ASN   B HB2  1 
ATOM   5843 H HB2  B ASN   B 1 99  ? 42.443 -26.408 9.469   0.60 17.93 ?  99  ASN   B HB2  1 
ATOM   5844 H HB3  A ASN   B 1 99  ? 42.106 -26.810 10.744  0.40 17.60 ?  99  ASN   B HB3  1 
ATOM   5845 H HB3  B ASN   B 1 99  ? 41.935 -26.967 10.868  0.60 17.93 ?  99  ASN   B HB3  1 
ATOM   5846 H HD21 A ASN   B 1 99  ? 45.315 -28.055 9.586   0.40 19.31 ?  99  ASN   B HD21 1 
ATOM   5847 H HD21 B ASN   B 1 99  ? 45.156 -28.273 9.780   0.60 19.26 ?  99  ASN   B HD21 1 
ATOM   5848 H HD22 A ASN   B 1 99  ? 44.722 -26.690 9.507   0.40 19.31 ?  99  ASN   B HD22 1 
ATOM   5849 H HD22 B ASN   B 1 99  ? 44.613 -26.889 9.694   0.60 19.26 ?  99  ASN   B HD22 1 
ATOM   5850 N N    A VAL   B 1 100 ? 39.905 -29.798 9.542   0.40 17.30 ?  100 VAL   B N    1 
ATOM   5851 N N    B VAL   B 1 100 ? 39.802 -29.894 9.439   0.60 16.61 ?  100 VAL   B N    1 
ATOM   5852 C CA   A VAL   B 1 100 ? 39.329 -30.901 10.308  0.40 19.60 ?  100 VAL   B CA   1 
ATOM   5853 C CA   B VAL   B 1 100 ? 39.165 -31.013 10.130  0.60 18.86 ?  100 VAL   B CA   1 
ATOM   5854 C C    A VAL   B 1 100 ? 40.366 -31.534 11.228  0.40 20.63 ?  100 VAL   B C    1 
ATOM   5855 C C    B VAL   B 1 100 ? 40.127 -31.673 11.108  0.60 19.40 ?  100 VAL   B C    1 
ATOM   5856 O O    A VAL   B 1 100 ? 40.035 -31.970 12.337  0.40 21.07 ?  100 VAL   B O    1 
ATOM   5857 O O    B VAL   B 1 100 ? 39.703 -32.212 12.138  0.60 19.62 ?  100 VAL   B O    1 
ATOM   5858 C CB   A VAL   B 1 100 ? 38.680 -31.927 9.354   0.40 21.49 ?  100 VAL   B CB   1 
ATOM   5859 C CB   B VAL   B 1 100 ? 38.599 -32.020 9.106   0.60 21.40 ?  100 VAL   B CB   1 
ATOM   5860 C CG1  A VAL   B 1 100 ? 38.195 -33.150 10.117  0.40 22.20 ?  100 VAL   B CG1  1 
ATOM   5861 C CG1  B VAL   B 1 100 ? 38.089 -33.274 9.804   0.60 22.52 ?  100 VAL   B CG1  1 
ATOM   5862 C CG2  A VAL   B 1 100 ? 37.527 -31.283 8.595   0.40 22.08 ?  100 VAL   B CG2  1 
ATOM   5863 C CG2  B VAL   B 1 100 ? 37.484 -31.378 8.295   0.60 22.31 ?  100 VAL   B CG2  1 
ATOM   5864 H H    A VAL   B 1 100 ? 39.888 -29.914 8.690   0.40 20.81 ?  100 VAL   B H    1 
ATOM   5865 H H    B VAL   B 1 100 ? 39.871 -30.001 8.585   0.60 19.99 ?  100 VAL   B H    1 
ATOM   5866 H HA   A VAL   B 1 100 ? 38.624 -30.551 10.872  0.40 23.58 ?  100 VAL   B HA   1 
ATOM   5867 H HA   B VAL   B 1 100 ? 38.415 -30.676 10.644  0.60 22.69 ?  100 VAL   B HA   1 
ATOM   5868 H HB   A VAL   B 1 100 ? 39.339 -32.222 8.707   0.40 25.84 ?  100 VAL   B HB   1 
ATOM   5869 H HB   B VAL   B 1 100 ? 39.304 -32.289 8.496   0.60 25.74 ?  100 VAL   B HB   1 
ATOM   5870 H HG11 A VAL   B 1 100 ? 37.610 -33.670 9.539   0.40 26.69 ?  100 VAL   B HG11 1 
ATOM   5871 H HG11 B VAL   B 1 100 ? 37.534 -33.777 9.184   0.60 27.09 ?  100 VAL   B HG11 1 
ATOM   5872 H HG12 A VAL   B 1 100 ? 38.959 -33.688 10.378  0.40 26.69 ?  100 VAL   B HG12 1 
ATOM   5873 H HG12 B VAL   B 1 100 ? 38.844 -33.819 10.081  0.60 27.09 ?  100 VAL   B HG12 1 
ATOM   5874 H HG13 A VAL   B 1 100 ? 37.707 -32.861 10.902  0.40 26.69 ?  100 VAL   B HG13 1 
ATOM   5875 H HG13 B VAL   B 1 100 ? 37.564 -33.016 10.577  0.60 27.09 ?  100 VAL   B HG13 1 
ATOM   5876 H HG21 A VAL   B 1 100 ? 37.110 -31.951 8.027   0.40 26.55 ?  100 VAL   B HG21 1 
ATOM   5877 H HG21 B VAL   B 1 100 ? 37.137 -32.028 7.663   0.60 26.83 ?  100 VAL   B HG21 1 
ATOM   5878 H HG22 A VAL   B 1 100 ? 36.880 -30.943 9.233   0.40 26.55 ?  100 VAL   B HG22 1 
ATOM   5879 H HG22 B VAL   B 1 100 ? 36.778 -31.096 8.899   0.60 26.83 ?  100 VAL   B HG22 1 
ATOM   5880 H HG23 A VAL   B 1 100 ? 37.872 -30.557 8.053   0.40 26.55 ?  100 VAL   B HG23 1 
ATOM   5881 H HG23 B VAL   B 1 100 ? 37.841 -30.614 7.822   0.60 26.83 ?  100 VAL   B HG23 1 
ATOM   5882 N N    A ASN   B 1 101 ? 41.631 -31.592 10.799  0.40 21.52 ?  101 ASN   B N    1 
ATOM   5883 N N    B ASN   B 1 101 ? 41.427 -31.672 10.796  0.60 20.17 ?  101 ASN   B N    1 
ATOM   5884 C CA   A ASN   B 1 101 ? 42.676 -32.130 11.665  0.40 23.03 ?  101 ASN   B CA   1 
ATOM   5885 C CA   B ASN   B 1 101 ? 42.417 -32.213 11.724  0.60 21.98 ?  101 ASN   B CA   1 
ATOM   5886 C C    A ASN   B 1 101 ? 42.892 -31.278 12.908  0.40 24.43 ?  101 ASN   B C    1 
ATOM   5887 C C    B ASN   B 1 101 ? 42.523 -31.386 13.000  0.60 23.52 ?  101 ASN   B C    1 
ATOM   5888 O O    A ASN   B 1 101 ? 43.558 -31.733 13.844  0.40 24.88 ?  101 ASN   B O    1 
ATOM   5889 O O    B ASN   B 1 101 ? 43.060 -31.878 13.999  0.60 24.62 ?  101 ASN   B O    1 
ATOM   5890 C CB   A ASN   B 1 101 ? 43.995 -32.278 10.899  0.40 23.25 ?  101 ASN   B CB   1 
ATOM   5891 C CB   B ASN   B 1 101 ? 43.780 -32.336 11.034  0.60 22.55 ?  101 ASN   B CB   1 
ATOM   5892 C CG   A ASN   B 1 101 ? 43.957 -33.407 9.886   0.40 23.44 ?  101 ASN   B CG   1 
ATOM   5893 C CG   B ASN   B 1 101 ? 43.787 -33.396 9.943   0.60 22.98 ?  101 ASN   B CG   1 
ATOM   5894 O OD1  A ASN   B 1 101 ? 43.323 -34.437 10.111  0.40 23.99 ?  101 ASN   B OD1  1 
ATOM   5895 O OD1  B ASN   B 1 101 ? 43.117 -34.421 10.056  0.60 23.99 ?  101 ASN   B OD1  1 
ATOM   5896 N ND2  A ASN   B 1 101 ? 44.638 -33.219 8.763   0.40 23.40 ?  101 ASN   B ND2  1 
ATOM   5897 N ND2  B ASN   B 1 101 ? 44.543 -33.150 8.880   0.60 23.07 ?  101 ASN   B ND2  1 
ATOM   5898 H H    A ASN   B 1 101 ? 41.907 -31.328 10.028  0.40 25.88 ?  101 ASN   B H    1 
ATOM   5899 H H    B ASN   B 1 101 ? 41.751 -31.383 10.054  0.60 24.26 ?  101 ASN   B H    1 
ATOM   5900 H HA   A ASN   B 1 101 ? 42.410 -33.016 11.956  0.40 27.69 ?  101 ASN   B HA   1 
ATOM   5901 H HA   B ASN   B 1 101 ? 42.146 -33.099 11.990  0.60 26.44 ?  101 ASN   B HA   1 
ATOM   5902 H HB2  A ASN   B 1 101 ? 44.183 -31.455 10.424  0.40 27.95 ?  101 ASN   B HB2  1 
ATOM   5903 H HB2  B ASN   B 1 101 ? 44.019 -31.490 10.624  0.60 27.12 ?  101 ASN   B HB2  1 
ATOM   5904 H HB3  A ASN   B 1 101 ? 44.710 -32.466 11.530  0.40 27.95 ?  101 ASN   B HB3  1 
ATOM   5905 H HB3  B ASN   B 1 101 ? 44.450 -32.582 11.693  0.60 27.12 ?  101 ASN   B HB3  1 
ATOM   5906 H HD21 A ASN   B 1 101 ? 44.647 -33.830 8.158   0.40 28.14 ?  101 ASN   B HD21 1 
ATOM   5907 H HD21 B ASN   B 1 101 ? 44.583 -33.722 8.238   0.60 27.75 ?  101 ASN   B HD21 1 
ATOM   5908 H HD22 A ASN   B 1 101 ? 45.073 -32.487 8.641   0.40 28.14 ?  101 ASN   B HD22 1 
ATOM   5909 H HD22 B ASN   B 1 101 ? 44.994 -32.419 8.831   0.60 27.75 ?  101 ASN   B HD22 1 
ATOM   5910 N N    A LYS   B 1 102 ? 42.363 -30.056 12.928  0.40 25.50 ?  102 LYS   B N    1 
ATOM   5911 N N    B LYS   B 1 102 ? 42.011 -30.152 12.990  0.60 24.79 ?  102 LYS   B N    1 
ATOM   5912 C CA   A LYS   B 1 102 ? 42.343 -29.210 14.114  0.40 26.97 ?  102 LYS   B CA   1 
ATOM   5913 C CA   B LYS   B 1 102 ? 41.954 -29.297 14.169  0.60 26.48 ?  102 LYS   B CA   1 
ATOM   5914 C C    A LYS   B 1 102 ? 40.977 -29.183 14.788  0.40 26.51 ?  102 LYS   B C    1 
ATOM   5915 C C    B LYS   B 1 102 ? 40.564 -29.268 14.796  0.60 26.12 ?  102 LYS   B C    1 
ATOM   5916 O O    A LYS   B 1 102 ? 40.776 -28.402 15.723  0.40 26.92 ?  102 LYS   B O    1 
ATOM   5917 O O    B LYS   B 1 102 ? 40.328 -28.486 15.723  0.60 26.68 ?  102 LYS   B O    1 
ATOM   5918 C CB   A LYS   B 1 102 ? 42.754 -27.781 13.753  0.40 29.27 ?  102 LYS   B CB   1 
ATOM   5919 C CB   B LYS   B 1 102 ? 42.370 -27.865 13.816  0.60 29.07 ?  102 LYS   B CB   1 
ATOM   5920 C CG   A LYS   B 1 102 ? 44.209 -27.610 13.363  0.40 31.46 ?  102 LYS   B CG   1 
ATOM   5921 C CG   B LYS   B 1 102 ? 43.824 -27.683 13.404  0.60 31.51 ?  102 LYS   B CG   1 
ATOM   5922 C CD   A LYS   B 1 102 ? 44.492 -26.155 13.019  0.40 33.43 ?  102 LYS   B CD   1 
ATOM   5923 C CD   B LYS   B 1 102 ? 44.082 -26.235 12.999  0.60 33.72 ?  102 LYS   B CD   1 
ATOM   5924 C CE   A LYS   B 1 102 ? 45.953 -25.923 12.680  0.40 34.94 ?  102 LYS   B CE   1 
ATOM   5925 C CE   B LYS   B 1 102 ? 45.536 -25.987 12.623  0.60 35.38 ?  102 LYS   B CE   1 
ATOM   5926 N NZ   A LYS   B 1 102 ? 46.208 -24.500 12.312  0.40 35.82 ?  102 LYS   B NZ   1 
ATOM   5927 N NZ   B LYS   B 1 102 ? 45.755 -24.579 12.172  0.60 36.34 ?  102 LYS   B NZ   1 
ATOM   5928 H H    A LYS   B 1 102 ? 42.009 -29.683 12.241  0.40 30.66 ?  102 LYS   B H    1 
ATOM   5929 H H    B LYS   B 1 102 ? 41.665 -29.780 12.290  0.60 29.81 ?  102 LYS   B H    1 
ATOM   5930 H HA   A LYS   B 1 102 ? 42.982 -29.551 14.756  0.40 32.42 ?  102 LYS   B HA   1 
ATOM   5931 H HA   B LYS   B 1 102 ? 42.581 -29.632 14.827  0.60 31.83 ?  102 LYS   B HA   1 
ATOM   5932 H HB2  A LYS   B 1 102 ? 42.214 -27.484 13.004  0.40 35.18 ?  102 LYS   B HB2  1 
ATOM   5933 H HB2  B LYS   B 1 102 ? 41.820 -27.555 13.080  0.60 34.94 ?  102 LYS   B HB2  1 
ATOM   5934 H HB3  A LYS   B 1 102 ? 42.589 -27.209 14.519  0.40 35.18 ?  102 LYS   B HB3  1 
ATOM   5935 H HB3  B LYS   B 1 102 ? 42.219 -27.301 14.592  0.60 34.94 ?  102 LYS   B HB3  1 
ATOM   5936 H HG2  A LYS   B 1 102 ? 44.778 -27.866 14.107  0.40 37.80 ?  102 LYS   B HG2  1 
ATOM   5937 H HG2  B LYS   B 1 102 ? 44.404 -27.899 14.152  0.60 37.87 ?  102 LYS   B HG2  1 
ATOM   5938 H HG3  A LYS   B 1 102 ? 44.403 -28.154 12.584  0.40 37.80 ?  102 LYS   B HG3  1 
ATOM   5939 H HG3  B LYS   B 1 102 ? 44.022 -28.254 12.646  0.60 37.87 ?  102 LYS   B HG3  1 
ATOM   5940 H HD2  A LYS   B 1 102 ? 43.958 -25.901 12.249  0.40 40.17 ?  102 LYS   B HD2  1 
ATOM   5941 H HD2  B LYS   B 1 102 ? 43.533 -26.016 12.229  0.60 40.53 ?  102 LYS   B HD2  1 
ATOM   5942 H HD3  A LYS   B 1 102 ? 44.265 -25.598 13.781  0.40 40.17 ?  102 LYS   B HD3  1 
ATOM   5943 H HD3  B LYS   B 1 102 ? 43.861 -25.651 13.742  0.60 40.53 ?  102 LYS   B HD3  1 
ATOM   5944 H HE2  A LYS   B 1 102 ? 46.499 -26.140 13.452  0.40 41.99 ?  102 LYS   B HE2  1 
ATOM   5945 H HE2  B LYS   B 1 102 ? 46.099 -26.148 13.397  0.60 42.51 ?  102 LYS   B HE2  1 
ATOM   5946 H HE3  A LYS   B 1 102 ? 46.200 -26.481 11.926  0.40 41.99 ?  102 LYS   B HE3  1 
ATOM   5947 H HE3  B LYS   B 1 102 ? 45.786 -26.580 11.897  0.60 42.51 ?  102 LYS   B HE3  1 
ATOM   5948 H HZ1  A LYS   B 1 102 ? 47.068 -24.385 12.117  0.40 43.04 ?  102 LYS   B HZ1  1 
ATOM   5949 H HZ1  B LYS   B 1 102 ? 46.610 -24.456 11.958  0.60 43.67 ?  102 LYS   B HZ1  1 
ATOM   5950 H HZ2  A LYS   B 1 102 ? 45.718 -24.278 11.603  0.40 43.04 ?  102 LYS   B HZ2  1 
ATOM   5951 H HZ2  B LYS   B 1 102 ? 45.251 -24.406 11.459  0.60 43.67 ?  102 LYS   B HZ2  1 
ATOM   5952 H HZ3  A LYS   B 1 102 ? 45.991 -23.967 12.991  0.40 43.04 ?  102 LYS   B HZ3  1 
ATOM   5953 H HZ3  B LYS   B 1 102 ? 45.536 -24.013 12.824  0.60 43.67 ?  102 LYS   B HZ3  1 
ATOM   5954 N N    A GLY   B 1 103 ? 40.032 -30.001 14.328  0.40 26.04 ?  103 GLY   B N    1 
ATOM   5955 N N    B GLY   B 1 103 ? 39.635 -30.082 14.303  0.60 25.45 ?  103 GLY   B N    1 
ATOM   5956 C CA   A GLY   B 1 103 ? 38.712 -30.043 14.923  0.40 25.79 ?  103 GLY   B CA   1 
ATOM   5957 C CA   B GLY   B 1 103 ? 38.292 -30.111 14.846  0.60 24.87 ?  103 GLY   B CA   1 
ATOM   5958 C C    A GLY   B 1 103 ? 37.760 -28.968 14.452  0.40 25.30 ?  103 GLY   B C    1 
ATOM   5959 C C    B GLY   B 1 103 ? 37.383 -28.997 14.376  0.60 23.84 ?  103 GLY   B C    1 
ATOM   5960 O O    A GLY   B 1 103 ? 36.660 -28.853 15.006  0.40 25.88 ?  103 GLY   B O    1 
ATOM   5961 O O    B GLY   B 1 103 ? 36.308 -28.810 14.958  0.60 24.71 ?  103 GLY   B O    1 
ATOM   5962 H H    A GLY   B 1 103 ? 40.135 -30.542 13.666  0.40 31.30 ?  103 GLY   B H    1 
ATOM   5963 H H    B GLY   B 1 103 ? 39.764 -30.629 13.653  0.60 30.60 ?  103 GLY   B H    1 
ATOM   5964 H HA2  A GLY   B 1 103 ? 38.313 -30.910 14.741  0.40 31.00 ?  103 GLY   B HA2  1 
ATOM   5965 H HA2  B GLY   B 1 103 ? 37.878 -30.952 14.606  0.60 29.90 ?  103 GLY   B HA2  1 
ATOM   5966 H HA3  A GLY   B 1 103 ? 38.796 -29.950 15.884  0.40 31.00 ?  103 GLY   B HA3  1 
ATOM   5967 H HA3  B GLY   B 1 103 ? 38.348 -30.071 15.816  0.60 29.90 ?  103 GLY   B HA3  1 
ATOM   5968 N N    A GLU   B 1 104 ? 38.143 -28.173 13.458  0.40 24.28 ?  104 GLU   B N    1 
ATOM   5969 N N    B GLU   B 1 104 ? 37.770 -28.255 13.343  0.60 22.18 ?  104 GLU   B N    1 
ATOM   5970 C CA   A GLU   B 1 104 ? 37.284 -27.098 12.986  0.40 23.32 ?  104 GLU   B CA   1 
ATOM   5971 C CA   B GLU   B 1 104 ? 36.966 -27.138 12.875  0.60 20.51 ?  104 GLU   B CA   1 
ATOM   5972 C C    A GLU   B 1 104 ? 36.107 -27.655 12.188  0.40 23.84 ?  104 GLU   B C    1 
ATOM   5973 C C    B GLU   B 1 104 ? 35.804 -27.638 12.023  0.60 20.99 ?  104 GLU   B C    1 
ATOM   5974 O O    A GLU   B 1 104 ? 36.164 -28.754 11.630  0.40 24.26 ?  104 GLU   B O    1 
ATOM   5975 O O    B GLU   B 1 104 ? 35.878 -28.689 11.379  0.60 21.99 ?  104 GLU   B O    1 
ATOM   5976 C CB   A GLU   B 1 104 ? 38.102 -26.101 12.164  0.40 22.39 ?  104 GLU   B CB   1 
ATOM   5977 C CB   B GLU   B 1 104 ? 37.842 -26.149 12.105  0.60 19.31 ?  104 GLU   B CB   1 
ATOM   5978 C CG   A GLU   B 1 104 ? 39.222 -25.458 12.980  0.40 21.57 ?  104 GLU   B CG   1 
ATOM   5979 C CG   B GLU   B 1 104 ? 38.962 -25.603 12.982  0.60 18.23 ?  104 GLU   B CG   1 
ATOM   5980 C CD   A GLU   B 1 104 ? 40.119 -24.544 12.158  0.40 20.98 ?  104 GLU   B CD   1 
ATOM   5981 C CD   B GLU   B 1 104 ? 39.957 -24.710 12.275  0.60 17.63 ?  104 GLU   B CD   1 
ATOM   5982 O OE1  A GLU   B 1 104 ? 40.101 -24.636 10.913  0.40 20.17 ?  104 GLU   B OE1  1 
ATOM   5983 O OE1  B GLU   B 1 104 ? 39.965 -24.632 11.030  0.60 16.94 ?  104 GLU   B OE1  1 
ATOM   5984 O OE2  A GLU   B 1 104 ? 40.842 -23.724 12.765  0.40 21.67 -1 104 GLU   B OE2  1 
ATOM   5985 O OE2  B GLU   B 1 104 ? 40.757 -24.089 13.005  0.60 18.01 -1 104 GLU   B OE2  1 
ATOM   5986 H H    A GLU   B 1 104 ? 38.899 -28.229 13.053  0.40 29.19 ?  104 GLU   B H    1 
ATOM   5987 H H    B GLU   B 1 104 ? 38.497 -28.380 12.902  0.60 26.68 ?  104 GLU   B H    1 
ATOM   5988 H HA   A GLU   B 1 104 ? 36.927 -26.628 13.750  0.40 28.04 ?  104 GLU   B HA   1 
ATOM   5989 H HA   B GLU   B 1 104 ? 36.597 -26.676 13.646  0.60 24.67 ?  104 GLU   B HA   1 
ATOM   5990 H HB2  A GLU   B 1 104 ? 38.507 -26.561 11.411  0.40 26.92 ?  104 GLU   B HB2  1 
ATOM   5991 H HB2  B GLU   B 1 104 ? 38.238 -26.601 11.346  0.60 23.23 ?  104 GLU   B HB2  1 
ATOM   5992 H HB3  A GLU   B 1 104 ? 37.519 -25.394 11.848  0.40 26.92 ?  104 GLU   B HB3  1 
ATOM   5993 H HB3  B GLU   B 1 104 ? 37.293 -25.407 11.809  0.60 23.23 ?  104 GLU   B HB3  1 
ATOM   5994 H HG2  A GLU   B 1 104 ? 38.827 -24.927 13.691  0.40 25.94 ?  104 GLU   B HG2  1 
ATOM   5995 H HG2  B GLU   B 1 104 ? 38.571 -25.083 13.700  0.60 21.94 ?  104 GLU   B HG2  1 
ATOM   5996 H HG3  A GLU   B 1 104 ? 39.771 -26.162 13.370  0.40 25.94 ?  104 GLU   B HG3  1 
ATOM   5997 H HG3  B GLU   B 1 104 ? 39.466 -26.344 13.346  0.60 21.94 ?  104 GLU   B HG3  1 
ATOM   5998 N N    A ASP   B 1 105 ? 35.023 -26.881 12.158  0.40 24.31 ?  105 ASP   B N    1 
ATOM   5999 N N    B ASP   B 1 105 ? 34.715 -26.875 12.041  0.60 21.26 ?  105 ASP   B N    1 
ATOM   6000 C CA   A ASP   B 1 105 ? 33.746 -27.343 11.625  0.40 24.96 ?  105 ASP   B CA   1 
ATOM   6001 C CA   B ASP   B 1 105 ? 33.453 -27.342 11.480  0.60 22.09 ?  105 ASP   B CA   1 
ATOM   6002 C C    A ASP   B 1 105 ? 33.784 -27.373 10.102  0.40 23.96 ?  105 ASP   B C    1 
ATOM   6003 C C    B ASP   B 1 105 ? 33.525 -27.369 9.957   0.60 20.28 ?  105 ASP   B C    1 
ATOM   6004 O O    A ASP   B 1 105 ? 33.960 -26.334 9.456   0.40 23.69 ?  105 ASP   B O    1 
ATOM   6005 O O    B ASP   B 1 105 ? 33.685 -26.327 9.312   0.60 19.02 ?  105 ASP   B O    1 
ATOM   6006 C CB   A ASP   B 1 105 ? 32.630 -26.417 12.104  0.40 26.66 ?  105 ASP   B CB   1 
ATOM   6007 C CB   B ASP   B 1 105 ? 32.314 -26.440 11.951  0.60 24.57 ?  105 ASP   B CB   1 
ATOM   6008 C CG   A ASP   B 1 105 ? 31.257 -26.881 11.664  0.40 28.08 ?  105 ASP   B CG   1 
ATOM   6009 C CG   B ASP   B 1 105 ? 30.944 -27.032 11.666  0.60 26.45 ?  105 ASP   B CG   1 
ATOM   6010 O OD1  A ASP   B 1 105 ? 31.144 -28.013 11.145  0.40 28.28 ?  105 ASP   B OD1  1 
ATOM   6011 O OD1  B ASP   B 1 105 ? 30.821 -27.851 10.732  0.60 27.03 ?  105 ASP   B OD1  1 
ATOM   6012 O OD2  A ASP   B 1 105 ? 30.291 -26.107 11.834  0.40 28.94 -1 105 ASP   B OD2  1 
ATOM   6013 O OD2  B ASP   B 1 105 ? 29.985 -26.679 12.384  0.60 26.85 -1 105 ASP   B OD2  1 
ATOM   6014 H H    A ASP   B 1 105 ? 35.002 -26.074 12.453  0.40 29.23 ?  105 ASP   B H    1 
ATOM   6015 H H    B ASP   B 1 105 ? 34.682 -26.084 12.376  0.60 25.56 ?  105 ASP   B H    1 
ATOM   6016 H HA   A ASP   B 1 105 ? 33.559 -28.239 11.951  0.40 30.00 ?  105 ASP   B HA   1 
ATOM   6017 H HA   B ASP   B 1 105 ? 33.272 -28.242 11.795  0.60 26.56 ?  105 ASP   B HA   1 
ATOM   6018 H HB2  A ASP   B 1 105 ? 32.648 -26.370 13.075  0.40 32.05 ?  105 ASP   B HB2  1 
ATOM   6019 H HB2  B ASP   B 1 105 ? 32.392 -26.304 12.913  0.60 29.54 ?  105 ASP   B HB2  1 
ATOM   6020 H HB3  A ASP   B 1 105 ? 32.767 -25.533 11.729  0.40 32.05 ?  105 ASP   B HB3  1 
ATOM   6021 H HB3  B ASP   B 1 105 ? 32.379 -25.584 11.496  0.60 29.54 ?  105 ASP   B HB3  1 
ATOM   6022 N N    A ILE   B 1 106 ? 33.586 -28.564 9.530   0.40 23.55 ?  106 ILE   B N    1 
ATOM   6023 N N    B ILE   B 1 106 ? 33.387 -28.569 9.386   0.60 20.28 ?  106 ILE   B N    1 
ATOM   6024 C CA   A ILE   B 1 106 ? 33.589 -28.732 8.081   0.40 23.05 ?  106 ILE   B CA   1 
ATOM   6025 C CA   B ILE   B 1 106 ? 33.401 -28.733 7.939   0.60 19.97 ?  106 ILE   B CA   1 
ATOM   6026 C C    A ILE   B 1 106 ? 32.494 -27.911 7.404   0.40 22.33 ?  106 ILE   B C    1 
ATOM   6027 C C    B ILE   B 1 106 ? 32.317 -27.896 7.273   0.60 18.87 ?  106 ILE   B C    1 
ATOM   6028 O O    A ILE   B 1 106 ? 32.596 -27.610 6.210   0.40 22.07 ?  106 ILE   B O    1 
ATOM   6029 O O    B ILE   B 1 106 ? 32.427 -27.565 6.087   0.60 17.75 ?  106 ILE   B O    1 
ATOM   6030 C CB   A ILE   B 1 106 ? 33.484 -30.238 7.740   0.40 23.45 ?  106 ILE   B CB   1 
ATOM   6031 C CB   B ILE   B 1 106 ? 33.282 -30.234 7.590   0.60 21.10 ?  106 ILE   B CB   1 
ATOM   6032 C CG1  A ILE   B 1 106 ? 33.710 -30.479 6.246   0.40 23.45 ?  106 ILE   B CG1  1 
ATOM   6033 C CG1  B ILE   B 1 106 ? 33.600 -30.479 6.116   0.60 21.59 ?  106 ILE   B CG1  1 
ATOM   6034 C CG2  A ILE   B 1 106 ? 32.130 -30.793 8.167   0.40 24.07 ?  106 ILE   B CG2  1 
ATOM   6035 C CG2  B ILE   B 1 106 ? 31.890 -30.758 7.929   0.60 21.99 ?  106 ILE   B CG2  1 
ATOM   6036 C CD1  A ILE   B 1 106 ? 35.057 -29.999 5.752   0.40 23.32 ?  106 ILE   B CD1  1 
ATOM   6037 C CD1  B ILE   B 1 106 ? 34.990 -30.039 5.715   0.60 21.57 ?  106 ILE   B CD1  1 
ATOM   6038 H H    A ILE   B 1 106 ? 33.454 -29.292 9.967   0.40 28.32 ?  106 ILE   B H    1 
ATOM   6039 H H    B ILE   B 1 106 ? 33.287 -29.298 9.823   0.60 24.40 ?  106 ILE   B H    1 
ATOM   6040 H HA   A ILE   B 1 106 ? 34.439 -28.416 7.746   0.40 27.72 ?  106 ILE   B HA   1 
ATOM   6041 H HA   B ILE   B 1 106 ? 34.252 -28.417 7.608   0.60 24.03 ?  106 ILE   B HA   1 
ATOM   6042 H HB   A ILE   B 1 106 ? 34.173 -30.713 8.231   0.40 28.20 ?  106 ILE   B HB   1 
ATOM   6043 H HB   B ILE   B 1 106 ? 33.928 -30.724 8.126   0.60 25.38 ?  106 ILE   B HB   1 
ATOM   6044 H HG12 A ILE   B 1 106 ? 33.657 -31.434 6.072   0.40 28.20 ?  106 ILE   B HG12 1 
ATOM   6045 H HG12 B ILE   B 1 106 ? 33.529 -31.430 5.934   0.60 25.97 ?  106 ILE   B HG12 1 
ATOM   6046 H HG13 A ILE   B 1 106 ? 33.025 -30.017 5.742   0.40 28.20 ?  106 ILE   B HG13 1 
ATOM   6047 H HG13 B ILE   B 1 106 ? 32.965 -29.992 5.571   0.60 25.97 ?  106 ILE   B HG13 1 
ATOM   6048 H HG21 A ILE   B 1 106 ? 32.136 -31.757 8.059   0.40 28.94 ?  106 ILE   B HG21 1 
ATOM   6049 H HG21 B ILE   B 1 106 ? 31.900 -31.727 7.886   0.60 26.44 ?  106 ILE   B HG21 1 
ATOM   6050 H HG22 A ILE   B 1 106 ? 31.975 -30.566 9.097   0.40 28.94 ?  106 ILE   B HG22 1 
ATOM   6051 H HG22 B ILE   B 1 106 ? 31.654 -30.469 8.824   0.60 26.44 ?  106 ILE   B HG22 1 
ATOM   6052 H HG23 A ILE   B 1 106 ? 31.437 -30.403 7.611   0.40 28.94 ?  106 ILE   B HG23 1 
ATOM   6053 H HG23 B ILE   B 1 106 ? 31.254 -30.404 7.289   0.60 26.44 ?  106 ILE   B HG23 1 
ATOM   6054 H HD11 A ILE   B 1 106 ? 35.234 -30.394 4.885   0.40 28.04 ?  106 ILE   B HD11 1 
ATOM   6055 H HD11 B ILE   B 1 106 ? 35.227 -30.462 4.876   0.60 25.94 ?  106 ILE   B HD11 1 
ATOM   6056 H HD12 A ILE   B 1 106 ? 35.039 -29.031 5.676   0.40 28.04 ?  106 ILE   B HD12 1 
ATOM   6057 H HD12 B ILE   B 1 106 ? 35.001 -29.073 5.611   0.60 25.94 ?  106 ILE   B HD12 1 
ATOM   6058 H HD13 A ILE   B 1 106 ? 35.741 -30.270 6.385   0.40 28.04 ?  106 ILE   B HD13 1 
ATOM   6059 H HD13 B ILE   B 1 106 ? 35.619 -30.304 6.406   0.60 25.94 ?  106 ILE   B HD13 1 
ATOM   6060 N N    A GLN   B 1 107 ? 31.446 -27.535 8.141   0.40 22.49 ?  107 GLN   B N    1 
ATOM   6061 N N    B GLN   B 1 107 ? 31.272 -27.527 8.016   0.60 20.20 ?  107 GLN   B N    1 
ATOM   6062 C CA   A GLN   B 1 107 ? 30.344 -26.782 7.545   0.40 22.63 ?  107 GLN   B CA   1 
ATOM   6063 C CA   B GLN   B 1 107 ? 30.222 -26.689 7.455   0.60 21.58 ?  107 GLN   B CA   1 
ATOM   6064 C C    A GLN   B 1 107 ? 30.808 -25.443 6.980   0.40 20.45 ?  107 GLN   B C    1 
ATOM   6065 C C    B GLN   B 1 107 ? 30.749 -25.335 6.995   0.60 20.11 ?  107 GLN   B C    1 
ATOM   6066 O O    A GLN   B 1 107 ? 30.194 -24.921 6.043   0.40 20.74 ?  107 GLN   B O    1 
ATOM   6067 O O    B GLN   B 1 107 ? 30.126 -24.703 6.138   0.60 21.07 ?  107 GLN   B O    1 
ATOM   6068 C CB   A GLN   B 1 107 ? 29.243 -26.575 8.588   0.40 25.46 ?  107 GLN   B CB   1 
ATOM   6069 C CB   B GLN   B 1 107 ? 29.102 -26.501 8.482   0.60 25.40 ?  107 GLN   B CB   1 
ATOM   6070 C CG   A GLN   B 1 107 ? 27.929 -26.039 8.034   0.40 28.25 ?  107 GLN   B CG   1 
ATOM   6071 C CG   B GLN   B 1 107 ? 27.748 -26.154 7.879   0.60 29.28 ?  107 GLN   B CG   1 
ATOM   6072 C CD   A GLN   B 1 107 ? 27.898 -24.525 7.946   0.40 30.43 ?  107 GLN   B CD   1 
ATOM   6073 C CD   B GLN   B 1 107 ? 27.538 -24.661 7.703   0.60 32.24 ?  107 GLN   B CD   1 
ATOM   6074 O OE1  A GLN   B 1 107 ? 28.738 -23.837 8.531   0.40 31.23 ?  107 GLN   B OE1  1 
ATOM   6075 O OE1  B GLN   B 1 107 ? 28.328 -23.847 8.182   0.60 33.54 ?  107 GLN   B OE1  1 
ATOM   6076 N NE2  A GLN   B 1 107 ? 26.922 -23.996 7.213   0.40 31.25 ?  107 GLN   B NE2  1 
ATOM   6077 N NE2  B GLN   B 1 107 ? 26.461 -24.294 7.016   0.60 33.18 ?  107 GLN   B NE2  1 
ATOM   6078 H H    A GLN   B 1 107 ? 31.348 -27.706 8.975   0.40 27.05 ?  107 GLN   B H    1 
ATOM   6079 H H    B GLN   B 1 107 ? 31.150 -27.749 8.837   0.60 24.30 ?  107 GLN   B H    1 
ATOM   6080 H HA   A GLN   B 1 107 ? 29.969 -27.298 6.813   0.40 27.22 ?  107 GLN   B HA   1 
ATOM   6081 H HA   B GLN   B 1 107 ? 29.843 -27.141 6.684   0.60 25.95 ?  107 GLN   B HA   1 
ATOM   6082 H HB2  A GLN   B 1 107 ? 29.054 -27.426 9.009   0.40 30.60 ?  107 GLN   B HB2  1 
ATOM   6083 H HB2  B GLN   B 1 107 ? 28.997 -27.326 8.980   0.60 30.53 ?  107 GLN   B HB2  1 
ATOM   6084 H HB3  A GLN   B 1 107 ? 29.560 -25.947 9.255   0.40 30.60 ?  107 GLN   B HB3  1 
ATOM   6085 H HB3  B GLN   B 1 107 ? 29.351 -25.785 9.088   0.60 30.53 ?  107 GLN   B HB3  1 
ATOM   6086 H HG2  A GLN   B 1 107 ? 27.790 -26.391 7.142   0.40 33.96 ?  107 GLN   B HG2  1 
ATOM   6087 H HG2  B GLN   B 1 107 ? 27.674 -26.570 7.006   0.60 35.20 ?  107 GLN   B HG2  1 
ATOM   6088 H HG3  A GLN   B 1 107 ? 27.201 -26.324 8.616   0.40 33.96 ?  107 GLN   B HG3  1 
ATOM   6089 H HG3  B GLN   B 1 107 ? 27.049 -26.491 8.464   0.60 35.20 ?  107 GLN   B HG3  1 
ATOM   6090 H HE21 A GLN   B 1 107 ? 26.354 -24.509 6.816   0.40 37.56 ?  107 GLN   B HE21 1 
ATOM   6091 H HE21 B GLN   B 1 107 ? 25.933 -24.890 6.693   0.60 39.88 ?  107 GLN   B HE21 1 
ATOM   6092 H HE22 A GLN   B 1 107 ? 26.855 -23.143 7.135   0.40 37.56 ?  107 GLN   B HE22 1 
ATOM   6093 H HE22 B GLN   B 1 107 ? 26.296 -23.459 6.892   0.60 39.88 ?  107 GLN   B HE22 1 
ATOM   6094 N N    . LEU   B 1 108 ? 31.894 -24.884 7.522   1.00 18.24 ?  108 LEU   B N    1 
ATOM   6095 C CA   . LEU   B 1 108 ? 32.452 -23.596 7.101   1.00 16.28 ?  108 LEU   B CA   1 
ATOM   6096 C C    . LEU   B 1 108 ? 33.097 -23.634 5.725   1.00 14.65 ?  108 LEU   B C    1 
ATOM   6097 O O    . LEU   B 1 108 ? 33.534 -22.585 5.230   1.00 14.74 ?  108 LEU   B O    1 
ATOM   6098 C CB   . LEU   B 1 108 ? 33.465 -23.118 8.139   1.00 17.23 ?  108 LEU   B CB   1 
ATOM   6099 C CG   . LEU   B 1 108 ? 32.841 -22.661 9.456   1.00 18.71 ?  108 LEU   B CG   1 
ATOM   6100 C CD1  . LEU   B 1 108 ? 33.878 -22.561 10.558  1.00 19.02 ?  108 LEU   B CD1  1 
ATOM   6101 C CD2  . LEU   B 1 108 ? 32.151 -21.322 9.263   1.00 20.37 ?  108 LEU   B CD2  1 
ATOM   6102 H H    A LEU   B 1 108 ? 32.336 -25.251 8.161   0.40 21.94 ?  108 LEU   B H    1 
ATOM   6103 H H    B LEU   B 1 108 ? 32.351 -25.298 8.121   0.60 21.94 ?  108 LEU   B H    1 
ATOM   6104 H HA   . LEU   B 1 108 ? 31.730 -22.953 7.069   1.00 19.60 ?  108 LEU   B HA   1 
ATOM   6105 H HB2  . LEU   B 1 108 ? 34.075 -23.841 8.343   1.00 20.73 ?  108 LEU   B HB2  1 
ATOM   6106 H HB3  . LEU   B 1 108 ? 33.952 -22.366 7.772   1.00 20.73 ?  108 LEU   B HB3  1 
ATOM   6107 H HG   . LEU   B 1 108 ? 32.169 -23.305 9.737   1.00 22.51 ?  108 LEU   B HG   1 
ATOM   6108 H HD11 . LEU   B 1 108 ? 33.442 -22.301 11.385  1.00 22.88 ?  108 LEU   B HD11 1 
ATOM   6109 H HD12 . LEU   B 1 108 ? 34.306 -23.424 10.667  1.00 22.88 ?  108 LEU   B HD12 1 
ATOM   6110 H HD13 . LEU   B 1 108 ? 34.538 -21.894 10.309  1.00 22.88 ?  108 LEU   B HD13 1 
ATOM   6111 H HD21 . LEU   B 1 108 ? 31.859 -20.987 10.126  1.00 24.50 ?  108 LEU   B HD21 1 
ATOM   6112 H HD22 . LEU   B 1 108 ? 32.778 -20.700 8.862   1.00 24.50 ?  108 LEU   B HD22 1 
ATOM   6113 H HD23 . LEU   B 1 108 ? 31.385 -21.442 8.679   1.00 24.50 ?  108 LEU   B HD23 1 
ATOM   6114 N N    . LEU   B 1 109 ? 33.164 -24.807 5.099   1.00 13.82 ?  109 LEU   B N    1 
ATOM   6115 C CA   . LEU   B 1 109 ? 33.796 -24.914 3.792   1.00 13.19 ?  109 LEU   B CA   1 
ATOM   6116 C C    . LEU   B 1 109 ? 33.032 -24.131 2.732   1.00 12.40 ?  109 LEU   B C    1 
ATOM   6117 O O    . LEU   B 1 109 ? 33.648 -23.537 1.841   1.00 12.30 ?  109 LEU   B O    1 
ATOM   6118 C CB   . LEU   B 1 109 ? 33.918 -26.389 3.406   1.00 13.19 ?  109 LEU   B CB   1 
ATOM   6119 C CG   . LEU   B 1 109 ? 34.699 -26.715 2.132   1.00 13.17 ?  109 LEU   B CG   1 
ATOM   6120 C CD1  . LEU   B 1 109 ? 36.077 -26.051 2.123   1.00 13.32 ?  109 LEU   B CD1  1 
ATOM   6121 C CD2  . LEU   B 1 109 ? 34.825 -28.223 1.978   1.00 13.96 ?  109 LEU   B CD2  1 
ATOM   6122 H H    . LEU   B 1 109 ? 32.855 -25.550 5.402   1.00 16.64 ?  109 LEU   B H    1 
ATOM   6123 H HA   . LEU   B 1 109 ? 34.691 -24.545 3.846   1.00 15.88 ?  109 LEU   B HA   1 
ATOM   6124 H HB2  . LEU   B 1 109 ? 34.359 -26.857 4.132   1.00 15.89 ?  109 LEU   B HB2  1 
ATOM   6125 H HB3  . LEU   B 1 109 ? 33.024 -26.749 3.292   1.00 15.89 ?  109 LEU   B HB3  1 
ATOM   6126 H HG   . LEU   B 1 109 ? 34.200 -26.381 1.365   1.00 15.87 ?  109 LEU   B HG   1 
ATOM   6127 H HD11 . LEU   B 1 109 ? 36.589 -26.395 1.377   1.00 16.05 ?  109 LEU   B HD11 1 
ATOM   6128 H HD12 . LEU   B 1 109 ? 35.963 -25.089 2.029   1.00 16.05 ?  109 LEU   B HD12 1 
ATOM   6129 H HD13 . LEU   B 1 109 ? 36.526 -26.250 2.957   1.00 16.05 ?  109 LEU   B HD13 1 
ATOM   6130 H HD21 . LEU   B 1 109 ? 35.395 -28.416 1.214   1.00 16.81 ?  109 LEU   B HD21 1 
ATOM   6131 H HD22 . LEU   B 1 109 ? 35.220 -28.589 2.783   1.00 16.81 ?  109 LEU   B HD22 1 
ATOM   6132 H HD23 . LEU   B 1 109 ? 33.945 -28.604 1.837   1.00 16.81 ?  109 LEU   B HD23 1 
ATOM   6133 N N    . LYS   B 1 110 ? 31.699 -24.101 2.810   1.00 12.25 ?  110 LYS   B N    1 
ATOM   6134 C CA   . LYS   B 1 110 ? 30.943 -23.335 1.820   1.00 12.31 ?  110 LYS   B CA   1 
ATOM   6135 C C    . LYS   B 1 110 ? 31.279 -21.847 1.910   1.00 12.16 ?  110 LYS   B C    1 
ATOM   6136 O O    . LYS   B 1 110 ? 31.536 -21.196 0.893   1.00 11.87 ?  110 LYS   B O    1 
ATOM   6137 C CB   . LYS   B 1 110 ? 29.441 -23.577 1.965   1.00 12.97 ?  110 LYS   B CB   1 
ATOM   6138 C CG   . LYS   B 1 110 ? 28.647 -22.944 0.831   1.00 13.14 ?  110 LYS   B CG   1 
ATOM   6139 C CD   . LYS   B 1 110 ? 27.184 -23.394 0.841   1.00 13.68 ?  110 LYS   B CD   1 
ATOM   6140 C CE   . LYS   B 1 110 ? 26.405 -22.854 -0.360  1.00 14.38 ?  110 LYS   B CE   1 
ATOM   6141 N NZ   . LYS   B 1 110 ? 26.735 -23.557 -1.632  1.00 14.54 ?  110 LYS   B NZ   1 
ATOM   6142 H H    . LYS   B 1 110 ? 31.225 -24.503 3.400   1.00 14.75 ?  110 LYS   B H    1 
ATOM   6143 H HA   . LYS   B 1 110 ? 31.205 -23.637 0.933   1.00 14.83 ?  110 LYS   B HA   1 
ATOM   6144 H HB2  . LYS   B 1 110 ? 29.275 -24.536 1.956   1.00 15.62 ?  110 LYS   B HB2  1 
ATOM   6145 H HB3  . LYS   B 1 110 ? 29.138 -23.196 2.800   1.00 15.62 ?  110 LYS   B HB3  1 
ATOM   6146 H HG2  . LYS   B 1 110 ? 28.662 -21.983 0.924   1.00 15.83 ?  110 LYS   B HG2  1 
ATOM   6147 H HG3  . LYS   B 1 110 ? 29.033 -23.208 -0.020  1.00 15.83 ?  110 LYS   B HG3  1 
ATOM   6148 H HD2  . LYS   B 1 110 ? 27.147 -24.369 0.811   1.00 16.48 ?  110 LYS   B HD2  1 
ATOM   6149 H HD3  . LYS   B 1 110 ? 26.755 -23.076 1.650   1.00 16.48 ?  110 LYS   B HD3  1 
ATOM   6150 H HE2  . LYS   B 1 110 ? 25.457 -22.961 -0.197  1.00 17.31 ?  110 LYS   B HE2  1 
ATOM   6151 H HE3  . LYS   B 1 110 ? 26.621 -21.916 -0.474  1.00 17.31 ?  110 LYS   B HE3  1 
ATOM   6152 H HZ1  . LYS   B 1 110 ? 26.265 -23.211 -2.300  1.00 17.51 ?  110 LYS   B HZ1  1 
ATOM   6153 H HZ2  . LYS   B 1 110 ? 27.603 -23.470 -1.810  1.00 17.51 ?  110 LYS   B HZ2  1 
ATOM   6154 H HZ3  . LYS   B 1 110 ? 26.541 -24.423 -1.558  1.00 17.51 ?  110 LYS   B HZ3  1 
ATOM   6155 N N    . SER   B 1 111 ? 31.301 -21.297 3.129   1.00 12.31 ?  111 SER   B N    1 
ATOM   6156 C CA   . SER   B 1 111 ? 31.688 -19.897 3.306   1.00 12.55 ?  111 SER   B CA   1 
ATOM   6157 C C    . SER   B 1 111 ? 33.073 -19.632 2.725   1.00 12.04 ?  111 SER   B C    1 
ATOM   6158 O O    . SER   B 1 111 ? 33.301 -18.599 2.082   1.00 12.43 ?  111 SER   B O    1 
ATOM   6159 C CB   . SER   B 1 111 ? 31.672 -19.548 4.790   1.00 13.81 ?  111 SER   B CB   1 
ATOM   6160 O OG   . SER   B 1 111 ? 30.359 -19.589 5.314   1.00 15.67 ?  111 SER   B OG   1 
ATOM   6161 H H    . SER   B 1 111 ? 31.097 -21.709 3.855   1.00 14.83 ?  111 SER   B H    1 
ATOM   6162 H HA   . SER   B 1 111 ? 31.052 -19.327 2.850   1.00 15.11 ?  111 SER   B HA   1 
ATOM   6163 H HB2  . SER   B 1 111 ? 32.217 -20.188 5.273   1.00 16.63 ?  111 SER   B HB2  1 
ATOM   6164 H HB3  . SER   B 1 111 ? 32.029 -18.655 4.907   1.00 16.63 ?  111 SER   B HB3  1 
ATOM   6165 H HG   . SER   B 1 111 ? 30.368 -19.388 6.135   1.00 18.86 ?  111 SER   B HG   1 
ATOM   6166 N N    . ALA   B 1 112 ? 34.013 -20.551 2.948   1.00 12.10 ?  112 ALA   B N    1 
ATOM   6167 C CA   . ALA   B 1 112 ? 35.357 -20.380 2.408   1.00 11.46 ?  112 ALA   B CA   1 
ATOM   6168 C C    . ALA   B 1 112 ? 35.325 -20.280 0.887   1.00 11.17 ?  112 ALA   B C    1 
ATOM   6169 O O    . ALA   B 1 112 ? 35.957 -19.399 0.296   1.00 11.41 ?  112 ALA   B O    1 
ATOM   6170 C CB   . ALA   B 1 112 ? 36.264 -21.520 2.883   1.00 12.22 ?  112 ALA   B CB   1 
ATOM   6171 H H    . ALA   B 1 112 ? 33.902 -21.272 3.410   1.00 14.58 ?  112 ALA   B H    1 
ATOM   6172 H HA   . ALA   B 1 112 ? 35.725 -19.549 2.752   1.00 13.81 ?  112 ALA   B HA   1 
ATOM   6173 H HB1  . ALA   B 1 112 ? 37.156 -21.382 2.523   1.00 14.72 ?  112 ALA   B HB1  1 
ATOM   6174 H HB2  . ALA   B 1 112 ? 36.302 -21.508 3.856   1.00 14.72 ?  112 ALA   B HB2  1 
ATOM   6175 H HB3  . ALA   B 1 112 ? 35.905 -22.360 2.576   1.00 14.72 ?  112 ALA   B HB3  1 
ATOM   6176 N N    . TYR   B 1 113 ? 34.591 -21.177 0.228   1.00 11.31 ?  113 TYR   B N    1 
ATOM   6177 C CA   . TYR   B 1 113 ? 34.515 -21.127 -1.227  1.00 11.28 ?  113 TYR   B CA   1 
ATOM   6178 C C    . TYR   B 1 113 ? 33.812 -19.872 -1.740  1.00 10.77 ?  113 TYR   B C    1 
ATOM   6179 O O    . TYR   B 1 113 ? 34.087 -19.442 -2.865  1.00 11.24 ?  113 TYR   B O    1 
ATOM   6180 C CB   . TYR   B 1 113 ? 33.841 -22.386 -1.778  1.00 11.18 ?  113 TYR   B CB   1 
ATOM   6181 C CG   . TYR   B 1 113 ? 34.795 -23.531 -2.048  1.00 11.64 ?  113 TYR   B CG   1 
ATOM   6182 C CD1  . TYR   B 1 113 ? 35.793 -23.423 -3.017  1.00 12.13 ?  113 TYR   B CD1  1 
ATOM   6183 C CD2  . TYR   B 1 113 ? 34.706 -24.722 -1.340  1.00 11.74 ?  113 TYR   B CD2  1 
ATOM   6184 C CE1  . TYR   B 1 113 ? 36.668 -24.461 -3.269  1.00 12.04 ?  113 TYR   B CE1  1 
ATOM   6185 C CE2  . TYR   B 1 113 ? 35.571 -25.775 -1.595  1.00 12.02 ?  113 TYR   B CE2  1 
ATOM   6186 C CZ   . TYR   B 1 113 ? 36.554 -25.638 -2.561  1.00 12.25 ?  113 TYR   B CZ   1 
ATOM   6187 O OH   . TYR   B 1 113 ? 37.436 -26.653 -2.845  1.00 13.03 ?  113 TYR   B OH   1 
ATOM   6188 H H    . TYR   B 1 113 ? 34.125 -21.805 0.598   1.00 13.64 ?  113 TYR   B H    1 
ATOM   6189 H HA   . TYR   B 1 113 ? 35.419 -21.110 -1.564  1.00 13.59 ?  113 TYR   B HA   1 
ATOM   6190 H HB2  . TYR   B 1 113 ? 33.186 -22.701 -1.136  1.00 13.47 ?  113 TYR   B HB2  1 
ATOM   6191 H HB3  . TYR   B 1 113 ? 33.406 -22.165 -2.613  1.00 13.47 ?  113 TYR   B HB3  1 
ATOM   6192 H HD1  . TYR   B 1 113 ? 35.873 -22.630 -3.501  1.00 14.62 ?  113 TYR   B HD1  1 
ATOM   6193 H HD2  . TYR   B 1 113 ? 34.046 -24.820 -0.698  1.00 14.14 ?  113 TYR   B HD2  1 
ATOM   6194 H HE1  . TYR   B 1 113 ? 37.324 -24.368 -3.925  1.00 14.50 ?  113 TYR   B HE1  1 
ATOM   6195 H HE2  . TYR   B 1 113 ? 35.495 -26.566 -1.118  1.00 14.48 ?  113 TYR   B HE2  1 
ATOM   6196 H HH   . TYR   B 1 113 ? 37.262 -27.316 -2.354  1.00 15.69 ?  113 TYR   B HH   1 
ATOM   6197 N N    . GLU   B 1 114 ? 32.885 -19.302 -0.963  1.00 11.03 ?  114 GLU   B N    1 
ATOM   6198 C CA   . GLU   B 1 114 ? 32.205 -18.094 -1.422  1.00 11.09 ?  114 GLU   B CA   1 
ATOM   6199 C C    . GLU   B 1 114 ? 33.189 -16.969 -1.714  1.00 10.91 ?  114 GLU   B C    1 
ATOM   6200 O O    . GLU   B 1 114 ? 32.905 -16.097 -2.544  1.00 11.28 ?  114 GLU   B O    1 
ATOM   6201 C CB   . GLU   B 1 114 ? 31.139 -17.665 -0.409  1.00 11.05 ?  114 GLU   B CB   1 
ATOM   6202 C CG   . GLU   B 1 114 ? 29.923 -18.589 -0.472  1.00 11.80 ?  114 GLU   B CG   1 
ATOM   6203 C CD   . GLU   B 1 114 ? 28.912 -18.407 0.645   1.00 11.71 ?  114 GLU   B CD   1 
ATOM   6204 O OE1  . GLU   B 1 114 ? 29.215 -17.791 1.690   1.00 12.31 ?  114 GLU   B OE1  1 
ATOM   6205 O OE2  . GLU   B 1 114 ? 27.782 -18.932 0.482   1.00 12.69 -1 114 GLU   B OE2  1 
ATOM   6206 H H    . GLU   B 1 114 ? 32.629 -19.594 -0.194  1.00 13.29 ?  114 GLU   B H    1 
ATOM   6207 H HA   . GLU   B 1 114 ? 31.746 -18.296 -2.250  1.00 13.36 ?  114 GLU   B HA   1 
ATOM   6208 H HB2  . GLU   B 1 114 ? 31.508 -17.712 0.489   1.00 13.32 ?  114 GLU   B HB2  1 
ATOM   6209 H HB3  . GLU   B 1 114 ? 30.846 -16.765 -0.606  1.00 13.32 ?  114 GLU   B HB3  1 
ATOM   6210 H HG2  . GLU   B 1 114 ? 29.459 -18.434 -1.308  1.00 14.22 ?  114 GLU   B HG2  1 
ATOM   6211 H HG3  . GLU   B 1 114 ? 30.231 -19.510 -0.437  1.00 14.22 ?  114 GLU   B HG3  1 
ATOM   6212 N N    . ASN   B 1 115 ? 34.354 -16.971 -1.064  1.00 11.21 ?  115 ASN   B N    1 
ATOM   6213 C CA   . ASN   B 1 115 ? 35.344 -15.940 -1.358  1.00 11.09 ?  115 ASN   B CA   1 
ATOM   6214 C C    . ASN   B 1 115 ? 35.753 -15.950 -2.818  1.00 10.87 ?  115 ASN   B C    1 
ATOM   6215 O O    . ASN   B 1 115 ? 36.138 -14.903 -3.365  1.00 11.56 ?  115 ASN   B O    1 
ATOM   6216 C CB   . ASN   B 1 115 ? 36.586 -16.117 -0.482  1.00 11.73 ?  115 ASN   B CB   1 
ATOM   6217 C CG   . ASN   B 1 115 ? 36.322 -15.853 0.978   1.00 12.25 ?  115 ASN   B CG   1 
ATOM   6218 O OD1  . ASN   B 1 115 ? 36.320 -14.703 1.416   1.00 14.12 ?  115 ASN   B OD1  1 
ATOM   6219 N ND2  . ASN   B 1 115 ? 36.165 -16.921 1.760   1.00 12.33 ?  115 ASN   B ND2  1 
ATOM   6220 H H    . ASN   B 1 115 ? 34.591 -17.541 -0.462  1.00 13.51 ?  115 ASN   B H    1 
ATOM   6221 H HA   . ASN   B 1 115 ? 34.965 -15.070 -1.158  1.00 13.36 ?  115 ASN   B HA   1 
ATOM   6222 H HB2  . ASN   B 1 115 ? 36.909 -17.028 -0.570  1.00 14.13 ?  115 ASN   B HB2  1 
ATOM   6223 H HB3  . ASN   B 1 115 ? 37.273 -15.496 -0.776  1.00 14.13 ?  115 ASN   B HB3  1 
ATOM   6224 H HD21 . ASN   B 1 115 ? 36.018 -16.819 2.602   1.00 14.86 ?  115 ASN   B HD21 1 
ATOM   6225 H HD22 . ASN   B 1 115 ? 36.179 -17.710 1.420   1.00 14.86 ?  115 ASN   B HD22 1 
ATOM   6226 N N    . PHE   B 1 116 ? 35.723 -17.121 -3.461  1.00 10.64 ?  116 PHE   B N    1 
ATOM   6227 C CA   . PHE   B 1 116 ? 36.151 -17.204 -4.849  1.00 10.83 ?  116 PHE   B CA   1 
ATOM   6228 C C    . PHE   B 1 116 ? 35.249 -16.377 -5.753  1.00 10.98 ?  116 PHE   B C    1 
ATOM   6229 O O    . PHE   B 1 116 ? 35.679 -15.956 -6.828  1.00 11.24 ?  116 PHE   B O    1 
ATOM   6230 C CB   . PHE   B 1 116 ? 36.128 -18.648 -5.383  1.00 10.71 ?  116 PHE   B CB   1 
ATOM   6231 C CG   . PHE   B 1 116 ? 37.199 -19.602 -4.832  1.00 10.72 ?  116 PHE   B CG   1 
ATOM   6232 C CD1  . PHE   B 1 116 ? 37.845 -19.420 -3.620  1.00 11.62 ?  116 PHE   B CD1  1 
ATOM   6233 C CD2  . PHE   B 1 116 ? 37.499 -20.740 -5.572  1.00 10.99 ?  116 PHE   B CD2  1 
ATOM   6234 C CE1  . PHE   B 1 116 ? 38.779 -20.349 -3.173  1.00 11.51 ?  116 PHE   B CE1  1 
ATOM   6235 C CE2  . PHE   B 1 116 ? 38.428 -21.674 -5.131  1.00 11.05 ?  116 PHE   B CE2  1 
ATOM   6236 C CZ   . PHE   B 1 116 ? 39.065 -21.480 -3.935  1.00 10.98 ?  116 PHE   B CZ   1 
ATOM   6237 H H    . PHE   B 1 116 ? 35.452 -17.869 -3.119  1.00 12.82 ?  116 PHE   B H    1 
ATOM   6238 H HA   . PHE   B 1 116 ? 37.052 -16.867 -4.926  1.00 13.05 ?  116 PHE   B HA   1 
ATOM   6239 H HB2  . PHE   B 1 116 ? 35.258 -19.036 -5.179  1.00 12.91 ?  116 PHE   B HB2  1 
ATOM   6240 H HB3  . PHE   B 1 116 ? 36.240 -18.617 -6.348  1.00 12.91 ?  116 PHE   B HB3  1 
ATOM   6241 H HD1  . PHE   B 1 116 ? 37.650 -18.668 -3.101  1.00 14.00 ?  116 PHE   B HD1  1 
ATOM   6242 H HD2  . PHE   B 1 116 ? 37.063 -20.887 -6.381  1.00 13.25 ?  116 PHE   B HD2  1 
ATOM   6243 H HE1  . PHE   B 1 116 ? 39.216 -20.211 -2.361  1.00 13.87 ?  116 PHE   B HE1  1 
ATOM   6244 H HE2  . PHE   B 1 116 ? 38.619 -22.423 -5.647  1.00 13.32 ?  116 PHE   B HE2  1 
ATOM   6245 H HZ   . PHE   B 1 116 ? 39.700 -22.090 -3.635  1.00 13.24 ?  116 PHE   B HZ   1 
ATOM   6246 N N    . ASN   B 1 117 ? 33.979 -16.183 -5.371  1.00 11.08 ?  117 ASN   B N    1 
ATOM   6247 C CA   . ASN   B 1 117 ? 33.040 -15.480 -6.242  1.00 11.07 ?  117 ASN   B CA   1 
ATOM   6248 C C    . ASN   B 1 117 ? 33.348 -13.998 -6.385  1.00 11.64 ?  117 ASN   B C    1 
ATOM   6249 O O    . ASN   B 1 117 ? 32.750 -13.336 -7.236  1.00 12.72 ?  117 ASN   B O    1 
ATOM   6250 C CB   . ASN   B 1 117 ? 31.607 -15.701 -5.766  1.00 11.40 ?  117 ASN   B CB   1 
ATOM   6251 C CG   . ASN   B 1 117 ? 31.168 -17.113 -5.999  1.00 11.42 ?  117 ASN   B CG   1 
ATOM   6252 O OD1  . ASN   B 1 117 ? 31.528 -17.704 -7.022  1.00 12.37 ?  117 ASN   B OD1  1 
ATOM   6253 N ND2  . ASN   B 1 117 ? 30.432 -17.679 -5.054  1.00 11.47 ?  117 ASN   B ND2  1 
ATOM   6254 H H    . ASN   B 1 117 ? 33.645 -16.447 -4.621  1.00 13.35 ?  117 ASN   B H    1 
ATOM   6255 H HA   . ASN   B 1 117 ? 33.103 -15.869 -7.122  1.00 13.34 ?  117 ASN   B HA   1 
ATOM   6256 H HB2  . ASN   B 1 117 ? 31.547 -15.516 -4.813  1.00 13.73 ?  117 ASN   B HB2  1 
ATOM   6257 H HB3  . ASN   B 1 117 ? 31.010 -15.105 -6.254  1.00 13.73 ?  117 ASN   B HB3  1 
ATOM   6258 H HD21 . ASN   B 1 117 ? 30.164 -18.487 -5.146  1.00 13.82 ?  117 ASN   B HD21 1 
ATOM   6259 H HD22 . ASN   B 1 117 ? 30.212 -17.227 -4.353  1.00 13.82 ?  117 ASN   B HD22 1 
ATOM   6260 N N    . GLN   B 1 118 ? 34.280 -13.474 -5.605  1.00 11.31 ?  118 GLN   B N    1 
ATOM   6261 C CA   . GLN   B 1 118 ? 34.713 -12.088 -5.739  1.00 11.82 ?  118 GLN   B CA   1 
ATOM   6262 C C    . GLN   B 1 118 ? 35.776 -11.892 -6.816  1.00 12.16 ?  118 GLN   B C    1 
ATOM   6263 O O    . GLN   B 1 118 ? 36.255 -10.761 -6.992  1.00 13.49 ?  118 GLN   B O    1 
ATOM   6264 C CB   . GLN   B 1 118 ? 35.199 -11.563 -4.387  1.00 12.34 ?  118 GLN   B CB   1 
ATOM   6265 C CG   . GLN   B 1 118 ? 34.122 -11.596 -3.312  1.00 12.54 ?  118 GLN   B CG   1 
ATOM   6266 C CD   . GLN   B 1 118 ? 32.946 -10.689 -3.642  1.00 12.34 ?  118 GLN   B CD   1 
ATOM   6267 O OE1  . GLN   B 1 118 ? 33.127 -9.545  -4.074  1.00 13.15 ?  118 GLN   B OE1  1 
ATOM   6268 N NE2  . GLN   B 1 118 ? 31.735 -11.183 -3.441  1.00 12.64 ?  118 GLN   B NE2  1 
ATOM   6269 H H    . GLN   B 1 118 ? 34.688 -13.901 -4.978  1.00 13.63 ?  118 GLN   B H    1 
ATOM   6270 H HA   . GLN   B 1 118 ? 33.944 -11.551 -5.996  1.00 14.24 ?  118 GLN   B HA   1 
ATOM   6271 H HB2  . GLN   B 1 118 ? 35.939 -12.109 -4.081  1.00 14.87 ?  118 GLN   B HB2  1 
ATOM   6272 H HB3  . GLN   B 1 118 ? 35.487 -10.641 -4.486  1.00 14.87 ?  118 GLN   B HB3  1 
ATOM   6273 H HG2  . GLN   B 1 118 ? 33.786 -12.503 -3.227  1.00 15.11 ?  118 GLN   B HG2  1 
ATOM   6274 H HG3  . GLN   B 1 118 ? 34.501 -11.302 -2.470  1.00 15.11 ?  118 GLN   B HG3  1 
ATOM   6275 H HE21 . GLN   B 1 118 ? 31.648 -11.984 -3.140  1.00 15.22 ?  118 GLN   B HE21 1 
ATOM   6276 H HE22 . GLN   B 1 118 ? 31.049 -10.708 -3.622  1.00 15.22 ?  118 GLN   B HE22 1 
ATOM   6277 N N    . HIS   B 1 119 ? 36.135 -12.953 -7.548  1.00 11.49 ?  119 HIS   B N    1 
ATOM   6278 C CA   . HIS   B 1 119 ? 37.177 -12.904 -8.567  1.00 11.85 ?  119 HIS   B CA   1 
ATOM   6279 C C    . HIS   B 1 119 ? 36.690 -13.637 -9.802  1.00 12.09 ?  119 HIS   B C    1 
ATOM   6280 O O    . HIS   B 1 119 ? 36.172 -14.747 -9.692  1.00 12.69 ?  119 HIS   B O    1 
ATOM   6281 C CB   . HIS   B 1 119 ? 38.454 -13.538 -8.016  1.00 12.58 ?  119 HIS   B CB   1 
ATOM   6282 C CG   . HIS   B 1 119 ? 38.950 -12.829 -6.803  1.00 13.98 ?  119 HIS   B CG   1 
ATOM   6283 N ND1  . HIS   B 1 119 ? 39.742 -11.703 -6.879  1.00 15.32 ?  119 HIS   B ND1  1 
ATOM   6284 C CD2  . HIS   B 1 119 ? 38.667 -13.006 -5.493  1.00 15.20 ?  119 HIS   B CD2  1 
ATOM   6285 C CE1  . HIS   B 1 119 ? 39.966 -11.250 -5.661  1.00 16.28 ?  119 HIS   B CE1  1 
ATOM   6286 N NE2  . HIS   B 1 119 ? 39.317 -12.015 -4.802  1.00 16.21 ?  119 HIS   B NE2  1 
ATOM   6287 H H    . HIS   B 1 119 ? 35.771 -13.730 -7.467  1.00 13.84 ?  119 HIS   B H    1 
ATOM   6288 H HA   . HIS   B 1 119 ? 37.362 -11.981 -8.800  1.00 14.28 ?  119 HIS   B HA   1 
ATOM   6289 H HB2  . HIS   B 1 119 ? 38.275 -14.462 -7.778  1.00 15.15 ?  119 HIS   B HB2  1 
ATOM   6290 H HB3  . HIS   B 1 119 ? 39.146 -13.499 -8.697  1.00 15.15 ?  119 HIS   B HB3  1 
ATOM   6291 H HD2  . HIS   B 1 119 ? 38.138 -13.678 -5.129  1.00 18.29 ?  119 HIS   B HD2  1 
ATOM   6292 H HE1  . HIS   B 1 119 ? 40.507 -10.526 -5.442  1.00 19.59 ?  119 HIS   B HE1  1 
ATOM   6293 H HE2  . HIS   B 1 119 ? 39.333 -11.928 -3.946  1.00 19.51 ?  119 HIS   B HE2  1 
ATOM   6294 N N    A GLU   B 1 120 ? 36.858 -13.026 -10.975 0.40 12.66 ?  120 GLU   B N    1 
ATOM   6295 N N    B GLU   B 1 120 ? 36.862 -13.030 -10.977 0.60 12.28 ?  120 GLU   B N    1 
ATOM   6296 C CA   A GLU   B 1 120 ? 36.267 -13.603 -12.179 0.40 13.78 ?  120 GLU   B CA   1 
ATOM   6297 C CA   B GLU   B 1 120 ? 36.263 -13.609 -12.176 0.60 13.25 ?  120 GLU   B CA   1 
ATOM   6298 C C    A GLU   B 1 120 ? 36.943 -14.905 -12.591 0.40 12.76 ?  120 GLU   B C    1 
ATOM   6299 C C    B GLU   B 1 120 ? 36.942 -14.906 -12.596 0.60 12.49 ?  120 GLU   B C    1 
ATOM   6300 O O    A GLU   B 1 120 ? 36.283 -15.787 -13.155 0.40 12.76 ?  120 GLU   B O    1 
ATOM   6301 O O    B GLU   B 1 120 ? 36.285 -15.786 -13.169 0.60 12.76 ?  120 GLU   B O    1 
ATOM   6302 C CB   A GLU   B 1 120 ? 36.292 -12.589 -13.320 0.40 16.70 ?  120 GLU   B CB   1 
ATOM   6303 C CB   B GLU   B 1 120 ? 36.262 -12.595 -13.318 0.60 16.15 ?  120 GLU   B CB   1 
ATOM   6304 C CG   A GLU   B 1 120 ? 35.317 -11.444 -13.127 0.40 20.16 ?  120 GLU   B CG   1 
ATOM   6305 C CG   B GLU   B 1 120 ? 35.323 -11.425 -13.069 0.60 20.15 ?  120 GLU   B CG   1 
ATOM   6306 C CD   A GLU   B 1 120 ? 35.249 -10.546 -14.342 0.40 23.27 ?  120 GLU   B CD   1 
ATOM   6307 C CD   B GLU   B 1 120 ? 34.965 -10.654 -14.322 0.60 23.84 ?  120 GLU   B CD   1 
ATOM   6308 O OE1  A GLU   B 1 120 ? 36.262 -10.487 -15.072 0.40 24.48 ?  120 GLU   B OE1  1 
ATOM   6309 O OE1  B GLU   B 1 120 ? 35.869 -10.089 -14.973 0.60 25.76 ?  120 GLU   B OE1  1 
ATOM   6310 O OE2  A GLU   B 1 120 ? 34.199 -9.905  -14.568 0.40 24.63 -1 120 GLU   B OE2  1 
ATOM   6311 O OE2  B GLU   B 1 120 ? 33.761 -10.615 -14.650 0.60 25.51 -1 120 GLU   B OE2  1 
ATOM   6312 H H    A GLU   B 1 120 ? 37.296 -12.295 -11.096 0.40 15.25 ?  120 GLU   B H    1 
ATOM   6313 H H    B GLU   B 1 120 ? 37.306 -12.304 -11.102 0.60 14.79 ?  120 GLU   B H    1 
ATOM   6314 H HA   A GLU   B 1 120 ? 35.341 -13.808 -11.995 0.40 16.59 ?  120 GLU   B HA   1 
ATOM   6315 H HA   B GLU   B 1 120 ? 35.341 -13.824 -11.977 0.60 15.95 ?  120 GLU   B HA   1 
ATOM   6316 H HB2  A GLU   B 1 120 ? 37.181 -12.209 -13.392 0.40 20.10 ?  120 GLU   B HB2  1 
ATOM   6317 H HB2  B GLU   B 1 120 ? 37.156 -12.240 -13.427 0.60 19.44 ?  120 GLU   B HB2  1 
ATOM   6318 H HB3  A GLU   B 1 120 ? 36.058 -13.039 -14.149 0.40 20.10 ?  120 GLU   B HB3  1 
ATOM   6319 H HB3  B GLU   B 1 120 ? 35.977 -13.038 -14.131 0.60 19.44 ?  120 GLU   B HB3  1 
ATOM   6320 H HG2  A GLU   B 1 120 ? 34.434 -11.808 -12.938 0.40 24.25 ?  120 GLU   B HG2  1 
ATOM   6321 H HG2  B GLU   B 1 120 ? 34.485 -11.761 -12.716 0.60 24.24 ?  120 GLU   B HG2  1 
ATOM   6322 H HG3  A GLU   B 1 120 ? 35.611 -10.897 -12.383 0.40 24.25 ?  120 GLU   B HG3  1 
ATOM   6323 H HG3  B GLU   B 1 120 ? 35.734 -10.820 -12.433 0.60 24.24 ?  120 GLU   B HG3  1 
ATOM   6324 N N    . VAL   B 1 121 ? 38.240 -15.046 -12.326 1.00 12.30 ?  121 VAL   B N    1 
ATOM   6325 C CA   . VAL   B 1 121 ? 38.986 -16.254 -12.673 1.00 12.27 ?  121 VAL   B CA   1 
ATOM   6326 C C    . VAL   B 1 121 ? 40.098 -16.456 -11.650 1.00 11.96 ?  121 VAL   B C    1 
ATOM   6327 O O    . VAL   B 1 121 ? 40.774 -15.500 -11.255 1.00 12.61 ?  121 VAL   B O    1 
ATOM   6328 C CB   . VAL   B 1 121 ? 39.500 -16.207 -14.131 1.00 13.92 ?  121 VAL   B CB   1 
ATOM   6329 C CG1  . VAL   B 1 121 ? 40.365 -14.980 -14.382 1.00 15.31 ?  121 VAL   B CG1  1 
ATOM   6330 C CG2  . VAL   B 1 121 ? 40.236 -17.487 -14.489 1.00 15.39 ?  121 VAL   B CG2  1 
ATOM   6331 H H    A VAL   B 1 121 ? 38.721 -14.445 -11.938 0.40 14.82 ?  121 VAL   B H    1 
ATOM   6332 H H    B VAL   B 1 121 ? 38.720 -14.444 -11.937 0.60 14.82 ?  121 VAL   B H    1 
ATOM   6333 H HA   . VAL   B 1 121 ? 38.379 -17.007 -12.606 1.00 14.78 ?  121 VAL   B HA   1 
ATOM   6334 H HB   . VAL   B 1 121 ? 38.731 -16.141 -14.722 1.00 16.77 ?  121 VAL   B HB   1 
ATOM   6335 H HG11 . VAL   B 1 121 ? 40.671 -14.993 -15.302 1.00 18.43 ?  121 VAL   B HG11 1 
ATOM   6336 H HG12 . VAL   B 1 121 ? 39.836 -14.180 -14.223 1.00 18.43 ?  121 VAL   B HG12 1 
ATOM   6337 H HG13 . VAL   B 1 121 ? 41.124 -14.998 -13.779 1.00 18.43 ?  121 VAL   B HG13 1 
ATOM   6338 H HG21 . VAL   B 1 121 ? 40.441 -17.475 -15.437 1.00 18.52 ?  121 VAL   B HG21 1 
ATOM   6339 H HG22 . VAL   B 1 121 ? 41.058 -17.532 -13.975 1.00 18.52 ?  121 VAL   B HG22 1 
ATOM   6340 H HG23 . VAL   B 1 121 ? 39.671 -18.245 -14.281 1.00 18.52 ?  121 VAL   B HG23 1 
ATOM   6341 N N    . LEU   B 1 122 ? 40.284 -17.713 -11.223 1.00 11.41 ?  122 LEU   B N    1 
ATOM   6342 C CA   . LEU   B 1 122 ? 41.259 -18.068 -10.196 1.00 11.12 ?  122 LEU   B CA   1 
ATOM   6343 C C    . LEU   B 1 122 ? 41.920 -19.394 -10.529 1.00 11.12 ?  122 LEU   B C    1 
ATOM   6344 O O    . LEU   B 1 122 ? 41.266 -20.315 -11.039 1.00 12.06 ?  122 LEU   B O    1 
ATOM   6345 C CB   . LEU   B 1 122 ? 40.596 -18.301 -8.828  1.00 12.49 ?  122 LEU   B CB   1 
ATOM   6346 C CG   . LEU   B 1 122 ? 39.579 -17.270 -8.331  1.00 13.11 ?  122 LEU   B CG   1 
ATOM   6347 C CD1  . LEU   B 1 122 ? 38.165 -17.603 -8.797  1.00 14.02 ?  122 LEU   B CD1  1 
ATOM   6348 C CD2  . LEU   B 1 122 ? 39.643 -17.166 -6.822  1.00 13.15 ?  122 LEU   B CD2  1 
ATOM   6349 H H    . LEU   B 1 122 ? 39.847 -18.389 -11.524 1.00 13.75 ?  122 LEU   B H    1 
ATOM   6350 H HA   . LEU   B 1 122 ? 41.932 -17.372 -10.110 1.00 13.40 ?  122 LEU   B HA   1 
ATOM   6351 H HB2  . LEU   B 1 122 ? 40.134 -19.148 -8.861  1.00 15.05 ?  122 LEU   B HB2  1 
ATOM   6352 H HB3  . LEU   B 1 122 ? 41.297 -18.343 -8.160  1.00 15.05 ?  122 LEU   B HB3  1 
ATOM   6353 H HG   . LEU   B 1 122 ? 39.815 -16.399 -8.691  1.00 15.79 ?  122 LEU   B HG   1 
ATOM   6354 H HD11 . LEU   B 1 122 ? 37.553 -16.941 -8.440  1.00 16.88 ?  122 LEU   B HD11 1 
ATOM   6355 H HD12 . LEU   B 1 122 ? 38.143 -17.584 -9.766  1.00 16.88 ?  122 LEU   B HD12 1 
ATOM   6356 H HD13 . LEU   B 1 122 ? 37.928 -18.484 -8.475  1.00 16.88 ?  122 LEU   B HD13 1 
ATOM   6357 H HD21 . LEU   B 1 122 ? 38.971 -16.538 -6.516  1.00 15.84 ?  122 LEU   B HD21 1 
ATOM   6358 H HD22 . LEU   B 1 122 ? 39.480 -18.041 -6.436  1.00 15.84 ?  122 LEU   B HD22 1 
ATOM   6359 H HD23 . LEU   B 1 122 ? 40.527 -16.852 -6.561  1.00 15.84 ?  122 LEU   B HD23 1 
ATOM   6360 N N    . LEU   B 1 123 ? 43.208 -19.492 -10.178 1.00 10.91 ?  123 LEU   B N    1 
ATOM   6361 C CA   . LEU   B 1 123 ? 43.925 -20.760 -10.057 1.00 11.02 ?  123 LEU   B CA   1 
ATOM   6362 C C    . LEU   B 1 123 ? 43.896 -21.156 -8.586  1.00 10.60 ?  123 LEU   B C    1 
ATOM   6363 O O    . LEU   B 1 123 ? 44.258 -20.334 -7.735  1.00 11.16 ?  123 LEU   B O    1 
ATOM   6364 C CB   . LEU   B 1 123 ? 45.374 -20.576 -10.513 1.00 11.57 ?  123 LEU   B CB   1 
ATOM   6365 C CG   . LEU   B 1 123 ? 46.315 -21.753 -10.265 1.00 11.74 ?  123 LEU   B CG   1 
ATOM   6366 C CD1  . LEU   B 1 123 ? 45.905 -22.997 -11.056 1.00 12.42 ?  123 LEU   B CD1  1 
ATOM   6367 C CD2  . LEU   B 1 123 ? 47.736 -21.349 -10.609 1.00 12.62 ?  123 LEU   B CD2  1 
ATOM   6368 H H    . LEU   B 1 123 ? 43.706 -18.810 -9.988  1.00 13.15 ?  123 LEU   B H    1 
ATOM   6369 H HA   . LEU   B 1 123 ? 43.492 -21.446 -10.591 1.00 13.28 ?  123 LEU   B HA   1 
ATOM   6370 H HB2  . LEU   B 1 123 ? 45.369 -20.405 -11.468 1.00 13.94 ?  123 LEU   B HB2  1 
ATOM   6371 H HB3  . LEU   B 1 123 ? 45.741 -19.810 -10.049 1.00 13.94 ?  123 LEU   B HB3  1 
ATOM   6372 H HG   . LEU   B 1 123 ? 46.298 -21.988 -9.324  1.00 14.15 ?  123 LEU   B HG   1 
ATOM   6373 H HD11 . LEU   B 1 123 ? 46.536 -23.710 -10.881 1.00 14.96 ?  123 LEU   B HD11 1 
ATOM   6374 H HD12 . LEU   B 1 123 ? 45.013 -23.269 -10.777 1.00 14.96 ?  123 LEU   B HD12 1 
ATOM   6375 H HD13 . LEU   B 1 123 ? 45.899 -22.782 -12.003 1.00 14.96 ?  123 LEU   B HD13 1 
ATOM   6376 H HD21 . LEU   B 1 123 ? 48.329 -22.101 -10.453 1.00 15.20 ?  123 LEU   B HD21 1 
ATOM   6377 H HD22 . LEU   B 1 123 ? 47.773 -21.086 -11.542 1.00 15.20 ?  123 LEU   B HD22 1 
ATOM   6378 H HD23 . LEU   B 1 123 ? 47.995 -20.602 -10.046 1.00 15.20 ?  123 LEU   B HD23 1 
ATOM   6379 N N    . ALA   B 1 124 ? 43.471 -22.388 -8.276  1.00 10.92 ?  124 ALA   B N    1 
ATOM   6380 C CA   . ALA   B 1 124 ? 43.202 -22.708 -6.882  1.00 11.05 ?  124 ALA   B CA   1 
ATOM   6381 C C    . ALA   B 1 124 ? 43.486 -24.170 -6.565  1.00 10.63 ?  124 ALA   B C    1 
ATOM   6382 O O    . ALA   B 1 124 ? 43.346 -25.051 -7.431  1.00 10.93 ?  124 ALA   B O    1 
ATOM   6383 C CB   . ALA   B 1 124 ? 41.743 -22.414 -6.527  1.00 11.46 ?  124 ALA   B CB   1 
ATOM   6384 H H    . ALA   B 1 124 ? 43.320 -23.032 -8.837  1.00 13.17 ?  124 ALA   B H    1 
ATOM   6385 H HA   . ALA   B 1 124 ? 43.762 -22.147 -6.331  1.00 13.32 ?  124 ALA   B HA   1 
ATOM   6386 H HB1  . ALA   B 1 124 ? 41.587 -22.633 -5.595  1.00 13.81 ?  124 ALA   B HB1  1 
ATOM   6387 H HB2  . ALA   B 1 124 ? 41.558 -21.473 -6.680  1.00 13.81 ?  124 ALA   B HB2  1 
ATOM   6388 H HB3  . ALA   B 1 124 ? 41.160 -22.955 -7.091  1.00 13.81 ?  124 ALA   B HB3  1 
ATOM   6389 N N    . PRO   B 1 125 ? 43.768 -24.465 -5.300  1.00 10.78 ?  125 PRO   B N    1 
ATOM   6390 C CA   . PRO   B 1 125 ? 43.712 -25.833 -4.786  1.00 11.60 ?  125 PRO   B CA   1 
ATOM   6391 C C    . PRO   B 1 125 ? 42.314 -26.107 -4.234  1.00 11.53 ?  125 PRO   B C    1 
ATOM   6392 O O    . PRO   B 1 125 ? 41.511 -25.193 -4.037  1.00 12.11 ?  125 PRO   B O    1 
ATOM   6393 C CB   . PRO   B 1 125 ? 44.706 -25.756 -3.623  1.00 12.53 ?  125 PRO   B CB   1 
ATOM   6394 C CG   . PRO   B 1 125 ? 44.435 -24.371 -3.042  1.00 12.62 ?  125 PRO   B CG   1 
ATOM   6395 C CD   . PRO   B 1 125 ? 44.090 -23.496 -4.234  1.00 11.35 ?  125 PRO   B CD   1 
ATOM   6396 H HA   . PRO   B 1 125 ? 43.983 -26.494 -5.442  1.00 13.98 ?  125 PRO   B HA   1 
ATOM   6397 H HB2  . PRO   B 1 125 ? 44.516 -26.450 -2.969  1.00 15.10 ?  125 PRO   B HB2  1 
ATOM   6398 H HB3  . PRO   B 1 125 ? 45.616 -25.823 -3.949  1.00 15.10 ?  125 PRO   B HB3  1 
ATOM   6399 H HG2  . PRO   B 1 125 ? 43.687 -24.414 -2.421  1.00 15.20 ?  125 PRO   B HG2  1 
ATOM   6400 H HG3  . PRO   B 1 125 ? 45.230 -24.042 -2.588  1.00 15.20 ?  125 PRO   B HG3  1 
ATOM   6401 H HD2  . PRO   B 1 125 ? 43.323 -22.934 -4.037  1.00 13.67 ?  125 PRO   B HD2  1 
ATOM   6402 H HD3  . PRO   B 1 125 ? 44.861 -22.956 -4.491  1.00 13.67 ?  125 PRO   B HD3  1 
ATOM   6403 N N    . LEU   B 1 126 ? 42.043 -27.389 -3.958  1.00 11.82 ?  126 LEU   B N    1 
ATOM   6404 C CA   . LEU   B 1 126 ? 40.819 -27.762 -3.257  1.00 12.02 ?  126 LEU   B CA   1 
ATOM   6405 C C    . LEU   B 1 126 ? 40.926 -27.361 -1.794  1.00 11.88 ?  126 LEU   B C    1 
ATOM   6406 O O    . LEU   B 1 126 ? 41.826 -27.808 -1.076  1.00 13.50 ?  126 LEU   B O    1 
ATOM   6407 C CB   . LEU   B 1 126 ? 40.572 -29.260 -3.383  1.00 13.33 ?  126 LEU   B CB   1 
ATOM   6408 C CG   . LEU   B 1 126 ? 40.037 -29.728 -4.735  1.00 14.30 ?  126 LEU   B CG   1 
ATOM   6409 C CD1  . LEU   B 1 126 ? 40.087 -31.241 -4.823  1.00 15.80 ?  126 LEU   B CD1  1 
ATOM   6410 C CD2  . LEU   B 1 126 ? 38.611 -29.228 -4.970  1.00 14.39 ?  126 LEU   B CD2  1 
ATOM   6411 H H    . LEU   B 1 126 ? 42.553 -28.051 -4.157  1.00 14.24 ?  126 LEU   B H    1 
ATOM   6412 H HA   . LEU   B 1 126 ? 40.070 -27.286 -3.650  1.00 14.49 ?  126 LEU   B HA   1 
ATOM   6413 H HB2  . LEU   B 1 126 ? 41.407 -29.721 -3.225  1.00 16.05 ?  126 LEU   B HB2  1 
ATOM   6414 H HB3  . LEU   B 1 126 ? 39.923 -29.518 -2.710  1.00 16.05 ?  126 LEU   B HB3  1 
ATOM   6415 H HG   . LEU   B 1 126 ? 40.599 -29.369 -5.441  1.00 17.22 ?  126 LEU   B HG   1 
ATOM   6416 H HD11 . LEU   B 1 126 ? 39.742 -31.518 -5.685  1.00 19.02 ?  126 LEU   B HD11 1 
ATOM   6417 H HD12 . LEU   B 1 126 ? 41.006 -31.530 -4.722  1.00 19.02 ?  126 LEU   B HD12 1 
ATOM   6418 H HD13 . LEU   B 1 126 ? 39.541 -31.613 -4.112  1.00 19.02 ?  126 LEU   B HD13 1 
ATOM   6419 H HD21 . LEU   B 1 126 ? 38.259 -29.641 -5.773  1.00 17.32 ?  126 LEU   B HD21 1 
ATOM   6420 H HD22 . LEU   B 1 126 ? 38.065 -29.463 -4.206  1.00 17.32 ?  126 LEU   B HD22 1 
ATOM   6421 H HD23 . LEU   B 1 126 ? 38.629 -28.261 -5.079  1.00 17.32 ?  126 LEU   B HD23 1 
ATOM   6422 N N    . LEU   B 1 127 ? 39.996 -26.530 -1.341  1.00 11.84 ?  127 LEU   B N    1 
ATOM   6423 C CA   . LEU   B 1 127 ? 40.051 -26.042 0.024   1.00 12.04 ?  127 LEU   B CA   1 
ATOM   6424 C C    . LEU   B 1 127 ? 39.787 -27.162 1.020   1.00 11.72 ?  127 LEU   B C    1 
ATOM   6425 O O    . LEU   B 1 127 ? 38.968 -28.058 0.794   1.00 12.51 ?  127 LEU   B O    1 
ATOM   6426 C CB   . LEU   B 1 127 ? 39.026 -24.928 0.228   1.00 12.53 ?  127 LEU   B CB   1 
ATOM   6427 C CG   . LEU   B 1 127 ? 39.212 -23.644 -0.591  1.00 13.01 ?  127 LEU   B CG   1 
ATOM   6428 C CD1  . LEU   B 1 127 ? 38.088 -22.675 -0.273  1.00 13.12 ?  127 LEU   B CD1  1 
ATOM   6429 C CD2  . LEU   B 1 127 ? 40.579 -23.001 -0.350  1.00 13.87 ?  127 LEU   B CD2  1 
ATOM   6430 H H    . LEU   B 1 127 ? 39.326 -26.230 -1.802  1.00 14.27 ?  127 LEU   B H    1 
ATOM   6431 H HA   . LEU   B 1 127 ? 40.929 -25.673 0.197   1.00 14.51 ?  127 LEU   B HA   1 
ATOM   6432 H HB2  . LEU   B 1 127 ? 38.143 -25.277 0.010   1.00 15.10 ?  127 LEU   B HB2  1 
ATOM   6433 H HB3  . LEU   B 1 127 ? 39.035 -24.667 1.165   1.00 15.10 ?  127 LEU   B HB3  1 
ATOM   6434 H HG   . LEU   B 1 127 ? 39.140 -23.862 -1.531  1.00 15.67 ?  127 LEU   B HG   1 
ATOM   6435 H HD11 . LEU   B 1 127 ? 38.211 -21.863 -0.790  1.00 15.81 ?  127 LEU   B HD11 1 
ATOM   6436 H HD12 . LEU   B 1 127 ? 37.236 -23.083 -0.497  1.00 15.81 ?  127 LEU   B HD12 1 
ATOM   6437 H HD13 . LEU   B 1 127 ? 38.109 -22.464 0.677   1.00 15.81 ?  127 LEU   B HD13 1 
ATOM   6438 H HD21 . LEU   B 1 127 ? 40.612 -22.147 -0.808  1.00 16.70 ?  127 LEU   B HD21 1 
ATOM   6439 H HD22 . LEU   B 1 127 ? 40.702 -22.870 0.604   1.00 16.70 ?  127 LEU   B HD22 1 
ATOM   6440 H HD23 . LEU   B 1 127 ? 41.265 -23.591 -0.695  1.00 16.70 ?  127 LEU   B HD23 1 
ATOM   6441 N N    . SER   B 1 128 ? 40.475 -27.082 2.150   1.00 11.95 ?  128 SER   B N    1 
ATOM   6442 C CA   . SER   B 1 128 ? 40.364 -27.999 3.275   1.00 12.56 ?  128 SER   B CA   1 
ATOM   6443 C C    . SER   B 1 128 ? 40.862 -29.405 2.950   1.00 13.15 ?  128 SER   B C    1 
ATOM   6444 O O    . SER   B 1 128 ? 40.779 -30.286 3.810   1.00 14.35 ?  128 SER   B O    1 
ATOM   6445 C CB   . SER   B 1 128 ? 38.965 -28.020 3.911   1.00 13.09 ?  128 SER   B CB   1 
ATOM   6446 O OG   . SER   B 1 128 ? 38.646 -26.743 4.459   1.00 13.79 ?  128 SER   B OG   1 
ATOM   6447 H H    . SER   B 1 128 ? 41.051 -26.456 2.295   1.00 14.40 ?  128 SER   B H    1 
ATOM   6448 H HA   . SER   B 1 128 ? 40.951 -27.661 3.959   1.00 15.13 ?  128 SER   B HA   1 
ATOM   6449 H HB2  . SER   B 1 128 ? 38.304 -28.250 3.240   1.00 15.76 ?  128 SER   B HB2  1 
ATOM   6450 H HB3  . SER   B 1 128 ? 38.951 -28.687 4.625   1.00 15.76 ?  128 SER   B HB3  1 
ATOM   6451 H HG   . SER   B 1 128 ? 39.214 -26.542 5.051   1.00 16.60 ?  128 SER   B HG   1 
ATOM   6452 N N    . ALA   B 1 129 ? 41.420 -29.628 1.763   1.00 13.77 ?  129 ALA   B N    1 
ATOM   6453 C CA   . ALA   B 1 129 ? 41.967 -30.924 1.399   1.00 14.73 ?  129 ALA   B CA   1 
ATOM   6454 C C    . ALA   B 1 129 ? 43.354 -31.109 2.004   1.00 13.88 ?  129 ALA   B C    1 
ATOM   6455 O O    . ALA   B 1 129 ? 43.921 -30.211 2.638   1.00 13.96 ?  129 ALA   B O    1 
ATOM   6456 C CB   . ALA   B 1 129 ? 42.031 -31.070 -0.119  1.00 16.62 ?  129 ALA   B CB   1 
ATOM   6457 H H    . ALA   B 1 129 ? 41.492 -29.036 1.143   1.00 16.58 ?  129 ALA   B H    1 
ATOM   6458 H HA   . ALA   B 1 129 ? 41.386 -31.620 1.746   1.00 17.73 ?  129 ALA   B HA   1 
ATOM   6459 H HB1  . ALA   B 1 129 ? 42.390 -31.945 -0.337  1.00 20.01 ?  129 ALA   B HB1  1 
ATOM   6460 H HB2  . ALA   B 1 129 ? 41.138 -30.978 -0.484  1.00 20.01 ?  129 ALA   B HB2  1 
ATOM   6461 H HB3  . ALA   B 1 129 ? 42.608 -30.377 -0.478  1.00 20.01 ?  129 ALA   B HB3  1 
ATOM   6462 N N    . GLY   B 1 130 ? 43.908 -32.303 1.793   1.00 14.32 ?  130 GLY   B N    1 
ATOM   6463 C CA   . GLY   B 1 130 ? 45.295 -32.548 2.150   1.00 14.77 ?  130 GLY   B CA   1 
ATOM   6464 C C    . GLY   B 1 130 ? 45.504 -32.441 3.642   1.00 14.52 ?  130 GLY   B C    1 
ATOM   6465 O O    . GLY   B 1 130 ? 44.806 -33.079 4.445   1.00 15.53 ?  130 GLY   B O    1 
ATOM   6466 H H    . GLY   B 1 130 ? 43.506 -32.978 1.441   1.00 17.24 ?  130 GLY   B H    1 
ATOM   6467 H HA2  . GLY   B 1 130 ? 45.555 -33.440 1.863   1.00 17.78 ?  130 GLY   B HA2  1 
ATOM   6468 H HA3  . GLY   B 1 130 ? 45.868 -31.904 1.706   1.00 17.78 ?  130 GLY   B HA3  1 
ATOM   6469 N N    . ILE   B 1 131 ? 46.474 -31.603 4.028   1.00 15.00 ?  131 ILE   B N    1 
ATOM   6470 C CA   . ILE   B 1 131 ? 46.828 -31.463 5.434   1.00 15.80 ?  131 ILE   B CA   1 
ATOM   6471 C C    . ILE   B 1 131 ? 45.709 -30.854 6.264   1.00 15.06 ?  131 ILE   B C    1 
ATOM   6472 O O    . ILE   B 1 131 ? 45.781 -30.905 7.495   1.00 16.38 ?  131 ILE   B O    1 
ATOM   6473 C CB   . ILE   B 1 131 ? 48.149 -30.684 5.627   1.00 17.13 ?  131 ILE   B CB   1 
ATOM   6474 C CG1  . ILE   B 1 131 ? 47.994 -29.215 5.202   1.00 18.19 ?  131 ILE   B CG1  1 
ATOM   6475 C CG2  . ILE   B 1 131 ? 49.288 -31.361 4.861   1.00 17.98 ?  131 ILE   B CG2  1 
ATOM   6476 C CD1  . ILE   B 1 131 ? 49.203 -28.344 5.531   1.00 19.54 ?  131 ILE   B CD1  1 
ATOM   6477 H H    . ILE   B 1 131 ? 46.939 -31.108 3.496   1.00 18.06 ?  131 ILE   B H    1 
ATOM   6478 H HA   . ILE   B 1 131 ? 46.978 -32.350 5.788   1.00 19.01 ?  131 ILE   B HA   1 
ATOM   6479 H HB   . ILE   B 1 131 ? 48.371 -30.699 6.572   1.00 20.61 ?  131 ILE   B HB   1 
ATOM   6480 H HG12 . ILE   B 1 131 ? 47.854 -29.183 4.243   1.00 21.88 ?  131 ILE   B HG12 1 
ATOM   6481 H HG13 . ILE   B 1 131 ? 47.226 -28.830 5.657   1.00 21.88 ?  131 ILE   B HG13 1 
ATOM   6482 H HG21 . ILE   B 1 131 ? 50.127 -30.946 5.114   1.00 21.64 ?  131 ILE   B HG21 1 
ATOM   6483 H HG22 . ILE   B 1 131 ? 49.299 -32.301 5.087   1.00 21.64 ?  131 ILE   B HG22 1 
ATOM   6484 H HG23 . ILE   B 1 131 ? 49.134 -31.248 3.910   1.00 21.64 ?  131 ILE   B HG23 1 
ATOM   6485 H HD11 . ILE   B 1 131 ? 48.994 -27.423 5.308   1.00 23.50 ?  131 ILE   B HD11 1 
ATOM   6486 H HD12 . ILE   B 1 131 ? 49.395 -28.420 6.478   1.00 23.50 ?  131 ILE   B HD12 1 
ATOM   6487 H HD13 . ILE   B 1 131 ? 49.960 -28.648 5.011   1.00 23.50 ?  131 ILE   B HD13 1 
ATOM   6488 N N    . PHE   B 1 132 ? 44.683 -30.283 5.628   1.00 13.68 ?  132 PHE   B N    1 
ATOM   6489 C CA   . PHE   B 1 132 ? 43.524 -29.777 6.357   1.00 14.00 ?  132 PHE   B CA   1 
ATOM   6490 C C    . PHE   B 1 132 ? 42.498 -30.866 6.675   1.00 15.00 ?  132 PHE   B C    1 
ATOM   6491 O O    . PHE   B 1 132 ? 41.587 -30.621 7.474   1.00 16.97 ?  132 PHE   B O    1 
ATOM   6492 C CB   . PHE   B 1 132 ? 42.856 -28.638 5.570   1.00 13.56 ?  132 PHE   B CB   1 
ATOM   6493 C CG   . PHE   B 1 132 ? 43.554 -27.297 5.694   1.00 13.90 ?  132 PHE   B CG   1 
ATOM   6494 C CD1  . PHE   B 1 132 ? 44.853 -27.113 5.234   1.00 15.20 ?  132 PHE   B CD1  1 
ATOM   6495 C CD2  . PHE   B 1 132 ? 42.874 -26.203 6.223   1.00 13.42 ?  132 PHE   B CD2  1 
ATOM   6496 C CE1  . PHE   B 1 132 ? 45.474 -25.873 5.339   1.00 16.09 ?  132 PHE   B CE1  1 
ATOM   6497 C CE2  . PHE   B 1 132 ? 43.488 -24.961 6.326   1.00 13.83 ?  132 PHE   B CE2  1 
ATOM   6498 C CZ   . PHE   B 1 132 ? 44.788 -24.799 5.883   1.00 15.19 ?  132 PHE   B CZ   1 
ATOM   6499 H H    . PHE   B 1 132 ? 44.640 -30.168 4.774   1.00 16.47 ?  132 PHE   B H    1 
ATOM   6500 H HA   . PHE   B 1 132 ? 43.833 -29.400 7.196   1.00 16.85 ?  132 PHE   B HA   1 
ATOM   6501 H HB2  . PHE   B 1 132 ? 42.849 -28.877 4.632   1.00 16.33 ?  132 PHE   B HB2  1 
ATOM   6502 H HB3  . PHE   B 1 132 ? 41.947 -28.532 5.891   1.00 16.33 ?  132 PHE   B HB3  1 
ATOM   6503 H HD1  . PHE   B 1 132 ? 45.316 -27.837 4.877   1.00 18.29 ?  132 PHE   B HD1  1 
ATOM   6504 H HD2  . PHE   B 1 132 ? 41.996 -26.311 6.521   1.00 16.16 ?  132 PHE   B HD2  1 
ATOM   6505 H HE1  . PHE   B 1 132 ? 46.348 -25.766 5.043   1.00 19.37 ?  132 PHE   B HE1  1 
ATOM   6506 H HE2  . PHE   B 1 132 ? 43.020 -24.241 6.690   1.00 16.65 ?  132 PHE   B HE2  1 
ATOM   6507 H HZ   . PHE   B 1 132 ? 45.198 -23.964 5.954   1.00 18.28 ?  132 PHE   B HZ   1 
ATOM   6508 N N    . GLY   B 1 133 ? 42.608 -32.056 6.075   1.00 14.46 ?  133 GLY   B N    1 
ATOM   6509 C CA   . GLY   B 1 133 ? 41.899 -33.226 6.565   1.00 15.13 ?  133 GLY   B CA   1 
ATOM   6510 C C    . GLY   B 1 133 ? 40.502 -33.487 6.035   1.00 15.68 ?  133 GLY   B C    1 
ATOM   6511 O O    . GLY   B 1 133 ? 39.909 -34.501 6.414   1.00 17.57 ?  133 GLY   B O    1 
ATOM   6512 H H    . GLY   B 1 133 ? 43.096 -32.202 5.381   1.00 17.41 ?  133 GLY   B H    1 
ATOM   6513 H HA2  . GLY   B 1 133 ? 42.437 -34.007 6.366   1.00 18.21 ?  133 GLY   B HA2  1 
ATOM   6514 H HA3  . GLY   B 1 133 ? 41.836 -33.155 7.531   1.00 18.21 ?  133 GLY   B HA3  1 
ATOM   6515 N N    . ALA   B 1 134 ? 39.947 -32.627 5.191   1.00 14.81 ?  134 ALA   B N    1 
ATOM   6516 C CA   . ALA   B 1 134 ? 38.619 -32.892 4.658   1.00 14.94 ?  134 ALA   B CA   1 
ATOM   6517 C C    . ALA   B 1 134 ? 38.695 -33.891 3.507   1.00 14.78 ?  134 ALA   B C    1 
ATOM   6518 O O    . ALA   B 1 134 ? 39.746 -34.091 2.892   1.00 15.94 ?  134 ALA   B O    1 
ATOM   6519 C CB   . ALA   B 1 134 ? 37.953 -31.600 4.190   1.00 15.80 ?  134 ALA   B CB   1 
ATOM   6520 H H    . ALA   B 1 134 ? 40.316 -31.895 4.913   1.00 17.83 ?  134 ALA   B H    1 
ATOM   6521 H HA   . ALA   B 1 134 ? 38.072 -33.275 5.362   1.00 17.98 ?  134 ALA   B HA   1 
ATOM   6522 H HB1  . ALA   B 1 134 ? 37.067 -31.807 3.857   1.00 19.02 ?  134 ALA   B HB1  1 
ATOM   6523 H HB2  . ALA   B 1 134 ? 37.890 -30.986 4.940   1.00 19.02 ?  134 ALA   B HB2  1 
ATOM   6524 H HB3  . ALA   B 1 134 ? 38.490 -31.205 3.485   1.00 19.02 ?  134 ALA   B HB3  1 
ATOM   6525 N N    . ASP   B 1 135 ? 37.560 -34.518 3.221   1.00 14.91 ?  135 ASP   B N    1 
ATOM   6526 C CA   . ASP   B 1 135 ? 37.452 -35.413 2.075   1.00 15.57 ?  135 ASP   B CA   1 
ATOM   6527 C C    . ASP   B 1 135 ? 37.558 -34.579 0.805   1.00 14.73 ?  135 ASP   B C    1 
ATOM   6528 O O    . ASP   B 1 135 ? 36.712 -33.704 0.582   1.00 14.36 ?  135 ASP   B O    1 
ATOM   6529 C CB   . ASP   B 1 135 ? 36.099 -36.127 2.138   1.00 16.89 ?  135 ASP   B CB   1 
ATOM   6530 C CG   . ASP   B 1 135 ? 35.885 -37.111 1.002   1.00 18.49 ?  135 ASP   B CG   1 
ATOM   6531 O OD1  . ASP   B 1 135 ? 36.736 -37.189 0.090   1.00 18.44 ?  135 ASP   B OD1  1 
ATOM   6532 O OD2  . ASP   B 1 135 ? 34.856 -37.830 1.040   1.00 21.47 -1 135 ASP   B OD2  1 
