data_7HFV
# 
_entry.id   7HFV 
# 
_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   7HFV         pdb_00007hfv 10.2210/pdb7hfv/pdb 
WWPDB D_1001407421 ?            ?                   
# 
_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                        7HFV 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                     18178.766 2   '3.4.19.121, 3.4.22.-' ? ? 
'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn '(2S,3R)-3-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butan-2-ol' 206.244   1   ?                      ? ? ? 
3 non-polymer syn '(2R,3R)-3-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butan-2-ol' 206.244   1   ?                      ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                 35.453    1   ?                      ? ? ? 
5 water       nat water                                                          18.015    412 ?                      ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2S,3R)-3-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butan-2-ol' A1BBY 
3 '(2R,3R)-3-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butan-2-ol' A1BBZ 
4 'CHLORIDE ION'                                                 CL    
5 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 
A1BBY non-polymer         . '(2S,3R)-3-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butan-2-ol' ? 'C10 H14 N4 O'   206.244 
A1BBZ non-polymer         . '(2R,3R)-3-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butan-2-ol' ? 'C10 H14 N4 O'   206.244 
ALA   'L-peptide linking' y ALANINE                                                        ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                       ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                     ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                ? 'C4 H7 N O4'     133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                 ? 'Cl -1'          35.453  
CYS   'L-peptide linking' y CYSTEINE                                                       ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                      ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                        ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                      ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                          ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                     ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                        ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                         ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                     ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                  ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                        ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                         ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                      ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                       ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                         ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1BBY 1   201 201  A1BBY LA1 A . 
D 3 A1BBZ 1   202 301  A1BBZ LA2 A . 
E 4 CL    1   203 1    CL    CL  A . 
F 5 HOH   1   301 1289 HOH   HOH A . 
F 5 HOH   2   302 196  HOH   HOH A . 
F 5 HOH   3   303 86   HOH   HOH A . 
F 5 HOH   4   304 292  HOH   HOH A . 
F 5 HOH   5   305 1313 HOH   HOH A . 
F 5 HOH   6   306 662  HOH   HOH A . 
F 5 HOH   7   307 105  HOH   HOH A . 
F 5 HOH   8   308 625  HOH   HOH A . 
F 5 HOH   9   309 409  HOH   HOH A . 
F 5 HOH   10  310 93   HOH   HOH A . 
F 5 HOH   11  311 109  HOH   HOH A . 
F 5 HOH   12  312 1301 HOH   HOH A . 
F 5 HOH   13  313 209  HOH   HOH A . 
F 5 HOH   14  314 192  HOH   HOH A . 
F 5 HOH   15  315 115  HOH   HOH A . 
F 5 HOH   16  316 247  HOH   HOH A . 
F 5 HOH   17  317 661  HOH   HOH A . 
F 5 HOH   18  318 124  HOH   HOH A . 
F 5 HOH   19  319 76   HOH   HOH A . 
F 5 HOH   20  320 151  HOH   HOH A . 
F 5 HOH   21  321 405  HOH   HOH A . 
F 5 HOH   22  322 1283 HOH   HOH A . 
F 5 HOH   23  323 225  HOH   HOH A . 
F 5 HOH   24  324 1308 HOH   HOH A . 
F 5 HOH   25  325 18   HOH   HOH A . 
F 5 HOH   26  326 49   HOH   HOH A . 
F 5 HOH   27  327 229  HOH   HOH A . 
F 5 HOH   28  328 469  HOH   HOH A . 
F 5 HOH   29  329 337  HOH   HOH A . 
F 5 HOH   30  330 218  HOH   HOH A . 
F 5 HOH   31  331 57   HOH   HOH A . 
F 5 HOH   32  332 164  HOH   HOH A . 
F 5 HOH   33  333 36   HOH   HOH A . 
F 5 HOH   34  334 393  HOH   HOH A . 
F 5 HOH   35  335 1295 HOH   HOH A . 
F 5 HOH   36  336 140  HOH   HOH A . 
F 5 HOH   37  337 15   HOH   HOH A . 
F 5 HOH   38  338 153  HOH   HOH A . 
F 5 HOH   39  339 241  HOH   HOH A . 
F 5 HOH   40  340 1309 HOH   HOH A . 
F 5 HOH   41  341 630  HOH   HOH A . 
F 5 HOH   42  342 165  HOH   HOH A . 
F 5 HOH   43  343 21   HOH   HOH A . 
F 5 HOH   44  344 155  HOH   HOH A . 
F 5 HOH   45  345 236  HOH   HOH A . 
F 5 HOH   46  346 964  HOH   HOH A . 
F 5 HOH   47  347 42   HOH   HOH A . 
F 5 HOH   48  348 24   HOH   HOH A . 
F 5 HOH   49  349 136  HOH   HOH A . 
F 5 HOH   50  350 396  HOH   HOH A . 
F 5 HOH   51  351 939  HOH   HOH A . 
F 5 HOH   52  352 169  HOH   HOH A . 
F 5 HOH   53  353 354  HOH   HOH A . 
F 5 HOH   54  354 320  HOH   HOH A . 
F 5 HOH   55  355 17   HOH   HOH A . 
F 5 HOH   56  356 92   HOH   HOH A . 
F 5 HOH   57  357 139  HOH   HOH A . 
F 5 HOH   58  358 56   HOH   HOH A . 
F 5 HOH   59  359 66   HOH   HOH A . 
F 5 HOH   60  360 33   HOH   HOH A . 
F 5 HOH   61  361 366  HOH   HOH A . 
F 5 HOH   62  362 132  HOH   HOH A . 
F 5 HOH   63  363 4    HOH   HOH A . 
F 5 HOH   64  364 1    HOH   HOH A . 
F 5 HOH   65  365 5    HOH   HOH A . 
F 5 HOH   66  366 2    HOH   HOH A . 
F 5 HOH   67  367 27   HOH   HOH A . 
F 5 HOH   68  368 81   HOH   HOH A . 
F 5 HOH   69  369 154  HOH   HOH A . 
F 5 HOH   70  370 45   HOH   HOH A . 
F 5 HOH   71  371 19   HOH   HOH A . 
F 5 HOH   72  372 138  HOH   HOH A . 
F 5 HOH   73  373 39   HOH   HOH A . 
F 5 HOH   74  374 46   HOH   HOH A . 
F 5 HOH   75  375 102  HOH   HOH A . 
F 5 HOH   76  376 85   HOH   HOH A . 
F 5 HOH   77  377 159  HOH   HOH A . 
F 5 HOH   78  378 162  HOH   HOH A . 
F 5 HOH   79  379 333  HOH   HOH A . 
F 5 HOH   80  380 1300 HOH   HOH A . 
F 5 HOH   81  381 296  HOH   HOH A . 
F 5 HOH   82  382 461  HOH   HOH A . 
F 5 HOH   83  383 26   HOH   HOH A . 
F 5 HOH   84  384 116  HOH   HOH A . 
F 5 HOH   85  385 12   HOH   HOH A . 
F 5 HOH   86  386 134  HOH   HOH A . 
F 5 HOH   87  387 62   HOH   HOH A . 
F 5 HOH   88  388 199  HOH   HOH A . 
F 5 HOH   89  389 35   HOH   HOH A . 
F 5 HOH   90  390 10   HOH   HOH A . 
F 5 HOH   91  391 186  HOH   HOH A . 
F 5 HOH   92  392 148  HOH   HOH A . 
F 5 HOH   93  393 381  HOH   HOH A . 
F 5 HOH   94  394 74   HOH   HOH A . 
F 5 HOH   95  395 3    HOH   HOH A . 
F 5 HOH   96  396 351  HOH   HOH A . 
F 5 HOH   97  397 58   HOH   HOH A . 
F 5 HOH   98  398 195  HOH   HOH A . 
F 5 HOH   99  399 78   HOH   HOH A . 
F 5 HOH   100 400 83   HOH   HOH A . 
F 5 HOH   101 401 67   HOH   HOH A . 
F 5 HOH   102 402 1315 HOH   HOH A . 
F 5 HOH   103 403 25   HOH   HOH A . 
F 5 HOH   104 404 4    HOH   HOH A . 
F 5 HOH   105 405 125  HOH   HOH A . 
F 5 HOH   106 406 281  HOH   HOH A . 
F 5 HOH   107 407 34   HOH   HOH A . 
F 5 HOH   108 408 1068 HOH   HOH A . 
F 5 HOH   109 409 278  HOH   HOH A . 
F 5 HOH   110 410 68   HOH   HOH A . 
F 5 HOH   111 411 122  HOH   HOH A . 
F 5 HOH   112 412 123  HOH   HOH A . 
F 5 HOH   113 413 7    HOH   HOH A . 
F 5 HOH   114 414 6    HOH   HOH A . 
F 5 HOH   115 415 493  HOH   HOH A . 
F 5 HOH   116 416 53   HOH   HOH A . 
F 5 HOH   117 417 303  HOH   HOH A . 
F 5 HOH   118 418 1286 HOH   HOH A . 
F 5 HOH   119 419 1275 HOH   HOH A . 
F 5 HOH   120 420 8    HOH   HOH A . 
F 5 HOH   121 421 96   HOH   HOH A . 
F 5 HOH   122 422 397  HOH   HOH A . 
F 5 HOH   123 423 156  HOH   HOH A . 
F 5 HOH   124 424 70   HOH   HOH A . 
F 5 HOH   125 425 1290 HOH   HOH A . 
F 5 HOH   126 426 1310 HOH   HOH A . 
F 5 HOH   127 427 121  HOH   HOH A . 
F 5 HOH   128 428 582  HOH   HOH A . 
F 5 HOH   129 429 95   HOH   HOH A . 
F 5 HOH   130 430 51   HOH   HOH A . 
F 5 HOH   131 431 1222 HOH   HOH A . 
F 5 HOH   132 432 212  HOH   HOH A . 
F 5 HOH   133 433 73   HOH   HOH A . 
F 5 HOH   134 434 5    HOH   HOH A . 
F 5 HOH   135 435 16   HOH   HOH A . 
F 5 HOH   136 436 1279 HOH   HOH A . 
F 5 HOH   137 437 952  HOH   HOH A . 
F 5 HOH   138 438 576  HOH   HOH A . 
F 5 HOH   139 439 80   HOH   HOH A . 
F 5 HOH   140 440 71   HOH   HOH A . 
F 5 HOH   141 441 188  HOH   HOH A . 
F 5 HOH   142 442 1189 HOH   HOH A . 
F 5 HOH   143 443 94   HOH   HOH A . 
F 5 HOH   144 444 944  HOH   HOH A . 
F 5 HOH   145 445 40   HOH   HOH A . 
F 5 HOH   146 446 104  HOH   HOH A . 
F 5 HOH   147 447 1238 HOH   HOH A . 
F 5 HOH   148 448 97   HOH   HOH A . 
F 5 HOH   149 449 1094 HOH   HOH A . 
F 5 HOH   150 450 1296 HOH   HOH A . 
F 5 HOH   151 451 79   HOH   HOH A . 
F 5 HOH   152 452 1119 HOH   HOH A . 
F 5 HOH   153 453 3    HOH   HOH A . 
F 5 HOH   154 454 509  HOH   HOH A . 
F 5 HOH   155 455 330  HOH   HOH A . 
F 5 HOH   156 456 1134 HOH   HOH A . 
F 5 HOH   157 457 107  HOH   HOH A . 
F 5 HOH   158 458 163  HOH   HOH A . 
F 5 HOH   159 459 726  HOH   HOH A . 
F 5 HOH   160 460 319  HOH   HOH A . 
F 5 HOH   161 461 756  HOH   HOH A . 
F 5 HOH   162 462 408  HOH   HOH A . 
F 5 HOH   163 463 280  HOH   HOH A . 
F 5 HOH   164 464 361  HOH   HOH A . 
F 5 HOH   165 465 126  HOH   HOH A . 
F 5 HOH   166 466 1307 HOH   HOH A . 
F 5 HOH   167 467 63   HOH   HOH A . 
F 5 HOH   168 468 556  HOH   HOH A . 
F 5 HOH   169 469 801  HOH   HOH A . 
F 5 HOH   170 470 342  HOH   HOH A . 
F 5 HOH   171 471 1276 HOH   HOH A . 
F 5 HOH   172 472 370  HOH   HOH A . 
F 5 HOH   173 473 250  HOH   HOH A . 
F 5 HOH   174 474 135  HOH   HOH A . 
F 5 HOH   175 475 695  HOH   HOH A . 
F 5 HOH   176 476 1306 HOH   HOH A . 
F 5 HOH   177 477 1287 HOH   HOH A . 
F 5 HOH   178 478 1314 HOH   HOH A . 
F 5 HOH   179 479 224  HOH   HOH A . 
F 5 HOH   180 480 674  HOH   HOH A . 
F 5 HOH   181 481 318  HOH   HOH A . 
F 5 HOH   182 482 919  HOH   HOH A . 
F 5 HOH   183 483 267  HOH   HOH A . 
F 5 HOH   184 484 202  HOH   HOH A . 
F 5 HOH   185 485 1299 HOH   HOH A . 
F 5 HOH   186 486 711  HOH   HOH A . 
F 5 HOH   187 487 331  HOH   HOH A . 
F 5 HOH   188 488 309  HOH   HOH A . 
F 5 HOH   189 489 315  HOH   HOH A . 
F 5 HOH   190 490 1284 HOH   HOH A . 
F 5 HOH   191 491 805  HOH   HOH A . 
F 5 HOH   192 492 941  HOH   HOH A . 
F 5 HOH   193 493 263  HOH   HOH A . 
F 5 HOH   194 494 208  HOH   HOH A . 
F 5 HOH   195 495 152  HOH   HOH A . 
F 5 HOH   196 496 521  HOH   HOH A . 
F 5 HOH   197 497 1071 HOH   HOH A . 
F 5 HOH   198 498 6    HOH   HOH A . 
F 5 HOH   199 499 180  HOH   HOH A . 
F 5 HOH   200 500 363  HOH   HOH A . 
F 5 HOH   201 501 371  HOH   HOH A . 
F 5 HOH   202 502 356  HOH   HOH A . 
F 5 HOH   203 503 313  HOH   HOH A . 
F 5 HOH   204 504 326  HOH   HOH A . 
F 5 HOH   205 505 429  HOH   HOH A . 
F 5 HOH   206 506 185  HOH   HOH A . 
F 5 HOH   207 507 772  HOH   HOH A . 
F 5 HOH   208 508 376  HOH   HOH A . 
F 5 HOH   209 509 1074 HOH   HOH A . 
F 5 HOH   210 510 346  HOH   HOH A . 
F 5 HOH   211 511 1292 HOH   HOH A . 
F 5 HOH   212 512 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 549  HOH   HOH B . 
G 5 HOH   3   203 240  HOH   HOH B . 
G 5 HOH   4   204 232  HOH   HOH B . 
G 5 HOH   5   205 332  HOH   HOH B . 
G 5 HOH   6   206 205  HOH   HOH B . 
G 5 HOH   7   207 364  HOH   HOH B . 
G 5 HOH   8   208 358  HOH   HOH B . 
G 5 HOH   9   209 398  HOH   HOH B . 
G 5 HOH   10  210 758  HOH   HOH B . 
G 5 HOH   11  211 50   HOH   HOH B . 
G 5 HOH   12  212 172  HOH   HOH B . 
G 5 HOH   13  213 654  HOH   HOH B . 
G 5 HOH   14  214 120  HOH   HOH B . 
G 5 HOH   15  215 531  HOH   HOH B . 
G 5 HOH   16  216 353  HOH   HOH B . 
G 5 HOH   17  217 75   HOH   HOH B . 
G 5 HOH   18  218 743  HOH   HOH B . 
G 5 HOH   19  219 1249 HOH   HOH B . 
G 5 HOH   20  220 264  HOH   HOH B . 
G 5 HOH   21  221 82   HOH   HOH B . 
G 5 HOH   22  222 1140 HOH   HOH B . 
G 5 HOH   23  223 54   HOH   HOH B . 
G 5 HOH   24  224 287  HOH   HOH B . 
G 5 HOH   25  225 900  HOH   HOH B . 
G 5 HOH   26  226 444  HOH   HOH B . 
G 5 HOH   27  227 1312 HOH   HOH B . 
G 5 HOH   28  228 110  HOH   HOH B . 
G 5 HOH   29  229 41   HOH   HOH B . 
G 5 HOH   30  230 133  HOH   HOH B . 
G 5 HOH   31  231 127  HOH   HOH B . 
G 5 HOH   32  232 1    HOH   HOH B . 
G 5 HOH   33  233 131  HOH   HOH B . 
G 5 HOH   34  234 231  HOH   HOH B . 
G 5 HOH   35  235 1278 HOH   HOH B . 
G 5 HOH   36  236 60   HOH   HOH B . 
G 5 HOH   37  237 30   HOH   HOH B . 
G 5 HOH   38  238 276  HOH   HOH B . 
G 5 HOH   39  239 723  HOH   HOH B . 
G 5 HOH   40  240 128  HOH   HOH B . 
G 5 HOH   41  241 150  HOH   HOH B . 
G 5 HOH   42  242 14   HOH   HOH B . 
G 5 HOH   43  243 52   HOH   HOH B . 
G 5 HOH   44  244 69   HOH   HOH B . 
G 5 HOH   45  245 343  HOH   HOH B . 
G 5 HOH   46  246 103  HOH   HOH B . 
G 5 HOH   47  247 181  HOH   HOH B . 
G 5 HOH   48  248 9    HOH   HOH B . 
G 5 HOH   49  249 300  HOH   HOH B . 
G 5 HOH   50  250 129  HOH   HOH B . 
G 5 HOH   51  251 47   HOH   HOH B . 
G 5 HOH   52  252 347  HOH   HOH B . 
G 5 HOH   53  253 325  HOH   HOH B . 
G 5 HOH   54  254 452  HOH   HOH B . 
G 5 HOH   55  255 271  HOH   HOH B . 
G 5 HOH   56  256 166  HOH   HOH B . 
G 5 HOH   57  257 272  HOH   HOH B . 
G 5 HOH   58  258 31   HOH   HOH B . 
G 5 HOH   59  259 59   HOH   HOH B . 
G 5 HOH   60  260 221  HOH   HOH B . 
G 5 HOH   61  261 77   HOH   HOH B . 
G 5 HOH   62  262 391  HOH   HOH B . 
G 5 HOH   63  263 114  HOH   HOH B . 
G 5 HOH   64  264 143  HOH   HOH B . 
G 5 HOH   65  265 144  HOH   HOH B . 
G 5 HOH   66  266 89   HOH   HOH B . 
G 5 HOH   67  267 235  HOH   HOH B . 
G 5 HOH   68  268 11   HOH   HOH B . 
G 5 HOH   69  269 72   HOH   HOH B . 
G 5 HOH   70  270 117  HOH   HOH B . 
G 5 HOH   71  271 20   HOH   HOH B . 
G 5 HOH   72  272 84   HOH   HOH B . 
G 5 HOH   73  273 302  HOH   HOH B . 
G 5 HOH   74  274 61   HOH   HOH B . 
G 5 HOH   75  275 216  HOH   HOH B . 
G 5 HOH   76  276 243  HOH   HOH B . 
G 5 HOH   77  277 242  HOH   HOH B . 
G 5 HOH   78  278 147  HOH   HOH B . 
G 5 HOH   79  279 1106 HOH   HOH B . 
G 5 HOH   80  280 22   HOH   HOH B . 
G 5 HOH   81  281 13   HOH   HOH B . 
G 5 HOH   82  282 416  HOH   HOH B . 
G 5 HOH   83  283 43   HOH   HOH B . 
G 5 HOH   84  284 99   HOH   HOH B . 
G 5 HOH   85  285 1305 HOH   HOH B . 
G 5 HOH   86  286 175  HOH   HOH B . 
G 5 HOH   87  287 1277 HOH   HOH B . 
G 5 HOH   88  288 252  HOH   HOH B . 
G 5 HOH   89  289 299  HOH   HOH B . 
G 5 HOH   90  290 316  HOH   HOH B . 
G 5 HOH   91  291 88   HOH   HOH B . 
G 5 HOH   92  292 282  HOH   HOH B . 
G 5 HOH   93  293 106  HOH   HOH B . 
G 5 HOH   94  294 215  HOH   HOH B . 
G 5 HOH   95  295 197  HOH   HOH B . 
G 5 HOH   96  296 220  HOH   HOH B . 
G 5 HOH   97  297 160  HOH   HOH B . 
G 5 HOH   98  298 141  HOH   HOH B . 
G 5 HOH   99  299 137  HOH   HOH B . 
G 5 HOH   100 300 297  HOH   HOH B . 
G 5 HOH   101 301 311  HOH   HOH B . 
G 5 HOH   102 302 38   HOH   HOH B . 
G 5 HOH   103 303 704  HOH   HOH B . 
G 5 HOH   104 304 1285 HOH   HOH B . 
G 5 HOH   105 305 112  HOH   HOH B . 
G 5 HOH   106 306 37   HOH   HOH B . 
G 5 HOH   107 307 1066 HOH   HOH B . 
G 5 HOH   108 308 170  HOH   HOH B . 
G 5 HOH   109 309 101  HOH   HOH B . 
G 5 HOH   110 310 142  HOH   HOH B . 
G 5 HOH   111 311 182  HOH   HOH B . 
G 5 HOH   112 312 23   HOH   HOH B . 
G 5 HOH   113 313 717  HOH   HOH B . 
G 5 HOH   114 314 387  HOH   HOH B . 
G 5 HOH   115 315 207  HOH   HOH B . 
G 5 HOH   116 316 48   HOH   HOH B . 
G 5 HOH   117 317 100  HOH   HOH B . 
G 5 HOH   118 318 177  HOH   HOH B . 
G 5 HOH   119 319 91   HOH   HOH B . 
G 5 HOH   120 320 118  HOH   HOH B . 
G 5 HOH   121 321 1291 HOH   HOH B . 
G 5 HOH   122 322 28   HOH   HOH B . 
G 5 HOH   123 323 635  HOH   HOH B . 
G 5 HOH   124 324 44   HOH   HOH B . 
G 5 HOH   125 325 1274 HOH   HOH B . 
G 5 HOH   126 326 32   HOH   HOH B . 
G 5 HOH   127 327 29   HOH   HOH B . 
G 5 HOH   128 328 98   HOH   HOH B . 
G 5 HOH   129 329 55   HOH   HOH B . 
G 5 HOH   130 330 960  HOH   HOH B . 
G 5 HOH   131 331 161  HOH   HOH B . 
G 5 HOH   132 332 65   HOH   HOH B . 
G 5 HOH   133 333 1294 HOH   HOH B . 
G 5 HOH   134 334 234  HOH   HOH B . 
G 5 HOH   135 335 334  HOH   HOH B . 
G 5 HOH   136 336 341  HOH   HOH B . 
G 5 HOH   137 337 362  HOH   HOH B . 
G 5 HOH   138 338 619  HOH   HOH B . 
G 5 HOH   139 339 1126 HOH   HOH B . 
G 5 HOH   140 340 1293 HOH   HOH B . 
G 5 HOH   141 341 178  HOH   HOH B . 
G 5 HOH   142 342 445  HOH   HOH B . 
G 5 HOH   143 343 339  HOH   HOH B . 
G 5 HOH   144 344 87   HOH   HOH B . 
G 5 HOH   145 345 463  HOH   HOH B . 
G 5 HOH   146 346 90   HOH   HOH B . 
G 5 HOH   147 347 1304 HOH   HOH B . 
G 5 HOH   148 348 191  HOH   HOH B . 
G 5 HOH   149 349 304  HOH   HOH B . 
G 5 HOH   150 350 1046 HOH   HOH B . 
G 5 HOH   151 351 335  HOH   HOH B . 
G 5 HOH   152 352 623  HOH   HOH B . 
G 5 HOH   153 353 1077 HOH   HOH B . 
G 5 HOH   154 354 1280 HOH   HOH B . 
G 5 HOH   155 355 203  HOH   HOH B . 
G 5 HOH   156 356 541  HOH   HOH B . 
G 5 HOH   157 357 290  HOH   HOH B . 
G 5 HOH   158 358 718  HOH   HOH B . 
G 5 HOH   159 359 389  HOH   HOH B . 
G 5 HOH   160 360 283  HOH   HOH B . 
G 5 HOH   161 361 1072 HOH   HOH B . 
G 5 HOH   162 362 479  HOH   HOH B . 
G 5 HOH   163 363 615  HOH   HOH B . 
G 5 HOH   164 364 291  HOH   HOH B . 
G 5 HOH   165 365 340  HOH   HOH B . 
G 5 HOH   166 366 898  HOH   HOH B . 
G 5 HOH   167 367 1316 HOH   HOH B . 
G 5 HOH   168 368 667  HOH   HOH B . 
G 5 HOH   169 369 1303 HOH   HOH B . 
G 5 HOH   170 370 310  HOH   HOH B . 
G 5 HOH   171 371 373  HOH   HOH B . 
G 5 HOH   172 372 190  HOH   HOH B . 
G 5 HOH   173 373 431  HOH   HOH B . 
G 5 HOH   174 374 1173 HOH   HOH B . 
G 5 HOH   175 375 183  HOH   HOH B . 
G 5 HOH   176 376 149  HOH   HOH B . 
G 5 HOH   177 377 1000 HOH   HOH B . 
G 5 HOH   178 378 418  HOH   HOH B . 
G 5 HOH   179 379 1163 HOH   HOH B . 
G 5 HOH   180 380 1311 HOH   HOH B . 
G 5 HOH   181 381 491  HOH   HOH B . 
G 5 HOH   182 382 981  HOH   HOH B . 
G 5 HOH   183 383 176  HOH   HOH B . 
G 5 HOH   184 384 424  HOH   HOH B . 
G 5 HOH   185 385 470  HOH   HOH B . 
G 5 HOH   186 386 350  HOH   HOH B . 
G 5 HOH   187 387 248  HOH   HOH B . 
G 5 HOH   188 388 265  HOH   HOH B . 
G 5 HOH   189 389 1298 HOH   HOH B . 
G 5 HOH   190 390 184  HOH   HOH B . 
G 5 HOH   191 391 360  HOH   HOH B . 
G 5 HOH   192 392 410  HOH   HOH B . 
G 5 HOH   193 393 355  HOH   HOH B . 
G 5 HOH   194 394 314  HOH   HOH B . 
G 5 HOH   195 395 274  HOH   HOH B . 
G 5 HOH   196 396 157  HOH   HOH B . 
G 5 HOH   197 397 566  HOH   HOH B . 
G 5 HOH   198 398 792  HOH   HOH B . 
G 5 HOH   199 399 321  HOH   HOH B . 
G 5 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HFV 
_cell.length_a           88.762 
_cell.length_b           88.762 
_cell.length_c           39.343 
_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                         7HFV 
_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          7HFV 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.13 
_exptl_crystal.density_percent_sol   42.39 
_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   2023-12-22 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HFV 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.380 
_reflns.d_resolution_high            0.990 
_reflns.number_obs                   169936 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.700 
_reflns.pdbx_Rmerge_I_obs            0.051 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        11.400 
_reflns.B_iso_Wilson_estimate        13.900 
_reflns.pdbx_redundancy              6.300 
_reflns.pdbx_Rrim_I_all              0.055 
_reflns.pdbx_Rpim_I_all              0.021 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1074899 
_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  ? 34112 7902 ? 2.645 ? ? ? 4.300 ? 0.400  ? ? ? ? ? ? 94.200 3.009 1.399 0.393 
1 2 5.420 44.380 ? 7619  1127 ? 0.036 ? ? ? 6.800 ? 44.800 ? ? ? ? ? ? 99.800 0.040 0.015 0.997 
# 
_refine.entry_id                                 7HFV 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9900 
_refine.ls_d_res_low                             44.3800 
_refine.pdbx_ls_sigma_F                          1.330 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.2700 
_refine.ls_number_reflns_obs                     169155 
_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                          0.1722 
_refine.ls_R_factor_R_work                       0.1713 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1888 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  8160 
_refine.ls_number_reflns_R_work                  160995 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               23.1059 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1400 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                61.100 
_refine.B_iso_min                                11.140 
_refine.pdbx_overall_phase_error                 29.7200 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       0.9900 
_refine_hist.d_res_low                        44.3800 
_refine_hist.pdbx_number_atoms_ligand         59 
_refine_hist.number_atoms_solvent             412 
_refine_hist.number_atoms_total               3013 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           19.26 
_refine_hist.pdbx_B_iso_mean_solvent          33.25 
_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 83.0000  4463 . 0.5884 0.5743 . 227 0.0000 4690 . 'X-RAY DIFFRACTION' 
1.0000 1.0100  30 98.0000  5309 . 0.5197 0.4858 . 273 0.0000 5582 . 'X-RAY DIFFRACTION' 
1.0100 1.0300  30 100.0000 5359 . 0.4622 0.4337 . 236 0.0000 5595 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5390 . 0.4232 0.4149 . 280 0.0000 5670 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5313 . 0.3860 0.3814 . 282 0.0000 5595 . 'X-RAY DIFFRACTION' 
1.0500 1.0700  30 100.0000 5355 . 0.3600 0.3720 . 326 0.0000 5681 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 5394 . 0.3432 0.3455 . 273 0.0000 5667 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 5365 . 0.3179 0.3540 . 240 0.0000 5605 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5364 . 0.2896 0.2964 . 284 0.0000 5648 . 'X-RAY DIFFRACTION' 
1.1200 1.1300  30 100.0000 5391 . 0.2694 0.3031 . 252 0.0000 5643 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 5414 . 0.2552 0.2692 . 263 0.0000 5677 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 5359 . 0.2288 0.2594 . 272 0.0000 5631 . 'X-RAY DIFFRACTION' 
1.1700 1.2000  30 100.0000 5416 . 0.2131 0.2546 . 269 0.0000 5685 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 100.0000 5347 . 0.1919 0.2331 . 295 0.0000 5642 . 'X-RAY DIFFRACTION' 
1.2200 1.2500  30 100.0000 5382 . 0.1877 0.2191 . 255 0.0000 5637 . 'X-RAY DIFFRACTION' 
1.2500 1.2800  30 100.0000 5387 . 0.1778 0.2150 . 263 0.0000 5650 . 'X-RAY DIFFRACTION' 
1.2800 1.3100  30 100.0000 5362 . 0.1644 0.1940 . 277 0.0000 5639 . 'X-RAY DIFFRACTION' 
1.3100 1.3400  30 100.0000 5385 . 0.1676 0.1994 . 278 0.0000 5663 . 'X-RAY DIFFRACTION' 
1.3400 1.3800  30 100.0000 5373 . 0.1630 0.1874 . 283 0.0000 5656 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 5433 . 0.1598 0.2010 . 255 0.0000 5688 . 'X-RAY DIFFRACTION' 
1.4300 1.4800  30 100.0000 5399 . 0.1516 0.1642 . 273 0.0000 5672 . 'X-RAY DIFFRACTION' 
1.4800 1.5400  30 100.0000 5377 . 0.1417 0.1528 . 286 0.0000 5663 . 'X-RAY DIFFRACTION' 
1.5400 1.6100  30 100.0000 5397 . 0.1374 0.1619 . 273 0.0000 5670 . 'X-RAY DIFFRACTION' 
1.6100 1.6900  30 100.0000 5426 . 0.1413 0.1685 . 266 0.0000 5692 . 'X-RAY DIFFRACTION' 
1.6900 1.8000  30 100.0000 5444 . 0.1526 0.1664 . 256 0.0000 5700 . 'X-RAY DIFFRACTION' 
1.8000 1.9400  30 100.0000 5411 . 0.1509 0.1574 . 302 0.0000 5713 . 'X-RAY DIFFRACTION' 
1.9400 2.1300  30 100.0000 5420 . 0.1518 0.1581 . 272 0.0000 5692 . 'X-RAY DIFFRACTION' 
2.1300 2.4400  30 100.0000 5446 . 0.1483 0.1612 . 300 0.0000 5746 . 'X-RAY DIFFRACTION' 
2.4400 3.0800  30 100.0000 5503 . 0.1601 0.1852 . 280 0.0000 5783 . 'X-RAY DIFFRACTION' 
3.0800 44.3800 30 100.0000 5611 . 0.1555 0.1735 . 269 0.0000 5880 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HFV 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0005158' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HFV 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
# 
_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 7HFV A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HFV 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 7HFV SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HFV MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HFV SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HFV MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F 
2 1 B,G       
# 
_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 ALA A 154 ? O ALA A 154 N ALA A 124 ? N ALA A 124 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HFV 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 HD1 A HIS 91  ? ? O A HOH 308 ? ? 1.58 
2 1 HZ2 A LYS 29  ? B O A HOH 305 ? ? 1.59 
3 1 O   B HOH 215 ? ? O B HOH 295 ? ? 2.15 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 56.85 -133.60 
2 1 SER A 128 ? B 74.53 -6.09   
3 1 HIS B 86  ? ? 57.29 -127.08 
# 
_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 511 ? 5.84 . 
2 1 O ? A HOH 512 ? 7.38 . 
3 1 O ? B HOH 400 ? 6.60 . 
# 
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 
A1BBY N2   N  Y N 1   
A1BBY C3   C  N R 2   
A1BBY C6   C  Y N 3   
A1BBY C9   C  Y N 4   
A1BBY C1   C  N N 5   
A1BBY C10  C  Y N 6   
A1BBY C2   C  N S 7   
A1BBY C4   C  N N 8   
A1BBY C5   C  Y N 9   
A1BBY C7   C  Y N 10  
A1BBY C8   C  Y N 11  
A1BBY N1   N  N N 12  
A1BBY N3   N  Y N 13  
A1BBY N4   N  Y N 14  
A1BBY O1   O  N N 15  
A1BBY H2   H  N N 16  
A1BBY H11  H  N N 17  
A1BBY H12  H  N N 18  
A1BBY H3   H  N N 19  
A1BBY H4   H  N N 20  
A1BBY H5   H  N N 21  
A1BBY H13  H  N N 22  
A1BBY H1   H  N N 23  
A1BBY H8   H  N N 24  
A1BBY H7   H  N N 25  
A1BBY H9   H  N N 26  
A1BBY H10  H  N N 27  
A1BBY H14  H  N N 28  
A1BBY H6   H  N N 29  
A1BBZ O1   O  N N 30  
A1BBZ C1   C  N N 31  
A1BBZ C2   C  N R 32  
A1BBZ C3   C  N R 33  
A1BBZ C4   C  N N 34  
A1BBZ C5   C  Y N 35  
A1BBZ C6   C  Y N 36  
A1BBZ C7   C  Y N 37  
A1BBZ C8   C  Y N 38  
A1BBZ C10  C  Y N 39  
A1BBZ C9   C  Y N 40  
A1BBZ N1   N  N N 41  
A1BBZ N2   N  Y N 42  
A1BBZ N3   N  Y N 43  
A1BBZ N4   N  Y N 44  
A1BBZ H6   H  N N 45  
A1BBZ H5   H  N N 46  
A1BBZ H3   H  N N 47  
A1BBZ H4   H  N N 48  
A1BBZ H1   H  N N 49  
A1BBZ H2   H  N N 50  
A1BBZ H8   H  N N 51  
A1BBZ H7   H  N N 52  
A1BBZ H9   H  N N 53  
A1BBZ H11  H  N N 54  
A1BBZ H13  H  N N 55  
A1BBZ H12  H  N N 56  
A1BBZ H10  H  N N 57  
A1BBZ H14  H  N N 58  
ALA   N    N  N N 59  
ALA   CA   C  N S 60  
ALA   C    C  N N 61  
ALA   O    O  N N 62  
ALA   CB   C  N N 63  
ALA   OXT  O  N N 64  
ALA   H    H  N N 65  
ALA   H2   H  N N 66  
ALA   HA   H  N N 67  
ALA   HB1  H  N N 68  
ALA   HB2  H  N N 69  
ALA   HB3  H  N N 70  
ALA   HXT  H  N N 71  
ARG   N    N  N N 72  
ARG   CA   C  N S 73  
ARG   C    C  N N 74  
ARG   O    O  N N 75  
ARG   CB   C  N N 76  
ARG   CG   C  N N 77  
ARG   CD   C  N N 78  
ARG   NE   N  N N 79  
ARG   CZ   C  N N 80  
ARG   NH1  N  N N 81  
ARG   NH2  N  N N 82  
ARG   OXT  O  N N 83  
ARG   H    H  N N 84  
ARG   H2   H  N N 85  
ARG   HA   H  N N 86  
ARG   HB2  H  N N 87  
ARG   HB3  H  N N 88  
ARG   HG2  H  N N 89  
ARG   HG3  H  N N 90  
ARG   HD2  H  N N 91  
ARG   HD3  H  N N 92  
ARG   HE   H  N N 93  
ARG   HH11 H  N N 94  
ARG   HH12 H  N N 95  
ARG   HH21 H  N N 96  
ARG   HH22 H  N N 97  
ARG   HXT  H  N N 98  
ASN   N    N  N N 99  
ASN   CA   C  N S 100 
ASN   C    C  N N 101 
ASN   O    O  N N 102 
ASN   CB   C  N N 103 
ASN   CG   C  N N 104 
ASN   OD1  O  N N 105 
ASN   ND2  N  N N 106 
ASN   OXT  O  N N 107 
ASN   H    H  N N 108 
ASN   H2   H  N N 109 
ASN   HA   H  N N 110 
ASN   HB2  H  N N 111 
ASN   HB3  H  N N 112 
ASN   HD21 H  N N 113 
ASN   HD22 H  N N 114 
ASN   HXT  H  N N 115 
ASP   N    N  N N 116 
ASP   CA   C  N S 117 
ASP   C    C  N N 118 
ASP   O    O  N N 119 
ASP   CB   C  N N 120 
ASP   CG   C  N N 121 
ASP   OD1  O  N N 122 
ASP   OD2  O  N N 123 
ASP   OXT  O  N N 124 
ASP   H    H  N N 125 
ASP   H2   H  N N 126 
ASP   HA   H  N N 127 
ASP   HB2  H  N N 128 
ASP   HB3  H  N N 129 
ASP   HD2  H  N N 130 
ASP   HXT  H  N N 131 
CL    CL   CL N N 132 
CYS   N    N  N N 133 
CYS   CA   C  N R 134 
CYS   C    C  N N 135 
CYS   O    O  N N 136 
CYS   CB   C  N N 137 
CYS   SG   S  N N 138 
CYS   OXT  O  N N 139 
CYS   H    H  N N 140 
CYS   H2   H  N N 141 
CYS   HA   H  N N 142 
CYS   HB2  H  N N 143 
CYS   HB3  H  N N 144 
CYS   HG   H  N N 145 
CYS   HXT  H  N N 146 
GLN   N    N  N N 147 
GLN   CA   C  N S 148 
GLN   C    C  N N 149 
GLN   O    O  N N 150 
GLN   CB   C  N N 151 
GLN   CG   C  N N 152 
GLN   CD   C  N N 153 
GLN   OE1  O  N N 154 
GLN   NE2  N  N N 155 
GLN   OXT  O  N N 156 
GLN   H    H  N N 157 
GLN   H2   H  N N 158 
GLN   HA   H  N N 159 
GLN   HB2  H  N N 160 
GLN   HB3  H  N N 161 
GLN   HG2  H  N N 162 
GLN   HG3  H  N N 163 
GLN   HE21 H  N N 164 
GLN   HE22 H  N N 165 
GLN   HXT  H  N N 166 
GLU   N    N  N N 167 
GLU   CA   C  N S 168 
GLU   C    C  N N 169 
GLU   O    O  N N 170 
GLU   CB   C  N N 171 
GLU   CG   C  N N 172 
GLU   CD   C  N N 173 
GLU   OE1  O  N N 174 
GLU   OE2  O  N N 175 
GLU   OXT  O  N N 176 
GLU   H    H  N N 177 
GLU   H2   H  N N 178 
GLU   HA   H  N N 179 
GLU   HB2  H  N N 180 
GLU   HB3  H  N N 181 
GLU   HG2  H  N N 182 
GLU   HG3  H  N N 183 
GLU   HE2  H  N N 184 
GLU   HXT  H  N N 185 
GLY   N    N  N N 186 
GLY   CA   C  N N 187 
GLY   C    C  N N 188 
GLY   O    O  N N 189 
GLY   OXT  O  N N 190 
GLY   H    H  N N 191 
GLY   H2   H  N N 192 
GLY   HA2  H  N N 193 
GLY   HA3  H  N N 194 
GLY   HXT  H  N N 195 
HIS   N    N  N N 196 
HIS   CA   C  N S 197 
HIS   C    C  N N 198 
HIS   O    O  N N 199 
HIS   CB   C  N N 200 
HIS   CG   C  Y N 201 
HIS   ND1  N  Y N 202 
HIS   CD2  C  Y N 203 
HIS   CE1  C  Y N 204 
HIS   NE2  N  Y N 205 
HIS   OXT  O  N N 206 
HIS   H    H  N N 207 
HIS   H2   H  N N 208 
HIS   HA   H  N N 209 
HIS   HB2  H  N N 210 
HIS   HB3  H  N N 211 
HIS   HD1  H  N N 212 
HIS   HD2  H  N N 213 
HIS   HE1  H  N N 214 
HIS   HE2  H  N N 215 
HIS   HXT  H  N N 216 
HOH   O    O  N N 217 
HOH   H1   H  N N 218 
HOH   H2   H  N N 219 
ILE   N    N  N N 220 
ILE   CA   C  N S 221 
ILE   C    C  N N 222 
ILE   O    O  N N 223 
ILE   CB   C  N S 224 
ILE   CG1  C  N N 225 
ILE   CG2  C  N N 226 
ILE   CD1  C  N N 227 
ILE   OXT  O  N N 228 
ILE   H    H  N N 229 
ILE   H2   H  N N 230 
ILE   HA   H  N N 231 
ILE   HB   H  N N 232 
ILE   HG12 H  N N 233 
ILE   HG13 H  N N 234 
ILE   HG21 H  N N 235 
ILE   HG22 H  N N 236 
ILE   HG23 H  N N 237 
ILE   HD11 H  N N 238 
ILE   HD12 H  N N 239 
ILE   HD13 H  N N 240 
ILE   HXT  H  N N 241 
LEU   N    N  N N 242 
LEU   CA   C  N S 243 
LEU   C    C  N N 244 
LEU   O    O  N N 245 
LEU   CB   C  N N 246 
LEU   CG   C  N N 247 
LEU   CD1  C  N N 248 
LEU   CD2  C  N N 249 
LEU   OXT  O  N N 250 
LEU   H    H  N N 251 
LEU   H2   H  N N 252 
LEU   HA   H  N N 253 
LEU   HB2  H  N N 254 
LEU   HB3  H  N N 255 
LEU   HG   H  N N 256 
LEU   HD11 H  N N 257 
LEU   HD12 H  N N 258 
LEU   HD13 H  N N 259 
LEU   HD21 H  N N 260 
LEU   HD22 H  N N 261 
LEU   HD23 H  N N 262 
LEU   HXT  H  N N 263 
LYS   N    N  N N 264 
LYS   CA   C  N S 265 
LYS   C    C  N N 266 
LYS   O    O  N N 267 
LYS   CB   C  N N 268 
LYS   CG   C  N N 269 
LYS   CD   C  N N 270 
LYS   CE   C  N N 271 
LYS   NZ   N  N N 272 
LYS   OXT  O  N N 273 
LYS   H    H  N N 274 
LYS   H2   H  N N 275 
LYS   HA   H  N N 276 
LYS   HB2  H  N N 277 
LYS   HB3  H  N N 278 
LYS   HG2  H  N N 279 
LYS   HG3  H  N N 280 
LYS   HD2  H  N N 281 
LYS   HD3  H  N N 282 
LYS   HE2  H  N N 283 
LYS   HE3  H  N N 284 
LYS   HZ1  H  N N 285 
LYS   HZ2  H  N N 286 
LYS   HZ3  H  N N 287 
LYS   HXT  H  N N 288 
MET   N    N  N N 289 
MET   CA   C  N S 290 
MET   C    C  N N 291 
MET   O    O  N N 292 
MET   CB   C  N N 293 
MET   CG   C  N N 294 
MET   SD   S  N N 295 
MET   CE   C  N N 296 
MET   OXT  O  N N 297 
MET   H    H  N N 298 
MET   H2   H  N N 299 
MET   HA   H  N N 300 
MET   HB2  H  N N 301 
MET   HB3  H  N N 302 
MET   HG2  H  N N 303 
MET   HG3  H  N N 304 
MET   HE1  H  N N 305 
MET   HE2  H  N N 306 
MET   HE3  H  N N 307 
MET   HXT  H  N N 308 
PHE   N    N  N N 309 
PHE   CA   C  N S 310 
PHE   C    C  N N 311 
PHE   O    O  N N 312 
PHE   CB   C  N N 313 
PHE   CG   C  Y N 314 
PHE   CD1  C  Y N 315 
PHE   CD2  C  Y N 316 
PHE   CE1  C  Y N 317 
PHE   CE2  C  Y N 318 
PHE   CZ   C  Y N 319 
PHE   OXT  O  N N 320 
PHE   H    H  N N 321 
PHE   H2   H  N N 322 
PHE   HA   H  N N 323 
PHE   HB2  H  N N 324 
PHE   HB3  H  N N 325 
PHE   HD1  H  N N 326 
PHE   HD2  H  N N 327 
PHE   HE1  H  N N 328 
PHE   HE2  H  N N 329 
PHE   HZ   H  N N 330 
PHE   HXT  H  N N 331 
PRO   N    N  N N 332 
PRO   CA   C  N S 333 
PRO   C    C  N N 334 
PRO   O    O  N N 335 
PRO   CB   C  N N 336 
PRO   CG   C  N N 337 
PRO   CD   C  N N 338 
PRO   OXT  O  N N 339 
PRO   H    H  N N 340 
PRO   HA   H  N N 341 
PRO   HB2  H  N N 342 
PRO   HB3  H  N N 343 
PRO   HG2  H  N N 344 
PRO   HG3  H  N N 345 
PRO   HD2  H  N N 346 
PRO   HD3  H  N N 347 
PRO   HXT  H  N N 348 
SER   N    N  N N 349 
SER   CA   C  N S 350 
SER   C    C  N N 351 
SER   O    O  N N 352 
SER   CB   C  N N 353 
SER   OG   O  N N 354 
SER   OXT  O  N N 355 
SER   H    H  N N 356 
SER   H2   H  N N 357 
SER   HA   H  N N 358 
SER   HB2  H  N N 359 
SER   HB3  H  N N 360 
SER   HG   H  N N 361 
SER   HXT  H  N N 362 
THR   N    N  N N 363 
THR   CA   C  N S 364 
THR   C    C  N N 365 
THR   O    O  N N 366 
THR   CB   C  N R 367 
THR   OG1  O  N N 368 
THR   CG2  C  N N 369 
THR   OXT  O  N N 370 
THR   H    H  N N 371 
THR   H2   H  N N 372 
THR   HA   H  N N 373 
THR   HB   H  N N 374 
THR   HG1  H  N N 375 
THR   HG21 H  N N 376 
THR   HG22 H  N N 377 
THR   HG23 H  N N 378 
THR   HXT  H  N N 379 
TYR   N    N  N N 380 
TYR   CA   C  N S 381 
TYR   C    C  N N 382 
TYR   O    O  N N 383 
TYR   CB   C  N N 384 
TYR   CG   C  Y N 385 
TYR   CD1  C  Y N 386 
TYR   CD2  C  Y N 387 
TYR   CE1  C  Y N 388 
TYR   CE2  C  Y N 389 
TYR   CZ   C  Y N 390 
TYR   OH   O  N N 391 
TYR   OXT  O  N N 392 
TYR   H    H  N N 393 
TYR   H2   H  N N 394 
TYR   HA   H  N N 395 
TYR   HB2  H  N N 396 
TYR   HB3  H  N N 397 
TYR   HD1  H  N N 398 
TYR   HD2  H  N N 399 
TYR   HE1  H  N N 400 
TYR   HE2  H  N N 401 
TYR   HH   H  N N 402 
TYR   HXT  H  N N 403 
VAL   N    N  N N 404 
VAL   CA   C  N S 405 
VAL   C    C  N N 406 
VAL   O    O  N N 407 
VAL   CB   C  N N 408 
VAL   CG1  C  N N 409 
VAL   CG2  C  N N 410 
VAL   OXT  O  N N 411 
VAL   H    H  N N 412 
VAL   H2   H  N N 413 
VAL   HA   H  N N 414 
VAL   HB   H  N N 415 
VAL   HG11 H  N N 416 
VAL   HG12 H  N N 417 
VAL   HG13 H  N N 418 
VAL   HG21 H  N N 419 
VAL   HG22 H  N N 420 
VAL   HG23 H  N N 421 
VAL   HXT  H  N N 422 
# 
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 
A1BBY C1  C2   sing N N 1   
A1BBY C2  O1   sing N N 2   
A1BBY C2  C3   sing N N 3   
A1BBY C3  N1   sing N N 4   
A1BBY C3  C4   sing N N 5   
A1BBY N1  C5   sing N N 6   
A1BBY C5  C8   doub Y N 7   
A1BBY C5  N2   sing Y N 8   
A1BBY C9  C8   sing Y N 9   
A1BBY C9  C10  doub Y N 10  
A1BBY C8  C7   sing Y N 11  
A1BBY N2  C6   doub Y N 12  
A1BBY C10 N4   sing Y N 13  
A1BBY C7  N4   sing Y N 14  
A1BBY C7  N3   doub Y N 15  
A1BBY C6  N3   sing Y N 16  
A1BBY C3  H2   sing N N 17  
A1BBY C6  H11  sing N N 18  
A1BBY C9  H12  sing N N 19  
A1BBY C1  H3   sing N N 20  
A1BBY C1  H4   sing N N 21  
A1BBY C1  H5   sing N N 22  
A1BBY C10 H13  sing N N 23  
A1BBY C2  H1   sing N N 24  
A1BBY C4  H8   sing N N 25  
A1BBY C4  H7   sing N N 26  
A1BBY C4  H9   sing N N 27  
A1BBY N1  H10  sing N N 28  
A1BBY N4  H14  sing N N 29  
A1BBY O1  H6   sing N N 30  
A1BBZ O1  C2   sing N N 31  
A1BBZ C1  C2   sing N N 32  
A1BBZ C2  C3   sing N N 33  
A1BBZ C3  N1   sing N N 34  
A1BBZ C3  C4   sing N N 35  
A1BBZ N1  C5   sing N N 36  
A1BBZ C9  C8   sing Y N 37  
A1BBZ C9  C10  doub Y N 38  
A1BBZ C5  C8   doub Y N 39  
A1BBZ C5  N2   sing Y N 40  
A1BBZ C8  C7   sing Y N 41  
A1BBZ N2  C6   doub Y N 42  
A1BBZ C10 N4   sing Y N 43  
A1BBZ C7  N4   sing Y N 44  
A1BBZ C7  N3   doub Y N 45  
A1BBZ C6  N3   sing Y N 46  
A1BBZ O1  H6   sing N N 47  
A1BBZ C1  H5   sing N N 48  
A1BBZ C1  H3   sing N N 49  
A1BBZ C1  H4   sing N N 50  
A1BBZ C2  H1   sing N N 51  
A1BBZ C3  H2   sing N N 52  
A1BBZ C4  H8   sing N N 53  
A1BBZ C4  H7   sing N N 54  
A1BBZ C4  H9   sing N N 55  
A1BBZ C6  H11  sing N N 56  
A1BBZ C10 H13  sing N N 57  
A1BBZ C9  H12  sing N N 58  
A1BBZ N1  H10  sing N N 59  
A1BBZ N4  H14  sing N N 60  
ALA   N   CA   sing N N 61  
ALA   N   H    sing N N 62  
ALA   N   H2   sing N N 63  
ALA   CA  C    sing N N 64  
ALA   CA  CB   sing N N 65  
ALA   CA  HA   sing N N 66  
ALA   C   O    doub N N 67  
ALA   C   OXT  sing N N 68  
ALA   CB  HB1  sing N N 69  
ALA   CB  HB2  sing N N 70  
ALA   CB  HB3  sing N N 71  
ALA   OXT HXT  sing N N 72  
ARG   N   CA   sing N N 73  
ARG   N   H    sing N N 74  
ARG   N   H2   sing N N 75  
ARG   CA  C    sing N N 76  
ARG   CA  CB   sing N N 77  
ARG   CA  HA   sing N N 78  
ARG   C   O    doub N N 79  
ARG   C   OXT  sing N N 80  
ARG   CB  CG   sing N N 81  
ARG   CB  HB2  sing N N 82  
ARG   CB  HB3  sing N N 83  
ARG   CG  CD   sing N N 84  
ARG   CG  HG2  sing N N 85  
ARG   CG  HG3  sing N N 86  
ARG   CD  NE   sing N N 87  
ARG   CD  HD2  sing N N 88  
ARG   CD  HD3  sing N N 89  
ARG   NE  CZ   sing N N 90  
ARG   NE  HE   sing N N 91  
ARG   CZ  NH1  sing N N 92  
ARG   CZ  NH2  doub N N 93  
ARG   NH1 HH11 sing N N 94  
ARG   NH1 HH12 sing N N 95  
ARG   NH2 HH21 sing N N 96  
ARG   NH2 HH22 sing N N 97  
ARG   OXT HXT  sing N N 98  
ASN   N   CA   sing N N 99  
ASN   N   H    sing N N 100 
ASN   N   H2   sing N N 101 
ASN   CA  C    sing N N 102 
ASN   CA  CB   sing N N 103 
ASN   CA  HA   sing N N 104 
ASN   C   O    doub N N 105 
ASN   C   OXT  sing N N 106 
ASN   CB  CG   sing N N 107 
ASN   CB  HB2  sing N N 108 
ASN   CB  HB3  sing N N 109 
ASN   CG  OD1  doub N N 110 
ASN   CG  ND2  sing N N 111 
ASN   ND2 HD21 sing N N 112 
ASN   ND2 HD22 sing N N 113 
ASN   OXT HXT  sing N N 114 
ASP   N   CA   sing N N 115 
ASP   N   H    sing N N 116 
ASP   N   H2   sing N N 117 
ASP   CA  C    sing N N 118 
ASP   CA  CB   sing N N 119 
ASP   CA  HA   sing N N 120 
ASP   C   O    doub N N 121 
ASP   C   OXT  sing N N 122 
ASP   CB  CG   sing N N 123 
ASP   CB  HB2  sing N N 124 
ASP   CB  HB3  sing N N 125 
ASP   CG  OD1  doub N N 126 
ASP   CG  OD2  sing N N 127 
ASP   OD2 HD2  sing N N 128 
ASP   OXT HXT  sing N N 129 
CYS   N   CA   sing N N 130 
CYS   N   H    sing N N 131 
CYS   N   H2   sing N N 132 
CYS   CA  C    sing N N 133 
CYS   CA  CB   sing N N 134 
CYS   CA  HA   sing N N 135 
CYS   C   O    doub N N 136 
CYS   C   OXT  sing N N 137 
CYS   CB  SG   sing N N 138 
CYS   CB  HB2  sing N N 139 
CYS   CB  HB3  sing N N 140 
CYS   SG  HG   sing N N 141 
CYS   OXT HXT  sing N N 142 
GLN   N   CA   sing N N 143 
GLN   N   H    sing N N 144 
GLN   N   H2   sing N N 145 
GLN   CA  C    sing N N 146 
GLN   CA  CB   sing N N 147 
GLN   CA  HA   sing N N 148 
GLN   C   O    doub N N 149 
GLN   C   OXT  sing N N 150 
GLN   CB  CG   sing N N 151 
GLN   CB  HB2  sing N N 152 
GLN   CB  HB3  sing N N 153 
GLN   CG  CD   sing N N 154 
GLN   CG  HG2  sing N N 155 
GLN   CG  HG3  sing N N 156 
GLN   CD  OE1  doub N N 157 
GLN   CD  NE2  sing N N 158 
GLN   NE2 HE21 sing N N 159 
GLN   NE2 HE22 sing N N 160 
GLN   OXT HXT  sing N N 161 
GLU   N   CA   sing N N 162 
GLU   N   H    sing N N 163 
GLU   N   H2   sing N N 164 
GLU   CA  C    sing N N 165 
GLU   CA  CB   sing N N 166 
GLU   CA  HA   sing N N 167 
GLU   C   O    doub N N 168 
GLU   C   OXT  sing N N 169 
GLU   CB  CG   sing N N 170 
GLU   CB  HB2  sing N N 171 
GLU   CB  HB3  sing N N 172 
GLU   CG  CD   sing N N 173 
GLU   CG  HG2  sing N N 174 
GLU   CG  HG3  sing N N 175 
GLU   CD  OE1  doub N N 176 
GLU   CD  OE2  sing N N 177 
GLU   OE2 HE2  sing N N 178 
GLU   OXT HXT  sing N N 179 
GLY   N   CA   sing N N 180 
GLY   N   H    sing N N 181 
GLY   N   H2   sing N N 182 
GLY   CA  C    sing N N 183 
GLY   CA  HA2  sing N N 184 
GLY   CA  HA3  sing N N 185 
GLY   C   O    doub N N 186 
GLY   C   OXT  sing N N 187 
GLY   OXT HXT  sing N N 188 
HIS   N   CA   sing N N 189 
HIS   N   H    sing N N 190 
HIS   N   H2   sing N N 191 
HIS   CA  C    sing N N 192 
HIS   CA  CB   sing N N 193 
HIS   CA  HA   sing N N 194 
HIS   C   O    doub N N 195 
HIS   C   OXT  sing N N 196 
HIS   CB  CG   sing N N 197 
HIS   CB  HB2  sing N N 198 
HIS   CB  HB3  sing N N 199 
HIS   CG  ND1  sing Y N 200 
HIS   CG  CD2  doub Y N 201 
HIS   ND1 CE1  doub Y N 202 
HIS   ND1 HD1  sing N N 203 
HIS   CD2 NE2  sing Y N 204 
HIS   CD2 HD2  sing N N 205 
HIS   CE1 NE2  sing Y N 206 
HIS   CE1 HE1  sing N N 207 
HIS   NE2 HE2  sing N N 208 
HIS   OXT HXT  sing N N 209 
HOH   O   H1   sing N N 210 
HOH   O   H2   sing N N 211 
ILE   N   CA   sing N N 212 
ILE   N   H    sing N N 213 
ILE   N   H2   sing N N 214 
ILE   CA  C    sing N N 215 
ILE   CA  CB   sing N N 216 
ILE   CA  HA   sing N N 217 
ILE   C   O    doub N N 218 
ILE   C   OXT  sing N N 219 
ILE   CB  CG1  sing N N 220 
ILE   CB  CG2  sing N N 221 
ILE   CB  HB   sing N N 222 
ILE   CG1 CD1  sing N N 223 
ILE   CG1 HG12 sing N N 224 
ILE   CG1 HG13 sing N N 225 
ILE   CG2 HG21 sing N N 226 
ILE   CG2 HG22 sing N N 227 
ILE   CG2 HG23 sing N N 228 
ILE   CD1 HD11 sing N N 229 
ILE   CD1 HD12 sing N N 230 
ILE   CD1 HD13 sing N N 231 
ILE   OXT HXT  sing N N 232 
LEU   N   CA   sing N N 233 
LEU   N   H    sing N N 234 
LEU   N   H2   sing N N 235 
LEU   CA  C    sing N N 236 
LEU   CA  CB   sing N N 237 
LEU   CA  HA   sing N N 238 
LEU   C   O    doub N N 239 
LEU   C   OXT  sing N N 240 
LEU   CB  CG   sing N N 241 
LEU   CB  HB2  sing N N 242 
LEU   CB  HB3  sing N N 243 
LEU   CG  CD1  sing N N 244 
LEU   CG  CD2  sing N N 245 
LEU   CG  HG   sing N N 246 
LEU   CD1 HD11 sing N N 247 
LEU   CD1 HD12 sing N N 248 
LEU   CD1 HD13 sing N N 249 
LEU   CD2 HD21 sing N N 250 
LEU   CD2 HD22 sing N N 251 
LEU   CD2 HD23 sing N N 252 
LEU   OXT HXT  sing N N 253 
LYS   N   CA   sing N N 254 
LYS   N   H    sing N N 255 
LYS   N   H2   sing N N 256 
LYS   CA  C    sing N N 257 
LYS   CA  CB   sing N N 258 
LYS   CA  HA   sing N N 259 
LYS   C   O    doub N N 260 
LYS   C   OXT  sing N N 261 
LYS   CB  CG   sing N N 262 
LYS   CB  HB2  sing N N 263 
LYS   CB  HB3  sing N N 264 
LYS   CG  CD   sing N N 265 
LYS   CG  HG2  sing N N 266 
LYS   CG  HG3  sing N N 267 
LYS   CD  CE   sing N N 268 
LYS   CD  HD2  sing N N 269 
LYS   CD  HD3  sing N N 270 
LYS   CE  NZ   sing N N 271 
LYS   CE  HE2  sing N N 272 
LYS   CE  HE3  sing N N 273 
LYS   NZ  HZ1  sing N N 274 
LYS   NZ  HZ2  sing N N 275 
LYS   NZ  HZ3  sing N N 276 
LYS   OXT HXT  sing N N 277 
MET   N   CA   sing N N 278 
MET   N   H    sing N N 279 
MET   N   H2   sing N N 280 
MET   CA  C    sing N N 281 
MET   CA  CB   sing N N 282 
MET   CA  HA   sing N N 283 
MET   C   O    doub N N 284 
MET   C   OXT  sing N N 285 
MET   CB  CG   sing N N 286 
MET   CB  HB2  sing N N 287 
MET   CB  HB3  sing N N 288 
MET   CG  SD   sing N N 289 
MET   CG  HG2  sing N N 290 
MET   CG  HG3  sing N N 291 
MET   SD  CE   sing N N 292 
MET   CE  HE1  sing N N 293 
MET   CE  HE2  sing N N 294 
MET   CE  HE3  sing N N 295 
MET   OXT HXT  sing N N 296 
PHE   N   CA   sing N N 297 
PHE   N   H    sing N N 298 
PHE   N   H2   sing N N 299 
PHE   CA  C    sing N N 300 
PHE   CA  CB   sing N N 301 
PHE   CA  HA   sing N N 302 
PHE   C   O    doub N N 303 
PHE   C   OXT  sing N N 304 
PHE   CB  CG   sing N N 305 
PHE   CB  HB2  sing N N 306 
PHE   CB  HB3  sing N N 307 
PHE   CG  CD1  doub Y N 308 
PHE   CG  CD2  sing Y N 309 
PHE   CD1 CE1  sing Y N 310 
PHE   CD1 HD1  sing N N 311 
PHE   CD2 CE2  doub Y N 312 
PHE   CD2 HD2  sing N N 313 
PHE   CE1 CZ   doub Y N 314 
PHE   CE1 HE1  sing N N 315 
PHE   CE2 CZ   sing Y N 316 
PHE   CE2 HE2  sing N N 317 
PHE   CZ  HZ   sing N N 318 
PHE   OXT HXT  sing N N 319 
PRO   N   CA   sing N N 320 
PRO   N   CD   sing N N 321 
PRO   N   H    sing N N 322 
PRO   CA  C    sing N N 323 
PRO   CA  CB   sing N N 324 
PRO   CA  HA   sing N N 325 
PRO   C   O    doub N N 326 
PRO   C   OXT  sing N N 327 
PRO   CB  CG   sing N N 328 
PRO   CB  HB2  sing N N 329 
PRO   CB  HB3  sing N N 330 
PRO   CG  CD   sing N N 331 
PRO   CG  HG2  sing N N 332 
PRO   CG  HG3  sing N N 333 
PRO   CD  HD2  sing N N 334 
PRO   CD  HD3  sing N N 335 
PRO   OXT HXT  sing N N 336 
SER   N   CA   sing N N 337 
SER   N   H    sing N N 338 
SER   N   H2   sing N N 339 
SER   CA  C    sing N N 340 
SER   CA  CB   sing N N 341 
SER   CA  HA   sing N N 342 
SER   C   O    doub N N 343 
SER   C   OXT  sing N N 344 
SER   CB  OG   sing N N 345 
SER   CB  HB2  sing N N 346 
SER   CB  HB3  sing N N 347 
SER   OG  HG   sing N N 348 
SER   OXT HXT  sing N N 349 
THR   N   CA   sing N N 350 
THR   N   H    sing N N 351 
THR   N   H2   sing N N 352 
THR   CA  C    sing N N 353 
THR   CA  CB   sing N N 354 
THR   CA  HA   sing N N 355 
THR   C   O    doub N N 356 
THR   C   OXT  sing N N 357 
THR   CB  OG1  sing N N 358 
THR   CB  CG2  sing N N 359 
THR   CB  HB   sing N N 360 
THR   OG1 HG1  sing N N 361 
THR   CG2 HG21 sing N N 362 
THR   CG2 HG22 sing N N 363 
THR   CG2 HG23 sing N N 364 
THR   OXT HXT  sing N N 365 
TYR   N   CA   sing N N 366 
TYR   N   H    sing N N 367 
TYR   N   H2   sing N N 368 
TYR   CA  C    sing N N 369 
TYR   CA  CB   sing N N 370 
TYR   CA  HA   sing N N 371 
TYR   C   O    doub N N 372 
TYR   C   OXT  sing N N 373 
TYR   CB  CG   sing N N 374 
TYR   CB  HB2  sing N N 375 
TYR   CB  HB3  sing N N 376 
TYR   CG  CD1  doub Y N 377 
TYR   CG  CD2  sing Y N 378 
TYR   CD1 CE1  sing Y N 379 
TYR   CD1 HD1  sing N N 380 
TYR   CD2 CE2  doub Y N 381 
TYR   CD2 HD2  sing N N 382 
TYR   CE1 CZ   doub Y N 383 
TYR   CE1 HE1  sing N N 384 
TYR   CE2 CZ   sing Y N 385 
TYR   CE2 HE2  sing N N 386 
TYR   CZ  OH   sing N N 387 
TYR   OH  HH   sing N N 388 
TYR   OXT HXT  sing N N 389 
VAL   N   CA   sing N N 390 
VAL   N   H    sing N N 391 
VAL   N   H2   sing N N 392 
VAL   CA  C    sing N N 393 
VAL   CA  CB   sing N N 394 
VAL   CA  HA   sing N N 395 
VAL   C   O    doub N N 396 
VAL   C   OXT  sing N N 397 
VAL   CB  CG1  sing N N 398 
VAL   CB  CG2  sing N N 399 
VAL   CB  HB   sing N N 400 
VAL   CG1 HG11 sing N N 401 
VAL   CG1 HG12 sing N N 402 
VAL   CG1 HG13 sing N N 403 
VAL   CG2 HG21 sing N N 404 
VAL   CG2 HG22 sing N N 405 
VAL   CG2 HG23 sing N N 406 
VAL   OXT HXT  sing N N 407 
# 
_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                    7HFV 
_atom_sites.fract_transf_matrix[1][1]   0.011266 
_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]   0.011266 
_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]   0.025417 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    A VAL   A 1 3   ? 19.665 -16.276 22.222  0.66 43.47 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.616 -16.378 22.202  0.34 41.93 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.694 -15.200 22.387  0.66 43.14 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.703 -15.258 22.398  0.34 41.63 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.340 -13.850 22.093  0.66 42.12 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.388 -13.945 22.037  0.34 40.64 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.458 -13.580 22.536  0.66 42.32 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.520 -13.692 22.453  0.34 40.78 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.057 -15.231 23.793  0.66 43.43 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.158 -15.226 23.842  0.34 42.05 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.044 -14.104 23.952  0.66 43.75 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.214 -14.045 24.031  0.34 42.32 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.399 -16.580 24.045  0.66 43.51 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.455 -16.534 24.176  0.34 42.15 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.982 -15.321 21.745  0.66 51.82 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.946 -15.364 21.805  0.34 50.01 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.749 -15.107 24.462  0.66 52.17 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.898 -15.119 24.460  0.34 50.51 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.528 -14.255 24.761  0.66 52.55 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.735 -14.155 24.867  0.34 50.84 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.515 -13.259 24.016  0.66 52.55 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.731 -13.225 24.053  0.34 50.84 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.453 -14.099 23.183  0.66 52.55 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.586 -14.023 23.292  0.34 50.84 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.951 -16.558 24.905  0.66 52.26 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 17.070 -16.468 25.064  0.34 50.64 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.755 -16.752 23.341  0.66 52.26 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.755 -16.691 23.523  0.34 50.64 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.082 -17.269 24.045  0.66 52.26 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.102 -17.256 24.149  0.34 50.64 ?  3   VAL   A HG23 1 
ATOM   31   N  N    A ASN   A 1 4   ? 18.637 -13.011 21.333  0.66 40.51 ?  4   ASN   A N    1 
ATOM   32   N  N    B ASN   A 1 4   ? 18.702 -13.115 21.253  0.34 39.23 ?  4   ASN   A N    1 
ATOM   33   C  CA   A ASN   A 1 4   ? 19.085 -11.658 21.031  0.66 38.81 ?  4   ASN   A CA   1 
ATOM   34   C  CA   B ASN   A 1 4   ? 19.168 -11.773 20.929  0.34 37.77 ?  4   ASN   A CA   1 
ATOM   35   C  C    A ASN   A 1 4   ? 17.931 -10.683 21.259  0.66 37.23 ?  4   ASN   A C    1 
ATOM   36   C  C    B ASN   A 1 4   ? 18.041 -10.775 21.180  0.34 36.45 ?  4   ASN   A C    1 
ATOM   37   O  O    A ASN   A 1 4   ? 16.809 -11.079 21.590  0.66 37.21 ?  4   ASN   A O    1 
ATOM   38   O  O    B ASN   A 1 4   ? 16.914 -11.148 21.521  0.34 36.56 ?  4   ASN   A O    1 
ATOM   39   C  CB   A ASN   A 1 4   ? 19.664 -11.554 19.612  0.66 38.60 ?  4   ASN   A CB   1 
ATOM   40   C  CB   B ASN   A 1 4   ? 19.709 -11.679 19.495  0.34 37.60 ?  4   ASN   A CB   1 
ATOM   41   C  CG   A ASN   A 1 4   ? 18.665 -11.931 18.537  0.66 38.33 ?  4   ASN   A CG   1 
ATOM   42   C  CG   B ASN   A 1 4   ? 18.674 -12.037 18.449  0.34 37.48 ?  4   ASN   A CG   1 
ATOM   43   O  OD1  A ASN   A 1 4   ? 17.545 -11.421 18.505  0.66 38.23 ?  4   ASN   A OD1  1 
ATOM   44   O  OD1  B ASN   A 1 4   ? 17.660 -11.355 18.302  0.34 37.39 ?  4   ASN   A OD1  1 
ATOM   45   N  ND2  A ASN   A 1 4   ? 19.069 -12.830 17.645  0.66 38.11 ?  4   ASN   A ND2  1 
ATOM   46   N  ND2  B ASN   A 1 4   ? 18.938 -13.099 17.695  0.34 37.37 ?  4   ASN   A ND2  1 
ATOM   47   H  H    A ASN   A 1 4   ? 17.880 -13.210 20.973  0.66 48.67 ?  4   ASN   A H    1 
ATOM   48   H  H    B ASN   A 1 4   ? 17.946 -13.314 20.892  0.34 47.13 ?  4   ASN   A H    1 
ATOM   49   H  HA   A ASN   A 1 4   ? 19.793 -11.425 21.646  0.66 46.63 ?  4   ASN   A HA   1 
ATOM   50   H  HA   B ASN   A 1 4   ? 19.895 -11.548 21.527  0.34 45.38 ?  4   ASN   A HA   1 
ATOM   51   H  HB2  A ASN   A 1 4   ? 19.945 -10.639 19.452  0.66 46.38 ?  4   ASN   A HB2  1 
ATOM   52   H  HB2  B ASN   A 1 4   ? 20.002 -10.768 19.328  0.34 45.17 ?  4   ASN   A HB2  1 
ATOM   53   H  HB3  A ASN   A 1 4   ? 20.424 -12.151 19.540  0.66 46.38 ?  4   ASN   A HB3  1 
ATOM   54   H  HB3  B ASN   A 1 4   ? 20.456 -12.289 19.400  0.34 45.17 ?  4   ASN   A HB3  1 
ATOM   55   H  HD21 A ASN   A 1 4   ? 18.541 -13.077 17.013  0.66 45.79 ?  4   ASN   A HD21 1 
ATOM   56   H  HD21 B ASN   A 1 4   ? 18.386 -13.342 17.082  0.34 44.89 ?  4   ASN   A HD21 1 
ATOM   57   H  HD22 A ASN   A 1 4   ? 19.860 -13.166 17.699  0.66 45.79 ?  4   ASN   A HD22 1 
ATOM   58   H  HD22 B ASN   A 1 4   ? 19.661 -13.548 17.824  0.34 44.89 ?  4   ASN   A HD22 1 
ATOM   59   N  N    A SER   A 1 5   ? 18.216 -9.394  21.075  0.66 35.61 ?  5   SER   A N    1 
ATOM   60   N  N    B SER   A 1 5   ? 18.354 -9.493  21.003  0.34 34.92 ?  5   SER   A N    1 
ATOM   61   C  CA   A SER   A 1 5   ? 17.296 -8.322  21.435  0.66 34.08 ?  5   SER   A CA   1 
ATOM   62   C  CA   B SER   A 1 5   ? 17.460 -8.409  21.392  0.34 33.35 ?  5   SER   A CA   1 
ATOM   63   C  C    A SER   A 1 5   ? 16.450 -7.832  20.264  0.66 31.57 ?  5   SER   A C    1 
ATOM   64   C  C    B SER   A 1 5   ? 16.575 -7.909  20.256  0.34 30.94 ?  5   SER   A C    1 
ATOM   65   O  O    A SER   A 1 5   ? 15.785 -6.799  20.389  0.66 32.14 ?  5   SER   A O    1 
ATOM   66   O  O    B SER   A 1 5   ? 15.805 -6.966  20.466  0.34 31.22 ?  5   SER   A O    1 
ATOM   67   C  CB   A SER   A 1 5   ? 18.063 -7.147  22.047  0.66 34.80 ?  5   SER   A CB   1 
ATOM   68   C  CB   B SER   A 1 5   ? 18.264 -7.241  21.975  0.34 33.91 ?  5   SER   A CB   1 
ATOM   69   O  OG   A SER   A 1 5   ? 19.051 -6.664  21.155  0.66 35.48 ?  5   SER   A OG   1 
ATOM   70   O  OG   B SER   A 1 5   ? 19.218 -6.763  21.043  0.34 34.35 ?  5   SER   A OG   1 
ATOM   71   H  H    A SER   A 1 5   ? 18.951 -9.112  20.731  0.66 42.79 ?  5   SER   A H    1 
ATOM   72   H  H    B SER   A 1 5   ? 19.090 -9.224  20.651  0.34 41.96 ?  5   SER   A H    1 
ATOM   73   H  HA   A SER   A 1 5   ? 16.695 -8.652  22.119  0.66 40.95 ?  5   SER   A HA   1 
ATOM   74   H  HA   B SER   A 1 5   ? 16.876 -8.731  22.092  0.34 40.08 ?  5   SER   A HA   1 
ATOM   75   H  HB2  A SER   A 1 5   ? 17.438 -6.428  22.243  0.66 41.82 ?  5   SER   A HB2  1 
ATOM   76   H  HB2  B SER   A 1 5   ? 17.655 -6.520  22.203  0.34 40.75 ?  5   SER   A HB2  1 
ATOM   77   H  HB3  A SER   A 1 5   ? 18.493 -7.439  22.867  0.66 41.82 ?  5   SER   A HB3  1 
ATOM   78   H  HB3  B SER   A 1 5   ? 18.727 -7.544  22.773  0.34 40.75 ?  5   SER   A HB3  1 
ATOM   79   H  HG   A SER   A 1 5   ? 19.465 -6.019  21.505  0.66 42.63 ?  5   SER   A HG   1 
ATOM   80   H  HG   B SER   A 1 5   ? 19.650 -6.124  21.378  0.34 41.27 ?  5   SER   A HG   1 
ATOM   81   N  N    A PHE   A 1 6   ? 16.458 -8.534  19.134  0.66 28.52 ?  6   PHE   A N    1 
ATOM   82   N  N    B PHE   A 1 6   ? 16.657 -8.503  19.069  0.34 28.28 ?  6   PHE   A N    1 
ATOM   83   C  CA   A PHE   A 1 6   ? 15.565 -8.173  18.041  0.66 25.64 ?  6   PHE   A CA   1 
ATOM   84   C  CA   B PHE   A 1 6   ? 15.728 -8.151  18.003  0.34 25.72 ?  6   PHE   A CA   1 
ATOM   85   C  C    A PHE   A 1 6   ? 14.129 -8.525  18.410  0.66 25.52 ?  6   PHE   A C    1 
ATOM   86   C  C    B PHE   A 1 6   ? 14.316 -8.549  18.414  0.34 25.16 ?  6   PHE   A C    1 
ATOM   87   O  O    A PHE   A 1 6   ? 13.861 -9.588  18.976  0.66 26.51 ?  6   PHE   A O    1 
ATOM   88   O  O    B PHE   A 1 6   ? 14.030 -9.734  18.613  0.34 25.33 ?  6   PHE   A O    1 
ATOM   89   C  CB   A PHE   A 1 6   ? 15.975 -8.891  16.757  0.66 23.72 ?  6   PHE   A CB   1 
ATOM   90   C  CB   B PHE   A 1 6   ? 16.117 -8.874  16.716  0.34 24.10 ?  6   PHE   A CB   1 
ATOM   91   C  CG   A PHE   A 1 6   ? 17.250 -8.366  16.154  0.66 22.10 ?  6   PHE   A CG   1 
ATOM   92   C  CG   B PHE   A 1 6   ? 17.355 -8.332  16.058  0.34 22.70 ?  6   PHE   A CG   1 
ATOM   93   C  CD1  A PHE   A 1 6   ? 17.248 -7.204  15.396  0.66 21.45 ?  6   PHE   A CD1  1 
ATOM   94   C  CD1  B PHE   A 1 6   ? 17.362 -7.065  15.498  0.34 21.98 ?  6   PHE   A CD1  1 
ATOM   95   C  CD2  A PHE   A 1 6   ? 18.450 -9.029  16.353  0.66 22.25 ?  6   PHE   A CD2  1 
ATOM   96   C  CD2  B PHE   A 1 6   ? 18.505 -9.101  15.978  0.34 22.27 ?  6   PHE   A CD2  1 
ATOM   97   C  CE1  A PHE   A 1 6   ? 18.422 -6.714  14.844  0.66 21.38 ?  6   PHE   A CE1  1 
ATOM   98   C  CE1  B PHE   A 1 6   ? 18.499 -6.567  14.883  0.34 21.71 ?  6   PHE   A CE1  1 
ATOM   99   C  CE2  A PHE   A 1 6   ? 19.620 -8.551  15.802  0.66 22.01 ?  6   PHE   A CE2  1 
ATOM   100  C  CE2  B PHE   A 1 6   ? 19.641 -8.612  15.363  0.34 21.99 ?  6   PHE   A CE2  1 
ATOM   101  C  CZ   A PHE   A 1 6   ? 19.608 -7.387  15.046  0.66 21.81 ?  6   PHE   A CZ   1 
ATOM   102  C  CZ   B PHE   A 1 6   ? 19.640 -7.342  14.815  0.34 21.75 ?  6   PHE   A CZ   1 
ATOM   103  H  H    A PHE   A 1 6   ? 16.962 -9.212  18.980  0.66 34.28 ?  6   PHE   A H    1 
ATOM   104  H  H    B PHE   A 1 6   ? 17.233 -9.105  18.858  0.34 34.00 ?  6   PHE   A H    1 
ATOM   105  H  HA   A PHE   A 1 6   ? 15.610 -7.222  17.889  0.66 30.82 ?  6   PHE   A HA   1 
ATOM   106  H  HA   B PHE   A 1 6   ? 15.751 -7.193  17.847  0.34 30.92 ?  6   PHE   A HA   1 
ATOM   107  H  HB2  A PHE   A 1 6   ? 16.102 -9.836  16.955  0.66 28.52 ?  6   PHE   A HB2  1 
ATOM   108  H  HB2  B PHE   A 1 6   ? 16.276 -9.808  16.924  0.34 28.98 ?  6   PHE   A HB2  1 
ATOM   109  H  HB3  A PHE   A 1 6   ? 15.267 -8.790  16.102  0.66 28.52 ?  6   PHE   A HB3  1 
ATOM   110  H  HB3  B PHE   A 1 6   ? 15.389 -8.796  16.084  0.34 28.98 ?  6   PHE   A HB3  1 
ATOM   111  H  HD1  A PHE   A 1 6   ? 16.445 -6.753  15.259  0.66 25.80 ?  6   PHE   A HD1  1 
ATOM   112  H  HD1  B PHE   A 1 6   ? 16.596 -6.540  15.544  0.34 26.43 ?  6   PHE   A HD1  1 
ATOM   113  H  HD2  A PHE   A 1 6   ? 18.464 -9.810  16.862  0.66 26.76 ?  6   PHE   A HD2  1 
ATOM   114  H  HD2  B PHE   A 1 6   ? 18.514 -9.955  16.346  0.34 26.78 ?  6   PHE   A HD2  1 
ATOM   115  H  HE1  A PHE   A 1 6   ? 18.403 -5.938  14.335  0.66 25.71 ?  6   PHE   A HE1  1 
ATOM   116  H  HE1  B PHE   A 1 6   ? 18.493 -5.713  14.514  0.34 26.11 ?  6   PHE   A HE1  1 
ATOM   117  H  HE2  A PHE   A 1 6   ? 20.422 -9.002  15.942  0.66 26.47 ?  6   PHE   A HE2  1 
ATOM   118  H  HE2  B PHE   A 1 6   ? 20.410 -9.136  15.319  0.34 26.44 ?  6   PHE   A HE2  1 
ATOM   119  H  HZ   A PHE   A 1 6   ? 20.394 -7.062  14.675  0.66 26.22 ?  6   PHE   A HZ   1 
ATOM   120  H  HZ   B PHE   A 1 6   ? 20.404 -7.011  14.401  0.34 26.16 ?  6   PHE   A HZ   1 
ATOM   121  N  N    A SER   A 1 7   ? 13.198 -7.623  18.089  0.66 24.14 ?  7   SER   A N    1 
ATOM   122  N  N    B SER   A 1 7   ? 13.431 -7.560  18.534  0.34 24.65 ?  7   SER   A N    1 
ATOM   123  C  CA   A SER   A 1 7   ? 11.825 -7.710  18.574  0.66 23.69 ?  7   SER   A CA   1 
ATOM   124  C  CA   B SER   A 1 7   ? 12.093 -7.766  19.068  0.34 24.46 ?  7   SER   A CA   1 
ATOM   125  C  C    A SER   A 1 7   ? 10.827 -7.489  17.444  0.66 21.81 ?  7   SER   A C    1 
ATOM   126  C  C    B SER   A 1 7   ? 11.048 -7.307  18.061  0.34 23.12 ?  7   SER   A C    1 
ATOM   127  O  O    A SER   A 1 7   ? 11.009 -6.609  16.600  0.66 21.49 ?  7   SER   A O    1 
ATOM   128  O  O    B SER   A 1 7   ? 11.233 -6.299  17.373  0.34 23.18 ?  7   SER   A O    1 
ATOM   129  C  CB   A SER   A 1 7   ? 11.584 -6.661  19.670  0.66 25.09 ?  7   SER   A CB   1 
ATOM   130  C  CB   B SER   A 1 7   ? 11.918 -6.996  20.381  0.34 25.56 ?  7   SER   A CB   1 
ATOM   131  O  OG   A SER   A 1 7   ? 10.265 -6.734  20.176  0.66 26.82 ?  7   SER   A OG   1 
ATOM   132  O  OG   B SER   A 1 7   ? 10.557 -6.949  20.766  0.34 26.36 ?  7   SER   A OG   1 
ATOM   133  H  H    A SER   A 1 7   ? 13.345 -6.945  17.582  0.66 29.02 ?  7   SER   A H    1 
ATOM   134  H  H    B SER   A 1 7   ? 13.587 -6.745  18.299  0.34 29.64 ?  7   SER   A H    1 
ATOM   135  H  HA   A SER   A 1 7   ? 11.671 -8.588  18.955  0.66 28.48 ?  7   SER   A HA   1 
ATOM   136  H  HA   B SER   A 1 7   ? 11.952 -8.708  19.244  0.34 29.41 ?  7   SER   A HA   1 
ATOM   137  H  HB2  A SER   A 1 7   ? 12.215 -6.811  20.394  0.66 30.16 ?  7   SER   A HB2  1 
ATOM   138  H  HB2  B SER   A 1 7   ? 12.419 -7.446  21.079  0.34 30.73 ?  7   SER   A HB2  1 
ATOM   139  H  HB3  A SER   A 1 7   ? 11.724 -5.777  19.295  0.66 30.16 ?  7   SER   A HB3  1 
ATOM   140  H  HB3  B SER   A 1 7   ? 12.254 -6.092  20.263  0.34 30.73 ?  7   SER   A HB3  1 
ATOM   141  H  HG   A SER   A 1 7   ? 10.158 -6.159  20.781  0.66 32.24 ?  7   SER   A HG   1 
ATOM   142  H  HG   B SER   A 1 7   ? 10.474 -6.509  21.476  0.34 31.69 ?  7   SER   A HG   1 
ATOM   143  N  N    A GLY   A 1 8   ? 9.755  -8.281  17.450  0.66 20.89 ?  8   GLY   A N    1 
ATOM   144  N  N    B GLY   A 1 8   ? 9.952  -8.056  17.976  0.34 21.65 ?  8   GLY   A N    1 
ATOM   145  C  CA   A GLY   A 1 8   ? 8.659  -8.072  16.522  0.66 19.85 ?  8   GLY   A CA   1 
ATOM   146  C  CA   B GLY   A 1 8   ? 8.852  -7.704  17.105  0.34 20.53 ?  8   GLY   A CA   1 
ATOM   147  C  C    A GLY   A 1 8   ? 8.879  -8.585  15.118  0.66 19.12 ?  8   GLY   A C    1 
ATOM   148  C  C    B GLY   A 1 8   ? 8.958  -8.217  15.690  0.34 19.10 ?  8   GLY   A C    1 
ATOM   149  O  O    A GLY   A 1 8   ? 8.155  -8.174  14.204  0.66 19.23 ?  8   GLY   A O    1 
ATOM   150  O  O    B GLY   A 1 8   ? 8.141  -7.828  14.848  0.34 19.18 ?  8   GLY   A O    1 
ATOM   151  H  H    A GLY   A 1 8   ? 9.642  -8.941  17.988  0.66 25.12 ?  8   GLY   A H    1 
ATOM   152  H  H    B GLY   A 1 8   ? 9.828  -8.784  18.414  0.34 26.04 ?  8   GLY   A H    1 
ATOM   153  H  HA2  A GLY   A 1 8   ? 7.864  -8.502  16.882  0.66 23.87 ?  8   GLY   A HA2  1 
ATOM   154  H  HA2  B GLY   A 1 8   ? 8.030  -8.056  17.474  0.34 24.69 ?  8   GLY   A HA2  1 
ATOM   155  H  HA3  A GLY   A 1 8   ? 8.477  -7.121  16.463  0.66 23.87 ?  8   GLY   A HA3  1 
ATOM   156  H  HA3  B GLY   A 1 8   ? 8.776  -6.738  17.066  0.34 24.69 ?  8   GLY   A HA3  1 
ATOM   157  N  N    A TYR   A 1 9   ? 9.853  -9.472  14.913  0.66 17.71 ?  9   TYR   A N    1 
ATOM   158  N  N    B TYR   A 1 9   ? 9.927  -9.080  15.399  0.34 17.86 ?  9   TYR   A N    1 
ATOM   159  C  CA   A TYR   A 1 9   ? 10.146 -10.007 13.592  0.66 16.44 ?  9   TYR   A CA   1 
ATOM   160  C  CA   B TYR   A 1 9   ? 10.119 -9.594  14.053  0.34 16.64 ?  9   TYR   A CA   1 
ATOM   161  C  C    A TYR   A 1 9   ? 9.285  -11.226 13.292  0.66 15.96 ?  9   TYR   A C    1 
ATOM   162  C  C    B TYR   A 1 9   ? 9.248  -10.821 13.819  0.34 15.63 ?  9   TYR   A C    1 
ATOM   163  O  O    A TYR   A 1 9   ? 9.015  -12.049 14.172  0.66 17.09 ?  9   TYR   A O    1 
ATOM   164  O  O    B TYR   A 1 9   ? 8.947  -11.584 14.741  0.34 16.11 ?  9   TYR   A O    1 
ATOM   165  C  CB   A TYR   A 1 9   ? 11.623 -10.401 13.491  0.66 16.87 ?  9   TYR   A CB   1 
ATOM   166  C  CB   B TYR   A 1 9   ? 11.590 -9.958  13.812  0.34 17.18 ?  9   TYR   A CB   1 
ATOM   167  C  CG   A TYR   A 1 9   ? 12.530 -9.209  13.315  0.66 16.87 ?  9   TYR   A CG   1 
ATOM   168  C  CG   B TYR   A 1 9   ? 12.480 -8.761  13.553  0.34 17.55 ?  9   TYR   A CG   1 
ATOM   169  C  CD1  A TYR   A 1 9   ? 12.873 -8.411  14.399  0.66 16.95 ?  9   TYR   A CD1  1 
ATOM   170  C  CD1  B TYR   A 1 9   ? 12.734 -7.840  14.554  0.34 17.66 ?  9   TYR   A CD1  1 
ATOM   171  C  CD2  A TYR   A 1 9   ? 13.014 -8.859  12.061  0.66 17.31 ?  9   TYR   A CD2  1 
ATOM   172  C  CD2  B TYR   A 1 9   ? 13.051 -8.548  12.304  0.34 17.35 ?  9   TYR   A CD2  1 
ATOM   173  C  CE1  A TYR   A 1 9   ? 13.684 -7.307  14.240  0.66 17.45 ?  9   TYR   A CE1  1 
ATOM   174  C  CE1  B TYR   A 1 9   ? 13.537 -6.746  14.328  0.34 17.68 ?  9   TYR   A CE1  1 
ATOM   175  C  CE2  A TYR   A 1 9   ? 13.822 -7.762  11.894  0.66 17.93 ?  9   TYR   A CE2  1 
ATOM   176  C  CE2  B TYR   A 1 9   ? 13.854 -7.449  12.065  0.34 17.48 ?  9   TYR   A CE2  1 
ATOM   177  C  CZ   A TYR   A 1 9   ? 14.147 -6.987  12.984  0.66 18.02 ?  9   TYR   A CZ   1 
ATOM   178  C  CZ   B TYR   A 1 9   ? 14.089 -6.552  13.083  0.34 17.64 ?  9   TYR   A CZ   1 
ATOM   179  O  OH   A TYR   A 1 9   ? 14.948 -5.892  12.811  0.66 19.46 ?  9   TYR   A OH   1 
ATOM   180  O  OH   B TYR   A 1 9   ? 14.881 -5.452  12.864  0.34 18.06 ?  9   TYR   A OH   1 
ATOM   181  H  H    A TYR   A 1 9   ? 10.357 -9.782  15.537  0.66 21.31 ?  9   TYR   A H    1 
ATOM   182  H  H    B TYR   A 1 9   ? 10.489 -9.390  15.972  0.34 21.49 ?  9   TYR   A H    1 
ATOM   183  H  HA   A TYR   A 1 9   ? 9.962  -9.333  12.924  0.66 19.79 ?  9   TYR   A HA   1 
ATOM   184  H  HA   B TYR   A 1 9   ? 9.869  -8.914  13.408  0.34 20.03 ?  9   TYR   A HA   1 
ATOM   185  H  HB2  A TYR   A 1 9   ? 11.883 -10.869 14.305  0.66 20.30 ?  9   TYR   A HB2  1 
ATOM   186  H  HB2  B TYR   A 1 9   ? 11.937 -10.429 14.586  0.34 20.68 ?  9   TYR   A HB2  1 
ATOM   187  H  HB3  A TYR   A 1 9   ? 11.733 -10.989 12.727  0.66 20.30 ?  9   TYR   A HB3  1 
ATOM   188  H  HB3  B TYR   A 1 9   ? 11.635 -10.532 13.033  0.34 20.68 ?  9   TYR   A HB3  1 
ATOM   189  H  HD1  A TYR   A 1 9   ? 12.544 -8.630  15.247  0.66 20.40 ?  9   TYR   A HD1  1 
ATOM   190  H  HD1  B TYR   A 1 9   ? 12.357 -7.965  15.395  0.34 21.25 ?  9   TYR   A HD1  1 
ATOM   191  H  HD2  A TYR   A 1 9   ? 12.789 -9.385  11.323  0.66 20.83 ?  9   TYR   A HD2  1 
ATOM   192  H  HD2  B TYR   A 1 9   ? 12.892 -9.157  11.617  0.34 20.87 ?  9   TYR   A HD2  1 
ATOM   193  H  HE1  A TYR   A 1 9   ? 13.907 -6.785  14.975  0.66 21.00 ?  9   TYR   A HE1  1 
ATOM   194  H  HE1  B TYR   A 1 9   ? 13.692 -6.133  15.008  0.34 21.28 ?  9   TYR   A HE1  1 
ATOM   195  H  HE2  A TYR   A 1 9   ? 14.148 -7.546  11.051  0.66 21.57 ?  9   TYR   A HE2  1 