ATOM   6533 H H    . ASP   B 1 135 ? 36.832 -34.430 3.672   1.00 17.95 ?  135 ASP   B H    1 
ATOM   6534 H HA   . ASP   B 1 135 ? 38.162 -36.067 2.107   1.00 18.74 ?  135 ASP   B HA   1 
ATOM   6535 H HB2  . ASP   B 1 135 ? 36.048 -36.619 2.969   1.00 20.32 ?  135 ASP   B HB2  1 
ATOM   6536 H HB3  . ASP   B 1 135 ? 35.394 -35.468 2.090   1.00 20.32 ?  135 ASP   B HB3  1 
ATOM   6537 N N    . PRO   B 1 136 ? 38.566 -34.795 -0.044  1.00 15.12 ?  136 PRO   B N    1 
ATOM   6538 C CA   . PRO   B 1 136 ? 38.677 -33.968 -1.257  1.00 14.38 ?  136 PRO   B CA   1 
ATOM   6539 C C    . PRO   B 1 136 ? 37.499 -34.121 -2.198  1.00 14.01 ?  136 PRO   B C    1 
ATOM   6540 O O    . PRO   B 1 136 ? 37.187 -33.174 -2.931  1.00 13.34 ?  136 PRO   B O    1 
ATOM   6541 C CB   . PRO   B 1 136 ? 39.997 -34.438 -1.887  1.00 15.22 ?  136 PRO   B CB   1 
ATOM   6542 C CG   . PRO   B 1 136 ? 40.183 -35.826 -1.362  1.00 16.31 ?  136 PRO   B CG   1 
ATOM   6543 C CD   . PRO   B 1 136 ? 39.628 -35.809 0.032   1.00 16.19 ?  136 PRO   B CD   1 
ATOM   6544 H HA   . PRO   B 1 136 ? 38.759 -33.033 -1.018  1.00 17.32 ?  136 PRO   B HA   1 
ATOM   6545 H HB2  . PRO   B 1 136 ? 39.918 -34.444 -2.855  1.00 18.32 ?  136 PRO   B HB2  1 
ATOM   6546 H HB3  . PRO   B 1 136 ? 40.719 -33.859 -1.602  1.00 18.32 ?  136 PRO   B HB3  1 
ATOM   6547 H HG2  . PRO   B 1 136 ? 39.697 -36.458 -1.914  1.00 19.64 ?  136 PRO   B HG2  1 
ATOM   6548 H HG3  . PRO   B 1 136 ? 41.129 -36.046 -1.344  1.00 19.64 ?  136 PRO   B HG3  1 
ATOM   6549 H HD2  . PRO   B 1 136 ? 39.248 -36.673 0.262   1.00 19.49 ?  136 PRO   B HD2  1 
ATOM   6550 H HD3  . PRO   B 1 136 ? 40.303 -35.536 0.674   1.00 19.49 ?  136 PRO   B HD3  1 
ATOM   6551 N N    . ILE   B 1 137 ? 36.838 -35.282 -2.204  1.00 14.49 ?  137 ILE   B N    1 
ATOM   6552 C CA   . ILE   B 1 137 ? 35.625 -35.445 -3.000  1.00 14.79 ?  137 ILE   B CA   1 
ATOM   6553 C C    . ILE   B 1 137 ? 34.548 -34.480 -2.524  1.00 14.22 ?  137 ILE   B C    1 
ATOM   6554 O O    . ILE   B 1 137 ? 33.828 -33.880 -3.329  1.00 14.05 ?  137 ILE   B O    1 
ATOM   6555 C CB   . ILE   B 1 137 ? 35.148 -36.914 -2.947  1.00 16.56 ?  137 ILE   B CB   1 
ATOM   6556 C CG1  . ILE   B 1 137 ? 36.151 -37.820 -3.664  1.00 19.08 ?  137 ILE   B CG1  1 
ATOM   6557 C CG2  . ILE   B 1 137 ? 33.761 -37.056 -3.563  1.00 17.15 ?  137 ILE   B CG2  1 
ATOM   6558 C CD1  . ILE   B 1 137 ? 35.821 -39.300 -3.584  1.00 21.59 ?  137 ILE   B CD1  1 
ATOM   6559 H H    . ILE   B 1 137 ? 37.066 -35.983 -1.768  1.00 17.44 ?  137 ILE   B H    1 
ATOM   6560 H HA   . ILE   B 1 137 ? 35.816 -35.236 -3.930  1.00 17.80 ?  137 ILE   B HA   1 
ATOM   6561 H HB   . ILE   B 1 137 ? 35.091 -37.185 -2.022  1.00 19.92 ?  137 ILE   B HB   1 
ATOM   6562 H HG12 . ILE   B 1 137 ? 36.178 -37.575 -4.602  1.00 22.96 ?  137 ILE   B HG12 1 
ATOM   6563 H HG13 . ILE   B 1 137 ? 37.022 -37.690 -3.264  1.00 22.96 ?  137 ILE   B HG13 1 
ATOM   6564 H HG21 . ILE   B 1 137 ? 33.502 -37.991 -3.563  1.00 20.64 ?  137 ILE   B HG21 1 
ATOM   6565 H HG22 . ILE   B 1 137 ? 33.121 -36.552 -3.041  1.00 20.64 ?  137 ILE   B HG22 1 
ATOM   6566 H HG23 . ILE   B 1 137 ? 33.785 -36.723 -4.474  1.00 20.64 ?  137 ILE   B HG23 1 
ATOM   6567 H HD11 . ILE   B 1 137 ? 36.492 -39.783 -4.085  1.00 25.97 ?  137 ILE   B HD11 1 
ATOM   6568 H HD12 . ILE   B 1 137 ? 35.829 -39.579 -2.655  1.00 25.97 ?  137 ILE   B HD12 1 
ATOM   6569 H HD13 . ILE   B 1 137 ? 34.949 -39.465 -3.974  1.00 25.97 ?  137 ILE   B HD13 1 
ATOM   6570 N N    . HIS   B 1 138 ? 34.414 -34.335 -1.207  1.00 14.20 ?  138 HIS   B N    1 
ATOM   6571 C CA   . HIS   B 1 138 ? 33.471 -33.365 -0.666  1.00 14.41 ?  138 HIS   B CA   1 
ATOM   6572 C C    . HIS   B 1 138 ? 33.894 -31.941 -0.995  1.00 13.84 ?  138 HIS   B C    1 
ATOM   6573 O O    . HIS   B 1 138 ? 33.051 -31.097 -1.316  1.00 14.42 ?  138 HIS   B O    1 
ATOM   6574 C CB   . HIS   B 1 138 ? 33.360 -33.531 0.842   1.00 15.51 ?  138 HIS   B CB   1 
ATOM   6575 C CG   . HIS   B 1 138 ? 32.412 -32.564 1.474   1.00 16.09 ?  138 HIS   B CG   1 
ATOM   6576 N ND1  . HIS   B 1 138 ? 31.074 -32.510 1.145   1.00 17.34 ?  138 HIS   B ND1  1 
ATOM   6577 C CD2  . HIS   B 1 138 ? 32.615 -31.585 2.387   1.00 16.68 ?  138 HIS   B CD2  1 
ATOM   6578 C CE1  . HIS   B 1 138 ? 30.491 -31.552 1.841   1.00 17.49 ?  138 HIS   B CE1  1 
ATOM   6579 N NE2  . HIS   B 1 138 ? 31.403 -30.974 2.602   1.00 17.42 ?  138 HIS   B NE2  1 
ATOM   6580 H H    . HIS   B 1 138 ? 34.855 -34.778 -0.620  1.00 17.10 ?  138 HIS   B H    1 
ATOM   6581 H HA   . HIS   B 1 138 ? 32.598 -33.521 -1.058  1.00 17.35 ?  138 HIS   B HA   1 
ATOM   6582 H HB2  . HIS   B 1 138 ? 33.041 -34.426 1.036   1.00 18.67 ?  138 HIS   B HB2  1 
ATOM   6583 H HB3  . HIS   B 1 138 ? 34.233 -33.397 1.239   1.00 18.67 ?  138 HIS   B HB3  1 
ATOM   6584 H HD1  . HIS   B 1 138 ? 30.684 -33.026 0.577   1.00 20.87 ?  138 HIS   B HD1  1 
ATOM   6585 H HD2  . HIS   B 1 138 ? 33.417 -31.368 2.801   1.00 20.07 ?  138 HIS   B HD2  1 
ATOM   6586 H HE1  . HIS   B 1 138 ? 29.587 -31.329 1.800   1.00 21.05 ?  138 HIS   B HE1  1 
ATOM   6587 N N    . SER   B 1 139 ? 35.189 -31.642 -0.911  1.00 13.47 ?  139 SER   B N    1 
ATOM   6588 C CA   . SER   B 1 139 ? 35.627 -30.291 -1.228  1.00 13.02 ?  139 SER   B CA   1 
ATOM   6589 C C    . SER   B 1 139 ? 35.286 -29.932 -2.667  1.00 12.31 ?  139 SER   B C    1 
ATOM   6590 O O    . SER   B 1 139 ? 34.839 -28.814 -2.939  1.00 12.47 ?  139 SER   B O    1 
ATOM   6591 C CB   . SER   B 1 139 ? 37.121 -30.146 -0.962  1.00 13.46 ?  139 SER   B CB   1 
ATOM   6592 O OG   . SER   B 1 139 ? 37.527 -28.813 -1.234  1.00 13.49 ?  139 SER   B OG   1 
ATOM   6593 H H    . SER   B 1 139 ? 35.811 -32.184 -0.683  1.00 16.22 ?  139 SER   B H    1 
ATOM   6594 H HA   . SER   B 1 139 ? 35.159 -29.665 -0.655  1.00 15.68 ?  139 SER   B HA   1 
ATOM   6595 H HB2  . SER   B 1 139 ? 37.300 -30.352 -0.030  1.00 16.21 ?  139 SER   B HB2  1 
ATOM   6596 H HB3  . SER   B 1 139 ? 37.612 -30.751 -1.539  1.00 16.21 ?  139 SER   B HB3  1 
ATOM   6597 H HG   . SER   B 1 139 ? 38.357 -28.734 -1.078  1.00 16.24 ?  139 SER   B HG   1 
ATOM   6598 N N    . LEU   B 1 140 ? 35.488 -30.869 -3.599  1.00 12.24 ?  140 LEU   B N    1 
ATOM   6599 C CA   . LEU   B 1 140 ? 35.123 -30.627 -4.989  1.00 12.42 ?  140 LEU   B CA   1 
ATOM   6600 C C    . LEU   B 1 140 ? 33.621 -30.395 -5.123  1.00 12.47 ?  140 LEU   B C    1 
ATOM   6601 O O    . LEU   B 1 140 ? 33.184 -29.499 -5.855  1.00 12.69 ?  140 LEU   B O    1 
ATOM   6602 C CB   . LEU   B 1 140 ? 35.593 -31.791 -5.864  1.00 12.57 ?  140 LEU   B CB   1 
ATOM   6603 C CG   . LEU   B 1 140 ? 35.238 -31.678 -7.341  1.00 12.92 ?  140 LEU   B CG   1 
ATOM   6604 C CD1  . LEU   B 1 140 ? 35.807 -30.407 -7.946  1.00 13.84 ?  140 LEU   B CD1  1 
ATOM   6605 C CD2  . LEU   B 1 140 ? 35.717 -32.910 -8.090  1.00 13.63 ?  140 LEU   B CD2  1 
ATOM   6606 H H    . LEU   B 1 140 ? 35.835 -31.640 -3.450  1.00 14.75 ?  140 LEU   B H    1 
ATOM   6607 H HA   . LEU   B 1 140 ? 35.577 -29.824 -5.296  1.00 14.96 ?  140 LEU   B HA   1 
ATOM   6608 H HB2  . LEU   B 1 140 ? 36.560 -31.853 -5.803  1.00 15.14 ?  140 LEU   B HB2  1 
ATOM   6609 H HB3  . LEU   B 1 140 ? 35.193 -32.607 -5.530  1.00 15.14 ?  140 LEU   B HB3  1 
ATOM   6610 H HG   . LEU   B 1 140 ? 34.272 -31.637 -7.427  1.00 15.56 ?  140 LEU   B HG   1 
ATOM   6611 H HD11 . LEU   B 1 140 ? 35.682 -30.435 -8.906  1.00 16.66 ?  140 LEU   B HD11 1 
ATOM   6612 H HD12 . LEU   B 1 140 ? 35.338 -29.643 -7.573  1.00 16.66 ?  140 LEU   B HD12 1 
ATOM   6613 H HD13 . LEU   B 1 140 ? 36.750 -30.355 -7.734  1.00 16.66 ?  140 LEU   B HD13 1 
ATOM   6614 H HD21 . LEU   B 1 140 ? 35.474 -32.817 -9.027  1.00 16.42 ?  140 LEU   B HD21 1 
ATOM   6615 H HD22 . LEU   B 1 140 ? 36.675 -32.980 -7.999  1.00 16.42 ?  140 LEU   B HD22 1 
ATOM   6616 H HD23 . LEU   B 1 140 ? 35.283 -33.691 -7.715  1.00 16.42 ?  140 LEU   B HD23 1 
ATOM   6617 N N    . ARG   B 1 141 ? 32.818 -31.188 -4.407  1.00 12.65 ?  141 ARG   B N    1 
ATOM   6618 C CA   . ARG   B 1 141 ? 31.367 -31.014 -4.395  1.00 13.57 ?  141 ARG   B CA   1 
ATOM   6619 C C    . ARG   B 1 141 ? 30.986 -29.601 -3.965  1.00 13.08 ?  141 ARG   B C    1 
ATOM   6620 O O    . ARG   B 1 141 ? 30.198 -28.915 -4.633  1.00 13.68 ?  141 ARG   B O    1 
ATOM   6621 C CB   . ARG   B 1 141 ? 30.778 -32.041 -3.415  1.00 15.29 ?  141 ARG   B CB   1 
ATOM   6622 C CG   . ARG   B 1 141 ? 29.299 -31.944 -3.116  1.00 17.85 ?  141 ARG   B CG   1 
ATOM   6623 C CD   . ARG   B 1 141 ? 28.528 -32.582 -4.193  1.00 20.08 ?  141 ARG   B CD   1 
ATOM   6624 N NE   . ARG   B 1 141 ? 28.249 -31.665 -5.286  1.00 20.60 ?  141 ARG   B NE   1 
ATOM   6625 C CZ   . ARG   B 1 141 ? 28.236 -32.006 -6.567  1.00 20.24 ?  141 ARG   B CZ   1 
ATOM   6626 N NH1  . ARG   B 1 141 ? 28.681 -33.185 -6.973  1.00 20.56 ?  141 ARG   B NH1  1 
ATOM   6627 N NH2  . ARG   B 1 141 ? 27.764 -31.142 -7.462  1.00 20.97 ?  141 ARG   B NH2  1 
ATOM   6628 H H    . ARG   B 1 141 ? 33.101 -31.837 -3.916  1.00 15.24 ?  141 ARG   B H    1 
ATOM   6629 H HA   . ARG   B 1 141 ? 31.010 -31.182 -5.277  1.00 16.34 ?  141 ARG   B HA   1 
ATOM   6630 H HB2  . ARG   B 1 141 ? 30.949 -32.932 -3.766  1.00 18.41 ?  141 ARG   B HB2  1 
ATOM   6631 H HB3  . ARG   B 1 141 ? 31.243 -31.952 -2.567  1.00 18.41 ?  141 ARG   B HB3  1 
ATOM   6632 H HG2  . ARG   B 1 141 ? 29.112 -32.394 -2.280  1.00 21.48 ?  141 ARG   B HG2  1 
ATOM   6633 H HG3  . ARG   B 1 141 ? 29.037 -31.006 -3.055  1.00 21.48 ?  141 ARG   B HG3  1 
ATOM   6634 H HD2  . ARG   B 1 141 ? 29.035 -33.336 -4.542  1.00 24.15 ?  141 ARG   B HD2  1 
ATOM   6635 H HD3  . ARG   B 1 141 ? 27.690 -32.901 -3.830  1.00 24.15 ?  141 ARG   B HD3  1 
ATOM   6636 H HE   . ARG   B 1 141 ? 28.080 -30.845 -5.084  1.00 24.78 ?  141 ARG   B HE   1 
ATOM   6637 H HH11 . ARG   B 1 141 ? 28.966 -33.762 -6.405  1.00 24.73 ?  141 ARG   B HH11 1 
ATOM   6638 H HH12 . ARG   B 1 141 ? 28.663 -33.380 -7.807  1.00 24.73 ?  141 ARG   B HH12 1 
ATOM   6639 H HH21 . ARG   B 1 141 ? 27.476 -30.370 -7.210  1.00 25.23 ?  141 ARG   B HH21 1 
ATOM   6640 H HH22 . ARG   B 1 141 ? 27.768 -31.343 -8.299  1.00 25.23 ?  141 ARG   B HH22 1 
ATOM   6641 N N    . VAL   B 1 142 ? 31.525 -29.159 -2.831  1.00 12.95 ?  142 VAL   B N    1 
ATOM   6642 C CA   . VAL   B 1 142 ? 31.198 -27.828 -2.337  1.00 12.81 ?  142 VAL   B CA   1 
ATOM   6643 C C    . VAL   B 1 142 ? 31.679 -26.765 -3.317  1.00 12.64 ?  142 VAL   B C    1 
ATOM   6644 O O    . VAL   B 1 142 ? 30.982 -25.778 -3.569  1.00 13.09 ?  142 VAL   B O    1 
ATOM   6645 C CB   . VAL   B 1 142 ? 31.745 -27.617 -0.914  1.00 13.40 ?  142 VAL   B CB   1 
ATOM   6646 C CG1  . VAL   B 1 142 ? 31.442 -26.190 -0.434  1.00 13.60 ?  142 VAL   B CG1  1 
ATOM   6647 C CG2  . VAL   B 1 142 ? 31.153 -28.633 0.049   1.00 14.43 ?  142 VAL   B CG2  1 
ATOM   6648 H H    . VAL   B 1 142 ? 32.079 -29.599 -2.338  1.00 15.60 ?  142 VAL   B H    1 
ATOM   6649 H HA   . VAL   B 1 142 ? 30.237 -27.751 -2.285  1.00 15.43 ?  142 VAL   B HA   1 
ATOM   6650 H HB   . VAL   B 1 142 ? 32.712 -27.734 -0.919  1.00 16.14 ?  142 VAL   B HB   1 
ATOM   6651 H HG11 . VAL   B 1 142 ? 31.627 -26.134 0.517   1.00 16.38 ?  142 VAL   B HG11 1 
ATOM   6652 H HG12 . VAL   B 1 142 ? 32.013 -25.567 -0.915  1.00 16.38 ?  142 VAL   B HG12 1 
ATOM   6653 H HG13 . VAL   B 1 142 ? 30.513 -25.993 -0.606  1.00 16.38 ?  142 VAL   B HG13 1 
ATOM   6654 H HG21 . VAL   B 1 142 ? 31.485 -28.455 0.943   1.00 17.37 ?  142 VAL   B HG21 1 
ATOM   6655 H HG22 . VAL   B 1 142 ? 30.186 -28.550 0.034   1.00 17.37 ?  142 VAL   B HG22 1 
ATOM   6656 H HG23 . VAL   B 1 142 ? 31.413 -29.523 -0.231  1.00 17.37 ?  142 VAL   B HG23 1 
ATOM   6657 N N    . CYS   B 1 143 ? 32.858 -26.968 -3.911  1.00 12.15 ?  143 CYS   B N    1 
ATOM   6658 C CA   . CYS   B 1 143 ? 33.356 -26.031 -4.914  1.00 12.17 ?  143 CYS   B CA   1 
ATOM   6659 C C    . CYS   B 1 143 ? 32.350 -25.875 -6.052  1.00 12.37 ?  143 CYS   B C    1 
ATOM   6660 O O    . CYS   B 1 143 ? 31.939 -24.761 -6.395  1.00 12.66 ?  143 CYS   B O    1 
ATOM   6661 C CB   . CYS   B 1 143 ? 34.712 -26.514 -5.443  1.00 12.47 ?  143 CYS   B CB   1 
ATOM   6662 S SG   . CYS   B 1 143 ? 35.458 -25.410 -6.652  1.00 12.81 ?  143 CYS   B SG   1 
ATOM   6663 H H    . CYS   B 1 143 ? 33.383 -27.637 -3.755  1.00 14.64 ?  143 CYS   B H    1 
ATOM   6664 H HA   . CYS   B 1 143 ? 33.485 -25.163 -4.501  1.00 14.66 ?  143 CYS   B HA   1 
ATOM   6665 H HB2  . CYS   B 1 143 ? 35.331 -26.601 -4.702  1.00 15.03 ?  143 CYS   B HB2  1 
ATOM   6666 H HB3  . CYS   B 1 143 ? 34.592 -27.374 -5.869  1.00 15.03 ?  143 CYS   B HB3  1 
ATOM   6667 H HG   . CYS   B 1 143 ? 36.527 -25.847 -6.977  1.00 15.43 ?  143 CYS   B HG   1 
ATOM   6668 N N    . VAL   B 1 144 ? 31.944 -26.993 -6.655  1.00 12.52 ?  144 VAL   B N    1 
ATOM   6669 C CA   . VAL   B 1 144 ? 31.040 -26.923 -7.800  1.00 13.62 ?  144 VAL   B CA   1 
ATOM   6670 C C    . VAL   B 1 144 ? 29.697 -26.312 -7.422  1.00 13.53 ?  144 VAL   B C    1 
ATOM   6671 O O    . VAL   B 1 144 ? 29.077 -25.604 -8.228  1.00 14.54 ?  144 VAL   B O    1 
ATOM   6672 C CB   . VAL   B 1 144 ? 30.886 -28.328 -8.394  1.00 15.95 ?  144 VAL   B CB   1 
ATOM   6673 C CG1  . VAL   B 1 144 ? 29.615 -28.453 -9.237  1.00 18.52 ?  144 VAL   B CG1  1 
ATOM   6674 C CG2  . VAL   B 1 144 ? 32.139 -28.716 -9.180  1.00 16.08 ?  144 VAL   B CG2  1 
ATOM   6675 H H    . VAL   B 1 144 ? 32.171 -27.792 -6.421  1.00 15.08 ?  144 VAL   B H    1 
ATOM   6676 H HA   . VAL   B 1 144 ? 31.438 -26.361 -8.478  1.00 16.40 ?  144 VAL   B HA   1 
ATOM   6677 H HB   . VAL   B 1 144 ? 30.805 -28.963 -7.662  1.00 19.19 ?  144 VAL   B HB   1 
ATOM   6678 H HG11 . VAL   B 1 144 ? 29.695 -29.234 -9.808  1.00 22.28 ?  144 VAL   B HG11 1 
ATOM   6679 H HG12 . VAL   B 1 144 ? 28.853 -28.554 -8.648  1.00 22.28 ?  144 VAL   B HG12 1 
ATOM   6680 H HG13 . VAL   B 1 144 ? 29.519 -27.657 -9.781  1.00 22.28 ?  144 VAL   B HG13 1 
ATOM   6681 H HG21 . VAL   B 1 144 ? 32.019 -29.610 -9.540  1.00 19.35 ?  144 VAL   B HG21 1 
ATOM   6682 H HG22 . VAL   B 1 144 ? 32.259 -28.082 -9.905  1.00 19.35 ?  144 VAL   B HG22 1 
ATOM   6683 H HG23 . VAL   B 1 144 ? 32.901 -28.695 -8.587  1.00 19.35 ?  144 VAL   B HG23 1 
ATOM   6684 N N    . ASP   B 1 145 ? 29.235 -26.556 -6.200  1.00 13.55 ?  145 ASP   B N    1 
ATOM   6685 C CA   . ASP   B 1 145 ? 27.928 -26.095 -5.757  1.00 13.93 ?  145 ASP   B CA   1 
ATOM   6686 C C    . ASP   B 1 145 ? 27.957 -24.676 -5.201  1.00 14.12 ?  145 ASP   B C    1 
ATOM   6687 O O    . ASP   B 1 145 ? 26.895 -24.141 -4.863  1.00 15.81 ?  145 ASP   B O    1 
ATOM   6688 C CB   . ASP   B 1 145 ? 27.350 -27.032 -4.686  1.00 15.28 ?  145 ASP   B CB   1 
ATOM   6689 C CG   . ASP   B 1 145 ? 26.982 -28.404 -5.219  1.00 16.59 ?  145 ASP   B CG   1 
ATOM   6690 O OD1  . ASP   B 1 145 ? 26.873 -28.575 -6.452  1.00 17.00 ?  145 ASP   B OD1  1 
ATOM   6691 O OD2  . ASP   B 1 145 ? 26.798 -29.308 -4.383  1.00 19.14 -1 145 ASP   B OD2  1 
ATOM   6692 H H    . ASP   B 1 145 ? 29.673 -26.985 -5.599  1.00 16.31 ?  145 ASP   B H    1 
ATOM   6693 H HA   . ASP   B 1 145 ? 27.326 -26.086 -6.516  1.00 16.78 ?  145 ASP   B HA   1 
ATOM   6694 H HB2  . ASP   B 1 145 ? 28.005 -27.148 -3.988  1.00 18.39 ?  145 ASP   B HB2  1 
ATOM   6695 H HB3  . ASP   B 1 145 ? 26.544 -26.624 -4.325  1.00 18.39 ?  145 ASP   B HB3  1 
ATOM   6696 N N    . THR   B 1 146 ? 29.135 -24.056 -5.091  1.00 12.54 ?  146 THR   B N    1 
ATOM   6697 C CA   . THR   B 1 146 ? 29.272 -22.745 -4.469  1.00 12.32 ?  146 THR   B CA   1 
ATOM   6698 C C    . THR   B 1 146 ? 29.904 -21.715 -5.382  1.00 11.96 ?  146 THR   B C    1 
ATOM   6699 O O    . THR   B 1 146 ? 29.443 -20.561 -5.430  1.00 12.46 ?  146 THR   B O    1 
ATOM   6700 C CB   . THR   B 1 146 ? 30.096 -22.858 -3.183  1.00 12.57 ?  146 THR   B CB   1 
ATOM   6701 O OG1  . THR   B 1 146 ? 29.523 -23.857 -2.334  1.00 12.46 ?  146 THR   B OG1  1 
ATOM   6702 C CG2  . THR   B 1 146 ? 30.158 -21.518 -2.451  1.00 12.94 ?  146 THR   B CG2  1 
ATOM   6703 H H    . THR   B 1 146 ? 29.888 -24.382 -5.373  1.00 15.11 ?  146 THR   B H    1 
ATOM   6704 H HA   . THR   B 1 146 ? 28.395 -22.419 -4.226  1.00 14.84 ?  146 THR   B HA   1 
ATOM   6705 H HB   . THR   B 1 146 ? 31.004 -23.115 -3.404  1.00 15.14 ?  146 THR   B HB   1 
ATOM   6706 H HG1  . THR   B 1 146 ? 29.552 -24.614 -2.713  1.00 15.00 ?  146 THR   B HG1  1 
ATOM   6707 H HG21 . THR   B 1 146 ? 30.508 -21.647 -1.555  1.00 15.58 ?  146 THR   B HG21 1 
ATOM   6708 H HG22 . THR   B 1 146 ? 30.741 -20.906 -2.928  1.00 15.58 ?  146 THR   B HG22 1 
ATOM   6709 H HG23 . THR   B 1 146 ? 29.272 -21.133 -2.391  1.00 15.58 ?  146 THR   B HG23 1 
ATOM   6710 N N    . VAL   B 1 147 ? 30.970 -22.085 -6.082  1.00 11.99 ?  147 VAL   B N    1 
ATOM   6711 C CA   . VAL   B 1 147 ? 31.688 -21.135 -6.917  1.00 11.95 ?  147 VAL   B CA   1 
ATOM   6712 C C    . VAL   B 1 147 ? 30.960 -21.001 -8.242  1.00 11.96 ?  147 VAL   B C    1 
ATOM   6713 O O    . VAL   B 1 147 ? 30.595 -22.004 -8.872  1.00 12.84 ?  147 VAL   B O    1 
ATOM   6714 C CB   . VAL   B 1 147 ? 33.141 -21.586 -7.125  1.00 12.11 ?  147 VAL   B CB   1 
ATOM   6715 C CG1  . VAL   B 1 147 ? 33.886 -20.570 -7.958  1.00 12.31 ?  147 VAL   B CG1  1 
ATOM   6716 C CG2  . VAL   B 1 147 ? 33.825 -21.789 -5.787  1.00 12.41 ?  147 VAL   B CG2  1 
ATOM   6717 H H    . VAL   B 1 147 ? 31.298 -22.883 -6.088  1.00 14.45 ?  147 VAL   B H    1 
ATOM   6718 H HA   . VAL   B 1 147 ? 31.698 -20.271 -6.483  1.00 14.40 ?  147 VAL   B HA   1 
ATOM   6719 H HB   . VAL   B 1 147 ? 33.150 -22.432 -7.602  1.00 14.59 ?  147 VAL   B HB   1 
ATOM   6720 H HG11 . VAL   B 1 147 ? 34.832 -20.776 -7.931  1.00 14.83 ?  147 VAL   B HG11 1 
ATOM   6721 H HG12 . VAL   B 1 147 ? 33.565 -20.615 -8.874  1.00 14.83 ?  147 VAL   B HG12 1 
ATOM   6722 H HG13 . VAL   B 1 147 ? 33.726 -19.688 -7.593  1.00 14.83 ?  147 VAL   B HG13 1 
ATOM   6723 H HG21 . VAL   B 1 147 ? 34.765 -21.979 -5.938  1.00 14.96 ?  147 VAL   B HG21 1 
ATOM   6724 H HG22 . VAL   B 1 147 ? 33.733 -20.980 -5.260  1.00 14.96 ?  147 VAL   B HG22 1 
ATOM   6725 H HG23 . VAL   B 1 147 ? 33.408 -22.533 -5.327  1.00 14.96 ?  147 VAL   B HG23 1 
ATOM   6726 N N    . ARG   B 1 148 ? 30.750 -19.751 -8.660  1.00 12.09 ?  148 ARG   B N    1 
ATOM   6727 C CA   . ARG   B 1 148 ? 30.117 -19.430 -9.928  1.00 12.50 ?  148 ARG   B CA   1 
ATOM   6728 C C    . ARG   B 1 148 ? 31.066 -18.756 -10.906 1.00 12.59 ?  148 ARG   B C    1 
ATOM   6729 O O    . ARG   B 1 148 ? 30.782 -18.748 -12.103 1.00 13.97 ?  148 ARG   B O    1 
ATOM   6730 C CB   . ARG   B 1 148 ? 28.885 -18.544 -9.701  1.00 12.72 ?  148 ARG   B CB   1 
ATOM   6731 C CG   . ARG   B 1 148 ? 27.806 -19.252 -8.899  1.00 13.36 ?  148 ARG   B CG   1 
ATOM   6732 C CD   . ARG   B 1 148 ? 26.608 -18.369 -8.595  1.00 14.12 ?  148 ARG   B CD   1 
ATOM   6733 N NE   . ARG   B 1 148 ? 26.990 -17.168 -7.862  1.00 13.92 ?  148 ARG   B NE   1 
ATOM   6734 C CZ   . ARG   B 1 148 ? 27.279 -17.135 -6.567  1.00 13.35 ?  148 ARG   B CZ   1 
ATOM   6735 N NH1  . ARG   B 1 148 ? 27.220 -18.223 -5.815  1.00 13.74 ?  148 ARG   B NH1  1 
ATOM   6736 N NH2  . ARG   B 1 148 ? 27.666 -15.986 -6.019  1.00 13.66 ?  148 ARG   B NH2  1 
ATOM   6737 H H    . ARG   B 1 148 ? 30.979 -19.051 -8.206  1.00 14.56 ?  148 ARG   B H    1 
ATOM   6738 H HA   . ARG   B 1 148 ? 29.815 -20.252 -10.339 1.00 15.06 ?  148 ARG   B HA   1 
ATOM   6739 H HB2  . ARG   B 1 148 ? 29.151 -17.747 -9.213  1.00 15.32 ?  148 ARG   B HB2  1 
ATOM   6740 H HB3  . ARG   B 1 148 ? 28.509 -18.295 -10.561 1.00 15.32 ?  148 ARG   B HB3  1 
ATOM   6741 H HG2  . ARG   B 1 148 ? 27.489 -20.018 -9.405  1.00 16.09 ?  148 ARG   B HG2  1 
ATOM   6742 H HG3  . ARG   B 1 148 ? 28.181 -19.547 -8.055  1.00 16.09 ?  148 ARG   B HG3  1 
ATOM   6743 H HD2  . ARG   B 1 148 ? 26.196 -18.091 -9.428  1.00 17.01 ?  148 ARG   B HD2  1 
ATOM   6744 H HD3  . ARG   B 1 148 ? 25.972 -18.863 -8.055  1.00 17.01 ?  148 ARG   B HD3  1 
ATOM   6745 H HE   . ARG   B 1 148 ? 27.033 -16.428 -8.296  1.00 16.76 ?  148 ARG   B HE   1 
ATOM   6746 H HH11 . ARG   B 1 148 ? 26.973 -18.975 -6.155  1.00 16.55 ?  148 ARG   B HH11 1 
ATOM   6747 H HH12 . ARG   B 1 148 ? 27.413 -18.181 -4.976  1.00 16.55 ?  148 ARG   B HH12 1 
ATOM   6748 H HH21 . ARG   B 1 148 ? 27.715 -15.275 -6.498  1.00 16.45 ?  148 ARG   B HH21 1 
ATOM   6749 H HH22 . ARG   B 1 148 ? 27.861 -15.951 -5.180  1.00 16.45 ?  148 ARG   B HH22 1 
ATOM   6750 N N    . THR   B 1 149 ? 32.182 -18.211 -10.425 1.00 12.42 ?  149 THR   B N    1 
ATOM   6751 C CA   . THR   B 1 149 ? 33.219 -17.650 -11.276 1.00 12.35 ?  149 THR   B CA   1 
ATOM   6752 C C    . THR   B 1 149 ? 34.108 -18.791 -11.778 1.00 12.40 ?  149 THR   B C    1 
ATOM   6753 O O    . THR   B 1 149 ? 33.919 -19.961 -11.429 1.00 12.77 ?  149 THR   B O    1 
ATOM   6754 C CB   . THR   B 1 149 ? 33.983 -16.588 -10.499 1.00 12.36 ?  149 THR   B CB   1 
ATOM   6755 O OG1  . THR   B 1 149 ? 34.435 -17.181 -9.281  1.00 12.56 ?  149 THR   B OG1  1 
ATOM   6756 C CG2  . THR   B 1 149 ? 33.084 -15.381 -10.222 1.00 13.33 ?  149 THR   B CG2  1 
ATOM   6757 H H    . THR   B 1 149 ? 32.354 -18.147 -9.584  1.00 14.97 ?  149 THR   B H    1 
ATOM   6758 H HA   . THR   B 1 149 ? 32.804 -17.226 -12.043 1.00 14.88 ?  149 THR   B HA   1 
ATOM   6759 H HB   . THR   B 1 149 ? 34.746 -16.300 -11.018 1.00 14.89 ?  149 THR   B HB   1 
ATOM   6760 H HG1  . THR   B 1 149 ? 34.853 -16.606 -8.821  1.00 15.13 ?  149 THR   B HG1  1 
ATOM   6761 H HG21 . THR   B 1 149 ? 33.585 -14.704 -9.744  1.00 16.05 ?  149 THR   B HG21 1 
ATOM   6762 H HG22 . THR   B 1 149 ? 32.770 -15.007 -11.062 1.00 16.05 ?  149 THR   B HG22 1 
ATOM   6763 H HG23 . THR   B 1 149 ? 32.321 -15.649 -9.691  1.00 16.05 ?  149 THR   B HG23 1 
ATOM   6764 N N    . ASN   B 1 150 ? 35.069 -18.472 -12.632 1.00 12.18 ?  150 ASN   B N    1 
ATOM   6765 C CA   . ASN   B 1 150 ? 35.840 -19.505 -13.319 1.00 12.63 ?  150 ASN   B CA   1 
ATOM   6766 C C    . ASN   B 1 150 ? 37.000 -19.949 -12.442 1.00 12.39 ?  150 ASN   B C    1 
ATOM   6767 O O    . ASN   B 1 150 ? 37.920 -19.175 -12.178 1.00 13.45 ?  150 ASN   B O    1 
ATOM   6768 C CB   . ASN   B 1 150 ? 36.323 -18.986 -14.666 1.00 14.53 ?  150 ASN   B CB   1 
ATOM   6769 C CG   . ASN   B 1 150 ? 35.184 -18.745 -15.610 1.00 16.70 ?  150 ASN   B CG   1 
ATOM   6770 O OD1  . ASN   B 1 150 ? 34.306 -19.591 -15.744 1.00 18.07 ?  150 ASN   B OD1  1 
ATOM   6771 N ND2  . ASN   B 1 150 ? 35.158 -17.578 -16.238 1.00 18.09 ?  150 ASN   B ND2  1 
ATOM   6772 H H    . ASN   B 1 150 ? 35.300 -17.665 -12.833 1.00 14.67 ?  150 ASN   B H    1 
ATOM   6773 H HA   . ASN   B 1 150 ? 35.264 -20.271 -13.479 1.00 15.22 ?  150 ASN   B HA   1 
ATOM   6774 H HB2  . ASN   B 1 150 ? 36.790 -18.149 -14.538 1.00 17.50 ?  150 ASN   B HB2  1 
ATOM   6775 H HB3  . ASN   B 1 150 ? 36.914 -19.645 -15.065 1.00 17.50 ?  150 ASN   B HB3  1 
ATOM   6776 H HD21 . ASN   B 1 150 ? 34.524 -17.393 -16.793 1.00 21.77 ?  150 ASN   B HD21 1 
ATOM   6777 H HD22 . ASN   B 1 150 ? 35.787 -17.004 -16.107 1.00 21.77 ?  150 ASN   B HD22 1 
ATOM   6778 N N    . VAL   B 1 151 ? 36.967 -21.202 -12.003 1.00 11.63 ?  151 VAL   B N    1 
ATOM   6779 C CA   . VAL   B 1 151 ? 37.987 -21.734 -11.116 1.00 12.02 ?  151 VAL   B CA   1 
ATOM   6780 C C    . VAL   B 1 151 ? 38.698 -22.897 -11.801 1.00 12.00 ?  151 VAL   B C    1 
ATOM   6781 O O    . VAL   B 1 151 ? 38.056 -23.833 -12.310 1.00 12.81 ?  151 VAL   B O    1 
ATOM   6782 C CB   . VAL   B 1 151 ? 37.426 -22.075 -9.719  1.00 13.23 ?  151 VAL   B CB   1 
ATOM   6783 C CG1  . VAL   B 1 151 ? 36.273 -23.072 -9.797  1.00 14.08 ?  151 VAL   B CG1  1 
ATOM   6784 C CG2  . VAL   B 1 151 ? 38.538 -22.567 -8.803  1.00 14.05 ?  151 VAL   B CG2  1 
ATOM   6785 H H    . VAL   B 1 151 ? 36.347 -21.768 -12.202 1.00 14.02 ?  151 VAL   B H    1 
ATOM   6786 H HA   . VAL   B 1 151 ? 38.651 -21.035 -10.974 1.00 14.48 ?  151 VAL   B HA   1 
ATOM   6787 H HB   . VAL   B 1 151 ? 37.072 -21.261 -9.318  1.00 15.93 ?  151 VAL   B HB   1 
ATOM   6788 H HG11 . VAL   B 1 151 ? 35.957 -23.269 -8.899  1.00 16.95 ?  151 VAL   B HG11 1 
ATOM   6789 H HG12 . VAL   B 1 151 ? 35.556 -22.693 -10.324 1.00 16.95 ?  151 VAL   B HG12 1 
ATOM   6790 H HG13 . VAL   B 1 151 ? 36.593 -23.892 -10.215 1.00 16.95 ?  151 VAL   B HG13 1 
ATOM   6791 H HG21 . VAL   B 1 151 ? 38.192 -22.654 -7.898  1.00 16.92 ?  151 VAL   B HG21 1 
ATOM   6792 H HG22 . VAL   B 1 151 ? 38.851 -23.430 -9.116  1.00 16.92 ?  151 VAL   B HG22 1 
ATOM   6793 H HG23 . VAL   B 1 151 ? 39.267 -21.927 -8.812  1.00 16.92 ?  151 VAL   B HG23 1 
ATOM   6794 N N    . TYR   B 1 152 ? 40.031 -22.804 -11.820 1.00 11.54 ?  152 TYR   B N    1 
ATOM   6795 C CA   . TYR   B 1 152 ? 40.934 -23.786 -12.404 1.00 11.81 ?  152 TYR   B CA   1 
ATOM   6796 C C    . TYR   B 1 152 ? 41.657 -24.458 -11.242 1.00 11.52 ?  152 TYR   B C    1 
ATOM   6797 O O    . TYR   B 1 152 ? 42.494 -23.836 -10.583 1.00 11.81 ?  152 TYR   B O    1 
ATOM   6798 C CB   . TYR   B 1 152 ? 41.906 -23.078 -13.350 1.00 12.45 ?  152 TYR   B CB   1 
ATOM   6799 C CG   . TYR   B 1 152 ? 41.224 -22.621 -14.615 1.00 12.94 ?  152 TYR   B CG   1 
ATOM   6800 C CD1  . TYR   B 1 152 ? 40.541 -21.411 -14.671 1.00 13.54 ?  152 TYR   B CD1  1 
ATOM   6801 C CD2  . TYR   B 1 152 ? 41.249 -23.409 -15.754 1.00 13.78 ?  152 TYR   B CD2  1 
ATOM   6802 C CE1  . TYR   B 1 152 ? 39.897 -21.003 -15.826 1.00 14.74 ?  152 TYR   B CE1  1 
ATOM   6803 C CE2  . TYR   B 1 152 ? 40.610 -23.016 -16.913 1.00 14.95 ?  152 TYR   B CE2  1 
ATOM   6804 C CZ   . TYR   B 1 152 ? 39.932 -21.811 -16.947 1.00 15.04 ?  152 TYR   B CZ   1 
ATOM   6805 O OH   . TYR   B 1 152 ? 39.298 -21.420 -18.100 1.00 17.28 ?  152 TYR   B OH   1 
ATOM   6806 H H    . TYR   B 1 152 ? 40.458 -22.132 -11.478 1.00 13.91 ?  152 TYR   B H    1 
ATOM   6807 H HA   . TYR   B 1 152 ? 40.427 -24.451 -12.895 1.00 14.23 ?  152 TYR   B HA   1 
ATOM   6808 H HB2  . TYR   B 1 152 ? 42.271 -22.299 -12.901 1.00 15.00 ?  152 TYR   B HB2  1 
ATOM   6809 H HB3  . TYR   B 1 152 ? 42.619 -23.690 -13.588 1.00 15.00 ?  152 TYR   B HB3  1 
ATOM   6810 H HD1  . TYR   B 1 152 ? 40.507 -20.873 -13.912 1.00 16.31 ?  152 TYR   B HD1  1 
ATOM   6811 H HD2  . TYR   B 1 152 ? 41.700 -24.229 -15.731 1.00 16.60 ?  152 TYR   B HD2  1 
ATOM   6812 H HE1  . TYR   B 1 152 ? 39.441 -20.194 -15.846 1.00 17.75 ?  152 TYR   B HE1  1 
ATOM   6813 H HE2  . TYR   B 1 152 ? 40.640 -23.560 -17.666 1.00 18.00 ?  152 TYR   B HE2  1 
ATOM   6814 H HH   . TYR   B 1 152 ? 38.932 -20.671 -17.978 1.00 20.79 ?  152 TYR   B HH   1 
ATOM   6815 N N    . LEU   B 1 153 ? 41.301 -25.719 -10.977 1.00 11.60 ?  153 LEU   B N    1 
ATOM   6816 C CA   . LEU   B 1 153 ? 41.801 -26.463 -9.828  1.00 11.29 ?  153 LEU   B CA   1 
ATOM   6817 C C    . LEU   B 1 153 ? 43.033 -27.270 -10.214 1.00 11.28 ?  153 LEU   B C    1 
ATOM   6818 O O    . LEU   B 1 153 ? 43.025 -27.996 -11.210 1.00 12.55 ?  153 LEU   B O    1 
ATOM   6819 C CB   . LEU   B 1 153 ? 40.721 -27.408 -9.302  1.00 11.69 ?  153 LEU   B CB   1 
ATOM   6820 C CG   . LEU   B 1 153 ? 39.457 -26.768 -8.735  1.00 12.43 ?  153 LEU   B CG   1 
ATOM   6821 C CD1  . LEU   B 1 153 ? 38.367 -27.818 -8.597  1.00 13.17 ?  153 LEU   B CD1  1 
ATOM   6822 C CD2  . LEU   B 1 153 ? 39.742 -26.115 -7.396  1.00 12.99 ?  153 LEU   B CD2  1 
ATOM   6823 H H    . LEU   B 1 153 ? 40.755 -26.178 -11.469 1.00 13.98 ?  153 LEU   B H    1 
ATOM   6824 H HA   . LEU   B 1 153 ? 42.035 -25.839 -9.127  1.00 13.60 ?  153 LEU   B HA   1 
ATOM   6825 H HB2  . LEU   B 1 153 ? 40.446 -27.992 -10.022 1.00 14.09 ?  153 LEU   B HB2  1 
ATOM   6826 H HB3  . LEU   B 1 153 ? 41.111 -27.944 -8.588  1.00 14.09 ?  153 LEU   B HB3  1 
ATOM   6827 H HG   . LEU   B 1 153 ? 39.142 -26.080 -9.342  1.00 14.97 ?  153 LEU   B HG   1 
ATOM   6828 H HD11 . LEU   B 1 153 ? 37.562 -27.393 -8.260  1.00 15.86 ?  153 LEU   B HD11 1 
ATOM   6829 H HD12 . LEU   B 1 153 ? 38.197 -28.205 -9.467  1.00 15.86 ?  153 LEU   B HD12 1 
ATOM   6830 H HD13 . LEU   B 1 153 ? 38.666 -28.499 -7.978  1.00 15.86 ?  153 LEU   B HD13 1 
ATOM   6831 H HD21 . LEU   B 1 153 ? 38.923 -25.732 -7.045  1.00 15.64 ?  153 LEU   B HD21 1 
ATOM   6832 H HD22 . LEU   B 1 153 ? 40.079 -26.790 -6.781  1.00 15.64 ?  153 LEU   B HD22 1 
ATOM   6833 H HD23 . LEU   B 1 153 ? 40.408 -25.420 -7.517  1.00 15.64 ?  153 LEU   B HD23 1 
ATOM   6834 N N    . ALA   B 1 154 ? 44.081 -27.160 -9.406  1.00 11.49 ?  154 ALA   B N    1 
ATOM   6835 C CA   . ALA   B 1 154 ? 45.311 -27.912 -9.591  1.00 12.29 ?  154 ALA   B CA   1 
ATOM   6836 C C    . ALA   B 1 154 ? 45.370 -28.997 -8.522  1.00 12.87 ?  154 ALA   B C    1 
ATOM   6837 O O    . ALA   B 1 154 ? 45.284 -28.709 -7.323  1.00 13.75 ?  154 ALA   B O    1 
ATOM   6838 C CB   . ALA   B 1 154 ? 46.528 -27.000 -9.509  1.00 13.17 ?  154 ALA   B CB   1 
ATOM   6839 H H    . ALA   B 1 154 ? 44.103 -26.632 -8.724  1.00 13.84 ?  154 ALA   B H    1 
ATOM   6840 H HA   . ALA   B 1 154 ? 45.303 -28.337 -10.462 1.00 14.80 ?  154 ALA   B HA   1 
ATOM   6841 H HB1  . ALA   B 1 154 ? 47.330 -27.528 -9.634  1.00 15.86 ?  154 ALA   B HB1  1 
ATOM   6842 H HB2  . ALA   B 1 154 ? 46.464 -26.324 -10.203 1.00 15.86 ?  154 ALA   B HB2  1 
ATOM   6843 H HB3  . ALA   B 1 154 ? 46.545 -26.572 -8.636  1.00 15.86 ?  154 ALA   B HB3  1 
ATOM   6844 N N    . VAL   B 1 155 ? 45.502 -30.242 -8.959  1.00 11.75 ?  155 VAL   B N    1 
ATOM   6845 C CA   . VAL   B 1 155 ? 45.604 -31.395 -8.071  1.00 12.08 ?  155 VAL   B CA   1 
ATOM   6846 C C    . VAL   B 1 155 ? 46.947 -32.063 -8.338  1.00 11.92 ?  155 VAL   B C    1 
ATOM   6847 O O    . VAL   B 1 155 ? 47.192 -32.552 -9.448  1.00 13.52 ?  155 VAL   B O    1 
ATOM   6848 C CB   . VAL   B 1 155 ? 44.444 -32.385 -8.277  1.00 13.75 ?  155 VAL   B CB   1 
ATOM   6849 C CG1  . VAL   B 1 155 ? 44.613 -33.596 -7.360  1.00 13.63 ?  155 VAL   B CG1  1 
ATOM   6850 C CG2  . VAL   B 1 155 ? 43.098 -31.702 -8.025  1.00 14.63 ?  155 VAL   B CG2  1 
ATOM   6851 H H    . VAL   B 1 155 ? 45.530 -30.456 -9.797  1.00 14.15 ?  155 VAL   B H    1 
ATOM   6852 H HA   . VAL   B 1 155 ? 45.586 -31.101 -7.153  1.00 14.55 ?  155 VAL   B HA   1 
ATOM   6853 H HB   . VAL   B 1 155 ? 44.450 -32.703 -9.194  1.00 16.56 ?  155 VAL   B HB   1 
ATOM   6854 H HG11 . VAL   B 1 155 ? 43.786 -34.109 -7.354  1.00 16.42 ?  155 VAL   B HG11 1 
ATOM   6855 H HG12 . VAL   B 1 155 ? 45.337 -34.152 -7.692  1.00 16.42 ?  155 VAL   B HG12 1 
ATOM   6856 H HG13 . VAL   B 1 155 ? 44.814 -33.290 -6.462  1.00 16.42 ?  155 VAL   B HG13 1 
ATOM   6857 H HG21 . VAL   B 1 155 ? 42.385 -32.352 -8.123  1.00 17.61 ?  155 VAL   B HG21 1 
ATOM   6858 H HG22 . VAL   B 1 155 ? 43.091 -31.338 -7.125  1.00 17.61 ?  155 VAL   B HG22 1 
ATOM   6859 H HG23 . VAL   B 1 155 ? 42.981 -30.985 -8.670  1.00 17.61 ?  155 VAL   B HG23 1 
ATOM   6860 N N    . PHE   B 1 156 ? 47.806 -32.100 -7.314  1.00 12.54 ?  156 PHE   B N    1 
ATOM   6861 C CA   . PHE   B 1 156 ? 49.184 -32.559 -7.498  1.00 13.59 ?  156 PHE   B CA   1 
ATOM   6862 C C    . PHE   B 1 156 ? 49.286 -34.057 -7.783  1.00 13.91 ?  156 PHE   B C    1 
ATOM   6863 O O    . PHE   B 1 156 ? 50.031 -34.481 -8.677  1.00 15.70 ?  156 PHE   B O    1 
ATOM   6864 C CB   . PHE   B 1 156 ? 50.003 -32.208 -6.258  1.00 14.23 ?  156 PHE   B CB   1 
ATOM   6865 C CG   . PHE   B 1 156 ? 51.430 -32.668 -6.317  1.00 14.54 ?  156 PHE   B CG   1 
ATOM   6866 C CD1  . PHE   B 1 156 ? 52.315 -32.123 -7.228  1.00 16.59 ?  156 PHE   B CD1  1 
ATOM   6867 C CD2  . PHE   B 1 156 ? 51.894 -33.629 -5.446  1.00 14.88 ?  156 PHE   B CD2  1 
ATOM   6868 C CE1  . PHE   B 1 156 ? 53.645 -32.521 -7.274  1.00 17.34 ?  156 PHE   B CE1  1 
ATOM   6869 C CE2  . PHE   B 1 156 ? 53.221 -34.041 -5.488  1.00 15.90 ?  156 PHE   B CE2  1 
ATOM   6870 C CZ   . PHE   B 1 156 ? 54.086 -33.488 -6.410  1.00 16.78 ?  156 PHE   B CZ   1 
ATOM   6871 H H    . PHE   B 1 156 ? 47.611 -31.860 -6.506  1.00 15.10 ?  156 PHE   B H    1 
ATOM   6872 H HA   . PHE   B 1 156 ? 49.567 -32.084 -8.246  1.00 16.37 ?  156 PHE   B HA   1 
ATOM   6873 H HB2  . PHE   B 1 156 ? 50.010 -31.245 -6.151  1.00 17.14 ?  156 PHE   B HB2  1 
ATOM   6874 H HB3  . PHE   B 1 156 ? 49.591 -32.621 -5.481  1.00 17.14 ?  156 PHE   B HB3  1 
ATOM   6875 H HD1  . PHE   B 1 156 ? 52.008 -31.464 -7.815  1.00 19.96 ?  156 PHE   B HD1  1 
ATOM   6876 H HD2  . PHE   B 1 156 ? 51.318 -34.010 -4.822  1.00 17.92 ?  156 PHE   B HD2  1 
ATOM   6877 H HE1  . PHE   B 1 156 ? 54.215 -32.144 -7.901  1.00 20.86 ?  156 PHE   B HE1  1 
ATOM   6878 H HE2  . PHE   B 1 156 ? 53.525 -34.699 -4.898  1.00 19.14 ?  156 PHE   B HE2  1 
ATOM   6879 H HZ   . PHE   B 1 156 ? 54.974 -33.767 -6.439  1.00 20.19 ?  156 PHE   B HZ   1 
ATOM   6880 N N    . ASP   B 1 157 ? 48.607 -34.881 -6.995  1.00 14.18 ?  157 ASP   B N    1 
ATOM   6881 C CA   . ASP   B 1 157 ? 48.760 -36.330 -7.092  1.00 15.23 ?  157 ASP   B CA   1 
ATOM   6882 C C    . ASP   B 1 157 ? 47.848 -36.872 -8.186  1.00 15.03 ?  157 ASP   B C    1 
ATOM   6883 O O    . ASP   B 1 157 ? 46.623 -36.756 -8.089  1.00 14.52 ?  157 ASP   B O    1 
ATOM   6884 C CB   . ASP   B 1 157 ? 48.403 -36.949 -5.747  1.00 16.57 ?  157 ASP   B CB   1 
ATOM   6885 C CG   . ASP   B 1 157 ? 48.532 -38.459 -5.738  1.00 18.51 ?  157 ASP   B CG   1 
ATOM   6886 O OD1  . ASP   B 1 157 ? 48.874 -39.062 -6.781  1.00 19.04 ?  157 ASP   B OD1  1 
ATOM   6887 O OD2  . ASP   B 1 157 ? 48.287 -39.043 -4.665  1.00 20.90 -1 157 ASP   B OD2  1 
ATOM   6888 H H    . ASP   B 1 157 ? 48.050 -34.625 -6.396  1.00 17.07 ?  157 ASP   B H    1 
ATOM   6889 H HA   . ASP   B 1 157 ? 49.677 -36.552 -7.311  1.00 18.34 ?  157 ASP   B HA   1 
ATOM   6890 H HB2  . ASP   B 1 157 ? 48.992 -36.590 -5.071  1.00 19.94 ?  157 ASP   B HB2  1 
ATOM   6891 H HB3  . ASP   B 1 157 ? 47.481 -36.730 -5.534  1.00 19.94 ?  157 ASP   B HB3  1 
ATOM   6892 N N    . LYS   B 1 158 ? 48.449 -37.489 -9.212  1.00 16.12 ?  158 LYS   B N    1 
ATOM   6893 C CA   . LYS   B 1 158 ? 47.674 -38.102 -10.294 1.00 16.72 ?  158 LYS   B CA   1 
ATOM   6894 C C    . LYS   B 1 158 ? 46.620 -39.073 -9.766  1.00 16.73 ?  158 LYS   B C    1 
ATOM   6895 O O    . LYS   B 1 158 ? 45.519 -39.162 -10.318 1.00 17.12 ?  158 LYS   B O    1 
ATOM   6896 C CB   . LYS   B 1 158 ? 48.620 -38.811 -11.273 1.00 18.27 ?  158 LYS   B CB   1 
ATOM   6897 C CG   . LYS   B 1 158 ? 47.931 -39.680 -12.320 1.00 20.50 ?  158 LYS   B CG   1 
ATOM   6898 C CD   . LYS   B 1 158 ? 47.079 -38.873 -13.274 1.00 22.87 ?  158 LYS   B CD   1 
ATOM   6899 C CE   . LYS   B 1 158 ? 46.487 -39.774 -14.346 1.00 24.47 ?  158 LYS   B CE   1 
ATOM   6900 N NZ   . LYS   B 1 158 ? 45.416 -39.093 -15.130 1.00 24.26 ?  158 LYS   B NZ   1 
ATOM   6901 H H    . LYS   B 1 158 ? 49.305 -37.562 -9.307  1.00 19.40 ?  158 LYS   B H    1 
ATOM   6902 H HA   . LYS   B 1 158 ? 47.217 -37.408 -10.790 1.00 20.12 ?  158 LYS   B HA   1 
ATOM   6903 H HB2  . LYS   B 1 158 ? 49.138 -38.142 -11.754 1.00 21.99 ?  158 LYS   B HB2  1 
ATOM   6904 H HB3  . LYS   B 1 158 ? 49.223 -39.384 -10.772 1.00 21.99 ?  158 LYS   B HB3  1 
ATOM   6905 H HG2  . LYS   B 1 158 ? 48.611 -40.136 -12.844 1.00 24.66 ?  158 LYS   B HG2  1 
ATOM   6906 H HG3  . LYS   B 1 158 ? 47.366 -40.339 -11.884 1.00 24.66 ?  158 LYS   B HG3  1 
ATOM   6907 H HD2  . LYS   B 1 158 ? 46.353 -38.455 -12.786 1.00 27.51 ?  158 LYS   B HD2  1 
ATOM   6908 H HD3  . LYS   B 1 158 ? 47.628 -38.201 -13.709 1.00 27.51 ?  158 LYS   B HD3  1 
ATOM   6909 H HE2  . LYS   B 1 158 ? 47.184 -40.042 -14.961 1.00 29.42 ?  158 LYS   B HE2  1 
ATOM   6910 H HE3  . LYS   B 1 158 ? 46.095 -40.557 -13.924 1.00 29.42 ?  158 LYS   B HE3  1 
ATOM   6911 H HZ1  . LYS   B 1 158 ? 45.088 -39.644 -15.746 1.00 29.17 ?  158 LYS   B HZ1  1 
ATOM   6912 H HZ2  . LYS   B 1 158 ? 44.755 -38.839 -14.589 1.00 29.17 ?  158 LYS   B HZ2  1 
ATOM   6913 H HZ3  . LYS   B 1 158 ? 45.748 -38.372 -15.535 1.00 29.17 ?  158 LYS   B HZ3  1 
ATOM   6914 N N    . ASN   B 1 159 ? 46.938 -39.826 -8.713  1.00 17.15 ?  159 ASN   B N    1 
ATOM   6915 C CA   . ASN   B 1 159 ? 45.977 -40.803 -8.212  1.00 17.64 ?  159 ASN   B CA   1 
ATOM   6916 C C    . ASN   B 1 159 ? 44.774 -40.130 -7.555  1.00 16.56 ?  159 ASN   B C    1 
ATOM   6917 O O    . ASN   B 1 159 ? 43.641 -40.613 -7.683  1.00 17.00 ?  159 ASN   B O    1 
ATOM   6918 C CB   . ASN   B 1 159 ? 46.670 -41.773 -7.267  1.00 18.94 ?  159 ASN   B CB   1 
ATOM   6919 C CG   . ASN   B 1 159 ? 47.701 -42.621 -7.977  1.00 20.99 ?  159 ASN   B CG   1 
ATOM   6920 O OD1  . ASN   B 1 159 ? 47.452 -43.133 -9.073  1.00 22.41 ?  159 ASN   B OD1  1 
ATOM   6921 N ND2  . ASN   B 1 159 ? 48.868 -42.771 -7.366  1.00 21.78 ?  159 ASN   B ND2  1 
ATOM   6922 H H    . ASN   B 1 159 ? 47.680 -39.784 -8.283  1.00 20.64 ?  159 ASN   B H    1 
ATOM   6923 H HA   . ASN   B 1 159 ? 45.643 -41.313 -8.962  1.00 21.22 ?  159 ASN   B HA   1 
ATOM   6924 H HB2  . ASN   B 1 159 ? 47.122 -41.280 -6.569  1.00 22.79 ?  159 ASN   B HB2  1 
ATOM   6925 H HB3  . ASN   B 1 159 ? 46.007 -42.369 -6.881  1.00 22.79 ?  159 ASN   B HB3  1 
ATOM   6926 H HD21 . ASN   B 1 159 ? 49.488 -43.254 -7.728  1.00 26.19 ?  159 ASN   B HD21 1 
ATOM   6927 H HD22 . ASN   B 1 159 ? 49.003 -42.412 -6.598  1.00 26.19 ?  159 ASN   B HD22 1 
ATOM   6928 N N    . LEU   B 1 160 ? 44.983 -39.000 -6.869  1.00 15.80 ?  160 LEU   B N    1 
ATOM   6929 C CA   . LEU   B 1 160 ? 43.848 -38.261 -6.327  1.00 14.99 ?  160 LEU   B CA   1 
ATOM   6930 C C    . LEU   B 1 160 ? 43.066 -37.594 -7.445  1.00 14.57 ?  160 LEU   B C    1 
ATOM   6931 O O    . LEU   B 1 160 ? 41.829 -37.593 -7.434  1.00 14.34 ?  160 LEU   B O    1 
ATOM   6932 C CB   . LEU   B 1 160 ? 44.306 -37.226 -5.298  1.00 14.76 ?  160 LEU   B CB   1 
ATOM   6933 C CG   . LEU   B 1 160 ? 43.183 -36.335 -4.755  1.00 14.58 ?  160 LEU   B CG   1 
ATOM   6934 C CD1  . LEU   B 1 160 ? 42.060 -37.149 -4.125  1.00 15.37 ?  160 LEU   B CD1  1 
ATOM   6935 C CD2  . LEU   B 1 160 ? 43.730 -35.325 -3.755  1.00 14.87 ?  160 LEU   B CD2  1 
ATOM   6936 H H    . LEU   B 1 160 ? 45.758 -38.646 -6.713  1.00 19.01 ?  160 LEU   B H    1 
ATOM   6937 H HA   . LEU   B 1 160 ? 43.263 -38.886 -5.878  1.00 18.04 ?  160 LEU   B HA   1 
ATOM   6938 H HB2  . LEU   B 1 160 ? 44.708 -37.688 -4.544  1.00 17.77 ?  160 LEU   B HB2  1 
ATOM   6939 H HB3  . LEU   B 1 160 ? 44.970 -36.646 -5.710  1.00 17.77 ?  160 LEU   B HB3  1 
ATOM   6940 H HG   . LEU   B 1 160 ? 42.803 -35.830 -5.489  1.00 17.55 ?  160 LEU   B HG   1 
ATOM   6941 H HD11 . LEU   B 1 160 ? 41.421 -36.545 -3.720  1.00 18.50 ?  160 LEU   B HD11 1 
ATOM   6942 H HD12 . LEU   B 1 160 ? 41.625 -37.676 -4.815  1.00 18.50 ?  160 LEU   B HD12 1 
ATOM   6943 H HD13 . LEU   B 1 160 ? 42.435 -37.737 -3.449  1.00 18.50 ?  160 LEU   B HD13 1 
ATOM   6944 H HD21 . LEU   B 1 160 ? 43.003 -34.758 -3.447  1.00 17.90 ?  160 LEU   B HD21 1 
ATOM   6945 H HD22 . LEU   B 1 160 ? 44.122 -35.797 -3.005  1.00 17.90 ?  160 LEU   B HD22 1 
ATOM   6946 H HD23 . LEU   B 1 160 ? 44.406 -34.779 -4.192  1.00 17.90 ?  160 LEU   B HD23 1 
ATOM   6947 N N    . TYR   B 1 161 ? 43.771 -37.026 -8.423  1.00 14.65 ?  161 TYR   B N    1 
ATOM   6948 C CA   . TYR   B 1 161 ? 43.098 -36.454 -9.581  1.00 14.30 ?  161 TYR   B CA   1 
ATOM   6949 C C    . TYR   B 1 161 ? 42.164 -37.474 -10.214 1.00 14.05 ?  161 TYR   B C    1 
ATOM   6950 O O    . TYR   B 1 161 ? 40.998 -37.174 -10.493 1.00 14.09 ?  161 TYR   B O    1 
ATOM   6951 C CB   . TYR   B 1 161 ? 44.149 -35.968 -10.585 1.00 14.88 ?  161 TYR   B CB   1 
ATOM   6952 C CG   . TYR   B 1 161 ? 43.583 -35.503 -11.901 1.00 15.36 ?  161 TYR   B CG   1 
ATOM   6953 C CD1  . TYR   B 1 161 ? 43.211 -34.178 -12.084 1.00 15.32 ?  161 TYR   B CD1  1 
ATOM   6954 C CD2  . TYR   B 1 161 ? 43.394 -36.389 -12.958 1.00 15.83 ?  161 TYR   B CD2  1 
ATOM   6955 C CE1  . TYR   B 1 161 ? 42.685 -33.747 -13.276 1.00 16.01 ?  161 TYR   B CE1  1 
ATOM   6956 C CE2  . TYR   B 1 161 ? 42.864 -35.963 -14.155 1.00 16.63 ?  161 TYR   B CE2  1 
ATOM   6957 C CZ   . TYR   B 1 161 ? 42.511 -34.640 -14.309 1.00 16.45 ?  161 TYR   B CZ   1 
ATOM   6958 O OH   . TYR   B 1 161 ? 41.978 -34.203 -15.493 1.00 18.20 ?  161 TYR   B OH   1 
ATOM   6959 H H    . TYR   B 1 161 ? 44.628 -36.964 -8.438  1.00 17.64 ?  161 TYR   B H    1 
ATOM   6960 H HA   . TYR   B 1 161 ? 42.568 -35.690 -9.298  1.00 17.22 ?  161 TYR   B HA   1 
ATOM   6961 H HB2  . TYR   B 1 161 ? 44.630 -35.220 -10.192 1.00 17.91 ?  161 TYR   B HB2  1 
ATOM   6962 H HB3  . TYR   B 1 161 ? 44.761 -36.692 -10.769 1.00 17.91 ?  161 TYR   B HB3  1 
ATOM   6963 H HD1  . TYR   B 1 161 ? 43.335 -33.562 -11.396 1.00 18.44 ?  161 TYR   B HD1  1 
ATOM   6964 H HD2  . TYR   B 1 161 ? 43.621 -37.281 -12.856 1.00 19.05 ?  161 TYR   B HD2  1 
ATOM   6965 H HE1  . TYR   B 1 161 ? 42.457 -32.847 -13.388 1.00 19.27 ?  161 TYR   B HE1  1 
ATOM   6966 H HE2  . TYR   B 1 161 ? 42.738 -36.561 -14.856 1.00 20.02 ?  161 TYR   B HE2  1 
ATOM   6967 H HH   . TYR   B 1 161 ? 41.929 -34.845 -16.036 1.00 21.90 ?  161 TYR   B HH   1 
ATOM   6968 N N    . ASP   B 1 162 ? 42.660 -38.697 -10.432 1.00 14.49 ?  162 ASP   B N    1 
ATOM   6969 C CA   . ASP   B 1 162 ? 41.837 -39.730 -11.052 1.00 14.88 ?  162 ASP   B CA   1 
ATOM   6970 C C    . ASP   B 1 162 ? 40.625 -40.062 -10.192 1.00 14.47 ?  162 ASP   B C    1 
ATOM   6971 O O    . ASP   B 1 162 ? 39.523 -40.285 -10.714 1.00 15.07 ?  162 ASP   B O    1 
ATOM   6972 C CB   . ASP   B 1 162 ? 42.671 -40.987 -11.311 1.00 16.36 ?  162 ASP   B CB   1 
ATOM   6973 C CG   . ASP   B 1 162 ? 43.668 -40.817 -12.443 1.00 17.47 ?  162 ASP   B CG   1 
ATOM   6974 O OD1  . ASP   B 1 162 ? 43.540 -39.868 -13.245 1.00 17.99 ?  162 ASP   B OD1  1 
ATOM   6975 O OD2  . ASP   B 1 162 ? 44.573 -41.670 -12.544 1.00 19.19 -1 162 ASP   B OD2  1 
ATOM   6976 H H    . ASP   B 1 162 ? 43.464 -38.947 -10.233 1.00 17.45 ?  162 ASP   B H    1 
ATOM   6977 H HA   . ASP   B 1 162 ? 41.516 -39.402 -11.903 1.00 17.92 ?  162 ASP   B HA   1 
ATOM   6978 H HB2  . ASP   B 1 162 ? 43.164 -41.209 -10.507 1.00 19.68 ?  162 ASP   B HB2  1 
ATOM   6979 H HB3  . ASP   B 1 162 ? 42.073 -41.713 -11.546 1.00 19.68 ?  162 ASP   B HB3  1 
ATOM   6980 N N    A LYS   B 1 163 ? 40.803 -40.116 -8.870  0.40 14.71 ?  163 LYS   B N    1 
ATOM   6981 N N    B LYS   B 1 163 ? 40.811 -40.137 -8.874  0.60 13.93 ?  163 LYS   B N    1 
ATOM   6982 C CA   A LYS   B 1 163 ? 39.676 -40.417 -7.992  0.40 15.40 ?  163 LYS   B CA   1 
ATOM   6983 C CA   B LYS   B 1 163 ? 39.682 -40.412 -7.993  0.60 14.24 ?  163 LYS   B CA   1 
ATOM   6984 C C    A LYS   B 1 163 ? 38.633 -39.305 -8.027  0.40 14.22 ?  163 LYS   B C    1 
ATOM   6985 C C    B LYS   B 1 163 ? 38.635 -39.309 -8.082  0.60 13.61 ?  163 LYS   B C    1 
ATOM   6986 O O    A LYS   B 1 163 ? 37.425 -39.573 -7.979  0.40 14.74 ?  163 LYS   B O    1 
ATOM   6987 O O    B LYS   B 1 163 ? 37.428 -39.583 -8.147  0.60 14.06 ?  163 LYS   B O    1 
ATOM   6988 C CB   A LYS   B 1 163 ? 40.162 -40.640 -6.562  0.40 17.93 ?  163 LYS   B CB   1 
ATOM   6989 C CB   B LYS   B 1 163 ? 40.164 -40.580 -6.553  0.60 16.32 ?  163 LYS   B CB   1 
ATOM   6990 C CG   A LYS   B 1 163 ? 39.085 -41.189 -5.644  0.40 21.41 ?  163 LYS   B CG   1 
ATOM   6991 C CG   B LYS   B 1 163 ? 39.068 -41.001 -5.596  0.60 20.40 ?  163 LYS   B CG   1 
ATOM   6992 C CD   A LYS   B 1 163 ? 39.507 -41.179 -4.187  0.40 24.45 ?  163 LYS   B CD   1 
ATOM   6993 C CD   B LYS   B 1 163 ? 39.630 -41.515 -4.281  0.60 24.26 ?  163 LYS   B CD   1 
ATOM   6994 C CE   A LYS   B 1 163 ? 38.433 -41.814 -3.316  0.40 26.51 ?  163 LYS   B CE   1 
ATOM   6995 C CE   B LYS   B 1 163 ? 38.552 -42.220 -3.467  0.60 26.90 ?  163 LYS   B CE   1 
ATOM   6996 N NZ   A LYS   B 1 163 ? 38.603 -41.493 -1.873  0.40 27.72 ?  163 LYS   B NZ   1 
ATOM   6997 N NZ   B LYS   B 1 163 ? 38.317 -41.575 -2.144  0.60 28.37 ?  163 LYS   B NZ   1 
ATOM   6998 H H    A LYS   B 1 163 ? 41.551 -39.987 -8.465  0.40 17.70 ?  163 LYS   B H    1 
ATOM   6999 H H    B LYS   B 1 163 ? 41.567 -40.036 -8.473  0.60 16.78 ?  163 LYS   B H    1 
ATOM   7000 H HA   A LYS   B 1 163 ? 39.249 -41.234 -8.293  0.40 18.54 ?  163 LYS   B HA   1 
ATOM   7001 H HA   B LYS   B 1 163 ? 39.264 -41.244 -8.268  0.60 17.14 ?  163 LYS   B HA   1 
ATOM   7002 H HB2  A LYS   B 1 163 ? 40.895 -41.278 -6.574  0.40 21.58 ?  163 LYS   B HB2  1 
ATOM   7003 H HB2  B LYS   B 1 163 ? 40.856 -41.264 -6.532  0.60 19.64 ?  163 LYS   B HB2  1 
ATOM   7004 H HB3  A LYS   B 1 163 ? 40.466 -39.796 -6.195  0.40 21.58 ?  163 LYS   B HB3  1 
ATOM   7005 H HB3  B LYS   B 1 163 ? 40.525 -39.738 -6.241  0.60 19.64 ?  163 LYS   B HB3  1 
ATOM   7006 H HG2  A LYS   B 1 163 ? 38.286 -40.645 -5.726  0.40 25.75 ?  163 LYS   B HG2  1 
ATOM   7007 H HG2  B LYS   B 1 163 ? 38.500 -40.240 -5.405  0.60 24.54 ?  163 LYS   B HG2  1 
ATOM   7008 H HG3  A LYS   B 1 163 ? 38.890 -42.106 -5.895  0.40 25.75 ?  163 LYS   B HG3  1 
ATOM   7009 H HG3  B LYS   B 1 163 ? 38.547 -41.714 -6.001  0.60 24.54 ?  163 LYS   B HG3  1 
ATOM   7010 H HD2  A LYS   B 1 163 ? 40.326 -41.690 -4.084  0.40 29.40 ?  163 LYS   B HD2  1 
ATOM   7011 H HD2  B LYS   B 1 163 ? 40.342 -42.149 -4.460  0.60 29.17 ?  163 LYS   B HD2  1 
ATOM   7012 H HD3  A LYS   B 1 163 ? 39.640 -40.264 -3.894  0.40 29.40 ?  163 LYS   B HD3  1 
ATOM   7013 H HD3  B LYS   B 1 163 ? 39.966 -40.768 -3.762  0.60 29.17 ?  163 LYS   B HD3  1 
ATOM   7014 H HE2  A LYS   B 1 163 ? 37.560 -41.502 -3.600  0.40 31.87 ?  163 LYS   B HE2  1 
ATOM   7015 H HE2  B LYS   B 1 163 ? 37.717 -42.202 -3.961  0.60 32.34 ?  163 LYS   B HE2  1 
ATOM   7016 H HE3  A LYS   B 1 163 ? 38.481 -42.777 -3.415  0.40 31.87 ?  163 LYS   B HE3  1 
ATOM   7017 H HE3  B LYS   B 1 163 ? 38.824 -43.138 -3.310  0.60 32.34 ?  163 LYS   B HE3  1 
ATOM   7018 H HZ1  A LYS   B 1 163 ? 37.956 -41.879 -1.398  0.40 33.32 ?  163 LYS   B HZ1  1 
ATOM   7019 H HZ1  B LYS   B 1 163 ? 37.683 -42.015 -1.700  0.60 34.11 ?  163 LYS   B HZ1  1 
ATOM   7020 H HZ2  A LYS   B 1 163 ? 39.390 -41.791 -1.587  0.40 33.32 ?  163 LYS   B HZ2  1 
ATOM   7021 H HZ2  B LYS   B 1 163 ? 39.066 -41.586 -1.664  0.60 34.11 ?  163 LYS   B HZ2  1 
ATOM   7022 H HZ3  A LYS   B 1 163 ? 38.564 -40.612 -1.750  0.40 33.32 ?  163 LYS   B HZ3  1 
ATOM   7023 H HZ3  B LYS   B 1 163 ? 38.058 -40.732 -2.258  0.60 34.11 ?  163 LYS   B HZ3  1 
ATOM   7024 N N    . LEU   B 1 164 ? 39.084 -38.052 -8.107  1.00 13.05 ?  164 LEU   B N    1 
ATOM   7025 C CA   . LEU   B 1 164 ? 38.166 -36.920 -8.159  1.00 13.15 ?  164 LEU   B CA   1 
ATOM   7026 C C    . LEU   B 1 164 ? 37.387 -36.897 -9.468  1.00 13.29 ?  164 LEU   B C    1 
ATOM   7027 O O    . LEU   B 1 164 ? 36.163 -36.703 -9.473  1.00 14.18 ?  164 LEU   B O    1 
ATOM   7028 C CB   . LEU   B 1 164 ? 38.967 -35.626 -7.999  1.00 12.88 ?  164 LEU   B CB   1 
ATOM   7029 C CG   . LEU   B 1 164 ? 39.501 -35.354 -6.598  1.00 13.41 ?  164 LEU   B CG   1 
ATOM   7030 C CD1  . LEU   B 1 164 ? 40.596 -34.304 -6.646  1.00 13.86 ?  164 LEU   B CD1  1 
ATOM   7031 C CD2  . LEU   B 1 164 ? 38.383 -34.913 -5.671  1.00 15.51 ?  164 LEU   B CD2  1 
ATOM   7032 H H    A LEU   B 1 164 ? 39.919 -37.834 -8.137  0.40 15.72 ?  164 LEU   B H    1 
ATOM   7033 H H    B LEU   B 1 164 ? 39.918 -37.831 -8.095  0.60 15.72 ?  164 LEU   B H    1 
ATOM   7034 H HA   . LEU   B 1 164 ? 37.537 -36.981 -7.427  1.00 15.84 ?  164 LEU   B HA   1 
ATOM   7035 H HB2  . LEU   B 1 164 ? 39.734 -35.661 -8.596  1.00 15.51 ?  164 LEU   B HB2  1 
ATOM   7036 H HB3  . LEU   B 1 164 ? 38.403 -34.879 -8.243  1.00 15.51 ?  164 LEU   B HB3  1 
ATOM   7037 H HG   . LEU   B 1 164 ? 39.891 -36.163 -6.237  1.00 16.15 ?  164 LEU   B HG   1 
ATOM   7038 H HD11 . LEU   B 1 164 ? 40.919 -34.132 -5.745  1.00 16.69 ?  164 LEU   B HD11 1 
ATOM   7039 H HD12 . LEU   B 1 164 ? 41.328 -34.630 -7.197  1.00 16.69 ?  164 LEU   B HD12 1 
ATOM   7040 H HD13 . LEU   B 1 164 ? 40.240 -33.485 -7.027  1.00 16.69 ?  164 LEU   B HD13 1 
ATOM   7041 H HD21 . LEU   B 1 164 ? 38.755 -34.692 -4.802  1.00 18.67 ?  164 LEU   B HD21 1 
ATOM   7042 H HD22 . LEU   B 1 164 ? 37.944 -34.135 -6.048  1.00 18.67 ?  164 LEU   B HD22 1 
ATOM   7043 H HD23 . LEU   B 1 164 ? 37.747 -35.640 -5.581  1.00 18.67 ?  164 LEU   B HD23 1 
ATOM   7044 N N    . VAL   B 1 165 ? 38.080 -37.065 -10.594 1.00 14.03 ?  165 VAL   B N    1 
ATOM   7045 C CA   . VAL   B 1 165 ? 37.428 -36.994 -11.899 1.00 14.80 ?  165 VAL   B CA   1 
ATOM   7046 C C    . VAL   B 1 165 ? 36.521 -38.198 -12.103 1.00 16.22 ?  165 VAL   B C    1 
ATOM   7047 O O    . VAL   B 1 165 ? 35.365 -38.065 -12.529 1.00 17.10 ?  165 VAL   B O    1 
ATOM   7048 C CB   . VAL   B 1 165 ? 38.480 -36.886 -13.019 1.00 15.79 ?  165 VAL   B CB   1 
ATOM   7049 C CG1  . VAL   B 1 165 ? 37.818 -36.985 -14.370 1.00 17.00 ?  165 VAL   B CG1  1 
ATOM   7050 C CG2  . VAL   B 1 165 ? 39.268 -35.601 -12.896 1.00 16.07 ?  165 VAL   B CG2  1 
ATOM   7051 H H    . VAL   B 1 165 ? 38.928 -37.219 -10.624 1.00 16.89 ?  165 VAL   B H    1 
ATOM   7052 H HA   . VAL   B 1 165 ? 36.877 -36.198 -11.929 1.00 17.82 ?  165 VAL   B HA   1 
ATOM   7053 H HB   . VAL   B 1 165 ? 39.107 -37.622 -12.931 1.00 19.01 ?  165 VAL   B HB   1 
ATOM   7054 H HG11 . VAL   B 1 165 ? 38.432 -36.670 -15.043 1.00 20.46 ?  165 VAL   B HG11 1 
ATOM   7055 H HG12 . VAL   B 1 165 ? 37.593 -37.916 -14.538 1.00 20.46 ?  165 VAL   B HG12 1 
ATOM   7056 H HG13 . VAL   B 1 165 ? 37.014 -36.446 -14.365 1.00 20.46 ?  165 VAL   B HG13 1 
ATOM   7057 H HG21 . VAL   B 1 165 ? 39.907 -35.548 -13.624 1.00 19.34 ?  165 VAL   B HG21 1 
ATOM   7058 H HG22 . VAL   B 1 165 ? 38.655 -34.847 -12.941 1.00 19.34 ?  165 VAL   B HG22 1 
ATOM   7059 H HG23 . VAL   B 1 165 ? 39.737 -35.590 -12.045 1.00 19.34 ?  165 VAL   B HG23 1 
ATOM   7060 N N    . SER   B 1 166 ? 37.035 -39.394 -11.796 1.00 16.93 ?  166 SER   B N    1 
ATOM   7061 C CA   . SER   B 1 166 ? 36.285 -40.611 -12.074 1.00 17.88 ?  166 SER   B CA   1 
ATOM   7062 C C    . SER   B 1 166 ? 35.022 -40.697 -11.232 1.00 18.11 ?  166 SER   B C    1 
ATOM   7063 O O    . SER   B 1 166 ? 34.049 -41.317 -11.663 1.00 19.50 ?  166 SER   B O    1 
ATOM   7064 C CB   . SER   B 1 166 ? 37.156 -41.864 -11.893 1.00 18.60 ?  166 SER   B CB   1 
ATOM   7065 O OG   . SER   B 1 166 ? 37.505 -42.076 -10.535 1.00 18.55 ?  166 SER   B OG   1 
ATOM   7066 H H    . SER   B 1 166 ? 37.809 -39.520 -11.432 1.00 20.37 ?  166 SER   B H    1 
ATOM   7067 H HA   . SER   B 1 166 ? 36.012 -40.589 -13.002 1.00 21.51 ?  166 SER   B HA   1 
ATOM   7068 H HB2  . SER   B 1 166 ? 36.662 -42.634 -12.216 1.00 22.38 ?  166 SER   B HB2  1 
ATOM   7069 H HB3  . SER   B 1 166 ? 37.971 -41.758 -12.412 1.00 22.38 ?  166 SER   B HB3  1 
ATOM   7070 H HG   . SER   B 1 166 ? 37.937 -41.420 -10.245 1.00 22.32 ?  166 SER   B HG   1 
ATOM   7071 N N    . SER   B 1 167 ? 35.005 -40.094 -10.044 1.00 17.00 ?  167 SER   B N    1 
ATOM   7072 C CA   . SER   B 1 167 ? 33.849 -40.155 -9.157  1.00 16.71 ?  167 SER   B CA   1 
ATOM   7073 C C    . SER   B 1 167 ? 32.928 -38.939 -9.265  1.00 16.67 ?  167 SER   B C    1 
ATOM   7074 O O    . SER   B 1 167 ? 31.850 -38.937 -8.657  1.00 16.83 ?  167 SER   B O    1 
ATOM   7075 C CB   . SER   B 1 167 ? 34.286 -40.335 -7.696  1.00 16.52 ?  167 SER   B CB   1 
ATOM   7076 O OG   . SER   B 1 167 ? 34.943 -39.175 -7.202  1.00 16.35 ?  167 SER   B OG   1 
ATOM   7077 H H    . SER   B 1 167 ? 35.664 -39.638 -9.728  1.00 20.46 ?  167 SER   B H    1 
ATOM   7078 H HA   . SER   B 1 167 ? 33.328 -40.935 -9.397  1.00 20.11 ?  167 SER   B HA   1 
ATOM   7079 H HB2  . SER   B 1 167 ? 33.499 -40.505 -7.153  1.00 19.89 ?  167 SER   B HB2  1 
ATOM   7080 H HB3  . SER   B 1 167 ? 34.889 -41.098 -7.640  1.00 19.89 ?  167 SER   B HB3  1 
ATOM   7081 H HG   . SER   B 1 167 ? 35.636 -39.033 -7.659  1.00 19.68 ?  167 SER   B HG   1 
ATOM   7082 N N    . PHE   B 1 168 ? 33.306 -37.910 -10.025 1.00 16.75 ?  168 PHE   B N    1 
ATOM   7083 C CA   . PHE   B 1 168 ? 32.474 -36.707 -10.091 1.00 16.06 ?  168 PHE   B CA   1 
ATOM   7084 C C    . PHE   B 1 168 ? 31.150 -36.963 -10.809 1.00 14.23 ?  168 PHE   B C    1 
ATOM   7085 O O    . PHE   B 1 168 ? 30.123 -36.345 -10.473 1.00 15.49 ?  168 PHE   B O    1 
ATOM   7086 C CB   . PHE   B 1 168 ? 33.226 -35.578 -10.792 1.00 16.88 ?  168 PHE   B CB   1 
ATOM   7087 C CG   . PHE   B 1 168 ? 32.429 -34.320 -10.899 1.00 17.11 ?  168 PHE   B CG   1 
ATOM   7088 C CD1  . PHE   B 1 168 ? 32.125 -33.588 -9.761  1.00 18.55 ?  168 PHE   B CD1  1 
ATOM   7089 C CD2  . PHE   B 1 168 ? 31.962 -33.882 -12.119 1.00 16.49 ?  168 PHE   B CD2  1 
ATOM   7090 C CE1  . PHE   B 1 168 ? 31.374 -32.430 -9.841  1.00 19.27 ?  168 PHE   B CE1  1 
ATOM   7091 C CE2  . PHE   B 1 168 ? 31.221 -32.709 -12.216 1.00 17.90 ?  168 PHE   B CE2  1 
ATOM   7092 C CZ   . PHE   B 1 168 ? 30.918 -31.988 -11.074 1.00 18.51 ?  168 PHE   B CZ   1 
ATOM   7093 H H    . PHE   B 1 168 ? 34.027 -37.879 -10.496 1.00 20.16 ?  168 PHE   B H    1 
ATOM   7094 H HA   . PHE   B 1 168 ? 32.272 -36.418 -9.189  1.00 19.33 ?  168 PHE   B HA   1 
ATOM   7095 H HB2  . PHE   B 1 168 ? 34.033 -35.380 -10.290 1.00 20.31 ?  168 PHE   B HB2  1 
ATOM   7096 H HB3  . PHE   B 1 168 ? 33.456 -35.862 -11.689 1.00 20.31 ?  168 PHE   B HB3  1 
ATOM   7097 H HD1  . PHE   B 1 168 ? 32.423 -33.889 -8.931  1.00 22.32 ?  168 PHE   B HD1  1 
ATOM   7098 H HD2  . PHE   B 1 168 ? 32.165 -34.359 -12.888 1.00 19.85 ?  168 PHE   B HD2  1 
ATOM   7099 H HE1  . PHE   B 1 168 ? 31.171 -31.950 -9.069  1.00 23.18 ?  168 PHE   B HE1  1 
ATOM   7100 H HE2  . PHE   B 1 168 ? 30.913 -32.420 -13.045 1.00 21.54 ?  168 PHE   B HE2  1 
ATOM   7101 H HZ   . PHE   B 1 168 ? 30.412 -31.207 -11.135 1.00 22.27 ?  168 PHE   B HZ   1 
ATOM   7102 N N    A LEU   B 1 169 ? 31.157 -37.856 -11.790 0.40 14.43 ?  169 LEU   B N    1 
ATOM   7103 N N    B LEU   B 1 169 ? 31.152 -37.853 -11.801 0.60 14.38 ?  169 LEU   B N    1 
ATOM   7104 C CA   A LEU   B 1 169 ? 29.967 -38.178 -12.551 0.40 15.67 ?  169 LEU   B CA   1 
ATOM   7105 C CA   B LEU   B 1 169 ? 29.962 -38.116 -12.608 0.60 16.14 ?  169 LEU   B CA   1 
ATOM   7106 C C    A LEU   B 1 169 ? 30.020 -39.639 -12.954 0.40 16.64 ?  169 LEU   B C    1 
ATOM   7107 C C    B LEU   B 1 169 ? 29.919 -39.524 -13.214 0.60 17.37 ?  169 LEU   B C    1 
ATOM   7108 O O    A LEU   B 1 169 ? 29.002 -40.259 -13.257 0.40 17.29 ?  169 LEU   B O    1 
ATOM   7109 O O    B LEU   B 1 169 ? 29.128 -39.794 -14.125 0.60 17.99 ?  169 LEU   B O    1 
ATOM   7110 C CB   A LEU   B 1 169 ? 29.881 -37.298 -13.798 0.40 17.51 ?  169 LEU   B CB   1 
ATOM   7111 C CB   B LEU   B 1 169 ? 29.855 -37.077 -13.729 0.60 18.56 ?  169 LEU   B CB   1 
ATOM   7112 C CG   A LEU   B 1 169 ? 28.681 -36.353 -13.858 0.40 19.99 ?  169 LEU   B CG   1 
ATOM   7113 C CG   B LEU   B 1 169 ? 28.562 -36.257 -13.799 0.60 21.74 ?  169 LEU   B CG   1 
ATOM   7114 C CD1  A LEU   B 1 169 ? 28.658 -35.600 -15.176 0.40 20.81 ?  169 LEU   B CD1  1 
ATOM   7115 C CD1  B LEU   B 1 169 ? 28.516 -35.443 -15.085 0.60 22.76 ?  169 LEU   B CD1  1 
ATOM   7116 C CD2  A LEU   B 1 169 ? 27.383 -37.113 -13.655 0.40 20.42 ?  169 LEU   B CD2  1 
ATOM   7117 C CD2  B LEU   B 1 169 ? 27.339 -37.143 -13.679 0.60 22.26 ?  169 LEU   B CD2  1 
ATOM   7118 O OXT  A LEU   B 1 169 ? 31.104 -40.220 -12.981 0.40 16.77 -1 169 LEU   B OXT  1 
ATOM   7119 O OXT  B LEU   B 1 169 ? 30.659 -40.421 -12.812 0.60 18.35 -1 169 LEU   B OXT  1 
ATOM   7120 H H    A LEU   B 1 169 ? 31.852 -38.305 -12.036 0.40 17.37 ?  169 LEU   B H    1 
ATOM   7121 H H    B LEU   B 1 169 ? 31.839 -38.320 -12.033 0.60 17.31 ?  169 LEU   B H    1 
ATOM   7122 H HA   A LEU   B 1 169 ? 29.182 -38.025 -12.004 0.40 18.86 ?  169 LEU   B HA   1 
ATOM   7123 H HA   B LEU   B 1 169 ? 29.187 -38.031 -12.037 0.60 19.42 ?  169 LEU   B HA   1 
ATOM   7124 H HB2  A LEU   B 1 169 ? 30.681 -36.753 -13.841 0.40 21.07 ?  169 LEU   B HB2  1 
ATOM   7125 H HB2  B LEU   B 1 169 ? 30.587 -36.444 -13.630 0.60 22.33 ?  169 LEU   B HB2  1 
ATOM   7126 H HB3  A LEU   B 1 169 ? 29.835 -37.869 -14.580 0.40 21.07 ?  169 LEU   B HB3  1 
ATOM   7127 H HB3  B LEU   B 1 169 ? 29.947 -37.537 -14.577 0.60 22.33 ?  169 LEU   B HB3  1 
ATOM   7128 H HG   A LEU   B 1 169 ? 28.757 -35.699 -13.145 0.40 24.05 ?  169 LEU   B HG   1 
ATOM   7129 H HG   B LEU   B 1 169 ? 28.551 -35.632 -13.058 0.60 26.14 ?  169 LEU   B HG   1 
ATOM   7130 H HD11 A LEU   B 1 169 ? 27.900 -34.992 -15.179 0.40 25.02 ?  169 LEU   B HD11 1 
ATOM   7131 H HD11 B LEU   B 1 169 ? 27.697 -34.924 -15.101 0.60 27.37 ?  169 LEU   B HD11 1 
ATOM   7132 H HD12 A LEU   B 1 169 ? 29.483 -35.099 -15.266 0.40 25.02 ?  169 LEU   B HD12 1 
ATOM   7133 H HD12 B LEU   B 1 169 ? 29.284 -34.852 -15.114 0.60 27.37 ?  169 LEU   B HD12 1 
ATOM   7134 H HD13 A LEU   B 1 169 ? 28.574 -36.237 -15.901 0.40 25.02 ?  169 LEU   B HD13 1 
ATOM   7135 H HD13 B LEU   B 1 169 ? 28.537 -36.050 -15.843 0.60 27.37 ?  169 LEU   B HD13 1 
ATOM   7136 H HD21 A LEU   B 1 169 ? 26.653 -36.608 -14.041 0.40 24.56 ?  169 LEU   B HD21 1 
ATOM   7137 H HD21 B LEU   B 1 169 ? 26.563 -36.656 -13.993 0.60 26.77 ?  169 LEU   B HD21 1 
ATOM   7138 H HD22 A LEU   B 1 169 ? 27.454 -37.979 -14.089 0.40 24.56 ?  169 LEU   B HD22 1 
ATOM   7139 H HD22 B LEU   B 1 169 ? 27.472 -37.940 -14.217 0.60 26.77 ?  169 LEU   B HD22 1 
ATOM   7140 H HD23 A LEU   B 1 169 ? 27.236 -37.234 -12.704 0.40 24.56 ?  169 LEU   B HD23 1 
ATOM   7141 H HD23 B LEU   B 1 169 ? 27.222 -37.389 -12.749 0.60 26.77 ?  169 LEU   B HD23 1 
HETATM 7142 N N2   B A1BA5 C 2 .   ? 15.557 3.482   6.671   0.60 14.63 ?  201 A1BA5 A N2   1 
HETATM 7143 C C3   B A1BA5 C 2 .   ? 14.295 0.302   1.611   0.60 17.34 ?  201 A1BA5 A C3   1 
HETATM 7144 C C6   B A1BA5 C 2 .   ? 14.056 2.805   -0.659  0.60 18.31 ?  201 A1BA5 A C6   1 
HETATM 7145 C C9   B A1BA5 C 2 .   ? 14.737 1.382   3.902   0.60 14.29 ?  201 A1BA5 A C9   1 
HETATM 7146 C C12  B A1BA5 C 2 .   ? 15.522 4.501   5.739   0.60 14.94 ?  201 A1BA5 A C12  1 
HETATM 7147 C C14  B A1BA5 C 2 .   ? 14.944 0.084   5.824   0.60 13.92 ?  201 A1BA5 A C14  1 
HETATM 7148 C C1   B A1BA5 C 2 .   ? 13.045 -1.763  0.740   0.60 17.92 ?  201 A1BA5 A C1   1 
HETATM 7149 C C10  B A1BA5 C 2 .   ? 15.057 2.533   4.686   0.60 14.15 ?  201 A1BA5 A C10  1 
HETATM 7150 C C11  B A1BA5 C 2 .   ? 15.210 3.962   4.515   0.60 15.21 ?  201 A1BA5 A C11  1 
HETATM 7151 C C13  B A1BA5 C 2 .   ? 15.284 2.277   6.060   0.60 13.94 ?  201 A1BA5 A C13  1 
HETATM 7152 C C15  B A1BA5 C 2 .   ? 11.826 -0.050  2.099   0.60 17.75 ?  201 A1BA5 A C15  1 
HETATM 7153 C C2   B A1BA5 C 2 .   ? 13.184 -0.757  1.902   0.60 17.28 ?  201 A1BA5 A C2   1 
HETATM 7154 C C4   B A1BA5 C 2 .   ? 14.412 0.848   0.187   0.60 17.85 ?  201 A1BA5 A C4   1 
HETATM 7155 C C5   B A1BA5 C 2 .   ? 13.259 1.508   -0.588  0.60 18.76 ?  201 A1BA5 A C5   1 
HETATM 7156 C C7   B A1BA5 C 2 .   ? 15.080 2.203   0.309   0.60 17.45 ?  201 A1BA5 A C7   1 
HETATM 7157 C C8   B A1BA5 C 2 .   ? 15.086 2.559   1.784   0.60 17.51 ?  201 A1BA5 A C8   1 
HETATM 7158 N N1   B A1BA5 C 2 .   ? 14.484 1.442   2.520   0.60 16.26 ?  201 A1BA5 A N1   1 
HETATM 7159 N N3   B A1BA5 C 2 .   ? 15.238 1.067   6.666   0.60 13.82 ?  201 A1BA5 A N3   1 
HETATM 7160 N N4   B A1BA5 C 2 .   ? 14.701 0.172   4.517   0.60 14.43 ?  201 A1BA5 A N4   1 
HETATM 7161 O O1   B A1BA5 C 2 .   ? 13.374 -1.524  3.076   0.60 16.38 ?  201 A1BA5 A O1   1 
HETATM 7162 H H16  B A1BA5 C 2 .   ? 15.769 3.632   7.654   0.60 17.62 ?  201 A1BA5 A H16  1 
HETATM 7163 H H1   B A1BA5 C 2 .   ? 15.215 -0.255  1.788   0.60 20.86 ?  201 A1BA5 A H1   1 
HETATM 7164 H H10  B A1BA5 C 2 .   ? 13.523 3.661   -0.248  0.60 22.03 ?  201 A1BA5 A H10  1 
HETATM 7165 H H11  B A1BA5 C 2 .   ? 14.458 3.027   -1.649  0.60 22.03 ?  201 A1BA5 A H11  1 
HETATM 7166 H H15  B A1BA5 C 2 .   ? 15.709 5.530   6.028   0.60 17.99 ?  201 A1BA5 A H15  1 
HETATM 7167 H H17  B A1BA5 C 2 .   ? 14.884 -0.904  6.263   0.60 16.76 ?  201 A1BA5 A H17  1 
HETATM 7168 H H4   B A1BA5 C 2 .   ? 13.014 -1.266  -0.230  0.60 21.56 ?  201 A1BA5 A H4   1 
HETATM 7169 H H5   B A1BA5 C 2 .   ? 12.145 -2.362  0.822   0.60 21.56 ?  201 A1BA5 A H5   1 
HETATM 7170 H H6   B A1BA5 C 2 .   ? 13.882 -2.460  0.725   0.60 21.56 ?  201 A1BA5 A H6   1 
HETATM 7171 H H14  B A1BA5 C 2 .   ? 15.098 4.501   3.595   0.60 18.31 ?  201 A1BA5 A H14  1 
HETATM 7172 H H20  B A1BA5 C 2 .   ? 11.331 0.166   1.151   0.60 21.35 ?  201 A1BA5 A H20  1 
HETATM 7173 H H19  B A1BA5 C 2 .   ? 11.935 0.895   2.630   0.60 21.35 ?  201 A1BA5 A H19  1 
HETATM 7174 H H18  B A1BA5 C 2 .   ? 11.141 -0.671  2.681   0.60 21.35 ?  201 A1BA5 A H18  1 
HETATM 7175 H H2   B A1BA5 C 2 .   ? 14.972 0.183   -0.472  0.60 21.48 ?  201 A1BA5 A H2   1 
HETATM 7176 H H8   B A1BA5 C 2 .   ? 13.078 1.042   -1.560  0.60 22.57 ?  201 A1BA5 A H8   1 
HETATM 7177 H H9   B A1BA5 C 2 .   ? 12.326 1.610   -0.039  0.60 22.57 ?  201 A1BA5 A H9   1 
HETATM 7178 H H3   B A1BA5 C 2 .   ? 16.073 2.205   -0.139  0.60 21.00 ?  201 A1BA5 A H3   1 
HETATM 7179 H H13  B A1BA5 C 2 .   ? 14.562 3.492   1.955   0.60 21.07 ?  201 A1BA5 A H13  1 
HETATM 7180 H H12  B A1BA5 C 2 .   ? 16.106 2.702   2.144   0.60 21.07 ?  201 A1BA5 A H12  1 
HETATM 7181 H H7   B A1BA5 C 2 .   ? 12.639 -2.114  3.168   0.60 19.71 ?  201 A1BA5 A H7   1 
HETATM 7182 O O    . HOH   D 3 .   ? 34.605 -1.895  12.495  1.00 41.94 ?  301 HOH   A O    1 
HETATM 7183 O O    . HOH   D 3 .   ? 28.830 0.432   -9.712  1.00 21.27 ?  302 HOH   A O    1 
HETATM 7184 O O    . HOH   D 3 .   ? 7.729  -6.406  -6.584  1.00 39.85 ?  303 HOH   A O    1 
HETATM 7185 O O    . HOH   D 3 .   ? 8.024  -12.713 -0.762  1.00 22.38 ?  304 HOH   A O    1 
HETATM 7186 O O    . HOH   D 3 .   ? 17.214 -18.188 15.225  1.00 27.69 ?  305 HOH   A O    1 
HETATM 7187 O O    . HOH   D 3 .   ? 14.912 -4.775  20.632  1.00 43.84 ?  306 HOH   A O    1 
HETATM 7188 O O    . HOH   D 3 .   ? 4.969  4.064   0.966   1.00 32.30 ?  307 HOH   A O    1 
HETATM 7189 O O    . HOH   D 3 .   ? 8.053  -21.494 4.034   1.00 46.91 ?  308 HOH   A O    1 
HETATM 7190 O O    . HOH   D 3 .   ? 28.255 -0.254  -13.392 1.00 33.78 ?  309 HOH   A O    1 
HETATM 7191 O O    B HOH   D 3 .   ? 18.858 -2.235  -1.064  0.60 45.90 ?  310 HOH   A O    1 
HETATM 7192 O O    . HOH   D 3 .   ? 42.444 10.557  5.291   1.00 19.28 ?  311 HOH   A O    1 
HETATM 7193 O O    . HOH   D 3 .   ? 15.150 3.615   17.887  1.00 38.84 ?  312 HOH   A O    1 
HETATM 7194 O O    . HOH   D 3 .   ? 15.298 -12.309 18.805  1.00 33.67 ?  313 HOH   A O    1 
HETATM 7195 O O    . HOH   D 3 .   ? 9.906  -21.418 5.905   1.00 21.06 ?  314 HOH   A O    1 
HETATM 7196 O O    . HOH   D 3 .   ? 14.141 -4.498  -11.622 1.00 38.37 ?  315 HOH   A O    1 
HETATM 7197 O O    . HOH   D 3 .   ? 0.803  -4.860  0.470   1.00 34.68 ?  316 HOH   A O    1 
HETATM 7198 O O    . HOH   D 3 .   ? 17.131 -19.352 4.960   1.00 14.91 ?  317 HOH   A O    1 
HETATM 7199 O O    . HOH   D 3 .   ? -0.470 -3.264  3.253   1.00 49.05 ?  318 HOH   A O    1 
HETATM 7200 O O    . HOH   D 3 .   ? 28.429 -6.423  19.587  1.00 41.63 ?  319 HOH   A O    1 
HETATM 7201 O O    . HOH   D 3 .   ? 39.729 -0.979  -5.238  1.00 19.78 ?  320 HOH   A O    1 
HETATM 7202 O O    . HOH   D 3 .   ? 42.508 4.308   5.199   1.00 29.12 ?  321 HOH   A O    1 
HETATM 7203 O O    . HOH   D 3 .   ? 26.774 11.360  1.731   1.00 16.45 ?  322 HOH   A O    1 
HETATM 7204 O O    . HOH   D 3 .   ? 36.202 -5.042  -0.549  1.00 32.26 ?  323 HOH   A O    1 
HETATM 7205 O O    . HOH   D 3 .   ? 25.690 -0.907  -7.448  1.00 16.73 ?  324 HOH   A O    1 
HETATM 7206 O O    B HOH   D 3 .   ? 14.363 7.307   7.957   0.60 28.66 ?  325 HOH   A O    1 
HETATM 7207 O O    . HOH   D 3 .   ? 10.571 -22.450 -1.300  1.00 45.95 ?  326 HOH   A O    1 
HETATM 7208 O O    . HOH   D 3 .   ? 44.862 -0.652  2.900   1.00 38.49 ?  327 HOH   A O    1 
HETATM 7209 O O    . HOH   D 3 .   ? 31.070 -18.190 7.759   1.00 26.51 ?  328 HOH   A O    1 
HETATM 7210 O O    . HOH   D 3 .   ? 19.899 -12.649 -8.668  1.00 26.20 ?  329 HOH   A O    1 
HETATM 7211 O O    . HOH   D 3 .   ? 33.925 -0.949  -8.899  1.00 27.47 ?  330 HOH   A O    1 
HETATM 7212 O O    . HOH   D 3 .   ? 30.275 -13.310 -8.565  1.00 19.34 ?  331 HOH   A O    1 
HETATM 7213 O O    . HOH   D 3 .   ? 12.241 0.292   15.055  1.00 34.60 ?  332 HOH   A O    1 
HETATM 7214 O O    A HOH   D 3 .   ? 14.683 -3.736  3.198   0.40 10.91 ?  333 HOH   A O    1 
HETATM 7215 O O    . HOH   D 3 .   ? 14.844 -14.046 16.835  1.00 22.37 ?  334 HOH   A O    1 
HETATM 7216 O O    . HOH   D 3 .   ? 11.934 -10.885 17.235  1.00 27.08 ?  335 HOH   A O    1 
HETATM 7217 O O    . HOH   D 3 .   ? 37.587 2.782   10.187  1.00 28.75 ?  336 HOH   A O    1 
HETATM 7218 O O    . HOH   D 3 .   ? 14.144 -4.993  17.649  1.00 25.42 ?  337 HOH   A O    1 
HETATM 7219 O O    . HOH   D 3 .   ? 11.677 -10.918 -10.050 1.00 44.81 ?  338 HOH   A O    1 
HETATM 7220 O O    . HOH   D 3 .   ? 38.076 -1.301  -1.994  1.00 18.62 ?  339 HOH   A O    1 
HETATM 7221 O O    . HOH   D 3 .   ? 26.527 -19.375 -1.864  1.00 13.32 ?  340 HOH   A O    1 
HETATM 7222 O O    . HOH   D 3 .   ? 17.183 -17.869 -4.962  1.00 26.55 ?  341 HOH   A O    1 
HETATM 7223 O O    . HOH   D 3 .   ? 21.302 -2.391  -2.165  1.00 17.85 ?  342 HOH   A O    1 
HETATM 7224 O O    . HOH   D 3 .   ? 18.771 -19.476 13.634  1.00 30.84 ?  343 HOH   A O    1 
HETATM 7225 O O    . HOH   D 3 .   ? 27.288 13.716  2.974   1.00 29.92 ?  344 HOH   A O    1 
HETATM 7226 O O    . HOH   D 3 .   ? 9.279  -10.382 19.593  1.00 46.48 ?  345 HOH   A O    1 
HETATM 7227 O O    . HOH   D 3 .   ? 41.622 1.572   4.844   1.00 37.20 ?  346 HOH   A O    1 
HETATM 7228 O O    . HOH   D 3 .   ? 8.801  -12.068 17.398  1.00 42.56 ?  347 HOH   A O    1 
HETATM 7229 O O    . HOH   D 3 .   ? 13.419 -1.381  -6.540  1.00 20.42 ?  348 HOH   A O    1 
HETATM 7230 O O    B HOH   D 3 .   ? 21.169 2.436   0.148   0.60 21.96 ?  349 HOH   A O    1 
HETATM 7231 O O    . HOH   D 3 .   ? 19.157 -22.016 6.898   1.00 31.20 ?  350 HOH   A O    1 
HETATM 7232 O O    . HOH   D 3 .   ? 20.652 -19.709 -5.124  1.00 27.64 ?  351 HOH   A O    1 
HETATM 7233 O O    . HOH   D 3 .   ? 22.438 5.217   19.116  1.00 41.36 ?  352 HOH   A O    1 
HETATM 7234 O O    . HOH   D 3 .   ? 35.854 -12.751 6.739   1.00 16.28 ?  353 HOH   A O    1 
HETATM 7235 O O    A HOH   D 3 .   ? 14.330 0.479   6.915   0.40 24.56 ?  354 HOH   A O    1 
HETATM 7236 O O    . HOH   D 3 .   ? 23.418 11.321  4.207   1.00 13.70 ?  355 HOH   A O    1 
HETATM 7237 O O    . HOH   D 3 .   ? 38.594 4.963   6.923   1.00 16.46 ?  356 HOH   A O    1 
HETATM 7238 O O    A HOH   D 3 .   ? 18.982 -0.729  -1.533  0.40 11.33 ?  357 HOH   A O    1 
HETATM 7239 O O    . HOH   D 3 .   ? 22.492 -19.378 11.376  1.00 30.67 ?  358 HOH   A O    1 
HETATM 7240 O O    . HOH   D 3 .   ? 3.732  -9.814  10.151  1.00 43.71 ?  359 HOH   A O    1 
HETATM 7241 O O    B HOH   D 3 .   ? 14.807 -4.179  3.861   0.60 20.55 ?  360 HOH   A O    1 
HETATM 7242 O O    . HOH   D 3 .   ? 37.327 11.945  4.945   1.00 31.85 ?  361 HOH   A O    1 
HETATM 7243 O O    . HOH   D 3 .   ? 43.850 8.493   -3.179  1.00 23.55 ?  362 HOH   A O    1 
HETATM 7244 O O    . HOH   D 3 .   ? 27.229 -6.124  -14.022 1.00 32.33 ?  363 HOH   A O    1 
HETATM 7245 O O    . HOH   D 3 .   ? 31.733 8.160   14.867  1.00 24.28 ?  364 HOH   A O    1 
HETATM 7246 O O    . HOH   D 3 .   ? 44.242 7.056   6.469   1.00 25.71 ?  365 HOH   A O    1 
HETATM 7247 O O    . HOH   D 3 .   ? 22.736 12.473  1.687   1.00 16.32 ?  366 HOH   A O    1 
HETATM 7248 O O    . HOH   D 3 .   ? 24.040 -2.168  -2.061  1.00 11.85 ?  367 HOH   A O    1 
HETATM 7249 O O    . HOH   D 3 .   ? 38.293 10.151  7.170   1.00 37.02 ?  368 HOH   A O    1 
HETATM 7250 O O    . HOH   D 3 .   ? 14.436 -21.280 -4.191  1.00 27.90 ?  369 HOH   A O    1 
HETATM 7251 O O    . HOH   D 3 .   ? 33.742 -7.181  4.226   1.00 16.49 ?  370 HOH   A O    1 
HETATM 7252 O O    . HOH   D 3 .   ? 31.124 -13.956 -2.530  1.00 13.45 ?  371 HOH   A O    1 
HETATM 7253 O O    A HOH   D 3 .   ? 17.530 -1.783  0.537   0.40 17.52 ?  372 HOH   A O    1 
HETATM 7254 O O    . HOH   D 3 .   ? 16.509 -22.050 1.029   1.00 29.06 ?  373 HOH   A O    1 
HETATM 7255 O O    . HOH   D 3 .   ? 21.409 10.212  15.187  1.00 32.02 ?  374 HOH   A O    1 
HETATM 7256 O O    A HOH   D 3 .   ? 7.040  -8.284  11.966  0.40 16.45 ?  375 HOH   A O    1 
HETATM 7257 O O    . HOH   D 3 .   ? 22.715 -12.061 21.998  1.00 49.30 ?  376 HOH   A O    1 
HETATM 7258 O O    . HOH   D 3 .   ? 6.600  -5.798  11.485  1.00 23.59 ?  377 HOH   A O    1 
HETATM 7259 O O    . HOH   D 3 .   ? 30.860 3.036   8.281   1.00 12.79 ?  378 HOH   A O    1 
HETATM 7260 O O    . HOH   D 3 .   ? 24.357 3.548   -1.707  1.00 16.06 ?  379 HOH   A O    1 
HETATM 7261 O O    . HOH   D 3 .   ? 6.830  -3.517  13.206  1.00 31.87 ?  380 HOH   A O    1 
HETATM 7262 O O    . HOH   D 3 .   ? 26.924 4.084   -0.560  1.00 13.27 ?  381 HOH   A O    1 
HETATM 7263 O O    . HOH   D 3 .   ? 21.947 -21.973 8.336   1.00 29.23 ?  382 HOH   A O    1 
HETATM 7264 O O    A HOH   D 3 .   ? 21.370 3.096   -0.254  0.40 9.39  ?  383 HOH   A O    1 
HETATM 7265 O O    . HOH   D 3 .   ? 27.702 -10.743 14.046  1.00 17.92 ?  384 HOH   A O    1 
HETATM 7266 O O    . HOH   D 3 .   ? 37.582 -2.005  5.744   1.00 27.07 ?  385 HOH   A O    1 
HETATM 7267 O O    . HOH   D 3 .   ? 18.555 9.315   9.085   1.00 23.73 ?  386 HOH   A O    1 
HETATM 7268 O O    A HOH   D 3 .   ? 15.852 -1.032  5.374   0.40 25.01 ?  387 HOH   A O    1 
HETATM 7269 O O    . HOH   D 3 .   ? 24.850 -17.662 12.731  1.00 24.00 ?  388 HOH   A O    1 
HETATM 7270 O O    . HOH   D 3 .   ? 13.532 -15.256 -7.349  1.00 28.37 ?  389 HOH   A O    1 
HETATM 7271 O O    . HOH   D 3 .   ? 27.634 2.264   18.787  1.00 32.31 ?  390 HOH   A O    1 
HETATM 7272 O O    . HOH   D 3 .   ? 15.136 -8.164  -9.494  1.00 24.77 ?  391 HOH   A O    1 
HETATM 7273 O O    . HOH   D 3 .   ? 37.229 -3.035  9.696   1.00 39.24 ?  392 HOH   A O    1 
HETATM 7274 O O    . HOH   D 3 .   ? 43.319 7.887   2.625   1.00 22.21 ?  393 HOH   A O    1 
HETATM 7275 O O    . HOH   D 3 .   ? 31.808 -7.300  -9.847  1.00 21.39 ?  394 HOH   A O    1 
HETATM 7276 O O    . HOH   D 3 .   ? 31.964 -9.319  -6.653  1.00 22.08 ?  395 HOH   A O    1 
HETATM 7277 O O    . HOH   D 3 .   ? 24.517 -7.951  14.504  1.00 18.31 ?  396 HOH   A O    1 
HETATM 7278 O O    . HOH   D 3 .   ? -1.335 -4.970  8.043   1.00 45.09 ?  397 HOH   A O    1 
HETATM 7279 O O    . HOH   D 3 .   ? 27.814 0.837   -7.176  1.00 14.66 ?  398 HOH   A O    1 
HETATM 7280 O O    . HOH   D 3 .   ? 15.358 -21.758 14.306  1.00 18.88 ?  399 HOH   A O    1 
HETATM 7281 O O    . HOH   D 3 .   ? 27.403 -3.317  19.259  1.00 34.75 ?  400 HOH   A O    1 
HETATM 7282 O O    . HOH   D 3 .   ? 11.115 1.506   12.966  1.00 24.18 ?  401 HOH   A O    1 
HETATM 7283 O O    . HOH   D 3 .   ? 23.940 3.911   -4.763  1.00 25.62 ?  402 HOH   A O    1 
HETATM 7284 O O    . HOH   D 3 .   ? 20.174 4.495   -7.674  1.00 32.32 ?  403 HOH   A O    1 
HETATM 7285 O O    . HOH   D 3 .   ? 5.185  2.420   5.273   1.00 34.82 ?  404 HOH   A O    1 
HETATM 7286 O O    . HOH   D 3 .   ? 10.487 -13.818 -1.597  1.00 18.90 ?  405 HOH   A O    1 
HETATM 7287 O O    . HOH   D 3 .   ? 22.767 7.937   18.432  1.00 45.36 ?  406 HOH   A O    1 
HETATM 7288 O O    . HOH   D 3 .   ? 14.130 -23.125 7.490   1.00 20.34 ?  407 HOH   A O    1 
HETATM 7289 O O    . HOH   D 3 .   ? 20.655 -20.054 2.766   1.00 17.09 ?  408 HOH   A O    1 
HETATM 7290 O O    B HOH   D 3 .   ? 6.924  1.452   7.458   0.60 28.86 ?  409 HOH   A O    1 
HETATM 7291 O O    . HOH   D 3 .   ? 32.866 -9.307  5.841   1.00 19.03 ?  410 HOH   A O    1 
HETATM 7292 O O    . HOH   D 3 .   ? 20.664 -17.794 24.792  1.00 50.15 ?  411 HOH   A O    1 
HETATM 7293 O O    . HOH   D 3 .   ? -0.706 -8.615  2.227   1.00 43.04 ?  412 HOH   A O    1 
HETATM 7294 O O    . HOH   D 3 .   ? 15.584 11.833  7.967   1.00 25.14 ?  413 HOH   A O    1 
HETATM 7295 O O    . HOH   D 3 .   ? 30.248 -10.224 12.974  1.00 20.75 ?  414 HOH   A O    1 
HETATM 7296 O O    . HOH   D 3 .   ? 16.361 16.743  8.794   1.00 29.90 ?  415 HOH   A O    1 
HETATM 7297 O O    . HOH   D 3 .   ? 30.937 1.684   16.694  1.00 21.71 ?  416 HOH   A O    1 
HETATM 7298 O O    . HOH   D 3 .   ? 21.320 -9.325  21.477  1.00 41.81 ?  417 HOH   A O    1 
HETATM 7299 O O    . HOH   D 3 .   ? 32.641 -10.648 3.144   1.00 27.36 ?  418 HOH   A O    1 
HETATM 7300 O O    . HOH   D 3 .   ? 16.305 -14.285 20.506  1.00 40.00 ?  419 HOH   A O    1 
HETATM 7301 O O    A HOH   D 3 .   ? 14.585 -24.783 11.610  0.40 17.20 ?  420 HOH   A O    1 
HETATM 7302 O O    . HOH   D 3 .   ? 30.534 -13.067 13.457  1.00 20.15 ?  421 HOH   A O    1 
HETATM 7303 O O    . HOH   D 3 .   ? 23.922 -8.156  17.095  1.00 23.39 ?  422 HOH   A O    1 
HETATM 7304 O O    . HOH   D 3 .   ? 36.807 -5.002  5.299   1.00 25.14 ?  423 HOH   A O    1 
HETATM 7305 O O    A HOH   D 3 .   ? 24.580 2.007   -6.909  0.40 12.71 ?  424 HOH   A O    1 
HETATM 7306 O O    A HOH   D 3 .   ? 16.276 2.882   -1.327  0.40 16.47 ?  425 HOH   A O    1 
HETATM 7307 O O    . HOH   D 3 .   ? 24.006 -15.812 -9.178  1.00 32.13 ?  426 HOH   A O    1 
HETATM 7308 O O    . HOH   D 3 .   ? 35.110 -5.220  -3.122  1.00 18.46 ?  427 HOH   A O    1 
HETATM 7309 O O    . HOH   D 3 .   ? 18.539 2.098   -0.781  1.00 16.62 ?  428 HOH   A O    1 
HETATM 7310 O O    . HOH   D 3 .   ? 23.972 -20.296 -1.337  1.00 15.33 ?  429 HOH   A O    1 
HETATM 7311 O O    A HOH   D 3 .   ? 11.105 -0.465  2.058   0.40 36.18 ?  430 HOH   A O    1 
HETATM 7312 O O    . HOH   D 3 .   ? 9.694  -16.346 -2.443  1.00 44.43 ?  431 HOH   A O    1 
HETATM 7313 O O    A HOH   D 3 .   ? 18.541 -2.479  -16.249 0.40 24.61 ?  432 HOH   A O    1 
HETATM 7314 O O    . HOH   D 3 .   ? 40.984 -8.268  -6.710  1.00 36.22 ?  433 HOH   A O    1 
HETATM 7315 O O    . HOH   D 3 .   ? 32.707 -4.274  -9.935  1.00 27.07 ?  434 HOH   A O    1 
HETATM 7316 O O    . HOH   D 3 .   ? 15.957 2.108   24.751  1.00 62.34 ?  435 HOH   A O    1 
HETATM 7317 O O    B HOH   D 3 .   ? 17.659 0.181   -1.055  0.60 45.41 ?  436 HOH   A O    1 
HETATM 7318 O O    . HOH   D 3 .   ? 14.450 -0.541  -11.980 1.00 38.63 ?  437 HOH   A O    1 
HETATM 7319 O O    . HOH   D 3 .   ? 19.674 -11.243 24.295  1.00 56.77 ?  438 HOH   A O    1 
HETATM 7320 O O    B HOH   D 3 .   ? 11.924 6.187   11.521  0.60 29.32 ?  439 HOH   A O    1 
HETATM 7321 O O    A HOH   D 3 .   ? 16.046 6.876   3.117   0.40 11.71 ?  440 HOH   A O    1 
HETATM 7322 O O    . HOH   D 3 .   ? 28.606 -10.632 -14.002 1.00 41.93 ?  441 HOH   A O    1 
HETATM 7323 O O    . HOH   D 3 .   ? 30.761 6.335   -12.385 1.00 33.22 ?  442 HOH   A O    1 
HETATM 7324 O O    . HOH   D 3 .   ? 18.586 -16.137 16.374  1.00 35.46 ?  443 HOH   A O    1 
HETATM 7325 O O    B HOH   D 3 .   ? 16.118 7.477   2.989   0.60 20.06 ?  444 HOH   A O    1 
HETATM 7326 O O    . HOH   D 3 .   ? 23.360 -21.014 1.256   1.00 16.44 ?  445 HOH   A O    1 
HETATM 7327 O O    . HOH   D 3 .   ? 34.443 -8.113  -0.593  1.00 28.38 ?  446 HOH   A O    1 
HETATM 7328 O O    . HOH   D 3 .   ? 21.649 -14.132 -8.104  1.00 48.37 ?  447 HOH   A O    1 
HETATM 7329 O O    . HOH   D 3 .   ? 18.452 4.862   -14.976 1.00 48.92 ?  448 HOH   A O    1 
HETATM 7330 O O    . HOH   D 3 .   ? 30.537 14.762  2.876   1.00 20.01 ?  449 HOH   A O    1 
HETATM 7331 O O    B HOH   D 3 .   ? 22.952 5.989   -1.650  0.60 23.74 ?  450 HOH   A O    1 
HETATM 7332 O O    . HOH   D 3 .   ? 12.018 -13.441 16.445  1.00 38.65 ?  451 HOH   A O    1 
HETATM 7333 O O    . HOH   D 3 .   ? 29.957 -16.074 10.520  1.00 36.26 ?  452 HOH   A O    1 
HETATM 7334 O O    . HOH   D 3 .   ? 31.396 -12.828 -0.037  1.00 18.30 ?  453 HOH   A O    1 
HETATM 7335 O O    B HOH   D 3 .   ? 20.352 4.060   -2.050  0.60 32.16 ?  454 HOH   A O    1 
HETATM 7336 O O    . HOH   D 3 .   ? 37.745 -8.828  -3.435  1.00 25.32 ?  455 HOH   A O    1 
HETATM 7337 O O    A HOH   D 3 .   ? 23.203 7.465   -3.135  0.40 16.56 ?  456 HOH   A O    1 
HETATM 7338 O O    A HOH   D 3 .   ? 14.071 -0.423  3.575   0.40 33.78 ?  457 HOH   A O    1 
HETATM 7339 O O    . HOH   D 3 .   ? 21.868 -14.699 17.994  1.00 46.54 ?  458 HOH   A O    1 
HETATM 7340 O O    . HOH   D 3 .   ? 27.679 7.038   -6.281  1.00 31.83 ?  459 HOH   A O    1 
HETATM 7341 O O    . HOH   D 3 .   ? 24.977 5.538   20.812  1.00 50.40 ?  460 HOH   A O    1 
HETATM 7342 O O    . HOH   D 3 .   ? 29.829 -2.091  -12.822 1.00 47.62 ?  461 HOH   A O    1 
HETATM 7343 O O    . HOH   D 3 .   ? 25.433 8.285   -4.761  1.00 26.97 ?  462 HOH   A O    1 
HETATM 7344 O O    . HOH   D 3 .   ? 19.987 -17.376 -5.087  1.00 25.81 ?  463 HOH   A O    1 
HETATM 7345 O O    . HOH   D 3 .   ? 32.476 -16.031 10.865  1.00 43.34 ?  464 HOH   A O    1 
HETATM 7346 O O    . HOH   D 3 .   ? 23.244 -22.330 -3.421  1.00 31.82 ?  465 HOH   A O    1 
HETATM 7347 O O    . HOH   D 3 .   ? 22.097 5.222   -6.198  1.00 37.58 ?  466 HOH   A O    1 
HETATM 7348 O O    . HOH   D 3 .   ? 24.530 14.388  7.941   1.00 29.54 ?  467 HOH   A O    1 
HETATM 7349 O O    . HOH   D 3 .   ? 26.891 11.526  -1.134  1.00 27.74 ?  468 HOH   A O    1 
HETATM 7350 O O    . HOH   D 3 .   ? 27.671 -11.449 16.489  1.00 37.69 ?  469 HOH   A O    1 
HETATM 7351 O O    . HOH   D 3 .   ? 39.646 -7.058  -3.642  1.00 40.66 ?  470 HOH   A O    1 
HETATM 7352 O O    . HOH   D 3 .   ? 18.820 10.715  11.491  1.00 33.46 ?  471 HOH   A O    1 
HETATM 7353 O O    . HOH   D 3 .   ? 11.096 -15.069 -6.022  1.00 34.41 ?  472 HOH   A O    1 
HETATM 7354 O O    . HOH   D 3 .   ? 23.466 13.679  5.598   1.00 21.43 ?  473 HOH   A O    1 
HETATM 7355 O O    . HOH   D 3 .   ? 15.828 -21.621 3.841   1.00 23.24 ?  474 HOH   A O    1 
HETATM 7356 O O    . HOH   D 3 .   ? 12.471 1.534   17.560  1.00 39.54 ?  475 HOH   A O    1 
HETATM 7357 O O    . HOH   D 3 .   ? 25.823 10.831  -3.527  1.00 23.46 ?  476 HOH   A O    1 
HETATM 7358 O O    . HOH   D 3 .   ? 23.189 11.897  -3.967  1.00 24.92 ?  477 HOH   A O    1 
HETATM 7359 O O    . HOH   D 3 .   ? 15.685 -17.162 -6.928  1.00 34.48 ?  478 HOH   A O    1 
HETATM 7360 O O    . HOH   D 3 .   ? 18.194 -16.306 -8.688  1.00 39.52 ?  479 HOH   A O    1 
HETATM 7361 O O    . HOH   D 3 .   ? 16.886 -20.632 16.358  1.00 31.18 ?  480 HOH   A O    1 
HETATM 7362 O O    . HOH   D 3 .   ? 35.266 7.393   12.359  1.00 45.78 ?  481 HOH   A O    1 
HETATM 7363 O O    . HOH   D 3 .   ? 28.847 8.951   17.610  1.00 36.71 ?  482 HOH   A O    1 
HETATM 7364 O O    . HOH   D 3 .   ? 17.522 -18.794 19.913  1.00 41.74 ?  483 HOH   A O    1 
HETATM 7365 O O    . HOH   D 3 .   ? 20.541 -16.092 -7.341  1.00 30.52 ?  484 HOH   A O    1 
HETATM 7366 O O    . HOH   D 3 .   ? 40.939 -4.016  -0.313  1.00 37.02 ?  485 HOH   A O    1 
HETATM 7367 O O    . HOH   D 3 .   ? 14.055 -10.308 -10.760 1.00 35.10 ?  486 HOH   A O    1 
HETATM 7368 O O    . HOH   D 3 .   ? 41.597 9.240   -4.245  1.00 29.95 ?  487 HOH   A O    1 
HETATM 7369 O O    . HOH   D 3 .   ? 31.007 0.511   19.273  1.00 40.76 ?  488 HOH   A O    1 
HETATM 7370 O O    . HOH   D 3 .   ? 15.951 -6.975  -11.616 1.00 42.25 ?  489 HOH   A O    1 
HETATM 7371 O O    . HOH   D 3 .   ? 14.035 -25.409 8.996   1.00 31.89 ?  490 HOH   A O    1 
HETATM 7372 O O    . HOH   D 3 .   ? 44.457 10.512  -1.654  1.00 33.15 ?  491 HOH   A O    1 
HETATM 7373 O O    . HOH   D 3 .   ? 28.625 -4.774  -12.306 1.00 34.39 ?  492 HOH   A O    1 
HETATM 7374 O O    . HOH   D 3 .   ? 28.601 -7.981  -15.212 1.00 45.33 ?  493 HOH   A O    1 
HETATM 7375 O O    . HOH   D 3 .   ? 18.566 -23.167 2.055   1.00 44.26 ?  494 HOH   A O    1 
HETATM 7376 O O    . HOH   D 3 .   ? 23.443 -13.109 19.445  1.00 42.36 ?  495 HOH   A O    1 
HETATM 7377 O O    B HOH   D 3 .   ? 16.972 9.984   6.388   0.60 22.48 ?  496 HOH   A O    1 
HETATM 7378 O O    . HOH   D 3 .   ? 31.422 -0.548  -10.592 1.00 25.60 ?  497 HOH   A O    1 
HETATM 7379 O O    . HOH   D 3 .   ? 40.486 -0.240  -7.812  1.00 32.80 ?  498 HOH   A O    1 
HETATM 7380 O O    . HOH   D 3 .   ? 20.088 -22.367 4.132   1.00 24.76 ?  499 HOH   A O    1 
HETATM 7381 O O    . HOH   D 3 .   ? 16.223 -23.454 5.856   1.00 30.16 ?  500 HOH   A O    1 
HETATM 7382 O O    . HOH   D 3 .   ? 39.199 2.358   7.561   1.00 31.68 ?  501 HOH   A O    1 
HETATM 7383 O O    . HOH   D 3 .   ? 30.732 -5.777  -11.816 1.00 48.53 ?  502 HOH   A O    1 
HETATM 7384 O O    . HOH   D 3 .   ? 30.634 5.829   -14.669 1.00 45.54 ?  503 HOH   A O    1 
HETATM 7385 O O    . HOH   D 3 .   ? 39.609 0.019   6.537   1.00 27.91 ?  504 HOH   A O    1 
HETATM 7386 O O    . HOH   D 3 .   ? 23.229 -23.821 1.719   1.00 27.79 ?  505 HOH   A O    1 
HETATM 7387 O O    . HOH   D 3 .   ? 37.487 -6.690  7.353   1.00 23.42 ?  506 HOH   A O    1 
HETATM 7388 O O    . HOH   D 3 .   ? 29.016 14.382  1.000   1.00 45.21 ?  507 HOH   A O    1 
HETATM 7389 O O    . HOH   D 3 .   ? 38.070 13.839  6.806   1.00 53.37 ?  508 HOH   A O    1 
HETATM 7390 O O    . HOH   D 3 .   ? 15.044 8.301   5.181   1.00 41.54 ?  509 HOH   A O    1 
HETATM 7391 O O    . HOH   D 3 .   ? 8.287  -2.809  -5.457  1.00 39.22 ?  510 HOH   A O    1 
HETATM 7392 O O    . HOH   D 3 .   ? 36.568 -6.563  10.124  1.00 40.26 ?  511 HOH   A O    1 
HETATM 7393 O O    . HOH   D 3 .   ? 17.348 -6.778  -13.997 1.00 38.04 ?  512 HOH   A O    1 
HETATM 7394 O O    . HOH   D 3 .   ? 16.217 -21.219 18.758  1.00 35.12 ?  513 HOH   A O    1 
HETATM 7395 O O    . HOH   D 3 .   ? 24.071 9.091   -7.196  1.00 36.47 ?  514 HOH   A O    1 
HETATM 7396 O O    . HOH   D 3 .   ? 16.083 -12.535 27.688  1.00 40.49 ?  515 HOH   A O    1 
HETATM 7397 O O    . HOH   D 3 .   ? 14.623 -22.782 19.985  1.00 37.49 ?  516 HOH   A O    1 
HETATM 7398 O O    . HOH   E 3 .   ? 29.836 -22.471 5.372   1.00 20.10 ?  201 HOH   B O    1 
HETATM 7399 O O    . HOH   E 3 .   ? 48.234 -6.929  15.518  1.00 33.76 ?  202 HOH   B O    1 
HETATM 7400 O O    . HOH   E 3 .   ? 49.354 -22.677 -19.830 1.00 49.34 ?  203 HOH   B O    1 
HETATM 7401 O O    . HOH   E 3 .   ? 41.499 -7.829  5.500   1.00 39.75 ?  204 HOH   B O    1 
HETATM 7402 O O    . HOH   E 3 .   ? 47.464 -7.506  -4.096  1.00 42.96 ?  205 HOH   B O    1 
HETATM 7403 O O    . HOH   E 3 .   ? 45.219 -34.807 6.843   1.00 35.40 ?  206 HOH   B O    1 
HETATM 7404 O O    . HOH   E 3 .   ? 27.783 -29.186 -2.017  1.00 32.13 ?  207 HOH   B O    1 
HETATM 7405 O O    . HOH   E 3 .   ? 59.164 -18.769 6.707   1.00 34.94 ?  208 HOH   B O    1 
HETATM 7406 O O    . HOH   E 3 .   ? 41.955 -35.918 -17.412 1.00 29.01 ?  209 HOH   B O    1 
HETATM 7407 O O    . HOH   E 3 .   ? 29.894 -26.360 3.883   1.00 27.55 ?  210 HOH   B O    1 
HETATM 7408 O O    . HOH   E 3 .   ? 58.320 -12.871 8.370   1.00 36.42 ?  211 HOH   B O    1 
HETATM 7409 O O    . HOH   E 3 .   ? 53.015 -13.435 -20.466 1.00 35.63 ?  212 HOH   B O    1 
HETATM 7410 O O    . HOH   E 3 .   ? 54.459 -9.375  -8.896  1.00 20.34 ?  213 HOH   B O    1 
HETATM 7411 O O    . HOH   E 3 .   ? 37.919 -39.512 -0.255  1.00 37.43 ?  214 HOH   B O    1 
HETATM 7412 O O    . HOH   E 3 .   ? 50.365 -3.414  7.111   1.00 32.00 ?  215 HOH   B O    1 
HETATM 7413 O O    . HOH   E 3 .   ? 56.393 -19.739 7.340   1.00 33.74 ?  216 HOH   B O    1 
HETATM 7414 O O    . HOH   E 3 .   ? 27.859 -41.842 -15.226 1.00 32.31 ?  217 HOH   B O    1 
HETATM 7415 O O    . HOH   E 3 .   ? 56.721 -30.794 -7.796  1.00 34.57 ?  218 HOH   B O    1 
HETATM 7416 O O    . HOH   E 3 .   ? 45.058 -43.468 -10.631 1.00 24.25 ?  219 HOH   B O    1 
HETATM 7417 O O    . HOH   E 3 .   ? 37.286 -19.664 -18.112 1.00 35.72 ?  220 HOH   B O    1 
HETATM 7418 O O    . HOH   E 3 .   ? 39.400 -10.953 6.056   1.00 28.27 ?  221 HOH   B O    1 
HETATM 7419 O O    . HOH   E 3 .   ? 55.466 -16.448 -14.427 1.00 35.72 ?  222 HOH   B O    1 
HETATM 7420 O O    . HOH   E 3 .   ? 30.242 -41.047 -8.271  1.00 15.51 ?  223 HOH   B O    1 
HETATM 7421 O O    . HOH   E 3 .   ? 36.017 -43.216 -8.618  1.00 26.55 ?  224 HOH   B O    1 
HETATM 7422 O O    . HOH   E 3 .   ? 44.451 -7.207  2.036   1.00 34.28 ?  225 HOH   B O    1 
HETATM 7423 O O    . HOH   E 3 .   ? 41.911 -23.552 9.252   1.00 15.76 ?  226 HOH   B O    1 
HETATM 7424 O O    . HOH   E 3 .   ? 29.737 -34.191 -0.471  1.00 31.15 ?  227 HOH   B O    1 
HETATM 7425 O O    . HOH   E 3 .   ? 50.769 -6.132  0.244   1.00 26.06 ?  228 HOH   B O    1 
HETATM 7426 O O    . HOH   E 3 .   ? 57.479 -16.230 -12.199 1.00 19.11 ?  229 HOH   B O    1 
HETATM 7427 O O    . HOH   E 3 .   ? 57.794 -24.475 4.871   1.00 36.16 ?  230 HOH   B O    1 
HETATM 7428 O O    . HOH   E 3 .   ? 50.780 -12.979 -0.547  1.00 12.91 ?  231 HOH   B O    1 
HETATM 7429 O O    . HOH   E 3 .   ? 41.463 -9.667  12.989  1.00 22.54 ?  232 HOH   B O    1 
HETATM 7430 O O    . HOH   E 3 .   ? 40.707 -16.025 14.146  1.00 26.46 ?  233 HOH   B O    1 
HETATM 7431 O O    . HOH   E 3 .   ? 35.156 -8.003  -3.119  1.00 17.79 ?  234 HOH   B O    1 
HETATM 7432 O O    . HOH   E 3 .   ? 48.156 -24.483 -17.750 1.00 27.64 ?  235 HOH   B O    1 
HETATM 7433 O O    . HOH   E 3 .   ? 28.453 -19.670 -13.169 1.00 22.79 ?  236 HOH   B O    1 
HETATM 7434 O O    . HOH   E 3 .   ? 34.578 -36.376 -7.274  1.00 16.52 ?  237 HOH   B O    1 
HETATM 7435 O O    . HOH   E 3 .   ? 30.743 -42.186 -10.727 1.00 27.28 ?  238 HOH   B O    1 
HETATM 7436 O O    . HOH   E 3 .   ? 57.197 -26.753 -7.676  1.00 38.68 ?  239 HOH   B O    1 
HETATM 7437 O O    . HOH   E 3 .   ? 30.841 -28.781 4.143   1.00 22.04 ?  240 HOH   B O    1 
HETATM 7438 O O    . HOH   E 3 .   ? 32.877 -43.783 -11.437 1.00 18.08 ?  241 HOH   B O    1 
HETATM 7439 O O    . HOH   E 3 .   ? 25.475 -25.982 -1.414  1.00 30.33 ?  242 HOH   B O    1 
HETATM 7440 O O    . HOH   E 3 .   ? 42.615 -25.401 2.550   1.00 14.48 ?  243 HOH   B O    1 
HETATM 7441 O O    . HOH   E 3 .   ? 51.742 -6.546  4.472   1.00 20.98 ?  244 HOH   B O    1 
HETATM 7442 O O    . HOH   E 3 .   ? 43.191 -43.256 -8.341  1.00 26.25 ?  245 HOH   B O    1 
HETATM 7443 O O    . HOH   E 3 .   ? 42.698 -22.914 3.816   1.00 11.73 ?  246 HOH   B O    1 
HETATM 7444 O O    . HOH   E 3 .   ? 44.572 -27.714 -0.759  1.00 22.87 ?  247 HOH   B O    1 
HETATM 7445 O O    . HOH   E 3 .   ? 40.374 -12.779 -11.582 1.00 15.35 ?  248 HOH   B O    1 
HETATM 7446 O O    . HOH   E 3 .   ? 41.534 -39.139 -15.013 1.00 19.74 ?  249 HOH   B O    1 
HETATM 7447 O O    . HOH   E 3 .   ? 29.778 -25.235 -10.926 1.00 15.55 ?  250 HOH   B O    1 
HETATM 7448 O O    . HOH   E 3 .   ? 46.477 -1.632  13.335  1.00 36.12 ?  251 HOH   B O    1 
HETATM 7449 O O    . HOH   E 3 .   ? 48.042 -22.809 5.757   1.00 16.90 ?  252 HOH   B O    1 
HETATM 7450 O O    . HOH   E 3 .   ? 57.629 -24.455 -3.876  1.00 23.06 ?  253 HOH   B O    1 
HETATM 7451 O O    . HOH   E 3 .   ? 37.469 -35.715 6.951   1.00 31.23 ?  254 HOH   B O    1 
HETATM 7452 O O    . HOH   E 3 .   ? 33.599 -17.084 7.986   1.00 18.69 ?  255 HOH   B O    1 
HETATM 7453 O O    . HOH   E 3 .   ? 43.331 -32.377 -17.160 1.00 19.62 ?  256 HOH   B O    1 
HETATM 7454 O O    . HOH   E 3 .   ? 49.417 -28.726 -6.992  1.00 15.13 ?  257 HOH   B O    1 
HETATM 7455 O O    . HOH   E 3 .   ? 51.613 -13.864 10.878  1.00 29.57 ?  258 HOH   B O    1 
HETATM 7456 O O    . HOH   E 3 .   ? 39.562 -11.148 0.278   1.00 17.21 ?  259 HOH   B O    1 
HETATM 7457 O O    . HOH   E 3 .   ? 58.174 -10.551 -4.103  1.00 22.02 ?  260 HOH   B O    1 
HETATM 7458 O O    . HOH   E 3 .   ? 30.931 -15.796 2.601   1.00 13.00 ?  261 HOH   B O    1 
HETATM 7459 O O    . HOH   E 3 .   ? 27.163 -31.835 -10.093 1.00 20.68 ?  262 HOH   B O    1 
HETATM 7460 O O    . HOH   E 3 .   ? 34.288 -18.620 11.386  1.00 22.32 ?  263 HOH   B O    1 
HETATM 7461 O O    . HOH   E 3 .   ? 38.514 -11.059 -2.310  1.00 18.58 ?  264 HOH   B O    1 
HETATM 7462 O O    . HOH   E 3 .   ? 34.575 -12.841 2.546   1.00 22.46 ?  265 HOH   B O    1 
HETATM 7463 O O    . HOH   E 3 .   ? 51.057 -39.964 -8.275  1.00 26.03 ?  266 HOH   B O    1 
HETATM 7464 O O    . HOH   E 3 .   ? 57.159 -12.157 12.272  1.00 36.97 ?  267 HOH   B O    1 
HETATM 7465 O O    . HOH   E 3 .   ? 28.341 -34.365 -9.619  1.00 21.13 ?  268 HOH   B O    1 
HETATM 7466 O O    . HOH   E 3 .   ? 28.879 -42.934 -12.444 1.00 33.25 ?  269 HOH   B O    1 
HETATM 7467 O O    . HOH   E 3 .   ? 42.230 -10.276 -15.016 1.00 29.21 ?  270 HOH   B O    1 
HETATM 7468 O O    . HOH   E 3 .   ? 34.930 -33.340 -19.304 1.00 24.47 ?  271 HOH   B O    1 
HETATM 7469 O O    . HOH   E 3 .   ? 57.044 -8.703  8.363   1.00 22.89 ?  272 HOH   B O    1 
HETATM 7470 O O    . HOH   E 3 .   ? 56.215 -23.505 -14.785 1.00 27.09 ?  273 HOH   B O    1 
HETATM 7471 O O    . HOH   E 3 .   ? 46.679 -31.304 -4.860  1.00 17.03 ?  274 HOH   B O    1 
HETATM 7472 O O    . HOH   E 3 .   ? 41.246 -24.458 15.755  1.00 41.88 ?  275 HOH   B O    1 
HETATM 7473 O O    . HOH   E 3 .   ? 34.988 -24.599 13.813  1.00 27.21 ?  276 HOH   B O    1 
HETATM 7474 O O    . HOH   E 3 .   ? 38.975 -12.093 12.411  1.00 31.09 ?  277 HOH   B O    1 
HETATM 7475 O O    . HOH   E 3 .   ? 57.573 -9.244  1.373   1.00 20.00 ?  278 HOH   B O    1 
HETATM 7476 O O    . HOH   E 3 .   ? 49.882 -0.567  10.257  1.00 30.71 ?  279 HOH   B O    1 
HETATM 7477 O O    . HOH   E 3 .   ? 43.631 -15.435 18.270  1.00 33.79 ?  280 HOH   B O    1 
HETATM 7478 O O    . HOH   E 3 .   ? 44.591 -24.680 9.593   1.00 18.51 ?  281 HOH   B O    1 
HETATM 7479 O O    . HOH   E 3 .   ? 42.417 -9.908  9.322   1.00 21.54 ?  282 HOH   B O    1 
HETATM 7480 O O    . HOH   E 3 .   ? 43.426 -15.819 -12.209 1.00 14.23 ?  283 HOH   B O    1 
HETATM 7481 O O    . HOH   E 3 .   ? 28.024 -22.903 -8.077  1.00 16.29 ?  284 HOH   B O    1 
HETATM 7482 O O    . HOH   E 3 .   ? 48.608 -36.495 -15.654 1.00 38.84 ?  285 HOH   B O    1 
HETATM 7483 O O    . HOH   E 3 .   ? 46.872 -29.544 9.751   1.00 31.22 ?  286 HOH   B O    1 
HETATM 7484 O O    . HOH   E 3 .   ? 31.873 -17.984 -14.625 1.00 30.73 ?  287 HOH   B O    1 
HETATM 7485 O O    . HOH   E 3 .   ? 35.123 -33.600 4.397   1.00 23.22 ?  288 HOH   B O    1 
HETATM 7486 O O    . HOH   E 3 .   ? 47.137 -34.048 -4.681  1.00 15.74 ?  289 HOH   B O    1 
HETATM 7487 O O    . HOH   E 3 .   ? 48.475 -25.079 3.024   1.00 12.98 ?  290 HOH   B O    1 
HETATM 7488 O O    . HOH   E 3 .   ? 28.524 -30.834 -14.846 1.00 27.70 ?  291 HOH   B O    1 
HETATM 7489 O O    . HOH   E 3 .   ? 37.670 -18.290 13.045  1.00 29.68 ?  292 HOH   B O    1 
HETATM 7490 O O    . HOH   E 3 .   ? 36.850 -12.776 -1.559  1.00 24.87 ?  293 HOH   B O    1 
HETATM 7491 O O    . HOH   E 3 .   ? 52.648 -10.525 12.958  1.00 24.23 ?  294 HOH   B O    1 
HETATM 7492 O O    . HOH   E 3 .   ? 48.773 -20.075 5.870   1.00 14.23 ?  295 HOH   B O    1 
HETATM 7493 O O    . HOH   E 3 .   ? 52.667 -35.659 -8.592  1.00 27.85 ?  296 HOH   B O    1 
HETATM 7494 O O    . HOH   E 3 .   ? 27.659 -26.806 -15.771 1.00 31.96 ?  297 HOH   B O    1 
HETATM 7495 O O    . HOH   E 3 .   ? 45.947 -40.438 -3.679  1.00 24.83 ?  298 HOH   B O    1 
HETATM 7496 O O    . HOH   E 3 .   ? 62.866 -20.221 -0.955  1.00 41.27 ?  299 HOH   B O    1 
HETATM 7497 O O    . HOH   E 3 .   ? 33.556 -15.330 -14.041 1.00 20.14 ?  300 HOH   B O    1 
HETATM 7498 O O    . HOH   E 3 .   ? 39.378 -23.308 -20.302 1.00 32.46 ?  301 HOH   B O    1 
HETATM 7499 O O    . HOH   E 3 .   ? 40.306 -10.837 -9.594  1.00 16.53 ?  302 HOH   B O    1 
HETATM 7500 O O    . HOH   E 3 .   ? 51.326 -37.640 -9.608  1.00 22.56 ?  303 HOH   B O    1 
HETATM 7501 O O    . HOH   E 3 .   ? 42.457 -34.735 3.727   1.00 24.33 ?  304 HOH   B O    1 
HETATM 7502 O O    . HOH   E 3 .   ? 52.660 -29.246 -13.019 1.00 22.66 ?  305 HOH   B O    1 
HETATM 7503 O O    . HOH   E 3 .   ? 45.545 -33.448 -15.997 1.00 20.47 ?  306 HOH   B O    1 
HETATM 7504 O O    . HOH   E 3 .   ? 26.010 -21.515 -3.578  1.00 15.45 ?  307 HOH   B O    1 
HETATM 7505 O O    . HOH   E 3 .   ? 44.086 -29.375 -4.751  1.00 24.01 ?  308 HOH   B O    1 
HETATM 7506 O O    . HOH   E 3 .   ? 59.831 -15.390 8.140   1.00 30.07 ?  309 HOH   B O    1 
HETATM 7507 O O    . HOH   E 3 .   ? 44.668 -27.475 1.918   1.00 14.91 ?  310 HOH   B O    1 
HETATM 7508 O O    . HOH   E 3 .   ? 37.869 -10.284 -10.792 1.00 16.82 ?  311 HOH   B O    1 
HETATM 7509 O O    . HOH   E 3 .   ? 49.970 -24.749 5.761   1.00 32.00 ?  312 HOH   B O    1 
HETATM 7510 O O    . HOH   E 3 .   ? 41.217 -5.495  11.471  1.00 41.63 ?  313 HOH   B O    1 
HETATM 7511 O O    . HOH   E 3 .   ? 53.455 -30.233 4.520   1.00 18.98 ?  314 HOH   B O    1 
HETATM 7512 O O    . HOH   E 3 .   ? 41.763 -8.144  1.339   1.00 25.24 ?  315 HOH   B O    1 
HETATM 7513 O O    . HOH   E 3 .   ? 32.877 -34.618 -6.015  1.00 15.06 ?  316 HOH   B O    1 
HETATM 7514 O O    . HOH   E 3 .   ? 42.945 -20.301 -20.833 1.00 36.96 ?  317 HOH   B O    1 
HETATM 7515 O O    . HOH   E 3 .   ? 53.446 -16.178 -12.671 1.00 29.98 ?  318 HOH   B O    1 
HETATM 7516 O O    . HOH   E 3 .   ? 38.381 -9.404  -13.333 1.00 27.77 ?  319 HOH   B O    1 
HETATM 7517 O O    . HOH   E 3 .   ? 43.270 -21.453 10.618  1.00 15.86 ?  320 HOH   B O    1 
HETATM 7518 O O    . HOH   E 3 .   ? 57.697 -22.087 3.094   1.00 26.85 ?  321 HOH   B O    1 
HETATM 7519 O O    . HOH   E 3 .   ? 62.766 -13.619 4.749   1.00 27.16 ?  322 HOH   B O    1 
HETATM 7520 O O    . HOH   E 3 .   ? 42.758 -12.233 -18.588 1.00 29.22 ?  323 HOH   B O    1 
HETATM 7521 O O    . HOH   E 3 .   ? 27.939 -14.806 -9.402  1.00 33.28 ?  324 HOH   B O    1 
HETATM 7522 O O    . HOH   E 3 .   ? 38.425 -12.888 7.865   1.00 18.59 ?  325 HOH   B O    1 
HETATM 7523 O O    . HOH   E 3 .   ? 26.396 -21.060 -6.294  1.00 15.64 ?  326 HOH   B O    1 
HETATM 7524 O O    . HOH   E 3 .   ? 48.225 -32.577 -16.707 1.00 45.32 ?  327 HOH   B O    1 
HETATM 7525 O O    . HOH   E 3 .   ? 51.657 -5.936  -7.972  1.00 52.37 ?  328 HOH   B O    1 
HETATM 7526 O O    . HOH   E 3 .   ? 59.970 -17.299 -10.568 1.00 35.65 ?  329 HOH   B O    1 
HETATM 7527 O O    . HOH   E 3 .   ? 51.490 -32.883 -10.785 1.00 33.28 ?  330 HOH   B O    1 
HETATM 7528 O O    . HOH   E 3 .   ? 33.694 -31.185 11.036  1.00 35.22 ?  331 HOH   B O    1 
HETATM 7529 O O    . HOH   E 3 .   ? 36.800 -12.451 4.273   1.00 18.57 ?  332 HOH   B O    1 
HETATM 7530 O O    . HOH   E 3 .   ? 37.324 -30.554 -21.190 1.00 30.11 ?  333 HOH   B O    1 
HETATM 7531 O O    . HOH   E 3 .   ? 53.687 -12.492 -22.414 1.00 34.22 ?  334 HOH   B O    1 
HETATM 7532 O O    . HOH   E 3 .   ? 47.170 -24.529 8.106   1.00 28.05 ?  335 HOH   B O    1 
HETATM 7533 O O    . HOH   E 3 .   ? 43.142 -34.679 -0.007  1.00 18.77 ?  336 HOH   B O    1 
HETATM 7534 O O    . HOH   E 3 .   ? 48.646 -11.916 -13.900 1.00 24.63 ?  337 HOH   B O    1 
HETATM 7535 O O    . HOH   E 3 .   ? 45.910 -36.262 -16.276 1.00 32.62 ?  338 HOH   B O    1 
HETATM 7536 O O    . HOH   E 3 .   ? 38.512 -12.279 -16.217 1.00 38.90 ?  339 HOH   B O    1 
HETATM 7537 O O    . HOH   E 3 .   ? 42.985 -43.497 -14.482 1.00 41.14 ?  340 HOH   B O    1 
HETATM 7538 O O    . HOH   E 3 .   ? 47.530 -27.479 1.940   1.00 14.94 ?  341 HOH   B O    1 
HETATM 7539 O O    . HOH   E 3 .   ? 46.975 -19.895 12.227  1.00 31.48 ?  342 HOH   B O    1 
HETATM 7540 O O    . HOH   E 3 .   ? 44.247 -1.686  7.537   1.00 43.92 ?  343 HOH   B O    1 
HETATM 7541 O O    . HOH   E 3 .   ? 36.997 -14.993 -16.478 1.00 34.76 ?  344 HOH   B O    1 
HETATM 7542 O O    . HOH   E 3 .   ? 23.326 -23.786 6.732   1.00 32.71 ?  345 HOH   B O    1 
HETATM 7543 O O    . HOH   E 3 .   ? 33.053 -14.710 1.005   1.00 17.04 ?  346 HOH   B O    1 
HETATM 7544 O O    . HOH   E 3 .   ? 44.277 -37.424 -17.776 1.00 30.26 ?  347 HOH   B O    1 
HETATM 7545 O O    . HOH   E 3 .   ? 39.807 -44.372 -11.364 1.00 35.86 ?  348 HOH   B O    1 
HETATM 7546 O O    . HOH   E 3 .   ? 40.467 -43.453 -9.292  1.00 25.62 ?  349 HOH   B O    1 
HETATM 7547 O O    . HOH   E 3 .   ? 55.689 -8.256  10.761  1.00 25.84 ?  350 HOH   B O    1 
HETATM 7548 O O    . HOH   E 3 .   ? 37.045 -45.373 -9.821  1.00 36.11 ?  351 HOH   B O    1 
HETATM 7549 O O    . HOH   E 3 .   ? 27.808 -26.673 -0.725  1.00 28.83 ?  352 HOH   B O    1 
HETATM 7550 O O    . HOH   E 3 .   ? 62.615 -20.129 -4.924  1.00 47.30 ?  353 HOH   B O    1 
HETATM 7551 O O    . HOH   E 3 .   ? 36.267 -8.555  -9.643  1.00 31.17 ?  354 HOH   B O    1 
HETATM 7552 O O    . HOH   E 3 .   ? 33.755 -9.258  -8.836  1.00 28.97 ?  355 HOH   B O    1 
HETATM 7553 O O    . HOH   E 3 .   ? 38.551 -22.371 15.068  1.00 38.85 ?  356 HOH   B O    1 
HETATM 7554 O O    . HOH   E 3 .   ? 56.604 -7.283  2.975   1.00 31.97 ?  357 HOH   B O    1 
HETATM 7555 O O    . HOH   E 3 .   ? 27.209 -26.004 -11.347 1.00 30.73 ?  358 HOH   B O    1 
HETATM 7556 O O    . HOH   E 3 .   ? 40.410 -8.819  9.931   1.00 41.07 ?  359 HOH   B O    1 
HETATM 7557 O O    . HOH   E 3 .   ? 34.827 -10.326 7.357   1.00 22.90 ?  360 HOH   B O    1 
HETATM 7558 O O    . HOH   E 3 .   ? 56.954 -21.482 -16.468 1.00 42.61 ?  361 HOH   B O    1 
HETATM 7559 O O    . HOH   E 3 .   ? 61.590 -19.956 1.536   1.00 31.36 ?  362 HOH   B O    1 
HETATM 7560 O O    . HOH   E 3 .   ? 34.166 -7.787  11.516  1.00 42.51 ?  363 HOH   B O    1 
HETATM 7561 O O    . HOH   E 3 .   ? 43.169 -12.758 -21.350 1.00 43.40 ?  364 HOH   B O    1 
HETATM 7562 O O    . HOH   E 3 .   ? 48.388 -26.602 8.806   1.00 38.43 ?  365 HOH   B O    1 
HETATM 7563 O O    . HOH   E 3 .   ? 39.989 -11.428 -14.054 1.00 32.70 ?  366 HOH   B O    1 
HETATM 7564 O O    . HOH   E 3 .   ? 32.544 -23.667 14.116  1.00 38.97 ?  367 HOH   B O    1 
HETATM 7565 O O    . HOH   E 3 .   ? 40.020 -7.035  7.754   1.00 41.81 ?  368 HOH   B O    1 
HETATM 7566 O O    . HOH   E 3 .   ? 54.271 -5.752  2.971   1.00 38.01 ?  369 HOH   B O    1 
HETATM 7567 O O    . HOH   E 3 .   ? 36.337 -8.817  8.921   1.00 37.39 ?  370 HOH   B O    1 
HETATM 7568 O O    . HOH   E 3 .   ? 52.100 -12.939 13.281  1.00 33.03 ?  371 HOH   B O    1 
HETATM 7569 O O    . HOH   E 3 .   ? 59.160 -10.507 9.036   1.00 40.21 ?  372 HOH   B O    1 
HETATM 7570 O O    . HOH   E 3 .   ? 56.037 -7.814  -0.565  1.00 37.37 ?  373 HOH   B O    1 
HETATM 7571 O O    . HOH   E 3 .   ? 41.962 -6.885  -4.914  1.00 47.36 ?  374 HOH   B O    1 
HETATM 7572 O O    . HOH   E 3 .   ? 38.138 -10.676 9.976   1.00 29.41 ?  375 HOH   B O    1 
HETATM 7573 O O    . HOH   E 3 .   ? 41.800 -9.963  -17.464 1.00 52.69 ?  376 HOH   B O    1 
HETATM 7574 O O    . HOH   E 3 .   ? 63.071 -12.407 6.864   1.00 37.90 ?  377 HOH   B O    1 
HETATM 7575 O O    . HOH   E 3 .   ? 44.087 -5.640  -3.546  1.00 42.12 ?  378 HOH   B O    1 
HETATM 7576 O O    . HOH   E 3 .   ? 36.605 -22.817 13.324  1.00 24.97 ?  379 HOH   B O    1 
HETATM 7577 O O    . HOH   E 3 .   ? 40.213 -7.728  3.165   1.00 36.60 ?  380 HOH   B O    1 
HETATM 7578 O O    . HOH   E 3 .   ? 60.483 -22.375 2.645   1.00 40.85 ?  381 HOH   B O    1 
HETATM 7579 O O    . HOH   E 3 .   ? 35.457 -33.809 7.110   1.00 40.26 ?  382 HOH   B O    1 
HETATM 7580 O O    . HOH   E 3 .   ? 52.855 -29.936 7.130   1.00 22.13 ?  383 HOH   B O    1 
HETATM 7581 O O    . HOH   E 3 .   ? 39.795 -14.033 15.763  1.00 50.66 ?  384 HOH   B O    1 
HETATM 7582 O O    . HOH   E 3 .   ? 42.612 -17.037 -23.402 1.00 41.67 ?  385 HOH   B O    1 
HETATM 7583 O O    . HOH   E 3 .   ? 24.002 -20.870 -7.803  1.00 26.18 ?  386 HOH   B O    1 
HETATM 7584 O O    . HOH   E 3 .   ? 25.787 -18.868 -12.014 1.00 38.62 ?  387 HOH   B O    1 
HETATM 7585 O O    . HOH   E 3 .   ? 35.325 -20.327 13.311  1.00 29.86 ?  388 HOH   B O    1 
HETATM 7586 O O    . HOH   E 3 .   ? 41.012 -9.871  15.856  1.00 44.26 ?  389 HOH   B O    1 
HETATM 7587 O O    . HOH   E 3 .   ? 46.744 -5.333  2.974   1.00 41.68 ?  390 HOH   B O    1 
HETATM 7588 O O    . HOH   E 3 .   ? 40.749 -6.645  -0.907  1.00 23.79 ?  391 HOH   B O    1 
HETATM 7589 O O    . HOH   E 3 .   ? 44.093 -31.758 -3.852  1.00 28.78 ?  392 HOH   B O    1 
HETATM 7590 O O    . HOH   E 3 .   ? 28.027 -27.111 2.177   1.00 33.21 ?  393 HOH   B O    1 
HETATM 7591 O O    . HOH   E 3 .   ? 26.713 -28.003 -13.590 1.00 33.17 ?  394 HOH   B O    1 
HETATM 7592 O O    . HOH   E 3 .   ? 34.517 -33.455 9.583   1.00 31.56 ?  395 HOH   B O    1 
HETATM 7593 O O    . HOH   E 3 .   ? 50.625 -30.828 8.659   1.00 26.44 ?  396 HOH   B O    1 
HETATM 7594 O O    . HOH   E 3 .   ? 24.632 -20.718 -10.477 1.00 36.32 ?  397 HOH   B O    1 
HETATM 7595 O O    . HOH   E 3 .   ? 45.926 -20.317 15.121  1.00 56.17 ?  398 HOH   B O    1 
HETATM 7596 O O    . HOH   E 3 .   ? 22.083 -24.125 4.410   1.00 26.92 ?  399 HOH   B O    1 
HETATM 7597 O O    . HOH   E 3 .   ? 26.868 -30.650 -12.713 1.00 30.95 ?  400 HOH   B O    1 
HETATM 7598 O O    . HOH   E 3 .   ? 57.626 -6.440  -2.411  1.00 34.14 ?  401 HOH   B O    1 
HETATM 7599 O O    . HOH   E 3 .   ? 40.846 -11.898 -22.537 1.00 48.30 ?  402 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.5836 0.5713 0.6392 0.0009  0.0055  0.0689  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.5882 0.5733 0.6542 -0.0004 0.0072  0.0808  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.5814 0.5692 0.6322 0.0002  0.0064  0.0697  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.5856 0.5709 0.6445 -0.0011 0.0082  0.0807  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.5709 0.5588 0.6060 -0.0022 0.0039  0.0782  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.5730 0.5596 0.6144 -0.0028 0.0045  0.0846  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.5726 0.5606 0.6137 -0.0004 0.0031  0.0789  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.5746 0.5614 0.6246 -0.0007 0.0034  0.0862  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.5876 0.5755 0.6463 0.0010  0.0103  0.0631  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.5933 0.5778 0.6588 -0.0007 0.0136  0.0768  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.5898 0.5777 0.6506 0.0014  0.0117  0.0606  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.5961 0.5801 0.6630 -0.0004 0.0153  0.0752  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.5895 0.5776 0.6505 0.0011  0.0119  0.0611  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.5958 0.5802 0.6625 -0.0008 0.0157  0.0758  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.5560 0.5444 0.5639 -0.0065 0.0028  0.0857  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.5230 0.5126 0.4668 -0.0155 0.0024  0.0902  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.4812 0.4803 0.4095 -0.0281 0.0150  0.0749  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.4812 0.4795 0.3927 -0.0297 0.0158  0.0857  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.5288 0.5110 0.4251 -0.0128 -0.0075 0.1081  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.5334 0.5079 0.3879 -0.0107 -0.0174 0.1251  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.5354 0.5057 0.3737 -0.0109 -0.0169 0.1295  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.5343 0.5068 0.3779 -0.0086 -0.0222 0.1327  4   ASN   A ND2 
46   N N   . SER   A 5   ? 0.4374 0.4449 0.3700 -0.0412 0.0231  0.0470  5   SER   A N   
47   C CA  . SER   A 5   ? 0.3932 0.4124 0.3361 -0.0518 0.0345  0.0180  5   SER   A CA  
48   C C   . SER   A 5   ? 0.3430 0.3638 0.2900 -0.0525 0.0500  -0.0028 5   SER   A C   
49   O O   . SER   A 5   ? 0.3482 0.3723 0.2901 -0.0404 0.0492  -0.0230 5   SER   A O   
50   C CB  . SER   A 5   ? 0.3996 0.4231 0.3504 -0.0586 0.0310  0.0129  5   SER   A CB  
51   O OG  . SER   A 5   ? 0.4051 0.4248 0.3594 -0.0610 0.0342  0.0113  5   SER   A OG  
57   N N   A PHE   A 6   ? 0.3069 0.3311 0.2691 -0.0597 0.0556  -0.0040 6   PHE   A N   
58   N N   B PHE   A 6   ? 0.3214 0.3379 0.2708 -0.0601 0.0660  0.0022  6   PHE   A N   
59   C CA  A PHE   A 6   ? 0.2732 0.2979 0.2437 -0.0646 0.0591  -0.0005 6   PHE   A CA  
60   C CA  B PHE   A 6   ? 0.3033 0.3112 0.2460 -0.0650 0.0788  0.0145  6   PHE   A CA  
61   C C   A PHE   A 6   ? 0.2525 0.2833 0.2408 -0.0702 0.0713  0.0010  6   PHE   A C   
62   C C   B PHE   A 6   ? 0.3074 0.3122 0.2647 -0.0656 0.0929  0.0168  6   PHE   A C   
63   O O   A PHE   A 6   ? 0.2492 0.2879 0.2439 -0.0730 0.0683  0.0058  6   PHE   A O   
64   O O   B PHE   A 6   ? 0.3080 0.3169 0.2753 -0.0712 0.0869  0.0265  6   PHE   A O   
65   C CB  A PHE   A 6   ? 0.2593 0.2811 0.2292 -0.0610 0.0539  -0.0007 6   PHE   A CB  
66   C CB  B PHE   A 6   ? 0.2825 0.2873 0.2239 -0.0631 0.0749  0.0168  6   PHE   A CB  
67   C CG  A PHE   A 6   ? 0.2509 0.2676 0.2214 -0.0575 0.0455  -0.0008 6   PHE   A CG  
68   C CG  B PHE   A 6   ? 0.2684 0.2693 0.2112 -0.0600 0.0690  0.0179  6   PHE   A CG  
69   C CD1 A PHE   A 6   ? 0.2496 0.2622 0.2153 -0.0548 0.0361  -0.0020 6   PHE   A CD1 
70   C CD1 B PHE   A 6   ? 0.2651 0.2623 0.2052 -0.0566 0.0576  0.0162  6   PHE   A CD1 
71   C CD2 A PHE   A 6   ? 0.2499 0.2635 0.2233 -0.0521 0.0391  -0.0049 6   PHE   A CD2 
72   C CD2 B PHE   A 6   ? 0.2671 0.2665 0.2135 -0.0513 0.0625  0.0093  6   PHE   A CD2 
73   C CE1 A PHE   A 6   ? 0.2480 0.2584 0.2156 -0.0551 0.0321  -0.0014 6   PHE   A CE1 
74   C CE1 B PHE   A 6   ? 0.2625 0.2586 0.2090 -0.0567 0.0522  0.0154  6   PHE   A CE1 
75   C CE2 A PHE   A 6   ? 0.2494 0.2598 0.2217 -0.0525 0.0348  -0.0047 6   PHE   A CE2 
76   C CE2 B PHE   A 6   ? 0.2663 0.2647 0.2163 -0.0498 0.0557  0.0053  6   PHE   A CE2 
77   C CZ  A PHE   A 6   ? 0.2492 0.2578 0.2139 -0.0548 0.0340  -0.0032 6   PHE   A CZ  
78   C CZ  B PHE   A 6   ? 0.2652 0.2612 0.2088 -0.0547 0.0537  0.0085  6   PHE   A CZ  
97   N N   A SER   A 7   ? 0.2333 0.2629 0.2310 -0.0741 0.0829  -0.0055 7   SER   A N   
98   N N   B SER   A 7   ? 0.3087 0.3070 0.2810 -0.0585 0.1027  0.0012  7   SER   A N   
99   C CA  A SER   A 7   ? 0.2228 0.2497 0.2285 -0.0722 0.0875  -0.0190 7   SER   A CA  
100  C CA  B SER   A 7   ? 0.3173 0.3075 0.2948 -0.0479 0.1000  -0.0186 7   SER   A CA  
101  C C   A SER   A 7   ? 0.2050 0.2273 0.2232 -0.0724 0.0834  -0.0187 7   SER   A C   
102  C C   B SER   A 7   ? 0.3135 0.2980 0.2822 -0.0358 0.1010  -0.0264 7   SER   A C   
103  O O   A SER   A 7   ? 0.2107 0.2218 0.2204 -0.0721 0.0850  -0.0195 7   SER   A O   
104  O O   B SER   A 7   ? 0.3179 0.2987 0.2814 -0.0338 0.1007  -0.0255 7   SER   A O   
105  C CB  A SER   A 7   ? 0.2339 0.2612 0.2425 -0.0643 0.0890  -0.0260 7   SER   A CB  
106  C CB  B SER   A 7   ? 0.3253 0.3144 0.3167 -0.0509 0.1021  -0.0270 7   SER   A CB  
107  O OG  A SER   A 7   ? 0.2448 0.2689 0.2666 -0.0609 0.0825  -0.0272 7   SER   A OG  
108  O OG  B SER   A 7   ? 0.3311 0.3196 0.3416 -0.0504 0.0990  -0.0299 7   SER   A OG  
119  N N   A GLY   A 8   ? 0.1908 0.2149 0.2326 -0.0709 0.0644  -0.0225 8   GLY   A N   
120  N N   B GLY   A 8   ? 0.3103 0.2936 0.2836 -0.0244 0.0940  -0.0267 8   GLY   A N   
121  C CA  A GLY   A 8   ? 0.1837 0.2070 0.2380 -0.0594 0.0514  -0.0117 8   GLY   A CA  
122  C CA  B GLY   A 8   ? 0.3035 0.2853 0.2823 -0.0181 0.0838  -0.0218 8   GLY   A CA  
123  C C   A GLY   A 8   ? 0.1714 0.2035 0.2378 -0.0484 0.0308  -0.0032 8   GLY   A C   
124  C C   B GLY   A 8   ? 0.2948 0.2771 0.2771 -0.0130 0.0738  -0.0109 8   GLY   A C   
125  O O   A GLY   A 8   ? 0.1670 0.2128 0.2488 -0.0414 0.0219  -0.0176 8   GLY   A O   
126  O O   B GLY   A 8   ? 0.3011 0.2845 0.3024 -0.0073 0.0682  -0.0150 8   GLY   A O   
133  N N   A TYR   A 9   ? 0.1546 0.1873 0.2100 -0.0468 0.0315  0.0183  9   TYR   A N   
134  N N   B TYR   A 9   ? 0.2736 0.2592 0.2656 -0.0150 0.0729  0.0076  9   TYR   A N   
135  C CA  A TYR   A 9   ? 0.1426 0.1679 0.1932 -0.0493 0.0163  0.0224  9   TYR   A CA  
136  C CA  B TYR   A 9   ? 0.2523 0.2379 0.2579 -0.0150 0.0625  0.0189  9   TYR   A CA  
137  C C   A TYR   A 9   ? 0.1459 0.1618 0.1940 -0.0479 0.0125  0.0416  9   TYR   A C   
138  C C   B TYR   A 9   ? 0.2455 0.2258 0.2512 -0.0264 0.0519  0.0393  9   TYR   A C   
139  O O   A TYR   A 9   ? 0.1550 0.1728 0.2093 -0.0509 0.0039  0.0493  9   TYR   A O   
140  O O   B TYR   A 9   ? 0.2594 0.2311 0.2589 -0.0294 0.0376  0.0577  9   TYR   A O   
141  C CB  A TYR   A 9   ? 0.1381 0.1640 0.1879 -0.0395 0.0137  0.0039  9   TYR   A CB  
142  C CB  B TYR   A 9   ? 0.2360 0.2319 0.2583 -0.0010 0.0637  0.0062  9   TYR   A CB  
143  C CG  A TYR   A 9   ? 0.1418 0.1627 0.1922 -0.0290 0.0241  -0.0119 9   TYR   A CG  
144  C CG  B TYR   A 9   ? 0.2180 0.2258 0.2444 0.0089  0.0705  0.0036  9   TYR   A CG  
145  C CD1 A TYR   A 9   ? 0.1520 0.1652 0.1991 -0.0314 0.0328  -0.0165 9   TYR   A CD1 
146  C CD1 B TYR   A 9   ? 0.2156 0.2251 0.2447 0.0071  0.0716  0.0029  9   TYR   A CD1 
147  C CD2 A TYR   A 9   ? 0.1465 0.1597 0.1901 -0.0219 0.0192  -0.0057 9   TYR   A CD2 
148  C CD2 B TYR   A 9   ? 0.2116 0.2203 0.2412 0.0132  0.0665  0.0115  9   TYR   A CD2 
149  C CE1 A TYR   A 9   ? 0.1516 0.1675 0.2067 -0.0314 0.0352  -0.0106 9   TYR   A CE1 
150  C CE1 B TYR   A 9   ? 0.2112 0.2198 0.2454 0.0085  0.0742  -0.0023 9   TYR   A CE1 
151  C CE2 A TYR   A 9   ? 0.1465 0.1618 0.2003 -0.0223 0.0280  -0.0086 9   TYR   A CE2 
152  C CE2 B TYR   A 9   ? 0.2041 0.2161 0.2352 0.0131  0.0727  0.0061  9   TYR   A CE2 
153  C CZ  A TYR   A 9   ? 0.1469 0.1648 0.2106 -0.0326 0.0406  -0.0055 9   TYR   A CZ  
154  C CZ  B TYR   A 9   ? 0.2065 0.2156 0.2448 0.0059  0.0838  0.0083  9   TYR   A CZ  
155  O OH  A TYR   A 9   ? 0.1518 0.1691 0.2353 -0.0351 0.0440  -0.0096 9   TYR   A OH  
156  O OH  B TYR   A 9   ? 0.2101 0.2135 0.2707 0.0042  0.0845  0.0115  9   TYR   A OH  
175  N N   A LEU   A 10  ? 0.1383 0.1531 0.1940 -0.0483 0.0013  0.0435  10  LEU   A N   
176  N N   B LEU   A 10  ? 0.2256 0.2140 0.2433 -0.0317 0.0486  0.0408  10  LEU   A N   
177  C CA  A LEU   A 10  ? 0.1428 0.1537 0.1921 -0.0521 -0.0068 0.0524  10  LEU   A CA  
178  C CA  B LEU   A 10  ? 0.2064 0.2130 0.2539 -0.0395 0.0392  0.0322  10  LEU   A CA  
179  C C   A LEU   A 10  ? 0.1378 0.1496 0.1832 -0.0460 -0.0158 0.0492  10  LEU   A C   
180  C C   B LEU   A 10  ? 0.1770 0.1902 0.2297 -0.0369 0.0276  0.0365  10  LEU   A C   
181  O O   A LEU   A 10  ? 0.1448 0.1457 0.1860 -0.0445 -0.0071 0.0525  10  LEU   A O   
182  O O   B LEU   A 10  ? 0.1690 0.1751 0.2113 -0.0380 0.0321  0.0408  10  LEU   A O   
183  C CB  A LEU   A 10  ? 0.1586 0.1597 0.2150 -0.0547 -0.0240 0.0670  10  LEU   A CB  
184  C CB  B LEU   A 10  ? 0.2209 0.2324 0.3026 -0.0524 0.0312  0.0361  10  LEU   A CB  
185  C CG  A LEU   A 10  ? 0.1821 0.1722 0.2519 -0.0518 -0.0512 0.0720  10  LEU   A CG  
186  C CG  B LEU   A 10  ? 0.2430 0.2527 0.3605 -0.0565 0.0167  0.0333  10  LEU   A CG  
187  C CD1 A LEU   A 10  ? 0.1951 0.1760 0.2715 -0.0483 -0.0569 0.0762  10  LEU   A CD1 
188  C CD1 B LEU   A 10  ? 0.2524 0.2561 0.3853 -0.0599 0.0112  0.0337  10  LEU   A CD1 
189  C CD2 A LEU   A 10  ? 0.1906 0.1807 0.2633 -0.0484 -0.0486 0.0586  10  LEU   A CD2 
190  C CD2 B LEU   A 10  ? 0.2498 0.2632 0.3707 -0.0584 0.0161  0.0299  10  LEU   A CD2 
213  N N   A LYS   A 11  ? 0.1265 0.1479 0.1722 -0.0417 -0.0187 0.0605  11  LYS   A N   
214  N N   B LYS   A 11  ? 0.1655 0.1858 0.2406 -0.0378 0.0221  0.0391  11  LYS   A N   
215  C CA  A LYS   A 11  ? 0.1265 0.1435 0.1775 -0.0434 -0.0150 0.0622  11  LYS   A CA  
216  C CA  B LYS   A 11  ? 0.1521 0.1831 0.2414 -0.0323 0.0091  0.0479  11  LYS   A CA  
217  C C   A LYS   A 11  ? 0.1256 0.1428 0.1725 -0.0370 -0.0135 0.0611  11  LYS   A C   
218  C C   B LYS   A 11  ? 0.1372 0.1727 0.2418 -0.0331 0.0077  0.0415  11  LYS   A C   
219  O O   A LYS   A 11  ? 0.1238 0.1594 0.1767 -0.0406 -0.0162 0.0708  11  LYS   A O   
220  O O   B LYS   A 11  ? 0.1295 0.1819 0.2428 -0.0407 -0.0017 0.0629  11  LYS   A O   
221  C CB  A LYS   A 11  ? 0.1338 0.1413 0.1839 -0.0430 -0.0052 0.0597  11  LYS   A CB  
222  C CB  B LYS   A 11  ? 0.1545 0.1820 0.2499 -0.0231 0.0069  0.0568  11  LYS   A CB  
223  C CG  A LYS   A 11  ? 0.1494 0.1402 0.2046 -0.0360 0.0082  0.0534  11  LYS   A CG  
224  C CG  B LYS   A 11  ? 0.1662 0.1838 0.2733 -0.0129 0.0128  0.0660  11  LYS   A CG  
225  C CD  A LYS   A 11  ? 0.1578 0.1378 0.2087 -0.0282 0.0100  0.0465  11  LYS   A CD  
226  C CD  B LYS   A 11  ? 0.1756 0.1808 0.2888 -0.0055 0.0159  0.0751  11  LYS   A CD  
227  C CE  A LYS   A 11  ? 0.1595 0.1373 0.2061 -0.0220 0.0138  0.0343  11  LYS   A CE  
228  C CE  B LYS   A 11  ? 0.1814 0.1795 0.2985 -0.0003 0.0200  0.0737  11  LYS   A CE  
229  N NZ  A LYS   A 11  ? 0.1575 0.1374 0.2009 -0.0160 0.0100  0.0221  11  LYS   A NZ  
230  N NZ  B LYS   A 11  ? 0.1825 0.1797 0.3027 0.0035  0.0238  0.0677  11  LYS   A NZ  
257  N N   A LEU   A 12  ? 0.1251 0.1325 0.1702 -0.0339 -0.0051 0.0370  12  LEU   A N   
258  N N   B LEU   A 12  ? 0.1376 0.1597 0.2509 -0.0361 0.0146  0.0167  12  LEU   A N   
259  C CA  A LEU   A 12  ? 0.1296 0.1210 0.1832 -0.0305 0.0053  0.0298  12  LEU   A CA  
260  C CA  B LEU   A 12  ? 0.1389 0.1686 0.2438 -0.0264 0.0155  0.0120  12  LEU   A CA  
261  C C   A LEU   A 12  ? 0.1263 0.1201 0.2066 -0.0339 0.0052  0.0203  12  LEU   A C   
262  C C   B LEU   A 12  ? 0.1396 0.1599 0.2249 -0.0236 0.0241  0.0115  12  LEU   A C   
263  O O   A LEU   A 12  ? 0.1237 0.1255 0.2210 -0.0359 0.0178  0.0087  12  LEU   A O   
264  O O   B LEU   A 12  ? 0.1476 0.1554 0.2188 -0.0163 0.0285  -0.0036 12  LEU   A O   
265  C CB  A LEU   A 12  ? 0.1367 0.1147 0.1904 -0.0281 0.0051  0.0294  12  LEU   A CB  
266  C CB  B LEU   A 12  ? 0.1430 0.1742 0.2537 -0.0212 0.0131  0.0065  12  LEU   A CB  
267  C CG  A LEU   A 12  ? 0.1494 0.1256 0.1982 -0.0137 0.0126  0.0269  12  LEU   A CG  
268  C CG  B LEU   A 12  ? 0.1448 0.1750 0.2570 -0.0190 0.0131  -0.0044 12  LEU   A CG  
269  C CD1 A LEU   A 12  ? 0.1580 0.1300 0.2063 -0.0041 0.0155  0.0266  12  LEU   A CD1 
270  C CD1 B LEU   A 12  ? 0.1472 0.1796 0.2551 -0.0156 0.0142  -0.0071 12  LEU   A CD1 
271  C CD2 A LEU   A 12  ? 0.1511 0.1315 0.1974 -0.0046 0.0117  0.0155  12  LEU   A CD2 
272  C CD2 B LEU   A 12  ? 0.1459 0.1806 0.2776 -0.0112 0.0085  -0.0128 12  LEU   A CD2 
295  N N   A THR   A 13  ? 0.1296 0.1239 0.2150 -0.0322 0.0035  0.0200  13  THR   A N   
296  N N   B THR   A 13  ? 0.1371 0.1566 0.2310 -0.0162 0.0170  0.0124  13  THR   A N   
297  C CA  A THR   A 13  ? 0.1361 0.1288 0.2244 -0.0303 0.0117  0.0251  13  THR   A CA  
298  C CA  B THR   A 13  ? 0.1364 0.1609 0.2353 -0.0184 0.0244  0.0189  13  THR   A CA  
299  C C   A THR   A 13  ? 0.1430 0.1247 0.2260 -0.0297 0.0089  0.0304  13  THR   A C   
300  C C   B THR   A 13  ? 0.1462 0.1743 0.2404 -0.0288 0.0225  0.0280  13  THR   A C   
301  O O   A THR   A 13  ? 0.1525 0.1284 0.2251 -0.0203 0.0123  0.0301  13  THR   A O   
302  O O   B THR   A 13  ? 0.1508 0.1764 0.2397 -0.0263 0.0175  0.0310  13  THR   A O   
303  C CB  A THR   A 13  ? 0.1410 0.1340 0.2432 -0.0255 0.0050  0.0246  13  THR   A CB  
304  C CB  B THR   A 13  ? 0.1347 0.1585 0.2433 -0.0077 0.0265  0.0173  13  THR   A CB  
305  O OG1 A THR   A 13  ? 0.1439 0.1227 0.2565 -0.0214 -0.0059 0.0300  13  THR   A OG1 
306  O OG1 B THR   A 13  ? 0.1274 0.1479 0.2628 -0.0087 0.0224  0.0205  13  THR   A OG1 
307  C CG2 A THR   A 13  ? 0.1463 0.1401 0.2571 -0.0197 0.0080  0.0174  13  THR   A CG2 
308  C CG2 B THR   A 13  ? 0.1417 0.1756 0.2536 0.0014  0.0277  0.0058  13  THR   A CG2 
323  N N   A ASP   A 14  ? 0.1475 0.1210 0.2259 -0.0314 0.0048  0.0307  14  ASP   A N   
324  N N   B ASP   A 14  ? 0.1588 0.1860 0.2558 -0.0347 0.0166  0.0326  14  ASP   A N   
325  C CA  A ASP   A 14  ? 0.1466 0.1194 0.2163 -0.0238 0.0091  0.0376  14  ASP   A CA  
326  C CA  B ASP   A 14  ? 0.1751 0.1979 0.2712 -0.0267 0.0126  0.0403  14  ASP   A CA  
327  C C   A ASP   A 14  ? 0.1420 0.1310 0.1945 -0.0256 0.0084  0.0419  14  ASP   A C   
328  C C   B ASP   A 14  ? 0.1686 0.1846 0.2356 -0.0234 0.0060  0.0435  14  ASP   A C   
329  O O   A ASP   A 14  ? 0.1367 0.1468 0.2010 -0.0314 0.0102  0.0451  14  ASP   A O   
330  O O   B ASP   A 14  ? 0.1700 0.1966 0.2293 -0.0216 0.0079  0.0429  14  ASP   A O   
331  C CB  A ASP   A 14  ? 0.1524 0.1242 0.2385 -0.0305 0.0080  0.0384  14  ASP   A CB  
332  C CB  B ASP   A 14  ? 0.2002 0.2301 0.3331 -0.0312 0.0138  0.0452  14  ASP   A CB  
333  C CG  A ASP   A 14  ? 0.1610 0.1557 0.2798 -0.0357 0.0031  0.0289  14  ASP   A CG  
334  C CG  B ASP   A 14  ? 0.2209 0.2641 0.3981 -0.0452 0.0146  0.0461  14  ASP   A CG  
335  O OD1 A ASP   A 14  ? 0.1628 0.1697 0.2762 -0.0227 -0.0110 0.0264  14  ASP   A OD1 
336  O OD1 B ASP   A 14  ? 0.2295 0.2757 0.4264 -0.0526 0.0240  0.0520  14  ASP   A OD1 
337  O OD2 A ASP   A 14  ? 0.1776 0.1794 0.3105 -0.0442 0.0121  0.0234  14  ASP   A OD2 
338  O OD2 B ASP   A 14  ? 0.2293 0.2755 0.4303 -0.0505 0.0117  0.0417  14  ASP   A OD2 
347  N N   A ASN   A 15  ? 0.1423 0.1281 0.1903 -0.0281 0.0154  0.0395  15  ASN   A N   
348  N N   B ASN   A 15  ? 0.1578 0.1583 0.2251 -0.0250 0.0094  0.0373  15  ASN   A N   
349  C CA  A ASN   A 15  ? 0.1408 0.1373 0.1896 -0.0254 0.0100  0.0249  15  ASN   A CA  
350  C CA  B ASN   A 15  ? 0.1495 0.1462 0.2214 -0.0201 0.0113  0.0219  15  ASN   A CA  
351  C C   A ASN   A 15  ? 0.1347 0.1348 0.1952 -0.0287 0.0191  0.0241  15  ASN   A C   
352  C C   B ASN   A 15  ? 0.1421 0.1399 0.2456 -0.0150 0.0181  0.0252  15  ASN   A C   
353  O O   A ASN   A 15  ? 0.1316 0.1353 0.1967 -0.0225 0.0220  0.0113  15  ASN   A O   
354  O O   B ASN   A 15  ? 0.1307 0.1311 0.2708 -0.0054 0.0213  0.0112  15  ASN   A O   
355  C CB  A ASN   A 15  ? 0.1375 0.1428 0.1877 -0.0168 -0.0027 0.0220  15  ASN   A CB  
356  C CB  B ASN   A 15  ? 0.1426 0.1393 0.2057 -0.0159 0.0019  0.0101  15  ASN   A CB  
357  C CG  A ASN   A 15  ? 0.1280 0.1424 0.1795 -0.0104 -0.0032 0.0140  15  ASN   A CG  
358  C CG  B ASN   A 15  ? 0.1383 0.1411 0.2081 -0.0167 0.0021  0.0064  15  ASN   A CG  
359  O OD1 A ASN   A 15  ? 0.1311 0.1477 0.1720 -0.0184 -0.0140 0.0206  15  ASN   A OD1 
360  O OD1 B ASN   A 15  ? 0.1463 0.1429 0.2101 -0.0265 -0.0157 0.0288  15  ASN   A OD1 
361  N ND2 A ASN   A 15  ? 0.1245 0.1416 0.1825 -0.0073 0.0130  0.0092  15  ASN   A ND2 
362  N ND2 B ASN   A 15  ? 0.1347 0.1510 0.2081 -0.0225 0.0160  -0.0080 15  ASN   A ND2 
375  N N   A VAL   A 16  ? 0.1339 0.1323 0.2081 -0.0283 0.0089  0.0269  16  VAL   A N   
376  N N   B VAL   A 16  ? 0.1474 0.1386 0.2500 -0.0093 0.0076  0.0303  16  VAL   A N   
377  C CA  A VAL   A 16  ? 0.1266 0.1330 0.2098 -0.0288 0.0072  0.0302  16  VAL   A CA  
378  C CA  B VAL   A 16  ? 0.1443 0.1410 0.2313 -0.0103 0.0130  0.0381  16  VAL   A CA  
379  C C   A VAL   A 16  ? 0.1185 0.1305 0.2108 -0.0281 0.0031  0.0320  16  VAL   A C   
380  C C   B VAL   A 16  ? 0.1449 0.1429 0.2194 -0.0189 0.0190  0.0390  16  VAL   A C   
381  O O   A VAL   A 16  ? 0.1084 0.1307 0.2113 -0.0261 0.0062  0.0292  16  VAL   A O   
382  O O   B VAL   A 16  ? 0.1461 0.1491 0.2185 -0.0230 0.0258  0.0295  16  VAL   A O   
383  C CB  A VAL   A 16  ? 0.1327 0.1473 0.2147 -0.0187 0.0196  0.0285  16  VAL   A CB  
384  C CB  B VAL   A 16  ? 0.1458 0.1478 0.2250 0.0071  0.0314  0.0350  16  VAL   A CB  
385  C CG1 A VAL   A 16  ? 0.1417 0.1548 0.2124 -0.0111 0.0201  0.0273  16  VAL   A CG1 
386  C CG1 B VAL   A 16  ? 0.1551 0.1561 0.2175 0.0235  0.0257  0.0286  16  VAL   A CG1 
387  C CG2 A VAL   A 16  ? 0.1390 0.1617 0.2181 -0.0144 0.0250  0.0237  16  VAL   A CG2 
388  C CG2 B VAL   A 16  ? 0.1483 0.1595 0.2380 0.0159  0.0329  0.0325  16  VAL   A CG2 
407  N N   A TYR   A 17  ? 0.1239 0.1292 0.2111 -0.0264 -0.0001 0.0308  17  TYR   A N   
408  N N   B TYR   A 17  ? 0.1477 0.1397 0.2233 -0.0176 0.0194  0.0323  17  TYR   A N   
409  C CA  A TYR   A 17  ? 0.1305 0.1377 0.1897 -0.0246 -0.0085 0.0317  17  TYR   A CA  
410  C CA  B TYR   A 17  ? 0.1468 0.1469 0.2048 -0.0151 0.0149  0.0294  17  TYR   A CA  
411  C C   A TYR   A 17  ? 0.1299 0.1311 0.1707 -0.0247 -0.0005 0.0226  17  TYR   A C   
412  C C   B TYR   A 17  ? 0.1471 0.1436 0.1962 -0.0198 0.0088  0.0284  17  TYR   A C   
413  O O   A TYR   A 17  ? 0.1247 0.1275 0.1690 -0.0262 0.0040  0.0246  17  TYR   A O   
414  O O   B TYR   A 17  ? 0.1416 0.1383 0.1914 -0.0196 0.0111  0.0289  17  TYR   A O   
415  C CB  A TYR   A 17  ? 0.1360 0.1423 0.1881 -0.0340 -0.0230 0.0434  17  TYR   A CB  
416  C CB  B TYR   A 17  ? 0.1450 0.1515 0.1995 -0.0091 0.0056  0.0310  17  TYR   A CB  
417  C CG  A TYR   A 17  ? 0.1520 0.1505 0.1941 -0.0405 -0.0251 0.0396  17  TYR   A CG  
418  C CG  B TYR   A 17  ? 0.1482 0.1630 0.1971 -0.0090 -0.0044 0.0241  17  TYR   A CG  
419  C CD1 A TYR   A 17  ? 0.1633 0.1609 0.2060 -0.0348 -0.0247 0.0325  17  TYR   A CD1 
420  C CD1 B TYR   A 17  ? 0.1578 0.1744 0.2153 0.0004  -0.0041 0.0243  17  TYR   A CD1 
421  C CD2 A TYR   A 17  ? 0.1556 0.1565 0.1863 -0.0471 -0.0251 0.0420  17  TYR   A CD2 
422  C CD2 B TYR   A 17  ? 0.1499 0.1740 0.1931 -0.0091 -0.0017 0.0185  17  TYR   A CD2 
423  C CE1 A TYR   A 17  ? 0.1684 0.1619 0.2068 -0.0382 -0.0340 0.0350  17  TYR   A CE1 
424  C CE1 B TYR   A 17  ? 0.1685 0.1788 0.2276 -0.0005 -0.0022 0.0278  17  TYR   A CE1 
425  C CE2 A TYR   A 17  ? 0.1624 0.1579 0.1968 -0.0448 -0.0319 0.0343  17  TYR   A CE2 
426  C CE2 B TYR   A 17  ? 0.1600 0.1756 0.2030 -0.0021 0.0063  0.0161  17  TYR   A CE2 
427  C CZ  A TYR   A 17  ? 0.1723 0.1575 0.2121 -0.0371 -0.0348 0.0403  17  TYR   A CZ  
428  C CZ  B TYR   A 17  ? 0.1668 0.1717 0.2213 0.0005  -0.0023 0.0310  17  TYR   A CZ  
429  O OH  A TYR   A 17  ? 0.1816 0.1560 0.2284 -0.0333 -0.0380 0.0427  17  TYR   A OH  
430  O OH  B TYR   A 17  ? 0.1716 0.1679 0.2390 0.0073  -0.0000 0.0360  17  TYR   A OH  
449  N N   A ILE   A 18  ? 0.1276 0.1295 0.1511 -0.0265 0.0059  0.0346  18  ILE   A N   
450  N N   B ILE   A 18  ? 0.1478 0.1403 0.1951 -0.0236 0.0194  0.0284  18  ILE   A N   
451  C CA  A ILE   A 18  ? 0.1352 0.1329 0.1428 -0.0269 0.0115  0.0246  18  ILE   A CA  
452  C CA  B ILE   A 18  ? 0.1508 0.1453 0.1809 -0.0211 0.0210  0.0188  18  ILE   A CA  
453  C C   A ILE   A 18  ? 0.1299 0.1376 0.1486 -0.0338 0.0154  0.0201  18  ILE   A C   
454  C C   B ILE   A 18  ? 0.1498 0.1544 0.1724 -0.0165 0.0166  0.0176  18  ILE   A C   
455  O O   A ILE   A 18  ? 0.1257 0.1432 0.1499 -0.0414 0.0171  0.0283  18  ILE   A O   
456  O O   B ILE   A 18  ? 0.1540 0.1701 0.1715 -0.0236 0.0251  0.0197  18  ILE   A O   
457  C CB  A ILE   A 18  ? 0.1554 0.1381 0.1383 -0.0198 0.0067  0.0250  18  ILE   A CB  
458  C CB  B ILE   A 18  ? 0.1610 0.1498 0.1632 -0.0252 0.0114  0.0170  18  ILE   A CB  
459  C CG1 A ILE   A 18  ? 0.1686 0.1437 0.1266 -0.0125 -0.0099 0.0190  18  ILE   A CG1 
460  C CG1 B ILE   A 18  ? 0.1731 0.1529 0.1579 -0.0251 0.0086  0.0340  18  ILE   A CG1 
461  C CG2 A ILE   A 18  ? 0.1558 0.1376 0.1448 -0.0193 0.0063  0.0122  18  ILE   A CG2 
462  C CG2 B ILE   A 18  ? 0.1602 0.1556 0.1536 -0.0293 0.0130  0.0136  18  ILE   A CG2 
463  C CD1 A ILE   A 18  ? 0.1857 0.1489 0.1470 -0.0109 -0.0126 0.0085  18  ILE   A CD1 
464  C CD1 B ILE   A 18  ? 0.1966 0.1620 0.1719 -0.0210 -0.0020 0.0275  18  ILE   A CD1 
487  N N   A LYS   A 19  ? 0.1283 0.1387 0.1533 -0.0317 0.0303  0.0191  19  LYS   A N   
488  N N   B LYS   A 19  ? 0.1509 0.1583 0.1686 -0.0091 0.0226  0.0197  19  LYS   A N   
489  C CA  A LYS   A 19  ? 0.1348 0.1478 0.1644 -0.0201 0.0289  0.0154  19  LYS   A CA  
490  C CA  B LYS   A 19  ? 0.1584 0.1724 0.1773 0.0009  0.0234  0.0084  19  LYS   A CA  
491  C C   A LYS   A 19  ? 0.1227 0.1463 0.1789 -0.0110 0.0288  0.0215  19  LYS   A C   
492  C C   B LYS   A 19  ? 0.1502 0.1687 0.1938 0.0013  0.0287  0.0073  19  LYS   A C   
493  O O   A LYS   A 19  ? 0.1139 0.1466 0.1868 -0.0154 0.0175  0.0157  19  LYS   A O   
494  O O   B LYS   A 19  ? 0.1507 0.1631 0.2077 -0.0084 0.0361  0.0162  19  LYS   A O   
495  C CB  A LYS   A 19  ? 0.1461 0.1598 0.1655 -0.0308 0.0350  0.0046  19  LYS   A CB  
496  C CB  B LYS   A 19  ? 0.1730 0.1902 0.1720 -0.0052 0.0333  0.0022  19  LYS   A CB  
497  C CG  A LYS   A 19  ? 0.1689 0.1737 0.1700 -0.0293 0.0313  -0.0103 19  LYS   A CG  
498  C CG  B LYS   A 19  ? 0.1919 0.2032 0.1696 -0.0054 0.0252  -0.0070 19  LYS   A CG  
499  C CD  A LYS   A 19  ? 0.1846 0.1878 0.1736 -0.0289 0.0268  -0.0218 19  LYS   A CD  
500  C CD  B LYS   A 19  ? 0.2056 0.2129 0.1769 -0.0103 0.0285  -0.0099 19  LYS   A CD  
501  C CE  A LYS   A 19  ? 0.1940 0.1932 0.1688 -0.0279 0.0281  -0.0334 19  LYS   A CE  
502  C CE  B LYS   A 19  ? 0.2148 0.2203 0.1806 -0.0100 0.0265  -0.0133 19  LYS   A CE  
503  N NZ  A LYS   A 19  ? 0.2020 0.2016 0.1577 -0.0221 0.0294  -0.0427 19  LYS   A NZ  
504  N NZ  B LYS   A 19  ? 0.2227 0.2215 0.1884 -0.0163 0.0288  -0.0203 19  LYS   A NZ  
531  N N   A ASN   A 20  ? 0.1279 0.1568 0.1926 -0.0137 0.0294  0.0329  20  ASN   A N   
532  N N   B ASN   A 20  ? 0.1604 0.1775 0.2130 0.0007  0.0297  0.0018  20  ASN   A N   
533  C CA  A ASN   A 20  ? 0.1420 0.1769 0.2038 0.0042  0.0406  0.0284  20  ASN   A CA  
534  C CA  B ASN   A 20  ? 0.1691 0.1959 0.2261 0.0111  0.0256  0.0057  20  ASN   A CA  
535  C C   A ASN   A 20  ? 0.1583 0.1854 0.2122 -0.0053 0.0372  0.0217  20  ASN   A C   
536  C C   B ASN   A 20  ? 0.1715 0.1926 0.2270 0.0026  0.0232  0.0089  20  ASN   A C   
537  O O   A ASN   A 20  ? 0.1670 0.1956 0.2179 -0.0056 0.0303  0.0101  20  ASN   A O   
538  O O   B ASN   A 20  ? 0.1803 0.1992 0.2319 0.0001  0.0175  0.0069  20  ASN   A O   
539  C CB  A ASN   A 20  ? 0.1389 0.1888 0.2160 0.0188  0.0432  0.0346  20  ASN   A CB  
540  C CB  B ASN   A 20  ? 0.1783 0.2183 0.2406 0.0240  0.0361  0.0005  20  ASN   A CB  
541  C CG  A ASN   A 20  ? 0.1454 0.1971 0.2395 0.0309  0.0437  0.0403  20  ASN   A CG  
542  C CG  B ASN   A 20  ? 0.1909 0.2369 0.2557 0.0319  0.0436  0.0085  20  ASN   A CG  
543  O OD1 A ASN   A 20  ? 0.1590 0.2031 0.2494 0.0416  0.0452  0.0332  20  ASN   A OD1 
544  O OD1 B ASN   A 20  ? 0.2083 0.2520 0.2728 0.0354  0.0304  0.0069  20  ASN   A OD1 
545  N ND2 A ASN   A 20  ? 0.1557 0.1979 0.2555 0.0276  0.0353  0.0403  20  ASN   A ND2 
546  N ND2 B ASN   A 20  ? 0.1990 0.2383 0.2621 0.0314  0.0423  0.0189  20  ASN   A ND2 
559  N N   A ALA   A 21  ? 0.1609 0.1829 0.2159 -0.0075 0.0324  0.0165  21  ALA   A N   
560  N N   B ALA   A 21  ? 0.1683 0.1872 0.2448 0.0041  0.0294  0.0069  21  ALA   A N   
561  C CA  A ALA   A 21  ? 0.1664 0.1819 0.2265 -0.0125 0.0270  0.0102  21  ALA   A CA  
562  C CA  B ALA   A 21  ? 0.1738 0.1816 0.2561 0.0039  0.0289  0.0083  21  ALA   A CA  
563  C C   A ALA   A 21  ? 0.1604 0.1821 0.2315 -0.0158 0.0215  0.0193  21  ALA   A C   
564  C C   B ALA   A 21  ? 0.1702 0.1744 0.2543 0.0009  0.0386  0.0103  21  ALA   A C   
565  O O   A ALA   A 21  ? 0.1599 0.1869 0.2350 -0.0192 0.0124  0.0331  21  ALA   A O   
566  O O   B ALA   A 21  ? 0.1728 0.1776 0.2571 -0.0024 0.0460  0.0181  21  ALA   A O   
567  C CB  A ALA   A 21  ? 0.1811 0.1883 0.2271 -0.0217 0.0150  0.0044  21  ALA   A CB  
568  C CB  B ALA   A 21  ? 0.1974 0.1972 0.2740 -0.0064 0.0169  0.0113  21  ALA   A CB  
579  N N   A ASP   A 22  ? 0.1612 0.1850 0.2428 -0.0240 0.0220  0.0165  22  ASP   A N   
580  N N   B ASP   A 22  ? 0.1698 0.1744 0.2718 -0.0028 0.0403  0.0013  22  ASP   A N   
581  C CA  A ASP   A 22  ? 0.1612 0.1856 0.2395 -0.0262 0.0211  0.0150  22  ASP   A CA  
582  C CA  B ASP   A 22  ? 0.1813 0.1788 0.2713 -0.0037 0.0385  -0.0034 22  ASP   A CA  
583  C C   A ASP   A 22  ? 0.1558 0.1868 0.2181 -0.0207 0.0271  0.0315  22  ASP   A C   
584  C C   B ASP   A 22  ? 0.1721 0.1696 0.2349 -0.0045 0.0377  0.0035  22  ASP   A C   
585  O O   A ASP   A 22  ? 0.1539 0.1915 0.2165 -0.0166 0.0354  0.0502  22  ASP   A O   
586  O O   B ASP   A 22  ? 0.1778 0.1702 0.2505 0.0008  0.0417  0.0101  22  ASP   A O   
587  C CB  A ASP   A 22  ? 0.1768 0.1848 0.2629 -0.0272 0.0351  -0.0005 22  ASP   A CB  
588  C CB  B ASP   A 22  ? 0.1977 0.1891 0.3087 0.0060  0.0542  -0.0114 22  ASP   A CB  
589  C CG  A ASP   A 22  ? 0.1962 0.1839 0.2797 -0.0284 0.0479  -0.0130 22  ASP   A CG  
590  C CG  B ASP   A 22  ? 0.2140 0.1952 0.3462 0.0071  0.0691  -0.0061 22  ASP   A CG  
591  O OD1 A ASP   A 22  ? 0.1979 0.1807 0.2877 -0.0360 0.0395  -0.0027 22  ASP   A OD1 
592  O OD1 B ASP   A 22  ? 0.2069 0.1887 0.3548 -0.0037 0.0654  0.0147  22  ASP   A OD1 
593  O OD2 A ASP   A 22  ? 0.2091 0.1931 0.2799 -0.0146 0.0710  -0.0358 22  ASP   A OD2 
594  O OD2 B ASP   A 22  ? 0.2371 0.2192 0.3795 0.0081  0.0663  -0.0085 22  ASP   A OD2 
603  N N   A ILE   A 23  ? 0.1613 0.1867 0.2059 -0.0173 0.0192  0.0292  23  ILE   A N   
604  N N   B ILE   A 23  ? 0.1629 0.1680 0.2224 -0.0026 0.0358  0.0068  23  ILE   A N   
605  C CA  A ILE   A 23  ? 0.1655 0.1779 0.1869 -0.0074 0.0184  0.0324  23  ILE   A CA  
606  C CA  B ILE   A 23  ? 0.1556 0.1719 0.2102 -0.0084 0.0239  0.0088  23  ILE   A CA  
607  C C   A ILE   A 23  ? 0.1660 0.1821 0.1826 0.0001  0.0278  0.0315  23  ILE   A C   
608  C C   B ILE   A 23  ? 0.1549 0.1774 0.1996 -0.0153 0.0336  0.0022  23  ILE   A C   
609  O O   A ILE   A 23  ? 0.1717 0.1752 0.1813 0.0105  0.0263  0.0303  23  ILE   A O   
610  O O   B ILE   A 23  ? 0.1604 0.1834 0.2103 -0.0089 0.0380  -0.0035 23  ILE   A O   
611  C CB  A ILE   A 23  ? 0.1722 0.1718 0.1747 -0.0048 0.0098  0.0313  23  ILE   A CB  
612  C CB  B ILE   A 23  ? 0.1503 0.1621 0.1953 -0.0034 0.0223  0.0131  23  ILE   A CB  
613  C CG1 A ILE   A 23  ? 0.1739 0.1757 0.1802 -0.0068 0.0129  0.0233  23  ILE   A CG1 
614  C CG1 B ILE   A 23  ? 0.1552 0.1636 0.1920 0.0012  0.0140  0.0149  23  ILE   A CG1 
615  C CG2 A ILE   A 23  ? 0.1748 0.1675 0.1710 -0.0049 0.0062  0.0353  23  ILE   A CG2 
616  C CG2 B ILE   A 23  ? 0.1481 0.1600 0.2015 0.0025  0.0219  0.0082  23  ILE   A CG2 
617  C CD1 A ILE   A 23  ? 0.1768 0.1785 0.1798 -0.0058 0.0090  0.0153  23  ILE   A CD1 
618  C CD1 B ILE   A 23  ? 0.1577 0.1615 0.1938 0.0064  0.0106  0.0044  23  ILE   A CD1 
641  N N   A VAL   A 24  ? 0.1714 0.1910 0.1866 0.0003  0.0256  0.0280  24  VAL   A N   
642  N N   B VAL   A 24  ? 0.1630 0.1853 0.2118 -0.0218 0.0287  -0.0002 24  VAL   A N   
643  C CA  A VAL   A 24  ? 0.1823 0.2018 0.1926 -0.0020 0.0180  0.0327  24  VAL   A CA  
644  C CA  B VAL   A 24  ? 0.1827 0.1949 0.2311 -0.0230 0.0312  -0.0081 24  VAL   A CA  
645  C C   A VAL   A 24  ? 0.1937 0.2151 0.1989 -0.0048 0.0281  0.0320  24  VAL   A C   
646  C C   B VAL   A 24  ? 0.1967 0.2033 0.2280 -0.0191 0.0460  -0.0202 24  VAL   A C   
647  O O   A VAL   A 24  ? 0.1934 0.2160 0.1882 0.0081  0.0282  0.0408  24  VAL   A O   
648  O O   B VAL   A 24  ? 0.2082 0.2047 0.2267 -0.0109 0.0568  -0.0269 24  VAL   A O   
649  C CB  A VAL   A 24  ? 0.1818 0.2028 0.1959 -0.0040 0.0102  0.0351  24  VAL   A CB  