ATOM   196  H  HE2  B TYR   A 1 9   ? 14.234 -7.317  11.224  0.34 21.04 ?  9   TYR   A HE2  1 
ATOM   197  H  HH   A TYR   A 1 9   ? 15.085 -5.519  13.550  0.66 23.41 ?  9   TYR   A HH   1 
ATOM   198  H  HH   B TYR   A 1 9   ? 15.016 -5.048  13.588  0.34 21.72 ?  9   TYR   A HH   1 
ATOM   199  N  N    A LEU   A 1 10  ? 8.890  -11.355 12.031  0.66 15.53 ?  10  LEU   A N    1 
ATOM   200  N  N    B LEU   A 1 10  ? 8.817  -10.977 12.570  0.34 14.89 ?  10  LEU   A N    1 
ATOM   201  C  CA   A LEU   A 1 10  ? 8.274  -12.575 11.535  0.66 15.42 ?  10  LEU   A CA   1 
ATOM   202  C  CA   B LEU   A 1 10  ? 8.172  -12.195 12.103  0.34 14.63 ?  10  LEU   A CA   1 
ATOM   203  C  C    A LEU   A 1 10  ? 9.387  -13.509 11.079  0.66 15.17 ?  10  LEU   A C    1 
ATOM   204  C  C    B LEU   A 1 10  ? 9.253  -13.157 11.632  0.34 13.70 ?  10  LEU   A C    1 
ATOM   205  O  O    A LEU   A 1 10  ? 10.325 -13.078 10.398  0.66 15.18 ?  10  LEU   A O    1 
ATOM   206  O  O    B LEU   A 1 10  ? 10.144 -12.770 10.870  0.34 13.60 ?  10  LEU   A O    1 
ATOM   207  C  CB   A LEU   A 1 10  ? 7.359  -12.252 10.357  0.66 16.19 ?  10  LEU   A CB   1 
ATOM   208  C  CB   B LEU   A 1 10  ? 7.236  -11.865 10.939  0.34 15.40 ?  10  LEU   A CB   1 
ATOM   209  C  CG   A LEU   A 1 10  ? 6.653  -13.441 9.708   0.66 18.24 ?  10  LEU   A CG   1 
ATOM   210  C  CG   B LEU   A 1 10  ? 6.509  -13.035 10.279  0.34 16.68 ?  10  LEU   A CG   1 
ATOM   211  C  CD1  A LEU   A 1 10  ? 5.599  -14.004 10.644  0.66 19.33 ?  10  LEU   A CD1  1 
ATOM   212  C  CD1  B LEU   A 1 10  ? 5.470  -13.622 11.219  0.34 17.58 ?  10  LEU   A CD1  1 
ATOM   213  C  CD2  A LEU   A 1 10  ? 6.042  -13.060 8.375   0.66 19.57 ?  10  LEU   A CD2  1 
ATOM   214  C  CD2  B LEU   A 1 10  ? 5.866  -12.570 8.985   0.34 17.65 ?  10  LEU   A CD2  1 
ATOM   215  H  H    A LEU   A 1 10  ? 8.972  -10.748 11.430  0.66 18.69 ?  10  LEU   A H    1 
ATOM   216  H  H    B LEU   A 1 10  ? 8.874  -10.364 11.966  0.34 17.92 ?  10  LEU   A H    1 
ATOM   217  H  HA   A LEU   A 1 10  ? 7.763  -13.012 12.240  0.66 18.56 ?  10  LEU   A HA   1 
ATOM   218  H  HA   B LEU   A 1 10  ? 7.659  -12.605 12.819  0.34 17.61 ?  10  LEU   A HA   1 
ATOM   219  H  HB2  A LEU   A 1 10  ? 6.672  -11.647 10.667  0.66 19.48 ?  10  LEU   A HB2  1 
ATOM   220  H  HB2  B LEU   A 1 10  ? 6.551  -11.253 11.255  0.34 18.53 ?  10  LEU   A HB2  1 
ATOM   221  H  HB3  A LEU   A 1 10  ? 7.889  -11.826 9.671   0.66 19.48 ?  10  LEU   A HB3  1 
ATOM   222  H  HB3  B LEU   A 1 10  ? 7.755  -11.428 10.244  0.34 18.53 ?  10  LEU   A HB3  1 
ATOM   223  H  HG   A LEU   A 1 10  ? 7.301  -14.147 9.545   0.66 21.94 ?  10  LEU   A HG   1 
ATOM   224  H  HG   B LEU   A 1 10  ? 7.150  -13.730 10.063  0.34 20.07 ?  10  LEU   A HG   1 
ATOM   225  H  HD11 A LEU   A 1 10  ? 5.248  -14.827 10.270  0.66 23.25 ?  10  LEU   A HD11 1 
ATOM   226  H  HD11 B LEU   A 1 10  ? 5.057  -14.389 10.791  0.34 21.15 ?  10  LEU   A HD11 1 
ATOM   227  H  HD12 A LEU   A 1 10  ? 5.999  -14.180 11.510  0.66 23.25 ?  10  LEU   A HD12 1 
ATOM   228  H  HD12 B LEU   A 1 10  ? 5.905  -13.895 12.040  0.34 21.15 ?  10  LEU   A HD12 1 
ATOM   229  H  HD13 A LEU   A 1 10  ? 4.885  -13.353 10.740  0.66 23.25 ?  10  LEU   A HD13 1 
ATOM   230  H  HD13 B LEU   A 1 10  ? 4.799  -12.947 11.407  0.34 21.15 ?  10  LEU   A HD13 1 
ATOM   231  H  HD21 A LEU   A 1 10  ? 5.603  -13.836 7.996   0.66 23.54 ?  10  LEU   A HD21 1 
ATOM   232  H  HD21 B LEU   A 1 10  ? 5.400  -13.319 8.581   0.34 21.23 ?  10  LEU   A HD21 1 
ATOM   233  H  HD22 A LEU   A 1 10  ? 5.398  -12.350 8.519   0.66 23.54 ?  10  LEU   A HD22 1 
ATOM   234  H  HD22 B LEU   A 1 10  ? 5.240  -11.857 9.185   0.34 21.23 ?  10  LEU   A HD22 1 
ATOM   235  H  HD23 A LEU   A 1 10  ? 6.747  -12.755 7.784   0.66 23.54 ?  10  LEU   A HD23 1 
ATOM   236  H  HD23 B LEU   A 1 10  ? 6.559  -12.248 8.388   0.34 21.23 ?  10  LEU   A HD23 1 
ATOM   237  N  N    A LYS   A 1 11  ? 9.291  -14.778 11.470  0.66 15.22 ?  11  LYS   A N    1 
ATOM   238  N  N    B LYS   A 1 11  ? 9.182  -14.399 12.092  0.34 14.16 ?  11  LYS   A N    1 
ATOM   239  C  CA   A LYS   A 1 11  ? 10.286 -15.781 11.118  0.66 15.52 ?  11  LYS   A CA   1 
ATOM   240  C  CA   B LYS   A 1 11  ? 10.148 -15.410 11.684  0.34 14.12 ?  11  LYS   A CA   1 
ATOM   241  C  C    A LYS   A 1 11  ? 9.921  -16.370 9.762   0.66 15.45 ?  11  LYS   A C    1 
ATOM   242  C  C    B LYS   A 1 11  ? 9.758  -15.961 10.317  0.34 13.86 ?  11  LYS   A C    1 
ATOM   243  O  O    A LYS   A 1 11  ? 8.853  -16.968 9.612   0.66 16.62 ?  11  LYS   A O    1 
ATOM   244  O  O    B LYS   A 1 11  ? 8.648  -16.476 10.144  0.34 14.48 ?  11  LYS   A O    1 
ATOM   245  C  CB   A LYS   A 1 11  ? 10.326 -16.867 12.194  0.66 15.20 ?  11  LYS   A CB   1 
ATOM   246  C  CB   B LYS   A 1 11  ? 10.190 -16.520 12.729  0.34 14.68 ?  11  LYS   A CB   1 
ATOM   247  C  CG   A LYS   A 1 11  ? 11.350 -17.975 11.973  0.66 15.53 ?  11  LYS   A CG   1 
ATOM   248  C  CG   B LYS   A 1 11  ? 11.191 -17.629 12.446  0.34 15.02 ?  11  LYS   A CG   1 
ATOM   249  C  CD   A LYS   A 1 11  ? 11.465 -18.835 13.230  0.66 16.00 ?  11  LYS   A CD   1 
ATOM   250  C  CD   B LYS   A 1 11  ? 11.276 -18.590 13.627  0.34 15.21 ?  11  LYS   A CD   1 
ATOM   251  C  CE   A LYS   A 1 11  ? 12.450 -19.975 13.069  0.66 16.32 ?  11  LYS   A CE   1 
ATOM   252  C  CE   B LYS   A 1 11  ? 12.293 -19.704 13.393  0.34 14.84 ?  11  LYS   A CE   1 
ATOM   253  N  NZ   A LYS   A 1 11  ? 13.814 -19.474 12.776  0.66 16.12 ?  11  LYS   A NZ   1 
ATOM   254  N  NZ   B LYS   A 1 11  ? 13.684 -19.189 13.240  0.34 14.55 ?  11  LYS   A NZ   1 
ATOM   255  H  H    A LYS   A 1 11  ? 8.642  -15.091 11.947  0.66 18.32 ?  11  LYS   A H    1 
ATOM   256  H  H    B LYS   A 1 11  ? 8.588  -14.670 12.651  0.34 17.05 ?  11  LYS   A H    1 
ATOM   257  H  HA   A LYS   A 1 11  ? 11.163 -15.373 11.060  0.66 18.67 ?  11  LYS   A HA   1 
ATOM   258  H  HA   B LYS   A 1 11  ? 11.025 -15.000 11.612  0.34 17.00 ?  11  LYS   A HA   1 
ATOM   259  H  HB2  A LYS   A 1 11  ? 10.535 -16.450 13.049  0.66 18.29 ?  11  LYS   A HB2  1 
ATOM   260  H  HB2  B LYS   A 1 11  ? 10.421 -16.123 13.583  0.34 17.68 ?  11  LYS   A HB2  1 
ATOM   261  H  HB3  A LYS   A 1 11  ? 9.454  -17.287 12.248  0.66 18.29 ?  11  LYS   A HB3  1 
ATOM   262  H  HB3  B LYS   A 1 11  ? 9.310  -16.920 12.782  0.34 17.68 ?  11  LYS   A HB3  1 
ATOM   263  H  HG2  A LYS   A 1 11  ? 11.065 -18.544 11.240  0.66 18.69 ?  11  LYS   A HG2  1 
ATOM   264  H  HG2  B LYS   A 1 11  ? 10.906 -18.126 11.662  0.34 18.07 ?  11  LYS   A HG2  1 
ATOM   265  H  HG3  A LYS   A 1 11  ? 12.219 -17.587 11.787  0.66 18.69 ?  11  LYS   A HG3  1 
ATOM   266  H  HG3  B LYS   A 1 11  ? 12.067 -17.239 12.298  0.34 18.07 ?  11  LYS   A HG3  1 
ATOM   267  H  HD2  A LYS   A 1 11  ? 11.767 -18.281 13.967  0.66 19.25 ?  11  LYS   A HD2  1 
ATOM   268  H  HD2  B LYS   A 1 11  ? 11.541 -18.098 14.419  0.34 18.31 ?  11  LYS   A HD2  1 
ATOM   269  H  HD3  A LYS   A 1 11  ? 10.597 -19.216 13.435  0.66 19.25 ?  11  LYS   A HD3  1 
ATOM   270  H  HD3  B LYS   A 1 11  ? 10.406 -19.000 13.765  0.34 18.31 ?  11  LYS   A HD3  1 
ATOM   271  H  HE2  A LYS   A 1 11  ? 12.486 -20.491 13.891  0.66 19.64 ?  11  LYS   A HE2  1 
ATOM   272  H  HE2  B LYS   A 1 11  ? 12.283 -20.311 14.149  0.34 17.86 ?  11  LYS   A HE2  1 
ATOM   273  H  HE3  A LYS   A 1 11  ? 12.170 -20.538 12.331  0.66 19.64 ?  11  LYS   A HE3  1 
ATOM   274  H  HE3  B LYS   A 1 11  ? 12.062 -20.182 12.581  0.34 17.86 ?  11  LYS   A HE3  1 
ATOM   275  H  HZ1  A LYS   A 1 11  ? 14.383 -20.158 12.712  0.66 19.40 ?  11  LYS   A HZ1  1 
ATOM   276  H  HZ1  B LYS   A 1 11  ? 14.073 -19.116 14.036  0.34 17.51 ?  11  LYS   A HZ1  1 
ATOM   277  H  HZ2  A LYS   A 1 11  ? 13.817 -19.025 12.008  0.66 19.40 ?  11  LYS   A HZ2  1 
ATOM   278  H  HZ2  B LYS   A 1 11  ? 14.162 -19.746 12.737  0.34 17.51 ?  11  LYS   A HZ2  1 
ATOM   279  H  HZ3  A LYS   A 1 11  ? 14.088 -18.934 13.428  0.66 19.40 ?  11  LYS   A HZ3  1 
ATOM   280  H  HZ3  B LYS   A 1 11  ? 13.674 -18.388 12.848  0.34 17.51 ?  11  LYS   A HZ3  1 
ATOM   281  N  N    A LEU   A 1 12  ? 10.797 -16.202 8.774   0.66 14.99 ?  12  LEU   A N    1 
ATOM   282  N  N    B LEU   A 1 12  ? 10.658 -15.830 9.339   0.34 13.76 ?  12  LEU   A N    1 
ATOM   283  C  CA   A LEU   A 1 12  ? 10.533 -16.782 7.460   0.66 15.01 ?  12  LEU   A CA   1 
ATOM   284  C  CA   B LEU   A 1 12  ? 10.409 -16.324 7.988   0.34 14.43 ?  12  LEU   A CA   1 
ATOM   285  C  C    A LEU   A 1 12  ? 11.121 -18.179 7.306   0.66 14.90 ?  12  LEU   A C    1 
ATOM   286  C  C    B LEU   A 1 12  ? 10.953 -17.733 7.774   0.34 14.37 ?  12  LEU   A C    1 
ATOM   287  O  O    A LEU   A 1 12  ? 10.496 -19.043 6.684   0.66 14.90 ?  12  LEU   A O    1 
ATOM   288  O  O    B LEU   A 1 12  ? 10.253 -18.599 7.239   0.34 14.40 ?  12  LEU   A O    1 
ATOM   289  C  CB   A LEU   A 1 12  ? 11.082 -15.881 6.353   0.66 15.62 ?  12  LEU   A CB   1 
ATOM   290  C  CB   B LEU   A 1 12  ? 11.009 -15.368 6.946   0.34 15.49 ?  12  LEU   A CB   1 
ATOM   291  C  CG   A LEU   A 1 12  ? 10.428 -14.509 6.194   0.66 16.26 ?  12  LEU   A CG   1 
ATOM   292  C  CG   B LEU   A 1 12  ? 10.279 -14.048 6.710   0.34 16.31 ?  12  LEU   A CG   1 
ATOM   293  C  CD1  A LEU   A 1 12  ? 11.172 -13.696 5.150   0.66 16.97 ?  12  LEU   A CD1  1 
ATOM   294  C  CD1  B LEU   A 1 12  ? 10.701 -13.431 5.379   0.34 16.84 ?  12  LEU   A CD1  1 
ATOM   295  C  CD2  A LEU   A 1 12  ? 8.950  -14.663 5.833   0.66 16.53 ?  12  LEU   A CD2  1 
ATOM   296  C  CD2  B LEU   A 1 12  ? 8.777  -14.261 6.755   0.34 16.38 ?  12  LEU   A CD2  1 
ATOM   297  H  H    A LEU   A 1 12  ? 11.540 -15.766 8.840   0.66 18.05 ?  12  LEU   A H    1 
ATOM   298  H  H    B LEU   A 1 12  ? 11.420 -15.432 9.428   0.34 16.57 ?  12  LEU   A H    1 
ATOM   299  H  HA   A LEU   A 1 12  ? 9.578  -16.858 7.346   0.66 18.07 ?  12  LEU   A HA   1 
ATOM   300  H  HA   B LEU   A 1 12  ? 9.454  -16.370 7.846   0.34 17.37 ?  12  LEU   A HA   1 
ATOM   301  H  HB2  A LEU   A 1 12  ? 12.024 -15.733 6.526   0.66 18.80 ?  12  LEU   A HB2  1 
ATOM   302  H  HB2  B LEU   A 1 12  ? 11.914 -15.140 7.217   0.34 18.64 ?  12  LEU   A HB2  1 
ATOM   303  H  HB3  A LEU   A 1 12  ? 10.981 -16.353 5.512   0.66 18.80 ?  12  LEU   A HB3  1 
ATOM   304  H  HB3  B LEU   A 1 12  ? 11.041 -15.824 6.090   0.34 18.64 ?  12  LEU   A HB3  1 
ATOM   305  H  HG   A LEU   A 1 12  ? 10.476 -14.040 7.038   0.66 19.57 ?  12  LEU   A HG   1 
ATOM   306  H  HG   B LEU   A 1 12  ? 10.520 -13.424 7.413   0.34 19.63 ?  12  LEU   A HG   1 
ATOM   307  H  HD11 A LEU   A 1 12  ? 10.729 -12.841 5.041   0.66 20.42 ?  12  LEU   A HD11 1 
ATOM   308  H  HD11 B LEU   A 1 12  ? 10.232 -12.589 5.258   0.34 20.26 ?  12  LEU   A HD11 1 
ATOM   309  H  HD12 A LEU   A 1 12  ? 12.085 -13.560 5.450   0.66 20.42 ?  12  LEU   A HD12 1 
ATOM   310  H  HD12 B LEU   A 1 12  ? 11.658 -13.278 5.385   0.34 20.26 ?  12  LEU   A HD12 1 
ATOM   311  H  HD13 A LEU   A 1 12  ? 11.170 -14.179 4.308   0.66 20.42 ?  12  LEU   A HD13 1 
ATOM   312  H  HD13 B LEU   A 1 12  ? 10.469 -14.041 4.659   0.34 20.26 ?  12  LEU   A HD13 1 
ATOM   313  H  HD21 A LEU   A 1 12  ? 8.586  -13.794 5.608   0.66 19.89 ?  12  LEU   A HD21 1 
ATOM   314  H  HD21 B LEU   A 1 12  ? 8.339  -13.494 6.366   0.34 19.71 ?  12  LEU   A HD21 1 
ATOM   315  H  HD22 A LEU   A 1 12  ? 8.866  -15.264 5.074   0.66 19.89 ?  12  LEU   A HD22 1 
ATOM   316  H  HD22 B LEU   A 1 12  ? 8.559  -15.062 6.251   0.34 19.71 ?  12  LEU   A HD22 1 
ATOM   317  H  HD23 A LEU   A 1 12  ? 8.470  -15.033 6.595   0.66 19.89 ?  12  LEU   A HD23 1 
ATOM   318  H  HD23 B LEU   A 1 12  ? 8.504  -14.368 7.681   0.34 19.71 ?  12  LEU   A HD23 1 
ATOM   319  N  N    A THR   A 1 13  ? 12.320 -18.400 7.843   0.66 15.62 ?  13  THR   A N    1 
ATOM   320  N  N    B THR   A 1 13  ? 12.202 -17.970 8.159   0.34 14.39 ?  13  THR   A N    1 
ATOM   321  C  CA   A THR   A 1 13  ? 13.035 -19.673 7.757   0.66 16.31 ?  13  THR   A CA   1 
ATOM   322  C  CA   B THR   A 1 13  ? 12.828 -19.271 7.980   0.34 15.16 ?  13  THR   A CA   1 
ATOM   323  C  C    A THR   A 1 13  ? 13.808 -19.872 9.056   0.66 17.05 ?  13  THR   A C    1 
ATOM   324  C  C    B THR   A 1 13  ? 13.640 -19.596 9.226   0.34 15.87 ?  13  THR   A C    1 
ATOM   325  O  O    A THR   A 1 13  ? 13.705 -19.071 9.990   0.66 17.10 ?  13  THR   A O    1 
ATOM   326  O  O    B THR   A 1 13  ? 13.573 -18.907 10.249  0.34 15.74 ?  13  THR   A O    1 
ATOM   327  C  CB   A THR   A 1 13  ? 14.012 -19.721 6.573   0.66 16.86 ?  13  THR   A CB   1 
ATOM   328  C  CB   B THR   A 1 13  ? 13.754 -19.295 6.756   0.34 15.35 ?  13  THR   A CB   1 
ATOM   329  O  OG1  A THR   A 1 13  ? 15.078 -18.797 6.804   0.66 17.11 ?  13  THR   A OG1  1 
ATOM   330  O  OG1  B THR   A 1 13  ? 14.853 -18.407 6.982   0.34 15.57 ?  13  THR   A OG1  1 
ATOM   331  C  CG2  A THR   A 1 13  ? 13.326 -19.391 5.260   0.66 17.14 ?  13  THR   A CG2  1 
ATOM   332  C  CG2  B THR   A 1 13  ? 13.025 -18.900 5.479   0.34 14.77 ?  13  THR   A CG2  1 
ATOM   333  H  H    A THR   A 1 13  ? 12.764 -17.808 8.278   0.66 18.79 ?  13  THR   A H    1 
ATOM   334  H  H    B THR   A 1 13  ? 12.715 -17.377 8.518   0.34 17.32 ?  13  THR   A H    1 
ATOM   335  H  HA   A THR   A 1 13  ? 12.401 -20.405 7.658   0.66 19.63 ?  13  THR   A HA   1 
ATOM   336  H  HA   B THR   A 1 13  ? 12.139 -19.945 7.862   0.34 18.25 ?  13  THR   A HA   1 
ATOM   337  H  HB   A THR   A 1 13  ? 14.385 -20.613 6.500   0.66 20.29 ?  13  THR   A HB   1 
ATOM   338  H  HB   B THR   A 1 13  ? 14.093 -20.191 6.629   0.34 18.47 ?  13  THR   A HB   1 
ATOM   339  H  HG1  A THR   A 1 13  ? 15.617 -18.809 6.155   0.66 20.59 ?  13  THR   A HG1  1 
ATOM   340  H  HG1  B THR   A 1 13  ? 15.365 -18.409 6.315   0.34 18.74 ?  13  THR   A HG1  1 
ATOM   341  H  HG21 A THR   A 1 13  ? 13.917 -19.607 4.520   0.66 20.62 ?  13  THR   A HG21 1 
ATOM   342  H  HG21 B THR   A 1 13  ? 13.627 -18.973 4.719   0.34 17.78 ?  13  THR   A HG21 1 
ATOM   343  H  HG22 A THR   A 1 13  ? 12.516 -19.918 5.175   0.66 20.62 ?  13  THR   A HG22 1 
ATOM   344  H  HG22 B THR   A 1 13  ? 12.268 -19.490 5.334   0.34 17.78 ?  13  THR   A HG22 1 
ATOM   345  H  HG23 A THR   A 1 13  ? 13.102 -18.453 5.229   0.66 20.62 ?  13  THR   A HG23 1 
ATOM   346  H  HG23 B THR   A 1 13  ? 12.708 -17.988 5.543   0.34 17.78 ?  13  THR   A HG23 1 
ATOM   347  N  N    A ASP   A 1 14  ? 14.618 -20.934 9.104   0.66 17.53 ?  14  ASP   A N    1 
ATOM   348  N  N    B ASP   A 1 14  ? 14.427 -20.663 9.107   0.34 16.77 ?  14  ASP   A N    1 
ATOM   349  C  CA   A ASP   A 1 14  ? 15.433 -21.180 10.288  0.66 18.30 ?  14  ASP   A CA   1 
ATOM   350  C  CA   B ASP   A 1 14  ? 15.332 -21.067 10.172  0.34 17.31 ?  14  ASP   A CA   1 
ATOM   351  C  C    A ASP   A 1 14  ? 16.221 -19.938 10.692  0.66 17.91 ?  14  ASP   A C    1 
ATOM   352  C  C    B ASP   A 1 14  ? 16.295 -19.952 10.564  0.34 16.43 ?  14  ASP   A C    1 
ATOM   353  O  O    A ASP   A 1 14  ? 16.350 -19.636 11.886  0.66 18.23 ?  14  ASP   A O    1 
ATOM   354  O  O    B ASP   A 1 14  ? 16.731 -19.897 11.720  0.34 16.46 ?  14  ASP   A O    1 
ATOM   355  C  CB   A ASP   A 1 14  ? 16.396 -22.336 10.034  0.66 19.87 ?  14  ASP   A CB   1 
ATOM   356  C  CB   B ASP   A 1 14  ? 16.106 -22.310 9.730   0.34 18.85 ?  14  ASP   A CB   1 
ATOM   357  C  CG   A ASP   A 1 14  ? 17.274 -22.612 11.229  0.66 23.11 ?  14  ASP   A CG   1 
ATOM   358  C  CG   B ASP   A 1 14  ? 17.137 -22.745 10.753  0.34 20.60 ?  14  ASP   A CG   1 
ATOM   359  O  OD1  A ASP   A 1 14  ? 16.753 -23.120 12.249  0.66 25.01 ?  14  ASP   A OD1  1 
ATOM   360  O  OD1  B ASP   A 1 14  ? 16.756 -22.973 11.920  0.34 21.30 ?  14  ASP   A OD1  1 
ATOM   361  O  OD2  A ASP   A 1 14  ? 18.474 -22.294 11.153  0.66 25.18 -1 14  ASP   A OD2  1 
ATOM   362  O  OD2  B ASP   A 1 14  ? 18.325 -22.862 10.393  0.34 21.42 -1 14  ASP   A OD2  1 
ATOM   363  H  H    A ASP   A 1 14  ? 14.718 -21.523 8.478   0.66 21.09 ?  14  ASP   A H    1 
ATOM   364  H  H    B ASP   A 1 14  ? 14.439 -21.168 8.419   0.34 20.17 ?  14  ASP   A H    1 
ATOM   365  H  HA   A ASP   A 1 14  ? 14.863 -21.433 11.029  0.66 22.01 ?  14  ASP   A HA   1 
ATOM   366  H  HA   B ASP   A 1 14  ? 14.810 -21.297 10.955  0.34 20.83 ?  14  ASP   A HA   1 
ATOM   367  H  HB2  A ASP   A 1 14  ? 15.882 -23.143 9.836   0.66 23.89 ?  14  ASP   A HB2  1 
ATOM   368  H  HB2  B ASP   A 1 14  ? 15.474 -23.042 9.592   0.34 22.67 ?  14  ASP   A HB2  1 
ATOM   369  H  HB3  A ASP   A 1 14  ? 16.968 -22.123 9.281   0.66 23.89 ?  14  ASP   A HB3  1 
ATOM   370  H  HB3  B ASP   A 1 14  ? 16.563 -22.118 8.894   0.34 22.67 ?  14  ASP   A HB3  1 
ATOM   371  N  N    A ASN   A 1 15  ? 16.741 -19.193 9.711   0.66 17.81 ?  15  ASN   A N    1 
ATOM   372  N  N    B ASN   A 1 15  ? 16.628 -19.043 9.635   0.34 16.35 ?  15  ASN   A N    1 
ATOM   373  C  CA   A ASN   A 1 15  ? 17.694 -18.127 9.983   0.66 18.06 ?  15  ASN   A CA   1 
ATOM   374  C  CA   B ASN   A 1 15  ? 17.643 -18.030 9.911   0.34 16.22 ?  15  ASN   A CA   1 
ATOM   375  C  C    A ASN   A 1 15  ? 17.336 -16.762 9.394   0.66 18.08 ?  15  ASN   A C    1 
ATOM   376  C  C    B ASN   A 1 15  ? 17.249 -16.592 9.599   0.34 15.81 ?  15  ASN   A C    1 
ATOM   377  O  O    A ASN   A 1 15  ? 18.111 -15.820 9.587   0.66 19.31 ?  15  ASN   A O    1 
ATOM   378  O  O    B ASN   A 1 15  ? 18.026 -15.686 9.920   0.34 16.63 ?  15  ASN   A O    1 
ATOM   379  C  CB   A ASN   A 1 15  ? 19.086 -18.528 9.467   0.66 17.28 ?  15  ASN   A CB   1 
ATOM   380  C  CB   B ASN   A 1 15  ? 18.987 -18.363 9.222   0.34 15.83 ?  15  ASN   A CB   1 
ATOM   381  C  CG   A ASN   A 1 15  ? 19.120 -18.644 7.964   0.66 17.52 ?  15  ASN   A CG   1 
ATOM   382  C  CG   B ASN   A 1 15  ? 18.871 -18.488 7.707   0.34 15.73 ?  15  ASN   A CG   1 
ATOM   383  O  OD1  A ASN   A 1 15  ? 18.423 -19.481 7.379   0.66 18.18 ?  15  ASN   A OD1  1 
ATOM   384  O  OD1  B ASN   A 1 15  ? 18.079 -19.283 7.197   0.34 16.10 ?  15  ASN   A OD1  1 
ATOM   385  N  ND2  A ASN   A 1 15  ? 19.917 -17.796 7.323   0.66 18.15 ?  15  ASN   A ND2  1 
ATOM   386  N  ND2  B ASN   A 1 15  ? 19.671 -17.700 6.979   0.34 15.82 ?  15  ASN   A ND2  1 
ATOM   387  H  H    A ASN   A 1 15  ? 16.564 -19.301 8.880   0.66 21.43 ?  15  ASN   A H    1 
ATOM   388  H  H    B ASN   A 1 15  ? 16.266 -18.984 8.857   0.34 19.68 ?  15  ASN   A H    1 
ATOM   389  H  HA   A ASN   A 1 15  ? 17.776 -18.024 10.945  0.66 21.73 ?  15  ASN   A HA   1 
ATOM   390  H  HA   B ASN   A 1 15  ? 17.815 -18.037 10.860  0.34 19.52 ?  15  ASN   A HA   1 
ATOM   391  H  HB2  A ASN   A 1 15  ? 19.736 -17.848 9.732   0.66 20.80 ?  15  ASN   A HB2  1 
ATOM   392  H  HB2  B ASN   A 1 15  ? 19.624 -17.654 9.416   0.34 19.05 ?  15  ASN   A HB2  1 
ATOM   393  H  HB3  A ASN   A 1 15  ? 19.343 -19.385 9.843   0.66 20.80 ?  15  ASN   A HB3  1 
ATOM   394  H  HB3  B ASN   A 1 15  ? 19.312 -19.204 9.566   0.34 19.05 ?  15  ASN   A HB3  1 
ATOM   395  H  HD21 A ASN   A 1 15  ? 19.971 -17.823 6.465   0.66 21.83 ?  15  ASN   A HD21 1 
ATOM   396  H  HD21 B ASN   A 1 15  ? 19.648 -17.737 6.117   0.34 19.04 ?  15  ASN   A HD21 1 
ATOM   397  H  HD22 A ASN   A 1 15  ? 20.397 -17.231 7.763   0.66 21.83 ?  15  ASN   A HD22 1 
ATOM   398  H  HD22 B ASN   A 1 15  ? 20.221 -17.160 7.365   0.34 19.04 ?  15  ASN   A HD22 1 
ATOM   399  N  N    A VAL   A 1 16  ? 16.220 -16.620 8.672   0.66 16.86 ?  16  VAL   A N    1 
ATOM   400  N  N    B VAL   A 1 16  ? 16.071 -16.342 9.031   0.34 14.86 ?  16  VAL   A N    1 
ATOM   401  C  CA   A VAL   A 1 16  ? 15.815 -15.346 8.073   0.66 15.46 ?  16  VAL   A CA   1 
ATOM   402  C  CA   B VAL   A 1 16  ? 15.694 -15.018 8.546   0.34 13.85 ?  16  VAL   A CA   1 
ATOM   403  C  C    A VAL   A 1 16  ? 14.535 -14.841 8.728   0.66 14.99 ?  16  VAL   A C    1 
ATOM   404  C  C    B VAL   A 1 16  ? 14.460 -14.531 9.305   0.34 13.62 ?  16  VAL   A C    1 
ATOM   405  O  O    A VAL   A 1 16  ? 13.526 -15.555 8.792   0.66 14.48 ?  16  VAL   A O    1 
ATOM   406  O  O    B VAL   A 1 16  ? 13.484 -15.275 9.463   0.34 13.31 ?  16  VAL   A O    1 
ATOM   407  C  CB   A VAL   A 1 16  ? 15.645 -15.448 6.548   0.66 15.17 ?  16  VAL   A CB   1 
ATOM   408  C  CB   B VAL   A 1 16  ? 15.462 -15.022 7.022   0.34 13.87 ?  16  VAL   A CB   1 
ATOM   409  C  CG1  A VAL   A 1 16  ? 15.137 -14.123 5.978   0.66 15.97 ?  16  VAL   A CG1  1 
ATOM   410  C  CG1  B VAL   A 1 16  ? 15.239 -13.604 6.509   0.34 13.77 ?  16  VAL   A CG1  1 
ATOM   411  C  CG2  A VAL   A 1 16  ? 16.951 -15.855 5.891   0.66 16.04 ?  16  VAL   A CG2  1 
ATOM   412  C  CG2  B VAL   A 1 16  ? 16.631 -15.673 6.293   0.34 14.35 ?  16  VAL   A CG2  1 
ATOM   413  H  H    A VAL   A 1 16  ? 15.682 -17.276 8.513   0.66 20.28 ?  16  VAL   A H    1 
ATOM   414  H  H    B VAL   A 1 16  ? 15.453 -16.929 8.918   0.34 17.89 ?  16  VAL   A H    1 
ATOM   415  H  HA   A VAL   A 1 16  ? 16.515 -14.700 8.247   0.66 18.61 ?  16  VAL   A HA   1 
ATOM   416  H  HA   B VAL   A 1 16  ? 16.410 -14.391 8.726   0.34 16.68 ?  16  VAL   A HA   1 
ATOM   417  H  HB   A VAL   A 1 16  ? 14.989 -16.137 6.355   0.66 18.25 ?  16  VAL   A HB   1 
ATOM   418  H  HB   B VAL   A 1 16  ? 14.664 -15.531 6.822   0.34 16.70 ?  16  VAL   A HB   1 
ATOM   419  H  HG11 A VAL   A 1 16  ? 15.227 -14.146 5.014   0.66 19.22 ?  16  VAL   A HG11 1 
ATOM   420  H  HG11 B VAL   A 1 16  ? 15.254 -13.610 5.537   0.34 16.58 ?  16  VAL   A HG11 1 
ATOM   421  H  HG12 A VAL   A 1 16  ? 14.201 -14.018 6.218   0.66 19.22 ?  16  VAL   A HG12 1 
ATOM   422  H  HG12 B VAL   A 1 16  ? 14.378 -13.284 6.821   0.34 16.58 ?  16  VAL   A HG12 1 
ATOM   423  H  HG13 A VAL   A 1 16  ? 15.660 -13.400 6.346   0.66 19.22 ?  16  VAL   A HG13 1 
ATOM   424  H  HG13 B VAL   A 1 16  ? 15.945 -13.028 6.843   0.34 16.58 ?  16  VAL   A HG13 1 
ATOM   425  H  HG21 A VAL   A 1 16  ? 16.862 -15.749 4.932   0.66 19.30 ?  16  VAL   A HG21 1 
ATOM   426  H  HG21 B VAL   A 1 16  ? 16.523 -15.538 5.336   0.34 17.28 ?  16  VAL   A HG21 1 
ATOM   427  H  HG22 A VAL   A 1 16  ? 17.661 -15.286 6.223   0.66 19.30 ?  16  VAL   A HG22 1 
ATOM   428  H  HG22 B VAL   A 1 16  ? 17.457 -15.266 6.592   0.34 17.28 ?  16  VAL   A HG22 1 
ATOM   429  H  HG23 A VAL   A 1 16  ? 17.141 -16.781 6.108   0.66 19.30 ?  16  VAL   A HG23 1 
ATOM   430  H  HG23 B VAL   A 1 16  ? 16.635 -16.621 6.493   0.34 17.28 ?  16  VAL   A HG23 1 
ATOM   431  N  N    A TYR   A 1 17  ? 14.574 -13.578 9.149   0.66 14.24 ?  17  TYR   A N    1 
ATOM   432  N  N    B TYR   A 1 17  ? 14.519 -13.280 9.770   0.34 13.58 ?  17  TYR   A N    1 
ATOM   433  C  CA   A TYR   A 1 17  ? 13.500 -12.890 9.848   0.66 14.15 ?  17  TYR   A CA   1 
ATOM   434  C  CA   B TYR   A 1 17  ? 13.436 -12.611 10.480  0.34 13.27 ?  17  TYR   A CA   1 
ATOM   435  C  C    A TYR   A 1 17  ? 13.233 -11.565 9.139   0.66 14.27 ?  17  TYR   A C    1 
ATOM   436  C  C    B TYR   A 1 17  ? 13.181 -11.267 9.818   0.34 12.80 ?  17  TYR   A C    1 
ATOM   437  O  O    A TYR   A 1 17  ? 14.136 -11.001 8.514   0.66 14.41 ?  17  TYR   A O    1 
ATOM   438  O  O    B TYR   A 1 17  ? 14.094 -10.679 9.234   0.34 12.55 ?  17  TYR   A O    1 
ATOM   439  C  CB   A TYR   A 1 17  ? 13.927 -12.633 11.302  0.66 14.62 ?  17  TYR   A CB   1 
ATOM   440  C  CB   B TYR   A 1 17  ? 13.815 -12.385 11.945  0.34 14.03 ?  17  TYR   A CB   1 
ATOM   441  C  CG   A TYR   A 1 17  ? 14.143 -13.899 12.112  0.66 15.17 ?  17  TYR   A CG   1 
ATOM   442  C  CG   B TYR   A 1 17  ? 14.017 -13.664 12.720  0.34 14.87 ?  17  TYR   A CG   1 
ATOM   443  C  CD1  A TYR   A 1 17  ? 15.325 -14.635 12.020  0.66 15.78 ?  17  TYR   A CD1  1 
ATOM   444  C  CD1  B TYR   A 1 17  ? 15.201 -14.387 12.623  0.34 15.52 ?  17  TYR   A CD1  1 
ATOM   445  C  CD2  A TYR   A 1 17  ? 13.156 -14.369 12.965  0.66 15.51 ?  17  TYR   A CD2  1 
ATOM   446  C  CD2  B TYR   A 1 17  ? 13.016 -14.154 13.546  0.34 15.61 ?  17  TYR   A CD2  1 
ATOM   447  C  CE1  A TYR   A 1 17  ? 15.505 -15.802 12.759  0.66 16.25 ?  17  TYR   A CE1  1 
ATOM   448  C  CE1  B TYR   A 1 17  ? 15.380 -15.564 13.332  0.34 16.35 ?  17  TYR   A CE1  1 
ATOM   449  C  CE2  A TYR   A 1 17  ? 13.331 -15.522 13.707  0.66 15.74 ?  17  TYR   A CE2  1 
ATOM   450  C  CE2  B TYR   A 1 17  ? 13.184 -15.327 14.254  0.34 16.30 ?  17  TYR   A CE2  1 
ATOM   451  C  CZ   A TYR   A 1 17  ? 14.503 -16.236 13.599  0.66 16.24 ?  17  TYR   A CZ   1 
ATOM   452  C  CZ   B TYR   A 1 17  ? 14.365 -16.030 14.146  0.34 16.57 ?  17  TYR   A CZ   1 
ATOM   453  O  OH   A TYR   A 1 17  ? 14.675 -17.385 14.338  0.66 17.46 ?  17  TYR   A OH   1 
ATOM   454  O  OH   B TYR   A 1 17  ? 14.531 -17.196 14.858  0.34 17.22 ?  17  TYR   A OH   1 
ATOM   455  H  H    A TYR   A 1 17  ? 15.262 -13.076 9.028   0.66 17.15 ?  17  TYR   A H    1 
ATOM   456  H  H    B TYR   A 1 17  ? 15.211 -12.769 9.675   0.34 16.35 ?  17  TYR   A H    1 
ATOM   457  H  HA   A TYR   A 1 17  ? 12.702 -13.444 9.845   0.66 17.04 ?  17  TYR   A HA   1 
ATOM   458  H  HA   B TYR   A 1 17  ? 12.626 -13.134 10.433  0.34 15.98 ?  17  TYR   A HA   1 
ATOM   459  H  HB2  A TYR   A 1 17  ? 14.762 -12.145 11.307  0.66 17.59 ?  17  TYR   A HB2  1 
ATOM   460  H  HB2  B TYR   A 1 17  ? 14.645 -11.886 11.969  0.34 16.89 ?  17  TYR   A HB2  1 
ATOM   461  H  HB3  A TYR   A 1 17  ? 13.239 -12.126 11.746  0.66 17.59 ?  17  TYR   A HB3  1 
ATOM   462  H  HB3  B TYR   A 1 17  ? 13.113 -11.879 12.380  0.34 16.89 ?  17  TYR   A HB3  1 
ATOM   463  H  HD1  A TYR   A 1 17  ? 16.006 -14.351 11.459  0.66 18.99 ?  17  TYR   A HD1  1 
ATOM   464  H  HD1  B TYR   A 1 17  ? 15.884 -14.076 12.070  0.34 18.67 ?  17  TYR   A HD1  1 
ATOM   465  H  HD2  A TYR   A 1 17  ? 12.361 -13.905 13.050  0.66 18.67 ?  17  TYR   A HD2  1 
ATOM   466  H  HD2  B TYR   A 1 17  ? 12.217 -13.685 13.620  0.34 18.79 ?  17  TYR   A HD2  1 
ATOM   467  H  HE1  A TYR   A 1 17  ? 16.305 -16.288 12.702  0.66 19.56 ?  17  TYR   A HE1  1 
ATOM   468  H  HE1  B TYR   A 1 17  ? 16.178 -16.040 13.254  0.34 19.67 ?  17  TYR   A HE1  1 
ATOM   469  H  HE2  A TYR   A 1 17  ? 12.657 -15.824 14.281  0.66 18.95 ?  17  TYR   A HE2  1 
ATOM   470  H  HE2  B TYR   A 1 17  ? 12.504 -15.641 14.803  0.34 19.61 ?  17  TYR   A HE2  1 
ATOM   471  H  HH   A TYR   A 1 17  ? 13.990 -17.545 14.801  0.66 21.01 ?  17  TYR   A HH   1 
ATOM   472  H  HH   B TYR   A 1 17  ? 13.785 -17.547 15.005  0.34 20.72 ?  17  TYR   A HH   1 
ATOM   473  N  N    A ILE   A 1 18  ? 11.997 -11.056 9.242   0.66 14.07 ?  18  ILE   A N    1 
ATOM   474  N  N    B ILE   A 1 18  ? 11.947 -10.764 9.914   0.34 12.69 ?  18  ILE   A N    1 
ATOM   475  C  CA   A ILE   A 1 18  ? 11.601 -9.858  8.505   0.66 14.25 ?  18  ILE   A CA   1 
ATOM   476  C  CA   B ILE   A 1 18  ? 11.566 -9.553  9.192   0.34 12.48 ?  18  ILE   A CA   1 
ATOM   477  C  C    A ILE   A 1 18  ? 10.632 -9.009  9.323   0.66 14.56 ?  18  ILE   A C    1 
ATOM   478  C  C    B ILE   A 1 18  ? 10.644 -8.691  10.046  0.34 12.95 ?  18  ILE   A C    1 
ATOM   479  O  O    A ILE   A 1 18  ? 9.812  -9.529  10.084  0.66 15.06 ?  18  ILE   A O    1 
ATOM   480  O  O    B ILE   A 1 18  ? 9.804  -9.204  10.794  0.34 13.14 ?  18  ILE   A O    1 
ATOM   481  C  CB   A ILE   A 1 18  ? 11.023 -10.252 7.127   0.66 14.67 ?  18  ILE   A CB   1 
ATOM   482  C  CB   B ILE   A 1 18  ? 10.945 -9.883  7.817   0.34 12.15 ?  18  ILE   A CB   1 
ATOM   483  C  CG1  A ILE   A 1 18  ? 10.940 -9.046  6.196   0.66 14.81 ?  18  ILE   A CG1  1 
ATOM   484  C  CG1  B ILE   A 1 18  ? 10.918 -8.644  6.919   0.34 12.29 ?  18  ILE   A CG1  1 
ATOM   485  C  CG2  A ILE   A 1 18  ? 9.679  -10.947 7.292   0.66 14.78 ?  18  ILE   A CG2  1 
ATOM   486  C  CG2  B ILE   A 1 18  ? 9.548  -10.474 7.976   0.34 12.79 ?  18  ILE   A CG2  1 
ATOM   487  C  CD1  A ILE   A 1 18  ? 10.647 -9.428  4.757   0.66 16.50 ?  18  ILE   A CD1  1 
ATOM   488  C  CD1  B ILE   A 1 18  ? 10.673 -8.970  5.462   0.34 12.78 ?  18  ILE   A CD1  1 
ATOM   489  H  H    A ILE   A 1 18  ? 11.377 -11.406 9.737   0.66 16.94 ?  18  ILE   A H    1 
ATOM   490  H  H    B ILE   A 1 18  ? 11.312 -11.103 10.388  0.34 15.29 ?  18  ILE   A H    1 
ATOM   491  H  HA   A ILE   A 1 18  ? 12.401 -9.335  8.349   0.66 17.15 ?  18  ILE   A HA   1 
ATOM   492  H  HA   B ILE   A 1 18  ? 12.364 -9.029  9.025   0.34 15.04 ?  18  ILE   A HA   1 
ATOM   493  H  HB   A ILE   A 1 18  ? 11.630 -10.894 6.726   0.66 17.66 ?  18  ILE   A HB   1 
ATOM   494  H  HB   B ILE   A 1 18  ? 11.505 -10.544 7.392   0.34 14.64 ?  18  ILE   A HB   1 
ATOM   495  H  HG12 A ILE   A 1 18  ? 10.235 -8.459  6.503   0.66 17.82 ?  18  ILE   A HG12 1 
ATOM   496  H  HG12 B ILE   A 1 18  ? 10.208 -8.050  7.212   0.34 14.80 ?  18  ILE   A HG12 1 
ATOM   497  H  HG13 A ILE   A 1 18  ? 11.793 -8.581  6.214   0.66 17.82 ?  18  ILE   A HG13 1 
ATOM   498  H  HG13 B ILE   A 1 18  ? 11.773 -8.188  6.978   0.34 14.80 ?  18  ILE   A HG13 1 
ATOM   499  H  HG21 A ILE   A 1 18  ? 9.418  -11.337 6.441   0.66 17.79 ?  18  ILE   A HG21 1 
ATOM   500  H  HG21 B ILE   A 1 18  ? 9.269  -10.855 7.126   0.34 15.40 ?  18  ILE   A HG21 1 
ATOM   501  H  HG22 A ILE   A 1 18  ? 9.762  -11.648 7.960   0.66 17.79 ?  18  ILE   A HG22 1 
ATOM   502  H  HG22 B ILE   A 1 18  ? 9.574  -11.165 8.654   0.34 15.40 ?  18  ILE   A HG22 1 
ATOM   503  H  HG23 A ILE   A 1 18  ? 9.017  -10.299 7.576   0.66 17.79 ?  18  ILE   A HG23 1 
ATOM   504  H  HG23 B ILE   A 1 18  ? 8.930  -9.774  8.240   0.34 15.40 ?  18  ILE   A HG23 1 
ATOM   505  H  HD11 A ILE   A 1 18  ? 10.666 -8.626  4.209   0.66 19.86 ?  18  ILE   A HD11 1 
ATOM   506  H  HD11 B ILE   A 1 18  ? 10.626 -8.144  4.954   0.34 15.39 ?  18  ILE   A HD11 1 
ATOM   507  H  HD12 A ILE   A 1 18  ? 11.320 -10.054 4.450   0.66 19.86 ?  18  ILE   A HD12 1 
ATOM   508  H  HD12 B ILE   A 1 18  ? 11.402 -9.519  5.133   0.34 15.39 ?  18  ILE   A HD12 1 
ATOM   509  H  HD13 A ILE   A 1 18  ? 9.768  -9.837  4.711   0.66 19.86 ?  18  ILE   A HD13 1 
ATOM   510  H  HD13 B ILE   A 1 18  ? 9.834  -9.452  5.382   0.34 15.39 ?  18  ILE   A HD13 1 
ATOM   511  N  N    A LYS   A 1 19  ? 10.717 -7.688  9.141   0.66 15.19 ?  19  LYS   A N    1 
ATOM   512  N  N    B LYS   A 1 19  ? 10.817 -7.370  9.933   0.34 13.71 ?  19  LYS   A N    1 
ATOM   513  C  CA   A LYS   A 1 19  ? 9.913  -6.737  9.903   0.66 15.91 ?  19  LYS   A CA   1 
ATOM   514  C  CA   B LYS   A 1 19  ? 10.030 -6.388  10.669  0.34 15.24 ?  19  LYS   A CA   1 
ATOM   515  C  C    A LYS   A 1 19  ? 9.716  -5.463  9.088   0.66 16.67 ?  19  LYS   A C    1 
ATOM   516  C  C    B LYS   A 1 19  ? 9.804  -5.188  9.762   0.34 16.18 ?  19  LYS   A C    1 
ATOM   517  O  O    A LYS   A 1 19  ? 10.595 -5.066  8.317   0.66 16.14 ?  19  LYS   A O    1 
ATOM   518  O  O    B LYS   A 1 19  ? 10.745 -4.716  9.120   0.34 16.24 ?  19  LYS   A O    1 
ATOM   519  C  CB   A LYS   A 1 19  ? 10.621 -6.403  11.227  0.66 16.74 ?  19  LYS   A CB   1 
ATOM   520  C  CB   B LYS   A 1 19  ? 10.783 -5.949  11.933  0.34 15.78 ?  19  LYS   A CB   1 
ATOM   521  C  CG   A LYS   A 1 19  ? 9.885  -5.451  12.162  0.66 18.36 ?  19  LYS   A CG   1 
ATOM   522  C  CG   B LYS   A 1 19  ? 10.053 -4.968  12.839  0.34 16.95 ?  19  LYS   A CG   1 
ATOM   523  C  CD   A LYS   A 1 19  ? 10.749 -5.177  13.387  0.66 19.61 ?  19  LYS   A CD   1 
ATOM   524  C  CD   B LYS   A 1 19  ? 10.997 -4.484  13.929  0.34 17.79 ?  19  LYS   A CD   1 
ATOM   525  C  CE   A LYS   A 1 19  ? 10.099 -4.231  14.377  0.66 20.41 ?  19  LYS   A CE   1 
ATOM   526  C  CE   B LYS   A 1 19  ? 10.280 -3.809  15.082  0.34 18.50 ?  19  LYS   A CE   1 
ATOM   527  N  NZ   A LYS   A 1 19  ? 10.996 -3.999  15.549  0.66 21.26 ?  19  LYS   A NZ   1 
ATOM   528  N  NZ   B LYS   A 1 19  ? 11.154 -3.783  16.292  0.34 19.13 ?  19  LYS   A NZ   1 
ATOM   529  H  H    A LYS   A 1 19  ? 11.234 -7.326  8.569   0.66 18.28 ?  19  LYS   A H    1 
ATOM   530  H  H    B LYS   A 1 19  ? 11.419 -7.000  9.426   0.34 16.50 ?  19  LYS   A H    1 
ATOM   531  H  HA   A LYS   A 1 19  ? 9.047  -7.136  10.106  0.66 19.15 ?  19  LYS   A HA   1 
ATOM   532  H  HA   B LYS   A 1 19  ? 9.177  -6.762  10.925  0.34 18.34 ?  19  LYS   A HA   1 
ATOM   533  H  HB2  A LYS   A 1 19  ? 10.762 -7.232  11.722  0.66 20.15 ?  19  LYS   A HB2  1 
ATOM   534  H  HB2  B LYS   A 1 19  ? 10.972 -6.734  12.468  0.34 18.99 ?  19  LYS   A HB2  1 
ATOM   535  H  HB3  A LYS   A 1 19  ? 11.477 -6.004  11.024  0.66 20.15 ?  19  LYS   A HB3  1 
ATOM   536  H  HB3  B LYS   A 1 19  ? 11.618 -5.528  11.672  0.34 18.99 ?  19  LYS   A HB3  1 
ATOM   537  H  HG2  A LYS   A 1 19  ? 9.715  -4.611  11.710  0.66 22.08 ?  19  LYS   A HG2  1 
ATOM   538  H  HG2  B LYS   A 1 19  ? 9.758  -4.200  12.326  0.34 20.40 ?  19  LYS   A HG2  1 
ATOM   539  H  HG3  A LYS   A 1 19  ? 9.051  -5.855  12.458  0.66 22.08 ?  19  LYS   A HG3  1 
ATOM   540  H  HG3  B LYS   A 1 19  ? 9.299  -5.409  13.261  0.34 20.40 ?  19  LYS   A HG3  1 
ATOM   541  H  HD2  A LYS   A 1 19  ? 10.925 -6.015  13.846  0.66 23.59 ?  19  LYS   A HD2  1 
ATOM   542  H  HD2  B LYS   A 1 19  ? 11.475 -5.241  14.290  0.34 21.40 ?  19  LYS   A HD2  1 
ATOM   543  H  HD3  A LYS   A 1 19  ? 11.587 -4.779  13.100  0.66 23.59 ?  19  LYS   A HD3  1 
ATOM   544  H  HD3  B LYS   A 1 19  ? 11.618 -3.846  13.543  0.34 21.40 ?  19  LYS   A HD3  1 
ATOM   545  H  HE2  A LYS   A 1 19  ? 9.932  -3.377  13.949  0.66 24.54 ?  19  LYS   A HE2  1 
ATOM   546  H  HE2  B LYS   A 1 19  ? 10.064 -2.896  14.840  0.34 22.25 ?  19  LYS   A HE2  1 
ATOM   547  H  HE3  A LYS   A 1 19  ? 9.270  -4.617  14.700  0.66 24.54 ?  19  LYS   A HE3  1 
ATOM   548  H  HE3  B LYS   A 1 19  ? 9.475  -4.306  15.295  0.34 22.25 ?  19  LYS   A HE3  1 
ATOM   549  H  HZ1  A LYS   A 1 19  ? 10.606 -3.441  16.125  0.66 25.57 ?  19  LYS   A HZ1  1 
ATOM   550  H  HZ1  B LYS   A 1 19  ? 10.728 -3.390  16.965  0.34 23.01 ?  19  LYS   A HZ1  1 
ATOM   551  H  HZ2  A LYS   A 1 19  ? 11.161 -4.770  15.964  0.66 25.57 ?  19  LYS   A HZ2  1 
ATOM   552  H  HZ2  B LYS   A 1 19  ? 11.366 -4.616  16.530  0.34 23.01 ?  19  LYS   A HZ2  1 
ATOM   553  H  HZ3  A LYS   A 1 19  ? 11.765 -3.645  15.280  0.66 25.57 ?  19  LYS   A HZ3  1 
ATOM   554  H  HZ3  B LYS   A 1 19  ? 11.901 -3.334  16.117  0.34 23.01 ?  19  LYS   A HZ3  1 
ATOM   555  N  N    A ASN   A 1 20  ? 8.550  -4.832  9.254   0.66 18.96 ?  20  ASN   A N    1 
ATOM   556  N  N    B ASN   A 1 20  ? 8.563  -4.709  9.689   0.34 17.83 ?  20  ASN   A N    1 
ATOM   557  C  CA   A ASN   A 1 20  ? 8.320  -3.486  8.733   0.66 20.64 ?  20  ASN   A CA   1 
ATOM   558  C  CA   B ASN   A 1 20  ? 8.251  -3.498  8.928   0.34 18.76 ?  20  ASN   A CA   1 
ATOM   559  C  C    A ASN   A 1 20  ? 8.931  -2.498  9.721   0.66 21.28 ?  20  ASN   A C    1 
ATOM   560  C  C    B ASN   A 1 20  ? 8.806  -2.300  9.685   0.34 19.17 ?  20  ASN   A C    1 
ATOM   561  O  O    A ASN   A 1 20  ? 8.424  -2.322  10.832  0.66 21.59 ?  20  ASN   A O    1 
ATOM   562  O  O    B ASN   A 1 20  ? 8.168  -1.775  10.600  0.34 19.73 ?  20  ASN   A O    1 
ATOM   563  C  CB   A ASN   A 1 20  ? 6.828  -3.222  8.531   0.66 21.92 ?  20  ASN   A CB   1 
ATOM   564  C  CB   B ASN   A 1 20  ? 6.744  -3.376  8.727   0.34 19.30 ?  20  ASN   A CB   1 
ATOM   565  C  CG   A ASN   A 1 20  ? 6.527  -1.757  8.204   0.66 23.18 ?  20  ASN   A CG   1 
ATOM   566  C  CG   B ASN   A 1 20  ? 6.326  -2.041  8.119   0.34 20.14 ?  20  ASN   A CG   1 
ATOM   567  O  OD1  A ASN   A 1 20  ? 5.651  -1.140  8.817   0.66 25.49 ?  20  ASN   A OD1  1 
ATOM   568  O  OD1  B ASN   A 1 20  ? 5.245  -1.519  8.426   0.34 20.93 ?  20  ASN   A OD1  1 
ATOM   569  N  ND2  A ASN   A 1 20  ? 7.258  -1.196  7.243   0.66 23.64 ?  20  ASN   A ND2  1 
ATOM   570  N  ND2  B ASN   A 1 20  ? 7.171  -1.485  7.253   0.34 20.98 ?  20  ASN   A ND2  1 
ATOM   571  H  H    A ASN   A 1 20  ? 7.871  -5.178  9.667   0.66 22.81 ?  20  ASN   A H    1 
ATOM   572  H  H    B ASN   A 1 20  ? 7.882  -5.081  10.059  0.34 21.45 ?  20  ASN   A H    1 
ATOM   573  H  HA   A ASN   A 1 20  ? 8.768  -3.400  7.882   0.66 24.82 ?  20  ASN   A HA   1 
ATOM   574  H  HA   B ASN   A 1 20  ? 8.688  -3.542  8.063   0.34 22.57 ?  20  ASN   A HA   1 
ATOM   575  H  HB2  A ASN   A 1 20  ? 6.509  -3.770  7.793   0.66 26.36 ?  20  ASN   A HB2  1 
ATOM   576  H  HB2  B ASN   A 1 20  ? 6.449  -4.077  8.136   0.34 23.21 ?  20  ASN   A HB2  1 
ATOM   577  H  HB3  A ASN   A 1 20  ? 6.352  -3.458  9.343   0.66 26.36 ?  20  ASN   A HB3  1 
ATOM   578  H  HB3  B ASN   A 1 20  ? 6.311  -3.463  9.588   0.34 23.21 ?  20  ASN   A HB3  1 
ATOM   579  H  HD21 A ASN   A 1 20  ? 7.125  -0.377  7.026   0.66 28.42 ?  20  ASN   A HD21 1 
ATOM   580  H  HD21 B ASN   A 1 20  ? 6.983  -0.729  6.893   0.34 25.23 ?  20  ASN   A HD21 1 
ATOM   581  H  HD22 A ASN   A 1 20  ? 7.866  -1.656  6.841   0.66 28.42 ?  20  ASN   A HD22 1 
ATOM   582  H  HD22 B ASN   A 1 20  ? 7.914  -1.878  7.053   0.34 25.23 ?  20  ASN   A HD22 1 
ATOM   583  N  N    A ALA   A 1 21  ? 10.046 -1.880  9.342   0.66 21.42 ?  21  ALA   A N    1 
ATOM   584  N  N    B ALA   A 1 21  ? 10.005 -1.861  9.307   0.34 19.19 ?  21  ALA   A N    1 
ATOM   585  C  CA   A ALA   A 1 21  ? 10.734 -0.988  10.261  0.66 21.10 ?  21  ALA   A CA   1 
ATOM   586  C  CA   B ALA   A 1 21  ? 10.672 -0.795  10.040  0.34 18.97 ?  21  ALA   A CA   1 
ATOM   587  C  C    A ALA   A 1 21  ? 11.719 -0.122  9.494   0.66 20.98 ?  21  ALA   A C    1 
ATOM   588  C  C    B ALA   A 1 21  ? 11.749 -0.165  9.171   0.34 18.38 ?  21  ALA   A C    1 
ATOM   589  O  O    A ALA   A 1 21  ? 12.200 -0.505  8.425   0.66 21.77 ?  21  ALA   A O    1 
ATOM   590  O  O    B ALA   A 1 21  ? 12.192 -0.743  8.175   0.34 18.69 ?  21  ALA   A O    1 
ATOM   591  C  CB   A ALA   A 1 21  ? 11.472 -1.776  11.347  0.66 21.63 ?  21  ALA   A CB   1 
ATOM   592  C  CB   B ALA   A 1 21  ? 11.288 -1.312  11.346  0.34 19.54 ?  21  ALA   A CB   1 
ATOM   593  H  H    A ALA   A 1 21  ? 10.418 -1.968  8.573   0.66 25.76 ?  21  ALA   A H    1 
ATOM   594  H  H    B ALA   A 1 21  ? 10.444 -2.158  8.629   0.34 23.08 ?  21  ALA   A H    1 
ATOM   595  H  HA   A ALA   A 1 21  ? 10.085 -0.407  10.690  0.66 25.38 ?  21  ALA   A HA   1 
ATOM   596  H  HA   B ALA   A 1 21  ? 10.021 -0.113  10.264  0.34 22.81 ?  21  ALA   A HA   1 
ATOM   597  H  HB1  A ALA   A 1 21  ? 11.881 -1.150  11.962  0.66 26.02 ?  21  ALA   A HB1  1 
ATOM   598  H  HB1  B ALA   A 1 21  ? 11.730 -0.576  11.798  0.34 23.51 ?  21  ALA   A HB1  1 
ATOM   599  H  HB2  A ALA   A 1 21  ? 10.831 -2.333  11.820  0.66 26.02 ?  21  ALA   A HB2  1 
ATOM   600  H  HB2  B ALA   A 1 21  ? 10.583 -1.671  11.909  0.34 23.51 ?  21  ALA   A HB2  1 
ATOM   601  H  HB3  A ALA   A 1 21  ? 12.147 -2.330  10.931  0.66 26.02 ?  21  ALA   A HB3  1 
ATOM   602  H  HB3  B ALA   A 1 21  ? 11.932 -2.007  11.139  0.34 23.51 ?  21  ALA   A HB3  1 
ATOM   603  N  N    A ASP   A 1 22  ? 11.997 1.054   10.056  0.66 20.20 ?  22  ASP   A N    1 
ATOM   604  N  N    B ASP   A 1 22  ? 12.138 1.047   9.561   0.34 17.82 ?  22  ASP   A N    1 
ATOM   605  C  CA   A ASP   A 1 22  ? 13.050 1.932   9.562   0.66 19.74 ?  22  ASP   A CA   1 
ATOM   606  C  CA   B ASP   A 1 22  ? 13.315 1.714   9.020   0.34 17.64 ?  22  ASP   A CA   1 
ATOM   607  C  C    A ASP   A 1 22  ? 14.380 1.447   10.130  0.66 18.19 ?  22  ASP   A C    1 
ATOM   608  C  C    B ASP   A 1 22  ? 14.557 1.092   9.650   0.34 15.92 ?  22  ASP   A C    1 
ATOM   609  O  O    A ASP   A 1 22  ? 14.580 1.465   11.349  0.66 18.70 ?  22  ASP   A O    1 
ATOM   610  O  O    B ASP   A 1 22  ? 14.658 1.000   10.877  0.34 16.06 ?  22  ASP   A O    1 
ATOM   611  C  CB   A ASP   A 1 22  ? 12.762 3.366   10.007  0.66 21.70 ?  22  ASP   A CB   1 
ATOM   612  C  CB   B ASP   A 1 22  ? 13.240 3.203   9.377   0.34 19.06 ?  22  ASP   A CB   1 
ATOM   613  C  CG   A ASP   A 1 22  ? 13.796 4.369   9.498   0.66 23.22 ?  22  ASP   A CG   1 
ATOM   614  C  CG   B ASP   A 1 22  ? 14.357 4.030   8.765   0.34 20.19 ?  22  ASP   A CG   1 
ATOM   615  O  OD1  A ASP   A 1 22  ? 14.855 3.973   8.970   0.66 23.22 ?  22  ASP   A OD1  1 
ATOM   616  O  OD1  B ASP   A 1 22  ? 15.269 3.455   8.141   0.34 20.05 ?  22  ASP   A OD1  1 
ATOM   617  O  OD2  A ASP   A 1 22  ? 13.529 5.582   9.629   0.66 24.80 -1 22  ASP   A OD2  1 
ATOM   618  O  OD2  B ASP   A 1 22  ? 14.321 5.270   8.914   0.34 20.81 -1 22  ASP   A OD2  1 
ATOM   619  H  H    A ASP   A 1 22  ? 11.570 1.374   10.731  0.66 24.29 ?  22  ASP   A H    1 
ATOM   620  H  H    B ASP   A 1 22  ? 11.715 1.516   10.146  0.34 21.43 ?  22  ASP   A H    1 
ATOM   621  H  HA   A ASP   A 1 22  ? 13.086 1.902   8.593   0.66 23.74 ?  22  ASP   A HA   1 
ATOM   622  H  HA   B ASP   A 1 22  ? 13.348 1.608   8.054   0.34 21.22 ?  22  ASP   A HA   1 
ATOM   623  H  HB2  A ASP   A 1 22  ? 11.891 3.634   9.668   0.66 26.10 ?  22  ASP   A HB2  1 
ATOM   624  H  HB2  B ASP   A 1 22  ? 12.402 3.561   9.057   0.34 22.93 ?  22  ASP   A HB2  1 
ATOM   625  H  HB3  A ASP   A 1 22  ? 12.757 3.400   10.978  0.66 26.10 ?  22  ASP   A HB3  1 
ATOM   626  H  HB3  B ASP   A 1 22  ? 13.300 3.294   10.339  0.34 22.93 ?  22  ASP   A HB3  1 
ATOM   627  N  N    A ILE   A 1 23  ? 15.274 0.992   9.247   0.66 17.47 ?  23  ILE   A N    1 
ATOM   628  N  N    B ILE   A 1 23  ? 15.495 0.645   8.809   0.34 15.40 ?  23  ILE   A N    1 
ATOM   629  C  CA   A ILE   A 1 23  ? 16.540 0.406   9.685   0.66 16.53 ?  23  ILE   A CA   1 
ATOM   630  C  CA   B ILE   A 1 23  ? 16.717 0.017   9.305   0.34 14.75 ?  23  ILE   A CA   1 
ATOM   631  C  C    A ILE   A 1 23  ? 17.326 1.377   10.555  0.66 17.25 ?  23  ILE   A C    1 
ATOM   632  C  C    B ILE   A 1 23  ? 17.478 0.966   10.215  0.34 15.31 ?  23  ILE   A C    1 
ATOM   633  O  O    A ILE   A 1 23  ? 18.048 0.961   11.469  0.66 18.02 ?  23  ILE   A O    1 
ATOM   634  O  O    B ILE   A 1 23  ? 18.159 0.531   11.150  0.34 15.63 ?  23  ILE   A O    1 
ATOM   635  C  CB   A ILE   A 1 23  ? 17.346 -0.091  8.465   0.66 16.48 ?  23  ILE   A CB   1 
ATOM   636  C  CB   B ILE   A 1 23  ? 17.597 -0.495  8.143   0.34 14.48 ?  23  ILE   A CB   1 
ATOM   637  C  CG1  A ILE   A 1 23  ? 18.539 -0.940  8.919   0.66 16.54 ?  23  ILE   A CG1  1 
ATOM   638  C  CG1  B ILE   A 1 23  ? 18.695 -1.414  8.687   0.34 14.01 ?  23  ILE   A CG1  1 
ATOM   639  C  CG2  A ILE   A 1 23  ? 17.783 1.082   7.589   0.66 16.58 ?  23  ILE   A CG2  1 
ATOM   640  C  CG2  B ILE   A 1 23  ? 18.215 0.666   7.365   0.34 14.57 ?  23  ILE   A CG2  1 
ATOM   641  C  CD1  A ILE   A 1 23  ? 19.214 -1.703  7.796   0.66 16.77 ?  23  ILE   A CD1  1 
ATOM   642  C  CD1  B ILE   A 1 23  ? 19.531 -2.088  7.619   0.34 13.80 ?  23  ILE   A CD1  1 
ATOM   643  H  H    A ILE   A 1 23  ? 15.166 1.010   8.398   0.66 21.02 ?  23  ILE   A H    1 
ATOM   644  H  H    B ILE   A 1 23  ? 15.454 0.686   7.969   0.34 18.53 ?  23  ILE   A H    1 
ATOM   645  H  HA   A ILE   A 1 23  ? 16.345 -0.371  10.230  0.66 19.89 ?  23  ILE   A HA   1 
ATOM   646  H  HA   B ILE   A 1 23  ? 16.461 -0.753  9.833   0.34 17.75 ?  23  ILE   A HA   1 
ATOM   647  H  HB   A ILE   A 1 23  ? 16.764 -0.659  7.933   0.66 19.83 ?  23  ILE   A HB   1 
ATOM   648  H  HB   B ILE   A 1 23  ? 17.042 -1.009  7.538   0.34 17.44 ?  23  ILE   A HB   1 
ATOM   649  H  HG12 A ILE   A 1 23  ? 19.203 -0.361  9.320   0.66 19.90 ?  23  ILE   A HG12 1 
ATOM   650  H  HG12 B ILE   A 1 23  ? 19.294 -0.893  9.243   0.34 16.87 ?  23  ILE   A HG12 1 
ATOM   651  H  HG13 A ILE   A 1 23  ? 18.232 -1.591  9.569   0.66 19.90 ?  23  ILE   A HG13 1 
ATOM   652  H  HG13 B ILE   A 1 23  ? 18.280 -2.112  9.218   0.34 16.87 ?  23  ILE   A HG13 1 
ATOM   653  H  HG21 A ILE   A 1 23  ? 18.162 0.739   6.764   0.66 19.95 ?  23  ILE   A HG21 1 
ATOM   654  H  HG21 B ILE   A 1 23  ? 18.583 0.326   6.532   0.34 17.54 ?  23  ILE   A HG21 1 
ATOM   655  H  HG22 A ILE   A 1 23  ? 17.006 1.631   7.388   0.66 19.95 ?  23  ILE   A HG22 1 
ATOM   656  H  HG22 B ILE   A 1 23  ? 17.529 1.322   7.180   0.34 17.54 ?  23  ILE   A HG22 1 
ATOM   657  H  HG23 A ILE   A 1 23  ? 18.443 1.607   8.064   0.66 19.95 ?  23  ILE   A HG23 1 
ATOM   658  H  HG23 B ILE   A 1 23  ? 18.922 1.064   7.897   0.34 17.54 ?  23  ILE   A HG23 1 
ATOM   659  H  HD11 A ILE   A 1 23  ? 19.930 -2.241  8.165   0.66 20.18 ?  23  ILE   A HD11 1 
ATOM   660  H  HD11 B ILE   A 1 23  ? 20.144 -2.710  8.045   0.34 16.61 ?  23  ILE   A HD11 1 
ATOM   661  H  HD12 A ILE   A 1 23  ? 18.559 -2.273  7.363   0.66 20.18 ?  23  ILE   A HD12 1 
ATOM   662  H  HD12 B ILE   A 1 23  ? 18.944 -2.566  7.014   0.34 16.61 ?  23  ILE   A HD12 1 
ATOM   663  H  HD13 A ILE   A 1 23  ? 19.574 -1.067  7.156   0.66 20.18 ?  23  ILE   A HD13 1 
ATOM   664  H  HD13 B ILE   A 1 23  ? 20.030 -1.413  7.134   0.34 16.61 ?  23  ILE   A HD13 1 
ATOM   665  N  N    A VAL   A 1 24  ? 17.186 2.679   10.306  0.66 17.94 ?  24  VAL   A N    1 
ATOM   666  N  N    B VAL   A 1 24  ? 17.380 2.270   9.959   0.34 16.12 ?  24  VAL   A N    1 
ATOM   667  C  CA   A VAL   A 1 24  ? 17.867 3.674   11.132  0.66 19.31 ?  24  VAL   A CA   1 
ATOM   668  C  CA   B VAL   A 1 24  ? 18.039 3.248   10.817  0.34 17.29 ?  24  VAL   A CA   1 
ATOM   669  C  C    A VAL   A 1 24  ? 17.356 3.614   12.564  0.66 20.08 ?  24  VAL   A C    1 
ATOM   670  C  C    B VAL   A 1 24  ? 17.435 3.219   12.213  0.34 18.05 ?  24  VAL   A C    1 
ATOM   671  O  O    A VAL   A 1 24  ? 18.135 3.556   13.524  0.66 20.82 ?  24  VAL   A O    1 
ATOM   672  O  O    B VAL   A 1 24  ? 18.155 3.265   13.217  0.34 18.99 ?  24  VAL   A O    1 
ATOM   673  C  CB   A VAL   A 1 24  ? 17.684 5.078   10.531  0.66 19.62 ?  24  VAL   A CB   1 
ATOM   674  C  CB   B VAL   A 1 24  ? 17.965 4.644   10.174  0.34 17.78 ?  24  VAL   A CB   1 
ATOM   675  C  CG1  A VAL   A 1 24  ? 18.163 6.139   11.509  0.66 19.90 ?  24  VAL   A CG1  1 
ATOM   676  C  CG1  B VAL   A 1 24  ? 18.655 5.670   11.048  0.34 18.46 ?  24  VAL   A CG1  1 
ATOM   677  C  CG2  A VAL   A 1 24  ? 18.418 5.186   9.204   0.66 19.90 ?  24  VAL   A CG2  1 
ATOM   678  C  CG2  B VAL   A 1 24  ? 18.588 4.603   8.792   0.34 17.77 ?  24  VAL   A CG2  1 
ATOM   679  H  H    A VAL   A 1 24  ? 16.709 3.006   9.671   0.66 21.58 ?  24  VAL   A H    1 
ATOM   680  H  H    B VAL   A 1 24  ? 16.946 2.608   9.305   0.34 19.40 ?  24  VAL   A H    1 
ATOM   681  H  HA   A VAL   A 1 24  ? 18.818 3.477   11.141  0.66 23.22 ?  24  VAL   A HA   1 
ATOM   682  H  HA   B VAL   A 1 24  ? 18.975 3.012   10.902  0.34 20.80 ?  24  VAL   A HA   1 
ATOM   683  H  HB   A VAL   A 1 24  ? 16.742 5.229   10.359  0.66 23.60 ?  24  VAL   A HB   1 
ATOM   684  H  HB   B VAL   A 1 24  ? 17.035 4.903   10.078  0.34 21.39 ?  24  VAL   A HB   1 
ATOM   685  H  HG11 A VAL   A 1 24  ? 18.318 6.964   11.025  0.66 23.93 ?  24  VAL   A HG11 1 
ATOM   686  H  HG11 B VAL   A 1 24  ? 18.730 6.501   10.557  0.34 22.21 ?  24  VAL   A HG11 1 
ATOM   687  H  HG12 A VAL   A 1 24  ? 17.484 6.274   12.187  0.66 23.93 ?  24  VAL   A HG12 1 
ATOM   688  H  HG12 B VAL   A 1 24  ? 18.126 5.807   11.850  0.34 22.21 ?  24  VAL   A HG12 1 
ATOM   689  H  HG13 A VAL   A 1 24  ? 18.990 5.837   11.918  0.66 23.93 ?  24  VAL   A HG13 1 
ATOM   690  H  HG13 B VAL   A 1 24  ? 19.536 5.341   11.282  0.34 22.21 ?  24  VAL   A HG13 1 
ATOM   691  H  HG21 A VAL   A 1 24  ? 18.212 6.042   8.796   0.66 23.94 ?  24  VAL   A HG21 1 
ATOM   692  H  HG21 B VAL   A 1 24  ? 18.772 5.508   8.501   0.34 21.37 ?  24  VAL   A HG21 1 
ATOM   693  H  HG22 A VAL   A 1 24  ? 19.373 5.120   9.364   0.66 23.94 ?  24  VAL   A HG22 1 
ATOM   694  H  HG22 B VAL   A 1 24  ? 19.415 4.096   8.837   0.34 21.37 ?  24  VAL   A HG22 1 
ATOM   695  H  HG23 A VAL   A 1 24  ? 18.130 4.466   8.620   0.66 23.94 ?  24  VAL   A HG23 1 
ATOM   696  H  HG23 B VAL   A 1 24  ? 17.973 4.172   8.181   0.34 21.37 ?  24  VAL   A HG23 1 
ATOM   697  N  N    A GLU   A 1 25  ? 16.032 3.648   12.730  0.66 21.48 ?  25  GLU   A N    1 
ATOM   698  N  N    B GLU   A 1 25  ? 16.106 3.111   12.302  0.34 18.47 ?  25  GLU   A N    1 
ATOM   699  C  CA   A GLU   A 1 25  ? 15.460 3.588   14.068  0.66 23.08 ?  25  GLU   A CA   1 
ATOM   700  C  CA   B GLU   A 1 25  ? 15.462 3.044   13.609  0.34 19.46 ?  25  GLU   A CA   1 
ATOM   701  C  C    A GLU   A 1 25  ? 15.690 2.229   14.712  0.66 21.75 ?  25  GLU   A C    1 
ATOM   702  C  C    B GLU   A 1 25  ? 15.727 1.706   14.290  0.34 19.40 ?  25  GLU   A C    1 
ATOM   703  O  O    A GLU   A 1 25  ? 15.898 2.151   15.928  0.66 22.51 ?  25  GLU   A O    1 
ATOM   704  O  O    B GLU   A 1 25  ? 15.952 1.658   15.504  0.34 19.56 ?  25  GLU   A O    1 
ATOM   705  C  CB   A GLU   A 1 25  ? 13.969 3.928   14.018  0.66 24.95 ?  25  GLU   A CB   1 
ATOM   706  C  CB   B GLU   A 1 25  ? 13.963 3.327   13.480  0.34 20.63 ?  25  GLU   A CB   1 
ATOM   707  C  CG   A GLU   A 1 25  ? 13.695 5.380   13.651  0.66 27.45 ?  25  GLU   A CG   1 
ATOM   708  C  CG   B GLU   A 1 25  ? 13.653 4.758   13.064  0.34 22.28 ?  25  GLU   A CG   1 
ATOM   709  C  CD   A GLU   A 1 25  ? 14.492 6.364   14.494  0.66 29.55 ?  25  GLU   A CD   1 
ATOM   710  C  CD   B GLU   A 1 25  ? 14.200 5.771   14.045  0.34 23.76 ?  25  GLU   A CD   1 
ATOM   711  O  OE1  A GLU   A 1 25  ? 14.561 6.179   15.727  0.66 29.93 ?  25  GLU   A OE1  1 
ATOM   712  O  OE1  B GLU   A 1 25  ? 14.180 5.481   15.261  0.34 24.33 ?  25  GLU   A OE1  1 
ATOM   713  O  OE2  A GLU   A 1 25  ? 15.073 7.308   13.918  0.66 30.95 -1 25  GLU   A OE2  1 
ATOM   714  O  OE2  B GLU   A 1 25  ? 14.656 6.846   13.605  0.34 24.57 -1 25  GLU   A OE2  1 
ATOM   715  H  H    A GLU   A 1 25  ? 15.458 3.714   12.092  0.66 25.84 ?  25  GLU   A H    1 
ATOM   716  H  H    B GLU   A 1 25  ? 15.568 3.073   11.632  0.34 22.22 ?  25  GLU   A H    1 
ATOM   717  H  HA   A GLU   A 1 25  ? 15.900 4.244   14.625  0.66 27.75 ?  25  GLU   A HA   1 
ATOM   718  H  HA   B GLU   A 1 25  ? 15.842 3.730   14.175  0.34 23.41 ?  25  GLU   A HA   1 
ATOM   719  H  HB2  A GLU   A 1 25  ? 13.537 3.367   13.350  0.66 30.00 ?  25  GLU   A HB2  1 
ATOM   720  H  HB2  B GLU   A 1 25  ? 13.584 2.741   12.809  0.34 24.81 ?  25  GLU   A HB2  1 
ATOM   721  H  HB3  A GLU   A 1 25  ? 13.574 3.761   14.888  0.66 30.00 ?  25  GLU   A HB3  1 
ATOM   722  H  HB3  B GLU   A 1 25  ? 13.535 3.172   14.337  0.34 24.81 ?  25  GLU   A HB3  1 
ATOM   723  H  HG2  A GLU   A 1 25  ? 13.949 5.522   12.729  0.66 33.00 ?  25  GLU   A HG2  1 
ATOM   724  H  HG2  B GLU   A 1 25  ? 14.045 4.932   12.193  0.34 26.79 ?  25  GLU   A HG2  1 
ATOM   725  H  HG3  A GLU   A 1 25  ? 12.747 5.557   13.768  0.66 33.00 ?  25  GLU   A HG3  1 
ATOM   726  H  HG3  B GLU   A 1 25  ? 12.694 4.886   13.030  0.34 26.79 ?  25  GLU   A HG3  1 
ATOM   727  N  N    A GLU   A 1 26  ? 15.669 1.156   13.918  0.66 20.96 ?  26  GLU   A N    1 
ATOM   728  N  N    B GLU   A 1 26  ? 15.715 0.609   13.530  0.34 19.54 ?  26  GLU   A N    1 
ATOM   729  C  CA   A GLU   A 1 26  ? 15.974 -0.168  14.453  0.66 21.24 ?  26  GLU   A CA   1 
ATOM   730  C  CA   B GLU   A 1 26  ? 16.121 -0.671  14.100  0.34 19.76 ?  26  GLU   A CA   1 
ATOM   731  C  C    A GLU   A 1 26  ? 17.395 -0.219  15.002  0.66 20.22 ?  26  GLU   A C    1 
ATOM   732  C  C    B GLU   A 1 26  ? 17.549 -0.599  14.621  0.34 19.29 ?  26  GLU   A C    1 
ATOM   733  O  O    A GLU   A 1 26  ? 17.625 -0.692  16.121  0.66 20.00 ?  26  GLU   A O    1 
ATOM   734  O  O    B GLU   A 1 26  ? 17.871 -1.183  15.662  0.34 18.98 ?  26  GLU   A O    1 
ATOM   735  C  CB   A GLU   A 1 26  ? 15.801 -1.229  13.364  0.66 23.09 ?  26  GLU   A CB   1 
ATOM   736  C  CB   B GLU   A 1 26  ? 15.983 -1.783  13.059  0.34 20.61 ?  26  GLU   A CB   1 
ATOM   737  C  CG   A GLU   A 1 26  ? 14.406 -1.800  13.220  0.66 25.46 ?  26  GLU   A CG   1 
ATOM   738  C  CG   B GLU   A 1 26  ? 14.553 -2.210  12.815  0.34 21.12 ?  26  GLU   A CG   1 
ATOM   739  C  CD   A GLU   A 1 26  ? 13.965 -2.575  14.453  0.66 27.35 ?  26  GLU   A CD   1 
ATOM   740  C  CD   B GLU   A 1 26  ? 13.897 -2.793  14.053  0.34 21.55 ?  26  GLU   A CD   1 
ATOM   741  O  OE1  A GLU   A 1 26  ? 14.472 -3.696  14.690  0.66 28.53 ?  26  GLU   A OE1  1 
ATOM   742  O  OE1  B GLU   A 1 26  ? 14.328 -3.876  14.521  0.34 22.33 ?  26  GLU   A OE1  1 
ATOM   743  O  OE2  A GLU   A 1 26  ? 13.116 -2.047  15.194  0.66 28.16 -1 26  GLU   A OE2  1 
ATOM   744  O  OE2  B GLU   A 1 26  ? 12.937 -2.173  14.551  0.34 21.10 -1 26  GLU   A OE2  1 
ATOM   745  H  H    A GLU   A 1 26  ? 15.481 1.173   13.079  0.66 25.20 ?  26  GLU   A H    1 
ATOM   746  H  H    B GLU   A 1 26  ? 15.483 0.580   12.703  0.34 23.50 ?  26  GLU   A H    1 
ATOM   747  H  HA   A GLU   A 1 26  ? 15.359 -0.367  15.176  0.66 25.54 ?  26  GLU   A HA   1 
ATOM   748  H  HA   B GLU   A 1 26  ? 15.546 -0.883  14.849  0.34 23.76 ?  26  GLU   A HA   1 
ATOM   749  H  HB2  A GLU   A 1 26  ? 16.045 -0.839  12.512  0.66 27.76 ?  26  GLU   A HB2  1 
ATOM   750  H  HB2  B GLU   A 1 26  ? 16.345 -1.472  12.214  0.34 24.79 ?  26  GLU   A HB2  1 
ATOM   751  H  HB3  A GLU   A 1 26  ? 16.398 -1.968  13.564  0.66 27.76 ?  26  GLU   A HB3  1 
ATOM   752  H  HB3  B GLU   A 1 26  ? 16.475 -2.563  13.360  0.34 24.79 ?  26  GLU   A HB3  1 
ATOM   753  H  HG2  A GLU   A 1 26  ? 13.780 -1.073  13.091  0.66 30.60 ?  26  GLU   A HG2  1 
ATOM   754  H  HG2  B GLU   A 1 26  ? 14.039 -1.439  12.520  0.34 25.40 ?  26  GLU   A HG2  1 
ATOM   755  H  HG3  A GLU   A 1 26  ? 14.383 -2.392  12.446  0.66 30.60 ?  26  GLU   A HG3  1 
ATOM   756  H  HG3  B GLU   A 1 26  ? 14.534 -2.902  12.141  0.34 25.40 ?  26  GLU   A HG3  1 
ATOM   757  N  N    A ALA   A 1 27  ? 18.367 0.258   14.218  0.66 19.69 ?  27  ALA   A N    1 
ATOM   758  N  N    B ALA   A 1 27  ? 18.419 0.122   13.915  0.34 19.13 ?  27  ALA   A N    1 
ATOM   759  C  CA   A ALA   A 1 27  ? 19.761 0.186   14.650  0.66 19.88 ?  27  ALA   A CA   1 
ATOM   760  C  CA   B ALA   A 1 27  ? 19.791 0.277   14.385  0.34 19.55 ?  27  ALA   A CA   1 
ATOM   761  C  C    A ALA   A 1 27  ? 19.983 0.981   15.930  0.66 21.19 ?  27  ALA   A C    1 
ATOM   762  C  C    B ALA   A 1 27  ? 19.851 1.162   15.626  0.34 20.66 ?  27  ALA   A C    1 
ATOM   763  O  O    A ALA   A 1 27  ? 20.667 0.515   16.849  0.66 21.68 ?  27  ALA   A O    1 
ATOM   764  O  O    B ALA   A 1 27  ? 20.520 0.821   16.608  0.34 21.01 ?  27  ALA   A O    1 
ATOM   765  C  CB   A ALA   A 1 27  ? 20.694 0.683   13.542  0.66 19.22 ?  27  ALA   A CB   1 
ATOM   766  C  CB   B ALA   A 1 27  ? 20.670 0.841   13.268  0.34 19.15 ?  27  ALA   A CB   1 
ATOM   767  H  H    A ALA   A 1 27  ? 18.245 0.621   13.448  0.66 23.69 ?  27  ALA   A H    1 
ATOM   768  H  H    B ALA   A 1 27  ? 18.243 0.516   13.170  0.34 23.01 ?  27  ALA   A H    1 
ATOM   769  H  HA   A ALA   A 1 27  ? 19.982 -0.740  14.829  0.66 23.91 ?  27  ALA   A HA   1 
ATOM   770  H  HA   B ALA   A 1 27  ? 20.138 -0.594  14.623  0.34 23.52 ?  27  ALA   A HA   1 
ATOM   771  H  HB1  A ALA   A 1 27  ? 21.612 0.622   13.852  0.66 23.12 ?  27  ALA   A HB1  1 
ATOM   772  H  HB1  B ALA   A 1 27  ? 21.580 0.910   13.595  0.34 23.03 ?  27  ALA   A HB1  1 
ATOM   773  H  HB2  A ALA   A 1 27  ? 20.575 0.126   12.755  0.66 23.12 ?  27  ALA   A HB2  1 
ATOM   774  H  HB2  B ALA   A 1 27  ? 20.637 0.240   12.508  0.34 23.03 ?  27  ALA   A HB2  1 
ATOM   775  H  HB3  A ALA   A 1 27  ? 20.476 1.603   13.332  0.66 23.12 ?  27  ALA   A HB3  1 
ATOM   776  H  HB3  B ALA   A 1 27  ? 20.339 1.716   13.015  0.34 23.03 ?  27  ALA   A HB3  1 
ATOM   777  N  N    A LYS   A 1 28  ? 19.403 2.179   16.015  0.66 23.13 ?  28  LYS   A N    1 
ATOM   778  N  N    B LYS   A 1 28  ? 19.142 2.295   15.610  0.34 21.98 ?  28  LYS   A N    1 
ATOM   779  C  CA   A LYS   A 1 28  ? 19.542 2.975   17.230  0.66 25.25 ?  28  LYS   A CA   1 
ATOM   780  C  CA   B LYS   A 1 28  ? 19.237 3.244   16.715  0.34 23.65 ?  28  LYS   A CA   1 
ATOM   781  C  C    A LYS   A 1 28  ? 18.965 2.243   18.434  0.66 26.34 ?  28  LYS   A C    1 
ATOM   782  C  C    B LYS   A 1 28  ? 18.832 2.633   18.050  0.34 24.90 ?  28  LYS   A C    1 
ATOM   783  O  O    A LYS   A 1 28  ? 19.539 2.286   19.529  0.66 27.09 ?  28  LYS   A O    1 
ATOM   784  O  O    B LYS   A 1 28  ? 19.279 3.114   19.096  0.34 24.97 ?  28  LYS   A O    1 
ATOM   785  C  CB   A LYS   A 1 28  ? 18.883 4.344   17.044  0.66 26.83 ?  28  LYS   A CB   1 
ATOM   786  C  CB   B LYS   A 1 28  ? 18.377 4.482   16.445  0.34 24.33 ?  28  LYS   A CB   1 
ATOM   787  C  CG   A LYS   A 1 28  ? 19.682 5.282   16.151  0.66 28.34 ?  28  LYS   A CG   1 
ATOM   788  C  CG   B LYS   A 1 28  ? 18.926 5.414   15.379  0.34 25.16 ?  28  LYS   A CG   1 
ATOM   789  C  CD   A LYS   A 1 28  ? 19.171 6.713   16.209  0.66 29.76 ?  28  LYS   A CD   1 
ATOM   790  C  CD   B LYS   A 1 28  ? 18.295 6.794   15.484  0.34 25.89 ?  28  LYS   A CD   1 
ATOM   791  C  CE   A LYS   A 1 28  ? 17.874 6.870   15.440  0.66 30.68 ?  28  LYS   A CE   1 
ATOM   792  C  CE   B LYS   A 1 28  ? 18.305 7.519   14.147  0.34 26.40 ?  28  LYS   A CE   1 
ATOM   793  N  NZ   A LYS   A 1 28  ? 17.438 8.293   15.390  0.66 31.04 ?  28  LYS   A NZ   1 
ATOM   794  N  NZ   B LYS   A 1 28  ? 18.173 8.996   14.307  0.34 26.76 ?  28  LYS   A NZ   1 
ATOM   795  H  H    A LYS   A 1 28  ? 18.933 2.541   15.400  0.66 27.82 ?  28  LYS   A H    1 
ATOM   796  H  H    B LYS   A 1 28  ? 18.600 2.530   14.985  0.34 26.43 ?  28  LYS   A H    1 
ATOM   797  H  HA   A LYS   A 1 28  ? 20.482 3.121   17.406  0.66 30.36 ?  28  LYS   A HA   1 
ATOM   798  H  HA   B LYS   A 1 28  ? 20.155 3.539   16.794  0.34 28.44 ?  28  LYS   A HA   1 
ATOM   799  H  HB2  A LYS   A 1 28  ? 18.011 4.222   16.638  0.66 32.25 ?  28  LYS   A HB2  1 
ATOM   800  H  HB2  B LYS   A 1 28  ? 17.498 4.193   16.155  0.34 29.25 ?  28  LYS   A HB2  1 
ATOM   801  H  HB3  A LYS   A 1 28  ? 18.788 4.770   17.909  0.66 32.25 ?  28  LYS   A HB3  1 
ATOM   802  H  HB3  B LYS   A 1 28  ? 18.298 4.993   17.266  0.34 29.25 ?  28  LYS   A HB3  1 
ATOM   803  H  HG2  A LYS   A 1 28  ? 20.608 5.282   16.437  0.66 34.07 ?  28  LYS   A HG2  1 
ATOM   804  H  HG2  B LYS   A 1 28  ? 19.884 5.506   15.496  0.34 30.25 ?  28  LYS   A HG2  1 
ATOM   805  H  HG3  A LYS   A 1 28  ? 19.616 4.978   15.232  0.66 34.07 ?  28  LYS   A HG3  1 
ATOM   806  H  HG3  B LYS   A 1 28  ? 18.728 5.060   14.500  0.34 30.25 ?  28  LYS   A HG3  1 
ATOM   807  H  HD2  A LYS   A 1 28  ? 19.008 6.958   17.133  0.66 35.76 ?  28  LYS   A HD2  1 
ATOM   808  H  HD2  B LYS   A 1 28  ? 17.374 6.703   15.774  0.34 31.12 ?  28  LYS   A HD2  1 
ATOM   809  H  HD3  A LYS   A 1 28  ? 19.832 7.305   15.816  0.66 35.76 ?  28  LYS   A HD3  1 
ATOM   810  H  HD3  B LYS   A 1 28  ? 18.797 7.327   16.121  0.34 31.12 ?  28  LYS   A HD3  1 
ATOM   811  H  HE2  A LYS   A 1 28  ? 18.003 6.560   14.530  0.66 36.87 ?  28  LYS   A HE2  1 
ATOM   812  H  HE2  B LYS   A 1 28  ? 19.140 7.337   13.691  0.34 31.73 ?  28  LYS   A HE2  1 
ATOM   813  H  HE3  A LYS   A 1 28  ? 17.179 6.355   15.876  0.66 36.87 ?  28  LYS   A HE3  1 
ATOM   814  H  HE3  B LYS   A 1 28  ? 17.556 7.207   13.612  0.34 31.73 ?  28  LYS   A HE3  1 
ATOM   815  H  HZ1  A LYS   A 1 28  ? 16.678 8.363   14.934  0.66 37.31 ?  28  LYS   A HZ1  1 
ATOM   816  H  HZ1  B LYS   A 1 28  ? 18.181 9.390   13.509  0.34 32.17 ?  28  LYS   A HZ1  1 
ATOM   817  H  HZ2  A LYS   A 1 28  ? 17.311 8.602   16.215  0.66 37.31 ?  28  LYS   A HZ2  1 
ATOM   818  H  HZ2  B LYS   A 1 28  ? 17.408 9.191   14.718  0.34 32.17 ?  28  LYS   A HZ2  1 
ATOM   819  H  HZ3  A LYS   A 1 28  ? 18.061 8.789   14.990  0.66 37.31 ?  28  LYS   A HZ3  1 
ATOM   820  H  HZ3  B LYS   A 1 28  ? 18.850 9.310   14.791  0.34 32.17 ?  28  LYS   A HZ3  1 
ATOM   821  N  N    A LYS   A 1 29  ? 17.841 1.548   18.248  0.66 27.18 ?  29  LYS   A N    1 
ATOM   822  N  N    B LYS   A 1 29  ? 18.000 1.592   18.042  0.34 26.38 ?  29  LYS   A N    1 
ATOM   823  C  CA   A LYS   A 1 29  ? 17.221 0.828   19.357  0.66 28.83 ?  29  LYS   A CA   1 
ATOM   824  C  CA   B LYS   A 1 29  ? 17.500 0.984   19.270  0.34 28.13 ?  29  LYS   A CA   1 
ATOM   825  C  C    A LYS   A 1 29  ? 18.023 -0.415  19.726  0.66 28.37 ?  29  LYS   A C    1 
ATOM   826  C  C    B LYS   A 1 29  ? 18.276 -0.270  19.657  0.34 28.14 ?  29  LYS   A C    1 
ATOM   827  O  O    A LYS   A 1 29  ? 18.291 -0.664  20.908  0.66 28.80 ?  29  LYS   A O    1 
ATOM   828  O  O    B LYS   A 1 29  ? 18.760 -0.381  20.787  0.34 28.76 ?  29  LYS   A O    1 
ATOM   829  C  CB   A LYS   A 1 29  ? 15.785 0.443   18.994  0.66 31.12 ?  29  LYS   A CB   1 
ATOM   830  C  CB   B LYS   A 1 29  ? 16.012 0.647   19.104  0.34 29.89 ?  29  LYS   A CB   1 
ATOM   831  C  CG   A LYS   A 1 29  ? 15.038 -0.279  20.107  0.66 33.39 ?  29  LYS   A CG   1 
ATOM   832  C  CG   B LYS   A 1 29  ? 15.359 0.041   20.337  0.34 31.31 ?  29  LYS   A CG   1 
ATOM   833  C  CD   A LYS   A 1 29  ? 14.745 0.654   21.271  0.66 35.35 ?  29  LYS   A CD   1 
ATOM   834  C  CD   B LYS   A 1 29  ? 15.115 1.089   21.409  0.34 32.58 ?  29  LYS   A CD   1 
ATOM   835  C  CE   A LYS   A 1 29  ? 13.869 -0.016  22.317  0.66 36.68 ?  29  LYS   A CE   1 
ATOM   836  C  CE   B LYS   A 1 29  ? 14.325 0.510   22.571  0.34 33.39 ?  29  LYS   A CE   1 
ATOM   837  N  NZ   A LYS   A 1 29  ? 13.457 0.938   23.384  0.66 37.32 ?  29  LYS   A NZ   1 
ATOM   838  N  NZ   B LYS   A 1 29  ? 13.986 1.549   23.581  0.34 33.79 ?  29  LYS   A NZ   1 
ATOM   839  H  H    A LYS   A 1 29  ? 17.420 1.483   17.501  0.66 32.67 ?  29  LYS   A H    1 
ATOM   840  H  H    B LYS   A 1 29  ? 17.706 1.213   17.325  0.34 31.71 ?  29  LYS   A H    1 
ATOM   841  H  HA   A LYS   A 1 29  ? 17.187 1.407   20.134  0.66 34.66 ?  29  LYS   A HA   1 
ATOM   842  H  HA   B LYS   A 1 29  ? 17.582 1.622   19.995  0.34 33.81 ?  29  LYS   A HA   1 
ATOM   843  H  HB2  A LYS   A 1 29  ? 15.286 1.247   18.783  0.66 37.39 ?  29  LYS   A HB2  1 
ATOM   844  H  HB2  B LYS   A 1 29  ? 15.530 1.464   18.891  0.34 35.92 ?  29  LYS   A HB2  1 
ATOM   845  H  HB3  A LYS   A 1 29  ? 15.802 -0.146  18.224  0.66 37.39 ?  29  LYS   A HB3  1 
ATOM   846  H  HB3  B LYS   A 1 29  ? 15.914 0.013   18.378  0.34 35.92 ?  29  LYS   A HB3  1 
ATOM   847  H  HG2  A LYS   A 1 29  ? 14.193 -0.607  19.764  0.66 40.13 ?  29  LYS   A HG2  1 
ATOM   848  H  HG2  B LYS   A 1 29  ? 14.504 -0.339  20.086  0.34 37.63 ?  29  LYS   A HG2  1 
ATOM   849  H  HG3  A LYS   A 1 29  ? 15.573 -1.019  20.437  0.66 40.13 ?  29  LYS   A HG3  1 
ATOM   850  H  HG3  B LYS   A 1 29  ? 15.933 -0.648  20.708  0.34 37.63 ?  29  LYS   A HG3  1 
ATOM   851  H  HD2  A LYS   A 1 29  ? 15.580 0.912   21.694  0.66 42.47 ?  29  LYS   A HD2  1 
ATOM   852  H  HD2  B LYS   A 1 29  ? 15.966 1.408   21.748  0.34 39.16 ?  29  LYS   A HD2  1 
ATOM   853  H  HD3  A LYS   A 1 29  ? 14.281 1.440   20.942  0.66 42.47 ?  29  LYS   A HD3  1 
ATOM   854  H  HD3  B LYS   A 1 29  ? 14.606 1.823   21.031  0.34 39.16 ?  29  LYS   A HD3  1 
ATOM   855  H  HE2  A LYS   A 1 29  ? 13.068 -0.358  21.890  0.66 44.07 ?  29  LYS   A HE2  1 
ATOM   856  H  HE2  B LYS   A 1 29  ? 13.497 0.130   22.237  0.34 40.12 ?  29  LYS   A HE2  1 
ATOM   857  H  HE3  A LYS   A 1 29  ? 14.364 -0.740  22.732  0.66 44.07 ?  29  LYS   A HE3  1 
ATOM   858  H  HE3  B LYS   A 1 29  ? 14.855 -0.176  23.007  0.34 40.12 ?  29  LYS   A HE3  1 
ATOM   859  H  HZ1  A LYS   A 1 29  ? 12.946 0.524   23.983  0.66 44.84 ?  29  LYS   A HZ1  1 
ATOM   860  H  HZ1  B LYS   A 1 29  ? 13.184 1.383   23.929  0.34 40.61 ?  29  LYS   A HZ1  1 
ATOM   861  H  HZ2  A LYS   A 1 29  ? 14.176 1.265   23.794  0.66 44.84 ?  29  LYS   A HZ2  1 
ATOM   862  H  HZ2  B LYS   A 1 29  ? 14.589 1.546   24.234  0.34 40.61 ?  29  LYS   A HZ2  1 
ATOM   863  H  HZ3  A LYS   A 1 29  ? 12.997 1.612   23.028  0.66 44.84 ?  29  LYS   A HZ3  1 
ATOM   864  H  HZ3  B LYS   A 1 29  ? 13.973 2.352   23.198  0.34 40.61 ?  29  LYS   A HZ3  1 
ATOM   865  N  N    . VAL   A 1 30  ? 18.396 -1.221  18.732  1.00 27.70 ?  30  VAL   A N    1 
ATOM   866  C  CA   . VAL   A 1 30  ? 19.053 -2.491  19.029  1.00 27.18 ?  30  VAL   A CA   1 
ATOM   867  C  C    . VAL   A 1 30  ? 20.549 -2.308  19.266  1.00 26.35 ?  30  VAL   A C    1 
ATOM   868  O  O    . VAL   A 1 30  ? 21.145 -3.002  20.097  1.00 26.93 ?  30  VAL   A O    1 
ATOM   869  C  CB   . VAL   A 1 30  ? 18.773 -3.497  17.899  1.00 27.36 ?  30  VAL   A CB   1 
ATOM   870  C  CG1  . VAL   A 1 30  ? 19.508 -4.800  18.155  1.00 27.83 ?  30  VAL   A CG1  1 
ATOM   871  C  CG2  . VAL   A 1 30  ? 17.274 -3.740  17.756  1.00 27.79 ?  30  VAL   A CG2  1 
ATOM   872  H  H    A VAL   A 1 30  ? 18.268 -1.067  17.896  0.66 33.30 ?  30  VAL   A H    1 
ATOM   873  H  H    B VAL   A 1 30  ? 18.094 -1.159  17.928  0.34 33.30 ?  30  VAL   A H    1 
ATOM   874  H  HA   . VAL   A 1 30  ? 18.658 -2.855  19.840  1.00 32.67 ?  30  VAL   A HA   1 
ATOM   875  H  HB   . VAL   A 1 30  ? 19.098 -3.132  17.062  1.00 32.89 ?  30  VAL   A HB   1 
ATOM   876  H  HG11 . VAL   A 1 30  ? 19.152 -5.483  17.565  1.00 33.45 ?  30  VAL   A HG11 1 
ATOM   877  H  HG12 . VAL   A 1 30  ? 20.452 -4.672  17.982  1.00 33.45 ?  30  VAL   A HG12 1 
ATOM   878  H  HG13 . VAL   A 1 30  ? 19.370 -5.061  19.080  1.00 33.45 ?  30  VAL   A HG13 1 
ATOM   879  H  HG21 . VAL   A 1 30  ? 17.128 -4.421  17.081  1.00 33.40 ?  30  VAL   A HG21 1 
ATOM   880  H  HG22 . VAL   A 1 30  ? 16.920 -4.035  18.608  1.00 33.40 ?  30  VAL   A HG22 1 
ATOM   881  H  HG23 . VAL   A 1 30  ? 16.846 -2.912  17.487  1.00 33.40 ?  30  VAL   A HG23 1 
ATOM   882  N  N    . LYS   A 1 31  ? 21.181 -1.392  18.541  1.00 25.74 ?  31  LYS   A N    1 
ATOM   883  C  CA   . LYS   A 1 31  ? 22.634 -1.288  18.487  1.00 27.03 ?  31  LYS   A CA   1 
ATOM   884  C  C    . LYS   A 1 31  ? 23.259 -2.654  18.187  1.00 24.55 ?  31  LYS   A C    1 
ATOM   885  O  O    . LYS   A 1 31  ? 24.032 -3.183  18.993  1.00 25.13 ?  31  LYS   A O    1 
ATOM   886  C  CB   . LYS   A 1 31  ? 23.212 -0.689  19.761  1.00 31.00 ?  31  LYS   A CB   1 
ATOM   887  C  CG   . LYS   A 1 31  ? 22.554 0.614   20.190  1.00 35.60 ?  31  LYS   A CG   1 
ATOM   888  C  CD   . LYS   A 1 31  ? 23.585 1.670   20.557  1.00 39.25 ?  31  LYS   A CD   1 
ATOM   889  C  CE   . LYS   A 1 31  ? 23.013 2.701   21.519  1.00 41.54 ?  31  LYS   A CE   1 
ATOM   890  N  NZ   . LYS   A 1 31  ? 21.764 3.340   21.021  1.00 42.86 ?  31  LYS   A NZ   1 
ATOM   891  H  H    . LYS   A 1 31  ? 20.777 -0.808  18.064  1.00 30.94 ?  31  LYS   A H    1 
ATOM   892  H  HA   . LYS   A 1 31  ? 22.863 -0.699  17.762  1.00 32.49 ?  31  LYS   A HA   1 
ATOM   893  H  HB2  . LYS   A 1 31  ? 23.083 -1.327  20.467  1.00 37.25 ?  31  LYS   A HB2  1 
ATOM   894  H  HB3  . LYS   A 1 31  ? 24.163 -0.522  19.631  1.00 37.25 ?  31  LYS   A HB3  1 
ATOM   895  H  HG2  . LYS   A 1 31  ? 22.015 0.956   19.460  1.00 42.78 ?  31  LYS   A HG2  1 
ATOM   896  H  HG3  . LYS   A 1 31  ? 21.998 0.449   20.969  1.00 42.78 ?  31  LYS   A HG3  1 
ATOM   897  H  HD2  . LYS   A 1 31  ? 24.344 1.245   20.987  1.00 47.15 ?  31  LYS   A HD2  1 
ATOM   898  H  HD3  . LYS   A 1 31  ? 23.871 2.132   19.753  1.00 47.15 ?  31  LYS   A HD3  1 
ATOM   899  H  HE2  . LYS   A 1 31  ? 22.807 2.263   22.358  1.00 49.91 ?  31  LYS   A HE2  1 
ATOM   900  H  HE3  . LYS   A 1 31  ? 23.670 3.400   21.663  1.00 49.91 ?  31  LYS   A HE3  1 
ATOM   901  H  HZ1  . LYS   A 1 31  ? 21.476 3.944   21.609  1.00 51.49 ?  31  LYS   A HZ1  1 
ATOM   902  H  HZ2  . LYS   A 1 31  ? 21.917 3.743   20.244  1.00 51.49 ?  31  LYS   A HZ2  1 
ATOM   903  H  HZ3  . LYS   A 1 31  ? 21.131 2.724   20.908  1.00 51.49 ?  31  LYS   A HZ3  1 
ATOM   904  N  N    . PRO   A 1 32  ? 22.949 -3.236  17.034  1.00 22.48 ?  32  PRO   A N    1 
ATOM   905  C  CA   . PRO   A 1 32  ? 23.424 -4.586  16.727  1.00 22.22 ?  32  PRO   A CA   1 
ATOM   906  C  C    . PRO   A 1 32  ? 24.923 -4.613  16.499  1.00 22.08 ?  32  PRO   A C    1 
ATOM   907  O  O    . PRO   A 1 32  ? 25.573 -3.588  16.281  1.00 21.99 ?  32  PRO   A O    1 
ATOM   908  C  CB   . PRO   A 1 32  ? 22.686 -4.915  15.428  1.00 22.08 ?  32  PRO   A CB   1 
ATOM   909  C  CG   . PRO   A 1 32  ? 22.525 -3.584  14.766  1.00 22.35 ?  32  PRO   A CG   1 
ATOM   910  C  CD   . PRO   A 1 32  ? 22.237 -2.638  15.893  1.00 22.08 ?  32  PRO   A CD   1 
ATOM   911  H  HA   . PRO   A 1 32  ? 23.175 -5.215  17.426  1.00 26.72 ?  32  PRO   A HA   1 
ATOM   912  H  HB2  . PRO   A 1 32  ? 23.225 -5.515  14.886  1.00 26.55 ?  32  PRO   A HB2  1 
ATOM   913  H  HB3  . PRO   A 1 32  ? 21.824 -5.314  15.631  1.00 26.55 ?  32  PRO   A HB3  1 
ATOM   914  H  HG2  . PRO   A 1 32  ? 23.348 -3.347  14.313  1.00 26.88 ?  32  PRO   A HG2  1 
ATOM   915  H  HG3  . PRO   A 1 32  ? 21.783 -3.620  14.144  1.00 26.88 ?  32  PRO   A HG3  1 
ATOM   916  H  HD2  . PRO   A 1 32  ? 22.595 -1.762  15.688  1.00 26.55 ?  32  PRO   A HD2  1 
ATOM   917  H  HD3  . PRO   A 1 32  ? 21.286 -2.607  16.068  1.00 26.55 ?  32  PRO   A HD3  1 
ATOM   918  N  N    . THR   A 1 33  ? 25.470 -5.828  16.529  1.00 21.89 ?  33  THR   A N    1 
ATOM   919  C  CA   . THR   A 1 33  ? 26.880 -6.005  16.213  1.00 21.67 ?  33  THR   A CA   1 
ATOM   920  C  C    . THR   A 1 33  ? 27.186 -5.532  14.798  1.00 20.11 ?  33  THR   A C    1 
ATOM   921  O  O    . THR   A 1 33  ? 28.213 -4.881  14.563  1.00 20.15 ?  33  THR   A O    1 
ATOM   922  C  CB   . THR   A 1 33  ? 27.269 -7.472  16.390  1.00 23.29 ?  33  THR   A CB   1 
ATOM   923  O  OG1  . THR   A 1 33  ? 26.980 -7.885  17.730  1.00 24.75 ?  33  THR   A OG1  1 
ATOM   924  C  CG2  . THR   A 1 33  ? 28.749 -7.670  16.122  1.00 23.83 ?  33  THR   A CG2  1 
ATOM   925  H  H    . THR   A 1 33  ? 25.050 -6.555  16.719  1.00 26.33 ?  33  THR   A H    1 
ATOM   926  H  HA   . THR   A 1 33  ? 27.413 -5.479  16.828  1.00 26.06 ?  33  THR   A HA   1 
ATOM   927  H  HB   . THR   A 1 33  ? 26.763 -8.021  15.767  1.00 28.01 ?  33  THR   A HB   1 
ATOM   928  H  HG1  . THR   A 1 33  ? 27.412 -7.414  18.277  1.00 29.76 ?  33  THR   A HG1  1 
ATOM   929  H  HG21 . THR   A 1 33  ? 29.018 -8.557  16.403  1.00 28.65 ?  33  THR   A HG21 1 
ATOM   930  H  HG22 . THR   A 1 33  ? 28.931 -7.570  15.175  1.00 28.65 ?  33  THR   A HG22 1 
ATOM   931  H  HG23 . THR   A 1 33  ? 29.261 -7.012  16.616  1.00 28.65 ?  33  THR   A HG23 1 
ATOM   932  N  N    . VAL   A 1 34  ? 26.313 -5.855  13.845  1.00 18.56 ?  34  VAL   A N    1 
ATOM   933  C  CA   . VAL   A 1 34  ? 26.503 -5.516  12.441  1.00 17.34 ?  34  VAL   A CA   1 
ATOM   934  C  C    . VAL   A 1 34  ? 25.202 -4.949  11.881  1.00 16.98 ?  34  VAL   A C    1 
ATOM   935  O  O    . VAL   A 1 34  ? 24.161 -5.613  11.927  1.00 17.34 ?  34  VAL   A O    1 
ATOM   936  C  CB   . VAL   A 1 34  ? 26.957 -6.728  11.606  1.00 17.84 ?  34  VAL   A CB   1 
ATOM   937  C  CG1  . VAL   A 1 34  ? 27.120 -6.334  10.145  1.00 18.23 ?  34  VAL   A CG1  1 
ATOM   938  C  CG2  . VAL   A 1 34  ? 28.251 -7.325  12.158  1.00 18.68 ?  34  VAL   A CG2  1 
ATOM   939  H  H    . VAL   A 1 34  ? 25.590 -6.301  13.993  1.00 22.33 ?  34  VAL   A H    1 
ATOM   940  H  HA   . VAL   A 1 34  ? 27.186 -4.830  12.370  1.00 20.87 ?  34  VAL   A HA   1 
ATOM   941  H  HB   . VAL   A 1 34  ? 26.277 -7.414  11.653  1.00 21.47 ?  34  VAL   A HB   1 
ATOM   942  H  HG11 . VAL   A 1 34  ? 27.609 -7.032  9.682   1.00 21.93 ?  34  VAL   A HG11 1 
ATOM   943  H  HG12 . VAL   A 1 34  ? 26.245 -6.224  9.746   1.00 21.93 ?  34  VAL   A HG12 1 
ATOM   944  H  HG13 . VAL   A 1 34  ? 27.616 -5.500  10.096  1.00 21.93 ?  34  VAL   A HG13 1 
ATOM   945  H  HG21 . VAL   A 1 34  ? 28.544 -8.043  11.573  1.00 22.48 ?  34  VAL   A HG21 1 
ATOM   946  H  HG22 . VAL   A 1 34  ? 28.932 -6.632  12.193  1.00 22.48 ?  34  VAL   A HG22 1 
ATOM   947  H  HG23 . VAL   A 1 34  ? 28.087 -7.671  13.048  1.00 22.48 ?  34  VAL   A HG23 1 
ATOM   948  N  N    . VAL   A 1 35  ? 25.265 -3.731  11.345  1.00 16.54 ?  35  VAL   A N    1 
ATOM   949  C  CA   . VAL   A 1 35  ? 24.231 -3.202  10.459  1.00 16.07 ?  35  VAL   A CA   1 
ATOM   950  C  C    . VAL   A 1 35  ? 24.778 -3.209  9.041   1.00 15.52 ?  35  VAL   A C    1 
ATOM   951  O  O    . VAL   A 1 35  ? 25.926 -2.810  8.813   1.00 15.68 ?  35  VAL   A O    1 
ATOM   952  C  CB   . VAL   A 1 35  ? 23.713 -1.804  10.866  1.00 16.51 ?  35  VAL   A CB   1 
ATOM   953  C  CG1  . VAL   A 1 35  ? 24.775 -0.723  10.712  1.00 16.72 ?  35  VAL   A CG1  1 
ATOM   954  C  CG2  . VAL   A 1 35  ? 22.480 -1.442  10.031  1.00 17.08 ?  35  VAL   A CG2  1 
ATOM   955  H  H    . VAL   A 1 35  ? 25.911 -3.184  11.479  1.00 19.90 ?  35  VAL   A H    1 
ATOM   956  H  HA   . VAL   A 1 35  ? 23.472 -3.804  10.485  1.00 19.34 ?  35  VAL   A HA   1 
ATOM   957  H  HB   . VAL   A 1 35  ? 23.438 -1.819  11.793  1.00 19.86 ?  35  VAL   A HB   1 
ATOM   958  H  HG11 . VAL   A 1 35  ? 24.444 0.105   11.096  1.00 20.11 ?  35  VAL   A HG11 1 
ATOM   959  H  HG12 . VAL   A 1 35  ? 25.576 -1.006  11.179  1.00 20.11 ?  35  VAL   A HG12 1 
ATOM   960  H  HG13 . VAL   A 1 35  ? 24.968 -0.596  9.770   1.00 20.11 ?  35  VAL   A HG13 1 
ATOM   961  H  HG21 . VAL   A 1 35  ? 22.123 -0.597  10.343  1.00 20.55 ?  35  VAL   A HG21 1 
ATOM   962  H  HG22 . VAL   A 1 35  ? 22.743 -1.364  9.098   1.00 20.55 ?  35  VAL   A HG22 1 
ATOM   963  H  HG23 . VAL   A 1 35  ? 21.818 -2.142  10.130  1.00 20.55 ?  35  VAL   A HG23 1 
ATOM   964  N  N    . VAL   A 1 36  ? 23.967 -3.674  8.096   1.00 14.40 ?  36  VAL   A N    1 
ATOM   965  C  CA   . VAL   A 1 36  ? 24.341 -3.684  6.689   1.00 14.56 ?  36  VAL   A CA   1 
ATOM   966  C  C    . VAL   A 1 36  ? 23.887 -2.388  6.036   1.00 14.89 ?  36  VAL   A C    1 
ATOM   967  O  O    . VAL   A 1 36  ? 22.728 -1.980  6.181   1.00 15.42 ?  36  VAL   A O    1 
ATOM   968  C  CB   . VAL   A 1 36  ? 23.738 -4.896  5.966   1.00 14.33 ?  36  VAL   A CB   1 
ATOM   969  C  CG1  . VAL   A 1 36  ? 24.000 -4.829  4.487   1.00 15.32 ?  36  VAL   A CG1  1 
ATOM   970  C  CG2  . VAL   A 1 36  ? 24.276 -6.191  6.537   1.00 15.48 ?  36  VAL   A CG2  1 
ATOM   971  H  H    . VAL   A 1 36  ? 23.172 -3.985  8.251   1.00 17.33 ?  36  VAL   A H    1 
ATOM   972  H  HA   . VAL   A 1 36  ? 25.301 -3.744  6.616   1.00 17.53 ?  36  VAL   A HA   1 
ATOM   973  H  HB   . VAL   A 1 36  ? 22.768 -4.886  6.093   1.00 17.25 ?  36  VAL   A HB   1 
ATOM   974  H  HG11 . VAL   A 1 36  ? 23.838 -5.705  4.100   1.00 18.44 ?  36  VAL   A HG11 1 
ATOM   975  H  HG12 . VAL   A 1 36  ? 23.401 -4.179  4.081   1.00 18.44 ?  36  VAL   A HG12 1 
ATOM   976  H  HG13 . VAL   A 1 36  ? 24.920 -4.569  4.344   1.00 18.44 ?  36  VAL   A HG13 1 
ATOM   977  H  HG21 . VAL   A 1 36  ? 23.872 -6.940  6.065   1.00 18.63 ?  36  VAL   A HG21 1 
ATOM   978  H  HG22 . VAL   A 1 36  ? 25.235 -6.209  6.427   1.00 18.63 ?  36  VAL   A HG22 1 
ATOM   979  H  HG23 . VAL   A 1 36  ? 24.048 -6.243  7.481   1.00 18.63 ?  36  VAL   A HG23 1 
ATOM   980  N  N    . ASN   A 1 37  ? 24.801 -1.753  5.305   1.00 13.78 ?  37  ASN   A N    1 
ATOM   981  C  CA   . ASN   A 1 37  ? 24.469 -0.631  4.441   1.00 13.30 ?  37  ASN   A CA   1 
ATOM   982  C  C    . ASN   A 1 37  ? 24.331 -1.089  2.996   1.00 13.04 ?  37  ASN   A C    1 
ATOM   983  O  O    . ASN   A 1 37  ? 25.115 -1.920  2.513   1.00 13.87 ?  37  ASN   A O    1 
ATOM   984  C  CB   . ASN   A 1 37  ? 25.554 0.444   4.514   1.00 13.06 ?  37  ASN   A CB   1 
ATOM   985  C  CG   . ASN   A 1 37  ? 25.230 1.648   3.666   1.00 13.69 ?  37  ASN   A CG   1 
ATOM   986  O  OD1  . ASN   A 1 37  ? 24.049 1.983   3.475   1.00 14.22 ?  37  ASN   A OD1  1 
ATOM   987  N  ND2  . ASN   A 1 37  ? 26.262 2.318   3.159   1.00 14.20 ?  37  ASN   A ND2  1 
ATOM   988  H  H    . ASN   A 1 37  ? 25.638 -1.954  5.301   1.00 16.60 ?  37  ASN   A H    1 
ATOM   989  H  HA   . ASN   A 1 37  ? 23.632 -0.238  4.726   1.00 16.02 ?  37  ASN   A HA   1 
ATOM   990  H  HB2  . ASN   A 1 37  ? 25.649 0.735   5.437   1.00 15.73 ?  37  ASN   A HB2  1 
ATOM   991  H  HB3  . ASN   A 1 37  ? 26.396 0.067   4.202   1.00 15.73 ?  37  ASN   A HB3  1 
ATOM   992  H  HD21 . ASN   A 1 37  ? 26.117 3.009   2.674   1.00 17.09 ?  37  ASN   A HD21 1 
ATOM   993  H  HD22 . ASN   A 1 37  ? 27.057 2.056   3.311   1.00 17.09 ?  37  ASN   A HD22 1 
ATOM   994  N  N    A ALA   A 1 38  ? 23.313 -0.542  2.325   0.66 13.98 ?  38  ALA   A N    1 
ATOM   995  N  N    B ALA   A 1 38  ? 23.309 -0.577  2.312   0.34 13.33 ?  38  ALA   A N    1 
ATOM   996  C  CA   A ALA   A 1 38  ? 23.129 -0.655  0.879   0.66 13.59 ?  38  ALA   A CA   1 
ATOM   997  C  CA   B ALA   A 1 38  ? 23.152 -0.810  0.878   0.34 13.18 ?  38  ALA   A CA   1 
ATOM   998  C  C    A ALA   A 1 38  ? 24.063 0.335   0.184   0.66 13.89 ?  38  ALA   A C    1 
ATOM   999  C  C    B ALA   A 1 38  ? 24.000 0.223   0.138   0.34 13.19 ?  38  ALA   A C    1 
ATOM   1000 O  O    A ALA   A 1 38  ? 23.679 1.449   -0.184  0.66 13.63 ?  38  ALA   A O    1 
ATOM   1001 O  O    B ALA   A 1 38  ? 23.510 1.203   -0.431  0.34 12.62 ?  38  ALA   A O    1 
ATOM   1002 C  CB   A ALA   A 1 38  ? 21.673 -0.373  0.523   0.66 14.60 ?  38  ALA   A CB   1 
ATOM   1003 C  CB   B ALA   A 1 38  ? 21.684 -0.757  0.478   0.34 13.49 ?  38  ALA   A CB   1 
ATOM   1004 H  H    A ALA   A 1 38  ? 22.703 -0.068  2.706   0.66 16.84 ?  38  ALA   A H    1 
ATOM   1005 H  H    B ALA   A 1 38  ? 22.698 -0.087  2.660   0.34 16.05 ?  38  ALA   A H    1 
ATOM   1006 H  HA   A ALA   A 1 38  ? 23.353 -1.557  0.594   0.66 16.36 ?  38  ALA   A HA   1 
ATOM   1007 H  HA   B ALA   A 1 38  ? 23.495 -1.695  0.663   0.34 15.87 ?  38  ALA   A HA   1 
ATOM   1008 H  HB1  A ALA   A 1 38  ? 21.560 -0.457  -0.436  0.66 17.57 ?  38  ALA   A HB1  1 
ATOM   1009 H  HB1  B ALA   A 1 38  ? 21.622 -0.838  -0.486  0.34 16.24 ?  38  ALA   A HB1  1 
ATOM   1010 H  HB2  A ALA   A 1 38  ? 21.101 -1.006  0.983   0.66 17.57 ?  38  ALA   A HB2  1 
ATOM   1011 H  HB2  B ALA   A 1 38  ? 21.212 -1.492  0.904   0.34 16.24 ?  38  ALA   A HB2  1 
ATOM   1012 H  HB3  A ALA   A 1 38  ? 21.451 0.533   0.802   0.66 17.57 ?  38  ALA   A HB3  1 
ATOM   1013 H  HB3  B ALA   A 1 38  ? 21.311 0.088   0.763   0.34 16.24 ?  38  ALA   A HB3  1 
ATOM   1014 N  N    A ALA   A 1 39  ? 25.307 -0.095  -0.023  0.66 13.85 ?  39  ALA   A N    1 
ATOM   1015 N  N    B ALA   A 1 39  ? 25.308 -0.019  0.152   0.34 13.39 ?  39  ALA   A N    1 
ATOM   1016 C  CA   A ALA   A 1 39  ? 26.379 0.761   -0.504  0.66 13.02 ?  39  ALA   A CA   1 
ATOM   1017 C  CA   B ALA   A 1 39  ? 26.288 0.928   -0.345  0.34 13.49 ?  39  ALA   A CA   1 
ATOM   1018 C  C    A ALA   A 1 39  ? 26.499 0.719   -2.029  0.66 12.95 ?  39  ALA   A C    1 
ATOM   1019 C  C    B ALA   A 1 39  ? 26.452 0.803   -1.856  0.34 12.81 ?  39  ALA   A C    1 
ATOM   1020 O  O    A ALA   A 1 39  ? 26.007 -0.192  -2.699  0.66 13.90 ?  39  ALA   A O    1 
ATOM   1021 O  O    B ALA   A 1 39  ? 25.998 -0.153  -2.490  0.34 13.28 ?  39  ALA   A O    1 
ATOM   1022 C  CB   A ALA   A 1 39  ? 27.697 0.324   0.141   0.66 13.26 ?  39  ALA   A CB   1 
ATOM   1023 C  CB   B ALA   A 1 39  ? 27.632 0.695   0.342   0.34 14.10 ?  39  ALA   A CB   1 
ATOM   1024 H  H    A ALA   A 1 39  ? 25.561 -0.908  0.114   0.66 16.68 ?  39  ALA   A H    1 
ATOM   1025 H  H    B ALA   A 1 39  ? 25.653 -0.747  0.447   0.34 16.12 ?  39  ALA   A H    1 
ATOM   1026 H  HA   A ALA   A 1 39  ? 26.201 1.679   -0.237  0.66 15.67 ?  39  ALA   A HA   1 
ATOM   1027 H  HA   B ALA   A 1 39  ? 25.995 1.828   -0.150  0.34 16.25 ?  39  ALA   A HA   1 
ATOM   1028 H  HB1  A ALA   A 1 39  ? 28.411 0.900   -0.177  0.66 15.97 ?  39  ALA   A HB1  1 
ATOM   1029 H  HB1  B ALA   A 1 39  ? 28.276 1.336   0.000   0.34 16.97 ?  39  ALA   A HB1  1 
ATOM   1030 H  HB2  A ALA   A 1 39  ? 27.619 0.406   1.109   0.66 15.97 ?  39  ALA   A HB2  1 
ATOM   1031 H  HB2  B ALA   A 1 39  ? 27.519 0.818   1.298   0.34 16.97 ?  39  ALA   A HB2  1 
ATOM   1032 H  HB3  A ALA   A 1 39  ? 27.878 -0.595  -0.098  0.66 15.97 ?  39  ALA   A HB3  1 
ATOM   1033 H  HB3  B ALA   A 1 39  ? 27.932 -0.208  0.156   0.34 16.97 ?  39  ALA   A HB3  1 
ATOM   1034 N  N    A ASN   A 1 40  ? 27.178 1.730   -2.572  0.66 13.67 ?  40  ASN   A N    1 
ATOM   1035 N  N    B ASN   A 1 40  ? 27.116 1.801   -2.432  0.34 12.78 ?  40  ASN   A N    1 
ATOM   1036 C  CA   A ASN   A 1 40  ? 27.699 1.699   -3.933  0.66 14.47 ?  40  ASN   A CA   1 
ATOM   1037 C  CA   B ASN   A 1 40  ? 27.626 1.736   -3.792  0.34 13.23 ?  40  ASN   A CA   1 
ATOM   1038 C  C    A ASN   A 1 40  ? 29.226 1.605   -3.876  0.66 14.63 ?  40  ASN   A C    1 
ATOM   1039 C  C    B ASN   A 1 40  ? 29.146 1.611   -3.747  0.34 13.33 ?  40  ASN   A C    1 
ATOM   1040 O  O    A ASN   A 1 40  ? 29.824 1.724   -2.807  0.66 14.75 ?  40  ASN   A O    1 
ATOM   1041 O  O    B ASN   A 1 40  ? 29.764 1.685   -2.682  0.34 13.13 ?  40  ASN   A O    1 
ATOM   1042 C  CB   A ASN   A 1 40  ? 27.199 2.892   -4.769  0.66 14.95 ?  40  ASN   A CB   1 
ATOM   1043 C  CB   B ASN   A 1 40  ? 27.174 2.947   -4.623  0.34 14.50 ?  40  ASN   A CB   1 
ATOM   1044 C  CG   A ASN   A 1 40  ? 27.591 4.237   -4.190  0.66 15.28 ?  40  ASN   A CG   1 
ATOM   1045 C  CG   B ASN   A 1 40  ? 27.518 4.270   -3.970  0.34 15.62 ?  40  ASN   A CG   1 
ATOM   1046 O  OD1  A ASN   A 1 40  ? 28.766 4.488   -3.906  0.66 16.45 ?  40  ASN   A OD1  1 
ATOM   1047 O  OD1  B ASN   A 1 40  ? 28.690 4.622   -3.832  0.34 16.49 ?  40  ASN   A OD1  1 
ATOM   1048 N  ND2  A ASN   A 1 40  ? 26.604 5.120   -4.033  0.66 15.09 ?  40  ASN   A ND2  1 
ATOM   1049 N  ND2  B ASN   A 1 40  ? 26.493 5.019   -3.581  0.34 16.24 ?  40  ASN   A ND2  1 
ATOM   1050 H  H    A ASN   A 1 40  ? 27.349 2.457   -2.157  0.66 16.46 ?  40  ASN   A H    1 
ATOM   1051 H  H    B ASN   A 1 40  ? 27.295 2.546   -2.044  0.34 15.39 ?  40  ASN   A H    1 
ATOM   1052 H  HA   A ASN   A 1 40  ? 27.372 0.890   -4.364  0.66 17.42 ?  40  ASN   A HA   1 
ATOM   1053 H  HA   B ASN   A 1 40  ? 27.290 0.937   -4.225  0.34 15.93 ?  40  ASN   A HA   1 
ATOM   1054 H  HB2  A ASN   A 1 40  ? 27.574 2.823   -5.662  0.66 17.99 ?  40  ASN   A HB2  1 
ATOM   1055 H  HB2  B ASN   A 1 40  ? 27.602 2.914   -5.494  0.34 17.45 ?  40  ASN   A HB2  1 
ATOM   1056 H  HB3  A ASN   A 1 40  ? 26.230 2.854   -4.818  0.66 17.99 ?  40  ASN   A HB3  1 
ATOM   1057 H  HB3  B ASN   A 1 40  ? 26.209 2.902   -4.731  0.34 17.45 ?  40  ASN   A HB3  1 
ATOM   1058 H  HD21 A ASN   A 1 40  ? 26.770 5.901   -3.711  0.66 18.17 ?  40  ASN   A HD21 1 
ATOM   1059 H  HD21 B ASN   A 1 40  ? 26.637 5.780   -3.212  0.34 19.54 ?  40  ASN   A HD21 1 
ATOM   1060 H  HD22 A ASN   A 1 40  ? 25.797 4.903   -4.238  0.66 18.17 ?  40  ASN   A HD22 1 
ATOM   1061 H  HD22 B ASN   A 1 40  ? 25.687 4.740   -3.697  0.34 19.54 ?  40  ASN   A HD22 1 
ATOM   1062 N  N    A VAL   A 1 41  ? 29.854 1.342   -5.025  0.66 14.86 ?  41  VAL   A N    1 
ATOM   1063 N  N    B VAL   A 1 41  ? 29.740 1.397   -4.923  0.34 13.27 ?  41  VAL   A N    1 
ATOM   1064 C  CA   A VAL   A 1 41  ? 31.288 1.039   -5.028  0.66 14.84 ?  41  VAL   A CA   1 
ATOM   1065 C  CA   B VAL   A 1 41  ? 31.163 1.063   -4.999  0.34 13.93 ?  41  VAL   A CA   1 
ATOM   1066 C  C    A VAL   A 1 41  ? 32.135 2.213   -4.568  0.66 14.63 ?  41  VAL   A C    1 
ATOM   1067 C  C    B VAL   A 1 41  ? 32.035 2.186   -4.451  0.34 14.15 ?  41  VAL   A C    1 
ATOM   1068 O  O    A VAL   A 1 41  ? 33.305 2.019   -4.215  0.66 13.80 ?  41  VAL   A O    1 
ATOM   1069 O  O    B VAL   A 1 41  ? 33.103 1.931   -3.878  0.34 13.94 ?  41  VAL   A O    1 
ATOM   1070 C  CB   A VAL   A 1 41  ? 31.810 0.531   -6.394  0.66 14.98 ?  41  VAL   A CB   1 
ATOM   1071 C  CB   B VAL   A 1 41  ? 31.554 0.661   -6.439  0.34 14.11 ?  41  VAL   A CB   1 
ATOM   1072 C  CG1  A VAL   A 1 41  ? 31.118 -0.758  -6.799  0.66 16.09 ?  41  VAL   A CG1  1 
ATOM   1073 C  CG1  B VAL   A 1 41  ? 30.913 -0.673  -6.807  0.34 15.21 ?  41  VAL   A CG1  1 
ATOM   1074 C  CG2  A VAL   A 1 41  ? 31.696 1.605   -7.475  0.66 14.67 ?  41  VAL   A CG2  1 
ATOM   1075 C  CG2  B VAL   A 1 41  ? 31.158 1.741   -7.445  0.34 14.26 ?  41  VAL   A CG2  1 
ATOM   1076 H  H    A VAL   A 1 41  ? 29.477 1.319   -5.795  0.66 17.88 ?  41  VAL   A H    1 
ATOM   1077 H  H    B VAL   A 1 41  ? 29.347 1.432   -5.687  0.34 15.97 ?  41  VAL   A H    1 
ATOM   1078 H  HA   A VAL   A 1 41  ? 31.438 0.317   -4.394  0.66 17.86 ?  41  VAL   A HA   1 
ATOM   1079 H  HA   B VAL   A 1 41  ? 31.329 0.291   -4.441  0.34 16.77 ?  41  VAL   A HA   1 
ATOM   1080 H  HB   A VAL   A 1 41  ? 32.755 0.326   -6.296  0.66 18.03 ?  41  VAL   A HB   1 
ATOM   1081 H  HB   B VAL   A 1 41  ? 32.516 0.542   -6.494  0.34 16.99 ?  41  VAL   A HB   1 
ATOM   1082 H  HG11 A VAL   A 1 41  ? 31.471 -1.055  -7.652  0.66 19.36 ?  41  VAL   A HG11 1 
ATOM   1083 H  HG11 B VAL   A 1 41  ? 31.248 -0.964  -7.670  0.34 18.31 ?  41  VAL   A HG11 1 
ATOM   1084 H  HG12 A VAL   A 1 41  ? 31.280 -1.433  -6.120  0.66 19.36 ?  41  VAL   A HG12 1 
ATOM   1085 H  HG12 B VAL   A 1 41  ? 31.138 -1.330  -6.128  0.34 18.31 ?  41  VAL   A HG12 1 
ATOM   1086 H  HG13 A VAL   A 1 41  ? 30.164 -0.592  -6.877  0.66 19.36 ?  41  VAL   A HG13 1 
ATOM   1087 H  HG13 B VAL   A 1 41  ? 29.950 -0.561  -6.848  0.34 18.31 ?  41  VAL   A HG13 1 
ATOM   1088 H  HG21 A VAL   A 1 41  ? 31.921 1.209   -8.333  0.66 17.66 ?  41  VAL   A HG21 1 
ATOM   1089 H  HG21 B VAL   A 1 41  ? 31.543 1.522   -8.311  0.34 17.17 ?  41  VAL   A HG21 1 
ATOM   1090 H  HG22 A VAL   A 1 41  ? 30.789 1.939   -7.490  0.66 17.66 ?  41  VAL   A HG22 1 
ATOM   1091 H  HG22 B VAL   A 1 41  ? 30.192 1.771   -7.517  0.34 17.17 ?  41  VAL   A HG22 1 
ATOM   1092 H  HG23 A VAL   A 1 41  ? 32.315 2.323   -7.271  0.66 17.66 ?  41  VAL   A HG23 1 
ATOM   1093 H  HG23 B VAL   A 1 41  ? 31.498 2.593   -7.140  0.34 17.17 ?  41  VAL   A HG23 1 
ATOM   1094 N  N    . TYR   A 1 42  ? 31.594 3.432   -4.602  1.00 14.52 ?  42  TYR   A N    1 
ATOM   1095 C  CA   . TYR   A 1 42  ? 32.334 4.613   -4.175  1.00 14.18 ?  42  TYR   A CA   1 
ATOM   1096 C  C    . TYR   A 1 42  ? 32.067 4.981   -2.725  1.00 13.93 ?  42  TYR   A C    1 
ATOM   1097 O  O    . TYR   A 1 42  ? 32.631 5.972   -2.237  1.00 14.76 ?  42  TYR   A O    1 
ATOM   1098 C  CB   . TYR   A 1 42  ? 31.992 5.812   -5.084  1.00 14.55 ?  42  TYR   A CB   1 
ATOM   1099 C  CG   . TYR   A 1 42  ? 32.166 5.510   -6.553  1.00 15.05 ?  42  TYR   A CG   1 
ATOM   1100 C  CD1  . TYR   A 1 42  ? 33.423 5.307   -7.097  1.00 15.97 ?  42  TYR   A CD1  1 
ATOM   1101 C  CD2  . TYR   A 1 42  ? 31.070 5.388   -7.391  1.00 16.68 ?  42  TYR   A CD2  1 
ATOM   1102 C  CE1  . TYR   A 1 42  ? 33.582 5.005   -8.437  1.00 16.58 ?  42  TYR   A CE1  1 
ATOM   1103 C  CE2  . TYR   A 1 42  ? 31.223 5.104   -8.732  1.00 17.71 ?  42  TYR   A CE2  1 
ATOM   1104 C  CZ   . TYR   A 1 42  ? 32.479 4.905   -9.252  1.00 17.88 ?  42  TYR   A CZ   1 
ATOM   1105 O  OH   . TYR   A 1 42  ? 32.629 4.615   -10.588 1.00 19.77 ?  42  TYR   A OH   1 
ATOM   1106 H  H    A TYR   A 1 42  ? 30.802 3.600   -4.889  0.66 17.48 ?  42  TYR   A H    1 
ATOM   1107 H  H    B TYR   A 1 42  ? 30.830 3.621   -4.948  0.34 17.48 ?  42  TYR   A H    1 
ATOM   1108 H  HA   . TYR   A 1 42  ? 33.284 4.444   -4.268  1.00 17.07 ?  42  TYR   A HA   1 
ATOM   1109 H  HB2  . TYR   A 1 42  ? 31.065 6.064   -4.940  1.00 17.51 ?  42  TYR   A HB2  1 
ATOM   1110 H  HB3  . TYR   A 1 42  ? 32.574 6.555   -4.864  1.00 17.51 ?  42  TYR   A HB3  1 
ATOM   1111 H  HD1  . TYR   A 1 42  ? 34.173 5.368   -6.553  1.00 19.22 ?  42  TYR   A HD1  1 
ATOM   1112 H  HD2  . TYR   A 1 42  ? 30.216 5.522   -7.048  1.00 20.07 ?  42  TYR   A HD2  1 
ATOM   1113 H  HE1  . TYR   A 1 42  ? 34.433 4.877   -8.789  1.00 19.95 ?  42  TYR   A HE1  1 
ATOM   1114 H  HE2  . TYR   A 1 42  ? 30.474 5.032   -9.279  1.00 21.31 ?  42  TYR   A HE2  1 
ATOM   1115 H  HH   . TYR   A 1 42  ? 33.443 4.514   -10.769 1.00 23.78 ?  42  TYR   A HH   1 
ATOM   1116 N  N    A LEU   A 1 43  ? 31.210 4.227   -2.041  0.66 13.87 ?  43  LEU   A N    1 
ATOM   1117 N  N    B LEU   A 1 43  ? 31.198 4.238   -2.041  0.34 13.72 ?  43  LEU   A N    1 
ATOM   1118 C  CA   A LEU   A 1 43  ? 30.776 4.556   -0.689  0.66 13.75 ?  43  LEU   A CA   1 
ATOM   1119 C  CA   B LEU   A 1 43  ? 30.740 4.589   -0.697  0.34 13.78 ?  43  LEU   A CA   1 
ATOM   1120 C  C    A LEU   A 1 43  ? 30.305 6.006   -0.587  0.66 13.84 ?  43  LEU   A C    1 
ATOM   1121 C  C    B LEU   A 1 43  ? 30.225 6.027   -0.635  0.34 14.20 ?  43  LEU   A C    1 
ATOM   1122 O  O    A LEU   A 1 43  ? 30.567 6.696   0.401   0.66 14.98 ?  43  LEU   A O    1 
ATOM   1123 O  O    B LEU   A 1 43  ? 30.475 6.758   0.326   0.34 14.79 ?  43  LEU   A O    1 
ATOM   1124 C  CB   A LEU   A 1 43  ? 31.837 4.228   0.358   0.66 14.48 ?  43  LEU   A CB   1 
ATOM   1125 C  CB   B LEU   A 1 43  ? 31.805 4.326   0.369   0.34 13.63 ?  43  LEU   A CB   1 
ATOM   1126 C  CG   A LEU   A 1 43  ? 32.338 2.783   0.382   0.66 14.60 ?  43  LEU   A CG   1 
ATOM   1127 C  CG   B LEU   A 1 43  ? 32.256 2.879   0.591   0.34 13.35 ?  43  LEU   A CG   1 
ATOM   1128 C  CD1  A LEU   A 1 43  ? 33.383 2.626   1.472   0.66 14.91 ?  43  LEU   A CD1  1 
ATOM   1129 C  CD1  B LEU   A 1 43  ? 33.315 2.833   1.684   0.34 13.34 ?  43  LEU   A CD1  1 
ATOM   1130 C  CD2  A LEU   A 1 43  ? 31.200 1.788   0.580   0.66 14.36 ?  43  LEU   A CD2  1 
ATOM   1131 C  CD2  B LEU   A 1 43  ? 31.084 1.963   0.934   0.34 13.04 ?  43  LEU   A CD2  1 
ATOM   1132 H  H    A LEU   A 1 43  ? 30.861 3.501   -2.347  0.66 16.70 ?  43  LEU   A H    1 
ATOM   1133 H  H    B LEU   A 1 43  ? 30.852 3.510   -2.340  0.34 16.52 ?  43  LEU   A H    1 
ATOM   1134 H  HA   A LEU   A 1 43  ? 30.006 3.999   -0.486  0.66 16.55 ?  43  LEU   A HA   1 
ATOM   1135 H  HA   B LEU   A 1 43  ? 29.988 4.013   -0.487  0.34 16.59 ?  43  LEU   A HA   1 
ATOM   1136 H  HB2  A LEU   A 1 43  ? 32.604 4.799   0.205   0.66 17.43 ?  43  LEU   A HB2  1 
ATOM   1137 H  HB2  B LEU   A 1 43  ? 32.594 4.840   0.141   0.34 16.41 ?  43  LEU   A HB2  1 
ATOM   1138 H  HB3  A LEU   A 1 43  ? 31.464 4.415   1.235   0.66 17.43 ?  43  LEU   A HB3  1 
ATOM   1139 H  HB3  B LEU   A 1 43  ? 31.451 4.638   1.216   0.34 16.41 ?  43  LEU   A HB3  1 
ATOM   1140 H  HG   A LEU   A 1 43  ? 32.766 2.580   -0.467  0.66 17.58 ?  43  LEU   A HG   1 
ATOM   1141 H  HG   B LEU   A 1 43  ? 32.661 2.549   -0.226  0.34 16.08 ?  43  LEU   A HG   1 
ATOM   1142 H  HD11 A LEU   A 1 43  ? 33.699 1.707   1.479   0.66 17.95 ?  43  LEU   A HD11 1 
ATOM   1143 H  HD11 B LEU   A 1 43  ? 33.595 1.913   1.815   0.34 16.07 ?  43  LEU   A HD11 1 
ATOM   1144 H  HD12 A LEU   A 1 43  ? 34.122 3.226   1.290   0.66 17.95 ?  43  LEU   A HD12 1 
ATOM   1145 H  HD12 B LEU   A 1 43  ? 34.074 3.373   1.411   0.34 16.07 ?  43  LEU   A HD12 1 
ATOM   1146 H  HD13 A LEU   A 1 43  ? 32.981 2.843   2.327   0.66 17.95 ?  43  LEU   A HD13 1 
ATOM   1147 H  HD13 B LEU   A 1 43  ? 32.938 3.184   2.505   0.34 16.07 ?  43  LEU   A HD13 1 
ATOM   1148 H  HD21 A LEU   A 1 43  ? 31.572 0.901   0.700   0.66 17.28 ?  43  LEU   A HD21 1 
ATOM   1149 H  HD21 B LEU   A 1 43  ? 31.428 1.093   1.184   0.34 15.70 ?  43  LEU   A HD21 1 
ATOM   1150 H  HD22 A LEU   A 1 43  ? 30.694 2.045   1.366   0.66 17.28 ?  43  LEU   A HD22 1 
ATOM   1151 H  HD22 B LEU   A 1 43  ? 30.588 2.351   1.670   0.34 15.70 ?  43  LEU   A HD22 1 
ATOM   1152 H  HD23 A LEU   A 1 43  ? 30.628 1.805   -0.203  0.66 17.28 ?  43  LEU   A HD23 1 
ATOM   1153 H  HD23 B LEU   A 1 43  ? 30.513 1.883   0.154   0.34 15.70 ?  43  LEU   A HD23 1 
ATOM   1154 N  N    A LYS   A 1 44  ? 29.590 6.461   -1.618  0.66 13.59 ?  44  LYS   A N    1 
ATOM   1155 N  N    B LYS   A 1 44  ? 29.489 6.434   -1.668  0.34 14.42 ?  44  LYS   A N    1 
ATOM   1156 C  CA   A LYS   A 1 44  ? 28.954 7.780   -1.621  0.66 14.28 ?  44  LYS   A CA   1 
ATOM   1157 C  CA   B LYS   A 1 44  ? 28.820 7.735   -1.691  0.34 15.25 ?  44  LYS   A CA   1 
ATOM   1158 C  C    A LYS   A 1 44  ? 27.518 7.594   -1.145  0.66 13.45 ?  44  LYS   A C    1 
ATOM   1159 C  C    B LYS   A 1 44  ? 27.416 7.548   -1.132  0.34 14.51 ?  44  LYS   A C    1 
ATOM   1160 O  O    A LYS   A 1 44  ? 26.665 7.080   -1.874  0.66 14.48 ?  44  LYS   A O    1 
ATOM   1161 O  O    B LYS   A 1 44  ? 26.514 7.071   -1.825  0.34 14.73 ?  44  LYS   A O    1 
ATOM   1162 C  CB   A LYS   A 1 44  ? 29.018 8.398   -3.010  0.66 16.32 ?  44  LYS   A CB   1 
ATOM   1163 C  CB   B LYS   A 1 44  ? 28.801 8.305   -3.106  0.34 17.34 ?  44  LYS   A CB   1 
ATOM   1164 C  CG   A LYS   A 1 44  ? 30.410 8.836   -3.438  0.66 19.55 ?  44  LYS   A CG   1 
ATOM   1165 C  CG   B LYS   A 1 44  ? 30.138 8.861   -3.576  0.34 19.66 ?  44  LYS   A CG   1 
ATOM   1166 C  CD   A LYS   A 1 44  ? 31.070 9.768   -2.423  0.66 23.79 ?  44  LYS   A CD   1 
ATOM   1167 C  CD   B LYS   A 1 44  ? 30.736 9.822   -2.553  0.34 22.46 ?  44  LYS   A CD   1 
ATOM   1168 C  CE   A LYS   A 1 44  ? 32.407 10.277  -2.929  0.66 26.43 ?  44  LYS   A CE   1 
ATOM   1169 C  CE   B LYS   A 1 44  ? 32.091 10.328  -2.993  0.34 24.35 ?  44  LYS   A CE   1 
ATOM   1170 N  NZ   A LYS   A 1 44  ? 33.239 10.844  -1.836  0.66 27.48 ?  44  LYS   A NZ   1 
ATOM   1171 N  NZ   B LYS   A 1 44  ? 32.845 10.940  -1.867  0.34 25.52 ?  44  LYS   A NZ   1 
ATOM   1172 H  H    A LYS   A 1 44  ? 29.456 6.011   -2.342  0.66 16.36 ?  44  LYS   A H    1 
ATOM   1173 H  H    B LYS   A 1 44  ? 29.360 5.968   -2.380  0.34 17.36 ?  44  LYS   A H    1 
ATOM   1174 H  HA   A LYS   A 1 44  ? 29.406 8.358   -0.987  0.66 17.19 ?  44  LYS   A HA   1 
ATOM   1175 H  HA   B LYS   A 1 44  ? 29.280 8.345   -1.094  0.34 18.36 ?  44  LYS   A HA   1 
ATOM   1176 H  HB2  A LYS   A 1 44  ? 28.701 7.750   -3.656  0.66 19.64 ?  44  LYS   A HB2  1 
ATOM   1177 H  HB2  B LYS   A 1 44  ? 28.545 7.600   -3.724  0.34 20.86 ?  44  LYS   A HB2  1 
ATOM   1178 H  HB3  A LYS   A 1 44  ? 28.447 9.184   -3.027  0.66 19.64 ?  44  LYS   A HB3  1 
ATOM   1179 H  HB3  B LYS   A 1 44  ? 28.154 9.026   -3.148  0.34 20.86 ?  44  LYS   A HB3  1 
ATOM   1180 H  HG2  A LYS   A 1 44  ? 30.975 8.051   -3.538  0.66 23.51 ?  44  LYS   A HG2  1 
ATOM   1181 H  HG2  B LYS   A 1 44  ? 30.763 8.131   -3.709  0.34 23.64 ?  44  LYS   A HG2  1 
ATOM   1182 H  HG3  A LYS   A 1 44  ? 30.352 9.309   -4.285  0.66 23.51 ?  44  LYS   A HG3  1 
ATOM   1183 H  HG3  B LYS   A 1 44  ? 30.012 9.348   -4.409  0.34 23.64 ?  44  LYS   A HG3  1 
ATOM   1184 H  HD2  A LYS   A 1 44  ? 30.485 10.524  -2.260  0.66 28.60 ?  44  LYS   A HD2  1 
ATOM   1185 H  HD2  B LYS   A 1 44  ? 30.135 10.575  -2.432  0.34 27.00 ?  44  LYS   A HD2  1 
ATOM   1186 H  HD3  A LYS   A 1 44  ? 31.228 9.280   -1.598  0.66 28.60 ?  44  LYS   A HD3  1 
ATOM   1187 H  HD3  B LYS   A 1 44  ? 30.874 9.363   -1.710  0.34 27.00 ?  44  LYS   A HD3  1 
ATOM   1188 H  HE2  A LYS   A 1 44  ? 32.896 9.540   -3.329  0.66 31.77 ?  44  LYS   A HE2  1 
ATOM   1189 H  HE2  B LYS   A 1 44  ? 32.611 9.583   -3.335  0.34 29.27 ?  44  LYS   A HE2  1 
ATOM   1190 H  HE3  A LYS   A 1 44  ? 32.252 10.971  -3.587  0.66 31.77 ?  44  LYS   A HE3  1 
ATOM   1191 H  HE3  B LYS   A 1 44  ? 31.972 10.998  -3.679  0.34 29.27 ?  44  LYS   A HE3  1 
ATOM   1192 H  HZ1  A LYS   A 1 44  ? 34.011 11.136  -2.163  0.66 33.04 ?  44  LYS   A HZ1  1 
ATOM   1193 H  HZ1  B LYS   A 1 44  ? 33.638 11.228  -2.153  0.34 30.68 ?  44  LYS   A HZ1  1 
ATOM   1194 H  HZ2  A LYS   A 1 44  ? 32.810 11.528  -1.455  0.66 33.04 ?  44  LYS   A HZ2  1 
ATOM   1195 H  HZ2  B LYS   A 1 44  ? 32.390 11.629  -1.534  0.34 30.68 ?  44  LYS   A HZ2  1 
ATOM   1196 H  HZ3  A LYS   A 1 44  ? 33.396 10.224  -1.220  0.66 33.04 ?  44  LYS   A HZ3  1 
ATOM   1197 H  HZ3  B LYS   A 1 44  ? 32.973 10.340  -1.221  0.34 30.68 ?  44  LYS   A HZ3  1 
ATOM   1198 N  N    A HIS   A 1 45  ? 27.275 7.957   0.110   0.66 13.30 ?  45  HIS   A N    1 
ATOM   1199 N  N    B HIS   A 1 45  ? 27.237 7.912   0.137   0.34 14.24 ?  45  HIS   A N    1 
ATOM   1200 C  CA   A HIS   A 1 45  ? 26.035 7.602   0.801   0.66 13.41 ?  45  HIS   A CA   1 
ATOM   1201 C  CA   B HIS   A 1 45  ? 25.985 7.668   0.852   0.34 14.21 ?  45  HIS   A CA   1 
ATOM   1202 C  C    A HIS   A 1 45  ? 24.999 8.716   0.638   0.66 13.98 ?  45  HIS   A C    1 
ATOM   1203 C  C    B HIS   A 1 45  ? 25.050 8.849   0.632   0.34 14.84 ?  45  HIS   A C    1 
ATOM   1204 O  O    A HIS   A 1 45  ? 24.630 9.421   1.581   0.66 13.91 ?  45  HIS   A O    1 
ATOM   1205 O  O    B HIS   A 1 45  ? 24.986 9.781   1.436   0.34 15.68 ?  45  HIS   A O    1 
ATOM   1206 C  CB   A HIS   A 1 45  ? 26.328 7.330   2.265   0.66 13.39 ?  45  HIS   A CB   1 
ATOM   1207 C  CB   B HIS   A 1 45  ? 26.260 7.450   2.332   0.34 13.57 ?  45  HIS   A CB   1 
ATOM   1208 C  CG   A HIS   A 1 45  ? 27.443 6.361   2.480   0.66 13.44 ?  45  HIS   A CG   1 
ATOM   1209 C  CG   B HIS   A 1 45  ? 27.389 6.508   2.596   0.34 13.09 ?  45  HIS   A CG   1 
ATOM   1210 N  ND1  A HIS   A 1 45  ? 27.428 5.074   1.981   0.66 13.71 ?  45  HIS   A ND1  1 
ATOM   1211 N  ND1  B HIS   A 1 45  ? 27.390 5.202   2.155   0.34 13.26 ?  45  HIS   A ND1  1 
ATOM   1212 C  CD2  A HIS   A 1 45  ? 28.620 6.500   3.132   0.66 13.90 ?  45  HIS   A CD2  1 
ATOM   1213 C  CD2  B HIS   A 1 45  ? 28.561 6.687   3.248   0.34 12.59 ?  45  HIS   A CD2  1 
ATOM   1214 C  CE1  A HIS   A 1 45  ? 28.545 4.462   2.331   0.66 14.08 ?  45  HIS   A CE1  1 
ATOM   1215 C  CE1  B HIS   A 1 45  ? 28.513 4.617   2.530   0.34 12.60 ?  45  HIS   A CE1  1 
ATOM   1216 N  NE2  A HIS   A 1 45  ? 29.290 5.308   3.020   0.66 14.30 ?  45  HIS   A NE2  1 
ATOM   1217 N  NE2  B HIS   A 1 45  ? 29.243 5.497   3.191   0.34 12.51 ?  45  HIS   A NE2  1 
ATOM   1218 H  H    A HIS   A 1 45  ? 27.816 8.426   0.588   0.66 16.01 ?  45  HIS   A H    1 
ATOM   1219 H  H    B HIS   A 1 45  ? 27.836 8.307   0.613   0.34 17.14 ?  45  HIS   A H    1 
ATOM   1220 H  HA   A HIS   A 1 45  ? 25.674 6.791   0.411   0.66 16.15 ?  45  HIS   A HA   1 
ATOM   1221 H  HA   B HIS   A 1 45  ? 25.563 6.874   0.496   0.34 17.10 ?  45  HIS   A HA   1 
ATOM   1222 H  HB2  A HIS   A 1 45  ? 26.570 8.160   2.701   0.66 16.13 ?  45  HIS   A HB2  1 
ATOM   1223 H  HB2  B HIS   A 1 45  ? 26.480 8.301   2.740   0.34 16.34 ?  45  HIS   A HB2  1 
ATOM   1224 H  HB3  A HIS   A 1 45  ? 25.533 6.958   2.682   0.66 16.13 ?  45  HIS   A HB3  1 
ATOM   1225 H  HB3  B HIS   A 1 45  ? 25.464 7.081   2.745   0.34 16.34 ?  45  HIS   A HB3  1 
ATOM   1226 H  HD2  A HIS   A 1 45  ? 28.929 7.264   3.565   0.66 16.74 ?  45  HIS   A HD2  1 
ATOM   1227 H  HD2  B HIS   A 1 45  ? 28.852 7.474   3.653   0.34 15.16 ?  45  HIS   A HD2  1 
ATOM   1228 H  HE1  A HIS   A 1 45  ? 28.773 3.577   2.128   0.66 16.95 ?  45  HIS   A HE1  1 
ATOM   1229 H  HE1  B HIS   A 1 45  ? 28.750 3.735   2.355   0.34 15.17 ?  45  HIS   A HE1  1 
ATOM   1230 H  HE2  A HIS   A 1 45  ? 30.067 5.131   3.357   0.66 17.21 ?  45  HIS   A HE2  1 
ATOM   1231 H  HE2  B HIS   A 1 45  ? 30.016 5.348   3.534   0.34 15.07 ?  45  HIS   A HE2  1 
ATOM   1232 N  N    A GLY   A 1 46  ? 24.510 8.850   -0.591  0.66 15.24 ?  46  GLY   A N    1 
ATOM   1233 N  N    B GLY   A 1 46  ? 24.302 8.805   -0.463  0.34 14.91 ?  46  GLY   A N    1 
ATOM   1234 C  CA   A GLY   A 1 46  ? 23.728 10.018  -0.957  0.66 15.37 ?  46  GLY   A CA   1 
ATOM   1235 C  CA   B GLY   A 1 46  ? 23.441 9.916   -0.810  0.34 14.47 ?  46  GLY   A CA   1 
ATOM   1236 C  C    A GLY   A 1 46  ? 22.228 9.911   -0.749  0.66 15.16 ?  46  GLY   A C    1 
ATOM   1237 C  C    B GLY   A 1 46  ? 21.999 9.769   -0.368  0.34 13.78 ?  46  GLY   A C    1 
ATOM   1238 O  O    A GLY   A 1 46  ? 21.559 10.921  -0.490  0.66 14.81 ?  46  GLY   A O    1 
ATOM   1239 O  O    B GLY   A 1 46  ? 21.401 10.730  0.131   0.34 13.94 ?  46  GLY   A O    1 
ATOM   1240 H  H    A GLY   A 1 46  ? 24.605 8.273   -1.221  0.66 18.34 ?  46  GLY   A H    1 
ATOM   1241 H  H    B GLY   A 1 46  ? 24.280 8.147   -1.018  0.34 17.95 ?  46  GLY   A H    1 
ATOM   1242 H  HA2  A GLY   A 1 46  ? 24.047 10.775  -0.439  0.66 18.49 ?  46  GLY   A HA2  1 
ATOM   1243 H  HA2  B GLY   A 1 46  ? 23.781 10.723  -0.398  0.34 17.42 ?  46  GLY   A HA2  1 
ATOM   1244 H  HA3  A GLY   A 1 46  ? 23.885 10.212  -1.893  0.66 18.49 ?  46  GLY   A HA3  1 
ATOM   1245 H  HA3  B GLY   A 1 46  ? 23.460 10.037  -1.770  0.34 17.42 ?  46  GLY   A HA3  1 
ATOM   1246 N  N    A GLY   A 1 47  ? 21.687 8.702   -0.864  0.66 15.07 ?  47  GLY   A N    1 
ATOM   1247 N  N    B GLY   A 1 47  ? 21.426 8.579   -0.541  0.34 13.35 ?  47  GLY   A N    1 
ATOM   1248 C  CA   A GLY   A 1 47  ? 20.251 8.507   -0.835  0.66 14.85 ?  47  GLY   A CA   1 
ATOM   1249 C  CA   B GLY   A 1 47  ? 20.009 8.390   -0.313  0.34 12.98 ?  47  GLY   A CA   1 
ATOM   1250 C  C    A GLY   A 1 47  ? 19.936 7.064   -0.506  0.66 14.41 ?  47  GLY   A C    1 
ATOM   1251 C  C    B GLY   A 1 47  ? 19.678 6.958   0.041   0.34 12.00 ?  47  GLY   A C    1 
ATOM   1252 O  O    A GLY   A 1 47  ? 20.831 6.239   -0.309  0.66 14.56 ?  47  GLY   A O    1 
ATOM   1253 O  O    B GLY   A 1 47  ? 20.561 6.111   0.202   0.34 12.09 ?  47  GLY   A O    1 
ATOM   1254 H  H    A GLY   A 1 47  ? 22.138 7.982   -0.943  0.66 18.14 ?  47  GLY   A H    1 
ATOM   1255 H  H    B GLY   A 1 47  ? 21.846 7.869   -0.787  0.34 16.07 ?  47  GLY   A H    1 
ATOM   1256 H  HA2  A GLY   A 1 47  ? 19.844 9.096   -0.173  0.66 17.88 ?  47  GLY   A HA2  1 
ATOM   1257 H  HA2  B GLY   A 1 47  ? 19.720 8.948   0.421   0.34 15.63 ?  47  GLY   A HA2  1 
ATOM   1258 H  HA3  A GLY   A 1 47  ? 19.875 8.711   -1.705  0.66 17.88 ?  47  GLY   A HA3  1 
ATOM   1259 H  HA3  B GLY   A 1 47  ? 19.511 8.644   -1.109  0.34 15.63 ?  47  GLY   A HA3  1 
ATOM   1260 N  N    A GLY   A 1 48  ? 18.645 6.753   -0.479  0.66 14.53 ?  48  GLY   A N    1 
ATOM   1261 N  N    B GLY   A 1 48  ? 18.376 6.694   0.164   0.34 11.88 ?  48  GLY   A N    1 
ATOM   1262 C  CA   A GLY   A 1 48  ? 18.248 5.419   -0.094  0.66 14.18 ?  48  GLY   A CA   1 
ATOM   1263 C  CA   B GLY   A 1 48  ? 17.935 5.369   0.560   0.34 11.14 ?  48  GLY   A CA   1 
ATOM   1264 C  C    A GLY   A 1 48  ? 18.656 5.117   1.333   0.66 13.89 ?  48  GLY   A C    1 
ATOM   1265 C  C    B GLY   A 1 48  ? 18.541 4.974   1.891   0.34 11.51 ?  48  GLY   A C    1 
ATOM   1266 O  O    A GLY   A 1 48  ? 18.832 6.017   2.167   0.66 13.81 ?  48  GLY   A O    1 
ATOM   1267 O  O    B GLY   A 1 48  ? 18.706 5.794   2.803   0.34 11.47 ?  48  GLY   A O    1 
ATOM   1268 H  H    A GLY   A 1 48  ? 18.000 7.279   -0.674  0.66 17.49 ?  48  GLY   A H    1 
ATOM   1269 H  H    B GLY   A 1 48  ? 17.734 7.267   0.027   0.34 14.31 ?  48  GLY   A H    1 
ATOM   1270 H  HA2  A GLY   A 1 48  ? 17.290 5.322   -0.170  0.66 17.07 ?  48  GLY   A HA2  1 
ATOM   1271 H  HA2  B GLY   A 1 48  ? 16.965 5.349   0.640   0.34 13.43 ?  48  GLY   A HA2  1 
ATOM   1272 H  HA3  A GLY   A 1 48  ? 18.680 4.768   -0.665  0.66 17.07 ?  48  GLY   A HA3  1 
ATOM   1273 H  HA3  B GLY   A 1 48  ? 18.199 4.718   -0.113  0.34 13.43 ?  48  GLY   A HA3  1 
ATOM   1274 N  N    A VAL   A 1 49  ? 18.823 3.821   1.615   0.66 14.65 ?  49  VAL   A N    1 
ATOM   1275 N  N    B VAL   A 1 49  ? 18.885 3.692   2.000   0.34 11.96 ?  49  VAL   A N    1 
ATOM   1276 C  CA   A VAL   A 1 49  ? 19.265 3.390   2.939   0.66 14.83 ?  49  VAL   A CA   1 
ATOM   1277 C  CA   B VAL   A 1 49  ? 19.503 3.181   3.218   0.34 12.20 ?  49  VAL   A CA   1 
ATOM   1278 C  C    A VAL   A 1 49  ? 20.587 4.046   3.308   0.66 14.25 ?  49  VAL   A C    1 
ATOM   1279 C  C    B VAL   A 1 49  ? 20.772 3.959   3.541   0.34 12.07 ?  49  VAL   A C    1 
ATOM   1280 O  O    A VAL   A 1 49  ? 20.788 4.445   4.458   0.66 15.05 ?  49  VAL   A O    1 
ATOM   1281 O  O    B VAL   A 1 49  ? 20.980 4.392   4.680   0.34 12.36 ?  49  VAL   A O    1 
ATOM   1282 C  CB   A VAL   A 1 49  ? 19.365 1.852   3.000   0.66 16.11 ?  49  VAL   A CB   1 
ATOM   1283 C  CB   B VAL   A 1 49  ? 19.777 1.673   3.082   0.34 12.46 ?  49  VAL   A CB   1 
ATOM   1284 C  CG1  A VAL   A 1 49  ? 20.097 1.405   4.268   0.66 16.28 ?  49  VAL   A CG1  1 
ATOM   1285 C  CG1  B VAL   A 1 49  ? 20.653 1.204   4.217   0.34 12.10 ?  49  VAL   A CG1  1 
ATOM   1286 C  CG2  A VAL   A 1 49  ? 17.980 1.223   2.935   0.66 17.62 ?  49  VAL   A CG2  1 
ATOM   1287 C  CG2  B VAL   A 1 49  ? 18.467 0.898   3.053   0.34 13.21 ?  49  VAL   A CG2  1 
ATOM   1288 H  H    A VAL   A 1 49  ? 18.687 3.173   1.066   0.66 17.64 ?  49  VAL   A H    1 
ATOM   1289 H  H    B VAL   A 1 49  ? 18.768 3.105   1.386   0.34 14.41 ?  49  VAL   A H    1 
ATOM   1290 H  HA   A VAL   A 1 49  ? 18.615 3.659   3.601   0.66 17.86 ?  49  VAL   A HA   1 
ATOM   1291 H  HA   B VAL   A 1 49  ? 18.891 3.302   3.956   0.34 14.69 ?  49  VAL   A HA   1 
ATOM   1292 H  HB   A VAL   A 1 49  ? 19.881 1.529   2.245   0.66 19.39 ?  49  VAL   A HB   1 
ATOM   1293 H  HB   B VAL   A 1 49  ? 20.245 1.501   2.248   0.34 15.01 ?  49  VAL   A HB   1 
ATOM   1294 H  HG11 A VAL   A 1 49  ? 19.905 0.468   4.431   0.66 19.59 ?  49  VAL   A HG11 1 
ATOM   1295 H  HG11 B VAL   A 1 49  ? 20.569 0.242   4.303   0.34 14.57 ?  49  VAL   A HG11 1 
ATOM   1296 H  HG12 A VAL   A 1 49  ? 21.052 1.529   4.150   0.66 19.59 ?  49  VAL   A HG12 1 
ATOM   1297 H  HG12 B VAL   A 1 49  ? 21.576 1.436   4.023   0.34 14.57 ?  49  VAL   A HG12 1 
ATOM   1298 H  HG13 A VAL   A 1 49  ? 19.782 1.938   5.017   0.66 19.59 ?  49  VAL   A HG13 1 
ATOM   1299 H  HG13 B VAL   A 1 49  ? 20.365 1.635   5.036   0.34 14.57 ?  49  VAL   A HG13 1 
ATOM   1300 H  HG21 A VAL   A 1 49  ? 18.069 0.259   2.975   0.66 21.20 ?  49  VAL   A HG21 1 
ATOM   1301 H  HG21 B VAL   A 1 49  ? 18.656 -0.047  2.959   0.34 15.91 ?  49  VAL   A HG21 1 
ATOM   1302 H  HG22 A VAL   A 1 49  ? 17.460 1.541   3.690   0.66 21.20 ?  49  VAL   A HG22 1 
ATOM   1303 H  HG22 B VAL   A 1 49  ? 17.988 1.060   3.882   0.34 15.91 ?  49  VAL   A HG22 1 
ATOM   1304 H  HG23 A VAL   A 1 49  ? 17.563 1.489   2.105   0.66 21.20 ?  49  VAL   A HG23 1 
ATOM   1305 H  HG23 B VAL   A 1 49  ? 17.935 1.206   2.301   0.34 15.91 ?  49  VAL   A HG23 1 
ATOM   1306 N  N    A ALA   A 1 50  ? 21.528 4.108   2.359   0.66 13.85 ?  50  ALA   A N    1 
ATOM   1307 N  N    B ALA   A 1 50  ? 21.644 4.133   2.543   0.34 12.23 ?  50  ALA   A N    1 
ATOM   1308 C  CA   A ALA   A 1 50  ? 22.850 4.654   2.661   0.66 14.23 ?  50  ALA   A CA   1 
ATOM   1309 C  CA   B ALA   A 1 50  ? 22.955 4.724   2.796   0.34 12.13 ?  50  ALA   A CA   1 
ATOM   1310 C  C    A ALA   A 1 50  ? 22.767 6.122   3.045   0.66 13.75 ?  50  ALA   A C    1 
ATOM   1311 C  C    B ALA   A 1 50  ? 22.828 6.160   3.287   0.34 12.04 ?  50  ALA   A C    1 
ATOM   1312 O  O    A ALA   A 1 50  ? 23.414 6.556   4.005   0.66 14.24 ?  50  ALA   A O    1 
ATOM   1313 O  O    B ALA   A 1 50  ? 23.416 6.533   4.310   0.34 12.35 ?  50  ALA   A O    1 
ATOM   1314 C  CB   A ALA   A 1 50  ? 23.779 4.472   1.460   0.66 14.77 ?  50  ALA   A CB   1 
ATOM   1315 C  CB   B ALA   A 1 50  ? 23.815 4.642   1.532   0.34 12.13 ?  50  ALA   A CB   1 
ATOM   1316 H  H    A ALA   A 1 50  ? 21.429 3.839   1.552   0.66 16.67 ?  50  ALA   A H    1 
ATOM   1317 H  H    B ALA   A 1 50  ? 21.498 3.924   1.719   0.34 14.73 ?  50  ALA   A H    1 
ATOM   1318 H  HA   A ALA   A 1 50  ? 23.233 4.171   3.410   0.66 17.14 ?  50  ALA   A HA   1 
ATOM   1319 H  HA   B ALA   A 1 50  ? 23.402 4.220   3.488   0.34 14.61 ?  50  ALA   A HA   1 
ATOM   1320 H  HB1  A ALA   A 1 50  ? 24.650 4.843   1.673   0.66 17.78 ?  50  ALA   A HB1  1 
ATOM   1321 H  HB1  B ALA   A 1 50  ? 24.684 5.035   1.710   0.34 14.61 ?  50  ALA   A HB1  1 
ATOM   1322 H  HB2  A ALA   A 1 50  ? 23.862 3.526   1.262   0.66 17.78 ?  50  ALA   A HB2  1 
ATOM   1323 H  HB2  B ALA   A 1 50  ? 23.923 3.708   1.280   0.34 14.61 ?  50  ALA   A HB2  1 
ATOM   1324 H  HB3  A ALA   A 1 50  ? 23.401 4.936   0.695   0.66 17.78 ?  50  ALA   A HB3  1 
ATOM   1325 H  HB3  B ALA   A 1 50  ? 23.375 5.124   0.813   0.34 14.61 ?  50  ALA   A HB3  1 
ATOM   1326 N  N    A GLY   A 1 51  ? 21.992 6.906   2.297   0.66 13.72 ?  51  GLY   A N    1 
ATOM   1327 N  N    B GLY   A 1 51  ? 22.050 6.980   2.579   0.34 12.13 ?  51  GLY   A N    1 
ATOM   1328 C  CA   A GLY   A 1 51  ? 21.820 8.303   2.653   0.66 14.09 ?  51  GLY   A CA   1 
ATOM   1329 C  CA   B GLY   A 1 51  ? 21.873 8.356   3.013   0.34 12.11 ?  51  GLY   A CA   1 
ATOM   1330 C  C    A GLY   A 1 51  ? 21.223 8.474   4.034   0.66 14.00 ?  51  GLY   A C    1 
ATOM   1331 C  C    B GLY   A 1 51  ? 21.244 8.440   4.390   0.34 12.22 ?  51  GLY   A C    1 
ATOM   1332 O  O    A GLY   A 1 51  ? 21.613 9.374   4.783   0.66 14.58 ?  51  GLY   A O    1 
ATOM   1333 O  O    B GLY   A 1 51  ? 21.609 9.294   5.204   0.34 12.78 ?  51  GLY   A O    1 
ATOM   1334 H  H    A GLY   A 1 51  ? 21.578 6.658   1.586   0.66 16.52 ?  51  GLY   A H    1 
ATOM   1335 H  H    B GLY   A 1 51  ? 21.617 6.767   1.863   0.34 14.61 ?  51  GLY   A H    1 
ATOM   1336 H  HA2  A GLY   A 1 51  ? 22.677 8.754   2.634   0.66 16.96 ?  51  GLY   A HA2  1 
ATOM   1337 H  HA2  B GLY   A 1 51  ? 22.735 8.801   3.038   0.34 14.59 ?  51  GLY   A HA2  1 
ATOM   1338 H  HA3  A GLY   A 1 51  ? 21.230 8.731   2.015   0.66 16.96 ?  51  GLY   A HA3  1 
ATOM   1339 H  HA3  B GLY   A 1 51  ? 21.308 8.827   2.373   0.34 14.59 ?  51  GLY   A HA3  1 
ATOM   1340 N  N    A ALA   A 1 52  ? 20.262 7.613   4.388   0.66 14.35 ?  52  ALA   A N    1 
ATOM   1341 N  N    B ALA   A 1 52  ? 20.298 7.542   4.675   0.34 12.74 ?  52  ALA   A N    1 
ATOM   1342 C  CA   A ALA   A 1 52  ? 19.624 7.711   5.696   0.66 14.86 ?  52  ALA   A CA   1 
ATOM   1343 C  CA   B ALA   A 1 52  ? 19.616 7.563   5.963   0.34 13.13 ?  52  ALA   A CA   1 
ATOM   1344 C  C    A ALA   A 1 52  ? 20.559 7.257   6.813   0.66 14.42 ?  52  ALA   A C    1 
ATOM   1345 C  C    B ALA   A 1 52  ? 20.560 7.175   7.097   0.34 12.64 ?  52  ALA   A C    1 
ATOM   1346 O  O    A ALA   A 1 52  ? 20.640 7.909   7.859   0.66 15.01 ?  52  ALA   A O    1 
ATOM   1347 O  O    B ALA   A 1 52  ? 20.591 7.830   8.146   0.34 13.30 ?  52  ALA   A O    1 
ATOM   1348 C  CB   A ALA   A 1 52  ? 18.315 6.920   5.703   0.66 15.82 ?  52  ALA   A CB   1 
ATOM   1349 C  CB   B ALA   A 1 52  ? 18.406 6.633   5.913   0.34 13.94 ?  52  ALA   A CB   1 
ATOM   1350 H  H    A ALA   A 1 52  ? 19.985 6.957   3.904   0.66 17.27 ?  52  ALA   A H    1 
ATOM   1351 H  H    B ALA   A 1 52  ? 20.046 6.913   4.140   0.34 15.34 ?  52  ALA   A H    1 
ATOM   1352 H  HA   A ALA   A 1 52  ? 19.407 8.633   5.864   0.66 17.88 ?  52  ALA   A HA   1 
ATOM   1353 H  HA   B ALA   A 1 52  ? 19.300 8.462   6.127   0.34 15.81 ?  52  ALA   A HA   1 
ATOM   1354 H  HB1  A ALA   A 1 52  ? 17.897 6.999   6.579   0.66 19.03 ?  52  ALA   A HB1  1 
ATOM   1355 H  HB1  B ALA   A 1 52  ? 17.938 6.687   6.758   0.34 16.79 ?  52  ALA   A HB1  1 
ATOM   1356 H  HB2  A ALA   A 1 52  ? 17.722 7.285   5.026   0.66 19.03 ?  52  ALA   A HB2  1 
ATOM   1357 H  HB2  B ALA   A 1 52  ? 17.821 6.919   5.192   0.34 16.79 ?  52  ALA   A HB2  1 
ATOM   1358 H  HB3  A ALA   A 1 52  ? 18.498 5.986   5.512   0.66 19.03 ?  52  ALA   A HB3  1 
ATOM   1359 H  HB3  B ALA   A 1 52  ? 18.709 5.727   5.752   0.34 16.79 ?  52  ALA   A HB3  1 
ATOM   1360 N  N    A LEU   A 1 53  ? 21.277 6.145   6.618   0.66 14.29 ?  53  LEU   A N    1 
ATOM   1361 N  N    B LEU   A 1 53  ? 21.334 6.103   6.913   0.34 12.18 ?  53  LEU   A N    1 
ATOM   1362 C  CA   A LEU   A 1 53  ? 22.229 5.703   7.635   0.66 14.65 ?  53  LEU   A CA   1 
ATOM   1363 C  CA   B LEU   A 1 53  ? 22.331 5.741   7.916   0.34 12.24 ?  53  LEU   A CA   1 
ATOM   1364 C  C    A LEU   A 1 53  ? 23.288 6.768   7.875   0.66 14.41 ?  53  LEU   A C    1 
ATOM   1365 C  C    B LEU   A 1 53  ? 23.347 6.863   8.090   0.34 12.58 ?  53  LEU   A C    1 
ATOM   1366 O  O    A LEU   A 1 53  ? 23.628 7.076   9.022   0.66 15.27 ?  53  LEU   A O    1 
ATOM   1367 O  O    B LEU   A 1 53  ? 23.621 7.303   9.212   0.34 12.92 ?  53  LEU   A O    1 
ATOM   1368 C  CB   A LEU   A 1 53  ? 22.878 4.375   7.225   0.66 15.07 ?  53  LEU   A CB   1 
ATOM   1369 C  CB   B LEU   A 1 53  ? 23.031 4.436   7.523   0.34 12.07 ?  53  LEU   A CB   1 
ATOM   1370 C  CG   A LEU   A 1 53  ? 22.000 3.118   7.298   0.66 15.70 ?  53  LEU   A CG   1 
ATOM   1371 C  CG   B LEU   A 1 53  ? 22.237 3.128   7.583   0.34 12.63 ?  53  LEU   A CG   1 
ATOM   1372 C  CD1  A LEU   A 1 53  ? 22.738 1.922   6.726   0.66 15.60 ?  53  LEU   A CD1  1 
ATOM   1373 C  CD1  B LEU   A 1 53  ? 23.053 2.007   6.965   0.34 13.04 ?  53  LEU   A CD1  1 
ATOM   1374 C  CD2  A LEU   A 1 53  ? 21.547 2.832   8.724   0.66 17.00 ?  53  LEU   A CD2  1 
ATOM   1375 C  CD2  B LEU   A 1 53  ? 21.866 2.780   9.010   0.34 13.26 ?  53  LEU   A CD2  1 
ATOM   1376 H  H    A LEU   A 1 53  ? 21.233 5.641   5.925   0.66 17.20 ?  53  LEU   A H    1 
ATOM   1377 H  H    B LEU   A 1 53  ? 21.298 5.576   6.231   0.34 14.67 ?  53  LEU   A H    1 
ATOM   1378 H  HA   A LEU   A 1 53  ? 21.762 5.554   8.470   0.66 17.64 ?  53  LEU   A HA   1 
ATOM   1379 H  HA   B LEU   A 1 53  ? 21.886 5.601   8.763   0.34 14.74 ?  53  LEU   A HA   1 
ATOM   1380 H  HB2  A LEU   A 1 53  ? 23.185 4.455   6.306   0.66 18.14 ?  53  LEU   A HB2  1 
ATOM   1381 H  HB2  B LEU   A 1 53  ? 23.347 4.529   6.610   0.34 14.54 ?  53  LEU   A HB2  1 
ATOM   1382 H  HB3  A LEU   A 1 53  ? 23.647 4.218   7.800   0.66 18.14 ?  53  LEU   A HB3  1 
ATOM   1383 H  HB3  B LEU   A 1 53  ? 23.797 4.322   8.108   0.34 14.54 ?  53  LEU   A HB3  1 
ATOM   1384 H  HG   A LEU   A 1 53  ? 21.211 3.262   6.757   0.66 18.89 ?  53  LEU   A HG   1 
ATOM   1385 H  HG   B LEU   A 1 53  ? 21.422 3.224   7.065   0.34 15.22 ?  53  LEU   A HG   1 
ATOM   1386 H  HD11 A LEU   A 1 53  ? 22.165 1.142   6.782   0.66 18.78 ?  53  LEU   A HD11 1 
ATOM   1387 H  HD11 B LEU   A 1 53  ? 22.543 1.182   7.010   0.34 15.70 ?  53  LEU   A HD11 1 
ATOM   1388 H  HD12 A LEU   A 1 53  ? 22.966 2.101   5.801   0.66 18.78 ?  53  LEU   A HD12 1 
ATOM   1389 H  HD12 B LEU   A 1 53  ? 23.245 2.225   6.039   0.34 15.70 ?  53  LEU   A HD12 1 
ATOM   1390 H  HD13 A LEU   A 1 53  ? 23.548 1.773   7.243   0.66 18.78 ?  53  LEU   A HD13 1 
ATOM   1391 H  HD13 B LEU   A 1 53  ? 23.882 1.909   7.459   0.34 15.70 ?  53  LEU   A HD13 1 
ATOM   1392 H  HD21 A LEU   A 1 53  ? 21.099 1.971   8.746   0.66 20.46 ?  53  LEU   A HD21 1 
ATOM   1393 H  HD21 B LEU   A 1 53  ? 21.226 2.050   8.996   0.34 15.97 ?  53  LEU   A HD21 1 
ATOM   1394 H  HD22 A LEU   A 1 53  ? 22.323 2.814   9.307   0.66 20.46 ?  53  LEU   A HD22 1 
ATOM   1395 H  HD22 B LEU   A 1 53  ? 22.663 2.515   9.487   0.34 15.97 ?  53  LEU   A HD22 1 
ATOM   1396 H  HD23 A LEU   A 1 53  ? 20.936 3.528   9.009   0.66 20.46 ?  53  LEU   A HD23 1 
ATOM   1397 H  HD23 B LEU   A 1 53  ? 21.467 3.557   9.431   0.34 15.97 ?  53  LEU   A HD23 1 
ATOM   1398 N  N    A ASN   A 1 54  ? 23.809 7.355   6.806   0.66 14.32 ?  54  ASN   A N    1 
ATOM   1399 N  N    B ASN   A 1 54  ? 23.903 7.351   6.983   0.34 12.84 ?  54  ASN   A N    1 
ATOM   1400 C  CA   A ASN   A 1 54  ? 24.870 8.331   6.972   0.66 14.29 ?  54  ASN   A CA   1 
ATOM   1401 C  CA   B ASN   A 1 54  ? 24.933 8.372   7.089   0.34 13.35 ?  54  ASN   A CA   1 
ATOM   1402 C  C    A ASN   A 1 54  ? 24.374 9.568   7.716   0.66 14.75 ?  54  ASN   A C    1 
ATOM   1403 C  C    B ASN   A 1 54  ? 24.391 9.634   7.742   0.34 14.03 ?  54  ASN   A C    1 
ATOM   1404 O  O    A ASN   A 1 54  ? 25.075 10.101  8.585   0.66 15.22 ?  54  ASN   A O    1 
ATOM   1405 O  O    B ASN   A 1 54  ? 25.072 10.252  8.570   0.34 14.06 ?  54  ASN   A O    1 
ATOM   1406 C  CB   A ASN   A 1 54  ? 25.430 8.702   5.612   0.66 14.52 ?  54  ASN   A CB   1 
ATOM   1407 C  CB   B ASN   A 1 54  ? 25.521 8.700   5.723   0.34 13.39 ?  54  ASN   A CB   1 
ATOM   1408 C  CG   A ASN   A 1 54  ? 26.479 9.768   5.716   0.66 14.89 ?  54  ASN   A CG   1 
ATOM   1409 C  CG   B ASN   A 1 54  ? 26.460 9.880   5.791   0.34 13.09 ?  54  ASN   A CG   1 
ATOM   1410 O  OD1  A ASN   A 1 54  ? 27.487 9.585   6.404   0.66 15.12 ?  54  ASN   A OD1  1 
ATOM   1411 O  OD1  B ASN   A 1 54  ? 27.500 9.807   6.445   0.34 12.40 ?  54  ASN   A OD1  1 
ATOM   1412 N  ND2  A ASN   A 1 54  ? 26.259 10.892  5.051   0.66 15.19 ?  54  ASN   A ND2  1 
ATOM   1413 N  ND2  B ASN   A 1 54  ? 26.093 10.981  5.146   0.34 13.73 ?  54  ASN   A ND2  1 
ATOM   1414 H  H    A ASN   A 1 54  ? 23.560 7.216   5.996   0.66 17.24 ?  54  ASN   A H    1 
ATOM   1415 H  H    B ASN   A 1 54  ? 23.695 7.123   6.181   0.34 15.46 ?  54  ASN   A H    1 
ATOM   1416 H  HA   A ASN   A 1 54  ? 25.584 7.934   7.496   0.66 17.21 ?  54  ASN   A HA   1 
ATOM   1417 H  HA   B ASN   A 1 54  ? 25.649 8.034   7.649   0.34 16.08 ?  54  ASN   A HA   1 
ATOM   1418 H  HB2  A ASN   A 1 54  ? 25.831 7.913   5.210   0.66 17.49 ?  54  ASN   A HB2  1 
ATOM   1419 H  HB2  B ASN   A 1 54  ? 26.021 7.933   5.400   0.34 16.12 ?  54  ASN   A HB2  1 
ATOM   1420 H  HB3  A ASN   A 1 54  ? 24.713 9.034   5.052   0.66 17.49 ?  54  ASN   A HB3  1 
ATOM   1421 H  HB3  B ASN   A 1 54  ? 24.804 8.917   5.110   0.34 16.12 ?  54  ASN   A HB3  1 
ATOM   1422 H  HD21 A ASN   A 1 54  ? 26.833 11.530  5.084   0.66 18.29 ?  54  ASN   A HD21 1 
ATOM   1423 H  HD21 B ASN   A 1 54  ? 26.595 11.682  5.167   0.34 16.53 ?  54  ASN   A HD21 1 
ATOM   1424 H  HD22 A ASN   A 1 54  ? 25.538 10.985  4.591   0.66 18.29 ?  54  ASN   A HD22 1 
ATOM   1425 H  HD22 B ASN   A 1 54  ? 25.356 10.996  4.705   0.34 16.53 ?  54  ASN   A HD22 1 
ATOM   1426 N  N    . LYS   A 1 55  ? 23.173 10.046  7.379   1.00 14.41 ?  55  LYS   A N    1 
ATOM   1427 C  CA   . LYS   A 1 55  ? 22.588 11.199  8.050   1.00 15.31 ?  55  LYS   A CA   1 
ATOM   1428 C  C    . LYS   A 1 55  ? 22.489 10.961  9.549   1.00 15.21 ?  55  LYS   A C    1 
ATOM   1429 O  O    . LYS   A 1 55  ? 22.771 11.863  10.352  1.00 16.58 ?  55  LYS   A O    1 
ATOM   1430 C  CB   . LYS   A 1 55  ? 21.219 11.499  7.441   1.00 16.07 ?  55  LYS   A CB   1 
ATOM   1431 C  CG   . LYS   A 1 55  ? 20.492 12.670  8.072   1.00 17.08 ?  55  LYS   A CG   1 
ATOM   1432 C  CD   . LYS   A 1 55  ? 19.162 12.926  7.361   1.00 17.66 ?  55  LYS   A CD   1 
ATOM   1433 C  CE   . LYS   A 1 55  ? 18.323 13.984  8.065   1.00 19.52 ?  55  LYS   A CE   1 
ATOM   1434 N  NZ   . LYS   A 1 55  ? 17.019 14.189  7.372   1.00 20.36 ?  55  LYS   A NZ   1 
ATOM   1435 H  H    A LYS   A 1 55  ? 22.674 9.712   6.763   0.66 17.35 ?  55  LYS   A H    1 
ATOM   1436 H  H    B LYS   A 1 55  ? 22.678 9.681   6.777   0.34 17.35 ?  55  LYS   A H    1 
ATOM   1437 H  HA   . LYS   A 1 55  ? 23.153 11.971  7.909   1.00 18.42 ?  55  LYS   A HA   1 
ATOM   1438 H  HB2  . LYS   A 1 55  ? 21.337 11.704  6.500   1.00 19.34 ?  55  LYS   A HB2  1 
ATOM   1439 H  HB3  . LYS   A 1 55  ? 20.653 10.718  7.538   1.00 19.34 ?  55  LYS   A HB3  1 
ATOM   1440 H  HG2  . LYS   A 1 55  ? 20.305 12.470  9.005   1.00 20.55 ?  55  LYS   A HG2  1 
ATOM   1441 H  HG3  . LYS   A 1 55  ? 21.040 13.467  8.001   1.00 20.55 ?  55  LYS   A HG3  1 
ATOM   1442 H  HD2  . LYS   A 1 55  ? 19.342 13.235  6.458   1.00 21.25 ?  55  LYS   A HD2  1 
ATOM   1443 H  HD3  . LYS   A 1 55  ? 18.653 12.101  7.335   1.00 21.25 ?  55  LYS   A HD3  1 
ATOM   1444 H  HE2  . LYS   A 1 55  ? 18.143 13.693  8.974   1.00 23.47 ?  55  LYS   A HE2  1 
ATOM   1445 H  HE3  . LYS   A 1 55  ? 18.804 14.824  8.069   1.00 23.47 ?  55  LYS   A HE3  1 
ATOM   1446 H  HZ1  . LYS   A 1 55  ? 16.408 14.475  7.952   1.00 24.49 ?  55  LYS   A HZ1  1 
ATOM   1447 H  HZ2  . LYS   A 1 55  ? 17.109 14.795  6.727   1.00 24.49 ?  55  LYS   A HZ2  1 
ATOM   1448 H  HZ3  . LYS   A 1 55  ? 16.738 13.422  7.015   1.00 24.49 ?  55  LYS   A HZ3  1 
ATOM   1449 N  N    . ALA   A 1 56  ? 22.098 9.745   9.946   1.00 15.47 ?  56  ALA   A N    1 
ATOM   1450 C  CA   . ALA   A 1 56  ? 21.980 9.416   11.360  1.00 16.42 ?  56  ALA   A CA   1 
ATOM   1451 C  C    . ALA   A 1 56  ? 23.317 9.453   12.086  1.00 16.42 ?  56  ALA   A C    1 
ATOM   1452 O  O    . ALA   A 1 56  ? 23.333 9.640   13.306  1.00 17.33 ?  56  ALA   A O    1 
ATOM   1453 C  CB   . ALA   A 1 56  ? 21.290 8.054   11.525  1.00 17.54 ?  56  ALA   A CB   1 
ATOM   1454 H  H    . ALA   A 1 56  ? 21.888 9.106   9.416   1.00 18.62 ?  56  ALA   A H    1 
ATOM   1455 H  HA   . ALA   A 1 56  ? 21.416 10.069  11.783  1.00 19.76 ?  56  ALA   A HA   1 
ATOM   1456 H  HB1  . ALA   A 1 56  ? 21.225 7.846   12.469  1.00 21.10 ?  56  ALA   A HB1  1 
ATOM   1457 H  HB2  . ALA   A 1 56  ? 20.403 8.105   11.134  1.00 21.10 ?  56  ALA   A HB2  1 
ATOM   1458 H  HB3  . ALA   A 1 56  ? 21.813 7.374   11.070  1.00 21.10 ?  56  ALA   A HB3  1 
ATOM   1459 N  N    . THR   A 1 57  ? 24.432 9.272   11.372  1.00 15.02 ?  57  THR   A N    1 
ATOM   1460 C  CA   . THR   A 1 57  ? 25.771 9.401   11.951  1.00 15.30 ?  57  THR   A CA   1 
ATOM   1461 C  C    . THR   A 1 57  ? 26.321 10.821  11.873  1.00 15.59 ?  57  THR   A C    1 
ATOM   1462 O  O    . THR   A 1 57  ? 27.507 11.031  12.163  1.00 16.24 ?  57  THR   A O    1 
ATOM   1463 C  CB   . THR   A 1 57  ? 26.784 8.449   11.285  1.00 15.18 ?  57  THR   A CB   1 
ATOM   1464 O  OG1  . THR   A 1 57  ? 27.170 8.946   9.994   1.00 15.03 ?  57  THR   A OG1  1 
ATOM   1465 C  CG2  . THR   A 1 57  ? 26.247 7.028   11.150  1.00 15.23 ?  57  THR   A CG2  1 
ATOM   1466 H  H    . THR   A 1 57  ? 24.443 9.058   10.538  1.00 18.08 ?  57  THR   A H    1 
ATOM   1467 H  HA   . THR   A 1 57  ? 25.724 9.143   12.890  1.00 18.42 ?  57  THR   A HA   1 
ATOM   1468 H  HB   . THR   A 1 57  ? 27.580 8.398   11.840  1.00 18.27 ?  57  THR   A HB   1 
ATOM   1469 H  HG1  . THR   A 1 57  ? 26.493 9.021   9.500   1.00 18.09 ?  57  THR   A HG1  1 
ATOM   1470 H  HG21 . THR   A 1 57  ? 26.979 6.392   11.053  1.00 18.33 ?  57  THR   A HG21 1 
ATOM   1471 H  HG22 . THR   A 1 57  ? 25.730 6.785   11.935  1.00 18.33 ?  57  THR   A HG22 1 
ATOM   1472 H  HG23 . THR   A 1 57  ? 25.674 6.955   10.367  1.00 18.33 ?  57  THR   A HG23 1 
ATOM   1473 N  N    . ASN   A 1 58  ? 25.505 11.795  11.473  1.00 15.89 ?  58  ASN   A N    1 
ATOM   1474 C  CA   . ASN   A 1 58  ? 25.968 13.175  11.376  1.00 17.10 ?  58  ASN   A CA   1 
ATOM   1475 C  C    . ASN   A 1 58  ? 27.119 13.309  10.371  1.00 15.69 ?  58  ASN   A C    1 
ATOM   1476 O  O    . ASN   A 1 58  ? 28.004 14.147  10.529  1.00 16.19 ?  58  ASN   A O    1 
ATOM   1477 C  CB   . ASN   A 1 58  ? 26.333 13.722  12.768  1.00 19.26 ?  58  ASN   A CB   1 
ATOM   1478 C  CG   . ASN   A 1 58  ? 26.750 15.181  12.750  1.00 22.37 ?  58  ASN   A CG   1 
ATOM   1479 O  OD1  . ASN   A 1 58  ? 26.127 16.008  12.091  1.00 23.98 ?  58  ASN   A OD1  1 
ATOM   1480 N  ND2  . ASN   A 1 58  ? 27.808 15.506  13.486  1.00 23.20 ?  58  ASN   A ND2  1 
ATOM   1481 H  H    . ASN   A 1 58  ? 24.678 11.670  11.257  1.00 19.13 ?  58  ASN   A H    1 
ATOM   1482 H  HA   . ASN   A 1 58  ? 25.233 13.704  11.045  1.00 20.58 ?  58  ASN   A HA   1 
ATOM   1483 H  HB2  . ASN   A 1 58  ? 25.556 13.640  13.357  1.00 23.17 ?  58  ASN   A HB2  1 
ATOM   1484 H  HB3  . ASN   A 1 58  ? 27.070 13.215  13.136  1.00 23.17 ?  58  ASN   A HB3  1 
ATOM   1485 H  HD21 . ASN   A 1 58  ? 28.074 16.325  13.510  1.00 27.90 ?  58  ASN   A HD21 1 
ATOM   1486 H  HD22 . ASN   A 1 58  ? 28.212 14.905  13.939  1.00 27.90 ?  58  ASN   A HD22 1 
ATOM   1487 N  N    . ASN   A 1 59  ? 27.107 12.490  9.319   1.00 14.89 ?  59  ASN   A N    1 
ATOM   1488 C  CA   . ASN   A 1 59  ? 28.089 12.466  8.224   1.00 14.13 ?  59  ASN   A CA   1 
ATOM   1489 C  C    . ASN   A 1 59  ? 29.402 11.783  8.618   1.00 14.33 ?  59  ASN   A C    1 
ATOM   1490 O  O    . ASN   A 1 59  ? 30.335 11.747  7.796   1.00 14.23 ?  59  ASN   A O    1 
ATOM   1491 C  CB   . ASN   A 1 59  ? 28.377 13.851  7.613   1.00 14.52 ?  59  ASN   A CB   1 
ATOM   1492 C  CG   . ASN   A 1 59  ? 28.725 13.784  6.134   1.00 14.58 ?  59  ASN   A CG   1 
ATOM   1493 O  OD1  . ASN   A 1 59  ? 28.023 13.149  5.342   1.00 14.60 ?  59  ASN   A OD1  1 
ATOM   1494 N  ND2  . ASN   A 1 59  ? 29.821 14.442  5.752   1.00 15.16 ?  59  ASN   A ND2  1 
ATOM   1495 H  H    . ASN   A 1 59  ? 26.496 11.897  9.205   1.00 17.93 ?  59  ASN   A H    1 
ATOM   1496 H  HA   . ASN   A 1 59  ? 27.712 11.938  7.514   1.00 17.01 ?  59  ASN   A HA   1 
ATOM   1497 H  HB2  . ASN   A 1 59  ? 27.596 14.417  7.703   1.00 17.48 ?  59  ASN   A HB2  1 
ATOM   1498 H  HB3  . ASN   A 1 59  ? 29.133 14.259  8.070   1.00 17.48 ?  59  ASN   A HB3  1 
ATOM   1499 H  HD21 . ASN   A 1 59  ? 30.063 14.443  4.922   1.00 18.24 ?  59  ASN   A HD21 1 
ATOM   1500 H  HD22 . ASN   A 1 59  ? 30.290 14.879  6.328   1.00 18.24 ?  59  ASN   A HD22 1 
ATOM   1501 N  N    . ALA   A 1 60  ? 29.522 11.246  9.832   1.00 14.31 ?  60  ALA   A N    1 
ATOM   1502 C  CA   . ALA   A 1 60  ? 30.758 10.562  10.195  1.00 14.35 ?  60  ALA   A CA   1 
ATOM   1503 C  C    . ALA   A 1 60  ? 30.987 9.323   9.336   1.00 14.51 ?  60  ALA   A C    1 
ATOM   1504 O  O    . ALA   A 1 60  ? 32.134 9.004   9.005   1.00 14.95 ?  60  ALA   A O    1 
ATOM   1505 C  CB   . ALA   A 1 60  ? 30.764 10.225  11.684  1.00 15.09 ?  60  ALA   A CB   1 
ATOM   1506 H  H    . ALA   A 1 60  ? 28.928 11.269  10.446  1.00 17.22 ?  60  ALA   A H    1 
ATOM   1507 H  HA   . ALA   A 1 60  ? 31.506 11.166  10.037  1.00 17.28 ?  60  ALA   A HA   1 
ATOM   1508 H  HB1  . ALA   A 1 60  ? 31.592 9.774   11.906  1.00 18.17 ?  60  ALA   A HB1  1 
ATOM   1509 H  HB2  . ALA   A 1 60  ? 30.693 11.052  12.196  1.00 18.17 ?  60  ALA   A HB2  1 
ATOM   1510 H  HB3  . ALA   A 1 60  ? 30.008 9.653   11.881  1.00 18.17 ?  60  ALA   A HB3  1 
ATOM   1511 N  N    . MET   A 1 61  ? 29.918 8.629   8.946   1.00 14.22 ?  61  MET   A N    1 
ATOM   1512 C  CA   . MET   A 1 61  ? 30.068 7.490   8.043   1.00 14.19 ?  61  MET   A CA   1 
ATOM   1513 C  C    . MET   A 1 61  ? 30.709 7.919   6.726   1.00 14.10 ?  61  MET   A C    1 
ATOM   1514 O  O    . MET   A 1 61  ? 31.607 7.238   6.216   1.00 14.45 ?  61  MET   A O    1 
ATOM   1515 C  CB   . MET   A 1 61  ? 28.707 6.835   7.809   1.00 14.32 ?  61  MET   A CB   1 
ATOM   1516 C  CG   . MET   A 1 61  ? 28.724 5.663   6.840   1.00 15.01 ?  61  MET   A CG   1 
ATOM   1517 S  SD   . MET   A 1 61  ? 27.104 4.911   6.638   1.00 15.01 ?  61  MET   A SD   1 
ATOM   1518 C  CE   . MET   A 1 61  ? 26.982 4.018   8.194   1.00 17.96 ?  61  MET   A CE   1 
ATOM   1519 H  H    . MET   A 1 61  ? 29.109 8.800   9.182   1.00 17.12 ?  61  MET   A H    1 
ATOM   1520 H  HA   . MET   A 1 61  ? 30.642 6.834   8.466   1.00 17.08 ?  61  MET   A HA   1 
ATOM   1521 H  HB2  . MET   A 1 61  ? 28.369 6.515   8.657   1.00 17.24 ?  61  MET   A HB2  1 
ATOM   1522 H  HB3  . MET   A 1 61  ? 28.101 7.504   7.449   1.00 17.24 ?  61  MET   A HB3  1 
ATOM   1523 H  HG2  . MET   A 1 61  ? 29.014 5.962   5.966   1.00 18.07 ?  61  MET   A HG2  1 
ATOM   1524 H  HG3  . MET   A 1 61  ? 29.325 4.978   7.174   1.00 18.07 ?  61  MET   A HG3  1 
ATOM   1525 H  HE1  . MET   A 1 61  ? 26.143 3.532   8.215   1.00 21.61 ?  61  MET   A HE1  1 
ATOM   1526 H  HE2  . MET   A 1 61  ? 27.726 3.402   8.263   1.00 21.61 ?  61  MET   A HE2  1 
ATOM   1527 H  HE3  . MET   A 1 61  ? 27.011 4.655   8.928   1.00 21.61 ?  61  MET   A HE3  1 
ATOM   1528 N  N    . GLN   A 1 62  ? 30.266 9.053   6.169   1.00 13.99 ?  62  GLN   A N    1 
ATOM   1529 C  CA   . GLN   A 1 62  ? 30.827 9.526   4.906   1.00 14.34 ?  62  GLN   A CA   1 
ATOM   1530 C  C    . GLN   A 1 62  ? 32.294 9.906   5.050   1.00 14.03 ?  62  GLN   A C    1 
ATOM   1531 O  O    . GLN   A 1 62  ? 33.108 9.577   4.182   1.00 14.26 ?  62  GLN   A O    1 
ATOM   1532 C  CB   . GLN   A 1 62  ? 30.032 10.714  4.371   1.00 14.27 ?  62  GLN   A CB   1 
ATOM   1533 C  CG   . GLN   A 1 62  ? 30.404 11.058  2.938   1.00 14.18 ?  62  GLN   A CG   1 
ATOM   1534 C  CD   . GLN   A 1 62  ? 30.064 9.929   1.997   1.00 14.51 ?  62  GLN   A CD   1 
ATOM   1535 O  OE1  . GLN   A 1 62  ? 28.885 9.621   1.796   1.00 15.25 ?  62  GLN   A OE1  1 
ATOM   1536 N  NE2  . GLN   A 1 62  ? 31.082 9.264   1.459   1.00 14.82 ?  62  GLN   A NE2  1 
ATOM   1537 H  H    . GLN   A 1 62  ? 29.649 9.551   6.494   1.00 16.85 ?  62  GLN   A H    1 
ATOM   1538 H  HA   . GLN   A 1 62  ? 30.778 8.813   4.254   1.00 17.26 ?  62  GLN   A HA   1 
ATOM   1539 H  HB2  . GLN   A 1 62  ? 29.090 10.505  4.397   1.00 17.17 ?  62  GLN   A HB2  1 
ATOM   1540 H  HB3  . GLN   A 1 62  ? 30.218 11.496  4.920   1.00 17.17 ?  62  GLN   A HB3  1 
ATOM   1541 H  HG2  . GLN   A 1 62  ? 29.905 11.841  2.658   1.00 17.07 ?  62  GLN   A HG2  1 
ATOM   1542 H  HG3  . GLN   A 1 62  ? 31.356 11.228  2.879   1.00 17.07 ?  62  GLN   A HG3  1 
ATOM   1543 H  HE21 . GLN   A 1 62  ? 31.888 9.498   1.637   1.00 17.83 ?  62  GLN   A HE21 1 
ATOM   1544 H  HE22 . GLN   A 1 62  ? 30.933 8.604   0.924   1.00 17.83 ?  62  GLN   A HE22 1 
ATOM   1545 N  N    . VAL   A 1 63  ? 32.646 10.590  6.141   1.00 14.53 ?  63  VAL   A N    1 
ATOM   1546 C  CA   . VAL   A 1 63  ? 34.036 10.977  6.364   1.00 15.05 ?  63  VAL   A CA   1 
ATOM   1547 C  C    . VAL   A 1 63  ? 34.929 9.741   6.431   1.00 14.50 ?  63  VAL   A C    1 
ATOM   1548 O  O    . VAL   A 1 63  ? 35.986 9.674   5.787   1.00 14.97 ?  63  VAL   A O    1 
ATOM   1549 C  CB   . VAL   A 1 63  ? 34.145 11.848  7.629   1.00 16.66 ?  63  VAL   A CB   1 
ATOM   1550 C  CG1  . VAL   A 1 63  ? 35.596 12.095  8.003   1.00 17.96 ?  63  VAL   A CG1  1 
ATOM   1551 C  CG2  . VAL   A 1 63  ? 33.435 13.181  7.402   1.00 16.96 ?  63  VAL   A CG2  1 
ATOM   1552 H  H    . VAL   A 1 63  ? 32.103 10.839  6.762   1.00 17.49 ?  63  VAL   A H    1 
ATOM   1553 H  HA   . VAL   A 1 63  ? 34.334 11.515  5.614   1.00 18.12 ?  63  VAL   A HA   1 
ATOM   1554 H  HB   . VAL   A 1 63  ? 33.709 11.399  8.371   1.00 20.05 ?  63  VAL   A HB   1 
ATOM   1555 H  HG11 . VAL   A 1 63  ? 35.633 12.824  8.641   1.00 21.61 ?  63  VAL   A HG11 1 
ATOM   1556 H  HG12 . VAL   A 1 63  ? 35.958 11.289  8.397   1.00 21.61 ?  63  VAL   A HG12 1 
ATOM   1557 H  HG13 . VAL   A 1 63  ? 36.086 12.329  7.202   1.00 21.61 ?  63  VAL   A HG13 1 
ATOM   1558 H  HG21 . VAL   A 1 63  ? 33.518 13.728  8.202   1.00 20.40 ?  63  VAL   A HG21 1 
ATOM   1559 H  HG22 . VAL   A 1 63  ? 33.848 13.637  6.651   1.00 20.40 ?  63  VAL   A HG22 1 
ATOM   1560 H  HG23 . VAL   A 1 63  ? 32.498 13.017  7.214   1.00 20.40 ?  63  VAL   A HG23 1 
ATOM   1561 N  N    . GLU   A 1 64  ? 34.507 8.729   7.197   1.00 14.56 ?  64  GLU   A N    1 
ATOM   1562 C  CA   . GLU   A 1 64  ? 35.275 7.495   7.290   1.00 14.87 ?  64  GLU   A CA   1 
ATOM   1563 C  C    . GLU   A 1 64  ? 35.372 6.823   5.929   1.00 14.33 ?  64  GLU   A C    1 
ATOM   1564 O  O    . GLU   A 1 64  ? 36.426 6.287   5.549   1.00 14.61 ?  64  GLU   A O    1 
ATOM   1565 C  CB   . GLU   A 1 64  ? 34.581 6.575   8.294   1.00 15.54 ?  64  GLU   A CB   1 
ATOM   1566 C  CG   . GLU   A 1 64  ? 35.234 5.220   8.436   1.00 15.91 ?  64  GLU   A CG   1 
ATOM   1567 C  CD   . GLU   A 1 64  ? 34.361 4.227   9.166   1.00 16.61 ?  64  GLU   A CD   1 
ATOM   1568 O  OE1  . GLU   A 1 64  ? 33.123 4.323   9.036   1.00 17.21 ?  64  GLU   A OE1  1 
ATOM   1569 O  OE2  . GLU   A 1 64  ? 34.923 3.344   9.857   1.00 17.08 -1 64  GLU   A OE2  1 
ATOM   1570 H  H    . GLU   A 1 64  ? 33.776 8.736   7.659   1.00 17.53 ?  64  GLU   A H    1 
ATOM   1571 H  HA   . GLU   A 1 64  ? 36.170 7.701   7.612   1.00 17.90 ?  64  GLU   A HA   1 
ATOM   1572 H  HB2  . GLU   A 1 64  ? 34.596 7.010   9.168   1.00 18.70 ?  64  GLU   A HB2  1 
ATOM   1573 H  HB3  . GLU   A 1 64  ? 33.666 6.452   8.009   1.00 18.70 ?  64  GLU   A HB3  1 
ATOM   1574 H  HG2  . GLU   A 1 64  ? 35.422 4.855   7.556   1.00 19.15 ?  64  GLU   A HG2  1 
ATOM   1575 H  HG3  . GLU   A 1 64  ? 36.055 5.314   8.937   1.00 19.15 ?  64  GLU   A HG3  1 
ATOM   1576 N  N    . SER   A 1 65  ? 34.253 6.808   5.199   1.00 14.21 ?  65  SER   A N    1 
ATOM   1577 C  CA   . SER   A 1 65  ? 34.203 6.150   3.901   1.00 14.16 ?  65  SER   A CA   1 
ATOM   1578 C  C    . SER   A 1 65  ? 35.128 6.816   2.895   1.00 14.27 ?  65  SER   A C    1 
ATOM   1579 O  O    . SER   A 1 65  ? 35.779 6.133   2.096   1.00 15.05 ?  65  SER   A O    1 