650  C CB  B VAL   A 24  ? 0.1783 0.2004 0.2485 -0.0267 0.0335  0.0034  24  VAL   A CB  
651  C CG1 A VAL   A 24  ? 0.1831 0.2029 0.1940 0.0017  0.0070  0.0273  24  VAL   A CG1 
652  C CG1 B VAL   A 24  ? 0.1814 0.2079 0.2608 -0.0289 0.0203  0.0015  24  VAL   A CG1 
653  C CG2 A VAL   A 24  ? 0.1835 0.2090 0.1973 -0.0012 0.0160  0.0408  24  VAL   A CG2 
654  C CG2 B VAL   A 24  ? 0.1808 0.2071 0.2581 -0.0194 0.0457  0.0144  24  VAL   A CG2 
673  N N   A GLU   A 25  ? 0.2054 0.2302 0.2209 -0.0130 0.0360  0.0225  25  GLU   A N   
674  N N   B GLU   A 25  ? 0.2075 0.2136 0.2448 -0.0157 0.0652  -0.0188 25  GLU   A N   
675  C CA  A GLU   A 25  ? 0.2200 0.2454 0.2315 -0.0197 0.0487  0.0188  25  GLU   A CA  
676  C CA  B GLU   A 25  ? 0.2286 0.2303 0.2625 -0.0154 0.0896  -0.0111 25  GLU   A CA  
677  C C   A GLU   A 25  ? 0.2077 0.2438 0.2150 -0.0266 0.0606  0.0193  25  GLU   A C   
678  C C   B GLU   A 25  ? 0.2277 0.2286 0.2479 -0.0111 0.0984  -0.0083 25  GLU   A C   
679  O O   A GLU   A 25  ? 0.2103 0.2489 0.2196 -0.0218 0.0640  0.0162  25  GLU   A O   
680  O O   B GLU   A 25  ? 0.2343 0.2341 0.2632 -0.0013 0.1041  -0.0094 25  GLU   A O   
681  C CB  A GLU   A 25  ? 0.2432 0.2613 0.2629 -0.0211 0.0532  0.0189  25  GLU   A CB  
682  C CB  B GLU   A 25  ? 0.2529 0.2474 0.2843 -0.0188 0.1087  -0.0043 25  GLU   A CB  
683  C CG  A GLU   A 25  ? 0.2660 0.2749 0.3002 -0.0258 0.0513  0.0172  25  GLU   A CG  
684  C CG  B GLU   A 25  ? 0.2800 0.2621 0.3045 -0.0208 0.1155  0.0048  25  GLU   A CG  
685  C CD  A GLU   A 25  ? 0.2820 0.2844 0.3341 -0.0324 0.0537  0.0193  25  GLU   A CD  
686  C CD  B GLU   A 25  ? 0.3065 0.2767 0.3303 -0.0250 0.1165  0.0104  25  GLU   A CD  
687  O OE1 A GLU   A 25  ? 0.2861 0.2866 0.3422 -0.0370 0.0527  0.0188  25  GLU   A OE1 
688  O OE1 B GLU   A 25  ? 0.3202 0.2826 0.3385 -0.0205 0.1087  0.0068  25  GLU   A OE1 
689  O OE2 A GLU   A 25  ? 0.2887 0.2873 0.3531 -0.0339 0.0541  0.0196  25  GLU   A OE2 
690  O OE2 B GLU   A 25  ? 0.3214 0.2843 0.3558 -0.0300 0.1129  0.0175  25  GLU   A OE2 
703  N N   A GLU   A 26  ? 0.2013 0.2379 0.2101 -0.0407 0.0665  0.0193  26  GLU   A N   
704  N N   B GLU   A 26  ? 0.2228 0.2192 0.2435 -0.0089 0.0907  -0.0103 26  GLU   A N   
705  C CA  A GLU   A 26  ? 0.2037 0.2323 0.2187 -0.0509 0.0647  0.0226  26  GLU   A CA  
706  C CA  B GLU   A 26  ? 0.2280 0.2178 0.2353 -0.0098 0.0834  -0.0057 26  GLU   A CA  
707  C C   A GLU   A 26  ? 0.1981 0.2249 0.1992 -0.0545 0.0608  0.0205  26  GLU   A C   
708  C C   B GLU   A 26  ? 0.2303 0.2253 0.2169 -0.0195 0.0777  -0.0124 26  GLU   A C   
709  O O   A GLU   A 26  ? 0.1982 0.2196 0.1910 -0.0524 0.0588  0.0215  26  GLU   A O   
710  O O   B GLU   A 26  ? 0.2359 0.2334 0.2228 -0.0205 0.0677  -0.0160 26  GLU   A O   
711  C CB  A GLU   A 26  ? 0.2145 0.2261 0.2416 -0.0622 0.0674  0.0281  26  GLU   A CB  
712  C CB  B GLU   A 26  ? 0.2343 0.2179 0.2495 -0.0062 0.0811  -0.0032 26  GLU   A CB  
713  C CG  A GLU   A 26  ? 0.2285 0.2240 0.2728 -0.0672 0.0703  0.0241  26  GLU   A CG  
714  C CG  B GLU   A 26  ? 0.2402 0.2151 0.2677 -0.0149 0.0846  0.0040  26  GLU   A CG  
715  C CD  A GLU   A 26  ? 0.2399 0.2292 0.3015 -0.0686 0.0797  0.0228  26  GLU   A CD  
716  C CD  B GLU   A 26  ? 0.2425 0.2110 0.2643 -0.0209 0.0946  0.0030  26  GLU   A CD  
717  O OE1 A GLU   A 26  ? 0.2448 0.2395 0.3156 -0.0608 0.0818  0.0130  26  GLU   A OE1 
718  O OE1 B GLU   A 26  ? 0.2380 0.2126 0.2502 -0.0245 0.0990  0.0050  26  GLU   A OE1 
719  O OE2 A GLU   A 26  ? 0.2521 0.2302 0.3131 -0.0664 0.0823  0.0260  26  GLU   A OE2 
720  O OE2 B GLU   A 26  ? 0.2560 0.2174 0.2696 -0.0138 0.1019  -0.0112 26  GLU   A OE2 
733  N N   A ALA   A 27  ? 0.1959 0.2243 0.1929 -0.0609 0.0556  0.0175  27  ALA   A N   
734  N N   B ALA   A 27  ? 0.2252 0.2266 0.2128 -0.0274 0.0722  -0.0162 27  ALA   A N   
735  C CA  A ALA   A 27  ? 0.2082 0.2334 0.1845 -0.0601 0.0520  0.0113  27  ALA   A CA  
736  C CA  B ALA   A 27  ? 0.2301 0.2311 0.2095 -0.0392 0.0729  -0.0238 27  ALA   A CA  
737  C C   A ALA   A 27  ? 0.2308 0.2510 0.1899 -0.0591 0.0531  -0.0074 27  ALA   A C   
738  C C   B ALA   A 27  ? 0.2578 0.2574 0.2138 -0.0450 0.0725  -0.0344 27  ALA   A C   
739  O O   A ALA   A 27  ? 0.2297 0.2457 0.1808 -0.0714 0.0458  -0.0128 27  ALA   A O   
740  O O   B ALA   A 27  ? 0.2618 0.2565 0.2078 -0.0488 0.0652  -0.0278 27  ALA   A O   
741  C CB  A ALA   A 27  ? 0.2016 0.2270 0.1784 -0.0615 0.0457  0.0132  27  ALA   A CB  
742  C CB  B ALA   A 27  ? 0.2157 0.2203 0.2132 -0.0387 0.0736  -0.0300 27  ALA   A CB  
753  N N   A LYS   A 28  ? 0.2597 0.2781 0.2183 -0.0438 0.0454  -0.0246 28  LYS   A N   
754  N N   B LYS   A 28  ? 0.2892 0.2888 0.2338 -0.0426 0.0698  -0.0530 28  LYS   A N   
755  C CA  A LYS   A 28  ? 0.2950 0.3102 0.2592 -0.0286 0.0371  -0.0356 28  LYS   A CA  
756  C CA  B LYS   A 28  ? 0.3246 0.3244 0.2668 -0.0368 0.0659  -0.0550 28  LYS   A CA  
757  C C   A LYS   A 28  ? 0.3175 0.3358 0.2632 -0.0275 0.0444  -0.0299 28  LYS   A C   
758  C C   B LYS   A 28  ? 0.3424 0.3476 0.2596 -0.0441 0.0734  -0.0475 28  LYS   A C   
759  O O   A LYS   A 28  ? 0.3217 0.3417 0.2804 -0.0244 0.0372  -0.0286 28  LYS   A O   
760  O O   B LYS   A 28  ? 0.3491 0.3532 0.2870 -0.0409 0.0546  -0.0422 28  LYS   A O   
761  C CB  A LYS   A 28  ? 0.3065 0.3178 0.2940 -0.0162 0.0257  -0.0503 28  LYS   A CB  
762  C CB  B LYS   A 28  ? 0.3388 0.3358 0.3001 -0.0245 0.0648  -0.0625 28  LYS   A CB  
763  C CG  A LYS   A 28  ? 0.3162 0.3253 0.3252 -0.0078 0.0186  -0.0566 28  LYS   A CG  
764  C CG  B LYS   A 28  ? 0.3521 0.3469 0.3348 -0.0131 0.0653  -0.0638 28  LYS   A CG  
765  C CD  A LYS   A 28  ? 0.3235 0.3330 0.3618 -0.0023 0.0116  -0.0587 28  LYS   A CD  
766  C CD  B LYS   A 28  ? 0.3640 0.3569 0.3793 -0.0045 0.0586  -0.0644 28  LYS   A CD  
767  C CE  A LYS   A 28  ? 0.3274 0.3381 0.3890 0.0013  0.0044  -0.0592 28  LYS   A CE  
768  C CE  B LYS   A 28  ? 0.3717 0.3623 0.4135 -0.0012 0.0528  -0.0653 28  LYS   A CE  
769  N NZ  A LYS   A 28  ? 0.3290 0.3402 0.4059 0.0034  0.0024  -0.0572 28  LYS   A NZ  
770  N NZ  B LYS   A 28  ? 0.3744 0.3648 0.4343 0.0005  0.0502  -0.0646 28  LYS   A NZ  
797  N N   A LYS   A 29  ? 0.3344 0.3543 0.2680 -0.0322 0.0589  -0.0207 29  LYS   A N   
798  N N   B LYS   A 29  ? 0.3504 0.3657 0.2526 -0.0545 0.0960  -0.0372 29  LYS   A N   
799  C CA  A LYS   A 29  ? 0.3526 0.3725 0.2890 -0.0358 0.0645  -0.0147 29  LYS   A CA  
800  C CA  B LYS   A 29  ? 0.3623 0.3823 0.2589 -0.0638 0.1104  -0.0272 29  LYS   A CA  
801  C C   A LYS   A 29  ? 0.3492 0.3666 0.2652 -0.0447 0.0596  -0.0116 29  LYS   A C   
802  C C   B LYS   A 29  ? 0.3501 0.3708 0.2178 -0.0769 0.1109  -0.0196 29  LYS   A C   
803  O O   A LYS   A 29  ? 0.3517 0.3691 0.2761 -0.0420 0.0570  -0.0128 29  LYS   A O   
804  O O   B LYS   A 29  ? 0.3524 0.3729 0.2220 -0.0729 0.1091  -0.0208 29  LYS   A O   
805  C CB  A LYS   A 29  ? 0.3702 0.3933 0.3414 -0.0307 0.0716  -0.0130 29  LYS   A CB  
806  C CB  B LYS   A 29  ? 0.3832 0.4084 0.3220 -0.0609 0.1184  -0.0256 29  LYS   A CB  
807  C CG  A LYS   A 29  ? 0.3856 0.4110 0.3985 -0.0266 0.0764  -0.0122 29  LYS   A CG  
808  C CG  B LYS   A 29  ? 0.4014 0.4306 0.3925 -0.0581 0.1235  -0.0242 29  LYS   A CG  
809  C CD  A LYS   A 29  ? 0.3994 0.4264 0.4523 -0.0232 0.0781  -0.0120 29  LYS   A CD  
810  C CD  B LYS   A 29  ? 0.4181 0.4484 0.4573 -0.0551 0.1251  -0.0248 29  LYS   A CD  
811  C CE  A LYS   A 29  ? 0.4097 0.4378 0.4918 -0.0200 0.0791  -0.0125 29  LYS   A CE  
812  C CE  B LYS   A 29  ? 0.4304 0.4609 0.5047 -0.0524 0.1261  -0.0246 29  LYS   A CE  
813  N NZ  A LYS   A 29  ? 0.4154 0.4446 0.5153 -0.0184 0.0788  -0.0132 29  LYS   A NZ  
814  N NZ  B LYS   A 29  ? 0.4374 0.4686 0.5333 -0.0506 0.1259  -0.0252 29  LYS   A NZ  
841  N N   A VAL   A 30  ? 0.3419 0.3563 0.2429 -0.0559 0.0551  -0.0095 30  VAL   A N   
842  N N   B VAL   A 30  ? 0.3336 0.3553 0.1907 -0.0938 0.1080  -0.0169 30  VAL   A N   
843  C CA  A VAL   A 30  ? 0.3390 0.3464 0.2333 -0.0642 0.0411  -0.0023 30  VAL   A CA  
844  C CA  B VAL   A 30  ? 0.3280 0.3449 0.1991 -0.1055 0.0820  -0.0110 30  VAL   A CA  
845  C C   A VAL   A 30  ? 0.3409 0.3354 0.2158 -0.0658 0.0368  -0.0070 30  VAL   A C   
846  C C   B VAL   A 30  ? 0.3269 0.3278 0.1661 -0.1064 0.0722  -0.0059 30  VAL   A C   
847  O O   A VAL   A 30  ? 0.3428 0.3333 0.2085 -0.0665 0.0380  -0.0091 30  VAL   A O   
848  O O   B VAL   A 30  ? 0.3301 0.3305 0.1667 -0.1062 0.0679  -0.0048 30  VAL   A O   
849  C CB  A VAL   A 30  ? 0.3354 0.3456 0.2474 -0.0681 0.0285  0.0031  30  VAL   A CB  
850  C CB  B VAL   A 30  ? 0.3241 0.3497 0.2394 -0.1138 0.0569  -0.0154 30  VAL   A CB  
851  C CG1 A VAL   A 30  ? 0.3346 0.3456 0.2500 -0.0696 0.0194  0.0048  30  VAL   A CG1 
852  C CG1 B VAL   A 30  ? 0.3251 0.3522 0.2509 -0.1166 0.0430  -0.0191 30  VAL   A CG1 
853  C CG2 A VAL   A 30  ? 0.3336 0.3445 0.2592 -0.0699 0.0265  0.0060  30  VAL   A CG2 
854  C CG2 B VAL   A 30  ? 0.3218 0.3500 0.2603 -0.1159 0.0532  -0.0150 30  VAL   A CG2 
873  N N   A LYS   A 31  ? 0.3397 0.3267 0.2195 -0.0665 0.0300  -0.0077 31  LYS   A N   
874  N N   B LYS   A 31  ? 0.3163 0.3087 0.1581 -0.1085 0.0670  -0.0080 31  LYS   A N   
875  C CA  A LYS   A 31  ? 0.3417 0.3217 0.2369 -0.0612 0.0145  -0.0088 31  LYS   A CA  
876  C CA  B LYS   A 31  ? 0.3226 0.2999 0.1712 -0.0950 0.0420  -0.0083 31  LYS   A CA  
877  C C   A LYS   A 31  ? 0.3229 0.3022 0.2007 -0.0605 0.0093  0.0100  31  LYS   A C   
878  C C   B LYS   A 31  ? 0.3056 0.2766 0.1400 -0.0878 0.0348  0.0048  31  LYS   A C   
879  O O   A LYS   A 31  ? 0.3250 0.3074 0.2024 -0.0591 0.0011  0.0116  31  LYS   A O   
880  O O   B LYS   A 31  ? 0.3065 0.2777 0.1605 -0.0856 0.0250  0.0142  31  LYS   A O   
881  C CB  A LYS   A 31  ? 0.3605 0.3362 0.3082 -0.0547 0.0035  -0.0229 31  LYS   A CB  
882  C CB  B LYS   A 31  ? 0.3508 0.3197 0.2698 -0.0839 0.0227  -0.0163 31  LYS   A CB  
883  C CG  A LYS   A 31  ? 0.3780 0.3505 0.3830 -0.0458 -0.0091 -0.0308 31  LYS   A CG  
884  C CG  B LYS   A 31  ? 0.3808 0.3413 0.3817 -0.0671 -0.0001 -0.0196 31  LYS   A CG  
885  C CD  A LYS   A 31  ? 0.3913 0.3617 0.4437 -0.0392 -0.0182 -0.0359 31  LYS   A CD  
886  C CD  B LYS   A 31  ? 0.4038 0.3589 0.4730 -0.0544 -0.0176 -0.0226 31  LYS   A CD  
887  C CE  A LYS   A 31  ? 0.4005 0.3704 0.4834 -0.0332 -0.0253 -0.0396 31  LYS   A CE  
888  C CE  B LYS   A 31  ? 0.4191 0.3718 0.5307 -0.0452 -0.0336 -0.0281 31  LYS   A CE  
889  N NZ  A LYS   A 31  ? 0.4060 0.3748 0.5037 -0.0297 -0.0282 -0.0420 31  LYS   A NZ  
890  N NZ  B LYS   A 31  ? 0.4268 0.3797 0.5597 -0.0411 -0.0417 -0.0307 31  LYS   A NZ  
917  N N   A PRO   A 32  ? 0.3008 0.2776 0.1771 -0.0622 0.0096  0.0190  32  PRO   A N   
918  N N   B PRO   A 32  ? 0.2839 0.2499 0.1076 -0.0809 0.0333  0.0014  32  PRO   A N   
919  C CA  A PRO   A 32  ? 0.2888 0.2610 0.1794 -0.0627 0.0025  0.0327  32  PRO   A CA  
920  C CA  B PRO   A 32  ? 0.2757 0.2318 0.1425 -0.0754 0.0203  0.0096  32  PRO   A CA  
921  C C   A PRO   A 32  ? 0.2775 0.2468 0.1782 -0.0586 -0.0074 0.0426  32  PRO   A C   
922  C C   B PRO   A 32  ? 0.2698 0.2211 0.1644 -0.0618 0.0057  0.0121  32  PRO   A C   
923  O O   A PRO   A 32  ? 0.2748 0.2421 0.1814 -0.0614 -0.0208 0.0460  32  PRO   A O   
924  O O   B PRO   A 32  ? 0.2626 0.2104 0.1609 -0.0638 0.0077  -0.0021 32  PRO   A O   
925  C CB  A PRO   A 32  ? 0.2911 0.2644 0.1809 -0.0609 0.0030  0.0274  32  PRO   A CB  
926  C CB  B PRO   A 32  ? 0.2771 0.2357 0.1449 -0.0752 0.0172  0.0079  32  PRO   A CB  
927  C CG  A PRO   A 32  ? 0.2930 0.2684 0.1705 -0.0584 0.0023  0.0246  32  PRO   A CG  
928  C CG  B PRO   A 32  ? 0.2743 0.2396 0.1087 -0.0761 0.0114  0.0100  32  PRO   A CG  
929  C CD  A PRO   A 32  ? 0.2951 0.2716 0.1725 -0.0603 0.0059  0.0217  32  PRO   A CD  
930  C CD  B PRO   A 32  ? 0.2777 0.2414 0.1043 -0.0818 0.0234  0.0098  32  PRO   A CD  
945  N N   A THR   A 33  ? 0.2705 0.2374 0.1824 -0.0517 -0.0073 0.0459  33  THR   A N   
946  N N   B THR   A 33  ? 0.2685 0.2220 0.1797 -0.0484 -0.0063 0.0237  33  THR   A N   
947  C CA  A THR   A 33  ? 0.2623 0.2293 0.1774 -0.0394 -0.0204 0.0444  33  THR   A CA  
948  C CA  B THR   A 33  ? 0.2695 0.2281 0.1898 -0.0367 -0.0201 0.0294  33  THR   A CA  
949  C C   A THR   A 33  ? 0.2416 0.2080 0.1670 -0.0385 -0.0243 0.0331  33  THR   A C   
950  C C   B THR   A 33  ? 0.2445 0.2096 0.1761 -0.0335 -0.0215 0.0226  33  THR   A C   
951  O O   A THR   A 33  ? 0.2387 0.2042 0.1691 -0.0375 -0.0346 0.0248  33  THR   A O   
952  O O   B THR   A 33  ? 0.2383 0.2090 0.1838 -0.0239 -0.0298 0.0176  33  THR   A O   
953  C CB  A THR   A 33  ? 0.2715 0.2398 0.1900 -0.0296 -0.0226 0.0537  33  THR   A CB  
954  C CB  B THR   A 33  ? 0.2902 0.2466 0.2107 -0.0291 -0.0256 0.0461  33  THR   A CB  
955  O OG1 A THR   A 33  ? 0.2775 0.2459 0.2094 -0.0218 -0.0146 0.0594  33  THR   A OG1 
956  O OG1 B THR   A 33  ? 0.3056 0.2584 0.2339 -0.0243 -0.0180 0.0598  33  THR   A OG1 
957  C CG2 A THR   A 33  ? 0.2733 0.2446 0.1967 -0.0284 -0.0267 0.0529  33  THR   A CG2 
958  C CG2 B THR   A 33  ? 0.2922 0.2521 0.2218 -0.0223 -0.0373 0.0441  33  THR   A CG2 
973  N N   . VAL   A 34  ? 0.2222 0.1916 0.1645 -0.0364 -0.0231 0.0316  34  VAL   A N   
974  C CA  . VAL   A 34  ? 0.1974 0.1723 0.1622 -0.0264 -0.0115 0.0333  34  VAL   A CA  
975  C C   . VAL   A 34  ? 0.1787 0.1628 0.1608 -0.0305 -0.0021 0.0276  34  VAL   A C   
976  O O   . VAL   A 34  ? 0.1796 0.1650 0.1898 -0.0425 0.0034  0.0326  34  VAL   A O   
977  C CB  . VAL   A 34  ? 0.1917 0.1666 0.1813 -0.0238 -0.0062 0.0163  34  VAL   A CB  
978  C CG1 . VAL   A 34  ? 0.1912 0.1633 0.1798 -0.0195 0.0049  0.0015  34  VAL   A CG1 
979  C CG2 . VAL   A 34  ? 0.1916 0.1783 0.1908 -0.0162 -0.0093 0.0141  34  VAL   A CG2 
990  N N   . VAL   A 35  ? 0.1608 0.1511 0.1520 -0.0343 -0.0004 0.0122  35  VAL   A N   
991  C CA  . VAL   A 35  ? 0.1524 0.1488 0.1537 -0.0301 0.0061  0.0059  35  VAL   A CA  
992  C C   . VAL   A 35  ? 0.1380 0.1315 0.1573 -0.0222 0.0085  0.0090  35  VAL   A C   
993  O O   . VAL   A 35  ? 0.1332 0.1374 0.1741 -0.0232 0.0026  0.0076  35  VAL   A O   
994  C CB  . VAL   A 35  ? 0.1576 0.1641 0.1601 -0.0235 0.0141  -0.0044 35  VAL   A CB  
995  C CG1 . VAL   A 35  ? 0.1671 0.1612 0.1748 -0.0183 0.0083  -0.0106 35  VAL   A CG1 
996  C CG2 . VAL   A 35  ? 0.1551 0.1617 0.1738 -0.0171 0.0226  -0.0068 35  VAL   A CG2 
1006 N N   . VAL   A 36  ? 0.1240 0.1285 0.1622 -0.0270 0.0145  0.0081  36  VAL   A N   
1007 C CA  . VAL   A 36  ? 0.1137 0.1224 0.1692 -0.0129 0.0077  0.0082  36  VAL   A CA  
1008 C C   . VAL   A 36  ? 0.1158 0.1172 0.1759 -0.0155 0.0020  0.0080  36  VAL   A C   
1009 O O   . VAL   A 36  ? 0.1242 0.1208 0.1991 -0.0017 0.0216  0.0028  36  VAL   A O   
1010 C CB  . VAL   A 36  ? 0.1187 0.1164 0.1726 -0.0131 0.0080  0.0160  36  VAL   A CB  
1011 C CG1 . VAL   A 36  ? 0.1277 0.1217 0.1837 -0.0193 0.0007  -0.0037 36  VAL   A CG1 
1012 C CG2 . VAL   A 36  ? 0.1275 0.1230 0.1972 -0.0085 -0.0002 0.0159  36  VAL   A CG2 
1022 N N   . ASN   A 37  ? 0.1086 0.1146 0.1726 -0.0096 -0.0004 0.0133  37  ASN   A N   
1023 C CA  . ASN   A 37  ? 0.1084 0.1159 0.1749 -0.0000 0.0048  0.0104  37  ASN   A CA  
1024 C C   . ASN   A 37  ? 0.1052 0.1152 0.1663 -0.0048 0.0117  0.0157  37  ASN   A C   
1025 O O   . ASN   A 37  ? 0.1177 0.1200 0.1633 0.0007  0.0081  0.0088  37  ASN   A O   
1026 C CB  . ASN   A 37  ? 0.1088 0.1114 0.1867 0.0026  0.0099  0.0095  37  ASN   A CB  
1027 C CG  . ASN   A 37  ? 0.1117 0.1100 0.1920 0.0098  0.0055  0.0091  37  ASN   A CG  
1028 O OD1 . ASN   A 37  ? 0.1149 0.1109 0.2041 0.0039  0.0060  0.0175  37  ASN   A OD1 
1029 N ND2 . ASN   A 37  ? 0.1158 0.1098 0.1964 -0.0033 0.0018  0.0222  37  ASN   A ND2 
1036 N N   A ALA   A 38  ? 0.1094 0.1195 0.1581 -0.0025 0.0040  0.0078  38  ALA   A N   
1037 N N   B ALA   A 38  ? 0.1081 0.1263 0.1829 -0.0013 0.0060  0.0104  38  ALA   A N   
1038 C CA  A ALA   A 38  ? 0.1154 0.1176 0.1517 -0.0038 -0.0007 -0.0054 38  ALA   A CA  
1039 C CA  B ALA   A 38  ? 0.1132 0.1359 0.1974 -0.0092 -0.0001 0.0070  38  ALA   A CA  
1040 C C   A ALA   A 38  ? 0.1163 0.1110 0.1455 0.0007  -0.0101 -0.0030 38  ALA   A C   
1041 C C   B ALA   A 38  ? 0.1069 0.1211 0.1940 0.0021  -0.0081 0.0045  38  ALA   A C   
1042 O O   A ALA   A 38  ? 0.1222 0.1056 0.1554 0.0048  -0.0180 -0.0077 38  ALA   A O   
1043 O O   B ALA   A 38  ? 0.1007 0.1186 0.2009 0.0030  -0.0166 0.0082  38  ALA   A O   
1044 C CB  A ALA   A 38  ? 0.1147 0.1240 0.1644 -0.0105 -0.0135 -0.0026 38  ALA   A CB  
1045 C CB  B ALA   A 38  ? 0.1135 0.1563 0.2163 -0.0137 -0.0138 0.0094  38  ALA   A CB  
1056 N N   A ALA   A 39  ? 0.1132 0.1080 0.1487 0.0006  -0.0029 0.0052  39  ALA   A N   
1057 N N   B ALA   A 39  ? 0.1130 0.1177 0.1997 0.0073  0.0013  0.0102  39  ALA   A N   
1058 C CA  A ALA   A 39  ? 0.1181 0.1160 0.1637 0.0013  0.0102  0.0085  39  ALA   A CA  
1059 C CA  B ALA   A 39  ? 0.1157 0.1120 0.1898 0.0039  0.0034  -0.0013 39  ALA   A CA  
1060 C C   A ALA   A 39  ? 0.1153 0.1155 0.1681 0.0032  -0.0019 0.0077  39  ALA   A C   
1061 C C   B ALA   A 39  ? 0.1078 0.1059 0.1855 0.0039  -0.0044 0.0005  39  ALA   A C   
1062 O O   A ALA   A 39  ? 0.1125 0.1151 0.1667 0.0020  -0.0060 0.0160  39  ALA   A O   
1063 O O   B ALA   A 39  ? 0.1213 0.1075 0.1781 0.0018  0.0010  -0.0097 39  ALA   A O   
1064 C CB  A ALA   A 39  ? 0.1166 0.1297 0.1620 -0.0013 0.0021  0.0065  39  ALA   A CB  
1065 C CB  B ALA   A 39  ? 0.1208 0.1271 0.1869 -0.0060 -0.0096 -0.0061 39  ALA   A CB  
1076 N N   A ASN   A 40  ? 0.1168 0.1207 0.1664 -0.0037 0.0095  0.0035  40  ASN   A N   
1077 N N   B ASN   A 40  ? 0.1159 0.1123 0.1792 -0.0068 0.0084  0.0023  40  ASN   A N   
1078 C CA  A ASN   A 40  ? 0.1239 0.1223 0.1606 0.0001  -0.0025 0.0027  40  ASN   A CA  
1079 C CA  B ASN   A 40  ? 0.1270 0.1099 0.1895 -0.0008 -0.0064 0.0143  40  ASN   A CA  
1080 C C   A ASN   A 40  ? 0.1274 0.1129 0.1439 -0.0051 -0.0011 0.0074  40  ASN   A C   
1081 C C   B ASN   A 40  ? 0.1281 0.1027 0.1755 -0.0052 0.0061  0.0167  40  ASN   A C   
1082 O O   A ASN   A 40  ? 0.1315 0.1147 0.1473 -0.0069 0.0056  0.0115  40  ASN   A O   
1083 O O   B ASN   A 40  ? 0.1246 0.1036 0.1741 -0.0053 0.0108  0.0142  40  ASN   A O   
1084 C CB  A ASN   A 40  ? 0.1288 0.1309 0.1660 -0.0014 0.0012  -0.0057 40  ASN   A CB  
1085 C CB  B ASN   A 40  ? 0.1299 0.1119 0.2053 -0.0001 -0.0147 0.0161  40  ASN   A CB  
1086 C CG  A ASN   A 40  ? 0.1350 0.1388 0.1853 -0.0080 0.0140  0.0019  40  ASN   A CG  
1087 C CG  B ASN   A 40  ? 0.1348 0.1081 0.2321 0.0045  -0.0146 0.0156  40  ASN   A CG  
1088 O OD1 A ASN   A 40  ? 0.1369 0.1391 0.1892 -0.0145 0.0405  0.0096  40  ASN   A OD1 
1089 O OD1 B ASN   A 40  ? 0.1454 0.1114 0.2671 -0.0010 -0.0086 -0.0004 40  ASN   A OD1 
1090 N ND2 A ASN   A 40  ? 0.1399 0.1502 0.2023 -0.0001 0.0097  -0.0077 40  ASN   A ND2 
1091 N ND2 B ASN   A 40  ? 0.1347 0.1213 0.2429 0.0070  -0.0209 0.0073  40  ASN   A ND2 
1104 N N   A VAL   A 41  ? 0.1263 0.1089 0.1282 -0.0030 -0.0044 0.0060  41  VAL   A N   
1105 N N   B VAL   A 41  ? 0.1280 0.1055 0.1766 0.0005  0.0014  0.0231  41  VAL   A N   
1106 C CA  A VAL   A 41  ? 0.1217 0.1162 0.1363 0.0011  -0.0038 0.0087  41  VAL   A CA  
1107 C CA  B VAL   A 41  ? 0.1355 0.1197 0.1772 -0.0025 -0.0026 0.0150  41  VAL   A CA  
1108 C C   A VAL   A 41  ? 0.1218 0.1153 0.1351 0.0014  -0.0056 0.0100  41  VAL   A C   
1109 C C   B VAL   A 41  ? 0.1311 0.1193 0.1656 -0.0022 0.0020  0.0109  41  VAL   A C   
1110 O O   A VAL   A 41  ? 0.1318 0.1135 0.1080 0.0015  -0.0137 0.0092  41  VAL   A O   
1111 O O   B VAL   A 41  ? 0.1415 0.1164 0.1251 0.0028  -0.0046 0.0084  41  VAL   A O   
1112 C CB  A VAL   A 41  ? 0.1184 0.1195 0.1212 0.0023  0.0020  0.0130  41  VAL   A CB  
1113 C CB  B VAL   A 41  ? 0.1476 0.1367 0.1835 -0.0092 0.0022  0.0119  41  VAL   A CB  
1114 C CG1 A VAL   A 41  ? 0.1143 0.1258 0.1273 0.0125  0.0005  0.0122  41  VAL   A CG1 
1115 C CG1 B VAL   A 41  ? 0.1587 0.1486 0.1904 -0.0104 0.0058  -0.0059 41  VAL   A CG1 
1116 C CG2 A VAL   A 41  ? 0.1181 0.1214 0.1129 -0.0099 0.0073  0.0191  41  VAL   A CG2 
1117 C CG2 B VAL   A 41  ? 0.1599 0.1492 0.1954 -0.0093 -0.0057 0.0200  41  VAL   A CG2 
1136 N N   A TYR   A 42  ? 0.1134 0.1140 0.1631 0.0024  -0.0001 0.0155  42  TYR   A N   
1137 N N   B TYR   A 42  ? 0.1163 0.1149 0.1885 -0.0051 0.0139  0.0229  42  TYR   A N   
1138 C CA  A TYR   A 42  ? 0.1257 0.1145 0.1723 -0.0021 0.0006  0.0150  42  TYR   A CA  
1139 C CA  B TYR   A 42  ? 0.1222 0.1113 0.1908 -0.0002 0.0095  0.0182  42  TYR   A CA  
1140 C C   A TYR   A 42  ? 0.1178 0.1085 0.1855 -0.0064 0.0022  0.0075  42  TYR   A C   
1141 C C   B TYR   A 42  ? 0.1199 0.1094 0.1865 -0.0036 0.0110  0.0190  42  TYR   A C   
1142 O O   A TYR   A 42  ? 0.1195 0.1125 0.1897 -0.0169 -0.0002 0.0010  42  TYR   A O   
1143 O O   B TYR   A 42  ? 0.1240 0.1142 0.1880 -0.0108 0.0075  0.0092  42  TYR   A O   
1144 C CB  A TYR   A 42  ? 0.1511 0.1267 0.1690 -0.0134 0.0041  0.0280  42  TYR   A CB  
1145 C CB  B TYR   A 42  ? 0.1434 0.1153 0.1898 -0.0019 0.0034  0.0249  42  TYR   A CB  
1146 C CG  A TYR   A 42  ? 0.1762 0.1397 0.1791 -0.0216 0.0034  0.0327  42  TYR   A CG  
1147 C CG  B TYR   A 42  ? 0.1788 0.1384 0.1929 -0.0017 0.0012  0.0251  42  TYR   A CG  
1148 C CD1 A TYR   A 42  ? 0.1884 0.1510 0.1907 -0.0259 0.0166  0.0277  42  TYR   A CD1 
1149 C CD1 B TYR   A 42  ? 0.1921 0.1496 0.1936 -0.0018 0.0092  0.0305  42  TYR   A CD1 
1150 C CD2 A TYR   A 42  ? 0.1905 0.1522 0.1920 -0.0221 -0.0076 0.0228  42  TYR   A CD2 
1151 C CD2 B TYR   A 42  ? 0.2023 0.1633 0.2017 -0.0002 -0.0054 0.0133  42  TYR   A CD2 
1152 C CE1 A TYR   A 42  ? 0.2010 0.1605 0.1939 -0.0304 0.0201  0.0199  42  TYR   A CE1 
1153 C CE1 B TYR   A 42  ? 0.2076 0.1633 0.2006 -0.0068 0.0146  0.0189  42  TYR   A CE1 
1154 C CE2 A TYR   A 42  ? 0.2019 0.1620 0.2024 -0.0325 0.0024  0.0228  42  TYR   A CE2 
1155 C CE2 B TYR   A 42  ? 0.2185 0.1775 0.2159 -0.0096 0.0037  0.0167  42  TYR   A CE2 
1156 C CZ  A TYR   A 42  ? 0.2114 0.1678 0.2029 -0.0344 0.0171  0.0253  42  TYR   A CZ  
1157 C CZ  B TYR   A 42  ? 0.2276 0.1805 0.2080 -0.0114 0.0153  0.0137  42  TYR   A CZ  
1158 O OH  A TYR   A 42  ? 0.2208 0.1876 0.2241 -0.0405 0.0345  0.0273  42  TYR   A OH  
1159 O OH  B TYR   A 42  ? 0.2432 0.2074 0.2318 -0.0206 0.0241  0.0070  42  TYR   A OH  
1178 N N   A LEU   A 43  ? 0.1188 0.1064 0.1793 -0.0093 -0.0003 -0.0021 43  LEU   A N   
1179 N N   B LEU   A 43  ? 0.1127 0.1151 0.1880 0.0022  0.0101  0.0128  43  LEU   A N   
1180 C CA  A LEU   A 43  ? 0.1175 0.1016 0.1747 -0.0084 -0.0006 -0.0093 43  LEU   A CA  
1181 C CA  B LEU   A 43  ? 0.1148 0.1126 0.1880 0.0029  0.0094  0.0073  43  LEU   A CA  
1182 C C   A LEU   A 43  ? 0.1225 0.1098 0.1761 -0.0116 0.0028  -0.0055 43  LEU   A C   
1183 C C   B LEU   A 43  ? 0.1190 0.1190 0.1893 0.0013  0.0067  0.0102  43  LEU   A C   
1184 O O   A LEU   A 43  ? 0.1324 0.1098 0.1822 -0.0098 0.0047  -0.0019 43  LEU   A O   
1185 O O   B LEU   A 43  ? 0.1356 0.1197 0.1935 0.0096  -0.0022 0.0120  43  LEU   A O   
1186 C CB  A LEU   A 43  ? 0.1213 0.1047 0.1762 -0.0072 -0.0032 -0.0114 43  LEU   A CB  
1187 C CB  B LEU   A 43  ? 0.1190 0.1112 0.1865 -0.0069 0.0036  0.0149  43  LEU   A CB  
1188 C CG  A LEU   A 43  ? 0.1232 0.1131 0.1830 -0.0046 -0.0044 -0.0050 43  LEU   A CG  
1189 C CG  B LEU   A 43  ? 0.1200 0.1160 0.1946 -0.0059 0.0001  0.0137  43  LEU   A CG  
1190 C CD1 A LEU   A 43  ? 0.1257 0.1208 0.1976 -0.0010 -0.0143 -0.0015 43  LEU   A CD1 
1191 C CD1 B LEU   A 43  ? 0.1288 0.1208 0.2228 -0.0013 -0.0083 0.0172  43  LEU   A CD1 
1192 C CD2 A LEU   A 43  ? 0.1286 0.1146 0.1804 -0.0039 -0.0023 -0.0030 43  LEU   A CD2 
1193 C CD2 B LEU   A 43  ? 0.1311 0.1202 0.1847 -0.0054 -0.0022 0.0215  43  LEU   A CD2 
1216 N N   A LYS   A 44  ? 0.1264 0.1093 0.1742 -0.0091 -0.0004 -0.0111 44  LYS   A N   
1217 N N   B LYS   A 44  ? 0.1172 0.1139 0.2020 0.0044  0.0028  0.0065  44  LYS   A N   
1218 C CA  A LYS   A 44  ? 0.1346 0.1174 0.1892 -0.0130 0.0002  -0.0012 44  LYS   A CA  
1219 C CA  B LYS   A 44  ? 0.1275 0.1148 0.2162 0.0006  0.0036  0.0152  44  LYS   A CA  
1220 C C   A LYS   A 44  ? 0.1282 0.1171 0.1886 -0.0035 -0.0022 -0.0064 44  LYS   A C   
1221 C C   B LYS   A 44  ? 0.1197 0.1053 0.2086 0.0019  -0.0034 0.0098  44  LYS   A C   
1222 O O   A LYS   A 44  ? 0.1331 0.1261 0.2028 -0.0017 -0.0072 -0.0137 44  LYS   A O   
1223 O O   B LYS   A 44  ? 0.1279 0.1188 0.2195 -0.0046 -0.0003 -0.0016 44  LYS   A O   
1224 C CB  A LYS   A 44  ? 0.1502 0.1322 0.2157 -0.0098 0.0007  0.0075  44  LYS   A CB  
1225 C CB  B LYS   A 44  ? 0.1486 0.1316 0.2604 0.0111  0.0195  0.0196  44  LYS   A CB  
1226 C CG  A LYS   A 44  ? 0.1726 0.1583 0.2515 -0.0088 0.0081  0.0198  44  LYS   A CG  
1227 C CG  B LYS   A 44  ? 0.1746 0.1685 0.3218 0.0121  0.0334  0.0241  44  LYS   A CG  
1228 C CD  A LYS   A 44  ? 0.2015 0.1945 0.3136 -0.0037 0.0019  0.0199  44  LYS   A CD  
1229 C CD  B LYS   A 44  ? 0.2034 0.2183 0.3993 0.0078  0.0178  0.0183  44  LYS   A CD  
1230 C CE  A LYS   A 44  ? 0.2191 0.2136 0.3555 -0.0002 0.0022  0.0188  44  LYS   A CE  
1231 C CE  B LYS   A 44  ? 0.2202 0.2441 0.4544 0.0033  0.0094  0.0179  44  LYS   A CE  
1232 N NZ  A LYS   A 44  ? 0.2274 0.2291 0.3750 0.0027  0.0007  0.0194  44  LYS   A NZ  
1233 N NZ  B LYS   A 44  ? 0.2358 0.2670 0.4863 -0.0042 0.0039  0.0166  44  LYS   A NZ  
1260 N N   A HIS   A 45  ? 0.1228 0.1151 0.1856 0.0029  0.0020  -0.0005 45  HIS   A N   
1261 N N   B HIS   A 45  ? 0.1203 0.0974 0.2017 -0.0005 -0.0118 0.0118  45  HIS   A N   
1262 C CA  A HIS   A 45  ? 0.1233 0.1225 0.1814 0.0059  0.0022  0.0009  45  HIS   A CA  
1263 C CA  B HIS   A 45  ? 0.1225 0.1056 0.2003 -0.0062 -0.0051 0.0115  45  HIS   A CA  
1264 C C   A HIS   A 45  ? 0.1237 0.1327 0.1898 0.0109  -0.0053 -0.0073 45  HIS   A C   
1265 C C   B HIS   A 45  ? 0.1165 0.1069 0.2073 -0.0110 -0.0069 0.0061  45  HIS   A C   
1266 O O   A HIS   A 45  ? 0.1288 0.1367 0.2080 0.0195  -0.0118 -0.0224 45  HIS   A O   
1267 O O   B HIS   A 45  ? 0.1150 0.1129 0.2318 0.0042  -0.0135 -0.0118 45  HIS   A O   
1268 C CB  A HIS   A 45  ? 0.1205 0.1204 0.1679 0.0086  0.0073  0.0036  45  HIS   A CB  
1269 C CB  B HIS   A 45  ? 0.1203 0.1100 0.1961 -0.0051 -0.0019 -0.0006 45  HIS   A CB  
1270 C CG  A HIS   A 45  ? 0.1235 0.1143 0.1553 0.0083  -0.0002 0.0078  45  HIS   A CG  
1271 C CG  B HIS   A 45  ? 0.1159 0.1094 0.1894 -0.0101 0.0065  -0.0033 45  HIS   A CG  
1272 N ND1 A HIS   A 45  ? 0.1200 0.1122 0.1497 0.0057  -0.0044 0.0131  45  HIS   A ND1 
1273 N ND1 B HIS   A 45  ? 0.1109 0.1132 0.2068 -0.0096 0.0029  0.0036  45  HIS   A ND1 
1274 C CD2 A HIS   A 45  ? 0.1284 0.1200 0.1608 0.0083  -0.0082 0.0195  45  HIS   A CD2 
1275 C CD2 B HIS   A 45  ? 0.1108 0.1067 0.1836 -0.0103 0.0053  -0.0030 45  HIS   A CD2 
1276 C CE1 A HIS   A 45  ? 0.1214 0.1185 0.1442 0.0039  -0.0058 0.0276  45  HIS   A CE1 
1277 C CE1 B HIS   A 45  ? 0.1070 0.1027 0.1813 -0.0117 0.0060  0.0009  45  HIS   A CE1 
1278 N NE2 A HIS   A 45  ? 0.1267 0.1209 0.1578 0.0096  -0.0059 0.0310  45  HIS   A NE2 
1279 N NE2 B HIS   A 45  ? 0.1100 0.1087 0.1684 -0.0081 0.0011  0.0004  45  HIS   A NE2 
1294 N N   A GLY   A 46  ? 0.1225 0.1368 0.1903 0.0140  -0.0091 0.0017  46  GLY   A N   
1295 N N   B GLY   A 46  ? 0.1281 0.1154 0.2113 -0.0007 -0.0130 0.0190  46  GLY   A N   
1296 C CA  A GLY   A 46  ? 0.1238 0.1327 0.1874 0.0097  -0.0121 0.0114  46  GLY   A CA  
1297 C CA  B GLY   A 46  ? 0.1299 0.1260 0.2210 0.0035  -0.0104 0.0184  46  GLY   A CA  
1298 C C   A GLY   A 46  ? 0.1277 0.1273 0.1759 0.0149  -0.0226 0.0286  46  GLY   A C   
1299 C C   B GLY   A 46  ? 0.1326 0.1284 0.2206 0.0168  -0.0076 0.0357  46  GLY   A C   
1300 O O   A GLY   A 46  ? 0.1428 0.1291 0.1720 0.0194  -0.0445 0.0407  46  GLY   A O   
1301 O O   B GLY   A 46  ? 0.1453 0.1330 0.2144 0.0226  -0.0163 0.0300  46  GLY   A O   
1308 N N   A GLY   A 47  ? 0.1242 0.1220 0.1729 0.0111  -0.0134 0.0314  47  GLY   A N   
1309 N N   B GLY   A 47  ? 0.1376 0.1355 0.2230 0.0115  0.0042  0.0299  47  GLY   A N   
1310 C CA  A GLY   A 47  ? 0.1331 0.1309 0.1573 0.0211  -0.0096 0.0259  47  GLY   A CA  
1311 C CA  B GLY   A 47  ? 0.1346 0.1384 0.2045 0.0129  -0.0026 0.0326  47  GLY   A CA  
1312 C C   A GLY   A 47  ? 0.1297 0.1308 0.1288 0.0243  0.0054  0.0169  47  GLY   A C   
1313 C C   B GLY   A 47  ? 0.1263 0.1300 0.1731 0.0185  0.0066  0.0277  47  GLY   A C   
1314 O O   A GLY   A 47  ? 0.1266 0.1277 0.1426 0.0258  0.0124  0.0197  47  GLY   A O   
1315 O O   B GLY   A 47  ? 0.1227 0.1238 0.1616 0.0237  0.0111  0.0289  47  GLY   A O   
1322 N N   A GLY   A 48  ? 0.1254 0.1371 0.1158 0.0223  0.0151  0.0038  48  GLY   A N   
1323 N N   B GLY   A 48  ? 0.1250 0.1365 0.1664 0.0104  0.0079  0.0330  48  GLY   A N   
1324 C CA  A GLY   A 48  ? 0.1102 0.1374 0.1139 0.0110  0.0077  -0.0006 48  GLY   A CA  
1325 C CA  B GLY   A 48  ? 0.1228 0.1274 0.1504 0.0053  0.0084  0.0146  48  GLY   A CA  
1326 C C   A GLY   A 48  ? 0.1139 0.1351 0.0983 0.0036  0.0082  -0.0052 48  GLY   A C   
1327 C C   B GLY   A 48  ? 0.1223 0.1220 0.1540 0.0037  0.0058  0.0109  48  GLY   A C   
1328 O O   A GLY   A 48  ? 0.1297 0.1446 0.0916 0.0049  -0.0041 -0.0089 48  GLY   A O   
1329 O O   B GLY   A 48  ? 0.1308 0.1248 0.1480 0.0129  0.0124  0.0002  48  GLY   A O   
1336 N N   A VAL   A 49  ? 0.1190 0.1360 0.1280 -0.0032 -0.0003 0.0050  49  VAL   A N   
1337 N N   B VAL   A 49  ? 0.1105 0.1118 0.1539 0.0016  -0.0071 -0.0016 49  VAL   A N   
1338 C CA  A VAL   A 49  ? 0.1255 0.1313 0.1274 -0.0127 -0.0050 0.0179  49  VAL   A CA  
1339 C CA  B VAL   A 49  ? 0.1128 0.1127 0.1734 0.0023  -0.0059 0.0137  49  VAL   A CA  
1340 C C   A VAL   A 49  ? 0.1228 0.1321 0.1077 -0.0013 -0.0075 0.0205  49  VAL   A C   
1341 C C   B VAL   A 49  ? 0.1135 0.1107 0.1665 0.0020  0.0061  -0.0047 49  VAL   A C   
1342 O O   A VAL   A 49  ? 0.1250 0.1404 0.1059 -0.0014 -0.0050 0.0095  49  VAL   A O   
1343 O O   B VAL   A 49  ? 0.1198 0.1097 0.1716 -0.0076 0.0135  -0.0163 49  VAL   A O   
1344 C CB  A VAL   A 49  ? 0.1388 0.1314 0.1553 -0.0232 -0.0165 0.0162  49  VAL   A CB  
1345 C CB  B VAL   A 49  ? 0.1162 0.1134 0.1981 -0.0042 -0.0229 0.0124  49  VAL   A CB  
1346 C CG1 A VAL   A 49  ? 0.1425 0.1332 0.1696 -0.0223 -0.0155 0.0140  49  VAL   A CG1 
1347 C CG1 B VAL   A 49  ? 0.1079 0.1152 0.2111 0.0062  -0.0139 0.0150  49  VAL   A CG1 
1348 C CG2 A VAL   A 49  ? 0.1455 0.1382 0.1697 -0.0282 -0.0223 0.0162  49  VAL   A CG2 
1349 C CG2 B VAL   A 49  ? 0.1319 0.1235 0.2091 -0.0087 -0.0460 0.0142  49  VAL   A CG2 
1368 N N   A ALA   A 50  ? 0.1143 0.1256 0.1159 -0.0002 -0.0151 0.0167  50  ALA   A N   
1369 N N   B ALA   A 50  ? 0.1102 0.1022 0.1564 -0.0003 -0.0011 0.0045  50  ALA   A N   
1370 C CA  A ALA   A 50  ? 0.1144 0.1228 0.1156 -0.0044 -0.0071 0.0123  50  ALA   A CA  
1371 C CA  B ALA   A 50  ? 0.1075 0.1028 0.1590 -0.0021 0.0065  -0.0019 50  ALA   A CA  
1372 C C   A ALA   A 50  ? 0.1105 0.1226 0.1131 -0.0038 -0.0005 0.0114  50  ALA   A C   
1373 C C   B ALA   A 50  ? 0.1049 0.1066 0.1650 -0.0026 0.0090  -0.0074 50  ALA   A C   
1374 O O   A ALA   A 50  ? 0.1081 0.1253 0.1263 -0.0068 -0.0039 0.0117  50  ALA   A O   
1375 O O   B ALA   A 50  ? 0.1126 0.1198 0.1500 0.0015  0.0073  -0.0101 50  ALA   A O   
1376 C CB  A ALA   A 50  ? 0.1139 0.1266 0.1396 -0.0045 -0.0043 0.0078  50  ALA   A CB  
1377 C CB  B ALA   A 50  ? 0.1055 0.0989 0.1644 0.0059  0.0023  -0.0081 50  ALA   A CB  
1388 N N   A GLY   A 51  ? 0.1147 0.1234 0.1154 0.0113  0.0005  0.0095  51  GLY   A N   
1389 N N   B GLY   A 51  ? 0.1122 0.1010 0.1796 0.0020  -0.0035 -0.0100 51  GLY   A N   
1390 C CA  A GLY   A 51  ? 0.1192 0.1267 0.1191 0.0152  -0.0020 0.0155  51  GLY   A CA  
1391 C CA  B GLY   A 51  ? 0.1286 0.1065 0.1634 0.0063  -0.0067 -0.0093 51  GLY   A CA  
1392 C C   A GLY   A 51  ? 0.1068 0.1308 0.1163 0.0023  -0.0014 0.0088  51  GLY   A C   
1393 C C   B GLY   A 51  ? 0.1186 0.1211 0.1684 -0.0022 0.0008  -0.0075 51  GLY   A C   
1394 O O   A GLY   A 51  ? 0.1075 0.1302 0.1042 -0.0002 -0.0131 0.0123  51  GLY   A O   
1395 O O   B GLY   A 51  ? 0.1384 0.1280 0.1602 0.0006  0.0101  -0.0113 51  GLY   A O   
1402 N N   A ALA   A 52  ? 0.1113 0.1339 0.1273 0.0043  -0.0015 0.0054  52  ALA   A N   
1403 N N   B ALA   A 52  ? 0.1201 0.1268 0.1818 0.0016  0.0050  -0.0172 52  ALA   A N   
1404 C CA  A ALA   A 52  ? 0.1190 0.1433 0.1271 0.0000  0.0005  0.0122  52  ALA   A CA  
1405 C CA  B ALA   A 52  ? 0.1198 0.1369 0.1770 0.0031  0.0027  -0.0044 52  ALA   A CA  
1406 C C   A ALA   A 52  ? 0.1242 0.1449 0.1307 -0.0073 -0.0019 0.0147  52  ALA   A C   
1407 C C   B ALA   A 52  ? 0.1131 0.1321 0.1749 -0.0094 0.0076  -0.0080 52  ALA   A C   
1408 O O   A ALA   A 52  ? 0.1353 0.1445 0.1216 -0.0033 -0.0104 0.0179  52  ALA   A O   
1409 O O   B ALA   A 52  ? 0.1214 0.1346 0.1829 -0.0095 0.0094  -0.0099 52  ALA   A O   
1410 C CB  A ALA   A 52  ? 0.1288 0.1547 0.1373 -0.0062 -0.0012 0.0144  52  ALA   A CB  
1411 C CB  B ALA   A 52  ? 0.1286 0.1530 0.1909 0.0010  -0.0130 0.0022  52  ALA   A CB  
1422 N N   A LEU   A 53  ? 0.1190 0.1429 0.1386 -0.0091 -0.0111 0.0240  53  LEU   A N   
1423 N N   B LEU   A 53  ? 0.1077 0.1347 0.1823 -0.0032 0.0042  -0.0071 53  LEU   A N   
1424 C CA  A LEU   A 53  ? 0.1273 0.1436 0.1514 -0.0094 -0.0055 0.0145  53  LEU   A CA  
1425 C CA  B LEU   A 53  ? 0.1101 0.1396 0.1714 -0.0018 -0.0004 -0.0061 53  LEU   A CA  
1426 C C   A LEU   A 53  ? 0.1317 0.1396 0.1546 -0.0069 0.0010  0.0063  53  LEU   A C   
1427 C C   B LEU   A 53  ? 0.1152 0.1437 0.1716 -0.0047 0.0044  -0.0123 53  LEU   A C   
1428 O O   A LEU   A 53  ? 0.1486 0.1473 0.1634 -0.0134 0.0073  0.0045  53  LEU   A O   
1429 O O   B LEU   A 53  ? 0.1227 0.1585 0.1872 -0.0168 0.0059  -0.0222 53  LEU   A O   
1430 C CB  A LEU   A 53  ? 0.1314 0.1493 0.1740 -0.0104 -0.0028 0.0163  53  LEU   A CB  
1431 C CB  B LEU   A 53  ? 0.1056 0.1373 0.1714 -0.0045 -0.0013 -0.0050 53  LEU   A CB  
1432 C CG  A LEU   A 53  ? 0.1380 0.1520 0.1872 -0.0109 0.0039  0.0139  53  LEU   A CG  
1433 C CG  B LEU   A 53  ? 0.1139 0.1378 0.1810 -0.0123 -0.0015 -0.0137 53  LEU   A CG  
1434 C CD1 A LEU   A 53  ? 0.1370 0.1548 0.1756 -0.0083 0.0008  0.0197  53  LEU   A CD1 
1435 C CD1 B LEU   A 53  ? 0.1264 0.1450 0.1770 -0.0032 -0.0016 -0.0150 53  LEU   A CD1 
1436 C CD2 A LEU   A 53  ? 0.1455 0.1593 0.2077 -0.0150 -0.0000 0.0132  53  LEU   A CD2 
1437 C CD2 B LEU   A 53  ? 0.1218 0.1345 0.2024 -0.0136 -0.0023 -0.0168 53  LEU   A CD2 
1460 N N   A ASN   A 54  ? 0.1220 0.1320 0.1578 -0.0051 -0.0007 -0.0022 54  ASN   A N   
1461 N N   B ASN   A 54  ? 0.1117 0.1319 0.1818 -0.0030 0.0017  -0.0095 54  ASN   A N   
1462 C CA  A ASN   A 54  ? 0.1195 0.1272 0.1690 -0.0064 -0.0006 -0.0128 54  ASN   A CA  
1463 C CA  B ASN   A 54  ? 0.1151 0.1268 0.1875 -0.0040 -0.0046 -0.0139 54  ASN   A CA  
1464 C C   A ASN   A 54  ? 0.1205 0.1342 0.1811 -0.0040 0.0022  -0.0155 54  ASN   A C   
1465 C C   B ASN   A 54  ? 0.1204 0.1339 0.1926 -0.0048 -0.0002 -0.0176 54  ASN   A C   
1466 O O   A ASN   A 54  ? 0.1228 0.1454 0.1825 -0.0013 0.0000  -0.0194 54  ASN   A O   
1467 O O   B ASN   A 54  ? 0.1265 0.1480 0.1968 -0.0020 -0.0023 -0.0263 54  ASN   A O   
1468 C CB  A ASN   A 54  ? 0.1118 0.1236 0.1742 -0.0107 -0.0048 -0.0185 54  ASN   A CB  
1469 C CB  B ASN   A 54  ? 0.1101 0.1263 0.1981 0.0015  -0.0148 -0.0106 54  ASN   A CB  
1470 C CG  A ASN   A 54  ? 0.1112 0.1257 0.1737 -0.0115 0.0045  -0.0183 54  ASN   A CG  
1471 C CG  B ASN   A 54  ? 0.1131 0.1314 0.2055 0.0112  -0.0048 -0.0027 54  ASN   A CG  
1472 O OD1 A ASN   A 54  ? 0.1114 0.1193 0.1607 -0.0135 0.0056  -0.0174 54  ASN   A OD1 
1473 O OD1 B ASN   A 54  ? 0.1212 0.1388 0.2115 0.0156  -0.0129 0.0096  54  ASN   A OD1 
1474 N ND2 A ASN   A 54  ? 0.1100 0.1298 0.1887 -0.0123 -0.0023 -0.0096 54  ASN   A ND2 
1475 N ND2 B ASN   A 54  ? 0.1166 0.1254 0.2081 0.0057  -0.0063 0.0109  54  ASN   A ND2 
1488 N N   . LYS   A 55  ? 0.1184 0.1355 0.2034 0.0040  0.0047  -0.0219 55  LYS   A N   
1489 C CA  . LYS   A 55  ? 0.1292 0.1425 0.1996 0.0093  -0.0029 -0.0265 55  LYS   A CA  
1490 C C   . LYS   A 55  ? 0.1286 0.1570 0.2057 -0.0054 0.0076  -0.0306 55  LYS   A C   
1491 O O   . LYS   A 55  ? 0.1418 0.1608 0.2136 0.0018  0.0051  -0.0425 55  LYS   A O   
1492 C CB  . LYS   A 55  ? 0.1455 0.1518 0.2181 0.0173  0.0004  -0.0302 55  LYS   A CB  
1493 C CG  . LYS   A 55  ? 0.1516 0.1752 0.2278 0.0228  -0.0054 -0.0346 55  LYS   A CG  
1494 C CD  . LYS   A 55  ? 0.1626 0.1987 0.2350 0.0369  -0.0047 -0.0293 55  LYS   A CD  
1495 C CE  . LYS   A 55  ? 0.1832 0.2204 0.2433 0.0450  -0.0171 -0.0324 55  LYS   A CE  
1496 N NZ  . LYS   A 55  ? 0.1935 0.2286 0.2496 0.0470  -0.0123 -0.0281 55  LYS   A NZ  
1511 N N   . ALA   A 56  ? 0.1335 0.1713 0.2095 -0.0075 0.0179  -0.0420 56  ALA   A N   
1512 C CA  . ALA   A 56  ? 0.1498 0.1814 0.2144 -0.0117 0.0141  -0.0371 56  ALA   A CA  
1513 C C   . ALA   A 56  ? 0.1539 0.1931 0.1906 -0.0106 0.0220  -0.0329 56  ALA   A C   
1514 O O   . ALA   A 56  ? 0.1571 0.2301 0.2148 -0.0044 0.0287  -0.0223 56  ALA   A O   
1515 C CB  . ALA   A 56  ? 0.1547 0.1906 0.2211 -0.0167 0.0200  -0.0249 56  ALA   A CB  
1521 N N   . THR   A 57  ? 0.1405 0.1656 0.1852 -0.0144 0.0161  -0.0334 57  THR   A N   
1522 C CA  . THR   A 57  ? 0.1435 0.1625 0.1899 -0.0134 0.0041  -0.0314 57  THR   A CA  
1523 C C   . THR   A 57  ? 0.1421 0.1674 0.2001 -0.0110 0.0038  -0.0375 57  THR   A C   
1524 O O   . THR   A 57  ? 0.1463 0.1658 0.2148 -0.0135 -0.0016 -0.0474 57  THR   A O   
1525 C CB  . THR   A 57  ? 0.1403 0.1592 0.1913 -0.0075 0.0101  -0.0245 57  THR   A CB  
1526 O OG1 . THR   A 57  ? 0.1273 0.1504 0.1972 -0.0065 0.0098  -0.0217 57  THR   A OG1 
1527 C CG2 . THR   A 57  ? 0.1425 0.1642 0.1759 -0.0068 0.0019  -0.0279 57  THR   A CG2 
1535 N N   . ASN   A 58  ? 0.1469 0.1630 0.2143 -0.0110 0.0109  -0.0471 58  ASN   A N   
1536 C CA  . ASN   A 58  ? 0.1711 0.1591 0.2363 -0.0089 0.0127  -0.0485 58  ASN   A CA  
1537 C C   . ASN   A 58  ? 0.1517 0.1408 0.2311 -0.0009 0.0045  -0.0344 58  ASN   A C   
1538 O O   . ASN   A 58  ? 0.1488 0.1477 0.2463 -0.0126 0.0064  -0.0441 58  ASN   A O   
1539 C CB  . ASN   A 58  ? 0.2312 0.1862 0.2595 -0.0236 0.0427  -0.0583 58  ASN   A CB  
1540 C CG  . ASN   A 58  ? 0.2916 0.2170 0.3212 -0.0247 0.0508  -0.0506 58  ASN   A CG  
1541 O OD1 . ASN   A 58  ? 0.3154 0.2074 0.3610 0.0079  0.0829  -0.0482 58  ASN   A OD1 
1542 N ND2 . ASN   A 58  ? 0.3202 0.2371 0.3403 -0.0329 0.0378  -0.0510 58  ASN   A ND2 
1549 N N   . ASN   A 59  ? 0.1303 0.1374 0.2050 -0.0025 -0.0029 -0.0335 59  ASN   A N   
1550 C CA  . ASN   A 59  ? 0.1328 0.1275 0.2082 0.0001  -0.0019 -0.0201 59  ASN   A CA  
1551 C C   . ASN   A 59  ? 0.1302 0.1264 0.1961 -0.0072 -0.0090 -0.0200 59  ASN   A C   
1552 O O   . ASN   A 59  ? 0.1239 0.1329 0.2015 -0.0069 0.0024  -0.0170 59  ASN   A O   
1553 C CB  . ASN   A 59  ? 0.1368 0.1252 0.2104 0.0007  -0.0208 -0.0269 59  ASN   A CB  
1554 C CG  . ASN   A 59  ? 0.1412 0.1268 0.2168 0.0012  -0.0208 -0.0118 59  ASN   A CG  
1555 O OD1 . ASN   A 59  ? 0.1504 0.1315 0.2050 -0.0109 -0.0286 -0.0031 59  ASN   A OD1 
1556 N ND2 . ASN   A 59  ? 0.1459 0.1315 0.2235 -0.0104 -0.0163 -0.0050 59  ASN   A ND2 
1563 N N   . ALA   A 60  ? 0.1229 0.1243 0.1858 -0.0033 -0.0020 -0.0201 60  ALA   A N   
1564 C CA  . ALA   A 60  ? 0.1266 0.1318 0.1976 0.0012  -0.0050 -0.0180 60  ALA   A CA  
1565 C C   . ALA   A 60  ? 0.1245 0.1220 0.1971 0.0033  -0.0007 -0.0086 60  ALA   A C   
1566 O O   . ALA   A 60  ? 0.1231 0.1290 0.2222 -0.0001 -0.0031 -0.0149 60  ALA   A O   
1567 C CB  . ALA   A 60  ? 0.1374 0.1450 0.2007 -0.0044 -0.0082 -0.0235 60  ALA   A CB  
1573 N N   . MET   A 61  ? 0.1260 0.1162 0.1906 -0.0073 0.0023  -0.0146 61  MET   A N   
1574 C CA  . MET   A 61  ? 0.1264 0.1163 0.1898 -0.0090 0.0071  -0.0042 61  MET   A CA  
1575 C C   . MET   A 61  ? 0.1167 0.1102 0.1874 -0.0045 -0.0054 -0.0058 61  MET   A C   
1576 O O   . MET   A 61  ? 0.1168 0.1143 0.1999 -0.0044 0.0066  -0.0044 61  MET   A O   
1577 C CB  . MET   A 61  ? 0.1277 0.1132 0.1853 -0.0087 0.0034  -0.0107 61  MET   A CB  
1578 C CG  . MET   A 61  ? 0.1249 0.1267 0.1912 -0.0015 -0.0031 -0.0178 61  MET   A CG  
1579 S SD  . MET   A 61  ? 0.1282 0.1299 0.2184 -0.0114 0.0026  -0.0252 61  MET   A SD  
1580 C CE  . MET   A 61  ? 0.1468 0.1428 0.2426 -0.0121 0.0184  -0.0186 61  MET   A CE  
1590 N N   . GLN   A 62  ? 0.1209 0.1118 0.2008 -0.0039 0.0026  -0.0116 62  GLN   A N   
1591 C CA  . GLN   A 62  ? 0.1251 0.1118 0.2109 -0.0027 0.0069  -0.0063 62  GLN   A CA  
1592 C C   . GLN   A 62  ? 0.1183 0.1088 0.2069 -0.0027 0.0033  -0.0048 62  GLN   A C   
1593 O O   . GLN   A 62  ? 0.1240 0.1224 0.2025 -0.0048 0.0106  -0.0078 62  GLN   A O   
1594 C CB  . GLN   A 62  ? 0.1193 0.1118 0.2036 -0.0010 0.0067  -0.0134 62  GLN   A CB  
1595 C CG  . GLN   A 62  ? 0.1200 0.1107 0.2031 -0.0049 0.0001  -0.0034 62  GLN   A CG  
1596 C CD  . GLN   A 62  ? 0.1272 0.1089 0.2148 -0.0041 0.0056  -0.0034 62  GLN   A CD  
1597 O OE1 . GLN   A 62  ? 0.1321 0.1197 0.2267 -0.0061 0.0023  -0.0055 62  GLN   A OE1 
1598 N NE2 . GLN   A 62  ? 0.1386 0.1147 0.2189 0.0031  -0.0041 -0.0167 62  GLN   A NE2 
1607 N N   . VAL   A 63  ? 0.1178 0.1162 0.2210 -0.0071 0.0097  -0.0268 63  VAL   A N   
1608 C CA  . VAL   A 63  ? 0.1173 0.1306 0.2337 -0.0167 0.0014  -0.0248 63  VAL   A CA  
1609 C C   . VAL   A 63  ? 0.1100 0.1277 0.2193 -0.0200 -0.0059 -0.0295 63  VAL   A C   
1610 O O   . VAL   A 63  ? 0.1112 0.1259 0.2338 -0.0169 -0.0002 -0.0280 63  VAL   A O   
1611 C CB  . VAL   A 63  ? 0.1358 0.1502 0.2541 -0.0164 -0.0023 -0.0420 63  VAL   A CB  
1612 C CG1 . VAL   A 63  ? 0.1421 0.1732 0.2709 -0.0201 -0.0100 -0.0602 63  VAL   A CG1 
1613 C CG2 . VAL   A 63  ? 0.1532 0.1366 0.2589 -0.0108 0.0108  -0.0439 63  VAL   A CG2 
1623 N N   . GLU   A 64  ? 0.1113 0.1321 0.2132 -0.0105 0.0043  -0.0238 64  GLU   A N   
1624 C CA  . GLU   A 64  ? 0.1152 0.1308 0.2059 -0.0109 -0.0104 -0.0094 64  GLU   A CA  
1625 C C   . GLU   A 64  ? 0.1103 0.1163 0.2029 -0.0125 0.0009  -0.0137 64  GLU   A C   
1626 O O   . GLU   A 64  ? 0.1167 0.1274 0.2126 -0.0023 0.0036  -0.0132 64  GLU   A O   
1627 C CB  . GLU   A 64  ? 0.1279 0.1409 0.2087 -0.0102 0.0033  -0.0150 64  GLU   A CB  
1628 C CG  . GLU   A 64  ? 0.1346 0.1419 0.2083 -0.0155 0.0080  -0.0151 64  GLU   A CG  
1629 C CD  . GLU   A 64  ? 0.1419 0.1444 0.2135 -0.0223 0.0089  -0.0160 64  GLU   A CD  
1630 O OE1 . GLU   A 64  ? 0.1377 0.1551 0.2233 -0.0234 0.0136  -0.0150 64  GLU   A OE1 
1631 O OE2 . GLU   A 64  ? 0.1497 0.1507 0.2230 -0.0225 -0.0066 -0.0078 64  GLU   A OE2 
1638 N N   . SER   A 65  ? 0.1063 0.1219 0.2044 -0.0036 0.0013  -0.0132 65  SER   A N   
1639 C CA  . SER   A 65  ? 0.1151 0.1102 0.1982 -0.0053 -0.0013 -0.0098 65  SER   A CA  
1640 C C   . SER   A 65  ? 0.1138 0.1164 0.2073 -0.0073 -0.0016 -0.0088 65  SER   A C   
1641 O O   . SER   A 65  ? 0.1187 0.1236 0.2181 -0.0007 0.0004  -0.0104 65  SER   A O   
1642 C CB  . SER   A 65  ? 0.1148 0.1124 0.1964 -0.0034 -0.0010 -0.0026 65  SER   A CB  
1643 O OG  . SER   A 65  ? 0.1123 0.1199 0.2089 -0.0096 -0.0063 0.0025  65  SER   A OG  
1649 N N   . ASP   A 66  ? 0.1187 0.1126 0.2074 -0.0083 0.0137  0.0023  66  ASP   A N   
1650 C CA  . ASP   A 66  ? 0.1304 0.1239 0.2126 0.0010  0.0059  0.0076  66  ASP   A CA  
1651 C C   . ASP   A 66  ? 0.1287 0.1259 0.2220 -0.0051 0.0056  0.0025  66  ASP   A C   
1652 O O   . ASP   A 66  ? 0.1327 0.1307 0.2402 0.0012  0.0170  0.0197  66  ASP   A O   
1653 C CB  . ASP   A 66  ? 0.1355 0.1338 0.2463 0.0042  0.0061  0.0175  66  ASP   A CB  
1654 C CG  . ASP   A 66  ? 0.1555 0.1439 0.2730 0.0070  -0.0059 0.0365  66  ASP   A CG  
1655 O OD1 . ASP   A 66  ? 0.1536 0.1750 0.2524 -0.0028 -0.0007 0.0462  66  ASP   A OD1 
1656 O OD2 . ASP   A 66  ? 0.1700 0.1621 0.3526 0.0279  -0.0271 0.0133  66  ASP   A OD2 
1661 N N   A ASP   A 67  ? 0.1177 0.1167 0.2207 -0.0055 0.0085  -0.0037 67  ASP   A N   
1662 N N   B ASP   A 67  ? 0.1206 0.1256 0.2276 -0.0019 0.0113  0.0045  67  ASP   A N   
1663 C CA  A ASP   A 67  ? 0.1155 0.1245 0.2304 -0.0030 0.0055  0.0000  67  ASP   A CA  
1664 C CA  B ASP   A 67  ? 0.1254 0.1436 0.2399 0.0034  0.0098  0.0109  67  ASP   A CA  
1665 C C   A ASP   A 67  ? 0.1132 0.1255 0.2234 -0.0036 0.0111  0.0043  67  ASP   A C   
1666 C C   B ASP   A 67  ? 0.1260 0.1447 0.2241 0.0011  0.0081  0.0171  67  ASP   A C   
1667 O O   A ASP   A 67  ? 0.1126 0.1335 0.2401 0.0019  0.0184  0.0038  67  ASP   A O   
1668 O O   B ASP   A 67  ? 0.1235 0.1462 0.2307 -0.0048 0.0213  0.0224  67  ASP   A O   
1669 C CB  A ASP   A 67  ? 0.1184 0.1280 0.2438 -0.0054 -0.0118 -0.0028 67  ASP   A CB  
1670 C CB  B ASP   A 67  ? 0.1324 0.1514 0.2532 -0.0008 -0.0036 0.0071  67  ASP   A CB  
1671 C CG  A ASP   A 67  ? 0.1203 0.1365 0.2440 -0.0099 -0.0249 -0.0056 67  ASP   A CG  
1672 C CG  B ASP   A 67  ? 0.1338 0.1616 0.2502 -0.0021 -0.0207 0.0010  67  ASP   A CG  
1673 O OD1 A ASP   A 67  ? 0.1160 0.1449 0.2615 -0.0071 -0.0230 -0.0064 67  ASP   A OD1 
1674 O OD1 B ASP   A 67  ? 0.1300 0.1677 0.2566 -0.0025 -0.0094 -0.0132 67  ASP   A OD1 
1675 O OD2 A ASP   A 67  ? 0.1261 0.1400 0.2375 -0.0130 -0.0272 -0.0083 67  ASP   A OD2 
1676 O OD2 B ASP   A 67  ? 0.1376 0.1675 0.2525 0.0021  -0.0283 0.0044  67  ASP   A OD2 
1685 N N   A TYR   A 68  ? 0.1082 0.1141 0.2036 -0.0082 0.0144  0.0091  68  TYR   A N   
1686 N N   B TYR   A 68  ? 0.1264 0.1352 0.2088 0.0069  0.0072  0.0188  68  TYR   A N   
1687 C CA  A TYR   A 68  ? 0.1144 0.1135 0.1931 -0.0115 0.0198  0.0063  68  TYR   A CA  
1688 C CA  B TYR   A 68  ? 0.1388 0.1344 0.2065 0.0083  0.0058  0.0153  68  TYR   A CA  
1689 C C   A TYR   A 68  ? 0.1085 0.1163 0.1965 -0.0109 0.0241  0.0048  68  TYR   A C   
1690 C C   B TYR   A 68  ? 0.1341 0.1331 0.2086 0.0090  0.0030  0.0194  68  TYR   A C   
1691 O O   A TYR   A 68  ? 0.1125 0.1182 0.2021 -0.0062 0.0318  0.0066  68  TYR   A O   
1692 O O   B TYR   A 68  ? 0.1355 0.1388 0.2063 0.0209  0.0026  0.0274  68  TYR   A O   
1693 C CB  A TYR   A 68  ? 0.1186 0.1123 0.1850 -0.0055 0.0242  0.0113  68  TYR   A CB  
1694 C CB  B TYR   A 68  ? 0.1334 0.1305 0.2105 0.0098  0.0136  0.0219  68  TYR   A CB  
1695 C CG  A TYR   A 68  ? 0.1245 0.1246 0.1944 -0.0084 0.0327  0.0043  68  TYR   A CG  
1696 C CG  B TYR   A 68  ? 0.1304 0.1436 0.2007 0.0127  0.0180  0.0099  68  TYR   A CG  
1697 C CD1 A TYR   A 68  ? 0.1249 0.1319 0.2103 -0.0291 0.0320  -0.0027 68  TYR   A CD1 
1698 C CD1 B TYR   A 68  ? 0.1423 0.1505 0.1955 0.0046  0.0073  0.0134  68  TYR   A CD1 
1699 C CD2 A TYR   A 68  ? 0.1397 0.1323 0.2119 -0.0049 0.0286  0.0046  68  TYR   A CD2 
1700 C CD2 B TYR   A 68  ? 0.1420 0.1478 0.2138 0.0075  0.0175  0.0064  68  TYR   A CD2 
1701 C CE1 A TYR   A 68  ? 0.1302 0.1463 0.2308 -0.0298 0.0270  -0.0271 68  TYR   A CE1 
1702 C CE1 B TYR   A 68  ? 0.1469 0.1507 0.1852 0.0069  0.0056  0.0290  68  TYR   A CE1 
1703 C CE2 A TYR   A 68  ? 0.1418 0.1409 0.2314 -0.0083 0.0353  -0.0025 68  TYR   A CE2 
1704 C CE2 B TYR   A 68  ? 0.1400 0.1472 0.1957 0.0023  0.0147  0.0068  68  TYR   A CE2 
1705 C CZ  A TYR   A 68  ? 0.1340 0.1419 0.2496 -0.0293 0.0262  -0.0389 68  TYR   A CZ  
1706 C CZ  B TYR   A 68  ? 0.1463 0.1439 0.1770 0.0051  0.0128  0.0201  68  TYR   A CZ  
1707 O OH  A TYR   A 68  ? 0.1518 0.1562 0.2990 -0.0249 0.0122  -0.0686 68  TYR   A OH  
1708 O OH  B TYR   A 68  ? 0.1772 0.1409 0.1710 0.0117  -0.0029 0.0206  68  TYR   A OH  
1727 N N   A ILE   A 69  ? 0.1077 0.1166 0.1855 -0.0047 0.0219  0.0021  69  ILE   A N   
1728 N N   B ILE   A 69  ? 0.1255 0.1241 0.2072 0.0049  0.0076  0.0215  69  ILE   A N   
1729 C CA  A ILE   A 69  ? 0.1185 0.1252 0.1805 -0.0004 0.0064  -0.0128 69  ILE   A CA  
1730 C CA  B ILE   A 69  ? 0.1375 0.1244 0.2048 0.0014  0.0045  0.0168  69  ILE   A CA  
1731 C C   A ILE   A 69  ? 0.1208 0.1274 0.1759 -0.0041 0.0161  -0.0003 69  ILE   A C   
1732 C C   B ILE   A 69  ? 0.1423 0.1226 0.1909 -0.0042 0.0025  0.0331  69  ILE   A C   
1733 O O   A ILE   A 69  ? 0.1228 0.1298 0.1699 -0.0010 0.0225  0.0096  69  ILE   A O   
1734 O O   B ILE   A 69  ? 0.1467 0.1317 0.1921 -0.0049 -0.0003 0.0345  69  ILE   A O   
1735 C CB  A ILE   A 69  ? 0.1272 0.1453 0.1959 0.0102  -0.0008 -0.0191 69  ILE   A CB  
1736 C CB  B ILE   A 69  ? 0.1417 0.1447 0.1996 0.0066  0.0047  0.0089  69  ILE   A CB  
1737 C CG1 A ILE   A 69  ? 0.1263 0.1574 0.2044 0.0104  -0.0004 -0.0272 69  ILE   A CG1 
1738 C CG1 B ILE   A 69  ? 0.1336 0.1486 0.1890 0.0108  0.0023  0.0022  69  ILE   A CG1 
1739 C CG2 A ILE   A 69  ? 0.1386 0.1580 0.2156 0.0189  -0.0097 -0.0191 69  ILE   A CG2 
1740 C CG2 B ILE   A 69  ? 0.1608 0.1610 0.2271 0.0067  0.0028  0.0116  69  ILE   A CG2 
1741 C CD1 A ILE   A 69  ? 0.1261 0.1615 0.2016 0.0073  -0.0028 -0.0290 69  ILE   A CD1 
1742 C CD1 B ILE   A 69  ? 0.1378 0.1512 0.1844 0.0074  -0.0025 0.0062  69  ILE   A CD1 
1765 N N   A ALA   A 70  ? 0.1266 0.1310 0.1877 -0.0096 0.0202  -0.0041 70  ALA   A N   
1766 N N   B ALA   A 70  ? 0.1461 0.1247 0.2022 -0.0112 -0.0030 0.0296  70  ALA   A N   
1767 C CA  A ALA   A 70  ? 0.1305 0.1440 0.2046 -0.0182 0.0312  -0.0048 70  ALA   A CA  
1768 C CA  B ALA   A 70  ? 0.1463 0.1371 0.2130 -0.0174 -0.0018 0.0324  70  ALA   A CA  
1769 C C   A ALA   A 70  ? 0.1233 0.1586 0.1836 -0.0136 0.0270  -0.0083 70  ALA   A C   
1770 C C   B ALA   A 70  ? 0.1429 0.1507 0.1946 -0.0168 -0.0014 0.0284  70  ALA   A C   
1771 O O   A ALA   A 70  ? 0.1258 0.1815 0.1797 -0.0041 0.0328  -0.0051 70  ALA   A O   
1772 O O   B ALA   A 70  ? 0.1515 0.1735 0.1986 -0.0151 0.0005  0.0246  70  ALA   A O   
1773 C CB  A ALA   A 70  ? 0.1351 0.1450 0.2178 -0.0230 0.0423  -0.0109 70  ALA   A CB  
1774 C CB  B ALA   A 70  ? 0.1483 0.1373 0.2254 -0.0218 -0.0002 0.0305  70  ALA   A CB  
1785 N N   A THR   A 71  ? 0.1141 0.1543 0.1782 -0.0158 0.0209  -0.0097 71  THR   A N   
1786 N N   B THR   A 71  ? 0.1364 0.1489 0.1967 -0.0079 0.0090  0.0294  71  THR   A N   
1787 C CA  A THR   A 71  ? 0.1203 0.1640 0.1875 -0.0074 0.0140  -0.0049 71  THR   A CA  
1788 C CA  B THR   A 71  ? 0.1483 0.1666 0.1948 0.0052  0.0120  0.0229  71  THR   A CA  
1789 C C   A THR   A 71  ? 0.1092 0.1559 0.1845 0.0015  0.0216  -0.0035 71  THR   A C   
1790 C C   B THR   A 71  ? 0.1451 0.1625 0.1933 0.0085  0.0137  0.0274  71  THR   A C   
1791 O O   A THR   A 71  ? 0.0990 0.1640 0.1965 0.0089  0.0161  -0.0041 71  THR   A O   
1792 O O   B THR   A 71  ? 0.1493 0.1818 0.1930 0.0068  0.0125  0.0217  71  THR   A O   
1793 C CB  A THR   A 71  ? 0.1443 0.1857 0.2152 -0.0032 -0.0093 0.0071  71  THR   A CB  
1794 C CB  B THR   A 71  ? 0.1735 0.1897 0.2041 0.0145  -0.0079 0.0108  71  THR   A CB  
1795 O OG1 A THR   A 71  ? 0.1614 0.2014 0.2437 -0.0015 -0.0233 0.0025  71  THR   A OG1 
1796 O OG1 B THR   A 71  ? 0.1928 0.2031 0.2114 0.0127  -0.0188 -0.0008 71  THR   A OG1 
1797 C CG2 A THR   A 71  ? 0.1499 0.1940 0.2166 0.0039  -0.0190 0.0230  71  THR   A CG2 
1798 C CG2 B THR   A 71  ? 0.1830 0.2023 0.2158 0.0239  -0.0223 0.0215  71  THR   A CG2 
1813 N N   A ASN   A 72  ? 0.1108 0.1389 0.1796 0.0022  0.0199  -0.0007 72  ASN   A N   
1814 N N   B ASN   A 72  ? 0.1407 0.1457 0.1962 0.0126  0.0117  0.0264  72  ASN   A N   
1815 C CA  A ASN   A 72  ? 0.1262 0.1376 0.1877 0.0090  0.0193  0.0001  72  ASN   A CA  
1816 C CA  B ASN   A 72  ? 0.1471 0.1459 0.1959 0.0125  0.0169  0.0182  72  ASN   A CA  
1817 C C   A ASN   A 72  ? 0.1260 0.1314 0.1811 0.0060  0.0309  -0.0026 72  ASN   A C   
1818 C C   B ASN   A 72  ? 0.1540 0.1453 0.2004 0.0088  0.0225  0.0248  72  ASN   A C   
1819 O O   A ASN   A 72  ? 0.1418 0.1267 0.1944 0.0103  0.0402  -0.0076 72  ASN   A O   
1820 O O   B ASN   A 72  ? 0.1713 0.1546 0.2230 0.0081  0.0253  0.0146  72  ASN   A O   
1821 C CB  A ASN   A 72  ? 0.1464 0.1522 0.1832 0.0107  0.0113  -0.0024 72  ASN   A CB  
1822 C CB  B ASN   A 72  ? 0.1582 0.1505 0.1936 0.0219  0.0169  0.0143  72  ASN   A CB  
1823 C CG  A ASN   A 72  ? 0.1687 0.1664 0.1954 0.0183  0.0095  0.0055  72  ASN   A CG  
1824 C CG  B ASN   A 72  ? 0.1796 0.1652 0.1852 0.0278  0.0143  0.0133  72  ASN   A CG  
1825 O OD1 A ASN   A 72  ? 0.1823 0.1824 0.2163 0.0179  0.0129  0.0156  72  ASN   A OD1 
1826 O OD1 B ASN   A 72  ? 0.1998 0.1900 0.1921 0.0202  0.0264  0.0160  72  ASN   A OD1 
1827 N ND2 A ASN   A 72  ? 0.1851 0.1721 0.2016 0.0262  0.0121  -0.0049 72  ASN   A ND2 
1828 N ND2 B ASN   A 72  ? 0.1788 0.1635 0.1809 0.0506  -0.0054 0.0062  72  ASN   A ND2 
1841 N N   A GLY   A 73  ? 0.1232 0.1319 0.1740 0.0035  0.0259  -0.0081 73  GLY   A N   
1842 N N   B GLY   A 73  ? 0.1551 0.1400 0.1941 0.0054  0.0175  0.0222  73  GLY   A N   
1843 C CA  A GLY   A 73  ? 0.1251 0.1318 0.1623 0.0003  0.0199  0.0060  73  GLY   A CA  
1844 C CA  B GLY   A 73  ? 0.1573 0.1360 0.1881 -0.0059 0.0140  0.0185  73  GLY   A CA  
1845 C C   A GLY   A 73  ? 0.1242 0.1311 0.1569 0.0011  0.0213  0.0143  73  GLY   A C   
1846 C C   B GLY   A 73  ? 0.1476 0.1268 0.1766 -0.0073 0.0210  0.0197  73  GLY   A C   
1847 O O   A GLY   A 73  ? 0.1132 0.1355 0.1670 -0.0036 0.0058  0.0016  73  GLY   A O   
1848 O O   B GLY   A 73  ? 0.1549 0.1354 0.1890 -0.0017 0.0163  0.0109  73  GLY   A O   
1855 N N   A PRO   A 74  ? 0.1397 0.1338 0.1620 -0.0015 0.0209  0.0158  74  PRO   A N   
1856 N N   B PRO   A 74  ? 0.1456 0.1289 0.1845 -0.0111 0.0165  0.0173  74  PRO   A N   
1857 C CA  A PRO   A 74  ? 0.1362 0.1312 0.1687 0.0030  0.0146  0.0090  74  PRO   A CA  
1858 C CA  B PRO   A 74  ? 0.1419 0.1332 0.1930 -0.0119 0.0122  0.0146  74  PRO   A CA  
1859 C C   A PRO   A 74  ? 0.1253 0.1163 0.1625 0.0010  0.0004  0.0040  74  PRO   A C   
1860 C C   B PRO   A 74  ? 0.1391 0.1224 0.1935 -0.0042 0.0047  0.0056  74  PRO   A C   
1861 O O   A PRO   A 74  ? 0.1278 0.1170 0.1698 0.0038  -0.0094 -0.0027 74  PRO   A O   
1862 O O   B PRO   A 74  ? 0.1348 0.1302 0.1918 0.0035  -0.0087 -0.0048 74  PRO   A O   
1863 C CB  A PRO   A 74  ? 0.1477 0.1545 0.1859 0.0042  0.0098  0.0213  74  PRO   A CB  
1864 C CB  B PRO   A 74  ? 0.1581 0.1636 0.2141 -0.0093 0.0111  0.0222  74  PRO   A CB  
1865 C CG  A PRO   A 74  ? 0.1628 0.1773 0.2072 0.0018  0.0030  0.0231  74  PRO   A CG  
1866 C CG  B PRO   A 74  ? 0.1709 0.1833 0.2319 -0.0085 -0.0022 0.0189  74  PRO   A CG  
1867 C CD  A PRO   A 74  ? 0.1523 0.1596 0.1784 -0.0059 0.0080  0.0241  74  PRO   A CD  
1868 C CD  B PRO   A 74  ? 0.1588 0.1638 0.2130 -0.0100 0.0061  0.0186  74  PRO   A CD  
1883 N N   A LEU   A 75  ? 0.1252 0.1158 0.1723 0.0022  0.0076  0.0098  75  LEU   A N   
1884 N N   B LEU   A 75  ? 0.1420 0.1137 0.1911 -0.0058 0.0173  0.0032  75  LEU   A N   
1885 C CA  A LEU   A 75  ? 0.1359 0.1237 0.1753 0.0089  0.0062  0.0113  75  LEU   A CA  
1886 C CA  B LEU   A 75  ? 0.1497 0.1149 0.1721 -0.0078 0.0086  0.0024  75  LEU   A CA  
1887 C C   A LEU   A 75  ? 0.1384 0.1257 0.1735 0.0066  0.0158  0.0092  75  LEU   A C   
1888 C C   B LEU   A 75  ? 0.1544 0.1210 0.1819 0.0006  0.0059  0.0132  75  LEU   A C   
1889 O O   A LEU   A 75  ? 0.1365 0.1441 0.1653 0.0121  0.0192  -0.0065 75  LEU   A O   
1890 O O   B LEU   A 75  ? 0.1641 0.1356 0.1931 0.0063  0.0029  0.0107  75  LEU   A O   
1891 C CB  A LEU   A 75  ? 0.1488 0.1351 0.1801 0.0170  0.0059  0.0231  75  LEU   A CB  
1892 C CB  B LEU   A 75  ? 0.1636 0.1203 0.1613 -0.0269 0.0107  0.0092  75  LEU   A CB  
1893 C CG  A LEU   A 75  ? 0.1665 0.1580 0.1831 0.0107  0.0115  0.0287  75  LEU   A CG  
1894 C CG  B LEU   A 75  ? 0.1883 0.1420 0.1709 -0.0596 0.0042  0.0132  75  LEU   A CG  
1895 C CD1 A LEU   A 75  ? 0.1726 0.1714 0.1914 0.0120  0.0084  0.0297  75  LEU   A CD1 
1896 C CD1 B LEU   A 75  ? 0.1999 0.1733 0.1809 -0.0601 -0.0067 -0.0001 75  LEU   A CD1 
1897 C CD2 A LEU   A 75  ? 0.1824 0.1826 0.2032 0.0171  0.0169  0.0262  75  LEU   A CD2 
1898 C CD2 B LEU   A 75  ? 0.2163 0.1853 0.2198 -0.0438 0.0062  0.0158  75  LEU   A CD2 
1921 N N   . LYS   A 76  ? 0.1594 0.1207 0.1926 -0.0044 0.0161  0.0023  76  LYS   A N   
1922 C CA  . LYS   A 76  ? 0.1619 0.1423 0.1968 -0.0127 0.0072  -0.0080 76  LYS   A CA  
1923 C C   . LYS   A 76  ? 0.1589 0.1236 0.1719 -0.0035 0.0093  0.0036  76  LYS   A C   
1924 O O   . LYS   A 76  ? 0.1590 0.1160 0.1805 -0.0034 0.0139  0.0043  76  LYS   A O   
1925 C CB  . LYS   A 76  ? 0.1655 0.1614 0.2333 0.0020  0.0100  -0.0341 76  LYS   A CB  
1926 C CG  . LYS   A 76  ? 0.1719 0.1567 0.2783 0.0044  0.0064  -0.0359 76  LYS   A CG  
1927 C CD  . LYS   A 76  ? 0.1763 0.1604 0.3107 0.0090  0.0026  -0.0415 76  LYS   A CD  
1928 C CE  . LYS   A 76  ? 0.1928 0.1784 0.3649 0.0009  0.0090  -0.0503 76  LYS   A CE  
1929 N NZ  . LYS   A 76  ? 0.1902 0.1729 0.4011 -0.0129 0.0100  -0.0631 76  LYS   A NZ  
1944 N N   . VAL   A 77  ? 0.1722 0.1289 0.1626 -0.0023 0.0229  0.0173  77  VAL   A N   
1945 C CA  . VAL   A 77  ? 0.1715 0.1292 0.1691 0.0063  0.0132  0.0165  77  VAL   A CA  
1946 C C   . VAL   A 77  ? 0.1572 0.1231 0.1654 0.0078  0.0066  0.0061  77  VAL   A C   
1947 O O   . VAL   A 77  ? 0.1637 0.1277 0.1747 0.0159  0.0239  0.0048  77  VAL   A O   
1948 C CB  . VAL   A 77  ? 0.1861 0.1452 0.1821 0.0062  0.0001  0.0175  77  VAL   A CB  
1949 C CG1 . VAL   A 77  ? 0.1828 0.1543 0.1970 0.0108  -0.0108 0.0178  77  VAL   A CG1 
1950 C CG2 . VAL   A 77  ? 0.2073 0.1579 0.2010 0.0022  -0.0073 0.0248  77  VAL   A CG2 
1960 N N   . GLY   A 78  ? 0.1550 0.1203 0.1626 0.0038  0.0142  0.0142  78  GLY   A N   
1961 C CA  . GLY   A 78  ? 0.1447 0.1206 0.1738 0.0024  0.0133  0.0138  78  GLY   A CA  
1962 C C   . GLY   A 78  ? 0.1327 0.1179 0.1718 0.0032  0.0128  0.0070  78  GLY   A C   
1963 O O   . GLY   A 78  ? 0.1394 0.1174 0.1920 0.0038  0.0150  0.0225  78  GLY   A O   
1967 N N   . GLY   A 79  ? 0.1347 0.1162 0.1719 0.0042  0.0101  0.0082  79  GLY   A N   
1968 C CA  . GLY   A 79  ? 0.1318 0.1183 0.1809 0.0012  0.0115  0.0096  79  GLY   A CA  
1969 C C   . GLY   A 79  ? 0.1229 0.1069 0.1907 -0.0014 0.0069  0.0005  79  GLY   A C   
1970 O O   . GLY   A 79  ? 0.1289 0.1252 0.1955 0.0181  0.0181  0.0047  79  GLY   A O   
1974 N N   . SER   A 80  ? 0.1162 0.1271 0.2017 -0.0034 0.0120  -0.0052 80  SER   A N   
1975 C CA  . SER   A 80  ? 0.1142 0.1230 0.1830 -0.0027 -0.0038 0.0008  80  SER   A CA  
1976 C C   . SER   A 80  ? 0.1205 0.1257 0.1818 -0.0038 -0.0003 0.0140  80  SER   A C   
1977 O O   . SER   A 80  ? 0.1154 0.1419 0.2115 0.0075  0.0079  0.0000  80  SER   A O   
1978 C CB  . SER   A 80  ? 0.1231 0.1179 0.1971 -0.0110 -0.0042 0.0115  80  SER   A CB  
1979 O OG  . SER   A 80  ? 0.1466 0.1253 0.2387 0.0023  -0.0094 0.0150  80  SER   A OG  
1985 N N   . CYS   A 81  ? 0.1080 0.1176 0.1757 -0.0054 -0.0102 0.0055  81  CYS   A N   
1986 C CA  . CYS   A 81  ? 0.1119 0.1254 0.1774 -0.0056 -0.0081 0.0144  81  CYS   A CA  
1987 C C   . CYS   A 81  ? 0.1121 0.1180 0.1806 -0.0097 -0.0010 0.0175  81  CYS   A C   
1988 O O   . CYS   A 81  ? 0.1150 0.1391 0.1991 0.0002  0.0029  0.0214  81  CYS   A O   
1989 C CB  . CYS   A 81  ? 0.1235 0.1328 0.2057 -0.0184 0.0050  0.0149  81  CYS   A CB  
1990 S SG  . CYS   A 81  ? 0.1337 0.1224 0.1904 -0.0165 -0.0015 0.0085  81  CYS   A SG  
1996 N N   . VAL   A 82  ? 0.1184 0.1359 0.1819 -0.0019 -0.0148 0.0113  82  VAL   A N   
1997 C CA  . VAL   A 82  ? 0.1275 0.1367 0.1761 -0.0016 -0.0080 0.0165  82  VAL   A CA  
1998 C C   . VAL   A 82  ? 0.1298 0.1429 0.1899 -0.0006 -0.0167 0.0184  82  VAL   A C   
1999 O O   . VAL   A 82  ? 0.1256 0.1517 0.2247 -0.0039 -0.0049 -0.0024 82  VAL   A O   
2000 C CB  . VAL   A 82  ? 0.1580 0.1503 0.1949 -0.0032 -0.0021 0.0205  82  VAL   A CB  
2001 C CG1 . VAL   A 82  ? 0.1842 0.1678 0.2073 0.0070  0.0033  0.0195  82  VAL   A CG1 
2002 C CG2 . VAL   A 82  ? 0.1693 0.1481 0.2272 -0.0040 -0.0121 0.0176  82  VAL   A CG2 
2012 N N   . LEU   A 83  ? 0.1215 0.1400 0.1831 -0.0083 -0.0165 0.0032  83  LEU   A N   
2013 C CA  . LEU   A 83  ? 0.1217 0.1467 0.1803 -0.0132 -0.0114 0.0015  83  LEU   A CA  
2014 C C   . LEU   A 83  ? 0.1301 0.1434 0.1876 -0.0128 -0.0177 -0.0010 83  LEU   A C   
2015 O O   . LEU   A 83  ? 0.1405 0.1450 0.1934 -0.0183 -0.0132 0.0114  83  LEU   A O   
2016 C CB  . LEU   A 83  ? 0.1311 0.1472 0.1783 -0.0121 -0.0158 0.0052  83  LEU   A CB  
2017 C CG  . LEU   A 83  ? 0.1446 0.1574 0.1963 -0.0114 0.0009  0.0041  83  LEU   A CG  
2018 C CD1 . LEU   A 83  ? 0.1592 0.1516 0.1952 -0.0153 -0.0003 0.0158  83  LEU   A CD1 
2019 C CD2 . LEU   A 83  ? 0.1514 0.1707 0.2079 -0.0105 0.0218  0.0120  83  LEU   A CD2 
2031 N N   . SER   A 84  ? 0.1445 0.1488 0.1891 -0.0135 -0.0132 0.0020  84  SER   A N   
2032 C CA  . SER   A 84  ? 0.1555 0.1595 0.1808 -0.0140 -0.0099 -0.0018 84  SER   A CA  
2033 C C   . SER   A 84  ? 0.1639 0.1528 0.1701 -0.0162 -0.0034 0.0019  84  SER   A C   
2034 O O   . SER   A 84  ? 0.1542 0.1629 0.1700 -0.0169 -0.0075 -0.0047 84  SER   A O   
2035 C CB  . SER   A 84  ? 0.1624 0.1766 0.1804 -0.0166 -0.0043 -0.0024 84  SER   A CB  
2036 O OG  . SER   A 84  ? 0.1717 0.2051 0.1966 -0.0113 -0.0076 -0.0183 84  SER   A OG  
2042 N N   . GLY   A 85  ? 0.1730 0.1662 0.1711 -0.0258 0.0118  0.0008  85  GLY   A N   
2043 C CA  . GLY   A 85  ? 0.1827 0.1756 0.1808 -0.0263 0.0158  -0.0066 85  GLY   A CA  
2044 C C   . GLY   A 85  ? 0.1820 0.1817 0.1803 -0.0225 0.0069  -0.0120 85  GLY   A C   
2045 O O   . GLY   A 85  ? 0.1787 0.1885 0.1969 -0.0244 0.0337  -0.0211 85  GLY   A O   
2049 N N   . HIS   A 86  ? 0.1860 0.1738 0.1773 -0.0220 0.0030  -0.0068 86  HIS   A N   
2050 C CA  . HIS   A 86  ? 0.1964 0.1832 0.1630 -0.0205 0.0000  -0.0094 86  HIS   A CA  
2051 C C   . HIS   A 86  ? 0.2204 0.1995 0.1714 -0.0209 0.0043  -0.0115 86  HIS   A C   
2052 O O   . HIS   A 86  ? 0.2261 0.2116 0.1753 -0.0084 0.0091  -0.0056 86  HIS   A O   
2053 C CB  . HIS   A 86  ? 0.1847 0.1710 0.1808 -0.0181 0.0072  -0.0079 86  HIS   A CB  
2054 C CG  . HIS   A 86  ? 0.1703 0.1689 0.1933 -0.0105 0.0143  -0.0068 86  HIS   A CG  
2055 N ND1 . HIS   A 86  ? 0.1733 0.1735 0.2185 -0.0243 0.0009  -0.0026 86  HIS   A ND1 
2056 C CD2 . HIS   A 86  ? 0.1700 0.1627 0.1827 -0.0051 0.0140  -0.0018 86  HIS   A CD2 
2057 C CE1 . HIS   A 86  ? 0.1663 0.1725 0.2084 -0.0241 0.0150  0.0045  86  HIS   A CE1 
2058 N NE2 . HIS   A 86  ? 0.1672 0.1623 0.1913 -0.0079 0.0169  0.0113  86  HIS   A NE2 
2066 N N   A ASN   A 87  ? 0.2277 0.2057 0.1762 -0.0203 0.0200  -0.0161 87  ASN   A N   
2067 N N   B ASN   A 87  ? 0.2248 0.2019 0.1798 -0.0259 0.0307  -0.0302 87  ASN   A N   
2068 C CA  A ASN   A 87  ? 0.2390 0.2165 0.1878 -0.0159 0.0343  -0.0109 87  ASN   A CA  
2069 C CA  B ASN   A 87  ? 0.2358 0.2122 0.1962 -0.0229 0.0550  -0.0340 87  ASN   A CA  
2070 C C   A ASN   A 87  ? 0.2392 0.2214 0.2022 -0.0190 0.0439  -0.0013 87  ASN   A C   
2071 C C   B ASN   A 87  ? 0.2292 0.2171 0.2076 -0.0270 0.0595  -0.0234 87  ASN   A C   
2072 O O   A ASN   A 87  ? 0.2456 0.2268 0.2181 -0.0184 0.0548  0.0047  87  ASN   A O   
2073 O O   B ASN   A 87  ? 0.2292 0.2214 0.2223 -0.0266 0.0667  -0.0058 87  ASN   A O   
2074 C CB  A ASN   A 87  ? 0.2497 0.2225 0.1938 -0.0102 0.0292  -0.0101 87  ASN   A CB  
2075 C CB  B ASN   A 87  ? 0.2550 0.2196 0.2050 -0.0163 0.0587  -0.0371 87  ASN   A CB  
2076 C CG  A ASN   A 87  ? 0.2593 0.2308 0.2029 -0.0028 0.0278  -0.0001 87  ASN   A CG  
2077 C CG  B ASN   A 87  ? 0.2706 0.2317 0.2074 -0.0073 0.0711  -0.0228 87  ASN   A CG  
2078 O OD1 A ASN   A 87  ? 0.2654 0.2292 0.2047 0.0070  0.0218  0.0092  87  ASN   A OD1 
2079 O OD1 B ASN   A 87  ? 0.2819 0.2323 0.2048 0.0039  0.0687  -0.0101 87  ASN   A OD1 
2080 N ND2 A ASN   A 87  ? 0.2639 0.2407 0.2154 -0.0015 0.0291  0.0022  87  ASN   A ND2 
2081 N ND2 B ASN   A 87  ? 0.2764 0.2441 0.2186 -0.0027 0.0758  -0.0199 87  ASN   A ND2 
2094 N N   A LEU   A 88  ? 0.2303 0.2199 0.2041 -0.0252 0.0399  0.0024  88  LEU   A N   
2095 N N   B LEU   A 88  ? 0.2216 0.2169 0.2043 -0.0357 0.0486  -0.0253 88  LEU   A N   
2096 C CA  A LEU   A 88  ? 0.2221 0.2175 0.2047 -0.0319 0.0384  0.0086  88  LEU   A CA  
2097 C CA  B LEU   A 88  ? 0.2151 0.2177 0.2033 -0.0431 0.0418  -0.0147 88  LEU   A CA  
2098 C C   A LEU   A 88  ? 0.2221 0.2156 0.1955 -0.0377 0.0371  0.0149  88  LEU   A C   
2099 C C   B LEU   A 88  ? 0.2201 0.2186 0.1972 -0.0453 0.0334  0.0028  88  LEU   A C   
2100 O O   A LEU   A 88  ? 0.2253 0.2206 0.1955 -0.0355 0.0447  0.0282  88  LEU   A O   
2101 O O   B LEU   A 88  ? 0.2275 0.2300 0.2034 -0.0443 0.0316  0.0095  88  LEU   A O   
2102 C CB  A LEU   A 88  ? 0.2219 0.2233 0.2266 -0.0314 0.0236  0.0089  88  LEU   A CB  
2103 C CB  B LEU   A 88  ? 0.2163 0.2273 0.2250 -0.0462 0.0211  -0.0196 88  LEU   A CB  
2104 C CG  A LEU   A 88  ? 0.2275 0.2299 0.2520 -0.0288 0.0168  0.0084  88  LEU   A CG  
2105 C CG  B LEU   A 88  ? 0.2254 0.2371 0.2437 -0.0430 0.0167  -0.0253 88  LEU   A CG  
2106 C CD1 A LEU   A 88  ? 0.2319 0.2340 0.2591 -0.0268 0.0155  0.0051  88  LEU   A CD1 
2107 C CD1 B LEU   A 88  ? 0.2304 0.2408 0.2346 -0.0419 0.0191  -0.0377 88  LEU   A CD1 
2108 C CD2 A LEU   A 88  ? 0.2340 0.2370 0.2669 -0.0257 0.0122  0.0040  88  LEU   A CD2 
2109 C CD2 B LEU   A 88  ? 0.2362 0.2472 0.2685 -0.0362 0.0090  -0.0278 88  LEU   A CD2 
2132 N N   . ALA   A 89  ? 0.2194 0.2071 0.1854 -0.0387 0.0343  0.0043  89  ALA   A N   
2133 C CA  . ALA   A 89  ? 0.2257 0.2030 0.1798 -0.0352 0.0131  0.0085  89  ALA   A CA  
2134 C C   . ALA   A 89  ? 0.2320 0.2153 0.1858 -0.0318 -0.0083 0.0069  89  ALA   A C   
2135 O O   . ALA   A 89  ? 0.2271 0.2076 0.2118 -0.0397 -0.0234 -0.0104 89  ALA   A O   
2136 C CB  . ALA   A 89  ? 0.2170 0.1994 0.1681 -0.0288 0.0142  0.0085  89  ALA   A CB  
2143 N N   A LYS   A 90  ? 0.2393 0.2260 0.1832 -0.0357 -0.0139 0.0062  90  LYS   A N   
2144 N N   B LYS   A 90  ? 0.2370 0.2215 0.1745 -0.0382 -0.0177 0.0162  90  LYS   A N   
2145 C CA  A LYS   A 90  ? 0.2459 0.2362 0.1956 -0.0333 -0.0204 -0.0010 90  LYS   A CA  
2146 C CA  B LYS   A 90  ? 0.2424 0.2285 0.1771 -0.0346 -0.0261 0.0136  90  LYS   A CA  
2147 C C   A LYS   A 90  ? 0.2250 0.2224 0.1880 -0.0311 -0.0214 -0.0089 90  LYS   A C   
2148 C C   B LYS   A 90  ? 0.2167 0.2058 0.1708 -0.0299 -0.0284 0.0143  90  LYS   A C   
2149 O O   A LYS   A 90  ? 0.2208 0.2294 0.2075 -0.0338 -0.0287 -0.0196 90  LYS   A O   
2150 O O   B LYS   A 90  ? 0.2136 0.2076 0.1933 -0.0319 -0.0405 0.0182  90  LYS   A O   
2151 C CB  A LYS   A 90  ? 0.2702 0.2599 0.2419 -0.0291 -0.0196 0.0065  90  LYS   A CB  
2152 C CB  B LYS   A 90  ? 0.2701 0.2576 0.2254 -0.0298 -0.0219 0.0201  90  LYS   A CB  
2153 C CG  A LYS   A 90  ? 0.2909 0.2813 0.3066 -0.0270 -0.0150 0.0120  90  LYS   A CG  
2154 C CG  B LYS   A 90  ? 0.2942 0.2836 0.2974 -0.0287 -0.0121 0.0267  90  LYS   A CG  
2155 C CD  A LYS   A 90  ? 0.3084 0.2995 0.3651 -0.0243 -0.0080 0.0212  90  LYS   A CD  
2156 C CD  B LYS   A 90  ? 0.3156 0.3066 0.3664 -0.0251 0.0007  0.0367  90  LYS   A CD  
2157 C CE  A LYS   A 90  ? 0.3199 0.3117 0.4095 -0.0226 -0.0035 0.0247  90  LYS   A CE  
2158 C CE  B LYS   A 90  ? 0.3290 0.3226 0.4217 -0.0229 0.0102  0.0411  90  LYS   A CE  
2159 N NZ  A LYS   A 90  ? 0.3279 0.3200 0.4333 -0.0208 -0.0013 0.0260  90  LYS   A NZ  
2160 N NZ  B LYS   A 90  ? 0.3397 0.3328 0.4533 -0.0198 0.0112  0.0452  90  LYS   A NZ  
2187 N N   A HIS   A 91  ? 0.2095 0.2022 0.1681 -0.0259 -0.0260 -0.0078 91  HIS   A N   
2188 N N   B HIS   A 91  ? 0.1997 0.1822 0.1537 -0.0238 -0.0327 0.0045  91  HIS   A N   
2189 C CA  A HIS   A 91  ? 0.1910 0.1909 0.1698 -0.0215 -0.0263 0.0013  91  HIS   A CA  
2190 C CA  B HIS   A 91  ? 0.1829 0.1737 0.1649 -0.0187 -0.0294 0.0075  91  HIS   A CA  
2191 C C   A HIS   A 91  ? 0.1641 0.1704 0.1524 -0.0215 -0.0188 0.0060  91  HIS   A C   
2192 C C   B HIS   A 91  ? 0.1560 0.1561 0.1519 -0.0208 -0.0146 0.0119  91  HIS   A C   
2193 O O   A HIS   A 91  ? 0.1621 0.1782 0.1714 -0.0218 -0.0117 0.0090  91  HIS   A O   
2194 O O   B HIS   A 91  ? 0.1497 0.1592 0.1766 -0.0191 0.0041  0.0095  91  HIS   A O   
2195 C CB  A HIS   A 91  ? 0.2036 0.2108 0.2022 -0.0105 -0.0378 0.0025  91  HIS   A CB  
2196 C CB  B HIS   A 91  ? 0.2005 0.2019 0.1952 0.0008  -0.0487 0.0010  91  HIS   A CB  
2197 C CG  A HIS   A 91  ? 0.2261 0.2405 0.2523 -0.0057 -0.0457 0.0032  91  HIS   A CG  
2198 C CG  B HIS   A 91  ? 0.2339 0.2467 0.2544 0.0102  -0.0630 -0.0047 91  HIS   A CG  
2199 N ND1 A HIS   A 91  ? 0.2322 0.2576 0.2771 -0.0034 -0.0481 0.0000  91  HIS   A ND1 
2200 N ND1 B HIS   A 91  ? 0.2459 0.2722 0.2835 0.0146  -0.0711 -0.0111 91  HIS   A ND1 
2201 C CD2 A HIS   A 91  ? 0.2378 0.2529 0.2735 -0.0044 -0.0459 0.0088  91  HIS   A CD2 
2202 C CD2 B HIS   A 91  ? 0.2503 0.2651 0.2792 0.0135  -0.0643 0.0010  91  HIS   A CD2 
2203 C CE1 A HIS   A 91  ? 0.2388 0.2614 0.2901 -0.0027 -0.0442 0.0092  91  HIS   A CE1 
2204 C CE1 B HIS   A 91  ? 0.2554 0.2786 0.2975 0.0198  -0.0728 -0.0002 91  HIS   A CE1 
2205 N NE2 A HIS   A 91  ? 0.2437 0.2621 0.2888 -0.0022 -0.0455 0.0111  91  HIS   A NE2 
2206 N NE2 B HIS   A 91  ? 0.2620 0.2781 0.3010 0.0170  -0.0709 0.0023  91  HIS   A NE2 
2221 N N   . CYS   A 92  ? 0.1479 0.1548 0.1557 -0.0215 -0.0102 0.0055  92  CYS   A N   
2222 C CA  . CYS   A 92  ? 0.1319 0.1425 0.1732 -0.0121 -0.0011 0.0114  92  CYS   A CA  
2223 C C   . CYS   A 92  ? 0.1210 0.1329 0.1653 -0.0116 0.0021  0.0091  92  CYS   A C   
2224 O O   . CYS   A 92  ? 0.1259 0.1441 0.1829 -0.0194 -0.0014 0.0041  92  CYS   A O   
2225 C CB  . CYS   A 92  ? 0.1342 0.1417 0.1879 -0.0081 -0.0069 0.0130  92  CYS   A CB  
2226 S SG  . CYS   A 92  ? 0.1320 0.1302 0.1785 -0.0123 -0.0004 0.0046  92  CYS   A SG  
2233 N N   . LEU   A 93  ? 0.1196 0.1207 0.1731 -0.0114 0.0069  0.0087  93  LEU   A N   
2234 C CA  . LEU   A 93  ? 0.1151 0.1198 0.1785 -0.0039 -0.0001 0.0045  93  LEU   A CA  
2235 C C   . LEU   A 93  ? 0.1108 0.1084 0.1789 -0.0019 0.0069  -0.0011 93  LEU   A C   
2236 O O   . LEU   A 93  ? 0.1107 0.1175 0.1745 -0.0068 0.0028  0.0123  93  LEU   A O   
2237 C CB  . LEU   A 93  ? 0.1256 0.1189 0.1758 -0.0015 0.0016  0.0210  93  LEU   A CB  
2238 C CG  . LEU   A 93  ? 0.1335 0.1182 0.1760 -0.0077 -0.0019 0.0189  93  LEU   A CG  
2239 C CD1 . LEU   A 93  ? 0.1434 0.1185 0.1921 -0.0045 0.0093  0.0059  93  LEU   A CD1 
2240 C CD2 . LEU   A 93  ? 0.1455 0.1258 0.1901 -0.0116 -0.0054 0.0144  93  LEU   A CD2 
2252 N N   . HIS   A 94  ? 0.1061 0.1047 0.1749 -0.0018 -0.0013 0.0098  94  HIS   A N   
2253 C CA  . HIS   A 94  ? 0.1058 0.1067 0.1755 -0.0035 -0.0057 0.0131  94  HIS   A CA  
2254 C C   . HIS   A 94  ? 0.1080 0.1016 0.1713 -0.0078 -0.0013 0.0063  94  HIS   A C   
2255 O O   . HIS   A 94  ? 0.1091 0.1206 0.1984 0.0036  0.0014  -0.0109 94  HIS   A O   
2256 C CB  . HIS   A 94  ? 0.1087 0.1079 0.1791 -0.0098 -0.0041 0.0124  94  HIS   A CB  
2257 C CG  . HIS   A 94  ? 0.1092 0.1078 0.1779 -0.0116 -0.0065 0.0168  94  HIS   A CG  
2258 N ND1 . HIS   A 94  ? 0.1114 0.1027 0.1846 -0.0067 0.0030  0.0101  94  HIS   A ND1 
2259 C CD2 . HIS   A 94  ? 0.1144 0.1189 0.1892 -0.0087 0.0012  0.0037  94  HIS   A CD2 
2260 C CE1 . HIS   A 94  ? 0.1168 0.1072 0.1785 -0.0110 -0.0090 0.0037  94  HIS   A CE1 
2261 N NE2 . HIS   A 94  ? 0.1218 0.1157 0.1742 -0.0078 -0.0065 -0.0024 94  HIS   A NE2 
2269 N N   . VAL   A 95  ? 0.1077 0.0997 0.1618 -0.0060 0.0059  0.0024  95  VAL   A N   
2270 C CA  . VAL   A 95  ? 0.1089 0.1080 0.1535 -0.0060 0.0035  0.0116  95  VAL   A CA  
2271 C C   . VAL   A 95  ? 0.1100 0.1057 0.1611 -0.0127 -0.0010 0.0074  95  VAL   A C   
2272 O O   . VAL   A 95  ? 0.1162 0.1159 0.1789 0.0077  0.0078  0.0049  95  VAL   A O   
2273 C CB  . VAL   A 95  ? 0.1155 0.1115 0.1694 -0.0138 -0.0020 0.0126  95  VAL   A CB  
2274 C CG1 . VAL   A 95  ? 0.1300 0.1135 0.1740 -0.0171 -0.0031 0.0002  95  VAL   A CG1 
2275 C CG2 . VAL   A 95  ? 0.1205 0.1153 0.1791 -0.0155 -0.0030 0.0176  95  VAL   A CG2 
2285 N N   . VAL   A 96  ? 0.1202 0.1059 0.1576 -0.0037 0.0032  0.0126  96  VAL   A N   
2286 C CA  . VAL   A 96  ? 0.1285 0.1050 0.1655 -0.0004 0.0062  0.0203  96  VAL   A CA  
2287 C C   . VAL   A 96  ? 0.1292 0.1143 0.1668 -0.0008 -0.0001 0.0220  96  VAL   A C   
2288 O O   . VAL   A 96  ? 0.1301 0.1177 0.1995 -0.0004 0.0060  -0.0018 96  VAL   A O   
2289 C CB  . VAL   A 96  ? 0.1302 0.1134 0.1786 -0.0013 0.0099  0.0201  96  VAL   A CB  
2290 C CG1 . VAL   A 96  ? 0.1411 0.1215 0.1727 0.0019  0.0092  0.0124  96  VAL   A CG1 
2291 C CG2 . VAL   A 96  ? 0.1246 0.1242 0.1993 -0.0161 0.0114  0.0203  96  VAL   A CG2 
2301 N N   A GLY   A 97  ? 0.1295 0.1145 0.1538 -0.0027 0.0044  0.0203  97  GLY   A N   
2302 N N   B GLY   A 97  ? 0.1211 0.1170 0.1538 -0.0048 -0.0018 0.0147  97  GLY   A N   
2303 C CA  A GLY   A 97  ? 0.1391 0.1239 0.1567 -0.0016 0.0049  0.0167  97  GLY   A CA  
2304 C CA  B GLY   A 97  ? 0.1269 0.1313 0.1601 -0.0039 0.0004  0.0089  97  GLY   A CA  
2305 C C   A GLY   A 97  ? 0.1448 0.1323 0.1502 0.0031  0.0010  0.0124  97  GLY   A C   
2306 C C   B GLY   A 97  ? 0.1276 0.1427 0.1499 -0.0024 -0.0024 0.0091  97  GLY   A C   
2307 O O   A GLY   A 97  ? 0.1477 0.1292 0.1589 -0.0039 0.0106  0.0158  97  GLY   A O   
2308 O O   B GLY   A 97  ? 0.1300 0.1426 0.1727 -0.0050 0.0100  0.0031  97  GLY   A O   
2315 N N   A PRO   A 98  ? 0.1503 0.1344 0.1448 0.0141  -0.0039 0.0073  98  PRO   A N   
2316 N N   B PRO   A 98  ? 0.1387 0.1431 0.1486 0.0023  -0.0104 0.0218  98  PRO   A N   
2317 C CA  A PRO   A 98  ? 0.1538 0.1496 0.1407 0.0120  -0.0014 -0.0032 98  PRO   A CA  
2318 C CA  B PRO   A 98  ? 0.1563 0.1575 0.1634 -0.0003 -0.0188 0.0133  98  PRO   A CA  
2319 C C   A PRO   A 98  ? 0.1525 0.1570 0.1332 0.0033  0.0090  0.0045  98  PRO   A C   
2320 C C   B PRO   A 98  ? 0.1809 0.1557 0.1631 -0.0063 -0.0197 0.0318  98  PRO   A C   
2321 O O   A PRO   A 98  ? 0.1478 0.1497 0.1479 0.0014  0.0099  0.0044  98  PRO   A O   
2322 O O   B PRO   A 98  ? 0.1712 0.1444 0.1932 -0.0025 -0.0239 0.0381  98  PRO   A O   
2323 C CB  A PRO   A 98  ? 0.1606 0.1545 0.1416 0.0191  -0.0062 -0.0093 98  PRO   A CB  
2324 C CB  B PRO   A 98  ? 0.1609 0.1627 0.1589 0.0042  -0.0264 0.0026  98  PRO   A CB  
2325 C CG  A PRO   A 98  ? 0.1652 0.1474 0.1624 0.0169  -0.0052 -0.0149 98  PRO   A CG  
2326 C CG  B PRO   A 98  ? 0.1671 0.1597 0.1828 -0.0007 -0.0253 0.0016  98  PRO   A CG  
2327 C CD  A PRO   A 98  ? 0.1589 0.1348 0.1539 0.0155  -0.0076 0.0009  98  PRO   A CD  
2328 C CD  B PRO   A 98  ? 0.1522 0.1436 0.1630 -0.0013 -0.0238 0.0155  98  PRO   A CD  
2343 N N   A ASN   A 99  ? 0.1545 0.1752 0.1283 0.0029  0.0111  0.0124  99  ASN   A N   
2344 N N   B ASN   A 99  ? 0.2204 0.1652 0.1528 -0.0033 -0.0241 0.0417  99  ASN   A N   
2345 C CA  A ASN   A 99  ? 0.1676 0.1872 0.1353 -0.0002 0.0065  0.0172  99  ASN   A CA  
2346 C CA  B ASN   A 99  ? 0.2600 0.1701 0.1644 -0.0012 -0.0342 0.0544  99  ASN   A CA  
2347 C C   A ASN   A 99  ? 0.1822 0.2098 0.1368 -0.0131 0.0025  0.0216  99  ASN   A C   
2348 C C   B ASN   A 99  ? 0.2903 0.1937 0.1647 -0.0023 -0.0441 0.0545  99  ASN   A C   
2349 O O   A ASN   A 99  ? 0.1893 0.2156 0.1259 -0.0031 0.0025  0.0124  99  ASN   A O   
2350 O O   B ASN   A 99  ? 0.3001 0.1842 0.1736 0.0013  -0.0490 0.0382  99  ASN   A O   
2351 C CB  A ASN   A 99  ? 0.1683 0.1856 0.1255 0.0086  0.0044  0.0220  99  ASN   A CB  
2352 C CB  B ASN   A 99  ? 0.2722 0.1690 0.1935 0.0023  -0.0496 0.0562  99  ASN   A CB  
2353 C CG  A ASN   A 99  ? 0.1717 0.1845 0.1353 0.0181  0.0026  0.0193  99  ASN   A CG  
2354 C CG  B ASN   A 99  ? 0.2848 0.1717 0.2343 0.0024  -0.0586 0.0614  99  ASN   A CG  
2355 O OD1 A ASN   A 99  ? 0.1789 0.1930 0.1534 0.0264  0.0015  0.0067  99  ASN   A OD1 
2356 O OD1 B ASN   A 99  ? 0.2970 0.1824 0.2387 0.0078  -0.0644 0.0617  99  ASN   A OD1 
2357 N ND2 A ASN   A 99  ? 0.1725 0.1824 0.1446 0.0224  -0.0059 0.0203  99  ASN   A ND2 
2358 N ND2 B ASN   A 99  ? 0.2836 0.1742 0.2631 0.0051  -0.0634 0.0434  99  ASN   A ND2 
2371 N N   A VAL   A 100 ? 0.1961 0.2270 0.1613 -0.0300 -0.0266 0.0275  100 VAL   A N   
2372 N N   B VAL   A 100 ? 0.3108 0.2316 0.1912 -0.0130 -0.0656 0.0505  100 VAL   A N   
2373 C CA  A VAL   A 100 ? 0.2191 0.2466 0.1924 -0.0357 -0.0362 0.0365  100 VAL   A CA  
2374 C CA  B VAL   A 100 ? 0.3356 0.2733 0.2343 -0.0224 -0.0654 0.0455  100 VAL   A CA  
2375 C C   A VAL   A 100 ? 0.2253 0.2532 0.1882 -0.0387 -0.0396 0.0575  100 VAL   A C   
2376 C C   B VAL   A 100 ? 0.3503 0.2939 0.2508 -0.0216 -0.0657 0.0564  100 VAL   A C   
2377 O O   A VAL   A 100 ? 0.2290 0.2562 0.2082 -0.0368 -0.0353 0.0586  100 VAL   A O   
2378 O O   B VAL   A 100 ? 0.3540 0.2929 0.2564 -0.0272 -0.0633 0.0504  100 VAL   A O   
2379 C CB  A VAL   A 100 ? 0.2390 0.2588 0.2395 -0.0405 -0.0447 0.0253  100 VAL   A CB  
2380 C CB  B VAL   A 100 ? 0.3464 0.2924 0.2662 -0.0309 -0.0677 0.0335  100 VAL   A CB  
2381 C CG1 A VAL   A 100 ? 0.2402 0.2671 0.2612 -0.0461 -0.0401 0.0244  100 VAL   A CG1 
2382 C CG1 B VAL   A 100 ? 0.3501 0.3031 0.2868 -0.0320 -0.0590 0.0319  100 VAL   A CG1 
2383 C CG2 A VAL   A 100 ? 0.2492 0.2602 0.2495 -0.0409 -0.0488 0.0180  100 VAL   A CG2 
2384 C CG2 B VAL   A 100 ? 0.3515 0.2981 0.2701 -0.0347 -0.0712 0.0230  100 VAL   A CG2 
2403 N N   A ASN   A 101 ? 0.2278 0.2549 0.1756 -0.0413 -0.0438 0.0781  101 ASN   A N   
2404 N N   B ASN   A 101 ? 0.3597 0.3128 0.2693 -0.0139 -0.0682 0.0741  101 ASN   A N   
2405 C CA  A ASN   A 101 ? 0.2415 0.2588 0.1827 -0.0420 -0.0507 0.0846  101 ASN   A CA  
2406 C CA  B ASN   A 101 ? 0.3697 0.3325 0.2886 -0.0062 -0.0728 0.0833  101 ASN   A CA  
2407 C C   A ASN   A 101 ? 0.2590 0.2759 0.2072 -0.0450 -0.0393 0.0944  101 ASN   A C   
2408 C C   B ASN   A 101 ? 0.3872 0.3480 0.2972 -0.0080 -0.0589 0.0984  101 ASN   A C   
2409 O O   A ASN   A 101 ? 0.2657 0.2754 0.2221 -0.0426 -0.0358 0.0993  101 ASN   A O   
2410 O O   B ASN   A 101 ? 0.3950 0.3485 0.3053 -0.0060 -0.0555 0.1064  101 ASN   A O   
2411 C CB  A ASN   A 101 ? 0.2410 0.2495 0.1650 -0.0348 -0.0673 0.0750  101 ASN   A CB  
2412 C CB  B ASN   A 101 ? 0.3612 0.3351 0.3034 -0.0001 -0.0840 0.0729  101 ASN   A CB  
2413 C CG  A ASN   A 101 ? 0.2398 0.2407 0.1544 -0.0280 -0.0800 0.0561  101 ASN   A CG  
2414 C CG  B ASN   A 101 ? 0.3536 0.3390 0.3159 0.0047  -0.0864 0.0599  101 ASN   A CG  
2415 O OD1 A ASN   A 101 ? 0.2424 0.2436 0.1652 -0.0195 -0.0738 0.0375  101 ASN   A OD1 
2416 O OD1 B ASN   A 101 ? 0.3473 0.3449 0.3143 0.0140  -0.0975 0.0553  101 ASN   A OD1 
2417 N ND2 A ASN   A 101 ? 0.2429 0.2341 0.1560 -0.0323 -0.0750 0.0501  101 ASN   A ND2 
2418 N ND2 B ASN   A 101 ? 0.3513 0.3364 0.3254 0.0051  -0.0864 0.0585  101 ASN   A ND2 
2431 N N   A LYS   A 102 ? 0.2681 0.2968 0.2331 -0.0515 -0.0320 0.0840  102 LYS   A N   
2432 N N   B LYS   A 102 ? 0.3947 0.3634 0.3060 -0.0128 -0.0455 0.0931  102 LYS   A N   
2433 C CA  A LYS   A 102 ? 0.2812 0.3174 0.2472 -0.0544 -0.0360 0.0661  102 LYS   A CA  
2434 C CA  B LYS   A 102 ? 0.4015 0.3756 0.2936 -0.0175 -0.0374 0.0893  102 LYS   A CA  
2435 C C   A LYS   A 102 ? 0.2937 0.3362 0.2414 -0.0500 -0.0302 0.0590  102 LYS   A C   
2436 C C   B LYS   A 102 ? 0.3994 0.3734 0.2569 -0.0262 -0.0355 0.0953  102 LYS   A C   
2437 O O   A LYS   A 102 ? 0.2986 0.3440 0.2501 -0.0478 -0.0280 0.0556  102 LYS   A O   
2438 O O   B LYS   A 102 ? 0.3998 0.3756 0.2549 -0.0300 -0.0343 0.1006  102 LYS   A O   
2439 C CB  A LYS   A 102 ? 0.2854 0.3199 0.2726 -0.0610 -0.0413 0.0528  102 LYS   A CB  
2440 C CB  B LYS   A 102 ? 0.4098 0.3893 0.3307 -0.0179 -0.0334 0.0695  102 LYS   A CB  
2441 C CG  A LYS   A 102 ? 0.2914 0.3211 0.2971 -0.0641 -0.0467 0.0368  102 LYS   A CG  
2442 C CG  B LYS   A 102 ? 0.4160 0.4001 0.3675 -0.0186 -0.0318 0.0510  102 LYS   A CG  
2443 C CD  A LYS   A 102 ? 0.2986 0.3243 0.3196 -0.0645 -0.0521 0.0170  102 LYS   A CD  
2444 C CD  B LYS   A 102 ? 0.4229 0.4112 0.4053 -0.0180 -0.0334 0.0321  102 LYS   A CD  
2445 C CE  A LYS   A 102 ? 0.3046 0.3258 0.3361 -0.0644 -0.0549 0.0057  102 LYS   A CE  
2446 C CE  B LYS   A 102 ? 0.4278 0.4198 0.4345 -0.0162 -0.0374 0.0193  102 LYS   A CE  
2447 N NZ  A LYS   A 102 ? 0.3074 0.3250 0.3438 -0.0670 -0.0518 -0.0006 102 LYS   A NZ  
2448 N NZ  B LYS   A 102 ? 0.4304 0.4235 0.4514 -0.0155 -0.0384 0.0104  102 LYS   A NZ  
2475 N N   A GLY   A 103 ? 0.2996 0.3472 0.2407 -0.0463 -0.0225 0.0499  103 GLY   A N   
2476 N N   B GLY   A 103 ? 0.3935 0.3678 0.2318 -0.0290 -0.0404 0.0814  103 GLY   A N   
2477 C CA  A GLY   A 103 ? 0.3061 0.3546 0.2340 -0.0424 -0.0156 0.0394  103 GLY   A CA  
2478 C CA  B GLY   A 103 ? 0.3862 0.3587 0.2100 -0.0338 -0.0374 0.0724  103 GLY   A CA  
2479 C C   A GLY   A 103 ? 0.3092 0.3618 0.2392 -0.0382 -0.0041 0.0277  103 GLY   A C   
2480 C C   B GLY   A 103 ? 0.3752 0.3468 0.2034 -0.0395 -0.0316 0.0545  103 GLY   A C   
2481 O O   A GLY   A 103 ? 0.3118 0.3643 0.2481 -0.0397 0.0007  0.0177  103 GLY   A O   
2482 O O   B GLY   A 103 ? 0.3794 0.3492 0.2197 -0.0405 -0.0217 0.0508  103 GLY   A O   
2489 N N   A GLU   A 104 ? 0.3079 0.3634 0.2221 -0.0332 0.0034  0.0267  104 GLU   A N   
2490 N N   B GLU   A 104 ? 0.3576 0.3296 0.1791 -0.0412 -0.0329 0.0469  104 GLU   A N   
2491 C CA  A GLU   A 104 ? 0.3018 0.3619 0.2131 -0.0322 0.0105  0.0246  104 GLU   A CA  
2492 C CA  B GLU   A 104 ? 0.3327 0.3078 0.1747 -0.0492 -0.0311 0.0383  104 GLU   A CA  
2493 C C   A GLU   A 104 ? 0.3086 0.3738 0.2230 -0.0340 0.0096  0.0163  104 GLU   A C   
2494 C C   B GLU   A 104 ? 0.3223 0.3118 0.1861 -0.0532 -0.0270 0.0211  104 GLU   A C   
2495 O O   A GLU   A 104 ? 0.3068 0.3763 0.2340 -0.0349 0.0077  0.0112  104 GLU   A O   
2496 O O   B GLU   A 104 ? 0.3211 0.3108 0.2097 -0.0490 -0.0312 0.0185  104 GLU   A O   
2497 C CB  A GLU   A 104 ? 0.2884 0.3489 0.1982 -0.0301 0.0201  0.0313  104 GLU   A CB  
2498 C CB  B GLU   A 104 ? 0.3167 0.2844 0.1714 -0.0549 -0.0280 0.0491  104 GLU   A CB  
2499 C CG  A GLU   A 104 ? 0.2758 0.3374 0.1955 -0.0265 0.0294  0.0351  104 GLU   A CG  
2500 C CG  B GLU   A 104 ? 0.3018 0.2677 0.1813 -0.0583 -0.0285 0.0537  104 GLU   A CG  
2501 C CD  A GLU   A 104 ? 0.2637 0.3269 0.1936 -0.0235 0.0383  0.0400  104 GLU   A CD  
2502 C CD  B GLU   A 104 ? 0.2857 0.2532 0.1728 -0.0616 -0.0283 0.0648  104 GLU   A CD  
2503 O OE1 A GLU   A 104 ? 0.2515 0.3207 0.1777 -0.0216 0.0454  0.0449  104 GLU   A OE1 
2504 O OE1 B GLU   A 104 ? 0.2729 0.2488 0.1559 -0.0590 -0.0412 0.0622  104 GLU   A OE1 
2505 O OE2 A GLU   A 104 ? 0.2690 0.3258 0.2133 -0.0198 0.0375  0.0331  104 GLU   A OE2 
2506 O OE2 B GLU   A 104 ? 0.2917 0.2455 0.1875 -0.0628 -0.0204 0.0714  104 GLU   A OE2 
2519 N N   A ASP   A 105 ? 0.3174 0.3835 0.2344 -0.0344 0.0124  0.0092  105 ASP   A N   
2520 N N   B ASP   A 105 ? 0.3133 0.3189 0.1887 -0.0615 -0.0145 0.0036  105 ASP   A N   
2521 C CA  A ASP   A 105 ? 0.3249 0.3916 0.2530 -0.0340 0.0091  -0.0008 105 ASP   A CA  
2522 C CA  B ASP   A 105 ? 0.3070 0.3280 0.2086 -0.0630 -0.0052 -0.0194 105 ASP   A CA  
2523 C C   A ASP   A 105 ? 0.3093 0.3834 0.2441 -0.0348 -0.0006 -0.0070 105 ASP   A C   
2524 C C   B ASP   A 105 ? 0.2690 0.3148 0.1853 -0.0690 -0.0046 -0.0244 105 ASP   A C   
2525 O O   A ASP   A 105 ? 0.3030 0.3827 0.2264 -0.0332 -0.0042 -0.0107 105 ASP   A O   
2526 O O   B ASP   A 105 ? 0.2454 0.2961 0.1460 -0.0734 -0.0089 -0.0382 105 ASP   A O   
2527 C CB  A ASP   A 105 ? 0.3449 0.4045 0.2848 -0.0316 0.0155  -0.0056 105 ASP   A CB  
2528 C CB  B ASP   A 105 ? 0.3366 0.3458 0.2640 -0.0564 -0.0001 -0.0388 105 ASP   A CB  
2529 C CG  A ASP   A 105 ? 0.3601 0.4142 0.3145 -0.0285 0.0189  -0.0106 105 ASP   A CG  
2530 C CG  B ASP   A 105 ? 0.3601 0.3597 0.3129 -0.0463 -0.0005 -0.0558 105 ASP   A CG  
2531 O OD1 A ASP   A 105 ? 0.3672 0.4191 0.3195 -0.0288 0.0166  -0.0187 105 ASP   A OD1 
2532 O OD1 B ASP   A 105 ? 0.3683 0.3593 0.3128 -0.0490 -0.0045 -0.0710 105 ASP   A OD1 
2533 O OD2 A ASP   A 105 ? 0.3654 0.4176 0.3334 -0.0273 0.0237  -0.0064 105 ASP   A OD2 
2534 O OD2 B ASP   A 105 ? 0.3741 0.3700 0.3512 -0.0419 -0.0019 -0.0538 105 ASP   A OD2 
2543 N N   A ILE   A 106 ? 0.2979 0.3736 0.2536 -0.0371 -0.0175 -0.0098 106 ILE   A N   
2544 N N   B ILE   A 106 ? 0.2541 0.3231 0.2061 -0.0665 -0.0254 -0.0148 106 ILE   A N   
2545 C CA  A ILE   A 106 ? 0.2823 0.3589 0.2599 -0.0409 -0.0285 -0.0173 106 ILE   A CA  
2546 C CA  B ILE   A 106 ? 0.2332 0.3215 0.2220 -0.0683 -0.0395 -0.0177 106 ILE   A CA  
2547 C C   A ILE   A 106 ? 0.2691 0.3368 0.2571 -0.0480 -0.0222 -0.0363 106 ILE   A C   
2548 C C   B ILE   A 106 ? 0.2140 0.2985 0.2221 -0.0793 -0.0466 -0.0396 106 ILE   A C   
2549 O O   A ILE   A 106 ? 0.2590 0.3311 0.2421 -0.0487 -0.0221 -0.0440 106 ILE   A O   
2550 O O   B ILE   A 106 ? 0.1933 0.2853 0.2234 -0.0803 -0.0332 -0.0436 106 ILE   A O   
2551 C CB  A ILE   A 106 ? 0.2831 0.3664 0.2760 -0.0355 -0.0445 -0.0046 106 ILE   A CB  
2552 C CB  B ILE   A 106 ? 0.2371 0.3431 0.2472 -0.0546 -0.0470 0.0006  106 ILE   A CB  
2553 C CG1 A ILE   A 106 ? 0.2809 0.3690 0.2872 -0.0288 -0.0517 0.0091  106 ILE   A CG1 
2554 C CG1 B ILE   A 106 ? 0.2349 0.3527 0.2716 -0.0397 -0.0495 0.0213  106 ILE   A CG1 
2555 C CG2 A ILE   A 106 ? 0.2842 0.3688 0.2849 -0.0356 -0.0475 -0.0045 106 ILE   A CG2 
2556 C CG2 B ILE   A 106 ? 0.2394 0.3498 0.2640 -0.0552 -0.0483 0.0009  106 ILE   A CG2 
2557 C CD1 A ILE   A 106 ? 0.2805 0.3683 0.2893 -0.0228 -0.0515 0.0165  106 ILE   A CD1 
2558 C CD1 B ILE   A 106 ? 0.2361 0.3541 0.2802 -0.0280 -0.0419 0.0336  106 ILE   A CD1 
2581 N N   A GLN   A 107 ? 0.2704 0.3206 0.2734 -0.0497 -0.0078 -0.0449 107 GLN   A N   
2582 N N   B GLN   A 107 ? 0.2351 0.2918 0.2426 -0.0729 -0.0397 -0.0455 107 GLN   A N   
2583 C CA  A GLN   A 107 ? 0.2722 0.3025 0.3109 -0.0459 0.0067  -0.0469 107 GLN   A CA  
2584 C CA  B GLN   A 107 ? 0.2584 0.2837 0.2964 -0.0572 -0.0178 -0.0454 107 GLN   A CA  
2585 C C   A GLN   A 107 ? 0.2439 0.2570 0.2862 -0.0418 0.0145  -0.0410 107 GLN   A C   
2586 C C   B GLN   A 107 ? 0.2372 0.2441 0.2848 -0.0464 0.0034  -0.0400 107 GLN   A C   
2587 O O   A GLN   A 107 ? 0.2480 0.2558 0.3134 -0.0410 0.0201  -0.0370 107 GLN   A O   
2588 O O   B GLN   A 107 ? 0.2421 0.2347 0.3119 -0.0453 0.0105  -0.0449 107 GLN   A O   
2589 C CB  A GLN   A 107 ? 0.2975 0.3254 0.3745 -0.0496 0.0076  -0.0486 107 GLN   A CB  
2590 C CB  B GLN   A 107 ? 0.2989 0.3121 0.3683 -0.0588 -0.0274 -0.0390 107 GLN   A CB  
2591 C CG  A GLN   A 107 ? 0.3205 0.3481 0.4413 -0.0510 0.0073  -0.0474 107 GLN   A CG  
2592 C CG  B GLN   A 107 ? 0.3342 0.3375 0.4432 -0.0613 -0.0330 -0.0267 107 GLN   A CG  
2593 C CD  A GLN   A 107 ? 0.3400 0.3644 0.4976 -0.0528 0.0089  -0.0425 107 GLN   A CD  
2594 C CD  B GLN   A 107 ? 0.3631 0.3610 0.5063 -0.0559 -0.0362 -0.0146 107 GLN   A CD  
2595 O OE1 A GLN   A 107 ? 0.3491 0.3717 0.5200 -0.0522 0.0103  -0.0437 107 GLN   A OE1 
2596 O OE1 B GLN   A 107 ? 0.3741 0.3716 0.5253 -0.0538 -0.0367 -0.0074 107 GLN   A OE1 
2597 N NE2 A GLN   A 107 ? 0.3452 0.3679 0.5157 -0.0559 0.0085  -0.0409 107 GLN   A NE2 
2598 N NE2 B GLN   A 107 ? 0.3736 0.3686 0.5298 -0.0538 -0.0376 -0.0110 107 GLN   A NE2 
2615 N N   . LEU   A 108 ? 0.2116 0.2110 0.2451 -0.0404 0.0132  -0.0443 108 LEU   A N   
2616 C CA  . LEU   A 108 ? 0.1817 0.1663 0.2208 -0.0133 0.0097  -0.0000 108 LEU   A CA  
2617 C C   . LEU   A 108 ? 0.1562 0.1396 0.2157 -0.0089 -0.0035 0.0191  108 LEU   A C   
2618 O O   . LEU   A 108 ? 0.1476 0.1482 0.2361 -0.0061 0.0044  0.0171  108 LEU   A O   
2619 C CB  . LEU   A 108 ? 0.1843 0.1778 0.2046 -0.0160 0.0127  -0.0027 108 LEU   A CB  
2620 C CG  . LEU   A 108 ? 0.2010 0.2010 0.2156 -0.0073 0.0221  -0.0093 108 LEU   A CG  
2621 C CD1 . LEU   A 108 ? 0.2241 0.2137 0.2149 -0.0151 0.0292  -0.0061 108 LEU   A CD1 
2622 C CD2 . LEU   A 108 ? 0.2033 0.2313 0.2562 0.0007  0.0328  -0.0041 108 LEU   A CD2 
2635 N N   . LEU   A 109 ? 0.1423 0.1375 0.2154 -0.0025 -0.0094 0.0268  109 LEU   A N   
2636 C CA  . LEU   A 109 ? 0.1393 0.1363 0.2070 0.0010  -0.0132 0.0229  109 LEU   A CA  
2637 C C   . LEU   A 109 ? 0.1276 0.1268 0.2003 -0.0052 -0.0075 0.0043  109 LEU   A C   
2638 O O   . LEU   A 109 ? 0.1356 0.1171 0.2091 -0.0045 -0.0122 0.0082  109 LEU   A O   
2639 C CB  . LEU   A 109 ? 0.1442 0.1425 0.2163 0.0008  -0.0237 0.0255  109 LEU   A CB  
2640 C CG  . LEU   A 109 ? 0.1444 0.1449 0.2300 0.0010  -0.0112 0.0331  109 LEU   A CG  
2641 C CD1 . LEU   A 109 ? 0.1533 0.1382 0.2397 -0.0003 -0.0110 0.0125  109 LEU   A CD1 
2642 C CD2 . LEU   A 109 ? 0.1465 0.1659 0.2488 0.0030  -0.0062 0.0296  109 LEU   A CD2 
2654 N N   . LYS   A 110 ? 0.1308 0.1197 0.2036 -0.0089 -0.0123 0.0112  110 LYS   A N   
2655 C CA  . LYS   A 110 ? 0.1257 0.1159 0.2002 -0.0084 -0.0110 0.0131  110 LYS   A CA  
2656 C C   . LYS   A 110 ? 0.1279 0.1091 0.1917 -0.0070 -0.0110 0.0032  110 LYS   A C   
2657 O O   . LYS   A 110 ? 0.1210 0.1120 0.2038 -0.0043 -0.0052 0.0017  110 LYS   A O   
2658 C CB  . LYS   A 110 ? 0.1346 0.1266 0.2221 -0.0074 -0.0226 0.0003  110 LYS   A CB  
2659 C CG  . LYS   A 110 ? 0.1382 0.1208 0.2204 -0.0026 -0.0146 -0.0008 110 LYS   A CG  
2660 C CD  . LYS   A 110 ? 0.1417 0.1211 0.2234 -0.0079 -0.0176 -0.0050 110 LYS   A CD  
2661 C CE  . LYS   A 110 ? 0.1495 0.1284 0.2368 -0.0002 -0.0018 -0.0015 110 LYS   A CE  
2662 N NZ  . LYS   A 110 ? 0.1496 0.1324 0.2512 -0.0093 0.0039  -0.0036 110 LYS   A NZ  
2676 N N   . SER   A 111 ? 0.1265 0.1130 0.1806 -0.0028 -0.0085 0.0091  111 SER   A N   
2677 C CA  . SER   A 111 ? 0.1241 0.1163 0.1950 -0.0005 -0.0003 0.0066  111 SER   A CA  
2678 C C   . SER   A 111 ? 0.1189 0.1148 0.1818 -0.0024 -0.0008 0.0190  111 SER   A C   
2679 O O   . SER   A 111 ? 0.1302 0.1078 0.1985 -0.0017 -0.0032 0.0119  111 SER   A O   
2680 C CB  . SER   A 111 ? 0.1463 0.1320 0.2050 -0.0020 0.0096  -0.0022 111 SER   A CB  
2681 O OG  . SER   A 111 ? 0.2013 0.1566 0.2206 -0.0050 0.0178  -0.0142 111 SER   A OG  
2687 N N   . ALA   A 112 ? 0.1189 0.1095 0.1917 0.0033  0.0098  0.0083  112 ALA   A N   
2688 C CA  . ALA   A 112 ? 0.1215 0.1097 0.1770 -0.0016 0.0061  0.0055  112 ALA   A CA  
2689 C C   . ALA   A 112 ? 0.1152 0.1001 0.1862 -0.0016 -0.0017 0.0041  112 ALA   A C   
2690 O O   . ALA   A 112 ? 0.1182 0.1080 0.1910 -0.0101 -0.0018 0.0117  112 ALA   A O   
2691 C CB  . ALA   A 112 ? 0.1339 0.1086 0.1878 -0.0064 -0.0003 0.0139  112 ALA   A CB  
2697 N N   . TYR   A 113 ? 0.1125 0.1023 0.2046 -0.0040 -0.0032 0.0103  113 TYR   A N   
2698 C CA  . TYR   A 113 ? 0.1089 0.1027 0.1919 -0.0039 0.0014  0.0175  113 TYR   A CA  
2699 C C   . TYR   A 113 ? 0.1109 0.1066 0.1889 -0.0129 -0.0001 0.0014  113 TYR   A C   
2700 O O   . TYR   A 113 ? 0.1082 0.1070 0.1999 -0.0005 0.0061  0.0061  113 TYR   A O   
2701 C CB  . TYR   A 113 ? 0.1131 0.1070 0.2049 -0.0014 -0.0124 0.0157  113 TYR   A CB  
2702 C CG  . TYR   A 113 ? 0.1166 0.1110 0.2052 -0.0092 0.0011  0.0153  113 TYR   A CG  
2703 C CD1 . TYR   A 113 ? 0.1209 0.1266 0.1977 -0.0046 -0.0028 0.0122  113 TYR   A CD1 
2704 C CD2 . TYR   A 113 ? 0.1237 0.1172 0.2052 -0.0092 -0.0128 0.0167  113 TYR   A CD2 
2705 C CE1 . TYR   A 113 ? 0.1169 0.1292 0.2155 -0.0029 0.0013  0.0184  113 TYR   A CE1 
2706 C CE2 . TYR   A 113 ? 0.1165 0.1264 0.2129 -0.0094 -0.0120 0.0189  113 TYR   A CE2 
2707 C CZ  . TYR   A 113 ? 0.1127 0.1204 0.2214 0.0032  -0.0000 0.0235  113 TYR   A CZ  
2708 O OH  . TYR   A 113 ? 0.1212 0.1306 0.2646 0.0055  -0.0080 0.0155  113 TYR   A OH  
2718 N N   . GLU   A 114 ? 0.1051 0.1050 0.1924 -0.0024 0.0025  0.0093  114 GLU   A N   
2719 C CA  . GLU   A 114 ? 0.1060 0.1008 0.1995 0.0014  0.0023  0.0227  114 GLU   A CA  
2720 C C   . GLU   A 114 ? 0.1055 0.1045 0.1962 0.0029  0.0125  0.0076  114 GLU   A C   
2721 O O   . GLU   A 114 ? 0.1194 0.1047 0.2003 -0.0017 -0.0020 0.0104  114 GLU   A O   
2722 C CB  . GLU   A 114 ? 0.1069 0.1104 0.2058 -0.0037 -0.0015 0.0155  114 GLU   A CB  
2723 C CG  . GLU   A 114 ? 0.1184 0.1113 0.2087 -0.0010 0.0001  0.0057  114 GLU   A CG  
2724 C CD  . GLU   A 114 ? 0.1243 0.1098 0.2095 -0.0046 -0.0062 0.0026  114 GLU   A CD  
2725 O OE1 . GLU   A 114 ? 0.1276 0.1117 0.2104 -0.0065 0.0049  -0.0029 114 GLU   A OE1 
2726 O OE2 . GLU   A 114 ? 0.1401 0.1164 0.2250 -0.0089 0.0019  -0.0049 114 GLU   A OE2 
2733 N N   . ASN   A 115 ? 0.1101 0.1029 0.1825 -0.0074 0.0006  0.0035  115 ASN   A N   
2734 C CA  . ASN   A 115 ? 0.1140 0.1090 0.1863 -0.0049 0.0066  0.0100  115 ASN   A CA  
2735 C C   . ASN   A 115 ? 0.1158 0.1145 0.1808 -0.0102 0.0059  -0.0023 115 ASN   A C   
2736 O O   . ASN   A 115 ? 0.1185 0.1260 0.1795 -0.0121 0.0036  0.0070  115 ASN   A O   
2737 C CB  . ASN   A 115 ? 0.1250 0.1148 0.1751 -0.0098 0.0069  0.0108  115 ASN   A CB  
2738 C CG  . ASN   A 115 ? 0.1174 0.1370 0.1868 -0.0100 0.0016  0.0107  115 ASN   A CG  
2739 O OD1 . ASN   A 115 ? 0.1272 0.2285 0.2057 -0.0074 0.0088  0.0304  115 ASN   A OD1 
2740 N ND2 . ASN   A 115 ? 0.1197 0.1221 0.1855 -0.0113 0.0149  0.0154  115 ASN   A ND2 
2747 N N   . PHE   A 116 ? 0.1138 0.1146 0.1866 -0.0066 0.0025  0.0142  116 PHE   A N   
2748 C CA  . PHE   A 116 ? 0.1103 0.1205 0.1822 0.0001  0.0062  0.0192  116 PHE   A CA  
2749 C C   . PHE   A 116 ? 0.1135 0.1252 0.1903 -0.0056 0.0092  0.0200  116 PHE   A C   
2750 O O   . PHE   A 116 ? 0.1258 0.1296 0.1993 -0.0019 0.0036  0.0231  116 PHE   A O   
2751 C CB  . PHE   A 116 ? 0.1129 0.1111 0.1968 -0.0030 0.0106  0.0152  116 PHE   A CB  
2752 C CG  . PHE   A 116 ? 0.1111 0.1104 0.1951 -0.0087 0.0089  0.0135  116 PHE   A CG  
2753 C CD1 . PHE   A 116 ? 0.1115 0.1205 0.2074 -0.0072 0.0039  0.0165  116 PHE   A CD1 
2754 C CD2 . PHE   A 116 ? 0.1177 0.1238 0.2042 -0.0065 0.0061  0.0082  116 PHE   A CD2 
2755 C CE1 . PHE   A 116 ? 0.1092 0.1180 0.2121 -0.0096 0.0031  0.0156  116 PHE   A CE1 
2756 C CE2 . PHE   A 116 ? 0.1127 0.1178 0.2122 -0.0040 0.0058  0.0066  116 PHE   A CE2 
2757 C CZ  . PHE   A 116 ? 0.1207 0.1128 0.2081 -0.0017 0.0046  0.0091  116 PHE   A CZ  
2767 N N   . ASN   A 117 ? 0.1149 0.1221 0.1931 -0.0054 0.0103  0.0152  117 ASN   A N   
2768 C CA  . ASN   A 117 ? 0.1209 0.1145 0.2015 -0.0019 0.0056  0.0244  117 ASN   A CA  
2769 C C   . ASN   A 117 ? 0.1179 0.1292 0.2141 0.0023  -0.0026 0.0287  117 ASN   A C   
2770 O O   . ASN   A 117 ? 0.1333 0.1319 0.2334 -0.0034 -0.0088 0.0392  117 ASN   A O   
2771 C CB  . ASN   A 117 ? 0.1161 0.1167 0.1994 0.0006  0.0057  0.0340  117 ASN   A CB  
2772 C CG  . ASN   A 117 ? 0.1152 0.1202 0.2031 -0.0054 0.0024  0.0331  117 ASN   A CG  
2773 O OD1 . ASN   A 117 ? 0.1199 0.1411 0.2073 -0.0156 0.0110  0.0193  117 ASN   A OD1 
2774 N ND2 . ASN   A 117 ? 0.1117 0.1223 0.2057 0.0011  0.0115  0.0259  117 ASN   A ND2 
2781 N N   . GLN   A 118 ? 0.1119 0.1243 0.2173 -0.0063 -0.0062 0.0303  118 GLN   A N   
2782 C CA  . GLN   A 118 ? 0.1250 0.1378 0.2127 -0.0076 -0.0070 0.0173  118 GLN   A CA  
2783 C C   . GLN   A 118 ? 0.1270 0.1459 0.2120 -0.0115 -0.0085 0.0147  118 GLN   A C   
2784 O O   . GLN   A 118 ? 0.1300 0.1770 0.2285 0.0004  -0.0195 0.0030  118 GLN   A O   
2785 C CB  . GLN   A 118 ? 0.1236 0.1413 0.2060 -0.0033 0.0036  0.0244  118 GLN   A CB  
2786 C CG  . GLN   A 118 ? 0.1180 0.1437 0.2123 -0.0012 0.0084  0.0153  118 GLN   A CG  
2787 C CD  . GLN   A 118 ? 0.1132 0.1410 0.2156 -0.0013 0.0039  0.0101  118 GLN   A CD  
2788 O OE1 . GLN   A 118 ? 0.1234 0.1494 0.2407 0.0067  -0.0158 0.0051  118 GLN   A OE1 
2789 N NE2 . GLN   A 118 ? 0.1258 0.1421 0.2089 0.0031  -0.0012 0.0125  118 GLN   A NE2 
2798 N N   . HIS   A 119 ? 0.1311 0.1435 0.2005 -0.0099 -0.0032 0.0231  119 HIS   A N   
2799 C CA  . HIS   A 119 ? 0.1445 0.1559 0.2018 -0.0081 -0.0043 0.0238  119 HIS   A CA  
2800 C C   . HIS   A 119 ? 0.1608 0.1664 0.1913 -0.0097 0.0039  0.0236  119 HIS   A C   
2801 O O   . HIS   A 119 ? 0.1526 0.1663 0.2119 -0.0260 -0.0040 0.0220  119 HIS   A O   
2802 C CB  . HIS   A 119 ? 0.1518 0.1501 0.2117 -0.0041 0.0108  0.0260  119 HIS   A CB  
2803 C CG  . HIS   A 119 ? 0.1558 0.1475 0.2383 0.0015  0.0079  0.0306  119 HIS   A CG  
2804 N ND1 . HIS   A 119 ? 0.1648 0.1631 0.2765 -0.0085 0.0103  0.0155  119 HIS   A ND1 
2805 C CD2 . HIS   A 119 ? 0.1625 0.1503 0.2618 0.0106  0.0245  0.0464  119 HIS   A CD2 
2806 C CE1 . HIS   A 119 ? 0.1584 0.1641 0.2984 -0.0168 0.0199  0.0308  119 HIS   A CE1 
2807 N NE2 . HIS   A 119 ? 0.1695 0.1616 0.2926 0.0048  0.0414  0.0492  119 HIS   A NE2 
2815 N N   A GLU   A 120 ? 0.1751 0.1906 0.1932 -0.0091 0.0028  0.0250  120 GLU   A N   
2816 N N   B GLU   A 120 ? 0.1651 0.1801 0.1827 -0.0056 -0.0055 0.0337  120 GLU   A N   
2817 C CA  A GLU   A 120 ? 0.1972 0.2159 0.2171 -0.0064 0.0101  0.0386  120 GLU   A CA  
2818 C CA  B GLU   A 120 ? 0.1864 0.1993 0.2024 0.0026  -0.0007 0.0621  120 GLU   A CA  
2819 C C   A GLU   A 120 ? 0.1800 0.2040 0.1963 -0.0143 0.0097  0.0399  120 GLU   A C   
2820 C C   B GLU   A 120 ? 0.1713 0.1850 0.1978 -0.0129 0.0015  0.0595  120 GLU   A C   
2821 O O   A GLU   A 120 ? 0.1776 0.2065 0.1891 -0.0138 0.0117  0.0365  120 GLU   A O   
2822 O O   B GLU   A 120 ? 0.1665 0.1687 0.2034 -0.0132 -0.0033 0.0806  120 GLU   A O   
2823 C CB  A GLU   A 120 ? 0.2438 0.2591 0.2815 0.0062  0.0164  0.0538  120 GLU   A CB  
2824 C CB  B GLU   A 120 ? 0.2355 0.2462 0.2541 0.0266  0.0034  0.0948  120 GLU   A CB  
2825 C CG  A GLU   A 120 ? 0.2963 0.3024 0.3626 0.0165  0.0215  0.0543  120 GLU   A CG  
2826 C CG  B GLU   A 120 ? 0.2954 0.2957 0.3489 0.0422  0.0126  0.0942  120 GLU   A CG  
2827 C CD  A GLU   A 120 ? 0.3338 0.3335 0.4379 0.0249  0.0294  0.0501  120 GLU   A CD  
2828 C CD  B GLU   A 120 ? 0.3440 0.3329 0.4420 0.0534  0.0262  0.0846  120 GLU   A CD  
2829 O OE1 A GLU   A 120 ? 0.3457 0.3486 0.4638 0.0268  0.0317  0.0482  120 GLU   A OE1 
2830 O OE1 B GLU   A 120 ? 0.3590 0.3506 0.4769 0.0537  0.0279  0.0797  120 GLU   A OE1 
2831 O OE2 A GLU   A 120 ? 0.3507 0.3442 0.4704 0.0268  0.0315  0.0480  120 GLU   A OE2 
2832 O OE2 B GLU   A 120 ? 0.3661 0.3462 0.4824 0.0555  0.0315  0.0800  120 GLU   A OE2 
2845 N N   . VAL   A 121 ? 0.1699 0.1932 0.1989 -0.0179 0.0098  0.0516  121 VAL   A N   
2846 C CA  . VAL   A 121 ? 0.1742 0.2011 0.1942 -0.0117 0.0217  0.0484  121 VAL   A CA  
2847 C C   . VAL   A 121 ? 0.1583 0.1799 0.1746 -0.0195 0.0150  0.0306  121 VAL   A C   
2848 O O   . VAL   A 121 ? 0.1634 0.1888 0.2010 -0.0328 -0.0005 0.0225  121 VAL   A O   
2849 C CB  . VAL   A 121 ? 0.2106 0.2420 0.2164 0.0025  0.0341  0.0479  121 VAL   A CB  
2850 C CG1 . VAL   A 121 ? 0.2176 0.2529 0.2104 0.0116  0.0352  0.0569  121 VAL   A CG1 
2851 C CG2 . VAL   A 121 ? 0.2309 0.2620 0.2498 -0.0036 0.0305  0.0317  121 VAL   A CG2 
2862 N N   . LEU   A 122 ? 0.1552 0.1612 0.1889 -0.0215 0.0175  0.0321  122 LEU   A N   
2863 C CA  . LEU   A 122 ? 0.1564 0.1521 0.1886 -0.0240 0.0293  0.0286  122 LEU   A CA  
2864 C C   . LEU   A 122 ? 0.1486 0.1490 0.1854 -0.0211 0.0191  0.0189  122 LEU   A C   
2865 O O   . LEU   A 122 ? 0.1480 0.1560 0.2105 -0.0272 0.0108  0.0256  122 LEU   A O   
2866 C CB  . LEU   A 122 ? 0.1746 0.1608 0.2219 -0.0163 0.0171  0.0307  122 LEU   A CB  
2867 C CG  . LEU   A 122 ? 0.1803 0.1611 0.2128 -0.0138 0.0263  0.0230  122 LEU   A CG  
2868 C CD1 . LEU   A 122 ? 0.1988 0.1623 0.2205 -0.0205 0.0284  0.0266  122 LEU   A CD1 
2869 C CD2 . LEU   A 122 ? 0.1757 0.1535 0.2055 -0.0200 0.0296  0.0219  122 LEU   A CD2 
2881 N N   A LEU   A 123 ? 0.1460 0.1455 0.1832 -0.0179 0.0160  0.0261  123 LEU   A N   
2882 N N   B LEU   A 123 ? 0.1412 0.1483 0.1777 -0.0236 0.0130  0.0200  123 LEU   A N   
2883 C CA  A LEU   A 123 ? 0.1481 0.1406 0.1752 -0.0136 0.0192  0.0299  123 LEU   A CA  
2884 C CA  B LEU   A 123 ? 0.1420 0.1459 0.1644 -0.0243 0.0167  0.0122  123 LEU   A CA  
2885 C C   A LEU   A 123 ? 0.1377 0.1250 0.1834 -0.0127 0.0188  0.0277  123 LEU   A C   
2886 C C   B LEU   A 123 ? 0.1388 0.1424 0.1577 -0.0273 0.0198  0.0046  123 LEU   A C   
2887 O O   A LEU   A 123 ? 0.1416 0.1232 0.1887 -0.0180 0.0198  0.0234  123 LEU   A O   
2888 O O   B LEU   A 123 ? 0.1381 0.1486 0.1679 -0.0333 0.0134  0.0006  123 LEU   A O   
2889 C CB  A LEU   A 123 ? 0.1629 0.1523 0.1785 -0.0168 0.0317  0.0251  123 LEU   A CB  
2890 C CB  B LEU   A 123 ? 0.1490 0.1508 0.1647 -0.0260 0.0245  0.0087  123 LEU   A CB  
2891 C CG  A LEU   A 123 ? 0.1703 0.1619 0.1741 -0.0155 0.0254  0.0146  123 LEU   A CG  
2892 C CG  B LEU   A 123 ? 0.1549 0.1618 0.1608 -0.0207 0.0180  0.0066  123 LEU   A CG  
2893 C CD1 A LEU   A 123 ? 0.1759 0.1628 0.1722 -0.0101 0.0174  0.0106  123 LEU   A CD1 
2894 C CD1 B LEU   A 123 ? 0.1638 0.1667 0.1687 -0.0121 0.0096  -0.0019 123 LEU   A CD1 
2895 C CD2 A LEU   A 123 ? 0.1752 0.1726 0.1706 -0.0178 0.0188  0.0043  123 LEU   A CD2 
2896 C CD2 B LEU   A 123 ? 0.1650 0.1748 0.1695 -0.0216 0.0140  -0.0083 123 LEU   A CD2 
2919 N N   A ALA   A 124 ? 0.1219 0.1190 0.1888 -0.0108 0.0211  0.0273  124 ALA   A N   
2920 N N   B ALA   A 124 ? 0.1397 0.1386 0.1635 -0.0248 0.0177  0.0061  124 ALA   A N   
2921 C CA  A ALA   A 124 ? 0.1037 0.1148 0.1947 -0.0084 0.0120  0.0281  124 ALA   A CA  
2922 C CA  B ALA   A 124 ? 0.1360 0.1395 0.1810 -0.0260 0.0072  0.0135  124 ALA   A CA  
2923 C C   A ALA   A 124 ? 0.1048 0.1173 0.1980 -0.0190 0.0087  0.0262  124 ALA   A C   
2924 C C   B ALA   A 124 ? 0.1294 0.1241 0.1904 -0.0187 0.0106  0.0168  124 ALA   A C   
2925 O O   A ALA   A 124 ? 0.1017 0.1257 0.2138 -0.0251 0.0180  0.0345  124 ALA   A O   
2926 O O   B ALA   A 124 ? 0.1353 0.1387 0.1955 -0.0080 0.0143  0.0225  124 ALA   A O   
2927 C CB  A ALA   A 124 ? 0.1016 0.1089 0.1896 0.0012  0.0061  0.0265  124 ALA   A CB  
2928 C CB  B ALA   A 124 ? 0.1503 0.1421 0.1823 -0.0324 -0.0044 0.0145  124 ALA   A CB  
2939 N N   A PRO   A 125 ? 0.1157 0.1260 0.1974 -0.0106 0.0061  0.0250  125 PRO   A N   
2940 N N   B PRO   A 125 ? 0.1185 0.1152 0.1944 -0.0088 0.0126  0.0232  125 PRO   A N   
2941 C CA  A PRO   A 125 ? 0.1233 0.1342 0.1898 -0.0067 -0.0057 0.0230  125 PRO   A CA  
2942 C CA  B PRO   A 125 ? 0.1214 0.1165 0.1968 -0.0066 0.0104  0.0266  125 PRO   A CA  
2943 C C   A PRO   A 125 ? 0.1204 0.1396 0.1897 -0.0096 -0.0065 0.0189  125 PRO   A C   
2944 C C   B PRO   A 125 ? 0.1204 0.1272 0.1989 -0.0082 0.0038  0.0208  125 PRO   A C   
2945 O O   A PRO   A 125 ? 0.1252 0.1334 0.2016 -0.0072 -0.0066 0.0219  125 PRO   A O   
2946 O O   B PRO   A 125 ? 0.1279 0.1250 0.2109 0.0028  -0.0010 0.0164  125 PRO   A O   
2947 C CB  A PRO   A 125 ? 0.1312 0.1354 0.1884 -0.0069 -0.0072 0.0176  125 PRO   A CB  
2948 C CB  B PRO   A 125 ? 0.1199 0.1102 0.2076 -0.0136 0.0148  0.0217  125 PRO   A CB  
2949 C CG  A PRO   A 125 ? 0.1362 0.1312 0.2031 -0.0060 -0.0062 0.0237  125 PRO   A CG  
2950 C CG  B PRO   A 125 ? 0.1145 0.1063 0.2154 -0.0134 0.0133  0.0225  125 PRO   A CG  
2951 C CD  A PRO   A 125 ? 0.1251 0.1274 0.1985 -0.0079 0.0026  0.0204  125 PRO   A CD  
2952 C CD  B PRO   A 125 ? 0.1116 0.0996 0.2034 -0.0141 0.0201  0.0163  125 PRO   A CD  
2967 N N   A LEU   A 126 ? 0.1193 0.1442 0.1932 -0.0039 -0.0033 0.0135  126 LEU   A N   
2968 N N   B LEU   A 126 ? 0.1192 0.1364 0.2027 -0.0066 0.0021  0.0243  126 LEU   A N   
2969 C CA  A LEU   A 126 ? 0.1180 0.1370 0.1988 -0.0046 -0.0024 0.0175  126 LEU   A CA  
2970 C CA  B LEU   A 126 ? 0.1182 0.1363 0.2173 -0.0163 0.0037  0.0258  126 LEU   A CA  
2971 C C   A LEU   A 126 ? 0.1189 0.1249 0.1813 0.0005  -0.0147 0.0090  126 LEU   A C   
2972 C C   B LEU   A 126 ? 0.1257 0.1299 0.2246 -0.0045 0.0037  0.0254  126 LEU   A C   
2973 O O   A LEU   A 126 ? 0.1180 0.1158 0.1570 -0.0089 -0.0149 -0.0029 126 LEU   A O   
2974 O O   B LEU   A 126 ? 0.1476 0.1295 0.2566 0.0037  0.0281  0.0178  126 LEU   A O   
2975 C CB  A LEU   A 126 ? 0.1216 0.1405 0.2180 -0.0079 -0.0017 0.0172  126 LEU   A CB  
2976 C CB  B LEU   A 126 ? 0.1236 0.1433 0.2323 -0.0292 -0.0093 0.0171  126 LEU   A CB  
2977 C CG  A LEU   A 126 ? 0.1186 0.1482 0.2325 -0.0053 0.0168  0.0208  126 LEU   A CG  
2978 C CG  B LEU   A 126 ? 0.1258 0.1551 0.2423 -0.0267 -0.0008 0.0090  126 LEU   A CG  
2979 C CD1 A LEU   A 126 ? 0.1217 0.1559 0.2411 -0.0047 0.0224  0.0284  126 LEU   A CD1 
2980 C CD1 B LEU   A 126 ? 0.1370 0.1688 0.2653 -0.0274 -0.0107 0.0031  126 LEU   A CD1 
2981 C CD2 A LEU   A 126 ? 0.1215 0.1400 0.2154 -0.0099 0.0346  0.0205  126 LEU   A CD2 
2982 C CD2 B LEU   A 126 ? 0.1351 0.1553 0.2294 -0.0305 0.0087  0.0236  126 LEU   A CD2 
3005 N N   A LEU   A 127 ? 0.1205 0.1260 0.1945 0.0046  -0.0065 0.0068  127 LEU   A N   
3006 N N   B LEU   A 127 ? 0.1183 0.1319 0.2153 -0.0086 0.0005  0.0336  127 LEU   A N   
3007 C CA  A LEU   A 127 ? 0.1269 0.1291 0.1863 0.0054  -0.0040 0.0024  127 LEU   A CA  
3008 C CA  B LEU   A 127 ? 0.1196 0.1416 0.2106 -0.0078 -0.0009 0.0308  127 LEU   A CA  
3009 C C   A LEU   A 127 ? 0.1253 0.1268 0.1730 0.0055  0.0066  -0.0016 127 LEU   A C   
3010 C C   B LEU   A 127 ? 0.1249 0.1308 0.2101 -0.0149 -0.0094 0.0241  127 LEU   A C   
3011 O O   A LEU   A 127 ? 0.1333 0.1347 0.1907 0.0082  0.0013  0.0086  127 LEU   A O   
3012 O O   B LEU   A 127 ? 0.1342 0.1327 0.2231 -0.0275 -0.0146 0.0300  127 LEU   A O   
3013 C CB  A LEU   A 127 ? 0.1379 0.1307 0.1869 0.0078  -0.0046 0.0091  127 LEU   A CB  
3014 C CB  B LEU   A 127 ? 0.1196 0.1636 0.2090 -0.0002 0.0028  0.0175  127 LEU   A CB  
3015 C CG  A LEU   A 127 ? 0.1386 0.1176 0.1806 0.0074  -0.0085 0.0135  127 LEU   A CG  
3016 C CG  B LEU   A 127 ? 0.1232 0.1915 0.1995 0.0011  -0.0033 0.0210  127 LEU   A CG  
3017 C CD1 A LEU   A 127 ? 0.1385 0.1089 0.1816 0.0027  -0.0138 -0.0065 127 LEU   A CD1 
3018 C CD1 B LEU   A 127 ? 0.1224 0.2033 0.2113 0.0022  -0.0003 0.0235  127 LEU   A CD1 
3019 C CD2 A LEU   A 127 ? 0.1441 0.1115 0.1765 0.0121  -0.0011 0.0157  127 LEU   A CD2 
3020 C CD2 B LEU   A 127 ? 0.1415 0.2050 0.2008 -0.0008 -0.0119 0.0101  127 LEU   A CD2 
3043 N N   A SER   A 128 ? 0.1279 0.1255 0.1637 -0.0003 0.0107  -0.0028 128 SER   A N   
3044 N N   B SER   A 128 ? 0.1410 0.1327 0.2084 -0.0170 -0.0105 0.0207  128 SER   A N   
3045 C CA  A SER   A 128 ? 0.1280 0.1340 0.1478 -0.0012 0.0020  -0.0023 128 SER   A CA  
3046 C CA  B SER   A 128 ? 0.1546 0.1518 0.1962 -0.0004 -0.0139 0.0257  128 SER   A CA  
3047 C C   A SER   A 128 ? 0.1333 0.1378 0.1469 -0.0050 -0.0008 0.0120  128 SER   A C   
3048 C C   B SER   A 128 ? 0.1747 0.1698 0.2048 0.0139  -0.0125 0.0356  128 SER   A C   
3049 O O   A SER   A 128 ? 0.1469 0.1482 0.1448 -0.0018 -0.0114 0.0064  128 SER   A O   
3050 O O   B SER   A 128 ? 0.1859 0.1758 0.2214 0.0253  -0.0138 0.0212  128 SER   A O   
3051 C CB  A SER   A 128 ? 0.1275 0.1352 0.1463 -0.0084 -0.0063 -0.0033 128 SER   A CB  
3052 C CB  B SER   A 128 ? 0.1520 0.1587 0.1796 -0.0054 -0.0209 0.0264  128 SER   A CB  
3053 O OG  A SER   A 128 ? 0.1201 0.1303 0.1539 -0.0048 -0.0134 -0.0159 128 SER   A OG  
3054 O OG  B SER   A 128 ? 0.1479 0.1570 0.1855 -0.0059 -0.0175 0.0157  128 SER   A OG  
3065 N N   A ALA   A 129 ? 0.1256 0.1425 0.1627 -0.0001 0.0002  0.0186  129 ALA   A N   
3066 N N   B ALA   A 129 ? 0.1845 0.1898 0.2112 0.0218  -0.0144 0.0431  129 ALA   A N   
3067 C CA  A ALA   A 129 ? 0.1192 0.1387 0.1574 0.0002  0.0012  0.0270  129 ALA   A CA  
3068 C CA  B ALA   A 129 ? 0.1965 0.2033 0.2261 0.0231  -0.0138 0.0325  129 ALA   A CA  
3069 C C   A ALA   A 129 ? 0.1241 0.1363 0.1483 -0.0006 0.0091  0.0032  129 ALA   A C   
3070 C C   B ALA   A 129 ? 0.2058 0.2051 0.2321 0.0202  -0.0242 0.0175  129 ALA   A C   
3071 O O   A ALA   A 129 ? 0.1343 0.1469 0.1548 -0.0191 0.0119  -0.0085 129 ALA   A O   
3072 O O   B ALA   A 129 ? 0.2094 0.2082 0.2230 0.0095  -0.0148 0.0056  129 ALA   A O   
3073 C CB  A ALA   A 129 ? 0.1223 0.1486 0.1772 0.0144  -0.0071 0.0475  129 ALA   A CB  
3074 C CB  B ALA   A 129 ? 0.2063 0.2236 0.2415 0.0258  -0.0003 0.0328  129 ALA   A CB  
3085 N N   A GLY   A 130 ? 0.1369 0.1306 0.1744 0.0029  0.0259  -0.0050 130 GLY   A N   
3086 N N   B GLY   A 130 ? 0.2213 0.2093 0.2546 0.0182  -0.0259 0.0099  130 GLY   A N   
3087 C CA  A GLY   A 130 ? 0.1623 0.1258 0.1884 0.0066  0.0349  0.0032  130 GLY   A CA  
3088 C CA  B GLY   A 130 ? 0.2427 0.2167 0.2789 0.0174  -0.0219 0.0082  130 GLY   A CA  
3089 C C   A GLY   A 130 ? 0.1713 0.1170 0.1703 0.0097  0.0353  0.0060  130 GLY   A C   
3090 C C   B GLY   A 130 ? 0.2513 0.2158 0.2948 0.0137  -0.0396 0.0064  130 GLY   A C   
3091 O O   A GLY   A 130 ? 0.1639 0.1010 0.1637 0.0051  0.0311  -0.0032 130 GLY   A O   
3092 O O   B GLY   A 130 ? 0.2541 0.2098 0.3005 0.0118  -0.0453 0.0090  130 GLY   A O   
3099 N N   A ILE   A 131 ? 0.1863 0.1205 0.1537 0.0045  0.0285  0.0080  131 ILE   A N   
3100 N N   B ILE   A 131 ? 0.2587 0.2206 0.3120 0.0120  -0.0464 0.0044  131 ILE   A N   
3101 C CA  A ILE   A 131 ? 0.1877 0.1185 0.1282 -0.0035 0.0080  0.0085  131 ILE   A CA  
3102 C CA  B ILE   A 131 ? 0.2589 0.2213 0.3162 0.0079  -0.0563 0.0077  131 ILE   A CA  
3103 C C   A ILE   A 131 ? 0.1661 0.1215 0.1123 -0.0111 -0.0021 0.0069  131 ILE   A C   
3104 C C   B ILE   A 131 ? 0.2517 0.2244 0.2760 0.0139  -0.0536 0.0289  131 ILE   A C   
3105 O O   A ILE   A 131 ? 0.1695 0.1353 0.1243 -0.0060 -0.0136 -0.0048 131 ILE   A O   
3106 O O   B ILE   A 131 ? 0.2522 0.2361 0.2601 0.0163  -0.0548 0.0422  131 ILE   A O   
3107 C CB  A ILE   A 131 ? 0.2104 0.1249 0.1319 -0.0051 0.0074  -0.0032 131 ILE   A CB  
3108 C CB  B ILE   A 131 ? 0.2723 0.2287 0.3651 -0.0018 -0.0627 -0.0056 131 ILE   A CB  
3109 C CG1 A ILE   A 131 ? 0.2273 0.1478 0.1440 -0.0092 0.0007  0.0007  131 ILE   A CG1 
3110 C CG1 B ILE   A 131 ? 0.2864 0.2401 0.3938 -0.0113 -0.0595 -0.0132 131 ILE   A CG1 
3111 C CG2 A ILE   A 131 ? 0.2167 0.1134 0.1471 -0.0063 0.0146  -0.0145 131 ILE   A CG2 
3112 C CG2 B ILE   A 131 ? 0.2776 0.2281 0.3830 -0.0022 -0.0636 -0.0075 131 ILE   A CG2 
3113 C CD1 A ILE   A 131 ? 0.2332 0.1600 0.1604 -0.0129 -0.0030 -0.0015 131 ILE   A CD1 
3114 C CD1 B ILE   A 131 ? 0.2948 0.2456 0.4088 -0.0136 -0.0578 -0.0188 131 ILE   A CD1 
3137 N N   A PHE   A 132 ? 0.1506 0.1173 0.1095 -0.0057 0.0022  0.0152  132 PHE   A N   
3138 N N   B PHE   A 132 ? 0.2434 0.2201 0.2587 0.0197  -0.0528 0.0372  132 PHE   A N   
3139 C CA  A PHE   A 132 ? 0.1426 0.1273 0.1220 -0.0050 0.0079  -0.0067 132 PHE   A CA  
3140 C CA  B PHE   A 132 ? 0.2452 0.2283 0.2550 0.0188  -0.0494 0.0334  132 PHE   A CA  
3141 C C   A PHE   A 132 ? 0.1462 0.1376 0.1240 0.0065  0.0084  -0.0066 132 PHE   A C   
3142 C C   B PHE   A 132 ? 0.2433 0.2322 0.2483 0.0209  -0.0424 0.0340  132 PHE   A C   
3143 O O   A PHE   A 132 ? 0.1559 0.1483 0.1341 0.0091  0.0120  -0.0190 132 PHE   A O   
3144 O O   B PHE   A 132 ? 0.2529 0.2360 0.2667 0.0216  -0.0381 0.0332  132 PHE   A O   
3145 C CB  A PHE   A 132 ? 0.1363 0.1169 0.1223 -0.0076 0.0002  0.0008  132 PHE   A CB  
3146 C CB  B PHE   A 132 ? 0.2465 0.2313 0.2661 0.0183  -0.0573 0.0355  132 PHE   A CB  
3147 C CG  A PHE   A 132 ? 0.1321 0.1121 0.1077 0.0047  -0.0051 0.0080  132 PHE   A CG  
3148 C CG  B PHE   A 132 ? 0.2575 0.2423 0.2926 0.0188  -0.0625 0.0210  132 PHE   A CG  
3149 C CD1 A PHE   A 132 ? 0.1341 0.1248 0.1086 0.0112  0.0048  -0.0060 132 PHE   A CD1 
3150 C CD1 B PHE   A 132 ? 0.2673 0.2547 0.3182 0.0171  -0.0625 0.0071  132 PHE   A CD1 
3151 C CD2 A PHE   A 132 ? 0.1322 0.1230 0.1066 -0.0001 -0.0123 -0.0017 132 PHE   A CD2 
3152 C CD2 B PHE   A 132 ? 0.2609 0.2491 0.3083 0.0191  -0.0616 0.0131  132 PHE   A CD2 
3153 C CE1 A PHE   A 132 ? 0.1343 0.1316 0.0988 0.0174  -0.0021 -0.0142 132 PHE   A CE1 
3154 C CE1 B PHE   A 132 ? 0.2696 0.2594 0.3336 0.0159  -0.0653 0.0029  132 PHE   A CE1 
3155 C CE2 A PHE   A 132 ? 0.1300 0.1254 0.1082 0.0065  -0.0091 -0.0045 132 PHE   A CE2 
3156 C CE2 B PHE   A 132 ? 0.2665 0.2556 0.3296 0.0156  -0.0624 0.0046  132 PHE   A CE2 
3157 C CZ  A PHE   A 132 ? 0.1263 0.1262 0.0989 0.0179  -0.0114 -0.0028 132 PHE   A CZ  
3158 C CZ  B PHE   A 132 ? 0.2677 0.2601 0.3377 0.0153  -0.0718 0.0030  132 PHE   A CZ  
3177 N N   A GLY   A 133 ? 0.1458 0.1427 0.1226 0.0104  -0.0018 -0.0034 133 GLY   A N   
3178 N N   B GLY   A 133 ? 0.2349 0.2318 0.2392 0.0170  -0.0445 0.0334  133 GLY   A N   
3179 C CA  A GLY   A 133 ? 0.1546 0.1518 0.1438 0.0087  -0.0201 -0.0039 133 GLY   A CA  
3180 C CA  B GLY   A 133 ? 0.2248 0.2331 0.2475 0.0153  -0.0480 0.0215  133 GLY   A CA  
3181 C C   A GLY   A 133 ? 0.1604 0.1697 0.1712 0.0030  -0.0351 -0.0080 133 GLY   A C   
3182 C C   B GLY   A 133 ? 0.2145 0.2359 0.2571 0.0108  -0.0583 0.0136  133 GLY   A C   
3183 O O   A GLY   A 133 ? 0.1686 0.1897 0.2076 -0.0030 -0.0471 -0.0137 133 GLY   A O   
3184 O O   B GLY   A 133 ? 0.2066 0.2525 0.2777 0.0151  -0.0559 0.0099  133 GLY   A O   
3191 N N   A ALA   A 134 ? 0.1554 0.1656 0.1808 0.0021  -0.0221 -0.0120 134 ALA   A N   
3192 N N   B ALA   A 134 ? 0.2078 0.2167 0.2565 0.0047  -0.0584 0.0094  134 ALA   A N   
3193 C CA  A ALA   A 134 ? 0.1542 0.1720 0.2172 0.0024  -0.0167 -0.0193 134 ALA   A CA  
3194 C CA  B ALA   A 134 ? 0.2048 0.2030 0.2680 -0.0014 -0.0646 0.0040  134 ALA   A CA  
3195 C C   A ALA   A 134 ? 0.1595 0.1823 0.2354 -0.0063 -0.0161 -0.0103 134 ALA   A C   
3196 C C   B ALA   A 134 ? 0.2053 0.1934 0.2871 -0.0054 -0.0538 0.0160  134 ALA   A C   
3197 O O   A ALA   A 134 ? 0.1626 0.1846 0.2554 -0.0118 -0.0034 -0.0052 134 ALA   A O   
3198 O O   B ALA   A 134 ? 0.2076 0.1866 0.3135 -0.0100 -0.0404 0.0334  134 ALA   A O   
3199 C CB  A ALA   A 134 ? 0.1553 0.1676 0.2354 0.0059  -0.0075 -0.0199 134 ALA   A CB  
3200 C CB  B ALA   A 134 ? 0.2075 0.1977 0.2693 -0.0046 -0.0675 -0.0022 134 ALA   A CB  
3211 N N   A ASP   A 135 ? 0.1632 0.1889 0.2354 -0.0156 -0.0268 -0.0052 135 ASP   A N   
3212 N N   B ASP   A 135 ? 0.2069 0.1971 0.2906 -0.0138 -0.0520 0.0155  135 ASP   A N   
3213 C CA  A ASP   A 135 ? 0.1594 0.1950 0.2343 -0.0252 -0.0411 0.0034  135 ASP   A CA  
3214 C CA  B ASP   A 135 ? 0.2055 0.1980 0.2912 -0.0192 -0.0576 0.0195  135 ASP   A CA  
3215 C C   A ASP   A 135 ? 0.1509 0.1755 0.2269 -0.0149 -0.0347 0.0232  135 ASP   A C   
3216 C C   B ASP   A 135 ? 0.1862 0.1771 0.2825 -0.0097 -0.0447 0.0263  135 ASP   A C   
3217 O O   A ASP   A 135 ? 0.1439 0.1645 0.2354 -0.0065 -0.0326 0.0258  135 ASP   A O   
3218 O O   B ASP   A 135 ? 0.1820 0.1684 0.2887 -0.0100 -0.0392 0.0188  135 ASP   A O   
3219 C CB  A ASP   A 135 ? 0.1660 0.2210 0.2505 -0.0374 -0.0579 0.0002  135 ASP   A CB  
3220 C CB  B ASP   A 135 ? 0.2250 0.2199 0.3057 -0.0239 -0.0700 0.0160  135 ASP   A CB  
3221 C CG  A ASP   A 135 ? 0.1743 0.2439 0.2760 -0.0481 -0.0602 -0.0050 135 ASP   A CG  
3222 C CG  B ASP   A 135 ? 0.2472 0.2485 0.3340 -0.0225 -0.0739 0.0188  135 ASP   A CG  
3223 O OD1 A ASP   A 135 ? 0.1646 0.2512 0.2906 -0.0510 -0.0654 -0.0195 135 ASP   A OD1 
3224 O OD1 B ASP   A 135 ? 0.2441 0.2545 0.3337 -0.0227 -0.0827 0.0163  135 ASP   A OD1 
3225 O OD2 A ASP   A 135 ? 0.1946 0.2601 0.3016 -0.0467 -0.0540 -0.0002 135 ASP   A OD2 
3226 O OD2 B ASP   A 135 ? 0.2666 0.2641 0.3630 -0.0215 -0.0720 0.0304  135 ASP   A OD2 
3235 N N   A PRO   A 136 ? 0.1521 0.1769 0.2297 -0.0038 -0.0182 0.0234  136 PRO   A N   
3236 N N   B PRO   A 136 ? 0.1730 0.1700 0.2781 0.0045  -0.0367 0.0270  136 PRO   A N   
3237 C CA  A PRO   A 136 ? 0.1474 0.1741 0.2325 -0.0017 -0.0177 0.0226  136 PRO   A CA  
3238 C CA  B PRO   A 136 ? 0.1590 0.1665 0.2738 0.0018  -0.0294 0.0214  136 PRO   A CA  
3239 C C   A PRO   A 136 ? 0.1299 0.1687 0.2378 -0.0024 -0.0147 0.0163  136 PRO   A C   
3240 C C   B PRO   A 136 ? 0.1350 0.1625 0.2644 -0.0015 -0.0190 0.0115  136 PRO   A C   
3241 O O   A PRO   A 136 ? 0.1233 0.1699 0.2443 -0.0054 -0.0116 0.0226  136 PRO   A O   
3242 O O   B PRO   A 136 ? 0.1248 0.1463 0.2550 -0.0017 -0.0057 0.0101  136 PRO   A O   
3243 C CB  A PRO   A 136 ? 0.1636 0.1760 0.2376 -0.0015 -0.0123 0.0207  136 PRO   A CB  
3244 C CB  B PRO   A 136 ? 0.1766 0.1620 0.2808 0.0043  -0.0279 0.0132  136 PRO   A CB  
3245 C CG  A PRO   A 136 ? 0.1703 0.1814 0.2449 0.0001  -0.0076 0.0160  136 PRO   A CG  
3246 C CG  B PRO   A 136 ? 0.1867 0.1684 0.2895 0.0109  -0.0256 0.0101  136 PRO   A CG  
3247 C CD  A PRO   A 136 ? 0.1599 0.1766 0.2362 0.0021  -0.0085 0.0301  136 PRO   A CD  
3248 C CD  B PRO   A 136 ? 0.1735 0.1617 0.2689 0.0147  -0.0256 0.0323  136 PRO   A CD  
3263 N N   A ILE   A 137 ? 0.1284 0.1679 0.2410 0.0023  -0.0259 0.0166  137 ILE   A N   
3264 N N   B ILE   A 137 ? 0.1344 0.1642 0.2644 -0.0050 -0.0284 0.0082  137 ILE   A N   
3265 C CA  A ILE   A 137 ? 0.1249 0.1714 0.2414 -0.0015 -0.0338 0.0122  137 ILE   A CA  
3266 C CA  B ILE   A 137 ? 0.1356 0.1720 0.2696 -0.0035 -0.0285 -0.0060 137 ILE   A CA  
3267 C C   A ILE   A 137 ? 0.1244 0.1596 0.2236 0.0005  -0.0380 0.0085  137 ILE   A C   
3268 C C   B ILE   A 137 ? 0.1374 0.1693 0.2507 -0.0080 -0.0294 0.0063  137 ILE   A C   
3269 O O   A ILE   A 137 ? 0.1306 0.1480 0.2321 -0.0053 -0.0320 -0.0047 137 ILE   A O   
3270 O O   B ILE   A 137 ? 0.1367 0.1694 0.2598 -0.0108 -0.0159 0.0074  137 ILE   A O   
3271 C CB  A ILE   A 137 ? 0.1274 0.1905 0.2541 -0.0004 -0.0464 0.0074  137 ILE   A CB  
3272 C CB  B ILE   A 137 ? 0.1416 0.1855 0.2943 0.0010  -0.0355 -0.0256 137 ILE   A CB  
3273 C CG1 A ILE   A 137 ? 0.1456 0.2051 0.2740 0.0026  -0.0449 -0.0040 137 ILE   A CG1 
3274 C CG1 B ILE   A 137 ? 0.1562 0.2027 0.3318 0.0114  -0.0272 -0.0376 137 ILE   A CG1 
3275 C CG2 A ILE   A 137 ? 0.1243 0.1931 0.2568 -0.0077 -0.0446 0.0009  137 ILE   A CG2 
3276 C CG2 B ILE   A 137 ? 0.1452 0.1872 0.3030 -0.0034 -0.0454 -0.0265 137 ILE   A CG2 
3277 C CD1 A ILE   A 137 ? 0.1601 0.2159 0.2943 0.0119  -0.0362 -0.0117 137 ILE   A CD1 
3278 C CD1 B ILE   A 137 ? 0.1708 0.2160 0.3572 0.0177  -0.0241 -0.0416 137 ILE   A CD1 
3301 N N   A HIS   A 138 ? 0.1297 0.1631 0.2160 0.0084  -0.0305 0.0054  138 HIS   A N   
3302 N N   B HIS   A 138 ? 0.1446 0.1754 0.2403 -0.0064 -0.0127 0.0012  138 HIS   A N   
3303 C CA  A HIS   A 138 ? 0.1370 0.1699 0.2018 0.0077  -0.0247 0.0002  138 HIS   A CA  
3304 C CA  B HIS   A 138 ? 0.1515 0.1691 0.2261 -0.0128 -0.0142 -0.0017 138 HIS   A CA  
3305 C C   A HIS   A 138 ? 0.1300 0.1643 0.1942 0.0049  -0.0180 -0.0008 138 HIS   A C   
3306 C C   B HIS   A 138 ? 0.1407 0.1449 0.2217 -0.0118 -0.0125 0.0035  138 HIS   A C   
3307 O O   A HIS   A 138 ? 0.1405 0.1720 0.1908 0.0024  -0.0168 -0.0021 138 HIS   A O   
3308 O O   B HIS   A 138 ? 0.1466 0.1441 0.2074 -0.0080 -0.0095 -0.0106 138 HIS   A O   
3309 C CB  A HIS   A 138 ? 0.1531 0.1811 0.2109 0.0039  -0.0309 -0.0047 138 HIS   A CB  
3310 C CB  B HIS   A 138 ? 0.1558 0.1836 0.2334 -0.0107 -0.0109 -0.0133 138 HIS   A CB  
3311 C CG  A HIS   A 138 ? 0.1683 0.1893 0.2208 0.0052  -0.0322 -0.0068 138 HIS   A CG  
3312 C CG  B HIS   A 138 ? 0.1682 0.1958 0.2483 -0.0100 -0.0192 -0.0161 138 HIS   A CG  
3313 N ND1 A HIS   A 138 ? 0.1764 0.1966 0.2329 0.0089  -0.0227 -0.0039 138 HIS   A ND1 
3314 N ND1 B HIS   A 138 ? 0.1772 0.2046 0.2716 -0.0046 -0.0227 -0.0118 138 HIS   A ND1 
3315 C CD2 A HIS   A 138 ? 0.1738 0.1972 0.2190 0.0080  -0.0310 -0.0042 138 HIS   A CD2 
3316 C CD2 B HIS   A 138 ? 0.1678 0.2015 0.2475 -0.0040 -0.0172 -0.0163 138 HIS   A CD2 
3317 C CE1 A HIS   A 138 ? 0.1798 0.2036 0.2266 0.0110  -0.0282 0.0008  138 HIS   A CE1 
3318 C CE1 B HIS   A 138 ? 0.1791 0.2088 0.2689 0.0026  -0.0185 -0.0143 138 HIS   A CE1 
3319 N NE2 A HIS   A 138 ? 0.1773 0.2024 0.2181 0.0116  -0.0237 -0.0005 138 HIS   A NE2 
3320 N NE2 B HIS   A 138 ? 0.1741 0.2072 0.2606 0.0026  -0.0059 -0.0125 138 HIS   A NE2 
3335 N N   A SER   A 139 ? 0.1173 0.1501 0.2038 0.0071  -0.0129 0.0004  139 SER   A N   
3336 N N   B SER   A 139 ? 0.1369 0.1295 0.2254 -0.0130 -0.0167 0.0165  139 SER   A N   
3337 C CA  A SER   A 139 ? 0.1078 0.1397 0.1971 0.0005  -0.0104 0.0049  139 SER   A CA  
3338 C CA  B SER   A 139 ? 0.1307 0.1291 0.2215 -0.0111 -0.0088 0.0140  139 SER   A CA  
3339 C C   A SER   A 139 ? 0.1059 0.1370 0.2079 -0.0067 -0.0069 0.0065  139 SER   A C   
3340 C C   B SER   A 139 ? 0.1256 0.1260 0.2288 -0.0128 -0.0034 0.0113  139 SER   A C   
3341 O O   A SER   A 139 ? 0.1036 0.1384 0.2177 -0.0089 0.0009  0.0053  139 SER   A O   
3342 O O   B SER   A 139 ? 0.1263 0.1145 0.2389 -0.0088 -0.0094 0.0205  139 SER   A O   
3343 C CB  A SER   A 139 ? 0.0991 0.1362 0.1870 -0.0001 -0.0049 -0.0005 139 SER   A CB  
3344 C CB  B SER   A 139 ? 0.1250 0.1300 0.2099 -0.0054 -0.0040 0.0137  139 SER   A CB  
3345 O OG  A SER   A 139 ? 0.0982 0.1317 0.1740 -0.0012 0.0026  -0.0014 139 SER   A OG  
3346 O OG  B SER   A 139 ? 0.1289 0.1329 0.2036 -0.0032 0.0066  0.0218  139 SER   A OG  
3357 N N   A LEU   A 140 ? 0.1082 0.1387 0.2235 -0.0017 -0.0165 0.0161  140 LEU   A N   
3358 N N   B LEU   A 140 ? 0.1218 0.1357 0.2396 -0.0139 -0.0009 0.0242  140 LEU   A N   
3359 C CA  A LEU   A 140 ? 0.1091 0.1337 0.2288 -0.0002 -0.0152 0.0219  140 LEU   A CA  
3360 C CA  B LEU   A 140 ? 0.1166 0.1341 0.2528 -0.0166 0.0050  0.0258  140 LEU   A CA  
3361 C C   A LEU   A 140 ? 0.1049 0.1336 0.2237 -0.0022 -0.0192 0.0247  140 LEU   A C   
3362 C C   B LEU   A 140 ? 0.1125 0.1388 0.2509 -0.0207 0.0009  0.0264  140 LEU   A C   
3363 O O   A LEU   A 140 ? 0.1081 0.1322 0.2245 0.0035  -0.0192 0.0270  140 LEU   A O   
3364 O O   B LEU   A 140 ? 0.1246 0.1415 0.2542 -0.0200 -0.0006 0.0337  140 LEU   A O   
3365 C CB  A LEU   A 140 ? 0.1175 0.1389 0.2439 0.0028  -0.0140 0.0248  140 LEU   A CB  
3366 C CB  B LEU   A 140 ? 0.1148 0.1500 0.2740 -0.0098 0.0084  0.0245  140 LEU   A CB  
3367 C CG  A LEU   A 140 ? 0.1231 0.1478 0.2476 -0.0109 -0.0077 0.0350  140 LEU   A CG  
3368 C CG  B LEU   A 140 ? 0.1178 0.1686 0.2763 -0.0225 0.0137  0.0228  140 LEU   A CG  
3369 C CD1 A LEU   A 140 ? 0.1262 0.1488 0.2466 -0.0069 -0.0119 0.0463  140 LEU   A CD1 
3370 C CD1 B LEU   A 140 ? 0.1176 0.1761 0.2694 -0.0144 0.0150  0.0266  140 LEU   A CD1 
3371 C CD2 A LEU   A 140 ? 0.1269 0.1525 0.2497 -0.0119 0.0016  0.0450  140 LEU   A CD2 
3372 C CD2 B LEU   A 140 ? 0.1220 0.1782 0.2859 -0.0238 0.0213  0.0285  140 LEU   A CD2 
3395 N N   A ARG   A 141 ? 0.1127 0.1329 0.2306 -0.0034 -0.0258 0.0239  141 ARG   A N   
3396 N N   B ARG   A 141 ? 0.1219 0.1495 0.2592 -0.0191 -0.0051 0.0229  141 ARG   A N   
3397 C CA  A ARG   A 141 ? 0.1256 0.1390 0.2392 -0.0164 -0.0294 0.0135  141 ARG   A CA  
3398 C CA  B ARG   A 141 ? 0.1346 0.1703 0.2665 -0.0249 -0.0193 0.0069  141 ARG   A CA  
3399 C C   A ARG   A 141 ? 0.1252 0.1319 0.2315 -0.0078 -0.0239 0.0177  141 ARG   A C   
3400 C C   B ARG   A 141 ? 0.1312 0.1545 0.2506 -0.0218 -0.0138 0.0150  141 ARG   A C   
3401 O O   A ARG   A 141 ? 0.1200 0.1244 0.2432 -0.0040 -0.0103 0.0135  141 ARG   A O   
3402 O O   B ARG   A 141 ? 0.1243 0.1505 0.2543 -0.0223 0.0040  0.0011  141 ARG   A O   
3403 C CB  A ARG   A 141 ? 0.1406 0.1531 0.2530 -0.0341 -0.0280 -0.0089 141 ARG   A CB  
3404 C CB  B ARG   A 141 ? 0.1586 0.2019 0.2886 -0.0253 -0.0383 -0.0131 141 ARG   A CB  
3405 C CG  A ARG   A 141 ? 0.1559 0.1771 0.2602 -0.0514 -0.0106 -0.0084 141 ARG   A CG  
3406 C CG  B ARG   A 141 ? 0.1855 0.2382 0.3141 -0.0289 -0.0459 -0.0117 141 ARG   A CG  
3407 C CD  A ARG   A 141 ? 0.1800 0.2023 0.2687 -0.0566 0.0053  -0.0096 141 ARG   A CD  
3408 C CD  B ARG   A 141 ? 0.2017 0.2682 0.3276 -0.0330 -0.0359 0.0040  141 ARG   A CD  
3409 N NE  A ARG   A 141 ? 0.1843 0.2251 0.2812 -0.0561 0.0001  -0.0156 141 ARG   A NE  
3410 N NE  B ARG   A 141 ? 0.1948 0.2866 0.3278 -0.0375 -0.0391 0.0192  141 ARG   A NE  
3411 C CZ  A ARG   A 141 ? 0.1915 0.2418 0.2906 -0.0606 -0.0046 -0.0125 141 ARG   A CZ  
3412 C CZ  B ARG   A 141 ? 0.1976 0.3051 0.3334 -0.0352 -0.0374 0.0243  141 ARG   A CZ  
3413 N NH1 A ARG   A 141 ? 0.1898 0.2491 0.2909 -0.0678 0.0041  -0.0176 141 ARG   A NH1 
3414 N NH1 B ARG   A 141 ? 0.1970 0.3132 0.3436 -0.0353 -0.0377 0.0289  141 ARG   A NH1 
3415 N NH2 A ARG   A 141 ? 0.1919 0.2516 0.3051 -0.0574 -0.0143 -0.0140 141 ARG   A NH2 
3416 N NH2 B ARG   A 141 ? 0.1931 0.3108 0.3300 -0.0283 -0.0441 0.0215  141 ARG   A NH2 
3443 N N   A VAL   A 142 ? 0.1238 0.1362 0.2148 -0.0066 -0.0176 0.0185  142 VAL   A N   
3444 N N   B VAL   A 142 ? 0.1245 0.1433 0.2324 -0.0189 -0.0106 0.0230  142 VAL   A N   
3445 C CA  A VAL   A 142 ? 0.1262 0.1434 0.2098 -0.0073 -0.0041 0.0105  142 VAL   A CA  
3446 C CA  B VAL   A 142 ? 0.1256 0.1429 0.2246 -0.0167 -0.0023 0.0160  142 VAL   A CA  
3447 C C   A VAL   A 142 ? 0.1192 0.1379 0.2086 -0.0112 -0.0028 0.0155  142 VAL   A C   
3448 C C   B VAL   A 142 ? 0.1138 0.1357 0.2188 -0.0160 -0.0005 0.0188  142 VAL   A C   
3449 O O   A VAL   A 142 ? 0.1262 0.1367 0.2119 -0.0024 -0.0051 0.0166  142 VAL   A O   
3450 O O   B VAL   A 142 ? 0.1206 0.1323 0.2308 -0.0032 -0.0068 0.0181  142 VAL   A O   
3451 C CB  A VAL   A 142 ? 0.1351 0.1554 0.2047 -0.0040 -0.0021 0.0110  142 VAL   A CB  
3452 C CB  B VAL   A 142 ? 0.1351 0.1538 0.2168 -0.0154 -0.0063 0.0256  142 VAL   A CB  
3453 C CG1 A VAL   A 142 ? 0.1363 0.1519 0.2018 -0.0055 -0.0004 0.0086  142 VAL   A CG1 
3454 C CG1 B VAL   A 142 ? 0.1327 0.1459 0.2134 -0.0220 -0.0093 0.0217  142 VAL   A CG1 
3455 C CG2 A VAL   A 142 ? 0.1406 0.1671 0.2120 0.0035  0.0000  0.0073  142 VAL   A CG2 
3456 C CG2 B VAL   A 142 ? 0.1467 0.1662 0.2213 -0.0039 -0.0079 0.0307  142 VAL   A CG2 
3475 N N   . CYS   A 143 ? 0.1171 0.1337 0.2225 -0.0125 -0.0131 0.0212  143 CYS   A N   
3476 C CA  . CYS   A 143 ? 0.1087 0.1291 0.2342 -0.0133 0.0017  0.0157  143 CYS   A CA  
3477 C C   . CYS   A 143 ? 0.1173 0.1269 0.2273 -0.0095 -0.0002 0.0211  143 CYS   A C   
3478 O O   . CYS   A 143 ? 0.1187 0.1301 0.2328 -0.0079 -0.0057 0.0312  143 CYS   A O   
3479 C CB  . CYS   A 143 ? 0.1218 0.1340 0.2422 -0.0099 0.0066  0.0190  143 CYS   A CB  
3480 S SG  . CYS   A 143 ? 0.1423 0.1419 0.2273 0.0014  0.0077  0.0133  143 CYS   A SG  
3487 N N   . VAL   A 144 ? 0.1205 0.1315 0.2392 -0.0143 0.0076  0.0280  144 VAL   A N   
3488 C CA  . VAL   A 144 ? 0.1269 0.1375 0.2644 -0.0149 0.0154  0.0268  144 VAL   A CA  
3489 C C   . VAL   A 144 ? 0.1268 0.1314 0.2528 -0.0182 -0.0061 0.0197  144 VAL   A C   
3490 O O   . VAL   A 144 ? 0.1421 0.1361 0.2520 -0.0082 -0.0057 0.0311  144 VAL   A O   
3491 C CB  . VAL   A 144 ? 0.1370 0.1573 0.3114 -0.0086 0.0292  0.0273  144 VAL   A CB  
3492 C CG1 . VAL   A 144 ? 0.1528 0.1731 0.3332 -0.0184 0.0119  0.0220  144 VAL   A CG1 
3493 C CG2 . VAL   A 144 ? 0.1309 0.1619 0.3237 -0.0071 0.0373  0.0368  144 VAL   A CG2 
3503 N N   . ASP   A 145 ? 0.1237 0.1290 0.2456 -0.0151 -0.0096 0.0161  145 ASP   A N   
3504 C CA  . ASP   A 145 ? 0.1354 0.1381 0.2622 -0.0211 -0.0056 0.0063  145 ASP   A CA  
3505 C C   . ASP   A 145 ? 0.1370 0.1340 0.2508 -0.0165 -0.0042 -0.0007 145 ASP   A C   
3506 O O   . ASP   A 145 ? 0.1465 0.1481 0.2999 -0.0167 -0.0047 -0.0312 145 ASP   A O   
3507 C CB  . ASP   A 145 ? 0.1490 0.1621 0.2750 -0.0197 -0.0118 -0.0026 145 ASP   A CB  
3508 C CG  . ASP   A 145 ? 0.1581 0.1874 0.3017 -0.0353 -0.0236 0.0025  145 ASP   A CG  
3509 O OD1 . ASP   A 145 ? 0.1586 0.1918 0.3150 -0.0487 -0.0138 0.0052  145 ASP   A OD1 
3510 O OD2 . ASP   A 145 ? 0.1852 0.2101 0.3205 -0.0448 -0.0426 -0.0033 145 ASP   A OD2 
3515 N N   . THR   A 146 ? 0.1241 0.1237 0.2180 -0.0161 -0.0002 0.0079  146 THR   A N   
3516 C CA  . THR   A 146 ? 0.1222 0.1251 0.2029 -0.0093 0.0018  0.0119  146 THR   A CA  
3517 C C   . THR   A 146 ? 0.1186 0.1207 0.2088 -0.0007 0.0021  0.0181  146 THR   A C   
3518 O O   . THR   A 146 ? 0.1297 0.1277 0.2338 0.0019  -0.0021 0.0117  146 THR   A O   
3519 C CB  . THR   A 146 ? 0.1183 0.1259 0.2001 -0.0044 0.0018  0.0062  146 THR   A CB  
3520 O OG1 . THR   A 146 ? 0.1199 0.1429 0.2119 0.0017  -0.0048 0.0041  146 THR   A OG1 
3521 C CG2 . THR   A 146 ? 0.1225 0.1262 0.2117 -0.0084 0.0011  0.0115  146 THR   A CG2 
3529 N N   . VAL   A 147 ? 0.1156 0.1221 0.2208 -0.0045 0.0044  0.0155  147 VAL   A N   
3530 C CA  . VAL   A 147 ? 0.1142 0.1306 0.2110 -0.0079 0.0175  0.0181  147 VAL   A CA  
3531 C C   . VAL   A 147 ? 0.1245 0.1230 0.2159 -0.0120 0.0123  0.0261  147 VAL   A C   
3532 O O   . VAL   A 147 ? 0.1278 0.1265 0.2496 -0.0183 0.0074  0.0271  147 VAL   A O   
3533 C CB  . VAL   A 147 ? 0.1306 0.1281 0.2120 -0.0116 0.0062  0.0235  147 VAL   A CB  
3534 C CG1 . VAL   A 147 ? 0.1583 0.1408 0.2196 -0.0063 0.0108  0.0285  147 VAL   A CG1 
3535 C CG2 . VAL   A 147 ? 0.1397 0.1218 0.2055 -0.0156 -0.0056 0.0242  147 VAL   A CG2 
3545 N N   . ARG   A 148 ? 0.1277 0.1238 0.2217 -0.0108 0.0106  0.0401  148 ARG   A N   
3546 C CA  . ARG   A 148 ? 0.1322 0.1252 0.2243 -0.0092 0.0019  0.0442  148 ARG   A CA  
3547 C C   . ARG   A 148 ? 0.1456 0.1331 0.2218 -0.0126 -0.0004 0.0499  148 ARG   A C   
3548 O O   . ARG   A 148 ? 0.1713 0.1421 0.2380 -0.0182 0.0093  0.0465  148 ARG   A O   
3549 C CB  . ARG   A 148 ? 0.1362 0.1322 0.2442 -0.0070 0.0108  0.0404  148 ARG   A CB  
3550 C CG  . ARG   A 148 ? 0.1441 0.1333 0.2535 -0.0057 0.0144  0.0241  148 ARG   A CG  
3551 C CD  . ARG   A 148 ? 0.1534 0.1364 0.2666 -0.0033 0.0288  0.0379  148 ARG   A CD  
3552 N NE  . ARG   A 148 ? 0.1498 0.1360 0.2752 0.0075  0.0344  0.0393  148 ARG   A NE  
3553 C CZ  . ARG   A 148 ? 0.1490 0.1298 0.2511 0.0041  0.0349  0.0386  148 ARG   A CZ  
3554 N NH1 . ARG   A 148 ? 0.1614 0.1280 0.2541 -0.0079 0.0322  0.0283  148 ARG   A NH1 
3555 N NH2 . ARG   A 148 ? 0.1454 0.1450 0.2631 0.0158  0.0289  0.0396  148 ARG   A NH2 
3569 N N   . THR   A 149 ? 0.1453 0.1398 0.2227 -0.0168 -0.0048 0.0423  149 THR   A N   
3570 C CA  . THR   A 149 ? 0.1464 0.1473 0.2156 -0.0168 0.0058  0.0436  149 THR   A CA  
3571 C C   . THR   A 149 ? 0.1451 0.1408 0.2077 -0.0208 0.0128  0.0401  149 THR   A C   
3572 O O   . THR   A 149 ? 0.1417 0.1532 0.2196 -0.0213 0.0001  0.0338  149 THR   A O   
3573 C CB  . THR   A 149 ? 0.1440 0.1598 0.2195 -0.0168 0.0100  0.0323  149 THR   A CB  
3574 O OG1 . THR   A 149 ? 0.1496 0.1490 0.2277 -0.0242 -0.0002 0.0279  149 THR   A OG1 
3575 C CG2 . THR   A 149 ? 0.1408 0.1773 0.2358 -0.0105 0.0071  0.0202  149 THR   A CG2 
3583 N N   . ASN   A 150 ? 0.1480 0.1417 0.2117 -0.0107 0.0122  0.0336  150 ASN   A N   
3584 C CA  . ASN   A 150 ? 0.1626 0.1557 0.2155 -0.0124 0.0177  0.0368  150 ASN   A CA  
3585 C C   . ASN   A 150 ? 0.1435 0.1448 0.2092 -0.0192 0.0181  0.0314  150 ASN   A C   
3586 O O   . ASN   A 150 ? 0.1571 0.1562 0.2577 -0.0209 -0.0061 0.0279  150 ASN   A O   
3587 C CB  . ASN   A 150 ? 0.2021 0.1842 0.2348 -0.0155 0.0447  0.0440  150 ASN   A CB  
3588 C CG  . ASN   A 150 ? 0.2582 0.2207 0.2906 -0.0129 0.0183  0.0507  150 ASN   A CG  
3589 O OD1 . ASN   A 150 ? 0.2766 0.2312 0.3068 -0.0241 0.0256  0.0630  150 ASN   A OD1 
3590 N ND2 . ASN   A 150 ? 0.2880 0.2434 0.3267 -0.0053 0.0044  0.0551  150 ASN   A ND2 
3597 N N   . VAL   A 151 ? 0.1431 0.1342 0.2121 -0.0157 0.0130  0.0394  151 VAL   A N   
3598 C CA  . VAL   A 151 ? 0.1494 0.1382 0.2246 -0.0179 0.0176  0.0246  151 VAL   A CA  
3599 C C   . VAL   A 151 ? 0.1416 0.1325 0.2269 -0.0226 0.0177  0.0265  151 VAL   A C   