ATOM   1580 C  CB   . SER   A 1 65  ? 32.773 6.153   3.369   1.00 14.19 ?  65  SER   A CB   1 
ATOM   1581 O  OG   . SER   A 1 65  ? 31.915 5.343   4.167   1.00 14.44 ?  65  SER   A OG   1 
ATOM   1582 H  H    . SER   A 1 65  ? 33.509 7.166   5.442   1.00 17.10 ?  65  SER   A H    1 
ATOM   1583 H  HA   . SER   A 1 65  ? 34.488 5.229   4.002   1.00 17.04 ?  65  SER   A HA   1 
ATOM   1584 H  HB2  . SER   A 1 65  ? 32.436 7.061   3.367   1.00 17.08 ?  65  SER   A HB2  1 
ATOM   1585 H  HB3  . SER   A 1 65  ? 32.781 5.804   2.462   1.00 17.08 ?  65  SER   A HB3  1 
ATOM   1586 H  HG   . SER   A 1 65  ? 31.911 5.641   4.955   1.00 17.39 ?  65  SER   A HG   1 
ATOM   1587 N  N    . ASP   A 1 66  ? 35.199 8.148   2.909   1.00 14.41 ?  66  ASP   A N    1 
ATOM   1588 C  CA   . ASP   A 1 66  ? 36.057 8.838   1.953   1.00 15.35 ?  66  ASP   A CA   1 
ATOM   1589 C  C    . ASP   A 1 66  ? 37.522 8.497   2.195   1.00 15.13 ?  66  ASP   A C    1 
ATOM   1590 O  O    . ASP   A 1 66  ? 38.291 8.316   1.245   1.00 15.96 ?  66  ASP   A O    1 
ATOM   1591 C  CB   . ASP   A 1 66  ? 35.833 10.342  2.040   1.00 16.46 ?  66  ASP   A CB   1 
ATOM   1592 C  CG   . ASP   A 1 66  ? 34.509 10.796  1.417   1.00 17.87 ?  66  ASP   A CG   1 
ATOM   1593 O  OD1  . ASP   A 1 66  ? 33.806 9.994   0.765   1.00 18.17 ?  66  ASP   A OD1  1 
ATOM   1594 O  OD2  . ASP   A 1 66  ? 34.194 11.991  1.571   1.00 20.74 -1 66  ASP   A OD2  1 
ATOM   1595 H  H    . ASP   A 1 66  ? 34.764 8.667   3.448   1.00 17.34 ?  66  ASP   A H    1 
ATOM   1596 H  HA   . ASP   A 1 66  ? 35.827 8.548   1.057   1.00 18.47 ?  66  ASP   A HA   1 
ATOM   1597 H  HB2  . ASP   A 1 66  ? 35.823 10.604  2.973   1.00 19.81 ?  66  ASP   A HB2  1 
ATOM   1598 H  HB3  . ASP   A 1 66  ? 36.558 10.792  1.577   1.00 19.81 ?  66  ASP   A HB3  1 
ATOM   1599 N  N    . ASP   A 1 67  ? 37.916 8.385   3.464   1.00 15.24 ?  67  ASP   A N    1 
ATOM   1600 C  CA   . ASP   A 1 67  ? 39.273 7.948   3.775   1.00 15.94 ?  67  ASP   A CA   1 
ATOM   1601 C  C    . ASP   A 1 67  ? 39.500 6.511   3.316   1.00 16.01 ?  67  ASP   A C    1 
ATOM   1602 O  O    . ASP   A 1 67  ? 40.565 6.183   2.782   1.00 16.08 ?  67  ASP   A O    1 
ATOM   1603 C  CB   . ASP   A 1 67  ? 39.532 8.084   5.274   1.00 16.91 ?  67  ASP   A CB   1 
ATOM   1604 C  CG   . ASP   A 1 67  ? 40.832 7.433   5.703   1.00 18.43 ?  67  ASP   A CG   1 
ATOM   1605 O  OD1  . ASP   A 1 67  ? 41.897 8.083   5.596   1.00 20.53 ?  67  ASP   A OD1  1 
ATOM   1606 O  OD2  . ASP   A 1 67  ? 40.783 6.267   6.150   1.00 18.53 -1 67  ASP   A OD2  1 
ATOM   1607 H  H    . ASP   A 1 67  ? 37.429 8.557   4.154   1.00 18.35 ?  67  ASP   A H    1 
ATOM   1608 H  HA   . ASP   A 1 67  ? 39.909 8.514   3.310   1.00 19.18 ?  67  ASP   A HA   1 
ATOM   1609 H  HB2  . ASP   A 1 67  ? 39.577 9.022   5.502   1.00 20.34 ?  67  ASP   A HB2  1 
ATOM   1610 H  HB3  . ASP   A 1 67  ? 38.812 7.653   5.760   1.00 20.34 ?  67  ASP   A HB3  1 
ATOM   1611 N  N    . TYR   A 1 68  ? 38.507 5.631   3.506   1.00 15.57 ?  68  TYR   A N    1 
ATOM   1612 C  CA   . TYR   A 1 68  ? 38.640 4.247   3.041   1.00 15.27 ?  68  TYR   A CA   1 
ATOM   1613 C  C    . TYR   A 1 68  ? 38.874 4.191   1.532   1.00 15.09 ?  68  TYR   A C    1 
ATOM   1614 O  O    . TYR   A 1 68  ? 39.750 3.455   1.055   1.00 15.95 ?  68  TYR   A O    1 
ATOM   1615 C  CB   . TYR   A 1 68  ? 37.402 3.415   3.431   1.00 15.83 ?  68  TYR   A CB   1 
ATOM   1616 C  CG   . TYR   A 1 68  ? 37.427 2.030   2.802   1.00 16.75 ?  68  TYR   A CG   1 
ATOM   1617 C  CD1  . TYR   A 1 68  ? 36.964 1.837   1.506   1.00 18.05 ?  68  TYR   A CD1  1 
ATOM   1618 C  CD2  . TYR   A 1 68  ? 37.970 0.947   3.469   1.00 18.08 ?  68  TYR   A CD2  1 
ATOM   1619 C  CE1  . TYR   A 1 68  ? 37.026 0.624   0.894   1.00 18.88 ?  68  TYR   A CE1  1 
ATOM   1620 C  CE2  . TYR   A 1 68  ? 38.023 -0.310  2.861   1.00 18.82 ?  68  TYR   A CE2  1 
ATOM   1621 C  CZ   . TYR   A 1 68  ? 37.560 -0.447  1.569   1.00 19.26 ?  68  TYR   A CZ   1 
ATOM   1622 O  OH   . TYR   A 1 68  ? 37.630 -1.662  0.937   1.00 21.07 ?  68  TYR   A OH   1 
ATOM   1623 H  H    . TYR   A 1 68  ? 37.764 5.808   3.903   1.00 18.73 ?  68  TYR   A H    1 
ATOM   1624 H  HA   . TYR   A 1 68  ? 39.411 3.848   3.474   1.00 18.38 ?  68  TYR   A HA   1 
ATOM   1625 H  HB2  . TYR   A 1 68  ? 37.377 3.307   4.395   1.00 19.05 ?  68  TYR   A HB2  1 
ATOM   1626 H  HB3  . TYR   A 1 68  ? 36.601 3.870   3.125   1.00 19.05 ?  68  TYR   A HB3  1 
ATOM   1627 H  HD1  . TYR   A 1 68  ? 36.617 2.562   1.039   1.00 21.72 ?  68  TYR   A HD1  1 
ATOM   1628 H  HD2  . TYR   A 1 68  ? 38.303 1.051   4.333   1.00 21.75 ?  68  TYR   A HD2  1 
ATOM   1629 H  HE1  . TYR   A 1 68  ? 36.709 0.520   0.027   1.00 22.71 ?  68  TYR   A HE1  1 
ATOM   1630 H  HE2  . TYR   A 1 68  ? 38.397 -1.040  3.303   1.00 22.64 ?  68  TYR   A HE2  1 
ATOM   1631 H  HH   . TYR   A 1 68  ? 37.971 -2.239  1.447   1.00 25.34 ?  68  TYR   A HH   1 
ATOM   1632 N  N    . ILE   A 1 69  ? 38.088 4.947   0.759   1.00 14.55 ?  69  ILE   A N    1 
ATOM   1633 C  CA   . ILE   A 1 69  ? 38.218 4.919   -0.696  1.00 15.00 ?  69  ILE   A CA   1 
ATOM   1634 C  C    . ILE   A 1 69  ? 39.546 5.533   -1.134  1.00 15.16 ?  69  ILE   A C    1 
ATOM   1635 O  O    . ILE   A 1 69  ? 40.195 5.044   -2.067  1.00 15.56 ?  69  ILE   A O    1 
ATOM   1636 C  CB   . ILE   A 1 69  ? 37.019 5.620   -1.361  1.00 15.23 ?  69  ILE   A CB   1 
ATOM   1637 C  CG1  . ILE   A 1 69  ? 35.712 4.881   -1.064  1.00 16.48 ?  69  ILE   A CG1  1 
ATOM   1638 C  CG2  . ILE   A 1 69  ? 37.250 5.772   -2.861  1.00 16.51 ?  69  ILE   A CG2  1 
ATOM   1639 C  CD1  . ILE   A 1 69  ? 35.542 3.593   -1.848  1.00 17.31 ?  69  ILE   A CD1  1 
ATOM   1640 H  H    . ILE   A 1 69  ? 37.482 5.487   1.053   1.00 17.51 ?  69  ILE   A H    1 
ATOM   1641 H  HA   . ILE   A 1 69  ? 38.217 3.993   -0.983  1.00 18.05 ?  69  ILE   A HA   1 
ATOM   1642 H  HB   . ILE   A 1 69  ? 36.946 6.504   -0.984  1.00 18.33 ?  69  ILE   A HB   1 
ATOM   1643 H  HG12 . ILE   A 1 69  ? 35.686 4.659   -0.118  1.00 19.83 ?  69  ILE   A HG12 1 
ATOM   1644 H  HG13 . ILE   A 1 69  ? 34.968 5.463   -1.282  1.00 19.83 ?  69  ILE   A HG13 1 
ATOM   1645 H  HG21 . ILE   A 1 69  ? 36.399 5.962   -3.294  1.00 19.87 ?  69  ILE   A HG21 1 
ATOM   1646 H  HG22 . ILE   A 1 69  ? 37.863 6.510   -3.015  1.00 19.87 ?  69  ILE   A HG22 1 
ATOM   1647 H  HG23 . ILE   A 1 69  ? 37.621 4.951   -3.216  1.00 19.87 ?  69  ILE   A HG23 1 
ATOM   1648 H  HD11 . ILE   A 1 69  ? 34.778 3.111   -1.496  1.00 20.82 ?  69  ILE   A HD11 1 
ATOM   1649 H  HD12 . ILE   A 1 69  ? 35.393 3.809   -2.782  1.00 20.82 ?  69  ILE   A HD12 1 
ATOM   1650 H  HD13 . ILE   A 1 69  ? 36.343 3.056   -1.754  1.00 20.82 ?  69  ILE   A HD13 1 
ATOM   1651 N  N    . ALA   A 1 70  ? 39.968 6.610   -0.478  1.00 15.93 ?  70  ALA   A N    1 
ATOM   1652 C  CA   . ALA   A 1 70  ? 41.242 7.229   -0.825  1.00 16.67 ?  70  ALA   A CA   1 
ATOM   1653 C  C    . ALA   A 1 70  ? 42.397 6.254   -0.650  1.00 17.09 ?  70  ALA   A C    1 
ATOM   1654 O  O    . ALA   A 1 70  ? 43.374 6.307   -1.402  1.00 18.80 ?  70  ALA   A O    1 
ATOM   1655 C  CB   . ALA   A 1 70  ? 41.462 8.482   0.025   1.00 17.19 ?  70  ALA   A CB   1 
ATOM   1656 H  H    . ALA   A 1 70  ? 39.540 7.000   0.153   1.00 19.18 ?  70  ALA   A H    1 
ATOM   1657 H  HA   . ALA   A 1 70  ? 41.222 7.504   -1.756  1.00 20.06 ?  70  ALA   A HA   1 
ATOM   1658 H  HB1  . ALA   A 1 70  ? 42.315 8.885   -0.215  1.00 20.68 ?  70  ALA   A HB1  1 
ATOM   1659 H  HB2  . ALA   A 1 70  ? 40.744 9.113   -0.144  1.00 20.68 ?  70  ALA   A HB2  1 
ATOM   1660 H  HB3  . ALA   A 1 70  ? 41.470 8.234   0.963   1.00 20.68 ?  70  ALA   A HB3  1 
ATOM   1661 N  N    . THR   A 1 71  ? 42.293 5.342   0.312   1.00 16.32 ?  71  THR   A N    1 
ATOM   1662 C  CA   . THR   A 1 71  ? 43.346 4.375   0.577   1.00 17.85 ?  71  THR   A CA   1 
ATOM   1663 C  C    . THR   A 1 71  ? 43.226 3.134   -0.295  1.00 17.88 ?  71  THR   A C    1 
ATOM   1664 O  O    . THR   A 1 71  ? 44.239 2.605   -0.768  1.00 20.13 ?  71  THR   A O    1 
ATOM   1665 C  CB   . THR   A 1 71  ? 43.282 3.949   2.044   1.00 20.28 ?  71  THR   A CB   1 
ATOM   1666 O  OG1  . THR   A 1 71  ? 43.537 5.082   2.877   1.00 22.13 ?  71  THR   A OG1  1 
ATOM   1667 C  CG2  . THR   A 1 71  ? 44.299 2.849   2.345   1.00 21.54 ?  71  THR   A CG2  1 
ATOM   1668 H  H    . THR   A 1 71  ? 41.605 5.253   0.822   1.00 19.64 ?  71  THR   A H    1 
ATOM   1669 H  HA   . THR   A 1 71  ? 44.208 4.782   0.412   1.00 21.47 ?  71  THR   A HA   1 
ATOM   1670 H  HB   . THR   A 1 71  ? 42.396 3.600   2.237   1.00 24.39 ?  71  THR   A HB   1 
ATOM   1671 H  HG1  . THR   A 1 71  ? 42.963 5.674   2.741   1.00 26.61 ?  71  THR   A HG1  1 
ATOM   1672 H  HG21 . THR   A 1 71  ? 44.442 2.785   3.304   1.00 25.91 ?  71  THR   A HG21 1 
ATOM   1673 H  HG22 . THR   A 1 71  ? 43.980 1.993   2.020   1.00 25.91 ?  71  THR   A HG22 1 
ATOM   1674 H  HG23 . THR   A 1 71  ? 45.147 3.054   1.918   1.00 25.91 ?  71  THR   A HG23 1 
ATOM   1675 N  N    . ASN   A 1 72  ? 42.006 2.643   -0.506  1.00 16.88 ?  72  ASN   A N    1 
ATOM   1676 C  CA   . ASN   A 1 72  ? 41.793 1.315   -1.059  1.00 16.89 ?  72  ASN   A CA   1 
ATOM   1677 C  C    . ASN   A 1 72  ? 41.180 1.300   -2.447  1.00 17.12 ?  72  ASN   A C    1 
ATOM   1678 O  O    . ASN   A 1 72  ? 41.175 0.241   -3.083  1.00 18.20 ?  72  ASN   A O    1 
ATOM   1679 C  CB   . ASN   A 1 72  ? 40.896 0.505   -0.117  1.00 17.65 ?  72  ASN   A CB   1 
ATOM   1680 C  CG   . ASN   A 1 72  ? 41.507 0.349   1.255   1.00 18.67 ?  72  ASN   A CG   1 
ATOM   1681 O  OD1  . ASN   A 1 72  ? 41.063 0.959   2.219   1.00 20.91 ?  72  ASN   A OD1  1 
ATOM   1682 N  ND2  . ASN   A 1 72  ? 42.547 -0.442  1.341   1.00 19.48 ?  72  ASN   A ND2  1 
ATOM   1683 H  H    . ASN   A 1 72  ? 41.277 3.069   -0.333  1.00 20.31 ?  72  ASN   A H    1 
ATOM   1684 H  HA   . ASN   A 1 72  ? 42.648 0.864   -1.117  1.00 20.33 ?  72  ASN   A HA   1 
ATOM   1685 H  HB2  . ASN   A 1 72  ? 40.042 0.958   -0.029  1.00 21.24 ?  72  ASN   A HB2  1 
ATOM   1686 H  HB3  . ASN   A 1 72  ? 40.767 -0.380  -0.493  1.00 21.24 ?  72  ASN   A HB3  1 
ATOM   1687 H  HD21 . ASN   A 1 72  ? 42.931 -0.554  2.102   1.00 23.43 ?  72  ASN   A HD21 1 
ATOM   1688 H  HD22 . ASN   A 1 72  ? 42.837 -0.846  0.644   1.00 23.43 ?  72  ASN   A HD22 1 
ATOM   1689 N  N    . GLY   A 1 73  ? 40.630 2.410   -2.918  1.00 16.68 ?  73  GLY   A N    1 
ATOM   1690 C  CA   . GLY   A 1 73  ? 39.909 2.404   -4.164  1.00 16.70 ?  73  GLY   A CA   1 
ATOM   1691 C  C    . GLY   A 1 73  ? 38.512 1.836   -4.000  1.00 16.26 ?  73  GLY   A C    1 
ATOM   1692 O  O    . GLY   A 1 73  ? 38.114 1.401   -2.914  1.00 16.62 ?  73  GLY   A O    1 
ATOM   1693 H  H    . GLY   A 1 73  ? 40.664 3.185   -2.534  1.00 20.07 ?  73  GLY   A H    1 
ATOM   1694 H  HA2  . GLY   A 1 73  ? 39.841 3.310   -4.504  1.00 20.09 ?  73  GLY   A HA2  1 
ATOM   1695 H  HA3  . GLY   A 1 73  ? 40.387 1.865   -4.814  1.00 20.09 ?  73  GLY   A HA3  1 
ATOM   1696 N  N    . PRO   A 1 74  ? 37.740 1.850   -5.087  1.00 16.32 ?  74  PRO   A N    1 
ATOM   1697 C  CA   . PRO   A 1 74  ? 36.336 1.426   -5.011  1.00 16.18 ?  74  PRO   A CA   1 
ATOM   1698 C  C    . PRO   A 1 74  ? 36.180 -0.055  -4.688  1.00 16.00 ?  74  PRO   A C    1 
ATOM   1699 O  O    . PRO   A 1 74  ? 37.043 -0.886  -4.982  1.00 17.13 ?  74  PRO   A O    1 
ATOM   1700 C  CB   . PRO   A 1 74  ? 35.806 1.711   -6.422  1.00 18.29 ?  74  PRO   A CB   1 
ATOM   1701 C  CG   . PRO   A 1 74  ? 36.774 2.665   -7.037  1.00 21.23 ?  74  PRO   A CG   1 
ATOM   1702 C  CD   . PRO   A 1 74  ? 38.097 2.335   -6.430  1.00 18.63 ?  74  PRO   A CD   1 
ATOM   1703 H  HA   . PRO   A 1 74  ? 35.848 1.957   -4.364  1.00 19.47 ?  74  PRO   A HA   1 
ATOM   1704 H  HB2  . PRO   A 1 74  ? 35.772 0.879   -6.927  1.00 22.00 ?  74  PRO   A HB2  1 
ATOM   1705 H  HB3  . PRO   A 1 74  ? 34.922 2.106   -6.362  1.00 22.00 ?  74  PRO   A HB3  1 
ATOM   1706 H  HG2  . PRO   A 1 74  ? 36.798 2.532   -7.998  1.00 25.53 ?  74  PRO   A HG2  1 
ATOM   1707 H  HG3  . PRO   A 1 74  ? 36.517 3.572   -6.821  1.00 25.53 ?  74  PRO   A HG3  1 
ATOM   1708 H  HD2  . PRO   A 1 74  ? 38.542 1.633   -6.937  1.00 22.42 ?  74  PRO   A HD2  1 
ATOM   1709 H  HD3  . PRO   A 1 74  ? 38.649 3.132   -6.375  1.00 22.42 ?  74  PRO   A HD3  1 
ATOM   1710 N  N    . LEU   A 1 75  ? 35.036 -0.379  -4.094  1.00 15.43 ?  75  LEU   A N    1 
ATOM   1711 C  CA   . LEU   A 1 75  ? 34.637 -1.769  -3.951  1.00 15.02 ?  75  LEU   A CA   1 
ATOM   1712 C  C    . LEU   A 1 75  ? 34.259 -2.347  -5.312  1.00 15.74 ?  75  LEU   A C    1 
ATOM   1713 O  O    . LEU   A 1 75  ? 34.122 -1.635  -6.311  1.00 16.65 ?  75  LEU   A O    1 
ATOM   1714 C  CB   . LEU   A 1 75  ? 33.445 -1.888  -3.003  1.00 15.56 ?  75  LEU   A CB   1 
ATOM   1715 C  CG   . LEU   A 1 75  ? 33.651 -1.476  -1.550  1.00 16.69 ?  75  LEU   A CG   1 
ATOM   1716 C  CD1  . LEU   A 1 75  ? 32.357 -1.676  -0.769  1.00 18.68 ?  75  LEU   A CD1  1 
ATOM   1717 C  CD2  . LEU   A 1 75  ? 34.781 -2.206  -0.892  1.00 19.33 ?  75  LEU   A CD2  1 
ATOM   1718 H  H    . LEU   A 1 75  ? 34.486 0.187   -3.760  1.00 18.57 ?  75  LEU   A H    1 
ATOM   1719 H  HA   . LEU   A 1 75  ? 35.376 -2.284  -3.588  1.00 18.08 ?  75  LEU   A HA   1 
ATOM   1720 H  HB2  . LEU   A 1 75  ? 32.728 -1.340  -3.355  1.00 18.72 ?  75  LEU   A HB2  1 
ATOM   1721 H  HB3  . LEU   A 1 75  ? 33.162 -2.817  -2.999  1.00 18.72 ?  75  LEU   A HB3  1 
ATOM   1722 H  HG   . LEU   A 1 75  ? 33.870 -0.531  -1.526  1.00 20.08 ?  75  LEU   A HG   1 
ATOM   1723 H  HD11 . LEU   A 1 75  ? 32.503 -1.408  0.151   1.00 22.47 ?  75  LEU   A HD11 1 
ATOM   1724 H  HD12 . LEU   A 1 75  ? 31.667 -1.126  -1.171  1.00 22.47 ?  75  LEU   A HD12 1 
ATOM   1725 H  HD13 . LEU   A 1 75  ? 32.108 -2.610  -0.811  1.00 22.47 ?  75  LEU   A HD13 1 
ATOM   1726 H  HD21 . LEU   A 1 75  ? 34.833 -1.935  0.038   1.00 23.25 ?  75  LEU   A HD21 1 
ATOM   1727 H  HD22 . LEU   A 1 75  ? 34.622 -3.159  -0.953  1.00 23.25 ?  75  LEU   A HD22 1 
ATOM   1728 H  HD23 . LEU   A 1 75  ? 35.613 -1.981  -1.344  1.00 23.25 ?  75  LEU   A HD23 1 
ATOM   1729 N  N    . LYS   A 1 76  ? 34.085 -3.668  -5.333  1.00 15.93 ?  76  LYS   A N    1 
ATOM   1730 C  CA   . LYS   A 1 76  ? 33.482 -4.383  -6.452  1.00 16.86 ?  76  LYS   A CA   1 
ATOM   1731 C  C    . LYS   A 1 76  ? 31.971 -4.461  -6.259  1.00 15.66 ?  76  LYS   A C    1 
ATOM   1732 O  O    . LYS   A 1 76  ? 31.485 -4.569  -5.134  1.00 15.62 ?  76  LYS   A O    1 
ATOM   1733 C  CB   . LYS   A 1 76  ? 34.025 -5.821  -6.514  1.00 18.19 ?  76  LYS   A CB   1 
ATOM   1734 C  CG   . LYS   A 1 76  ? 35.542 -5.928  -6.704  1.00 19.31 ?  76  LYS   A CG   1 
ATOM   1735 C  CD   . LYS   A 1 76  ? 36.053 -7.346  -6.537  1.00 20.36 ?  76  LYS   A CD   1 
ATOM   1736 C  CE   . LYS   A 1 76  ? 37.566 -7.407  -6.654  1.00 22.45 ?  76  LYS   A CE   1 
ATOM   1737 N  NZ   . LYS   A 1 76  ? 38.096 -8.776  -6.509  1.00 22.94 ?  76  LYS   A NZ   1 
ATOM   1738 H  H    . LYS   A 1 76  ? 34.315 -4.187  -4.684  1.00 19.17 ?  76  LYS   A H    1 
ATOM   1739 H  HA   . LYS   A 1 76  ? 33.681 -3.930  -7.288  1.00 20.28 ?  76  LYS   A HA   1 
ATOM   1740 H  HB2  . LYS   A 1 76  ? 33.803 -6.273  -5.686  1.00 21.88 ?  76  LYS   A HB2  1 
ATOM   1741 H  HB3  . LYS   A 1 76  ? 33.607 -6.279  -7.260  1.00 21.88 ?  76  LYS   A HB3  1 
ATOM   1742 H  HG2  . LYS   A 1 76  ? 35.776 -5.628  -7.598  1.00 23.23 ?  76  LYS   A HG2  1 
ATOM   1743 H  HG3  . LYS   A 1 76  ? 35.988 -5.371  -6.043  1.00 23.23 ?  76  LYS   A HG3  1 
ATOM   1744 H  HD2  . LYS   A 1 76  ? 35.800 -7.679  -5.662  1.00 24.48 ?  76  LYS   A HD2  1 
ATOM   1745 H  HD3  . LYS   A 1 76  ? 35.671 -7.909  -7.232  1.00 24.48 ?  76  LYS   A HD3  1 
ATOM   1746 H  HE2  . LYS   A 1 76  ? 37.833 -7.079  -7.524  1.00 26.99 ?  76  LYS   A HE2  1 
ATOM   1747 H  HE3  . LYS   A 1 76  ? 37.961 -6.867  -5.955  1.00 26.99 ?  76  LYS   A HE3  1 
ATOM   1748 H  HZ1  . LYS   A 1 76  ? 38.984 -8.783  -6.583  1.00 27.58 ?  76  LYS   A HZ1  1 
ATOM   1749 H  HZ2  . LYS   A 1 76  ? 37.875 -9.119  -5.714  1.00 27.58 ?  76  LYS   A HZ2  1 
ATOM   1750 H  HZ3  . LYS   A 1 76  ? 37.758 -9.312  -7.145  1.00 27.58 ?  76  LYS   A HZ3  1 
ATOM   1751 N  N    . VAL   A 1 77  ? 31.229 -4.427  -7.367  1.00 15.80 ?  77  VAL   A N    1 
ATOM   1752 C  CA   . VAL   A 1 77  ? 29.822 -4.814  -7.292  1.00 15.96 ?  77  VAL   A CA   1 
ATOM   1753 C  C    . VAL   A 1 77  ? 29.759 -6.266  -6.848  1.00 15.82 ?  77  VAL   A C    1 
ATOM   1754 O  O    . VAL   A 1 77  ? 30.419 -7.140  -7.426  1.00 16.09 ?  77  VAL   A O    1 
ATOM   1755 C  CB   . VAL   A 1 77  ? 29.110 -4.604  -8.636  1.00 17.17 ?  77  VAL   A CB   1 
ATOM   1756 C  CG1  . VAL   A 1 77  ? 27.650 -5.034  -8.535  1.00 17.44 ?  77  VAL   A CG1  1 
ATOM   1757 C  CG2  . VAL   A 1 77  ? 29.199 -3.145  -9.058  1.00 18.90 ?  77  VAL   A CG2  1 
ATOM   1758 H  H    . VAL   A 1 77  ? 31.511 -4.182  -8.145  1.00 19.02 ?  77  VAL   A H    1 
ATOM   1759 H  HA   . VAL   A 1 77  ? 29.376 -4.272  -6.628  1.00 19.21 ?  77  VAL   A HA   1 
ATOM   1760 H  HB   . VAL   A 1 77  ? 29.545 -5.139  -9.321  1.00 20.65 ?  77  VAL   A HB   1 
ATOM   1761 H  HG11 . VAL   A 1 77  ? 27.319 -5.203  -9.427  1.00 20.98 ?  77  VAL   A HG11 1 
ATOM   1762 H  HG12 . VAL   A 1 77  ? 27.579 -5.844  -8.010  1.00 20.98 ?  77  VAL   A HG12 1 
ATOM   1763 H  HG13 . VAL   A 1 77  ? 27.148 -4.323  -8.116  1.00 20.98 ?  77  VAL   A HG13 1 
ATOM   1764 H  HG21 . VAL   A 1 77  ? 28.687 -3.021  -9.873  1.00 22.74 ?  77  VAL   A HG21 1 
ATOM   1765 H  HG22 . VAL   A 1 77  ? 28.834 -2.592  -8.350  1.00 22.74 ?  77  VAL   A HG22 1 
ATOM   1766 H  HG23 . VAL   A 1 77  ? 30.128 -2.914  -9.212  1.00 22.74 ?  77  VAL   A HG23 1 
ATOM   1767 N  N    . GLY   A 1 78  ? 28.972 -6.530  -5.808  1.00 15.27 ?  78  GLY   A N    1 
ATOM   1768 C  CA   . GLY   A 1 78  ? 28.940 -7.825  -5.170  1.00 15.78 ?  78  GLY   A CA   1 
ATOM   1769 C  C    . GLY   A 1 78  ? 29.852 -7.934  -3.973  1.00 15.52 ?  78  GLY   A C    1 
ATOM   1770 O  O    . GLY   A 1 78  ? 29.794 -8.948  -3.260  1.00 16.31 ?  78  GLY   A O    1 
ATOM   1771 H  H    . GLY   A 1 78  ? 28.445 -5.955  -5.455  1.00 18.38 ?  78  GLY   A H    1 
ATOM   1772 H  HA2  . GLY   A 1 78  ? 28.034 -8.013  -4.886  1.00 18.99 ?  78  GLY   A HA2  1 
ATOM   1773 H  HA3  . GLY   A 1 78  ? 29.203 -8.505  -5.814  1.00 18.99 ?  78  GLY   A HA3  1 
ATOM   1774 N  N    . GLY   A 1 79  ? 30.698 -6.926  -3.733  1.00 15.21 ?  79  GLY   A N    1 
ATOM   1775 C  CA   . GLY   A 1 79  ? 31.658 -6.956  -2.654  1.00 15.39 ?  79  GLY   A CA   1 
ATOM   1776 C  C    . GLY   A 1 79  ? 31.212 -6.153  -1.445  1.00 14.66 ?  79  GLY   A C    1 
ATOM   1777 O  O    . GLY   A 1 79  ? 30.097 -5.627  -1.375  1.00 15.59 ?  79  GLY   A O    1 
ATOM   1778 H  H    . GLY   A 1 79  ? 30.733 -6.205  -4.200  1.00 18.30 ?  79  GLY   A H    1 
ATOM   1779 H  HA2  . GLY   A 1 79  ? 31.799 -7.884  -2.378  1.00 18.53 ?  79  GLY   A HA2  1 
ATOM   1780 H  HA3  . GLY   A 1 79  ? 32.504 -6.606  -2.964  1.00 18.53 ?  79  GLY   A HA3  1 
ATOM   1781 N  N    . SER   A 1 80  ? 32.116 -6.058  -0.472  1.00 15.51 ?  80  SER   A N    1 
ATOM   1782 C  CA   . SER   A 1 80  ? 31.792 -5.425  0.797   1.00 14.99 ?  80  SER   A CA   1 
ATOM   1783 C  C    . SER   A 1 80  ? 33.066 -4.974  1.490   1.00 15.20 ?  80  SER   A C    1 
ATOM   1784 O  O    . SER   A 1 80  ? 34.176 -5.409  1.163   1.00 16.05 ?  80  SER   A O    1 
ATOM   1785 C  CB   . SER   A 1 80  ? 31.023 -6.376  1.721   1.00 15.66 ?  80  SER   A CB   1 
ATOM   1786 O  OG   . SER   A 1 80  ? 31.853 -7.420  2.214   1.00 17.04 ?  80  SER   A OG   1 
ATOM   1787 H  H    . SER   A 1 80  ? 32.928 -6.340  -0.530  1.00 18.67 ?  80  SER   A H    1 
ATOM   1788 H  HA   . SER   A 1 80  ? 31.241 -4.649  0.619   1.00 18.04 ?  80  SER   A HA   1 
ATOM   1789 H  HB2  . SER   A 1 80  ? 30.672 -5.871  2.469   1.00 18.84 ?  80  SER   A HB2  1 
ATOM   1790 H  HB3  . SER   A 1 80  ? 30.293 -6.777  1.221   1.00 18.84 ?  80  SER   A HB3  1 
ATOM   1791 H  HG   . SER   A 1 80  ? 32.177 -7.856  1.574   1.00 20.50 ?  80  SER   A HG   1 
ATOM   1792 N  N    . CYS   A 1 81  ? 32.879 -4.127  2.495   1.00 15.14 ?  81  CYS   A N    1 
ATOM   1793 C  CA   . CYS   A 1 81  ? 33.931 -3.836  3.454   1.00 15.25 ?  81  CYS   A CA   1 
ATOM   1794 C  C    . CYS   A 1 81  ? 33.284 -3.595  4.808   1.00 14.98 ?  81  CYS   A C    1 
ATOM   1795 O  O    . CYS   A 1 81  ? 32.111 -3.202  4.892   1.00 16.04 ?  81  CYS   A O    1 
ATOM   1796 C  CB   . CYS   A 1 81  ? 34.790 -2.645  3.017   1.00 16.10 ?  81  CYS   A CB   1 
ATOM   1797 S  SG   . CYS   A 1 81  ? 33.902 -1.072  3.063   1.00 14.94 ?  81  CYS   A SG   1 
ATOM   1798 H  H    . CYS   A 1 81  ? 32.139 -3.706  2.650   1.00 18.22 ?  81  CYS   A H    1 
ATOM   1799 H  HA   . CYS   A 1 81  ? 34.509 -4.614  3.534   1.00 18.35 ?  81  CYS   A HA   1 
ATOM   1800 H  HB2  . CYS   A 1 81  ? 35.560 -2.587  3.609   1.00 19.37 ?  81  CYS   A HB2  1 
ATOM   1801 H  HB3  . CYS   A 1 81  ? 35.092 -2.803  2.106   1.00 19.37 ?  81  CYS   A HB3  1 
ATOM   1802 H  HG   . CYS   A 1 81  ? 34.645 -0.196  2.713   1.00 17.98 ?  81  CYS   A HG   1 
ATOM   1803 N  N    . VAL   A 1 82  ? 34.044 -3.864  5.864   1.00 15.42 ?  82  VAL   A N    1 
ATOM   1804 C  CA   . VAL   A 1 82  ? 33.620 -3.629  7.237   1.00 15.72 ?  82  VAL   A CA   1 
ATOM   1805 C  C    . VAL   A 1 82  ? 34.220 -2.317  7.710   1.00 15.96 ?  82  VAL   A C    1 
ATOM   1806 O  O    . VAL   A 1 82  ? 35.447 -2.150  7.695   1.00 16.64 ?  82  VAL   A O    1 
ATOM   1807 C  CB   . VAL   A 1 82  ? 34.052 -4.774  8.165   1.00 16.82 ?  82  VAL   A CB   1 
ATOM   1808 C  CG1  . VAL   A 1 82  ? 33.627 -4.483  9.598   1.00 17.94 ?  82  VAL   A CG1  1 
ATOM   1809 C  CG2  . VAL   A 1 82  ? 33.487 -6.099  7.694   1.00 17.86 ?  82  VAL   A CG2  1 
ATOM   1810 H  H    . VAL   A 1 82  ? 34.830 -4.221  5.810   1.00 18.56 ?  82  VAL   A H    1 
ATOM   1811 H  HA   . VAL   A 1 82  ? 32.656 -3.552  7.270   1.00 18.92 ?  82  VAL   A HA   1 
ATOM   1812 H  HB   . VAL   A 1 82  ? 35.019 -4.838  8.155   1.00 20.24 ?  82  VAL   A HB   1 
ATOM   1813 H  HG11 . VAL   A 1 82  ? 33.716 -5.292  10.123  1.00 21.58 ?  82  VAL   A HG11 1 
ATOM   1814 H  HG12 . VAL   A 1 82  ? 34.199 -3.788  9.966   1.00 21.58 ?  82  VAL   A HG12 1 
ATOM   1815 H  HG13 . VAL   A 1 82  ? 32.704 -4.185  9.601   1.00 21.58 ?  82  VAL   A HG13 1 
ATOM   1816 H  HG21 . VAL   A 1 82  ? 33.739 -6.794  8.325   1.00 21.49 ?  82  VAL   A HG21 1 
ATOM   1817 H  HG22 . VAL   A 1 82  ? 32.519 -6.034  7.648   1.00 21.49 ?  82  VAL   A HG22 1 
ATOM   1818 H  HG23 . VAL   A 1 82  ? 33.847 -6.304  6.818   1.00 21.49 ?  82  VAL   A HG23 1 
ATOM   1819 N  N    . LEU   A 1 83  ? 33.365 -1.396  8.138   1.00 15.46 ?  83  LEU   A N    1 
ATOM   1820 C  CA   . LEU   A 1 83  ? 33.788 -0.133  8.720   1.00 15.34 ?  83  LEU   A CA   1 
ATOM   1821 C  C    . LEU   A 1 83  ? 33.064 0.043   10.051  1.00 15.61 ?  83  LEU   A C    1 
ATOM   1822 O  O    . LEU   A 1 83  ? 32.324 -0.840  10.505  1.00 16.17 ?  83  LEU   A O    1 
ATOM   1823 C  CB   . LEU   A 1 83  ? 33.531 1.025   7.744   1.00 15.56 ?  83  LEU   A CB   1 
ATOM   1824 C  CG   . LEU   A 1 83  ? 34.435 1.029   6.507   1.00 16.14 ?  83  LEU   A CG   1 
ATOM   1825 C  CD1  . LEU   A 1 83  ? 34.014 2.089   5.509   1.00 16.27 ?  83  LEU   A CD1  1 
ATOM   1826 C  CD2  . LEU   A 1 83  ? 35.899 1.248   6.906   1.00 16.87 ?  83  LEU   A CD2  1 
ATOM   1827 H  H    . LEU   A 1 83  ? 32.507 -1.476  8.095   1.00 18.60 ?  83  LEU   A H    1 
ATOM   1828 H  HA   . LEU   A 1 83  ? 34.744 -0.157  8.894   1.00 18.47 ?  83  LEU   A HA   1 
ATOM   1829 H  HB2  . LEU   A 1 83  ? 32.613 0.978   7.426   1.00 18.72 ?  83  LEU   A HB2  1 
ATOM   1830 H  HB3  . LEU   A 1 83  ? 33.669 1.872   8.200   1.00 18.72 ?  83  LEU   A HB3  1 
ATOM   1831 H  HG   . LEU   A 1 83  ? 34.374 0.165   6.066   1.00 19.43 ?  83  LEU   A HG   1 
ATOM   1832 H  HD11 . LEU   A 1 83  ? 34.604 2.053   4.736   1.00 19.58 ?  83  LEU   A HD11 1 
ATOM   1833 H  HD12 . LEU   A 1 83  ? 33.101 1.918   5.232   1.00 19.58 ?  83  LEU   A HD12 1 
ATOM   1834 H  HD13 . LEU   A 1 83  ? 34.076 2.961   5.928   1.00 19.58 ?  83  LEU   A HD13 1 
ATOM   1835 H  HD21 . LEU   A 1 83  ? 36.423 1.438   6.110   1.00 20.29 ?  83  LEU   A HD21 1 
ATOM   1836 H  HD22 . LEU   A 1 83  ? 35.948 2.003   7.517   1.00 20.29 ?  83  LEU   A HD22 1 
ATOM   1837 H  HD23 . LEU   A 1 83  ? 36.235 0.451   7.340   1.00 20.29 ?  83  LEU   A HD23 1 
ATOM   1838 N  N    . SER   A 1 84  ? 33.274 1.196   10.680  1.00 15.95 ?  84  SER   A N    1 
ATOM   1839 C  CA   . SER   A 1 84  ? 32.628 1.454   11.957  1.00 15.90 ?  84  SER   A CA   1 
ATOM   1840 C  C    . SER   A 1 84  ? 31.113 1.540   11.808  1.00 16.20 ?  84  SER   A C    1 
ATOM   1841 O  O    . SER   A 1 84  ? 30.588 1.990   10.788  1.00 15.68 ?  84  SER   A O    1 
ATOM   1842 C  CB   . SER   A 1 84  ? 33.124 2.774   12.535  1.00 17.02 ?  84  SER   A CB   1 
ATOM   1843 O  OG   . SER   A 1 84  ? 32.494 3.051   13.767  1.00 18.28 ?  84  SER   A OG   1 
ATOM   1844 H  H    . SER   A 1 84  ? 33.781 1.837   10.397  1.00 19.19 ?  84  SER   A H    1 
ATOM   1845 H  HA   . SER   A 1 84  ? 32.846 0.740   12.576  1.00 19.13 ?  84  SER   A HA   1 
ATOM   1846 H  HB2  . SER   A 1 84  ? 34.085 2.718   12.665  1.00 20.48 ?  84  SER   A HB2  1 
ATOM   1847 H  HB3  . SER   A 1 84  ? 32.912 3.487   11.920  1.00 20.48 ?  84  SER   A HB3  1 
ATOM   1848 H  HG   . SER   A 1 84  ? 32.791 3.767   14.092  1.00 21.99 ?  84  SER   A HG   1 
ATOM   1849 N  N    . GLY   A 1 85  ? 30.407 1.106   12.852  1.00 16.59 ?  85  GLY   A N    1 
ATOM   1850 C  CA   . GLY   A 1 85  ? 28.983 1.333   12.948  1.00 17.40 ?  85  GLY   A CA   1 
ATOM   1851 C  C    . GLY   A 1 85  ? 28.603 2.661   13.565  1.00 17.60 ?  85  GLY   A C    1 
ATOM   1852 O  O    . GLY   A 1 85  ? 27.412 2.977   13.654  1.00 18.35 ?  85  GLY   A O    1 
ATOM   1853 H  H    . GLY   A 1 85  ? 30.745 0.675   13.518  1.00 19.97 ?  85  GLY   A H    1 
ATOM   1854 H  HA2  . GLY   A 1 85  ? 28.597 1.281   12.058  1.00 20.94 ?  85  GLY   A HA2  1 
ATOM   1855 H  HA3  . GLY   A 1 85  ? 28.588 0.624   13.482  1.00 20.94 ?  85  GLY   A HA3  1 
ATOM   1856 N  N    . HIS   A 1 86  ? 29.583 3.442   14.009  1.00 17.10 ?  86  HIS   A N    1 
ATOM   1857 C  CA   . HIS   A 1 86  ? 29.356 4.784   14.561  1.00 17.74 ?  86  HIS   A CA   1 
ATOM   1858 C  C    . HIS   A 1 86  ? 28.382 4.676   15.730  1.00 18.82 ?  86  HIS   A C    1 
ATOM   1859 O  O    . HIS   A 1 86  ? 28.570 3.800   16.591  1.00 19.77 ?  86  HIS   A O    1 
ATOM   1860 C  CB   . HIS   A 1 86  ? 28.985 5.756   13.448  1.00 17.63 ?  86  HIS   A CB   1 
ATOM   1861 C  CG   . HIS   A 1 86  ? 30.050 5.863   12.410  1.00 17.44 ?  86  HIS   A CG   1 
ATOM   1862 N  ND1  . HIS   A 1 86  ? 31.133 6.707   12.541  1.00 17.99 ?  86  HIS   A ND1  1 
ATOM   1863 C  CD2  . HIS   A 1 86  ? 30.238 5.179   11.259  1.00 17.09 ?  86  HIS   A CD2  1 
ATOM   1864 C  CE1  . HIS   A 1 86  ? 31.926 6.555   11.495  1.00 17.32 ?  86  HIS   A CE1  1 
ATOM   1865 N  NE2  . HIS   A 1 86  ? 31.415 5.623   10.712  1.00 16.78 ?  86  HIS   A NE2  1 
ATOM   1866 H  H    . HIS   A 1 86  ? 30.403 3.208   14.013  1.00 20.58 ?  86  HIS   A H    1 
ATOM   1867 H  HA   . HIS   A 1 86  ? 30.188 5.092   14.929  1.00 21.34 ?  86  HIS   A HA   1 
ATOM   1868 H  HB2  . HIS   A 1 86  ? 28.167 5.462   13.016  1.00 21.21 ?  86  HIS   A HB2  1 
ATOM   1869 H  HB3  . HIS   A 1 86  ? 28.852 6.642   13.829  1.00 21.21 ?  86  HIS   A HB3  1 
ATOM   1870 H  HD2  . HIS   A 1 86  ? 29.677 4.519   10.906  1.00 20.57 ?  86  HIS   A HD2  1 
ATOM   1871 H  HE1  . HIS   A 1 86  ? 32.715 7.017   11.337  1.00 20.84 ?  86  HIS   A HE1  1 
ATOM   1872 H  HE2  . HIS   A 1 86  ? 31.749 5.355   9.961   1.00 20.19 ?  86  HIS   A HE2  1 
ATOM   1873 N  N    . ASN   A 1 87  ? 27.368 5.528   15.808  1.00 19.18 ?  87  ASN   A N    1 
ATOM   1874 C  CA   . ASN   A 1 87  ? 26.386 5.508   16.879  1.00 20.21 ?  87  ASN   A CA   1 
ATOM   1875 C  C    . ASN   A 1 87  ? 25.264 4.506   16.644  1.00 21.03 ?  87  ASN   A C    1 
ATOM   1876 O  O    . ASN   A 1 87  ? 24.343 4.437   17.463  1.00 23.00 ?  87  ASN   A O    1 
ATOM   1877 C  CB   . ASN   A 1 87  ? 25.785 6.912   17.043  1.00 21.02 ?  87  ASN   A CB   1 
ATOM   1878 C  CG   . ASN   A 1 87  ? 25.284 7.492   15.728  1.00 21.49 ?  87  ASN   A CG   1 
ATOM   1879 O  OD1  . ASN   A 1 87  ? 25.918 7.346   14.685  1.00 21.78 ?  87  ASN   A OD1  1 
ATOM   1880 N  ND2  . ASN   A 1 87  ? 24.141 8.158   15.775  1.00 22.73 ?  87  ASN   A ND2  1 
ATOM   1881 H  H    . ASN   A 1 87  ? 27.223 6.146   15.231  1.00 23.08 ?  87  ASN   A H    1 
ATOM   1882 H  HA   . ASN   A 1 87  ? 26.822 5.273   17.712  1.00 24.31 ?  87  ASN   A HA   1 
ATOM   1883 H  HB2  . ASN   A 1 87  ? 25.034 6.866   17.657  1.00 25.28 ?  87  ASN   A HB2  1 
ATOM   1884 H  HB3  . ASN   A 1 87  ? 26.466 7.504   17.397  1.00 25.28 ?  87  ASN   A HB3  1 
ATOM   1885 H  HD21 . ASN   A 1 87  ? 23.817 8.503   15.059  1.00 27.33 ?  87  ASN   A HD21 1 
ATOM   1886 H  HD22 . ASN   A 1 87  ? 23.723 8.243   16.523  1.00 27.33 ?  87  ASN   A HD22 1 
ATOM   1887 N  N    . LEU   A 1 88  ? 25.312 3.733   15.563  1.00 20.17 ?  88  LEU   A N    1 
ATOM   1888 C  CA   . LEU   A 1 88  ? 24.200 2.876   15.171  1.00 19.31 ?  88  LEU   A CA   1 
ATOM   1889 C  C    . LEU   A 1 88  ? 24.421 1.396   15.448  1.00 19.55 ?  88  LEU   A C    1 
ATOM   1890 O  O    . LEU   A 1 88  ? 23.446 0.664   15.625  1.00 19.89 ?  88  LEU   A O    1 
ATOM   1891 C  CB   . LEU   A 1 88  ? 23.923 3.048   13.676  1.00 19.25 ?  88  LEU   A CB   1 
ATOM   1892 C  CG   . LEU   A 1 88  ? 23.647 4.476   13.199  1.00 20.38 ?  88  LEU   A CG   1 
ATOM   1893 C  CD1  . LEU   A 1 88  ? 23.501 4.491   11.691  1.00 21.08 ?  88  LEU   A CD1  1 
ATOM   1894 C  CD2  . LEU   A 1 88  ? 22.399 5.049   13.863  1.00 22.15 ?  88  LEU   A CD2  1 
ATOM   1895 H  H    . LEU   A 1 88  ? 25.994 3.681   15.041  1.00 24.26 ?  88  LEU   A H    1 
ATOM   1896 H  HA   . LEU   A 1 88  ? 23.407 3.157   15.653  1.00 23.23 ?  88  LEU   A HA   1 
ATOM   1897 H  HB2  . LEU   A 1 88  ? 24.690 2.727   13.183  1.00 23.16 ?  88  LEU   A HB2  1 
ATOM   1898 H  HB3  . LEU   A 1 88  ? 23.145 2.519   13.448  1.00 23.16 ?  88  LEU   A HB3  1 
ATOM   1899 H  HG   . LEU   A 1 88  ? 24.399 5.044   13.431  1.00 24.51 ?  88  LEU   A HG   1 
ATOM   1900 H  HD11 . LEU   A 1 88  ? 23.329 5.401   11.398  1.00 25.35 ?  88  LEU   A HD11 1 
ATOM   1901 H  HD12 . LEU   A 1 88  ? 24.320 4.164   11.290  1.00 25.35 ?  88  LEU   A HD12 1 
ATOM   1902 H  HD13 . LEU   A 1 88  ? 22.757 3.919   11.441  1.00 25.35 ?  88  LEU   A HD13 1 
ATOM   1903 H  HD21 . LEU   A 1 88  ? 22.210 5.921   13.481  1.00 26.64 ?  88  LEU   A HD21 1 
ATOM   1904 H  HD22 . LEU   A 1 88  ? 21.655 4.449   13.703  1.00 26.64 ?  88  LEU   A HD22 1 
ATOM   1905 H  HD23 . LEU   A 1 88  ? 22.560 5.132   14.815  1.00 26.64 ?  88  LEU   A HD23 1 
ATOM   1906 N  N    . ALA   A 1 89  ? 25.669 0.945   15.478  1.00 19.22 ?  89  ALA   A N    1 
ATOM   1907 C  CA   . ALA   A 1 89  ? 26.009 -0.466  15.591  1.00 18.92 ?  89  ALA   A CA   1 
ATOM   1908 C  C    . ALA   A 1 89  ? 27.491 -0.533  15.921  1.00 19.09 ?  89  ALA   A C    1 
ATOM   1909 O  O    . ALA   A 1 89  ? 28.204 0.467   15.826  1.00 19.53 ?  89  ALA   A O    1 
ATOM   1910 C  CB   . ALA   A 1 89  ? 25.741 -1.191  14.275  1.00 19.01 ?  89  ALA   A CB   1 
ATOM   1911 H  H    . ALA   A 1 89  ? 26.358 1.455   15.428  1.00 23.11 ?  89  ALA   A H    1 
ATOM   1912 H  HA   . ALA   A 1 89  ? 25.496 -0.882  16.304  1.00 22.75 ?  89  ALA   A HA   1 
ATOM   1913 H  HB1  . ALA   A 1 89  ? 25.988 -2.124  14.372  1.00 22.86 ?  89  ALA   A HB1  1 
ATOM   1914 H  HB2  . ALA   A 1 89  ? 24.797 -1.121  14.059  1.00 22.86 ?  89  ALA   A HB2  1 
ATOM   1915 H  HB3  . ALA   A 1 89  ? 26.271 -0.780  13.574  1.00 22.86 ?  89  ALA   A HB3  1 
ATOM   1916 N  N    . LYS   A 1 90  ? 27.963 -1.719  16.297  1.00 19.81 ?  90  LYS   A N    1 
ATOM   1917 C  CA   . LYS   A 1 90  ? 29.404 -1.879  16.456  1.00 21.02 ?  90  LYS   A CA   1 
ATOM   1918 C  C    . LYS   A 1 90  ? 30.115 -1.696  15.121  1.00 19.55 ?  90  LYS   A C    1 
ATOM   1919 O  O    . LYS   A 1 90  ? 31.051 -0.892  15.002  1.00 20.76 ?  90  LYS   A O    1 
ATOM   1920 C  CB   . LYS   A 1 90  ? 29.731 -3.241  17.069  1.00 23.80 ?  90  LYS   A CB   1 
ATOM   1921 C  CG   . LYS   A 1 90  ? 31.215 -3.411  17.377  1.00 28.31 ?  90  LYS   A CG   1 
ATOM   1922 C  CD   . LYS   A 1 90  ? 31.451 -4.524  18.387  1.00 31.76 ?  90  LYS   A CD   1 
ATOM   1923 C  CE   . LYS   A 1 90  ? 32.869 -4.486  18.944  1.00 34.78 ?  90  LYS   A CE   1 
ATOM   1924 N  NZ   . LYS   A 1 90  ? 33.874 -5.050  18.002  1.00 37.93 ?  90  LYS   A NZ   1 
ATOM   1925 H  H    . LYS   A 1 90  ? 27.489 -2.414  16.458  1.00 23.83 ?  90  LYS   A H    1 
ATOM   1926 H  HA   . LYS   A 1 90  ? 29.730 -1.194  17.057  1.00 25.28 ?  90  LYS   A HA   1 
ATOM   1927 H  HB2  . LYS   A 1 90  ? 29.236 -3.338  17.901  1.00 28.61 ?  90  LYS   A HB2  1 
ATOM   1928 H  HB3  . LYS   A 1 90  ? 29.468 -3.940  16.449  1.00 28.61 ?  90  LYS   A HB3  1 
ATOM   1929 H  HG2  . LYS   A 1 90  ? 31.687 -3.634  16.560  1.00 34.02 ?  90  LYS   A HG2  1 
ATOM   1930 H  HG3  . LYS   A 1 90  ? 31.559 -2.584  17.748  1.00 34.02 ?  90  LYS   A HG3  1 
ATOM   1931 H  HD2  . LYS   A 1 90  ? 30.831 -4.422  19.127  1.00 38.16 ?  90  LYS   A HD2  1 
ATOM   1932 H  HD3  . LYS   A 1 90  ? 31.317 -5.382  17.955  1.00 38.16 ?  90  LYS   A HD3  1 
ATOM   1933 H  HE2  . LYS   A 1 90  ? 33.113 -3.564  19.125  1.00 41.79 ?  90  LYS   A HE2  1 
ATOM   1934 H  HE3  . LYS   A 1 90  ? 32.901 -5.004  19.763  1.00 41.79 ?  90  LYS   A HE3  1 
ATOM   1935 H  HZ1  . LYS   A 1 90  ? 34.687 -5.010  18.365  1.00 45.57 ?  90  LYS   A HZ1  1 
ATOM   1936 H  HZ2  . LYS   A 1 90  ? 33.680 -5.901  17.825  1.00 45.57 ?  90  LYS   A HZ2  1 
ATOM   1937 H  HZ3  . LYS   A 1 90  ? 33.874 -4.588  17.243  1.00 45.57 ?  90  LYS   A HZ3  1 
ATOM   1938 N  N    . HIS   A 1 91  ? 29.656 -2.416  14.098  1.00 17.48 ?  91  HIS   A N    1 
ATOM   1939 C  CA   . HIS   A 1 91  ? 30.234 -2.396  12.768  1.00 16.68 ?  91  HIS   A CA   1 
ATOM   1940 C  C    . HIS   A 1 91  ? 29.151 -2.112  11.741  1.00 15.97 ?  91  HIS   A C    1 
ATOM   1941 O  O    . HIS   A 1 91  ? 27.981 -2.458  11.933  1.00 16.62 ?  91  HIS   A O    1 
ATOM   1942 C  CB   . HIS   A 1 91  ? 30.841 -3.761  12.402  1.00 18.55 ?  91  HIS   A CB   1 
ATOM   1943 C  CG   . HIS   A 1 91  ? 31.840 -4.271  13.392  1.00 22.43 ?  91  HIS   A CG   1 
ATOM   1944 N  ND1  . HIS   A 1 91  ? 33.118 -3.765  13.487  1.00 24.22 ?  91  HIS   A ND1  1 
ATOM   1945 C  CD2  . HIS   A 1 91  ? 31.756 -5.253  14.320  1.00 24.22 ?  91  HIS   A CD2  1 
ATOM   1946 C  CE1  . HIS   A 1 91  ? 33.777 -4.410  14.434  1.00 24.99 ?  91  HIS   A CE1  1 
ATOM   1947 N  NE2  . HIS   A 1 91  ? 32.972 -5.319  14.956  1.00 25.25 ?  91  HIS   A NE2  1 
ATOM   1948 H  H    . HIS   A 1 91  ? 28.975 -2.955  14.158  1.00 21.03 ?  91  HIS   A H    1 
ATOM   1949 H  HA   . HIS   A 1 91  ? 30.922 -1.724  12.708  1.00 20.07 ?  91  HIS   A HA   1 
ATOM   1950 H  HB2  . HIS   A 1 91  ? 30.132 -4.419  12.339  1.00 22.31 ?  91  HIS   A HB2  1 
ATOM   1951 H  HB3  . HIS   A 1 91  ? 31.292 -3.684  11.544  1.00 22.31 ?  91  HIS   A HB3  1 
ATOM   1952 H  HD1  . HIS   A 1 91  ? 33.440 -3.129  13.001  1.00 29.12 ?  91  HIS   A HD1  1 
ATOM   1953 H  HD2  . HIS   A 1 91  ? 31.018 -5.784  14.497  1.00 29.12 ?  91  HIS   A HD2  1 
ATOM   1954 H  HE1  . HIS   A 1 91  ? 34.661 -4.246  14.689  1.00 30.04 ?  91  HIS   A HE1  1 
ATOM   1955 N  N    . CYS   A 1 92  ? 29.557 -1.504  10.635  1.00 15.79 ?  92  CYS   A N    1 
ATOM   1956 C  CA   . CYS   A 1 92  ? 28.737 -1.428  9.436   1.00 15.48 ?  92  CYS   A CA   1 
ATOM   1957 C  C    . CYS   A 1 92  ? 29.384 -2.251  8.334   1.00 15.43 ?  92  CYS   A C    1 
ATOM   1958 O  O    . CYS   A 1 92  ? 30.538 -2.000  7.959   1.00 15.64 ?  92  CYS   A O    1 
ATOM   1959 C  CB   . CYS   A 1 92  ? 28.542 0.012   8.971   1.00 15.83 ?  92  CYS   A CB   1 
ATOM   1960 S  SG   . CYS   A 1 92  ? 27.512 0.129   7.476   1.00 14.53 ?  92  CYS   A SG   1 
ATOM   1961 H  H    . CYS   A 1 92  ? 30.323 -1.113  10.560  1.00 19.00 ?  92  CYS   A H    1 
ATOM   1962 H  HA   . CYS   A 1 92  ? 27.864 -1.801  9.629   1.00 18.63 ?  92  CYS   A HA   1 
ATOM   1963 H  HB2  . CYS   A 1 92  ? 28.106 0.521   9.675   1.00 19.05 ?  92  CYS   A HB2  1 
ATOM   1964 H  HB3  . CYS   A 1 92  ? 29.408 0.402   8.771   1.00 19.05 ?  92  CYS   A HB3  1 
ATOM   1965 H  HG   . CYS   A 1 92  ? 27.385 1.283   7.187   1.00 17.50 ?  92  CYS   A HG   1 
ATOM   1966 N  N    . LEU   A 1 93  ? 28.641 -3.229  7.828   1.00 14.97 ?  93  LEU   A N    1 
ATOM   1967 C  CA   . LEU   A 1 93  ? 29.050 -3.994  6.658   1.00 14.91 ?  93  LEU   A CA   1 
ATOM   1968 C  C    . LEU   A 1 93  ? 28.456 -3.297  5.443   1.00 14.76 ?  93  LEU   A C    1 
ATOM   1969 O  O    . LEU   A 1 93  ? 27.246 -3.355  5.205   1.00 14.65 ?  93  LEU   A O    1 
ATOM   1970 C  CB   . LEU   A 1 93  ? 28.570 -5.437  6.773   1.00 15.17 ?  93  LEU   A CB   1 
ATOM   1971 C  CG   . LEU   A 1 93  ? 28.955 -6.328  5.596   1.00 15.51 ?  93  LEU   A CG   1 
ATOM   1972 C  CD1  . LEU   A 1 93  ? 30.461 -6.595  5.578   1.00 16.57 ?  93  LEU   A CD1  1 
ATOM   1973 C  CD2  . LEU   A 1 93  ? 28.192 -7.642  5.670   1.00 15.86 ?  93  LEU   A CD2  1 
ATOM   1974 H  H    . LEU   A 1 93  ? 27.883 -3.472  8.162   1.00 18.02 ?  93  LEU   A H    1 
ATOM   1975 H  HA   . LEU   A 1 93  ? 30.013 -3.982  6.588   1.00 17.95 ?  93  LEU   A HA   1 
ATOM   1976 H  HB2  . LEU   A 1 93  ? 28.954 -5.826  7.577   1.00 18.26 ?  93  LEU   A HB2  1 
ATOM   1977 H  HB3  . LEU   A 1 93  ? 27.603 -5.440  6.843   1.00 18.26 ?  93  LEU   A HB3  1 
ATOM   1978 H  HG   . LEU   A 1 93  ? 28.719 -5.888  4.769   1.00 18.67 ?  93  LEU   A HG   1 
ATOM   1979 H  HD11 . LEU   A 1 93  ? 30.666 -7.205  4.850   1.00 19.94 ?  93  LEU   A HD11 1 
ATOM   1980 H  HD12 . LEU   A 1 93  ? 30.935 -5.761  5.454   1.00 19.94 ?  93  LEU   A HD12 1 
ATOM   1981 H  HD13 . LEU   A 1 93  ? 30.723 -7.002  6.424   1.00 19.94 ?  93  LEU   A HD13 1 
ATOM   1982 H  HD21 . LEU   A 1 93  ? 28.454 -8.203  4.923   1.00 19.09 ?  93  LEU   A HD21 1 
ATOM   1983 H  HD22 . LEU   A 1 93  ? 28.407 -8.088  6.507   1.00 19.09 ?  93  LEU   A HD22 1 
ATOM   1984 H  HD23 . LEU   A 1 93  ? 27.241 -7.459  5.631   1.00 19.09 ?  93  LEU   A HD23 1 
ATOM   1985 N  N    . HIS   A 1 94  ? 29.305 -2.585  4.700   1.00 14.04 ?  94  HIS   A N    1 
ATOM   1986 C  CA   . HIS   A 1 94  ? 28.893 -1.915  3.469   1.00 14.14 ?  94  HIS   A CA   1 
ATOM   1987 C  C    . HIS   A 1 94  ? 28.901 -2.946  2.352   1.00 14.02 ?  94  HIS   A C    1 
ATOM   1988 O  O    . HIS   A 1 94  ? 29.967 -3.452  1.993   1.00 15.42 ?  94  HIS   A O    1 
ATOM   1989 C  CB   . HIS   A 1 94  ? 29.848 -0.767  3.141   1.00 14.29 ?  94  HIS   A CB   1 
ATOM   1990 C  CG   . HIS   A 1 94  ? 29.833 0.327   4.154   1.00 14.15 ?  94  HIS   A CG   1 
ATOM   1991 N  ND1  . HIS   A 1 94  ? 28.941 1.379   4.109   1.00 14.19 ?  94  HIS   A ND1  1 
ATOM   1992 C  CD2  . HIS   A 1 94  ? 30.571 0.500   5.272   1.00 14.95 ?  94  HIS   A CD2  1 
ATOM   1993 C  CE1  . HIS   A 1 94  ? 29.154 2.166   5.148   1.00 14.49 ?  94  HIS   A CE1  1 
ATOM   1994 N  NE2  . HIS   A 1 94  ? 30.139 1.658   5.866   1.00 13.97 ?  94  HIS   A NE2  1 
ATOM   1995 H  H    . HIS   A 1 94  ? 30.134 -2.473  4.893   1.00 16.90 ?  94  HIS   A H    1 
ATOM   1996 H  HA   . HIS   A 1 94  ? 27.992 -1.558  3.568   1.00 17.02 ?  94  HIS   A HA   1 
ATOM   1997 H  HB2  . HIS   A 1 94  ? 30.747 -1.109  3.094   1.00 17.20 ?  94  HIS   A HB2  1 
ATOM   1998 H  HB3  . HIS   A 1 94  ? 29.589 -0.378  2.289   1.00 17.20 ?  94  HIS   A HB3  1 
ATOM   1999 H  HD2  . HIS   A 1 94  ? 31.253 -0.046  5.571   1.00 17.99 ?  94  HIS   A HD2  1 
ATOM   2000 H  HE1  . HIS   A 1 94  ? 28.684 2.951   5.338   1.00 17.44 ?  94  HIS   A HE1  1 
ATOM   2001 H  HE2  . HIS   A 1 94  ? 30.454 2.005   6.588   1.00 16.82 ?  94  HIS   A HE2  1 
ATOM   2002 N  N    . VAL   A 1 95  ? 27.729 -3.277  1.811   1.00 13.37 ?  95  VAL   A N    1 
ATOM   2003 C  CA   . VAL   A 1 95  ? 27.588 -4.316  0.791   1.00 13.83 ?  95  VAL   A CA   1 
ATOM   2004 C  C    . VAL   A 1 95  ? 27.039 -3.673  -0.469  1.00 13.50 ?  95  VAL   A C    1 
ATOM   2005 O  O    . VAL   A 1 95  ? 26.043 -2.949  -0.410  1.00 14.11 ?  95  VAL   A O    1 
ATOM   2006 C  CB   . VAL   A 1 95  ? 26.652 -5.453  1.240   1.00 14.42 ?  95  VAL   A CB   1 
ATOM   2007 C  CG1  . VAL   A 1 95  ? 26.547 -6.494  0.130   1.00 15.04 ?  95  VAL   A CG1  1 
ATOM   2008 C  CG2  . VAL   A 1 95  ? 27.144 -6.063  2.528   1.00 14.99 ?  95  VAL   A CG2  1 
ATOM   2009 H  H    . VAL   A 1 95  ? 26.979 -2.915  2.034   1.00 16.09 ?  95  VAL   A H    1 
ATOM   2010 H  HA   . VAL   A 1 95  ? 28.454 -4.695  0.591   1.00 16.65 ?  95  VAL   A HA   1 
ATOM   2011 H  HB   . VAL   A 1 95  ? 25.766 -5.095  1.398   1.00 17.35 ?  95  VAL   A HB   1 
ATOM   2012 H  HG11 . VAL   A 1 95  ? 26.163 -7.308  0.494   1.00 18.10 ?  95  VAL   A HG11 1 
ATOM   2013 H  HG12 . VAL   A 1 95  ? 25.980 -6.152  -0.579  1.00 18.10 ?  95  VAL   A HG12 1 
ATOM   2014 H  HG13 . VAL   A 1 95  ? 27.436 -6.680  -0.217  1.00 18.10 ?  95  VAL   A HG13 1 
ATOM   2015 H  HG21 . VAL   A 1 95  ? 26.589 -6.831  2.749   1.00 18.05 ?  95  VAL   A HG21 1 
ATOM   2016 H  HG22 . VAL   A 1 95  ? 28.065 -6.347  2.415   1.00 18.05 ?  95  VAL   A HG22 1 
ATOM   2017 H  HG23 . VAL   A 1 95  ? 27.086 -5.402  3.235   1.00 18.05 ?  95  VAL   A HG23 1 
ATOM   2018 N  N    A VAL   A 1 96  ? 27.675 -3.961  -1.604  0.66 13.42 ?  96  VAL   A N    1 
ATOM   2019 N  N    B VAL   A 1 96  ? 27.672 -3.938  -1.606  0.34 13.19 ?  96  VAL   A N    1 
ATOM   2020 C  CA   A VAL   A 1 96  ? 27.267 -3.432  -2.898  0.66 13.93 ?  96  VAL   A CA   1 
ATOM   2021 C  CA   B VAL   A 1 96  ? 27.269 -3.335  -2.871  0.34 13.48 ?  96  VAL   A CA   1 
ATOM   2022 C  C    A VAL   A 1 96  ? 26.482 -4.503  -3.641  0.66 14.59 ?  96  VAL   A C    1 
ATOM   2023 C  C    B VAL   A 1 96  ? 26.435 -4.348  -3.645  0.34 13.79 ?  96  VAL   A C    1 
ATOM   2024 O  O    A VAL   A 1 96  ? 27.062 -5.463  -4.158  0.66 15.54 ?  96  VAL   A O    1 
ATOM   2025 O  O    B VAL   A 1 96  ? 26.971 -5.269  -4.267  0.34 13.71 ?  96  VAL   A O    1 
ATOM   2026 C  CB   A VAL   A 1 96  ? 28.471 -2.973  -3.731  0.66 14.25 ?  96  VAL   A CB   1 
ATOM   2027 C  CB   B VAL   A 1 96  ? 28.468 -2.844  -3.682  0.34 13.53 ?  96  VAL   A CB   1 
ATOM   2028 C  CG1  A VAL   A 1 96  ? 27.974 -2.283  -4.984  0.66 14.45 ?  96  VAL   A CG1  1 
ATOM   2029 C  CG1  B VAL   A 1 96  ? 27.991 -2.303  -5.015  0.34 13.64 ?  96  VAL   A CG1  1 
ATOM   2030 C  CG2  A VAL   A 1 96  ? 29.375 -2.055  -2.923  0.66 14.21 ?  96  VAL   A CG2  1 
ATOM   2031 C  CG2  B VAL   A 1 96  ? 29.219 -1.777  -2.911  0.34 13.36 ?  96  VAL   A CG2  1 
ATOM   2032 H  H    A VAL   A 1 96  ? 28.366 -4.476  -1.644  0.66 16.15 ?  96  VAL   A H    1 
ATOM   2033 H  H    B VAL   A 1 96  ? 28.351 -4.468  -1.668  0.34 15.88 ?  96  VAL   A H    1 
ATOM   2034 H  HA   A VAL   A 1 96  ? 26.690 -2.668  -2.763  0.66 16.77 ?  96  VAL   A HA   1 
ATOM   2035 H  HA   B VAL   A 1 96  ? 26.706 -2.571  -2.686  0.34 16.23 ?  96  VAL   A HA   1 
ATOM   2036 H  HB   A VAL   A 1 96  ? 28.991 -3.749  -3.999  0.66 17.16 ?  96  VAL   A HB   1 
ATOM   2037 H  HB   B VAL   A 1 96  ? 29.071 -3.585  -3.850  0.34 16.29 ?  96  VAL   A HB   1 
ATOM   2038 H  HG11 A VAL   A 1 96  ? 28.724 -1.862  -5.431  0.66 17.40 ?  96  VAL   A HG11 1 
ATOM   2039 H  HG11 B VAL   A 1 96  ? 28.712 -1.802  -5.425  0.34 16.42 ?  96  VAL   A HG11 1 
ATOM   2040 H  HG12 A VAL   A 1 96  ? 27.565 -2.939  -5.569  0.66 17.40 ?  96  VAL   A HG12 1 
ATOM   2041 H  HG12 B VAL   A 1 96  ? 27.734 -3.041  -5.588  0.34 16.42 ?  96  VAL   A HG12 1 
ATOM   2042 H  HG13 A VAL   A 1 96  ? 27.321 -1.609  -4.733  0.66 17.40 ?  96  VAL   A HG13 1 
ATOM   2043 H  HG13 B VAL   A 1 96  ? 27.230 -1.719  -4.864  0.34 16.42 ?  96  VAL   A HG13 1 
ATOM   2044 H  HG21 A VAL   A 1 96  ? 30.068 -1.704  -3.505  0.66 17.11 ?  96  VAL   A HG21 1 
ATOM   2045 H  HG21 B VAL   A 1 96  ? 29.954 -1.455  -3.454  0.34 16.09 ?  96  VAL   A HG21 1 
ATOM   2046 H  HG22 A VAL   A 1 96  ? 28.844 -1.328  -2.565  0.66 17.11 ?  96  VAL   A HG22 1 
ATOM   2047 H  HG22 B VAL   A 1 96  ? 28.610 -1.048  -2.711  0.34 16.09 ?  96  VAL   A HG22 1 
ATOM   2048 H  HG23 A VAL   A 1 96  ? 29.776 -2.562  -2.200  0.66 17.11 ?  96  VAL   A HG23 1 
ATOM   2049 H  HG23 B VAL   A 1 96  ? 29.556 -2.161  -2.087  0.34 16.09 ?  96  VAL   A HG23 1 
ATOM   2050 N  N    A GLY   A 1 97  ? 25.166 -4.340  -3.703  0.66 14.13 ?  97  GLY   A N    1 
ATOM   2051 N  N    B GLY   A 1 97  ? 25.118 -4.165  -3.624  0.34 14.26 ?  97  GLY   A N    1 
ATOM   2052 C  CA   A GLY   A 1 97  ? 24.360 -5.101  -4.624  0.66 14.51 ?  97  GLY   A CA   1 
ATOM   2053 C  CA   B GLY   A 1 97  ? 24.244 -4.916  -4.488  0.34 14.84 ?  97  GLY   A CA   1 
ATOM   2054 C  C    A GLY   A 1 97  ? 24.350 -4.414  -5.974  0.66 15.05 ?  97  GLY   A C    1 
ATOM   2055 C  C    B GLY   A 1 97  ? 24.282 -4.356  -5.895  0.34 15.32 ?  97  GLY   A C    1 
ATOM   2056 O  O    A GLY   A 1 97  ? 24.690 -3.231  -6.083  0.66 15.60 ?  97  GLY   A O    1 
ATOM   2057 O  O    B GLY   A 1 97  ? 24.479 -3.154  -6.098  0.34 15.60 ?  97  GLY   A O    1 
ATOM   2058 H  H    A GLY   A 1 97  ? 24.720 -3.792  -3.215  0.66 17.01 ?  97  GLY   A H    1 
ATOM   2059 H  H    B GLY   A 1 97  ? 24.710 -3.603  -3.111  0.34 17.16 ?  97  GLY   A H    1 
ATOM   2060 H  HA2  A GLY   A 1 97  ? 24.727 -5.993  -4.720  0.66 17.47 ?  97  GLY   A HA2  1 
ATOM   2061 H  HA2  B GLY   A 1 97  ? 24.526 -5.840  -4.500  0.34 17.87 ?  97  GLY   A HA2  1 
ATOM   2062 H  HA3  A GLY   A 1 97  ? 23.451 -5.166  -4.293  0.66 17.47 ?  97  GLY   A HA3  1 
ATOM   2063 H  HA3  B GLY   A 1 97  ? 23.332 -4.867  -4.161  0.34 17.87 ?  97  GLY   A HA3  1 
ATOM   2064 N  N    A PRO   A 1 98  ? 23.985 -5.134  -7.030  0.66 15.02 ?  98  PRO   A N    1 
ATOM   2065 N  N    B PRO   A 1 98  ? 24.105 -5.213  -6.897  0.34 15.17 ?  98  PRO   A N    1 
ATOM   2066 C  CA   A PRO   A 1 98  ? 23.864 -4.493  -8.345  0.66 15.66 ?  98  PRO   A CA   1 
ATOM   2067 C  CA   B PRO   A 1 98  ? 24.092 -4.725  -8.279  0.34 15.81 ?  98  PRO   A CA   1 
ATOM   2068 C  C    A PRO   A 1 98  ? 22.763 -3.435  -8.361  0.66 16.10 ?  98  PRO   A C    1 
ATOM   2069 C  C    B PRO   A 1 98  ? 22.965 -3.731  -8.504  0.34 16.18 ?  98  PRO   A C    1 
ATOM   2070 O  O    A PRO   A 1 98  ? 21.700 -3.604  -7.758  0.66 15.58 ?  98  PRO   A O    1 
ATOM   2071 O  O    B PRO   A 1 98  ? 21.837 -3.919  -8.045  0.34 16.36 ?  98  PRO   A O    1 
ATOM   2072 C  CB   A PRO   A 1 98  ? 23.546 -5.666  -9.284  0.66 15.99 ?  98  PRO   A CB   1 
ATOM   2073 C  CB   B PRO   A 1 98  ? 23.888 -6.000  -9.106  0.34 16.09 ?  98  PRO   A CB   1 
ATOM   2074 C  CG   A PRO   A 1 98  ? 22.950 -6.722  -8.396  0.66 15.88 ?  98  PRO   A CG   1 
ATOM   2075 C  CG   B PRO   A 1 98  ? 23.259 -6.966  -8.164  0.34 15.96 ?  98  PRO   A CG   1 
ATOM   2076 C  CD   A PRO   A 1 98  ? 23.667 -6.574  -7.076  0.66 15.32 ?  98  PRO   A CD   1 
ATOM   2077 C  CD   B PRO   A 1 98  ? 23.862 -6.662  -6.826  0.34 15.02 ?  98  PRO   A CD   1 
ATOM   2078 H  HA   A PRO   A 1 98  ? 24.708 -4.096  -8.606  0.66 18.85 ?  98  PRO   A HA   1 
ATOM   2079 H  HA   B PRO   A 1 98  ? 24.938 -4.309  -8.511  0.34 19.02 ?  98  PRO   A HA   1 
ATOM   2080 H  HB2  A PRO   A 1 98  ? 22.906 -5.389  -9.955  0.66 19.25 ?  98  PRO   A HB2  1 
ATOM   2081 H  HB2  B PRO   A 1 98  ? 23.300 -5.811  -9.856  0.34 19.37 ?  98  PRO   A HB2  1 
ATOM   2082 H  HB3  A PRO   A 1 98  ? 24.362 -5.992  -9.698  0.66 19.25 ?  98  PRO   A HB3  1 
ATOM   2083 H  HB3  B PRO   A 1 98  ? 24.746 -6.325  -9.416  0.34 19.37 ?  98  PRO   A HB3  1 
ATOM   2084 H  HG2  A PRO   A 1 98  ? 22.001 -6.568  -8.288  0.66 19.11 ?  98  PRO   A HG2  1 
ATOM   2085 H  HG2  B PRO   A 1 98  ? 22.298 -6.826  -8.148  0.34 19.20 ?  98  PRO   A HG2  1 
ATOM   2086 H  HG3  A PRO   A 1 98  ? 23.113 -7.604  -8.775  0.66 19.11 ?  98  PRO   A HG3  1 
ATOM   2087 H  HG3  B PRO   A 1 98  ? 23.470 -7.870  -8.440  0.34 19.20 ?  98  PRO   A HG3  1 
ATOM   2088 H  HD2  A PRO   A 1 98  ? 23.080 -6.823  -6.340  0.66 18.44 ?  98  PRO   A HD2  1 
ATOM   2089 H  HD2  B PRO   A 1 98  ? 23.237 -6.868  -6.116  0.34 18.08 ?  98  PRO   A HD2  1 
ATOM   2090 H  HD3  A PRO   A 1 98  ? 24.483 -7.106  -7.067  0.66 18.44 ?  98  PRO   A HD3  1 
ATOM   2091 H  HD3  B PRO   A 1 98  ? 24.702 -7.133  -6.714  0.34 18.08 ?  98  PRO   A HD3  1 
ATOM   2092 N  N    A ASN   A 1 99  ? 23.028 -2.332  -9.064  0.66 16.96 ?  99  ASN   A N    1 
ATOM   2093 N  N    B ASN   A 1 99  ? 23.282 -2.654  -9.210  0.34 16.37 ?  99  ASN   A N    1 
ATOM   2094 C  CA   A ASN   A 1 99  ? 22.059 -1.252  -9.259  0.66 18.07 ?  99  ASN   A CA   1 
ATOM   2095 C  CA   B ASN   A 1 99  ? 22.288 -1.654  -9.572  0.34 16.79 ?  99  ASN   A CA   1 
ATOM   2096 C  C    A ASN   A 1 99  ? 21.471 -1.386  -10.659 0.66 19.02 ?  99  ASN   A C    1 
ATOM   2097 C  C    B ASN   A 1 99  ? 21.759 -1.971  -10.965 0.34 17.02 ?  99  ASN   A C    1 
ATOM   2098 O  O    A ASN   A 1 99  ? 22.111 -1.021  -11.650 0.66 19.54 ?  99  ASN   A O    1 
ATOM   2099 O  O    B ASN   A 1 99  ? 22.487 -1.864  -11.956 0.34 15.95 ?  99  ASN   A O    1 
ATOM   2100 C  CB   A ASN   A 1 99  ? 22.719 0.109   -9.083  0.66 18.52 ?  99  ASN   A CB   1 
ATOM   2101 C  CB   B ASN   A 1 99  ? 22.879 -0.251  -9.535  0.34 17.54 ?  99  ASN   A CB   1 
ATOM   2102 C  CG   A ASN   A 1 99  ? 21.713 1.253   -9.048  0.66 18.94 ?  99  ASN   A CG   1 
ATOM   2103 C  CG   B ASN   A 1 99  ? 21.828 0.806   -9.740  0.34 18.03 ?  99  ASN   A CG   1 
ATOM   2104 O  OD1  A ASN   A 1 99  ? 20.685 1.218   -9.726  0.66 18.35 ?  99  ASN   A OD1  1 
ATOM   2105 O  OD1  B ASN   A 1 99  ? 21.188 0.842   -10.786 0.34 18.02 ?  99  ASN   A OD1  1 
ATOM   2106 N  ND2  A ASN   A 1 99  ? 22.015 2.277   -8.258  0.66 19.23 ?  99  ASN   A ND2  1 
ATOM   2107 N  ND2  B ASN   A 1 99  ? 21.627 1.666   -8.735  0.34 18.08 ?  99  ASN   A ND2  1 
ATOM   2108 H  H    A ASN   A 1 99  ? 23.789 -2.185  -9.433  0.66 20.40 ?  99  ASN   A H    1 
ATOM   2109 H  H    B ASN   A 1 99  ? 24.074 -2.461  -9.477  0.34 19.69 ?  99  ASN   A H    1 
ATOM   2110 H  HA   A ASN   A 1 99  ? 21.341 -1.348  -8.614  0.66 21.74 ?  99  ASN   A HA   1 
ATOM   2111 H  HA   B ASN   A 1 99  ? 21.546 -1.682  -8.946  0.34 20.20 ?  99  ASN   A HA   1 
ATOM   2112 H  HB2  A ASN   A 1 99  ? 23.216 0.107   -8.255  0.66 22.28 ?  99  ASN   A HB2  1 
ATOM   2113 H  HB2  B ASN   A 1 99  ? 23.297 -0.091  -8.678  0.34 21.10 ?  99  ASN   A HB2  1 
ATOM   2114 H  HB3  A ASN   A 1 99  ? 23.321 0.254   -9.834  0.66 22.28 ?  99  ASN   A HB3  1 
ATOM   2115 H  HB3  B ASN   A 1 99  ? 23.532 -0.154  -10.249 0.34 21.10 ?  99  ASN   A HB3  1 
ATOM   2116 H  HD21 A ASN   A 1 99  ? 21.485 2.948   -8.203  0.66 23.13 ?  99  ASN   A HD21 1 
ATOM   2117 H  HD21 B ASN   A 1 99  ? 21.037 2.295   -8.799  0.34 21.75 ?  99  ASN   A HD21 1 
ATOM   2118 H  HD22 A ASN   A 1 99  ? 22.748 2.266   -7.805  0.66 23.13 ?  99  ASN   A HD22 1 
ATOM   2119 H  HD22 B ASN   A 1 99  ? 22.091 1.596   -8.011  0.34 21.75 ?  99  ASN   A HD22 1 
ATOM   2120 N  N    A VAL   A 1 100 ? 20.231 -1.883  -10.728 0.66 20.00 ?  100 VAL   A N    1 
ATOM   2121 N  N    B VAL   A 1 100 ? 20.475 -2.322  -11.038 0.34 18.76 ?  100 VAL   A N    1 
ATOM   2122 C  CA   A VAL   A 1 100 ? 19.580 -2.143  -12.013 0.66 22.25 ?  100 VAL   A CA   1 
ATOM   2123 C  CA   B VAL   A 1 100 ? 19.877 -2.735  -12.301 0.34 20.30 ?  100 VAL   A CA   1 
ATOM   2124 C  C    A VAL   A 1 100 ? 19.452 -0.864  -12.827 0.66 23.76 ?  100 VAL   A C    1 
ATOM   2125 C  C    B VAL   A 1 100 ? 19.814 -1.582  -13.294 0.34 20.38 ?  100 VAL   A C    1 
ATOM   2126 O  O    A VAL   A 1 100 ? 19.537 -0.887  -14.061 0.66 24.79 ?  100 VAL   A O    1 
ATOM   2127 O  O    B VAL   A 1 100 ? 19.819 -1.806  -14.511 0.34 20.31 ?  100 VAL   A O    1 
ATOM   2128 C  CB   A VAL   A 1 100 ? 18.221 -2.848  -11.793 0.66 23.54 ?  100 VAL   A CB   1 
ATOM   2129 C  CB   B VAL   A 1 100 ? 18.485 -3.333  -12.039 0.34 21.48 ?  100 VAL   A CB   1 
ATOM   2130 C  CG1  A VAL   A 1 100 ? 17.449 -2.990  -13.105 0.66 24.05 ?  100 VAL   A CG1  1 
ATOM   2131 C  CG1  B VAL   A 1 100 ? 17.850 -3.796  -13.339 0.34 21.66 ?  100 VAL   A CG1  1 
ATOM   2132 C  CG2  A VAL   A 1 100 ? 18.439 -4.217  -11.167 0.66 24.01 ?  100 VAL   A CG2  1 
ATOM   2133 C  CG2  B VAL   A 1 100 ? 18.593 -4.471  -11.045 0.34 21.88 ?  100 VAL   A CG2  1 
ATOM   2134 H  H    A VAL   A 1 100 ? 19.734 -2.079  -10.046 0.66 24.05 ?  100 VAL   A H    1 
ATOM   2135 H  H    B VAL   A 1 100 ? 19.933 -2.324  -10.372 0.34 22.57 ?  100 VAL   A H    1 
ATOM   2136 H  HA   A VAL   A 1 100 ? 20.127 -2.759  -12.523 0.66 26.76 ?  100 VAL   A HA   1 
ATOM   2137 H  HA   B VAL   A 1 100 ? 20.429 -3.424  -12.693 0.34 24.42 ?  100 VAL   A HA   1 
ATOM   2138 H  HB   A VAL   A 1 100 ? 17.675 -2.328  -11.184 0.66 28.30 ?  100 VAL   A HB   1 
ATOM   2139 H  HB   B VAL   A 1 100 ? 17.916 -2.645  -11.657 0.34 25.84 ?  100 VAL   A HB   1 
ATOM   2140 H  HG11 A VAL   A 1 100 ? 16.711 -3.613  -12.976 0.66 28.92 ?  100 VAL   A HG11 1 
ATOM   2141 H  HG11 B VAL   A 1 100 ? 17.053 -4.304  -13.130 0.34 26.04 ?  100 VAL   A HG11 1 
ATOM   2142 H  HG12 A VAL   A 1 100 ? 17.100 -2.124  -13.365 0.66 28.92 ?  100 VAL   A HG12 1 
ATOM   2143 H  HG12 B VAL   A 1 100 ? 17.617 -3.021  -13.875 0.34 26.04 ?  100 VAL   A HG12 1 
ATOM   2144 H  HG13 A VAL   A 1 100 ? 18.045 -3.331  -13.789 0.66 28.92 ?  100 VAL   A HG13 1 
ATOM   2145 H  HG13 B VAL   A 1 100 ? 18.484 -4.352  -13.817 0.34 26.04 ?  100 VAL   A HG13 1 
ATOM   2146 H  HG21 A VAL   A 1 100 ? 17.581 -4.664  -11.063 0.66 28.87 ?  100 VAL   A HG21 1 
ATOM   2147 H  HG21 B VAL   A 1 100 ? 17.741 -4.929  -11.000 0.34 26.31 ?  100 VAL   A HG21 1 
ATOM   2148 H  HG22 A VAL   A 1 100 ? 19.011 -4.744  -11.749 0.66 28.87 ?  100 VAL   A HG22 1 
ATOM   2149 H  HG22 B VAL   A 1 100 ? 19.284 -5.082  -11.343 0.34 26.31 ?  100 VAL   A HG22 1 
ATOM   2150 H  HG23 A VAL   A 1 100 ? 18.859 -4.106  -10.302 0.66 28.87 ?  100 VAL   A HG23 1 
ATOM   2151 H  HG23 B VAL   A 1 100 ? 18.823 -4.110  -10.174 0.34 26.31 ?  100 VAL   A HG23 1 
ATOM   2152 N  N    A ASN   A 1 101 ? 19.254 0.268   -12.163 0.66 24.48 ?  101 ASN   A N    1 
ATOM   2153 N  N    B ASN   A 1 101 ? 19.728 -0.341  -12.808 0.34 21.16 ?  101 ASN   A N    1 
ATOM   2154 C  CA   A ASN   A 1 101 ? 19.212 1.538   -12.873 0.66 25.74 ?  101 ASN   A CA   1 
ATOM   2155 C  CA   B ASN   A 1 101 ? 19.663 0.811   -13.704 0.34 22.27 ?  101 ASN   A CA   1 
ATOM   2156 C  C    A ASN   A 1 101 ? 20.583 1.965   -13.396 0.66 28.38 ?  101 ASN   A C    1 
ATOM   2157 C  C    B ASN   A 1 101 ? 20.990 1.092   -14.399 0.34 24.00 ?  101 ASN   A C    1 
ATOM   2158 O  O    A ASN   A 1 101 ? 20.691 3.059   -13.963 0.66 29.47 ?  101 ASN   A O    1 
ATOM   2159 O  O    B ASN   A 1 101 ? 20.994 1.753   -15.443 0.34 23.95 ?  101 ASN   A O    1 
ATOM   2160 C  CB   A ASN   A 1 101 ? 18.599 2.604   -11.968 0.66 24.38 ?  101 ASN   A CB   1 
ATOM   2161 C  CB   B ASN   A 1 101 ? 19.196 2.053   -12.937 0.34 22.33 ?  101 ASN   A CB   1 
ATOM   2162 C  CG   A ASN   A 1 101 ? 17.251 2.177   -11.399 0.66 23.51 ?  101 ASN   A CG   1 
ATOM   2163 C  CG   B ASN   A 1 101 ? 17.982 1.777   -12.071 0.34 22.92 ?  101 ASN   A CG   1 
ATOM   2164 O  OD1  A ASN   A 1 101 ? 16.387 1.668   -12.116 0.66 23.47 ?  101 ASN   A OD1  1 
ATOM   2165 O  OD1  B ASN   A 1 101 ? 17.042 1.104   -12.497 0.34 23.99 ?  101 ASN   A OD1  1 
ATOM   2166 N  ND2  A ASN   A 1 101 ? 17.074 2.363   -10.100 0.66 23.66 ?  101 ASN   A ND2  1 
ATOM   2167 N  ND2  B ASN   A 1 101 ? 18.001 2.284   -10.844 0.34 22.73 ?  101 ASN   A ND2  1 
ATOM   2168 H  H    A ASN   A 1 101 ? 19.138 0.325   -11.319 0.66 29.44 ?  101 ASN   A H    1 
ATOM   2169 H  H    B ASN   A 1 101 ? 19.692 -0.138  -11.973 0.34 25.45 ?  101 ASN   A H    1 
ATOM   2170 H  HA   A ASN   A 1 101 ? 18.627 1.440   -13.641 0.66 30.94 ?  101 ASN   A HA   1 
ATOM   2171 H  HA   B ASN   A 1 101 ? 19.009 0.635   -14.396 0.34 26.78 ?  101 ASN   A HA   1 
ATOM   2172 H  HB2  A ASN   A 1 101 ? 19.201 2.774   -11.228 0.66 29.31 ?  101 ASN   A HB2  1 
ATOM   2173 H  HB2  B ASN   A 1 101 ? 19.910 2.363   -12.361 0.34 26.85 ?  101 ASN   A HB2  1 
ATOM   2174 H  HB3  A ASN   A 1 101 ? 18.468 3.417   -12.484 0.66 29.31 ?  101 ASN   A HB3  1 
ATOM   2175 H  HB3  B ASN   A 1 101 ? 18.956 2.750   -13.573 0.34 26.85 ?  101 ASN   A HB3  1 
ATOM   2176 H  HD21 A ASN   A 1 101 ? 16.332 2.137   -9.736  0.66 28.45 ?  101 ASN   A HD21 1 
ATOM   2177 H  HD21 B ASN   A 1 101 ? 17.338 2.153   -10.312 0.34 27.33 ?  101 ASN   A HD21 1 
ATOM   2178 H  HD22 A ASN   A 1 101 ? 17.698 2.717   -9.629  0.66 28.45 ?  101 ASN   A HD22 1 
ATOM   2179 H  HD22 B ASN   A 1 101 ? 18.679 2.744   -10.580 0.34 27.33 ?  101 ASN   A HD22 1 
ATOM   2180 N  N    A LYS   A 1 102 ? 21.615 1.132   -13.220 0.66 30.24 ?  102 LYS   A N    1 
ATOM   2181 N  N    B LYS   A 1 102 ? 22.109 0.612   -13.853 0.34 25.73 ?  102 LYS   A N    1 
ATOM   2182 C  CA   A LYS   A 1 102 ? 22.916 1.318   -13.854 0.66 31.88 ?  102 LYS   A CA   1 
ATOM   2183 C  CA   B LYS   A 1 102 ? 23.428 0.823   -14.439 0.34 27.49 ?  102 LYS   A CA   1 
ATOM   2184 C  C    A LYS   A 1 102 ? 23.250 0.220   -14.856 0.66 32.36 ?  102 LYS   A C    1 
ATOM   2185 C  C    B LYS   A 1 102 ? 23.892 -0.367  -15.278 0.34 27.56 ?  102 LYS   A C    1 
ATOM   2186 O  O    A LYS   A 1 102 ? 24.346 0.240   -15.427 0.66 32.70 ?  102 LYS   A O    1 
ATOM   2187 O  O    B LYS   A 1 102 ? 25.089 -0.496  -15.554 0.34 27.56 ?  102 LYS   A O    1 
ATOM   2188 C  CB   A LYS   A 1 102 ? 24.030 1.370   -12.799 0.66 32.96 ?  102 LYS   A CB   1 
ATOM   2189 C  CB   B LYS   A 1 102 ? 24.464 1.134   -13.355 0.34 29.25 ?  102 LYS   A CB   1 
ATOM   2190 C  CG   A LYS   A 1 102 ? 23.918 2.509   -11.806 0.66 34.04 ?  102 LYS   A CG   1 
ATOM   2191 C  CG   B LYS   A 1 102 ? 24.391 2.540   -12.777 0.34 30.79 ?  102 LYS   A CG   1 
ATOM   2192 C  CD   A LYS   A 1 102 ? 25.078 2.476   -10.818 0.66 35.16 ?  102 LYS   A CD   1 
ATOM   2193 C  CD   B LYS   A 1 102 ? 25.573 2.813   -11.852 0.34 32.16 ?  102 LYS   A CD   1 
ATOM   2194 C  CE   A LYS   A 1 102 ? 25.020 3.646   -9.850  0.66 35.79 ?  102 LYS   A CE   1 
ATOM   2195 C  CE   B LYS   A 1 102 ? 25.528 4.223   -11.281 0.34 33.23 ?  102 LYS   A CE   1 
ATOM   2196 N  NZ   A LYS   A 1 102 ? 26.110 3.583   -8.835  0.66 36.34 ?  102 LYS   A NZ   1 
ATOM   2197 N  NZ   B LYS   A 1 102 ? 26.639 4.476   -10.317 0.34 33.80 ?  102 LYS   A NZ   1 
ATOM   2198 H  H    A LYS   A 1 102 ? 21.585 0.435   -12.716 0.66 36.34 ?  102 LYS   A H    1 
ATOM   2199 H  H    B LYS   A 1 102 ? 22.126 0.146   -13.131 0.34 30.94 ?  102 LYS   A H    1 
ATOM   2200 H  HA   A LYS   A 1 102 ? 22.915 2.157   -14.333 0.66 38.31 ?  102 LYS   A HA   1 
ATOM   2201 H  HA   B LYS   A 1 102 ? 23.383 1.604   -15.014 0.34 33.04 ?  102 LYS   A HA   1 
ATOM   2202 H  HB2  A LYS   A 1 102 ? 24.022 0.541   -12.297 0.66 39.61 ?  102 LYS   A HB2  1 
ATOM   2203 H  HB2  B LYS   A 1 102 ? 24.340 0.514   -12.623 0.34 35.15 ?  102 LYS   A HB2  1 
ATOM   2204 H  HB3  A LYS   A 1 102 ? 24.882 1.463   -13.256 0.66 39.61 ?  102 LYS   A HB3  1 
ATOM   2205 H  HB3  B LYS   A 1 102 ? 25.352 1.025   -13.731 0.34 35.15 ?  102 LYS   A HB3  1 
ATOM   2206 H  HG2  A LYS   A 1 102 ? 23.943 3.355   -12.280 0.66 40.90 ?  102 LYS   A HG2  1 
ATOM   2207 H  HG2  B LYS   A 1 102 ? 24.413 3.190   -13.497 0.34 37.00 ?  102 LYS   A HG2  1 
ATOM   2208 H  HG3  A LYS   A 1 102 ? 23.089 2.423   -11.309 0.66 40.90 ?  102 LYS   A HG3  1 
ATOM   2209 H  HG3  B LYS   A 1 102 ? 23.575 2.636   -12.261 0.34 37.00 ?  102 LYS   A HG3  1 
ATOM   2210 H  HD2  A LYS   A 1 102 ? 25.039 1.653   -10.305 0.66 42.25 ?  102 LYS   A HD2  1 
ATOM   2211 H  HD2  B LYS   A 1 102 ? 25.554 2.186   -11.112 0.34 38.64 ?  102 LYS   A HD2  1 
ATOM   2212 H  HD3  A LYS   A 1 102 ? 25.915 2.525   -11.307 0.66 42.25 ?  102 LYS   A HD3  1 
ATOM   2213 H  HD3  B LYS   A 1 102 ? 26.400 2.716   -12.351 0.34 38.64 ?  102 LYS   A HD3  1 
ATOM   2214 H  HE2  A LYS   A 1 102 ? 25.115 4.474   -10.348 0.66 43.01 ?  102 LYS   A HE2  1 
ATOM   2215 H  HE2  B LYS   A 1 102 ? 25.608 4.864   -12.005 0.34 39.93 ?  102 LYS   A HE2  1 
ATOM   2216 H  HE3  A LYS   A 1 102 ? 24.169 3.632   -9.385  0.66 43.01 ?  102 LYS   A HE3  1 
ATOM   2217 H  HE3  B LYS   A 1 102 ? 24.689 4.351   -10.813 0.34 39.93 ?  102 LYS   A HE3  1 
ATOM   2218 H  HZ1  A LYS   A 1 102 ? 26.052 4.279   -8.283  0.66 43.66 ?  102 LYS   A HZ1  1 
ATOM   2219 H  HZ1  B LYS   A 1 102 ? 26.585 5.306   -10.001 0.34 40.61 ?  102 LYS   A HZ1  1 
ATOM   2220 H  HZ2  A LYS   A 1 102 ? 26.041 2.832   -8.362  0.66 43.66 ?  102 LYS   A HZ2  1 
ATOM   2221 H  HZ2  B LYS   A 1 102 ? 26.587 3.904   -9.636  0.34 40.61 ?  102 LYS   A HZ2  1 
ATOM   2222 H  HZ3  A LYS   A 1 102 ? 26.903 3.599   -9.239  0.66 43.66 ?  102 LYS   A HZ3  1 
ATOM   2223 H  HZ3  B LYS   A 1 102 ? 27.424 4.371   -10.722 0.34 40.61 ?  102 LYS   A HZ3  1 
ATOM   2224 N  N    A GLY   A 1 103 ? 22.352 -0.738  -15.080 0.66 32.75 ?  103 GLY   A N    1 
ATOM   2225 N  N    B GLY   A 1 103 ? 22.974 -1.243  -15.680 0.34 27.77 ?  103 GLY   A N    1 
ATOM   2226 C  CA   A GLY   A 1 103 ? 22.630 -1.831  -15.991 0.66 32.96 ?  103 GLY   A CA   1 
ATOM   2227 C  CA   B GLY   A 1 103 ? 23.330 -2.386  -16.498 0.34 27.97 ?  103 GLY   A CA   1 
ATOM   2228 C  C    A GLY   A 1 103 ? 23.434 -2.969  -15.404 0.66 32.72 ?  103 GLY   A C    1 
ATOM   2229 C  C    B GLY   A 1 103 ? 24.014 -3.515  -15.763 0.34 28.24 ?  103 GLY   A C    1 
ATOM   2230 O  O    A GLY   A 1 103 ? 23.935 -3.806  -16.163 0.66 33.59 ?  103 GLY   A O    1 
ATOM   2231 O  O    B GLY   A 1 103 ? 24.541 -4.427  -16.411 0.34 28.77 ?  103 GLY   A O    1 
ATOM   2232 H  H    A GLY   A 1 103 ? 21.573 -0.775  -14.716 0.66 39.35 ?  103 GLY   A H    1 
ATOM   2233 H  H    B GLY   A 1 103 ? 22.139 -1.187  -15.489 0.34 33.38 ?  103 GLY   A H    1 
ATOM   2234 H  HA2  A GLY   A 1 103 ? 21.793 -2.193  -16.324 0.66 39.61 ?  103 GLY   A HA2  1 
ATOM   2235 H  HA2  B GLY   A 1 103 ? 22.529 -2.738  -16.918 0.34 33.62 ?  103 GLY   A HA2  1 
ATOM   2236 H  HA3  A GLY   A 1 103 ? 23.126 -1.483  -16.751 0.66 39.61 ?  103 GLY   A HA3  1 
ATOM   2237 H  HA3  B GLY   A 1 103 ? 23.932 -2.082  -17.198 0.34 33.62 ?  103 GLY   A HA3  1 
ATOM   2238 N  N    A GLU   A 1 104 ? 23.564 -3.040  -14.083 0.66 31.05 ?  104 GLU   A N    1 
ATOM   2239 N  N    B GLU   A 1 104 ? 24.017 -3.490  -14.435 0.34 27.83 ?  104 GLU   A N    1 
ATOM   2240 C  CA   A GLU   A 1 104 ? 24.439 -4.019  -13.456 0.66 29.20 ?  104 GLU   A CA   1 
ATOM   2241 C  CA   B GLU   A 1 104 ? 24.755 -4.480  -13.665 0.34 27.50 ?  104 GLU   A CA   1 
ATOM   2242 C  C    A GLU   A 1 104 ? 23.759 -5.379  -13.323 0.66 29.31 ?  104 GLU   A C    1 
ATOM   2243 C  C    B GLU   A 1 104 ? 24.131 -5.865  -13.794 0.34 27.45 ?  104 GLU   A C    1 
ATOM   2244 O  O    A GLU   A 1 104 ? 22.550 -5.483  -13.090 0.66 28.53 ?  104 GLU   A O    1 
ATOM   2245 O  O    B GLU   A 1 104 ? 22.911 -6.019  -13.905 0.34 27.23 ?  104 GLU   A O    1 
ATOM   2246 C  CB   A GLU   A 1 104 ? 24.928 -3.503  -12.101 0.66 27.07 ?  104 GLU   A CB   1 
ATOM   2247 C  CB   B GLU   A 1 104 ? 24.761 -4.098  -12.190 0.34 27.56 ?  104 GLU   A CB   1 
ATOM   2248 C  CG   A GLU   A 1 104 ? 25.894 -2.328  -12.257 0.66 25.92 ?  104 GLU   A CG   1 
ATOM   2249 C  CG   B GLU   A 1 104 ? 26.089 -3.583  -11.685 0.34 27.73 ?  104 GLU   A CG   1 
ATOM   2250 C  CD   A GLU   A 1 104 ? 26.235 -1.593  -10.971 0.66 24.49 ?  104 GLU   A CD   1 
ATOM   2251 C  CD   B GLU   A 1 104 ? 25.983 -2.214  -11.039 0.34 27.57 ?  104 GLU   A CD   1 
ATOM   2252 O  OE1  A GLU   A 1 104 ? 25.628 -1.869  -9.917  0.66 23.68 ?  104 GLU   A OE1  1 
ATOM   2253 O  OE1  B GLU   A 1 104 ? 25.828 -1.217  -11.775 0.34 27.69 ?  104 GLU   A OE1  1 
ATOM   2254 O  OE2  A GLU   A 1 104 ? 27.127 -0.714  -11.033 0.66 25.04 -1 104 GLU   A OE2  1 
ATOM   2255 O  OE2  B GLU   A 1 104 ? 26.045 -2.136  -9.795  0.34 27.44 -1 104 GLU   A OE2  1 
ATOM   2256 H  H    A GLU   A 1 104 ? 23.155 -2.525  -13.530 0.66 37.32 ?  104 GLU   A H    1 
ATOM   2257 H  H    B GLU   A 1 104 ? 23.604 -2.900  -13.965 0.34 33.46 ?  104 GLU   A H    1 
ATOM   2258 H  HA   A GLU   A 1 104 ? 25.215 -4.137  -14.022 0.66 35.09 ?  104 GLU   A HA   1 
ATOM   2259 H  HA   B GLU   A 1 104 ? 25.671 -4.514  -13.990 0.34 33.06 ?  104 GLU   A HA   1 
ATOM   2260 H  HB2  A GLU   A 1 104 ? 24.162 -3.210  -11.585 0.66 32.54 ?  104 GLU   A HB2  1 
ATOM   2261 H  HB2  B GLU   A 1 104 ? 24.099 -3.411  -12.042 0.34 33.12 ?  104 GLU   A HB2  1 
ATOM   2262 H  HB3  A GLU   A 1 104 ? 25.388 -4.222  -11.644 0.66 32.54 ?  104 GLU   A HB3  1 
ATOM   2263 H  HB3  B GLU   A 1 104 ? 24.526 -4.889  -11.677 0.34 33.12 ?  104 GLU   A HB3  1 
ATOM   2264 H  HG2  A GLU   A 1 104 ? 26.724 -2.660  -12.619 0.66 31.16 ?  104 GLU   A HG2  1 
ATOM   2265 H  HG2  B GLU   A 1 104 ? 26.430 -4.215  -11.037 0.34 33.33 ?  104 GLU   A HG2  1 
ATOM   2266 H  HG3  A GLU   A 1 104 ? 25.497 -1.685  -12.864 0.66 31.16 ?  104 GLU   A HG3  1 
ATOM   2267 H  HG3  B GLU   A 1 104 ? 26.704 -3.505  -12.428 0.34 33.33 ?  104 GLU   A HG3  1 
ATOM   2268 N  N    A ASP   A 1 105 ? 24.564 -6.428  -13.467 0.66 30.39 ?  105 ASP   A N    1 
ATOM   2269 N  N    B ASP   A 1 105 ? 24.991 -6.880  -13.752 0.34 27.90 ?  105 ASP   A N    1 
ATOM   2270 C  CA   A ASP   A 1 105 ? 24.061 -7.789  -13.602 0.66 31.46 ?  105 ASP   A CA   1 
ATOM   2271 C  CA   B ASP   A 1 105 ? 24.537 -8.264  -13.785 0.34 28.45 ?  105 ASP   A CA   1 
ATOM   2272 C  C    A ASP   A 1 105 ? 23.404 -8.245  -12.303 0.66 29.27 ?  105 ASP   A C    1 
ATOM   2273 C  C    B ASP   A 1 105 ? 23.652 -8.557  -12.580 0.34 27.94 ?  105 ASP   A C    1 
ATOM   2274 O  O    A ASP   A 1 105 ? 24.070 -8.373  -11.270 0.66 27.62 ?  105 ASP   A O    1 
ATOM   2275 O  O    B ASP   A 1 105 ? 24.028 -8.285  -11.436 0.34 27.96 ?  105 ASP   A O    1 
ATOM   2276 C  CB   A ASP   A 1 105 ? 25.224 -8.708  -13.969 0.66 34.35 ?  105 ASP   A CB   1 
ATOM   2277 C  CB   B ASP   A 1 105 ? 25.756 -9.182  -13.749 0.34 29.32 ?  105 ASP   A CB   1 
ATOM   2278 C  CG   A ASP   A 1 105 ? 24.784 -10.130 -14.226 0.66 36.66 ?  105 ASP   A CG   1 
ATOM   2279 C  CG   B ASP   A 1 105 ? 25.420 -10.611 -14.095 0.34 29.84 ?  105 ASP   A CG   1 
ATOM   2280 O  OD1  A ASP   A 1 105 ? 23.561 -10.362 -14.314 0.66 37.19 ?  105 ASP   A OD1  1 
ATOM   2281 O  OD1  B ASP   A 1 105 ? 24.243 -10.885 -14.407 0.34 29.96 ?  105 ASP   A OD1  1 
ATOM   2282 O  OD2  A ASP   A 1 105 ? 25.661 -11.013 -14.341 0.66 37.82 -1 105 ASP   A OD2  1 
ATOM   2283 O  OD2  B ASP   A 1 105 ? 26.337 -11.459 -14.054 0.34 30.16 -1 105 ASP   A OD2  1 
ATOM   2284 H  H    A ASP   A 1 105 ? 25.421 -6.377  -13.483 0.66 36.52 ?  105 ASP   A H    1 
ATOM   2285 H  H    B ASP   A 1 105 ? 25.848 -6.787  -13.708 0.34 33.54 ?  105 ASP   A H    1 
ATOM   2286 H  HA   A ASP   A 1 105 ? 23.403 -7.832  -14.316 0.66 37.80 ?  105 ASP   A HA   1 
ATOM   2287 H  HA   B ASP   A 1 105 ? 24.036 -8.429  -14.604 0.34 34.20 ?  105 ASP   A HA   1 
ATOM   2288 H  HB2  A ASP   A 1 105 ? 25.651 -8.373  -14.777 0.66 41.28 ?  105 ASP   A HB2  1 
ATOM   2289 H  HB2  B ASP   A 1 105 ? 26.416 -8.861  -14.379 0.34 35.25 ?  105 ASP   A HB2  1 
ATOM   2290 H  HB3  A ASP   A 1 105 ? 25.865 -8.714  -13.240 0.66 41.28 ?  105 ASP   A HB3  1 
ATOM   2291 H  HB3  B ASP   A 1 105 ? 26.121 -9.171  -12.851 0.34 35.25 ?  105 ASP   A HB3  1 
ATOM   2292 N  N    A ILE   A 1 106 ? 22.093 -8.497  -12.357 0.66 28.62 ?  106 ILE   A N    1 
ATOM   2293 N  N    B ILE   A 1 106 ? 22.469 -9.120  -12.837 0.34 27.61 ?  106 ILE   A N    1 
ATOM   2294 C  CA   A ILE   A 1 106 ? 21.362 -8.941  -11.176 0.66 27.01 ?  106 ILE   A CA   1 
ATOM   2295 C  CA   B ILE   A 1 106 ? 21.539 -9.405  -11.748 0.34 27.15 ?  106 ILE   A CA   1 
ATOM   2296 C  C    A ILE   A 1 106 ? 21.898 -10.255 -10.638 0.66 26.30 ?  106 ILE   A C    1 
ATOM   2297 C  C    B ILE   A 1 106 ? 21.981 -10.616 -10.929 0.34 26.66 ?  106 ILE   A C    1 
ATOM   2298 O  O    A ILE   A 1 106 ? 21.716 -10.549 -9.451  0.66 25.66 ?  106 ILE   A O    1 
ATOM   2299 O  O    B ILE   A 1 106 ? 21.638 -10.728 -9.746  0.34 26.75 ?  106 ILE   A O    1 
ATOM   2300 C  CB   A ILE   A 1 106 ? 19.846 -9.021  -11.461 0.66 27.45 ?  106 ILE   A CB   1 
ATOM   2301 C  CB   B ILE   A 1 106 ? 20.095 -9.522  -12.277 0.34 26.82 ?  106 ILE   A CB   1 
ATOM   2302 C  CG1  A ILE   A 1 106 ? 19.050 -9.065  -10.155 0.66 27.60 ?  106 ILE   A CG1  1 
ATOM   2303 C  CG1  B ILE   A 1 106 ? 19.094 -9.573  -11.119 0.34 26.68 ?  106 ILE   A CG1  1 
ATOM   2304 C  CG2  A ILE   A 1 106 ? 19.517 -10.251 -12.286 0.66 27.61 ?  106 ILE   A CG2  1 
ATOM   2305 C  CG2  B ILE   A 1 106 ? 19.933 -10.732 -13.186 0.34 26.81 ?  106 ILE   A CG2  1 
ATOM   2306 C  CD1  A ILE   A 1 106 ? 19.231 -7.844  -9.284  0.66 27.83 ?  106 ILE   A CD1  1 
ATOM   2307 C  CD1  B ILE   A 1 106 ? 18.990 -8.272  -10.349 0.34 26.60 ?  106 ILE   A CD1  1 
ATOM   2308 H  H    A ILE   A 1 106 ? 21.611 -8.407  -13.058 0.66 34.40 ?  106 ILE   A H    1 
ATOM   2309 H  H    B ILE   A 1 106 ? 22.183 -9.319  -13.621 0.34 33.19 ?  106 ILE   A H    1 
ATOM   2310 H  HA   A ILE   A 1 106 ? 21.499 -8.290  -10.480 0.66 32.46 ?  106 ILE   A HA   1 
ATOM   2311 H  HA   B ILE   A 1 106 ? 21.556 -8.656  -11.145 0.34 32.64 ?  106 ILE   A HA   1 
ATOM   2312 H  HB   A ILE   A 1 106 ? 19.584 -8.234  -11.961 0.66 32.99 ?  106 ILE   A HB   1 
ATOM   2313 H  HB   B ILE   A 1 106 ? 19.908 -8.728  -12.797 0.34 32.24 ?  106 ILE   A HB   1 
ATOM   2314 H  HG12 A ILE   A 1 106 ? 18.107 -9.138  -10.369 0.66 33.18 ?  106 ILE   A HG12 1 
ATOM   2315 H  HG12 B ILE   A 1 106 ? 18.216 -9.773  -11.478 0.34 32.07 ?  106 ILE   A HG12 1 
ATOM   2316 H  HG13 A ILE   A 1 106 ? 19.332 -9.839  -9.643  0.66 33.18 ?  106 ILE   A HG13 1 
ATOM   2317 H  HG13 B ILE   A 1 106 ? 19.359 -10.267 -10.497 0.34 32.07 ?  106 ILE   A HG13 1 
ATOM   2318 H  HG21 A ILE   A 1 106 ? 18.639 -10.138 -12.677 0.66 33.19 ?  106 ILE   A HG21 1 
ATOM   2319 H  HG21 B ILE   A 1 106 ? 19.029 -10.734 -13.544 0.34 32.23 ?  106 ILE   A HG21 1 
ATOM   2320 H  HG22 A ILE   A 1 106 ? 20.184 -10.347 -12.982 0.66 33.19 ?  106 ILE   A HG22 1 
ATOM   2321 H  HG22 B ILE   A 1 106 ? 20.573 -10.670 -13.911 0.34 32.23 ?  106 ILE   A HG22 1 
ATOM   2322 H  HG23 A ILE   A 1 106 ? 19.526 -11.029 -11.707 0.66 33.19 ?  106 ILE   A HG23 1 
ATOM   2323 H  HG23 B ILE   A 1 106 ? 20.086 -11.540 -12.674 0.34 32.23 ?  106 ILE   A HG23 1 
ATOM   2324 H  HD11 A ILE   A 1 106 ? 18.502 -7.801  -8.649  0.66 33.45 ?  106 ILE   A HD11 1 
ATOM   2325 H  HD11 B ILE   A 1 106 ? 18.230 -8.324  -9.749  0.34 31.97 ?  106 ILE   A HD11 1 
ATOM   2326 H  HD12 A ILE   A 1 106 ? 20.077 -7.913  -8.813  0.66 33.45 ?  106 ILE   A HD12 1 
ATOM   2327 H  HD12 B ILE   A 1 106 ? 19.805 -8.139  -9.841  0.34 31.97 ?  106 ILE   A HD12 1 
ATOM   2328 H  HD13 A ILE   A 1 106 ? 19.228 -7.053  -9.846  0.66 33.45 ?  106 ILE   A HD13 1 
ATOM   2329 H  HD13 B ILE   A 1 106 ? 18.866 -7.544  -10.978 0.34 31.97 ?  106 ILE   A HD13 1 
ATOM   2330 N  N    A GLN   A 1 107 ? 22.571 -11.051 -11.480 0.66 27.14 ?  107 GLN   A N    1 
ATOM   2331 N  N    B GLN   A 1 107 ? 22.754 -11.530 -11.524 0.34 26.61 ?  107 GLN   A N    1 
ATOM   2332 C  CA   A GLN   A 1 107 ? 23.214 -12.272 -11.009 0.66 28.68 ?  107 GLN   A CA   1 
ATOM   2333 C  CA   B GLN   A 1 107 ? 23.277 -12.665 -10.769 0.34 27.08 ?  107 GLN   A CA   1 
ATOM   2334 C  C    A GLN   A 1 107 ? 24.203 -11.992 -9.888  0.66 25.87 ?  107 GLN   A C    1 
ATOM   2335 C  C    B GLN   A 1 107 ? 24.206 -12.214 -9.648  0.34 24.84 ?  107 GLN   A C    1 
ATOM   2336 O  O    A GLN   A 1 107 ? 24.477 -12.882 -9.079  0.66 27.38 ?  107 GLN   A O    1 
ATOM   2337 O  O    B GLN   A 1 107 ? 24.385 -12.948 -8.669  0.34 24.96 ?  107 GLN   A O    1 
ATOM   2338 C  CB   A GLN   A 1 107 ? 23.915 -12.982 -12.176 0.66 32.36 ?  107 GLN   A CB   1 
ATOM   2339 C  CB   B GLN   A 1 107 ? 24.005 -13.640 -11.705 0.34 30.12 ?  107 GLN   A CB   1 
ATOM   2340 C  CG   A GLN   A 1 107 ? 22.994 -13.287 -13.353 0.66 36.09 ?  107 GLN   A CG   1 
ATOM   2341 C  CG   B GLN   A 1 107 ? 23.443 -13.712 -13.124 0.34 32.93 ?  107 GLN   A CG   1 
ATOM   2342 C  CD   A GLN   A 1 107 ? 21.772 -14.085 -12.945 0.66 39.20 ?  107 GLN   A CD   1 
ATOM   2343 C  CD   B GLN   A 1 107 ? 22.005 -14.195 -13.177 0.34 35.22 ?  107 GLN   A CD   1 
ATOM   2344 O  OE1  A GLN   A 1 107 ? 21.883 -15.120 -12.287 0.66 40.61 ?  107 GLN   A OE1  1 
ATOM   2345 O  OE1  B GLN   A 1 107 ? 21.608 -15.085 -12.425 0.34 36.28 ?  107 GLN   A OE1  1 
ATOM   2346 N  NE2  A GLN   A 1 107 ? 20.595 -13.600 -13.325 0.66 40.36 ?  107 GLN   A NE2  1 
ATOM   2347 N  NE2  B GLN   A 1 107 ? 21.218 -13.610 -14.074 0.34 36.01 ?  107 GLN   A NE2  1 
ATOM   2348 H  H    A GLN   A 1 107 ? 22.678 -10.903 -12.322 0.66 32.63 ?  107 GLN   A H    1 
ATOM   2349 H  H    B GLN   A 1 107 ? 22.989 -11.510 -12.346 0.34 31.99 ?  107 GLN   A H    1 
ATOM   2350 H  HA   A GLN   A 1 107 ? 22.545 -12.876 -10.662 0.66 34.47 ?  107 GLN   A HA   1 
ATOM   2351 H  HA   B GLN   A 1 107 ? 22.544 -13.149 -10.362 0.34 32.55 ?  107 GLN   A HA   1 
ATOM   2352 H  HB2  A GLN   A 1 107 ? 24.635 -12.423 -12.507 0.66 38.89 ?  107 GLN   A HB2  1 
ATOM   2353 H  HB2  B GLN   A 1 107 ? 24.936 -13.379 -11.774 0.34 36.19 ?  107 GLN   A HB2  1 
ATOM   2354 H  HB3  A GLN   A 1 107 ? 24.277 -13.830 -11.866 0.66 38.89 ?  107 GLN   A HB3  1 
ATOM   2355 H  HB3  B GLN   A 1 107 ? 23.947 -14.538 -11.335 0.34 36.19 ?  107 GLN   A HB3  1 
ATOM   2356 H  HG2  A GLN   A 1 107 ? 22.689 -12.454 -13.743 0.66 43.37 ?  107 GLN   A HG2  1 
ATOM   2357 H  HG2  B GLN   A 1 107 ? 23.489 -12.841 -13.545 0.34 39.57 ?  107 GLN   A HG2  1 
ATOM   2358 H  HG3  A GLN   A 1 107 ? 23.483 -13.803 -14.015 0.66 43.37 ?  107 GLN   A HG3  1 
ATOM   2359 H  HG3  B GLN   A 1 107 ? 23.981 -14.333 -13.629 0.34 39.57 ?  107 GLN   A HG3  1 
ATOM   2360 H  HE21 A GLN   A 1 107 ? 20.556 -12.874 -13.782 0.66 48.49 ?  107 GLN   A HE21 1 
ATOM   2361 H  HE21 B GLN   A 1 107 ? 21.528 -12.990 -14.583 0.34 43.27 ?  107 GLN   A HE21 1 
ATOM   2362 H  HE22 A GLN   A 1 107 ? 19.872 -14.017 -13.117 0.66 48.49 ?  107 GLN   A HE22 1 
ATOM   2363 H  HE22 B GLN   A 1 107 ? 20.396 -13.854 -14.146 0.34 43.27 ?  107 GLN   A HE22 1 
ATOM   2364 N  N    A LEU   A 1 108 ? 24.730 -10.769 -9.806  0.66 21.66 ?  108 LEU   A N    1 
ATOM   2365 N  N    B LEU   A 1 108 ? 24.779 -11.012 -9.756  0.34 22.54 ?  108 LEU   A N    1 
ATOM   2366 C  CA   A LEU   A 1 108 ? 25.654 -10.420 -8.732  0.66 19.29 ?  108 LEU   A CA   1 
ATOM   2367 C  CA   B LEU   A 1 108 ? 25.662 -10.487 -8.722  0.34 20.52 ?  108 LEU   A CA   1 
ATOM   2368 C  C    A LEU   A 1 108 ? 24.954 -10.268 -7.391  0.66 17.71 ?  108 LEU   A C    1 
ATOM   2369 C  C    B LEU   A 1 108 ? 24.957 -10.296 -7.387  0.34 18.65 ?  108 LEU   A C    1 
ATOM   2370 O  O    A LEU   A 1 108 ? 25.630 -10.124 -6.372  0.66 18.03 ?  108 LEU   A O    1 
ATOM   2371 O  O    B LEU   A 1 108 ? 25.635 -10.119 -6.371  0.34 18.70 ?  108 LEU   A O    1 
ATOM   2372 C  CB   A LEU   A 1 108 ? 26.440 -9.153  -9.086  0.66 19.33 ?  108 LEU   A CB   1 
ATOM   2373 C  CB   B LEU   A 1 108 ? 26.290 -9.166  -9.184  0.34 20.75 ?  108 LEU   A CB   1 
ATOM   2374 C  CG   A LEU   A 1 108 ? 27.465 -9.364  -10.202 0.66 20.69 ?  108 LEU   A CG   1 
ATOM   2375 C  CG   B LEU   A 1 108 ? 27.343 -9.284  -10.290 0.34 21.43 ?  108 LEU   A CG   1 
ATOM   2376 C  CD1  A LEU   A 1 108 ? 27.955 -8.033  -10.749 0.66 21.33 ?  108 LEU   A CD1  1 
ATOM   2377 C  CD1  B LEU   A 1 108 ? 27.692 -7.911  -10.851 0.34 21.65 ?  108 LEU   A CD1  1 
ATOM   2378 C  CD2  A LEU   A 1 108 ? 28.644 -10.200 -9.713  0.66 21.93 ?  108 LEU   A CD2  1 
ATOM   2379 C  CD2  B LEU   A 1 108 ? 28.595 -9.980  -9.778  0.34 22.07 ?  108 LEU   A CD2  1 
ATOM   2380 H  H    A LEU   A 1 108 ? 24.572 -10.136 -10.358 0.66 26.05 ?  108 LEU   A H    1 
ATOM   2381 H  H    B LEU   A 1 108 ? 24.672 -10.483 -10.422 0.34 27.10 ?  108 LEU   A H    1 
ATOM   2382 H  HA   A LEU   A 1 108 ? 26.292 -11.141 -8.631  0.66 23.20 ?  108 LEU   A HA   1 
ATOM   2383 H  HA   B LEU   A 1 108 ? 26.381 -11.117 -8.574  0.34 24.68 ?  108 LEU   A HA   1 
ATOM   2384 H  HB2  A LEU   A 1 108 ? 25.819 -8.473  -9.381  0.66 23.25 ?  108 LEU   A HB2  1 
ATOM   2385 H  HB2  B LEU   A 1 108 ? 25.585 -8.590  -9.517  0.34 24.96 ?  108 LEU   A HB2  1 
ATOM   2386 H  HB3  A LEU   A 1 108 ? 26.917 -8.853  -8.299  0.66 23.25 ?  108 LEU   A HB3  1 
ATOM   2387 H  HB3  B LEU   A 1 108 ? 26.719 -8.746  -8.424  0.34 24.96 ?  108 LEU   A HB3  1 
ATOM   2388 H  HG   A LEU   A 1 108 ? 27.046 -9.847  -10.931 0.66 24.89 ?  108 LEU   A HG   1 
ATOM   2389 H  HG   B LEU   A 1 108 ? 26.983 -9.821  -11.012 0.34 25.77 ?  108 LEU   A HG   1 
ATOM   2390 H  HD11 A LEU   A 1 108 ? 28.602 -8.197  -11.453 0.66 25.65 ?  108 LEU   A HD11 1 
ATOM   2391 H  HD11 B LEU   A 1 108 ? 28.354 -8.014  -11.554 0.34 26.03 ?  108 LEU   A HD11 1 
ATOM   2392 H  HD12 A LEU   A 1 108 ? 27.197 -7.541  -11.104 0.66 25.65 ?  108 LEU   A HD12 1 
ATOM   2393 H  HD12 B LEU   A 1 108 ? 26.889 -7.502  -11.210 0.34 26.03 ?  108 LEU   A HD12 1 
ATOM   2394 H  HD13 A LEU   A 1 108 ? 28.369 -7.529  -10.030 0.66 25.65 ?  108 LEU   A HD13 1 
ATOM   2395 H  HD13 B LEU   A 1 108 ? 28.053 -7.361  -10.137 0.34 26.03 ?  108 LEU   A HD13 1 
ATOM   2396 H  HD21 A LEU   A 1 108 ? 29.333 -10.203 -10.395 0.66 26.38 ?  108 LEU   A HD21 1 
ATOM   2397 H  HD21 B LEU   A 1 108 ? 29.285 -9.931  -10.458 0.34 26.54 ?  108 LEU   A HD21 1 
ATOM   2398 H  HD22 A LEU   A 1 108 ? 28.990 -9.807  -8.896  0.66 26.38 ?  108 LEU   A HD22 1 
ATOM   2399 H  HD22 B LEU   A 1 108 ? 28.894 -9.535  -8.970  0.34 26.54 ?  108 LEU   A HD22 1 
ATOM   2400 H  HD23 A LEU   A 1 108 ? 28.342 -11.105 -9.543  0.66 26.38 ?  108 LEU   A HD23 1 
ATOM   2401 H  HD23 B LEU   A 1 108 ? 28.385 -10.907 -9.586  0.34 26.54 ?  108 LEU   A HD23 1 
ATOM   2402 N  N    . LEU   A 1 109 ? 23.622 -10.341 -7.353  1.00 17.46 ?  109 LEU   A N    1 
ATOM   2403 C  CA   . LEU   A 1 109 ? 22.926 -10.214 -6.079  1.00 17.05 ?  109 LEU   A CA   1 
ATOM   2404 C  C    . LEU   A 1 109 ? 23.289 -11.359 -5.137  1.00 15.97 ?  109 LEU   A C    1 
ATOM   2405 O  O    . LEU   A 1 109 ? 23.445 -11.156 -3.928  1.00 16.38 ?  109 LEU   A O    1 
ATOM   2406 C  CB   . LEU   A 1 109 ? 21.417 -10.144 -6.319  1.00 18.21 ?  109 LEU   A CB   1 
ATOM   2407 C  CG   . LEU   A 1 109 ? 20.537 -9.829  -5.106  1.00 18.58 ?  109 LEU   A CG   1 
ATOM   2408 C  CD1  . LEU   A 1 109 ? 20.991 -8.539  -4.436  1.00 18.72 ?  109 LEU   A CD1  1 
ATOM   2409 C  CD2  . LEU   A 1 109 ? 19.070 -9.734  -5.517  1.00 19.51 ?  109 LEU   A CD2  1 
ATOM   2410 H  H    A LEU   A 1 109 ? 23.107 -10.464 -8.033  0.66 21.01 ?  109 LEU   A H    1 
ATOM   2411 H  H    B LEU   A 1 109 ? 23.107 -10.445 -8.035  0.34 21.01 ?  109 LEU   A H    1 
ATOM   2412 H  HA   . LEU   A 1 109 ? 23.201 -9.387  -5.658  1.00 20.52 ?  109 LEU   A HA   1 
ATOM   2413 H  HB2  . LEU   A 1 109 ? 21.244 -9.454  -6.979  1.00 21.91 ?  109 LEU   A HB2  1 
ATOM   2414 H  HB3  . LEU   A 1 109 ? 21.120 -10.999 -6.665  1.00 21.91 ?  109 LEU   A HB3  1 
ATOM   2415 H  HG   . LEU   A 1 109 ? 20.615 -10.544 -4.459  1.00 22.35 ?  109 LEU   A HG   1 
ATOM   2416 H  HD11 . LEU   A 1 109 ? 20.314 -8.246  -3.806  1.00 22.51 ?  109 LEU   A HD11 1 
ATOM   2417 H  HD12 . LEU   A 1 109 ? 21.827 -8.698  -3.972  1.00 22.51 ?  109 LEU   A HD12 1 
ATOM   2418 H  HD13 . LEU   A 1 109 ? 21.118 -7.856  -5.118  1.00 22.51 ?  109 LEU   A HD13 1 
ATOM   2419 H  HD21 . LEU   A 1 109 ? 18.549 -9.383  -4.775  1.00 23.47 ?  109 LEU   A HD21 1 
ATOM   2420 H  HD22 . LEU   A 1 109 ? 18.987 -9.141  -6.282  1.00 23.47 ?  109 LEU   A HD22 1 
ATOM   2421 H  HD23 . LEU   A 1 109 ? 18.745 -10.620 -5.754  1.00 23.47 ?  109 LEU   A HD23 1 
ATOM   2422 N  N    . LYS   A 1 110 ? 23.429 -12.577 -5.663  1.00 16.31 ?  110 LYS   A N    1 
ATOM   2423 C  CA   . LYS   A 1 110 ? 23.809 -13.684 -4.792  1.00 16.15 ?  110 LYS   A CA   1 
ATOM   2424 C  C    . LYS   A 1 110 ? 25.193 -13.455 -4.196  1.00 15.80 ?  110 LYS   A C    1 
ATOM   2425 O  O    . LYS   A 1 110 ? 25.394 -13.647 -2.993  1.00 16.30 ?  110 LYS   A O    1 
ATOM   2426 C  CB   . LYS   A 1 110 ? 23.724 -15.013 -5.537  1.00 17.27 ?  110 LYS   A CB   1 
ATOM   2427 C  CG   . LYS   A 1 110 ? 23.919 -16.222 -4.616  1.00 17.48 ?  110 LYS   A CG   1 
ATOM   2428 C  CD   . LYS   A 1 110 ? 23.722 -17.545 -5.337  1.00 17.96 ?  110 LYS   A CD   1 
ATOM   2429 C  CE   . LYS   A 1 110 ? 23.832 -18.733 -4.385  1.00 18.86 ?  110 LYS   A CE   1 
ATOM   2430 N  NZ   . LYS   A 1 110 ? 22.654 -18.871 -3.488  1.00 19.30 ?  110 LYS   A NZ   1 
ATOM   2431 H  H    . LYS   A 1 110 ? 23.313 -12.784 -6.487  1.00 19.63 ?  110 LYS   A H    1 
ATOM   2432 H  HA   . LYS   A 1 110 ? 23.176 -13.729 -4.055  1.00 19.43 ?  110 LYS   A HA   1 
ATOM   2433 H  HB2  . LYS   A 1 110 ? 22.849 -15.093 -5.951  1.00 20.77 ?  110 LYS   A HB2  1 
ATOM   2434 H  HB3  . LYS   A 1 110 ? 24.416 -15.044 -6.214  1.00 20.77 ?  110 LYS   A HB3  1 
ATOM   2435 H  HG2  . LYS   A 1 110 ? 24.816 -16.202 -4.252  1.00 21.04 ?  110 LYS   A HG2  1 
ATOM   2436 H  HG3  . LYS   A 1 110 ? 23.268 -16.174 -3.896  1.00 21.04 ?  110 LYS   A HG3  1 
ATOM   2437 H  HD2  . LYS   A 1 110 ? 22.845 -17.563 -5.742  1.00 21.61 ?  110 LYS   A HD2  1 
ATOM   2438 H  HD3  . LYS   A 1 110 ? 24.410 -17.636 -6.018  1.00 21.61 ?  110 LYS   A HD3  1 
ATOM   2439 H  HE2  . LYS   A 1 110 ? 23.917 -19.547 -4.905  1.00 22.69 ?  110 LYS   A HE2  1 
ATOM   2440 H  HE3  . LYS   A 1 110 ? 24.624 -18.617 -3.828  1.00 22.69 ?  110 LYS   A HE3  1 
ATOM   2441 H  HZ1  . LYS   A 1 110 ? 22.759 -19.572 -2.952  1.00 23.21 ?  110 LYS   A HZ1  1 
ATOM   2442 H  HZ2  . LYS   A 1 110 ? 22.562 -18.137 -2.992  1.00 23.21 ?  110 LYS   A HZ2  1 
ATOM   2443 H  HZ3  . LYS   A 1 110 ? 21.917 -18.985 -3.975  1.00 23.21 ?  110 LYS   A HZ3  1 
ATOM   2444 N  N    . SER   A 1 111 ? 26.150 -13.016 -5.016  1.00 16.07 ?  111 SER   A N    1 
ATOM   2445 C  CA   . SER   A 1 111 ? 27.480 -12.717 -4.500  1.00 16.26 ?  111 SER   A CA   1 
ATOM   2446 C  C    . SER   A 1 111 ? 27.417 -11.662 -3.397  1.00 16.39 ?  111 SER   A C    1 
ATOM   2447 O  O    . SER   A 1 111 ? 28.117 -11.763 -2.382  1.00 16.86 ?  111 SER   A O    1 
ATOM   2448 C  CB   . SER   A 1 111 ? 28.373 -12.224 -5.643  1.00 17.73 ?  111 SER   A CB   1 
ATOM   2449 O  OG   . SER   A 1 111 ? 28.511 -13.220 -6.650  1.00 18.89 ?  111 SER   A OG   1 
ATOM   2450 H  H    . SER   A 1 111 ? 26.046 -12.887 -5.859  1.00 19.34 ?  111 SER   A H    1 
ATOM   2451 H  HA   . SER   A 1 111 ? 27.871 -13.524 -4.132  1.00 19.57 ?  111 SER   A HA   1 
ATOM   2452 H  HB2  . SER   A 1 111 ? 27.970 -11.442 -6.047  1.00 21.34 ?  111 SER   A HB2  1 
ATOM   2453 H  HB3  . SER   A 1 111 ? 29.247 -12.000 -5.285  1.00 21.34 ?  111 SER   A HB3  1 
ATOM   2454 H  HG   . SER   A 1 111 ? 29.025 -12.940 -7.260  1.00 22.72 ?  111 SER   A HG   1 
ATOM   2455 N  N    . ALA   A 1 112 ? 26.566 -10.649 -3.573  1.00 16.28 ?  112 ALA   A N    1 
ATOM   2456 C  CA   . ALA   A 1 112 ? 26.428 -9.604  -2.559  1.00 16.38 ?  112 ALA   A CA   1 
ATOM   2457 C  C    . ALA   A 1 112 ? 25.943 -10.197 -1.241  1.00 16.40 ?  112 ALA   A C    1 
ATOM   2458 O  O    . ALA   A 1 112 ? 26.493 -9.909  -0.173  1.00 16.46 ?  112 ALA   A O    1 
ATOM   2459 C  CB   . ALA   A 1 112 ? 25.473 -8.518  -3.056  1.00 16.49 ?  112 ALA   A CB   1 
ATOM   2460 H  H    . ALA   A 1 112 ? 26.071 -10.536 -4.267  1.00 19.59 ?  112 ALA   A H    1 
ATOM   2461 H  HA   . ALA   A 1 112 ? 27.296 -9.186  -2.407  1.00 19.71 ?  112 ALA   A HA   1 
ATOM   2462 H  HB1  . ALA   A 1 112 ? 25.412 -7.814  -2.386  1.00 19.85 ?  112 ALA   A HB1  1 
ATOM   2463 H  HB2  . ALA   A 1 112 ? 25.809 -8.147  -3.888  1.00 19.85 ?  112 ALA   A HB2  1 
ATOM   2464 H  HB3  . ALA   A 1 112 ? 24.596 -8.908  -3.201  1.00 19.85 ?  112 ALA   A HB3  1 
ATOM   2465 N  N    . TYR   A 1 113 ? 24.913 -11.048 -1.298  1.00 16.27 ?  113 TYR   A N    1 
ATOM   2466 C  CA   . TYR   A 1 113 ? 24.401 -11.656 -0.072  1.00 15.78 ?  113 TYR   A CA   1 
ATOM   2467 C  C    . TYR   A 1 113 ? 25.405 -12.600 0.584   1.00 15.71 ?  113 TYR   A C    1 
ATOM   2468 O  O    . TYR   A 1 113 ? 25.367 -12.775 1.808   1.00 16.20 ?  113 TYR   A O    1 
ATOM   2469 C  CB   . TYR   A 1 113 ? 23.087 -12.391 -0.344  1.00 15.90 ?  113 TYR   A CB   1 
ATOM   2470 C  CG   . TYR   A 1 113 ? 21.870 -11.502 -0.257  1.00 16.13 ?  113 TYR   A CG   1 
ATOM   2471 C  CD1  . TYR   A 1 113 ? 21.505 -10.912 0.946   1.00 16.29 ?  113 TYR   A CD1  1 
ATOM   2472 C  CD2  . TYR   A 1 113 ? 21.074 -11.266 -1.369  1.00 16.32 ?  113 TYR   A CD2  1 
ATOM   2473 C  CE1  . TYR   A 1 113 ? 20.382 -10.118 1.043   1.00 16.74 ?  113 TYR   A CE1  1 
ATOM   2474 C  CE2  . TYR   A 1 113 ? 19.925 -10.462 -1.283  1.00 16.41 ?  113 TYR   A CE2  1 
ATOM   2475 C  CZ   . TYR   A 1 113 ? 19.592 -9.893  -0.071  1.00 16.40 ?  113 TYR   A CZ   1 
ATOM   2476 O  OH   . TYR   A 1 113 ? 18.467 -9.105  0.043   1.00 17.16 ?  113 TYR   A OH   1 
ATOM   2477 H  H    . TYR   A 1 113 ? 24.512 -11.282 -2.023  1.00 19.58 ?  113 TYR   A H    1 
ATOM   2478 H  HA   . TYR   A 1 113 ? 24.221 -10.950 0.563   1.00 18.99 ?  113 TYR   A HA   1 
ATOM   2479 H  HB2  . TYR   A 1 113 ? 23.116 -12.763 -1.239  1.00 19.13 ?  113 TYR   A HB2  1 
ATOM   2480 H  HB3  . TYR   A 1 113 ? 22.990 -13.103 0.306   1.00 19.13 ?  113 TYR   A HB3  1 
ATOM   2481 H  HD1  . TYR   A 1 113 ? 22.028 -11.066 1.703   1.00 19.60 ?  113 TYR   A HD1  1 
ATOM   2482 H  HD2  . TYR   A 1 113 ? 21.296 -11.666 -2.179  1.00 19.64 ?  113 TYR   A HD2  1 
ATOM   2483 H  HE1  . TYR   A 1 113 ? 20.156 -9.739  1.857   1.00 20.14 ?  113 TYR   A HE1  1 
ATOM   2484 H  HE2  . TYR   A 1 113 ? 19.394 -10.319 -2.034  1.00 19.75 ?  113 TYR   A HE2  1 
ATOM   2485 H  HH   . TYR   A 1 113 ? 18.085 -9.061  -0.710  1.00 20.65 ?  113 TYR   A HH   1 
ATOM   2486 N  N    . GLU   A 1 114 ? 26.312 -13.209 -0.192  1.00 15.77 ?  114 GLU   A N    1 
ATOM   2487 C  CA   . GLU   A 1 114 ? 27.299 -14.106 0.406   1.00 16.00 ?  114 GLU   A CA   1 
ATOM   2488 C  C    . GLU   A 1 114 ? 28.149 -13.394 1.452   1.00 15.91 ?  114 GLU   A C    1 
ATOM   2489 O  O    . GLU   A 1 114 ? 28.634 -14.030 2.394   1.00 16.23 ?  114 GLU   A O    1 
ATOM   2490 C  CB   . GLU   A 1 114 ? 28.171 -14.755 -0.680  1.00 16.33 ?  114 GLU   A CB   1 
ATOM   2491 C  CG   . GLU   A 1 114 ? 27.409 -15.788 -1.473  1.00 16.87 ?  114 GLU   A CG   1 
ATOM   2492 C  CD   . GLU   A 1 114 ? 28.127 -16.331 -2.697  1.00 17.49 ?  114 GLU   A CD   1 
ATOM   2493 O  OE1  . GLU   A 1 114 ? 29.084 -15.702 -3.196  1.00 17.57 ?  114 GLU   A OE1  1 
ATOM   2494 O  OE2  . GLU   A 1 114 ? 27.690 -17.392 -3.181  1.00 18.16 -1 114 GLU   A OE2  1 
ATOM   2495 H  H    . GLU   A 1 114 ? 26.372 -13.118 -1.049  1.00 18.98 ?  114 GLU   A H    1 
ATOM   2496 H  HA   . GLU   A 1 114 ? 26.822 -14.819 0.856   1.00 19.25 ?  114 GLU   A HA   1 
ATOM   2497 H  HB2  . GLU   A 1 114 ? 28.474 -14.070 -1.300  1.00 19.65 ?  114 GLU   A HB2  1 
ATOM   2498 H  HB3  . GLU   A 1 114 ? 28.926 -15.191 -0.266  1.00 19.65 ?  114 GLU   A HB3  1 
ATOM   2499 H  HG2  . GLU   A 1 114 ? 27.225 -16.547 -0.895  1.00 20.29 ?  114 GLU   A HG2  1 
ATOM   2500 H  HG3  . GLU   A 1 114 ? 26.570 -15.402 -1.770  1.00 20.29 ?  114 GLU   A HG3  1 
ATOM   2501 N  N    . ASN   A 1 115 ? 28.328 -12.076 1.322   1.00 15.82 ?  115 ASN   A N    1 
ATOM   2502 C  CA   . ASN   A 1 115 ? 29.087 -11.342 2.330   1.00 16.40 ?  115 ASN   A CA   1 
ATOM   2503 C  C    . ASN   A 1 115 ? 28.464 -11.479 3.714   1.00 16.92 ?  115 ASN   A C    1 
ATOM   2504 O  O    . ASN   A 1 115 ? 29.171 -11.414 4.723   1.00 17.30 ?  115 ASN   A O    1 
ATOM   2505 C  CB   . ASN   A 1 115 ? 29.183 -9.865  1.945   1.00 16.52 ?  115 ASN   A CB   1 
ATOM   2506 C  CG   . ASN   A 1 115 ? 29.991 -9.644  0.691   1.00 16.73 ?  115 ASN   A CG   1 
ATOM   2507 O  OD1  . ASN   A 1 115 ? 31.210 -9.745  0.717   1.00 19.72 ?  115 ASN   A OD1  1 
ATOM   2508 N  ND2  . ASN   A 1 115 ? 29.332 -9.352  -0.409  1.00 16.17 ?  115 ASN   A ND2  1 
ATOM   2509 H  H    . ASN   A 1 115 ? 28.022 -11.590 0.676   1.00 19.04 ?  115 ASN   A H    1 
ATOM   2510 H  HA   . ASN   A 1 115 ? 29.986 -11.699 2.367   1.00 19.74 ?  115 ASN   A HA   1 
ATOM   2511 H  HB2  . ASN   A 1 115 ? 28.289 -9.516  1.799   1.00 19.87 ?  115 ASN   A HB2  1 
ATOM   2512 H  HB3  . ASN   A 1 115 ? 29.614 -9.379  2.667   1.00 19.87 ?  115 ASN   A HB3  1 
ATOM   2513 H  HD21 . ASN   A 1 115 ? 29.762 -9.217  -1.146  1.00 19.46 ?  115 ASN   A HD21 1 
ATOM   2514 H  HD22 . ASN   A 1 115 ? 28.477 -9.288  -0.395  1.00 19.46 ?  115 ASN   A HD22 1 
ATOM   2515 N  N    . PHE   A 1 116 ? 27.139 -11.653 3.789   1.00 16.63 ?  116 PHE   A N    1 
ATOM   2516 C  CA   . PHE   A 1 116 ? 26.493 -11.747 5.094   1.00 16.43 ?  116 PHE   A CA   1 
ATOM   2517 C  C    . PHE   A 1 116 ? 26.966 -12.979 5.862   1.00 16.22 ?  116 PHE   A C    1 
ATOM   2518 O  O    . PHE   A 1 116 ? 26.900 -13.000 7.096   1.00 16.38 ?  116 PHE   A O    1 
ATOM   2519 C  CB   . PHE   A 1 116 ? 24.968 -11.879 4.952   1.00 16.64 ?  116 PHE   A CB   1 
ATOM   2520 C  CG   . PHE   A 1 116 ? 24.214 -10.632 4.489   1.00 16.00 ?  116 PHE   A CG   1 
ATOM   2521 C  CD1  . PHE   A 1 116 ? 24.790 -9.604  3.761   1.00 15.97 ?  116 PHE   A CD1  1 
ATOM   2522 C  CD2  . PHE   A 1 116 ? 22.857 -10.531 4.797   1.00 16.45 ?  116 PHE   A CD2  1 
ATOM   2523 C  CE1  . PHE   A 1 116 ? 24.029 -8.530  3.350   1.00 16.33 ?  116 PHE   A CE1  1 
ATOM   2524 C  CE2  . PHE   A 1 116 ? 22.101 -9.457  4.393   1.00 16.43 ?  116 PHE   A CE2  1 
ATOM   2525 C  CZ   . PHE   A 1 116 ? 22.680 -8.456  3.671   1.00 15.91 ?  116 PHE   A CZ   1 
ATOM   2526 H  H    . PHE   A 1 116 ? 26.604 -11.707 3.114   1.00 20.01 ?  116 PHE   A H    1 
ATOM   2527 H  HA   . PHE   A 1 116 ? 26.686 -10.956 5.619   1.00 19.77 ?  116 PHE   A HA   1 
ATOM   2528 H  HB2  . PHE   A 1 116 ? 24.780 -12.580 4.309   1.00 20.02 ?  116 PHE   A HB2  1 
ATOM   2529 H  HB3  . PHE   A 1 116 ? 24.602 -12.130 5.815   1.00 20.02 ?  116 PHE   A HB3  1 
ATOM   2530 H  HD1  . PHE   A 1 116 ? 25.686 -9.652  3.534   1.00 19.22 ?  116 PHE   A HD1  1 
ATOM   2531 H  HD2  . PHE   A 1 116 ? 22.444 -11.219 5.281   1.00 19.79 ?  116 PHE   A HD2  1 
ATOM   2532 H  HE1  . PHE   A 1 116 ? 24.429 -7.848  2.864   1.00 19.65 ?  116 PHE   A HE1  1 
ATOM   2533 H  HE2  . PHE   A 1 116 ? 21.193 -9.418  4.612   1.00 19.77 ?  116 PHE   A HE2  1 
ATOM   2534 H  HZ   . PHE   A 1 116 ? 22.178 -7.722  3.400   1.00 19.15 ?  116 PHE   A HZ   1 
ATOM   2535 N  N    . ASN   A 1 117 ? 27.416 -14.023 5.157   1.00 16.38 ?  117 ASN   A N    1 
ATOM   2536 C  CA   . ASN   A 1 117 ? 27.782 -15.272 5.823   1.00 16.54 ?  117 ASN   A CA   1 
ATOM   2537 C  C    . ASN   A 1 117 ? 29.041 -15.149 6.658   1.00 17.11 ?  117 ASN   A C    1 
ATOM   2538 O  O    . ASN   A 1 117 ? 29.359 -16.077 7.409   1.00 18.73 ?  117 ASN   A O    1 
ATOM   2539 C  CB   . ASN   A 1 117 ? 27.914 -16.394 4.796   1.00 16.76 ?  117 ASN   A CB   1 
ATOM   2540 C  CG   . ASN   A 1 117 ? 26.563 -16.795 4.248   1.00 16.74 ?  117 ASN   A CG   1 
ATOM   2541 O  OD1  . ASN   A 1 117 ? 25.582 -16.823 4.993   1.00 17.70 ?  117 ASN   A OD1  1 
ATOM   2542 N  ND2  . ASN   A 1 117 ? 26.488 -17.034 2.948   1.00 16.59 ?  117 ASN   A ND2  1 
ATOM   2543 H  H    . ASN   A 1 117 ? 27.494 -14.038 4.298   1.00 19.72 ?  117 ASN   A H    1 
ATOM   2544 H  HA   . ASN   A 1 117 ? 27.057 -15.515 6.420   1.00 19.90 ?  117 ASN   A HA   1 
ATOM   2545 H  HB2  . ASN   A 1 117 ? 28.472 -16.092 4.059   1.00 20.16 ?  117 ASN   A HB2  1 
ATOM   2546 H  HB3  . ASN   A 1 117 ? 28.311 -17.169 5.221   1.00 20.16 ?  117 ASN   A HB3  1 
ATOM   2547 H  HD21 . ASN   A 1 117 ? 25.742 -17.259 2.593   1.00 19.96 ?  117 ASN   A HD21 1 
ATOM   2548 H  HD22 . ASN   A 1 117 ? 27.201 -16.988 2.457   1.00 19.96 ?  117 ASN   A HD22 1 
ATOM   2549 N  N    . GLN   A 1 118 ? 29.771 -14.046 6.536   1.00 16.46 ?  118 GLN   A N    1 
ATOM   2550 C  CA   . GLN   A 1 118 ? 30.944 -13.798 7.360   1.00 17.66 ?  118 GLN   A CA   1 
ATOM   2551 C  C    . GLN   A 1 118 ? 30.601 -13.229 8.731   1.00 17.60 ?  118 GLN   A C    1 
ATOM   2552 O  O    . GLN   A 1 118 ? 31.519 -12.924 9.503   1.00 18.60 ?  118 GLN   A O    1 
ATOM   2553 C  CB   . GLN   A 1 118 ? 31.925 -12.887 6.619   1.00 17.64 ?  118 GLN   A CB   1 
ATOM   2554 C  CG   . GLN   A 1 118 ? 32.397 -13.478 5.301   1.00 17.50 ?  118 GLN   A CG   1 
ATOM   2555 C  CD   . GLN   A 1 118 ? 33.252 -14.719 5.487   1.00 18.07 ?  118 GLN   A CD   1 
ATOM   2556 O  OE1  . GLN   A 1 118 ? 34.115 -14.767 6.367   1.00 18.82 ?  118 GLN   A OE1  1 
ATOM   2557 N  NE2  . GLN   A 1 118 ? 33.016 -15.730 4.654   1.00 18.09 ?  118 GLN   A NE2  1 
ATOM   2558 H  H    . GLN   A 1 118 ? 29.595 -13.409 5.978   1.00 19.81 ?  118 GLN   A H    1 
ATOM   2559 H  HA   . GLN   A 1 118 ? 31.386 -14.646 7.503   1.00 21.24 ?  118 GLN   A HA   1 
ATOM   2560 H  HB2  . GLN   A 1 118 ? 31.482 -12.041 6.431   1.00 21.23 ?  118 GLN   A HB2  1 
ATOM   2561 H  HB3  . GLN   A 1 118 ? 32.696 -12.739 7.182   1.00 21.23 ?  118 GLN   A HB3  1 
ATOM   2562 H  HG2  . GLN   A 1 118 ? 31.624 -13.721 4.762   1.00 21.06 ?  118 GLN   A HG2  1 
ATOM   2563 H  HG3  . GLN   A 1 118 ? 32.929 -12.818 4.832   1.00 21.06 ?  118 GLN   A HG3  1 
ATOM   2564 H  HE21 . GLN   A 1 118 ? 32.396 -15.660 4.054   1.00 21.76 ?  118 GLN   A HE21 1 
ATOM   2565 H  HE22 . GLN   A 1 118 ? 33.464 -16.458 4.718   1.00 21.76 ?  118 GLN   A HE22 1 
ATOM   2566 N  N    . HIS   A 1 119 ? 29.313 -13.082 9.048   1.00 17.11 ?  119 HIS   A N    1 
ATOM   2567 C  CA   . HIS   A 1 119 ? 28.866 -12.475 10.297  1.00 17.22 ?  119 HIS   A CA   1 
ATOM   2568 C  C    . HIS   A 1 119 ? 27.732 -13.301 10.872  1.00 17.47 ?  119 HIS   A C    1 
ATOM   2569 O  O    . HIS   A 1 119 ? 26.784 -13.633 10.156  1.00 18.17 ?  119 HIS   A O    1 
ATOM   2570 C  CB   . HIS   A 1 119 ? 28.403 -11.043 10.034  1.00 17.55 ?  119 HIS   A CB   1 
ATOM   2571 C  CG   . HIS   A 1 119 ? 29.475 -10.234 9.402   1.00 18.93 ?  119 HIS   A CG   1 
ATOM   2572 N  ND1  . HIS   A 1 119 ? 30.450 -9.608  10.142  1.00 20.89 ?  119 HIS   A ND1  1 
ATOM   2573 C  CD2  . HIS   A 1 119 ? 29.804 -10.057 8.103   1.00 19.57 ?  119 HIS   A CD2  1 
ATOM   2574 C  CE1  . HIS   A 1 119 ? 31.306 -9.026  9.322   1.00 20.60 ?  119 HIS   A CE1  1 
ATOM   2575 N  NE2  . HIS   A 1 119 ? 30.942 -9.290  8.079   1.00 20.53 ?  119 HIS   A NE2  1 
ATOM   2576 H  H    . HIS   A 1 119 ? 28.660 -13.338 8.543   1.00 20.58 ?  119 HIS   A H    1 
ATOM   2577 H  HA   . HIS   A 1 119 ? 29.598 -12.461 10.933  1.00 20.72 ?  119 HIS   A HA   1 
ATOM   2578 H  HB2  . HIS   A 1 119 ? 27.637 -11.063 9.438   1.00 21.11 ?  119 HIS   A HB2  1 
ATOM   2579 H  HB3  . HIS   A 1 119 ? 28.161 -10.630 10.877  1.00 21.11 ?  119 HIS   A HB3  1 
ATOM   2580 H  HD2  . HIS   A 1 119 ? 29.343 -10.384 7.363   1.00 23.54 ?  119 HIS   A HD2  1 
ATOM   2581 H  HE1  . HIS   A 1 119 ? 32.040 -8.514  9.576   1.00 24.78 ?  119 HIS   A HE1  1 
ATOM   2582 H  HE2  . HIS   A 1 119 ? 31.344 -9.009  7.369   1.00 24.69 ?  119 HIS   A HE2  1 
ATOM   2583 N  N    . GLU   A 1 120 ? 27.816 -13.608 12.169  1.00 18.69 ?  120 GLU   A N    1 
ATOM   2584 C  CA   . GLU   A 1 120 ? 26.866 -14.550 12.764  1.00 20.58 ?  120 GLU   A CA   1 
ATOM   2585 C  C    . GLU   A 1 120 ? 25.445 -13.993 12.808  1.00 19.21 ?  120 GLU   A C    1 
ATOM   2586 O  O    . GLU   A 1 120 ? 24.472 -14.752 12.681  1.00 19.56 ?  120 GLU   A O    1 
ATOM   2587 C  CB   . GLU   A 1 120 ? 27.322 -14.942 14.171  1.00 24.31 ?  120 GLU   A CB   1 
ATOM   2588 C  CG   . GLU   A 1 120 ? 28.543 -15.843 14.199  1.00 28.65 ?  120 GLU   A CG   1 
ATOM   2589 C  CD   . GLU   A 1 120 ? 28.647 -16.638 15.482  1.00 32.98 ?  120 GLU   A CD   1 
ATOM   2590 O  OE1  . GLU   A 1 120 ? 28.361 -16.071 16.558  1.00 35.66 ?  120 GLU   A OE1  1 
ATOM   2591 O  OE2  . GLU   A 1 120 ? 29.006 -17.833 15.414  1.00 36.17 -1 120 GLU   A OE2  1 
ATOM   2592 H  H    . GLU   A 1 120 ? 28.419 -13.309 12.714  1.00 22.48 ?  120 GLU   A H    1 
ATOM   2593 H  HA   . GLU   A 1 120 ? 26.856 -15.360 12.231  1.00 24.75 ?  120 GLU   A HA   1 
ATOM   2594 H  HB2  . GLU   A 1 120 ? 27.539 -14.139 14.670  1.00 29.23 ?  120 GLU   A HB2  1 
ATOM   2595 H  HB3  . GLU   A 1 120 ? 26.598 -15.416 14.616  1.00 29.23 ?  120 GLU   A HB3  1 
ATOM   2596 H  HG2  . GLU   A 1 120 ? 28.499 -16.459 13.453  1.00 34.44 ?  120 GLU   A HG2  1 
ATOM   2597 H  HG3  . GLU   A 1 120 ? 29.341 -15.297 14.139  1.00 34.44 ?  120 GLU   A HG3  1 
ATOM   2598 N  N    . VAL   A 1 121 ? 25.307 -12.688 13.038  1.00 18.63 ?  121 VAL   A N    1 
ATOM   2599 C  CA   . VAL   A 1 121 ? 24.013 -12.025 13.168  1.00 18.79 ?  121 VAL   A CA   1 
ATOM   2600 C  C    . VAL   A 1 121 ? 24.120 -10.645 12.526  1.00 17.94 ?  121 VAL   A C    1 
ATOM   2601 O  O    . VAL   A 1 121 ? 25.092 -9.919  12.762  1.00 18.56 ?  121 VAL   A O    1 
ATOM   2602 C  CB   . VAL   A 1 121 ? 23.604 -11.871 14.651  1.00 20.95 ?  121 VAL   A CB   1 
ATOM   2603 C  CG1  . VAL   A 1 121 ? 22.216 -11.244 14.761  1.00 21.15 ?  121 VAL   A CG1  1 
ATOM   2604 C  CG2  . VAL   A 1 121 ? 23.640 -13.202 15.385  1.00 22.91 ?  121 VAL   A CG2  1 
ATOM   2605 H  H    . VAL   A 1 121 ? 25.968 -12.151 13.136  1.00 22.41 ?  121 VAL   A H    1 
ATOM   2606 H  HA   . VAL   A 1 121 ? 23.329 -12.544 12.712  1.00 22.60 ?  121 VAL   A HA   1 
ATOM   2607 H  HB   . VAL   A 1 121 ? 24.232 -11.274 15.087  1.00 25.19 ?  121 VAL   A HB   1 
ATOM   2608 H  HG11 . VAL   A 1 121 ? 21.920 -11.291 15.685  1.00 25.44 ?  121 VAL   A HG11 1 
ATOM   2609 H  HG12 . VAL   A 1 121 ? 22.259 -10.318 14.477  1.00 25.44 ?  121 VAL   A HG12 1 
ATOM   2610 H  HG13 . VAL   A 1 121 ? 21.600 -11.737 14.195  1.00 25.44 ?  121 VAL   A HG13 1 
ATOM   2611 H  HG21 . VAL   A 1 121 ? 23.306 -13.071 16.292  1.00 27.54 ?  121 VAL   A HG21 1 
ATOM   2612 H  HG22 . VAL   A 1 121 ? 23.073 -13.837 14.919  1.00 27.54 ?  121 VAL   A HG22 1 
ATOM   2613 H  HG23 . VAL   A 1 121 ? 24.550 -13.526 15.414  1.00 27.54 ?  121 VAL   A HG23 1 
ATOM   2614 N  N    . LEU   A 1 122 ? 23.105 -10.257 11.749  1.00 16.88 ?  122 LEU   A N    1 
ATOM   2615 C  CA   . LEU   A 1 122 ? 23.117 -8.957  11.091  1.00 16.55 ?  122 LEU   A CA   1 
ATOM   2616 C  C    . LEU   A 1 122 ? 21.719 -8.366  11.016  1.00 17.05 ?  122 LEU   A C    1 
ATOM   2617 O  O    . LEU   A 1 122 ? 20.726 -9.081  10.874  1.00 17.98 ?  122 LEU   A O    1 
ATOM   2618 C  CB   . LEU   A 1 122 ? 23.565 -9.048  9.635   1.00 18.16 ?  122 LEU   A CB   1 
ATOM   2619 C  CG   . LEU   A 1 122 ? 24.758 -9.909  9.262   1.00 18.24 ?  122 LEU   A CG   1 
ATOM   2620 C  CD1  . LEU   A 1 122 ? 24.310 -11.343 9.023   1.00 18.20 ?  122 LEU   A CD1  1 
ATOM   2621 C  CD2  . LEU   A 1 122 ? 25.435 -9.339  8.027   1.00 17.22 ?  122 LEU   A CD2  1 
ATOM   2622 H  H    . LEU   A 1 122 ? 22.389 -10.728 11.600  1.00 20.31 ?  122 LEU   A H    1 
ATOM   2623 H  HA   . LEU   A 1 122 ? 23.701 -8.348  11.572  1.00 19.91 ?  122 LEU   A HA   1 
ATOM   2624 H  HB2  . LEU   A 1 122 ? 22.823 -9.379  9.118   1.00 21.85 ?  122 LEU   A HB2  1 
ATOM   2625 H  HB3  . LEU   A 1 122 ? 23.785 -8.152  9.342   1.00 21.85 ?  122 LEU   A HB3  1 
ATOM   2626 H  HG   . LEU   A 1 122 ? 25.411 -9.919  9.985   1.00 21.94 ?  122 LEU   A HG   1 
ATOM   2627 H  HD11 . LEU   A 1 122 ? 25.067 -11.883 8.747   1.00 21.89 ?  122 LEU   A HD11 1 
ATOM   2628 H  HD12 . LEU   A 1 122 ? 23.935 -11.703 9.845   1.00 21.89 ?  122 LEU   A HD12 1 
ATOM   2629 H  HD13 . LEU   A 1 122 ? 23.631 -11.352 8.326   1.00 21.89 ?  122 LEU   A HD13 1 
ATOM   2630 H  HD21 . LEU   A 1 122 ? 26.167 -9.924  7.759   1.00 20.72 ?  122 LEU   A HD21 1 
ATOM   2631 H  HD22 . LEU   A 1 122 ? 24.787 -9.278  7.311   1.00 20.72 ?  122 LEU   A HD22 1 
ATOM   2632 H  HD23 . LEU   A 1 122 ? 25.784 -8.458  8.237   1.00 20.72 ?  122 LEU   A HD23 1 
ATOM   2633 N  N    A LEU   A 1 123 ? 21.664 -7.040  11.112  0.66 16.51 ?  123 LEU   A N    1 
ATOM   2634 N  N    B LEU   A 1 123 ? 21.662 -7.040  11.107  0.34 15.82 ?  123 LEU   A N    1 
ATOM   2635 C  CA   A LEU   A 1 123 ? 20.487 -6.247  10.781  0.66 16.33 ?  123 LEU   A CA   1 
ATOM   2636 C  CA   B LEU   A 1 123 ? 20.507 -6.262  10.678  0.34 15.16 ?  123 LEU   A CA   1 
ATOM   2637 C  C    A LEU   A 1 123 ? 20.705 -5.672  9.391   0.66 15.82 ?  123 LEU   A C    1 
ATOM   2638 C  C    B LEU   A 1 123 ? 20.776 -5.800  9.253   0.34 14.62 ?  123 LEU   A C    1 
ATOM   2639 O  O    A LEU   A 1 123 ? 21.739 -5.049  9.146   0.66 16.15 ?  123 LEU   A O    1 
ATOM   2640 O  O    B LEU   A 1 123 ? 21.853 -5.267  8.972   0.34 14.80 ?  123 LEU   A O    1 
ATOM   2641 C  CB   A LEU   A 1 123 ? 20.340 -5.098  11.777  0.66 17.17 ?  123 LEU   A CB   1 
ATOM   2642 C  CB   B LEU   A 1 123 ? 20.341 -5.050  11.594  0.34 15.36 ?  123 LEU   A CB   1 
ATOM   2643 C  CG   A LEU   A 1 123 ? 19.314 -4.027  11.406  0.66 17.82 ?  123 LEU   A CG   1 
ATOM   2644 C  CG   B LEU   A 1 123 ? 19.297 -3.995  11.225  0.34 15.83 ?  123 LEU   A CG   1 
ATOM   2645 C  CD1  A LEU   A 1 123 ? 17.920 -4.637  11.360  0.66 18.36 ?  123 LEU   A CD1  1 
ATOM   2646 C  CD1  B LEU   A 1 123 ? 17.886 -4.556  11.327  0.34 16.12 ?  123 LEU   A CD1  1 
ATOM   2647 C  CD2  A LEU   A 1 123 ? 19.377 -2.876  12.390  0.66 18.44 ?  123 LEU   A CD2  1 
ATOM   2648 C  CD2  B LEU   A 1 123 ? 19.461 -2.780  12.121  0.34 16.02 ?  123 LEU   A CD2  1 
ATOM   2649 H  H    A LEU   A 1 123 ? 22.332 -6.555  11.358  0.66 19.87 ?  123 LEU   A H    1 
ATOM   2650 H  H    B LEU   A 1 123 ? 22.302 -6.556  11.420  0.34 19.04 ?  123 LEU   A H    1 
ATOM   2651 H  HA   A LEU   A 1 123 ? 19.687 -6.795  10.784  0.66 19.65 ?  123 LEU   A HA   1 
ATOM   2652 H  HA   B LEU   A 1 123 ? 19.706 -6.810  10.707  0.34 18.25 ?  123 LEU   A HA   1 
ATOM   2653 H  HB2  A LEU   A 1 123 ? 20.071 -5.469  12.633  0.66 20.65 ?  123 LEU   A HB2  1 
ATOM   2654 H  HB2  B LEU   A 1 123 ? 20.106 -5.377  12.478  0.34 18.49 ?  123 LEU   A HB2  1 
ATOM   2655 H  HB3  A LEU   A 1 123 ? 21.197 -4.658  11.870  0.66 20.65 ?  123 LEU   A HB3  1 
ATOM   2656 H  HB3  B LEU   A 1 123 ? 21.193 -4.596  11.641  0.34 18.49 ?  123 LEU   A HB3  1 
ATOM   2657 H  HG   A LEU   A 1 123 ? 19.514 -3.673  10.523  0.66 21.44 ?  123 LEU   A HG   1 
ATOM   2658 H  HG   B LEU   A 1 123 ? 19.439 -3.712  10.309  0.34 19.05 ?  123 LEU   A HG   1 
ATOM   2659 H  HD11 A LEU   A 1 123 ? 17.274 -3.935  11.193  0.66 22.08 ?  123 LEU   A HD11 1 
ATOM   2660 H  HD11 B LEU   A 1 123 ? 17.249 -3.836  11.198  0.34 19.39 ?  123 LEU   A HD11 1 
ATOM   2661 H  HD12 A LEU   A 1 123 ? 17.885 -5.296  10.646  0.66 22.08 ?  123 LEU   A HD12 1 
ATOM   2662 H  HD12 B LEU   A 1 123 ? 17.764 -5.231  10.641  0.34 19.39 ?  123 LEU   A HD12 1 
ATOM   2663 H  HD13 A LEU   A 1 123 ? 17.736 -5.064  12.211  0.66 22.08 ?  123 LEU   A HD13 1 
ATOM   2664 H  HD13 B LEU   A 1 123 ? 17.765 -4.951  12.205  0.34 19.39 ?  123 LEU   A HD13 1 
ATOM   2665 H  HD21 A LEU   A 1 123 ? 18.721 -2.209  12.134  0.66 22.19 ?  123 LEU   A HD21 1 
ATOM   2666 H  HD21 B LEU   A 1 123 ? 18.793 -2.120  11.884  0.34 19.28 ?  123 LEU   A HD21 1 
ATOM   2667 H  HD22 A LEU   A 1 123 ? 19.183 -3.212  13.277  0.66 22.19 ?  123 LEU   A HD22 1 
ATOM   2668 H  HD22 B LEU   A 1 123 ? 19.344 -3.054  13.045  0.34 19.28 ?  123 LEU   A HD22 1 
ATOM   2669 H  HD23 A LEU   A 1 123 ? 20.267 -2.492  12.365  0.66 22.19 ?  123 LEU   A HD23 1 
ATOM   2670 H  HD23 B LEU   A 1 123 ? 20.350 -2.415  11.993  0.34 19.28 ?  123 LEU   A HD23 1 
ATOM   2671 N  N    A ALA   A 1 124 ? 19.745 -5.855  8.489   0.66 15.40 ?  124 ALA   A N    1 
ATOM   2672 N  N    B ALA   A 1 124 ? 19.815 -6.001  8.352   0.34 14.02 ?  124 ALA   A N    1 
ATOM   2673 C  CA   A ALA   A 1 124 ? 20.013 -5.551  7.093   0.66 14.83 ?  124 ALA   A CA   1 
ATOM   2674 C  CA   B ALA   A 1 124 ? 20.122 -5.852  6.936   0.34 13.96 ?  124 ALA   A CA   1 
ATOM   2675 C  C    A ALA   A 1 124 ? 18.765 -5.083  6.361   0.66 14.45 ?  124 ALA   A C    1 
ATOM   2676 C  C    B ALA   A 1 124 ? 18.922 -5.383  6.125   0.34 13.82 ?  124 ALA   A C    1 
ATOM   2677 O  O    A ALA   A 1 124 ? 17.639 -5.426  6.752   0.66 14.96 ?  124 ALA   A O    1 
ATOM   2678 O  O    B ALA   A 1 124 ? 17.774 -5.696  6.465   0.34 14.19 ?  124 ALA   A O    1 
ATOM   2679 C  CB   A ALA   A 1 124 ? 20.607 -6.763  6.363   0.66 14.48 ?  124 ALA   A CB   1 
ATOM   2680 C  CB   B ALA   A 1 124 ? 20.659 -7.163  6.347   0.34 14.32 ?  124 ALA   A CB   1 
ATOM   2681 H  H    A ALA   A 1 124 ? 18.947 -6.143  8.649   0.66 18.54 ?  124 ALA   A H    1 
ATOM   2682 H  H    B ALA   A 1 124 ? 19.003 -6.220  8.533   0.34 16.88 ?  124 ALA   A H    1 
ATOM   2683 H  HA   A ALA   A 1 124 ? 20.671 -4.837  7.056   0.66 17.85 ?  124 ALA   A HA   1 
ATOM   2684 H  HA   B ALA   A 1 124 ? 20.817 -5.189  6.858   0.34 16.80 ?  124 ALA   A HA   1 
ATOM   2685 H  HB1  A ALA   A 1 124 ? 20.782 -6.526  5.439   0.66 17.43 ?  124 ALA   A HB1  1 
ATOM   2686 H  HB1  B ALA   A 1 124 ? 20.854 -7.031  5.407   0.34 17.24 ?  124 ALA   A HB1  1 
ATOM   2687 H  HB2  A ALA   A 1 124 ? 21.440 -7.014  6.800   0.66 17.43 ?  124 ALA   A HB2  1 
ATOM   2688 H  HB2  B ALA   A 1 124 ? 21.471 -7.414  6.820   0.34 17.24 ?  124 ALA   A HB2  1 
ATOM   2689 H  HB3  A ALA   A 1 124 ? 19.978 -7.497  6.407   0.66 17.43 ?  124 ALA   A HB3  1 
ATOM   2690 H  HB3  B ALA   A 1 124 ? 19.990 -7.857  6.453   0.34 17.24 ?  124 ALA   A HB3  1 
ATOM   2691 N  N    A PRO   A 1 125 ? 18.938 -4.314  5.292   0.66 14.10 ?  125 PRO   A N    1 
ATOM   2692 N  N    B PRO   A 1 125 ? 19.165 -4.655  5.028   0.34 12.83 ?  125 PRO   A N    1 
ATOM   2693 C  CA   A PRO   A 1 125 ? 17.868 -4.090  4.324   0.66 14.90 ?  125 PRO   A CA   1 
ATOM   2694 C  CA   B PRO   A 1 125 ? 18.094 -4.304  4.093   0.34 13.10 ?  125 PRO   A CA   1 
ATOM   2695 C  C    A PRO   A 1 125 ? 17.950 -5.171  3.250   0.66 14.75 ?  125 PRO   A C    1 
ATOM   2696 C  C    B PRO   A 1 125 ? 18.037 -5.270  2.923   0.34 13.64 ?  125 PRO   A C    1 
ATOM   2697 O  O    A PRO   A 1 125 ? 18.904 -5.951  3.191   0.66 14.65 ?  125 PRO   A O    1 
ATOM   2698 O  O    B PRO   A 1 125 ? 18.971 -6.048  2.700   0.34 13.87 ?  125 PRO   A O    1 
ATOM   2699 C  CB   A PRO   A 1 125 ? 18.265 -2.729  3.736   0.66 15.76 ?  125 PRO   A CB   1 
ATOM   2700 C  CB   B PRO   A 1 125 ? 18.551 -2.939  3.587   0.34 12.72 ?  125 PRO   A CB   1 
ATOM   2701 C  CG   A PRO   A 1 125 ? 19.767 -2.837  3.656   0.66 16.20 ?  125 PRO   A CG   1 
ATOM   2702 C  CG   B PRO   A 1 125 ? 20.046 -3.117  3.487   0.34 11.91 ?  125 PRO   A CG   1 
ATOM   2703 C  CD   A PRO   A 1 125 ? 20.178 -3.623  4.890   0.66 15.17 ?  125 PRO   A CD   1 
ATOM   2704 C  CD   B PRO   A 1 125 ? 20.437 -4.013  4.650   0.34 11.66 ?  125 PRO   A CD   1 
ATOM   2705 H  HA   A PRO   A 1 125 ? 16.989 -4.064  4.733   0.66 17.94 ?  125 PRO   A HA   1 
ATOM   2706 H  HA   B PRO   A 1 125 ? 17.232 -4.248  4.544   0.34 15.77 ?  125 PRO   A HA   1 
ATOM   2707 H  HB2  A PRO   A 1 125 ? 17.870 -2.613  2.858   0.66 18.97 ?  125 PRO   A HB2  1 
ATOM   2708 H  HB2  B PRO   A 1 125 ? 18.153 -2.769  2.719   0.34 15.32 ?  125 PRO   A HB2  1 
ATOM   2709 H  HB3  A PRO   A 1 125 ? 17.995 -2.016  4.339   0.66 18.97 ?  125 PRO   A HB3  1 
ATOM   2710 H  HB3  B PRO   A 1 125 ? 18.313 -2.259  4.229   0.34 15.32 ?  125 PRO   A HB3  1 
ATOM   2711 H  HG2  A PRO   A 1 125 ? 20.018 -3.310  2.845   0.66 19.50 ?  125 PRO   A HG2  1 
ATOM   2712 H  HG2  B PRO   A 1 125 ? 20.267 -3.541  2.643   0.34 14.35 ?  125 PRO   A HG2  1 
ATOM   2713 H  HG3  A PRO   A 1 125 ? 20.160 -1.948  3.665   0.66 19.50 ?  125 PRO   A HG3  1 
ATOM   2714 H  HG3  B PRO   A 1 125 ? 20.475 -2.253  3.561   0.34 14.35 ?  125 PRO   A HG3  1 
ATOM   2715 H  HD2  A PRO   A 1 125 ? 20.873 -4.259  4.665   0.66 18.26 ?  125 PRO   A HD2  1 
ATOM   2716 H  HD2  B PRO   A 1 125 ? 21.084 -4.679  4.367   0.34 14.04 ?  125 PRO   A HD2  1 
ATOM   2717 H  HD3  A PRO   A 1 125 ? 20.464 -3.015  5.591   0.66 18.26 ?  125 PRO   A HD3  1 
ATOM   2718 H  HD3  B PRO   A 1 125 ? 20.778 -3.479  5.387   0.34 14.04 ?  125 PRO   A HD3  1 
ATOM   2719 N  N    A LEU   A 1 126 ? 16.925 -5.204  2.397   0.66 15.80 ?  126 LEU   A N    1 
ATOM   2720 N  N    B LEU   A 1 126 ? 16.965 -5.192  2.142   0.34 14.69 ?  126 LEU   A N    1 
ATOM   2721 C  CA   A LEU   A 1 126 ? 16.973 -6.054  1.215   0.66 15.50 ?  126 LEU   A CA   1 
ATOM   2722 C  CA   B LEU   A 1 126 ? 16.851 -5.947  0.899   0.34 14.90 ?  126 LEU   A CA   1 
ATOM   2723 C  C    A LEU   A 1 126 ? 17.922 -5.451  0.189   0.66 15.51 ?  126 LEU   A C    1 
ATOM   2724 C  C    B LEU   A 1 126 ? 17.798 -5.348  -0.131  0.34 14.32 ?  126 LEU   A C    1 
ATOM   2725 O  O    A LEU   A 1 126 ? 17.744 -4.305  -0.231  0.66 15.79 ?  126 LEU   A O    1 
ATOM   2726 O  O    B LEU   A 1 126 ? 17.510 -4.314  -0.738  0.34 13.47 ?  126 LEU   A O    1 
ATOM   2727 C  CB   A LEU   A 1 126 ? 15.581 -6.241  0.618   0.66 15.51 ?  126 LEU   A CB   1 
ATOM   2728 C  CB   B LEU   A 1 126 ? 15.415 -5.894  0.403   0.34 15.50 ?  126 LEU   A CB   1 
ATOM   2729 C  CG   A LEU   A 1 126 ? 14.665 -7.227  1.343   0.66 16.20 ?  126 LEU   A CG   1 
ATOM   2730 C  CG   B LEU   A 1 126 ? 14.435 -6.698  1.245   0.34 15.58 ?  126 LEU   A CG   1 
ATOM   2731 C  CD1  A LEU   A 1 126 ? 13.238 -7.101  0.848   0.66 16.78 ?  126 LEU   A CD1  1 
ATOM   2732 C  CD1  B LEU   A 1 126 ? 13.053 -6.528  0.672   0.34 15.69 ?  126 LEU   A CD1  1 
ATOM   2733 C  CD2  A LEU   A 1 126 ? 15.164 -8.659  1.158   0.66 16.57 ?  126 LEU   A CD2  1 
ATOM   2734 C  CD2  B LEU   A 1 126 ? 14.834 -8.161  1.266   0.34 15.76 ?  126 LEU   A CD2  1 
ATOM   2735 H  H    A LEU   A 1 126 ? 16.207 -4.730  2.462   0.66 19.02 ?  126 LEU   A H    1 
ATOM   2736 H  H    B LEU   A 1 126 ? 16.282 -4.696  2.316   0.34 17.68 ?  126 LEU   A H    1 
ATOM   2737 H  HA   A LEU   A 1 126 ? 17.316 -6.916  1.455   0.66 18.65 ?  126 LEU   A HA   1 
ATOM   2738 H  HA   B LEU   A 1 126 ? 17.095 -6.875  1.054   0.34 17.94 ?  126 LEU   A HA   1 
ATOM   2739 H  HB2  A LEU   A 1 126 ? 15.124 -5.384  0.615   0.66 18.67 ?  126 LEU   A HB2  1 
ATOM   2740 H  HB2  B LEU   A 1 126 ? 15.120 -4.970  0.411   0.34 18.65 ?  126 LEU   A HB2  1 
ATOM   2741 H  HB3  A LEU   A 1 126 ? 15.672 -6.555  -0.297  0.66 18.67 ?  126 LEU   A HB3  1 
ATOM   2742 H  HB3  B LEU   A 1 126 ? 15.376 -6.240  -0.500  0.34 18.65 ?  126 LEU   A HB3  1 
ATOM   2743 H  HG   A LEU   A 1 126 ? 14.673 -7.033  2.292   0.66 19.49 ?  126 LEU   A HG   1 
ATOM   2744 H  HG   B LEU   A 1 126 ? 14.432 -6.358  2.158   0.34 18.75 ?  126 LEU   A HG   1 
ATOM   2745 H  HD11 A LEU   A 1 126 ? 12.681 -7.741  1.320   0.66 20.19 ?  126 LEU   A HD11 1 
ATOM   2746 H  HD11 B LEU   A 1 126 ? 12.435 -7.072  1.182   0.34 18.88 ?  126 LEU   A HD11 1 
ATOM   2747 H  HD12 A LEU   A 1 126 ? 12.926 -6.200  1.020   0.66 20.19 ?  126 LEU   A HD12 1 
ATOM   2748 H  HD12 B LEU   A 1 126 ? 12.800 -5.594  0.727   0.34 18.88 ?  126 LEU   A HD12 1 
ATOM   2749 H  HD13 A LEU   A 1 126 ? 13.217 -7.284  -0.105  0.66 20.19 ?  126 LEU   A HD13 1 
ATOM   2750 H  HD13 B LEU   A 1 126 ? 13.064 -6.816  -0.254  0.34 18.88 ?  126 LEU   A HD13 1 
ATOM   2751 H  HD21 A LEU   A 1 126 ? 14.519 -9.273  1.537   0.66 19.94 ?  126 LEU   A HD21 1 
ATOM   2752 H  HD21 B LEU   A 1 126 ? 14.076 -8.690  1.549   0.34 18.97 ?  126 LEU   A HD21 1 
ATOM   2753 H  HD22 A LEU   A 1 126 ? 15.273 -8.835  0.209   0.66 19.94 ?  126 LEU   A HD22 1 
ATOM   2754 H  HD22 B LEU   A 1 126 ? 15.107 -8.419  0.372   0.34 18.97 ?  126 LEU   A HD22 1 
ATOM   2755 H  HD23 A LEU   A 1 126 ? 16.020 -8.756  1.609   0.66 19.94 ?  126 LEU   A HD23 1 
ATOM   2756 H  HD23 B LEU   A 1 126 ? 15.572 -8.276  1.884   0.34 18.97 ?  126 LEU   A HD23 1 
ATOM   2757 N  N    A LEU   A 1 127 ? 18.922 -6.229  -0.219  0.66 15.45 ?  127 LEU   A N    1 
ATOM   2758 N  N    B LEU   A 1 127 ? 18.932 -6.007  -0.341  0.34 13.76 ?  127 LEU   A N    1 
ATOM   2759 C  CA   A LEU   A 1 127 ? 19.918 -5.749  -1.166  0.66 15.34 ?  127 LEU   A CA   1 
ATOM   2760 C  CA   B LEU   A 1 127 ? 19.921 -5.480  -1.269  0.34 13.41 ?  127 LEU   A CA   1 
ATOM   2761 C  C    A LEU   A 1 127 ? 19.290 -5.498  -2.526  0.66 14.80 ?  127 LEU   A C    1 
ATOM   2762 C  C    B LEU   A 1 127 ? 19.371 -5.422  -2.694  0.34 13.43 ?  127 LEU   A C    1 
ATOM   2763 O  O    A LEU   A 1 127 ? 18.424 -6.250  -2.985  0.66 15.91 ?  127 LEU   A O    1 
ATOM   2764 O  O    B LEU   A 1 127 ? 18.590 -6.279  -3.121  0.34 13.99 ?  127 LEU   A O    1 
ATOM   2765 C  CB   A LEU   A 1 127 ? 21.041 -6.775  -1.316  0.66 15.59 ?  127 LEU   A CB   1 
ATOM   2766 C  CB   B LEU   A 1 127 ? 21.188 -6.333  -1.221  0.34 13.95 ?  127 LEU   A CB   1 
ATOM   2767 C  CG   A LEU   A 1 127 ? 21.907 -6.992  -0.077  0.66 15.36 ?  127 LEU   A CG   1 
ATOM   2768 C  CG   B LEU   A 1 127 ? 21.963 -6.339  0.101   0.34 14.48 ?  127 LEU   A CG   1 
ATOM   2769 C  CD1  A LEU   A 1 127 ? 22.997 -8.000  -0.358  0.66 15.95 ?  127 LEU   A CD1  1 
ATOM   2770 C  CD1  B LEU   A 1 127 ? 23.095 -7.346  0.037   0.34 15.16 ?  127 LEU   A CD1  1 
ATOM   2771 C  CD2  A LEU   A 1 127 ? 22.516 -5.684  0.391   0.66 15.80 ?  127 LEU   A CD2  1 
ATOM   2772 C  CD2  B LEU   A 1 127 ? 22.501 -4.951  0.417   0.34 15.34 ?  127 LEU   A CD2  1 
ATOM   2773 H  H    A LEU   A 1 127 ? 19.038 -7.036  0.036   0.66 18.59 ?  127 LEU   A H    1 
ATOM   2774 H  H    B LEU   A 1 127 ? 19.153 -6.742  0.056   0.34 16.56 ?  127 LEU   A H    1 
ATOM   2775 H  HA   A LEU   A 1 127 ? 20.292 -4.919  -0.846  0.66 18.46 ?  127 LEU   A HA   1 
ATOM   2776 H  HA   B LEU   A 1 127 ? 20.153 -4.581  -0.994  0.34 16.15 ?  127 LEU   A HA   1 
ATOM   2777 H  HB2  A LEU   A 1 127 ? 20.644 -7.632  -1.551  0.66 18.77 ?  127 LEU   A HB2  1 
ATOM   2778 H  HB2  B LEU   A 1 127 ? 20.942 -7.249  -1.414  0.34 16.79 ?  127 LEU   A HB2  1 
ATOM   2779 H  HB3  A LEU   A 1 127 ? 21.625 -6.487  -2.036  0.66 18.77 ?  127 LEU   A HB3  1 
ATOM   2780 H  HB3  B LEU   A 1 127 ? 21.787 -6.006  -1.905  0.34 16.79 ?  127 LEU   A HB3  1 
ATOM   2781 H  HG   A LEU   A 1 127 ? 21.352 -7.341  0.636   0.66 18.49 ?  127 LEU   A HG   1 
ATOM   2782 H  HG   B LEU   A 1 127 ? 21.369 -6.603  0.820   0.34 17.43 ?  127 LEU   A HG   1 
ATOM   2783 H  HD11 A LEU   A 1 127 ? 23.477 -8.184  0.467   0.66 19.19 ?  127 LEU   A HD11 1 
ATOM   2784 H  HD11 B LEU   A 1 127 ? 23.612 -7.291  0.855   0.34 18.24 ?  127 LEU   A HD11 1 
ATOM   2785 H  HD12 A LEU   A 1 127 ? 22.594 -8.820  -0.691  0.66 19.19 ?  127 LEU   A HD12 1 
ATOM   2786 H  HD12 B LEU   A 1 127 ? 22.719 -8.235  -0.059  0.34 18.24 ?  127 LEU   A HD12 1 
ATOM   2787 H  HD13 A LEU   A 1 127 ? 23.602 -7.639  -1.021  0.66 19.19 ?  127 LEU   A HD13 1 
ATOM   2788 H  HD13 B LEU   A 1 127 ? 23.657 -7.139  -0.725  0.34 18.24 ?  127 LEU   A HD13 1 
ATOM   2789 H  HD21 A LEU   A 1 127 ? 23.213 -5.875  1.038   0.66 19.01 ?  127 LEU   A HD21 1 
ATOM   2790 H  HD21 B LEU   A 1 127 ? 23.079 -5.005  1.194   0.34 18.46 ?  127 LEU   A HD21 1 
ATOM   2791 H  HD22 A LEU   A 1 127 ? 22.897 -5.222  -0.376  0.66 19.01 ?  127 LEU   A HD22 1 
ATOM   2792 H  HD22 B LEU   A 1 127 ? 23.003 -4.626  -0.347  0.34 18.46 ?  127 LEU   A HD22 1 
ATOM   2793 H  HD23 A LEU   A 1 127 ? 21.826 -5.139  0.794   0.66 19.01 ?  127 LEU   A HD23 1 
ATOM   2794 H  HD23 B LEU   A 1 127 ? 21.756 -4.358  0.600   0.34 18.46 ?  127 LEU   A HD23 1 
ATOM   2795 N  N    A SER   A 1 128 ? 19.742 -4.429  -3.169  0.66 14.29 ?  128 SER   A N    1 
ATOM   2796 N  N    B SER   A 1 128 ? 19.789 -4.384  -3.414  0.34 13.41 ?  128 SER   A N    1 
ATOM   2797 C  CA   A SER   A 1 128 ? 19.330 -4.009  -4.500  0.66 14.11 ?  128 SER   A CA   1 
ATOM   2798 C  CA   B SER   A 1 128 ? 19.461 -4.131  -4.814  0.34 13.28 ?  128 SER   A CA   1 
ATOM   2799 C  C    A SER   A 1 128 ? 17.871 -3.568  -4.569  0.66 14.16 ?  128 SER   A C    1 
ATOM   2800 C  C    B SER   A 1 128 ? 18.036 -3.636  -5.030  0.34 13.60 ?  128 SER   A C    1 
ATOM   2801 O  O    A SER   A 1 128 ? 17.389 -3.262  -5.657  0.66 14.63 ?  128 SER   A O    1 
ATOM   2802 O  O    B SER   A 1 128 ? 17.685 -3.268  -6.155  0.34 13.82 ?  128 SER   A O    1 
ATOM   2803 C  CB   A SER   A 1 128 ? 19.656 -5.048  -5.580  0.66 14.21 ?  128 SER   A CB   1 
ATOM   2804 C  CB   B SER   A 1 128 ? 19.762 -5.333  -5.712  0.34 13.94 ?  128 SER   A CB   1 
ATOM   2805 O  OG   A SER   A 1 128 ? 21.064 -5.235  -5.676  0.66 14.87 ?  128 SER   A OG   1 
ATOM   2806 O  OG   B SER   A 1 128 ? 21.160 -5.551  -5.801  0.34 14.49 ?  128 SER   A OG   1 
ATOM   2807 H  H    A SER   A 1 128 ? 20.341 -3.898  -2.833  0.66 17.20 ?  128 SER   A H    1 
ATOM   2808 H  H    B SER   A 1 128 ? 20.305 -3.784  -3.081  0.34 16.15 ?  128 SER   A H    1 
ATOM   2809 H  HA   A SER   A 1 128 ? 19.854 -3.227  -4.723  0.66 16.99 ?  128 SER   A HA   1 
ATOM   2810 H  HA   B SER   A 1 128 ? 20.033 -3.414  -5.103  0.34 16.00 ?  128 SER   A HA   1 
ATOM   2811 H  HB2  A SER   A 1 128 ? 19.234 -5.891  -5.348  0.66 17.11 ?  128 SER   A HB2  1 
ATOM   2812 H  HB2  B SER   A 1 128 ? 19.327 -6.117  -5.355  0.34 16.78 ?  128 SER   A HB2  1 
ATOM   2813 H  HB3  A SER   A 1 128 ? 19.322 -4.734  -6.435  0.66 17.11 ?  128 SER   A HB3  1 
ATOM   2814 H  HB3  B SER   A 1 128 ? 19.421 -5.136  -6.601  0.34 16.78 ?  128 SER   A HB3  1 
ATOM   2815 H  HG   A SER   A 1 128 ? 21.437 -4.512  -5.867  0.66 17.89 ?  128 SER   A HG   1 
ATOM   2816 H  HG   B SER   A 1 128 ? 21.533 -4.860  -6.091  0.34 17.45 ?  128 SER   A HG   1 
ATOM   2817 N  N    A ALA   A 1 129 ? 17.166 -3.505  -3.442  0.66 14.22 ?  129 ALA   A N    1 
ATOM   2818 N  N    B ALA   A 1 129 ? 17.224 -3.608  -3.973  0.34 13.58 ?  129 ALA   A N    1 
ATOM   2819 C  CA   A ALA   A 1 129 ? 15.803 -2.994  -3.434  0.66 14.63 ?  129 ALA   A CA   1 
ATOM   2820 C  CA   B ALA   A 1 129 ? 15.855 -3.122  -4.069  0.34 13.95 ?  129 ALA   A CA   1 
ATOM   2821 C  C    A ALA   A 1 129 ? 15.824 -1.463  -3.457  0.66 15.64 ?  129 ALA   A C    1 
ATOM   2822 C  C    B ALA   A 1 129 ? 15.804 -1.631  -3.718  0.34 14.65 ?  129 ALA   A C    1 
ATOM   2823 O  O    A ALA   A 1 129 ? 16.883 -0.832  -3.534  0.66 16.28 ?  129 ALA   A O    1 
ATOM   2824 O  O    B ALA   A 1 129 ? 16.833 -0.950  -3.667  0.34 14.85 ?  129 ALA   A O    1 
ATOM   2825 C  CB   A ALA   A 1 129 ? 15.029 -3.568  -2.246  0.66 14.56 ?  129 ALA   A CB   1 
ATOM   2826 C  CB   B ALA   A 1 129 ? 14.931 -4.015  -3.241  0.34 14.12 ?  129 ALA   A CB   1 
ATOM   2827 H  H    A ALA   A 1 129 ? 17.457 -3.743  -2.670  0.66 17.12 ?  129 ALA   A H    1 
ATOM   2828 H  H    B ALA   A 1 129 ? 17.443 -3.880  -3.178  0.34 16.35 ?  129 ALA   A H    1 
ATOM   2829 H  HA   A ALA   A 1 129 ? 15.358 -3.288  -4.239  0.66 17.62 ?  129 ALA   A HA   1 
ATOM   2830 H  HA   B ALA   A 1 129 ? 15.570 -3.206  -4.983  0.34 16.80 ?  129 ALA   A HA   1 
ATOM   2831 H  HB1  A ALA   A 1 129 ? 14.126 -3.217  -2.259  0.66 17.53 ?  129 ALA   A HB1  1 
ATOM   2832 H  HB1  B ALA   A 1 129 ? 14.052 -3.603  -3.180  0.34 17.00 ?  129 ALA   A HB1  1 
ATOM   2833 H  HB2  A ALA   A 1 129 ? 15.013 -4.534  -2.321  0.66 17.53 ?  129 ALA   A HB2  1 
ATOM   2834 H  HB2  B ALA   A 1 129 ? 14.851 -4.876  -3.678  0.34 17.00 ?  129 ALA   A HB2  1 
ATOM   2835 H  HB3  A ALA   A 1 129 ? 15.475 -3.307  -1.424  0.66 17.53 ?  129 ALA   A HB3  1 
ATOM   2836 H  HB3  B ALA   A 1 129 ? 15.312 -4.141  -2.354  0.34 17.00 ?  129 ALA   A HB3  1 
ATOM   2837 N  N    A GLY   A 1 130 ? 14.643 -0.854  -3.415  0.66 16.65 ?  130 GLY   A N    1 
ATOM   2838 N  N    B GLY   A 1 130 ? 14.603 -1.103  -3.492  0.34 15.19 ?  130 GLY   A N    1 
ATOM   2839 C  CA   A GLY   A 1 130 ? 14.582 0.600   -3.437  0.66 17.50 ?  130 GLY   A CA   1 
ATOM   2840 C  CA   B GLY   A 1 130 ? 14.465 0.323   -3.239  0.34 15.30 ?  130 GLY   A CA   1 
ATOM   2841 C  C    A GLY   A 1 130 ? 15.226 1.167   -4.688  0.66 16.80 ?  130 GLY   A C    1 
ATOM   2842 C  C    B GLY   A 1 130 ? 14.991 1.128   -4.405  0.34 14.81 ?  130 GLY   A C    1 
ATOM   2843 O  O    A GLY   A 1 130 ? 14.984 0.700   -5.807  0.66 17.58 ?  130 GLY   A O    1 
ATOM   2844 O  O    B GLY   A 1 130 ? 14.764 0.795   -5.573  0.34 14.83 ?  130 GLY   A O    1 
ATOM   2845 H  H    A GLY   A 1 130 ? 13.876 -1.248  -3.370  0.66 20.04 ?  130 GLY   A H    1 
ATOM   2846 H  H    B GLY   A 1 130 ? 13.864 -1.546  -3.486  0.34 18.28 ?  130 GLY   A H    1 
ATOM   2847 H  HA2  A GLY   A 1 130 ? 13.656 0.889   -3.406  0.66 21.06 ?  130 GLY   A HA2  1 
ATOM   2848 H  HA2  B GLY   A 1 130 ? 13.530 0.541   -3.068  0.34 18.41 ?  130 GLY   A HA2  1 
ATOM   2849 H  HA3  A GLY   A 1 130 ? 15.043 0.957   -2.663  0.66 21.06 ?  130 GLY   A HA3  1 
ATOM   2850 H  HA3  B GLY   A 1 130 ? 14.991 0.586   -2.469  0.34 18.41 ?  130 GLY   A HA3  1 
ATOM   2851 N  N    A ILE   A 1 131 ? 16.071 2.188   -4.497  0.66 15.37 ?  131 ILE   A N    1 
ATOM   2852 N  N    B ILE   A 1 131 ? 15.721 2.202   -4.088  0.34 14.62 ?  131 ILE   A N    1 
ATOM   2853 C  CA   A ILE   A 1 131 ? 16.627 2.943   -5.620  0.66 14.88 ?  131 ILE   A CA   1 
ATOM   2854 C  CA   B ILE   A 1 131 ? 16.276 3.068   -5.120  0.34 14.50 ?  131 ILE   A CA   1 
ATOM   2855 C  C    A ILE   A 1 131 ? 17.616 2.149   -6.458  0.66 14.68 ?  131 ILE   A C    1 
ATOM   2856 C  C    B ILE   A 1 131 ? 17.317 2.362   -5.981  0.34 13.84 ?  131 ILE   A C    1 
ATOM   2857 O  O    A ILE   A 1 131 ? 18.019 2.628   -7.525  0.66 14.91 ?  131 ILE   A O    1 
ATOM   2858 O  O    B ILE   A 1 131 ? 17.745 2.915   -6.997  0.34 13.59 ?  131 ILE   A O    1 
ATOM   2859 C  CB   A ILE   A 1 131 ? 17.235 4.294   -5.185  0.66 15.71 ?  131 ILE   A CB   1 
ATOM   2860 C  CB   B ILE   A 1 131 ? 16.830 4.388   -4.528  0.34 15.41 ?  131 ILE   A CB   1 
ATOM   2861 C  CG1  A ILE   A 1 131 ? 18.495 4.098   -4.340  0.66 17.35 ?  131 ILE   A CG1  1 
ATOM   2862 C  CG1  B ILE   A 1 131 ? 18.062 4.133   -3.652  0.34 15.87 ?  131 ILE   A CG1  1 
ATOM   2863 C  CG2  A ILE   A 1 131 ? 16.210 5.112   -4.418  0.66 16.20 ?  131 ILE   A CG2  1 
ATOM   2864 C  CG2  B ILE   A 1 131 ? 15.744 5.124   -3.746  0.34 15.89 ?  131 ILE   A CG2  1 
ATOM   2865 C  CD1  A ILE   A 1 131 ? 19.142 5.417   -3.919  0.66 18.63 ?  131 ILE   A CD1  1 
ATOM   2866 C  CD1  B ILE   A 1 131 ? 18.755 5.410   -3.177  0.34 16.22 ?  131 ILE   A CD1  1 
ATOM   2867 H  H    A ILE   A 1 131 ? 16.331 2.463   -3.725  0.66 18.50 ?  131 ILE   A H    1 
ATOM   2868 H  H    B ILE   A 1 131 ? 15.897 2.451   -3.283  0.34 17.59 ?  131 ILE   A H    1 
ATOM   2869 H  HA   A ILE   A 1 131 ? 15.900 3.149   -6.216  0.66 17.92 ?  131 ILE   A HA   1 
ATOM   2870 H  HA   B ILE   A 1 131 ? 15.547 3.320   -5.707  0.34 17.46 ?  131 ILE   A HA   1 
ATOM   2871 H  HB   A ILE   A 1 131 ? 17.477 4.787   -5.984  0.66 18.91 ?  131 ILE   A HB   1 
ATOM   2872 H  HB   B ILE   A 1 131 ? 17.098 4.957   -5.264  0.34 18.54 ?  131 ILE   A HB   1 
ATOM   2873 H  HG12 A ILE   A 1 131 ? 18.263 3.608   -3.535  0.66 20.87 ?  131 ILE   A HG12 1 
ATOM   2874 H  HG12 B ILE   A 1 131 ? 17.791 3.633   -2.868  0.34 19.10 ?  131 ILE   A HG12 1 
ATOM   2875 H  HG13 A ILE   A 1 131 ? 19.151 3.601   -4.853  0.66 20.87 ?  131 ILE   A HG13 1 
ATOM   2876 H  HG13 B ILE   A 1 131 ? 18.710 3.623   -4.161  0.34 19.10 ?  131 ILE   A HG13 1 
ATOM   2877 H  HG21 A ILE   A 1 131 ? 16.524 6.025   -4.345  0.66 19.49 ?  131 ILE   A HG21 1 
ATOM   2878 H  HG21 B ILE   A 1 131 ? 16.068 6.007   -3.507  0.34 19.13 ?  131 ILE   A HG21 1 
ATOM   2879 H  HG22 A ILE   A 1 131 ? 15.368 5.086   -4.895  0.66 19.49 ?  131 ILE   A HG22 1 
ATOM   2880 H  HG22 B ILE   A 1 131 ? 14.954 5.203   -4.304  0.34 19.13 ?  131 ILE   A HG22 1 
ATOM   2881 H  HG23 A ILE   A 1 131 ? 16.101 4.726   -3.533  0.66 19.49 ?  131 ILE   A HG23 1 
ATOM   2882 H  HG23 B ILE   A 1 131 ? 15.534 4.620   -2.945  0.34 19.13 ?  131 ILE   A HG23 1 
ATOM   2883 H  HD11 A ILE   A 1 131 ? 20.013 5.234   -3.536  0.66 22.42 ?  131 ILE   A HD11 1 
ATOM   2884 H  HD11 B ILE   A 1 131 ? 19.575 5.170   -2.717  0.34 19.52 ?  131 ILE   A HD11 1 
ATOM   2885 H  HD12 A ILE   A 1 131 ? 19.236 5.985   -4.700  0.66 22.42 ?  131 ILE   A HD12 1 
ATOM   2886 H  HD12 B ILE   A 1 131 ? 18.959 5.964   -3.947  0.34 19.52 ?  131 ILE   A HD12 1 
ATOM   2887 H  HD13 A ILE   A 1 131 ? 18.576 5.853   -3.261  0.66 22.42 ?  131 ILE   A HD13 1 
ATOM   2888 H  HD13 B ILE   A 1 131 ? 18.164 5.886   -2.573  0.34 19.52 ?  131 ILE   A HD13 1 
ATOM   2889 N  N    A PHE   A 1 132 ? 18.020 0.956   -6.009  0.66 14.74 ?  132 PHE   A N    1 
ATOM   2890 N  N    B PHE   A 1 132 ? 17.734 1.148   -5.609  0.34 13.91 ?  132 PHE   A N    1 
ATOM   2891 C  CA   A PHE   A 1 132 ? 18.881 0.102   -6.819  0.66 15.18 ?  132 PHE   A CA   1 
ATOM   2892 C  CA   B PHE   A 1 132 ? 18.653 0.385   -6.445  0.34 14.26 ?  132 PHE   A CA   1 
ATOM   2893 C  C    A PHE   A 1 132 ? 18.108 -0.663  -7.891  0.66 16.44 ?  132 PHE   A C    1 
ATOM   2894 C  C    B PHE   A 1 132 ? 17.965 -0.312  -7.618  0.34 14.93 ?  132 PHE   A C    1 
ATOM   2895 O  O    A PHE   A 1 132 ? 18.730 -1.311  -8.739  0.66 17.32 ?  132 PHE   A O    1 
ATOM   2896 O  O    B PHE   A 1 132 ? 18.656 -0.779  -8.529  0.34 15.25 ?  132 PHE   A O    1 
ATOM   2897 C  CB   A PHE   A 1 132 ? 19.674 -0.867  -5.932  0.66 14.05 ?  132 PHE   A CB   1 
ATOM   2898 C  CB   B PHE   A 1 132 ? 19.441 -0.627  -5.606  0.34 13.75 ?  132 PHE   A CB   1 
ATOM   2899 C  CG   A PHE   A 1 132 ? 20.891 -0.255  -5.269  0.66 14.21 ?  132 PHE   A CG   1 
ATOM   2900 C  CG   B PHE   A 1 132 ? 20.688 -0.059  -4.967  0.34 13.80 ?  132 PHE   A CG   1 
ATOM   2901 C  CD1  A PHE   A 1 132 ? 20.771 0.780   -4.358  0.66 14.94 ?  132 PHE   A CD1  1 
ATOM   2902 C  CD1  B PHE   A 1 132 ? 20.603 0.893   -3.964  0.34 14.55 ?  132 PHE   A CD1  1 
ATOM   2903 C  CD2  A PHE   A 1 132 ? 22.153 -0.766  -5.524  0.66 15.27 ?  132 PHE   A CD2  1 
ATOM   2904 C  CD2  B PHE   A 1 132 ? 21.941 -0.499  -5.359  0.34 13.64 ?  132 PHE   A CD2  1 
ATOM   2905 C  CE1  A PHE   A 1 132 ? 21.897 1.319   -3.744  0.66 15.90 ?  132 PHE   A CE1  1 
ATOM   2906 C  CE1  B PHE   A 1 132 ? 21.748 1.409   -3.375  0.34 14.76 ?  132 PHE   A CE1  1 
ATOM   2907 C  CE2  A PHE   A 1 132 ? 23.272 -0.243  -4.911  0.66 15.97 ?  132 PHE   A CE2  1 
ATOM   2908 C  CE2  B PHE   A 1 132 ? 23.088 0.009   -4.772  0.34 14.27 ?  132 PHE   A CE2  1 
ATOM   2909 C  CZ   A PHE   A 1 132 ? 23.143 0.803   -4.020  0.66 15.82 ?  132 PHE   A CZ   1 
ATOM   2910 C  CZ   B PHE   A 1 132 ? 22.989 0.964   -3.778  0.34 14.52 ?  132 PHE   A CZ   1 
ATOM   2911 H  H    A PHE   A 1 132 ? 17.803 0.619   -5.242  0.66 17.75 ?  132 PHE   A H    1 
ATOM   2912 H  H    B PHE   A 1 132 ? 17.501 0.753   -4.884  0.34 16.75 ?  132 PHE   A H    1 
ATOM   2913 H  HA   A PHE   A 1 132 ? 19.527 0.666   -7.266  0.66 18.27 ?  132 PHE   A HA   1 
ATOM   2914 H  HA   B PHE   A 1 132 ? 19.295 1.006   -6.817  0.34 17.17 ?  132 PHE   A HA   1 
ATOM   2915 H  HB2  A PHE   A 1 132 ? 19.094 -1.192  -5.227  0.66 16.91 ?  132 PHE   A HB2  1 
ATOM   2916 H  HB2  B PHE   A 1 132 ? 18.869 -0.956  -4.897  0.34 16.56 ?  132 PHE   A HB2  1 
ATOM   2917 H  HB3  A PHE   A 1 132 ? 19.981 -1.611  -6.474  0.66 16.91 ?  132 PHE   A HB3  1 
ATOM   2918 H  HB3  B PHE   A 1 132 ? 19.708 -1.360  -6.181  0.34 16.56 ?  132 PHE   A HB3  1 
ATOM   2919 H  HD1  A PHE   A 1 132 ? 19.933 1.135   -4.162  0.66 17.99 ?  132 PHE   A HD1  1 
ATOM   2920 H  HD1  B PHE   A 1 132 ? 19.767 1.198   -3.690  0.34 17.51 ?  132 PHE   A HD1  1 
ATOM   2921 H  HD2  A PHE   A 1 132 ? 22.249 -1.472  -6.122  0.66 18.38 ?  132 PHE   A HD2  1 
ATOM   2922 H  HD2  B PHE   A 1 132 ? 22.012 -1.141  -6.030  0.34 16.42 ?  132 PHE   A HD2  1 
ATOM   2923 H  HE1  A PHE   A 1 132 ? 21.810 2.022   -3.136  0.66 19.14 ?  132 PHE   A HE1  1 
ATOM   2924 H  HE1  B PHE   A 1 132 ? 21.679 2.051   -2.706  0.34 17.77 ?  132 PHE   A HE1  1 
ATOM   2925 H  HE2  A PHE   A 1 132 ? 24.113 -0.591  -5.102  0.66 19.22 ?  132 PHE   A HE2  1 
ATOM   2926 H  HE2  B PHE   A 1 132 ? 23.924 -0.292  -5.050  0.34 17.18 ?  132 PHE   A HE2  1 
ATOM   2927 H  HZ   A PHE   A 1 132 ? 23.897 1.161   -3.607  0.66 19.04 ?  132 PHE   A HZ   1 
ATOM   2928 H  HZ   B PHE   A 1 132 ? 23.760 1.307   -3.386  0.34 17.48 ?  132 PHE   A HZ   1 
ATOM   2929 N  N    A GLY   A 1 133 ? 16.775 -0.614  -7.869  0.66 17.12 ?  133 GLY   A N    1 
ATOM   2930 N  N    B GLY   A 1 133 ? 16.637 -0.410  -7.627  0.34 15.38 ?  133 GLY   A N    1 
ATOM   2931 C  CA   A GLY   A 1 133 ? 15.983 -0.984  -9.021  0.66 17.83 ?  133 GLY   A CA   1 
ATOM   2932 C  CA   B GLY   A 1 133 ? 15.906 -0.716  -8.838  0.34 16.14 ?  133 GLY   A CA   1 
ATOM   2933 C  C    A GLY   A 1 133 ? 15.614 -2.445  -9.171  0.66 17.74 ?  133 GLY   A C    1 
ATOM   2934 C  C    B GLY   A 1 133 ? 15.506 -2.160  -9.056  0.34 16.24 ?  133 GLY   A C    1 
ATOM   2935 O  O    A GLY   A 1 133 ? 14.948 -2.787  -10.156 0.66 18.95 ?  133 GLY   A O    1 
ATOM   2936 O  O    B GLY   A 1 133 ? 14.764 -2.425  -10.009 0.34 16.39 ?  133 GLY   A O    1 
ATOM   2937 H  H    A GLY   A 1 133 ? 16.311 -0.370  -7.183  0.66 20.60 ?  133 GLY   A H    1 
ATOM   2938 H  H    B GLY   A 1 133 ? 16.139 -0.303  -6.938  0.34 18.51 ?  133 GLY   A H    1 
ATOM   2939 H  HA2  A GLY   A 1 133 ? 15.160 -0.475  -8.999  0.66 21.46 ?  133 GLY   A HA2  1 
ATOM   2940 H  HA2  B GLY   A 1 133 ? 15.088 -0.209  -8.843  0.34 19.43 ?  133 GLY   A HA2  1 
ATOM   2941 H  HA3  A GLY   A 1 133 ? 16.469 -0.730  -9.818  0.66 21.46 ?  133 GLY   A HA3  1 
ATOM   2942 H  HA3  B GLY   A 1 133 ? 16.433 -0.440  -9.607  0.34 19.43 ?  133 GLY   A HA3  1 
ATOM   2943 N  N    A ALA   A 1 134 ? 16.014 -3.317  -8.250  0.66 16.92 ?  134 ALA   A N    1 
ATOM   2944 N  N    B ALA   A 1 134 ? 15.956 -3.100  -8.229  0.34 16.57 ?  134 ALA   A N    1 
ATOM   2945 C  CA   A ALA   A 1 134 ? 15.665 -4.724  -8.379  0.66 16.91 ?  134 ALA   A CA   1 
ATOM   2946 C  CA   B ALA   A 1 134 ? 15.604 -4.493  -8.463  0.34 16.92 ?  134 ALA   A CA   1 
ATOM   2947 C  C    A ALA   A 1 134 ? 14.293 -5.007  -7.765  0.66 17.79 ?  134 ALA   A C    1 
ATOM   2948 C  C    B ALA   A 1 134 ? 14.297 -4.860  -7.761  0.34 17.27 ?  134 ALA   A C    1 
ATOM   2949 O  O    A ALA   A 1 134 ? 13.732 -4.205  -7.014  0.66 18.96 ?  134 ALA   A O    1 
ATOM   2950 O  O    B ALA   A 1 134 ? 13.805 -4.153  -6.877  0.34 17.70 ?  134 ALA   A O    1 
ATOM   2951 C  CB   A ALA   A 1 134 ? 16.731 -5.609  -7.734  0.66 17.26 ?  134 ALA   A CB   1 
ATOM   2952 C  CB   B ALA   A 1 134 ? 16.726 -5.434  -8.025  0.34 17.37 ?  134 ALA   A CB   1 
ATOM   2953 H  H    A ALA   A 1 134 ? 16.486 -3.122  -7.553  0.66 20.35 ?  134 ALA   A H    1 
ATOM   2954 H  H    B ALA   A 1 134 ? 16.454 -2.958  -7.542  0.34 19.94 ?  134 ALA   A H    1 
ATOM   2955 H  HA   A ALA   A 1 134 ? 15.621 -4.949  -9.321  0.66 20.34 ?  134 ALA   A HA   1 
ATOM   2956 H  HA   B ALA   A 1 134 ? 15.476 -4.618  -9.416  0.34 20.36 ?  134 ALA   A HA   1 
ATOM   2957 H  HB1  A ALA   A 1 134 ? 16.484 -6.537  -7.853  0.66 20.76 ?  134 ALA   A HB1  1 
ATOM   2958 H  HB1  B ALA   A 1 134 ? 16.468 -6.346  -8.237  0.34 20.90 ?  134 ALA   A HB1  1 
ATOM   2959 H  HB2  A ALA   A 1 134 ? 17.585 -5.436  -8.166  0.66 20.76 ?  134 ALA   A HB2  1 
ATOM   2960 H  HB2  B ALA   A 1 134 ? 17.536 -5.201  -8.502  0.34 20.90 ?  134 ALA   A HB2  1 
ATOM   2961 H  HB3  A ALA   A 1 134 ? 16.791 -5.396  -6.791  0.66 20.76 ?  134 ALA   A HB3  1 
ATOM   2962 H  HB3  B ALA   A 1 134 ? 16.862 -5.342  -7.071  0.34 20.90 ?  134 ALA   A HB3  1 
ATOM   2963 N  N    A ASP   A 1 135 ? 13.759 -6.183  -8.097  0.66 18.37 ?  135 ASP   A N    1 