3600 O O   . VAL   A 151 ? 0.1437 0.1386 0.2494 -0.0199 0.0205  0.0263  151 VAL   A O   
3601 C CB  . VAL   A 151 ? 0.1710 0.1498 0.2239 -0.0100 0.0184  0.0307  151 VAL   A CB  
3602 C CG1 . VAL   A 151 ? 0.1681 0.1669 0.2364 -0.0125 0.0132  0.0216  151 VAL   A CG1 
3603 C CG2 . VAL   A 151 ? 0.1800 0.1527 0.2212 -0.0125 0.0339  0.0265  151 VAL   A CG2 
3613 N N   . TYR   A 152 ? 0.1367 0.1384 0.2225 -0.0207 0.0141  0.0338  152 TYR   A N   
3614 C CA  . TYR   A 152 ? 0.1426 0.1398 0.2117 -0.0254 0.0311  0.0264  152 TYR   A CA  
3615 C C   . TYR   A 152 ? 0.1366 0.1312 0.2101 -0.0214 0.0345  0.0262  152 TYR   A C   
3616 O O   . TYR   A 152 ? 0.1409 0.1328 0.2235 -0.0275 0.0300  0.0263  152 TYR   A O   
3617 C CB  . TYR   A 152 ? 0.1574 0.1484 0.2062 -0.0192 0.0257  0.0286  152 TYR   A CB  
3618 C CG  . TYR   A 152 ? 0.1769 0.1653 0.2062 -0.0244 0.0330  0.0259  152 TYR   A CG  
3619 C CD1 . TYR   A 152 ? 0.1881 0.1883 0.2185 -0.0140 0.0281  0.0355  152 TYR   A CD1 
3620 C CD2 . TYR   A 152 ? 0.1799 0.1746 0.2029 -0.0333 0.0405  0.0244  152 TYR   A CD2 
3621 C CE1 . TYR   A 152 ? 0.2054 0.2015 0.2284 -0.0095 0.0238  0.0414  152 TYR   A CE1 
3622 C CE2 . TYR   A 152 ? 0.1993 0.1913 0.2093 -0.0316 0.0360  0.0291  152 TYR   A CE2 
3623 C CZ  . TYR   A 152 ? 0.2165 0.1973 0.2168 -0.0240 0.0295  0.0449  152 TYR   A CZ  
3624 O OH  . TYR   A 152 ? 0.2408 0.2111 0.2349 -0.0144 0.0286  0.0533  152 TYR   A OH  
3634 N N   A LEU   A 153 ? 0.1295 0.1285 0.2137 -0.0196 0.0291  0.0334  153 LEU   A N   
3635 N N   B LEU   A 153 ? 0.1361 0.1324 0.2192 -0.0195 0.0262  0.0327  153 LEU   A N   
3636 C CA  A LEU   A 153 ? 0.1182 0.1222 0.2164 -0.0129 0.0279  0.0304  153 LEU   A CA  
3637 C CA  B LEU   A 153 ? 0.1295 0.1275 0.2220 -0.0084 0.0236  0.0221  153 LEU   A CA  
3638 C C   A LEU   A 153 ? 0.1178 0.1233 0.2046 -0.0202 0.0313  0.0275  153 LEU   A C   
3639 C C   B LEU   A 153 ? 0.1396 0.1434 0.2175 -0.0134 0.0237  0.0133  153 LEU   A C   
3640 O O   A LEU   A 153 ? 0.1233 0.1294 0.2166 -0.0197 0.0380  0.0258  153 LEU   A O   
3641 O O   B LEU   A 153 ? 0.1427 0.1532 0.2316 -0.0178 0.0266  0.0173  153 LEU   A O   
3642 C CB  A LEU   A 153 ? 0.1096 0.1202 0.2264 -0.0110 0.0269  0.0291  153 LEU   A CB  
3643 C CB  B LEU   A 153 ? 0.1169 0.1165 0.2264 -0.0028 0.0148  0.0268  153 LEU   A CB  
3644 C CG  A LEU   A 153 ? 0.1141 0.1232 0.2242 -0.0006 0.0253  0.0183  153 LEU   A CG  
3645 C CG  B LEU   A 153 ? 0.1217 0.1113 0.2078 0.0013  0.0189  0.0203  153 LEU   A CG  
3646 C CD1 A LEU   A 153 ? 0.1228 0.1238 0.2339 0.0078  0.0219  0.0103  153 LEU   A CD1 
3647 C CD1 B LEU   A 153 ? 0.1224 0.1199 0.2107 0.0015  0.0223  0.0172  153 LEU   A CD1 
3648 C CD2 A LEU   A 153 ? 0.1242 0.1356 0.2202 -0.0053 0.0325  0.0141  153 LEU   A CD2 
3649 C CD2 B LEU   A 153 ? 0.1370 0.1181 0.2206 0.0058  0.0291  0.0021  153 LEU   A CD2 
3672 N N   A ALA   A 154 ? 0.1092 0.1172 0.1789 -0.0193 0.0253  0.0300  154 ALA   A N   
3673 N N   B ALA   A 154 ? 0.1399 0.1455 0.1908 -0.0033 0.0269  0.0099  154 ALA   A N   
3674 C CA  A ALA   A 154 ? 0.1148 0.1269 0.1767 -0.0239 0.0315  0.0280  154 ALA   A CA  
3675 C CA  B ALA   A 154 ? 0.1464 0.1551 0.1774 -0.0034 0.0275  0.0033  154 ALA   A CA  
3676 C C   A ALA   A 154 ? 0.1216 0.1207 0.1851 -0.0131 0.0219  0.0239  154 ALA   A C   
3677 C C   B ALA   A 154 ? 0.1448 0.1499 0.1770 -0.0052 0.0174  0.0100  154 ALA   A C   
3678 O O   A ALA   A 154 ? 0.1315 0.1227 0.1860 -0.0110 0.0117  0.0182  154 ALA   A O   
3679 O O   B ALA   A 154 ? 0.1503 0.1489 0.1651 -0.0058 0.0136  0.0252  154 ALA   A O   
3680 C CB  A ALA   A 154 ? 0.1243 0.1355 0.1768 -0.0210 0.0259  0.0179  154 ALA   A CB  
3681 C CB  B ALA   A 154 ? 0.1596 0.1606 0.1771 -0.0062 0.0148  -0.0097 154 ALA   A CB  
3692 N N   A VAL   A 155 ? 0.1271 0.1292 0.2054 -0.0109 0.0209  0.0290  155 VAL   A N   
3693 N N   B VAL   A 155 ? 0.1503 0.1659 0.2050 -0.0146 0.0049  0.0210  155 VAL   A N   
3694 C CA  A VAL   A 155 ? 0.1289 0.1380 0.2322 -0.0065 0.0121  0.0384  155 VAL   A CA  
3695 C CA  B VAL   A 155 ? 0.1520 0.1810 0.2474 -0.0215 0.0043  0.0343  155 VAL   A CA  
3696 C C   A VAL   A 155 ? 0.1336 0.1468 0.2658 0.0141  0.0175  0.0410  155 VAL   A C   
3697 C C   B VAL   A 155 ? 0.1575 0.1912 0.3051 -0.0151 0.0099  0.0387  155 VAL   A C   
3698 O O   A VAL   A 155 ? 0.1317 0.1530 0.2958 0.0219  0.0331  0.0363  155 VAL   A O   
3699 O O   B VAL   A 155 ? 0.1597 0.1979 0.3427 -0.0098 0.0102  0.0401  155 VAL   A O   
3700 C CB  A VAL   A 155 ? 0.1328 0.1426 0.2288 -0.0104 -0.0108 0.0427  155 VAL   A CB  
3701 C CB  B VAL   A 155 ? 0.1578 0.1903 0.2608 -0.0253 -0.0129 0.0308  155 VAL   A CB  
3702 C CG1 A VAL   A 155 ? 0.1481 0.1559 0.2257 -0.0109 -0.0208 0.0419  155 VAL   A CG1 
3703 C CG1 B VAL   A 155 ? 0.1706 0.2027 0.2721 -0.0235 -0.0312 0.0348  155 VAL   A CG1 
3704 C CG2 A VAL   A 155 ? 0.1385 0.1410 0.2377 -0.0054 -0.0219 0.0421  155 VAL   A CG2 
3705 C CG2 B VAL   A 155 ? 0.1607 0.1908 0.2682 -0.0253 -0.0259 0.0162  155 VAL   A CG2 
3724 N N   A PHE   A 156 ? 0.1456 0.1523 0.2789 0.0296  0.0028  0.0424  156 PHE   A N   
3725 N N   B PHE   A 156 ? 0.1644 0.1959 0.3189 -0.0084 0.0193  0.0354  156 PHE   A N   
3726 C CA  A PHE   A 156 ? 0.1737 0.1603 0.2955 0.0389  -0.0084 0.0395  156 PHE   A CA  
3727 C CA  B PHE   A 156 ? 0.1839 0.2103 0.3519 0.0009  0.0228  0.0245  156 PHE   A CA  
3728 C C   A PHE   A 156 ? 0.1742 0.1574 0.3019 0.0462  -0.0019 0.0444  156 PHE   A C   
3729 C C   B PHE   A 156 ? 0.1961 0.2134 0.3704 0.0073  0.0183  0.0327  156 PHE   A C   
3730 O O   A PHE   A 156 ? 0.1795 0.1750 0.3245 0.0405  0.0089  0.0194  156 PHE   A O   
3731 O O   B PHE   A 156 ? 0.2013 0.2055 0.3820 0.0112  0.0179  0.0245  156 PHE   A O   
3732 C CB  A PHE   A 156 ? 0.2046 0.1708 0.3001 0.0391  -0.0233 0.0334  156 PHE   A CB  
3733 C CB  B PHE   A 156 ? 0.2034 0.2279 0.3698 0.0032  0.0300  -0.0045 156 PHE   A CB  
3734 C CG  A PHE   A 156 ? 0.2367 0.1851 0.3098 0.0433  -0.0381 0.0288  156 PHE   A CG  
3735 C CG  B PHE   A 156 ? 0.2246 0.2468 0.3858 0.0104  0.0307  -0.0308 156 PHE   A CG  
3736 C CD1 A PHE   A 156 ? 0.2523 0.1906 0.3081 0.0455  -0.0429 0.0330  156 PHE   A CD1 
3737 C CD1 B PHE   A 156 ? 0.2347 0.2581 0.3926 0.0113  0.0334  -0.0416 156 PHE   A CD1 
3738 C CD2 A PHE   A 156 ? 0.2508 0.1989 0.3157 0.0463  -0.0472 0.0249  156 PHE   A CD2 
3739 C CD2 B PHE   A 156 ? 0.2326 0.2475 0.3892 0.0123  0.0198  -0.0434 156 PHE   A CD2 
3740 C CE1 A PHE   A 156 ? 0.2607 0.1983 0.3156 0.0467  -0.0425 0.0206  156 PHE   A CE1 
3741 C CE1 B PHE   A 156 ? 0.2420 0.2642 0.4001 0.0182  0.0298  -0.0484 156 PHE   A CE1 
3742 C CE2 A PHE   A 156 ? 0.2611 0.2074 0.3159 0.0464  -0.0429 0.0187  156 PHE   A CE2 
3743 C CE2 B PHE   A 156 ? 0.2411 0.2521 0.3989 0.0196  0.0186  -0.0501 156 PHE   A CE2 
3744 C CZ  A PHE   A 156 ? 0.2618 0.2038 0.3180 0.0507  -0.0413 0.0095  156 PHE   A CZ  
3745 C CZ  B PHE   A 156 ? 0.2435 0.2598 0.3997 0.0226  0.0261  -0.0526 156 PHE   A CZ  
3764 N N   A ASP   A 157 ? 0.1781 0.1570 0.2814 0.0358  0.0037  0.0647  157 ASP   A N   
3765 N N   B ASP   A 157 ? 0.1993 0.2294 0.3674 0.0055  0.0204  0.0473  157 ASP   A N   
3766 C CA  A ASP   A 157 ? 0.1808 0.1651 0.2779 0.0236  0.0127  0.0680  157 ASP   A CA  
3767 C CA  B ASP   A 157 ? 0.2120 0.2467 0.3838 0.0020  0.0246  0.0624  157 ASP   A CA  
3768 C C   A ASP   A 157 ? 0.1642 0.1657 0.2938 0.0278  0.0251  0.0779  157 ASP   A C   
3769 C C   B ASP   A 157 ? 0.2060 0.2580 0.3933 -0.0006 0.0368  0.0614  157 ASP   A C   
3770 O O   A ASP   A 157 ? 0.1476 0.1512 0.3019 0.0273  0.0376  0.0792  157 ASP   A O   
3771 O O   B ASP   A 157 ? 0.1989 0.2509 0.3956 -0.0046 0.0293  0.0620  157 ASP   A O   
3772 C CB  A ASP   A 157 ? 0.1970 0.1726 0.2756 0.0168  -0.0005 0.0745  157 ASP   A CB  
3773 C CB  B ASP   A 157 ? 0.2200 0.2466 0.3884 0.0004  0.0212  0.0795  157 ASP   A CB  
3774 C CG  A ASP   A 157 ? 0.2111 0.1861 0.2838 0.0151  -0.0134 0.0757  157 ASP   A CG  
3775 C CG  B ASP   A 157 ? 0.2258 0.2464 0.3846 -0.0005 0.0192  0.1021  157 ASP   A CG  
3776 O OD1 A ASP   A 157 ? 0.2300 0.1983 0.3146 0.0051  -0.0338 0.0643  157 ASP   A OD1 
3777 O OD1 B ASP   A 157 ? 0.2236 0.2442 0.3692 -0.0018 0.0080  0.1143  157 ASP   A OD1 
3778 O OD2 A ASP   A 157 ? 0.2064 0.1858 0.2866 0.0120  -0.0033 0.0754  157 ASP   A OD2 
3779 O OD2 B ASP   A 157 ? 0.2293 0.2511 0.3992 -0.0001 0.0181  0.1012  157 ASP   A OD2 
3788 N N   A LYS   A 158 ? 0.1661 0.1858 0.3033 0.0289  0.0295  0.0812  158 LYS   A N   
3789 N N   B LYS   A 158 ? 0.2134 0.2753 0.4016 -0.0001 0.0513  0.0672  158 LYS   A N   
3790 C CA  A LYS   A 158 ? 0.1576 0.2069 0.3078 0.0390  0.0401  0.0879  158 LYS   A CA  
3791 C CA  B LYS   A 158 ? 0.2166 0.2918 0.4101 0.0074  0.0573  0.0703  158 LYS   A CA  
3792 C C   A LYS   A 158 ? 0.1425 0.2180 0.3086 0.0419  0.0337  0.0974  158 LYS   A C   
3793 C C   B LYS   A 158 ? 0.2085 0.2952 0.3998 0.0053  0.0415  0.0768  158 LYS   A C   
3794 O O   A LYS   A 158 ? 0.1305 0.2175 0.3252 0.0345  0.0431  0.1024  158 LYS   A O   
3795 O O   B LYS   A 158 ? 0.1980 0.2915 0.4061 0.0027  0.0469  0.0772  158 LYS   A O   
3796 C CB  A LYS   A 158 ? 0.1728 0.2206 0.3139 0.0410  0.0581  0.0895  158 LYS   A CB  
3797 C CB  B LYS   A 158 ? 0.2319 0.3028 0.4322 0.0156  0.0709  0.0708  158 LYS   A CB  
3798 C CG  A LYS   A 158 ? 0.1946 0.2420 0.3371 0.0351  0.0651  0.0865  158 LYS   A CG  
3799 C CG  B LYS   A 158 ? 0.2461 0.3111 0.4485 0.0178  0.0836  0.0778  158 LYS   A CG  
3800 C CD  A LYS   A 158 ? 0.2126 0.2602 0.3576 0.0298  0.0683  0.0903  158 LYS   A CD  
3801 C CD  B LYS   A 158 ? 0.2546 0.3168 0.4590 0.0157  0.0994  0.0833  158 LYS   A CD  
3802 C CE  A LYS   A 158 ? 0.2203 0.2730 0.3767 0.0247  0.0718  0.0930  158 LYS   A CE  
3803 C CE  B LYS   A 158 ? 0.2596 0.3195 0.4584 0.0160  0.1137  0.0911  158 LYS   A CE  
3804 N NZ  A LYS   A 158 ? 0.2234 0.2775 0.3831 0.0182  0.0747  0.0996  158 LYS   A NZ  
3805 N NZ  B LYS   A 158 ? 0.2641 0.3238 0.4608 0.0132  0.1200  0.0952  158 LYS   A NZ  
3832 N N   A ASN   A 159 ? 0.1474 0.2351 0.3069 0.0410  0.0214  0.0947  159 ASN   A N   
3833 N N   B ASN   A 159 ? 0.2071 0.3009 0.3819 0.0047  0.0222  0.0882  159 ASN   A N   
3834 C CA  A ASN   A 159 ? 0.1564 0.2481 0.2979 0.0448  0.0072  0.0956  159 ASN   A CA  
3835 C CA  B ASN   A 159 ? 0.2073 0.3038 0.3726 0.0129  -0.0017 0.0962  159 ASN   A CA  
3836 C C   A ASN   A 159 ? 0.1428 0.2416 0.2777 0.0316  0.0009  0.0999  159 ASN   A C   
3837 C C   B ASN   A 159 ? 0.1797 0.2823 0.3447 0.0078  -0.0141 0.1001  159 ASN   A C   
3838 O O   A ASN   A 159 ? 0.1325 0.2554 0.2828 0.0307  -0.0150 0.0981  159 ASN   A O   
3839 O O   B ASN   A 159 ? 0.1523 0.2805 0.3481 0.0069  -0.0245 0.1047  159 ASN   A O   
3840 C CB  A ASN   A 159 ? 0.1824 0.2654 0.3134 0.0459  0.0035  0.0845  159 ASN   A CB  
3841 C CB  B ASN   A 159 ? 0.2353 0.3236 0.3924 0.0137  -0.0037 0.0974  159 ASN   A CB  
3842 C CG  A ASN   A 159 ? 0.2063 0.2807 0.3343 0.0418  0.0040  0.0723  159 ASN   A CG  
3843 C CG  B ASN   A 159 ? 0.2574 0.3380 0.4110 0.0100  0.0028  0.0982  159 ASN   A CG  
3844 O OD1 A ASN   A 159 ? 0.2129 0.2882 0.3376 0.0376  0.0126  0.0650  159 ASN   A OD1 
3845 O OD1 B ASN   A 159 ? 0.2735 0.3456 0.4208 0.0076  0.0019  0.1025  159 ASN   A OD1 
3846 N ND2 A ASN   A 159 ? 0.2142 0.2878 0.3446 0.0389  0.0003  0.0663  159 ASN   A ND2 
3847 N ND2 B ASN   A 159 ? 0.2688 0.3435 0.4178 0.0066  0.0091  0.0955  159 ASN   A ND2 
3860 N N   A LEU   A 160 ? 0.1339 0.2242 0.2620 0.0208  -0.0109 0.1024  160 LEU   A N   
3861 N N   B LEU   A 160 ? 0.1725 0.2663 0.3239 -0.0029 -0.0093 0.0907  160 LEU   A N   
3862 C CA  A LEU   A 160 ? 0.1309 0.2085 0.2348 0.0088  -0.0082 0.1000  160 LEU   A CA  
3863 C CA  B LEU   A 160 ? 0.1633 0.2572 0.2892 -0.0047 -0.0151 0.0768  160 LEU   A CA  
3864 C C   A LEU   A 160 ? 0.1112 0.1998 0.2172 0.0004  0.0075  0.0994  160 LEU   A C   
3865 C C   B LEU   A 160 ? 0.1470 0.2494 0.2674 -0.0095 -0.0088 0.0640  160 LEU   A C   
3866 O O   A LEU   A 160 ? 0.1069 0.2029 0.2297 -0.0002 0.0031  0.0902  160 LEU   A O   
3867 O O   B LEU   A 160 ? 0.1440 0.2455 0.2718 -0.0184 0.0009  0.0720  160 LEU   A O   
3868 C CB  A LEU   A 160 ? 0.1481 0.2079 0.2215 -0.0019 -0.0098 0.0845  160 LEU   A CB  
3869 C CB  B LEU   A 160 ? 0.1749 0.2590 0.2817 -0.0081 -0.0125 0.0681  160 LEU   A CB  
3870 C CG  A LEU   A 160 ? 0.1548 0.2089 0.2171 -0.0123 -0.0087 0.0609  160 LEU   A CG  
3871 C CG  B LEU   A 160 ? 0.1771 0.2563 0.2607 -0.0203 -0.0051 0.0554  160 LEU   A CG  
3872 C CD1 A LEU   A 160 ? 0.1659 0.2157 0.2210 -0.0126 -0.0017 0.0471  160 LEU   A CD1 
3873 C CD1 B LEU   A 160 ? 0.1887 0.2623 0.2673 -0.0199 -0.0080 0.0431  160 LEU   A CD1 
3874 C CD2 A LEU   A 160 ? 0.1538 0.2048 0.2200 -0.0175 -0.0053 0.0559  160 LEU   A CD2 
3875 C CD2 B LEU   A 160 ? 0.1767 0.2505 0.2399 -0.0265 0.0049  0.0561  160 LEU   A CD2 
3898 N N   A TYR   A 161 ? 0.1142 0.2029 0.2153 -0.0019 0.0162  0.0930  161 TYR   A N   
3899 N N   B TYR   A 161 ? 0.1491 0.2555 0.2625 -0.0036 -0.0013 0.0472  161 TYR   A N   
3900 C CA  A TYR   A 161 ? 0.1170 0.2065 0.2092 -0.0019 0.0191  0.0878  161 TYR   A CA  
3901 C CA  B TYR   A 161 ? 0.1477 0.2601 0.2525 -0.0033 0.0089  0.0385  161 TYR   A CA  
3902 C C   A TYR   A 161 ? 0.1160 0.2094 0.2168 -0.0027 0.0141  0.0805  161 TYR   A C   
3903 C C   B TYR   A 161 ? 0.1440 0.2672 0.2641 -0.0042 0.0111  0.0388  161 TYR   A C   
3904 O O   A TYR   A 161 ? 0.1169 0.2058 0.2061 -0.0066 0.0142  0.0799  161 TYR   A O   
3905 O O   B TYR   A 161 ? 0.1457 0.2621 0.2563 -0.0101 0.0109  0.0355  161 TYR   A O   
3906 C CB  A TYR   A 161 ? 0.1254 0.2104 0.2099 -0.0048 0.0173  0.0703  161 TYR   A CB  
3907 C CB  B TYR   A 161 ? 0.1570 0.2619 0.2502 -0.0068 0.0170  0.0374  161 TYR   A CB  
3908 C CG  A TYR   A 161 ? 0.1293 0.2135 0.2100 -0.0060 0.0174  0.0556  161 TYR   A CG  
3909 C CG  B TYR   A 161 ? 0.1635 0.2632 0.2587 -0.0095 0.0255  0.0313  161 TYR   A CG  
3910 C CD1 A TYR   A 161 ? 0.1279 0.2114 0.2117 -0.0060 0.0139  0.0540  161 TYR   A CD1 
3911 C CD1 B TYR   A 161 ? 0.1650 0.2605 0.2591 -0.0108 0.0334  0.0334  161 TYR   A CD1 
3912 C CD2 A TYR   A 161 ? 0.1320 0.2253 0.2127 -0.0126 0.0106  0.0468  161 TYR   A CD2 
3913 C CD2 B TYR   A 161 ? 0.1715 0.2762 0.2746 -0.0163 0.0251  0.0229  161 TYR   A CD2 
3914 C CE1 A TYR   A 161 ? 0.1342 0.2143 0.2119 -0.0145 0.0122  0.0571  161 TYR   A CE1 
3915 C CE1 B TYR   A 161 ? 0.1834 0.2675 0.2772 -0.0201 0.0359  0.0323  161 TYR   A CE1 
3916 C CE2 A TYR   A 161 ? 0.1327 0.2239 0.2107 -0.0198 0.0088  0.0469  161 TYR   A CE2 
3917 C CE2 B TYR   A 161 ? 0.1834 0.2796 0.2889 -0.0240 0.0276  0.0221  161 TYR   A CE2 
3918 C CZ  A TYR   A 161 ? 0.1429 0.2206 0.2158 -0.0190 0.0051  0.0551  161 TYR   A CZ  
3919 C CZ  B TYR   A 161 ? 0.1970 0.2781 0.3007 -0.0236 0.0351  0.0317  161 TYR   A CZ  
3920 O OH  A TYR   A 161 ? 0.1517 0.2247 0.2238 -0.0304 0.0009  0.0608  161 TYR   A OH  
3921 O OH  B TYR   A 161 ? 0.2157 0.2880 0.3245 -0.0300 0.0393  0.0368  161 TYR   A OH  
3940 N N   A ASP   A 162 ? 0.1147 0.2192 0.2307 -0.0027 0.0203  0.0790  162 ASP   A N   
3941 N N   B ASP   A 162 ? 0.1399 0.2831 0.2906 -0.0023 0.0051  0.0347  162 ASP   A N   
3942 C CA  A ASP   A 162 ? 0.1170 0.2377 0.2407 -0.0100 0.0159  0.0832  162 ASP   A CA  
3943 C CA  B ASP   A 162 ? 0.1387 0.3046 0.3135 -0.0025 0.0092  0.0360  162 ASP   A CA  
3944 C C   A ASP   A 162 ? 0.1099 0.2366 0.2555 -0.0199 0.0079  0.0760  162 ASP   A C   
3945 C C   B ASP   A 162 ? 0.1419 0.3043 0.3300 -0.0049 0.0027  0.0313  162 ASP   A C   
3946 O O   A ASP   A 162 ? 0.1077 0.2299 0.2781 -0.0358 0.0034  0.0679  162 ASP   A O   
3947 O O   B ASP   A 162 ? 0.1372 0.3019 0.3503 -0.0036 -0.0013 0.0272  162 ASP   A O   
3948 C CB  A ASP   A 162 ? 0.1236 0.2569 0.2484 -0.0053 0.0146  0.0825  162 ASP   A CB  
3949 C CB  B ASP   A 162 ? 0.1438 0.3280 0.3259 0.0004  0.0148  0.0368  162 ASP   A CB  
3950 C CG  A ASP   A 162 ? 0.1341 0.2785 0.2522 0.0062  0.0135  0.0794  162 ASP   A CG  
3951 C CG  B ASP   A 162 ? 0.1616 0.3509 0.3439 0.0043  0.0246  0.0401  162 ASP   A CG  
3952 O OD1 A ASP   A 162 ? 0.1448 0.2897 0.2613 0.0037  0.0207  0.0764  162 ASP   A OD1 
3953 O OD1 B ASP   A 162 ? 0.1729 0.3590 0.3501 -0.0005 0.0426  0.0447  162 ASP   A OD1 
3954 O OD2 A ASP   A 162 ? 0.1447 0.2893 0.2658 0.0211  -0.0023 0.0693  162 ASP   A OD2 
3955 O OD2 B ASP   A 162 ? 0.1840 0.3620 0.3502 0.0097  0.0223  0.0417  162 ASP   A OD2 
3964 N N   A LYS   A 163 ? 0.1185 0.2446 0.2647 -0.0153 -0.0073 0.0692  163 LYS   A N   
3965 N N   B LYS   A 163 ? 0.1620 0.3104 0.3324 -0.0057 -0.0110 0.0351  163 LYS   A N   
3966 C CA  A LYS   A 163 ? 0.1212 0.2471 0.2698 -0.0139 -0.0029 0.0596  163 LYS   A CA  
3967 C CA  B LYS   A 163 ? 0.1863 0.3178 0.3427 -0.0125 -0.0098 0.0319  163 LYS   A CA  
3968 C C   A LYS   A 163 ? 0.1045 0.2266 0.2770 -0.0171 0.0150  0.0508  163 LYS   A C   
3969 C C   B LYS   A 163 ? 0.1817 0.3032 0.3460 -0.0212 0.0041  0.0342  163 LYS   A C   
3970 O O   A LYS   A 163 ? 0.1021 0.2401 0.2892 -0.0178 0.0184  0.0462  163 LYS   A O   
3971 O O   B LYS   A 163 ? 0.1822 0.3106 0.3386 -0.0234 0.0183  0.0247  163 LYS   A O   
3972 C CB  A LYS   A 163 ? 0.1568 0.2716 0.2942 -0.0072 -0.0105 0.0499  163 LYS   A CB  
3973 C CB  B LYS   A 163 ? 0.2178 0.3427 0.3616 -0.0111 -0.0135 0.0262  163 LYS   A CB  
3974 C CG  A LYS   A 163 ? 0.1926 0.2930 0.3334 -0.0068 -0.0027 0.0463  163 LYS   A CG  
3975 C CG  B LYS   A 163 ? 0.2503 0.3655 0.3913 -0.0107 -0.0122 0.0218  163 LYS   A CG  
3976 C CD  A LYS   A 163 ? 0.2211 0.3116 0.3746 -0.0031 -0.0016 0.0391  163 LYS   A CD  
3977 C CD  B LYS   A 163 ? 0.2782 0.3847 0.4219 -0.0098 -0.0065 0.0171  163 LYS   A CD  
3978 C CE  A LYS   A 163 ? 0.2392 0.3226 0.4079 -0.0006 0.0024  0.0373  163 LYS   A CE  
3979 C CE  B LYS   A 163 ? 0.2966 0.3981 0.4474 -0.0089 0.0010  0.0145  163 LYS   A CE  
3980 N NZ  A LYS   A 163 ? 0.2458 0.3277 0.4263 0.0009  0.0040  0.0373  163 LYS   A NZ  
3981 N NZ  B LYS   A 163 ? 0.3044 0.4049 0.4626 -0.0097 0.0067  0.0148  163 LYS   A NZ  
4008 N N   A LEU   A 164 ? 0.0973 0.2058 0.2859 -0.0187 0.0062  0.0386  164 LEU   A N   
4009 N N   B LEU   A 164 ? 0.1773 0.2840 0.3596 -0.0226 -0.0028 0.0372  164 LEU   A N   
4010 C CA  A LEU   A 164 ? 0.1003 0.1840 0.2829 -0.0261 0.0085  0.0395  164 LEU   A CA  
4011 C CA  B LEU   A 164 ? 0.1868 0.2646 0.3625 -0.0242 0.0013  0.0494  164 LEU   A CA  
4012 C C   A LEU   A 164 ? 0.1024 0.1773 0.2833 -0.0305 0.0163  0.0338  164 LEU   A C   
4013 C C   B LEU   A 164 ? 0.1999 0.2601 0.3831 -0.0188 0.0074  0.0546  164 LEU   A C   
4014 O O   A LEU   A 164 ? 0.1092 0.1850 0.2941 -0.0277 0.0253  0.0186  164 LEU   A O   
4015 O O   B LEU   A 164 ? 0.2048 0.2613 0.4018 -0.0190 0.0180  0.0452  164 LEU   A O   
4016 C CB  A LEU   A 164 ? 0.1025 0.1768 0.2820 -0.0249 0.0128  0.0495  164 LEU   A CB  
4017 C CB  B LEU   A 164 ? 0.1867 0.2544 0.3487 -0.0305 0.0007  0.0547  164 LEU   A CB  
4018 C CG  A LEU   A 164 ? 0.1036 0.1772 0.2748 -0.0156 0.0063  0.0473  164 LEU   A CG  
4019 C CG  B LEU   A 164 ? 0.1869 0.2495 0.3291 -0.0308 -0.0031 0.0525  164 LEU   A CG  
4020 C CD1 A LEU   A 164 ? 0.0967 0.1761 0.2604 -0.0068 -0.0036 0.0571  164 LEU   A CD1 
4021 C CD1 B LEU   A 164 ? 0.1803 0.2464 0.3220 -0.0331 -0.0102 0.0552  164 LEU   A CD1 
4022 C CD2 A LEU   A 164 ? 0.1241 0.1807 0.2767 -0.0087 0.0041  0.0404  164 LEU   A CD2 
4023 C CD2 B LEU   A 164 ? 0.1991 0.2496 0.3237 -0.0290 0.0019  0.0493  164 LEU   A CD2 
4046 N N   A VAL   A 165 ? 0.1066 0.1737 0.2715 -0.0407 0.0217  0.0259  165 VAL   A N   
4047 N N   B VAL   A 165 ? 0.2150 0.2654 0.3835 -0.0144 0.0022  0.0572  165 VAL   A N   
4048 C CA  A VAL   A 165 ? 0.1144 0.1714 0.2503 -0.0529 0.0323  0.0205  165 VAL   A CA  
4049 C CA  B VAL   A 165 ? 0.2301 0.2744 0.3748 -0.0166 -0.0036 0.0641  165 VAL   A CA  
4050 C C   A VAL   A 165 ? 0.1032 0.1873 0.2394 -0.0494 0.0441  0.0016  165 VAL   A C   
4051 C C   B VAL   A 165 ? 0.2338 0.2759 0.3613 -0.0223 -0.0106 0.0658  165 VAL   A C   
4052 O O   A VAL   A 165 ? 0.1044 0.1930 0.2371 -0.0332 0.0426  -0.0097 165 VAL   A O   
4053 O O   B VAL   A 165 ? 0.2289 0.2611 0.3510 -0.0289 -0.0047 0.0757  165 VAL   A O   
4054 C CB  A VAL   A 165 ? 0.1340 0.1681 0.2482 -0.0572 0.0307  0.0204  165 VAL   A CB  
4055 C CB  B VAL   A 165 ? 0.2453 0.2892 0.3910 -0.0133 -0.0059 0.0633  165 VAL   A CB  
4056 C CG1 A VAL   A 165 ? 0.1433 0.1666 0.2455 -0.0545 0.0380  0.0180  165 VAL   A CG1 
4057 C CG1 B VAL   A 165 ? 0.2500 0.2942 0.3932 -0.0171 -0.0040 0.0648  165 VAL   A CG1 
4058 C CG2 A VAL   A 165 ? 0.1486 0.1652 0.2590 -0.0596 0.0235  0.0221  165 VAL   A CG2 
4059 C CG2 B VAL   A 165 ? 0.2527 0.2927 0.3988 -0.0108 -0.0055 0.0649  165 VAL   A CG2 
4078 N N   A SER   A 166 ? 0.0962 0.2046 0.2377 -0.0441 0.0452  0.0001  166 SER   A N   
4079 N N   B SER   A 166 ? 0.2499 0.2964 0.3635 -0.0235 -0.0166 0.0624  166 SER   A N   
4080 C CA  A SER   A 166 ? 0.1017 0.2304 0.2353 -0.0461 0.0406  -0.0004 166 SER   A CA  
4081 C CA  B SER   A 166 ? 0.2643 0.3188 0.3668 -0.0196 -0.0268 0.0440  166 SER   A CA  
4082 C C   A SER   A 166 ? 0.0989 0.2441 0.2341 -0.0505 0.0191  -0.0113 166 SER   A C   
4083 C C   B SER   A 166 ? 0.2763 0.3299 0.3595 -0.0243 -0.0327 0.0390  166 SER   A C   
4084 O O   A SER   A 166 ? 0.1136 0.2472 0.2553 -0.0498 0.0266  -0.0242 166 SER   A O   
4085 O O   B SER   A 166 ? 0.2756 0.3296 0.3470 -0.0266 -0.0387 0.0393  166 SER   A O   
4086 C CB  A SER   A 166 ? 0.1360 0.2427 0.2567 -0.0326 0.0325  0.0004  166 SER   A CB  
4087 C CB  B SER   A 166 ? 0.2733 0.3343 0.3843 -0.0103 -0.0325 0.0269  166 SER   A CB  
4088 O OG  A SER   A 166 ? 0.1655 0.2596 0.2767 -0.0287 0.0432  0.0102  166 SER   A OG  
4089 O OG  B SER   A 166 ? 0.2884 0.3454 0.4073 -0.0086 -0.0335 0.0205  166 SER   A OG  
4100 N N   A SER   A 167 ? 0.1039 0.2523 0.2150 -0.0390 0.0038  -0.0132 167 SER   A N   
4101 N N   B SER   A 167 ? 0.2896 0.3402 0.3742 -0.0221 -0.0301 0.0355  167 SER   A N   
4102 C CA  A SER   A 167 ? 0.1229 0.2636 0.1939 -0.0225 -0.0096 -0.0200 167 SER   A CA  
4103 C CA  B SER   A 167 ? 0.3090 0.3509 0.3916 -0.0191 -0.0208 0.0324  167 SER   A CA  
4104 C C   A SER   A 167 ? 0.1336 0.2637 0.1911 -0.0087 0.0048  -0.0213 167 SER   A C   
4105 C C   B SER   A 167 ? 0.3235 0.3580 0.4039 -0.0161 -0.0139 0.0317  167 SER   A C   
4106 O O   A SER   A 167 ? 0.1451 0.2726 0.2114 -0.0044 -0.0033 -0.0224 167 SER   A O   
4107 O O   B SER   A 167 ? 0.3261 0.3579 0.4044 -0.0169 -0.0108 0.0346  167 SER   A O   
4108 C CB  A SER   A 167 ? 0.1391 0.2742 0.1904 -0.0185 -0.0144 -0.0134 167 SER   A CB  
4109 C CB  B SER   A 167 ? 0.3133 0.3540 0.3968 -0.0170 -0.0151 0.0288  167 SER   A CB  
4110 O OG  A SER   A 167 ? 0.1485 0.2826 0.1837 -0.0211 0.0024  -0.0041 167 SER   A OG  
4111 O OG  B SER   A 167 ? 0.3148 0.3559 0.3981 -0.0157 -0.0066 0.0285  167 SER   A OG  
4122 N N   A PHE   A 168 ? 0.1349 0.2566 0.1731 0.0023  0.0170  -0.0257 168 PHE   A N   
4123 N N   B PHE   A 168 ? 0.3349 0.3661 0.4114 -0.0132 -0.0094 0.0329  168 PHE   A N   
4124 C CA  A PHE   A 168 ? 0.1413 0.2547 0.1802 -0.0037 0.0166  -0.0178 168 PHE   A CA  
4125 C CA  B PHE   A 168 ? 0.3456 0.3762 0.4228 -0.0093 -0.0011 0.0253  168 PHE   A CA  
4126 C C   A PHE   A 168 ? 0.1508 0.2711 0.2109 -0.0228 0.0370  -0.0263 168 PHE   A C   
4127 C C   B PHE   A 168 ? 0.3802 0.4060 0.4782 -0.0061 0.0055  0.0002  168 PHE   A C   
4128 O O   A PHE   A 168 ? 0.1480 0.2724 0.2362 -0.0410 0.0447  -0.0229 168 PHE   A O   
4129 O O   B PHE   A 168 ? 0.3813 0.4053 0.4813 -0.0044 0.0169  -0.0060 168 PHE   A O   
4130 C CB  A PHE   A 168 ? 0.1518 0.2411 0.1677 -0.0022 -0.0007 -0.0064 168 PHE   A CB  
4131 C CB  B PHE   A 168 ? 0.3240 0.3594 0.3766 -0.0106 0.0028  0.0475  168 PHE   A CB  
4132 C CG  A PHE   A 168 ? 0.1490 0.2242 0.1615 -0.0124 -0.0144 0.0019  168 PHE   A CG  
4133 C CG  B PHE   A 168 ? 0.2988 0.3439 0.3330 -0.0167 0.0034  0.0630  168 PHE   A CG  
4134 C CD1 A PHE   A 168 ? 0.1503 0.2191 0.1685 -0.0181 -0.0195 0.0060  168 PHE   A CD1 
4135 C CD1 B PHE   A 168 ? 0.2886 0.3376 0.3167 -0.0207 -0.0029 0.0652  168 PHE   A CD1 
4136 C CD2 A PHE   A 168 ? 0.1432 0.2148 0.1618 -0.0085 -0.0044 0.0080  168 PHE   A CD2 
4137 C CD2 B PHE   A 168 ? 0.2875 0.3370 0.3172 -0.0188 0.0076  0.0723  168 PHE   A CD2 
4138 C CE1 A PHE   A 168 ? 0.1399 0.2170 0.1749 -0.0197 -0.0180 0.0118  168 PHE   A CE1 
4139 C CE1 B PHE   A 168 ? 0.2799 0.3344 0.3068 -0.0246 -0.0051 0.0666  168 PHE   A CE1 
4140 C CE2 A PHE   A 168 ? 0.1397 0.2082 0.1709 -0.0137 0.0013  0.0186  168 PHE   A CE2 
4141 C CE2 B PHE   A 168 ? 0.2791 0.3317 0.3066 -0.0229 0.0085  0.0773  168 PHE   A CE2 
4142 C CZ  A PHE   A 168 ? 0.1374 0.2113 0.1732 -0.0174 -0.0098 0.0174  168 PHE   A CZ  
4143 C CZ  B PHE   A 168 ? 0.2763 0.3323 0.3015 -0.0250 0.0005  0.0723  168 PHE   A CZ  
4162 N N   A LEU   A 169 ? 0.1868 0.2836 0.2472 -0.0263 0.0309  -0.0325 169 LEU   A N   
4163 N N   B LEU   A 169 ? 0.4103 0.4346 0.5240 -0.0005 0.0013  -0.0166 169 LEU   A N   
4164 C CA  A LEU   A 169 ? 0.2342 0.3051 0.3026 -0.0181 0.0107  -0.0296 169 LEU   A CA  
4165 C CA  B LEU   A 169 ? 0.4403 0.4615 0.5596 0.0042  -0.0003 -0.0299 169 LEU   A CA  
4166 C C   A LEU   A 169 ? 0.2420 0.3088 0.2991 -0.0161 0.0126  -0.0189 169 LEU   A C   
4167 C C   B LEU   A 169 ? 0.4511 0.4703 0.5784 0.0089  -0.0009 -0.0326 169 LEU   A C   
4168 O O   A LEU   A 169 ? 0.2450 0.3093 0.2916 -0.0134 0.0106  -0.0139 169 LEU   A O   
4169 O O   B LEU   A 169 ? 0.4539 0.4740 0.5860 0.0111  -0.0004 -0.0331 169 LEU   A O   
4170 C CB  A LEU   A 169 ? 0.2666 0.3224 0.3613 -0.0111 -0.0051 -0.0297 169 LEU   A CB  
4171 C CB  B LEU   A 169 ? 0.4563 0.4767 0.5731 0.0043  -0.0003 -0.0368 169 LEU   A CB  
4172 C CG  A LEU   A 169 ? 0.2915 0.3356 0.4071 -0.0083 -0.0196 -0.0292 169 LEU   A CG  
4173 C CG  B LEU   A 169 ? 0.4696 0.4882 0.5810 0.0041  0.0006  -0.0437 169 LEU   A CG  
4174 C CD1 A LEU   A 169 ? 0.3001 0.3397 0.4239 -0.0059 -0.0245 -0.0263 169 LEU   A CD1 
4175 C CD1 B LEU   A 169 ? 0.4747 0.4927 0.5845 0.0042  0.0014  -0.0463 169 LEU   A CD1 
4176 C CD2 A LEU   A 169 ? 0.2994 0.3403 0.4225 -0.0084 -0.0237 -0.0311 169 LEU   A CD2 
4177 C CD2 B LEU   A 169 ? 0.4728 0.4913 0.5841 0.0037  0.0011  -0.0460 169 LEU   A CD2 
4178 O OXT A LEU   A 169 ? 0.2409 0.3113 0.2978 -0.0164 0.0244  -0.0142 169 LEU   A OXT 
4179 O OXT B LEU   A 169 ? 0.4567 0.4734 0.5828 0.0109  -0.0017 -0.0336 169 LEU   A OXT 
4202 N N   A SER   B 1   ? 0.3596 0.3513 0.4083 -0.0995 -0.0528 0.0557  1   SER   B N   
4203 N N   B SER   B 1   ? 0.3898 0.3317 0.3572 -0.0810 -0.0541 0.0168  1   SER   B N   
4204 C CA  A SER   B 1   ? 0.3501 0.3450 0.3962 -0.1051 -0.0512 0.0603  1   SER   B CA  
4205 C CA  B SER   B 1   ? 0.3837 0.3340 0.3568 -0.0853 -0.0570 0.0181  1   SER   B CA  
4206 C C   A SER   B 1   ? 0.3272 0.3344 0.3746 -0.1071 -0.0569 0.0702  1   SER   B C   
4207 C C   B SER   B 1   ? 0.3658 0.3408 0.3477 -0.0815 -0.0628 0.0420  1   SER   B C   
4208 O O   A SER   B 1   ? 0.3312 0.3344 0.3602 -0.1037 -0.0610 0.0667  1   SER   B O   
4209 O O   B SER   B 1   ? 0.3668 0.3370 0.3257 -0.0796 -0.0694 0.0420  1   SER   B O   
4210 C CB  A SER   B 1   ? 0.3588 0.3458 0.4058 -0.1073 -0.0421 0.0558  1   SER   B CB  
4211 C CB  B SER   B 1   ? 0.3920 0.3260 0.3629 -0.0878 -0.0496 -0.0034 1   SER   B CB  
4212 O OG  A SER   B 1   ? 0.3668 0.3501 0.4232 -0.1086 -0.0358 0.0544  1   SER   B OG  
4213 O OG  B SER   B 1   ? 0.4008 0.3262 0.3790 -0.0861 -0.0473 -0.0138 1   SER   B OG  
4228 N N   A MET   B 2   ? 0.3014 0.3210 0.3635 -0.1094 -0.0561 0.0909  2   MET   B N   
4229 N N   B MET   B 2   ? 0.3495 0.3492 0.3545 -0.0737 -0.0591 0.0714  2   MET   B N   
4230 C CA  A MET   B 2   ? 0.2843 0.3110 0.3616 -0.0975 -0.0579 0.0975  2   MET   B CA  
4231 C CA  B MET   B 2   ? 0.3377 0.3562 0.3673 -0.0571 -0.0533 0.0866  2   MET   B CA  
4232 C C   A MET   B 2   ? 0.2457 0.2771 0.3105 -0.0947 -0.0713 0.1138  2   MET   B C   
4233 C C   B MET   B 2   ? 0.3080 0.3325 0.3295 -0.0459 -0.0506 0.1053  2   MET   B C   
4234 O O   A MET   B 2   ? 0.2311 0.2720 0.2891 -0.0989 -0.0858 0.1239  2   MET   B O   
4235 O O   B MET   B 2   ? 0.3089 0.3394 0.3348 -0.0406 -0.0457 0.1181  2   MET   B O   
4236 C CB  A MET   B 2   ? 0.3127 0.3394 0.4193 -0.0764 -0.0484 0.0796  2   MET   B CB  
4237 C CB  B MET   B 2   ? 0.3611 0.3870 0.4269 -0.0439 -0.0519 0.0778  2   MET   B CB  
4238 C CG  A MET   B 2   ? 0.3376 0.3634 0.4753 -0.0578 -0.0365 0.0698  2   MET   B CG  
4239 C CG  B MET   B 2   ? 0.3819 0.4141 0.4858 -0.0319 -0.0462 0.0746  2   MET   B CG  
4240 S SD  A MET   B 2   ? 0.3588 0.3842 0.5268 -0.0440 -0.0277 0.0611  2   MET   B SD  
4241 S SD  B MET   B 2   ? 0.4005 0.4393 0.5386 -0.0224 -0.0405 0.0706  2   MET   B SD  
4242 C CE  A MET   B 2   ? 0.3612 0.3881 0.5256 -0.0407 -0.0231 0.0616  2   MET   B CE  
4243 C CE  B MET   B 2   ? 0.4006 0.4448 0.5400 -0.0206 -0.0384 0.0683  2   MET   B CE  
4262 N N   A VAL   B 3   ? 0.2222 0.2407 0.2874 -0.0991 -0.0669 0.1152  3   VAL   B N   
4263 N N   B VAL   B 3   ? 0.2761 0.2969 0.2964 -0.0496 -0.0483 0.1014  3   VAL   B N   
4264 C CA  A VAL   B 3   ? 0.2156 0.2133 0.2741 -0.0865 -0.0650 0.0954  3   VAL   B CA  
4265 C CA  B VAL   B 3   ? 0.2523 0.2615 0.2770 -0.0479 -0.0482 0.0807  3   VAL   B CA  
4266 C C   A VAL   B 3   ? 0.2014 0.2052 0.2466 -0.0682 -0.0623 0.0917  3   VAL   B C   
4267 C C   B VAL   B 3   ? 0.2200 0.2368 0.2461 -0.0475 -0.0467 0.0811  3   VAL   B C   
4268 O O   A VAL   B 3   ? 0.1967 0.2009 0.2553 -0.0688 -0.0627 0.1021  3   VAL   B O   
4269 O O   B VAL   B 3   ? 0.2167 0.2472 0.2534 -0.0401 -0.0448 0.0818  3   VAL   B O   
4270 C CB  A VAL   B 3   ? 0.2295 0.2066 0.2951 -0.0816 -0.0613 0.0820  3   VAL   B CB  
4271 C CB  B VAL   B 3   ? 0.2661 0.2555 0.2927 -0.0453 -0.0463 0.0692  3   VAL   B CB  
4272 C CG1 A VAL   B 3   ? 0.2332 0.2005 0.3054 -0.0814 -0.0613 0.0808  3   VAL   B CG1 
4273 C CG1 B VAL   B 3   ? 0.2698 0.2520 0.2985 -0.0450 -0.0485 0.0672  3   VAL   B CG1 
4274 C CG2 A VAL   B 3   ? 0.2322 0.2067 0.3058 -0.0813 -0.0554 0.0835  3   VAL   B CG2 
4275 C CG2 B VAL   B 3   ? 0.2706 0.2547 0.3017 -0.0434 -0.0432 0.0706  3   VAL   B CG2 
4294 N N   . ASN   B 4   ? 0.1971 0.2043 0.2314 -0.0535 -0.0515 0.0810  4   ASN   B N   
4295 C CA  . ASN   B 4   ? 0.1922 0.2025 0.2007 -0.0576 -0.0401 0.0450  4   ASN   B CA  
4296 C C   . ASN   B 4   ? 0.2037 0.2114 0.2026 -0.0596 -0.0238 0.0269  4   ASN   B C   
4297 O O   . ASN   B 4   ? 0.2039 0.2200 0.2330 -0.0538 -0.0179 0.0090  4   ASN   B O   
4298 C CB  . ASN   B 4   ? 0.1916 0.1960 0.1970 -0.0467 -0.0476 0.0347  4   ASN   B CB  
4299 C CG  . ASN   B 4   ? 0.1838 0.1766 0.1929 -0.0413 -0.0350 0.0280  4   ASN   B CG  
4300 O OD1 . ASN   B 4   ? 0.1710 0.1648 0.1977 -0.0403 -0.0399 0.0207  4   ASN   B OD1 
4301 N ND2 . ASN   B 4   ? 0.2070 0.1853 0.2002 -0.0224 -0.0274 0.0292  4   ASN   B ND2 
4309 N N   . SER   B 5   ? 0.2283 0.2266 0.2274 -0.0584 0.0021  0.0270  5   SER   B N   
4310 C CA  . SER   B 5   ? 0.2596 0.2606 0.2574 -0.0439 0.0260  0.0363  5   SER   B CA  
4311 C C   . SER   B 5   ? 0.2664 0.2577 0.2843 -0.0558 0.0465  0.0322  5   SER   B C   
4312 O O   . SER   B 5   ? 0.2758 0.2597 0.3474 -0.0543 0.0663  0.0320  5   SER   B O   
4313 C CB  . SER   B 5   ? 0.2789 0.2890 0.2922 -0.0361 0.0272  0.0434  5   SER   B CB  
4314 O OG  . SER   B 5   ? 0.3022 0.3155 0.3441 -0.0276 0.0265  0.0446  5   SER   B OG  
4320 N N   . PHE   B 6   ? 0.2719 0.2618 0.2450 -0.0576 0.0533  0.0312  6   PHE   B N   
4321 C CA  . PHE   B 6   ? 0.2734 0.2600 0.2057 -0.0726 0.0457  0.0198  6   PHE   B CA  
4322 C C   . PHE   B 6   ? 0.3197 0.2855 0.2361 -0.0700 0.0571  -0.0058 6   PHE   B C   
4323 O O   . PHE   B 6   ? 0.3359 0.3177 0.2797 -0.0605 0.0360  -0.0245 6   PHE   B O   
4324 C CB  . PHE   B 6   ? 0.2423 0.2436 0.1963 -0.0662 0.0157  0.0193  6   PHE   B CB  
4325 C CG  . PHE   B 6   ? 0.2052 0.2183 0.1882 -0.0611 0.0061  0.0160  6   PHE   B CG  
4326 C CD1 . PHE   B 6   ? 0.1976 0.1954 0.1809 -0.0570 -0.0108 0.0148  6   PHE   B CD1 
4327 C CD2 . PHE   B 6   ? 0.1856 0.2189 0.1877 -0.0449 0.0087  0.0265  6   PHE   B CD2 
4328 C CE1 . PHE   B 6   ? 0.1955 0.1804 0.1921 -0.0399 -0.0033 0.0019  6   PHE   B CE1 
4329 C CE2 . PHE   B 6   ? 0.1839 0.2048 0.2218 -0.0329 0.0091  0.0300  6   PHE   B CE2 
4330 C CZ  . PHE   B 6   ? 0.1897 0.1831 0.2156 -0.0341 0.0091  0.0079  6   PHE   B CZ  
4340 N N   A SER   B 7   ? 0.3321 0.2741 0.2413 -0.0775 0.0680  -0.0191 7   SER   B N   
4341 N N   B SER   B 7   ? 0.3363 0.2728 0.2371 -0.0787 0.0744  -0.0147 7   SER   B N   
4342 C CA  A SER   B 7   ? 0.3448 0.2707 0.2560 -0.0755 0.0740  -0.0271 7   SER   B CA  
4343 C CA  B SER   B 7   ? 0.3541 0.2731 0.2531 -0.0726 0.0839  -0.0157 7   SER   B CA  
4344 C C   A SER   B 7   ? 0.3401 0.2555 0.2442 -0.0800 0.0771  -0.0294 7   SER   B C   
4345 C C   B SER   B 7   ? 0.3494 0.2611 0.2353 -0.0763 0.0871  -0.0185 7   SER   B C   
4346 O O   A SER   B 7   ? 0.3422 0.2552 0.2589 -0.0811 0.0768  -0.0253 7   SER   B O   
4347 O O   B SER   B 7   ? 0.3534 0.2631 0.2574 -0.0758 0.0869  -0.0103 7   SER   B O   
4348 C CB  A SER   B 7   ? 0.3574 0.2814 0.2898 -0.0696 0.0788  -0.0314 7   SER   B CB  
4349 C CB  B SER   B 7   ? 0.3700 0.2838 0.2917 -0.0637 0.0908  -0.0171 7   SER   B CB  
4350 O OG  A SER   B 7   ? 0.3651 0.2927 0.3220 -0.0662 0.0759  -0.0325 7   SER   B OG  
4351 O OG  B SER   B 7   ? 0.3799 0.2949 0.3335 -0.0580 0.0858  -0.0181 7   SER   B OG  
4362 N N   A GLY   B 8   ? 0.3377 0.2425 0.2442 -0.0749 0.0761  -0.0349 8   GLY   B N   
4363 N N   B GLY   B 8   ? 0.3458 0.2494 0.2399 -0.0698 0.0827  -0.0293 8   GLY   B N   
4364 C CA  A GLY   B 8   ? 0.3290 0.2294 0.2460 -0.0717 0.0778  -0.0370 8   GLY   B CA  
4365 C CA  B GLY   B 8   ? 0.3331 0.2358 0.2412 -0.0680 0.0817  -0.0360 8   GLY   B CA  
4366 C C   A GLY   B 8   ? 0.3188 0.2125 0.2401 -0.0715 0.0767  -0.0348 8   GLY   B C   
4367 C C   B GLY   B 8   ? 0.3182 0.2172 0.2340 -0.0717 0.0745  -0.0352 8   GLY   B C   
4368 O O   A GLY   B 8   ? 0.3217 0.2073 0.2557 -0.0743 0.0825  -0.0365 8   GLY   B O   
4369 O O   B GLY   B 8   ? 0.3208 0.2222 0.2425 -0.0697 0.0761  -0.0376 8   GLY   B O   
4376 N N   . TYR   B 9   ? 0.3072 0.2048 0.2286 -0.0652 0.0662  -0.0365 9   TYR   B N   
4377 C CA  . TYR   B 9   ? 0.2842 0.1836 0.1957 -0.0412 0.0422  -0.0277 9   TYR   B CA  
4378 C C   . TYR   B 9   ? 0.2732 0.1898 0.1890 -0.0351 0.0030  -0.0091 9   TYR   B C   
4379 O O   . TYR   B 9   ? 0.2919 0.2199 0.2300 -0.0401 0.0039  0.0010  9   TYR   B O   
4380 C CB  . TYR   B 9   ? 0.2813 0.1624 0.2107 -0.0312 0.0512  -0.0157 9   TYR   B CB  
4381 C CG  . TYR   B 9   ? 0.2740 0.1477 0.2245 -0.0438 0.0469  -0.0241 9   TYR   B CG  
4382 C CD1 . TYR   B 9   ? 0.2812 0.1517 0.2332 -0.0595 0.0509  -0.0272 9   TYR   B CD1 
4383 C CD2 . TYR   B 9   ? 0.2599 0.1378 0.2265 -0.0429 0.0484  -0.0331 9   TYR   B CD2 
4384 C CE1 . TYR   B 9   ? 0.2757 0.1555 0.2419 -0.0694 0.0557  -0.0359 9   TYR   B CE1 
4385 C CE2 . TYR   B 9   ? 0.2613 0.1425 0.2320 -0.0411 0.0539  -0.0307 9   TYR   B CE2 
4386 C CZ  . TYR   B 9   ? 0.2697 0.1603 0.2444 -0.0575 0.0579  -0.0431 9   TYR   B CZ  
4387 O OH  . TYR   B 9   ? 0.2710 0.1763 0.2606 -0.0694 0.0509  -0.0550 9   TYR   B OH  
4398 N N   A LEU   B 10  ? 0.2639 0.1759 0.1785 -0.0360 -0.0095 -0.0115 10  LEU   B N   
4399 N N   B LEU   B 10  ? 0.2548 0.1674 0.1766 -0.0356 -0.0083 -0.0135 10  LEU   B N   
4400 C CA  A LEU   B 10  ? 0.2591 0.1708 0.1831 -0.0380 -0.0230 -0.0134 10  LEU   B CA  
4401 C CA  B LEU   B 10  ? 0.2439 0.1595 0.1819 -0.0395 -0.0207 -0.0164 10  LEU   B CA  
4402 C C   A LEU   B 10  ? 0.2427 0.1675 0.1830 -0.0353 -0.0291 -0.0111 10  LEU   B C   
4403 C C   B LEU   B 10  ? 0.2288 0.1569 0.1818 -0.0378 -0.0294 -0.0105 10  LEU   B C   
4404 O O   A LEU   B 10  ? 0.2399 0.1662 0.1772 -0.0296 -0.0209 -0.0061 10  LEU   B O   
4405 O O   B LEU   B 10  ? 0.2212 0.1536 0.1772 -0.0291 -0.0183 -0.0041 10  LEU   B O   
4406 C CB  A LEU   B 10  ? 0.2738 0.1713 0.2044 -0.0390 -0.0306 -0.0076 10  LEU   B CB  
4407 C CB  B LEU   B 10  ? 0.2543 0.1588 0.2074 -0.0403 -0.0264 -0.0089 10  LEU   B CB  
4408 C CG  A LEU   B 10  ? 0.2855 0.1756 0.2230 -0.0380 -0.0430 -0.0022 10  LEU   B CG  
4409 C CG  B LEU   B 10  ? 0.2594 0.1657 0.2270 -0.0388 -0.0412 -0.0005 10  LEU   B CG  
4410 C CD1 A LEU   B 10  ? 0.2911 0.1814 0.2303 -0.0361 -0.0450 -0.0037 10  LEU   B CD1 
4411 C CD1 B LEU   B 10  ? 0.2589 0.1783 0.2348 -0.0398 -0.0447 -0.0050 10  LEU   B CD1 
4412 C CD2 A LEU   B 10  ? 0.2924 0.1793 0.2418 -0.0372 -0.0456 0.0050  10  LEU   B CD2 
4413 C CD2 B LEU   B 10  ? 0.2721 0.1705 0.2550 -0.0378 -0.0455 0.0097  10  LEU   B CD2 
4436 N N   . LYS   B 11  ? 0.2381 0.1762 0.1989 -0.0289 -0.0348 -0.0166 11  LYS   B N   
4437 C CA  . LYS   B 11  ? 0.2529 0.2123 0.2137 -0.0220 -0.0438 -0.0137 11  LYS   B CA  
4438 C C   . LYS   B 11  ? 0.2429 0.1972 0.2255 -0.0479 -0.0394 -0.0207 11  LYS   B C   
4439 O O   . LYS   B 11  ? 0.2582 0.2168 0.2511 -0.0678 -0.0309 -0.0582 11  LYS   B O   
4440 C CB  . LYS   B 11  ? 0.2852 0.2701 0.2553 0.0028  -0.0435 0.0022  11  LYS   B CB  
4441 C CG  . LYS   B 11  ? 0.3158 0.3076 0.3082 0.0187  -0.0369 0.0025  11  LYS   B CG  
4442 C CD  . LYS   B 11  ? 0.3399 0.3342 0.3700 0.0278  -0.0288 -0.0059 11  LYS   B CD  
4443 C CE  . LYS   B 11  ? 0.3572 0.3493 0.4159 0.0286  -0.0189 -0.0091 11  LYS   B CE  
4444 N NZ  . LYS   B 11  ? 0.3679 0.3581 0.4447 0.0273  -0.0104 -0.0115 11  LYS   B NZ  
4459 N N   . LEU   B 12  ? 0.2182 0.1734 0.2237 -0.0458 -0.0396 -0.0227 12  LEU   B N   
4460 C CA  . LEU   B 12  ? 0.2040 0.1631 0.2363 -0.0454 -0.0347 -0.0297 12  LEU   B CA  
4461 C C   . LEU   B 12  ? 0.1944 0.1660 0.2511 -0.0435 -0.0415 -0.0262 12  LEU   B C   
4462 O O   . LEU   B 12  ? 0.1920 0.1731 0.2801 -0.0510 -0.0461 -0.0177 12  LEU   B O   
4463 C CB  . LEU   B 12  ? 0.2048 0.1458 0.2398 -0.0317 -0.0188 -0.0259 12  LEU   B CB  
4464 C CG  . LEU   B 12  ? 0.2073 0.1367 0.2505 -0.0311 -0.0150 -0.0241 12  LEU   B CG  
4465 C CD1 . LEU   B 12  ? 0.2163 0.1475 0.2429 -0.0173 -0.0162 -0.0087 12  LEU   B CD1 
4466 C CD2 . LEU   B 12  ? 0.2183 0.1436 0.2631 -0.0297 -0.0161 -0.0289 12  LEU   B CD2 
4478 N N   . THR   B 13  ? 0.1896 0.1673 0.2559 -0.0415 -0.0421 -0.0292 13  THR   B N   
4479 C CA  . THR   B 13  ? 0.1928 0.1684 0.2412 -0.0495 -0.0504 -0.0207 13  THR   B CA  
4480 C C   . THR   B 13  ? 0.2281 0.1853 0.2542 -0.0535 -0.0595 -0.0128 13  THR   B C   
4481 O O   . THR   B 13  ? 0.2435 0.1858 0.2765 -0.0523 -0.0182 -0.0212 13  THR   B O   
4482 C CB  . THR   B 13  ? 0.1829 0.1739 0.2543 -0.0446 -0.0508 -0.0183 13  THR   B CB  
4483 O OG1 . THR   B 13  ? 0.1749 0.1684 0.2595 -0.0405 -0.0469 -0.0182 13  THR   B OG1 
4484 C CG2 . THR   B 13  ? 0.1989 0.1767 0.2616 -0.0373 -0.0396 -0.0178 13  THR   B CG2 
4492 N N   A ASP   B 14  ? 0.2391 0.1970 0.2645 -0.0570 -0.0766 -0.0089 14  ASP   B N   
4493 N N   B ASP   B 14  ? 0.2426 0.2007 0.2611 -0.0552 -0.0809 -0.0073 14  ASP   B N   
4494 C CA  A ASP   B 14  ? 0.2501 0.2137 0.2857 -0.0574 -0.0814 0.0041  14  ASP   B CA  
4495 C CA  B ASP   B 14  ? 0.2585 0.2241 0.2808 -0.0522 -0.0832 0.0107  14  ASP   B CA  
4496 C C   A ASP   B 14  ? 0.2400 0.2004 0.2610 -0.0552 -0.0704 0.0113  14  ASP   B C   
4497 C C   B ASP   B 14  ? 0.2464 0.2078 0.2597 -0.0533 -0.0703 0.0159  14  ASP   B C   
4498 O O   A ASP   B 14  ? 0.2590 0.2150 0.2655 -0.0575 -0.0715 0.0184  14  ASP   B O   
4499 O O   B ASP   B 14  ? 0.2707 0.2277 0.2682 -0.0560 -0.0721 0.0273  14  ASP   B O   
4500 C CB  A ASP   B 14  ? 0.2655 0.2403 0.3367 -0.0613 -0.0925 0.0056  14  ASP   B CB  
4501 C CB  B ASP   B 14  ? 0.2806 0.2598 0.3289 -0.0494 -0.0909 0.0157  14  ASP   B CB  
4502 C CG  A ASP   B 14  ? 0.2838 0.2644 0.3869 -0.0632 -0.0904 0.0013  14  ASP   B CG  
4503 C CG  B ASP   B 14  ? 0.3070 0.2950 0.3804 -0.0454 -0.0813 0.0104  14  ASP   B CG  
4504 O OD1 A ASP   B 14  ? 0.2895 0.2693 0.3927 -0.0720 -0.0941 -0.0052 14  ASP   B OD1 
4505 O OD1 B ASP   B 14  ? 0.3181 0.3036 0.3853 -0.0464 -0.0781 0.0028  14  ASP   B OD1 
4506 O OD2 A ASP   B 14  ? 0.2924 0.2750 0.4202 -0.0626 -0.0832 0.0040  14  ASP   B OD2 
4507 O OD2 B ASP   B 14  ? 0.3177 0.3142 0.4168 -0.0468 -0.0748 0.0138  14  ASP   B OD2 
4516 N N   . ASN   B 15  ? 0.2117 0.1740 0.2410 -0.0471 -0.0671 0.0133  15  ASN   B N   
4517 C CA  . ASN   B 15  ? 0.1685 0.1515 0.2232 -0.0287 -0.0428 0.0063  15  ASN   B CA  
4518 C C   . ASN   B 15  ? 0.1472 0.1399 0.2211 -0.0148 -0.0339 0.0001  15  ASN   B C   
4519 O O   . ASN   B 15  ? 0.1470 0.1385 0.2453 -0.0204 -0.0508 -0.0114 15  ASN   B O   
4520 C CB  . ASN   B 15  ? 0.1591 0.1530 0.2241 -0.0071 -0.0446 0.0006  15  ASN   B CB  
4521 C CG  . ASN   B 15  ? 0.1440 0.1479 0.2459 -0.0145 -0.0254 0.0086  15  ASN   B CG  
4522 O OD1 . ASN   B 15  ? 0.1513 0.1755 0.2740 -0.0340 -0.0272 0.0124  15  ASN   B OD1 
4523 N ND2 . ASN   B 15  ? 0.1566 0.1249 0.2465 -0.0157 -0.0072 -0.0059 15  ASN   B ND2 
4531 N N   . VAL   B 16  ? 0.1551 0.1290 0.2244 -0.0244 -0.0411 -0.0027 16  VAL   B N   
4532 C CA  . VAL   B 16  ? 0.1536 0.1265 0.2045 -0.0226 -0.0351 -0.0141 16  VAL   B CA  
4533 C C   . VAL   B 16  ? 0.1499 0.1357 0.2019 -0.0248 -0.0382 -0.0126 16  VAL   B C   
4534 O O   . VAL   B 16  ? 0.1580 0.1523 0.2272 -0.0233 -0.0329 -0.0260 16  VAL   B O   
4535 C CB  . VAL   B 16  ? 0.1598 0.1282 0.2079 -0.0093 -0.0276 -0.0148 16  VAL   B CB  
4536 C CG1 . VAL   B 16  ? 0.1707 0.1348 0.2132 0.0031  -0.0230 -0.0075 16  VAL   B CG1 
4537 C CG2 . VAL   B 16  ? 0.1629 0.1335 0.2256 -0.0084 -0.0256 -0.0134 16  VAL   B CG2 
4547 N N   . TYR   B 17  ? 0.1566 0.1390 0.1992 -0.0182 -0.0272 -0.0106 17  TYR   B N   
4548 C CA  . TYR   B 17  ? 0.1645 0.1489 0.1889 -0.0212 -0.0224 0.0011  17  TYR   B CA  
4549 C C   . TYR   B 17  ? 0.1559 0.1327 0.1942 -0.0307 -0.0150 -0.0034 17  TYR   B C   
4550 O O   . TYR   B 17  ? 0.1601 0.1364 0.2101 -0.0242 -0.0297 -0.0230 17  TYR   B O   
4551 C CB  . TYR   B 17  ? 0.1936 0.1827 0.1965 -0.0075 -0.0186 0.0255  17  TYR   B CB  
4552 C CG  . TYR   B 17  ? 0.2237 0.2229 0.2177 -0.0002 -0.0217 0.0253  17  TYR   B CG  
4553 C CD1 . TYR   B 17  ? 0.2421 0.2345 0.2239 0.0071  -0.0297 0.0317  17  TYR   B CD1 
4554 C CD2 . TYR   B 17  ? 0.2500 0.2509 0.2285 0.0028  -0.0245 0.0185  17  TYR   B CD2 
4555 C CE1 . TYR   B 17  ? 0.2625 0.2603 0.2343 0.0171  -0.0309 0.0237  17  TYR   B CE1 
4556 C CE2 . TYR   B 17  ? 0.2673 0.2723 0.2389 0.0155  -0.0327 0.0188  17  TYR   B CE2 
4557 C CZ  . TYR   B 17  ? 0.2757 0.2783 0.2397 0.0246  -0.0427 0.0234  17  TYR   B CZ  
4558 O OH  . TYR   B 17  ? 0.2957 0.2974 0.2585 0.0372  -0.0490 0.0265  17  TYR   B OH  
4568 N N   . ILE   B 18  ? 0.1614 0.1356 0.1809 -0.0259 -0.0098 -0.0179 18  ILE   B N   
4569 C CA  . ILE   B 18  ? 0.1680 0.1293 0.1863 -0.0199 -0.0157 -0.0095 18  ILE   B CA  
4570 C C   . ILE   B 18  ? 0.1799 0.1311 0.1853 -0.0283 -0.0166 -0.0151 18  ILE   B C   
4571 O O   . ILE   B 18  ? 0.1966 0.1477 0.2033 -0.0251 -0.0044 -0.0229 18  ILE   B O   
4572 C CB  . ILE   B 18  ? 0.1705 0.1312 0.1882 -0.0341 -0.0118 -0.0116 18  ILE   B CB  
4573 C CG1 . ILE   B 18  ? 0.1831 0.1355 0.2059 -0.0331 -0.0098 0.0011  18  ILE   B CG1 
4574 C CG2 . ILE   B 18  ? 0.1808 0.1466 0.2026 -0.0409 -0.0139 -0.0042 18  ILE   B CG2 
4575 C CD1 . ILE   B 18  ? 0.1923 0.1689 0.2353 -0.0335 -0.0276 0.0161  18  ILE   B CD1 
4587 N N   . LYS   B 19  ? 0.1808 0.1321 0.1977 -0.0153 0.0078  -0.0204 19  LYS   B N   
4588 C CA  . LYS   B 19  ? 0.1844 0.1397 0.2008 -0.0212 0.0099  -0.0190 19  LYS   B CA  
4589 C C   . LYS   B 19  ? 0.1723 0.1362 0.2047 -0.0133 0.0211  -0.0177 19  LYS   B C   
4590 O O   . LYS   B 19  ? 0.1734 0.1414 0.2026 -0.0105 0.0104  -0.0218 19  LYS   B O   
4591 C CB  . LYS   B 19  ? 0.2046 0.1569 0.2121 -0.0138 0.0142  -0.0203 19  LYS   B CB  
4592 C CG  . LYS   B 19  ? 0.2279 0.1776 0.2226 -0.0177 0.0247  -0.0181 19  LYS   B CG  
4593 C CD  . LYS   B 19  ? 0.2545 0.2059 0.2196 -0.0325 0.0316  0.0000  19  LYS   B CD  
4594 C CE  . LYS   B 19  ? 0.2749 0.2320 0.2418 -0.0402 0.0276  0.0001  19  LYS   B CE  
4595 N NZ  . LYS   B 19  ? 0.2887 0.2473 0.2599 -0.0476 0.0298  -0.0001 19  LYS   B NZ  
4609 N N   . ASN   B 20  ? 0.1673 0.1456 0.2278 -0.0079 0.0228  -0.0325 20  ASN   B N   
4610 C CA  . ASN   B 20  ? 0.1697 0.1576 0.2465 -0.0047 0.0255  -0.0420 20  ASN   B CA  
4611 C C   . ASN   B 20  ? 0.1689 0.1773 0.2548 -0.0122 0.0364  -0.0482 20  ASN   B C   
4612 O O   . ASN   B 20  ? 0.1796 0.2137 0.2878 -0.0249 0.0453  -0.0483 20  ASN   B O   
4613 C CB  . ASN   B 20  ? 0.1958 0.1547 0.2521 0.0040  0.0162  -0.0423 20  ASN   B CB  
4614 C CG  . ASN   B 20  ? 0.2242 0.1589 0.2774 0.0331  0.0125  -0.0454 20  ASN   B CG  
4615 O OD1 . ASN   B 20  ? 0.2540 0.1942 0.3068 0.0585  0.0101  -0.0564 20  ASN   B OD1 
4616 N ND2 . ASN   B 20  ? 0.2216 0.1626 0.2741 0.0244  -0.0003 -0.0402 20  ASN   B ND2 
4623 N N   . ALA   B 21  ? 0.1773 0.1607 0.2384 -0.0204 0.0335  -0.0355 21  ALA   B N   
4624 C CA  . ALA   B 21  ? 0.1870 0.1715 0.2565 -0.0311 0.0324  -0.0223 21  ALA   B CA  
4625 C C   . ALA   B 21  ? 0.1807 0.1514 0.2537 -0.0223 0.0297  -0.0237 21  ALA   B C   
4626 O O   . ALA   B 21  ? 0.1859 0.1445 0.2605 -0.0283 0.0257  -0.0219 21  ALA   B O   
4627 C CB  . ALA   B 21  ? 0.2015 0.1962 0.2620 -0.0422 0.0241  0.0011  21  ALA   B CB  
4633 N N   . ASP   B 22  ? 0.1687 0.1405 0.2489 -0.0225 0.0193  -0.0152 22  ASP   B N   
4634 C CA  . ASP   B 22  ? 0.1653 0.1352 0.2484 -0.0095 0.0121  -0.0119 22  ASP   B CA  
4635 C C   . ASP   B 22  ? 0.1624 0.1359 0.2165 -0.0099 0.0089  0.0022  22  ASP   B C   
4636 O O   . ASP   B 22  ? 0.1704 0.1367 0.2295 -0.0088 0.0122  0.0101  22  ASP   B O   
4637 C CB  . ASP   B 22  ? 0.1785 0.1458 0.2802 -0.0094 0.0147  -0.0013 22  ASP   B CB  
4638 C CG  . ASP   B 22  ? 0.1840 0.1607 0.3123 0.0030  -0.0087 0.0050  22  ASP   B CG  
4639 O OD1 . ASP   B 22  ? 0.2010 0.1631 0.3114 0.0044  -0.0195 -0.0010 22  ASP   B OD1 
4640 O OD2 . ASP   B 22  ? 0.1951 0.1872 0.3578 0.0128  -0.0326 -0.0150 22  ASP   B OD2 
4645 N N   . ILE   B 23  ? 0.1697 0.1326 0.2027 -0.0108 0.0025  0.0188  23  ILE   B N   
4646 C CA  . ILE   B 23  ? 0.1599 0.1374 0.2029 -0.0080 -0.0046 0.0068  23  ILE   B CA  
4647 C C   . ILE   B 23  ? 0.1555 0.1353 0.2032 -0.0034 -0.0093 -0.0005 23  ILE   B C   
4648 O O   . ILE   B 23  ? 0.1491 0.1287 0.2078 -0.0040 -0.0156 0.0039  23  ILE   B O   
4649 C CB  . ILE   B 23  ? 0.1580 0.1446 0.2161 -0.0182 0.0045  0.0144  23  ILE   B CB  
4650 C CG1 . ILE   B 23  ? 0.1605 0.1564 0.2269 -0.0159 0.0092  0.0339  23  ILE   B CG1 
4651 C CG2 . ILE   B 23  ? 0.1660 0.1609 0.2352 -0.0215 0.0069  0.0091  23  ILE   B CG2 
4652 C CD1 . ILE   B 23  ? 0.1669 0.1665 0.2389 -0.0069 0.0059  0.0224  23  ILE   B CD1 
4664 N N   . VAL   B 24  ? 0.1565 0.1383 0.1994 -0.0100 -0.0100 0.0022  24  VAL   B N   
4665 C CA  . VAL   B 24  ? 0.1504 0.1450 0.2298 -0.0098 -0.0113 -0.0022 24  VAL   B CA  
4666 C C   . VAL   B 24  ? 0.1477 0.1381 0.2365 -0.0108 -0.0105 0.0047  24  VAL   B C   
4667 O O   . VAL   B 24  ? 0.1449 0.1415 0.2505 -0.0142 -0.0045 0.0193  24  VAL   B O   
4668 C CB  . VAL   B 24  ? 0.1611 0.1642 0.2310 -0.0046 -0.0245 0.0043  24  VAL   B CB  
4669 C CG1 . VAL   B 24  ? 0.1550 0.1620 0.2495 -0.0132 -0.0197 0.0002  24  VAL   B CG1 
4670 C CG2 . VAL   B 24  ? 0.1692 0.1965 0.2388 0.0049  -0.0206 -0.0038 24  VAL   B CG2 
4680 N N   . GLU   B 25  ? 0.1745 0.1488 0.2495 -0.0089 -0.0078 0.0125  25  GLU   B N   
4681 C CA  . GLU   B 25  ? 0.1818 0.1771 0.2596 0.0008  0.0001  0.0085  25  GLU   B CA  
4682 C C   . GLU   B 25  ? 0.1747 0.1663 0.2318 -0.0087 0.0087  0.0088  25  GLU   B C   
4683 O O   . GLU   B 25  ? 0.1779 0.1740 0.2435 -0.0099 0.0131  0.0245  25  GLU   B O   
4684 C CB  . GLU   B 25  ? 0.2201 0.2336 0.3043 0.0249  0.0012  0.0155  25  GLU   B CB  
4685 C CG  . GLU   B 25  ? 0.2607 0.3066 0.3980 0.0381  0.0060  0.0099  25  GLU   B CG  
4686 C CD  . GLU   B 25  ? 0.3109 0.3683 0.4891 0.0364  0.0116  0.0042  25  GLU   B CD  
4687 O OE1 . GLU   B 25  ? 0.3245 0.3886 0.5218 0.0411  0.0197  0.0030  25  GLU   B OE1 
4688 O OE2 . GLU   B 25  ? 0.3227 0.3888 0.5293 0.0337  0.0101  -0.0006 25  GLU   B OE2 
4695 N N   . GLU   B 26  ? 0.1697 0.1575 0.1986 -0.0240 0.0039  0.0121  26  GLU   B N   
4696 C CA  . GLU   B 26  ? 0.1703 0.1750 0.2056 -0.0358 -0.0042 0.0194  26  GLU   B CA  
4697 C C   . GLU   B 26  ? 0.1592 0.1742 0.2038 -0.0220 0.0056  0.0267  26  GLU   B C   
4698 O O   . GLU   B 26  ? 0.1751 0.1966 0.2101 -0.0132 0.0015  0.0351  26  GLU   B O   
4699 C CB  . GLU   B 26  ? 0.2061 0.1998 0.2228 -0.0461 -0.0042 0.0247  26  GLU   B CB  
4700 C CG  . GLU   B 26  ? 0.2479 0.2305 0.2595 -0.0554 0.0005  0.0100  26  GLU   B CG  
4701 C CD  . GLU   B 26  ? 0.2775 0.2523 0.2624 -0.0773 0.0140  -0.0205 26  GLU   B CD  
4702 O OE1 . GLU   B 26  ? 0.2990 0.2320 0.2706 -0.0879 0.0460  -0.0136 26  GLU   B OE1 
4703 O OE2 . GLU   B 26  ? 0.2776 0.2907 0.2943 -0.0723 0.0074  -0.0226 26  GLU   B OE2 
4710 N N   . ALA   B 27  ? 0.1453 0.1548 0.2136 -0.0153 0.0049  0.0269  27  ALA   B N   
4711 C CA  . ALA   B 27  ? 0.1557 0.1532 0.2334 -0.0109 0.0051  0.0363  27  ALA   B CA  
4712 C C   . ALA   B 27  ? 0.1576 0.1626 0.2535 -0.0082 0.0226  0.0441  27  ALA   B C   
4713 O O   . ALA   B 27  ? 0.1697 0.1655 0.2649 -0.0018 0.0191  0.0529  27  ALA   B O   
4714 C CB  . ALA   B 27  ? 0.1696 0.1451 0.2294 -0.0115 0.0041  0.0255  27  ALA   B CB  
4720 N N   A LYS   B 28  ? 0.1755 0.1926 0.2683 -0.0017 0.0249  0.0534  28  LYS   B N   
4721 N N   B LYS   B 28  ? 0.1401 0.1689 0.2794 -0.0169 0.0324  0.0616  28  LYS   B N   
4722 C CA  A LYS   B 28  ? 0.2061 0.2345 0.2832 0.0067  0.0343  0.0619  28  LYS   B CA  
4723 C CA  B LYS   B 28  ? 0.1528 0.2040 0.2957 -0.0134 0.0527  0.0787  28  LYS   B CA  
4724 C C   A LYS   B 28  ? 0.2276 0.2529 0.2751 0.0132  0.0429  0.0619  28  LYS   B C   
4725 C C   B LYS   B 28  ? 0.1772 0.2207 0.2812 0.0011  0.0648  0.0757  28  LYS   B C   
4726 O O   A LYS   B 28  ? 0.2385 0.2570 0.2744 0.0112  0.0433  0.0620  28  LYS   B O   
4727 O O   B LYS   B 28  ? 0.1988 0.2247 0.2841 -0.0023 0.0608  0.0751  28  LYS   B O   
4728 C CB  A LYS   B 28  ? 0.2227 0.2618 0.3139 0.0118  0.0392  0.0682  28  LYS   B CB  
4729 C CB  B LYS   B 28  ? 0.1641 0.2375 0.3288 -0.0099 0.0631  0.0929  28  LYS   B CB  
4730 C CG  A LYS   B 28  ? 0.2401 0.2876 0.3505 0.0183  0.0406  0.0716  28  LYS   B CG  
4731 C CG  B LYS   B 28  ? 0.1831 0.2728 0.3658 -0.0004 0.0626  0.1004  28  LYS   B CG  
4732 C CD  A LYS   B 28  ? 0.2577 0.3127 0.3864 0.0222  0.0488  0.0725  28  LYS   B CD  
4733 C CD  B LYS   B 28  ? 0.2085 0.3157 0.4030 0.0103  0.0744  0.0980  28  LYS   B CD  
4734 C CE  A LYS   B 28  ? 0.2720 0.3310 0.4162 0.0261  0.0509  0.0748  28  LYS   B CE  
4735 C CE  B LYS   B 28  ? 0.2306 0.3433 0.4362 0.0205  0.0735  0.0994  28  LYS   B CE  
4736 N NZ  A LYS   B 28  ? 0.2795 0.3409 0.4319 0.0293  0.0501  0.0778  28  LYS   B NZ  
4737 N NZ  B LYS   B 28  ? 0.2425 0.3527 0.4564 0.0291  0.0663  0.1045  28  LYS   B NZ  
4764 N N   A LYS   B 29  ? 0.2425 0.2700 0.2826 0.0226  0.0433  0.0565  29  LYS   B N   
4765 N N   B LYS   B 29  ? 0.1965 0.2448 0.2830 0.0249  0.0647  0.0636  29  LYS   B N   
4766 C CA  A LYS   B 29  ? 0.2629 0.2885 0.3001 0.0248  0.0398  0.0558  29  LYS   B CA  
4767 C CA  B LYS   B 29  ? 0.2344 0.2750 0.2985 0.0323  0.0533  0.0612  29  LYS   B CA  
4768 C C   A LYS   B 29  ? 0.2498 0.2822 0.2714 0.0245  0.0408  0.0681  29  LYS   B C   
4769 C C   B LYS   B 29  ? 0.2341 0.2781 0.2690 0.0289  0.0429  0.0692  29  LYS   B C   
4770 O O   A LYS   B 29  ? 0.2583 0.2906 0.2730 0.0270  0.0426  0.0705  29  LYS   B O   
4771 O O   B LYS   B 29  ? 0.2417 0.2940 0.2767 0.0296  0.0365  0.0647  29  LYS   B O   
4772 C CB  A LYS   B 29  ? 0.2972 0.3145 0.3584 0.0240  0.0327  0.0401  29  LYS   B CB  
4773 C CB  B LYS   B 29  ? 0.2781 0.3070 0.3614 0.0341  0.0442  0.0478  29  LYS   B CB  
4774 C CG  A LYS   B 29  ? 0.3231 0.3346 0.4144 0.0208  0.0310  0.0326  29  LYS   B CG  
4775 C CG  B LYS   B 29  ? 0.3123 0.3324 0.4215 0.0302  0.0418  0.0463  29  LYS   B CG  
4776 C CD  A LYS   B 29  ? 0.3420 0.3477 0.4617 0.0174  0.0333  0.0243  29  LYS   B CD  
4777 C CD  B LYS   B 29  ? 0.3368 0.3486 0.4740 0.0260  0.0442  0.0409  29  LYS   B CD  
4778 C CE  A LYS   B 29  ? 0.3549 0.3564 0.4956 0.0156  0.0348  0.0187  29  LYS   B CE  
4779 C CE  B LYS   B 29  ? 0.3542 0.3600 0.5107 0.0233  0.0483  0.0371  29  LYS   B CE  
4780 N NZ  A LYS   B 29  ? 0.3620 0.3611 0.5162 0.0153  0.0350  0.0158  29  LYS   B NZ  
4781 N NZ  B LYS   B 29  ? 0.3631 0.3681 0.5342 0.0235  0.0491  0.0342  29  LYS   B NZ  
4808 N N   . VAL   B 30  ? 0.2251 0.2662 0.2614 0.0155  0.0432  0.0730  30  VAL   B N   
4809 C CA  . VAL   B 30  ? 0.2103 0.2571 0.2874 0.0015  0.0131  0.0814  30  VAL   B CA  
4810 C C   . VAL   B 30  ? 0.1837 0.2470 0.2856 0.0016  0.0215  0.1031  30  VAL   B C   
4811 O O   . VAL   B 30  ? 0.1947 0.2655 0.2915 0.0077  0.0301  0.1215  30  VAL   B O   
4812 C CB  . VAL   B 30  ? 0.2221 0.2542 0.3176 -0.0143 -0.0182 0.0722  30  VAL   B CB  
4813 C CG1 . VAL   B 30  ? 0.2281 0.2618 0.3204 -0.0147 -0.0106 0.0654  30  VAL   B CG1 
4814 C CG2 . VAL   B 30  ? 0.2345 0.2595 0.3326 -0.0211 -0.0355 0.0537  30  VAL   B CG2 
4825 N N   . LYS   B 31  ? 0.1617 0.2107 0.3194 -0.0157 0.0143  0.0991  31  LYS   B N   
4826 C CA  . LYS   B 31  ? 0.1617 0.2052 0.3582 -0.0283 0.0090  0.1054  31  LYS   B CA  
4827 C C   . LYS   B 31  ? 0.1534 0.1747 0.3109 -0.0250 -0.0164 0.0827  31  LYS   B C   
4828 O O   . LYS   B 31  ? 0.1603 0.1934 0.3250 -0.0196 -0.0086 0.1008  31  LYS   B O   
4829 C CB  . LYS   B 31  ? 0.1726 0.2554 0.4172 -0.0255 0.0305  0.1256  31  LYS   B CB  
4830 C CG  . LYS   B 31  ? 0.2135 0.3048 0.4583 -0.0241 0.0458  0.1307  31  LYS   B CG  
4831 C CD  . LYS   B 31  ? 0.2586 0.3512 0.4913 -0.0159 0.0434  0.1245  31  LYS   B CD  
4832 C CE  . LYS   B 31  ? 0.2903 0.3806 0.5233 -0.0121 0.0383  0.1160  31  LYS   B CE  
4833 N NZ  . LYS   B 31  ? 0.3358 0.4011 0.5447 -0.0047 0.0290  0.1045  31  LYS   B NZ  
4847 N N   . PRO   B 32  ? 0.1633 0.1420 0.2500 -0.0249 -0.0362 0.0475  32  PRO   B N   
4848 C CA  . PRO   B 32  ? 0.1681 0.1383 0.2180 -0.0309 -0.0314 0.0352  32  PRO   B CA  
4849 C C   . PRO   B 32  ? 0.1772 0.1251 0.2175 -0.0299 -0.0465 0.0406  32  PRO   B C   
4850 O O   . PRO   B 32  ? 0.1910 0.1328 0.2460 -0.0365 -0.0719 0.0322  32  PRO   B O   
4851 C CB  . PRO   B 32  ? 0.1821 0.1384 0.2141 -0.0321 -0.0240 0.0126  32  PRO   B CB  
4852 C CG  . PRO   B 32  ? 0.1940 0.1328 0.2254 -0.0225 -0.0355 0.0225  32  PRO   B CG  
4853 C CD  . PRO   B 32  ? 0.1842 0.1314 0.2420 -0.0138 -0.0482 0.0251  32  PRO   B CD  
4861 N N   . THR   B 33  ? 0.1792 0.1246 0.2071 -0.0259 -0.0438 0.0280  33  THR   B N   
4862 C CA  . THR   B 33  ? 0.1859 0.1306 0.2068 -0.0272 -0.0417 0.0184  33  THR   B CA  
4863 C C   . THR   B 33  ? 0.1930 0.1181 0.1997 -0.0239 -0.0419 0.0183  33  THR   B C   
4864 O O   . THR   B 33  ? 0.2131 0.1212 0.2060 -0.0422 -0.0473 0.0207  33  THR   B O   
4865 C CB  . THR   B 33  ? 0.1965 0.1393 0.2139 -0.0130 -0.0503 0.0273  33  THR   B CB  
4866 O OG1 . THR   B 33  ? 0.1824 0.1465 0.2212 -0.0235 -0.0477 0.0348  33  THR   B OG1 
4867 C CG2 . THR   B 33  ? 0.2151 0.1430 0.2308 -0.0056 -0.0538 0.0126  33  THR   B CG2 
4875 N N   . VAL   B 34  ? 0.1749 0.1149 0.1921 -0.0251 -0.0362 0.0152  34  VAL   B N   
4876 C CA  . VAL   B 34  ? 0.1592 0.1152 0.1870 -0.0208 -0.0358 0.0155  34  VAL   B CA  
4877 C C   . VAL   B 34  ? 0.1490 0.1147 0.1637 -0.0212 -0.0144 0.0117  34  VAL   B C   
4878 O O   . VAL   B 34  ? 0.1648 0.1156 0.1754 -0.0252 -0.0340 0.0060  34  VAL   B O   
4879 C CB  . VAL   B 34  ? 0.1631 0.1261 0.2107 -0.0026 -0.0247 0.0052  34  VAL   B CB  
4880 C CG1 . VAL   B 34  ? 0.1603 0.1417 0.2211 -0.0079 -0.0167 -0.0057 34  VAL   B CG1 
4881 C CG2 . VAL   B 34  ? 0.1684 0.1377 0.2254 -0.0044 -0.0315 0.0005  34  VAL   B CG2 
4891 N N   . VAL   B 35  ? 0.1363 0.1138 0.1700 -0.0178 -0.0174 0.0134  35  VAL   B N   
4892 C CA  . VAL   B 35  ? 0.1326 0.1132 0.1747 -0.0161 -0.0058 0.0051  35  VAL   B CA  
4893 C C   . VAL   B 35  ? 0.1185 0.1063 0.1706 -0.0145 -0.0093 0.0077  35  VAL   B C   
4894 O O   . VAL   B 35  ? 0.1288 0.1110 0.1743 -0.0210 -0.0058 -0.0009 35  VAL   B O   
4895 C CB  . VAL   B 35  ? 0.1376 0.1262 0.1864 -0.0176 -0.0002 -0.0006 35  VAL   B CB  
4896 C CG1 . VAL   B 35  ? 0.1317 0.1314 0.2105 -0.0214 -0.0088 0.0068  35  VAL   B CG1 
4897 C CG2 . VAL   B 35  ? 0.1398 0.1317 0.1885 -0.0041 -0.0011 -0.0032 35  VAL   B CG2 
4907 N N   . VAL   B 36  ? 0.1210 0.1092 0.1747 -0.0166 -0.0160 0.0082  36  VAL   B N   
4908 C CA  . VAL   B 36  ? 0.1199 0.1028 0.1666 -0.0100 -0.0039 0.0043  36  VAL   B CA  
4909 C C   . VAL   B 36  ? 0.1156 0.0986 0.1595 -0.0127 -0.0046 0.0022  36  VAL   B C   
4910 O O   . VAL   B 36  ? 0.1219 0.1121 0.1829 -0.0090 -0.0073 -0.0047 36  VAL   B O   
4911 C CB  . VAL   B 36  ? 0.1221 0.1092 0.1738 -0.0142 -0.0059 0.0023  36  VAL   B CB  
4912 C CG1 . VAL   B 36  ? 0.1213 0.1220 0.1880 -0.0201 -0.0052 -0.0027 36  VAL   B CG1 
4913 C CG2 . VAL   B 36  ? 0.1213 0.1091 0.1873 -0.0144 -0.0145 0.0067  36  VAL   B CG2 
4923 N N   . ASN   B 37  ? 0.1213 0.1116 0.1603 -0.0035 -0.0061 -0.0001 37  ASN   B N   
4924 C CA  . ASN   B 37  ? 0.1197 0.1103 0.1758 0.0009  -0.0118 0.0053  37  ASN   B CA  
4925 C C   . ASN   B 37  ? 0.1160 0.1143 0.1773 0.0061  -0.0149 0.0005  37  ASN   B C   
4926 O O   . ASN   B 37  ? 0.1260 0.1143 0.1748 0.0034  -0.0050 0.0031  37  ASN   B O   
4927 C CB  . ASN   B 37  ? 0.1197 0.1145 0.1700 -0.0006 -0.0102 0.0008  37  ASN   B CB  
4928 C CG  . ASN   B 37  ? 0.1197 0.1160 0.1798 0.0005  -0.0155 -0.0021 37  ASN   B CG  
4929 O OD1 . ASN   B 37  ? 0.1260 0.1244 0.1941 0.0061  -0.0187 -0.0017 37  ASN   B OD1 
4930 N ND2 . ASN   B 37  ? 0.1287 0.1179 0.1779 -0.0009 -0.0188 0.0124  37  ASN   B ND2 
4937 N N   . ALA   B 38  ? 0.1183 0.1111 0.1719 0.0090  -0.0049 0.0038  38  ALA   B N   
4938 C CA  . ALA   B 38  ? 0.1278 0.1147 0.1741 0.0004  0.0008  0.0068  38  ALA   B CA  
4939 C C   . ALA   B 38  ? 0.1280 0.1126 0.1756 -0.0010 -0.0052 -0.0006 38  ALA   B C   
4940 O O   . ALA   B 38  ? 0.1402 0.1209 0.1890 0.0116  0.0005  0.0081  38  ALA   B O   
4941 C CB  . ALA   B 38  ? 0.1484 0.1291 0.1737 -0.0055 0.0095  0.0028  38  ALA   B CB  
4947 N N   . ALA   B 39  ? 0.1305 0.1192 0.1636 0.0055  -0.0096 -0.0071 39  ALA   B N   
4948 C CA  . ALA   B 39  ? 0.1359 0.1238 0.1728 0.0047  -0.0051 0.0019  39  ALA   B CA  
4949 C C   . ALA   B 39  ? 0.1386 0.1233 0.1573 0.0061  -0.0033 -0.0061 39  ALA   B C   
4950 O O   . ALA   B 39  ? 0.1454 0.1306 0.1783 0.0012  -0.0028 0.0052  39  ALA   B O   
4951 C CB  . ALA   B 39  ? 0.1462 0.1270 0.1823 -0.0068 -0.0114 0.0017  39  ALA   B CB  
4957 N N   . ASN   B 40  ? 0.1449 0.1501 0.1623 -0.0098 -0.0004 -0.0112 40  ASN   B N   
4958 C CA  . ASN   B 40  ? 0.1534 0.1520 0.1762 -0.0010 -0.0081 -0.0091 40  ASN   B CA  
4959 C C   . ASN   B 40  ? 0.1597 0.1585 0.1597 0.0056  -0.0223 0.0019  40  ASN   B C   
4960 O O   . ASN   B 40  ? 0.1523 0.1519 0.1814 0.0070  -0.0239 0.0032  40  ASN   B O   
4961 C CB  . ASN   B 40  ? 0.1614 0.1541 0.1965 0.0008  -0.0118 -0.0035 40  ASN   B CB  
4962 C CG  . ASN   B 40  ? 0.1698 0.1606 0.2223 0.0026  -0.0237 0.0021  40  ASN   B CG  
4963 O OD1 . ASN   B 40  ? 0.1647 0.1610 0.2860 -0.0007 -0.0338 0.0065  40  ASN   B OD1 
4964 N ND2 . ASN   B 40  ? 0.1780 0.1576 0.2231 0.0107  -0.0178 0.0092  40  ASN   B ND2 
4971 N N   . VAL   B 41  ? 0.1610 0.1686 0.1617 0.0168  -0.0075 0.0016  41  VAL   B N   
4972 C CA  . VAL   B 41  ? 0.1733 0.1819 0.1669 0.0170  -0.0188 -0.0193 41  VAL   B CA  
4973 C C   . VAL   B 41  ? 0.1691 0.1757 0.1759 0.0238  -0.0226 -0.0301 41  VAL   B C   
4974 O O   . VAL   B 41  ? 0.1676 0.1708 0.1865 0.0174  -0.0200 -0.0282 41  VAL   B O   
4975 C CB  . VAL   B 41  ? 0.1844 0.2018 0.1741 0.0005  0.0048  -0.0331 41  VAL   B CB  
4976 C CG1 . VAL   B 41  ? 0.1830 0.2047 0.1874 -0.0034 0.0186  -0.0446 41  VAL   B CG1 
4977 C CG2 . VAL   B 41  ? 0.1913 0.2212 0.1847 -0.0102 0.0137  -0.0311 41  VAL   B CG2 
4987 N N   . TYR   B 42  ? 0.1734 0.1767 0.1867 0.0251  -0.0364 -0.0213 42  TYR   B N   
4988 C CA  . TYR   B 42  ? 0.1797 0.1910 0.1937 0.0289  -0.0449 -0.0301 42  TYR   B CA  
4989 C C   . TYR   B 42  ? 0.1609 0.1638 0.1966 0.0264  -0.0354 -0.0299 42  TYR   B C   
4990 O O   . TYR   B 42  ? 0.1653 0.1739 0.2280 0.0173  -0.0420 -0.0361 42  TYR   B O   
4991 C CB  . TYR   B 42  ? 0.2045 0.2334 0.2044 0.0218  -0.0471 -0.0256 42  TYR   B CB  
4992 C CG  . TYR   B 42  ? 0.2157 0.2584 0.1986 0.0111  -0.0318 -0.0124 42  TYR   B CG  
4993 C CD1 . TYR   B 42  ? 0.2150 0.2629 0.1686 0.0074  -0.0205 -0.0209 42  TYR   B CD1 
4994 C CD2 . TYR   B 42  ? 0.2369 0.2768 0.2362 0.0088  -0.0182 -0.0016 42  TYR   B CD2 
4995 C CE1 . TYR   B 42  ? 0.2321 0.2822 0.1870 0.0096  -0.0178 -0.0165 42  TYR   B CE1 
4996 C CE2 . TYR   B 42  ? 0.2448 0.2876 0.2330 0.0077  -0.0038 0.0082  42  TYR   B CE2 
4997 C CZ  . TYR   B 42  ? 0.2528 0.2950 0.2207 0.0212  0.0015  0.0013  42  TYR   B CZ  
4998 O OH  . TYR   B 42  ? 0.2835 0.3154 0.2751 0.0343  0.0250  0.0180  42  TYR   B OH  
5008 N N   . LEU   B 43  ? 0.1492 0.1523 0.1873 0.0140  -0.0287 -0.0265 43  LEU   B N   
5009 C CA  . LEU   B 43  ? 0.1472 0.1489 0.1885 0.0113  -0.0191 -0.0096 43  LEU   B CA  
5010 C C   . LEU   B 43  ? 0.1553 0.1525 0.1920 0.0133  -0.0190 -0.0038 43  LEU   B C   
5011 O O   . LEU   B 43  ? 0.1524 0.1551 0.2141 0.0050  -0.0278 -0.0006 43  LEU   B O   
5012 C CB  . LEU   B 43  ? 0.1467 0.1418 0.1946 0.0019  -0.0316 -0.0170 43  LEU   B CB  
5013 C CG  . LEU   B 43  ? 0.1518 0.1369 0.1992 0.0042  -0.0329 -0.0081 43  LEU   B CG  
5014 C CD1 . LEU   B 43  ? 0.1698 0.1477 0.2202 0.0056  -0.0400 -0.0109 43  LEU   B CD1 
5015 C CD2 . LEU   B 43  ? 0.1490 0.1413 0.2047 -0.0025 -0.0387 -0.0166 43  LEU   B CD2 
5027 N N   . LYS   B 44  ? 0.1474 0.1459 0.1961 0.0116  -0.0166 -0.0111 44  LYS   B N   
5028 C CA  . LYS   B 44  ? 0.1592 0.1555 0.1923 0.0069  -0.0165 0.0029  44  LYS   B CA  
5029 C C   . LYS   B 44  ? 0.1463 0.1513 0.1852 0.0136  -0.0128 -0.0007 44  LYS   B C   
5030 O O   . LYS   B 44  ? 0.1657 0.1468 0.2066 0.0070  -0.0079 0.0004  44  LYS   B O   
5031 C CB  . LYS   B 44  ? 0.1877 0.1766 0.2010 0.0029  -0.0228 -0.0055 44  LYS   B CB  
5032 C CG  . LYS   B 44  ? 0.2345 0.2105 0.2388 0.0039  -0.0365 -0.0057 44  LYS   B CG  
5033 C CD  . LYS   B 44  ? 0.2721 0.2322 0.2695 -0.0075 -0.0467 -0.0041 44  LYS   B CD  
5034 C CE  . LYS   B 44  ? 0.3011 0.2567 0.3031 -0.0179 -0.0563 0.0078  44  LYS   B CE  
5035 N NZ  . LYS   B 44  ? 0.3150 0.2669 0.3302 -0.0159 -0.0686 0.0173  44  LYS   B NZ  
5049 N N   . HIS   B 45  ? 0.1450 0.1452 0.1727 0.0079  -0.0173 -0.0000 45  HIS   B N   
5050 C CA  . HIS   B 45  ? 0.1530 0.1513 0.1822 0.0085  -0.0148 -0.0005 45  HIS   B CA  
5051 C C   . HIS   B 45  ? 0.1758 0.1756 0.2058 0.0141  -0.0316 -0.0072 45  HIS   B C   
5052 O O   . HIS   B 45  ? 0.1866 0.2058 0.2544 0.0463  0.0037  0.0004  45  HIS   B O   
5053 C CB  . HIS   B 45  ? 0.1449 0.1511 0.1808 0.0018  -0.0118 -0.0047 45  HIS   B CB  
5054 C CG  . HIS   B 45  ? 0.1445 0.1433 0.1905 -0.0036 -0.0137 0.0028  45  HIS   B CG  
5055 N ND1 . HIS   B 45  ? 0.1454 0.1390 0.1931 -0.0006 -0.0252 -0.0118 45  HIS   B ND1 
5056 C CD2 . HIS   B 45  ? 0.1542 0.1479 0.2017 -0.0074 -0.0173 0.0028  45  HIS   B CD2 
5057 C CE1 . HIS   B 45  ? 0.1574 0.1308 0.1797 -0.0039 -0.0263 -0.0199 45  HIS   B CE1 
5058 N NE2 . HIS   B 45  ? 0.1608 0.1409 0.1910 -0.0014 -0.0221 -0.0042 45  HIS   B NE2 
5066 N N   A GLY   B 46  ? 0.1872 0.1797 0.2167 0.0185  -0.0405 0.0004  46  GLY   B N   
5067 N N   B GLY   B 46  ? 0.1892 0.1792 0.2151 0.0209  -0.0476 0.0079  46  GLY   B N   
5068 C CA  A GLY   B 46  ? 0.1966 0.1891 0.2424 0.0165  -0.0406 0.0011  46  GLY   B CA  
5069 C CA  B GLY   B 46  ? 0.2008 0.1920 0.2388 0.0175  -0.0502 0.0123  46  GLY   B CA  
5070 C C   A GLY   B 46  ? 0.1993 0.1996 0.2791 0.0212  -0.0334 -0.0022 46  GLY   B C   
5071 C C   B GLY   B 46  ? 0.2041 0.2072 0.2759 0.0228  -0.0416 0.0111  46  GLY   B C   
5072 O O   A GLY   B 46  ? 0.2068 0.2090 0.3328 0.0250  -0.0216 -0.0172 46  GLY   B O   
5073 O O   B GLY   B 46  ? 0.2173 0.2291 0.3263 0.0218  -0.0279 0.0051  46  GLY   B O   
5080 N N   . GLY   B 47  ? 0.1995 0.2029 0.2729 0.0123  -0.0192 -0.0037 47  GLY   B N   
5081 C CA  . GLY   B 47  ? 0.1813 0.1702 0.2362 0.0128  -0.0054 -0.0051 47  GLY   B CA  
5082 C C   . GLY   B 47  ? 0.1622 0.1493 0.2117 0.0140  -0.0044 0.0046  47  GLY   B C   
5083 O O   . GLY   B 47  ? 0.1747 0.1345 0.2261 0.0090  -0.0116 0.0091  47  GLY   B O   
5088 N N   . GLY   B 48  ? 0.1412 0.1427 0.2058 0.0068  -0.0121 0.0125  48  GLY   B N   
5089 C CA  . GLY   B 48  ? 0.1461 0.1390 0.1943 0.0015  -0.0020 0.0175  48  GLY   B CA  
5090 C C   . GLY   B 48  ? 0.1395 0.1290 0.1905 0.0056  0.0065  0.0025  48  GLY   B C   
5091 O O   . GLY   B 48  ? 0.1358 0.1344 0.2210 0.0082  -0.0077 0.0032  48  GLY   B O   