ATOM   2964 N  N    B ASP   A 1 135 ? 13.745 -5.997  -8.168  0.34 17.91 ?  135 ASP   A N    1 
ATOM   2965 C  CA   A ASP   A 1 135 ? 12.496 -6.644  -7.532  0.66 18.97 ?  135 ASP   A CA   1 
ATOM   2966 C  CA   B ASP   A 1 135 ? 12.489 -6.501  -7.626  0.34 18.43 ?  135 ASP   A CA   1 
ATOM   2967 C  C    A ASP   A 1 135 ? 12.735 -7.103  -6.098  0.66 18.27 ?  135 ASP   A C    1 
ATOM   2968 C  C    B ASP   A 1 135 ? 12.689 -6.917  -6.174  0.34 18.05 ?  135 ASP   A C    1 
ATOM   2969 O  O    A ASP   A 1 135 ? 13.516 -8.036  -5.884  0.66 18.48 ?  135 ASP   A O    1 
ATOM   2970 O  O    B ASP   A 1 135 ? 13.446 -7.861  -5.909  0.34 17.92 ?  135 ASP   A O    1 
ATOM   2971 C  CB   A ASP   A 1 135 ? 11.964 -7.810  -8.368  0.66 21.31 ?  135 ASP   A CB   1 
ATOM   2972 C  CB   B ASP   A 1 135 ? 12.062 -7.704  -8.459  0.34 19.80 ?  135 ASP   A CB   1 
ATOM   2973 C  CG   A ASP   A 1 135 ? 10.628 -8.360  -7.858  0.66 23.49 ?  135 ASP   A CG   1 
ATOM   2974 C  CG   B ASP   A 1 135 ? 10.867 -8.437  -7.873  0.34 21.15 ?  135 ASP   A CG   1 
ATOM   2975 O  OD1  A ASP   A 1 135 ? 10.187 -7.978  -6.752  0.66 23.52 ?  135 ASP   A OD1  1 
ATOM   2976 O  OD1  B ASP   A 1 135 ? 10.065 -7.804  -7.153  0.34 21.73 ?  135 ASP   A OD1  1 
ATOM   2977 O  OD2  A ASP   A 1 135 ? 10.014 -9.176  -8.580  0.66 25.34 -1 135 ASP   A OD2  1 
ATOM   2978 O  OD2  B ASP   A 1 135 ? 10.746 -9.657  -8.122  0.34 21.66 -1 135 ASP   A OD2  1 
ATOM   2979 H  H    A ASP   A 1 135 ? 14.114 -6.735  -8.652  0.66 22.09 ?  135 ASP   A H    1 
ATOM   2980 H  H    B ASP   A 1 135 ? 14.084 -6.504  -8.770  0.34 21.54 ?  135 ASP   A H    1 
ATOM   2981 H  HA   A ASP   A 1 135 ? 11.845 -5.927  -7.552  0.66 22.81 ?  135 ASP   A HA   1 
ATOM   2982 H  HA   B ASP   A 1 135 ? 11.801 -5.816  -7.689  0.34 22.17 ?  135 ASP   A HA   1 
ATOM   2983 H  HB2  A ASP   A 1 135 ? 11.829 -7.507  -9.281  0.66 25.63 ?  135 ASP   A HB2  1 
ATOM   2984 H  HB2  B ASP   A 1 135 ? 11.852 -7.400  -9.361  0.34 23.82 ?  135 ASP   A HB2  1 
ATOM   2985 H  HB3  A ASP   A 1 135 ? 12.619 -8.529  -8.356  0.66 25.63 ?  135 ASP   A HB3  1 
ATOM   2986 H  HB3  B ASP   A 1 135 ? 12.792 -8.339  -8.490  0.34 23.82 ?  135 ASP   A HB3  1 
ATOM   2987 N  N    A PRO   A 1 136 ? 12.107 -6.481  -5.097  0.66 17.86 ?  136 PRO   A N    1 
ATOM   2988 N  N    B PRO   A 1 136 ? 12.040 -6.261  -5.209  0.34 18.11 ?  136 PRO   A N    1 
ATOM   2989 C  CA   A PRO   A 1 136 ? 12.352 -6.910  -3.710  0.66 18.12 ?  136 PRO   A CA   1 
ATOM   2990 C  CA   B PRO   A 1 136 ? 12.277 -6.612  -3.798  0.34 18.15 ?  136 PRO   A CA   1 
ATOM   2991 C  C    A PRO   A 1 136 ? 11.917 -8.333  -3.415  0.66 17.77 ?  136 PRO   A C    1 
ATOM   2992 C  C    B PRO   A 1 136 ? 11.852 -8.026  -3.435  0.34 17.89 ?  136 PRO   A C    1 
ATOM   2993 O  O    A PRO   A 1 136 ? 12.500 -8.972  -2.534  0.66 17.76 ?  136 PRO   A O    1 
ATOM   2994 O  O    B PRO   A 1 136 ? 12.438 -8.623  -2.524  0.34 17.54 ?  136 PRO   A O    1 
ATOM   2995 C  CB   A PRO   A 1 136 ? 11.564 -5.888  -2.880  0.66 18.98 ?  136 PRO   A CB   1 
ATOM   2996 C  CB   B PRO   A 1 136 ? 11.476 -5.547  -3.034  0.34 18.60 ?  136 PRO   A CB   1 
ATOM   2997 C  CG   A PRO   A 1 136 ? 10.535 -5.345  -3.817  0.66 19.79 ?  136 PRO   A CG   1 
ATOM   2998 C  CG   B PRO   A 1 136 ? 10.419 -5.110  -4.002  0.34 18.90 ?  136 PRO   A CG   1 
ATOM   2999 C  CD   A PRO   A 1 136 ? 11.177 -5.341  -5.168  0.66 18.74 ?  136 PRO   A CD   1 
ATOM   3000 C  CD   B PRO   A 1 136 ? 11.053 -5.177  -5.354  0.34 18.53 ?  136 PRO   A CD   1 
ATOM   3001 H  HA   A PRO   A 1 136 ? 13.295 -6.829  -3.500  0.66 21.80 ?  136 PRO   A HA   1 
ATOM   3002 H  HA   B PRO   A 1 136 ? 13.217 -6.508  -3.580  0.34 21.84 ?  136 PRO   A HA   1 
ATOM   3003 H  HB2  A PRO   A 1 136 ? 11.144 -6.335  -2.128  0.66 22.83 ?  136 PRO   A HB2  1 
ATOM   3004 H  HB2  B PRO   A 1 136 ? 11.078 -5.935  -2.240  0.34 22.37 ?  136 PRO   A HB2  1 
ATOM   3005 H  HB3  A PRO   A 1 136 ? 12.162 -5.190  -2.576  0.66 22.83 ?  136 PRO   A HB3  1 
ATOM   3006 H  HB3  B PRO   A 1 136 ? 12.057 -4.802  -2.799  0.34 22.37 ?  136 PRO   A HB3  1 
ATOM   3007 H  HG2  A PRO   A 1 136 ? 9.754  -5.918  -3.815  0.66 23.80 ?  136 PRO   A HG2  1 
ATOM   3008 H  HG2  B PRO   A 1 136 ? 9.665  -5.716  -3.952  0.34 22.73 ?  136 PRO   A HG2  1 
ATOM   3009 H  HG3  A PRO   A 1 136 ? 10.300 -4.442  -3.553  0.66 23.80 ?  136 PRO   A HG3  1 
ATOM   3010 H  HG3  B PRO   A 1 136 ? 10.147 -4.203  -3.801  0.34 22.73 ?  136 PRO   A HG3  1 
ATOM   3011 H  HD2  A PRO   A 1 136 ? 10.511 -5.492  -5.860  0.66 22.54 ?  136 PRO   A HD2  1 
ATOM   3012 H  HD2  B PRO   A 1 136 ? 10.392 -5.410  -6.026  0.34 22.29 ?  136 PRO   A HD2  1 
ATOM   3013 H  HD3  A PRO   A 1 136 ? 11.663 -4.514  -5.318  0.66 22.54 ?  136 PRO   A HD3  1 
ATOM   3014 H  HD3  B PRO   A 1 136 ? 11.499 -4.341  -5.567  0.34 22.29 ?  136 PRO   A HD3  1 
ATOM   3015 N  N    A ILE   A 1 137 ? 10.880 -8.838  -4.089  0.66 17.78 ?  137 ILE   A N    1 
ATOM   3016 N  N    B ILE   A 1 137 ? 10.843 -8.580  -4.111  0.34 17.95 ?  137 ILE   A N    1 
ATOM   3017 C  CA   A ILE   A 1 137 ? 10.509 -10.243 -3.921  0.66 17.95 ?  137 ILE   A CA   1 
ATOM   3018 C  CA   B ILE   A 1 137 ? 10.456 -9.968  -3.866  0.34 18.25 ?  137 ILE   A CA   1 
ATOM   3019 C  C    A ILE   A 1 137 ? 11.661 -11.141 -4.346  0.66 18.16 ?  137 ILE   A C    1 
ATOM   3020 C  C    B ILE   A 1 137 ? 11.624 -10.894 -4.177  0.34 18.04 ?  137 ILE   A C    1 
ATOM   3021 O  O    A ILE   A 1 137 ? 11.978 -12.132 -3.678  0.66 18.13 ?  137 ILE   A O    1 
ATOM   3022 O  O    B ILE   A 1 137 ? 11.946 -11.808 -3.407  0.34 18.14 ?  137 ILE   A O    1 
ATOM   3023 C  CB   A ILE   A 1 137 ? 9.214  -10.560 -4.694  0.66 19.21 ?  137 ILE   A CB   1 
ATOM   3024 C  CB   B ILE   A 1 137 ? 9.217  -10.334 -4.706  0.34 19.23 ?  137 ILE   A CB   1 
ATOM   3025 C  CG1  A ILE   A 1 137 ? 8.050  -9.711  -4.169  0.66 21.23 ?  137 ILE   A CG1  1 
ATOM   3026 C  CG1  B ILE   A 1 137 ? 8.010  -9.482  -4.306  0.34 20.42 ?  137 ILE   A CG1  1 
ATOM   3027 C  CG2  A ILE   A 1 137 ? 8.872  -12.049 -4.590  0.66 19.64 ?  137 ILE   A CG2  1 
ATOM   3028 C  CG2  B ILE   A 1 137 ? 8.895  -11.822 -4.573  0.34 19.49 ?  137 ILE   A CG2  1 
ATOM   3029 C  CD1  A ILE   A 1 137 ? 6.748  -9.918  -4.915  0.66 22.91 ?  137 ILE   A CD1  1 
ATOM   3030 C  CD1  B ILE   A 1 137 ? 6.745  -9.844  -5.063  0.34 21.31 ?  137 ILE   A CD1  1 
ATOM   3031 H  H    A ILE   A 1 137 ? 10.382 -8.407  -4.639  0.66 21.39 ?  137 ILE   A H    1 
ATOM   3032 H  H    B ILE   A 1 137 ? 10.381 -8.180  -4.715  0.34 21.60 ?  137 ILE   A H    1 
ATOM   3033 H  HA   A ILE   A 1 137 ? 10.344 -10.422 -2.986  0.66 21.60 ?  137 ILE   A HA   1 
ATOM   3034 H  HA   B ILE   A 1 137 ? 10.226 -10.073 -2.929  0.34 21.96 ?  137 ILE   A HA   1 
ATOM   3035 H  HB   A ILE   A 1 137 ? 9.349  -10.349 -5.629  0.66 23.10 ?  137 ILE   A HB   1 
ATOM   3036 H  HB   B ILE   A 1 137 ? 9.416  -10.147 -5.635  0.34 23.13 ?  137 ILE   A HB   1 
ATOM   3037 H  HG12 A ILE   A 1 137 ? 7.897  -9.928  -3.236  0.66 25.53 ?  137 ILE   A HG12 1 
ATOM   3038 H  HG12 B ILE   A 1 137 ? 7.835  -9.601  -3.358  0.34 24.56 ?  137 ILE   A HG12 1 
ATOM   3039 H  HG13 A ILE   A 1 137 ? 8.291  -8.771  -4.250  0.66 25.53 ?  137 ILE   A HG13 1 
ATOM   3040 H  HG13 B ILE   A 1 137 ? 8.205  -8.547  -4.489  0.34 24.56 ?  137 ILE   A HG13 1 
ATOM   3041 H  HG21 A ILE   A 1 137 ? 8.125  -12.247 -5.174  0.66 23.62 ?  137 ILE   A HG21 1 
ATOM   3042 H  HG21 B ILE   A 1 137 ? 8.214  -12.065 -5.215  0.34 23.45 ?  137 ILE   A HG21 1 
ATOM   3043 H  HG22 A ILE   A 1 137 ? 9.634  -12.579 -4.862  0.66 23.62 ?  137 ILE   A HG22 1 
ATOM   3044 H  HG22 B ILE   A 1 137 ? 9.687  -12.343 -4.750  0.34 23.45 ?  137 ILE   A HG22 1 
ATOM   3045 H  HG23 A ILE   A 1 137 ? 8.638  -12.251 -3.671  0.66 23.62 ?  137 ILE   A HG23 1 
ATOM   3046 H  HG23 B ILE   A 1 137 ? 8.579  -11.988 -3.674  0.34 23.45 ?  137 ILE   A HG23 1 
ATOM   3047 H  HD11 A ILE   A 1 137 ? 6.049  -9.485  -4.413  0.66 27.55 ?  137 ILE   A HD11 1 
ATOM   3048 H  HD11 B ILE   A 1 137 ? 6.063  -10.113 -4.428  0.34 25.62 ?  137 ILE   A HD11 1 
ATOM   3049 H  HD12 A ILE   A 1 137 ? 6.821  -9.527  -5.801  0.66 27.55 ?  137 ILE   A HD12 1 
ATOM   3050 H  HD12 B ILE   A 1 137 ? 6.456  -9.072  -5.561  0.34 25.62 ?  137 ILE   A HD12 1 
ATOM   3051 H  HD13 A ILE   A 1 137 ? 6.553  -10.865 -4.985  0.66 27.55 ?  137 ILE   A HD13 1 
ATOM   3052 H  HD13 B ILE   A 1 137 ? 6.922  -10.565 -5.685  0.34 25.62 ?  137 ILE   A HD13 1 
ATOM   3053 N  N    A HIS   A 1 138 ? 12.313 -10.801 -5.459  0.66 18.80 ?  138 HIS   A N    1 
ATOM   3054 N  N    B HIS   A 1 138 ? 12.263 -10.672 -5.327  0.34 18.07 ?  138 HIS   A N    1 
ATOM   3055 C  CA   A HIS   A 1 138 ? 13.502 -11.538 -5.868  0.66 18.72 ?  138 HIS   A CA   1 
ATOM   3056 C  CA   B HIS   A 1 138 ? 13.376 -11.513 -5.750  0.34 17.59 ?  138 HIS   A CA   1 
ATOM   3057 C  C    A HIS   A 1 138 ? 14.621 -11.393 -4.843  0.66 18.32 ?  138 HIS   A C    1 
ATOM   3058 C  C    B HIS   A 1 138 ? 14.551 -11.395 -4.790  0.34 17.45 ?  138 HIS   A C    1 
ATOM   3059 O  O    A HIS   A 1 138 ? 15.284 -12.378 -4.496  0.66 18.92 ?  138 HIS   A O    1 
ATOM   3060 O  O    B HIS   A 1 138 ? 15.192 -12.398 -4.453  0.34 17.63 ?  138 HIS   A O    1 
ATOM   3061 C  CB   A HIS   A 1 138 ? 13.957 -11.085 -7.254  0.66 20.14 ?  138 HIS   A CB   1 
ATOM   3062 C  CB   B HIS   A 1 138 ? 13.782 -11.117 -7.169  0.34 17.51 ?  138 HIS   A CB   1 
ATOM   3063 C  CG   A HIS   A 1 138 ? 15.177 -11.802 -7.743  0.66 21.12 ?  138 HIS   A CG   1 
ATOM   3064 C  CG   B HIS   A 1 138 ? 15.112 -11.656 -7.591  0.34 17.47 ?  138 HIS   A CG   1 
ATOM   3065 N  ND1  A HIS   A 1 138 ? 15.213 -13.168 -7.923  0.66 21.81 ?  138 HIS   A ND1  1 
ATOM   3066 N  ND1  B HIS   A 1 138 ? 15.302 -12.976 -7.938  0.34 17.81 ?  138 HIS   A ND1  1 
ATOM   3067 C  CD2  A HIS   A 1 138 ? 16.408 -11.345 -8.073  0.66 21.49 ?  138 HIS   A CD2  1 
ATOM   3068 C  CD2  B HIS   A 1 138 ? 16.316 -11.054 -7.723  0.34 17.12 ?  138 HIS   A CD2  1 
ATOM   3069 C  CE1  A HIS   A 1 138 ? 16.412 -13.521 -8.353  0.66 22.01 ?  138 HIS   A CE1  1 
ATOM   3070 C  CE1  B HIS   A 1 138 ? 16.568 -13.163 -8.267  0.34 17.85 ?  138 HIS   A CE1  1 
ATOM   3071 N  NE2  A HIS   A 1 138 ? 17.157 -12.434 -8.448  0.66 21.75 ?  138 HIS   A NE2  1 
ATOM   3072 N  NE2  B HIS   A 1 138 ? 17.205 -12.013 -8.144  0.34 17.42 ?  138 HIS   A NE2  1 
ATOM   3073 H  H    A HIS   A 1 138 ? 12.088 -10.159 -5.990  0.66 22.62 ?  138 HIS   A H    1 
ATOM   3074 H  H    B HIS   A 1 138 ? 12.072 -10.039 -5.876  0.34 21.74 ?  138 HIS   A H    1 
ATOM   3075 H  HA   A HIS   A 1 138 ? 13.277 -12.477 -5.930  0.66 22.52 ?  138 HIS   A HA   1 
ATOM   3076 H  HA   B HIS   A 1 138 ? 13.090 -12.438 -5.766  0.34 21.17 ?  138 HIS   A HA   1 
ATOM   3077 H  HB2  A HIS   A 1 138 ? 13.238 -11.250 -7.889  0.66 24.22 ?  138 HIS   A HB2  1 
ATOM   3078 H  HB2  B HIS   A 1 138 ? 13.114 -11.451 -7.790  0.34 21.06 ?  138 HIS   A HB2  1 
ATOM   3079 H  HB3  A HIS   A 1 138 ? 14.158 -10.137 -7.227  0.66 24.22 ?  138 HIS   A HB3  1 
ATOM   3080 H  HB3  B HIS   A 1 138 ? 13.824 -10.149 -7.224  0.34 21.06 ?  138 HIS   A HB3  1 
ATOM   3081 H  HD1  A HIS   A 1 138 ? 14.556 -13.707 -7.785  0.66 26.23 ?  138 HIS   A HD1  1 
ATOM   3082 H  HD2  A HIS   A 1 138 ? 16.689 -10.459 -8.049  0.66 25.85 ?  138 HIS   A HD2  1 
ATOM   3083 H  HD2  B HIS   A 1 138 ? 16.504 -10.160 -7.560  0.34 20.60 ?  138 HIS   A HD2  1 
ATOM   3084 H  HE1  A HIS   A 1 138 ? 16.686 -14.386 -8.548  0.66 26.47 ?  138 HIS   A HE1  1 
ATOM   3085 H  HE1  B HIS   A 1 138 ? 16.945 -13.970 -8.538  0.34 21.47 ?  138 HIS   A HE1  1 
ATOM   3086 H  HE2  B HIS   A 1 138 ? 18.039 -11.886 -8.302  0.34 20.96 ?  138 HIS   A HE2  1 
ATOM   3087 N  N    . SER   A 1 139 ? 14.847 -10.178 -4.338  1.00 17.60 ?  139 SER   A N    1 
ATOM   3088 C  CA   . SER   A 1 139 ? 15.920 -9.988  -3.371  1.00 17.92 ?  139 SER   A CA   1 
ATOM   3089 C  C    . SER   A 1 139 ? 15.694 -10.832 -2.122  1.00 17.69 ?  139 SER   A C    1 
ATOM   3090 O  O    . SER   A 1 139 ? 16.641 -11.422 -1.586  1.00 17.88 ?  139 SER   A O    1 
ATOM   3091 C  CB   . SER   A 1 139 ? 16.042 -8.509  -3.014  1.00 17.69 ?  139 SER   A CB   1 
ATOM   3092 O  OG   . SER   A 1 139 ? 17.136 -8.332  -2.131  1.00 17.76 ?  139 SER   A OG   1 
ATOM   3093 H  H    A SER   A 1 139 ? 14.406 -9.469  -4.531  0.66 21.17 ?  139 SER   A H    1 
ATOM   3094 H  H    B SER   A 1 139 ? 14.441 -9.458  -4.564  0.34 21.17 ?  139 SER   A H    1 
ATOM   3095 H  HA   . SER   A 1 139 ? 16.763 -10.266 -3.767  1.00 21.56 ?  139 SER   A HA   1 
ATOM   3096 H  HB2  . SER   A 1 139 ? 16.206 -7.990  -3.817  1.00 21.28 ?  139 SER   A HB2  1 
ATOM   3097 H  HB3  . SER   A 1 139 ? 15.227 -8.209  -2.580  1.00 21.28 ?  139 SER   A HB3  1 
ATOM   3098 H  HG   . SER   A 1 139 ? 17.209 -7.515  -1.914  1.00 21.37 ?  139 SER   A HG   1 
ATOM   3099 N  N    . LEU   A 1 140 ? 14.451 -10.897 -1.637  1.00 17.63 ?  140 LEU   A N    1 
ATOM   3100 C  CA   . LEU   A 1 140 ? 14.180 -11.713 -0.459  1.00 17.59 ?  140 LEU   A CA   1 
ATOM   3101 C  C    . LEU   A 1 140 ? 14.434 -13.189 -0.743  1.00 18.04 ?  140 LEU   A C    1 
ATOM   3102 O  O    . LEU   A 1 140 ? 14.994 -13.905 0.098   1.00 18.77 ?  140 LEU   A O    1 
ATOM   3103 C  CB   . LEU   A 1 140 ? 12.746 -11.483 0.014   1.00 18.22 ?  140 LEU   A CB   1 
ATOM   3104 C  CG   . LEU   A 1 140 ? 12.266 -12.370 1.160   1.00 18.71 ?  140 LEU   A CG   1 
ATOM   3105 C  CD1  . LEU   A 1 140 ? 13.158 -12.202 2.381   1.00 19.48 ?  140 LEU   A CD1  1 
ATOM   3106 C  CD2  . LEU   A 1 140 ? 10.802 -12.048 1.496   1.00 19.17 ?  140 LEU   A CD2  1 
ATOM   3107 H  H    . LEU   A 1 140 ? 13.773 -10.480 -1.957  1.00 21.21 ?  140 LEU   A H    1 
ATOM   3108 H  HA   . LEU   A 1 140 ? 14.773 -11.447 0.259   1.00 21.17 ?  140 LEU   A HA   1 
ATOM   3109 H  HB2  . LEU   A 1 140 ? 12.666 -10.567 0.319   1.00 21.92 ?  140 LEU   A HB2  1 
ATOM   3110 H  HB3  . LEU   A 1 140 ? 12.147 -11.631 -0.732  1.00 21.92 ?  140 LEU   A HB3  1 
ATOM   3111 H  HG   . LEU   A 1 140 ? 12.303 -13.306 0.882   1.00 22.51 ?  140 LEU   A HG   1 
ATOM   3112 H  HD11 . LEU   A 1 140 ? 12.780 -12.709 3.119   1.00 23.43 ?  140 LEU   A HD11 1 
ATOM   3113 H  HD12 . LEU   A 1 140 ? 14.044 -12.543 2.172   1.00 23.43 ?  140 LEU   A HD12 1 
ATOM   3114 H  HD13 . LEU   A 1 140 ? 13.204 -11.266 2.608   1.00 23.43 ?  140 LEU   A HD13 1 
ATOM   3115 H  HD21 . LEU   A 1 140 ? 10.503 -12.632 2.212   1.00 23.06 ?  140 LEU   A HD21 1 
ATOM   3116 H  HD22 . LEU   A 1 140 ? 10.743 -11.124 1.782   1.00 23.06 ?  140 LEU   A HD22 1 
ATOM   3117 H  HD23 . LEU   A 1 140 ? 10.254 -12.188 0.707   1.00 23.06 ?  140 LEU   A HD23 1 
ATOM   3118 N  N    . ARG   A 1 141 ? 14.055 -13.651 -1.937  1.00 18.42 ?  141 ARG   A N    1 
ATOM   3119 C  CA   . ARG   A 1 141 ? 14.286 -15.043 -2.308  1.00 19.10 ?  141 ARG   A CA   1 
ATOM   3120 C  C    . ARG   A 1 141 ? 15.781 -15.356 -2.323  1.00 18.25 ?  141 ARG   A C    1 
ATOM   3121 O  O    . ARG   A 1 141 ? 16.227 -16.376 -1.779  1.00 18.51 ?  141 ARG   A O    1 
ATOM   3122 C  CB   . ARG   A 1 141 ? 13.671 -15.297 -3.685  1.00 20.40 ?  141 ARG   A CB   1 
ATOM   3123 C  CG   . ARG   A 1 141 ? 13.676 -16.746 -4.133  1.00 22.83 ?  141 ARG   A CG   1 
ATOM   3124 C  CD   . ARG   A 1 141 ? 12.636 -17.530 -3.386  1.00 25.25 ?  141 ARG   A CD   1 
ATOM   3125 N  NE   . ARG   A 1 141 ? 13.228 -18.312 -2.312  1.00 26.13 ?  141 ARG   A NE   1 
ATOM   3126 C  CZ   . ARG   A 1 141 ? 12.533 -18.849 -1.316  1.00 26.31 ?  141 ARG   A CZ   1 
ATOM   3127 N  NH1  . ARG   A 1 141 ? 11.247 -18.584 -1.146  1.00 25.67 ?  141 ARG   A NH1  1 
ATOM   3128 N  NH2  . ARG   A 1 141 ? 13.149 -19.654 -0.455  1.00 27.50 ?  141 ARG   A NH2  1 
ATOM   3129 H  H    . ARG   A 1 141 ? 13.664 -13.180 -2.547  1.00 22.15 ?  141 ARG   A H    1 
ATOM   3130 H  HA   . ARG   A 1 141 ? 13.858 -15.624 -1.668  1.00 22.97 ?  141 ARG   A HA   1 
ATOM   3131 H  HB2  . ARG   A 1 141 ? 12.746 -14.996 -3.676  1.00 24.53 ?  141 ARG   A HB2  1 
ATOM   3132 H  HB3  . ARG   A 1 141 ? 14.165 -14.788 -4.347  1.00 24.53 ?  141 ARG   A HB3  1 
ATOM   3133 H  HG2  . ARG   A 1 141 ? 13.479 -16.795 -5.083  1.00 27.45 ?  141 ARG   A HG2  1 
ATOM   3134 H  HG3  . ARG   A 1 141 ? 14.548 -17.140 -3.953  1.00 27.45 ?  141 ARG   A HG3  1 
ATOM   3135 H  HD2  . ARG   A 1 141 ? 11.999 -16.919 -2.983  1.00 30.36 ?  141 ARG   A HD2  1 
ATOM   3136 H  HD3  . ARG   A 1 141 ? 12.177 -18.125 -4.004  1.00 30.36 ?  141 ARG   A HD3  1 
ATOM   3137 H  HE   . ARG   A 1 141 ? 14.048 -18.553 -2.397  1.00 31.42 ?  141 ARG   A HE   1 
ATOM   3138 H  HH11 . ARG   A 1 141 ? 10.830 -18.077 -1.701  1.00 30.86 ?  141 ARG   A HH11 1 
ATOM   3139 H  HH12 . ARG   A 1 141 ? 10.818 -18.935 -0.485  1.00 30.86 ?  141 ARG   A HH12 1 
ATOM   3140 H  HH21 . ARG   A 1 141 ? 13.984 -19.835 -0.556  1.00 33.05 ?  141 ARG   A HH21 1 
ATOM   3141 H  HH22 . ARG   A 1 141 ? 12.714 -19.994 0.206   1.00 33.05 ?  141 ARG   A HH22 1 
ATOM   3142 N  N    . VAL   A 1 142 ? 16.580 -14.484 -2.945  1.00 17.41 ?  142 VAL   A N    1 
ATOM   3143 C  CA   . VAL   A 1 142 ? 18.023 -14.702 -2.971  1.00 17.11 ?  142 VAL   A CA   1 
ATOM   3144 C  C    . VAL   A 1 142 ? 18.587 -14.691 -1.558  1.00 16.57 ?  142 VAL   A C    1 
ATOM   3145 O  O    . VAL   A 1 142 ? 19.457 -15.497 -1.214  1.00 17.53 ?  142 VAL   A O    1 
ATOM   3146 C  CB   . VAL   A 1 142 ? 18.722 -13.676 -3.879  1.00 17.82 ?  142 VAL   A CB   1 
ATOM   3147 C  CG1  . VAL   A 1 142 ? 20.233 -13.895 -3.833  1.00 17.29 ?  142 VAL   A CG1  1 
ATOM   3148 C  CG2  . VAL   A 1 142 ? 18.237 -13.813 -5.308  1.00 18.69 ?  142 VAL   A CG2  1 
ATOM   3149 H  H    . VAL   A 1 142 ? 16.316 -13.765 -3.353  1.00 20.95 ?  142 VAL   A H    1 
ATOM   3150 H  HA   . VAL   A 1 142 ? 18.196 -15.572 -3.350  1.00 20.59 ?  142 VAL   A HA   1 
ATOM   3151 H  HB   . VAL   A 1 142 ? 18.537 -12.769 -3.575  1.00 21.44 ?  142 VAL   A HB   1 
ATOM   3152 H  HG11 . VAL   A 1 142 ? 20.651 -13.403 -4.563  1.00 20.81 ?  142 VAL   A HG11 1 
ATOM   3153 H  HG12 . VAL   A 1 142 ? 20.581 -13.569 -2.986  1.00 20.81 ?  142 VAL   A HG12 1 
ATOM   3154 H  HG13 . VAL   A 1 142 ? 20.420 -14.839 -3.928  1.00 20.81 ?  142 VAL   A HG13 1 
ATOM   3155 H  HG21 . VAL   A 1 142 ? 18.714 -13.175 -5.868  1.00 22.48 ?  142 VAL   A HG21 1 
ATOM   3156 H  HG22 . VAL   A 1 142 ? 18.418 -14.715 -5.612  1.00 22.48 ?  142 VAL   A HG22 1 
ATOM   3157 H  HG23 . VAL   A 1 142 ? 17.289 -13.632 -5.336  1.00 22.48 ?  142 VAL   A HG23 1 
ATOM   3158 N  N    . CYS   A 1 143 ? 18.121 -13.763 -0.723  1.00 16.70 ?  143 CYS   A N    1 
ATOM   3159 C  CA   . CYS   A 1 143 ? 18.590 -13.712 0.655   1.00 17.16 ?  143 CYS   A CA   1 
ATOM   3160 C  C    . CYS   A 1 143 ? 18.357 -15.048 1.354   1.00 17.24 ?  143 CYS   A C    1 
ATOM   3161 O  O    . CYS   A 1 143 ? 19.277 -15.632 1.937   1.00 17.44 ?  143 CYS   A O    1 
ATOM   3162 C  CB   . CYS   A 1 143 ? 17.884 -12.581 1.397   1.00 17.73 ?  143 CYS   A CB   1 
ATOM   3163 S  SG   . CYS   A 1 143 ? 18.344 -12.423 3.124   1.00 17.59 ?  143 CYS   A SG   1 
ATOM   3164 H  H    . CYS   A 1 143 ? 17.540 -13.166 -0.930  1.00 20.09 ?  143 CYS   A H    1 
ATOM   3165 H  HA   . CYS   A 1 143 ? 19.540 -13.540 0.661   1.00 20.64 ?  143 CYS   A HA   1 
ATOM   3166 H  HB2  . CYS   A 1 143 ? 18.089 -11.744 0.954   1.00 21.33 ?  143 CYS   A HB2  1 
ATOM   3167 H  HB3  . CYS   A 1 143 ? 16.930 -12.738 1.362   1.00 21.33 ?  143 CYS   A HB3  1 
ATOM   3168 H  HG   . CYS   A 1 143 ? 17.781 -11.474 3.579   1.00 21.16 ?  143 CYS   A HG   1 
ATOM   3169 N  N    . VAL   A 1 144 ? 17.127 -15.553 1.290   1.00 18.35 ?  144 VAL   A N    1 
ATOM   3170 C  CA   . VAL   A 1 144 ? 16.788 -16.788 1.985   1.00 19.38 ?  144 VAL   A CA   1 
ATOM   3171 C  C    . VAL   A 1 144 ? 17.604 -17.956 1.452   1.00 18.66 ?  144 VAL   A C    1 
ATOM   3172 O  O    . VAL   A 1 144 ? 17.971 -18.869 2.205   1.00 19.28 ?  144 VAL   A O    1 
ATOM   3173 C  CB   . VAL   A 1 144 ? 15.271 -17.030 1.871   1.00 21.51 ?  144 VAL   A CB   1 
ATOM   3174 C  CG1  . VAL   A 1 144 ? 14.918 -18.452 2.253   1.00 23.05 ?  144 VAL   A CG1  1 
ATOM   3175 C  CG2  . VAL   A 1 144 ? 14.524 -16.029 2.742   1.00 21.26 ?  144 VAL   A CG2  1 
ATOM   3176 H  H    . VAL   A 1 144 ? 16.473 -15.201 0.851   1.00 22.07 ?  144 VAL   A H    1 
ATOM   3177 H  HA   . VAL   A 1 144 ? 16.995 -16.688 2.922   1.00 23.31 ?  144 VAL   A HA   1 
ATOM   3178 H  HB   . VAL   A 1 144 ? 14.988 -16.892 0.949   1.00 25.87 ?  144 VAL   A HB   1 
ATOM   3179 H  HG11 . VAL   A 1 144 ? 13.964 -18.505 2.433   1.00 27.71 ?  144 VAL   A HG11 1 
ATOM   3180 H  HG12 . VAL   A 1 144 ? 15.145 -19.045 1.521   1.00 27.71 ?  144 VAL   A HG12 1 
ATOM   3181 H  HG13 . VAL   A 1 144 ? 15.416 -18.695 3.048   1.00 27.71 ?  144 VAL   A HG13 1 
ATOM   3182 H  HG21 . VAL   A 1 144 ? 13.585 -16.278 2.788   1.00 25.56 ?  144 VAL   A HG21 1 
ATOM   3183 H  HG22 . VAL   A 1 144 ? 14.907 -16.032 3.631   1.00 25.56 ?  144 VAL   A HG22 1 
ATOM   3184 H  HG23 . VAL   A 1 144 ? 14.606 -15.142 2.350   1.00 25.56 ?  144 VAL   A HG23 1 
ATOM   3185 N  N    . ASP   A 1 145 ? 17.861 -17.976 0.147   1.00 18.62 ?  145 ASP   A N    1 
ATOM   3186 C  CA   . ASP   A 1 145 ? 18.570 -19.086 -0.483  1.00 19.65 ?  145 ASP   A CA   1 
ATOM   3187 C  C    . ASP   A 1 145 ? 20.091 -18.943 -0.444  1.00 19.08 ?  145 ASP   A C    1 
ATOM   3188 O  O    . ASP   A 1 145 ? 20.794 -19.837 -0.928  1.00 20.50 ?  145 ASP   A O    1 
ATOM   3189 C  CB   . ASP   A 1 145 ? 18.124 -19.232 -1.937  1.00 21.23 ?  145 ASP   A CB   1 
ATOM   3190 C  CG   . ASP   A 1 145 ? 16.676 -19.675 -2.060  1.00 23.34 ?  145 ASP   A CG   1 
ATOM   3191 O  OD1  . ASP   A 1 145 ? 16.110 -20.192 -1.068  1.00 23.85 ?  145 ASP   A OD1  1 
ATOM   3192 O  OD2  . ASP   A 1 145 ? 16.113 -19.494 -3.154  1.00 24.80 -1 145 ASP   A OD2  1 
ATOM   3193 H  H    . ASP   A 1 145 ? 17.614 -17.367 -0.407  1.00 22.40 ?  145 ASP   A H    1 
ATOM   3194 H  HA   . ASP   A 1 145 ? 18.342 -19.909 -0.027  1.00 23.64 ?  145 ASP   A HA   1 
ATOM   3195 H  HB2  . ASP   A 1 145 ? 18.234 -18.376 -2.390  1.00 25.53 ?  145 ASP   A HB2  1 
ATOM   3196 H  HB3  . ASP   A 1 145 ? 18.673 -19.904 -2.373  1.00 25.53 ?  145 ASP   A HB3  1 
ATOM   3197 N  N    . THR   A 1 146 ? 20.622 -17.855 0.111   1.00 17.72 ?  146 THR   A N    1 
ATOM   3198 C  CA   . THR   A 1 146 ? 22.062 -17.603 0.123   1.00 16.78 ?  146 THR   A CA   1 
ATOM   3199 C  C    . THR   A 1 146 ? 22.608 -17.420 1.527   1.00 17.10 ?  146 THR   A C    1 
ATOM   3200 O  O    . THR   A 1 146 ? 23.682 -17.953 1.844   1.00 18.24 ?  146 THR   A O    1 
ATOM   3201 C  CB   . THR   A 1 146 ? 22.374 -16.350 -0.715  1.00 17.09 ?  146 THR   A CB   1 
ATOM   3202 O  OG1  . THR   A 1 146 ? 21.865 -16.517 -2.038  1.00 17.99 ?  146 THR   A OG1  1 
ATOM   3203 C  CG2  . THR   A 1 146 ? 23.885 -16.100 -0.789  1.00 17.31 ?  146 THR   A CG2  1 
ATOM   3204 H  H    . THR   A 1 146 ? 20.162 -17.232 0.490   1.00 21.32 ?  146 THR   A H    1 
ATOM   3205 H  HA   . THR   A 1 146 ? 22.524 -18.351 -0.276  1.00 20.20 ?  146 THR   A HA   1 
ATOM   3206 H  HB   . THR   A 1 146 ? 21.960 -15.573 -0.311  1.00 20.56 ?  146 THR   A HB   1 
ATOM   3207 H  HG1  . THR   A 1 146 ? 21.034 -16.616 -2.016  1.00 21.64 ?  146 THR   A HG1  1 
ATOM   3208 H  HG21 . THR   A 1 146 ? 24.076 -15.430 -1.464  1.00 20.83 ?  146 THR   A HG21 1 
ATOM   3209 H  HG22 . THR   A 1 146 ? 24.212 -15.785 0.068   1.00 20.83 ?  146 THR   A HG22 1 
ATOM   3210 H  HG23 . THR   A 1 146 ? 24.344 -16.921 -1.022  1.00 20.83 ?  146 THR   A HG23 1 
ATOM   3211 N  N    . VAL   A 1 147 ? 21.936 -16.626 2.356   1.00 17.11 ?  147 VAL   A N    1 
ATOM   3212 C  CA   . VAL   A 1 147 ? 22.430 -16.326 3.693   1.00 17.13 ?  147 VAL   A CA   1 
ATOM   3213 C  C    . VAL   A 1 147 ? 22.120 -17.498 4.616   1.00 17.50 ?  147 VAL   A C    1 
ATOM   3214 O  O    . VAL   A 1 147 ? 20.978 -17.977 4.677   1.00 18.00 ?  147 VAL   A O    1 
ATOM   3215 C  CB   . VAL   A 1 147 ? 21.809 -15.023 4.212   1.00 17.06 ?  147 VAL   A CB   1 
ATOM   3216 C  CG1  . VAL   A 1 147 ? 22.320 -14.728 5.597   1.00 17.94 ?  147 VAL   A CG1  1 
ATOM   3217 C  CG2  . VAL   A 1 147 ? 22.063 -13.868 3.240   1.00 17.31 ?  147 VAL   A CG2  1 
ATOM   3218 H  H    . VAL   A 1 147 ? 21.188 -16.240 2.164   1.00 20.58 ?  147 VAL   A H    1 
ATOM   3219 H  HA   . VAL   A 1 147 ? 23.389 -16.211 3.662   1.00 20.62 ?  147 VAL   A HA   1 
ATOM   3220 H  HB   . VAL   A 1 147 ? 20.849 -15.146 4.281   1.00 20.53 ?  147 VAL   A HB   1 
ATOM   3221 H  HG11 . VAL   A 1 147 ? 22.091 -13.819 5.828   1.00 21.59 ?  147 VAL   A HG11 1 
ATOM   3222 H  HG12 . VAL   A 1 147 ? 21.897 -15.344 6.225   1.00 21.59 ?  147 VAL   A HG12 1 
ATOM   3223 H  HG13 . VAL   A 1 147 ? 23.278 -14.851 5.611   1.00 21.59 ?  147 VAL   A HG13 1 
ATOM   3224 H  HG21 . VAL   A 1 147 ? 21.735 -13.046 3.636   1.00 20.83 ?  147 VAL   A HG21 1 
ATOM   3225 H  HG22 . VAL   A 1 147 ? 23.011 -13.803 3.069   1.00 20.83 ?  147 VAL   A HG22 1 
ATOM   3226 H  HG23 . VAL   A 1 147 ? 21.586 -14.048 2.412   1.00 20.83 ?  147 VAL   A HG23 1 
ATOM   3227 N  N    . ARG   A 1 148 ? 23.147 -17.972 5.321   1.00 18.16 ?  148 ARG   A N    1 
ATOM   3228 C  CA   . ARG   A 1 148 ? 23.009 -19.054 6.285   1.00 18.20 ?  148 ARG   A CA   1 
ATOM   3229 C  C    . ARG   A 1 148 ? 23.127 -18.579 7.720   1.00 17.64 ?  148 ARG   A C    1 
ATOM   3230 O  O    . ARG   A 1 148 ? 22.707 -19.293 8.636   1.00 19.63 ?  148 ARG   A O    1 
ATOM   3231 C  CB   . ARG   A 1 148 ? 24.055 -20.146 6.027   1.00 18.34 ?  148 ARG   A CB   1 
ATOM   3232 C  CG   . ARG   A 1 148 ? 23.933 -20.771 4.657   1.00 19.41 ?  148 ARG   A CG   1 
ATOM   3233 C  CD   . ARG   A 1 148 ? 25.020 -21.803 4.398   1.00 20.30 ?  148 ARG   A CD   1 
ATOM   3234 N  NE   . ARG   A 1 148 ? 26.353 -21.214 4.426   1.00 20.31 ?  148 ARG   A NE   1 
ATOM   3235 C  CZ   . ARG   A 1 148 ? 26.863 -20.484 3.445   1.00 19.26 ?  148 ARG   A CZ   1 
ATOM   3236 N  NH1  . ARG   A 1 148 ? 26.197 -20.270 2.322   1.00 19.80 ?  148 ARG   A NH1  1 
ATOM   3237 N  NH2  . ARG   A 1 148 ? 28.071 -19.943 3.595   1.00 19.54 ?  148 ARG   A NH2  1 
ATOM   3238 H  H    . ARG   A 1 148 ? 23.949 -17.670 5.248   1.00 21.85 ?  148 ARG   A H    1 
ATOM   3239 H  HA   . ARG   A 1 148 ? 22.134 -19.452 6.179   1.00 21.90 ?  148 ARG   A HA   1 
ATOM   3240 H  HB2  . ARG   A 1 148 ? 24.941 -19.764 6.101   1.00 22.06 ?  148 ARG   A HB2  1 
ATOM   3241 H  HB3  . ARG   A 1 148 ? 23.940 -20.852 6.684   1.00 22.06 ?  148 ARG   A HB3  1 
ATOM   3242 H  HG2  . ARG   A 1 148 ? 23.070 -21.208 4.588   1.00 23.34 ?  148 ARG   A HG2  1 
ATOM   3243 H  HG3  . ARG   A 1 148 ? 24.008 -20.072 3.988   1.00 23.34 ?  148 ARG   A HG3  1 
ATOM   3244 H  HD2  . ARG   A 1 148 ? 24.978 -22.488 5.084   1.00 24.41 ?  148 ARG   A HD2  1 
ATOM   3245 H  HD3  . ARG   A 1 148 ? 24.879 -22.199 3.523   1.00 24.41 ?  148 ARG   A HD3  1 
ATOM   3246 H  HE   . ARG   A 1 148 ? 26.838 -21.349 5.121   1.00 24.43 ?  148 ARG   A HE   1 
ATOM   3247 H  HH11 . ARG   A 1 148 ? 25.414 -20.602 2.213   1.00 23.81 ?  148 ARG   A HH11 1 
ATOM   3248 H  HH12 . ARG   A 1 148 ? 26.548 -19.786 1.701   1.00 23.81 ?  148 ARG   A HH12 1 
ATOM   3249 H  HH21 . ARG   A 1 148 ? 28.514 -20.073 4.320   1.00 23.50 ?  148 ARG   A HH21 1 
ATOM   3250 H  HH22 . ARG   A 1 148 ? 28.413 -19.465 2.964   1.00 23.50 ?  148 ARG   A HH22 1 
ATOM   3251 N  N    . THR   A 1 149 ? 23.681 -17.387 7.926   1.00 18.02 ?  149 THR   A N    1 
ATOM   3252 C  CA   . THR   A 1 149 ? 23.751 -16.792 9.243   1.00 18.19 ?  149 THR   A CA   1 
ATOM   3253 C  C    . THR   A 1 149 ? 22.426 -16.093 9.550   1.00 18.01 ?  149 THR   A C    1 
ATOM   3254 O  O    . THR   A 1 149 ? 21.487 -16.085 8.741   1.00 18.02 ?  149 THR   A O    1 
ATOM   3255 C  CB   . THR   A 1 149 ? 24.948 -15.851 9.302   1.00 18.77 ?  149 THR   A CB   1 
ATOM   3256 O  OG1  . THR   A 1 149 ? 24.808 -14.902 8.245   1.00 18.91 ?  149 THR   A OG1  1 
ATOM   3257 C  CG2  . THR   A 1 149 ? 26.255 -16.640 9.134   1.00 18.71 ?  149 THR   A CG2  1 
ATOM   3258 H  H    . THR   A 1 149 ? 24.030 -16.896 7.304   1.00 21.69 ?  149 THR   A H    1 
ATOM   3259 H  HA   . THR   A 1 149 ? 23.876 -17.502 9.896   1.00 21.89 ?  149 THR   A HA   1 
ATOM   3260 H  HB   . THR   A 1 149 ? 24.959 -15.409 10.163  1.00 22.58 ?  149 THR   A HB   1 
ATOM   3261 H  HG1  . THR   A 1 149 ? 25.453 -14.366 8.266   1.00 22.75 ?  149 THR   A HG1  1 
ATOM   3262 H  HG21 . THR   A 1 149 ? 27.015 -16.043 9.210   1.00 22.51 ?  149 THR   A HG21 1 
ATOM   3263 H  HG22 . THR   A 1 149 ? 26.328 -17.328 9.818   1.00 22.51 ?  149 THR   A HG22 1 
ATOM   3264 H  HG23 . THR   A 1 149 ? 26.280 -17.069 8.261   1.00 22.51 ?  149 THR   A HG23 1 
ATOM   3265 N  N    . ASN   A 1 150 ? 22.309 -15.566 10.760  1.00 17.54 ?  150 ASN   A N    1 
ATOM   3266 C  CA   . ASN   A 1 150 ? 21.029 -15.055 11.255  1.00 18.54 ?  150 ASN   A CA   1 
ATOM   3267 C  C    . ASN   A 1 150 ? 20.842 -13.612 10.791  1.00 17.71 ?  150 ASN   A C    1 
ATOM   3268 O  O    . ASN   A 1 150 ? 21.576 -12.713 11.217  1.00 18.84 ?  150 ASN   A O    1 
ATOM   3269 C  CB   . ASN   A 1 150 ? 20.989 -15.158 12.774  1.00 20.99 ?  150 ASN   A CB   1 
ATOM   3270 C  CG   . ASN   A 1 150 ? 20.817 -16.580 13.249  1.00 25.29 ?  150 ASN   A CG   1 
ATOM   3271 O  OD1  . ASN   A 1 150 ? 20.193 -17.389 12.570  1.00 26.51 ?  150 ASN   A OD1  1 
ATOM   3272 N  ND2  . ASN   A 1 150 ? 21.378 -16.896 14.413  1.00 27.94 ?  150 ASN   A ND2  1 
ATOM   3273 H  H    . ASN   A 1 150 ? 22.957 -15.495 11.318  1.00 21.11 ?  150 ASN   A H    1 
ATOM   3274 H  HA   . ASN   A 1 150 ? 20.308 -15.594 10.891  1.00 22.30 ?  150 ASN   A HA   1 
ATOM   3275 H  HB2  . ASN   A 1 150 ? 21.822 -14.822 13.136  1.00 25.24 ?  150 ASN   A HB2  1 
ATOM   3276 H  HB3  . ASN   A 1 150 ? 20.243 -14.640 13.106  1.00 25.24 ?  150 ASN   A HB3  1 
ATOM   3277 H  HD21 . ASN   A 1 150 ? 21.307 -17.696 14.730  1.00 33.59 ?  150 ASN   A HD21 1 
ATOM   3278 H  HD22 . ASN   A 1 150 ? 21.810 -16.300 14.859  1.00 33.59 ?  150 ASN   A HD22 1 
ATOM   3279 N  N    . VAL   A 1 151 ? 19.857 -13.386 9.923   1.00 17.78 ?  151 VAL   A N    1 
ATOM   3280 C  CA   . VAL   A 1 151 ? 19.640 -12.082 9.314   1.00 17.52 ?  151 VAL   A CA   1 
ATOM   3281 C  C    . VAL   A 1 151 ? 18.261 -11.555 9.693   1.00 17.20 ?  151 VAL   A C    1 
ATOM   3282 O  O    . VAL   A 1 151 ? 17.243 -12.259 9.572   1.00 18.92 ?  151 VAL   A O    1 
ATOM   3283 C  CB   . VAL   A 1 151 ? 19.906 -12.084 7.793   1.00 18.26 ?  151 VAL   A CB   1 
ATOM   3284 C  CG1  . VAL   A 1 151 ? 19.073 -13.119 7.068   1.00 19.08 ?  151 VAL   A CG1  1 
ATOM   3285 C  CG2  . VAL   A 1 151 ? 19.717 -10.676 7.202   1.00 18.44 ?  151 VAL   A CG2  1 
ATOM   3286 H  H    . VAL   A 1 151 ? 19.297 -13.987 9.664   1.00 21.39 ?  151 VAL   A H    1 
ATOM   3287 H  HA   . VAL   A 1 151 ? 20.291 -11.468 9.695   1.00 21.08 ?  151 VAL   A HA   1 
ATOM   3288 H  HB   . VAL   A 1 151 ? 20.835 -12.327 7.651   1.00 21.97 ?  151 VAL   A HB   1 
ATOM   3289 H  HG11 . VAL   A 1 151 ? 19.228 -13.046 6.112   1.00 22.95 ?  151 VAL   A HG11 1 
ATOM   3290 H  HG12 . VAL   A 1 151 ? 19.332 -14.009 7.372   1.00 22.95 ?  151 VAL   A HG12 1 
ATOM   3291 H  HG13 . VAL   A 1 151 ? 18.136 -12.970 7.262   1.00 22.95 ?  151 VAL   A HG13 1 
ATOM   3292 H  HG21 . VAL   A 1 151 ? 20.008 -10.686 6.273   1.00 22.18 ?  151 VAL   A HG21 1 
ATOM   3293 H  HG22 . VAL   A 1 151 ? 18.780 -10.436 7.250   1.00 22.18 ?  151 VAL   A HG22 1 
ATOM   3294 H  HG23 . VAL   A 1 151 ? 20.253 -10.049 7.707   1.00 22.18 ?  151 VAL   A HG23 1 
ATOM   3295 N  N    A TYR   A 1 152 ? 18.240 -10.306 10.131  0.66 16.98 ?  152 TYR   A N    1 
ATOM   3296 N  N    B TYR   A 1 152 ? 18.254 -10.316 10.190  0.34 16.58 ?  152 TYR   A N    1 
ATOM   3297 C  CA   A TYR   A 1 152 ? 17.031 -9.581  10.479  0.66 16.67 ?  152 TYR   A CA   1 
ATOM   3298 C  CA   B TYR   A 1 152 ? 17.072 -9.607  10.657  0.34 16.18 ?  152 TYR   A CA   1 
ATOM   3299 C  C    A TYR   A 1 152 ? 16.827 -8.498  9.426   0.66 15.85 ?  152 TYR   A C    1 
ATOM   3300 C  C    B TYR   A 1 152 ? 16.866 -8.423  9.729   0.34 15.31 ?  152 TYR   A C    1 
ATOM   3301 O  O    A TYR   A 1 152 ? 17.566 -7.506  9.388   0.66 16.77 ?  152 TYR   A O    1 
ATOM   3302 O  O    B TYR   A 1 152 ? 17.684 -7.498  9.701   0.34 15.76 ?  152 TYR   A O    1 
ATOM   3303 C  CB   A TYR   A 1 152 ? 17.170 -9.035  11.898  0.66 16.89 ?  152 TYR   A CB   1 
ATOM   3304 C  CB   B TYR   A 1 152 ? 17.272 -9.146  12.098  0.34 16.75 ?  152 TYR   A CB   1 
ATOM   3305 C  CG   A TYR   A 1 152 ? 17.176 -10.164 12.907  0.66 17.40 ?  152 TYR   A CG   1 
ATOM   3306 C  CG   B TYR   A 1 152 ? 17.126 -10.275 13.081  0.34 17.49 ?  152 TYR   A CG   1 
ATOM   3307 C  CD1  A TYR   A 1 152 ? 18.338 -10.863 13.207  0.66 18.08 ?  152 TYR   A CD1  1 
ATOM   3308 C  CD1  B TYR   A 1 152 ? 18.162 -11.172 13.300  0.34 17.55 ?  152 TYR   A CD1  1 
ATOM   3309 C  CD2  A TYR   A 1 152 ? 16.001 -10.574 13.520  0.66 17.75 ?  152 TYR   A CD2  1 
ATOM   3310 C  CD2  B TYR   A 1 152 ? 15.941 -10.461 13.774  0.34 17.66 ?  152 TYR   A CD2  1 
ATOM   3311 C  CE1  A TYR   A 1 152 ? 18.340 -11.924 14.106  0.66 18.58 ?  152 TYR   A CE1  1 
ATOM   3312 C  CE1  B TYR   A 1 152 ? 18.023 -12.223 14.190  0.34 17.99 ?  152 TYR   A CE1  1 
ATOM   3313 C  CE2  A TYR   A 1 152 ? 15.989 -11.638 14.421  0.66 18.31 ?  152 TYR   A CE2  1 
ATOM   3314 C  CE2  B TYR   A 1 152 ? 15.790 -11.509 14.664  0.34 18.24 ?  152 TYR   A CE2  1 
ATOM   3315 C  CZ   A TYR   A 1 152 ? 17.165 -12.306 14.710  0.66 19.00 ?  152 TYR   A CZ   1 
ATOM   3316 C  CZ   B TYR   A 1 152 ? 16.835 -12.386 14.871  0.34 18.49 ?  152 TYR   A CZ   1 
ATOM   3317 O  OH   A TYR   A 1 152 ? 17.174 -13.364 15.602  0.66 20.86 ?  152 TYR   A OH   1 
ATOM   3318 O  OH   B TYR   A 1 152 ? 16.687 -13.431 15.758  0.34 19.53 ?  152 TYR   A OH   1 
ATOM   3319 H  H    A TYR   A 1 152 ? 18.955 -9.827  10.226  0.66 20.44 ?  152 TYR   A H    1 
ATOM   3320 H  H    B TYR   A 1 152 ? 18.971 -9.832  10.253  0.34 19.95 ?  152 TYR   A H    1 
ATOM   3321 H  HA   A TYR   A 1 152 ? 16.276 -10.193 10.454  0.66 20.05 ?  152 TYR   A HA   1 
ATOM   3322 H  HA   B TYR   A 1 152 ? 16.297 -10.183 10.609  0.34 19.47 ?  152 TYR   A HA   1 
ATOM   3323 H  HB2  A TYR   A 1 152 ? 18.005 -8.560  11.980  0.66 20.32 ?  152 TYR   A HB2  1 
ATOM   3324 H  HB2  B TYR   A 1 152 ? 18.165 -8.778  12.191  0.34 20.16 ?  152 TYR   A HB2  1 
ATOM   3325 H  HB3  A TYR   A 1 152 ? 16.422 -8.456  12.096  0.66 20.32 ?  152 TYR   A HB3  1 
ATOM   3326 H  HB3  B TYR   A 1 152 ? 16.609 -8.472  12.310  0.34 20.16 ?  152 TYR   A HB3  1 
ATOM   3327 H  HD1  A TYR   A 1 152 ? 19.133 -10.617 12.803  0.66 21.76 ?  152 TYR   A HD1  1 
ATOM   3328 H  HD1  B TYR   A 1 152 ? 18.965 -11.064 12.837  0.34 21.11 ?  152 TYR   A HD1  1 
ATOM   3329 H  HD2  A TYR   A 1 152 ? 15.199 -10.137 13.330  0.66 21.35 ?  152 TYR   A HD2  1 
ATOM   3330 H  HD2  B TYR   A 1 152 ? 15.232 -9.872  13.629  0.34 21.25 ?  152 TYR   A HD2  1 
ATOM   3331 H  HE1  A TYR   A 1 152 ? 19.129 -12.377 14.306  0.66 22.35 ?  152 TYR   A HE1  1 
ATOM   3332 H  HE1  B TYR   A 1 152 ? 18.730 -12.811 14.329  0.34 21.64 ?  152 TYR   A HE1  1 
ATOM   3333 H  HE2  A TYR   A 1 152 ? 15.190 -11.897 14.833  0.66 22.02 ?  152 TYR   A HE2  1 
ATOM   3334 H  HE2  B TYR   A 1 152 ? 14.990 -11.618 15.123  0.34 21.94 ?  152 TYR   A HE2  1 
ATOM   3335 H  HH   A TYR   A 1 152 ? 16.395 -13.494 15.908  0.66 25.09 ?  152 TYR   A HH   1 
ATOM   3336 H  HH   B TYR   A 1 152 ? 15.923 -13.400 16.101  0.34 23.49 ?  152 TYR   A HH   1 
ATOM   3337 N  N    A LEU   A 1 153 ? 15.847 -8.719  8.549   0.66 15.41 ?  153 LEU   A N    1 
ATOM   3338 N  N    B LEU   A 1 153 ? 15.778 -8.456  8.972   0.34 14.69 ?  153 LEU   A N    1 
ATOM   3339 C  CA   A LEU   A 1 153 ? 15.569 -7.831  7.428   0.66 15.02 ?  153 LEU   A CA   1 
ATOM   3340 C  CA   B LEU   A 1 153 ? 15.532 -7.498  7.909   0.34 13.58 ?  153 LEU   A CA   1 
ATOM   3341 C  C    A LEU   A 1 153 ? 14.575 -6.755  7.834   0.66 15.04 ?  153 LEU   A C    1 
ATOM   3342 C  C    B LEU   A 1 153 ? 14.534 -6.451  8.373   0.34 13.93 ?  153 LEU   A C    1 
ATOM   3343 O  O    A LEU   A 1 153 ? 13.455 -7.066  8.255   0.66 15.70 ?  153 LEU   A O    1 
ATOM   3344 O  O    B LEU   A 1 153 ? 13.486 -6.787  8.938   0.34 14.11 ?  153 LEU   A O    1 
ATOM   3345 C  CB   A LEU   A 1 153 ? 14.994 -8.631  6.261   0.66 14.65 ?  153 LEU   A CB   1 
ATOM   3346 C  CB   B LEU   A 1 153 ? 14.980 -8.208  6.674   0.34 13.14 ?  153 LEU   A CB   1 
ATOM   3347 C  CG   A LEU   A 1 153 ? 15.965 -9.608  5.602   0.66 14.66 ?  153 LEU   A CG   1 
ATOM   3348 C  CG   B LEU   A 1 153 ? 15.855 -9.300  6.058   0.34 13.00 ?  153 LEU   A CG   1 
ATOM   3349 C  CD1  A LEU   A 1 153 ? 15.203 -10.545 4.692   0.66 14.70 ?  153 LEU   A CD1  1 
ATOM   3350 C  CD1  B LEU   A 1 153 ? 15.047 -10.081 5.035   0.34 13.01 ?  153 LEU   A CD1  1 
ATOM   3351 C  CD2  A LEU   A 1 153 ? 17.034 -8.854  4.824   0.66 15.05 ?  153 LEU   A CD2  1 
ATOM   3352 C  CD2  B LEU   A 1 153 ? 17.111 -8.710  5.423   0.34 13.31 ?  153 LEU   A CD2  1 
ATOM   3353 H  H    A LEU   A 1 153 ? 15.316 -9.412  8.582   0.66 18.55 ?  153 LEU   A H    1 
ATOM   3354 H  H    B LEU   A 1 153 ? 15.152 -9.036  9.060   0.34 17.68 ?  153 LEU   A H    1 
ATOM   3355 H  HA   A LEU   A 1 153 ? 16.389 -7.410  7.150   0.66 18.08 ?  153 LEU   A HA   1 
ATOM   3356 H  HA   B LEU   A 1 153 ? 16.359 -7.054  7.675   0.34 16.36 ?  153 LEU   A HA   1 
ATOM   3357 H  HB2  A LEU   A 1 153 ? 14.232 -9.143  6.582   0.66 17.64 ?  153 LEU   A HB2  1 
ATOM   3358 H  HB2  B LEU   A 1 153 ? 14.137 -8.617  6.914   0.34 15.82 ?  153 LEU   A HB2  1 
ATOM   3359 H  HB3  A LEU   A 1 153 ? 14.702 -8.009  5.579   0.66 17.64 ?  153 LEU   A HB3  1 
ATOM   3360 H  HB3  B LEU   A 1 153 ? 14.830 -7.540  5.987   0.34 15.82 ?  153 LEU   A HB3  1 
ATOM   3361 H  HG   A LEU   A 1 153 ? 16.399 -10.138 6.293   0.66 17.65 ?  153 LEU   A HG   1 
ATOM   3362 H  HG   B LEU   A 1 153 ? 16.131 -9.916  6.753   0.34 15.66 ?  153 LEU   A HG   1 
ATOM   3363 H  HD11 A LEU   A 1 153 ? 15.781 -11.286 4.449   0.66 17.69 ?  153 LEU   A HD11 1 
ATOM   3364 H  HD11 B LEU   A 1 153 ? 15.608 -10.765 4.642   0.34 15.66 ?  153 LEU   A HD11 1 
ATOM   3365 H  HD12 A LEU   A 1 153 ? 14.424 -10.882 5.164   0.66 17.69 ?  153 LEU   A HD12 1 
ATOM   3366 H  HD12 B LEU   A 1 153 ? 14.286 -10.489 5.479   0.34 15.66 ?  153 LEU   A HD12 1 
ATOM   3367 H  HD13 A LEU   A 1 153 ? 14.929 -10.061 3.902   0.66 17.69 ?  153 LEU   A HD13 1 
ATOM   3368 H  HD13 B LEU   A 1 153 ? 14.736 -9.471  4.345   0.34 15.66 ?  153 LEU   A HD13 1 
ATOM   3369 H  HD21 A LEU   A 1 153 ? 17.662 -9.492  4.458   0.66 18.11 ?  153 LEU   A HD21 1 
ATOM   3370 H  HD21 B LEU   A 1 153 ? 17.633 -9.427  5.026   0.34 16.02 ?  153 LEU   A HD21 1 
ATOM   3371 H  HD22 A LEU   A 1 153 ? 16.605 -8.359  4.109   0.66 18.11 ?  153 LEU   A HD22 1 
ATOM   3372 H  HD22 B LEU   A 1 153 ? 16.853 -8.073  4.738   0.34 16.02 ?  153 LEU   A HD22 1 
ATOM   3373 H  HD23 A LEU   A 1 153 ? 17.490 -8.247  5.424   0.66 18.11 ?  153 LEU   A HD23 1 
ATOM   3374 H  HD23 B LEU   A 1 153 ? 17.633 -8.264  6.109   0.34 16.02 ?  153 LEU   A HD23 1 
ATOM   3375 N  N    A ALA   A 1 154 ? 14.973 -5.496  7.667   0.66 15.30 ?  154 ALA   A N    1 
ATOM   3376 N  N    B ALA   A 1 154 ? 14.868 -5.184  8.139   0.34 14.75 ?  154 ALA   A N    1 
ATOM   3377 C  CA   A ALA   A 1 154 ? 14.115 -4.349  7.931   0.66 16.12 ?  154 ALA   A CA   1 
ATOM   3378 C  CA   B ALA   A 1 154 ? 13.953 -4.064  8.307   0.34 15.44 ?  154 ALA   A CA   1 
ATOM   3379 C  C    A ALA   A 1 154 ? 13.595 -3.807  6.609   0.66 17.16 ?  154 ALA   A C    1 
ATOM   3380 C  C    B ALA   A 1 154 ? 13.547 -3.586  6.917   0.34 15.97 ?  154 ALA   A C    1 
ATOM   3381 O  O    A ALA   A 1 154 ? 14.385 -3.468  5.717   0.66 17.34 ?  154 ALA   A O    1 
ATOM   3382 O  O    B ALA   A 1 154 ? 14.400 -3.144  6.139   0.34 15.79 ?  154 ALA   A O    1 
ATOM   3383 C  CB   A ALA   A 1 154 ? 14.887 -3.250  8.658   0.66 16.26 ?  154 ALA   A CB   1 
ATOM   3384 C  CB   B ALA   A 1 154 ? 14.632 -2.937  9.086   0.34 15.63 ?  154 ALA   A CB   1 
ATOM   3385 H  H    A ALA   A 1 154 ? 15.766 -5.283  7.402   0.66 18.42 ?  154 ALA   A H    1 
ATOM   3386 H  H    B ALA   A 1 154 ? 15.656 -4.938  7.883   0.34 17.76 ?  154 ALA   A H    1 
ATOM   3387 H  HA   A ALA   A 1 154 ? 13.363 -4.627  8.479   0.66 19.40 ?  154 ALA   A HA   1 
ATOM   3388 H  HA   B ALA   A 1 154 ? 13.165 -4.345  8.796   0.34 18.58 ?  154 ALA   A HA   1 
ATOM   3389 H  HB1  A ALA   A 1 154 ? 14.292 -2.502  8.814   0.66 19.57 ?  154 ALA   A HB1  1 
ATOM   3390 H  HB1  B ALA   A 1 154 ? 14.000 -2.212  9.215   0.34 18.81 ?  154 ALA   A HB1  1 
ATOM   3391 H  HB2  A ALA   A 1 154 ? 15.216 -3.597  9.501   0.66 19.57 ?  154 ALA   A HB2  1 
ATOM   3392 H  HB2  B ALA   A 1 154 ? 14.925 -3.276  9.948   0.34 18.81 ?  154 ALA   A HB2  1 
ATOM   3393 H  HB3  A ALA   A 1 154 ? 15.633 -2.970  8.101   0.66 19.57 ?  154 ALA   A HB3  1 
ATOM   3394 H  HB3  B ALA   A 1 154 ? 15.399 -2.620  8.582   0.34 18.81 ?  154 ALA   A HB3  1 
ATOM   3395 N  N    A VAL   A 1 155 ? 12.273 -3.714  6.500   0.66 18.51 ?  155 VAL   A N    1 
ATOM   3396 N  N    B VAL   A 1 155 ? 12.256 -3.694  6.603   0.34 17.17 ?  155 VAL   A N    1 
ATOM   3397 C  CA   A VAL   A 1 155 ? 11.594 -3.213  5.312   0.66 19.56 ?  155 VAL   A CA   1 
ATOM   3398 C  CA   B VAL   A 1 155 ? 11.707 -3.341  5.295   0.34 17.56 ?  155 VAL   A CA   1 
ATOM   3399 C  C    A VAL   A 1 155 ? 10.882 -1.922  5.703   0.66 20.53 ?  155 VAL   A C    1 
ATOM   3400 C  C    B VAL   A 1 155 ? 10.861 -2.082  5.461   0.34 18.11 ?  155 VAL   A C    1 
ATOM   3401 O  O    A VAL   A 1 155 ? 9.949  -1.941  6.515   0.66 21.84 ?  155 VAL   A O    1 
ATOM   3402 O  O    B VAL   A 1 155 ? 9.878  -2.077  6.211   0.34 18.34 ?  155 VAL   A O    1 
ATOM   3403 C  CB   A VAL   A 1 155 ? 10.617 -4.247  4.735   0.66 19.46 ?  155 VAL   A CB   1 
ATOM   3404 C  CB   B VAL   A 1 155 ? 10.888 -4.494  4.688   0.34 17.54 ?  155 VAL   A CB   1 
ATOM   3405 C  CG1  A VAL   A 1 155 ? 9.904  -3.684  3.521   0.66 20.22 ?  155 VAL   A CG1  1 
ATOM   3406 C  CG1  B VAL   A 1 155 ? 10.150 -4.029  3.441   0.34 17.60 ?  155 VAL   A CG1  1 
ATOM   3407 C  CG2  A VAL   A 1 155 ? 11.364 -5.536  4.379   0.66 19.57 ?  155 VAL   A CG2  1 
ATOM   3408 C  CG2  B VAL   A 1 155 ? 11.798 -5.666  4.349   0.34 17.73 ?  155 VAL   A CG2  1 
ATOM   3409 H  H    A VAL   A 1 155 ? 11.729 -3.961  7.127   0.66 22.27 ?  155 VAL   A H    1 
ATOM   3410 H  H    B VAL   A 1 155 ? 11.664 -3.977  7.154   0.34 20.66 ?  155 VAL   A H    1 
ATOM   3411 H  HA   A VAL   A 1 155 ? 12.253 -3.002  4.639   0.66 23.53 ?  155 VAL   A HA   1 
ATOM   3412 H  HA   B VAL   A 1 155 ? 12.435 -3.143  4.683   0.34 21.13 ?  155 VAL   A HA   1 
ATOM   3413 H  HB   A VAL   A 1 155 ? 9.947  -4.461  5.405   0.66 23.40 ?  155 VAL   A HB   1 
ATOM   3414 H  HB   B VAL   A 1 155 ? 10.235 -4.802  5.334   0.34 21.10 ?  155 VAL   A HB   1 
ATOM   3415 H  HG11 A VAL   A 1 155 ? 9.422  -4.402  3.080   0.66 24.32 ?  155 VAL   A HG11 1 
ATOM   3416 H  HG11 B VAL   A 1 155 ? 9.784  -4.801  2.988   0.34 21.17 ?  155 VAL   A HG11 1 
ATOM   3417 H  HG12 A VAL   A 1 155 ? 9.279  -2.998  3.808   0.66 24.32 ?  155 VAL   A HG12 1 
ATOM   3418 H  HG12 B VAL   A 1 155 ? 9.427  -3.436  3.696   0.34 21.17 ?  155 VAL   A HG12 1 
ATOM   3419 H  HG13 A VAL   A 1 155 ? 10.559 -3.306  2.917   0.66 24.32 ?  155 VAL   A HG13 1 
ATOM   3420 H  HG13 B VAL   A 1 155 ? 10.770 -3.570  2.854   0.34 21.17 ?  155 VAL   A HG13 1 
ATOM   3421 H  HG21 A VAL   A 1 155 ? 10.744 -6.157  3.966   0.66 23.54 ?  155 VAL   A HG21 1 
ATOM   3422 H  HG21 B VAL   A 1 155 ? 11.298 -6.317  3.831   0.34 21.34 ?  155 VAL   A HG21 1 
ATOM   3423 H  HG22 A VAL   A 1 155 ? 12.082 -5.325  3.761   0.66 23.54 ?  155 VAL   A HG22 1 
ATOM   3424 H  HG22 B VAL   A 1 155 ? 12.550 -5.341  3.829   0.34 21.34 ?  155 VAL   A HG22 1 
ATOM   3425 H  HG23 A VAL   A 1 155 ? 11.730 -5.925  5.189   0.66 23.54 ?  155 VAL   A HG23 1 
ATOM   3426 H  HG23 B VAL   A 1 155 ? 12.115 -6.069  5.172   0.34 21.34 ?  155 VAL   A HG23 1 
ATOM   3427 N  N    A PHE   A 1 156 ? 11.317 -0.801  5.120   0.66 20.85 ?  156 PHE   A N    1 
ATOM   3428 N  N    B PHE   A 1 156 ? 11.231 -1.026  4.733   0.34 19.11 ?  156 PHE   A N    1 
ATOM   3429 C  CA   A PHE   A 1 156 ? 10.772 0.500   5.501   0.66 21.93 ?  156 PHE   A CA   1 
ATOM   3430 C  CA   B PHE   A 1 156 ? 10.708 0.314   4.996   0.34 19.92 ?  156 PHE   A CA   1 
ATOM   3431 C  C    A PHE   A 1 156 ? 9.301  0.629   5.125   0.66 22.11 ?  156 PHE   A C    1 
ATOM   3432 C  C    B PHE   A 1 156 ? 9.230  0.451   4.629   0.34 20.55 ?  156 PHE   A C    1 
ATOM   3433 O  O    A PHE   A 1 156 ? 8.483  1.098   5.928   0.66 23.43 ?  156 PHE   A O    1 
ATOM   3434 O  O    B PHE   A 1 156 ? 8.487  1.170   5.308   0.34 21.18 ?  156 PHE   A O    1 
ATOM   3435 C  CB   A PHE   A 1 156 ? 11.590 1.612   4.841   0.66 22.75 ?  156 PHE   A CB   1 
ATOM   3436 C  CB   B PHE   A 1 156 ? 11.563 1.339   4.241   0.34 20.44 ?  156 PHE   A CB   1 
ATOM   3437 C  CG   A PHE   A 1 156 ? 11.109 2.995   5.169   0.66 24.17 ?  156 PHE   A CG   1 
ATOM   3438 C  CG   B PHE   A 1 156 ? 11.250 2.776   4.575   0.34 21.35 ?  156 PHE   A CG   1 
ATOM   3439 C  CD1  A PHE   A 1 156 ? 11.032 3.412   6.485   0.66 24.73 ?  156 PHE   A CD1  1 
ATOM   3440 C  CD1  B PHE   A 1 156 ? 11.888 3.415   5.631   0.34 21.74 ?  156 PHE   A CD1  1 
ATOM   3441 C  CD2  A PHE   A 1 156 ? 10.752 3.882   4.164   0.66 24.87 ?  156 PHE   A CD2  1 
ATOM   3442 C  CD2  B PHE   A 1 156 ? 10.343 3.495   3.815   0.34 21.93 ?  156 PHE   A CD2  1 
ATOM   3443 C  CE1  A PHE   A 1 156 ? 10.592 4.686   6.799   0.66 25.70 ?  156 PHE   A CE1  1 
ATOM   3444 C  CE1  B PHE   A 1 156 ? 11.610 4.738   5.932   0.34 22.02 ?  156 PHE   A CE1  1 
ATOM   3445 C  CE2  A PHE   A 1 156 ? 10.312 5.162   4.470   0.66 25.82 ?  156 PHE   A CE2  1 
ATOM   3446 C  CE2  B PHE   A 1 156 ? 10.058 4.818   4.112   0.34 22.20 ?  156 PHE   A CE2  1 
ATOM   3447 C  CZ   A PHE   A 1 156 ? 10.236 5.564   5.791   0.66 26.26 ?  156 PHE   A CZ   1 
ATOM   3448 C  CZ   B PHE   A 1 156 ? 10.695 5.441   5.171   0.34 22.30 ?  156 PHE   A CZ   1 
ATOM   3449 H  H    A PHE   A 1 156 ? 11.919 -0.768  4.506   0.66 25.08 ?  156 PHE   A H    1 
ATOM   3450 H  H    B PHE   A 1 156 ? 11.797 -1.060  4.099   0.34 22.98 ?  156 PHE   A H    1 
ATOM   3451 H  HA   A PHE   A 1 156 ? 10.843 0.613   6.455   0.66 26.37 ?  156 PHE   A HA   1 
ATOM   3452 H  HA   B PHE   A 1 156 ? 10.795 0.494   5.941   0.34 23.96 ?  156 PHE   A HA   1 
ATOM   3453 H  HB2  A PHE   A 1 156 ? 12.511 1.547   5.139   0.66 27.35 ?  156 PHE   A HB2  1 
ATOM   3454 H  HB2  B PHE   A 1 156 ? 12.497 1.185   4.460   0.34 24.58 ?  156 PHE   A HB2  1 
ATOM   3455 H  HB3  A PHE   A 1 156 ? 11.550 1.512   3.876   0.66 27.35 ?  156 PHE   A HB3  1 
ATOM   3456 H  HB3  B PHE   A 1 156 ? 11.428 1.222   3.289   0.34 24.58 ?  156 PHE   A HB3  1 
ATOM   3457 H  HD1  A PHE   A 1 156 ? 11.273 2.825   7.163   0.66 29.73 ?  156 PHE   A HD1  1 
ATOM   3458 H  HD1  B PHE   A 1 156 ? 12.503 2.946   6.148   0.34 26.14 ?  156 PHE   A HD1  1 
ATOM   3459 H  HD2  A PHE   A 1 156 ? 10.803 3.615   3.273   0.66 29.90 ?  156 PHE   A HD2  1 
ATOM   3460 H  HD2  B PHE   A 1 156 ? 9.911  3.082   3.103   0.34 26.37 ?  156 PHE   A HD2  1 
ATOM   3461 H  HE1  A PHE   A 1 156 ? 10.544 4.952   7.689   0.66 30.90 ?  156 PHE   A HE1  1 
ATOM   3462 H  HE1  B PHE   A 1 156 ? 12.036 5.153   6.647   0.34 26.48 ?  156 PHE   A HE1  1 
ATOM   3463 H  HE2  A PHE   A 1 156 ? 10.072 5.747   3.790   0.66 31.04 ?  156 PHE   A HE2  1 
ATOM   3464 H  HE2  B PHE   A 1 156 ? 9.441  5.288   3.597   0.34 26.69 ?  156 PHE   A HE2  1 
ATOM   3465 H  HZ   A PHE   A 1 156 ? 9.941  6.420   6.001   0.66 31.57 ?  156 PHE   A HZ   1 
ATOM   3466 H  HZ   B PHE   A 1 156 ? 10.504 6.329   5.373   0.34 26.81 ?  156 PHE   A HZ   1 
ATOM   3467 N  N    A ASP   A 1 157 ? 8.956  0.261   3.896   0.66 21.84 ?  157 ASP   A N    1 
ATOM   3468 N  N    B ASP   A 1 157 ? 8.779  -0.211  3.564   0.34 20.80 ?  157 ASP   A N    1 
ATOM   3469 C  CA   A ASP   A 1 157 ? 7.629  0.520   3.354   0.66 22.78 ?  157 ASP   A CA   1 
ATOM   3470 C  CA   B ASP   A 1 157 ? 7.443  0.013   3.017   0.34 20.69 ?  157 ASP   A CA   1 
ATOM   3471 C  C    A ASP   A 1 157 ? 6.649  -0.516  3.890   0.66 22.72 ?  157 ASP   A C    1 
ATOM   3472 C  C    B ASP   A 1 157 ? 6.488  -1.075  3.497   0.34 19.59 ?  157 ASP   A C    1 
ATOM   3473 O  O    A ASP   A 1 157 ? 6.846  -1.720  3.688   0.66 22.71 ?  157 ASP   A O    1 
ATOM   3474 O  O    B ASP   A 1 157 ? 6.703  -2.261  3.222   0.34 18.96 ?  157 ASP   A O    1 
ATOM   3475 C  CB   A ASP   A 1 157 ? 7.693  0.431   1.833   0.66 24.34 ?  157 ASP   A CB   1 
ATOM   3476 C  CB   B ASP   A 1 157 ? 7.483  0.029   1.491   0.34 21.81 ?  157 ASP   A CB   1 
ATOM   3477 C  CG   A ASP   A 1 157 ? 6.420  0.892   1.176   0.66 25.54 ?  157 ASP   A CG   1 
ATOM   3478 C  CG   B ASP   A 1 157 ? 6.114  0.247   0.878   0.34 22.79 ?  157 ASP   A CG   1 
ATOM   3479 O  OD1  A ASP   A 1 157 ? 6.225  2.116   1.047   0.66 27.29 ?  157 ASP   A OD1  1 
ATOM   3480 O  OD1  B ASP   A 1 157 ? 5.282  0.906   1.533   0.34 23.73 ?  157 ASP   A OD1  1 
ATOM   3481 O  OD2  A ASP   A 1 157 ? 5.601  0.029   0.801   0.66 25.44 -1 157 ASP   A OD2  1 
ATOM   3482 O  OD2  B ASP   A 1 157 ? 5.861  -0.248  -0.242  0.34 22.99 -1 157 ASP   A OD2  1 
ATOM   3483 H  H    A ASP   A 1 157 ? 9.477  -0.139  3.343   0.66 26.26 ?  157 ASP   A H    1 
ATOM   3484 H  H    B ASP   A 1 157 ? 9.226  -0.813  3.143   0.34 25.01 ?  157 ASP   A H    1 
ATOM   3485 H  HA   A ASP   A 1 157 ? 7.322  1.411   3.600   0.66 27.39 ?  157 ASP   A HA   1 
ATOM   3486 H  HA   B ASP   A 1 157 ? 7.106  0.868   3.325   0.34 24.88 ?  157 ASP   A HA   1 
ATOM   3487 H  HB2  A ASP   A 1 157 ? 8.431  0.972   1.508   0.66 29.26 ?  157 ASP   A HB2  1 
ATOM   3488 H  HB2  B ASP   A 1 157 ? 8.055  0.755   1.207   0.34 26.22 ?  157 ASP   A HB2  1 
ATOM   3489 H  HB3  A ASP   A 1 157 ? 7.823  -0.492  1.571   0.66 29.26 ?  157 ASP   A HB3  1 
ATOM   3490 H  HB3  B ASP   A 1 157 ? 7.837  -0.813  1.173   0.34 26.22 ?  157 ASP   A HB3  1 
ATOM   3491 N  N    A LYS   A 1 158 ? 5.584  -0.055  4.559   0.66 23.97 ?  158 LYS   A N    1 
ATOM   3492 N  N    B LYS   A 1 158 ? 5.413  -0.663  4.181   0.34 19.99 ?  158 LYS   A N    1 
ATOM   3493 C  CA   A LYS   A 1 158 ? 4.617  -1.001  5.108   0.66 24.90 ?  158 LYS   A CA   1 
ATOM   3494 C  CA   B LYS   A 1 158 ? 4.486  -1.630  4.768   0.34 20.33 ?  158 LYS   A CA   1 
ATOM   3495 C  C    A LYS   A 1 158 ? 3.923  -1.774  3.998   0.66 24.28 ?  158 LYS   A C    1 
ATOM   3496 C  C    B LYS   A 1 158 ? 3.792  -2.460  3.691   0.34 19.43 ?  158 LYS   A C    1 
ATOM   3497 O  O    A LYS   A 1 158 ? 3.732  -2.992  4.104   0.66 24.08 ?  158 LYS   A O    1 
ATOM   3498 O  O    B LYS   A 1 158 ? 3.714  -3.688  3.792   0.34 19.12 ?  158 LYS   A O    1 
ATOM   3499 C  CB   A LYS   A 1 158 ? 3.600  -0.280  5.998   0.66 26.47 ?  158 LYS   A CB   1 
ATOM   3500 C  CB   B LYS   A 1 158 ? 3.469  -0.912  5.662   0.34 22.06 ?  158 LYS   A CB   1 
ATOM   3501 C  CG   A LYS   A 1 158 ? 2.390  -1.133  6.411   0.66 28.20 ?  158 LYS   A CG   1 
ATOM   3502 C  CG   B LYS   A 1 158 ? 2.319  -1.796  6.138   0.34 23.72 ?  158 LYS   A CG   1 
ATOM   3503 C  CD   A LYS   A 1 158 ? 2.784  -2.421  7.153   0.66 29.47 ?  158 LYS   A CD   1 
ATOM   3504 C  CD   B LYS   A 1 158 ? 1.981  -1.541  7.601   0.34 25.03 ?  158 LYS   A CD   1 
ATOM   3505 C  CE   A LYS   A 1 158 ? 1.540  -3.198  7.606   0.66 30.69 ?  158 LYS   A CE   1 
ATOM   3506 C  CE   B LYS   A 1 158 ? 2.408  -2.709  8.480   0.34 26.10 ?  158 LYS   A CE   1 
ATOM   3507 N  NZ   A LYS   A 1 158 ? 1.852  -4.554  8.160   0.66 31.21 ?  158 LYS   A NZ   1 
ATOM   3508 N  NZ   B LYS   A 1 158 ? 1.341  -3.741  8.612   0.34 26.66 ?  158 LYS   A NZ   1 
ATOM   3509 H  H    A LYS   A 1 158 ? 5.405  0.772   4.705   0.66 28.82 ?  158 LYS   A H    1 
ATOM   3510 H  H    B LYS   A 1 158 ? 5.202  0.162   4.323   0.34 24.04 ?  158 LYS   A H    1 
ATOM   3511 H  HA   A LYS   A 1 158 ? 5.084  -1.642  5.664   0.66 29.93 ?  158 LYS   A HA   1 
ATOM   3512 H  HA   B LYS   A 1 158 ? 4.984  -2.236  5.335   0.34 24.45 ?  158 LYS   A HA   1 
ATOM   3513 H  HB2  A LYS   A 1 158 ? 4.045  0.005   6.813   0.66 31.82 ?  158 LYS   A HB2  1 
ATOM   3514 H  HB2  B LYS   A 1 158 ? 3.933  -0.575  6.449   0.34 26.52 ?  158 LYS   A HB2  1 
ATOM   3515 H  HB3  A LYS   A 1 158 ? 3.262  0.495   5.524   0.66 31.82 ?  158 LYS   A HB3  1 
ATOM   3516 H  HB3  B LYS   A 1 158 ? 3.082  -0.170  5.173   0.34 26.52 ?  158 LYS   A HB3  1 
ATOM   3517 H  HG2  A LYS   A 1 158 ? 1.828  -0.612  7.004   0.66 33.89 ?  158 LYS   A HG2  1 
ATOM   3518 H  HG2  B LYS   A 1 158 ? 1.528  -1.602  5.611   0.34 28.52 ?  158 LYS   A HG2  1 
ATOM   3519 H  HG3  A LYS   A 1 158 ? 1.886  -1.383  5.620   0.66 33.89 ?  158 LYS   A HG3  1 
ATOM   3520 H  HG3  B LYS   A 1 158 ? 2.564  -2.729  6.043   0.34 28.52 ?  158 LYS   A HG3  1 
ATOM   3521 H  HD2  A LYS   A 1 158 ? 3.301  -2.988  6.562   0.66 35.42 ?  158 LYS   A HD2  1 
ATOM   3522 H  HD2  B LYS   A 1 158 ? 2.437  -0.743  7.914   0.34 30.09 ?  158 LYS   A HD2  1 
ATOM   3523 H  HD3  A LYS   A 1 158 ? 3.303  -2.189  7.939   0.66 35.42 ?  158 LYS   A HD3  1 
ATOM   3524 H  HD3  B LYS   A 1 158 ? 1.023  -1.431  7.689   0.34 30.09 ?  158 LYS   A HD3  1 
ATOM   3525 H  HE2  A LYS   A 1 158 ? 1.090  -2.691  8.298   0.66 36.88 ?  158 LYS   A HE2  1 
ATOM   3526 H  HE2  B LYS   A 1 158 ? 3.189  -3.134  8.093   0.34 31.38 ?  158 LYS   A HE2  1 
ATOM   3527 H  HE3  A LYS   A 1 158 ? 0.952  -3.316  6.845   0.66 36.88 ?  158 LYS   A HE3  1 
ATOM   3528 H  HE3  B LYS   A 1 158 ? 2.613  -2.378  9.364   0.34 31.38 ?  158 LYS   A HE3  1 
ATOM   3529 H  HZ1  A LYS   A 1 158 ? 1.100  -4.962  8.406   0.66 37.51 ?  158 LYS   A HZ1  1 
ATOM   3530 H  HZ1  B LYS   A 1 158 ? 1.624  -4.405  9.133   0.34 32.04 ?  158 LYS   A HZ1  1 
ATOM   3531 H  HZ2  A LYS   A 1 158 ? 2.259  -5.050  7.542   0.66 37.51 ?  158 LYS   A HZ2  1 
ATOM   3532 H  HZ2  B LYS   A 1 158 ? 0.613  -3.380  8.977   0.34 32.04 ?  158 LYS   A HZ2  1 
ATOM   3533 H  HZ3  A LYS   A 1 158 ? 2.385  -4.479  8.868   0.66 37.51 ?  158 LYS   A HZ3  1 
ATOM   3534 H  HZ3  B LYS   A 1 158 ? 1.131  -4.069  7.813   0.34 32.04 ?  158 LYS   A HZ3  1 
ATOM   3535 N  N    A ASN   A 1 159 ? 3.541  -1.090  2.920   0.66 24.98 ?  159 ASN   A N    1 
ATOM   3536 N  N    B ASN   A 1 159 ? 3.280  -1.807  2.649   0.34 19.40 ?  159 ASN   A N    1 
ATOM   3537 C  CA   A ASN   A 1 159 ? 2.894  -1.790  1.818   0.66 25.39 ?  159 ASN   A CA   1 
ATOM   3538 C  CA   B ASN   A 1 159 ? 2.608  -2.543  1.582   0.34 20.22 ?  159 ASN   A CA   1 
ATOM   3539 C  C    A ASN   A 1 159 ? 3.809  -2.863  1.238   0.66 24.54 ?  159 ASN   A C    1 
ATOM   3540 C  C    B ASN   A 1 159 ? 3.560  -3.546  0.934   0.34 18.94 ?  159 ASN   A C    1 
ATOM   3541 O  O    A ASN   A 1 159 ? 3.368  -3.986  0.972   0.66 23.88 ?  159 ASN   A O    1 
ATOM   3542 O  O    B ASN   A 1 159 ? 3.168  -4.677  0.612   0.34 19.06 ?  159 ASN   A O    1 
ATOM   3543 C  CB   A ASN   A 1 159 ? 2.426  -0.792  0.753   0.66 27.23 ?  159 ASN   A CB   1 
ATOM   3544 C  CB   B ASN   A 1 159 ? 2.037  -1.547  0.572   0.34 22.75 ?  159 ASN   A CB   1 
ATOM   3545 C  CG   A ASN   A 1 159 ? 1.128  -0.096  1.138   0.66 29.89 ?  159 ASN   A CG   1 
ATOM   3546 C  CG   B ASN   A 1 159 ? 1.353  -0.367  1.247   0.34 25.21 ?  159 ASN   A CG   1 
ATOM   3547 O  OD1  A ASN   A 1 159 ? 0.250  -0.703  1.744   0.66 31.60 ?  159 ASN   A OD1  1 
ATOM   3548 O  OD1  B ASN   A 1 159 ? 1.778  0.776   1.095   0.34 26.26 ?  159 ASN   A OD1  1 
ATOM   3549 N  ND2  A ASN   A 1 159 ? 1.004  1.180   0.786   0.66 30.60 ?  159 ASN   A ND2  1 
ATOM   3550 N  ND2  B ASN   A 1 159 ? 0.302  -0.647  2.016   0.34 26.07 ?  159 ASN   A ND2  1 
ATOM   3551 H  H    A ASN   A 1 159 ? 3.641  -0.242  2.808   0.66 30.03 ?  159 ASN   A H    1 
ATOM   3552 H  H    B ASN   A 1 159 ? 3.316  -0.952  2.544   0.34 23.34 ?  159 ASN   A H    1 
ATOM   3553 H  HA   A ASN   A 1 159 ? 2.100  -2.235  2.158   0.66 30.52 ?  159 ASN   A HA   1 
ATOM   3554 H  HA   B ASN   A 1 159 ? 1.867  -3.034  1.959   0.34 24.32 ?  159 ASN   A HA   1 
ATOM   3555 H  HB2  A ASN   A 1 159 ? 3.097  -0.106  0.635   0.66 32.73 ?  159 ASN   A HB2  1 
ATOM   3556 H  HB2  B ASN   A 1 159 ? 2.754  -1.191  0.024   0.34 27.36 ?  159 ASN   A HB2  1 
ATOM   3557 H  HB3  A ASN   A 1 159 ? 2.272  -1.261  -0.082  0.66 32.73 ?  159 ASN   A HB3  1 
ATOM   3558 H  HB3  B ASN   A 1 159 ? 1.377  -1.987  0.020   0.34 27.36 ?  159 ASN   A HB3  1 
ATOM   3559 H  HD21 A ASN   A 1 159 ? 0.285  1.613   0.980   0.66 36.78 ?  159 ASN   A HD21 1 
ATOM   3560 H  HD21 B ASN   A 1 159 ? -0.119 -0.017  2.429   0.34 31.33 ?  159 ASN   A HD21 1 
ATOM   3561 H  HD22 A ASN   A 1 159 ? 1.640  1.570   0.364   0.66 36.78 ?  159 ASN   A HD22 1 
ATOM   3562 H  HD22 B ASN   A 1 159 ? 0.035  -1.461  2.098   0.34 31.33 ?  159 ASN   A HD22 1 
ATOM   3563 N  N    A LEU   A 1 160 ? 5.093  -2.558  1.072   0.66 23.80 ?  160 LEU   A N    1 
ATOM   3564 N  N    B LEU   A 1 160 ? 4.826  -3.157  0.768   0.34 18.26 ?  160 LEU   A N    1 
ATOM   3565 C  CA   A LEU   A 1 160 ? 5.991  -3.564  0.516   0.66 23.29 ?  160 LEU   A CA   1 
ATOM   3566 C  CA   B LEU   A 1 160 ? 5.846  -4.087  0.294   0.34 18.48 ?  160 LEU   A CA   1 
ATOM   3567 C  C    A LEU   A 1 160 ? 6.136  -4.754  1.454   0.66 22.96 ?  160 LEU   A C    1 
ATOM   3568 C  C    B LEU   A 1 160 ? 6.134  -5.160  1.339   0.34 18.72 ?  160 LEU   A C    1 
ATOM   3569 O  O    A LEU   A 1 160 ? 6.185  -5.904  1.005   0.66 24.19 ?  160 LEU   A O    1 
ATOM   3570 O  O    B LEU   A 1 160 ? 6.166  -6.354  1.023   0.34 19.17 ?  160 LEU   A O    1 
ATOM   3571 C  CB   A LEU   A 1 160 ? 7.355  -2.962  0.198   0.66 23.25 ?  160 LEU   A CB   1 
ATOM   3572 C  CB   B LEU   A 1 160 ? 7.115  -3.307  -0.040  0.34 18.61 ?  160 LEU   A CB   1 
ATOM   3573 C  CG   A LEU   A 1 160 ? 8.355  -4.016  -0.284  0.66 23.71 ?  160 LEU   A CG   1 
ATOM   3574 C  CG   B LEU   A 1 160 ? 8.370  -4.100  -0.386  0.34 19.17 ?  160 LEU   A CG   1 
ATOM   3575 C  CD1  A LEU   A 1 160 ? 7.862  -4.680  -1.558  0.66 24.38 ?  160 LEU   A CD1  1 
ATOM   3576 C  CD1  B LEU   A 1 160 ? 8.065  -5.077  -1.490  0.34 19.50 ?  160 LEU   A CD1  1 
ATOM   3577 C  CD2  A LEU   A 1 160 ? 9.715  -3.398  -0.497  0.66 23.14 ?  160 LEU   A CD2  1 
ATOM   3578 C  CD2  B LEU   A 1 160 ? 9.481  -3.143  -0.796  0.34 19.13 ?  160 LEU   A CD2  1 
ATOM   3579 H  H    A LEU   A 1 160 ? 5.455  -1.803  1.276   0.66 28.62 ?  160 LEU   A H    1 
ATOM   3580 H  H    B LEU   A 1 160 ? 5.120  -2.361  0.925   0.34 21.96 ?  160 LEU   A H    1 
ATOM   3581 H  HA   A LEU   A 1 160 ? 5.605  -3.886  -0.310  0.66 28.00 ?  160 LEU   A HA   1 
ATOM   3582 H  HA   B LEU   A 1 160 ? 5.529  -4.516  -0.516  0.34 22.24 ?  160 LEU   A HA   1 
ATOM   3583 H  HB2  A LEU   A 1 160 ? 7.253  -2.291  -0.500  0.66 27.95 ?  160 LEU   A HB2  1 
ATOM   3584 H  HB2  B LEU   A 1 160 ? 6.927  -2.725  -0.793  0.34 22.39 ?  160 LEU   A HB2  1 
ATOM   3585 H  HB3  A LEU   A 1 160 ? 7.714  -2.555  1.000   0.66 27.95 ?  160 LEU   A HB3  1 
ATOM   3586 H  HB3  B LEU   A 1 160 ? 7.332  -2.772  0.734   0.34 22.39 ?  160 LEU   A HB3  1 
ATOM   3587 H  HG   A LEU   A 1 160 ? 8.452  -4.703  0.392   0.66 28.50 ?  160 LEU   A HG   1 
ATOM   3588 H  HG   B LEU   A 1 160 ? 8.668  -4.592  0.396   0.34 23.05 ?  160 LEU   A HG   1 
ATOM   3589 H  HD11 A LEU   A 1 160 ? 8.572  -5.234  -1.914  0.66 29.31 ?  160 LEU   A HD11 1 
ATOM   3590 H  HD11 B LEU   A 1 160 ? 8.879  -5.534  -1.737  0.34 23.46 ?  160 LEU   A HD11 1 
ATOM   3591 H  HD12 A LEU   A 1 160 ? 7.088  -5.229  -1.353  0.66 29.31 ?  160 LEU   A HD12 1 
ATOM   3592 H  HD12 B LEU   A 1 160 ? 7.407  -5.714  -1.173  0.34 23.46 ?  160 LEU   A HD12 1 
ATOM   3593 H  HD13 A LEU   A 1 160 ? 7.622  -3.994  -2.200  0.66 29.31 ?  160 LEU   A HD13 1 
ATOM   3594 H  HD13 B LEU   A 1 160 ? 7.712  -4.586  -2.250  0.34 23.46 ?  160 LEU   A HD13 1 
ATOM   3595 H  HD21 A LEU   A 1 160 ? 10.327 -4.087  -0.796  0.66 27.82 ?  160 LEU   A HD21 1 
ATOM   3596 H  HD21 B LEU   A 1 160 ? 10.277 -3.652  -1.011  0.34 23.01 ?  160 LEU   A HD21 1 
ATOM   3597 H  HD22 A LEU   A 1 160 ? 9.641  -2.703  -1.169  0.66 27.82 ?  160 LEU   A HD22 1 
ATOM   3598 H  HD22 B LEU   A 1 160 ? 9.192  -2.638  -1.575  0.34 23.01 ?  160 LEU   A HD22 1 
ATOM   3599 H  HD23 A LEU   A 1 160 ? 10.021 -3.020  0.341   0.66 27.82 ?  160 LEU   A HD23 1 
ATOM   3600 H  HD23 B LEU   A 1 160 ? 9.666  -2.533  -0.062  0.34 23.01 ?  160 LEU   A HD23 1 
ATOM   3601 N  N    A TYR   A 1 161 ? 6.197  -4.498  2.760   0.66 22.10 ?  161 TYR   A N    1 
ATOM   3602 N  N    B TYR   A 1 161 ? 6.366  -4.749  2.589   0.34 18.58 ?  161 TYR   A N    1 
ATOM   3603 C  CA   A TYR   A 1 161 ? 6.373  -5.583  3.718   0.66 21.72 ?  161 TYR   A CA   1 
ATOM   3604 C  CA   B TYR   A 1 161 ? 6.465  -5.709  3.686   0.34 19.07 ?  161 TYR   A CA   1 
ATOM   3605 C  C    A TYR   A 1 161 ? 5.268  -6.632  3.606   0.66 22.59 ?  161 TYR   A C    1 
ATOM   3606 C  C    B TYR   A 1 161 ? 5.249  -6.621  3.707   0.34 19.99 ?  161 TYR   A C    1 
ATOM   3607 O  O    A TYR   A 1 161 ? 5.547  -7.835  3.639   0.66 22.76 ?  161 TYR   A O    1 
ATOM   3608 O  O    B TYR   A 1 161 ? 5.376  -7.849  3.695   0.34 20.28 ?  161 TYR   A O    1 
ATOM   3609 C  CB   A TYR   A 1 161 ? 6.456  -5.015  5.133   0.66 21.58 ?  161 TYR   A CB   1 
ATOM   3610 C  CB   B TYR   A 1 161 ? 6.597  -4.974  5.024   0.34 19.05 ?  161 TYR   A CB   1 
ATOM   3611 C  CG   A TYR   A 1 161 ? 6.372  -6.066  6.200   0.66 21.04 ?  161 TYR   A CG   1 
ATOM   3612 C  CG   B TYR   A 1 161 ? 6.475  -5.870  6.248   0.34 18.89 ?  161 TYR   A CG   1 
ATOM   3613 C  CD1  A TYR   A 1 161 ? 7.495  -6.794  6.566   0.66 20.27 ?  161 TYR   A CD1  1 
ATOM   3614 C  CD1  B TYR   A 1 161 ? 5.235  -6.137  6.826   0.34 19.13 ?  161 TYR   A CD1  1 
ATOM   3615 C  CD2  A TYR   A 1 161 ? 5.168  -6.341  6.835   0.66 21.48 ?  161 TYR   A CD2  1 
ATOM   3616 C  CD2  B TYR   A 1 161 ? 7.603  -6.434  6.835   0.34 18.77 ?  161 TYR   A CD2  1 
ATOM   3617 C  CE1  A TYR   A 1 161 ? 7.424  -7.763  7.536   0.66 19.80 ?  161 TYR   A CE1  1 
ATOM   3618 C  CE1  B TYR   A 1 161 ? 5.126  -6.954  7.944   0.34 19.10 ?  161 TYR   A CE1  1 
ATOM   3619 C  CE2  A TYR   A 1 161 ? 5.086  -7.306  7.806   0.66 21.00 ?  161 TYR   A CE2  1 
ATOM   3620 C  CE2  B TYR   A 1 161 ? 7.501  -7.250  7.950   0.34 18.97 ?  161 TYR   A CE2  1 
ATOM   3621 C  CZ   A TYR   A 1 161 ? 6.216  -8.016  8.153   0.66 20.10 ?  161 TYR   A CZ   1 
ATOM   3622 C  CZ   B TYR   A 1 161 ? 6.265  -7.505  8.501   0.34 19.28 ?  161 TYR   A CZ   1 
ATOM   3623 O  OH   A TYR   A 1 161 ? 6.133  -8.977  9.127   0.66 19.92 ?  161 TYR   A OH   1 
ATOM   3624 O  OH   B TYR   A 1 161 ? 6.170  -8.318  9.611   0.34 20.04 ?  161 TYR   A OH   1 
ATOM   3625 H  H    A TYR   A 1 161 ? 6.134  -3.718  3.116   0.66 26.57 ?  161 TYR   A H    1 
ATOM   3626 H  H    B TYR   A 1 161 ? 6.473  -3.936  2.819   0.34 22.35 ?  161 TYR   A H    1 
ATOM   3627 H  HA   A TYR   A 1 161 ? 7.205  -6.033  3.532   0.66 26.12 ?  161 TYR   A HA   1 
ATOM   3628 H  HA   B TYR   A 1 161 ? 7.255  -6.259  3.566   0.34 22.94 ?  161 TYR   A HA   1 
ATOM   3629 H  HB2  A TYR   A 1 161 ? 7.308  -4.557  5.235   0.66 25.95 ?  161 TYR   A HB2  1 
ATOM   3630 H  HB2  B TYR   A 1 161 ? 7.466  -4.543  5.057   0.34 22.91 ?  161 TYR   A HB2  1 
ATOM   3631 H  HB3  A TYR   A 1 161 ? 5.728  -4.392  5.273   0.66 25.95 ?  161 TYR   A HB3  1 
ATOM   3632 H  HB3  B TYR   A 1 161 ? 5.898  -4.303  5.078   0.34 22.91 ?  161 TYR   A HB3  1 
ATOM   3633 H  HD1  A TYR   A 1 161 ? 8.308  -6.626  6.147   0.66 24.38 ?  161 TYR   A HD1  1 
ATOM   3634 H  HD1  B TYR   A 1 161 ? 4.466  -5.770  6.456   0.34 23.01 ?  161 TYR   A HD1  1 
ATOM   3635 H  HD2  A TYR   A 1 161 ? 4.407  -5.861  6.601   0.66 25.84 ?  161 TYR   A HD2  1 
ATOM   3636 H  HD2  B TYR   A 1 161 ? 8.441  -6.264  6.469   0.34 22.58 ?  161 TYR   A HD2  1 
ATOM   3637 H  HE1  A TYR   A 1 161 ? 8.182  -8.250  7.772   0.66 23.81 ?  161 TYR   A HE1  1 
ATOM   3638 H  HE1  B TYR   A 1 161 ? 4.291  -7.129  8.320   0.34 22.97 ?  161 TYR   A HE1  1 
ATOM   3639 H  HE2  A TYR   A 1 161 ? 4.272  -7.481  8.224   0.66 25.26 ?  161 TYR   A HE2  1 
ATOM   3640 H  HE2  B TYR   A 1 161 ? 8.267  -7.620  8.331   0.34 22.81 ?  161 TYR   A HE2  1 
ATOM   3641 H  HH   A TYR   A 1 161 ? 5.331  -9.032  9.410   0.66 23.96 ?  161 TYR   A HH   1 
ATOM   3642 H  HH   B TYR   A 1 161 ? 6.927  -8.581  9.850   0.34 24.11 ?  161 TYR   A HH   1 
ATOM   3643 N  N    A ASP   A 1 162 ? 4.010  -6.203  3.470   0.66 23.30 ?  162 ASP   A N    1 
ATOM   3644 N  N    B ASP   A 1 162 ? 4.054  -6.028  3.748   0.34 20.57 ?  162 ASP   A N    1 
ATOM   3645 C  CA   A ASP   A 1 162 ? 2.906  -7.164  3.458   0.66 23.74 ?  162 ASP   A CA   1 
ATOM   3646 C  CA   B ASP   A 1 162 ? 2.835  -6.820  3.639   0.34 21.26 ?  162 ASP   A CA   1 
ATOM   3647 C  C    A ASP   A 1 162 ? 2.946  -8.056  2.220   0.66 23.57 ?  162 ASP   A C    1 
ATOM   3648 C  C    B ASP   A 1 162 ? 2.876  -7.692  2.393   0.34 21.28 ?  162 ASP   A C    1 
ATOM   3649 O  O    A ASP   A 1 162 ? 2.559  -9.229  2.286   0.66 24.63 ?  162 ASP   A O    1 
ATOM   3650 O  O    B ASP   A 1 162 ? 2.577  -8.890  2.447   0.34 22.09 ?  162 ASP   A O    1 
ATOM   3651 C  CB   A ASP   A 1 162 ? 1.556  -6.438  3.534   0.66 24.69 ?  162 ASP   A CB   1 
ATOM   3652 C  CB   B ASP   A 1 162 ? 1.604  -5.909  3.610   0.34 21.97 ?  162 ASP   A CB   1 
ATOM   3653 C  CG   A ASP   A 1 162 ? 1.295  -5.797  4.885   0.66 25.72 ?  162 ASP   A CG   1 
ATOM   3654 C  CG   B ASP   A 1 162 ? 1.277  -5.304  4.966   0.34 22.89 ?  162 ASP   A CG   1 
ATOM   3655 O  OD1  A ASP   A 1 162 ? 2.017  -6.102  5.853   0.66 26.91 ?  162 ASP   A OD1  1 
ATOM   3656 O  OD1  B ASP   A 1 162 ? 1.700  -5.862  5.999   0.34 23.46 ?  162 ASP   A OD1  1 
ATOM   3657 O  OD2  A ASP   A 1 162 ? 0.326  -5.003  4.979   0.66 26.02 -1 162 ASP   A OD2  1 
ATOM   3658 O  OD2  B ASP   A 1 162 ? 0.574  -4.268  4.996   0.34 23.55 -1 162 ASP   A OD2  1 
ATOM   3659 H  H    A ASP   A 1 162 ? 3.760  -5.387  3.374   0.66 28.02 ?  162 ASP   A H    1 
ATOM   3660 H  H    B ASP   A 1 162 ? 3.926  -5.186  3.836   0.34 24.73 ?  162 ASP   A H    1 
ATOM   3661 H  HA   A ASP   A 1 162 ? 2.963  -7.738  4.241   0.66 28.55 ?  162 ASP   A HA   1 
ATOM   3662 H  HA   B ASP   A 1 162 ? 2.763  -7.403  4.406   0.34 25.57 ?  162 ASP   A HA   1 
ATOM   3663 H  HB2  A ASP   A 1 162 ? 1.517  -5.748  2.858   0.66 29.69 ?  162 ASP   A HB2  1 
ATOM   3664 H  HB2  B ASP   A 1 162 ? 1.768  -5.168  3.013   0.34 26.42 ?  162 ASP   A HB2  1 
ATOM   3665 H  HB3  A ASP   A 1 162 ? 0.829  -7.072  3.404   0.66 29.69 ?  162 ASP   A HB3  1 
ATOM   3666 H  HB3  B ASP   A 1 162 ? 0.839  -6.426  3.298   0.34 26.42 ?  162 ASP   A HB3  1 
ATOM   3667 N  N    A LYS   A 1 163 ? 3.409  -7.522  1.092   0.66 23.97 ?  163 LYS   A N    1 
ATOM   3668 N  N    B LYS   A 1 163 ? 3.242  -7.105  1.252   0.34 21.67 ?  163 LYS   A N    1 
ATOM   3669 C  CA   A LYS   A 1 163 ? 3.465  -8.289  -0.149  0.66 24.25 ?  163 LYS   A CA   1 
ATOM   3670 C  CA   B LYS   A 1 163 ? 3.412  -7.903  0.043   0.34 21.80 ?  163 LYS   A CA   1 
ATOM   3671 C  C    A LYS   A 1 163 ? 4.543  -9.369  -0.090  0.66 23.47 ?  163 LYS   A C    1 
ATOM   3672 C  C    B LYS   A 1 163 ? 4.550  -8.902  0.202   0.34 20.56 ?  163 LYS   A C    1 
ATOM   3673 O  O    A LYS   A 1 163 ? 4.352  -10.478 -0.602  0.66 24.59 ?  163 LYS   A O    1 
ATOM   3674 O  O    B LYS   A 1 163 ? 4.448  -10.044 -0.255  0.34 20.94 ?  163 LYS   A O    1 
ATOM   3675 C  CB   A LYS   A 1 163 ? 3.731  -7.324  -1.302  0.66 26.78 ?  163 LYS   A CB   1 
ATOM   3676 C  CB   B LYS   A 1 163 ? 3.657  -6.990  -1.155  0.34 23.87 ?  163 LYS   A CB   1 
ATOM   3677 C  CG   A LYS   A 1 163 ? 3.721  -7.951  -2.672  0.66 29.96 ?  163 LYS   A CG   1 
ATOM   3678 C  CG   B LYS   A 1 163 ? 3.765  -7.689  -2.494  0.34 26.09 ?  163 LYS   A CG   1 
ATOM   3679 C  CD   A LYS   A 1 163 ? 4.098  -6.938  -3.736  0.66 32.55 ?  163 LYS   A CD   1 
ATOM   3680 C  CD   B LYS   A 1 163 ? 3.848  -6.638  -3.587  0.34 28.15 ?  163 LYS   A CD   1 
ATOM   3681 C  CE   A LYS   A 1 163 ? 4.022  -7.554  -5.121  0.66 34.16 ?  163 LYS   A CE   1 
ATOM   3682 C  CE   B LYS   A 1 163 ? 4.430  -7.181  -4.872  0.34 29.52 ?  163 LYS   A CE   1 
ATOM   3683 N  NZ   A LYS   A 1 163 ? 4.676  -6.711  -6.155  0.66 35.85 ?  163 LYS   A NZ   1 
ATOM   3684 N  NZ   B LYS   A 1 163 ? 4.875  -6.079  -5.769  0.34 30.58 ?  163 LYS   A NZ   1 
ATOM   3685 H  H    A LYS   A 1 163 ? 3.698  -6.723  1.030   0.66 28.81 ?  163 LYS   A H    1 
ATOM   3686 H  H    B LYS   A 1 163 ? 3.381  -6.260  1.152   0.34 26.06 ?  163 LYS   A H    1 
ATOM   3687 H  HA   A LYS   A 1 163 ? 2.610  -8.720  -0.300  0.66 29.16 ?  163 LYS   A HA   1 
ATOM   3688 H  HA   B LYS   A 1 163 ? 2.596  -8.401  -0.122  0.34 26.21 ?  163 LYS   A HA   1 
ATOM   3689 H  HB2  A LYS   A 1 163 ? 3.047  -6.636  -1.289  0.66 32.19 ?  163 LYS   A HB2  1 
ATOM   3690 H  HB2  B LYS   A 1 163 ? 2.924  -6.362  -1.222  0.34 28.69 ?  163 LYS   A HB2  1 
ATOM   3691 H  HB3  A LYS   A 1 163 ? 4.602  -6.919  -1.171  0.66 32.19 ?  163 LYS   A HB3  1 
ATOM   3692 H  HB3  B LYS   A 1 163 ? 4.487  -6.513  -1.016  0.34 28.69 ?  163 LYS   A HB3  1 
ATOM   3693 H  HG2  A LYS   A 1 163 ? 4.364  -8.674  -2.700  0.66 36.00 ?  163 LYS   A HG2  1 
ATOM   3694 H  HG2  B LYS   A 1 163 ? 4.569  -8.235  -2.519  0.34 31.37 ?  163 LYS   A HG2  1 
ATOM   3695 H  HG3  A LYS   A 1 163 ? 2.830  -8.280  -2.866  0.66 36.00 ?  163 LYS   A HG3  1 
ATOM   3696 H  HG3  B LYS   A 1 163 ? 2.977  -8.238  -2.646  0.34 31.37 ?  163 LYS   A HG3  1 
ATOM   3697 H  HD2  A LYS   A 1 163 ? 3.479  -6.188  -3.701  0.66 39.11 ?  163 LYS   A HD2  1 
ATOM   3698 H  HD2  B LYS   A 1 163 ? 2.957  -6.308  -3.775  0.34 33.84 ?  163 LYS   A HD2  1 
ATOM   3699 H  HD3  A LYS   A 1 163 ? 5.005  -6.630  -3.582  0.66 39.11 ?  163 LYS   A HD3  1 
ATOM   3700 H  HD3  B LYS   A 1 163 ? 4.417  -5.914  -3.283  0.34 33.84 ?  163 LYS   A HD3  1 
ATOM   3701 H  HE2  A LYS   A 1 163 ? 4.453  -8.422  -5.113  0.66 41.05 ?  163 LYS   A HE2  1 
ATOM   3702 H  HE2  B LYS   A 1 163 ? 5.199  -7.723  -4.654  0.34 35.48 ?  163 LYS   A HE2  1 
ATOM   3703 H  HE3  A LYS   A 1 163 ? 3.092  -7.655  -5.363  0.66 41.05 ?  163 LYS   A HE3  1 
ATOM   3704 H  HE3  B LYS   A 1 163 ? 3.762  -7.710  -5.338  0.34 35.48 ?  163 LYS   A HE3  1 
ATOM   3705 H  HZ1  A LYS   A 1 163 ? 4.615  -7.106  -6.949  0.66 43.07 ?  163 LYS   A HZ1  1 
ATOM   3706 H  HZ1  B LYS   A 1 163 ? 4.186  -5.554  -5.971  0.34 36.76 ?  163 LYS   A HZ1  1 
ATOM   3707 H  HZ2  A LYS   A 1 163 ? 4.277  -5.917  -6.194  0.66 43.07 ?  163 LYS   A HZ2  1 
ATOM   3708 H  HZ2  B LYS   A 1 163 ? 5.500  -5.591  -5.362  0.34 36.76 ?  163 LYS   A HZ2  1 
ATOM   3709 H  HZ3  A LYS   A 1 163 ? 5.535  -6.595  -5.955  0.66 43.07 ?  163 LYS   A HZ3  1 
ATOM   3710 H  HZ3  B LYS   A 1 163 ? 5.215  -6.414  -6.520  0.34 36.76 ?  163 LYS   A HZ3  1 
ATOM   3711 N  N    A LEU   A 1 164 ? 5.695  -9.050  0.508   0.66 21.38 ?  164 LEU   A N    1 
ATOM   3712 N  N    B LEU   A 1 164 ? 5.648  -8.493  0.843   0.34 18.71 ?  164 LEU   A N    1 
ATOM   3713 C  CA   A LEU   A 1 164 ? 6.774  -10.026 0.644   0.66 20.03 ?  164 LEU   A CA   1 
ATOM   3714 C  CA   B LEU   A 1 164 ? 6.759  -9.415  1.065   0.34 17.47 ?  164 LEU   A CA   1 
ATOM   3715 C  C    A LEU   A 1 164 ? 6.335  -11.203 1.502   0.66 19.51 ?  164 LEU   A C    1 
ATOM   3716 C  C    B LEU   A 1 164 ? 6.347  -10.553 1.988   0.34 16.96 ?  164 LEU   A C    1 
ATOM   3717 O  O    A LEU   A 1 164 ? 6.636  -12.361 1.190   0.66 20.49 ?  164 LEU   A O    1 
ATOM   3718 O  O    B LEU   A 1 164 ? 6.652  -11.721 1.726   0.34 16.81 ?  164 LEU   A O    1 
ATOM   3719 C  CB   A LEU   A 1 164 ? 7.998  -9.357  1.273   0.66 20.16 ?  164 LEU   A CB   1 
ATOM   3720 C  CB   B LEU   A 1 164 ? 7.952  -8.667  1.654   0.34 17.09 ?  164 LEU   A CB   1 
ATOM   3721 C  CG   A LEU   A 1 164 ? 8.652  -8.202  0.509   0.66 20.80 ?  164 LEU   A CG   1 
ATOM   3722 C  CG   B LEU   A 1 164 ? 8.848  -7.925  0.665   0.34 17.13 ?  164 LEU   A CG   1 
ATOM   3723 C  CD1  A LEU   A 1 164 ? 9.578  -7.376  1.406   0.66 21.06 ?  164 LEU   A CD1  1 
ATOM   3724 C  CD1  B LEU   A 1 164 ? 9.704  -6.944  1.425   0.34 16.73 ?  164 LEU   A CD1  1 
ATOM   3725 C  CD2  A LEU   A 1 164 ? 9.423  -8.738  -0.683  0.66 20.63 ?  164 LEU   A CD2  1 
ATOM   3726 C  CD2  B LEU   A 1 164 ? 9.713  -8.899  -0.120  0.34 17.15 ?  164 LEU   A CD2  1 
ATOM   3727 H  H    A LEU   A 1 164 ? 5.871  -8.290  0.848   0.66 25.71 ?  164 LEU   A H    1 
ATOM   3728 H  H    B LEU   A 1 164 ? 5.769  -7.703  1.150   0.34 22.50 ?  164 LEU   A H    1 
ATOM   3729 H  HA   A LEU   A 1 164 ? 7.017  -10.371 -0.226  0.66 24.09 ?  164 LEU   A HA   1 
ATOM   3730 H  HA   B LEU   A 1 164 ? 7.032  -9.792  0.213   0.34 21.02 ?  164 LEU   A HA   1 
ATOM   3731 H  HB2  A LEU   A 1 164 ? 7.738  -9.017  2.140   0.66 24.24 ?  164 LEU   A HB2  1 
ATOM   3732 H  HB2  B LEU   A 1 164 ? 7.620  -8.014  2.286   0.34 20.57 ?  164 LEU   A HB2  1 
ATOM   3733 H  HB3  A LEU   A 1 164 ? 8.680  -10.040 1.392   0.66 24.24 ?  164 LEU   A HB3  1 
ATOM   3734 H  HB3  B LEU   A 1 164 ? 8.513  -9.308  2.117   0.34 20.57 ?  164 LEU   A HB3  1 
ATOM   3735 H  HG   A LEU   A 1 164 ? 7.958  -7.614  0.178   0.66 25.02 ?  164 LEU   A HG   1 
ATOM   3736 H  HG   B LEU   A 1 164 ? 8.298  -7.430  0.038   0.34 20.61 ?  164 LEU   A HG   1 
ATOM   3737 H  HD11 A LEU   A 1 164 ? 9.966  -6.658  0.883   0.66 25.33 ?  164 LEU   A HD11 1 
ATOM   3738 H  HD11 B LEU   A 1 164 ? 10.216 -6.410  0.800   0.34 20.13 ?  164 LEU   A HD11 1 
ATOM   3739 H  HD12 A LEU   A 1 164 ? 9.059  -7.006  2.140   0.66 25.33 ?  164 LEU   A HD12 1 
ATOM   3740 H  HD12 B LEU   A 1 164 ? 9.110  -6.380  1.941   0.34 20.13 ?  164 LEU   A HD12 1 
ATOM   3741 H  HD13 A LEU   A 1 164 ? 10.278 -7.949  1.755   0.66 25.33 ?  164 LEU   A HD13 1 
ATOM   3742 H  HD13 B LEU   A 1 164 ? 10.298 -7.432  2.018   0.34 20.13 ?  164 LEU   A HD13 1 
ATOM   3743 H  HD21 A LEU   A 1 164 ? 9.806  -7.993  -1.169  0.66 24.81 ?  164 LEU   A HD21 1 
ATOM   3744 H  HD21 B LEU   A 1 164 ? 10.212 -8.410  -0.794  0.34 20.63 ?  164 LEU   A HD21 1 
ATOM   3745 H  HD22 A LEU   A 1 164 ? 10.126 -9.326  -0.366  0.66 24.81 ?  164 LEU   A HD22 1 
ATOM   3746 H  HD22 B LEU   A 1 164 ? 10.330 -9.337  0.489   0.34 20.63 ?  164 LEU   A HD22 1 
ATOM   3747 H  HD23 A LEU   A 1 164 ? 8.813  -9.229  -1.255  0.66 24.81 ?  164 LEU   A HD23 1 
ATOM   3748 H  HD23 B LEU   A 1 164 ? 9.146  -9.560  -0.547  0.34 20.63 ?  164 LEU   A HD23 1 
ATOM   3749 N  N    A VAL   A 1 165 ? 5.639  -10.917 2.600   0.66 18.29 ?  165 VAL   A N    1 
ATOM   3750 N  N    B VAL   A 1 165 ? 5.664  -10.230 3.085   0.34 16.10 ?  165 VAL   A N    1 
ATOM   3751 C  CA   A VAL   A 1 165 ? 5.164  -11.967 3.494   0.66 17.48 ?  165 VAL   A CA   1 
ATOM   3752 C  CA   B VAL   A 1 165 ? 5.198  -11.273 3.993   0.34 16.36 ?  165 VAL   A CA   1 
ATOM   3753 C  C    A VAL   A 1 165 ? 4.118  -12.827 2.794   0.66 18.39 ?  165 VAL   A C    1 
ATOM   3754 C  C    B VAL   A 1 165 ? 4.136  -12.127 3.317   0.34 16.19 ?  165 VAL   A C    1 
ATOM   3755 O  O    A VAL   A 1 165 ? 4.220  -14.058 2.756   0.66 18.44 ?  165 VAL   A O    1 
ATOM   3756 O  O    B VAL   A 1 165 ? 4.227  -13.360 3.292   0.34 16.29 ?  165 VAL   A O    1 
ATOM   3757 C  CB   A VAL   A 1 165 ? 4.612  -11.334 4.788   0.66 17.50 ?  165 VAL   A CB   1 
ATOM   3758 C  CB   B VAL   A 1 165 ? 4.670  -10.656 5.302   0.34 17.28 ?  165 VAL   A CB   1 
ATOM   3759 C  CG1  A VAL   A 1 165 ? 3.878  -12.363 5.633   0.66 18.12 ?  165 VAL   A CG1  1 
ATOM   3760 C  CG1  B VAL   A 1 165 ? 3.900  -11.699 6.107   0.34 17.92 ?  165 VAL   A CG1  1 
ATOM   3761 C  CG2  A VAL   A 1 165 ? 5.734  -10.682 5.584   0.66 18.08 ?  165 VAL   A CG2  1 
ATOM   3762 C  CG2  B VAL   A 1 165 ? 5.814  -10.076 6.114   0.34 17.49 ?  165 VAL   A CG2  1 
ATOM   3763 H  H    A VAL   A 1 165 ? 5.415  -10.130 2.851   0.66 22.00 ?  165 VAL   A H    1 
ATOM   3764 H  H    B VAL   A 1 165 ? 5.452  -9.430  3.313   0.34 19.38 ?  165 VAL   A H    1 
ATOM   3765 H  HA   A VAL   A 1 165 ? 5.902  -12.544 3.745   0.66 21.03 ?  165 VAL   A HA   1 
ATOM   3766 H  HA   B VAL   A 1 165 ? 5.942  -11.850 4.214   0.34 19.69 ?  165 VAL   A HA   1 
ATOM   3767 H  HB   A VAL   A 1 165 ? 3.976  -10.643 4.556   0.66 21.06 ?  165 VAL   A HB   1 
ATOM   3768 H  HB   B VAL   A 1 165 ? 4.059  -9.933  5.086   0.34 20.80 ?  165 VAL   A HB   1 
ATOM   3769 H  HG11 A VAL   A 1 165 ? 3.783  -12.017 6.537   0.66 21.80 ?  165 VAL   A HG11 1 
ATOM   3770 H  HG11 B VAL   A 1 165 ? 3.833  -11.399 7.026   0.34 21.56 ?  165 VAL   A HG11 1 
ATOM   3771 H  HG12 A VAL   A 1 165 ? 2.999  -12.517 5.250   0.66 21.80 ?  165 VAL   A HG12 1 
ATOM   3772 H  HG12 B VAL   A 1 165 ? 3.010  -11.800 5.730   0.34 21.56 ?  165 VAL   A HG12 1 
ATOM   3773 H  HG13 A VAL   A 1 165 ? 4.388  -13.184 5.646   0.66 21.80 ?  165 VAL   A HG13 1 
ATOM   3774 H  HG13 B VAL   A 1 165 ? 4.375  -12.543 6.069   0.34 21.56 ?  165 VAL   A HG13 1 
ATOM   3775 H  HG21 A VAL   A 1 165 ? 5.368  -10.293 6.396   0.66 21.75 ?  165 VAL   A HG21 1 
ATOM   3776 H  HG21 B VAL   A 1 165 ? 5.460  -9.715  6.941   0.34 21.05 ?  165 VAL   A HG21 1 
ATOM   3777 H  HG22 A VAL   A 1 165 ? 6.396  -11.355 5.813   0.66 21.75 ?  165 VAL   A HG22 1 
ATOM   3778 H  HG22 B VAL   A 1 165 ? 6.452  -10.780 6.305   0.34 21.05 ?  165 VAL   A HG22 1 
ATOM   3779 H  HG23 A VAL   A 1 165 ? 6.142  -9.989  5.043   0.66 21.75 ?  165 VAL   A HG23 1 
ATOM   3780 H  HG23 B VAL   A 1 165 ? 6.239  -9.372  5.599   0.34 21.05 ?  165 VAL   A HG23 1 
ATOM   3781 N  N    A SER   A 1 166 ? 3.097  -12.186 2.226   0.66 19.60 ?  166 SER   A N    1 
ATOM   3782 N  N    B SER   A 1 166 ? 3.108  -11.481 2.765   0.34 16.23 ?  166 SER   A N    1 
ATOM   3783 C  CA   A SER   A 1 166 ? 1.979  -12.925 1.649   0.66 20.80 ?  166 SER   A CA   1 
ATOM   3784 C  CA   B SER   A 1 166 ? 1.968  -12.230 2.249   0.34 17.08 ?  166 SER   A CA   1 
ATOM   3785 C  C    A SER   A 1 166 ? 2.406  -13.723 0.427   0.66 21.65 ?  166 SER   A C    1 
ATOM   3786 C  C    B SER   A 1 166 ? 2.360  -13.129 1.092   0.34 17.66 ?  166 SER   A C    1 
ATOM   3787 O  O    A SER   A 1 166 ? 1.794  -14.754 0.113   0.66 23.07 ?  166 SER   A O    1 
ATOM   3788 O  O    B SER   A 1 166 ? 1.721  -14.162 0.873   0.34 18.73 ?  166 SER   A O    1 
ATOM   3789 C  CB   A SER   A 1 166 ? 0.857  -11.953 1.271   0.66 22.45 ?  166 SER   A CB   1 
ATOM   3790 C  CB   B SER   A 1 166 ? 0.872  -11.281 1.776   0.34 17.70 ?  166 SER   A CB   1 
ATOM   3791 O  OG   A SER   A 1 166 ? 0.382  -11.232 2.401   0.66 24.47 ?  166 SER   A OG   1 
ATOM   3792 O  OG   B SER   A 1 166 ? 1.101  -10.903 0.431   0.34 18.29 ?  166 SER   A OG   1 
ATOM   3793 H  H    A SER   A 1 166 ? 3.021  -11.340 2.177   0.66 23.58 ?  166 SER   A H    1 
ATOM   3794 H  H    B SER   A 1 166 ? 3.039  -10.627 2.690   0.34 19.53 ?  166 SER   A H    1 
ATOM   3795 H  HA   A SER   A 1 166 ? 1.620  -13.549 2.306   0.66 25.01 ?  166 SER   A HA   1 
ATOM   3796 H  HA   B SER   A 1 166 ? 1.598  -12.784 2.957   0.34 20.55 ?  166 SER   A HA   1 
ATOM   3797 H  HB2  A SER   A 1 166 ? 1.196  -11.322 0.616   0.66 26.99 ?  166 SER   A HB2  1 
ATOM   3798 H  HB2  B SER   A 1 166 ? 0.009  -11.733 1.849   0.34 21.29 ?  166 SER   A HB2  1 
ATOM   3799 H  HB3  A SER   A 1 166 ? 0.114  -12.451 0.894   0.66 26.99 ?  166 SER   A HB3  1 
ATOM   3800 H  HB3  B SER   A 1 166 ? 0.869  -10.486 2.325   0.34 21.29 ?  166 SER   A HB3  1 
ATOM   3801 H  HG   A SER   A 1 166 ? 1.017  -10.783 2.736   0.66 29.42 ?  166 SER   A HG   1 
ATOM   3802 H  HG   B SER   A 1 166 ? 0.479  -10.406 0.164   0.34 22.00 ?  166 SER   A HG   1 
ATOM   3803 N  N    A SER   A 1 167 ? 3.443  -13.263 -0.268  0.66 21.99 ?  167 SER   A N    1 
ATOM   3804 N  N    B SER   A 1 167 ? 3.381  -12.757 0.325   0.34 17.98 ?  167 SER   A N    1 
ATOM   3805 C  CA   A SER   A 1 167 ? 3.950  -13.929 -1.455  0.66 23.05 ?  167 SER   A CA   1 
ATOM   3806 C  CA   B SER   A 1 167 ? 3.783  -13.561 -0.820  0.34 19.06 ?  167 SER   A CA   1 
ATOM   3807 C  C    A SER   A 1 167 ? 5.096  -14.880 -1.148  0.66 23.26 ?  167 SER   A C    1 
ATOM   3808 C  C    B SER   A 1 167 ? 4.971  -14.468 -0.528  0.34 19.84 ?  167 SER   A C    1 
ATOM   3809 O  O    A SER   A 1 167 ? 5.648  -15.480 -2.076  0.66 23.39 ?  167 SER   A O    1 
ATOM   3810 O  O    B SER   A 1 167 ? 5.348  -15.264 -1.393  0.34 20.26 ?  167 SER   A O    1 
ATOM   3811 C  CB   A SER   A 1 167 ? 4.393  -12.885 -2.497  0.66 23.60 ?  167 SER   A CB   1 
ATOM   3812 C  CB   B SER   A 1 167 ? 4.106  -12.667 -2.021  0.34 19.85 ?  167 SER   A CB   1 
ATOM   3813 O  OG   A SER   A 1 167 ? 5.312  -11.948 -1.950  0.66 23.96 ?  167 SER   A OG   1 
ATOM   3814 O  OG   B SER   A 1 167 ? 5.473  -12.780 -2.378  0.34 20.10 ?  167 SER   A OG   1 
ATOM   3815 H  H    A SER   A 1 167 ? 3.867  -12.543 -0.066  0.66 26.45 ?  167 SER   A H    1 
ATOM   3816 H  H    B SER   A 1 167 ? 3.846  -12.039 0.445   0.34 21.64 ?  167 SER   A H    1 
ATOM   3817 H  HA   A SER   A 1 167 ? 3.237  -14.449 -1.849  0.66 27.72 ?  167 SER   A HA   1 
ATOM   3818 H  HA   B SER   A 1 167 ? 3.034  -14.127 -1.070  0.34 22.92 ?  167 SER   A HA   1 
ATOM   3819 H  HB2  A SER   A 1 167 ? 4.825  -13.338 -3.234  0.66 28.37 ?  167 SER   A HB2  1 
ATOM   3820 H  HB2  B SER   A 1 167 ? 3.557  -12.947 -2.773  0.34 23.88 ?  167 SER   A HB2  1 
ATOM   3821 H  HB3  A SER   A 1 167 ? 3.601  -12.414 -2.824  0.66 28.37 ?  167 SER   A HB3  1 
ATOM   3822 H  HB3  B SER   A 1 167 ? 3.911  -11.746 -1.795  0.34 23.88 ?  167 SER   A HB3  1 
ATOM   3823 H  HG   A SER   A 1 167 ? 5.515  -11.373 -2.532  0.66 28.80 ?  167 SER   A HG   1 
ATOM   3824 H  HG   B SER   A 1 167 ? 5.948  -12.443 -1.774  0.34 24.17 ?  167 SER   A HG   1 
ATOM   3825 N  N    A PHE   A 1 168 ? 5.464  -15.046 0.123   0.66 23.15 ?  168 PHE   A N    1 
ATOM   3826 N  N    B PHE   A 1 168 ? 5.568  -14.375 0.660   0.34 20.59 ?  168 PHE   A N    1 
ATOM   3827 C  CA   A PHE   A 1 168 ? 6.655  -15.819 0.451   0.66 23.33 ?  168 PHE   A CA   1 
ATOM   3828 C  CA   B PHE   A 1 168 ? 6.736  -15.190 0.965   0.34 21.49 ?  168 PHE   A CA   1 
ATOM   3829 C  C    A PHE   A 1 168 ? 6.382  -17.307 0.312   0.66 26.24 ?  168 PHE   A C    1 
ATOM   3830 C  C    B PHE   A 1 168 ? 6.376  -16.665 0.915   0.34 22.86 ?  168 PHE   A C    1 
ATOM   3831 O  O    A PHE   A 1 168 ? 5.406  -17.827 0.862   0.66 26.96 ?  168 PHE   A O    1 
ATOM   3832 O  O    B PHE   A 1 168 ? 5.353  -17.086 1.465   0.34 22.56 ?  168 PHE   A O    1 
ATOM   3833 C  CB   A PHE   A 1 168 ? 7.149  -15.537 1.869   0.66 21.54 ?  168 PHE   A CB   1 
ATOM   3834 C  CB   B PHE   A 1 168 ? 7.275  -14.857 2.352   0.34 21.04 ?  168 PHE   A CB   1 
ATOM   3835 C  CG   A PHE   A 1 168 ? 8.437  -16.249 2.193   0.66 19.86 ?  168 PHE   A CG   1 
ATOM   3836 C  CG   B PHE   A 1 168 ? 8.500  -15.645 2.720   0.34 21.04 ?  168 PHE   A CG   1 
ATOM   3837 C  CD1  A PHE   A 1 168 ? 9.607  -15.882 1.557   0.66 19.52 ?  168 PHE   A CD1  1 
ATOM   3838 C  CD1  B PHE   A 1 168 ? 9.729  -15.307 2.188   0.34 20.95 ?  168 PHE   A CD1  1 
ATOM   3839 C  CD2  A PHE   A 1 168 ? 8.481  -17.300 3.098   0.66 18.73 ?  168 PHE   A CD2  1 
ATOM   3840 C  CD2  B PHE   A 1 168 ? 8.424  -16.730 3.581   0.34 21.06 ?  168 PHE   A CD2  1 
ATOM   3841 C  CE1  A PHE   A 1 168 ? 10.797 -16.527 1.825   0.66 18.73 ?  168 PHE   A CE1  1 
ATOM   3842 C  CE1  B PHE   A 1 168 ? 10.861 -16.027 2.509   0.34 20.90 ?  168 PHE   A CE1  1 
ATOM   3843 C  CE2  A PHE   A 1 168 ? 9.678  -17.952 3.370   0.66 18.70 ?  168 PHE   A CE2  1 
ATOM   3844 C  CE2  B PHE   A 1 168 ? 9.557  -17.455 3.908   0.34 21.23 ?  168 PHE   A CE2  1 
ATOM   3845 C  CZ   A PHE   A 1 168 ? 10.833 -17.561 2.730   0.66 18.64 ?  168 PHE   A CZ   1 
ATOM   3846 C  CZ   B PHE   A 1 168 ? 10.776 -17.102 3.372   0.34 21.06 ?  168 PHE   A CZ   1 
ATOM   3847 H  H    A PHE   A 1 168 ? 5.051  -14.717 0.802   0.66 27.84 ?  168 PHE   A H    1 
ATOM   3848 H  H    B PHE   A 1 168 ? 5.317  -13.854 1.296   0.34 24.77 ?  168 PHE   A H    1 
ATOM   3849 H  HA   A PHE   A 1 168 ? 7.368  -15.582 -0.166  0.66 28.06 ?  168 PHE   A HA   1 
ATOM   3850 H  HA   B PHE   A 1 168 ? 7.430  -15.019 0.309   0.34 25.85 ?  168 PHE   A HA   1 
ATOM   3851 H  HB2  A PHE   A 1 168 ? 7.305  -14.585 1.969   0.66 25.90 ?  168 PHE   A HB2  1 
ATOM   3852 H  HB2  B PHE   A 1 168 ? 7.506  -13.916 2.381   0.34 25.31 ?  168 PHE   A HB2  1 
ATOM   3853 H  HB3  A PHE   A 1 168 ? 6.477  -15.831 2.501   0.66 25.90 ?  168 PHE   A HB3  1 
ATOM   3854 H  HB3  B PHE   A 1 168 ? 6.588  -15.048 3.009   0.34 25.31 ?  168 PHE   A HB3  1 
ATOM   3855 H  HD1  A PHE   A 1 168 ? 9.597  -15.184 0.945   0.66 23.48 ?  168 PHE   A HD1  1 
ATOM   3856 H  HD1  B PHE   A 1 168 ? 9.794  -14.584 1.606   0.34 25.19 ?  168 PHE   A HD1  1 
ATOM   3857 H  HD2  A PHE   A 1 168 ? 7.699  -17.569 3.532   0.66 22.53 ?  168 PHE   A HD2  1 
ATOM   3858 H  HD2  B PHE   A 1 168 ? 7.602  -16.971 3.945   0.34 25.33 ?  168 PHE   A HD2  1 
ATOM   3859 H  HE1  A PHE   A 1 168 ? 11.580 -16.265 1.394   0.66 22.53 ?  168 PHE   A HE1  1 
ATOM   3860 H  HE1  B PHE   A 1 168 ? 11.683 -15.786 2.145   0.34 25.13 ?  168 PHE   A HE1  1 
ATOM   3861 H  HE2  A PHE   A 1 168 ? 9.695  -18.656 3.982   0.66 22.49 ?  168 PHE   A HE2  1 
ATOM   3862 H  HE2  B PHE   A 1 168 ? 9.495  -18.179 4.488   0.34 25.53 ?  168 PHE   A HE2  1 
ATOM   3863 H  HZ   A PHE   A 1 168 ? 11.636 -18.000 2.911   0.66 22.43 ?  168 PHE   A HZ   1 
ATOM   3864 H  HZ   B PHE   A 1 168 ? 11.539 -17.587 3.589   0.34 25.33 ?  168 PHE   A HZ   1 
ATOM   3865 N  N    A LEU   A 1 169 ? 7.268  -17.995 -0.398  0.66 29.55 ?  169 LEU   A N    1 
ATOM   3866 N  N    B LEU   A 1 169 ? 7.229  -17.454 0.273   0.34 25.12 ?  169 LEU   A N    1 
ATOM   3867 C  CA   A LEU   A 1 169 ? 7.137  -19.429 -0.560  0.66 33.89 ?  169 LEU   A CA   1 
ATOM   3868 C  CA   B LEU   A 1 169 ? 6.979  -18.878 0.166   0.34 27.46 ?  169 LEU   A CA   1 
ATOM   3869 C  C    A LEU   A 1 169 ? 8.043  -20.152 0.426   0.66 35.64 ?  169 LEU   A C    1 
ATOM   3870 C  C    B LEU   A 1 169 ? 7.899  -19.660 1.093   0.34 27.50 ?  169 LEU   A C    1 
ATOM   3871 O  O    A LEU   A 1 169 ? 7.579  -20.665 1.445   0.66 36.68 ?  169 LEU   A O    1 
ATOM   3872 O  O    B LEU   A 1 169 ? 7.447  -20.206 2.100   0.34 27.69 ?  169 LEU   A O    1 
ATOM   3873 C  CB   A LEU   A 1 169 ? 7.481  -19.842 -1.991  0.66 36.26 ?  169 LEU   A CB   1 
ATOM   3874 C  CB   B LEU   A 1 169 ? 7.152  -19.343 -1.282  0.34 29.31 ?  169 LEU   A CB   1 
ATOM   3875 C  CG   A LEU   A 1 169 ? 7.111  -21.280 -2.355  0.66 37.82 ?  169 LEU   A CG   1 
ATOM   3876 C  CG   B LEU   A 1 169 ? 6.447  -20.648 -1.659  0.34 30.61 ?  169 LEU   A CG   1 
ATOM   3877 C  CD1  A LEU   A 1 169 ? 5.681  -21.587 -1.932  0.66 38.72 ?  169 LEU   A CD1  1 
ATOM   3878 C  CD1  B LEU   A 1 169 ? 5.068  -20.730 -1.017  0.34 31.41 ?  169 LEU   A CD1  1 
ATOM   3879 C  CD2  A LEU   A 1 169 ? 7.288  -21.508 -3.845  0.66 38.39 ?  169 LEU   A CD2  1 
ATOM   3880 C  CD2  B LEU   A 1 169 ? 6.333  -20.754 -3.171  0.34 31.13 ?  169 LEU   A CD2  1 
ATOM   3881 O  OXT  A LEU   A 1 169 ? 9.257  -20.229 0.231   0.66 35.99 -1 169 LEU   A OXT  1 
ATOM   3882 O  OXT  B LEU   A 1 169 ? 9.107  -19.758 0.866   0.34 27.37 -1 169 LEU   A OXT  1 
ATOM   3883 H  H    A LEU   A 1 169 ? 7.948  -17.650 -0.798  0.66 35.52 ?  169 LEU   A H    1 
ATOM   3884 H  H    B LEU   A 1 169 ? 7.953  -17.187 -0.106  0.34 30.20 ?  169 LEU   A H    1 
ATOM   3885 H  HA   A LEU   A 1 169 ? 6.218  -19.672 -0.373  0.66 40.73 ?  169 LEU   A HA   1 
ATOM   3886 H  HA   B LEU   A 1 169 ? 6.064  -19.034 0.444   0.34 33.01 ?  169 LEU   A HA   1 
ATOM   3887 H  HB2  A LEU   A 1 169 ? 7.014  -19.255 -2.604  0.66 43.57 ?  169 LEU   A HB2  1 
ATOM   3888 H  HB2  B LEU   A 1 169 ? 6.811  -18.651 -1.869  0.34 35.23 ?  169 LEU   A HB2  1 
ATOM   3889 H  HB3  A LEU   A 1 169 ? 8.439  -19.747 -2.115  0.66 43.57 ?  169 LEU   A HB3  1 
ATOM   3890 H  HB3  B LEU   A 1 169 ? 8.099  -19.469 -1.448  0.34 35.23 ?  169 LEU   A HB3  1 
ATOM   3891 H  HG   A LEU   A 1 169 ? 7.701  -21.889 -1.884  0.66 45.44 ?  169 LEU   A HG   1 
ATOM   3892 H  HG   B LEU   A 1 169 ? 6.974  -21.399 -1.343  0.34 36.79 ?  169 LEU   A HG   1 
ATOM   3893 H  HD11 A LEU   A 1 169 ? 5.371  -22.365 -2.416  0.66 46.51 ?  169 LEU   A HD11 1 
ATOM   3894 H  HD11 B LEU   A 1 169 ? 4.546  -21.396 -1.480  0.34 37.75 ?  169 LEU   A HD11 1 
ATOM   3895 H  HD12 A LEU   A 1 169 ? 5.664  -21.762 -0.977  0.66 46.51 ?  169 LEU   A HD12 1 
ATOM   3896 H  HD12 B LEU   A 1 169 ? 5.169  -20.976 -0.083  0.34 37.75 ?  169 LEU   A HD12 1 
ATOM   3897 H  HD13 A LEU   A 1 169 ? 5.121  -20.822 -2.140  0.66 46.51 ?  169 LEU   A HD13 1 
ATOM   3898 H  HD13 B LEU   A 1 169 ? 4.637  -19.861 -1.087  0.34 37.75 ?  169 LEU   A HD13 1 
ATOM   3899 H  HD21 A LEU   A 1 169 ? 7.060  -22.428 -4.051  0.66 46.12 ?  169 LEU   A HD21 1 
ATOM   3900 H  HD21 B LEU   A 1 169 ? 5.912  -21.597 -3.397  0.34 37.41 ?  169 LEU   A HD21 1 
ATOM   3901 H  HD22 A LEU   A 1 169 ? 6.700  -20.905 -4.327  0.66 46.12 ?  169 LEU   A HD22 1 
ATOM   3902 H  HD22 B LEU   A 1 169 ? 5.794  -20.016 -3.498  0.34 37.41 ?  169 LEU   A HD22 1 
ATOM   3903 H  HD23 A LEU   A 1 169 ? 8.211  -21.333 -4.083  0.66 46.12 ?  169 LEU   A HD23 1 
ATOM   3904 H  HD23 B LEU   A 1 169 ? 7.221  -20.712 -3.558  0.34 37.41 ?  169 LEU   A HD23 1 
ATOM   3905 N  N    . SER   B 1 1   ? 50.946 -9.306  -23.702 1.00 27.72 ?  1   SER   B N    1 
ATOM   3906 C  CA   . SER   B 1 1   ? 51.387 -10.323 -22.727 1.00 27.39 ?  1   SER   B CA   1 
ATOM   3907 C  C    . SER   B 1 1   ? 50.321 -11.393 -22.533 1.00 27.14 ?  1   SER   B C    1 
ATOM   3908 O  O    . SER   B 1 1   ? 49.120 -11.184 -22.787 1.00 27.54 ?  1   SER   B O    1 
ATOM   3909 C  CB   . SER   B 1 1   ? 51.730 -9.683  -21.384 1.00 28.59 ?  1   SER   B CB   1 
ATOM   3910 O  OG   . SER   B 1 1   ? 50.567 -9.500  -20.601 1.00 30.84 ?  1   SER   B OG   1 
ATOM   3911 H  H1   . SER   B 1 1   ? 50.901 -9.680  -24.506 1.00 33.32 ?  1   SER   B H1   1 
ATOM   3912 H  H2   . SER   B 1 1   ? 50.150 -9.004  -23.461 1.00 33.32 ?  1   SER   B H2   1 
ATOM   3913 H  H3   . SER   B 1 1   ? 51.535 -8.642  -23.711 1.00 33.32 ?  1   SER   B H3   1 
ATOM   3914 H  HA   . SER   B 1 1   ? 52.189 -10.743 -23.073 1.00 32.92 ?  1   SER   B HA   1 
ATOM   3915 H  HB2  . SER   B 1 1   ? 52.331 -10.271 -20.905 1.00 34.36 ?  1   SER   B HB2  1 
ATOM   3916 H  HB3  . SER   B 1 1   ? 52.157 -8.825  -21.540 1.00 34.36 ?  1   SER   B HB3  1 
ATOM   3917 H  HG   . SER   B 1 1   ? 50.765 -9.084  -19.895 1.00 37.06 ?  1   SER   B HG   1 
ATOM   3918 N  N    A MET   B 1 2   ? 50.776 -12.552 -22.078 0.66 27.02 ?  2   MET   B N    1 
ATOM   3919 N  N    B MET   B 1 2   ? 50.767 -12.555 -22.069 0.34 27.01 ?  2   MET   B N    1 
ATOM   3920 C  CA   A MET   B 1 2   ? 49.940 -13.729 -21.915 0.66 27.49 ?  2   MET   B CA   1 
ATOM   3921 C  CA   B MET   B 1 2   ? 49.916 -13.727 -21.922 0.34 26.92 ?  2   MET   B CA   1 
ATOM   3922 C  C    A MET   B 1 2   ? 49.666 -13.922 -20.431 0.66 25.71 ?  2   MET   B C    1 
ATOM   3923 C  C    B MET   B 1 2   ? 49.657 -13.955 -20.442 0.34 25.23 ?  2   MET   B C    1 
ATOM   3924 O  O    A MET   B 1 2   ? 50.595 -14.157 -19.651 0.66 26.35 ?  2   MET   B O    1 
ATOM   3925 O  O    B MET   B 1 2   ? 50.580 -14.260 -19.680 0.34 25.55 ?  2   MET   B O    1 
ATOM   3926 C  CB   A MET   B 1 2   ? 50.664 -14.939 -22.492 0.66 30.88 ?  2   MET   B CB   1 
ATOM   3927 C  CB   B MET   B 1 2   ? 50.593 -14.933 -22.550 0.34 29.04 ?  2   MET   B CB   1 
ATOM   3928 C  CG   A MET   B 1 2   ? 49.818 -16.192 -22.607 0.66 34.33 ?  2   MET   B CG   1 
ATOM   3929 C  CG   B MET   B 1 2   ? 49.681 -16.132 -22.757 0.34 31.08 ?  2   MET   B CG   1 
ATOM   3930 S  SD   A MET   B 1 2   ? 50.640 -17.425 -23.632 0.66 37.59 ?  2   MET   B SD   1 
ATOM   3931 S  SD   B MET   B 1 2   ? 50.487 -17.422 -23.717 0.34 32.80 ?  2   MET   B SD   1 
ATOM   3932 C  CE   A MET   B 1 2   ? 51.147 -16.391 -24.995 0.66 37.74 ?  2   MET   B CE   1 
ATOM   3933 C  CE   B MET   B 1 2   ? 51.602 -16.421 -24.693 0.34 32.73 ?  2   MET   B CE   1 
ATOM   3934 H  H    A MET   B 1 2   ? 51.599 -12.691 -21.855 0.66 32.48 ?  2   MET   B H    1 
ATOM   3935 H  H    B MET   B 1 2   ? 51.585 -12.697 -21.833 0.34 32.47 ?  2   MET   B H    1 
ATOM   3936 H  HA   A MET   B 1 2   ? 49.107 -13.617 -22.399 0.66 33.04 ?  2   MET   B HA   1 
ATOM   3937 H  HA   B MET   B 1 2   ? 49.080 -13.585 -22.391 0.34 32.36 ?  2   MET   B HA   1 
ATOM   3938 H  HB2  A MET   B 1 2   ? 50.975 -14.674 -23.370 0.66 37.11 ?  2   MET   B HB2  1 
ATOM   3939 H  HB2  B MET   B 1 2   ? 50.896 -14.609 -23.406 0.34 34.91 ?  2   MET   B HB2  1 
ATOM   3940 H  HB3  A MET   B 1 2   ? 51.423 -15.161 -21.937 0.66 37.11 ?  2   MET   B HB3  1 
ATOM   3941 H  HB3  B MET   B 1 2   ? 51.349 -15.226 -22.013 0.34 34.91 ?  2   MET   B HB3  1 
ATOM   3942 H  HG2  A MET   B 1 2   ? 49.679 -16.569 -21.719 0.66 41.25 ?  2   MET   B HG2  1 
ATOM   3943 H  HG2  B MET   B 1 2   ? 49.432 -16.501 -21.892 0.34 37.35 ?  2   MET   B HG2  1 
ATOM   3944 H  HG3  A MET   B 1 2   ? 48.966 -15.978 -23.017 0.66 41.25 ?  2   MET   B HG3  1 
ATOM   3945 H  HG3  B MET   B 1 2   ? 48.892 -15.857 -23.243 0.34 37.35 ?  2   MET   B HG3  1 
ATOM   3946 H  HE1  A MET   B 1 2   ? 51.282 -16.944 -25.764 0.66 45.35 ?  2   MET   B HE1  1 
ATOM   3947 H  HE1  B MET   B 1 2   ? 52.000 -16.980 -25.352 0.34 39.33 ?  2   MET   B HE1  1 
ATOM   3948 H  HE2  A MET   B 1 2   ? 50.445 -15.739 -25.166 0.66 45.35 ?  2   MET   B HE2  1 
ATOM   3949 H  HE2  B MET   B 1 2   ? 51.090 -15.712 -25.123 0.34 39.33 ?  2   MET   B HE2  1 
ATOM   3950 H  HE3  A MET   B 1 2   ? 51.973 -15.933 -24.759 0.66 45.35 ?  2   MET   B HE3  1 
ATOM   3951 H  HE3  B MET   B 1 2   ? 52.297 -16.037 -24.123 0.34 39.33 ?  2   MET   B HE3  1 
ATOM   3952 N  N    . VAL   B 1 3   ? 48.397 -13.810 -20.043 1.00 23.41 ?  3   VAL   B N    1 
ATOM   3953 C  CA   . VAL   B 1 3   ? 47.980 -14.010 -18.665 1.00 22.41 ?  3   VAL   B CA   1 
ATOM   3954 C  C    . VAL   B 1 3   ? 46.735 -14.884 -18.672 1.00 20.82 ?  3   VAL   B C    1 
ATOM   3955 O  O    . VAL   B 1 3   ? 46.004 -14.960 -19.663 1.00 21.12 ?  3   VAL   B O    1 
ATOM   3956 C  CB   . VAL   B 1 3   ? 47.690 -12.682 -17.934 1.00 23.67 ?  3   VAL   B CB   1 
ATOM   3957 C  CG1  . VAL   B 1 3   ? 48.950 -11.817 -17.841 1.00 24.05 ?  3   VAL   B CG1  1 
ATOM   3958 C  CG2  . VAL   B 1 3   ? 46.564 -11.939 -18.628 1.00 24.06 ?  3   VAL   B CG2  1 
ATOM   3959 H  H    A VAL   B 1 3   ? 47.749 -13.625 -20.580 0.66 28.15 ?  3   VAL   B H    1 
ATOM   3960 H  H    B VAL   B 1 3   ? 47.753 -13.595 -20.572 0.34 28.15 ?  3   VAL   B H    1 
ATOM   3961 H  HA   . VAL   B 1 3   ? 48.682 -14.481 -18.184 1.00 26.94 ?  3   VAL   B HA   1 
ATOM   3962 H  HB   . VAL   B 1 3   ? 47.401 -12.890 -17.031 1.00 28.46 ?  3   VAL   B HB   1 
ATOM   3963 H  HG11 . VAL   B 1 3   ? 48.731 -10.999 -17.368 1.00 28.91 ?  3   VAL   B HG11 1 
ATOM   3964 H  HG12 . VAL   B 1 3   ? 49.634 -12.306 -17.355 1.00 28.91 ?  3   VAL   B HG12 1 
ATOM   3965 H  HG13 . VAL   B 1 3   ? 49.259 -11.613 -18.735 1.00 28.91 ?  3   VAL   B HG13 1 
ATOM   3966 H  HG21 . VAL   B 1 3   ? 46.511 -11.046 -18.263 1.00 28.93 ?  3   VAL   B HG21 1 
ATOM   3967 H  HG22 . VAL   B 1 3   ? 46.748 -11.904 -19.578 1.00 28.93 ?  3   VAL   B HG22 1 
ATOM   3968 H  HG23 . VAL   B 1 3   ? 45.729 -12.412 -18.471 1.00 28.93 ?  3   VAL   B HG23 1 
ATOM   3969 N  N    . ASN   B 1 4   ? 46.491 -15.530 -17.539 1.00 19.08 ?  4   ASN   B N    1 
ATOM   3970 C  CA   . ASN   B 1 4   ? 45.356 -16.438 -17.403 1.00 18.54 ?  4   ASN   B CA   1 
ATOM   3971 C  C    . ASN   B 1 4   ? 45.287 -17.403 -18.585 1.00 19.04 ?  4   ASN   B C    1 
ATOM   3972 O  O    . ASN   B 1 4   ? 44.232 -17.626 -19.171 1.00 19.53 ?  4   ASN   B O    1 
ATOM   3973 C  CB   . ASN   B 1 4   ? 44.045 -15.663 -17.244 1.00 18.00 ?  4   ASN   B CB   1 
ATOM   3974 C  CG   . ASN   B 1 4   ? 43.996 -14.855 -15.956 1.00 17.44 ?  4   ASN   B CG   1 
ATOM   3975 O  OD1  . ASN   B 1 4   ? 44.292 -15.361 -14.877 1.00 17.39 ?  4   ASN   B OD1  1 
ATOM   3976 N  ND2  . ASN   B 1 4   ? 43.650 -13.576 -16.073 1.00 18.36 ?  4   ASN   B ND2  1 
ATOM   3977 H  H    . ASN   B 1 4   ? 46.970 -15.463 -16.831 1.00 22.95 ?  4   ASN   B H    1 
ATOM   3978 H  HA   . ASN   B 1 4   ? 45.483 -16.970 -16.605 1.00 22.30 ?  4   ASN   B HA   1 
ATOM   3979 H  HB2  . ASN   B 1 4   ? 43.945 -15.050 -17.989 1.00 21.65 ?  4   ASN   B HB2  1 
ATOM   3980 H  HB3  . ASN   B 1 4   ? 43.305 -16.295 -17.237 1.00 21.65 ?  4   ASN   B HB3  1 
ATOM   3981 H  HD21 . ASN   B 1 4   ? 43.603 -13.078 -15.370 1.00 22.09 ?  4   ASN   B HD21 1 
ATOM   3982 H  HD22 . ASN   B 1 4   ? 43.451 -13.250 -16.842 1.00 22.09 ?  4   ASN   B HD22 1 
ATOM   3983 N  N    . SER   B 1 5   ? 46.438 -17.973 -18.948 1.00 20.00 ?  5   SER   B N    1 
ATOM   3984 C  CA   . SER   B 1 5   ? 46.523 -18.907 -20.070 1.00 22.34 ?  5   SER   B CA   1 
ATOM   3985 C  C    . SER   B 1 5   ? 46.510 -20.313 -19.488 1.00 23.83 ?  5   SER   B C    1 
ATOM   3986 O  O    . SER   B 1 5   ? 47.544 -20.950 -19.298 1.00 25.13 ?  5   SER   B O    1 
ATOM   3987 C  CB   . SER   B 1 5   ? 47.778 -18.648 -20.900 1.00 23.93 ?  5   SER   B CB   1 
ATOM   3988 O  OG   . SER   B 1 5   ? 48.948 -18.830 -20.124 1.00 27.67 ?  5   SER   B OG   1 
ATOM   3989 H  H    . SER   B 1 5   ? 47.192 -17.839 -18.559 1.00 24.06 ?  5   SER   B H    1 
ATOM   3990 H  HA   . SER   B 1 5   ? 45.752 -18.807 -20.645 1.00 26.87 ?  5   SER   B HA   1 
ATOM   3991 H  HB2  . SER   B 1 5   ? 47.792 -19.263 -21.654 1.00 28.77 ?  5   SER   B HB2  1 
ATOM   3992 H  HB3  . SER   B 1 5   ? 47.749 -17.735 -21.226 1.00 28.77 ?  5   SER   B HB3  1 
ATOM   3993 H  HG   . SER   B 1 5   ? 49.006 -19.630 -19.873 1.00 33.26 ?  5   SER   B HG   1 
ATOM   3994 N  N    . PHE   B 1 6   ? 45.304 -20.779 -19.174 1.00 25.62 ?  6   PHE   B N    1 
ATOM   3995 C  CA   . PHE   B 1 6   ? 45.094 -22.110 -18.626 1.00 25.78 ?  6   PHE   B CA   1 
ATOM   3996 C  C    . PHE   B 1 6   ? 44.998 -23.098 -19.778 1.00 29.56 ?  6   PHE   B C    1 
ATOM   3997 O  O    . PHE   B 1 6   ? 44.272 -22.858 -20.747 1.00 31.33 ?  6   PHE   B O    1 
ATOM   3998 C  CB   . PHE   B 1 6   ? 43.808 -22.139 -17.799 1.00 24.24 ?  6   PHE   B CB   1 
ATOM   3999 C  CG   . PHE   B 1 6   ? 43.848 -21.261 -16.578 1.00 22.45 ?  6   PHE   B CG   1 
ATOM   4000 C  CD1  . PHE   B 1 6   ? 44.346 -21.743 -15.383 1.00 21.08 ?  6   PHE   B CD1  1 
ATOM   4001 C  CD2  . PHE   B 1 6   ? 43.374 -19.961 -16.626 1.00 21.60 ?  6   PHE   B CD2  1 
ATOM   4002 C  CE1  . PHE   B 1 6   ? 44.374 -20.940 -14.250 1.00 20.52 ?  6   PHE   B CE1  1 
ATOM   4003 C  CE2  . PHE   B 1 6   ? 43.400 -19.153 -15.507 1.00 21.42 ?  6   PHE   B CE2  1 
ATOM   4004 C  CZ   . PHE   B 1 6   ? 43.908 -19.633 -14.320 1.00 20.64 ?  6   PHE   B CZ   1 
ATOM   4005 H  H    . PHE   B 1 6   ? 44.577 -20.331 -19.273 1.00 30.80 ?  6   PHE   B H    1 
ATOM   4006 H  HA   . PHE   B 1 6   ? 45.835 -22.360 -18.059 1.00 30.99 ?  6   PHE   B HA   1 
ATOM   4007 H  HB2  . PHE   B 1 6   ? 43.069 -21.840 -18.355 1.00 29.14 ?  6   PHE   B HB2  1 
ATOM   4008 H  HB3  . PHE   B 1 6   ? 43.644 -23.050 -17.504 1.00 29.14 ?  6   PHE   B HB3  1 
ATOM   4009 H  HD1  . PHE   B 1 6   ? 44.670 -22.615 -15.338 1.00 25.35 ?  6   PHE   B HD1  1 
ATOM   4010 H  HD2  . PHE   B 1 6   ? 43.026 -19.629 -17.422 1.00 25.97 ?  6   PHE   B HD2  1 
ATOM   4011 H  HE1  . PHE   B 1 6   ? 44.724 -21.268 -13.453 1.00 24.68 ?  6   PHE   B HE1  1 
ATOM   4012 H  HE2  . PHE   B 1 6   ? 43.075 -18.283 -15.556 1.00 25.75 ?  6   PHE   B HE2  1 
ATOM   4013 H  HZ   . PHE   B 1 6   ? 43.923 -19.095 -13.564 1.00 24.82 ?  6   PHE   B HZ   1 
ATOM   4014 N  N    . SER   B 1 7   ? 45.749 -24.193 -19.680 1.00 31.39 ?  7   SER   B N    1 
ATOM   4015 C  CA   . SER   B 1 7   ? 45.823 -25.176 -20.751 1.00 34.36 ?  7   SER   B CA   1 
ATOM   4016 C  C    . SER   B 1 7   ? 45.756 -26.580 -20.170 1.00 33.77 ?  7   SER   B C    1 
ATOM   4017 O  O    . SER   B 1 7   ? 46.395 -26.875 -19.156 1.00 34.12 ?  7   SER   B O    1 
ATOM   4018 C  CB   . SER   B 1 7   ? 47.116 -25.008 -21.561 1.00 37.15 ?  7   SER   B CB   1 
ATOM   4019 O  OG   . SER   B 1 7   ? 47.085 -25.789 -22.744 1.00 39.64 ?  7   SER   B OG   1 
ATOM   4020 H  H    . SER   B 1 7   ? 46.237 -24.384 -18.996 1.00 37.73 ?  7   SER   B H    1 
ATOM   4021 H  HA   . SER   B 1 7   ? 45.072 -25.060 -21.350 1.00 41.29 ?  7   SER   B HA   1 
ATOM   4022 H  HB2  . SER   B 1 7   ? 47.220 -24.070 -21.801 1.00 44.63 ?  7   SER   B HB2  1 
ATOM   4023 H  HB3  . SER   B 1 7   ? 47.871 -25.291 -21.020 1.00 44.63 ?  7   SER   B HB3  1 
ATOM   4024 H  HG   . SER   B 1 7   ? 47.798 -25.678 -23.179 1.00 47.62 ?  7   SER   B HG   1 
ATOM   4025 N  N    . GLY   B 1 8   ? 44.979 -27.442 -20.823 1.00 33.18 ?  8   GLY   B N    1 
ATOM   4026 C  CA   . GLY   B 1 8   ? 44.913 -28.833 -20.431 1.00 32.03 ?  8   GLY   B CA   1 
ATOM   4027 C  C    . GLY   B 1 8   ? 44.000 -29.130 -19.271 1.00 30.73 ?  8   GLY   B C    1 
ATOM   4028 O  O    . GLY   B 1 8   ? 44.175 -30.163 -18.611 1.00 31.76 ?  8   GLY   B O    1 
ATOM   4029 H  H    . GLY   B 1 8   ? 44.489 -27.238 -21.497 1.00 39.87 ?  8   GLY   B H    1 
ATOM   4030 H  HA2  . GLY   B 1 8   ? 44.607 -29.355 -21.187 1.00 38.49 ?  8   GLY   B HA2  1 
ATOM   4031 H  HA3  . GLY   B 1 8   ? 45.798 -29.137 -20.190 1.00 38.49 ?  8   GLY   B HA3  1 
ATOM   4032 N  N    . TYR   B 1 9   ? 43.003 -28.286 -19.020 1.00 29.20 ?  9   TYR   B N    1 
ATOM   4033 C  CA   . TYR   B 1 9   ? 42.070 -28.521 -17.931 1.00 27.22 ?  9   TYR   B CA   1 
ATOM   4034 C  C    . TYR   B 1 9   ? 40.857 -29.298 -18.412 1.00 27.01 ?  9   TYR   B C    1 
ATOM   4035 O  O    . TYR   B 1 9   ? 40.397 -29.138 -19.547 1.00 28.53 ?  9   TYR   B O    1 
ATOM   4036 C  CB   . TYR   B 1 9   ? 41.604 -27.210 -17.309 1.00 26.29 ?  9   TYR   B CB   1 
ATOM   4037 C  CG   . TYR   B 1 9   ? 42.631 -26.611 -16.383 1.00 25.16 ?  9   TYR   B CG   1 
ATOM   4038 C  CD1  . TYR   B 1 9   ? 43.769 -25.992 -16.888 1.00 25.14 ?  9   TYR   B CD1  1 
ATOM   4039 C  CD2  . TYR   B 1 9   ? 42.474 -26.668 -15.006 1.00 24.66 ?  9   TYR   B CD2  1 
ATOM   4040 C  CE1  . TYR   B 1 9   ? 44.724 -25.446 -16.048 1.00 24.99 ?  9   TYR   B CE1  1 
ATOM   4041 C  CE2  . TYR   B 1 9   ? 43.427 -26.125 -14.155 1.00 24.57 ?  9   TYR   B CE2  1 
ATOM   4042 C  CZ   . TYR   B 1 9   ? 44.550 -25.508 -14.684 1.00 24.86 ?  9   TYR   B CZ   1 
ATOM   4043 O  OH   . TYR   B 1 9   ? 45.506 -24.961 -13.855 1.00 24.83 ?  9   TYR   B OH   1 
ATOM   4044 H  H    . TYR   B 1 9   ? 42.820 -27.584 -19.483 1.00 35.09 ?  9   TYR   B H    1 
ATOM   4045 H  HA   . TYR   B 1 9   ? 42.495 -29.043 -17.239 1.00 32.72 ?  9   TYR   B HA   1 
ATOM   4046 H  HB2  . TYR   B 1 9   ? 41.413 -26.564 -18.011 1.00 31.61 ?  9   TYR   B HB2  1 
ATOM   4047 H  HB3  . TYR   B 1 9   ? 40.803 -27.379 -16.791 1.00 31.61 ?  9   TYR   B HB3  1 
ATOM   4048 H  HD1  . TYR   B 1 9   ? 43.893 -25.949 -17.809 1.00 30.22 ?  9   TYR   B HD1  1 
ATOM   4049 H  HD2  . TYR   B 1 9   ? 41.714 -27.078 -14.649 1.00 29.65 ?  9   TYR   B HD2  1 
ATOM   4050 H  HE1  . TYR   B 1 9   ? 45.476 -25.044 -16.404 1.00 30.05 ?  9   TYR   B HE1  1 
ATOM   4051 H  HE2  . TYR   B 1 9   ? 43.301 -26.170 -13.233 1.00 29.54 ?  9   TYR   B HE2  1 
ATOM   4052 H  HH   . TYR   B 1 9   ? 46.119 -24.639 -14.310 1.00 29.85 ?  9   TYR   B HH   1 
ATOM   4053 N  N    . LEU   B 1 10  ? 40.346 -30.150 -17.526 1.00 25.48 ?  10  LEU   B N    1 
ATOM   4054 C  CA   . LEU   B 1 10  ? 39.136 -30.911 -17.772 1.00 25.23 ?  10  LEU   B CA   1 
ATOM   4055 C  C    . LEU   B 1 10  ? 37.954 -30.132 -17.226 1.00 24.73 ?  10  LEU   B C    1 
ATOM   4056 O  O    . LEU   B 1 10  ? 37.961 -29.726 -16.059 1.00 24.65 ?  10  LEU   B O    1 
ATOM   4057 C  CB   . LEU   B 1 10  ? 39.224 -32.256 -17.055 1.00 25.99 ?  10  LEU   B CB   1 
ATOM   4058 C  CG   . LEU   B 1 10  ? 38.134 -33.265 -17.404 1.00 26.90 ?  10  LEU   B CG   1 
ATOM   4059 C  CD1  . LEU   B 1 10  ? 38.341 -33.775 -18.820 1.00 27.61 ?  10  LEU   B CD1  1 
ATOM   4060 C  CD2  . LEU   B 1 10  ? 38.120 -34.411 -16.409 1.00 27.33 ?  10  LEU   B CD2  1 
ATOM   4061 H  H    . LEU   B 1 10  ? 40.674 -30.300 -16.742 1.00 30.63 ?  10  LEU   B H    1 
ATOM   4062 H  HA   . LEU   B 1 10  ? 39.001 -31.057 -18.718 1.00 30.33 ?  10  LEU   B HA   1 
ATOM   4063 H  HB2  . LEU   B 1 10  ? 40.072 -32.662 -17.276 1.00 31.24 ?  10  LEU   B HB2  1 
ATOM   4064 H  HB3  . LEU   B 1 10  ? 39.173 -32.104 -16.097 1.00 31.24 ?  10  LEU   B HB3  1 
ATOM   4065 H  HG   . LEU   B 1 10  ? 37.265 -32.828 -17.367 1.00 32.33 ?  10  LEU   B HG   1 
ATOM   4066 H  HD11 . LEU   B 1 10  ? 37.703 -34.481 -18.998 1.00 33.19 ?  10  LEU   B HD11 1 
ATOM   4067 H  HD12 . LEU   B 1 10  ? 38.206 -33.042 -19.441 1.00 33.19 ?  10  LEU   B HD12 1 
ATOM   4068 H  HD13 . LEU   B 1 10  ? 39.245 -34.115 -18.900 1.00 33.19 ?  10  LEU   B HD13 1 
ATOM   4069 H  HD21 . LEU   B 1 10  ? 37.422 -35.037 -16.658 1.00 32.85 ?  10  LEU   B HD21 1 
ATOM   4070 H  HD22 . LEU   B 1 10  ? 38.983 -34.849 -16.427 1.00 32.85 ?  10  LEU   B HD22 1 
ATOM   4071 H  HD23 . LEU   B 1 10  ? 37.945 -34.054 -15.524 1.00 32.85 ?  10  LEU   B HD23 1 
ATOM   4072 N  N    . LYS   B 1 11  ? 36.943 -29.937 -18.066 1.00 25.90 ?  11  LYS   B N    1 
ATOM   4073 C  CA   . LYS   B 1 11  ? 35.729 -29.254 -17.658 1.00 27.95 ?  11  LYS   B CA   1 
ATOM   4074 C  C    . LYS   B 1 11  ? 34.899 -30.195 -16.793 1.00 26.69 ?  11  LYS   B C    1 
ATOM   4075 O  O    . LYS   B 1 11  ? 34.600 -31.327 -17.199 1.00 28.18 ?  11  LYS   B O    1 
ATOM   4076 C  CB   . LYS   B 1 11  ? 34.948 -28.849 -18.911 1.00 31.20 ?  11  LYS   B CB   1 
ATOM   4077 C  CG   . LYS   B 1 11  ? 33.860 -27.820 -18.698 1.00 34.16 ?  11  LYS   B CG   1 
ATOM   4078 C  CD   . LYS   B 1 11  ? 33.115 -27.554 -19.999 1.00 36.29 ?  11  LYS   B CD   1 
ATOM   4079 C  CE   . LYS   B 1 11  ? 32.093 -26.444 -19.839 1.00 38.05 ?  11  LYS   B CE   1 
ATOM   4080 N  NZ   . LYS   B 1 11  ? 32.740 -25.118 -19.644 1.00 39.11 ?  11  LYS   B NZ   1 
ATOM   4081 H  H    . LYS   B 1 11  ? 36.920 -30.204 -18.885 1.00 31.13 ?  11  LYS   B H    1 
ATOM   4082 H  HA   . LYS   B 1 11  ? 35.938 -28.455 -17.148 1.00 33.59 ?  11  LYS   B HA   1 
ATOM   4083 H  HB2  . LYS   B 1 11  ? 35.572 -28.475 -19.556 1.00 37.50 ?  11  LYS   B HB2  1 
ATOM   4084 H  HB3  . LYS   B 1 11  ? 34.527 -29.636 -19.289 1.00 37.50 ?  11  LYS   B HB3  1 
ATOM   4085 H  HG2  . LYS   B 1 11  ? 33.226 -28.152 -18.047 1.00 41.04 ?  11  LYS   B HG2  1 
ATOM   4086 H  HG3  . LYS   B 1 11  ? 34.256 -26.988 -18.399 1.00 41.04 ?  11  LYS   B HG3  1 
ATOM   4087 H  HD2  . LYS   B 1 11  ? 33.750 -27.287 -20.683 1.00 43.61 ?  11  LYS   B HD2  1 
ATOM   4088 H  HD3  . LYS   B 1 11  ? 32.650 -28.361 -20.272 1.00 43.61 ?  11  LYS   B HD3  1 
ATOM   4089 H  HE2  . LYS   B 1 11  ? 31.544 -26.399 -20.637 1.00 45.71 ?  11  LYS   B HE2  1 
ATOM   4090 H  HE3  . LYS   B 1 11  ? 31.542 -26.635 -19.065 1.00 45.71 ?  11  LYS   B HE3  1 
ATOM   4091 H  HZ1  . LYS   B 1 11  ? 32.119 -24.486 -19.565 1.00 46.98 ?  11  LYS   B HZ1  1 
ATOM   4092 H  HZ2  . LYS   B 1 11  ? 33.238 -25.128 -18.907 1.00 46.98 ?  11  LYS   B HZ2  1 
ATOM   4093 H  HZ3  . LYS   B 1 11  ? 33.259 -24.927 -20.341 1.00 46.98 ?  11  LYS   B HZ3  1 
ATOM   4094 N  N    . LEU   B 1 12  ? 34.543 -29.739 -15.592 1.00 24.69 ?  12  LEU   B N    1 
ATOM   4095 C  CA   . LEU   B 1 12  ? 33.587 -30.445 -14.745 1.00 23.65 ?  12  LEU   B CA   1 
ATOM   4096 C  C    . LEU   B 1 12  ? 32.202 -29.826 -14.816 1.00 24.01 ?  12  LEU   B C    1 
ATOM   4097 O  O    . LEU   B 1 12  ? 31.216 -30.539 -14.988 1.00 24.51 ?  12  LEU   B O    1 
ATOM   4098 C  CB   . LEU   B 1 12  ? 34.050 -30.476 -13.285 1.00 22.80 ?  12  LEU   B CB   1 
ATOM   4099 C  CG   . LEU   B 1 12  ? 35.401 -31.140 -13.027 1.00 22.39 ?  12  LEU   B CG   1 
ATOM   4100 C  CD1  . LEU   B 1 12  ? 35.762 -31.088 -11.555 1.00 22.40 ?  12  LEU   B CD1  1 
ATOM   4101 C  CD2  . LEU   B 1 12  ? 35.398 -32.570 -13.532 1.00 22.70 ?  12  LEU   B CD2  1 
ATOM   4102 H  H    . LEU   B 1 12  ? 34.828 -29.008 -15.243 1.00 29.69 ?  12  LEU   B H    1 
ATOM   4103 H  HA   . LEU   B 1 12  ? 33.493 -31.357 -15.059 1.00 28.44 ?  12  LEU   B HA   1 
ATOM   4104 H  HB2  . LEU   B 1 12  ? 34.099 -29.563 -12.971 1.00 27.42 ?  12  LEU   B HB2  1 
ATOM   4105 H  HB3  . LEU   B 1 12  ? 33.379 -30.957 -12.770 1.00 27.42 ?  12  LEU   B HB3  1 
ATOM   4106 H  HG   . LEU   B 1 12  ? 36.073 -30.650 -13.519 1.00 26.92 ?  12  LEU   B HG   1 
ATOM   4107 H  HD11 . LEU   B 1 12  ? 36.626 -31.510 -11.431 1.00 26.94 ?  12  LEU   B HD11 1 
ATOM   4108 H  HD12 . LEU   B 1 12  ? 35.807 -30.158 -11.270 1.00 26.94 ?  12  LEU   B HD12 1 
ATOM   4109 H  HD13 . LEU   B 1 12  ? 35.087 -31.556 -11.041 1.00 26.94 ?  12  LEU   B HD13 1 
ATOM   4110 H  HD21 . LEU   B 1 12  ? 36.209 -33.005 -13.237 1.00 27.30 ?  12  LEU   B HD21 1 
ATOM   4111 H  HD22 . LEU   B 1 12  ? 34.622 -33.032 -13.173 1.00 27.30 ?  12  LEU   B HD22 1 
ATOM   4112 H  HD23 . LEU   B 1 12  ? 35.356 -32.564 -14.502 1.00 27.30 ?  12  LEU   B HD23 1 
ATOM   4113 N  N    . THR   B 1 13  ? 32.110 -28.512 -14.666 1.00 23.84 ?  13  THR   B N    1 
ATOM   4114 C  CA   . THR   B 1 13  ? 30.888 -27.762 -14.883 1.00 23.96 ?  13  THR   B CA   1 
ATOM   4115 C  C    . THR   B 1 13  ? 31.245 -26.595 -15.794 1.00 25.82 ?  13  THR   B C    1 
ATOM   4116 O  O    . THR   B 1 13  ? 32.398 -26.435 -16.216 1.00 27.00 ?  13  THR   B O    1 
ATOM   4117 C  CB   . THR   B 1 13  ? 30.300 -27.258 -13.559 1.00 23.72 ?  13  THR   B CB   1 
ATOM   4118 O  OG1  . THR   B 1 13  ? 31.181 -26.266 -13.011 1.00 23.47 ?  13  THR   B OG1  1 
ATOM   4119 C  CG2  . THR   B 1 13  ? 30.140 -28.400 -12.565 1.00 23.90 ?  13  THR   B CG2  1 
ATOM   4120 H  H    . THR   B 1 13  ? 32.765 -28.010 -14.424 1.00 28.66 ?  13  THR   B H    1 
ATOM   4121 H  HA   . THR   B 1 13  ? 30.223 -28.321 -15.309 1.00 28.81 ?  13  THR   B HA   1 
ATOM   4122 H  HB   . THR   B 1 13  ? 29.411 -26.865 -13.710 1.00 28.51 ?  13  THR   B HB   1 
ATOM   4123 H  HG1  . THR   B 1 13  ? 30.912 -25.490 -13.231 1.00 28.21 ?  13  THR   B HG1  1 
ATOM   4124 H  HG21 . THR   B 1 13  ? 29.618 -28.106 -11.798 1.00 28.74 ?  13  THR   B HG21 1 
ATOM   4125 H  HG22 . THR   B 1 13  ? 29.681 -29.140 -12.989 1.00 28.74 ?  13  THR   B HG22 1 
ATOM   4126 H  HG23 . THR   B 1 13  ? 31.009 -28.692 -12.264 1.00 28.74 ?  13  THR   B HG23 1 
ATOM   4127 N  N    A ASP   B 1 14  ? 30.250 -25.762 -16.095 0.66 26.72 ?  14  ASP   B N    1 
ATOM   4128 N  N    B ASP   B 1 14  ? 30.249 -25.754 -16.085 0.34 26.30 ?  14  ASP   B N    1 
ATOM   4129 C  CA   A ASP   B 1 14  ? 30.507 -24.620 -16.963 0.66 27.75 ?  14  ASP   B CA   1 
ATOM   4130 C  CA   B ASP   B 1 14  ? 30.481 -24.608 -16.956 0.34 26.83 ?  14  ASP   B CA   1 
ATOM   4131 C  C    A ASP   B 1 14  ? 31.620 -23.735 -16.418 0.66 26.04 ?  14  ASP   B C    1 
ATOM   4132 C  C    B ASP   B 1 14  ? 31.524 -23.648 -16.400 0.34 25.35 ?  14  ASP   B C    1 
ATOM   4133 O  O    A ASP   B 1 14  ? 32.336 -23.096 -17.199 0.66 27.46 ?  14  ASP   B O    1 
ATOM   4134 O  O    B ASP   B 1 14  ? 32.071 -22.845 -17.164 0.34 25.85 ?  14  ASP   B O    1 
ATOM   4135 C  CB   A ASP   B 1 14  ? 29.225 -23.813 -17.168 0.66 30.62 ?  14  ASP   B CB   1 
ATOM   4136 C  CB   B ASP   B 1 14  ? 29.177 -23.844 -17.192 0.34 29.05 ?  14  ASP   B CB   1 
ATOM   4137 C  CG   A ASP   B 1 14  ? 28.232 -24.510 -18.072 0.66 33.34 ?  14  ASP   B CG   1 
ATOM   4138 C  CG   B ASP   B 1 14  ? 28.228 -24.583 -18.113 0.34 31.00 ?  14  ASP   B CG   1 
ATOM   4139 O  OD1  A ASP   B 1 14  ? 28.586 -25.533 -18.703 0.66 34.28 ?  14  ASP   B OD1  1 
ATOM   4140 O  OD1  B ASP   B 1 14  ? 28.709 -25.294 -19.021 0.34 31.81 ?  14  ASP   B OD1  1 
ATOM   4141 O  OD2  A ASP   B 1 14  ? 27.080 -24.035 -18.142 0.66 34.72 -1 14  ASP   B OD2  1 
ATOM   4142 O  OD2  B ASP   B 1 14  ? 26.999 -24.458 -17.928 0.34 31.79 -1 14  ASP   B OD2  1 
ATOM   4143 H  H    A ASP   B 1 14  ? 29.441 -25.825 -15.810 0.66 32.12 ?  14  ASP   B H    1 
ATOM   4144 H  H    B ASP   B 1 14  ? 29.443 -25.822 -15.792 0.34 31.62 ?  14  ASP   B H    1 
ATOM   4145 H  HA   A ASP   B 1 14  ? 30.797 -24.938 -17.827 0.66 33.36 ?  14  ASP   B HA   1 
ATOM   4146 H  HA   B ASP   B 1 14  ? 30.800 -24.924 -17.815 0.34 32.25 ?  14  ASP   B HA   1 
ATOM   4147 H  HB2  A ASP   B 1 14  ? 28.783 -23.686 -16.317 0.66 36.80 ?  14  ASP   B HB2  1 
ATOM   4148 H  HB2  B ASP   B 1 14  ? 28.727 -23.719 -16.343 0.34 34.91 ?  14  ASP   B HB2  1 
ATOM   4149 H  HB3  A ASP   B 1 14  ? 29.445 -22.953 -17.562 0.66 36.80 ?  14  ASP   B HB3  1 
ATOM   4150 H  HB3  B ASP   B 1 14  ? 29.386 -22.977 -17.584 0.34 34.91 ?  14  ASP   B HB3  1 
ATOM   4151 N  N    . ASN   B 1 15  ? 31.796 -23.690 -15.092 1.00 23.96 ?  15  ASN   B N    1 
ATOM   4152 C  CA   . ASN   B 1 15  ? 32.764 -22.781 -14.481 1.00 21.12 ?  15  ASN   B CA   1 
ATOM   4153 C  C    . ASN   B 1 15  ? 33.861 -23.435 -13.647 1.00 19.63 ?  15  ASN   B C    1 
ATOM   4154 O  O    . ASN   B 1 15  ? 34.740 -22.716 -13.156 1.00 19.15 ?  15  ASN   B O    1 
ATOM   4155 C  CB   . ASN   B 1 15  ? 32.051 -21.729 -13.617 1.00 20.80 ?  15  ASN   B CB   1 
ATOM   4156 C  CG   . ASN   B 1 15  ? 31.447 -22.328 -12.368 1.00 20.42 ?  15  ASN   B CG   1 
ATOM   4157 O  OD1  . ASN   B 1 15  ? 30.501 -23.125 -12.444 1.00 22.19 ?  15  ASN   B OD1  1 
ATOM   4158 N  ND2  . ASN   B 1 15  ? 31.988 -21.974 -11.214 1.00 19.03 ?  15  ASN   B ND2  1 
ATOM   4159 H  H    A ASN   B 1 15  ? 31.358 -24.165 -14.526 0.66 28.81 ?  15  ASN   B H    1 
ATOM   4160 H  H    B ASN   B 1 15  ? 31.408 -24.211 -14.533 0.34 28.81 ?  15  ASN   B H    1 
ATOM   4161 H  HA   . ASN   B 1 15  ? 33.211 -22.289 -15.178 1.00 25.40 ?  15  ASN   B HA   1 
ATOM   4162 H  HB2  . ASN   B 1 15  ? 32.689 -21.040 -13.350 1.00 25.02 ?  15  ASN   B HB2  1 
ATOM   4163 H  HB3  . ASN   B 1 15  ? 31.332 -21.316 -14.131 1.00 25.02 ?  15  ASN   B HB3  1 
ATOM   4164 H  HD21 . ASN   B 1 15  ? 31.682 -22.282 -10.472 1.00 22.89 ?  15  ASN   B HD21 1 
ATOM   4165 H  HD22 . ASN   B 1 15  ? 32.662 -21.424 -11.196 1.00 22.89 ?  15  ASN   B HD22 1 
ATOM   4166 N  N    . VAL   B 1 16  ? 33.840 -24.748 -13.450 1.00 19.08 ?  16  VAL   B N    1 
ATOM   4167 C  CA   . VAL   B 1 16  ? 34.853 -25.433 -12.654 1.00 19.30 ?  16  VAL   B CA   1 
ATOM   4168 C  C    . VAL   B 1 16  ? 35.641 -26.364 -13.564 1.00 19.61 ?  16  VAL   B C    1 
ATOM   4169 O  O    . VAL   B 1 16  ? 35.066 -27.248 -14.219 1.00 20.91 ?  16  VAL   B O    1 
ATOM   4170 C  CB   . VAL   B 1 16  ? 34.239 -26.201 -11.473 1.00 19.17 ?  16  VAL   B CB   1 
ATOM   4171 C  CG1  . VAL   B 1 16  ? 35.327 -26.926 -10.677 1.00 19.38 ?  16  VAL   B CG1  1 
ATOM   4172 C  CG2  . VAL   B 1 16  ? 33.433 -25.260 -10.581 1.00 19.46 ?  16  VAL   B CG2  1 
ATOM   4173 H  H    . VAL   B 1 16  ? 33.214 -25.269 -13.751 1.00 22.95 ?  16  VAL   B H    1 
ATOM   4174 H  HA   . VAL   B 1 16  ? 35.456 -24.772 -12.287 1.00 23.22 ?  16  VAL   B HA   1 
ATOM   4175 H  HB   . VAL   B 1 16  ? 33.626 -26.874 -11.814 1.00 23.06 ?  16  VAL   B HB   1 
ATOM   4176 H  HG11 . VAL   B 1 16  ? 34.946 -27.244 -9.841  1.00 23.31 ?  16  VAL   B HG11 1 
ATOM   4177 H  HG12 . VAL   B 1 16  ? 35.653 -27.673 -11.196 1.00 23.31 ?  16  VAL   B HG12 1 
ATOM   4178 H  HG13 . VAL   B 1 16  ? 36.046 -26.302 -10.493 1.00 23.31 ?  16  VAL   B HG13 1 
ATOM   4179 H  HG21 . VAL   B 1 16  ? 33.118 -25.752 -9.802  1.00 23.41 ?  16  VAL   B HG21 1 
ATOM   4180 H  HG22 . VAL   B 1 16  ? 33.997 -24.527 -10.301 1.00 23.41 ?  16  VAL   B HG22 1 
ATOM   4181 H  HG23 . VAL   B 1 16  ? 32.672 -24.923 -11.082 1.00 23.41 ?  16  VAL   B HG23 1 
ATOM   4182 N  N    . TYR   B 1 17  ? 36.957 -26.183 -13.560 1.00 20.45 ?  17  TYR   B N    1 
ATOM   4183 C  CA   . TYR   B 1 17  ? 37.894 -26.943 -14.368 1.00 20.51 ?  17  TYR   B CA   1 
ATOM   4184 C  C    . TYR   B 1 17  ? 38.952 -27.547 -13.452 1.00 19.40 ?  17  TYR   B C    1 
ATOM   4185 O  O    . TYR   B 1 17  ? 39.233 -27.023 -12.372 1.00 19.75 ?  17  TYR   B O    1 
ATOM   4186 C  CB   . TYR   B 1 17  ? 38.599 -26.029 -15.383 1.00 23.20 ?  17  TYR   B CB   1 
ATOM   4187 C  CG   . TYR   B 1 17  ? 37.679 -25.270 -16.312 1.00 26.74 ?  17  TYR   B CG   1 
ATOM   4188 C  CD1  . TYR   B 1 17  ? 37.103 -24.069 -15.923 1.00 28.48 ?  17  TYR   B CD1  1 
ATOM   4189 C  CD2  . TYR   B 1 17  ? 37.400 -25.750 -17.585 1.00 29.00 ?  17  TYR   B CD2  1 
ATOM   4190 C  CE1  . TYR   B 1 17  ? 36.265 -23.368 -16.772 1.00 30.00 ?  17  TYR   B CE1  1 
ATOM   4191 C  CE2  . TYR   B 1 17  ? 36.565 -25.057 -18.442 1.00 30.29 ?  17  TYR   B CE2  1 
ATOM   4192 C  CZ   . TYR   B 1 17  ? 36.000 -23.868 -18.029 1.00 31.05 ?  17  TYR   B CZ   1 
ATOM   4193 O  OH   . TYR   B 1 17  ? 35.168 -23.173 -18.875 1.00 32.41 ?  17  TYR   B OH   1 
ATOM   4194 H  H    . TYR   B 1 17  ? 37.337 -25.582 -13.077 1.00 24.59 ?  17  TYR   B H    1 
ATOM   4195 H  HA   . TYR   B 1 17  ? 37.415 -27.644 -14.839 1.00 24.66 ?  17  TYR   B HA   1 
ATOM   4196 H  HB2  . TYR   B 1 17  ? 39.135 -25.383 -14.903 1.00 27.89 ?  17  TYR   B HB2  1 
ATOM   4197 H  HB3  . TYR   B 1 17  ? 39.158 -26.584 -15.935 1.00 27.89 ?  17  TYR   B HB3  1 
ATOM   4198 H  HD1  . TYR   B 1 17  ? 37.277 -23.729 -15.077 1.00 34.24 ?  17  TYR   B HD1  1 
ATOM   4199 H  HD2  . TYR   B 1 17  ? 37.777 -26.550 -17.865 1.00 34.86 ?  17  TYR   B HD2  1 
ATOM   4200 H  HE1  . TYR   B 1 17  ? 35.880 -22.564 -16.499 1.00 36.06 ?  17  TYR   B HE1  1 
ATOM   4201 H  HE2  . TYR   B 1 17  ? 36.382 -25.392 -19.293 1.00 36.40 ?  17  TYR   B HE2  1 
ATOM   4202 H  HH   . TYR   B 1 17  ? 35.087 -23.580 -19.606 1.00 38.95 ?  17  TYR   B HH   1 
ATOM   4203 N  N    . ILE   B 1 18  ? 39.548 -28.655 -13.880 1.00 19.13 ?  18  ILE   B N    1 
ATOM   4204 C  CA   . ILE   B 1 18  ? 40.473 -29.378 -13.019 1.00 19.44 ?  18  ILE   B CA   1 
ATOM   4205 C  C    . ILE   B 1 18  ? 41.625 -29.939 -13.842 1.00 19.96 ?  18  ILE   B C    1 
ATOM   4206 O  O    . ILE   B 1 18  ? 41.466 -30.320 -15.006 1.00 21.20 ?  18  ILE   B O    1 
ATOM   4207 C  CB   . ILE   B 1 18  ? 39.727 -30.480 -12.214 1.00 19.64 ?  18  ILE   B CB   1 
ATOM   4208 C  CG1  . ILE   B 1 18  ? 40.610 -31.031 -11.094 1.00 19.89 ?  18  ILE   B CG1  1 
ATOM   4209 C  CG2  . ILE   B 1 18  ? 39.205 -31.601 -13.137 1.00 19.96 ?  18  ILE   B CG2  1 
ATOM   4210 C  CD1  . ILE   B 1 18  ? 39.836 -31.848 -10.067 1.00 20.91 ?  18  ILE   B CD1  1 
ATOM   4211 H  H    . ILE   B 1 18  ? 39.415 -29.001 -14.650 1.00 23.02 ?  18  ILE   B H    1 
ATOM   4212 H  HA   . ILE   B 1 18  ? 40.829 -28.752 -12.369 1.00 23.38 ?  18  ILE   B HA   1 
ATOM   4213 H  HB   . ILE   B 1 18  ? 38.948 -30.078 -11.790 1.00 23.62 ?  18  ILE   B HB   1 
ATOM   4214 H  HG12 . ILE   B 1 18  ? 41.286 -31.605 -11.480 1.00 23.92 ?  18  ILE   B HG12 1 
ATOM   4215 H  HG13 . ILE   B 1 18  ? 41.026 -30.289 -10.629 1.00 23.92 ?  18  ILE   B HG13 1 
ATOM   4216 H  HG21 . ILE   B 1 18  ? 38.629 -32.194 -12.625 1.00 24.00 ?  18  ILE   B HG21 1 
ATOM   4217 H  HG22 . ILE   B 1 18  ? 38.697 -31.199 -13.861 1.00 24.00 ?  18  ILE   B HG22 1 
ATOM   4218 H  HG23 . ILE   B 1 18  ? 39.956 -32.095 -13.492 1.00 24.00 ?  18  ILE   B HG23 1 
ATOM   4219 H  HD11 . ILE   B 1 18  ? 40.443 -32.129 -9.365  1.00 25.14 ?  18  ILE   B HD11 1 
ATOM   4220 H  HD12 . ILE   B 1 18  ? 39.130 -31.297 -9.691  1.00 25.14 ?  18  ILE   B HD12 1 
ATOM   4221 H  HD13 . ILE   B 1 18  ? 39.452 -32.624 -10.503 1.00 25.14 ?  18  ILE   B HD13 1 
ATOM   4222 N  N    . LYS   B 1 19  ? 42.800 -29.985 -13.222 1.00 20.36 ?  19  LYS   B N    1 
ATOM   4223 C  CA   . LYS   B 1 19  ? 44.007 -30.452 -13.888 1.00 20.78 ?  19  LYS   B CA   1 
ATOM   4224 C  C    . LYS   B 1 19  ? 44.929 -31.117 -12.873 1.00 20.44 ?  19  LYS   B C    1 
ATOM   4225 O  O    . LYS   B 1 19  ? 45.012 -30.693 -11.719 1.00 20.08 ?  19  LYS   B O    1 
ATOM   4226 C  CB   . LYS   B 1 19  ? 44.748 -29.279 -14.539 1.00 22.50 ?  19  LYS   B CB   1 
ATOM   4227 C  CG   . LYS   B 1 19  ? 45.905 -29.687 -15.425 1.00 24.46 ?  19  LYS   B CG   1 
ATOM   4228 C  CD   . LYS   B 1 19  ? 46.673 -28.471 -15.918 1.00 26.10 ?  19  LYS   B CD   1 
ATOM   4229 C  CE   . LYS   B 1 19  ? 47.821 -28.869 -16.827 1.00 27.88 ?  19  LYS   B CE   1 
ATOM   4230 N  NZ   . LYS   B 1 19  ? 48.607 -27.694 -17.291 1.00 29.29 ?  19  LYS   B NZ   1 
ATOM   4231 H  H    . LYS   B 1 19  ? 42.896 -29.757 -12.406 1.00 24.49 ?  19  LYS   B H    1 
ATOM   4232 H  HA   . LYS   B 1 19  ? 43.753 -31.096 -14.578 1.00 24.99 ?  19  LYS   B HA   1 
ATOM   4233 H  HB2  . LYS   B 1 19  ? 44.117 -28.781 -15.085 1.00 27.06 ?  19  LYS   B HB2  1 
ATOM   4234 H  HB3  . LYS   B 1 19  ? 45.088 -28.710 -13.833 1.00 27.06 ?  19  LYS   B HB3  1 
ATOM   4235 H  HG2  . LYS   B 1 19  ? 46.505 -30.255 -14.920 1.00 29.41 ?  19  LYS   B HG2  1 
ATOM   4236 H  HG3  . LYS   B 1 19  ? 45.555 -30.170 -16.195 1.00 29.41 ?  19  LYS   B HG3  1 
ATOM   4237 H  HD2  . LYS   B 1 19  ? 46.071 -27.897 -16.417 1.00 31.38 ?  19  LYS   B HD2  1 
ATOM   4238 H  HD3  . LYS   B 1 19  ? 47.035 -27.996 -15.155 1.00 31.38 ?  19  LYS   B HD3  1 
ATOM   4239 H  HE2  . LYS   B 1 19  ? 48.416 -29.462 -16.342 1.00 33.51 ?  19  LYS   B HE2  1 
ATOM   4240 H  HE3  . LYS   B 1 19  ? 47.462 -29.323 -17.607 1.00 33.51 ?  19  LYS   B HE3  1 
ATOM   4241 H  HZ1  . LYS   B 1 19  ? 49.242 -27.956 -17.857 1.00 35.20 ?  19  LYS   B HZ1  1 
ATOM   4242 H  HZ2  . LYS   B 1 19  ? 48.073 -27.114 -17.705 1.00 35.20 ?  19  LYS   B HZ2  1 
ATOM   4243 H  HZ3  . LYS   B 1 19  ? 48.988 -27.289 -16.596 1.00 35.20 ?  19  LYS   B HZ3  1 
ATOM   4244 N  N    . ASN   B 1 20  ? 45.616 -32.170 -13.306 1.00 21.46 ?  20  ASN   B N    1 
ATOM   4245 C  CA   . ASN   B 1 20  ? 46.641 -32.804 -12.482 1.00 22.40 ?  20  ASN   B CA   1 
ATOM   4246 C  C    . ASN   B 1 20  ? 47.937 -32.017 -12.666 1.00 22.75 ?  20  ASN   B C    1 
ATOM   4247 O  O    . ASN   B 1 20  ? 48.571 -32.101 -13.725 1.00 24.85 ?  20  ASN   B O    1 
ATOM   4248 C  CB   . ASN   B 1 20  ? 46.786 -34.270 -12.896 1.00 24.00 ?  20  ASN   B CB   1 
ATOM   4249 C  CG   . ASN   B 1 20  ? 47.951 -34.985 -12.213 1.00 25.45 ?  20  ASN   B CG   1 
ATOM   4250 O  OD1  . ASN   B 1 20  ? 48.596 -35.849 -12.820 1.00 27.95 ?  20  ASN   B OD1  1 
ATOM   4251 N  ND2  . ASN   B 1 20  ? 48.208 -34.657 -10.951 1.00 25.08 ?  20  ASN   B ND2  1 
ATOM   4252 H  H    . ASN   B 1 20  ? 45.511 -32.523 -14.081 1.00 25.80 ?  20  ASN   B H    1 
ATOM   4253 H  HA   . ASN   B 1 20  ? 46.363 -32.765 -11.550 1.00 26.93 ?  20  ASN   B HA   1 
ATOM   4254 H  HB2  . ASN   B 1 20  ? 45.963 -34.741 -12.671 1.00 28.85 ?  20  ASN   B HB2  1 
ATOM   4255 H  HB3  . ASN   B 1 20  ? 46.928 -34.305 -13.853 1.00 28.85 ?  20  ASN   B HB3  1 
ATOM   4256 H  HD21 . ASN   B 1 20  ? 48.854 -35.031 -10.530 1.00 30.16 ?  20  ASN   B HD21 1 
ATOM   4257 H  HD22 . ASN   B 1 20  ? 47.735 -34.050 -10.551 1.00 30.16 ?  20  ASN   B HD22 1 
ATOM   4258 N  N    . ALA   B 1 21  ? 48.325 -31.236 -11.656 1.00 22.41 ?  21  ALA   B N    1 
ATOM   4259 C  CA   . ALA   B 1 21  ? 49.457 -30.336 -11.817 1.00 22.80 ?  21  ALA   B CA   1 
ATOM   4260 C  C    . ALA   B 1 21  ? 49.918 -29.808 -10.465 1.00 21.71 ?  21  ALA   B C    1 
ATOM   4261 O  O    . ALA   B 1 21  ? 49.179 -29.818 -9.477  1.00 21.59 ?  21  ALA   B O    1 
ATOM   4262 C  CB   . ALA   B 1 21  ? 49.086 -29.178 -12.738 1.00 23.95 ?  21  ALA   B CB   1 
ATOM   4263 H  H    . ALA   B 1 21  ? 47.949 -31.223 -10.881 1.00 26.94 ?  21  ALA   B H    1 
ATOM   4264 H  HA   . ALA   B 1 21  ? 50.188 -30.832 -12.225 1.00 27.42 ?  21  ALA   B HA   1 
ATOM   4265 H  HB1  . ALA   B 1 21  ? 49.880 -28.654 -12.893 1.00 28.80 ?  21  ALA   B HB1  1 
ATOM   4266 H  HB2  . ALA   B 1 21  ? 48.754 -29.542 -13.575 1.00 28.80 ?  21  ALA   B HB2  1 
ATOM   4267 H  HB3  . ALA   B 1 21  ? 48.400 -28.650 -12.309 1.00 28.80 ?  21  ALA   B HB3  1 
ATOM   4268 N  N    . ASP   B 1 22  ? 51.169 -29.348 -10.455 1.00 20.45 ?  22  ASP   B N    1 
ATOM   4269 C  CA   . ASP   B 1 22  ? 51.784 -28.654 -9.328  1.00 19.82 ?  22  ASP   B CA   1 
ATOM   4270 C  C    . ASP   B 1 22  ? 51.372 -27.185 -9.402  1.00 18.83 ?  22  ASP   B C    1 
ATOM   4271 O  O    . ASP   B 1 22  ? 51.682 -26.507 -10.386 1.00 18.78 ?  22  ASP   B O    1 
ATOM   4272 C  CB   . ASP   B 1 22  ? 53.301 -28.822 -9.487  1.00 21.17 ?  22  ASP   B CB   1 
ATOM   4273 C  CG   . ASP   B 1 22  ? 54.124 -28.088 -8.436  1.00 22.68 ?  22  ASP   B CG   1 
ATOM   4274 O  OD1  . ASP   B 1 22  ? 53.783 -26.954 -8.053  1.00 22.63 ?  22  ASP   B OD1  1 
ATOM   4275 O  OD2  . ASP   B 1 22  ? 55.167 -28.646 -8.024  1.00 24.72 -1 22  ASP   B OD2  1 
ATOM   4276 H  H    . ASP   B 1 22  ? 51.708 -29.438 -11.124 1.00 24.59 ?  22  ASP   B H    1 
ATOM   4277 H  HA   . ASP   B 1 22  ? 51.497 -29.038 -8.485  1.00 23.84 ?  22  ASP   B HA   1 
ATOM   4278 H  HB2  . ASP   B 1 22  ? 53.525 -29.758 -9.425  1.00 25.46 ?  22  ASP   B HB2  1 
ATOM   4279 H  HB3  . ASP   B 1 22  ? 53.566 -28.471 -10.352 1.00 25.46 ?  22  ASP   B HB3  1 
ATOM   4280 N  N    . ILE   B 1 23  ? 50.662 -26.696 -8.376  1.00 18.24 ?  23  ILE   B N    1 
ATOM   4281 C  CA   . ILE   B 1 23  ? 50.070 -25.356 -8.443  1.00 17.05 ?  23  ILE   B CA   1 
ATOM   4282 C  C    . ILE   B 1 23  ? 51.127 -24.265 -8.588  1.00 16.69 ?  23  ILE   B C    1 
ATOM   4283 O  O    . ILE   B 1 23  ? 50.861 -23.225 -9.196  1.00 15.70 ?  23  ILE   B O    1 
ATOM   4284 C  CB   . ILE   B 1 23  ? 49.133 -25.106 -7.244  1.00 17.33 ?  23  ILE   B CB   1 
ATOM   4285 C  CG1  . ILE   B 1 23  ? 48.333 -23.817 -7.444  1.00 17.62 ?  23  ILE   B CG1  1 
ATOM   4286 C  CG2  . ILE   B 1 23  ? 49.903 -25.082 -5.941  1.00 18.19 ?  23  ILE   B CG2  1 
ATOM   4287 C  CD1  . ILE   B 1 23  ? 47.169 -23.664 -6.481  1.00 18.13 ?  23  ILE   B CD1  1 
ATOM   4288 H  H    . ILE   B 1 23  ? 50.511 -27.115 -7.645  1.00 21.95 ?  23  ILE   B H    1 
ATOM   4289 H  HA   . ILE   B 1 23  ? 49.519 -25.314 -9.239  1.00 20.51 ?  23  ILE   B HA   1 
ATOM   4290 H  HB   . ILE   B 1 23  ? 48.501 -25.842 -7.206  1.00 20.85 ?  23  ILE   B HB   1 
ATOM   4291 H  HG12 . ILE   B 1 23  ? 48.931 -23.058 -7.314  1.00 21.20 ?  23  ILE   B HG12 1 
ATOM   4292 H  HG13 . ILE   B 1 23  ? 47.982 -23.800 -8.348  1.00 21.20 ?  23  ILE   B HG13 1 
ATOM   4293 H  HG21 . ILE   B 1 23  ? 49.274 -25.051 -5.204  1.00 21.88 ?  23  ILE   B HG21 1 
ATOM   4294 H  HG22 . ILE   B 1 23  ? 50.443 -25.887 -5.879  1.00 21.88 ?  23  ILE   B HG22 1 
ATOM   4295 H  HG23 . ILE   B 1 23  ? 50.474 -24.300 -5.924  1.00 21.88 ?  23  ILE   B HG23 1 
ATOM   4296 H  HD11 . ILE   B 1 23  ? 46.683 -22.856 -6.702  1.00 21.81 ?  23  ILE   B HD11 1 
ATOM   4297 H  HD12 . ILE   B 1 23  ? 46.590 -24.437 -6.571  1.00 21.81 ?  23  ILE   B HD12 1 
ATOM   4298 H  HD13 . ILE   B 1 23  ? 47.513 -23.610 -5.577  1.00 21.81 ?  23  ILE   B HD13 1 
ATOM   4299 N  N    . VAL   B 1 24  ? 52.327 -24.469 -8.040  1.00 16.60 ?  24  VAL   B N    1 
ATOM   4300 C  CA   . VAL   B 1 24  ? 53.399 -23.487 -8.210  1.00 16.91 ?  24  VAL   B CA   1 
ATOM   4301 C  C    . VAL   B 1 24  ? 53.853 -23.452 -9.662  1.00 17.50 ?  24  VAL   B C    1 
ATOM   4302 O  O    . VAL   B 1 24  ? 53.995 -22.381 -10.266 1.00 17.37 ?  24  VAL   B O    1 
ATOM   4303 C  CB   . VAL   B 1 24  ? 54.574 -23.793 -7.261  1.00 17.63 ?  24  VAL   B CB   1 
ATOM   4304 C  CG1  . VAL   B 1 24  ? 55.777 -22.906 -7.588  1.00 17.69 ?  24  VAL   B CG1  1 
ATOM   4305 C  CG2  . VAL   B 1 24  ? 54.155 -23.608 -5.823  1.00 18.20 ?  24  VAL   B CG2  1 
ATOM   4306 H  H    . VAL   B 1 24  ? 52.544 -25.158 -7.578  1.00 19.97 ?  24  VAL   B H    1 
ATOM   4307 H  HA   . VAL   B 1 24  ? 53.060 -22.607 -7.984  1.00 20.35 ?  24  VAL   B HA   1 
ATOM   4308 H  HB   . VAL   B 1 24  ? 54.846 -24.715 -7.375  1.00 21.21 ?  24  VAL   B HB   1 
ATOM   4309 H  HG11 . VAL   B 1 24  ? 56.379 -22.897 -6.825  1.00 21.29 ?  24  VAL   B HG11 1 
ATOM   4310 H  HG12 . VAL   B 1 24  ? 56.235 -23.265 -8.362  1.00 21.29 ?  24  VAL   B HG12 1 
ATOM   4311 H  HG13 . VAL   B 1 24  ? 55.467 -22.005 -7.769  1.00 21.29 ?  24  VAL   B HG13 1 
ATOM   4312 H  HG21 . VAL   B 1 24  ? 54.886 -23.866 -5.241  1.00 21.89 ?  24  VAL   B HG21 1 
ATOM   4313 H  HG22 . VAL   B 1 24  ? 53.931 -22.673 -5.676  1.00 21.89 ?  24  VAL   B HG22 1 
ATOM   4314 H  HG23 . VAL   B 1 24  ? 53.379 -24.163 -5.645  1.00 21.89 ?  24  VAL   B HG23 1 
ATOM   4315 N  N    . GLU   B 1 25  ? 54.119 -24.627 -10.238 1.00 18.10 ?  25  GLU   B N    1 
ATOM   4316 C  CA   . GLU   B 1 25  ? 54.499 -24.672 -11.643 1.00 19.79 ?  25  GLU   B CA   1 
ATOM   4317 C  C    . GLU   B 1 25  ? 53.383 -24.136 -12.524 1.00 18.64 ?  25  GLU   B C    1 
ATOM   4318 O  O    . GLU   B 1 25  ? 53.642 -23.421 -13.501 1.00 19.53 ?  25  GLU   B O    1 
ATOM   4319 C  CB   . GLU   B 1 25  ? 54.904 -26.093 -12.035 1.00 24.32 ?  25  GLU   B CB   1 
ATOM   4320 C  CG   . GLU   B 1 25  ? 56.209 -26.541 -11.380 1.00 29.07 ?  25  GLU   B CG   1 
ATOM   4321 C  CD   . GLU   B 1 25  ? 57.296 -25.472 -11.385 1.00 33.28 ?  25  GLU   B CD   1 
ATOM   4322 O  OE1  . GLU   B 1 25  ? 57.679 -25.003 -12.478 1.00 35.69 ?  25  GLU   B OE1  1 
ATOM   4323 O  OE2  . GLU   B 1 25  ? 57.760 -25.089 -10.286 1.00 35.25 -1 25  GLU   B OE2  1 
ATOM   4324 H  H    . GLU   B 1 25  ? 54.078 -25.388 -9.846  1.00 21.78 ?  25  GLU   B H    1 
ATOM   4325 H  HA   . GLU   B 1 25  ? 55.251 -24.084 -11.783 1.00 23.80 ?  25  GLU   B HA   1 
ATOM   4326 H  HB2  . GLU   B 1 25  ? 54.205 -26.711 -11.757 1.00 29.24 ?  25  GLU   B HB2  1 
ATOM   4327 H  HB3  . GLU   B 1 25  ? 55.015 -26.139 -12.998 1.00 29.24 ?  25  GLU   B HB3  1 
ATOM   4328 H  HG2  . GLU   B 1 25  ? 56.040 -26.750 -10.456 1.00 34.93 ?  25  GLU   B HG2  1 
ATOM   4329 H  HG3  . GLU   B 1 25  ? 56.545 -27.316 -11.853 1.00 34.93 ?  25  GLU   B HG3  1 
ATOM   4330 N  N    A GLU   B 1 26  ? 52.132 -24.454 -12.184 0.66 17.76 ?  26  GLU   B N    1 
ATOM   4331 N  N    B GLU   B 1 26  ? 52.130 -24.454 -12.185 0.34 17.68 ?  26  GLU   B N    1 
ATOM   4332 C  CA   A GLU   B 1 26  ? 51.002 -23.939 -12.952 0.66 18.37 ?  26  GLU   B CA   1 
ATOM   4333 C  CA   B GLU   B 1 26  ? 51.000 -23.941 -12.954 0.34 17.58 ?  26  GLU   B CA   1 
ATOM   4334 C  C    A GLU   B 1 26  ? 50.951 -22.422 -12.893 0.66 17.52 ?  26  GLU   B C    1 
ATOM   4335 C  C    B GLU   B 1 26  ? 50.946 -22.422 -12.893 0.34 16.99 ?  26  GLU   B C    1 
ATOM   4336 O  O    A GLU   B 1 26  ? 50.763 -21.758 -13.917 0.66 18.67 ?  26  GLU   B O    1 
ATOM   4337 O  O    B GLU   B 1 26  ? 50.758 -21.757 -13.917 0.34 17.55 ?  26  GLU   B O    1 
ATOM   4338 C  CB   A GLU   B 1 26  ? 49.692 -24.521 -12.420 0.66 20.43 ?  26  GLU   B CB   1 
ATOM   4339 C  CB   B GLU   B 1 26  ? 49.689 -24.533 -12.429 0.34 18.69 ?  26  GLU   B CB   1 
ATOM   4340 C  CG   A GLU   B 1 26  ? 49.291 -25.826 -13.064 0.66 23.32 ?  26  GLU   B CG   1 
ATOM   4341 C  CG   B GLU   B 1 26  ? 49.217 -25.761 -13.182 0.34 20.35 ?  26  GLU   B CG   1 
ATOM   4342 C  CD   A GLU   B 1 26  ? 49.057 -25.699 -14.563 0.66 24.77 ?  26  GLU   B CD   1 
ATOM   4343 C  CD   B GLU   B 1 26  ? 48.831 -25.451 -14.629 0.34 20.68 ?  26  GLU   B CD   1 
ATOM   4344 O  OE1  A GLU   B 1 26  ? 48.234 -24.857 -14.980 0.66 25.51 ?  26  GLU   B OE1  1 
ATOM   4345 O  OE1  B GLU   B 1 26  ? 47.714 -24.934 -14.863 0.34 21.42 ?  26  GLU   B OE1  1 
ATOM   4346 O  OE2  A GLU   B 1 26  ? 49.702 -26.449 -15.321 0.66 25.64 -1 26  GLU   B OE2  1 
ATOM   4347 O  OE2  B GLU   B 1 26  ? 49.646 -25.719 -15.530 0.34 20.65 -1 26  GLU   B OE2  1 
ATOM   4348 H  H    A GLU   B 1 26  ? 51.910 -24.959 -11.522 0.66 21.37 ?  26  GLU   B H    1 