5095 N N   . VAL   B 49  ? 0.1431 0.1326 0.1904 0.0095  -0.0015 0.0066  49  VAL   B N   
5096 C CA  . VAL   B 49  ? 0.1464 0.1360 0.1926 0.0127  -0.0113 0.0076  49  VAL   B CA  
5097 C C   . VAL   B 49  ? 0.1342 0.1311 0.1888 0.0138  -0.0020 0.0061  49  VAL   B C   
5098 O O   . VAL   B 49  ? 0.1406 0.1390 0.1882 0.0082  -0.0097 0.0055  49  VAL   B O   
5099 C CB  . VAL   B 49  ? 0.1477 0.1550 0.2126 0.0009  -0.0181 0.0053  49  VAL   B CB  
5100 C CG1 . VAL   B 49  ? 0.1392 0.1642 0.2185 0.0043  -0.0253 0.0151  49  VAL   B CG1 
5101 C CG2 . VAL   B 49  ? 0.1616 0.1659 0.2361 -0.0084 -0.0315 0.0114  49  VAL   B CG2 
5111 N N   . ALA   B 50  ? 0.1332 0.1290 0.1894 0.0069  -0.0024 0.0042  50  ALA   B N   
5112 C CA  . ALA   B 50  ? 0.1250 0.1244 0.1888 0.0100  -0.0081 0.0065  50  ALA   B CA  
5113 C C   . ALA   B 50  ? 0.1293 0.1305 0.1913 0.0064  -0.0089 0.0040  50  ALA   B C   
5114 O O   . ALA   B 50  ? 0.1348 0.1330 0.1987 0.0064  -0.0067 -0.0010 50  ALA   B O   
5115 C CB  . ALA   B 50  ? 0.1312 0.1306 0.1904 -0.0010 0.0024  0.0084  50  ALA   B CB  
5121 N N   . GLY   B 51  ? 0.1291 0.1424 0.2023 0.0152  -0.0205 0.0018  51  GLY   B N   
5122 C CA  . GLY   B 51  ? 0.1374 0.1489 0.2047 0.0208  -0.0114 0.0112  51  GLY   B CA  
5123 C C   . GLY   B 51  ? 0.1371 0.1383 0.2094 0.0243  -0.0106 0.0135  51  GLY   B C   
5124 O O   . GLY   B 51  ? 0.1412 0.1536 0.2266 0.0129  -0.0114 0.0052  51  GLY   B O   
5128 N N   . ALA   B 52  ? 0.1408 0.1362 0.2065 0.0240  -0.0078 0.0071  52  ALA   B N   
5129 C CA  . ALA   B 52  ? 0.1456 0.1438 0.2042 0.0222  0.0005  -0.0044 52  ALA   B CA  
5130 C C   . ALA   B 52  ? 0.1450 0.1377 0.1986 0.0110  -0.0008 0.0056  52  ALA   B C   
5131 O O   . ALA   B 52  ? 0.1399 0.1476 0.2109 0.0109  0.0037  0.0087  52  ALA   B O   
5132 C CB  . ALA   B 52  ? 0.1643 0.1512 0.2094 0.0128  0.0133  -0.0038 52  ALA   B CB  
5138 N N   . LEU   B 53  ? 0.1381 0.1388 0.1816 0.0240  0.0033  0.0069  53  LEU   B N   
5139 C CA  . LEU   B 53  ? 0.1338 0.1455 0.1867 0.0179  -0.0017 0.0094  53  LEU   B CA  
5140 C C   . LEU   B 53  ? 0.1319 0.1378 0.1857 0.0130  0.0007  0.0116  53  LEU   B C   
5141 O O   . LEU   B 53  ? 0.1418 0.1486 0.2015 0.0028  -0.0014 0.0215  53  LEU   B O   
5142 C CB  . LEU   B 53  ? 0.1322 0.1507 0.1963 0.0113  -0.0075 0.0190  53  LEU   B CB  
5143 C CG  . LEU   B 53  ? 0.1274 0.1673 0.1992 0.0076  -0.0031 0.0263  53  LEU   B CG  
5144 C CD1 . LEU   B 53  ? 0.1348 0.1920 0.2215 0.0116  0.0011  0.0062  53  LEU   B CD1 
5145 C CD2 . LEU   B 53  ? 0.1427 0.1865 0.2256 0.0008  -0.0094 -0.0022 53  LEU   B CD2 
5157 N N   . ASN   B 54  ? 0.1345 0.1328 0.1942 -0.0006 -0.0091 0.0147  54  ASN   B N   
5158 C CA  . ASN   B 54  ? 0.1406 0.1432 0.2074 0.0037  -0.0100 0.0121  54  ASN   B CA  
5159 C C   . ASN   B 54  ? 0.1336 0.1430 0.2175 0.0055  -0.0080 0.0091  54  ASN   B C   
5160 O O   . ASN   B 54  ? 0.1307 0.1538 0.2267 -0.0029 -0.0030 0.0064  54  ASN   B O   
5161 C CB  . ASN   B 54  ? 0.1403 0.1530 0.2137 0.0021  0.0072  0.0043  54  ASN   B CB  
5162 C CG  . ASN   B 54  ? 0.1393 0.1637 0.2121 0.0033  -0.0116 0.0092  54  ASN   B CG  
5163 O OD1 . ASN   B 54  ? 0.1343 0.1634 0.2231 -0.0005 -0.0127 0.0018  54  ASN   B OD1 
5164 N ND2 . ASN   B 54  ? 0.1497 0.1887 0.2423 0.0050  -0.0283 0.0167  54  ASN   B ND2 
5171 N N   A LYS   B 55  ? 0.1359 0.1520 0.2240 0.0147  -0.0038 0.0089  55  LYS   B N   
5172 N N   B LYS   B 55  ? 0.1334 0.1498 0.2327 0.0204  -0.0017 0.0149  55  LYS   B N   
5173 C CA  A LYS   B 55  ? 0.1461 0.1691 0.2257 0.0207  -0.0036 0.0056  55  LYS   B CA  
5174 C CA  B LYS   B 55  ? 0.1451 0.1703 0.2338 0.0291  -0.0023 0.0163  55  LYS   B CA  
5175 C C   A LYS   B 55  ? 0.1408 0.1677 0.2254 0.0163  -0.0017 0.0019  55  LYS   B C   
5176 C C   B LYS   B 55  ? 0.1393 0.1669 0.2348 0.0209  -0.0001 0.0068  55  LYS   B C   
5177 O O   A LYS   B 55  ? 0.1414 0.1751 0.2369 0.0141  0.0011  0.0035  55  LYS   B O   
5178 O O   B LYS   B 55  ? 0.1390 0.1771 0.2535 0.0207  0.0065  0.0087  55  LYS   B O   
5179 C CB  A LYS   B 55  ? 0.1639 0.1820 0.2450 0.0283  0.0064  0.0075  55  LYS   B CB  
5180 C CB  B LYS   B 55  ? 0.1657 0.1869 0.2515 0.0419  0.0101  0.0276  55  LYS   B CB  
5181 C CG  A LYS   B 55  ? 0.1903 0.2015 0.2931 0.0307  0.0178  0.0159  55  LYS   B CG  
5182 C CG  B LYS   B 55  ? 0.2002 0.2139 0.3084 0.0442  0.0239  0.0413  55  LYS   B CG  
5183 C CD  A LYS   B 55  ? 0.2113 0.2196 0.3328 0.0345  0.0313  0.0181  55  LYS   B CD  
5184 C CD  B LYS   B 55  ? 0.2276 0.2396 0.3561 0.0486  0.0368  0.0484  55  LYS   B CD  
5185 C CE  A LYS   B 55  ? 0.2219 0.2325 0.3669 0.0365  0.0417  0.0191  55  LYS   B CE  
5186 C CE  B LYS   B 55  ? 0.2435 0.2582 0.3947 0.0527  0.0397  0.0544  55  LYS   B CE  
5187 N NZ  A LYS   B 55  ? 0.2296 0.2429 0.3878 0.0363  0.0340  0.0228  55  LYS   B NZ  
5188 N NZ  B LYS   B 55  ? 0.2542 0.2719 0.4214 0.0517  0.0339  0.0553  55  LYS   B NZ  
5215 N N   . ALA   B 56  ? 0.1383 0.1690 0.2228 0.0163  0.0006  0.0025  56  ALA   B N   
5216 C CA  . ALA   B 56  ? 0.1493 0.1812 0.2151 0.0079  0.0014  0.0052  56  ALA   B CA  
5217 C C   . ALA   B 56  ? 0.1468 0.1761 0.2082 0.0061  0.0130  0.0145  56  ALA   B C   
5218 O O   . ALA   B 56  ? 0.1604 0.1862 0.2375 0.0073  0.0305  0.0174  56  ALA   B O   
5219 C CB  . ALA   B 56  ? 0.1640 0.2035 0.2146 -0.0095 0.0076  0.0061  56  ALA   B CB  
5226 N N   . THR   B 57  ? 0.1485 0.1635 0.2227 0.0098  0.0124  0.0078  57  THR   B N   
5227 C CA  . THR   B 57  ? 0.1513 0.1692 0.2251 0.0040  0.0147  0.0180  57  THR   B CA  
5228 C C   . THR   B 57  ? 0.1490 0.1813 0.2450 -0.0004 0.0129  0.0182  57  THR   B C   
5229 O O   . THR   B 57  ? 0.1564 0.1757 0.2516 -0.0111 0.0113  0.0130  57  THR   B O   
5230 C CB  . THR   B 57  ? 0.1595 0.1640 0.2157 0.0068  0.0090  0.0153  57  THR   B CB  
5231 O OG1 . THR   B 57  ? 0.1527 0.1501 0.2248 0.0027  0.0111  0.0069  57  THR   B OG1 
5232 C CG2 . THR   B 57  ? 0.1494 0.1753 0.1991 0.0029  0.0074  0.0095  57  THR   B CG2 
5240 N N   . ASN   B 58  ? 0.1285 0.2076 0.2580 -0.0114 0.0012  -0.0001 58  ASN   B N   
5241 C CA  . ASN   B 58  ? 0.1591 0.2498 0.2978 -0.0232 0.0173  0.0120  58  ASN   B CA  
5242 C C   . ASN   B 58  ? 0.1329 0.2220 0.2651 -0.0122 -0.0013 0.0065  58  ASN   B C   
5243 O O   . ASN   B 58  ? 0.1382 0.2267 0.2725 -0.0155 0.0058  0.0073  58  ASN   B O   
5244 C CB  . ASN   B 58  ? 0.2549 0.3256 0.4140 -0.0340 0.0481  0.0234  58  ASN   B CB  
5245 C CG  . ASN   B 58  ? 0.3493 0.3829 0.5506 -0.0353 0.0703  0.0486  58  ASN   B CG  
5246 O OD1 . ASN   B 58  ? 0.4029 0.4029 0.6003 -0.0355 0.0755  0.0577  58  ASN   B OD1 
5247 N ND2 . ASN   B 58  ? 0.4395 0.4395 0.6000 -0.0368 0.0786  0.0555  58  ASN   B ND2 
5254 N N   . ASN   B 59  ? 0.1339 0.2046 0.2496 -0.0089 0.0015  0.0067  59  ASN   B N   
5255 C CA  . ASN   B 59  ? 0.1367 0.2043 0.2391 -0.0111 -0.0065 0.0131  59  ASN   B CA  
5256 C C   . ASN   B 59  ? 0.1318 0.1942 0.2263 -0.0133 -0.0154 0.0030  59  ASN   B C   
5257 O O   . ASN   B 59  ? 0.1353 0.1865 0.2258 -0.0134 -0.0188 -0.0045 59  ASN   B O   
5258 C CB  . ASN   B 59  ? 0.1449 0.2226 0.2500 -0.0035 -0.0242 0.0157  59  ASN   B CB  
5259 C CG  . ASN   B 59  ? 0.1561 0.2340 0.2650 0.0079  -0.0320 0.0118  59  ASN   B CG  
5260 O OD1 . ASN   B 59  ? 0.1692 0.2360 0.2738 0.0087  -0.0204 0.0206  59  ASN   B OD1 
5261 N ND2 . ASN   B 59  ? 0.1630 0.2442 0.2776 -0.0035 -0.0329 0.0055  59  ASN   B ND2 
5268 N N   . ALA   B 60  ? 0.1311 0.1785 0.2281 -0.0108 -0.0028 0.0049  60  ALA   B N   
5269 C CA  . ALA   B 60  ? 0.1443 0.1707 0.2431 -0.0142 -0.0041 0.0098  60  ALA   B CA  
5270 C C   . ALA   B 60  ? 0.1409 0.1529 0.2258 -0.0092 -0.0109 0.0061  60  ALA   B C   
5271 O O   . ALA   B 60  ? 0.1446 0.1519 0.2303 -0.0090 -0.0090 -0.0020 60  ALA   B O   
5272 C CB  . ALA   B 60  ? 0.1580 0.1733 0.2621 -0.0145 0.0038  0.0117  60  ALA   B CB  
5278 N N   . MET   B 61  ? 0.1321 0.1513 0.2147 -0.0088 -0.0050 0.0088  61  MET   B N   
5279 C CA  . MET   B 61  ? 0.1313 0.1420 0.2157 -0.0079 -0.0043 0.0057  61  MET   B CA  
5280 C C   . MET   B 61  ? 0.1318 0.1450 0.2152 -0.0099 -0.0136 0.0076  61  MET   B C   
5281 O O   . MET   B 61  ? 0.1337 0.1420 0.2205 -0.0053 -0.0170 -0.0103 61  MET   B O   
5282 C CB  . MET   B 61  ? 0.1281 0.1393 0.2176 0.0032  -0.0047 0.0041  61  MET   B CB  
5283 C CG  . MET   B 61  ? 0.1276 0.1434 0.2188 -0.0007 -0.0115 -0.0040 61  MET   B CG  
5284 S SD  . MET   B 61  ? 0.1311 0.1434 0.2244 -0.0018 -0.0086 -0.0086 61  MET   B SD  
5285 C CE  . MET   B 61  ? 0.1445 0.1577 0.2569 -0.0023 -0.0086 -0.0119 61  MET   B CE  
5295 N N   . GLN   B 62  ? 0.1351 0.1525 0.2110 -0.0047 -0.0189 0.0010  62  GLN   B N   
5296 C CA  . GLN   B 62  ? 0.1358 0.1571 0.2197 -0.0049 -0.0268 -0.0103 62  GLN   B CA  
5297 C C   . GLN   B 62  ? 0.1349 0.1594 0.2262 -0.0018 -0.0305 -0.0055 62  GLN   B C   
5298 O O   . GLN   B 62  ? 0.1526 0.1588 0.2268 -0.0007 -0.0300 -0.0184 62  GLN   B O   
5299 C CB  . GLN   B 62  ? 0.1441 0.1563 0.2156 -0.0006 -0.0192 -0.0017 62  GLN   B CB  
5300 C CG  . GLN   B 62  ? 0.1460 0.1596 0.2267 -0.0022 -0.0247 -0.0102 62  GLN   B CG  
5301 C CD  . GLN   B 62  ? 0.1412 0.1558 0.2180 0.0012  -0.0219 0.0050  62  GLN   B CD  
5302 O OE1 . GLN   B 62  ? 0.1441 0.1578 0.2184 0.0013  -0.0375 -0.0027 62  GLN   B OE1 
5303 N NE2 . GLN   B 62  ? 0.1392 0.1639 0.2268 0.0006  -0.0220 -0.0088 62  GLN   B NE2 
5312 N N   . VAL   B 63  ? 0.1358 0.1613 0.2417 -0.0142 -0.0308 -0.0148 63  VAL   B N   
5313 C CA  . VAL   B 63  ? 0.1485 0.1650 0.2532 -0.0159 -0.0304 -0.0076 63  VAL   B CA  
5314 C C   . VAL   B 63  ? 0.1506 0.1507 0.2408 -0.0130 -0.0244 -0.0165 63  VAL   B C   
5315 O O   . VAL   B 63  ? 0.1598 0.1588 0.2555 -0.0138 -0.0416 -0.0231 63  VAL   B O   
5316 C CB  . VAL   B 63  ? 0.1529 0.1823 0.2967 -0.0213 -0.0287 -0.0095 63  VAL   B CB  
5317 C CG1 . VAL   B 63  ? 0.1549 0.1866 0.3110 -0.0322 -0.0242 -0.0228 63  VAL   B CG1 
5318 C CG2 . VAL   B 63  ? 0.1489 0.2036 0.3059 -0.0128 -0.0294 -0.0118 63  VAL   B CG2 
5328 N N   . GLU   B 64  ? 0.1518 0.1458 0.2322 -0.0096 -0.0235 -0.0142 64  GLU   B N   
5329 C CA  . GLU   B 64  ? 0.1505 0.1393 0.2345 -0.0112 -0.0269 -0.0109 64  GLU   B CA  
5330 C C   . GLU   B 64  ? 0.1443 0.1416 0.2240 -0.0084 -0.0283 -0.0195 64  GLU   B C   
5331 O O   . GLU   B 64  ? 0.1594 0.1487 0.2265 -0.0093 -0.0266 -0.0152 64  GLU   B O   
5332 C CB  . GLU   B 64  ? 0.1481 0.1487 0.2351 -0.0136 -0.0140 -0.0016 64  GLU   B CB  
5333 C CG  . GLU   B 64  ? 0.1542 0.1435 0.2324 -0.0264 -0.0239 -0.0188 64  GLU   B CG  
5334 C CD  . GLU   B 64  ? 0.1565 0.1525 0.2429 -0.0345 -0.0302 -0.0125 64  GLU   B CD  
5335 O OE1 . GLU   B 64  ? 0.1630 0.1697 0.2533 -0.0376 -0.0256 -0.0215 64  GLU   B OE1 
5336 O OE2 . GLU   B 64  ? 0.1713 0.1620 0.2454 -0.0338 -0.0481 -0.0170 64  GLU   B OE2 
5343 N N   . SER   B 65  ? 0.1475 0.1376 0.2213 -0.0134 -0.0150 -0.0188 65  SER   B N   
5344 C CA  . SER   B 65  ? 0.1512 0.1322 0.2251 -0.0029 -0.0206 -0.0173 65  SER   B CA  
5345 C C   . SER   B 65  ? 0.1445 0.1379 0.2260 -0.0054 -0.0231 -0.0205 65  SER   B C   
5346 O O   . SER   B 65  ? 0.1511 0.1433 0.2301 -0.0080 -0.0297 -0.0275 65  SER   B O   
5347 C CB  . SER   B 65  ? 0.1496 0.1359 0.2243 -0.0080 -0.0271 -0.0182 65  SER   B CB  
5348 O OG  . SER   B 65  ? 0.1465 0.1413 0.2208 -0.0074 -0.0219 -0.0276 65  SER   B OG  
5354 N N   . ASP   B 66  ? 0.1496 0.1469 0.2343 -0.0047 -0.0302 -0.0284 66  ASP   B N   
5355 C CA  . ASP   B 66  ? 0.1624 0.1609 0.2322 -0.0014 -0.0302 -0.0240 66  ASP   B CA  
5356 C C   . ASP   B 66  ? 0.1639 0.1663 0.2306 -0.0072 -0.0279 -0.0163 66  ASP   B C   
5357 O O   . ASP   B 66  ? 0.1712 0.1679 0.2327 0.0048  -0.0328 -0.0191 66  ASP   B O   
5358 C CB  . ASP   B 66  ? 0.1841 0.1780 0.2454 0.0092  -0.0456 -0.0264 66  ASP   B CB  
5359 C CG  . ASP   B 66  ? 0.2077 0.1867 0.2589 0.0198  -0.0581 -0.0111 66  ASP   B CG  
5360 O OD1 . ASP   B 66  ? 0.2264 0.1842 0.2515 0.0109  -0.0581 -0.0127 66  ASP   B OD1 
5361 O OD2 . ASP   B 66  ? 0.2222 0.2138 0.3137 0.0368  -0.0542 -0.0079 66  ASP   B OD2 
5366 N N   . ASP   B 67  ? 0.1594 0.1534 0.2238 -0.0110 -0.0245 -0.0244 67  ASP   B N   
5367 C CA  . ASP   B 67  ? 0.1822 0.1526 0.2318 -0.0146 -0.0312 -0.0183 67  ASP   B CA  
5368 C C   . ASP   B 67  ? 0.1799 0.1474 0.2345 -0.0006 -0.0260 -0.0230 67  ASP   B C   
5369 O O   . ASP   B 67  ? 0.1871 0.1481 0.2461 -0.0032 -0.0204 -0.0279 67  ASP   B O   
5370 C CB  . ASP   B 67  ? 0.2041 0.1622 0.2463 -0.0115 -0.0449 -0.0128 67  ASP   B CB  
5371 C CG  . ASP   B 67  ? 0.2391 0.1766 0.2512 -0.0068 -0.0708 -0.0169 67  ASP   B CG  
5372 O OD1 . ASP   B 67  ? 0.2601 0.1828 0.2547 -0.0115 -0.0760 -0.0161 67  ASP   B OD1 
5373 O OD2 . ASP   B 67  ? 0.2513 0.1866 0.2679 0.0059  -0.0765 -0.0195 67  ASP   B OD2 
5378 N N   . TYR   B 68  ? 0.1686 0.1497 0.2271 -0.0093 -0.0403 -0.0312 68  TYR   B N   
5379 C CA  . TYR   B 68  ? 0.1710 0.1651 0.2382 0.0005  -0.0467 -0.0353 68  TYR   B CA  
5380 C C   . TYR   B 68  ? 0.1610 0.1591 0.2257 0.0028  -0.0421 -0.0374 68  TYR   B C   
5381 O O   . TYR   B 68  ? 0.1720 0.1701 0.2315 0.0099  -0.0437 -0.0506 68  TYR   B O   
5382 C CB  . TYR   B 68  ? 0.1756 0.1859 0.2344 0.0098  -0.0511 -0.0458 68  TYR   B CB  
5383 C CG  . TYR   B 68  ? 0.1901 0.2059 0.2460 0.0181  -0.0336 -0.0594 68  TYR   B CG  
5384 C CD1 . TYR   B 68  ? 0.1936 0.2090 0.2613 0.0031  -0.0330 -0.0730 68  TYR   B CD1 
5385 C CD2 . TYR   B 68  ? 0.1987 0.2209 0.2554 0.0198  -0.0388 -0.0585 68  TYR   B CD2 
5386 C CE1 . TYR   B 68  ? 0.2000 0.2221 0.2748 0.0062  -0.0332 -0.0736 68  TYR   B CE1 
5387 C CE2 . TYR   B 68  ? 0.1975 0.2228 0.2617 0.0227  -0.0382 -0.0657 68  TYR   B CE2 
5388 C CZ  . TYR   B 68  ? 0.1905 0.2239 0.2765 0.0095  -0.0403 -0.0684 68  TYR   B CZ  
5389 O OH  . TYR   B 68  ? 0.1864 0.2370 0.3039 0.0129  -0.0365 -0.0475 68  TYR   B OH  
5399 N N   . ILE   B 69  ? 0.1642 0.1514 0.2390 0.0042  -0.0347 -0.0398 69  ILE   B N   
5400 C CA  . ILE   B 69  ? 0.1684 0.1614 0.2532 -0.0033 -0.0294 -0.0496 69  ILE   B CA  
5401 C C   . ILE   B 69  ? 0.1687 0.1556 0.2367 0.0085  -0.0463 -0.0428 69  ILE   B C   
5402 O O   . ILE   B 69  ? 0.1804 0.1627 0.2415 0.0088  -0.0336 -0.0373 69  ILE   B O   
5403 C CB  . ILE   B 69  ? 0.1762 0.1692 0.2694 -0.0026 0.0035  -0.0425 69  ILE   B CB  
5404 C CG1 . ILE   B 69  ? 0.1791 0.1785 0.2733 -0.0122 0.0093  -0.0361 69  ILE   B CG1 
5405 C CG2 . ILE   B 69  ? 0.1917 0.1738 0.2870 0.0011  -0.0009 -0.0330 69  ILE   B CG2 
5406 C CD1 . ILE   B 69  ? 0.1652 0.1801 0.2799 -0.0172 0.0072  -0.0374 69  ILE   B CD1 
5418 N N   . ALA   B 70  ? 0.1673 0.1589 0.2318 0.0087  -0.0434 -0.0350 70  ALA   B N   
5419 C CA  . ALA   B 70  ? 0.1703 0.1672 0.2168 0.0032  -0.0441 -0.0328 70  ALA   B CA  
5420 C C   . ALA   B 70  ? 0.1738 0.1666 0.2077 -0.0018 -0.0499 -0.0321 70  ALA   B C   
5421 O O   . ALA   B 70  ? 0.1843 0.1647 0.2143 0.0030  -0.0422 -0.0285 70  ALA   B O   
5422 C CB  . ALA   B 70  ? 0.1703 0.1765 0.2216 -0.0017 -0.0436 -0.0319 70  ALA   B CB  
5428 N N   . THR   B 71  ? 0.1813 0.1670 0.2155 0.0027  -0.0570 -0.0344 71  THR   B N   
5429 C CA  . THR   B 71  ? 0.1967 0.1697 0.2353 0.0060  -0.0591 -0.0439 71  THR   B CA  
5430 C C   . THR   B 71  ? 0.1912 0.1695 0.2679 0.0269  -0.0599 -0.0573 71  THR   B C   
5431 O O   . THR   B 71  ? 0.2026 0.1820 0.3022 0.0324  -0.0656 -0.0780 71  THR   B O   
5432 C CB  . THR   B 71  ? 0.2198 0.2003 0.2474 -0.0005 -0.0633 -0.0250 71  THR   B CB  
5433 O OG1 . THR   B 71  ? 0.2373 0.2282 0.2702 -0.0201 -0.0601 -0.0078 71  THR   B OG1 
5434 C CG2 . THR   B 71  ? 0.2356 0.2036 0.2607 0.0066  -0.0546 -0.0126 71  THR   B CG2 
5442 N N   . ASN   B 72  ? 0.1773 0.1718 0.2656 0.0130  -0.0537 -0.0706 72  ASN   B N   
5443 C CA  . ASN   B 72  ? 0.1807 0.1924 0.2514 0.0167  -0.0458 -0.0683 72  ASN   B CA  
5444 C C   . ASN   B 72  ? 0.1779 0.2003 0.2539 0.0037  -0.0274 -0.0724 72  ASN   B C   
5445 O O   . ASN   B 72  ? 0.1795 0.2157 0.2701 0.0094  -0.0162 -0.0667 72  ASN   B O   
5446 C CB  . ASN   B 72  ? 0.1883 0.2027 0.2564 0.0176  -0.0536 -0.0602 72  ASN   B CB  
5447 C CG  . ASN   B 72  ? 0.2083 0.2213 0.2691 0.0315  -0.0519 -0.0398 72  ASN   B CG  
5448 O OD1 . ASN   B 72  ? 0.2289 0.2307 0.2757 0.0187  -0.0444 -0.0500 72  ASN   B OD1 
5449 N ND2 . ASN   B 72  ? 0.2159 0.2300 0.2958 0.0456  -0.0467 -0.0130 72  ASN   B ND2 
5456 N N   . GLY   B 73  ? 0.1828 0.2014 0.2421 0.0008  -0.0356 -0.0676 73  GLY   B N   
5457 C CA  . GLY   B 73  ? 0.1826 0.2063 0.2162 0.0005  -0.0330 -0.0582 73  GLY   B CA  
5458 C C   . GLY   B 73  ? 0.1756 0.2065 0.1896 0.0065  -0.0308 -0.0486 73  GLY   B C   
5459 O O   . GLY   B 73  ? 0.1741 0.1999 0.2017 0.0063  -0.0298 -0.0378 73  GLY   B O   
5463 N N   . PRO   B 74  ? 0.1775 0.2093 0.1871 0.0054  -0.0323 -0.0409 74  PRO   B N   
5464 C CA  . PRO   B 74  ? 0.1689 0.2036 0.1723 0.0084  -0.0316 -0.0327 74  PRO   B CA  
5465 C C   . PRO   B 74  ? 0.1561 0.1929 0.1874 0.0086  -0.0263 -0.0277 74  PRO   B C   
5466 O O   . PRO   B 74  ? 0.1591 0.1961 0.2123 0.0084  -0.0258 -0.0397 74  PRO   B O   
5467 C CB  . PRO   B 74  ? 0.1876 0.2201 0.1837 0.0089  -0.0307 -0.0294 74  PRO   B CB  
5468 C CG  . PRO   B 74  ? 0.2067 0.2305 0.2163 0.0071  -0.0179 -0.0288 74  PRO   B CG  
5469 C CD  . PRO   B 74  ? 0.2012 0.2251 0.1999 0.0059  -0.0171 -0.0388 74  PRO   B CD  
5477 N N   . LEU   B 75  ? 0.1462 0.1827 0.1675 0.0127  -0.0259 -0.0314 75  LEU   B N   
5478 C CA  . LEU   B 75  ? 0.1461 0.1811 0.1623 0.0125  -0.0222 -0.0174 75  LEU   B CA  
5479 C C   . LEU   B 75  ? 0.1528 0.1884 0.1585 0.0097  -0.0158 -0.0155 75  LEU   B C   
5480 O O   . LEU   B 75  ? 0.1689 0.1986 0.1777 0.0012  -0.0143 -0.0091 75  LEU   B O   
5481 C CB  . LEU   B 75  ? 0.1528 0.1762 0.1709 -0.0002 -0.0269 -0.0048 75  LEU   B CB  
5482 C CG  . LEU   B 75  ? 0.1859 0.1956 0.1936 -0.0338 -0.0201 -0.0166 75  LEU   B CG  
5483 C CD1 . LEU   B 75  ? 0.2159 0.2083 0.2000 -0.0458 -0.0046 -0.0234 75  LEU   B CD1 
5484 C CD2 . LEU   B 75  ? 0.2250 0.2211 0.2483 -0.0218 -0.0057 -0.0094 75  LEU   B CD2 
5496 N N   . LYS   B 76  ? 0.1574 0.2074 0.1941 0.0028  -0.0068 -0.0122 76  LYS   B N   
5497 C CA  . LYS   B 76  ? 0.1704 0.2140 0.2165 0.0023  0.0172  -0.0137 76  LYS   B CA  
5498 C C   . LYS   B 76  ? 0.1592 0.1960 0.1936 0.0121  0.0049  0.0052  76  LYS   B C   
5499 O O   . LYS   B 76  ? 0.1551 0.1821 0.1974 0.0039  -0.0018 0.0061  76  LYS   B O   
5500 C CB  . LYS   B 76  ? 0.1925 0.2299 0.2838 -0.0028 0.0499  -0.0482 76  LYS   B CB  
5501 C CG  . LYS   B 76  ? 0.2050 0.2538 0.3289 0.0063  0.0377  -0.0553 76  LYS   B CG  
5502 C CD  . LYS   B 76  ? 0.2052 0.2671 0.3863 0.0074  0.0179  -0.0619 76  LYS   B CD  
5503 C CE  . LYS   B 76  ? 0.2125 0.2855 0.4384 0.0103  0.0021  -0.0690 76  LYS   B CE  
5504 N NZ  . LYS   B 76  ? 0.2100 0.2929 0.4652 0.0046  -0.0195 -0.0811 76  LYS   B NZ  
5518 N N   . VAL   B 77  ? 0.1587 0.2005 0.1736 0.0211  0.0005  0.0085  77  VAL   B N   
5519 C CA  . VAL   B 77  ? 0.1617 0.1914 0.1671 0.0229  0.0018  0.0249  77  VAL   B CA  
5520 C C   . VAL   B 77  ? 0.1530 0.1731 0.1764 0.0256  0.0020  0.0196  77  VAL   B C   
5521 O O   . VAL   B 77  ? 0.1551 0.1693 0.1924 0.0288  0.0112  0.0170  77  VAL   B O   
5522 C CB  . VAL   B 77  ? 0.1721 0.2010 0.1863 0.0201  0.0099  0.0343  77  VAL   B CB  
5523 C CG1 . VAL   B 77  ? 0.1767 0.1892 0.2133 0.0158  0.0228  0.0396  77  VAL   B CG1 
5524 C CG2 . VAL   B 77  ? 0.1826 0.2245 0.2186 0.0218  -0.0014 0.0377  77  VAL   B CG2 
5534 N N   . GLY   B 78  ? 0.1494 0.1672 0.1761 0.0161  -0.0028 0.0140  78  GLY   B N   
5535 C CA  . GLY   B 78  ? 0.1387 0.1575 0.1673 0.0128  0.0036  -0.0032 78  GLY   B CA  
5536 C C   . GLY   B 78  ? 0.1348 0.1528 0.1620 0.0119  0.0066  0.0083  78  GLY   B C   
5537 O O   . GLY   B 78  ? 0.1407 0.1558 0.1788 0.0139  -0.0031 0.0141  78  GLY   B O   
5541 N N   . GLY   B 79  ? 0.1328 0.1580 0.1862 0.0085  0.0119  -0.0026 79  GLY   B N   
5542 C CA  . GLY   B 79  ? 0.1324 0.1482 0.1828 0.0074  0.0015  -0.0023 79  GLY   B CA  
5543 C C   . GLY   B 79  ? 0.1303 0.1384 0.1871 0.0097  -0.0027 -0.0014 79  GLY   B C   
5544 O O   . GLY   B 79  ? 0.1338 0.1376 0.2056 0.0158  0.0067  0.0150  79  GLY   B O   
5548 N N   . SER   B 80  ? 0.1322 0.1313 0.1928 0.0066  0.0076  -0.0086 80  SER   B N   
5549 C CA  . SER   B 80  ? 0.1304 0.1294 0.2045 -0.0000 -0.0030 -0.0077 80  SER   B CA  
5550 C C   . SER   B 80  ? 0.1265 0.1239 0.1998 0.0110  -0.0190 -0.0103 80  SER   B C   
5551 O O   . SER   B 80  ? 0.1436 0.1284 0.2281 0.0105  -0.0109 -0.0125 80  SER   B O   
5552 C CB  . SER   B 80  ? 0.1365 0.1326 0.1998 -0.0054 -0.0067 -0.0008 80  SER   B CB  
5553 O OG  . SER   B 80  ? 0.1401 0.1437 0.2187 0.0019  -0.0282 0.0018  80  SER   B OG  
5559 N N   . CYS   B 81  ? 0.1317 0.1158 0.2038 0.0036  -0.0170 -0.0146 81  CYS   B N   
5560 C CA  . CYS   B 81  ? 0.1277 0.1120 0.2198 0.0043  -0.0229 -0.0104 81  CYS   B CA  
5561 C C   . CYS   B 81  ? 0.1333 0.1118 0.1928 0.0044  -0.0254 -0.0056 81  CYS   B C   
5562 O O   . CYS   B 81  ? 0.1533 0.1157 0.2036 0.0084  -0.0133 -0.0083 81  CYS   B O   
5563 C CB  . CYS   B 81  ? 0.1487 0.1253 0.2297 -0.0082 -0.0218 -0.0145 81  CYS   B CB  
5564 S SG  . CYS   B 81  ? 0.1499 0.1467 0.1923 -0.0048 -0.0297 -0.0140 81  CYS   B SG  
5570 N N   . VAL   B 82  ? 0.1384 0.1102 0.1953 0.0020  -0.0191 -0.0081 82  VAL   B N   
5571 C CA  . VAL   B 82  ? 0.1351 0.1146 0.2033 -0.0014 -0.0181 0.0000  82  VAL   B CA  
5572 C C   . VAL   B 82  ? 0.1473 0.1060 0.2145 -0.0001 -0.0129 0.0011  82  VAL   B C   
5573 O O   . VAL   B 82  ? 0.1569 0.1117 0.2266 -0.0026 -0.0194 -0.0207 82  VAL   B O   
5574 C CB  . VAL   B 82  ? 0.1482 0.1378 0.2260 -0.0006 -0.0188 -0.0008 82  VAL   B CB  
5575 C CG1 . VAL   B 82  ? 0.1680 0.1607 0.2316 0.0110  -0.0177 0.0051  82  VAL   B CG1 
5576 C CG2 . VAL   B 82  ? 0.1640 0.1478 0.2274 -0.0067 -0.0282 0.0032  82  VAL   B CG2 
5586 N N   . LEU   B 83  ? 0.1385 0.1069 0.2138 -0.0124 -0.0265 -0.0097 83  LEU   B N   
5587 C CA  . LEU   B 83  ? 0.1360 0.1134 0.2062 -0.0109 -0.0250 -0.0066 83  LEU   B CA  
5588 C C   . LEU   B 83  ? 0.1357 0.1107 0.2105 -0.0190 -0.0218 -0.0026 83  LEU   B C   
5589 O O   . LEU   B 83  ? 0.1390 0.1225 0.1939 -0.0182 -0.0177 0.0088  83  LEU   B O   
5590 C CB  . LEU   B 83  ? 0.1373 0.1233 0.2179 -0.0134 -0.0232 -0.0157 83  LEU   B CB  
5591 C CG  . LEU   B 83  ? 0.1598 0.1456 0.2196 -0.0119 -0.0186 -0.0126 83  LEU   B CG  
5592 C CD1 . LEU   B 83  ? 0.1775 0.1520 0.2096 -0.0137 -0.0308 -0.0025 83  LEU   B CD1 
5593 C CD2 . LEU   B 83  ? 0.1791 0.1539 0.2440 -0.0051 -0.0098 -0.0243 83  LEU   B CD2 
5605 N N   . SER   B 84  ? 0.1415 0.1246 0.2271 -0.0192 -0.0213 0.0009  84  SER   B N   
5606 C CA  . SER   B 84  ? 0.1429 0.1467 0.2191 -0.0220 -0.0218 0.0175  84  SER   B CA  
5607 C C   . SER   B 84  ? 0.1360 0.1603 0.1835 -0.0174 -0.0282 0.0185  84  SER   B C   
5608 O O   . SER   B 84  ? 0.1440 0.1426 0.1825 -0.0182 -0.0224 -0.0033 84  SER   B O   
5609 C CB  . SER   B 84  ? 0.1612 0.1492 0.2624 -0.0325 0.0060  0.0277  84  SER   B CB  
5610 O OG  . SER   B 84  ? 0.1675 0.1682 0.3110 -0.0320 0.0134  0.0353  84  SER   B OG  
5616 N N   . GLY   B 85  ? 0.1404 0.1823 0.1914 -0.0220 -0.0124 0.0366  85  GLY   B N   
5617 C CA  . GLY   B 85  ? 0.1435 0.1886 0.1960 -0.0320 -0.0116 0.0080  85  GLY   B CA  
5618 C C   . GLY   B 85  ? 0.1419 0.1676 0.1934 -0.0380 -0.0077 0.0065  85  GLY   B C   
5619 O O   . GLY   B 85  ? 0.1539 0.1709 0.1969 -0.0494 0.0092  -0.0071 85  GLY   B O   
5623 N N   . HIS   B 86  ? 0.1434 0.1517 0.2105 -0.0308 -0.0231 0.0195  86  HIS   B N   
5624 C CA  . HIS   B 86  ? 0.1407 0.1488 0.2107 -0.0329 -0.0238 0.0253  86  HIS   B CA  
5625 C C   . HIS   B 86  ? 0.1460 0.1613 0.2045 -0.0409 -0.0146 0.0361  86  HIS   B C   
5626 O O   . HIS   B 86  ? 0.1597 0.1703 0.2016 -0.0280 -0.0053 0.0372  86  HIS   B O   
5627 C CB  . HIS   B 86  ? 0.1500 0.1473 0.2233 -0.0233 -0.0355 0.0126  86  HIS   B CB  
5628 C CG  . HIS   B 86  ? 0.1484 0.1566 0.2015 -0.0127 -0.0292 0.0168  86  HIS   B CG  
5629 N ND1 . HIS   B 86  ? 0.1654 0.1801 0.2263 -0.0253 -0.0352 -0.0034 86  HIS   B ND1 
5630 C CD2 . HIS   B 86  ? 0.1509 0.1615 0.2193 -0.0146 -0.0273 0.0167  86  HIS   B CD2 
5631 C CE1 . HIS   B 86  ? 0.1679 0.1760 0.2171 -0.0214 -0.0286 -0.0191 86  HIS   B CE1 
5632 N NE2 . HIS   B 86  ? 0.1597 0.1645 0.2067 -0.0077 -0.0285 -0.0000 86  HIS   B NE2 
5640 N N   . ASN   B 87  ? 0.1438 0.1653 0.2168 -0.0371 -0.0115 0.0413  87  ASN   B N   
5641 C CA  . ASN   B 87  ? 0.1553 0.1835 0.2149 -0.0332 0.0147  0.0280  87  ASN   B CA  
5642 C C   . ASN   B 87  ? 0.1695 0.1692 0.2002 -0.0284 0.0198  0.0176  87  ASN   B C   
5643 O O   . ASN   B 87  ? 0.1984 0.1788 0.2273 -0.0197 0.0398  0.0105  87  ASN   B O   
5644 C CB  . ASN   B 87  ? 0.1536 0.2196 0.2400 -0.0267 0.0201  0.0193  87  ASN   B CB  
5645 C CG  . ASN   B 87  ? 0.1645 0.2375 0.2602 0.0049  0.0315  0.0322  87  ASN   B CG  
5646 O OD1 . ASN   B 87  ? 0.1612 0.2177 0.2407 0.0112  0.0374  0.0502  87  ASN   B OD1 
5647 N ND2 . ASN   B 87  ? 0.1986 0.2511 0.2911 0.0106  0.0427  0.0300  87  ASN   B ND2 
5654 N N   . LEU   B 88  ? 0.1575 0.1584 0.1904 -0.0360 0.0130  0.0138  88  LEU   B N   
5655 C CA  . LEU   B 88  ? 0.1641 0.1496 0.1855 -0.0271 0.0020  0.0010  88  LEU   B CA  
5656 C C   . LEU   B 88  ? 0.1604 0.1421 0.1892 -0.0324 0.0004  0.0046  88  LEU   B C   
5657 O O   . LEU   B 88  ? 0.1837 0.1557 0.2210 -0.0197 -0.0231 -0.0106 88  LEU   B O   
5658 C CB  . LEU   B 88  ? 0.1727 0.1587 0.2087 -0.0342 -0.0124 0.0214  88  LEU   B CB  
5659 C CG  . LEU   B 88  ? 0.2069 0.1896 0.2201 -0.0214 -0.0262 0.0395  88  LEU   B CG  
5660 C CD1 . LEU   B 88  ? 0.2203 0.2209 0.2306 -0.0350 -0.0211 0.0466  88  LEU   B CD1 
5661 C CD2 . LEU   B 88  ? 0.2407 0.2204 0.2587 0.0147  -0.0476 0.0163  88  LEU   B CD2 
5673 N N   . ALA   B 89  ? 0.1511 0.1419 0.1906 -0.0326 0.0126  0.0107  89  ALA   B N   
5674 C CA  . ALA   B 89  ? 0.1462 0.1344 0.1836 -0.0324 -0.0009 0.0071  89  ALA   B CA  
5675 C C   . ALA   B 89  ? 0.1546 0.1321 0.1845 -0.0340 0.0153  -0.0021 89  ALA   B C   
5676 O O   . ALA   B 89  ? 0.1489 0.1436 0.2097 -0.0384 0.0090  -0.0194 89  ALA   B O   
5677 C CB  . ALA   B 89  ? 0.1378 0.1324 0.1871 -0.0345 0.0005  0.0166  89  ALA   B CB  
5683 N N   . LYS   B 90  ? 0.1819 0.1261 0.1952 -0.0374 -0.0106 0.0058  90  LYS   B N   
5684 C CA  . LYS   B 90  ? 0.1981 0.1300 0.1992 -0.0402 -0.0059 0.0085  90  LYS   B CA  
5685 C C   . LYS   B 90  ? 0.1915 0.1201 0.2032 -0.0420 -0.0073 -0.0027 90  LYS   B C   
5686 O O   . LYS   B 90  ? 0.2031 0.1389 0.2169 -0.0593 -0.0015 0.0051  90  LYS   B O   
5687 C CB  . LYS   B 90  ? 0.2195 0.1271 0.2159 -0.0308 0.0051  0.0181  90  LYS   B CB  
5688 C CG  . LYS   B 90  ? 0.2301 0.1474 0.2258 -0.0220 0.0263  0.0087  90  LYS   B CG  
5689 C CD  . LYS   B 90  ? 0.2608 0.1926 0.2708 -0.0169 0.0435  -0.0002 90  LYS   B CD  
5690 C CE  . LYS   B 90  ? 0.2732 0.2164 0.3181 -0.0237 0.0500  -0.0128 90  LYS   B CE  
5691 N NZ  . LYS   B 90  ? 0.2766 0.2148 0.3236 -0.0348 0.0640  -0.0100 90  LYS   B NZ  
5705 N N   . HIS   B 91  ? 0.1630 0.1141 0.1825 -0.0272 -0.0194 0.0024  91  HIS   B N   
5706 C CA  . HIS   B 91  ? 0.1559 0.1161 0.1866 -0.0221 -0.0083 0.0025  91  HIS   B CA  
5707 C C   . HIS   B 91  ? 0.1417 0.1180 0.1687 -0.0260 -0.0045 0.0065  91  HIS   B C   
5708 O O   . HIS   B 91  ? 0.1592 0.1223 0.1703 -0.0261 -0.0147 0.0003  91  HIS   B O   
5709 C CB  . HIS   B 91  ? 0.1769 0.1192 0.2227 -0.0028 -0.0025 0.0147  91  HIS   B CB  
5710 C CG  . HIS   B 91  ? 0.2216 0.1379 0.2752 0.0065  0.0215  0.0276  91  HIS   B CG  
5711 N ND1 . HIS   B 91  ? 0.2573 0.1407 0.3199 -0.0024 0.0292  0.0150  91  HIS   B ND1 
5712 C CD2 . HIS   B 91  ? 0.2362 0.1652 0.3085 0.0221  0.0155  0.0609  91  HIS   B CD2 
5713 C CE1 . HIS   B 91  ? 0.2609 0.1553 0.3297 0.0186  0.0291  0.0250  91  HIS   B CE1 
5714 N NE2 . HIS   B 91  ? 0.2472 0.1704 0.3338 0.0296  0.0252  0.0588  91  HIS   B NE2 
5722 N N   . CYS   B 92  ? 0.1326 0.1190 0.1752 -0.0235 -0.0143 0.0021  92  CYS   B N   
5723 C CA  . CYS   B 92  ? 0.1365 0.1149 0.1666 -0.0221 -0.0092 0.0078  92  CYS   B CA  
5724 C C   . CYS   B 92  ? 0.1321 0.1059 0.1715 -0.0077 -0.0099 0.0056  92  CYS   B C   
5725 O O   . CYS   B 92  ? 0.1426 0.1121 0.1851 -0.0165 -0.0045 -0.0032 92  CYS   B O   
5726 C CB  . CYS   B 92  ? 0.1381 0.1233 0.1795 -0.0161 -0.0096 0.0070  92  CYS   B CB  
5727 S SG  . CYS   B 92  ? 0.1300 0.1267 0.1758 -0.0102 -0.0143 0.0031  92  CYS   B SG  
5733 N N   . LEU   B 93  ? 0.1230 0.1116 0.1720 -0.0130 -0.0092 -0.0005 93  LEU   B N   
5734 C CA  . LEU   B 93  ? 0.1250 0.1128 0.1629 -0.0047 -0.0126 0.0036  93  LEU   B CA  
5735 C C   . LEU   B 93  ? 0.1136 0.1114 0.1582 0.0010  -0.0202 -0.0033 93  LEU   B C   
5736 O O   . LEU   B 93  ? 0.1219 0.1164 0.1838 -0.0025 -0.0084 -0.0005 93  LEU   B O   
5737 C CB  . LEU   B 93  ? 0.1271 0.1186 0.1766 -0.0069 -0.0128 0.0049  93  LEU   B CB  
5738 C CG  . LEU   B 93  ? 0.1248 0.1249 0.1924 -0.0019 -0.0038 0.0114  93  LEU   B CG  
5739 C CD1 . LEU   B 93  ? 0.1327 0.1411 0.1946 0.0074  -0.0046 -0.0041 93  LEU   B CD1 
5740 C CD2 . LEU   B 93  ? 0.1221 0.1231 0.2091 -0.0066 -0.0140 0.0019  93  LEU   B CD2 
5752 N N   . HIS   B 94  ? 0.1193 0.1085 0.1770 -0.0046 -0.0220 0.0045  94  HIS   B N   
5753 C CA  . HIS   B 94  ? 0.1206 0.1067 0.1670 -0.0008 -0.0110 -0.0013 94  HIS   B CA  
5754 C C   . HIS   B 94  ? 0.1170 0.1137 0.1810 -0.0017 -0.0074 -0.0019 94  HIS   B C   
5755 O O   . HIS   B 94  ? 0.1234 0.1213 0.2224 -0.0002 0.0034  -0.0134 94  HIS   B O   
5756 C CB  . HIS   B 94  ? 0.1223 0.1178 0.1657 -0.0027 -0.0091 0.0015  94  HIS   B CB  
5757 C CG  . HIS   B 94  ? 0.1271 0.1101 0.1725 -0.0090 -0.0282 -0.0043 94  HIS   B CG  
5758 N ND1 . HIS   B 94  ? 0.1342 0.1144 0.1713 0.0006  -0.0286 -0.0055 94  HIS   B ND1 
5759 C CD2 . HIS   B 94  ? 0.1274 0.1154 0.1801 -0.0016 -0.0257 0.0031  94  HIS   B CD2 
5760 C CE1 . HIS   B 94  ? 0.1326 0.1181 0.1730 -0.0095 -0.0223 0.0009  94  HIS   B CE1 
5761 N NE2 . HIS   B 94  ? 0.1249 0.1258 0.1743 -0.0114 -0.0208 -0.0005 94  HIS   B NE2 
5769 N N   . VAL   B 95  ? 0.1143 0.1099 0.1849 -0.0029 -0.0091 -0.0043 95  VAL   B N   
5770 C CA  . VAL   B 95  ? 0.1163 0.1139 0.1775 0.0003  -0.0030 0.0090  95  VAL   B CA  
5771 C C   . VAL   B 95  ? 0.1158 0.1208 0.1710 0.0026  0.0051  -0.0041 95  VAL   B C   
5772 O O   . VAL   B 95  ? 0.1262 0.1194 0.1860 0.0059  -0.0003 0.0103  95  VAL   B O   
5773 C CB  . VAL   B 95  ? 0.1268 0.1141 0.1750 -0.0012 -0.0102 -0.0013 95  VAL   B CB  
5774 C CG1 . VAL   B 95  ? 0.1342 0.1329 0.1814 -0.0080 -0.0129 -0.0011 95  VAL   B CG1 
5775 C CG2 . VAL   B 95  ? 0.1363 0.1131 0.1831 0.0046  -0.0144 -0.0067 95  VAL   B CG2 
5785 N N   . VAL   B 96  ? 0.1298 0.1241 0.1810 0.0042  -0.0011 0.0029  96  VAL   B N   
5786 C CA  . VAL   B 96  ? 0.1386 0.1325 0.1702 0.0087  -0.0076 0.0105  96  VAL   B CA  
5787 C C   . VAL   B 96  ? 0.1361 0.1322 0.1777 0.0151  0.0015  0.0074  96  VAL   B C   
5788 O O   . VAL   B 96  ? 0.1390 0.1412 0.1855 0.0087  0.0075  -0.0007 96  VAL   B O   
5789 C CB  . VAL   B 96  ? 0.1427 0.1534 0.1770 0.0120  -0.0029 -0.0026 96  VAL   B CB  
5790 C CG1 . VAL   B 96  ? 0.1424 0.1665 0.1796 0.0172  -0.0028 -0.0028 96  VAL   B CG1 
5791 C CG2 . VAL   B 96  ? 0.1484 0.1663 0.1898 0.0097  0.0001  -0.0041 96  VAL   B CG2 
5801 N N   . GLY   B 97  ? 0.1415 0.1318 0.1850 0.0130  -0.0006 0.0094  97  GLY   B N   
5802 C CA  . GLY   B 97  ? 0.1471 0.1360 0.1776 0.0053  0.0076  0.0005  97  GLY   B CA  
5803 C C   . GLY   B 97  ? 0.1585 0.1472 0.1804 0.0119  0.0004  0.0028  97  GLY   B C   
5804 O O   . GLY   B 97  ? 0.1652 0.1594 0.1790 0.0094  -0.0062 0.0136  97  GLY   B O   
5808 N N   . PRO   B 98  ? 0.1666 0.1455 0.1845 0.0103  0.0076  0.0157  98  PRO   B N   
5809 C CA  . PRO   B 98  ? 0.1759 0.1621 0.1955 0.0167  0.0146  0.0178  98  PRO   B CA  
5810 C C   . PRO   B 98  ? 0.1825 0.1662 0.1569 0.0262  0.0136  0.0272  98  PRO   B C   
5811 O O   . PRO   B 98  ? 0.1788 0.1631 0.1648 0.0215  0.0144  0.0247  98  PRO   B O   
5812 C CB  . PRO   B 98  ? 0.1586 0.1630 0.2061 0.0149  0.0311  0.0144  98  PRO   B CB  
5813 C CG  . PRO   B 98  ? 0.1567 0.1527 0.1909 0.0057  0.0238  0.0224  98  PRO   B CG  
5814 C CD  . PRO   B 98  ? 0.1470 0.1447 0.1928 0.0076  0.0132  0.0177  98  PRO   B CD  
5822 N N   A ASN   B 99  ? 0.1898 0.1786 0.1576 0.0457  0.0256  0.0206  99  ASN   B N   
5823 N N   B ASN   B 99  ? 0.1916 0.1750 0.1626 0.0236  0.0118  0.0172  99  ASN   B N   
5824 C CA  A ASN   B 99  ? 0.2013 0.1869 0.1584 0.0604  0.0272  0.0320  99  ASN   B CA  
5825 C CA  B ASN   B 99  ? 0.2058 0.1785 0.1598 0.0179  -0.0016 0.0302  99  ASN   B CA  
5826 C C   A ASN   B 99  ? 0.2128 0.2084 0.1675 0.0611  0.0278  0.0368  99  ASN   B C   
5827 C C   B ASN   B 99  ? 0.2190 0.1976 0.1617 0.0066  -0.0052 0.0417  99  ASN   B C   
5828 O O   A ASN   B 99  ? 0.2188 0.2130 0.1789 0.0636  0.0187  0.0402  99  ASN   B O   
5829 O O   B ASN   B 99  ? 0.2241 0.2008 0.1809 0.0027  -0.0083 0.0415  99  ASN   B O   
5830 C CB  A ASN   B 99  ? 0.2059 0.1834 0.1661 0.0622  0.0314  0.0376  99  ASN   B CB  
5831 C CB  B ASN   B 99  ? 0.2079 0.1723 0.1858 0.0140  -0.0123 0.0305  99  ASN   B CB  
5832 C CG  A ASN   B 99  ? 0.2119 0.1907 0.1951 0.0588  0.0292  0.0303  99  ASN   B CG  
5833 C CG  B ASN   B 99  ? 0.2090 0.1806 0.2073 0.0098  -0.0285 0.0290  99  ASN   B CG  
5834 O OD1 A ASN   B 99  ? 0.2179 0.1891 0.2186 0.0631  0.0334  0.0349  99  ASN   B OD1 
5835 O OD1 B ASN   B 99  ? 0.2148 0.1805 0.2326 0.0089  -0.0307 0.0285  99  ASN   B OD1 
5836 N ND2 A ASN   B 99  ? 0.2128 0.1961 0.2007 0.0564  0.0194  0.0233  99  ASN   B ND2 
5837 N ND2 B ASN   B 99  ? 0.2036 0.1861 0.2183 0.0094  -0.0404 0.0256  99  ASN   B ND2 
5850 N N   A VAL   B 100 ? 0.2300 0.2251 0.2021 0.0443  0.0249  0.0400  100 VAL   B N   
5851 N N   B VAL   B 100 ? 0.2338 0.2100 0.1872 -0.0071 -0.0117 0.0507  100 VAL   B N   
5852 C CA  A VAL   B 100 ? 0.2576 0.2454 0.2419 0.0261  0.0249  0.0420  100 VAL   B CA  
5853 C CA  B VAL   B 100 ? 0.2654 0.2249 0.2262 -0.0155 -0.0013 0.0588  100 VAL   B CA  
5854 C C   A VAL   B 100 ? 0.2814 0.2557 0.2467 0.0281  0.0226  0.0483  100 VAL   B C   
5855 C C   B VAL   B 100 ? 0.2915 0.2242 0.2214 -0.0020 -0.0040 0.0679  100 VAL   B C   
5856 O O   A VAL   B 100 ? 0.2845 0.2603 0.2557 0.0292  0.0311  0.0459  100 VAL   B O   
5857 O O   B VAL   B 100 ? 0.2944 0.2258 0.2252 -0.0100 0.0079  0.0539  100 VAL   B O   
5858 C CB  A VAL   B 100 ? 0.2668 0.2580 0.2917 0.0045  0.0178  0.0400  100 VAL   B CB  
5859 C CB  B VAL   B 100 ? 0.2779 0.2466 0.2888 -0.0347 0.0009  0.0638  100 VAL   B CB  
5860 C CG1 A VAL   B 100 ? 0.2719 0.2624 0.3090 -0.0001 0.0177  0.0395  100 VAL   B CG1 
5861 C CG1 B VAL   B 100 ? 0.2850 0.2548 0.3160 -0.0394 0.0076  0.0654  100 VAL   B CG1 
5862 C CG2 A VAL   B 100 ? 0.2700 0.2615 0.3074 -0.0022 0.0168  0.0411  100 VAL   B CG2 
5863 C CG2 B VAL   B 100 ? 0.2845 0.2546 0.3087 -0.0361 0.0054  0.0707  100 VAL   B CG2 
5882 N N   A ASN   B 101 ? 0.3021 0.2663 0.2492 0.0319  0.0105  0.0536  101 ASN   B N   
5883 N N   B ASN   B 101 ? 0.3143 0.2290 0.2229 0.0182  -0.0206 0.0913  101 ASN   B N   
5884 C CA  A ASN   B 101 ? 0.3268 0.2817 0.2665 0.0309  -0.0002 0.0547  101 ASN   B CA  
5885 C CA  B ASN   B 101 ? 0.3443 0.2461 0.2448 0.0313  -0.0307 0.1077  101 ASN   B CA  
5886 C C   A ASN   B 101 ? 0.3518 0.3039 0.2726 0.0276  -0.0059 0.0554  101 ASN   B C   
5887 C C   B ASN   B 101 ? 0.3706 0.2773 0.2458 0.0303  -0.0397 0.1092  101 ASN   B C   
5888 O O   A ASN   B 101 ? 0.3522 0.3088 0.2845 0.0290  -0.0040 0.0552  101 ASN   B O   
5889 O O   B ASN   B 101 ? 0.3763 0.2902 0.2692 0.0351  -0.0461 0.0957  101 ASN   B O   
5890 C CB  A ASN   B 101 ? 0.3279 0.2777 0.2777 0.0278  -0.0004 0.0473  101 ASN   B CB  
5891 C CB  B ASN   B 101 ? 0.3499 0.2417 0.2653 0.0321  -0.0215 0.1031  101 ASN   B CB  
5892 C CG  A ASN   B 101 ? 0.3284 0.2741 0.2881 0.0244  -0.0032 0.0432  101 ASN   B CG  
5893 C CG  B ASN   B 101 ? 0.3526 0.2385 0.2822 0.0345  -0.0178 0.0984  101 ASN   B CG  
5894 O OD1 A ASN   B 101 ? 0.3322 0.2762 0.3032 0.0207  0.0054  0.0395  101 ASN   B OD1 
5895 O OD1 B ASN   B 101 ? 0.3611 0.2423 0.3083 0.0287  -0.0014 0.0935  101 ASN   B OD1 
5896 N ND2 A ASN   B 101 ? 0.3274 0.2742 0.2875 0.0231  -0.0115 0.0377  101 ASN   B ND2 
5897 N ND2 B ASN   B 101 ? 0.3497 0.2430 0.2840 0.0380  -0.0263 0.0816  101 ASN   B ND2 
5910 N N   A LYS   B 102 ? 0.3736 0.3201 0.2752 0.0236  -0.0074 0.0473  102 LYS   B N   
5911 N N   B LYS   B 102 ? 0.3886 0.2984 0.2548 0.0229  -0.0281 0.0966  102 LYS   B N   
5912 C CA  A LYS   B 102 ? 0.3969 0.3404 0.2874 0.0166  -0.0044 0.0402  102 LYS   B CA  
5913 C CA  B LYS   B 102 ? 0.4080 0.3289 0.2691 0.0133  -0.0122 0.0795  102 LYS   B CA  
5914 C C   A LYS   B 102 ? 0.3992 0.3413 0.2668 0.0223  0.0068  0.0412  102 LYS   B C   
5915 C C   B LYS   B 102 ? 0.4077 0.3325 0.2522 0.0190  0.0017  0.0778  102 LYS   B C   
5916 O O   A LYS   B 102 ? 0.4057 0.3447 0.2723 0.0231  0.0007  0.0361  102 LYS   B O   
5917 O O   B LYS   B 102 ? 0.4146 0.3395 0.2598 0.0214  -0.0035 0.0693  102 LYS   B O   
5918 C CB  A LYS   B 102 ? 0.4166 0.3592 0.3365 0.0057  -0.0036 0.0266  102 LYS   B CB  
5919 C CB  B LYS   B 102 ? 0.4264 0.3551 0.3229 0.0001  -0.0022 0.0505  102 LYS   B CB  
5920 C CG  A LYS   B 102 ? 0.4321 0.3751 0.3880 -0.0024 -0.0017 0.0115  102 LYS   B CG  
5921 C CG  B LYS   B 102 ? 0.4406 0.3776 0.3792 -0.0091 0.0073  0.0186  102 LYS   B CG  
5922 C CD  A LYS   B 102 ? 0.4443 0.3882 0.4377 -0.0088 0.0012  -0.0006 102 LYS   B CD  
5923 C CD  B LYS   B 102 ? 0.4521 0.3960 0.4333 -0.0167 0.0147  -0.0044 102 LYS   B CD  
5924 C CE  A LYS   B 102 ? 0.4527 0.3979 0.4771 -0.0140 0.0037  -0.0090 102 LYS   B CE  
5925 C CE  B LYS   B 102 ? 0.4600 0.4091 0.4752 -0.0230 0.0196  -0.0212 102 LYS   B CE  
5926 N NZ  A LYS   B 102 ? 0.4574 0.4037 0.4999 -0.0169 0.0051  -0.0141 102 LYS   B NZ  
5927 N NZ  B LYS   B 102 ? 0.4642 0.4168 0.4998 -0.0255 0.0226  -0.0303 102 LYS   B NZ  
5954 N N   A GLY   B 103 ? 0.3924 0.3378 0.2592 0.0270  0.0243  0.0437  103 GLY   B N   
5955 N N   B GLY   B 103 ? 0.3962 0.3271 0.2438 0.0217  0.0268  0.0828  103 GLY   B N   
5956 C CA  A GLY   B 103 ? 0.3841 0.3330 0.2628 0.0323  0.0430  0.0393  103 GLY   B CA  
5957 C CA  B GLY   B 103 ? 0.3835 0.3196 0.2419 0.0253  0.0477  0.0723  103 GLY   B CA  
5958 C C   A GLY   B 103 ? 0.3726 0.3250 0.2635 0.0354  0.0577  0.0325  103 GLY   B C   
5959 C C   B GLY   B 103 ? 0.3669 0.3078 0.2311 0.0227  0.0650  0.0586  103 GLY   B C   
5960 O O   A GLY   B 103 ? 0.3764 0.3295 0.2776 0.0343  0.0586  0.0354  103 GLY   B O   
5961 O O   B GLY   B 103 ? 0.3710 0.3141 0.2540 0.0249  0.0647  0.0542  103 GLY   B O   
5968 N N   A GLU   B 104 ? 0.3558 0.3115 0.2550 0.0397  0.0678  0.0177  104 GLU   B N   
5969 N N   B GLU   B 104 ? 0.3462 0.2866 0.2100 0.0170  0.0707  0.0387  104 GLU   B N   
5970 C CA  A GLU   B 104 ? 0.3397 0.3013 0.2451 0.0414  0.0685  0.0058  104 GLU   B CA  
5971 C CA  B GLU   B 104 ? 0.3274 0.2700 0.1818 0.0080  0.0628  0.0244  104 GLU   B CA  
5972 C C   A GLU   B 104 ? 0.3430 0.3033 0.2597 0.0263  0.0790  0.0027  104 GLU   B C   
5973 C C   B GLU   B 104 ? 0.3297 0.2750 0.1928 -0.0083 0.0743  0.0110  104 GLU   B C   
5974 O O   A GLU   B 104 ? 0.3456 0.3050 0.2713 0.0229  0.0760  0.0008  104 GLU   B O   
5975 O O   B GLU   B 104 ? 0.3369 0.2811 0.2177 -0.0110 0.0692  0.0046  104 GLU   B O   
5976 C CB  A GLU   B 104 ? 0.3245 0.2878 0.2383 0.0570  0.0523  -0.0089 104 GLU   B CB  
5977 C CB  B GLU   B 104 ? 0.3131 0.2471 0.1735 0.0109  0.0368  0.0146  104 GLU   B CB  
5978 C CG  A GLU   B 104 ? 0.3113 0.2778 0.2304 0.0703  0.0343  -0.0288 104 GLU   B CG  
5979 C CG  B GLU   B 104 ? 0.3034 0.2296 0.1598 0.0127  0.0135  -0.0038 104 GLU   B CG  
5980 C CD  A GLU   B 104 ? 0.3000 0.2684 0.2286 0.0829  0.0155  -0.0381 104 GLU   B CD  
5981 C CD  B GLU   B 104 ? 0.2965 0.2125 0.1610 0.0071  -0.0022 -0.0024 104 GLU   B CD  
5982 O OE1 A GLU   B 104 ? 0.2874 0.2596 0.2194 0.0939  0.0225  -0.0394 104 GLU   B OE1 
5983 O OE1 B GLU   B 104 ? 0.2794 0.1919 0.1723 0.0050  0.0085  0.0044  104 GLU   B OE1 
5984 O OE2 A GLU   B 104 ? 0.3020 0.2736 0.2478 0.0800  -0.0046 -0.0399 104 GLU   B OE2 
5985 O OE2 B GLU   B 104 ? 0.3023 0.2224 0.1596 -0.0053 -0.0213 0.0052  104 GLU   B OE2 
5998 N N   A ASP   B 105 ? 0.3428 0.3072 0.2738 0.0137  0.0886  0.0033  105 ASP   B N   
5999 N N   B ASP   B 105 ? 0.3229 0.2790 0.2057 -0.0241 0.0904  0.0083  105 ASP   B N   
6000 C CA  A ASP   B 105 ? 0.3447 0.3095 0.2940 0.0028  0.0950  0.0005  105 ASP   B CA  
6001 C CA  B ASP   B 105 ? 0.3199 0.2821 0.2372 -0.0395 0.1035  -0.0028 105 ASP   B CA  
6002 C C   A ASP   B 105 ? 0.3366 0.2937 0.2802 -0.0010 0.0941  -0.0036 105 ASP   B C   
6003 C C   B ASP   B 105 ? 0.3006 0.2495 0.2205 -0.0507 0.0949  -0.0156 105 ASP   B C   
6004 O O   A ASP   B 105 ? 0.3324 0.2910 0.2768 0.0005  0.0995  -0.0040 105 ASP   B O   
6005 O O   B ASP   B 105 ? 0.2775 0.2349 0.2104 -0.0585 0.0901  -0.0258 105 ASP   B O   
6006 C CB  A ASP   B 105 ? 0.3523 0.3241 0.3366 -0.0002 0.0994  -0.0011 105 ASP   B CB  
6007 C CB  B ASP   B 105 ? 0.3309 0.3104 0.2921 -0.0378 0.1228  -0.0110 105 ASP   B CB  
6008 C CG  A ASP   B 105 ? 0.3574 0.3337 0.3758 -0.0038 0.1067  0.0001  105 ASP   B CG  
6009 C CG  B ASP   B 105 ? 0.3381 0.3293 0.3376 -0.0375 0.1438  -0.0130 105 ASP   B CG  
6010 O OD1 A ASP   B 105 ? 0.3582 0.3389 0.3772 -0.0066 0.1090  0.0060  105 ASP   B OD1 
6011 O OD1 B ASP   B 105 ? 0.3409 0.3413 0.3446 -0.0392 0.1484  -0.0129 105 ASP   B OD1 
6012 O OD2 A ASP   B 105 ? 0.3598 0.3376 0.4023 -0.0037 0.1060  -0.0027 105 ASP   B OD2 
6013 O OD2 B ASP   B 105 ? 0.3366 0.3355 0.3479 -0.0403 0.1612  -0.0087 105 ASP   B OD2 
6022 N N   A ILE   B 106 ? 0.3324 0.2800 0.2824 -0.0019 0.0820  -0.0048 106 ILE   B N   
6023 N N   B ILE   B 106 ? 0.3032 0.2323 0.2351 -0.0509 0.0813  -0.0151 106 ILE   B N   
6024 C CA  A ILE   B 106 ? 0.3225 0.2660 0.2874 -0.0021 0.0807  -0.0056 106 ILE   B CA  
6025 C CA  B ILE   B 106 ? 0.2935 0.2161 0.2493 -0.0521 0.0886  -0.0103 106 ILE   B CA  
6026 C C   A ILE   B 106 ? 0.3045 0.2626 0.2814 0.0007  0.0836  -0.0149 106 ILE   B C   
6027 C C   B ILE   B 106 ? 0.2667 0.2165 0.2339 -0.0502 0.0957  -0.0301 106 ILE   B C   
6028 O O   A ILE   B 106 ? 0.3027 0.2521 0.2840 0.0037  0.0788  -0.0147 106 ILE   B O   
6029 O O   B ILE   B 106 ? 0.2530 0.1936 0.2280 -0.0565 0.0840  -0.0369 106 ILE   B O   
6030 C CB  A ILE   B 106 ? 0.3320 0.2596 0.2994 -0.0058 0.0739  0.0023  106 ILE   B CB  
6031 C CB  B ILE   B 106 ? 0.3125 0.2100 0.2792 -0.0521 0.0843  0.0098  106 ILE   B CB  
6032 C CG1 A ILE   B 106 ? 0.3360 0.2561 0.2991 -0.0026 0.0665  0.0038  106 ILE   B CG1 
6033 C CG1 B ILE   B 106 ? 0.3217 0.2107 0.2880 -0.0361 0.0754  0.0105  106 ILE   B CG1 
6034 C CG2 A ILE   B 106 ? 0.3365 0.2618 0.3162 -0.0101 0.0717  0.0061  106 ILE   B CG2 
6035 C CG2 B ILE   B 106 ? 0.3196 0.2119 0.3040 -0.0615 0.0837  0.0177  106 ILE   B CG2 
6036 C CD1 A ILE   B 106 ? 0.3375 0.2551 0.2935 0.0010  0.0655  0.0087  106 ILE   B CD1 
6037 C CD1 B ILE   B 106 ? 0.3257 0.2127 0.2810 -0.0239 0.0771  0.0203  106 ILE   B CD1 
6060 N N   A GLN   B 107 ? 0.2906 0.2721 0.2919 -0.0051 0.0806  -0.0177 107 GLN   B N   
6061 N N   B GLN   B 107 ? 0.2603 0.2471 0.2601 -0.0492 0.0950  -0.0323 107 GLN   B N   
6062 C CA  A GLN   B 107 ? 0.2764 0.2780 0.3056 -0.0091 0.0737  -0.0171 107 GLN   B CA  
6063 C CA  B GLN   B 107 ? 0.2567 0.2721 0.2912 -0.0402 0.0906  -0.0305 107 GLN   B CA  
6064 C C   A GLN   B 107 ? 0.2433 0.2556 0.2781 -0.0031 0.0577  -0.0261 107 GLN   B C   
6065 C C   B GLN   B 107 ? 0.2319 0.2579 0.2742 -0.0198 0.0646  -0.0363 107 GLN   B C   
6066 O O   A GLN   B 107 ? 0.2416 0.2563 0.2902 0.0074  0.0462  -0.0334 107 GLN   B O   
6067 O O   B GLN   B 107 ? 0.2307 0.2706 0.2994 -0.0101 0.0459  -0.0499 107 GLN   B O   
6068 C CB  A GLN   B 107 ? 0.2987 0.3073 0.3612 -0.0134 0.0688  -0.0108 107 GLN   B CB  
6069 C CB  B GLN   B 107 ? 0.2883 0.3129 0.3637 -0.0400 0.0843  -0.0259 107 GLN   B CB  
6070 C CG  A GLN   B 107 ? 0.3209 0.3322 0.4203 -0.0127 0.0548  -0.0051 107 GLN   B CG  
6071 C CG  B GLN   B 107 ? 0.3234 0.3478 0.4414 -0.0319 0.0608  -0.0217 107 GLN   B CG  
6072 C CD  A GLN   B 107 ? 0.3366 0.3514 0.4682 -0.0128 0.0459  0.0012  107 GLN   B CD  
6073 C CD  B GLN   B 107 ? 0.3492 0.3739 0.5020 -0.0264 0.0435  -0.0169 107 GLN   B CD  
6074 O OE1 A GLN   B 107 ? 0.3413 0.3601 0.4853 -0.0105 0.0467  0.0005  107 GLN   B OE1 
6075 O OE1 B GLN   B 107 ? 0.3608 0.3866 0.5271 -0.0228 0.0421  -0.0159 107 GLN   B OE1 
6076 N NE2 A GLN   B 107 ? 0.3438 0.3572 0.4865 -0.0116 0.0414  0.0068  107 GLN   B NE2 
6077 N NE2 B GLN   B 107 ? 0.3597 0.3804 0.5207 -0.0245 0.0345  -0.0146 107 GLN   B NE2 
6094 N N   . LEU   B 108 ? 0.2091 0.2329 0.2509 -0.0058 0.0552  -0.0271 108 LEU   B N   
6095 C CA  . LEU   B 108 ? 0.1960 0.2086 0.2141 0.0149  0.0384  -0.0053 108 LEU   B CA  
6096 C C   . LEU   B 108 ? 0.1710 0.1719 0.2137 0.0170  0.0157  0.0138  108 LEU   B C   
6097 O O   . LEU   B 108 ? 0.1775 0.1598 0.2227 0.0228  0.0101  0.0142  108 LEU   B O   
6098 C CB  . LEU   B 108 ? 0.2197 0.2307 0.2043 0.0174  0.0367  -0.0081 108 LEU   B CB  
6099 C CG  . LEU   B 108 ? 0.2390 0.2550 0.2170 0.0229  0.0310  -0.0264 108 LEU   B CG  
6100 C CD1 . LEU   B 108 ? 0.2463 0.2711 0.2052 0.0104  0.0288  -0.0291 108 LEU   B CD1 
6101 C CD2 . LEU   B 108 ? 0.2601 0.2660 0.2477 0.0299  0.0250  -0.0371 108 LEU   B CD2 
6114 N N   . LEU   B 109 ? 0.1618 0.1528 0.2105 0.0213  0.0196  0.0217  109 LEU   B N   
6115 C CA  . LEU   B 109 ? 0.1468 0.1326 0.2216 0.0073  0.0174  0.0212  109 LEU   B CA  
6116 C C   . LEU   B 109 ? 0.1364 0.1166 0.2180 0.0022  0.0155  0.0122  109 LEU   B C   
6117 O O   . LEU   B 109 ? 0.1306 0.1204 0.2165 0.0061  0.0100  0.0203  109 LEU   B O   
6118 C CB  . LEU   B 109 ? 0.1575 0.1278 0.2159 0.0116  0.0068  0.0317  109 LEU   B CB  
6119 C CG  . LEU   B 109 ? 0.1608 0.1286 0.2112 0.0102  0.0025  0.0200  109 LEU   B CG  
6120 C CD1 . LEU   B 109 ? 0.1583 0.1384 0.2096 0.0130  0.0095  0.0127  109 LEU   B CD1 
6121 C CD2 . LEU   B 109 ? 0.1688 0.1348 0.2268 0.0084  -0.0028 0.0118  109 LEU   B CD2 
6133 N N   . LYS   B 110 ? 0.1341 0.1161 0.2152 0.0008  0.0209  0.0258  110 LYS   B N   
6134 C CA  . LYS   B 110 ? 0.1320 0.1157 0.2200 0.0050  0.0175  0.0135  110 LYS   B CA  
6135 C C   . LYS   B 110 ? 0.1285 0.1220 0.2116 0.0059  0.0137  0.0063  110 LYS   B C   
6136 O O   . LYS   B 110 ? 0.1279 0.1208 0.2022 -0.0014 0.0095  0.0067  110 LYS   B O   
6137 C CB  . LYS   B 110 ? 0.1363 0.1224 0.2341 -0.0031 0.0153  0.0100  110 LYS   B CB  
6138 C CG  . LYS   B 110 ? 0.1370 0.1199 0.2425 -0.0090 0.0025  0.0127  110 LYS   B CG  
6139 C CD  . LYS   B 110 ? 0.1438 0.1218 0.2543 -0.0096 -0.0023 0.0107  110 LYS   B CD  
6140 C CE  . LYS   B 110 ? 0.1353 0.1344 0.2765 -0.0054 -0.0052 0.0019  110 LYS   B CE  
6141 N NZ  . LYS   B 110 ? 0.1280 0.1479 0.2766 -0.0019 -0.0147 0.0070  110 LYS   B NZ  
6155 N N   . SER   B 111 ? 0.1342 0.1211 0.2125 0.0001  0.0153  0.0146  111 SER   B N   
6156 C CA  . SER   B 111 ? 0.1394 0.1244 0.2129 0.0053  0.0042  0.0160  111 SER   B CA  
6157 C C   . SER   B 111 ? 0.1320 0.1227 0.2027 0.0013  0.0032  0.0058  111 SER   B C   
6158 O O   . SER   B 111 ? 0.1314 0.1209 0.2198 -0.0012 -0.0010 0.0002  111 SER   B O   
6159 C CB  . SER   B 111 ? 0.1545 0.1467 0.2236 0.0065  0.0124  0.0164  111 SER   B CB  
6160 O OG  . SER   B 111 ? 0.1736 0.1887 0.2331 0.0079  0.0266  0.0222  111 SER   B OG  
6166 N N   . ALA   B 112 ? 0.1222 0.1300 0.2076 0.0106  0.0081  0.0168  112 ALA   B N   
6167 C CA  . ALA   B 112 ? 0.1170 0.1303 0.1882 0.0072  0.0004  0.0032  112 ALA   B CA  
6168 C C   . ALA   B 112 ? 0.1124 0.1160 0.1961 0.0038  -0.0004 -0.0004 112 ALA   B C   
6169 O O   . ALA   B 112 ? 0.1195 0.1151 0.1989 -0.0053 -0.0035 -0.0047 112 ALA   B O   
6170 C CB  . ALA   B 112 ? 0.1328 0.1363 0.1950 0.0135  -0.0025 0.0070  112 ALA   B CB  
6176 N N   . TYR   B 113 ? 0.1125 0.1087 0.2088 0.0033  -0.0008 0.0057  113 TYR   B N   
6177 C CA  . TYR   B 113 ? 0.1133 0.1121 0.2032 -0.0017 0.0073  -0.0046 113 TYR   B CA  
6178 C C   . TYR   B 113 ? 0.1113 0.1055 0.1925 -0.0009 -0.0006 0.0003  113 TYR   B C   
6179 O O   . TYR   B 113 ? 0.1156 0.1076 0.2039 -0.0030 -0.0047 -0.0072 113 TYR   B O   
6180 C CB  . TYR   B 113 ? 0.1175 0.1062 0.2010 0.0001  0.0026  0.0044  113 TYR   B CB  
6181 C CG  . TYR   B 113 ? 0.1224 0.1123 0.2076 -0.0080 -0.0059 0.0075  113 TYR   B CG  
6182 C CD1 . TYR   B 113 ? 0.1289 0.1092 0.2228 -0.0072 0.0037  0.0207  113 TYR   B CD1 
6183 C CD2 . TYR   B 113 ? 0.1305 0.1063 0.2091 -0.0055 -0.0018 0.0126  113 TYR   B CD2 
6184 C CE1 . TYR   B 113 ? 0.1295 0.1113 0.2166 -0.0028 0.0158  0.0054  113 TYR   B CE1 
6185 C CE2 . TYR   B 113 ? 0.1330 0.1026 0.2210 0.0021  0.0028  0.0159  113 TYR   B CE2 
6186 C CZ  . TYR   B 113 ? 0.1260 0.1107 0.2287 0.0009  -0.0026 0.0047  113 TYR   B CZ  
6187 O OH  . TYR   B 113 ? 0.1328 0.1070 0.2551 0.0102  0.0112  0.0121  113 TYR   B OH  
6197 N N   . GLU   B 114 ? 0.1124 0.1049 0.2016 0.0025  -0.0004 0.0127  114 GLU   B N   
6198 C CA  . GLU   B 114 ? 0.1131 0.1027 0.2055 0.0023  0.0001  0.0003  114 GLU   B CA  
6199 C C   . GLU   B 114 ? 0.1112 0.1013 0.2022 0.0052  0.0025  -0.0006 114 GLU   B C   
6200 O O   . GLU   B 114 ? 0.1130 0.1076 0.2079 0.0022  -0.0059 0.0048  114 GLU   B O   
6201 C CB  . GLU   B 114 ? 0.1168 0.1037 0.1994 0.0036  0.0012  0.0138  114 GLU   B CB  
6202 C CG  . GLU   B 114 ? 0.1218 0.1146 0.2120 -0.0012 0.0041  0.0069  114 GLU   B CG  
6203 C CD  . GLU   B 114 ? 0.1210 0.1130 0.2110 -0.0086 -0.0005 0.0079  114 GLU   B CD  
6204 O OE1 . GLU   B 114 ? 0.1189 0.1281 0.2207 -0.0068 0.0104  0.0079  114 GLU   B OE1 
6205 O OE2 . GLU   B 114 ? 0.1170 0.1348 0.2304 -0.0140 0.0008  0.0143  114 GLU   B OE2 
6212 N N   . ASN   B 115 ? 0.1129 0.1019 0.2112 -0.0024 -0.0095 -0.0017 115 ASN   B N   
6213 C CA  . ASN   B 115 ? 0.1169 0.1064 0.1980 -0.0026 -0.0052 0.0016  115 ASN   B CA  
6214 C C   . ASN   B 115 ? 0.1082 0.1071 0.1977 -0.0087 -0.0069 -0.0001 115 ASN   B C   
6215 O O   . ASN   B 115 ? 0.1193 0.1114 0.2086 -0.0103 -0.0030 0.0012  115 ASN   B O   
6216 C CB  . ASN   B 115 ? 0.1253 0.1248 0.1957 -0.0032 -0.0033 0.0019  115 ASN   B CB  
6217 C CG  . ASN   B 115 ? 0.1357 0.1294 0.2004 0.0093  -0.0004 -0.0010 115 ASN   B CG  
6218 O OD1 . ASN   B 115 ? 0.1794 0.1381 0.2190 0.0025  0.0075  -0.0096 115 ASN   B OD1 
6219 N ND2 . ASN   B 115 ? 0.1360 0.1344 0.1982 -0.0005 -0.0041 0.0051  115 ASN   B ND2 
6226 N N   . PHE   B 116 ? 0.1140 0.1041 0.1860 -0.0019 -0.0023 0.0032  116 PHE   B N   
6227 C CA  . PHE   B 116 ? 0.1184 0.1044 0.1887 -0.0062 -0.0052 0.0036  116 PHE   B CA  
6228 C C   . PHE   B 116 ? 0.1244 0.0953 0.1976 -0.0071 -0.0050 0.0044  116 PHE   B C   
6229 O O   . PHE   B 116 ? 0.1230 0.1062 0.1978 -0.0018 -0.0133 0.0055  116 PHE   B O   
6230 C CB  . PHE   B 116 ? 0.1144 0.1062 0.1865 -0.0030 -0.0099 0.0012  116 PHE   B CB  
6231 C CG  . PHE   B 116 ? 0.1126 0.1097 0.1852 -0.0031 -0.0103 -0.0027 116 PHE   B CG  
6232 C CD1 . PHE   B 116 ? 0.1286 0.1100 0.2028 0.0019  -0.0068 0.0013  116 PHE   B CD1 
6233 C CD2 . PHE   B 116 ? 0.1201 0.1130 0.1845 -0.0008 0.0040  -0.0026 116 PHE   B CD2 
6234 C CE1 . PHE   B 116 ? 0.1271 0.1165 0.1936 -0.0011 -0.0110 0.0039  116 PHE   B CE1 
6235 C CE2 . PHE   B 116 ? 0.1196 0.1127 0.1876 0.0027  -0.0009 -0.0024 116 PHE   B CE2 
6236 C CZ  . PHE   B 116 ? 0.1129 0.1193 0.1851 -0.0011 -0.0083 0.0065  116 PHE   B CZ  
6246 N N   . ASN   B 117 ? 0.1200 0.1004 0.2004 0.0006  -0.0123 0.0021  117 ASN   B N   
6247 C CA  . ASN   B 117 ? 0.1198 0.1064 0.1943 0.0054  -0.0092 0.0041  117 ASN   B CA  
6248 C C   . ASN   B 117 ? 0.1247 0.1020 0.2156 0.0027  -0.0068 0.0037  117 ASN   B C   
6249 O O   . ASN   B 117 ? 0.1348 0.1138 0.2347 -0.0038 -0.0305 0.0085  117 ASN   B O   
6250 C CB  . ASN   B 117 ? 0.1237 0.1138 0.1956 0.0029  -0.0095 0.0040  117 ASN   B CB  
6251 C CG  . ASN   B 117 ? 0.1194 0.1127 0.2018 0.0012  -0.0144 -0.0048 117 ASN   B CG  
6252 O OD1 . ASN   B 117 ? 0.1415 0.1146 0.2139 -0.0102 -0.0031 0.0010  117 ASN   B OD1 
6253 N ND2 . ASN   B 117 ? 0.1206 0.1177 0.1974 -0.0016 -0.0006 -0.0030 117 ASN   B ND2 
6260 N N   . GLN   B 118 ? 0.1291 0.0975 0.2031 -0.0029 -0.0187 0.0026  118 GLN   B N   
6261 C CA  . GLN   B 118 ? 0.1303 0.1102 0.2086 0.0006  -0.0122 0.0008  118 GLN   B CA  
6262 C C   . GLN   B 118 ? 0.1334 0.1128 0.2159 0.0005  -0.0121 -0.0018 118 GLN   B C   
6263 O O   . GLN   B 118 ? 0.1479 0.1060 0.2587 -0.0107 0.0085  0.0045  118 GLN   B O   
6264 C CB  . GLN   B 118 ? 0.1321 0.1136 0.2233 0.0006  -0.0139 0.0028  118 GLN   B CB  
6265 C CG  . GLN   B 118 ? 0.1433 0.1168 0.2165 0.0077  -0.0126 -0.0052 118 GLN   B CG  
6266 C CD  . GLN   B 118 ? 0.1458 0.1132 0.2098 -0.0000 -0.0071 -0.0107 118 GLN   B CD  
6267 O OE1 . GLN   B 118 ? 0.1543 0.1195 0.2256 -0.0011 0.0043  0.0068  118 GLN   B OE1 
6268 N NE2 . GLN   B 118 ? 0.1567 0.1080 0.2154 0.0048  -0.0192 0.0104  118 GLN   B NE2 
6277 N N   . HIS   B 119 ? 0.1358 0.1067 0.1940 -0.0045 -0.0135 0.0091  119 HIS   B N   
6278 C CA  . HIS   B 119 ? 0.1445 0.1166 0.1891 -0.0001 -0.0192 0.0071  119 HIS   B CA  
6279 C C   . HIS   B 119 ? 0.1537 0.1213 0.1845 0.0001  -0.0263 0.0100  119 HIS   B C   
6280 O O   . HIS   B 119 ? 0.1498 0.1205 0.2121 -0.0213 -0.0088 0.0012  119 HIS   B O   
6281 C CB  . HIS   B 119 ? 0.1491 0.1282 0.2007 0.0009  -0.0219 -0.0016 119 HIS   B CB  
6282 C CG  . HIS   B 119 ? 0.1540 0.1531 0.2240 0.0124  -0.0381 -0.0140 119 HIS   B CG  
6283 N ND1 . HIS   B 119 ? 0.1705 0.1684 0.2430 0.0068  -0.0484 -0.0353 119 HIS   B ND1 
6284 C CD2 . HIS   B 119 ? 0.1705 0.1770 0.2299 0.0360  -0.0527 -0.0200 119 HIS   B CD2 
6285 C CE1 . HIS   B 119 ? 0.1881 0.1809 0.2496 0.0246  -0.0557 -0.0428 119 HIS   B CE1 
6286 N NE2 . HIS   B 119 ? 0.1878 0.1943 0.2338 0.0354  -0.0542 -0.0402 119 HIS   B NE2 
6294 N N   A GLU   B 120 ? 0.1694 0.1276 0.1842 -0.0016 -0.0253 0.0099  120 GLU   B N   
6295 N N   B GLU   B 120 ? 0.1649 0.1164 0.1853 -0.0051 -0.0276 0.0115  120 GLU   B N   
6296 C CA  A GLU   B 120 ? 0.1867 0.1416 0.1951 0.0016  -0.0299 0.0189  120 GLU   B CA  
6297 C CA  B GLU   B 120 ? 0.1814 0.1268 0.1952 -0.0010 -0.0359 0.0264  120 GLU   B CA  
6298 C C   A GLU   B 120 ? 0.1696 0.1300 0.1852 -0.0058 -0.0287 0.0201  120 GLU   B C   
6299 C C   B GLU   B 120 ? 0.1650 0.1200 0.1897 -0.0097 -0.0332 0.0273  120 GLU   B C   
6300 O O   A GLU   B 120 ? 0.1666 0.1396 0.1787 -0.0092 -0.0276 0.0120  120 GLU   B O   
6301 O O   B GLU   B 120 ? 0.1592 0.1336 0.1919 -0.0178 -0.0330 0.0155  120 GLU   B O   
6302 C CB  A GLU   B 120 ? 0.2269 0.1695 0.2383 0.0129  -0.0408 0.0306  120 GLU   B CB  
6303 C CB  B GLU   B 120 ? 0.2251 0.1520 0.2367 0.0115  -0.0518 0.0472  120 GLU   B CB  
6304 C CG  A GLU   B 120 ? 0.2600 0.2039 0.3020 0.0185  -0.0500 0.0397  120 GLU   B CG  
6305 C CG  B GLU   B 120 ? 0.2592 0.1959 0.3107 0.0141  -0.0637 0.0581  120 GLU   B CG  
6306 C CD  A GLU   B 120 ? 0.2873 0.2338 0.3629 0.0165  -0.0523 0.0559  120 GLU   B CD  
6307 C CD  B GLU   B 120 ? 0.2875 0.2335 0.3846 0.0031  -0.0605 0.0757  120 GLU   B CD  
6308 O OE1 A GLU   B 120 ? 0.3010 0.2470 0.3819 0.0230  -0.0533 0.0720  120 GLU   B OE1 
6309 O OE1 B GLU   B 120 ? 0.3059 0.2604 0.4126 -0.0005 -0.0470 0.0839  120 GLU   B OE1 
6310 O OE2 A GLU   B 120 ? 0.2989 0.2455 0.3915 0.0109  -0.0566 0.0520  120 GLU   B OE2 
6311 O OE2 B GLU   B 120 ? 0.3004 0.2467 0.4222 -0.0102 -0.0607 0.0761  120 GLU   B OE2 
6324 N N   . VAL   B 121 ? 0.1557 0.1186 0.1932 -0.0096 -0.0246 0.0175  121 VAL   B N   
6325 C CA  . VAL   B 121 ? 0.1458 0.1310 0.1893 -0.0092 -0.0154 0.0164  121 VAL   B CA  
6326 C C   . VAL   B 121 ? 0.1398 0.1259 0.1887 -0.0171 -0.0134 0.0138  121 VAL   B C   
6327 O O   . VAL   B 121 ? 0.1515 0.1202 0.2074 -0.0244 -0.0212 0.0071  121 VAL   B O   
6328 C CB  . VAL   B 121 ? 0.1721 0.1720 0.1849 0.0001  -0.0201 0.0208  121 VAL   B CB  
6329 C CG1 . VAL   B 121 ? 0.1790 0.1851 0.2178 -0.0119 -0.0111 0.0171  121 VAL   B CG1 
6330 C CG2 . VAL   B 121 ? 0.1964 0.1939 0.1944 0.0085  -0.0103 0.0111  121 VAL   B CG2 
6341 N N   . LEU   B 122 ? 0.1370 0.1180 0.1784 -0.0133 -0.0235 0.0085  122 LEU   B N   
6342 C CA  . LEU   B 122 ? 0.1284 0.1233 0.1707 -0.0158 -0.0183 0.0074  122 LEU   B CA  
6343 C C   . LEU   B 122 ? 0.1312 0.1127 0.1785 -0.0210 -0.0167 0.0125  122 LEU   B C   
6344 O O   . LEU   B 122 ? 0.1402 0.1189 0.1993 -0.0237 -0.0260 0.0035  122 LEU   B O   
6345 C CB  . LEU   B 122 ? 0.1466 0.1338 0.1943 -0.0044 -0.0188 0.0112  122 LEU   B CB  
6346 C CG  . LEU   B 122 ? 0.1450 0.1458 0.2073 -0.0097 -0.0076 0.0094  122 LEU   B CG  
6347 C CD1 . LEU   B 122 ? 0.1513 0.1660 0.2156 -0.0096 -0.0155 0.0168  122 LEU   B CD1 
6348 C CD2 . LEU   B 122 ? 0.1457 0.1508 0.2030 -0.0069 -0.0092 0.0037  122 LEU   B CD2 
6360 N N   . LEU   B 123 ? 0.1321 0.1104 0.1720 -0.0164 -0.0059 0.0077  123 LEU   B N   
6361 C CA  . LEU   B 123 ? 0.1316 0.1154 0.1717 -0.0205 -0.0130 0.0051  123 LEU   B CA  
6362 C C   . LEU   B 123 ? 0.1247 0.1104 0.1675 -0.0204 -0.0170 0.0036  123 LEU   B C   
6363 O O   . LEU   B 123 ? 0.1428 0.1158 0.1654 -0.0290 -0.0181 -0.0004 123 LEU   B O   
6364 C CB  . LEU   B 123 ? 0.1386 0.1187 0.1823 -0.0248 -0.0075 0.0068  123 LEU   B CB  
6365 C CG  . LEU   B 123 ? 0.1367 0.1206 0.1889 -0.0129 -0.0035 0.0101  123 LEU   B CG  
6366 C CD1 . LEU   B 123 ? 0.1432 0.1272 0.2015 -0.0136 0.0004  -0.0086 123 LEU   B CD1 
6367 C CD2 . LEU   B 123 ? 0.1438 0.1305 0.2053 -0.0082 0.0034  0.0208  123 LEU   B CD2 
6379 N N   . ALA   B 124 ? 0.1248 0.1080 0.1823 -0.0191 -0.0070 -0.0026 124 ALA   B N   
6380 C CA  . ALA   B 124 ? 0.1241 0.1077 0.1881 -0.0140 -0.0052 -0.0083 124 ALA   B CA  
6381 C C   . ALA   B 124 ? 0.1155 0.1092 0.1793 -0.0174 -0.0093 -0.0037 124 ALA   B C   
6382 O O   . ALA   B 124 ? 0.1305 0.1078 0.1770 -0.0145 -0.0110 -0.0011 124 ALA   B O   
6383 C CB  . ALA   B 124 ? 0.1274 0.1180 0.1900 -0.0105 -0.0020 0.0022  124 ALA   B CB  
6389 N N   . PRO   B 125 ? 0.1271 0.1116 0.1710 -0.0152 -0.0174 0.0043  125 PRO   B N   
6390 C CA  . PRO   B 125 ? 0.1328 0.1155 0.1925 -0.0153 -0.0203 0.0159  125 PRO   B CA  
6391 C C   . PRO   B 125 ? 0.1275 0.1099 0.2008 -0.0171 -0.0181 0.0026  125 PRO   B C   
6392 O O   . PRO   B 125 ? 0.1324 0.1076 0.2202 -0.0140 -0.0028 0.0115  125 PRO   B O   
6393 C CB  . PRO   B 125 ? 0.1419 0.1363 0.1981 -0.0199 -0.0194 0.0186  125 PRO   B CB  
6394 C CG  . PRO   B 125 ? 0.1485 0.1382 0.1926 -0.0280 -0.0241 0.0202  125 PRO   B CG  
6395 C CD  . PRO   B 125 ? 0.1382 0.1223 0.1706 -0.0264 -0.0129 0.0099  125 PRO   B CD  
6403 N N   . LEU   B 126 ? 0.1351 0.1074 0.2066 -0.0119 0.0140  0.0057  126 LEU   B N   
6404 C CA  . LEU   B 126 ? 0.1405 0.1100 0.2064 -0.0099 0.0098  0.0137  126 LEU   B CA  
6405 C C   . LEU   B 126 ? 0.1301 0.1157 0.2057 -0.0003 0.0118  0.0134  126 LEU   B C   
6406 O O   . LEU   B 126 ? 0.1487 0.1472 0.2169 0.0177  -0.0052 -0.0097 126 LEU   B O   
6407 C CB  . LEU   B 126 ? 0.1537 0.1208 0.2319 -0.0149 0.0236  0.0068  126 LEU   B CB  
6408 C CG  . LEU   B 126 ? 0.1715 0.1268 0.2451 -0.0262 0.0142  -0.0059 126 LEU   B CG  
6409 C CD1 . LEU   B 126 ? 0.1874 0.1336 0.2794 -0.0231 0.0058  -0.0151 126 LEU   B CD1 
6410 C CD2 . LEU   B 126 ? 0.1690 0.1356 0.2420 -0.0289 0.0013  -0.0037 126 LEU   B CD2 
6422 N N   . LEU   B 127 ? 0.1282 0.1152 0.2067 0.0036  0.0114  0.0142  127 LEU   B N   
6423 C CA  . LEU   B 127 ? 0.1302 0.1229 0.2045 -0.0027 0.0151  0.0116  127 LEU   B CA  
6424 C C   . LEU   B 127 ? 0.1301 0.1140 0.2011 0.0017  0.0152  0.0165  127 LEU   B C   
6425 O O   . LEU   B 127 ? 0.1356 0.1184 0.2213 -0.0100 0.0083  0.0133  127 LEU   B O   
6426 C CB  . LEU   B 127 ? 0.1431 0.1208 0.2124 -0.0002 0.0119  0.0197  127 LEU   B CB  
6427 C CG  . LEU   B 127 ? 0.1560 0.1192 0.2192 0.0062  0.0107  0.0168  127 LEU   B CG  
6428 C CD1 . LEU   B 127 ? 0.1586 0.1220 0.2180 0.0090  -0.0019 0.0149  127 LEU   B CD1 
6429 C CD2 . LEU   B 127 ? 0.1603 0.1312 0.2353 -0.0005 0.0109  0.0302  127 LEU   B CD2 
6441 N N   . SER   B 128 ? 0.1340 0.1173 0.2028 0.0009  -0.0092 0.0090  128 SER   B N   
6442 C CA  . SER   B 128 ? 0.1467 0.1248 0.2058 0.0094  -0.0064 0.0116  128 SER   B CA  
6443 C C   . SER   B 128 ? 0.1553 0.1313 0.2132 0.0055  -0.0230 0.0157  128 SER   B C   
6444 O O   . SER   B 128 ? 0.1690 0.1305 0.2457 0.0080  -0.0192 0.0315  128 SER   B O   
6445 C CB  . SER   B 128 ? 0.1562 0.1286 0.2125 0.0115  -0.0003 0.0203  128 SER   B CB  
6446 O OG  . SER   B 128 ? 0.1605 0.1432 0.2202 0.0169  0.0039  0.0243  128 SER   B OG  
6452 N N   . ALA   B 129 ? 0.1667 0.1303 0.2260 0.0260  -0.0167 0.0019  129 ALA   B N   
6453 C CA  . ALA   B 129 ? 0.1811 0.1439 0.2345 0.0321  -0.0168 -0.0036 129 ALA   B CA  
6454 C C   . ALA   B 129 ? 0.1638 0.1380 0.2256 0.0233  0.0035  0.0027  129 ALA   B C   
6455 O O   . ALA   B 129 ? 0.1532 0.1405 0.2365 0.0138  -0.0101 0.0128  129 ALA   B O   
6456 C CB  . ALA   B 129 ? 0.2021 0.1663 0.2633 0.0338  -0.0167 -0.0076 129 ALA   B CB  
6462 N N   . GLY   B 130 ? 0.1704 0.1333 0.2405 0.0263  0.0068  -0.0007 130 GLY   B N   
6463 C CA  . GLY   B 130 ? 0.1697 0.1452 0.2463 0.0312  0.0278  0.0042  130 GLY   B CA  
6464 C C   . GLY   B 130 ? 0.1739 0.1461 0.2317 0.0229  0.0135  0.0137  130 GLY   B C   
6465 O O   . GLY   B 130 ? 0.1920 0.1542 0.2439 0.0202  0.0014  0.0150  130 GLY   B O   
6469 N N   . ILE   B 131 ? 0.1650 0.1592 0.2458 0.0377  0.0091  0.0009  131 ILE   B N   
6470 C CA  . ILE   B 131 ? 0.1849 0.1722 0.2431 0.0327  -0.0022 0.0074  131 ILE   B CA  
6471 C C   . ILE   B 131 ? 0.1925 0.1644 0.2154 0.0264  -0.0048 0.0143  131 ILE   B C   
6472 O O   . ILE   B 131 ? 0.2147 0.1862 0.2216 0.0319  -0.0246 0.0216  131 ILE   B O   
6473 C CB  . ILE   B 131 ? 0.1846 0.2072 0.2589 0.0327  -0.0094 0.0113  131 ILE   B CB  
6474 C CG1 . ILE   B 131 ? 0.1966 0.2269 0.2675 0.0071  -0.0039 0.0078  131 ILE   B CG1 
6475 C CG2 . ILE   B 131 ? 0.1821 0.2277 0.2735 0.0315  -0.0074 0.0094  131 ILE   B CG2 
6476 C CD1 . ILE   B 131 ? 0.2132 0.2487 0.2804 -0.0093 -0.0070 0.0088  131 ILE   B CD1 
6488 N N   . PHE   B 132 ? 0.1737 0.1401 0.2058 0.0223  0.0056  0.0137  132 PHE   B N   
6489 C CA  . PHE   B 132 ? 0.1819 0.1458 0.2042 0.0109  0.0123  0.0082  132 PHE   B CA  
6490 C C   . PHE   B 132 ? 0.1969 0.1621 0.2110 0.0085  0.0130  0.0078  132 PHE   B C   
6491 O O   . PHE   B 132 ? 0.2197 0.1839 0.2411 0.0065  0.0206  0.0081  132 PHE   B O   
6492 C CB  . PHE   B 132 ? 0.1632 0.1479 0.2041 0.0118  0.0146  0.0136  132 PHE   B CB  
6493 C CG  . PHE   B 132 ? 0.1637 0.1523 0.2123 0.0181  0.0135  0.0118  132 PHE   B CG  
6494 C CD1 . PHE   B 132 ? 0.1794 0.1522 0.2459 0.0129  0.0301  0.0202  132 PHE   B CD1 
6495 C CD2 . PHE   B 132 ? 0.1684 0.1536 0.1877 0.0224  0.0030  0.0181  132 PHE   B CD2 
6496 C CE1 . PHE   B 132 ? 0.1863 0.1628 0.2622 0.0110  0.0208  0.0129  132 PHE   B CE1 
6497 C CE2 . PHE   B 132 ? 0.1744 0.1612 0.1898 0.0190  0.0066  0.0063  132 PHE   B CE2 
6498 C CZ  . PHE   B 132 ? 0.1872 0.1610 0.2289 0.0139  0.0003  0.0236  132 PHE   B CZ  
6508 N N   . GLY   B 133 ? 0.1992 0.1512 0.1989 0.0069  0.0061  0.0198  133 GLY   B N   
6509 C CA  . GLY   B 133 ? 0.2098 0.1613 0.2036 -0.0133 0.0100  0.0299  133 GLY   B CA  
6510 C C   . GLY   B 133 ? 0.2131 0.1700 0.2127 -0.0250 0.0137  0.0329  133 GLY   B C   
6511 O O   . GLY   B 133 ? 0.2292 0.1792 0.2593 -0.0375 0.0195  0.0440  133 GLY   B O   
6515 N N   . ALA   B 134 ? 0.1962 0.1687 0.1978 -0.0200 0.0129  0.0179  134 ALA   B N   
6516 C CA  . ALA   B 134 ? 0.1971 0.1589 0.2115 -0.0126 0.0141  0.0073  134 ALA   B CA  
6517 C C   . ALA   B 134 ? 0.2022 0.1507 0.2085 -0.0057 0.0202  0.0105  134 ALA   B C   
6518 O O   . ALA   B 134 ? 0.2067 0.1739 0.2251 0.0015  0.0269  0.0039  134 ALA   B O   
6519 C CB  . ALA   B 134 ? 0.2005 0.1565 0.2435 -0.0028 0.0106  0.0052  134 ALA   B CB  
6525 N N   . ASP   B 135 ? 0.2095 0.1480 0.2090 -0.0105 0.0047  0.0147  135 ASP   B N   
6526 C CA  . ASP   B 135 ? 0.2240 0.1420 0.2257 -0.0064 -0.0117 0.0225  135 ASP   B CA  
6527 C C   . ASP   B 135 ? 0.2062 0.1381 0.2151 0.0009  -0.0047 0.0093  135 ASP   B C   
6528 O O   . ASP   B 135 ? 0.1922 0.1251 0.2285 0.0022  0.0036  0.0132  135 ASP   B O   
6529 C CB  . ASP   B 135 ? 0.2524 0.1499 0.2393 -0.0294 -0.0092 0.0237  135 ASP   B CB  
6530 C CG  . ASP   B 135 ? 0.2798 0.1527 0.2701 -0.0457 -0.0017 0.0191  135 ASP   B CG  
6531 O OD1 . ASP   B 135 ? 0.2931 0.1482 0.2593 -0.0304 -0.0074 0.0164  135 ASP   B OD1 
6532 O OD2 . ASP   B 135 ? 0.3017 0.1832 0.3308 -0.0593 -0.0009 -0.0009 135 ASP   B OD2 
6537 N N   . PRO   B 136 ? 0.2046 0.1413 0.2284 0.0173  -0.0104 0.0125  136 PRO   B N   
6538 C CA  . PRO   B 136 ? 0.1879 0.1347 0.2239 0.0125  -0.0099 0.0032  136 PRO   B CA  
6539 C C   . PRO   B 136 ? 0.1715 0.1267 0.2343 0.0127  -0.0002 0.0005  136 PRO   B C   
6540 O O   . PRO   B 136 ? 0.1557 0.1213 0.2297 0.0112  0.0008  0.0103  136 PRO   B O   
6541 C CB  . PRO   B 136 ? 0.1893 0.1547 0.2342 0.0282  -0.0090 -0.0032 136 PRO   B CB  
6542 C CG  . PRO   B 136 ? 0.2064 0.1592 0.2543 0.0304  -0.0087 -0.0013 136 PRO   B CG  
6543 C CD  . PRO   B 136 ? 0.2128 0.1549 0.2476 0.0401  -0.0064 0.0043  136 PRO   B CD  
6551 N N   . ILE   B 137 ? 0.1799 0.1209 0.2497 0.0112  -0.0050 0.0015  137 ILE   B N   
6552 C CA  . ILE   B 137 ? 0.1833 0.1187 0.2599 -0.0038 -0.0080 -0.0001 137 ILE   B CA  
6553 C C   . ILE   B 137 ? 0.1694 0.1206 0.2501 -0.0091 -0.0006 0.0132  137 ILE   B C   
6554 O O   . ILE   B 137 ? 0.1570 0.1290 0.2480 -0.0061 0.0023  0.0207  137 ILE   B O   
6555 C CB  . ILE   B 137 ? 0.2147 0.1236 0.2908 -0.0012 -0.0124 0.0002  137 ILE   B CB  
6556 C CG1 . ILE   B 137 ? 0.2483 0.1376 0.3392 0.0089  -0.0011 -0.0161 137 ILE   B CG1 
6557 C CG2 . ILE   B 137 ? 0.2197 0.1303 0.3018 -0.0302 -0.0215 0.0047  137 ILE   B CG2 
6558 C CD1 . ILE   B 137 ? 0.2753 0.1667 0.3784 0.0219  -0.0040 -0.0047 137 ILE   B CD1 
6570 N N   . HIS   B 138 ? 0.1746 0.1150 0.2499 -0.0028 0.0071  0.0050  138 HIS   B N   
6571 C CA  . HIS   B 138 ? 0.1799 0.1269 0.2409 -0.0005 0.0164  0.0017  138 HIS   B CA  
6572 C C   . HIS   B 138 ? 0.1642 0.1213 0.2405 -0.0035 0.0195  0.0113  138 HIS   B C   
6573 O O   . HIS   B 138 ? 0.1582 0.1288 0.2610 0.0009  0.0227  0.0267  138 HIS   B O   
6574 C CB  . HIS   B 138 ? 0.2024 0.1415 0.2453 -0.0022 0.0306  0.0027  138 HIS   B CB  
6575 C CG  . HIS   B 138 ? 0.2164 0.1544 0.2406 -0.0012 0.0335  0.0207  138 HIS   B CG  
6576 N ND1 . HIS   B 138 ? 0.2237 0.1676 0.2676 0.0048  0.0425  0.0118  138 HIS   B ND1 
6577 C CD2 . HIS   B 138 ? 0.2308 0.1614 0.2414 -0.0030 0.0390  0.0142  138 HIS   B CD2 
6578 C CE1 . HIS   B 138 ? 0.2298 0.1707 0.2640 0.0057  0.0429  0.0193  138 HIS   B CE1 
6579 N NE2 . HIS   B 138 ? 0.2362 0.1642 0.2614 0.0067  0.0444  0.0151  138 HIS   B NE2 
6587 N N   . SER   B 139 ? 0.1601 0.1085 0.2431 0.0027  0.0145  0.0043  139 SER   B N   
6588 C CA  . SER   B 139 ? 0.1544 0.1075 0.2328 0.0004  0.0035  0.0005  139 SER   B CA  
6589 C C   . SER   B 139 ? 0.1380 0.1065 0.2234 -0.0017 0.0057  -0.0062 139 SER   B C   
6590 O O   . SER   B 139 ? 0.1378 0.1032 0.2328 0.0048  0.0030  0.0026  139 SER   B O   
6591 C CB  . SER   B 139 ? 0.1645 0.1116 0.2355 0.0004  0.0040  0.0081  139 SER   B CB  
6592 O OG  . SER   B 139 ? 0.1652 0.1116 0.2357 -0.0011 -0.0197 0.0173  139 SER   B OG  
6598 N N   . LEU   B 140 ? 0.1382 0.1047 0.2224 -0.0041 0.0112  -0.0026 140 LEU   B N   
6599 C CA  . LEU   B 140 ? 0.1342 0.1120 0.2258 -0.0037 0.0110  0.0036  140 LEU   B CA  
6600 C C   . LEU   B 140 ? 0.1320 0.1053 0.2365 -0.0019 0.0043  -0.0045 140 LEU   B C   
6601 O O   . LEU   B 140 ? 0.1328 0.1117 0.2379 0.0005  -0.0045 0.0039  140 LEU   B O   
6602 C CB  . LEU   B 140 ? 0.1348 0.1123 0.2304 -0.0061 0.0119  -0.0064 140 LEU   B CB  
6603 C CG  . LEU   B 140 ? 0.1466 0.1189 0.2253 -0.0132 0.0050  0.0008  140 LEU   B CG  
6604 C CD1 . LEU   B 140 ? 0.1638 0.1194 0.2424 -0.0122 0.0088  -0.0048 140 LEU   B CD1 
6605 C CD2 . LEU   B 140 ? 0.1606 0.1219 0.2355 -0.0025 -0.0040 -0.0140 140 LEU   B CD2 
6617 N N   . ARG   B 141 ? 0.1269 0.1065 0.2473 -0.0034 0.0027  0.0018  141 ARG   B N   
6618 C CA  . ARG   B 141 ? 0.1266 0.1059 0.2832 -0.0093 0.0131  0.0017  141 ARG   B CA  
6619 C C   . ARG   B 141 ? 0.1212 0.1054 0.2702 -0.0127 0.0034  -0.0048 141 ARG   B C   
6620 O O   . ARG   B 141 ? 0.1333 0.1137 0.2729 -0.0120 -0.0077 -0.0136 141 ARG   B O   
6621 C CB  . ARG   B 141 ? 0.1423 0.1219 0.3168 -0.0173 0.0201  -0.0039 141 ARG   B CB  
6622 C CG  . ARG   B 141 ? 0.1737 0.1474 0.3572 -0.0277 0.0284  0.0081  141 ARG   B CG  
6623 C CD  . ARG   B 141 ? 0.2276 0.1723 0.3629 -0.0156 0.0141  -0.0060 141 ARG   B CD  
6624 N NE  . ARG   B 141 ? 0.2521 0.1740 0.3565 -0.0327 0.0303  -0.0088 141 ARG   B NE  
6625 C CZ  . ARG   B 141 ? 0.2663 0.1520 0.3506 -0.0277 0.0484  -0.0260 141 ARG   B CZ  
6626 N NH1 . ARG   B 141 ? 0.2770 0.1433 0.3609 -0.0258 0.0435  -0.0302 141 ARG   B NH1 
6627 N NH2 . ARG   B 141 ? 0.2736 0.1669 0.3564 -0.0177 0.0380  -0.0188 141 ARG   B NH2 
6641 N N   . VAL   B 142 ? 0.1326 0.1074 0.2522 -0.0064 0.0002  -0.0090 142 VAL   B N   
6642 C CA  . VAL   B 142 ? 0.1265 0.1073 0.2529 -0.0020 0.0054  -0.0099 142 VAL   B CA  
6643 C C   . VAL   B 142 ? 0.1278 0.1065 0.2459 0.0001  0.0048  -0.0056 142 VAL   B C   
6644 O O   . VAL   B 142 ? 0.1309 0.1073 0.2590 0.0050  -0.0017 0.0014  142 VAL   B O   
6645 C CB  . VAL   B 142 ? 0.1339 0.1221 0.2534 -0.0008 0.0136  0.0012  142 VAL   B CB  
6646 C CG1 . VAL   B 142 ? 0.1404 0.1188 0.2575 0.0065  0.0167  0.0032  142 VAL   B CG1 
6647 C CG2 . VAL   B 142 ? 0.1610 0.1245 0.2627 -0.0057 0.0116  0.0116  142 VAL   B CG2 
6657 N N   . CYS   B 143 ? 0.1261 0.1073 0.2284 -0.0015 0.0014  0.0066  143 CYS   B N   
6658 C CA  . CYS   B 143 ? 0.1232 0.1092 0.2300 -0.0051 -0.0067 0.0042  143 CYS   B CA  
6659 C C   . CYS   B 143 ? 0.1195 0.1162 0.2343 -0.0071 -0.0039 0.0022  143 CYS   B C   
6660 O O   . CYS   B 143 ? 0.1236 0.1099 0.2474 -0.0039 -0.0099 0.0010  143 CYS   B O   
6661 C CB  . CYS   B 143 ? 0.1311 0.1139 0.2290 -0.0065 -0.0032 0.0007  143 CYS   B CB  
6662 S SG  . CYS   B 143 ? 0.1340 0.1327 0.2199 -0.0028 0.0030  0.0070  143 CYS   B SG  
6668 N N   . VAL   B 144 ? 0.1253 0.1135 0.2368 -0.0061 -0.0036 -0.0078 144 VAL   B N   
6669 C CA  . VAL   B 144 ? 0.1310 0.1202 0.2664 -0.0151 -0.0120 -0.0165 144 VAL   B CA  
6670 C C   . VAL   B 144 ? 0.1276 0.1208 0.2658 -0.0100 -0.0151 -0.0022 144 VAL   B C   
6671 O O   . VAL   B 144 ? 0.1361 0.1407 0.2757 0.0031  -0.0133 0.0147  144 VAL   B O   
6672 C CB  . VAL   B 144 ? 0.1520 0.1375 0.3164 -0.0089 -0.0141 -0.0212 144 VAL   B CB  
6673 C CG1 . VAL   B 144 ? 0.1741 0.1764 0.3531 -0.0045 -0.0301 -0.0173 144 VAL   B CG1 
6674 C CG2 . VAL   B 144 ? 0.1680 0.1361 0.3068 -0.0012 -0.0243 -0.0300 144 VAL   B CG2 
6684 N N   . ASP   B 145 ? 0.1323 0.1119 0.2705 -0.0052 -0.0067 -0.0132 145 ASP   B N   
6685 C CA  . ASP   B 145 ? 0.1266 0.1172 0.2856 -0.0082 -0.0064 -0.0120 145 ASP   B CA  
6686 C C   . ASP   B 145 ? 0.1266 0.1225 0.2874 -0.0015 -0.0025 -0.0038 145 ASP   B C   
6687 O O   . ASP   B 145 ? 0.1269 0.1384 0.3355 -0.0074 0.0052  -0.0264 145 ASP   B O   
6688 C CB  . ASP   B 145 ? 0.1471 0.1320 0.3014 -0.0149 0.0075  -0.0024 145 ASP   B CB  
6689 C CG  . ASP   B 145 ? 0.1598 0.1376 0.3328 -0.0268 0.0134  0.0000  145 ASP   B CG  
6690 O OD1 . ASP   B 145 ? 0.1654 0.1409 0.3395 -0.0276 -0.0098 -0.0127 145 ASP   B OD1 
6691 O OD2 . ASP   B 145 ? 0.1927 0.1461 0.3885 -0.0269 0.0304  0.0143  145 ASP   B OD2 
6696 N N   . THR   B 146 ? 0.1176 0.1169 0.2420 -0.0099 -0.0028 0.0041  146 THR   B N   
6697 C CA  . THR   B 146 ? 0.1238 0.1136 0.2306 -0.0078 0.0024  -0.0027 146 THR   B CA  
6698 C C   . THR   B 146 ? 0.1232 0.1082 0.2230 -0.0022 -0.0031 -0.0003 146 THR   B C   
6699 O O   . THR   B 146 ? 0.1300 0.1098 0.2334 -0.0011 -0.0053 0.0015  146 THR   B O   
6700 C CB  . THR   B 146 ? 0.1298 0.1113 0.2364 -0.0016 0.0095  -0.0039 146 THR   B CB  
6701 O OG1 . THR   B 146 ? 0.1306 0.1105 0.2321 -0.0004 0.0017  0.0079  146 THR   B OG1 
6702 C CG2 . THR   B 146 ? 0.1470 0.1149 0.2297 -0.0043 0.0037  -0.0063 146 THR   B CG2 
6710 N N   . VAL   B 147 ? 0.1311 0.1118 0.2126 -0.0023 0.0047  0.0024  147 VAL   B N   
6711 C CA  . VAL   B 147 ? 0.1261 0.1166 0.2115 -0.0079 -0.0037 0.0012  147 VAL   B CA  
6712 C C   . VAL   B 147 ? 0.1217 0.1157 0.2171 -0.0091 -0.0157 -0.0033 147 VAL   B C   
6713 O O   . VAL   B 147 ? 0.1365 0.1194 0.2320 -0.0183 -0.0268 -0.0057 147 VAL   B O   
6714 C CB  . VAL   B 147 ? 0.1284 0.1243 0.2074 -0.0085 -0.0148 0.0070  147 VAL   B CB  
6715 C CG1 . VAL   B 147 ? 0.1339 0.1406 0.1932 -0.0080 -0.0122 0.0085  147 VAL   B CG1 
6716 C CG2 . VAL   B 147 ? 0.1391 0.1200 0.2127 -0.0101 -0.0163 0.0082  147 VAL   B CG2 
6726 N N   . ARG   B 148 ? 0.1249 0.1121 0.2223 -0.0051 -0.0231 -0.0034 148 ARG   B N   
6727 C CA  . ARG   B 148 ? 0.1339 0.1214 0.2196 -0.0028 -0.0309 -0.0076 148 ARG   B CA  
6728 C C   . ARG   B 148 ? 0.1425 0.1300 0.2057 -0.0078 -0.0204 -0.0041 148 ARG   B C   
6729 O O   . ARG   B 148 ? 0.1577 0.1607 0.2124 -0.0189 -0.0293 0.0035  148 ARG   B O   
6730 C CB  . ARG   B 148 ? 0.1364 0.1324 0.2144 -0.0008 -0.0340 -0.0025 148 ARG   B CB  
6731 C CG  . ARG   B 148 ? 0.1386 0.1444 0.2247 -0.0097 -0.0258 -0.0230 148 ARG   B CG  
6732 C CD  . ARG   B 148 ? 0.1506 0.1630 0.2230 0.0089  -0.0243 -0.0224 148 ARG   B CD  
6733 N NE  . ARG   B 148 ? 0.1493 0.1564 0.2233 0.0262  -0.0247 -0.0255 148 ARG   B NE  
6734 C CZ  . ARG   B 148 ? 0.1492 0.1511 0.2070 0.0232  -0.0238 -0.0208 148 ARG   B CZ  
6735 N NH1 . ARG   B 148 ? 0.1453 0.1543 0.2225 0.0053  -0.0173 -0.0139 148 ARG   B NH1 
6736 N NH2 . ARG   B 148 ? 0.1644 0.1419 0.2128 0.0218  -0.0255 -0.0130 148 ARG   B NH2 
6750 N N   . THR   B 149 ? 0.1463 0.1215 0.2043 -0.0070 -0.0218 0.0029  149 THR   B N   
6751 C CA  . THR   B 149 ? 0.1460 0.1267 0.1967 -0.0124 -0.0220 0.0089  149 THR   B CA  
6752 C C   . THR   B 149 ? 0.1439 0.1246 0.2027 -0.0114 -0.0199 0.0050  149 THR   B C   
6753 O O   . THR   B 149 ? 0.1500 0.1219 0.2132 -0.0163 -0.0144 0.0017  149 THR   B O   
6754 C CB  . THR   B 149 ? 0.1470 0.1240 0.1987 -0.0127 -0.0226 0.0017  149 THR   B CB  
6755 O OG1 . THR   B 149 ? 0.1511 0.1275 0.1987 -0.0195 -0.0324 -0.0028 149 THR   B OG1 
6756 C CG2 . THR   B 149 ? 0.1588 0.1367 0.2108 -0.0062 -0.0122 -0.0015 149 THR   B CG2 
6764 N N   . ASN   B 150 ? 0.1490 0.1208 0.1929 -0.0096 -0.0313 0.0026  150 ASN   B N   
6765 C CA  . ASN   B 150 ? 0.1545 0.1329 0.1926 -0.0126 -0.0267 -0.0081 150 ASN   B CA  
6766 C C   . ASN   B 150 ? 0.1449 0.1237 0.2023 -0.0080 -0.0276 -0.0023 150 ASN   B C   
6767 O O   . ASN   B 150 ? 0.1571 0.1276 0.2264 -0.0240 -0.0439 0.0014  150 ASN   B O   
6768 C CB  . ASN   B 150 ? 0.1808 0.1654 0.2060 -0.0190 -0.0210 0.0010  150 ASN   B CB  
6769 C CG  . ASN   B 150 ? 0.2052 0.2090 0.2205 -0.0127 -0.0283 0.0202  150 ASN   B CG  
6770 O OD1 . ASN   B 150 ? 0.2170 0.2283 0.2411 -0.0247 -0.0516 0.0149  150 ASN   B OD1 
6771 N ND2 . ASN   B 150 ? 0.2130 0.2341 0.2404 -0.0007 -0.0364 0.0510  150 ASN   B ND2 
6778 N N   . VAL   B 151 ? 0.1380 0.1214 0.1827 -0.0145 -0.0306 0.0093  151 VAL   B N   
6779 C CA  . VAL   B 151 ? 0.1383 0.1287 0.1896 -0.0163 -0.0272 0.0040  151 VAL   B CA  
6780 C C   . VAL   B 151 ? 0.1405 0.1201 0.1954 -0.0242 -0.0213 0.0046  151 VAL   B C   
6781 O O   . VAL   B 151 ? 0.1463 0.1293 0.2110 -0.0227 -0.0207 -0.0096 151 VAL   B O   
6782 C CB  . VAL   B 151 ? 0.1587 0.1469 0.1970 -0.0007 -0.0107 0.0012  151 VAL   B CB  
6783 C CG1 . VAL   B 151 ? 0.1772 0.1508 0.2069 -0.0087 -0.0041 -0.0139 151 VAL   B CG1 
6784 C CG2 . VAL   B 151 ? 0.1740 0.1607 0.1993 0.0147  -0.0177 0.0057  151 VAL   B CG2 
6794 N N   . TYR   B 152 ? 0.1378 0.1084 0.1923 -0.0185 -0.0215 0.0005  152 TYR   B N   
6795 C CA  . TYR   B 152 ? 0.1385 0.1215 0.1888 -0.0147 -0.0157 -0.0036 152 TYR   B CA  
6796 C C   . TYR   B 152 ? 0.1366 0.1178 0.1832 -0.0187 -0.0100 -0.0073 152 TYR   B C   
6797 O O   . TYR   B 152 ? 0.1443 0.1135 0.1909 -0.0251 -0.0163 0.0012  152 TYR   B O   
6798 C CB  . TYR   B 152 ? 0.1479 0.1359 0.1893 -0.0129 -0.0121 0.0025  152 TYR   B CB  
6799 C CG  . TYR   B 152 ? 0.1658 0.1414 0.1845 -0.0310 -0.0141 0.0085  152 TYR   B CG  
6800 C CD1 . TYR   B 152 ? 0.1751 0.1550 0.1845 -0.0226 -0.0279 0.0043  152 TYR   B CD1 
6801 C CD2 . TYR   B 152 ? 0.1873 0.1530 0.1834 -0.0307 -0.0182 0.0063  152 TYR   B CD2 
6802 C CE1 . TYR   B 152 ? 0.1901 0.1717 0.1982 -0.0155 -0.0230 0.0210  152 TYR   B CE1 
6803 C CE2 . TYR   B 152 ? 0.1993 0.1773 0.1914 -0.0246 -0.0212 0.0080  152 TYR   B CE2 
6804 C CZ  . TYR   B 152 ? 0.2001 0.1892 0.1820 -0.0219 -0.0431 0.0223  152 TYR   B CZ  
6805 O OH  . TYR   B 152 ? 0.2264 0.2209 0.2090 -0.0127 -0.0359 0.0199  152 TYR   B OH  
6815 N N   . LEU   B 153 ? 0.1367 0.1163 0.1878 -0.0202 -0.0221 -0.0060 153 LEU   B N   
6816 C CA  . LEU   B 153 ? 0.1419 0.1133 0.1737 -0.0131 -0.0052 -0.0065 153 LEU   B CA  
6817 C C   . LEU   B 153 ? 0.1414 0.1108 0.1764 -0.0228 -0.0077 -0.0081 153 LEU   B C   
6818 O O   . LEU   B 153 ? 0.1501 0.1351 0.1917 -0.0130 -0.0094 -0.0273 153 LEU   B O   
6819 C CB  . LEU   B 153 ? 0.1455 0.1160 0.1828 -0.0219 -0.0015 -0.0011 153 LEU   B CB  
6820 C CG  . LEU   B 153 ? 0.1376 0.1244 0.2102 -0.0240 -0.0033 -0.0075 153 LEU   B CG  
6821 C CD1 . LEU   B 153 ? 0.1414 0.1397 0.2193 -0.0287 0.0058  0.0080  153 LEU   B CD1 
6822 C CD2 . LEU   B 153 ? 0.1412 0.1377 0.2146 -0.0304 0.0047  -0.0029 153 LEU   B CD2 
6834 N N   . ALA   B 154 ? 0.1434 0.1144 0.1786 -0.0053 -0.0145 -0.0032 154 ALA   B N   
6835 C CA  . ALA   B 154 ? 0.1479 0.1218 0.1973 0.0000  -0.0147 -0.0118 154 ALA   B CA  
6836 C C   . ALA   B 154 ? 0.1595 0.1292 0.2005 0.0029  -0.0200 -0.0216 154 ALA   B C   
6837 O O   . ALA   B 154 ? 0.1806 0.1323 0.2096 0.0069  -0.0130 -0.0089 154 ALA   B O   
6838 C CB  . ALA   B 154 ? 0.1446 0.1396 0.2162 -0.0022 -0.0161 -0.0182 154 ALA   B CB  
6844 N N   . VAL   B 155 ? 0.1320 0.1172 0.1970 -0.0018 -0.0140 -0.0076 155 VAL   B N   
6845 C CA  . VAL   B 155 ? 0.1283 0.1189 0.2117 -0.0017 -0.0116 0.0020  155 VAL   B CA  
6846 C C   . VAL   B 155 ? 0.1320 0.1213 0.1998 0.0016  -0.0091 -0.0128 155 VAL   B C   
6847 O O   . VAL   B 155 ? 0.1500 0.1388 0.2251 0.0080  -0.0091 -0.0194 155 VAL   B O   
6848 C CB  . VAL   B 155 ? 0.1392 0.1338 0.2496 -0.0085 -0.0123 0.0080  155 VAL   B CB  
6849 C CG1 . VAL   B 155 ? 0.1374 0.1296 0.2510 -0.0127 -0.0123 0.0080  155 VAL   B CG1 
6850 C CG2 . VAL   B 155 ? 0.1318 0.1493 0.2747 -0.0045 -0.0049 0.0311  155 VAL   B CG2 
6860 N N   . PHE   B 156 ? 0.1287 0.1272 0.2204 0.0099  -0.0050 -0.0075 156 PHE   B N   
6861 C CA  . PHE   B 156 ? 0.1330 0.1303 0.2532 0.0102  -0.0043 -0.0041 156 PHE   B CA  
6862 C C   . PHE   B 156 ? 0.1253 0.1379 0.2652 0.0143  -0.0155 -0.0216 156 PHE   B C   
6863 O O   . PHE   B 156 ? 0.1506 0.1549 0.2911 0.0267  -0.0046 -0.0178 156 PHE   B O   
6864 C CB  . PHE   B 156 ? 0.1363 0.1339 0.2707 0.0036  -0.0236 -0.0019 156 PHE   B CB  
6865 C CG  . PHE   B 156 ? 0.1328 0.1330 0.2865 -0.0050 -0.0250 0.0102  156 PHE   B CG  
6866 C CD1 . PHE   B 156 ? 0.1445 0.1644 0.3214 0.0025  -0.0217 0.0435  156 PHE   B CD1 
6867 C CD2 . PHE   B 156 ? 0.1409 0.1474 0.2771 0.0056  -0.0317 0.0086  156 PHE   B CD2 
6868 C CE1 . PHE   B 156 ? 0.1476 0.1831 0.3280 0.0019  -0.0201 0.0421  156 PHE   B CE1 
6869 C CE2 . PHE   B 156 ? 0.1407 0.1676 0.2959 0.0076  -0.0349 0.0117  156 PHE   B CE2 
6870 C CZ  . PHE   B 156 ? 0.1422 0.1785 0.3168 0.0062  -0.0337 0.0194  156 PHE   B CZ  
6880 N N   . ASP   B 157 ? 0.1323 0.1279 0.2787 0.0110  -0.0164 -0.0136 157 ASP   B N   
6881 C CA  . ASP   B 157 ? 0.1396 0.1354 0.3038 0.0084  -0.0241 -0.0145 157 ASP   B CA  
6882 C C   . ASP   B 157 ? 0.1414 0.1258 0.3039 0.0121  -0.0255 -0.0298 157 ASP   B C   
6883 O O   . ASP   B 157 ? 0.1274 0.1321 0.2922 0.0055  -0.0231 -0.0197 157 ASP   B O   
6884 C CB  . ASP   B 157 ? 0.1638 0.1518 0.3139 0.0009  -0.0373 -0.0051 157 ASP   B CB  
6885 C CG  . ASP   B 157 ? 0.1952 0.1654 0.3426 0.0017  -0.0372 -0.0053 157 ASP   B CG  
6886 O OD1 . ASP   B 157 ? 0.1990 0.1641 0.3605 0.0085  -0.0367 -0.0001 157 ASP   B OD1 
6887 O OD2 . ASP   B 157 ? 0.2309 0.1820 0.3813 0.0038  -0.0183 -0.0010 157 ASP   B OD2 
6892 N N   . LYS   B 158 ? 0.1357 0.1534 0.3232 0.0057  -0.0089 -0.0418 158 LYS   B N   
6893 C CA  . LYS   B 158 ? 0.1489 0.1647 0.3216 0.0041  -0.0098 -0.0509 158 LYS   B CA  
6894 C C   . LYS   B 158 ? 0.1516 0.1524 0.3317 0.0012  -0.0166 -0.0460 158 LYS   B C   
6895 O O   . LYS   B 158 ? 0.1526 0.1544 0.3434 -0.0040 -0.0149 -0.0572 158 LYS   B O   
6896 C CB  . LYS   B 158 ? 0.1704 0.2029 0.3210 0.0062  -0.0047 -0.0701 158 LYS   B CB  
6897 C CG  . LYS   B 158 ? 0.2048 0.2424 0.3318 0.0126  0.0001  -0.0815 158 LYS   B CG  
6898 C CD  . LYS   B 158 ? 0.2320 0.2875 0.3496 0.0108  0.0042  -0.0844 158 LYS   B CD  
6899 C CE  . LYS   B 158 ? 0.2491 0.3151 0.3654 0.0160  0.0052  -0.0861 158 LYS   B CE  
6900 N NZ  . LYS   B 158 ? 0.2361 0.3220 0.3638 0.0146  0.0131  -0.0884 158 LYS   B NZ  
6914 N N   . ASN   B 159 ? 0.1565 0.1456 0.3497 0.0032  -0.0181 -0.0428 159 ASN   B N   
6915 C CA  . ASN   B 159 ? 0.1680 0.1425 0.3596 0.0152  -0.0308 -0.0327 159 ASN   B CA  
6916 C C   . ASN   B 159 ? 0.1558 0.1262 0.3473 0.0168  -0.0319 -0.0329 159 ASN   B C   
6917 O O   . ASN   B 159 ? 0.1537 0.1250 0.3673 -0.0077 -0.0345 -0.0264 159 ASN   B O   
6918 C CB  . ASN   B 159 ? 0.1903 0.1501 0.3793 0.0227  -0.0357 -0.0265 159 ASN   B CB  
6919 C CG  . ASN   B 159 ? 0.2106 0.1719 0.4149 0.0267  -0.0469 -0.0442 159 ASN   B CG  
6920 O OD1 . ASN   B 159 ? 0.2284 0.1890 0.4341 0.0338  -0.0463 -0.0549 159 ASN   B OD1 
6921 N ND2 . ASN   B 159 ? 0.2097 0.1832 0.4347 0.0315  -0.0481 -0.0458 159 ASN   B ND2 
6928 N N   . LEU   B 160 ? 0.1479 0.1282 0.3241 0.0096  -0.0352 -0.0273 160 LEU   B N   
6929 C CA  . LEU   B 160 ? 0.1417 0.1315 0.2963 0.0053  -0.0293 -0.0077 160 LEU   B CA  
6930 C C   . LEU   B 160 ? 0.1374 0.1279 0.2881 -0.0008 -0.0269 -0.0158 160 LEU   B C   
6931 O O   . LEU   B 160 ? 0.1284 0.1318 0.2848 -0.0015 -0.0222 -0.0095 160 LEU   B O   
6932 C CB  . LEU   B 160 ? 0.1435 0.1412 0.2763 0.0090  -0.0318 -0.0068 160 LEU   B CB  
6933 C CG  . LEU   B 160 ? 0.1466 0.1536 0.2537 0.0097  -0.0305 -0.0017 160 LEU   B CG  
6934 C CD1 . LEU   B 160 ? 0.1617 0.1690 0.2533 -0.0022 -0.0099 -0.0063 160 LEU   B CD1 
6935 C CD2 . LEU   B 160 ? 0.1470 0.1575 0.2606 0.0145  -0.0379 -0.0199 160 LEU   B CD2 
6947 N N   . TYR   B 161 ? 0.1351 0.1311 0.2906 -0.0004 -0.0100 -0.0241 161 TYR   B N   
6948 C CA  . TYR   B 161 ? 0.1391 0.1269 0.2773 -0.0102 0.0039  -0.0377 161 TYR   B CA  
6949 C C   . TYR   B 161 ? 0.1425 0.1299 0.2614 -0.0047 0.0022  -0.0280 161 TYR   B C   
6950 O O   . TYR   B 161 ? 0.1481 0.1264 0.2610 -0.0086 -0.0031 -0.0249 161 TYR   B O   
6951 C CB  . TYR   B 161 ? 0.1499 0.1402 0.2753 -0.0179 0.0091  -0.0363 161 TYR   B CB  
6952 C CG  . TYR   B 161 ? 0.1712 0.1421 0.2704 -0.0205 0.0145  -0.0368 161 TYR   B CG  
6953 C CD1 . TYR   B 161 ? 0.1753 0.1385 0.2684 -0.0289 0.0145  -0.0389 161 TYR   B CD1 
6954 C CD2 . TYR   B 161 ? 0.1943 0.1496 0.2574 -0.0159 0.0088  -0.0394 161 TYR   B CD2 
6955 C CE1 . TYR   B 161 ? 0.1900 0.1521 0.2662 -0.0353 0.0144  -0.0383 161 TYR   B CE1 
6956 C CE2 . TYR   B 161 ? 0.2085 0.1647 0.2587 -0.0301 0.0162  -0.0259 161 TYR   B CE2 
6957 C CZ  . TYR   B 161 ? 0.2026 0.1642 0.2584 -0.0399 0.0185  -0.0196 161 TYR   B CZ  
6958 O OH  . TYR   B 161 ? 0.2303 0.1848 0.2765 -0.0365 0.0146  -0.0187 161 TYR   B OH  
6968 N N   . ASP   B 162 ? 0.1431 0.1320 0.2757 -0.0053 -0.0076 -0.0363 162 ASP   B N   
6969 C CA  . ASP   B 162 ? 0.1557 0.1388 0.2710 -0.0113 -0.0036 -0.0378 162 ASP   B CA  
6970 C C   . ASP   B 162 ? 0.1530 0.1286 0.2682 -0.0165 -0.0041 -0.0375 162 ASP   B C   
6971 O O   . ASP   B 162 ? 0.1609 0.1379 0.2737 -0.0196 -0.0174 -0.0312 162 ASP   B O   
6972 C CB  . ASP   B 162 ? 0.1771 0.1556 0.2887 0.0032  -0.0078 -0.0428 162 ASP   B CB  
6973 C CG  . ASP   B 162 ? 0.1848 0.1771 0.3018 0.0144  -0.0105 -0.0589 162 ASP   B CG  
6974 O OD1 . ASP   B 162 ? 0.1794 0.1980 0.3060 0.0100  -0.0036 -0.0551 162 ASP   B OD1 
6975 O OD2 . ASP   B 162 ? 0.2012 0.2023 0.3257 0.0306  -0.0002 -0.0591 162 ASP   B OD2 
6980 N N   A LYS   B 163 ? 0.1569 0.1366 0.2652 -0.0146 -0.0135 -0.0270 163 LYS   B N   
6981 N N   B LYS   B 163 ? 0.1477 0.1183 0.2634 -0.0121 -0.0157 -0.0296 163 LYS   B N   
6982 C CA  A LYS   B 163 ? 0.1665 0.1488 0.2700 -0.0181 -0.0139 -0.0114 163 LYS   B CA  
6983 C CA  B LYS   B 163 ? 0.1555 0.1215 0.2640 -0.0172 -0.0141 -0.0107 163 LYS   B CA  
6984 C C   A LYS   B 163 ? 0.1401 0.1357 0.2646 -0.0176 -0.0194 -0.0056 163 LYS   B C   
6985 C C   B LYS   B 163 ? 0.1326 0.1226 0.2618 -0.0179 -0.0188 -0.0088 163 LYS   B C   
6986 O O   A LYS   B 163 ? 0.1407 0.1404 0.2789 -0.0207 -0.0178 -0.0003 163 LYS   B O   
6987 O O   B LYS   B 163 ? 0.1345 0.1314 0.2684 -0.0229 -0.0138 -0.0086 163 LYS   B O   
6988 C CB  A LYS   B 163 ? 0.2037 0.1813 0.2965 -0.0143 -0.0100 -0.0022 163 LYS   B CB  
6989 C CB  B LYS   B 163 ? 0.1926 0.1426 0.2849 -0.0031 -0.0094 0.0084  163 LYS   B CB  
6990 C CG  A LYS   B 163 ? 0.2484 0.2277 0.3374 -0.0129 -0.0078 0.0000  163 LYS   B CG  
6991 C CG  B LYS   B 163 ? 0.2471 0.1986 0.3295 -0.0035 -0.0074 0.0095  163 LYS   B CG  
6992 C CD  A LYS   B 163 ? 0.2834 0.2636 0.3821 -0.0145 -0.0094 -0.0044 163 LYS   B CD  
6993 C CD  B LYS   B 163 ? 0.2888 0.2484 0.3846 -0.0061 -0.0122 0.0036  163 LYS   B CD  
6994 C CE  A LYS   B 163 ? 0.3076 0.2848 0.4148 -0.0181 -0.0074 -0.0058 163 LYS   B CE  
6995 C CE  B LYS   B 163 ? 0.3195 0.2755 0.4271 -0.0124 -0.0116 -0.0000 163 LYS   B CE  
6996 N NZ  A LYS   B 163 ? 0.3223 0.2922 0.4387 -0.0212 -0.0071 -0.0072 163 LYS   B NZ  
6997 N NZ  B LYS   B 163 ? 0.3385 0.2851 0.4545 -0.0170 -0.0113 -0.0041 163 LYS   B NZ  
7024 N N   . LEU   B 164 ? 0.1209 0.1216 0.2533 -0.0135 -0.0211 -0.0013 164 LEU   B N   
7025 C CA  . LEU   B 164 ? 0.1309 0.1204 0.2485 -0.0063 -0.0243 -0.0083 164 LEU   B CA  
7026 C C   . LEU   B 164 ? 0.1375 0.1254 0.2421 -0.0085 -0.0276 -0.0035 164 LEU   B C   
7027 O O   . LEU   B 164 ? 0.1365 0.1432 0.2589 -0.0078 -0.0308 -0.0061 164 LEU   B O   
7028 C CB  . LEU   B 164 ? 0.1310 0.1203 0.2381 -0.0087 -0.0109 -0.0056 164 LEU   B CB  
7029 C CG  . LEU   B 164 ? 0.1345 0.1354 0.2396 -0.0068 -0.0102 -0.0029 164 LEU   B CG  
7030 C CD1 . LEU   B 164 ? 0.1443 0.1347 0.2475 -0.0124 -0.0208 -0.0016 164 LEU   B CD1 
7031 C CD2 . LEU   B 164 ? 0.1558 0.1795 0.2539 -0.0004 0.0002  -0.0202 164 LEU   B CD2 
7044 N N   . VAL   B 165 ? 0.1549 0.1267 0.2515 -0.0211 -0.0288 -0.0161 165 VAL   B N   
7045 C CA  . VAL   B 165 ? 0.1850 0.1361 0.2411 -0.0256 -0.0404 -0.0039 165 VAL   B CA  
7046 C C   . VAL   B 165 ? 0.2121 0.1506 0.2536 -0.0378 -0.0659 0.0009  165 VAL   B C   
7047 O O   . VAL   B 165 ? 0.2281 0.1589 0.2627 -0.0372 -0.0687 0.0011  165 VAL   B O   
7048 C CB  . VAL   B 165 ? 0.2053 0.1545 0.2402 -0.0138 -0.0165 -0.0058 165 VAL   B CB  
7049 C CG1 . VAL   B 165 ? 0.2198 0.1599 0.2664 -0.0150 -0.0100 -0.0112 165 VAL   B CG1 
7050 C CG2 . VAL   B 165 ? 0.2036 0.1646 0.2424 -0.0169 -0.0088 -0.0055 165 VAL   B CG2 
7060 N N   . SER   B 166 ? 0.2198 0.1449 0.2785 -0.0341 -0.0744 -0.0156 166 SER   B N   
7061 C CA  . SER   B 166 ? 0.2170 0.1442 0.3181 -0.0333 -0.0576 -0.0249 166 SER   B CA  
7062 C C   . SER   B 166 ? 0.2039 0.1476 0.3365 -0.0357 -0.0619 -0.0047 166 SER   B C   
7063 O O   . SER   B 166 ? 0.2066 0.1659 0.3684 -0.0474 -0.0777 -0.0167 166 SER   B O   
7064 C CB  . SER   B 166 ? 0.2186 0.1477 0.3404 -0.0320 -0.0443 -0.0313 166 SER   B CB  
7065 O OG  . SER   B 166 ? 0.2075 0.1457 0.3518 -0.0223 -0.0434 -0.0171 166 SER   B OG  
7071 N N   . SER   B 167 ? 0.1862 0.1446 0.3153 -0.0307 -0.0600 0.0210  167 SER   B N   
7072 C CA  . SER   B 167 ? 0.1799 0.1484 0.3068 -0.0310 -0.0413 0.0198  167 SER   B CA  
7073 C C   . SER   B 167 ? 0.1768 0.1575 0.2991 -0.0425 -0.0330 0.0315  167 SER   B C   
7074 O O   . SER   B 167 ? 0.1811 0.1672 0.2911 -0.0426 -0.0308 0.0282  167 SER   B O   
7075 C CB  . SER   B 167 ? 0.1768 0.1540 0.2971 -0.0304 -0.0177 0.0239  167 SER   B CB  
7076 O OG  . SER   B 167 ? 0.1723 0.1615 0.2875 -0.0220 -0.0126 0.0220  167 SER   B OG  
7082 N N   . PHE   B 168 ? 0.1826 0.1556 0.2983 -0.0384 -0.0320 0.0351  168 PHE   B N   
7083 C CA  . PHE   B 168 ? 0.1832 0.1511 0.2759 -0.0410 -0.0299 0.0195  168 PHE   B CA  
7084 C C   . PHE   B 168 ? 0.1548 0.1434 0.2425 -0.0190 -0.0098 0.0099  168 PHE   B C   
7085 O O   . PHE   B 168 ? 0.1860 0.1326 0.2699 0.0036  -0.0103 -0.0041 168 PHE   B O   
7086 C CB  . PHE   B 168 ? 0.2006 0.1555 0.2852 -0.0460 -0.0493 0.0351  168 PHE   B CB  
7087 C CG  . PHE   B 168 ? 0.2246 0.1439 0.2816 -0.0513 -0.0493 0.0196  168 PHE   B CG  
7088 C CD1 . PHE   B 168 ? 0.2592 0.1525 0.2931 -0.0445 -0.0548 0.0202  168 PHE   B CD1 
7089 C CD2 . PHE   B 168 ? 0.2147 0.1368 0.2752 -0.0497 -0.0457 0.0311  168 PHE   B CD2 
7090 C CE1 . PHE   B 168 ? 0.2740 0.1645 0.2938 -0.0249 -0.0483 0.0231  168 PHE   B CE1 
7091 C CE2 . PHE   B 168 ? 0.2420 0.1519 0.2863 -0.0310 -0.0522 0.0257  168 PHE   B CE2 
7092 C CZ  . PHE   B 168 ? 0.2601 0.1527 0.2904 -0.0157 -0.0542 0.0283  168 PHE   B CZ  
7102 N N   A LEU   B 169 ? 0.1570 0.1533 0.2379 -0.0121 -0.0067 -0.0020 169 LEU   B N   
7103 N N   B LEU   B 169 ? 0.1535 0.1578 0.2350 -0.0004 -0.0047 -0.0040 169 LEU   B N   
7104 C CA  A LEU   B 169 ? 0.1749 0.1697 0.2507 -0.0178 -0.0065 -0.0178 169 LEU   B CA  
7105 C CA  B LEU   B 169 ? 0.1777 0.1849 0.2506 -0.0067 -0.0059 -0.0223 169 LEU   B CA  
7106 C C   A LEU   B 169 ? 0.1851 0.1772 0.2699 -0.0138 -0.0064 -0.0276 169 LEU   B C   
7107 C C   B LEU   B 169 ? 0.2022 0.1952 0.2625 0.0122  -0.0060 -0.0266 169 LEU   B C   
7108 O O   A LEU   B 169 ? 0.1984 0.1795 0.2791 -0.0178 -0.0040 -0.0280 169 LEU   B O   
7109 O O   B LEU   B 169 ? 0.2185 0.1992 0.2659 0.0017  0.0004  -0.0286 169 LEU   B O   
7110 C CB  A LEU   B 169 ? 0.1973 0.2002 0.2679 -0.0185 -0.0094 -0.0026 169 LEU   B CB  
7111 C CB  B LEU   B 169 ? 0.2007 0.2253 0.2793 -0.0225 -0.0161 -0.0036 169 LEU   B CB  
7112 C CG  A LEU   B 169 ? 0.2303 0.2300 0.2993 -0.0074 -0.0023 0.0063  169 LEU   B CG  
7113 C CG  B LEU   B 169 ? 0.2408 0.2626 0.3223 -0.0104 -0.0118 0.0082  169 LEU   B CG  
7114 C CD1 A LEU   B 169 ? 0.2396 0.2464 0.3045 -0.0051 -0.0028 0.0168  169 LEU   B CD1 
7115 C CD1 B LEU   B 169 ? 0.2511 0.2796 0.3341 -0.0037 -0.0160 0.0211  169 LEU   B CD1 
7116 C CD2 A LEU   B 169 ? 0.2332 0.2350 0.3076 0.0010  0.0066  0.0054  169 LEU   B CD2 
7117 C CD2 B LEU   B 169 ? 0.2439 0.2698 0.3321 0.0010  -0.0008 0.0054  169 LEU   B CD2 
7118 O OXT A LEU   B 169 ? 0.1778 0.1868 0.2725 -0.0160 0.0004  -0.0244 169 LEU   B OXT 
7119 O OXT B LEU   B 169 ? 0.2127 0.2051 0.2793 0.0384  0.0037  -0.0179 169 LEU   B OXT 
7142 N N2  B A1BA5 C .   ? 0.1511 0.1562 0.2487 -0.0122 -0.0158 0.0293  201 A1BA5 A N2  
7143 C C3  B A1BA5 C .   ? 0.1934 0.1884 0.2770 -0.0125 -0.0247 0.0429  201 A1BA5 A C3  
7144 C C6  B A1BA5 C .   ? 0.2220 0.1981 0.2757 -0.0131 -0.0281 0.0614  201 A1BA5 A C6  
7145 C C9  B A1BA5 C .   ? 0.1477 0.1576 0.2377 0.0061  -0.0057 0.0298  201 A1BA5 A C9  
7146 C C12 B A1BA5 C .   ? 0.1598 0.1606 0.2474 -0.0235 -0.0269 0.0343  201 A1BA5 A C12 
7147 C C14 B A1BA5 C .   ? 0.1422 0.1571 0.2295 0.0074  0.0050  0.0033  201 A1BA5 A C14 
7148 C C1  B A1BA5 C .   ? 0.1833 0.2013 0.2962 -0.0284 -0.0396 0.0067  201 A1BA5 A C1  
7149 C C10 B A1BA5 C .   ? 0.1418 0.1583 0.2375 -0.0173 -0.0028 0.0311  201 A1BA5 A C10 
7150 C C11 B A1BA5 C .   ? 0.1696 0.1646 0.2436 -0.0183 -0.0158 0.0409  201 A1BA5 A C11 
7151 C C13 B A1BA5 C .   ? 0.1382 0.1555 0.2360 -0.0155 0.0032  0.0307  201 A1BA5 A C13 
7152 C C15 B A1BA5 C .   ? 0.1722 0.1960 0.3062 -0.0193 -0.0295 0.0271  201 A1BA5 A C15 
7153 C C2  B A1BA5 C .   ? 0.1781 0.1923 0.2861 -0.0234 -0.0270 0.0267  201 A1BA5 A C2  
7154 C C4  B A1BA5 C .   ? 0.2112 0.1882 0.2788 -0.0161 -0.0240 0.0532  201 A1BA5 A C4  
7155 C C5  B A1BA5 C .   ? 0.2236 0.2044 0.2848 -0.0185 -0.0313 0.0515  201 A1BA5 A C5  
7156 C C7  B A1BA5 C .   ? 0.2103 0.1816 0.2711 -0.0137 -0.0208 0.0686  201 A1BA5 A C7  
7157 C C8  B A1BA5 C .   ? 0.2046 0.1790 0.2815 -0.0066 -0.0158 0.0618  201 A1BA5 A C8  
7158 N N1  B A1BA5 C .   ? 0.1812 0.1699 0.2667 -0.0003 -0.0183 0.0398  201 A1BA5 A N1  
7159 N N3  B A1BA5 C .   ? 0.1455 0.1523 0.2275 -0.0105 0.0105  0.0260  201 A1BA5 A N3  
7160 N N4  B A1BA5 C .   ? 0.1532 0.1582 0.2369 0.0118  -0.0018 0.0071  201 A1BA5 A N4  
7161 O O1  B A1BA5 C .   ? 0.1735 0.1781 0.2707 -0.0369 -0.0023 0.0283  201 A1BA5 A O1  
7182 O O   . HOH   D .   ? 0.6788 0.5347 0.3800 0.2847  -0.0856 0.0649  301 HOH   A O   
7183 O O   . HOH   D .   ? 0.3212 0.2864 0.2005 -0.0316 0.0610  0.0484  302 HOH   A O   
7184 O O   . HOH   D .   ? 0.2692 0.6877 0.5572 -0.0134 -0.0793 0.1310  303 HOH   A O   
7185 O O   . HOH   D .   ? 0.1531 0.3355 0.3619 -0.0092 0.0018  0.0375  304 HOH   A O   
7186 O O   . HOH   D .   ? 0.2524 0.2346 0.5653 -0.0031 -0.0678 0.1144  305 HOH   A O   
7187 O O   . HOH   D .   ? 0.4702 0.7554 0.4403 -0.1258 0.0846  0.0004  306 HOH   A O   
7188 O O   . HOH   D .   ? 0.6072 0.2208 0.3992 -0.0067 -0.1034 0.0826  307 HOH   A O   
7189 O O   . HOH   D .   ? 0.7585 0.4818 0.5420 -0.0691 -0.1372 -0.0651 308 HOH   A O   
7190 O O   . HOH   D .   ? 0.5128 0.4289 0.3418 -0.1082 0.1509  0.0701  309 HOH   A O   
7191 O O   B HOH   D .   ? 0.5587 0.5540 0.6313 -0.0512 -0.1006 -0.1017 310 HOH   A O   
7192 O O   . HOH   D .   ? 0.2078 0.1747 0.3502 -0.0466 0.0185  -0.0279 311 HOH   A O   
7193 O O   . HOH   D .   ? 0.4736 0.5823 0.4201 0.1657  0.1293  -0.0522 312 HOH   A O   
7194 O O   . HOH   D .   ? 0.4286 0.3697 0.4810 -0.0590 0.1090  0.1123  313 HOH   A O   
7195 O O   . HOH   D .   ? 0.3111 0.2164 0.2727 -0.0854 0.0220  0.0031  314 HOH   A O   
7196 O O   . HOH   D .   ? 0.4663 0.5349 0.4566 -0.1174 -0.0776 -0.0767 315 HOH   A O   
7197 O O   . HOH   D .   ? 0.2668 0.5565 0.4944 -0.0322 -0.0639 0.0746  316 HOH   A O   
7198 O O   . HOH   D .   ? 0.1658 0.1503 0.2505 -0.0165 -0.0031 0.0319  317 HOH   A O   
7199 O O   . HOH   D .   ? 0.3798 0.7515 0.7322 0.0826  0.1594  -0.0089 318 HOH   A O   
7200 O O   . HOH   D .   ? 0.6549 0.5741 0.3529 0.1198  0.0110  0.1134  319 HOH   A O   
7201 O O   . HOH   D .   ? 0.1883 0.2007 0.3625 0.0021  0.0733  -0.0333 320 HOH   A O   
7202 O O   . HOH   D .   ? 0.3936 0.3559 0.3571 0.1696  0.0385  0.0393  321 HOH   A O   
7203 O O   . HOH   D .   ? 0.1950 0.1715 0.2585 0.0295  -0.0341 0.0099  322 HOH   A O   
7204 O O   . HOH   D .   ? 0.4612 0.3325 0.4320 -0.0223 0.2121  0.0643  323 HOH   A O   
7205 O O   . HOH   D .   ? 0.1830 0.2135 0.2390 -0.0193 0.0052  0.0581  324 HOH   A O   
7206 O O   B HOH   D .   ? 0.4885 0.2548 0.3456 -0.0945 -0.1221 0.0446  325 HOH   A O   
7207 O O   . HOH   D .   ? 0.5659 0.6763 0.5036 0.0275  0.0744  0.0016  326 HOH   A O   
7208 O O   . HOH   D .   ? 0.7175 0.3380 0.4070 0.1452  -0.0908 0.0697  327 HOH   A O   
7209 O O   . HOH   D .   ? 0.4605 0.2903 0.2566 0.1790  0.0264  0.0414  328 HOH   A O   
7210 O O   . HOH   D .   ? 0.1939 0.2795 0.5223 -0.0254 0.0202  -0.0554 329 HOH   A O   
7211 O O   . HOH   D .   ? 0.3349 0.4612 0.2477 -0.0140 0.0558  0.0593  330 HOH   A O   
7212 O O   . HOH   D .   ? 0.1762 0.2568 0.3020 0.0310  -0.0263 -0.0165 331 HOH   A O   
7213 O O   . HOH   D .   ? 0.4196 0.3337 0.5615 -0.0106 0.1402  -0.0773 332 HOH   A O   
7214 O O   A HOH   D .   ? 0.1068 0.1576 0.1502 0.0257  0.0076  0.0422  333 HOH   A O   
7215 O O   . HOH   D .   ? 0.2854 0.2765 0.2881 -0.0867 0.0222  0.0487  334 HOH   A O   
7216 O O   . HOH   D .   ? 0.4209 0.2695 0.3386 -0.0127 0.0596  0.0492  335 HOH   A O   
7217 O O   . HOH   D .   ? 0.2090 0.4101 0.4734 0.0017  -0.0406 0.1687  336 HOH   A O   
7218 O O   . HOH   D .   ? 0.3138 0.2565 0.3955 -0.0294 0.1328  0.0174  337 HOH   A O   
7219 O O   . HOH   D .   ? 0.5801 0.7102 0.4122 -0.0823 -0.1440 -0.0374 338 HOH   A O   
7220 O O   . HOH   D .   ? 0.2471 0.1930 0.2676 -0.0552 -0.0087 0.0420  339 HOH   A O   
7221 O O   . HOH   D .   ? 0.1370 0.1336 0.2356 -0.0170 0.0062  0.0051  340 HOH   A O   
7222 O O   . HOH   D .   ? 0.2846 0.4249 0.2992 -0.0648 0.0173  0.0233  341 HOH   A O   
7223 O O   . HOH   D .   ? 0.1485 0.1790 0.3509 -0.0046 -0.0250 -0.0465 342 HOH   A O   
7224 O O   . HOH   D .   ? 0.3968 0.3866 0.3883 -0.1754 -0.0306 0.1429  343 HOH   A O   
7225 O O   . HOH   D .   ? 0.4983 0.2013 0.4372 0.0339  -0.0900 0.0801  344 HOH   A O   
7226 O O   . HOH   D .   ? 0.8806 0.4523 0.4331 -0.1109 0.1335  0.1255  345 HOH   A O   
7227 O O   . HOH   D .   ? 0.4410 0.6354 0.3370 -0.0828 -0.0310 0.1430  346 HOH   A O   
7228 O O   . HOH   D .   ? 0.5318 0.4799 0.6053 -0.1359 0.0523  0.1281  347 HOH   A O   
7229 O O   . HOH   D .   ? 0.2541 0.1737 0.3479 0.0126  -0.0280 -0.0156 348 HOH   A O   
7230 O O   B HOH   D .   ? 0.1868 0.3221 0.3256 0.0256  -0.0291 -0.0673 349 HOH   A O   
7231 O O   . HOH   D .   ? 0.4841 0.2143 0.4871 0.0850  0.0053  0.0070  350 HOH   A O   
7232 O O   . HOH   D .   ? 0.3018 0.4191 0.3292 -0.1239 -0.1019 -0.0262 351 HOH   A O   
7233 O O   . HOH   D .   ? 0.6059 0.5293 0.4364 0.0508  0.2027  -0.1313 352 HOH   A O   
7234 O O   . HOH   D .   ? 0.1380 0.1695 0.3110 0.0098  -0.0240 0.0023  353 HOH   A O   
7235 O O   A HOH   D .   ? 0.2634 0.4013 0.2684 0.0888  -0.0665 -0.0408 354 HOH   A O   
7236 O O   . HOH   D .   ? 0.1460 0.1360 0.2387 0.0038  -0.0161 -0.0027 355 HOH   A O   
7237 O O   . HOH   D .   ? 0.1451 0.2114 0.2690 0.0089  0.0010  0.0488  356 HOH   A O   
7238 O O   A HOH   D .   ? 0.1117 0.1349 0.1839 0.0067  -0.0128 -0.0028 357 HOH   A O   
7239 O O   . HOH   D .   ? 0.5030 0.3810 0.2812 0.0280  0.0614  0.0730  358 HOH   A O   
7240 O O   . HOH   D .   ? 0.3668 0.6301 0.6640 -0.1495 0.0629  0.2366  359 HOH   A O   
7241 O O   B HOH   D .   ? 0.1839 0.3781 0.2187 0.0343  -0.0128 0.0203  360 HOH   A O   
7242 O O   . HOH   D .   ? 0.6008 0.2380 0.3714 -0.1522 0.1538  -0.0479 361 HOH   A O   
7243 O O   . HOH   D .   ? 0.2601 0.3590 0.2759 0.0225  0.0597  0.1057  362 HOH   A O   
7244 O O   . HOH   D .   ? 0.3030 0.5840 0.3414 -0.0672 0.0355  0.0931  363 HOH   A O   
7245 O O   . HOH   D .   ? 0.3089 0.3374 0.2762 -0.0780 -0.0420 -0.0634 364 HOH   A O   
7246 O O   . HOH   D .   ? 0.2205 0.3879 0.3684 0.0743  -0.0616 -0.0164 365 HOH   A O   
7247 O O   . HOH   D .   ? 0.1796 0.1641 0.2765 0.0086  -0.0238 0.0220  366 HOH   A O   
7248 O O   . HOH   D .   ? 0.1259 0.1213 0.2031 -0.0041 0.0099  0.0134  367 HOH   A O   
7249 O O   . HOH   D .   ? 0.4368 0.5594 0.4102 -0.0115 -0.1408 -0.1548 368 HOH   A O   
7250 O O   . HOH   D .   ? 0.2892 0.2976 0.4735 -0.0721 -0.0867 -0.0757 369 HOH   A O   
7251 O O   . HOH   D .   ? 0.1908 0.1846 0.2513 -0.0425 0.0126  0.0235  370 HOH   A O   
7252 O O   . HOH   D .   ? 0.1478 0.1183 0.2448 -0.0031 0.0115  -0.0121 371 HOH   A O   
7253 O O   A HOH   D .   ? 0.3427 0.1418 0.1814 0.0334  0.0128  -0.0255 372 HOH   A O   
7254 O O   . HOH   D .   ? 0.3388 0.2192 0.5461 -0.0866 -0.0567 0.0507  373 HOH   A O   
7255 O O   . HOH   D .   ? 0.3253 0.5025 0.3887 0.0507  0.0872  -0.1049 374 HOH   A O   
7256 O O   A HOH   D .   ? 0.1673 0.1824 0.2754 -0.0461 0.0704  0.0152  375 HOH   A O   
7257 O O   . HOH   D .   ? 0.6598 0.5560 0.6572 0.0068  -0.0630 0.2007  376 HOH   A O   
7258 O O   . HOH   D .   ? 0.1834 0.2798 0.4331 -0.0394 0.1062  0.0324  377 HOH   A O   
7259 O O   . HOH   D .   ? 0.1439 0.1417 0.2003 -0.0074 -0.0170 -0.0147 378 HOH   A O   
7260 O O   . HOH   D .   ? 0.1811 0.1868 0.2424 0.0051  0.0106  0.0033  379 HOH   A O   
7261 O O   . HOH   D .   ? 0.3248 0.3457 0.5405 -0.0309 0.1563  -0.0070 380 HOH   A O   
7262 O O   . HOH   D .   ? 0.1609 0.1256 0.2179 -0.0183 0.0055  0.0022  381 HOH   A O   
7263 O O   . HOH   D .   ? 0.3885 0.2083 0.5138 -0.1060 0.1019  0.0363  382 HOH   A O   
7264 O O   A HOH   D .   ? 0.0851 0.1151 0.1566 0.0160  -0.0252 -0.0353 383 HOH   A O   
7265 O O   . HOH   D .   ? 0.2169 0.2274 0.2368 -0.0230 -0.0362 0.0285  384 HOH   A O   
7266 O O   . HOH   D .   ? 0.2657 0.4712 0.2916 -0.0470 0.0788  -0.1042 385 HOH   A O   
7267 O O   . HOH   D .   ? 0.2114 0.3108 0.3794 0.0541  0.0841  -0.0464 386 HOH   A O   
7268 O O   A HOH   D .   ? 0.2378 0.3631 0.3494 -0.0436 -0.0031 0.0461  387 HOH   A O   
7269 O O   . HOH   D .   ? 0.2972 0.2626 0.3523 0.0156  -0.0183 0.0975  388 HOH   A O   
7270 O O   . HOH   D .   ? 0.3830 0.2884 0.4065 -0.1018 -0.0607 -0.0123 389 HOH   A O   
7271 O O   . HOH   D .   ? 0.6107 0.4087 0.2084 -0.0454 0.0773  0.0158  390 HOH   A O   
7272 O O   . HOH   D .   ? 0.3111 0.2769 0.3531 0.0142  -0.0630 -0.0109 391 HOH   A O   
7273 O O   . HOH   D .   ? 0.4088 0.5802 0.5018 -0.0325 -0.1323 -0.0749 392 HOH   A O   
7274 O O   . HOH   D .   ? 0.2231 0.2940 0.3266 -0.0373 -0.0116 0.0170  393 HOH   A O   
7275 O O   . HOH   D .   ? 0.2999 0.2834 0.2295 0.0575  0.0605  0.0368  394 HOH   A O   
7276 O O   . HOH   D .   ? 0.3996 0.1916 0.2476 0.1267  0.0432  0.0247  395 HOH   A O   
7277 O O   . HOH   D .   ? 0.2744 0.1940 0.2273 -0.0607 0.0210  0.0252  396 HOH   A O   
7278 O O   . HOH   D .   ? 0.6182 0.6124 0.4828 -0.1451 0.1271  0.0966  397 HOH   A O   
7279 O O   . HOH   D .   ? 0.1999 0.1587 0.1985 -0.0056 0.0067  0.0071  398 HOH   A O   
7280 O O   . HOH   D .   ? 0.2010 0.2166 0.2999 -0.0115 0.0321  0.0608  399 HOH   A O   
7281 O O   . HOH   D .   ? 0.4813 0.5168 0.3222 -0.0233 -0.1158 0.0123  400 HOH   A O   
7282 O O   . HOH   D .   ? 0.2509 0.3007 0.3671 -0.0019 0.1032  -0.0004 401 HOH   A O   
7283 O O   . HOH   D .   ? 0.2280 0.2524 0.4931 0.0035  -0.0624 -0.0605 402 HOH   A O   
7284 O O   . HOH   D .   ? 0.2432 0.3692 0.6158 0.0824  0.0337  0.0461  403 HOH   A O   
7285 O O   . HOH   D .   ? 0.3337 0.2932 0.6961 0.0530  0.0992  -0.0365 404 HOH   A O   
7286 O O   . HOH   D .   ? 0.1690 0.2113 0.3379 -0.0286 -0.0186 0.0410  405 HOH   A O   
7287 O O   . HOH   D .   ? 0.5591 0.7535 0.4109 0.0521  0.2703  -0.0681 406 HOH   A O   
7288 O O   . HOH   D .   ? 0.2930 0.1935 0.2866 -0.0259 0.0213  0.0255  407 HOH   A O   
7289 O O   . HOH   D .   ? 0.1972 0.1452 0.3070 0.0024  -0.0251 0.0218  408 HOH   A O   
7290 O O   B HOH   D .   ? 0.4010 0.2997 0.3957 0.0294  0.0614  0.0293  409 HOH   A O   
7291 O O   . HOH   D .   ? 0.1698 0.1827 0.3708 0.0357  0.0912  0.0814  410 HOH   A O   
7292 O O   . HOH   D .   ? 0.6310 0.6497 0.6250 0.0450  -0.0998 0.0757  411 HOH   A O   
7293 O O   . HOH   D .   ? 0.6358 0.4507 0.5488 -0.0080 -0.1200 0.0224  412 HOH   A O   
7294 O O   . HOH   D .   ? 0.2617 0.3266 0.3669 0.0689  -0.0046 -0.0010 413 HOH   A O   
7295 O O   . HOH   D .   ? 0.2077 0.2592 0.3213 -0.0254 -0.0050 0.0098  414 HOH   A O   
7296 O O   . HOH   D .   ? 0.4037 0.3567 0.3756 0.1377  -0.0732 -0.1381 415 HOH   A O   
7297 O O   . HOH   D .   ? 0.2814 0.2723 0.2713 -0.0799 -0.0583 0.0217  416 HOH   A O   
7298 O O   . HOH   D .   ? 0.5027 0.5441 0.5417 -0.1770 0.1062  -0.1194 417 HOH   A O   
7299 O O   . HOH   D .   ? 0.3859 0.1877 0.4661 -0.0554 -0.1919 0.0658  418 HOH   A O   
7300 O O   . HOH   D .   ? 0.4947 0.5025 0.5226 -0.0799 -0.0266 -0.0950 419 HOH   A O   
7301 O O   A HOH   D .   ? 0.1832 0.2255 0.2448 -0.0056 0.0030  -0.0241 420 HOH   A O   
7302 O O   . HOH   D .   ? 0.2254 0.2844 0.2557 0.0109  -0.0551 0.0360  421 HOH   A O   
7303 O O   . HOH   D .   ? 0.4009 0.2613 0.2265 -0.1056 0.0460  0.0452  422 HOH   A O   
7304 O O   . HOH   D .   ? 0.2292 0.4660 0.2598 0.1709  -0.0157 -0.0148 423 HOH   A O   
7305 O O   A HOH   D .   ? 0.1450 0.1336 0.2045 0.0100  -0.0262 0.0219  424 HOH   A O   
7306 O O   A HOH   D .   ? 0.2056 0.1812 0.2389 0.0312  -0.0813 -0.0844 425 HOH   A O   
7307 O O   . HOH   D .   ? 0.5290 0.2979 0.3941 0.1112  -0.1335 -0.0615 426 HOH   A O   
7308 O O   . HOH   D .   ? 0.3305 0.1213 0.2498 -0.0000 -0.0627 0.0104  427 HOH   A O   
7309 O O   . HOH   D .   ? 0.2285 0.1374 0.2657 -0.0127 0.0351  0.0035  428 HOH   A O   
7310 O O   . HOH   D .   ? 0.1420 0.1541 0.2865 0.0013  -0.0026 0.0111  429 HOH   A O   
7311 O O   A HOH   D .   ? 0.6117 0.2933 0.4696 0.0034  0.0453  0.0418  430 HOH   A O   
7312 O O   . HOH   D .   ? 0.4332 0.4786 0.7765 0.1279  -0.0703 -0.1562 431 HOH   A O   
7313 O O   A HOH   D .   ? 0.4017 0.3144 0.2190 -0.0458 0.0625  0.0389  432 HOH   A O   
7314 O O   . HOH   D .   ? 0.2883 0.3908 0.6971 -0.0233 0.1457  -0.0289 433 HOH   A O   
7315 O O   . HOH   D .   ? 0.3006 0.5414 0.1866 -0.0425 0.0435  0.0163  434 HOH   A O   
7316 O O   . HOH   D .   ? 0.7781 0.8622 0.7284 0.1266  -0.0810 0.0920  435 HOH   A O   
7317 O O   B HOH   D .   ? 0.6295 0.5167 0.5793 0.0450  0.0427  -0.0372 436 HOH   A O   
7318 O O   . HOH   D .   ? 0.4794 0.5826 0.4057 -0.0785 -0.1399 -0.0753 437 HOH   A O   
7319 O O   . HOH   D .   ? 0.7450 0.7293 0.6827 -0.0738 0.0472  -0.0734 438 HOH   A O   
7320 O O   B HOH   D .   ? 0.3888 0.2632 0.4620 0.0541  0.0763  -0.0366 439 HOH   A O   
7321 O O   A HOH   D .   ? 0.1439 0.0776 0.2234 0.0184  -0.0273 0.0403  440 HOH   A O   
7322 O O   . HOH   D .   ? 0.6299 0.6013 0.3621 0.2597  -0.0225 -0.0289 441 HOH   A O   
7323 O O   . HOH   D .   ? 0.5661 0.3735 0.3224 -0.1236 0.1009  0.0663  442 HOH   A O   
7324 O O   . HOH   D .   ? 0.3802 0.4182 0.5489 -0.0767 -0.0880 -0.1086 443 HOH   A O   
7325 O O   B HOH   D .   ? 0.3106 0.1361 0.3154 0.0679  -0.0393 0.0656  444 HOH   A O   
7326 O O   . HOH   D .   ? 0.2058 0.1451 0.2739 -0.0035 0.0002  0.0113  445 HOH   A O   
7327 O O   . HOH   D .   ? 0.4014 0.3616 0.3153 0.2219  -0.0717 -0.0679 446 HOH   A O   
7328 O O   . HOH   D .   ? 0.4657 0.7694 0.6027 0.2251  -0.0791 -0.0199 447 HOH   A O   
7329 O O   . HOH   D .   ? 0.7043 0.6844 0.4701 0.2053  -0.0932 0.1894  448 HOH   A O   
7330 O O   . HOH   D .   ? 0.2277 0.2197 0.3128 0.0211  0.0431  0.0140  449 HOH   A O   
7331 O O   B HOH   D .   ? 0.3111 0.3368 0.2542 0.1808  0.0179  0.0196  450 HOH   A O   
7332 O O   . HOH   D .   ? 0.4796 0.4930 0.4958 0.1695  0.1544  0.1954  451 HOH   A O   
7333 O O   . HOH   D .   ? 0.5650 0.3321 0.4808 0.0909  0.0235  0.1655  452 HOH   A O   
7334 O O   . HOH   D .   ? 0.2014 0.2441 0.2500 -0.0001 -0.0133 -0.0396 453 HOH   A O   
7335 O O   B HOH   D .   ? 0.4674 0.2686 0.4858 0.0975  0.0548  -0.0406 454 HOH   A O   
7336 O O   . HOH   D .   ? 0.1710 0.2047 0.5863 -0.0183 -0.0854 0.0451  455 HOH   A O   
7337 O O   A HOH   D .   ? 0.1631 0.2467 0.2193 0.0370  0.0010  -0.0319 456 HOH   A O   
7338 O O   A HOH   D .   ? 0.5123 0.3947 0.3764 0.1119  0.1725  0.1414  457 HOH   A O   
7339 O O   . HOH   D .   ? 0.4522 0.6353 0.6809 0.0036  -0.1348 0.2172  458 HOH   A O   
7340 O O   . HOH   D .   ? 0.4187 0.4023 0.3885 0.0009  -0.0531 0.1038  459 HOH   A O   
7341 O O   . HOH   D .   ? 0.6478 0.8113 0.4559 0.0343  -0.0455 -0.1004 460 HOH   A O   
7342 O O   . HOH   D .   ? 0.6653 0.6704 0.4739 -0.1009 0.1578  0.0863  461 HOH   A O   
7343 O O   . HOH   D .   ? 0.2716 0.2894 0.4637 0.0408  -0.0563 0.0828  462 HOH   A O   
7344 O O   . HOH   D .   ? 0.3380 0.3035 0.3390 -0.1081 0.0114  -0.0468 463 HOH   A O   
7345 O O   . HOH   D .   ? 0.6787 0.4102 0.5578 0.0472  0.0140  0.1461  464 HOH   A O   
7346 O O   . HOH   D .   ? 0.2470 0.5171 0.4447 -0.1095 0.0425  -0.1540 465 HOH   A O   
7347 O O   . HOH   D .   ? 0.4838 0.4126 0.5315 0.0173  -0.0477 -0.0771 466 HOH   A O   
7348 O O   . HOH   D .   ? 0.3598 0.3705 0.3920 0.0764  0.0113  0.0114  467 HOH   A O   
7349 O O   . HOH   D .   ? 0.3252 0.3914 0.3373 -0.0040 -0.0567 0.0180  468 HOH   A O   
7350 O O   . HOH   D .   ? 0.4367 0.5999 0.3956 -0.0867 -0.0539 0.1753  469 HOH   A O   
7351 O O   . HOH   D .   ? 0.5640 0.2637 0.7174 0.0540  0.1800  0.1494  470 HOH   A O   
7352 O O   . HOH   D .   ? 0.2916 0.4829 0.4967 0.0947  0.0253  -0.1571 471 HOH   A O   
7353 O O   . HOH   D .   ? 0.3931 0.5696 0.3447 0.0633  -0.1054 -0.0445 472 HOH   A O   
7354 O O   . HOH   D .   ? 0.3441 0.1715 0.2985 0.0468  -0.1003 -0.0284 473 HOH   A O   
7355 O O   . HOH   D .   ? 0.2571 0.2800 0.3460 -0.1075 0.0344  -0.0412 474 HOH   A O   
7356 O O   . HOH   D .   ? 0.5616 0.4768 0.4638 -0.0198 0.1657  0.0077  475 HOH   A O   
7357 O O   . HOH   D .   ? 0.2604 0.2802 0.3507 0.0315  0.0160  -0.0024 476 HOH   A O   
7358 O O   . HOH   D .   ? 0.2758 0.3458 0.3254 0.0982  0.0447  0.0708  477 HOH   A O   
7359 O O   . HOH   D .   ? 0.4850 0.4980 0.3272 0.0263  -0.0562 0.0724  478 HOH   A O   
7360 O O   . HOH   D .   ? 0.4718 0.5317 0.4982 0.0911  -0.1125 -0.1005 479 HOH   A O   
7361 O O   . HOH   D .   ? 0.5181 0.2890 0.3776 0.0198  -0.0257 0.0587  480 HOH   A O   
7362 O O   . HOH   D .   ? 0.5525 0.5926 0.5945 -0.1754 -0.0658 0.0780  481 HOH   A O   
7363 O O   . HOH   D .   ? 0.4195 0.4389 0.5364 -0.2269 0.0264  -0.0230 482 HOH   A O   
7364 O O   . HOH   D .   ? 0.5631 0.4345 0.5883 -0.0614 0.0094  0.0402  483 HOH   A O   
7365 O O   . HOH   D .   ? 0.3307 0.5053 0.3237 -0.0280 -0.0257 -0.0228 484 HOH   A O   
7366 O O   . HOH   D .   ? 0.5471 0.5126 0.3468 0.0386  0.0600  -0.1432 485 HOH   A O   
7367 O O   . HOH   D .   ? 0.5213 0.4392 0.3731 -0.0864 -0.0786 -0.0222 486 HOH   A O   
7368 O O   . HOH   D .   ? 0.3180 0.4962 0.3238 0.1148  0.0933  0.1816  487 HOH   A O   
7369 O O   . HOH   D .   ? 0.8281 0.4130 0.3076 -0.0512 -0.1026 -0.0607 488 HOH   A O   
7370 O O   . HOH   D .   ? 0.5416 0.5816 0.4822 -0.0748 -0.0799 -0.0951 489 HOH   A O   
7371 O O   . HOH   D .   ? 0.4744 0.3632 0.3741 -0.1655 0.0748  0.0533  490 HOH   A O   
7372 O O   . HOH   D .   ? 0.3067 0.4935 0.4596 -0.0471 0.0389  0.1808  491 HOH   A O   
7373 O O   . HOH   D .   ? 0.4823 0.3920 0.4324 -0.0310 0.1112  0.0027  492 HOH   A O   
7374 O O   . HOH   D .   ? 0.5121 0.5813 0.6291 0.0403  0.2454  -0.1420 493 HOH   A O   
7375 O O   . HOH   D .   ? 0.5911 0.5764 0.5143 -0.0741 -0.1185 0.0719  494 HOH   A O   
7376 O O   . HOH   D .   ? 0.6576 0.5338 0.4180 0.0757  0.1570  0.1013  495 HOH   A O   
7377 O O   B HOH   D .   ? 0.2525 0.2546 0.3471 0.0389  -0.0172 -0.0336 496 HOH   A O   
7378 O O   . HOH   D .   ? 0.3828 0.3236 0.2661 -0.0394 0.0827  -0.0046 497 HOH   A O   
7379 O O   . HOH   D .   ? 0.4944 0.3248 0.4271 -0.0670 0.1954  0.0265  498 HOH   A O   
7380 O O   . HOH   D .   ? 0.2674 0.1910 0.4825 -0.0050 0.0389  0.0602  499 HOH   A O   
7381 O O   . HOH   D .   ? 0.2657 0.3801 0.5002 0.0046  0.1087  -0.0831 500 HOH   A O   
7382 O O   . HOH   D .   ? 0.2506 0.2684 0.6849 -0.0194 -0.1544 0.0331  501 HOH   A O   
7383 O O   . HOH   D .   ? 0.3793 0.9214 0.5432 -0.1312 -0.0646 0.2361  502 HOH   A O   
7384 O O   . HOH   D .   ? 0.7772 0.3031 0.6499 0.0091  0.0863  0.1733  503 HOH   A O   
7385 O O   . HOH   D .   ? 0.2532 0.4196 0.3878 0.0369  -0.0326 0.0422  504 HOH   A O   
7386 O O   . HOH   D .   ? 0.4534 0.2184 0.3841 -0.1253 0.0461  0.0025  505 HOH   A O   
7387 O O   . HOH   D .   ? 0.2140 0.3075 0.3684 0.0446  -0.0264 0.0275  506 HOH   A O   
7388 O O   . HOH   D .   ? 0.5419 0.6605 0.5153 0.0741  -0.0925 0.0088  507 HOH   A O   
7389 O O   . HOH   D .   ? 0.7091 0.6065 0.7121 -0.0634 0.0232  -0.0458 508 HOH   A O   
7390 O O   . HOH   D .   ? 0.3950 0.7138 0.4697 0.2055  0.1211  -0.0602 509 HOH   A O   
7391 O O   . HOH   D .   ? 0.4562 0.4925 0.5416 0.0712  -0.1388 -0.0819 510 HOH   A O   
7392 O O   . HOH   D .   ? 0.4540 0.6498 0.4261 0.2767  -0.0513 0.0065  511 HOH   A O   
7393 O O   . HOH   D .   ? 0.4001 0.5826 0.4627 -0.0114 -0.0371 -0.1356 512 HOH   A O   
7394 O O   . HOH   D .   ? 0.4401 0.3809 0.5135 0.0571  0.0266  0.0544  513 HOH   A O   
7395 O O   . HOH   D .   ? 0.3078 0.7148 0.3631 0.1071  0.0183  0.0167  514 HOH   A O   
7396 O O   . HOH   D .   ? 0.4860 0.5411 0.5115 -0.0682 -0.0873 0.0520  515 HOH   A O   
7397 O O   . HOH   D .   ? 0.4917 0.3875 0.5451 -0.0775 -0.1004 0.2078  516 HOH   A O   
7398 O O   . HOH   E .   ? 0.2370 0.2120 0.3149 0.0314  0.0630  0.0309  201 HOH   B O   
7399 O O   . HOH   E .   ? 0.6464 0.3863 0.2500 0.0897  -0.0698 -0.0935 202 HOH   B O   
7400 O O   . HOH   E .   ? 0.5956 0.6223 0.6567 0.1804  0.0749  0.0071  203 HOH   B O   
7401 O O   . HOH   E .   ? 0.5252 0.5713 0.4137 0.3095  -0.1158 -0.0465 204 HOH   B O   
7402 O O   . HOH   E .   ? 0.5895 0.4345 0.6083 0.1172  -0.0877 0.2547  205 HOH   B O   
7403 O O   . HOH   E .   ? 0.4974 0.5586 0.2889 0.1074  -0.0785 -0.0338 206 HOH   B O   
7404 O O   . HOH   E .   ? 0.3388 0.3401 0.5420 -0.0441 0.0754  -0.0630 207 HOH   B O   
7405 O O   . HOH   E .   ? 0.3286 0.6741 0.3251 0.0660  -0.0020 0.1770  208 HOH   B O   
7406 O O   . HOH   E .   ? 0.5009 0.2667 0.3347 -0.0108 -0.0162 -0.0736 209 HOH   B O   
7407 O O   . HOH   E .   ? 0.3104 0.2047 0.5317 0.0440  0.1830  0.1008  210 HOH   B O   
7408 O O   . HOH   E .   ? 0.4306 0.5660 0.3870 -0.0457 -0.1077 0.1856  211 HOH   B O   
7409 O O   . HOH   E .   ? 0.3949 0.4230 0.5358 -0.1238 0.0612  -0.1282 212 HOH   B O   
7410 O O   . HOH   E .   ? 0.2111 0.2332 0.3285 0.0007  -0.0025 -0.0221 213 HOH   B O   
7411 O O   . HOH   E .   ? 0.6658 0.2293 0.5272 0.0794  0.1545  0.0126  214 HOH   B O   
7412 O O   . HOH   E .   ? 0.3959 0.4619 0.3580 0.2018  -0.0524 -0.0244 215 HOH   B O   
7413 O O   . HOH   E .   ? 0.2869 0.2829 0.7122 0.0689  -0.1196 0.0548  216 HOH   B O   
7414 O O   . HOH   E .   ? 0.2087 0.5489 0.4702 -0.0289 0.0704  -0.2267 217 HOH   B O   
7415 O O   . HOH   E .   ? 0.2500 0.4600 0.6034 0.0259  -0.0489 0.0697  218 HOH   B O   
7416 O O   . HOH   E .   ? 0.3097 0.2195 0.3920 0.0657  -0.0305 -0.0561 219 HOH   B O   
7417 O O   . HOH   E .   ? 0.3993 0.6318 0.3262 0.2553  -0.0389 -0.0362 220 HOH   B O   
7418 O O   . HOH   E .   ? 0.2672 0.3626 0.4441 -0.0831 0.0496  -0.1139 221 HOH   B O   
7419 O O   . HOH   E .   ? 0.5733 0.3207 0.4630 -0.1779 0.0740  -0.0034 222 HOH   B O   
7420 O O   . HOH   E .   ? 0.1450 0.1722 0.2721 -0.0207 -0.0009 -0.0055 223 HOH   B O   
7421 O O   . HOH   E .   ? 0.3251 0.2332 0.4505 -0.0097 0.0996  0.0103  224 HOH   B O   
7422 O O   . HOH   E .   ? 0.4021 0.4702 0.4302 -0.0132 0.0645  -0.1653 225 HOH   B O   
7423 O O   . HOH   E .   ? 0.1985 0.1986 0.2016 0.0120  -0.0111 0.0011  226 HOH   B O   
7424 O O   . HOH   E .   ? 0.3355 0.3838 0.4643 -0.1425 0.0356  0.0401  227 HOH   B O   
7425 O O   . HOH   E .   ? 0.4871 0.1924 0.3107 -0.0092 -0.0802 0.0093  228 HOH   B O   
7426 O O   . HOH   E .   ? 0.2486 0.1736 0.3038 -0.0347 0.0873  0.0177  229 HOH   B O   
7427 O O   . HOH   E .   ? 0.3826 0.5962 0.3949 0.2670  0.0017  -0.0588 230 HOH   B O   
7428 O O   . HOH   E .   ? 0.1361 0.1326 0.2218 -0.0064 -0.0077 0.0019  231 HOH   B O   
7429 O O   . HOH   E .   ? 0.2939 0.2435 0.3191 0.0405  0.0020  -0.0852 232 HOH   B O   
7430 O O   . HOH   E .   ? 0.3494 0.3660 0.2899 0.0575  0.0656  0.0451  233 HOH   B O   
7431 O O   . HOH   E .   ? 0.1987 0.1208 0.3563 0.0159  -0.0660 -0.0185 234 HOH   B O   
7432 O O   . HOH   E .   ? 0.3848 0.3015 0.3641 -0.0783 0.0254  -0.0547 235 HOH   B O   
7433 O O   . HOH   E .   ? 0.2203 0.3627 0.2827 -0.0308 -0.0508 -0.0425 236 HOH   B O   
7434 O O   . HOH   E .   ? 0.1612 0.1895 0.2771 -0.0088 -0.0057 -0.0132 237 HOH   B O   
7435 O O   . HOH   E .   ? 0.4331 0.3348 0.2685 0.0820  -0.0292 -0.1031 238 HOH   B O   
7436 O O   . HOH   E .   ? 0.4256 0.3679 0.6763 -0.0360 -0.1798 -0.0914 239 HOH   B O   
7437 O O   . HOH   E .   ? 0.2865 0.2039 0.3469 0.0011  0.0906  -0.0100 240 HOH   B O   
7438 O O   . HOH   E .   ? 0.1928 0.2148 0.2795 -0.0450 0.0124  -0.0283 241 HOH   B O   
7439 O O   . HOH   E .   ? 0.4660 0.3125 0.3740 -0.2191 0.0354  -0.0210 242 HOH   B O   
7440 O O   . HOH   E .   ? 0.1414 0.1433 0.2656 -0.0111 0.0003  -0.0212 243 HOH   B O   
7441 O O   . HOH   E .   ? 0.3686 0.1878 0.2406 0.0167  -0.0822 -0.0173 244 HOH   B O   
7442 O O   . HOH   E .   ? 0.2969 0.1662 0.5341 -0.0236 -0.1288 -0.0356 245 HOH   B O   
7443 O O   . HOH   E .   ? 0.1375 0.1200 0.1881 -0.0034 -0.0092 0.0132  246 HOH   B O   
7444 O O   . HOH   E .   ? 0.2053 0.4220 0.2418 -0.0519 -0.0301 0.0570  247 HOH   B O   
7445 O O   . HOH   E .   ? 0.2065 0.1352 0.2416 -0.0217 -0.0397 0.0235  248 HOH   B O   
7446 O O   . HOH   E .   ? 0.1966 0.1985 0.3550 -0.0303 -0.0347 -0.0441 249 HOH   B O   
7447 O O   . HOH   E .   ? 0.1555 0.1567 0.2785 -0.0168 -0.0292 0.0113  250 HOH   B O   
7448 O O   . HOH   E .   ? 0.3646 0.5426 0.4650 0.1296  -0.0917 -0.1813 251 HOH   B O   
7449 O O   . HOH   E .   ? 0.2096 0.2016 0.2309 0.0030  -0.0029 -0.0107 252 HOH   B O   
7450 O O   . HOH   E .   ? 0.3085 0.2463 0.3215 0.1203  0.0837  0.0401  253 HOH   B O   
7451 O O   . HOH   E .   ? 0.4083 0.3057 0.4725 -0.0772 0.0461  0.0981  254 HOH   B O   
7452 O O   . HOH   E .   ? 0.1823 0.2539 0.2739 0.0578  0.0268  0.0898  255 HOH   B O   
7453 O O   . HOH   E .   ? 0.2550 0.2158 0.2745 -0.0240 -0.0014 -0.0289 256 HOH   B O   
7454 O O   . HOH   E .   ? 0.1870 0.1423 0.2456 -0.0331 -0.0181 0.0179  257 HOH   B O   
7455 O O   . HOH   E .   ? 0.2596 0.4747 0.3890 -0.1090 -0.0260 -0.0958 258 HOH   B O   
7456 O O   . HOH   E .   ? 0.2297 0.1850 0.2392 -0.0345 -0.0424 0.0049  259 HOH   B O   
7457 O O   . HOH   E .   ? 0.2060 0.3609 0.2697 -0.0688 0.0096  0.0978  260 HOH   B O   
7458 O O   . HOH   E .   ? 0.1275 0.1419 0.2247 -0.0047 0.0057  0.0122  261 HOH   B O   
7459 O O   . HOH   E .   ? 0.2251 0.1877 0.3729 0.0024  -0.0555 -0.0433 262 HOH   B O   
7460 O O   . HOH   E .   ? 0.3276 0.2785 0.2420 0.0673  0.0416  0.0171  263 HOH   B O   
7461 O O   . HOH   E .   ? 0.2162 0.2091 0.2806 0.0708  -0.0780 -0.0585 264 HOH   B O   
7462 O O   . HOH   E .   ? 0.2497 0.2582 0.3454 -0.0324 0.0489  -0.0827 265 HOH   B O   
7463 O O   . HOH   E .   ? 0.2234 0.3090 0.4565 0.0792  -0.0742 -0.0682 266 HOH   B O   
7464 O O   . HOH   E .   ? 0.3969 0.4305 0.5772 -0.0285 -0.1348 -0.0185 267 HOH   B O   
7465 O O   . HOH   E .   ? 0.1623 0.1365 0.5039 -0.0152 -0.0385 -0.0024 268 HOH   B O   
7466 O O   . HOH   E .   ? 0.1892 0.4247 0.6493 -0.0668 -0.0441 0.0781  269 HOH   B O   
7467 O O   . HOH   E .   ? 0.3650 0.4679 0.2770 0.2033  -0.0350 -0.0177 270 HOH   B O   
7468 O O   . HOH   E .   ? 0.2602 0.2783 0.3911 -0.0101 -0.0115 -0.1159 271 HOH   B O   
7469 O O   . HOH   E .   ? 0.2436 0.3133 0.3128 -0.0810 -0.0686 -0.0173 272 HOH   B O   
7470 O O   . HOH   E .   ? 0.2730 0.3743 0.3820 0.0195  0.1113  0.0154  273 HOH   B O   
7471 O O   . HOH   E .   ? 0.2075 0.1902 0.2493 0.0486  -0.0238 -0.0093 274 HOH   B O   
7472 O O   . HOH   E .   ? 0.6143 0.5276 0.4495 -0.1143 0.0414  0.0819  275 HOH   B O   
7473 O O   . HOH   E .   ? 0.4720 0.2992 0.2628 0.0748  0.0465  -0.0231 276 HOH   B O   
7474 O O   . HOH   E .   ? 0.3311 0.4267 0.4233 0.0092  -0.0074 -0.0937 277 HOH   B O   
7475 O O   . HOH   E .   ? 0.2583 0.1938 0.3077 -0.0600 0.0144  -0.0092 278 HOH   B O   
7476 O O   . HOH   E .   ? 0.4202 0.3155 0.4311 -0.0721 -0.0960 -0.0542 279 HOH   B O   
7477 O O   . HOH   E .   ? 0.4666 0.5505 0.2670 0.1102  -0.0040 -0.0376 280 HOH   B O   
7478 O O   . HOH   E .   ? 0.2212 0.1961 0.2861 0.0125  -0.0290 0.0139  281 HOH   B O   
7479 O O   . HOH   E .   ? 0.2807 0.2736 0.2640 -0.0411 -0.0845 -0.0045 282 HOH   B O   
7480 O O   . HOH   E .   ? 0.1755 0.1717 0.1934 -0.0369 -0.0383 0.0038  283 HOH   B O   
7481 O O   . HOH   E .   ? 0.1542 0.1431 0.3215 -0.0087 0.0031  -0.0054 284 HOH   B O   
7482 O O   . HOH   E .   ? 0.5261 0.4415 0.5081 0.1554  -0.0296 -0.0561 285 HOH   B O   
7483 O O   . HOH   E .   ? 0.3943 0.3539 0.4380 0.1457  -0.1266 -0.1134 286 HOH   B O   
7484 O O   . HOH   E .   ? 0.3139 0.4979 0.3558 -0.0388 -0.0829 0.1324  287 HOH   B O   
7485 O O   . HOH   E .   ? 0.2782 0.2209 0.3834 -0.0358 0.0885  -0.0111 288 HOH   B O   
7486 O O   . HOH   E .   ? 0.1580 0.1664 0.2735 0.0175  -0.0032 0.0033  289 HOH   B O   
7487 O O   . HOH   E .   ? 0.1472 0.1443 0.2019 0.0029  0.0101  -0.0001 290 HOH   B O   
7488 O O   . HOH   E .   ? 0.2061 0.4514 0.3951 -0.0517 -0.0409 -0.0741 291 HOH   B O   
7489 O O   . HOH   E .   ? 0.4214 0.4974 0.2089 -0.0043 0.0409  0.0352  292 HOH   B O   
7490 O O   . HOH   E .   ? 0.3440 0.1946 0.4065 -0.0580 -0.1921 0.0563  293 HOH   B O   
7491 O O   . HOH   E .   ? 0.3558 0.3222 0.2425 0.0781  -0.0848 -0.0335 294 HOH   B O   
7492 O O   . HOH   E .   ? 0.1513 0.1898 0.1995 -0.0127 -0.0161 -0.0081 295 HOH   B O   
7493 O O   . HOH   E .   ? 0.2045 0.2498 0.6039 0.0403  -0.0711 -0.0951 296 HOH   B O   
7494 O O   . HOH   E .   ? 0.2361 0.5210 0.4572 -0.1077 -0.0974 0.1195  297 HOH   B O   
7495 O O   . HOH   E .   ? 0.2621 0.2486 0.4328 0.0054  -0.0271 0.0868  298 HOH   B O   
7496 O O   . HOH   E .   ? 0.4243 0.4312 0.7126 0.1236  -0.0059 0.0786  299 HOH   B O   
7497 O O   . HOH   E .   ? 0.2297 0.2606 0.2750 0.0282  -0.0535 0.0350  300 HOH   B O   
7498 O O   . HOH   E .   ? 0.5008 0.4346 0.2978 -0.0468 -0.0730 0.0276  301 HOH   B O   
7499 O O   . HOH   E .   ? 0.1967 0.1480 0.2835 -0.0190 -0.0259 -0.0019 302 HOH   B O   
7500 O O   . HOH   E .   ? 0.1567 0.2898 0.4106 0.0138  -0.0123 -0.1043 303 HOH   B O   
7501 O O   . HOH   E .   ? 0.2786 0.2095 0.4363 0.0393  0.0512  0.0580  304 HOH   B O   
7502 O O   . HOH   E .   ? 0.2744 0.2830 0.3037 -0.0397 0.0800  -0.0528 305 HOH   B O   
7503 O O   . HOH   E .   ? 0.2811 0.2492 0.2475 0.0003  -0.0117 -0.0712 306 HOH   B O   
7504 O O   . HOH   E .   ? 0.1477 0.1483 0.2909 0.0072  -0.0058 0.0004  307 HOH   B O   
7505 O O   . HOH   E .   ? 0.3384 0.1744 0.3996 0.0745  0.1320  0.0583  308 HOH   B O   
7506 O O   . HOH   E .   ? 0.2360 0.6330 0.2733 0.0295  -0.0272 -0.0261 309 HOH   B O   
7507 O O   . HOH   E .   ? 0.1632 0.1476 0.2556 0.0093  0.0011  0.0143  310 HOH   B O   
7508 O O   . HOH   E .   ? 0.2256 0.1338 0.2798 -0.0125 -0.0069 0.0233  311 HOH   B O   
7509 O O   . HOH   E .   ? 0.5544 0.3734 0.2882 0.2599  0.0707  0.0478  312 HOH   B O   
7510 O O   . HOH   E .   ? 0.2989 0.5715 0.7113 0.0875  -0.0501 -0.1089 313 HOH   B O   
7511 O O   . HOH   E .   ? 0.2037 0.1445 0.3730 0.0345  -0.1042 -0.0080 314 HOH   B O   
7512 O O   . HOH   E .   ? 0.4086 0.2181 0.3321 0.1443  0.1100  0.0291  315 HOH   B O   
7513 O O   . HOH   E .   ? 0.1559 0.1776 0.2389 -0.0255 -0.0091 0.0035  316 HOH   B O   
7514 O O   . HOH   E .   ? 0.4654 0.6496 0.2892 -0.0352 -0.0547 0.1808  317 HOH   B O   
7515 O O   . HOH   E .   ? 0.5613 0.2847 0.2932 -0.1986 0.1006  -0.0191 318 HOH   B O   
7516 O O   . HOH   E .   ? 0.5216 0.2190 0.3144 0.0511  0.0861  0.0649  319 HOH   B O   
7517 O O   . HOH   E .   ? 0.1927 0.1965 0.2133 0.0015  0.0101  0.0037  320 HOH   B O   
7518 O O   . HOH   E .   ? 0.2632 0.3333 0.4236 -0.0438 -0.1389 0.0994  321 HOH   B O   
7519 O O   . HOH   E .   ? 0.2200 0.3477 0.4644 -0.0486 -0.0537 0.0343  322 HOH   B O   
7520 O O   . HOH   E .   ? 0.4434 0.3817 0.2851 0.1433  -0.0961 0.0423  323 HOH   B O   
7521 O O   . HOH   E .   ? 0.7588 0.2107 0.2949 -0.0279 -0.0777 0.0270  324 HOH   B O   
7522 O O   . HOH   E .   ? 0.1457 0.2930 0.2677 -0.0022 -0.0367 0.0443  325 HOH   B O   
7523 O O   . HOH   E .   ? 0.1487 0.1414 0.3041 -0.0133 -0.0136 -0.0045 326 HOH   B O   
7524 O O   . HOH   E .   ? 0.6960 0.5122 0.5138 0.2512  0.1667  0.0471  327 HOH   B O   
7525 O O   . HOH   E .   ? 0.7580 0.6681 0.5637 0.3258  0.0326  -0.0453 328 HOH   B O   
7526 O O   . HOH   E .   ? 0.4814 0.3445 0.5285 0.1554  0.1901  0.2037  329 HOH   B O   
7527 O O   . HOH   E .   ? 0.2782 0.3012 0.6849 -0.0179 -0.0606 0.1418  330 HOH   B O   
7528 O O   . HOH   E .   ? 0.6752 0.3269 0.3363 -0.0309 0.0900  0.0709  331 HOH   B O   
7529 O O   . HOH   E .   ? 0.1900 0.1875 0.3279 0.0355  0.0226  0.0103  332 HOH   B O   
7530 O O   . HOH   E .   ? 0.4401 0.4926 0.2112 0.0844  -0.0368 -0.0408 333 HOH   B O   
7531 O O   . HOH   E .   ? 0.2152 0.5163 0.5688 -0.0349 -0.0104 -0.0538 334 HOH   B O   
7532 O O   . HOH   E .   ? 0.2567 0.2006 0.6085 -0.0048 0.0252  0.0049  335 HOH   B O   
7533 O O   . HOH   E .   ? 0.1681 0.2731 0.2719 0.0156  -0.0101 -0.0688 336 HOH   B O   
7534 O O   . HOH   E .   ? 0.2326 0.2096 0.4937 -0.0505 0.0091  0.1083  337 HOH   B O   
7535 O O   . HOH   E .   ? 0.5347 0.3452 0.3595 0.0522  0.0022  -0.1588 338 HOH   B O   
7536 O O   . HOH   E .   ? 0.5812 0.6001 0.2968 -0.0012 -0.0800 0.1731  339 HOH   B O   
7537 O O   . HOH   E .   ? 0.5445 0.5083 0.5102 -0.0524 -0.0918 -0.1196 340 HOH   B O   
7538 O O   . HOH   E .   ? 0.1599 0.1432 0.2644 0.0075  -0.0270 0.0078  341 HOH   B O   
7539 O O   . HOH   E .   ? 0.5102 0.3537 0.3324 0.1192  -0.1274 -0.0817 342 HOH   B O   
7540 O O   . HOH   E .   ? 0.5371 0.5662 0.5655 0.0598  -0.1024 0.2027  343 HOH   B O   
7541 O O   . HOH   E .   ? 0.4701 0.5513 0.2992 0.0985  -0.0026 0.0186  344 HOH   B O   
7542 O O   . HOH   E .   ? 0.5209 0.2231 0.4988 -0.0427 0.1654  0.0408  345 HOH   B O   
7543 O O   . HOH   E .   ? 0.2044 0.1672 0.2760 -0.0074 0.0339  -0.0033 346 HOH   B O   
7544 O O   . HOH   E .   ? 0.3143 0.4089 0.4266 -0.1447 0.0243  0.0265  347 HOH   B O   
7545 O O   . HOH   E .   ? 0.4126 0.4850 0.4650 0.0164  -0.0964 0.0923  348 HOH   B O   
7546 O O   . HOH   E .   ? 0.2533 0.2214 0.4986 -0.0289 -0.0608 -0.0528 349 HOH   B O   
7547 O O   . HOH   E .   ? 0.3424 0.2209 0.4185 -0.0519 -0.0394 -0.0766 350 HOH   B O   
7548 O O   . HOH   E .   ? 0.4176 0.5580 0.3962 -0.0856 -0.1197 -0.0740 351 HOH   B O   
7549 O O   . HOH   E .   ? 0.2185 0.3843 0.4925 0.0078  0.0181  0.0269  352 HOH   B O   
7550 O O   . HOH   E .   ? 0.4719 0.6418 0.6836 0.1090  0.0407  -0.0410 353 HOH   B O   
7551 O O   . HOH   E .   ? 0.4385 0.3716 0.3741 0.0381  0.0910  -0.0183 354 HOH   B O   
7552 O O   . HOH   E .   ? 0.2059 0.5602 0.3348 0.1249  -0.0370 -0.0975 355 HOH   B O   
7553 O O   . HOH   E .   ? 0.5027 0.5250 0.4485 -0.0982 0.0398  0.0205  356 HOH   B O   
7554 O O   . HOH   E .   ? 0.4144 0.2750 0.5252 -0.1041 -0.0521 -0.0250 357 HOH   B O   
7555 O O   . HOH   E .   ? 0.2214 0.3389 0.6074 -0.0449 -0.0681 -0.0487 358 HOH   B O   
7556 O O   . HOH   E .   ? 0.5171 0.6733 0.3701 0.1873  -0.0702 0.0260  359 HOH   B O   
7557 O O   . HOH   E .   ? 0.3000 0.1943 0.3757 0.0523  -0.1095 -0.0499 360 HOH   B O   
7558 O O   . HOH   E .   ? 0.5834 0.4110 0.6247 -0.0385 0.0486  0.0492  361 HOH   B O   
7559 O O   . HOH   E .   ? 0.3992 0.3834 0.4089 0.0705  -0.1563 -0.0434 362 HOH   B O   
7560 O O   . HOH   E .   ? 0.4835 0.6158 0.5158 0.1599  -0.1131 0.1878  363 HOH   B O   
7561 O O   . HOH   E .   ? 0.5271 0.5850 0.5370 -0.0426 0.0484  0.0225  364 HOH   B O   
7562 O O   . HOH   E .   ? 0.4262 0.6016 0.4324 -0.0545 -0.0905 -0.1028 365 HOH   B O   
7563 O O   . HOH   E .   ? 0.5942 0.1880 0.4602 -0.0051 0.0915  0.0107  366 HOH   B O   
7564 O O   . HOH   E .   ? 0.6045 0.4298 0.4463 0.1220  0.1610  0.0663  367 HOH   B O   
7565 O O   . HOH   E .   ? 0.4512 0.5954 0.5421 0.2674  0.0232  0.1085  368 HOH   B O   
7566 O O   . HOH   E .   ? 0.5676 0.3165 0.5600 -0.1564 -0.0400 0.0019  369 HOH   B O   
7567 O O   . HOH   E .   ? 0.4676 0.3980 0.5550 0.0476  -0.1541 -0.0521 370 HOH   B O   
7568 O O   . HOH   E .   ? 0.4458 0.4046 0.4046 0.0234  -0.1513 -0.0242 371 HOH   B O   
7569 O O   . HOH   E .   ? 0.6002 0.5885 0.3393 0.1550  -0.1036 0.0763  372 HOH   B O   
7570 O O   . HOH   E .   ? 0.6882 0.3837 0.3481 -0.1177 -0.0906 -0.0850 373 HOH   B O   
7571 O O   . HOH   E .   ? 0.4671 0.7250 0.6074 0.1857  0.0796  0.2990  374 HOH   B O   
7572 O O   . HOH   E .   ? 0.2413 0.3933 0.4828 0.0420  -0.0875 -0.0511 375 HOH   B O   
7573 O O   . HOH   E .   ? 0.7126 0.7492 0.5401 0.2817  -0.1317 0.0688  376 HOH   B O   
7574 O O   . HOH   E .   ? 0.4681 0.4621 0.5099 -0.1131 -0.1128 0.0600  377 HOH   B O   
7575 O O   . HOH   E .   ? 0.6726 0.3567 0.5710 -0.0381 -0.0659 -0.0435 378 HOH   B O   
7576 O O   . HOH   E .   ? 0.3515 0.3518 0.2453 0.0831  0.0103  0.0000  379 HOH   B O   
7577 O O   . HOH   E .   ? 0.3343 0.5627 0.4936 0.0618  -0.0515 0.0452  380 HOH   B O   
7578 O O   . HOH   E .   ? 0.3115 0.7274 0.5134 0.1133  0.1235  0.1613  381 HOH   B O   
7579 O O   . HOH   E .   ? 0.5975 0.4337 0.4987 -0.0718 -0.0607 -0.0048 382 HOH   B O   
7580 O O   . HOH   E .   ? 0.2840 0.2411 0.3159 -0.0004 -0.0048 0.0319  383 HOH   B O   
7581 O O   . HOH   E .   ? 0.5501 0.7674 0.6073 0.0018  0.2436  0.1476  384 HOH   B O   
7582 O O   . HOH   E .   ? 0.5461 0.6614 0.3759 -0.1234 0.0287  -0.1381 385 HOH   B O   
7583 O O   . HOH   E .   ? 0.2575 0.3756 0.3614 -0.0868 -0.1054 0.0118  386 HOH   B O   
7584 O O   . HOH   E .   ? 0.5685 0.5120 0.3867 -0.0241 -0.0909 -0.0590 387 HOH   B O   
7585 O O   . HOH   E .   ? 0.5372 0.3413 0.2561 0.0588  0.0348  -0.0070 388 HOH   B O   
7586 O O   . HOH   E .   ? 0.6544 0.5801 0.4472 0.2256  0.0404  0.0951  389 HOH   B O   
7587 O O   . HOH   E .   ? 0.6887 0.4186 0.4764 0.0419  0.1067  -0.1374 390 HOH   B O   
7588 O O   . HOH   E .   ? 0.3683 0.2165 0.3192 0.0849  -0.0310 0.0045  391 HOH   B O   
7589 O O   . HOH   E .   ? 0.3503 0.4096 0.3337 -0.0382 -0.0133 0.0396  392 HOH   B O   
7590 O O   . HOH   E .   ? 0.5283 0.2271 0.5066 -0.1065 0.0919  0.0357  393 HOH   B O   
7591 O O   . HOH   E .   ? 0.2478 0.4114 0.6013 -0.1301 -0.0975 0.0536  394 HOH   B O   
7592 O O   . HOH   E .   ? 0.4154 0.3804 0.4034 -0.0093 0.0925  0.0826  395 HOH   B O   
7593 O O   . HOH   E .   ? 0.3287 0.3751 0.3007 0.0260  0.0341  -0.0584 396 HOH   B O   
7594 O O   . HOH   E .   ? 0.4247 0.6243 0.3311 0.1162  -0.0409 -0.1017 397 HOH   B O   
7595 O O   . HOH   E .   ? 0.6741 0.6751 0.7851 0.2746  0.0344  0.2682  398 HOH   B O   
7596 O O   . HOH   E .   ? 0.3207 0.2117 0.4905 0.0348  0.0820  0.0926  399 HOH   B O   
7597 O O   . HOH   E .   ? 0.2281 0.3169 0.6310 -0.0829 -0.1076 0.1010  400 HOH   B O   
7598 O O   . HOH   E .   ? 0.5943 0.3875 0.3152 -0.2088 -0.0038 0.0900  401 HOH   B O   
7599 O O   . HOH   E .   ? 0.6529 0.7387 0.4435 0.1409  -0.0086 0.0700  402 HOH   B O   
# 