ATOM   4349 H  H    B GLU   B 1 26  ? 51.911 -24.956 -11.521 0.34 21.27 ?  26  GLU   B H    1 
ATOM   4350 H  HA   A GLU   B 1 26  ? 51.100 -24.201 -13.879 0.66 22.09 ?  26  GLU   B HA   1 
ATOM   4351 H  HA   B GLU   B 1 26  ? 51.103 -24.202 -13.881 0.34 21.15 ?  26  GLU   B HA   1 
ATOM   4352 H  HB2  A GLU   B 1 26  ? 49.783 -24.677 -11.465 0.66 24.57 ?  26  GLU   B HB2  1 
ATOM   4353 H  HB2  B GLU   B 1 26  ? 49.807 -24.779 -11.498 0.34 22.48 ?  26  GLU   B HB2  1 
ATOM   4354 H  HB3  A GLU   B 1 26  ? 48.978 -23.880 -12.577 0.66 24.57 ?  26  GLU   B HB3  1 
ATOM   4355 H  HB3  B GLU   B 1 26  ? 48.992 -23.861 -12.503 0.34 22.48 ?  26  GLU   B HB3  1 
ATOM   4356 H  HG2  A GLU   B 1 26  ? 50.003 -26.463 -12.929 0.66 28.03 ?  26  GLU   B HG2  1 
ATOM   4357 H  HG2  B GLU   B 1 26  ? 49.923 -26.431 -13.139 0.34 24.47 ?  26  GLU   B HG2  1 
ATOM   4358 H  HG3  A GLU   B 1 26  ? 48.472 -26.138 -12.648 0.66 28.03 ?  26  GLU   B HG3  1 
ATOM   4359 H  HG3  B GLU   B 1 26  ? 48.416 -26.098 -12.759 0.34 24.47 ?  26  GLU   B HG3  1 
ATOM   4360 N  N    . ALA   B 1 27  ? 51.094 -21.857 -11.693 1.00 16.64 ?  27  ALA   B N    1 
ATOM   4361 C  CA   . ALA   B 1 27  ? 51.061 -20.407 -11.558 1.00 17.14 ?  27  ALA   B CA   1 
ATOM   4362 C  C    . ALA   B 1 27  ? 52.128 -19.748 -12.424 1.00 17.95 ?  27  ALA   B C    1 
ATOM   4363 O  O    . ALA   B 1 27  ? 51.862 -18.747 -13.102 1.00 18.53 ?  27  ALA   B O    1 
ATOM   4364 C  CB   . ALA   B 1 27  ? 51.206 -20.019 -10.087 1.00 17.33 ?  27  ALA   B CB   1 
ATOM   4365 H  H    A ALA   B 1 27  ? 51.209 -22.286 -10.956 0.66 20.02 ?  27  ALA   B H    1 
ATOM   4366 H  H    B ALA   B 1 27  ? 51.214 -22.286 -10.957 0.34 20.02 ?  27  ALA   B H    1 
ATOM   4367 H  HA   . ALA   B 1 27  ? 50.199 -20.084 -11.859 1.00 20.62 ?  27  ALA   B HA   1 
ATOM   4368 H  HB1  . ALA   B 1 27  ? 51.174 -19.052 -10.008 1.00 20.85 ?  27  ALA   B HB1  1 
ATOM   4369 H  HB2  . ALA   B 1 27  ? 50.470 -20.411 -9.583  1.00 20.85 ?  27  ALA   B HB2  1 
ATOM   4370 H  HB3  . ALA   B 1 27  ? 52.049 -20.352 -9.750  1.00 20.85 ?  27  ALA   B HB3  1 
ATOM   4371 N  N    . LYS   B 1 28  ? 53.337 -20.312 -12.443 1.00 19.29 ?  28  LYS   B N    1 
ATOM   4372 C  CA   . LYS   B 1 28  ? 54.406 -19.691 -13.216 1.00 21.23 ?  28  LYS   B CA   1 
ATOM   4373 C  C    . LYS   B 1 28  ? 54.148 -19.784 -14.715 1.00 22.48 ?  28  LYS   B C    1 
ATOM   4374 O  O    . LYS   B 1 28  ? 54.563 -18.894 -15.469 1.00 23.59 ?  28  LYS   B O    1 
ATOM   4375 C  CB   . LYS   B 1 28  ? 55.767 -20.267 -12.810 1.00 23.92 ?  28  LYS   B CB   1 
ATOM   4376 C  CG   . LYS   B 1 28  ? 56.154 -19.884 -11.381 1.00 27.36 ?  28  LYS   B CG   1 
ATOM   4377 C  CD   . LYS   B 1 28  ? 57.594 -20.241 -11.032 1.00 30.65 ?  28  LYS   B CD   1 
ATOM   4378 C  CE   . LYS   B 1 28  ? 57.735 -21.705 -10.683 1.00 34.91 ?  28  LYS   B CE   1 
ATOM   4379 N  NZ   . LYS   B 1 28  ? 59.095 -22.015 -10.159 1.00 38.66 ?  28  LYS   B NZ   1 
ATOM   4380 H  H    . LYS   B 1 28  ? 53.557 -21.039 -12.034 1.00 23.20 ?  28  LYS   B H    1 
ATOM   4381 H  HA   . LYS   B 1 28  ? 54.426 -18.750 -12.998 1.00 25.53 ?  28  LYS   B HA   1 
ATOM   4382 H  HB2  . LYS   B 1 28  ? 55.737 -21.234 -12.862 1.00 28.76 ?  28  LYS   B HB2  1 
ATOM   4383 H  HB3  . LYS   B 1 28  ? 56.451 -19.922 -13.407 1.00 28.76 ?  28  LYS   B HB3  1 
ATOM   4384 H  HG2  . LYS   B 1 28  ? 56.050 -18.925 -11.275 1.00 32.88 ?  28  LYS   B HG2  1 
ATOM   4385 H  HG3  . LYS   B 1 28  ? 55.572 -20.350 -10.763 1.00 32.88 ?  28  LYS   B HG3  1 
ATOM   4386 H  HD2  . LYS   B 1 28  ? 58.164 -20.051 -11.794 1.00 36.83 ?  28  LYS   B HD2  1 
ATOM   4387 H  HD3  . LYS   B 1 28  ? 57.874 -19.715 -10.265 1.00 36.83 ?  28  LYS   B HD3  1 
ATOM   4388 H  HE2  . LYS   B 1 28  ? 57.085 -21.933 -9.999  1.00 41.95 ?  28  LYS   B HE2  1 
ATOM   4389 H  HE3  . LYS   B 1 28  ? 57.585 -22.238 -11.479 1.00 41.95 ?  28  LYS   B HE3  1 
ATOM   4390 H  HZ1  . LYS   B 1 28  ? 59.153 -22.880 -9.961  1.00 46.45 ?  28  LYS   B HZ1  1 
ATOM   4391 H  HZ2  . LYS   B 1 28  ? 59.708 -21.815 -10.771 1.00 46.45 ?  28  LYS   B HZ2  1 
ATOM   4392 H  HZ3  . LYS   B 1 28  ? 59.253 -21.537 -9.424  1.00 46.45 ?  28  LYS   B HZ3  1 
ATOM   4393 N  N    A LYS   B 1 29  ? 53.455 -20.831 -15.166 0.66 23.60 ?  29  LYS   B N    1 
ATOM   4394 N  N    B LYS   B 1 29  ? 53.438 -20.822 -15.162 0.34 23.61 ?  29  LYS   B N    1 
ATOM   4395 C  CA   A LYS   B 1 29  ? 53.158 -20.972 -16.587 0.66 25.86 ?  29  LYS   B CA   1 
ATOM   4396 C  CA   B LYS   B 1 29  ? 53.151 -20.993 -16.582 0.34 25.37 ?  29  LYS   B CA   1 
ATOM   4397 C  C    A LYS   B 1 29  ? 51.893 -20.226 -16.999 0.66 24.94 ?  29  LYS   B C    1 
ATOM   4398 C  C    B LYS   B 1 29  ? 51.881 -20.268 -17.016 0.34 24.42 ?  29  LYS   B C    1 
ATOM   4399 O  O    A LYS   B 1 29  ? 51.878 -19.580 -18.052 0.66 26.41 ?  29  LYS   B O    1 
ATOM   4400 O  O    B LYS   B 1 29  ? 51.847 -19.683 -18.104 0.34 25.14 ?  29  LYS   B O    1 
ATOM   4401 C  CB   A LYS   B 1 29  ? 53.034 -22.450 -16.961 0.66 29.63 ?  29  LYS   B CB   1 
ATOM   4402 C  CB   B LYS   B 1 29  ? 53.037 -22.482 -16.922 0.34 28.42 ?  29  LYS   B CB   1 
ATOM   4403 C  CG   A LYS   B 1 29  ? 52.840 -22.695 -18.450 0.66 33.13 ?  29  LYS   B CG   1 
ATOM   4404 C  CG   B LYS   B 1 29  ? 52.849 -22.761 -18.406 0.34 31.20 ?  29  LYS   B CG   1 
ATOM   4405 C  CD   A LYS   B 1 29  ? 53.042 -24.160 -18.801 0.66 35.81 ?  29  LYS   B CD   1 
ATOM   4406 C  CD   B LYS   B 1 29  ? 53.074 -24.231 -18.736 0.34 33.43 ?  29  LYS   B CD   1 
ATOM   4407 C  CE   A LYS   B 1 29  ? 51.986 -25.040 -18.155 0.66 37.65 ?  29  LYS   B CE   1 
ATOM   4408 C  CE   B LYS   B 1 29  ? 51.993 -25.118 -18.140 0.34 35.09 ?  29  LYS   B CE   1 
ATOM   4409 N  NZ   A LYS   B 1 29  ? 52.215 -26.479 -18.454 0.66 38.70 ?  29  LYS   B NZ   1 
ATOM   4410 N  NZ   B LYS   B 1 29  ? 52.246 -26.560 -18.423 0.34 35.96 ?  29  LYS   B NZ   1 
ATOM   4411 H  H    A LYS   B 1 29  ? 53.154 -21.472 -14.674 0.66 28.37 ?  29  LYS   B H    1 
ATOM   4412 H  H    B LYS   B 1 29  ? 53.110 -21.442 -14.661 0.34 28.39 ?  29  LYS   B H    1 
ATOM   4413 H  HA   A LYS   B 1 29  ? 53.892 -20.604 -17.097 0.66 31.09 ?  29  LYS   B HA   1 
ATOM   4414 H  HA   B LYS   B 1 29  ? 53.887 -20.629 -17.094 0.34 30.50 ?  29  LYS   B HA   1 
ATOM   4415 H  HB2  A LYS   B 1 29  ? 53.845 -22.911 -16.692 0.66 35.61 ?  29  LYS   B HB2  1 
ATOM   4416 H  HB2  B LYS   B 1 29  ? 53.849 -22.932 -16.638 0.34 34.16 ?  29  LYS   B HB2  1 
ATOM   4417 H  HB3  A LYS   B 1 29  ? 52.272 -22.827 -16.498 0.66 35.61 ?  29  LYS   B HB3  1 
ATOM   4418 H  HB3  B LYS   B 1 29  ? 52.274 -22.855 -16.453 0.34 34.16 ?  29  LYS   B HB3  1 
ATOM   4419 H  HG2  A LYS   B 1 29  ? 51.936 -22.446 -18.701 0.66 39.81 ?  29  LYS   B HG2  1 
ATOM   4420 H  HG2  B LYS   B 1 29  ? 51.943 -22.527 -18.663 0.34 37.49 ?  29  LYS   B HG2  1 
ATOM   4421 H  HG3  A LYS   B 1 29  ? 53.484 -22.170 -18.950 0.66 39.81 ?  29  LYS   B HG3  1 
ATOM   4422 H  HG3  B LYS   B 1 29  ? 53.487 -22.234 -18.913 0.34 37.49 ?  29  LYS   B HG3  1 
ATOM   4423 H  HD2  A LYS   B 1 29  ? 52.983 -24.270 -19.764 0.66 43.03 ?  29  LYS   B HD2  1 
ATOM   4424 H  HD2  B LYS   B 1 29  ? 53.064 -24.348 -19.699 0.34 40.17 ?  29  LYS   B HD2  1 
ATOM   4425 H  HD3  A LYS   B 1 29  ? 53.913 -24.448 -18.484 0.66 43.03 ?  29  LYS   B HD3  1 
ATOM   4426 H  HD3  B LYS   B 1 29  ? 53.929 -24.513 -18.374 0.34 40.17 ?  29  LYS   B HD3  1 
ATOM   4427 H  HE2  A LYS   B 1 29  ? 52.014 -24.925 -17.192 0.66 45.23 ?  29  LYS   B HE2  1 
ATOM   4428 H  HE2  B LYS   B 1 29  ? 51.972 -24.998 -17.178 0.34 42.16 ?  29  LYS   B HE2  1 
ATOM   4429 H  HE3  A LYS   B 1 29  ? 51.112 -24.791 -18.497 0.66 45.23 ?  29  LYS   B HE3  1 
ATOM   4430 H  HE3  B LYS   B 1 29  ? 51.135 -24.878 -18.526 0.34 42.16 ?  29  LYS   B HE3  1 
ATOM   4431 H  HZ1  A LYS   B 1 29  ? 51.586 -26.973 -18.066 0.66 46.49 ?  29  LYS   B HZ1  1 
ATOM   4432 H  HZ1  B LYS   B 1 29  ? 51.601 -27.058 -18.065 0.34 43.21 ?  29  LYS   B HZ1  1 
ATOM   4433 H  HZ2  A LYS   B 1 29  ? 52.190 -26.614 -19.333 0.66 46.49 ?  29  LYS   B HZ2  1 
ATOM   4434 H  HZ2  B LYS   B 1 29  ? 52.265 -26.699 -19.302 0.34 43.21 ?  29  LYS   B HZ2  1 
ATOM   4435 H  HZ3  A LYS   B 1 29  ? 53.012 -26.729 -18.146 0.66 46.49 ?  29  LYS   B HZ3  1 
ATOM   4436 H  HZ3  B LYS   B 1 29  ? 53.028 -26.805 -18.075 0.34 43.21 ?  29  LYS   B HZ3  1 
ATOM   4437 N  N    . VAL   B 1 30  ? 50.833 -20.304 -16.190 1.00 22.97 ?  30  VAL   B N    1 
ATOM   4438 C  CA   . VAL   B 1 30  ? 49.555 -19.691 -16.555 1.00 22.05 ?  30  VAL   B CA   1 
ATOM   4439 C  C    . VAL   B 1 30  ? 49.570 -18.179 -16.397 1.00 20.13 ?  30  VAL   B C    1 
ATOM   4440 O  O    . VAL   B 1 30  ? 48.819 -17.472 -17.088 1.00 20.87 ?  30  VAL   B O    1 
ATOM   4441 C  CB   . VAL   B 1 30  ? 48.447 -20.292 -15.672 1.00 22.78 ?  30  VAL   B CB   1 
ATOM   4442 C  CG1  . VAL   B 1 30  ? 47.152 -19.508 -15.816 1.00 24.13 ?  30  VAL   B CG1  1 
ATOM   4443 C  CG2  . VAL   B 1 30  ? 48.244 -21.763 -16.000 1.00 23.30 ?  30  VAL   B CG2  1 
ATOM   4444 H  H    A VAL   B 1 30  ? 50.826 -20.715 -15.432 0.66 27.62 ?  30  VAL   B H    1 
ATOM   4445 H  H    B VAL   B 1 30  ? 50.832 -20.693 -15.420 0.34 27.62 ?  30  VAL   B H    1 
ATOM   4446 H  HA   . VAL   B 1 30  ? 49.351 -19.912 -17.479 1.00 26.52 ?  30  VAL   B HA   1 
ATOM   4447 H  HB   . VAL   B 1 30  ? 48.720 -20.240 -14.743 1.00 27.39 ?  30  VAL   B HB   1 
ATOM   4448 H  HG11 . VAL   B 1 30  ? 46.412 -20.107 -15.626 1.00 29.01 ?  30  VAL   B HG11 1 
ATOM   4449 H  HG12 . VAL   B 1 30  ? 47.152 -18.776 -15.186 1.00 29.01 ?  30  VAL   B HG12 1 
ATOM   4450 H  HG13 . VAL   B 1 30  ? 47.077 -19.185 -16.722 1.00 29.01 ?  30  VAL   B HG13 1 
ATOM   4451 H  HG21 . VAL   B 1 30  ? 47.539 -22.125 -15.432 1.00 28.02 ?  30  VAL   B HG21 1 
ATOM   4452 H  HG22 . VAL   B 1 30  ? 47.982 -21.849 -16.933 1.00 28.02 ?  30  VAL   B HG22 1 
ATOM   4453 H  HG23 . VAL   B 1 30  ? 49.069 -22.245 -15.843 1.00 28.02 ?  30  VAL   B HG23 1 
ATOM   4454 N  N    A LYS   B 1 31  ? 50.392 -17.663 -15.489 0.66 19.34 ?  31  LYS   B N    1 
ATOM   4455 N  N    B LYS   B 1 31  ? 50.391 -17.669 -15.487 0.34 19.77 ?  31  LYS   B N    1 
ATOM   4456 C  CA   A LYS   B 1 31  ? 50.412 -16.247 -15.137 0.66 19.64 ?  31  LYS   B CA   1 
ATOM   4457 C  CA   B LYS   B 1 31  ? 50.412 -16.256 -15.132 0.34 19.92 ?  31  LYS   B CA   1 
ATOM   4458 C  C    A LYS   B 1 31  ? 49.022 -15.738 -14.744 0.66 18.19 ?  31  LYS   B C    1 
ATOM   4459 C  C    B LYS   B 1 31  ? 49.014 -15.756 -14.756 0.34 18.32 ?  31  LYS   B C    1 
ATOM   4460 O  O    A LYS   B 1 31  ? 48.487 -14.819 -15.375 0.66 18.95 ?  31  LYS   B O    1 
ATOM   4461 O  O    B LYS   B 1 31  ? 48.468 -14.863 -15.412 0.34 18.43 ?  31  LYS   B O    1 
ATOM   4462 C  CB   A LYS   B 1 31  ? 51.027 -15.400 -16.243 0.66 22.46 ?  31  LYS   B CB   1 
ATOM   4463 C  CB   B LYS   B 1 31  ? 51.026 -15.414 -16.241 0.34 22.12 ?  31  LYS   B CB   1 
ATOM   4464 C  CG   A LYS   B 1 31  ? 52.481 -15.766 -16.529 0.66 25.54 ?  31  LYS   B CG   1 
ATOM   4465 C  CG   B LYS   B 1 31  ? 52.440 -15.866 -16.586 0.34 24.30 ?  31  LYS   B CG   1 
ATOM   4466 C  CD   A LYS   B 1 31  ? 53.049 -14.979 -17.694 0.66 28.18 ?  31  LYS   B CD   1 
ATOM   4467 C  CD   B LYS   B 1 31  ? 53.029 -15.092 -17.745 0.34 26.32 ?  31  LYS   B CD   1 
ATOM   4468 C  CE   A LYS   B 1 31  ? 54.530 -15.248 -17.861 0.66 30.04 ?  31  LYS   B CE   1 
ATOM   4469 C  CE   B LYS   B 1 31  ? 54.512 -15.375 -17.882 0.34 27.90 ?  31  LYS   B CE   1 
ATOM   4470 N  NZ   A LYS   B 1 31  ? 55.292 -14.835 -16.649 0.66 32.04 ?  31  LYS   B NZ   1 
ATOM   4471 N  NZ   B LYS   B 1 31  ? 55.246 -15.015 -16.636 0.34 28.90 ?  31  LYS   B NZ   1 
ATOM   4472 H  H    A LYS   B 1 31  ? 50.970 -18.135 -15.055 0.66 23.26 ?  31  LYS   B H    1 
ATOM   4473 H  H    B LYS   B 1 31  ? 50.966 -18.140 -15.054 0.34 23.78 ?  31  LYS   B H    1 
ATOM   4474 H  HA   A LYS   B 1 31  ? 50.975 -16.154 -14.360 0.66 23.62 ?  31  LYS   B HA   1 
ATOM   4475 H  HA   B LYS   B 1 31  ? 50.972 -16.160 -14.353 0.34 23.96 ?  31  LYS   B HA   1 
ATOM   4476 H  HB2  A LYS   B 1 31  ? 50.519 -15.525 -17.059 0.66 27.00 ?  31  LYS   B HB2  1 
ATOM   4477 H  HB2  B LYS   B 1 31  ? 50.483 -15.485 -17.039 0.34 26.60 ?  31  LYS   B HB2  1 
ATOM   4478 H  HB3  A LYS   B 1 31  ? 50.999 -14.471 -15.971 0.66 27.00 ?  31  LYS   B HB3  1 
ATOM   4479 H  HB3  B LYS   B 1 31  ? 51.070 -14.491 -15.945 0.34 26.60 ?  31  LYS   B HB3  1 
ATOM   4480 H  HG2  A LYS   B 1 31  ? 53.014 -15.576 -15.741 0.66 30.71 ?  31  LYS   B HG2  1 
ATOM   4481 H  HG2  B LYS   B 1 31  ? 53.008 -15.737 -15.810 0.34 29.21 ?  31  LYS   B HG2  1 
ATOM   4482 H  HG3  A LYS   B 1 31  ? 52.535 -16.711 -16.747 0.66 30.71 ?  31  LYS   B HG3  1 
ATOM   4483 H  HG3  B LYS   B 1 31  ? 52.425 -16.805 -16.831 0.34 29.21 ?  31  LYS   B HG3  1 
ATOM   4484 H  HD2  A LYS   B 1 31  ? 52.592 -15.246 -18.507 0.66 33.87 ?  31  LYS   B HD2  1 
ATOM   4485 H  HD2  B LYS   B 1 31  ? 52.588 -15.361 -18.566 0.34 31.64 ?  31  LYS   B HD2  1 
ATOM   4486 H  HD3  A LYS   B 1 31  ? 52.922 -14.034 -17.528 0.66 33.87 ?  31  LYS   B HD3  1 
ATOM   4487 H  HD3  B LYS   B 1 31  ? 52.910 -14.144 -17.590 0.34 31.64 ?  31  LYS   B HD3  1 
ATOM   4488 H  HE2  A LYS   B 1 31  ? 54.671 -16.198 -18.002 0.66 36.10 ?  31  LYS   B HE2  1 
ATOM   4489 H  HE2  B LYS   B 1 31  ? 54.645 -16.322 -18.051 0.34 33.54 ?  31  LYS   B HE2  1 
ATOM   4490 H  HE3  A LYS   B 1 31  ? 54.862 -14.742 -18.618 0.66 36.10 ?  31  LYS   B HE3  1 
ATOM   4491 H  HE3  B LYS   B 1 31  ? 54.873 -14.849 -18.612 0.34 33.54 ?  31  LYS   B HE3  1 
ATOM   4492 H  HZ1  A LYS   B 1 31  ? 56.166 -14.897 -16.804 0.66 38.50 ?  31  LYS   B HZ1  1 
ATOM   4493 H  HZ1  B LYS   B 1 31  ? 56.122 -15.016 -16.787 0.34 34.74 ?  31  LYS   B HZ1  1 
ATOM   4494 H  HZ2  A LYS   B 1 31  ? 55.094 -13.994 -16.437 0.66 38.50 ?  31  LYS   B HZ2  1 
ATOM   4495 H  HZ2  B LYS   B 1 31  ? 55.000 -14.204 -16.363 0.34 34.74 ?  31  LYS   B HZ2  1 
ATOM   4496 H  HZ3  A LYS   B 1 31  ? 55.083 -15.363 -15.962 0.66 38.50 ?  31  LYS   B HZ3  1 
ATOM   4497 H  HZ3  B LYS   B 1 31  ? 55.063 -15.603 -15.993 0.34 34.74 ?  31  LYS   B HZ3  1 
ATOM   4498 N  N    . PRO   B 1 32  ? 48.414 -16.313 -13.706 1.00 17.28 ?  32  PRO   B N    1 
ATOM   4499 C  CA   . PRO   B 1 32  ? 47.043 -15.943 -13.346 1.00 17.07 ?  32  PRO   B CA   1 
ATOM   4500 C  C    . PRO   B 1 32  ? 46.978 -14.606 -12.635 1.00 16.86 ?  32  PRO   B C    1 
ATOM   4501 O  O    . PRO   B 1 32  ? 47.910 -14.189 -11.940 1.00 17.87 ?  32  PRO   B O    1 
ATOM   4502 C  CB   . PRO   B 1 32  ? 46.640 -17.057 -12.374 1.00 17.26 ?  32  PRO   B CB   1 
ATOM   4503 C  CG   . PRO   B 1 32  ? 47.946 -17.402 -11.690 1.00 17.25 ?  32  PRO   B CG   1 
ATOM   4504 C  CD   . PRO   B 1 32  ? 49.001 -17.273 -12.750 1.00 17.34 ?  32  PRO   B CD   1 
ATOM   4505 H  HA   . PRO   B 1 32  ? 46.459 -15.952 -14.127 1.00 20.53 ?  32  PRO   B HA   1 
ATOM   4506 H  HB2  . PRO   B 1 32  ? 45.984 -16.724 -11.739 1.00 20.76 ?  32  PRO   B HB2  1 
ATOM   4507 H  HB3  . PRO   B 1 32  ? 46.288 -17.823 -12.864 1.00 20.76 ?  32  PRO   B HB3  1 
ATOM   4508 H  HG2  . PRO   B 1 32  ? 48.106 -16.774 -10.966 1.00 20.75 ?  32  PRO   B HG2  1 
ATOM   4509 H  HG3  . PRO   B 1 32  ? 47.909 -18.310 -11.350 1.00 20.75 ?  32  PRO   B HG3  1 
ATOM   4510 H  HD2  . PRO   B 1 32  ? 49.812 -16.907 -12.365 1.00 20.86 ?  32  PRO   B HD2  1 
ATOM   4511 H  HD3  . PRO   B 1 32  ? 49.155 -18.130 -13.168 1.00 20.86 ?  32  PRO   B HD3  1 
ATOM   4512 N  N    . THR   B 1 33  ? 45.827 -13.952 -12.793 1.00 16.36 ?  33  THR   B N    1 
ATOM   4513 C  CA   . THR   B 1 33  ? 45.540 -12.772 -11.986 1.00 16.91 ?  33  THR   B CA   1 
ATOM   4514 C  C    . THR   B 1 33  ? 45.494 -13.120 -10.503 1.00 16.36 ?  33  THR   B C    1 
ATOM   4515 O  O    . THR   B 1 33  ? 45.979 -12.339 -9.666  1.00 16.94 ?  33  THR   B O    1 
ATOM   4516 C  CB   . THR   B 1 33  ? 44.228 -12.123 -12.435 1.00 17.71 ?  33  THR   B CB   1 
ATOM   4517 O  OG1  . THR   B 1 33  ? 44.253 -11.889 -13.845 1.00 17.61 ?  33  THR   B OG1  1 
ATOM   4518 C  CG2  . THR   B 1 33  ? 43.994 -10.821 -11.703 1.00 18.92 ?  33  THR   B CG2  1 
ATOM   4519 H  H    . THR   B 1 33  ? 45.208 -14.175 -13.352 1.00 19.68 ?  33  THR   B H    1 
ATOM   4520 H  HA   . THR   B 1 33  ? 46.250 -12.131 -12.120 1.00 20.35 ?  33  THR   B HA   1 
ATOM   4521 H  HB   . THR   B 1 33  ? 43.491 -12.726 -12.230 1.00 21.31 ?  33  THR   B HB   1 
ATOM   4522 H  HG1  . THR   B 1 33  ? 43.537 -11.520 -14.090 1.00 21.18 ?  33  THR   B HG1  1 
ATOM   4523 H  HG21 . THR   B 1 33  ? 43.239 -10.356 -12.091 1.00 22.75 ?  33  THR   B HG21 1 
ATOM   4524 H  HG22 . THR   B 1 33  ? 43.815 -10.991 -10.766 1.00 22.75 ?  33  THR   B HG22 1 
ATOM   4525 H  HG23 . THR   B 1 33  ? 44.783 -10.258 -11.777 1.00 22.75 ?  33  THR   B HG23 1 
ATOM   4526 N  N    . VAL   B 1 34  ? 44.924 -14.284 -10.158 1.00 15.50 ?  34  VAL   B N    1 
ATOM   4527 C  CA   . VAL   B 1 34  ? 44.711 -14.669 -8.766  1.00 15.53 ?  34  VAL   B CA   1 
ATOM   4528 C  C    . VAL   B 1 34  ? 45.137 -16.119 -8.590  1.00 14.86 ?  34  VAL   B C    1 
ATOM   4529 O  O    . VAL   B 1 34  ? 44.609 -17.008 -9.269  1.00 15.27 ?  34  VAL   B O    1 
ATOM   4530 C  CB   . VAL   B 1 34  ? 43.237 -14.525 -8.344  1.00 16.29 ?  34  VAL   B CB   1 
ATOM   4531 C  CG1  . VAL   B 1 34  ? 43.059 -14.953 -6.897  1.00 16.12 ?  34  VAL   B CG1  1 
ATOM   4532 C  CG2  . VAL   B 1 34  ? 42.739 -13.102 -8.558  1.00 16.95 ?  34  VAL   B CG2  1 
ATOM   4533 H  H    . VAL   B 1 34  ? 44.655 -14.876 -10.722 1.00 18.65 ?  34  VAL   B H    1 
ATOM   4534 H  HA   . VAL   B 1 34  ? 45.254 -14.120 -8.185  1.00 18.70 ?  34  VAL   B HA   1 
ATOM   4535 H  HB   . VAL   B 1 34  ? 42.697 -15.113 -8.896  1.00 19.60 ?  34  VAL   B HB   1 
ATOM   4536 H  HG11 . VAL   B 1 34  ? 42.195 -14.634 -6.581  1.00 19.40 ?  34  VAL   B HG11 1 
ATOM   4537 H  HG12 . VAL   B 1 34  ? 43.087 -15.921 -6.842  1.00 19.40 ?  34  VAL   B HG12 1 
ATOM   4538 H  HG13 . VAL   B 1 34  ? 43.766 -14.566 -6.361  1.00 19.40 ?  34  VAL   B HG13 1 
ATOM   4539 H  HG21 . VAL   B 1 34  ? 41.820 -13.039 -8.258  1.00 20.40 ?  34  VAL   B HG21 1 
ATOM   4540 H  HG22 . VAL   B 1 34  ? 43.297 -12.492 -8.048  1.00 20.40 ?  34  VAL   B HG22 1 
ATOM   4541 H  HG23 . VAL   B 1 34  ? 42.794 -12.885 -9.503  1.00 20.40 ?  34  VAL   B HG23 1 
ATOM   4542 N  N    . VAL   B 1 35  ? 46.039 -16.372 -7.646  1.00 14.07 ?  35  VAL   B N    1 
ATOM   4543 C  CA   . VAL   B 1 35  ? 46.262 -17.714 -7.120  1.00 14.01 ?  35  VAL   B CA   1 
ATOM   4544 C  C    . VAL   B 1 35  ? 45.723 -17.761 -5.700  1.00 13.36 ?  35  VAL   B C    1 
ATOM   4545 O  O    . VAL   B 1 35  ? 45.939 -16.833 -4.910  1.00 13.22 ?  35  VAL   B O    1 
ATOM   4546 C  CB   . VAL   B 1 35  ? 47.744 -18.149 -7.186  1.00 15.06 ?  35  VAL   B CB   1 
ATOM   4547 C  CG1  . VAL   B 1 35  ? 48.645 -17.326 -6.244  1.00 15.38 ?  35  VAL   B CG1  1 
ATOM   4548 C  CG2  . VAL   B 1 35  ? 47.880 -19.653 -6.886  1.00 15.47 ?  35  VAL   B CG2  1 
ATOM   4549 H  H    . VAL   B 1 35  ? 46.545 -15.770 -7.289  1.00 16.94 ?  35  VAL   B H    1 
ATOM   4550 H  HA   . VAL   B 1 35  ? 45.752 -18.346 -7.641  1.00 16.87 ?  35  VAL   B HA   1 
ATOM   4551 H  HB   . VAL   B 1 35  ? 48.063 -18.003 -8.089  1.00 18.13 ?  35  VAL   B HB   1 
ATOM   4552 H  HG11 . VAL   B 1 35  ? 49.569 -17.551 -6.431  1.00 18.51 ?  35  VAL   B HG11 1 
ATOM   4553 H  HG12 . VAL   B 1 35  ? 48.485 -16.390 -6.399  1.00 18.51 ?  35  VAL   B HG12 1 
ATOM   4554 H  HG13 . VAL   B 1 35  ? 48.427 -17.561 -5.326  1.00 18.51 ?  35  VAL   B HG13 1 
ATOM   4555 H  HG21 . VAL   B 1 35  ? 48.807 -19.923 -6.974  1.00 18.61 ?  35  VAL   B HG21 1 
ATOM   4556 H  HG22 . VAL   B 1 35  ? 47.569 -19.837 -5.982  1.00 18.61 ?  35  VAL   B HG22 1 
ATOM   4557 H  HG23 . VAL   B 1 35  ? 47.334 -20.160 -7.520  1.00 18.61 ?  35  VAL   B HG23 1 
ATOM   4558 N  N    . VAL   B 1 36  ? 45.013 -18.844 -5.382  1.00 13.81 ?  36  VAL   B N    1 
ATOM   4559 C  CA   . VAL   B 1 36  ? 44.455 -19.037 -4.053  1.00 13.43 ?  36  VAL   B CA   1 
ATOM   4560 C  C    . VAL   B 1 36  ? 45.455 -19.799 -3.196  1.00 13.42 ?  36  VAL   B C    1 
ATOM   4561 O  O    . VAL   B 1 36  ? 46.000 -20.831 -3.616  1.00 14.01 ?  36  VAL   B O    1 
ATOM   4562 C  CB   . VAL   B 1 36  ? 43.122 -19.801 -4.137  1.00 13.92 ?  36  VAL   B CB   1 
ATOM   4563 C  CG1  . VAL   B 1 36  ? 42.620 -20.150 -2.741  1.00 14.27 ?  36  VAL   B CG1  1 
ATOM   4564 C  CG2  . VAL   B 1 36  ? 42.107 -18.980 -4.901  1.00 14.59 ?  36  VAL   B CG2  1 
ATOM   4565 H  H    . VAL   B 1 36  ? 44.863 -19.497 -5.916  1.00 16.63 ?  36  VAL   B H    1 
ATOM   4566 H  HA   . VAL   B 1 36  ? 44.290 -18.173 -3.640  1.00 16.17 ?  36  VAL   B HA   1 
ATOM   4567 H  HB   . VAL   B 1 36  ? 43.265 -20.627 -4.620  1.00 16.76 ?  36  VAL   B HB   1 
ATOM   4568 H  HG11 . VAL   B 1 36  ? 41.677 -20.365 -2.793  1.00 17.18 ?  36  VAL   B HG11 1 
ATOM   4569 H  HG12 . VAL   B 1 36  ? 43.118 -20.908 -2.404  1.00 17.18 ?  36  VAL   B HG12 1 
ATOM   4570 H  HG13 . VAL   B 1 36  ? 42.750 -19.380 -2.160  1.00 17.18 ?  36  VAL   B HG13 1 
ATOM   4571 H  HG21 . VAL   B 1 36  ? 41.265 -19.461 -4.926  1.00 17.57 ?  36  VAL   B HG21 1 
ATOM   4572 H  HG22 . VAL   B 1 36  ? 41.987 -18.126 -4.457  1.00 17.57 ?  36  VAL   B HG22 1 
ATOM   4573 H  HG23 . VAL   B 1 36  ? 42.430 -18.838 -5.807  1.00 17.57 ?  36  VAL   B HG23 1 
ATOM   4574 N  N    . ASN   B 1 37  ? 45.672 -19.309 -1.979  1.00 13.59 ?  37  ASN   B N    1 
ATOM   4575 C  CA   . ASN   B 1 37  ? 46.432 -20.032 -0.975  1.00 14.01 ?  37  ASN   B CA   1 
ATOM   4576 C  C    . ASN   B 1 37  ? 45.482 -20.704 0.008   1.00 14.23 ?  37  ASN   B C    1 
ATOM   4577 O  O    . ASN   B 1 37  ? 44.475 -20.120 0.418   1.00 14.13 ?  37  ASN   B O    1 
ATOM   4578 C  CB   . ASN   B 1 37  ? 47.356 -19.092 -0.214  1.00 14.08 ?  37  ASN   B CB   1 
ATOM   4579 C  CG   . ASN   B 1 37  ? 48.194 -19.814 0.797   1.00 14.40 ?  37  ASN   B CG   1 
ATOM   4580 O  OD1  . ASN   B 1 37  ? 48.533 -20.988 0.618   1.00 15.08 ?  37  ASN   B OD1  1 
ATOM   4581 N  ND2  . ASN   B 1 37  ? 48.547 -19.121 1.872   1.00 14.35 ?  37  ASN   B ND2  1 
ATOM   4582 H  H    . ASN   B 1 37  ? 45.377 -18.548 -1.699  1.00 16.36 ?  37  ASN   B H    1 
ATOM   4583 H  HA   . ASN   B 1 37  ? 46.965 -20.721 -1.394  1.00 16.87 ?  37  ASN   B HA   1 
ATOM   4584 H  HB2  . ASN   B 1 37  ? 47.957 -18.666 -0.847  1.00 16.96 ?  37  ASN   B HB2  1 
ATOM   4585 H  HB3  . ASN   B 1 37  ? 46.832 -18.426 0.251   1.00 16.96 ?  37  ASN   B HB3  1 
ATOM   4586 H  HD21 . ASN   B 1 37  ? 49.038 -19.488 2.478   1.00 17.27 ?  37  ASN   B HD21 1 
ATOM   4587 H  HD22 . ASN   B 1 37  ? 48.297 -18.309 1.965   1.00 17.27 ?  37  ASN   B HD22 1 
ATOM   4588 N  N    . ALA   B 1 38  ? 45.820 -21.942 0.379   1.00 14.59 ?  38  ALA   B N    1 
ATOM   4589 C  CA   . ALA   B 1 38  ? 45.164 -22.684 1.458   1.00 15.12 ?  38  ALA   B CA   1 
ATOM   4590 C  C    . ALA   B 1 38  ? 45.760 -22.199 2.777   1.00 14.59 ?  38  ALA   B C    1 
ATOM   4591 O  O    . ALA   B 1 38  ? 46.655 -22.816 3.363   1.00 15.32 ?  38  ALA   B O    1 
ATOM   4592 C  CB   . ALA   B 1 38  ? 45.388 -24.182 1.277   1.00 16.60 ?  38  ALA   B CB   1 
ATOM   4593 H  H    . ALA   B 1 38  ? 46.468 -22.381 0.025   1.00 17.57 ?  38  ALA   B H    1 
ATOM   4594 H  HA   . ALA   B 1 38  ? 44.214 -22.502 1.458   1.00 18.20 ?  38  ALA   B HA   1 
ATOM   4595 H  HB1  . ALA   B 1 38  ? 44.943 -24.658 2.002   1.00 19.98 ?  38  ALA   B HB1  1 
ATOM   4596 H  HB2  . ALA   B 1 38  ? 45.013 -24.453 0.428   1.00 19.98 ?  38  ALA   B HB2  1 
ATOM   4597 H  HB3  . ALA   B 1 38  ? 46.338 -24.367 1.299   1.00 19.98 ?  38  ALA   B HB3  1 
ATOM   4598 N  N    . ALA   B 1 39  ? 45.246 -21.058 3.240   1.00 14.56 ?  39  ALA   B N    1 
ATOM   4599 C  CA   . ALA   B 1 39  ? 45.799 -20.327 4.368   1.00 14.99 ?  39  ALA   B CA   1 
ATOM   4600 C  C    . ALA   B 1 39  ? 45.173 -20.765 5.690   1.00 15.06 ?  39  ALA   B C    1 
ATOM   4601 O  O    . ALA   B 1 39  ? 44.147 -21.445 5.734   1.00 15.89 ?  39  ALA   B O    1 
ATOM   4602 C  CB   . ALA   B 1 39  ? 45.570 -18.824 4.175   1.00 14.84 ?  39  ALA   B CB   1 
ATOM   4603 H  H    . ALA   B 1 39  ? 44.552 -20.683 2.905   1.00 17.52 ?  39  ALA   B H    1 
ATOM   4604 H  HA   . ALA   B 1 39  ? 46.754 -20.483 4.417   1.00 18.05 ?  39  ALA   B HA   1 
ATOM   4605 H  HB1  . ALA   B 1 39  ? 45.944 -18.347 4.931   1.00 17.87 ?  39  ALA   B HB1  1 
ATOM   4606 H  HB2  . ALA   B 1 39  ? 46.006 -18.542 3.355   1.00 17.87 ?  39  ALA   B HB2  1 
ATOM   4607 H  HB3  . ALA   B 1 39  ? 44.616 -18.656 4.115   1.00 17.87 ?  39  ALA   B HB3  1 
ATOM   4608 N  N    . ASN   B 1 40  ? 45.808 -20.346 6.782   1.00 15.52 ?  40  ASN   B N    1 
ATOM   4609 C  CA   . ASN   B 1 40  ? 45.244 -20.398 8.122   1.00 16.30 ?  40  ASN   B CA   1 
ATOM   4610 C  C    . ASN   B 1 40  ? 45.049 -18.974 8.642   1.00 16.19 ?  40  ASN   B C    1 
ATOM   4611 O  O    . ASN   B 1 40  ? 45.461 -17.995 8.012   1.00 16.19 ?  40  ASN   B O    1 
ATOM   4612 C  CB   . ASN   B 1 40  ? 46.106 -21.256 9.063   1.00 17.00 ?  40  ASN   B CB   1 
ATOM   4613 C  CG   . ASN   B 1 40  ? 47.560 -20.851 9.066   1.00 18.15 ?  40  ASN   B CG   1 
ATOM   4614 O  OD1  . ASN   B 1 40  ? 47.884 -19.666 9.116   1.00 19.69 ?  40  ASN   B OD1  1 
ATOM   4615 N  ND2  . ASN   B 1 40  ? 48.443 -21.827 9.016   1.00 17.84 ?  40  ASN   B ND2  1 
ATOM   4616 H  H    . ASN   B 1 40  ? 46.593 -19.995 6.762   1.00 18.68 ?  40  ASN   B H    1 
ATOM   4617 H  HA   . ASN   B 1 40  ? 44.368 -20.807 8.072   1.00 19.61 ?  40  ASN   B HA   1 
ATOM   4618 H  HB2  . ASN   B 1 40  ? 45.764 -21.167 9.964   1.00 20.45 ?  40  ASN   B HB2  1 
ATOM   4619 H  HB3  . ASN   B 1 40  ? 46.052 -22.180 8.775   1.00 20.45 ?  40  ASN   B HB3  1 
ATOM   4620 H  HD21 . ASN   B 1 40  ? 49.283 -21.655 9.013   1.00 21.46 ?  40  ASN   B HD21 1 
ATOM   4621 H  HD22 . ASN   B 1 40  ? 48.173 -22.647 8.978   1.00 21.46 ?  40  ASN   B HD22 1 
ATOM   4622 N  N    . VAL   B 1 41  ? 44.401 -18.853 9.803   1.00 16.67 ?  41  VAL   B N    1 
ATOM   4623 C  CA   . VAL   B 1 41  ? 43.938 -17.533 10.249  1.00 17.26 ?  41  VAL   B CA   1 
ATOM   4624 C  C    . VAL   B 1 41  ? 45.088 -16.568 10.525  1.00 17.20 ?  41  VAL   B C    1 
ATOM   4625 O  O    . VAL   B 1 41  ? 44.913 -15.346 10.423  1.00 16.88 ?  41  VAL   B O    1 
ATOM   4626 C  CB   . VAL   B 1 41  ? 42.969 -17.620 11.448  1.00 18.40 ?  41  VAL   B CB   1 
ATOM   4627 C  CG1  . VAL   B 1 41  ? 41.660 -18.286 11.041  1.00 18.45 ?  41  VAL   B CG1  1 
ATOM   4628 C  CG2  . VAL   B 1 41  ? 43.614 -18.336 12.626  1.00 19.33 ?  41  VAL   B CG2  1 
ATOM   4629 H  H    . VAL   B 1 41  ? 44.223 -19.499 10.335  1.00 20.05 ?  41  VAL   B H    1 
ATOM   4630 H  HA   . VAL   B 1 41  ? 43.429 -17.148 9.524   1.00 20.77 ?  41  VAL   B HA   1 
ATOM   4631 H  HB   . VAL   B 1 41  ? 42.759 -16.720 11.739  1.00 22.13 ?  41  VAL   B HB   1 
ATOM   4632 H  HG11 . VAL   B 1 41  ? 41.057 -18.288 11.800  1.00 22.19 ?  41  VAL   B HG11 1 
ATOM   4633 H  HG12 . VAL   B 1 41  ? 41.270 -17.790 10.306  1.00 22.19 ?  41  VAL   B HG12 1 
ATOM   4634 H  HG13 . VAL   B 1 41  ? 41.845 -19.199 10.763  1.00 22.19 ?  41  VAL   B HG13 1 
ATOM   4635 H  HG21 . VAL   B 1 41  ? 42.997 -18.331 13.374  1.00 23.25 ?  41  VAL   B HG21 1 
ATOM   4636 H  HG22 . VAL   B 1 41  ? 43.813 -19.252 12.371  1.00 23.25 ?  41  VAL   B HG22 1 
ATOM   4637 H  HG23 . VAL   B 1 41  ? 44.432 -17.876 12.869  1.00 23.25 ?  41  VAL   B HG23 1 
ATOM   4638 N  N    . TYR   B 1 42  ? 46.260 -17.078 10.900  1.00 17.06 ?  42  TYR   B N    1 
ATOM   4639 C  CA   . TYR   B 1 42  ? 47.409 -16.224 11.171  1.00 17.28 ?  42  TYR   B CA   1 
ATOM   4640 C  C    . TYR   B 1 42  ? 48.389 -16.162 10.003  1.00 16.81 ?  42  TYR   B C    1 
ATOM   4641 O  O    . TYR   B 1 42  ? 49.477 -15.587 10.146  1.00 17.81 ?  42  TYR   B O    1 
ATOM   4642 C  CB   . TYR   B 1 42  ? 48.093 -16.622 12.481  1.00 18.54 ?  42  TYR   B CB   1 
ATOM   4643 C  CG   . TYR   B 1 42  ? 47.515 -15.911 13.699  1.00 18.47 ?  42  TYR   B CG   1 
ATOM   4644 C  CD1  . TYR   B 1 42  ? 47.758 -14.559 13.912  1.00 17.51 ?  42  TYR   B CD1  1 
ATOM   4645 C  CD2  . TYR   B 1 42  ? 46.740 -16.589 14.632  1.00 19.29 ?  42  TYR   B CD2  1 
ATOM   4646 C  CE1  . TYR   B 1 42  ? 47.244 -13.906 15.006  1.00 17.77 ?  42  TYR   B CE1  1 
ATOM   4647 C  CE2  . TYR   B 1 42  ? 46.219 -15.937 15.740  1.00 18.89 ?  42  TYR   B CE2  1 
ATOM   4648 C  CZ   . TYR   B 1 42  ? 46.482 -14.592 15.922  1.00 18.80 ?  42  TYR   B CZ   1 
ATOM   4649 O  OH   . TYR   B 1 42  ? 45.989 -13.900 17.013  1.00 21.52 ?  42  TYR   B OH   1 
ATOM   4650 H  H    . TYR   B 1 42  ? 46.413 -17.922 11.000  1.00 20.53 ?  42  TYR   B H    1 
ATOM   4651 H  HA   . TYR   B 1 42  ? 47.076 -15.323 11.297  1.00 20.79 ?  42  TYR   B HA   1 
ATOM   4652 H  HB2  . TYR   B 1 42  ? 47.989 -17.575 12.617  1.00 22.30 ?  42  TYR   B HB2  1 
ATOM   4653 H  HB3  . TYR   B 1 42  ? 49.036 -16.396 12.423  1.00 22.30 ?  42  TYR   B HB3  1 
ATOM   4654 H  HD1  . TYR   B 1 42  ? 48.281 -14.083 13.302  1.00 21.07 ?  42  TYR   B HD1  1 
ATOM   4655 H  HD2  . TYR   B 1 42  ? 46.565 -17.495 14.506  1.00 23.20 ?  42  TYR   B HD2  1 
ATOM   4656 H  HE1  . TYR   B 1 42  ? 47.422 -13.000 15.134  1.00 21.38 ?  42  TYR   B HE1  1 
ATOM   4657 H  HE2  . TYR   B 1 42  ? 45.699 -16.405 16.354  1.00 22.73 ?  42  TYR   B HE2  1 
ATOM   4658 H  HH   . TYR   B 1 42  ? 46.229 -13.097 16.972  1.00 25.87 ?  42  TYR   B HH   1 
ATOM   4659 N  N    . LEU   B 1 43  ? 47.993 -16.667 8.836   1.00 15.72 ?  43  LEU   B N    1 
ATOM   4660 C  CA   . LEU   B 1 43  ? 48.805 -16.604 7.623   1.00 15.45 ?  43  LEU   B CA   1 
ATOM   4661 C  C    . LEU   B 1 43  ? 50.218 -17.113 7.879   1.00 15.61 ?  43  LEU   B C    1 
ATOM   4662 O  O    . LEU   B 1 43  ? 51.200 -16.510 7.442   1.00 16.06 ?  43  LEU   B O    1 
ATOM   4663 C  CB   . LEU   B 1 43  ? 48.829 -15.198 7.021   1.00 15.48 ?  43  LEU   B CB   1 
ATOM   4664 C  CG   . LEU   B 1 43  ? 47.472 -14.586 6.654   1.00 15.35 ?  43  LEU   B CG   1 
ATOM   4665 C  CD1  . LEU   B 1 43  ? 47.677 -13.188 6.066   1.00 16.27 ?  43  LEU   B CD1  1 
ATOM   4666 C  CD2  . LEU   B 1 43  ? 46.709 -15.487 5.694   1.00 15.70 ?  43  LEU   B CD2  1 
ATOM   4667 H  H    . LEU   B 1 43  ? 47.244 -17.069 8.717   1.00 18.92 ?  43  LEU   B H    1 
ATOM   4668 H  HA   . LEU   B 1 43  ? 48.410 -17.188 6.961   1.00 18.60 ?  43  LEU   B HA   1 
ATOM   4669 H  HB2  . LEU   B 1 43  ? 49.254 -14.598 7.656   1.00 18.63 ?  43  LEU   B HB2  1 
ATOM   4670 H  HB3  . LEU   B 1 43  ? 49.359 -15.227 6.207   1.00 18.63 ?  43  LEU   B HB3  1 
ATOM   4671 H  HG   . LEU   B 1 43  ? 46.948 -14.494 7.460   1.00 18.48 ?  43  LEU   B HG   1 
ATOM   4672 H  HD11 . LEU   B 1 43  ? 46.811 -12.812 5.839   1.00 19.58 ?  43  LEU   B HD11 1 
ATOM   4673 H  HD12 . LEU   B 1 43  ? 48.115 -12.627 6.728   1.00 19.58 ?  43  LEU   B HD12 1 
ATOM   4674 H  HD13 . LEU   B 1 43  ? 48.228 -13.251 5.272   1.00 19.58 ?  43  LEU   B HD13 1 
ATOM   4675 H  HD21 . LEU   B 1 43  ? 45.915 -15.020 5.386   1.00 18.90 ?  43  LEU   B HD21 1 
ATOM   4676 H  HD22 . LEU   B 1 43  ? 47.277 -15.707 4.940   1.00 18.90 ?  43  LEU   B HD22 1 
ATOM   4677 H  HD23 . LEU   B 1 43  ? 46.451 -16.300 6.161   1.00 18.90 ?  43  LEU   B HD23 1 
ATOM   4678 N  N    . LYS   B 1 44  ? 50.316 -18.234 8.600   1.00 15.51 ?  44  LYS   B N    1 
ATOM   4679 C  CA   . LYS   B 1 44  ? 51.580 -18.913 8.855   1.00 16.37 ?  44  LYS   B CA   1 
ATOM   4680 C  C    . LYS   B 1 44  ? 51.696 -20.030 7.830   1.00 15.90 ?  44  LYS   B C    1 
ATOM   4681 O  O    . LYS   B 1 44  ? 51.010 -21.048 7.922   1.00 17.62 ?  44  LYS   B O    1 
ATOM   4682 C  CB   . LYS   B 1 44  ? 51.615 -19.418 10.293  1.00 18.32 ?  44  LYS   B CB   1 
ATOM   4683 C  CG   . LYS   B 1 44  ? 51.855 -18.300 11.298  1.00 21.34 ?  44  LYS   B CG   1 
ATOM   4684 C  CD   . LYS   B 1 44  ? 53.039 -17.441 10.833  1.00 24.08 ?  44  LYS   B CD   1 
ATOM   4685 C  CE   . LYS   B 1 44  ? 53.580 -16.531 11.902  1.00 27.33 ?  44  LYS   B CE   1 
ATOM   4686 N  NZ   . LYS   B 1 44  ? 54.748 -15.736 11.437  1.00 28.76 ?  44  LYS   B NZ   1 
ATOM   4687 H  H    . LYS   B 1 44  ? 49.640 -18.616 8.966   1.00 18.67 ?  44  LYS   B H    1 
ATOM   4688 H  HA   . LYS   B 1 44  ? 52.313 -18.311 8.682   1.00 19.70 ?  44  LYS   B HA   1 
ATOM   4689 H  HB2  . LYS   B 1 44  ? 50.755 -19.831 10.504  1.00 22.04 ?  44  LYS   B HB2  1 
ATOM   4690 H  HB3  . LYS   B 1 44  ? 52.322 -20.070 10.385  1.00 22.04 ?  44  LYS   B HB3  1 
ATOM   4691 H  HG2  . LYS   B 1 44  ? 51.067 -17.743 11.364  1.00 25.67 ?  44  LYS   B HG2  1 
ATOM   4692 H  HG3  . LYS   B 1 44  ? 52.074 -18.688 12.164  1.00 25.67 ?  44  LYS   B HG3  1 
ATOM   4693 H  HD2  . LYS   B 1 44  ? 53.752 -18.034 10.524  1.00 28.95 ?  44  LYS   B HD2  1 
ATOM   4694 H  HD3  . LYS   B 1 44  ? 52.742 -16.879 10.099  1.00 28.95 ?  44  LYS   B HD3  1 
ATOM   4695 H  HE2  . LYS   B 1 44  ? 52.884 -15.915 12.163  1.00 32.85 ?  44  LYS   B HE2  1 
ATOM   4696 H  HE3  . LYS   B 1 44  ? 53.864 -17.066 12.653  1.00 32.85 ?  44  LYS   B HE3  1 
ATOM   4697 H  HZ1  . LYS   B 1 44  ? 55.004 -15.173 12.077  1.00 34.57 ?  44  LYS   B HZ1  1 
ATOM   4698 H  HZ2  . LYS   B 1 44  ? 55.427 -16.274 11.235  1.00 34.57 ?  44  LYS   B HZ2  1 
ATOM   4699 H  HZ3  . LYS   B 1 44  ? 54.528 -15.265 10.712  1.00 34.57 ?  44  LYS   B HZ3  1 
ATOM   4700 N  N    . HIS   B 1 45  ? 52.545 -19.810 6.827   1.00 15.83 ?  45  HIS   B N    1 
ATOM   4701 C  CA   . HIS   B 1 45  ? 52.572 -20.645 5.627   1.00 16.11 ?  45  HIS   B CA   1 
ATOM   4702 C  C    . HIS   B 1 45  ? 53.586 -21.773 5.802   1.00 17.94 ?  45  HIS   B C    1 
ATOM   4703 O  O    . HIS   B 1 45  ? 54.648 -21.805 5.187   1.00 20.25 ?  45  HIS   B O    1 
ATOM   4704 C  CB   . HIS   B 1 45  ? 52.890 -19.795 4.408   1.00 16.06 ?  45  HIS   B CB   1 
ATOM   4705 C  CG   . HIS   B 1 45  ? 52.027 -18.588 4.295   1.00 15.36 ?  45  HIS   B CG   1 
ATOM   4706 N  ND1  . HIS   B 1 45  ? 50.649 -18.658 4.276   1.00 15.60 ?  45  HIS   B ND1  1 
ATOM   4707 C  CD2  . HIS   B 1 45  ? 52.349 -17.277 4.207   1.00 15.30 ?  45  HIS   B CD2  1 
ATOM   4708 C  CE1  . HIS   B 1 45  ? 50.165 -17.434 4.168   1.00 15.16 ?  45  HIS   B CE1  1 
ATOM   4709 N  NE2  . HIS   B 1 45  ? 51.173 -16.578 4.131   1.00 15.84 ?  45  HIS   B NE2  1 
ATOM   4710 H  H    . HIS   B 1 45  ? 53.108 -19.157 6.809   1.00 19.06 ?  45  HIS   B H    1 
ATOM   4711 H  HA   . HIS   B 1 45  ? 51.691 -21.036 5.494   1.00 19.38 ?  45  HIS   B HA   1 
ATOM   4712 H  HB2  . HIS   B 1 45  ? 53.810 -19.501 4.458   1.00 19.33 ?  45  HIS   B HB2  1 
ATOM   4713 H  HB3  . HIS   B 1 45  ? 52.756 -20.330 3.606   1.00 19.33 ?  45  HIS   B HB3  1 
ATOM   4714 H  HD2  . HIS   B 1 45  ? 53.209 -16.916 4.197   1.00 18.42 ?  45  HIS   B HD2  1 
ATOM   4715 H  HE1  . HIS   B 1 45  ? 49.263 -17.203 4.132   1.00 18.24 ?  45  HIS   B HE1  1 
ATOM   4716 H  HE2  . HIS   B 1 45  ? 51.104 -15.720 4.064   1.00 19.06 ?  45  HIS   B HE2  1 
ATOM   4717 N  N    . GLY   B 1 46  ? 53.210 -22.723 6.648   1.00 18.83 ?  46  GLY   B N    1 
ATOM   4718 C  CA   . GLY   B 1 46  ? 54.111 -23.788 7.040   1.00 20.91 ?  46  GLY   B CA   1 
ATOM   4719 C  C    . GLY   B 1 46  ? 54.182 -24.997 6.126   1.00 22.95 ?  46  GLY   B C    1 
ATOM   4720 O  O    . GLY   B 1 46  ? 55.275 -25.443 5.773   1.00 26.04 ?  46  GLY   B O    1 
ATOM   4721 H  H    . GLY   B 1 46  ? 52.433 -22.755 7.026   1.00 22.65 ?  46  GLY   B H    1 
ATOM   4722 H  HA2  . GLY   B 1 46  ? 55.003 -23.421 7.118   1.00 25.15 ?  46  GLY   B HA2  1 
ATOM   4723 H  HA3  . GLY   B 1 46  ? 53.844 -24.104 7.919   1.00 25.15 ?  46  GLY   B HA3  1 
ATOM   4724 N  N    . GLY   B 1 47  ? 53.037 -25.555 5.745   1.00 22.10 ?  47  GLY   B N    1 
ATOM   4725 C  CA   . GLY   B 1 47  ? 52.996 -26.850 5.091   1.00 19.59 ?  47  GLY   B CA   1 
ATOM   4726 C  C    . GLY   B 1 47  ? 52.084 -26.841 3.878   1.00 18.06 ?  47  GLY   B C    1 
ATOM   4727 O  O    . GLY   B 1 47  ? 51.437 -25.840 3.578   1.00 17.84 ?  47  GLY   B O    1 
ATOM   4728 H  H    . GLY   B 1 47  ? 52.259 -25.205 5.868   1.00 26.57 ?  47  GLY   B H    1 
ATOM   4729 H  HA2  . GLY   B 1 47  ? 53.887 -27.102 4.805   1.00 23.56 ?  47  GLY   B HA2  1 
ATOM   4730 H  HA3  . GLY   B 1 47  ? 52.674 -27.522 5.718   1.00 23.56 ?  47  GLY   B HA3  1 
ATOM   4731 N  N    . GLY   B 1 48  ? 52.033 -27.989 3.202   1.00 17.34 ?  48  GLY   B N    1 
ATOM   4732 C  CA   . GLY   B 1 48  ? 51.114 -28.138 2.084   1.00 17.11 ?  48  GLY   B CA   1 
ATOM   4733 C  C    . GLY   B 1 48  ? 51.255 -27.019 1.074   1.00 16.43 ?  48  GLY   B C    1 
ATOM   4734 O  O    . GLY   B 1 48  ? 52.358 -26.545 0.787   1.00 16.83 ?  48  GLY   B O    1 
ATOM   4735 H  H    . GLY   B 1 48  ? 52.514 -28.678 3.368   1.00 20.86 ?  48  GLY   B H    1 
ATOM   4736 H  HA2  . GLY   B 1 48  ? 51.283 -28.983 1.639   1.00 20.58 ?  48  GLY   B HA2  1 
ATOM   4737 H  HA3  . GLY   B 1 48  ? 50.202 -28.138 2.410   1.00 20.58 ?  48  GLY   B HA3  1 
ATOM   4738 N  N    . VAL   B 1 49  ? 50.112 -26.575 0.542   1.00 16.36 ?  49  VAL   B N    1 
ATOM   4739 C  CA   . VAL   B 1 49  ? 50.108 -25.550 -0.503  1.00 16.38 ?  49  VAL   B CA   1 
ATOM   4740 C  C    . VAL   B 1 49  ? 50.759 -24.267 -0.009  1.00 15.33 ?  49  VAL   B C    1 
ATOM   4741 O  O    . VAL   B 1 49  ? 51.560 -23.648 -0.719  1.00 16.30 ?  49  VAL   B O    1 
ATOM   4742 C  CB   . VAL   B 1 49  ? 48.670 -25.292 -0.996  1.00 17.28 ?  49  VAL   B CB   1 
ATOM   4743 C  CG1  . VAL   B 1 49  ? 48.595 -24.018 -1.839  1.00 17.21 ?  49  VAL   B CG1  1 
ATOM   4744 C  CG2  . VAL   B 1 49  ? 48.158 -26.485 -1.788  1.00 18.80 ?  49  VAL   B CG2  1 
ATOM   4745 H  H    . VAL   B 1 49  ? 49.326 -26.853 0.762   1.00 19.68 ?  49  VAL   B H    1 
ATOM   4746 H  HA   . VAL   B 1 49  ? 50.620 -25.869 -1.260  1.00 19.71 ?  49  VAL   B HA   1 
ATOM   4747 H  HB   . VAL   B 1 49  ? 48.089 -25.172 -0.230  1.00 20.79 ?  49  VAL   B HB   1 
ATOM   4748 H  HG11 . VAL   B 1 49  ? 47.770 -24.024 -2.348  1.00 20.71 ?  49  VAL   B HG11 1 
ATOM   4749 H  HG12 . VAL   B 1 49  ? 48.611 -23.245 -1.250  1.00 20.71 ?  49  VAL   B HG12 1 
ATOM   4750 H  HG13 . VAL   B 1 49  ? 49.354 -23.991 -2.441  1.00 20.71 ?  49  VAL   B HG13 1 
ATOM   4751 H  HG21 . VAL   B 1 49  ? 47.251 -26.303 -2.083  1.00 22.61 ?  49  VAL   B HG21 1 
ATOM   4752 H  HG22 . VAL   B 1 49  ? 48.734 -26.622 -2.557  1.00 22.61 ?  49  VAL   B HG22 1 
ATOM   4753 H  HG23 . VAL   B 1 49  ? 48.171 -27.267 -1.219  1.00 22.61 ?  49  VAL   B HG23 1 
ATOM   4754 N  N    . ALA   B 1 50  ? 50.407 -23.830 1.202   1.00 15.23 ?  50  ALA   B N    1 
ATOM   4755 C  CA   . ALA   B 1 50  ? 50.927 -22.556 1.691   1.00 14.81 ?  50  ALA   B CA   1 
ATOM   4756 C  C    . ALA   B 1 50  ? 52.443 -22.586 1.800   1.00 15.20 ?  50  ALA   B C    1 
ATOM   4757 O  O    . ALA   B 1 50  ? 53.121 -21.615 1.438   1.00 14.94 ?  50  ALA   B O    1 
ATOM   4758 C  CB   . ALA   B 1 50  ? 50.307 -22.213 3.042   1.00 14.72 ?  50  ALA   B CB   1 
ATOM   4759 H  H    . ALA   B 1 50  ? 49.879 -24.237 1.744   1.00 18.33 ?  50  ALA   B H    1 
ATOM   4760 H  HA   . ALA   B 1 50  ? 50.695 -21.856 1.067   1.00 17.83 ?  50  ALA   B HA   1 
ATOM   4761 H  HB1  . ALA   B 1 50  ? 50.661 -21.363 3.348   1.00 17.72 ?  50  ALA   B HB1  1 
ATOM   4762 H  HB2  . ALA   B 1 50  ? 49.343 -22.149 2.938   1.00 17.72 ?  50  ALA   B HB2  1 
ATOM   4763 H  HB3  . ALA   B 1 50  ? 50.523 -22.911 3.679   1.00 17.72 ?  50  ALA   B HB3  1 
ATOM   4764 N  N    . GLY   B 1 51  ? 52.993 -23.680 2.318   1.00 15.77 ?  51  GLY   B N    1 
ATOM   4765 C  CA   . GLY   B 1 51  ? 54.437 -23.786 2.392   1.00 16.29 ?  51  GLY   B CA   1 
ATOM   4766 C  C    . GLY   B 1 51  ? 55.083 -23.727 1.023   1.00 16.16 ?  51  GLY   B C    1 
ATOM   4767 O  O    . GLY   B 1 51  ? 56.126 -23.093 0.842   1.00 16.67 ?  51  GLY   B O    1 
ATOM   4768 H  H    . GLY   B 1 51  ? 52.561 -24.364 2.623   1.00 18.98 ?  51  GLY   B H    1 
ATOM   4769 H  HA2  . GLY   B 1 51  ? 54.788 -23.060 2.927   1.00 19.60 ?  51  GLY   B HA2  1 
ATOM   4770 H  HA3  . GLY   B 1 51  ? 54.680 -24.628 2.818   1.00 19.60 ?  51  GLY   B HA3  1 
ATOM   4771 N  N    . ALA   B 1 52  ? 54.476 -24.388 0.039   1.00 15.50 ?  52  ALA   B N    1 
ATOM   4772 C  CA   . ALA   B 1 52  ? 55.041 -24.394 -1.304  1.00 15.99 ?  52  ALA   B CA   1 
ATOM   4773 C  C    . ALA   B 1 52  ? 54.967 -23.015 -1.951  1.00 15.32 ?  52  ALA   B C    1 
ATOM   4774 O  O    . ALA   B 1 52  ? 55.944 -22.557 -2.562  1.00 16.28 ?  52  ALA   B O    1 
ATOM   4775 C  CB   . ALA   B 1 52  ? 54.341 -25.436 -2.168  1.00 16.46 ?  52  ALA   B CB   1 
ATOM   4776 H  H    . ALA   B 1 52  ? 53.733 -24.820 0.120   1.00 18.65 ?  52  ALA   B H    1 
ATOM   4777 H  HA   . ALA   B 1 52  ? 55.974 -24.643 -1.241  1.00 19.24 ?  52  ALA   B HA   1 
ATOM   4778 H  HB1  . ALA   B 1 52  ? 54.737 -25.423 -3.054  1.00 19.80 ?  52  ALA   B HB1  1 
ATOM   4779 H  HB2  . ALA   B 1 52  ? 54.458 -26.310 -1.766  1.00 19.80 ?  52  ALA   B HB2  1 
ATOM   4780 H  HB3  . ALA   B 1 52  ? 53.398 -25.218 -2.223  1.00 19.80 ?  52  ALA   B HB3  1 
ATOM   4781 N  N    . LEU   B 1 53  ? 53.825 -22.334 -1.833  1.00 14.89 ?  53  LEU   B N    1 
ATOM   4782 C  CA   . LEU   B 1 53  ? 53.719 -20.991 -2.402  1.00 15.30 ?  53  LEU   B CA   1 
ATOM   4783 C  C    . LEU   B 1 53  ? 54.727 -20.052 -1.750  1.00 14.86 ?  53  LEU   B C    1 
ATOM   4784 O  O    . LEU   B 1 53  ? 55.440 -19.306 -2.434  1.00 15.56 ?  53  LEU   B O    1 
ATOM   4785 C  CB   . LEU   B 1 53  ? 52.297 -20.452 -2.234  1.00 15.63 ?  53  LEU   B CB   1 
ATOM   4786 C  CG   . LEU   B 1 53  ? 51.156 -21.174 -2.958  1.00 15.83 ?  53  LEU   B CG   1 
ATOM   4787 C  CD1  . LEU   B 1 53  ? 49.827 -20.546 -2.611  1.00 17.03 ?  53  LEU   B CD1  1 
ATOM   4788 C  CD2  . LEU   B 1 53  ? 51.364 -21.174 -4.465  1.00 17.84 ?  53  LEU   B CD2  1 
ATOM   4789 H  H    . LEU   B 1 53  ? 53.114 -22.620 -1.438  1.00 17.92 ?  53  LEU   B H    1 
ATOM   4790 H  HA   . LEU   B 1 53  ? 53.917 -21.037 -3.353  1.00 18.41 ?  53  LEU   B HA   1 
ATOM   4791 H  HB2  . LEU   B 1 53  ? 52.084 -20.471 -1.290  1.00 18.81 ?  53  LEU   B HB2  1 
ATOM   4792 H  HB3  . LEU   B 1 53  ? 52.291 -19.537 -2.546  1.00 18.81 ?  53  LEU   B HB3  1 
ATOM   4793 H  HG   . LEU   B 1 53  ? 51.124 -22.094 -2.662  1.00 19.05 ?  53  LEU   B HG   1 
ATOM   4794 H  HD11 . LEU   B 1 53  ? 49.121 -21.019 -3.079  1.00 20.49 ?  53  LEU   B HD11 1 
ATOM   4795 H  HD12 . LEU   B 1 53  ? 49.688 -20.611 -1.652  1.00 20.49 ?  53  LEU   B HD12 1 
ATOM   4796 H  HD13 . LEU   B 1 53  ? 49.836 -19.615 -2.880  1.00 20.49 ?  53  LEU   B HD13 1 
ATOM   4797 H  HD21 . LEU   B 1 53  ? 50.629 -21.643 -4.889  1.00 21.47 ?  53  LEU   B HD21 1 
ATOM   4798 H  HD22 . LEU   B 1 53  ? 51.395 -20.257 -4.782  1.00 21.47 ?  53  LEU   B HD22 1 
ATOM   4799 H  HD23 . LEU   B 1 53  ? 52.201 -21.621 -4.667  1.00 21.47 ?  53  LEU   B HD23 1 
ATOM   4800 N  N    . ASN   B 1 54  ? 54.811 -20.085 -0.421  1.00 14.38 ?  54  ASN   B N    1 
ATOM   4801 C  CA   . ASN   B 1 54  ? 55.732 -19.181 0.253   1.00 15.16 ?  54  ASN   B CA   1 
ATOM   4802 C  C    . ASN   B 1 54  ? 57.174 -19.465 -0.148  1.00 16.37 ?  54  ASN   B C    1 
ATOM   4803 O  O    . ASN   B 1 54  ? 57.955 -18.533 -0.383  1.00 16.58 ?  54  ASN   B O    1 
ATOM   4804 C  CB   . ASN   B 1 54  ? 55.569 -19.255 1.766   1.00 15.86 ?  54  ASN   B CB   1 
ATOM   4805 C  CG   . ASN   B 1 54  ? 56.544 -18.343 2.482   1.00 16.64 ?  54  ASN   B CG   1 
ATOM   4806 O  OD1  . ASN   B 1 54  ? 56.568 -17.133 2.250   1.00 16.66 ?  54  ASN   B OD1  1 
ATOM   4807 N  ND2  . ASN   B 1 54  ? 57.371 -18.925 3.340   1.00 17.80 ?  54  ASN   B ND2  1 
ATOM   4808 H  H    . ASN   B 1 54  ? 54.360 -20.608 0.091   1.00 17.31 ?  54  ASN   B H    1 
ATOM   4809 H  HA   . ASN   B 1 54  ? 55.524 -18.276 -0.019  1.00 18.25 ?  54  ASN   B HA   1 
ATOM   4810 H  HB2  . ASN   B 1 54  ? 54.663 -18.980 2.004   1.00 19.09 ?  54  ASN   B HB2  1 
ATOM   4811 H  HB3  . ASN   B 1 54  ? 55.722 -20.166 2.063   1.00 19.09 ?  54  ASN   B HB3  1 
ATOM   4812 H  HD21 . ASN   B 1 54  ? 57.952 -18.453 3.770   1.00 21.42 ?  54  ASN   B HD21 1 
ATOM   4813 H  HD22 . ASN   B 1 54  ? 57.341 -19.778 3.468   1.00 21.42 ?  54  ASN   B HD22 1 
ATOM   4814 N  N    . LYS   B 1 55  ? 57.553 -20.744 -0.214  1.00 16.84 ?  55  LYS   B N    1 
ATOM   4815 C  CA   . LYS   B 1 55  ? 58.909 -21.086 -0.625  1.00 17.57 ?  55  LYS   B CA   1 
ATOM   4816 C  C    . LYS   B 1 55  ? 59.208 -20.549 -2.020  1.00 17.14 ?  55  LYS   B C    1 
ATOM   4817 O  O    . LYS   B 1 55  ? 60.307 -20.040 -2.274  1.00 17.89 ?  55  LYS   B O    1 
ATOM   4818 C  CB   . LYS   B 1 55  ? 59.099 -22.601 -0.567  1.00 19.50 ?  55  LYS   B CB   1 
ATOM   4819 C  CG   . LYS   B 1 55  ? 60.479 -23.068 -1.011  1.00 22.96 ?  55  LYS   B CG   1 
ATOM   4820 C  CD   . LYS   B 1 55  ? 60.645 -24.576 -0.876  1.00 26.26 ?  55  LYS   B CD   1 
ATOM   4821 C  CE   . LYS   B 1 55  ? 60.701 -25.017 0.585   1.00 28.22 ?  55  LYS   B CE   1 
ATOM   4822 N  NZ   . LYS   B 1 55  ? 61.026 -26.459 0.723   1.00 29.52 ?  55  LYS   B NZ   1 
ATOM   4823 H  H    . LYS   B 1 55  ? 57.048 -21.416 -0.032  1.00 20.26 ?  55  LYS   B H    1 
ATOM   4824 H  HA   . LYS   B 1 55  ? 59.539 -20.684 -0.010  1.00 21.13 ?  55  LYS   B HA   1 
ATOM   4825 H  HB2  . LYS   B 1 55  ? 58.967 -22.895 0.350   1.00 23.45 ?  55  LYS   B HB2  1 
ATOM   4826 H  HB3  . LYS   B 1 55  ? 58.445 -23.024 -1.143  1.00 23.45 ?  55  LYS   B HB3  1 
ATOM   4827 H  HG2  . LYS   B 1 55  ? 60.613 -22.834 -1.942  1.00 27.60 ?  55  LYS   B HG2  1 
ATOM   4828 H  HG3  . LYS   B 1 55  ? 61.153 -22.639 -0.459  1.00 27.60 ?  55  LYS   B HG3  1 
ATOM   4829 H  HD2  . LYS   B 1 55  ? 59.892 -25.021 -1.296  1.00 31.56 ?  55  LYS   B HD2  1 
ATOM   4830 H  HD3  . LYS   B 1 55  ? 61.474 -24.848 -1.304  1.00 31.56 ?  55  LYS   B HD3  1 
ATOM   4831 H  HE2  . LYS   B 1 55  ? 61.388 -24.503 1.042   1.00 33.92 ?  55  LYS   B HE2  1 
ATOM   4832 H  HE3  . LYS   B 1 55  ? 59.837 -24.857 0.997   1.00 33.92 ?  55  LYS   B HE3  1 
ATOM   4833 H  HZ1  . LYS   B 1 55  ? 61.047 -26.681 1.585   1.00 35.48 ?  55  LYS   B HZ1  1 
ATOM   4834 H  HZ2  . LYS   B 1 55  ? 60.406 -26.948 0.313   1.00 35.48 ?  55  LYS   B HZ2  1 
ATOM   4835 H  HZ3  . LYS   B 1 55  ? 61.818 -26.628 0.360   1.00 35.48 ?  55  LYS   B HZ3  1 
ATOM   4836 N  N    . ALA   B 1 56  ? 58.235 -20.631 -2.933  1.00 16.96 ?  56  ALA   B N    1 
ATOM   4837 C  CA   . ALA   B 1 56  ? 58.453 -20.122 -4.282  1.00 17.72 ?  56  ALA   B CA   1 
ATOM   4838 C  C    . ALA   B 1 56  ? 58.738 -18.627 -4.273  1.00 17.38 ?  56  ALA   B C    1 
ATOM   4839 O  O    . ALA   B 1 56  ? 59.489 -18.134 -5.124  1.00 18.09 ?  56  ALA   B O    1 
ATOM   4840 C  CB   . ALA   B 1 56  ? 57.247 -20.433 -5.171  1.00 18.41 ?  56  ALA   B CB   1 
ATOM   4841 H  H    . ALA   B 1 56  ? 57.452 -20.965 -2.799  1.00 20.41 ?  56  ALA   B H    1 
ATOM   4842 H  HA   . ALA   B 1 56  ? 59.223 -20.561 -4.665  1.00 21.32 ?  56  ALA   B HA   1 
ATOM   4843 H  HB1  . ALA   B 1 56  ? 57.416 -20.089 -6.064  1.00 22.15 ?  56  ALA   B HB1  1 
ATOM   4844 H  HB2  . ALA   B 1 56  ? 57.126 -21.396 -5.207  1.00 22.15 ?  56  ALA   B HB2  1 
ATOM   4845 H  HB3  . ALA   B 1 56  ? 56.459 -20.013 -4.798  1.00 22.15 ?  56  ALA   B HB3  1 
ATOM   4846 N  N    . THR   B 1 57  ? 58.156 -17.891 -3.326  1.00 17.13 ?  57  THR   B N    1 
ATOM   4847 C  CA   . THR   B 1 57  ? 58.406 -16.457 -3.218  1.00 17.25 ?  57  THR   B CA   1 
ATOM   4848 C  C    . THR   B 1 57  ? 59.653 -16.129 -2.403  1.00 17.93 ?  57  THR   B C    1 
ATOM   4849 O  O    . THR   B 1 57  ? 59.890 -14.953 -2.106  1.00 18.44 ?  57  THR   B O    1 
ATOM   4850 C  CB   . THR   B 1 57  ? 57.208 -15.719 -2.603  1.00 16.49 ?  57  THR   B CB   1 
ATOM   4851 O  OG1  . THR   B 1 57  ? 57.178 -15.932 -1.183  1.00 17.29 ?  57  THR   B OG1  1 
ATOM   4852 C  CG2  . THR   B 1 57  ? 55.894 -16.141 -3.252  1.00 16.18 ?  57  THR   B CG2  1 
ATOM   4853 H  H    . THR   B 1 57  ? 57.601 -18.199 -2.738  1.00 20.61 ?  57  THR   B H    1 
ATOM   4854 H  HA   . THR   B 1 57  ? 58.533 -16.103 -4.111  1.00 20.76 ?  57  THR   B HA   1 
ATOM   4855 H  HB   . THR   B 1 57  ? 57.321 -14.765 -2.771  1.00 19.85 ?  57  THR   B HB   1 
ATOM   4856 H  HG1  . THR   B 1 57  ? 57.097 -16.748 -1.022  1.00 20.81 ?  57  THR   B HG1  1 
ATOM   4857 H  HG21 . THR   B 1 57  ? 55.171 -15.577 -2.941  1.00 19.47 ?  57  THR   B HG21 1 
ATOM   4858 H  HG22 . THR   B 1 57  ? 55.960 -16.065 -4.219  1.00 19.47 ?  57  THR   B HG22 1 
ATOM   4859 H  HG23 . THR   B 1 57  ? 55.695 -17.063 -3.026  1.00 19.47 ?  57  THR   B HG23 1 
ATOM   4860 N  N    . ASN   B 1 58  ? 60.444 -17.131 -2.031  1.00 18.60 ?  58  ASN   B N    1 
ATOM   4861 C  CA   . ASN   B 1 58  ? 61.638 -16.911 -1.217  1.00 20.79 ?  58  ASN   B CA   1 
ATOM   4862 C  C    . ASN   B 1 58  ? 61.295 -16.191 0.087   1.00 19.15 ?  58  ASN   B C    1 
ATOM   4863 O  O    . ASN   B 1 58  ? 62.028 -15.307 0.542   1.00 19.77 ?  58  ASN   B O    1 
ATOM   4864 C  CB   . ASN   B 1 58  ? 62.733 -16.172 -1.993  1.00 26.47 ?  58  ASN   B CB   1 
ATOM   4865 C  CG   . ASN   B 1 58  ? 64.110 -16.370 -1.387  1.00 35.76 ?  58  ASN   B CG   1 
ATOM   4866 O  OD1  . ASN   B 1 58  ? 64.395 -17.408 -0.789  1.00 39.02 ?  58  ASN   B OD1  1 
ATOM   4867 N  ND2  . ASN   B 1 58  ? 64.971 -15.373 -1.539  1.00 41.44 ?  58  ASN   B ND2  1 
ATOM   4868 H  H    . ASN   B 1 58  ? 60.314 -17.956 -2.239  1.00 22.38 ?  58  ASN   B H    1 
ATOM   4869 H  HA   . ASN   B 1 58  ? 61.999 -17.780 -0.982  1.00 25.00 ?  58  ASN   B HA   1 
ATOM   4870 H  HB2  . ASN   B 1 58  ? 62.757 -16.502 -2.907  1.00 31.82 ?  58  ASN   B HB2  1 
ATOM   4871 H  HB3  . ASN   B 1 58  ? 62.541 -15.222 -1.990  1.00 31.82 ?  58  ASN   B HB3  1 
ATOM   4872 H  HD21 . ASN   B 1 58  ? 65.765 -15.440 -1.214  1.00 49.78 ?  58  ASN   B HD21 1 
ATOM   4873 H  HD22 . ASN   B 1 58  ? 64.736 -14.663 -1.961  1.00 49.78 ?  58  ASN   B HD22 1 
ATOM   4874 N  N    . ASN   B 1 59  ? 60.172 -16.580 0.696   1.00 18.45 ?  59  ASN   B N    1 
ATOM   4875 C  CA   . ASN   B 1 59  ? 59.696 -16.110 1.997   1.00 18.19 ?  59  ASN   B CA   1 
ATOM   4876 C  C    . ASN   B 1 59  ? 59.103 -14.705 1.932   1.00 17.46 ?  59  ASN   B C    1 
ATOM   4877 O  O    . ASN   B 1 59  ? 58.676 -14.190 2.974   1.00 17.53 ?  59  ASN   B O    1 
ATOM   4878 C  CB   . ASN   B 1 59  ? 60.770 -16.160 3.098   1.00 19.09 ?  59  ASN   B CB   1 
ATOM   4879 C  CG   . ASN   B 1 59  ? 60.185 -16.341 4.480   1.00 20.17 ?  59  ASN   B CG   1 
ATOM   4880 O  OD1  . ASN   B 1 59  ? 59.360 -17.232 4.710   1.00 20.71 ?  59  ASN   B OD1  1 
ATOM   4881 N  ND2  . ASN   B 1 59  ? 60.598 -15.490 5.410   1.00 21.12 ?  59  ASN   B ND2  1 
ATOM   4882 H  H    . ASN   B 1 59  ? 59.637 -17.165 0.352   1.00 22.20 ?  59  ASN   B H    1 
ATOM   4883 H  HA   . ASN   B 1 59  ? 58.985 -16.706 2.278   1.00 21.88 ?  59  ASN   B HA   1 
ATOM   4884 H  HB2  . ASN   B 1 59  ? 61.364 -16.908 2.936   1.00 22.97 ?  59  ASN   B HB2  1 
ATOM   4885 H  HB3  . ASN   B 1 59  ? 61.268 -15.331 3.098   1.00 22.97 ?  59  ASN   B HB3  1 
ATOM   4886 H  HD21 . ASN   B 1 59  ? 60.288 -15.544 6.211   1.00 25.40 ?  59  ASN   B HD21 1 
ATOM   4887 H  HD22 . ASN   B 1 59  ? 61.165 -14.877 5.209   1.00 25.40 ?  59  ASN   B HD22 1 
ATOM   4888 N  N    . ALA   B 1 60  ? 59.048 -14.069 0.757   1.00 16.90 ?  60  ALA   B N    1 
ATOM   4889 C  CA   . ALA   B 1 60  ? 58.450 -12.737 0.665   1.00 17.24 ?  60  ALA   B CA   1 
ATOM   4890 C  C    . ALA   B 1 60  ? 56.980 -12.764 1.068   1.00 16.49 ?  60  ALA   B C    1 
ATOM   4891 O  O    . ALA   B 1 60  ? 56.469 -11.811 1.669   1.00 17.03 ?  60  ALA   B O    1 
ATOM   4892 C  CB   . ALA   B 1 60  ? 58.602 -12.189 -0.753  1.00 18.07 ?  60  ALA   B CB   1 
ATOM   4893 H  H    . ALA   B 1 60  ? 59.353 -14.380 0.014   1.00 20.34 ?  60  ALA   B H    1 
ATOM   4894 H  HA   . ALA   B 1 60  ? 58.915 -12.137 1.263   1.00 20.75 ?  60  ALA   B HA   1 
ATOM   4895 H  HB1  . ALA   B 1 60  ? 58.200 -11.308 -0.797  1.00 21.74 ?  60  ALA   B HB1  1 
ATOM   4896 H  HB2  . ALA   B 1 60  ? 59.548 -12.131 -0.971  1.00 21.74 ?  60  ALA   B HB2  1 
ATOM   4897 H  HB3  . ALA   B 1 60  ? 58.159 -12.787 -1.375  1.00 21.74 ?  60  ALA   B HB3  1 
ATOM   4898 N  N    . MET   B 1 61  ? 56.278 -13.840 0.722   1.00 15.67 ?  61  MET   B N    1 
ATOM   4899 C  CA   . MET   B 1 61  ? 54.883 -13.967 1.114   1.00 15.12 ?  61  MET   B CA   1 
ATOM   4900 C  C    . MET   B 1 61  ? 54.739 -13.976 2.632   1.00 15.31 ?  61  MET   B C    1 
ATOM   4901 O  O    . MET   B 1 61  ? 53.831 -13.331 3.179   1.00 15.30 ?  61  MET   B O    1 
ATOM   4902 C  CB   . MET   B 1 61  ? 54.306 -15.236 0.488   1.00 15.67 ?  61  MET   B CB   1 
ATOM   4903 C  CG   . MET   B 1 61  ? 52.860 -15.534 0.900   1.00 15.49 ?  61  MET   B CG   1 
ATOM   4904 S  SD   . MET   B 1 61  ? 52.216 -17.025 0.137   1.00 15.13 ?  61  MET   B SD   1 
ATOM   4905 C  CE   . MET   B 1 61  ? 51.994 -16.466 -1.543  1.00 17.34 ?  61  MET   B CE   1 
ATOM   4906 H  H    . MET   B 1 61  ? 56.583 -14.505 0.256   1.00 18.86 ?  61  MET   B H    1 
ATOM   4907 H  HA   . MET   B 1 61  ? 54.388 -13.219 0.760   1.00 18.19 ?  61  MET   B HA   1 
ATOM   4908 H  HB2  . MET   B 1 61  ? 54.325 -15.144 -0.481  1.00 18.86 ?  61  MET   B HB2  1 
ATOM   4909 H  HB3  . MET   B 1 61  ? 54.852 -15.996 0.749   1.00 18.86 ?  61  MET   B HB3  1 
ATOM   4910 H  HG2  . MET   B 1 61  ? 52.824 -15.654 1.860   1.00 18.64 ?  61  MET   B HG2  1 
ATOM   4911 H  HG3  . MET   B 1 61  ? 52.299 -14.792 0.633   1.00 18.64 ?  61  MET   B HG3  1 
ATOM   4912 H  HE1  . MET   B 1 61  ? 51.606 -17.179 -2.068  1.00 20.86 ?  61  MET   B HE1  1 
ATOM   4913 H  HE2  . MET   B 1 61  ? 51.407 -15.692 -1.545  1.00 20.86 ?  61  MET   B HE2  1 
ATOM   4914 H  HE3  . MET   B 1 61  ? 52.861 -16.218 -1.910  1.00 20.86 ?  61  MET   B HE3  1 
ATOM   4915 N  N    . GLN   B 1 62  ? 55.619 -14.694 3.335   1.00 15.69 ?  62  GLN   B N    1 
ATOM   4916 C  CA   . GLN   B 1 62  ? 55.514 -14.747 4.790   1.00 16.01 ?  62  GLN   B CA   1 
ATOM   4917 C  C    . GLN   B 1 62  ? 55.797 -13.390 5.423   1.00 16.30 ?  62  GLN   B C    1 
ATOM   4918 O  O    . GLN   B 1 62  ? 55.117 -12.990 6.373   1.00 16.40 ?  62  GLN   B O    1 
ATOM   4919 C  CB   . GLN   B 1 62  ? 56.466 -15.797 5.358   1.00 16.34 ?  62  GLN   B CB   1 
ATOM   4920 C  CG   . GLN   B 1 62  ? 56.226 -16.067 6.829   1.00 17.42 ?  62  GLN   B CG   1 
ATOM   4921 C  CD   . GLN   B 1 62  ? 54.846 -16.670 7.069   1.00 16.64 ?  62  GLN   B CD   1 
ATOM   4922 O  OE1  . GLN   B 1 62  ? 54.585 -17.816 6.705   1.00 16.55 ?  62  GLN   B OE1  1 
ATOM   4923 N  NE2  . GLN   B 1 62  ? 53.944 -15.885 7.646   1.00 16.58 ?  62  GLN   B NE2  1 
ATOM   4924 H  H    . GLN   B 1 62  ? 56.275 -15.152 3.002   1.00 18.88 ?  62  GLN   B H    1 
ATOM   4925 H  HA   . GLN   B 1 62  ? 54.613 -15.007 5.026   1.00 19.27 ?  62  GLN   B HA   1 
ATOM   4926 H  HB2  . GLN   B 1 62  ? 56.347 -16.636 4.877   1.00 19.66 ?  62  GLN   B HB2  1 
ATOM   4927 H  HB3  . GLN   B 1 62  ? 57.383 -15.491 5.257   1.00 19.66 ?  62  GLN   B HB3  1 
ATOM   4928 H  HG2  . GLN   B 1 62  ? 56.893 -16.700 7.150   1.00 20.96 ?  62  GLN   B HG2  1 
ATOM   4929 H  HG3  . GLN   B 1 62  ? 56.285 -15.241 7.324   1.00 20.96 ?  62  GLN   B HG3  1 
ATOM   4930 H  HE21 . GLN   B 1 62  ? 54.161 -15.091 7.882   1.00 19.95 ?  62  GLN   B HE21 1 
ATOM   4931 H  HE22 . GLN   B 1 62  ? 53.155 -16.186 7.798   1.00 19.95 ?  62  GLN   B HE22 1 
ATOM   4932 N  N    . VAL   B 1 63  ? 56.813 -12.678 4.934   1.00 16.64 ?  63  VAL   B N    1 
ATOM   4933 C  CA   . VAL   B 1 63  ? 57.115 -11.359 5.486   1.00 17.06 ?  63  VAL   B CA   1 
ATOM   4934 C  C    . VAL   B 1 63  ? 55.921 -10.430 5.300   1.00 16.48 ?  63  VAL   B C    1 
ATOM   4935 O  O    . VAL   B 1 63  ? 55.505 -9.722  6.227   1.00 17.11 ?  63  VAL   B O    1 
ATOM   4936 C  CB   . VAL   B 1 63  ? 58.411 -10.801 4.868   1.00 18.24 ?  63  VAL   B CB   1 
ATOM   4937 C  CG1  . VAL   B 1 63  ? 58.638 -9.355  5.302   1.00 18.75 ?  63  VAL   B CG1  1 
ATOM   4938 C  CG2  . VAL   B 1 63  ? 59.589 -11.673 5.270   1.00 18.69 ?  63  VAL   B CG2  1 
ATOM   4939 H  H    . VAL   B 1 63  ? 57.329 -12.931 4.291   1.00 20.02 ?  63  VAL   B H    1 
ATOM   4940 H  HA   . VAL   B 1 63  ? 57.268 -11.453 6.437   1.00 20.52 ?  63  VAL   B HA   1 
ATOM   4941 H  HB   . VAL   B 1 63  ? 58.341 -10.823 3.899   1.00 21.95 ?  63  VAL   B HB   1 
ATOM   4942 H  HG11 . VAL   B 1 63  ? 59.553 -9.108  5.098   1.00 22.56 ?  63  VAL   B HG11 1 
ATOM   4943 H  HG12 . VAL   B 1 63  ? 58.024 -8.783  4.820   1.00 22.56 ?  63  VAL   B HG12 1 
ATOM   4944 H  HG13 . VAL   B 1 63  ? 58.482 -9.289  6.256   1.00 22.56 ?  63  VAL   B HG13 1 
ATOM   4945 H  HG21 . VAL   B 1 63  ? 60.405 -11.301 4.897   1.00 22.49 ?  63  VAL   B HG21 1 
ATOM   4946 H  HG22 . VAL   B 1 63  ? 59.652 -11.693 6.240   1.00 22.49 ?  63  VAL   B HG22 1 
ATOM   4947 H  HG23 . VAL   B 1 63  ? 59.453 -12.573 4.932   1.00 22.49 ?  63  VAL   B HG23 1 
ATOM   4948 N  N    . GLU   B 1 64  ? 55.360 -10.420 4.092   1.00 16.27 ?  64  GLU   B N    1 
ATOM   4949 C  CA   . GLU   B 1 64  ? 54.191 -9.591  3.811   1.00 15.66 ?  64  GLU   B CA   1 
ATOM   4950 C  C    . GLU   B 1 64  ? 53.008 -9.986  4.689   1.00 15.21 ?  64  GLU   B C    1 
ATOM   4951 O  O    . GLU   B 1 64  ? 52.256 -9.120  5.173   1.00 15.69 ?  64  GLU   B O    1 
ATOM   4952 C  CB   . GLU   B 1 64  ? 53.841 -9.737  2.331   1.00 15.88 ?  64  GLU   B CB   1 
ATOM   4953 C  CG   . GLU   B 1 64  ? 52.576 -9.001  1.902   1.00 16.62 ?  64  GLU   B CG   1 
ATOM   4954 C  CD   . GLU   B 1 64  ? 52.029 -9.496  0.573   1.00 17.19 ?  64  GLU   B CD   1 
ATOM   4955 O  OE1  . GLU   B 1 64  ? 52.215 -10.705 0.264   1.00 17.83 ?  64  GLU   B OE1  1 
ATOM   4956 O  OE2  . GLU   B 1 64  ? 51.393 -8.683  -0.145  1.00 17.82 -1 64  GLU   B OE2  1 
ATOM   4957 H  H    . GLU   B 1 64  ? 55.638 -10.885 3.418   1.00 19.58 ?  64  GLU   B H    1 
ATOM   4958 H  HA   . GLU   B 1 64  ? 54.402 -8.665  3.983   1.00 18.84 ?  64  GLU   B HA   1 
ATOM   4959 H  HB2  . GLU   B 1 64  ? 54.573 -9.381  1.797   1.00 19.11 ?  64  GLU   B HB2  1 
ATOM   4960 H  HB3  . GLU   B 1 64  ? 53.719 -10.676 2.126   1.00 19.11 ?  64  GLU   B HB3  1 
ATOM   4961 H  HG2  . GLU   B 1 64  ? 51.879 -9.128  2.570   1.00 20.00 ?  64  GLU   B HG2  1 
ATOM   4962 H  HG3  . GLU   B 1 64  ? 52.773 -8.057  1.812   1.00 20.00 ?  64  GLU   B HG3  1 
ATOM   4963 N  N    . SER   B 1 65  ? 52.830 -11.294 4.894   1.00 14.90 ?  65  SER   B N    1 
ATOM   4964 C  CA   . SER   B 1 65  ? 51.713 -11.795 5.685   1.00 14.89 ?  65  SER   B CA   1 
ATOM   4965 C  C    . SER   B 1 65  ? 51.837 -11.397 7.150   1.00 15.41 ?  65  SER   B C    1 
ATOM   4966 O  O    . SER   B 1 65  ? 50.835 -11.027 7.778   1.00 15.33 ?  65  SER   B O    1 
ATOM   4967 C  CB   . SER   B 1 65  ? 51.611 -13.319 5.550   1.00 15.66 ?  65  SER   B CB   1 
ATOM   4968 O  OG   . SER   B 1 65  ? 51.284 -13.710 4.228   1.00 15.59 ?  65  SER   B OG   1 
ATOM   4969 H  H    . SER   B 1 65  ? 53.349 -11.914 4.590   1.00 17.94 ?  65  SER   B H    1 
ATOM   4970 H  HA   . SER   B 1 65  ? 50.891 -11.416 5.342   1.00 17.92 ?  65  SER   B HA   1 
ATOM   4971 H  HB2  . SER   B 1 65  ? 52.459 -13.717 5.787   1.00 18.85 ?  65  SER   B HB2  1 
ATOM   4972 H  HB3  . SER   B 1 65  ? 50.916 -13.639 6.152   1.00 18.85 ?  65  SER   B HB3  1 
ATOM   4973 H  HG   . SER   B 1 65  ? 51.866 -13.427 3.690   1.00 18.77 ?  65  SER   B HG   1 
ATOM   4974 N  N    . ASP   B 1 66  ? 53.043 -11.490 7.722   1.00 15.62 ?  66  ASP   B N    1 
ATOM   4975 C  CA   . ASP   B 1 66  ? 53.229 -11.099 9.115   1.00 15.79 ?  66  ASP   B CA   1 
ATOM   4976 C  C    . ASP   B 1 66  ? 52.924 -9.619  9.314   1.00 16.82 ?  66  ASP   B C    1 
ATOM   4977 O  O    . ASP   B 1 66  ? 52.337 -9.227  10.331  1.00 16.86 ?  66  ASP   B O    1 
ATOM   4978 C  CB   . ASP   B 1 66  ? 54.658 -11.413 9.560   1.00 17.64 ?  66  ASP   B CB   1 
ATOM   4979 C  CG   . ASP   B 1 66  ? 54.909 -12.911 9.734   1.00 19.05 ?  66  ASP   B CG   1 
ATOM   4980 O  OD1  . ASP   B 1 66  ? 53.941 -13.708 9.637   1.00 20.13 ?  66  ASP   B OD1  1 
ATOM   4981 O  OD2  . ASP   B 1 66  ? 56.080 -13.294 9.975   1.00 21.38 -1 66  ASP   B OD2  1 
ATOM   4982 H  H    . ASP   B 1 66  ? 53.745 -11.799 7.334   1.00 18.80 ?  66  ASP   B H    1 
ATOM   4983 H  HA   . ASP   B 1 66  ? 52.625 -11.605 9.677   1.00 19.00 ?  66  ASP   B HA   1 
ATOM   4984 H  HB2  . ASP   B 1 66  ? 55.280 -11.074 8.895   1.00 21.22 ?  66  ASP   B HB2  1 
ATOM   4985 H  HB3  . ASP   B 1 66  ? 54.824 -10.982 10.416  1.00 21.22 ?  66  ASP   B HB3  1 
ATOM   4986 N  N    . ASP   B 1 67  ? 53.311 -8.778  8.354   1.00 16.27 ?  67  ASP   B N    1 
ATOM   4987 C  CA   . ASP   B 1 67  ? 52.963 -7.366  8.429   1.00 16.50 ?  67  ASP   B CA   1 
ATOM   4988 C  C    . ASP   B 1 67  ? 51.453 -7.160  8.337   1.00 16.48 ?  67  ASP   B C    1 
ATOM   4989 O  O    . ASP   B 1 67  ? 50.882 -6.349  9.078   1.00 16.93 ?  67  ASP   B O    1 
ATOM   4990 C  CB   . ASP   B 1 67  ? 53.682 -6.609  7.319   1.00 17.48 ?  67  ASP   B CB   1 
ATOM   4991 C  CG   . ASP   B 1 67  ? 53.256 -5.166  7.251   1.00 19.28 ?  67  ASP   B CG   1 
ATOM   4992 O  OD1  . ASP   B 1 67  ? 53.783 -4.336  8.029   1.00 20.67 ?  67  ASP   B OD1  1 
ATOM   4993 O  OD2  . ASP   B 1 67  ? 52.370 -4.872  6.435   1.00 20.55 -1 67  ASP   B OD2  1 
ATOM   4994 H  H    . ASP   B 1 67  ? 53.764 -9.001  7.659   1.00 19.58 ?  67  ASP   B H    1 
ATOM   4995 H  HA   . ASP   B 1 67  ? 53.263 -7.009  9.279   1.00 19.85 ?  67  ASP   B HA   1 
ATOM   4996 H  HB2  . ASP   B 1 67  ? 54.641 -6.642  7.484   1.00 21.03 ?  67  ASP   B HB2  1 
ATOM   4997 H  HB3  . ASP   B 1 67  ? 53.484 -7.034  6.466   1.00 21.03 ?  67  ASP   B HB3  1 
ATOM   4998 N  N    . TYR   B 1 68  ? 50.784 -7.894  7.442   1.00 16.45 ?  68  TYR   B N    1 
ATOM   4999 C  CA   . TYR   B 1 68  ? 49.330 -7.809  7.363   1.00 17.21 ?  68  TYR   B CA   1 
ATOM   5000 C  C    . TYR   B 1 68  ? 48.691 -8.147  8.707   1.00 16.34 ?  68  TYR   B C    1 
ATOM   5001 O  O    . TYR   B 1 68  ? 47.751 -7.473  9.147   1.00 17.03 ?  68  TYR   B O    1 
ATOM   5002 C  CB   . TYR   B 1 68  ? 48.801 -8.749  6.274   1.00 17.53 ?  68  TYR   B CB   1 
ATOM   5003 C  CG   . TYR   B 1 68  ? 47.299 -8.902  6.325   1.00 18.39 ?  68  TYR   B CG   1 
ATOM   5004 C  CD1  . TYR   B 1 68  ? 46.708 -9.866  7.130   1.00 18.78 ?  68  TYR   B CD1  1 
ATOM   5005 C  CD2  . TYR   B 1 68  ? 46.473 -8.063  5.598   1.00 19.44 ?  68  TYR   B CD2  1 
ATOM   5006 C  CE1  . TYR   B 1 68  ? 45.343 -9.998  7.202   1.00 19.74 ?  68  TYR   B CE1  1 
ATOM   5007 C  CE2  . TYR   B 1 68  ? 45.095 -8.189  5.664   1.00 20.15 ?  68  TYR   B CE2  1 
ATOM   5008 C  CZ   . TYR   B 1 68  ? 44.547 -9.159  6.469   1.00 20.14 ?  68  TYR   B CZ   1 
ATOM   5009 O  OH   . TYR   B 1 68  ? 43.177 -9.287  6.552   1.00 21.37 ?  68  TYR   B OH   1 
ATOM   5010 H  H    . TYR   B 1 68  ? 51.142 -8.444  6.884   1.00 19.79 ?  68  TYR   B H    1 
ATOM   5011 H  HA   . TYR   B 1 68  ? 49.075 -6.904  7.129   1.00 20.71 ?  68  TYR   B HA   1 
ATOM   5012 H  HB2  . TYR   B 1 68  ? 49.036 -8.391  5.404   1.00 21.10 ?  68  TYR   B HB2  1 
ATOM   5013 H  HB3  . TYR   B 1 68  ? 49.197 -9.627  6.391   1.00 21.10 ?  68  TYR   B HB3  1 
ATOM   5014 H  HD1  . TYR   B 1 68  ? 47.244 -10.443 7.627   1.00 22.60 ?  68  TYR   B HD1  1 
ATOM   5015 H  HD2  . TYR   B 1 68  ? 46.854 -7.404  5.062   1.00 23.39 ?  68  TYR   B HD2  1 
ATOM   5016 H  HE1  . TYR   B 1 68  ? 44.958 -10.657 7.737   1.00 23.74 ?  68  TYR   B HE1  1 
ATOM   5017 H  HE2  . TYR   B 1 68  ? 44.547 -7.620  5.171   1.00 24.23 ?  68  TYR   B HE2  1 
ATOM   5018 H  HH   . TYR   B 1 68  ? 42.787 -8.728  6.053   1.00 25.70 ?  68  TYR   B HH   1 
ATOM   5019 N  N    . ILE   B 1 69  ? 49.180 -9.202  9.364   1.00 15.99 ?  69  ILE   B N    1 
ATOM   5020 C  CA   . ILE   B 1 69  ? 48.616 -9.628  10.641  1.00 16.58 ?  69  ILE   B CA   1 
ATOM   5021 C  C    . ILE   B 1 69  ? 48.860 -8.583  11.723  1.00 15.88 ?  69  ILE   B C    1 
ATOM   5022 O  O    . ILE   B 1 69  ? 47.979 -8.303  12.547  1.00 16.02 ?  69  ILE   B O    1 
ATOM   5023 C  CB   . ILE   B 1 69  ? 49.184 -11.007 11.029  1.00 17.12 ?  69  ILE   B CB   1 
ATOM   5024 C  CG1  . ILE   B 1 69  ? 48.643 -12.107 10.107  1.00 17.18 ?  69  ILE   B CG1  1 
ATOM   5025 C  CG2  . ILE   B 1 69  ? 48.898 -11.321 12.490  1.00 18.34 ?  69  ILE   B CG2  1 
ATOM   5026 C  CD1  . ILE   B 1 69  ? 47.163 -12.420 10.288  1.00 17.98 ?  69  ILE   B CD1  1 
ATOM   5027 H  H    . ILE   B 1 69  ? 49.836 -9.686  9.089   1.00 19.25 ?  69  ILE   B H    1 
ATOM   5028 H  HA   . ILE   B 1 69  ? 47.660 -9.723  10.541  1.00 19.95 ?  69  ILE   B HA   1 
ATOM   5029 H  HB   . ILE   B 1 69  ? 50.149 -10.974 10.920  1.00 20.60 ?  69  ILE   B HB   1 
ATOM   5030 H  HG12 . ILE   B 1 69  ? 48.775 -11.824 9.188   1.00 20.67 ?  69  ILE   B HG12 1 
ATOM   5031 H  HG13 . ILE   B 1 69  ? 49.141 -12.920 10.274  1.00 20.67 ?  69  ILE   B HG13 1 
ATOM   5032 H  HG21 . ILE   B 1 69  ? 49.037 -12.273 12.634  1.00 22.07 ?  69  ILE   B HG21 1 
ATOM   5033 H  HG22 . ILE   B 1 69  ? 49.505 -10.815 13.051  1.00 22.07 ?  69  ILE   B HG22 1 
ATOM   5034 H  HG23 . ILE   B 1 69  ? 47.980 -11.089 12.689  1.00 22.07 ?  69  ILE   B HG23 1 
ATOM   5035 H  HD11 . ILE   B 1 69  ? 46.915 -13.114 9.660   1.00 21.63 ?  69  ILE   B HD11 1 
ATOM   5036 H  HD12 . ILE   B 1 69  ? 47.013 -12.727 11.196  1.00 21.63 ?  69  ILE   B HD12 1 
ATOM   5037 H  HD13 . ILE   B 1 69  ? 46.644 -11.619 10.119  1.00 21.63 ?  69  ILE   B HD13 1 
ATOM   5038 N  N    . ALA   B 1 70  ? 50.057 -7.994  11.751  1.00 16.15 ?  70  ALA   B N    1 
ATOM   5039 C  CA   . ALA   B 1 70  ? 50.334 -6.949  12.732  1.00 16.13 ?  70  ALA   B CA   1 
ATOM   5040 C  C    . ALA   B 1 70  ? 49.322 -5.817  12.625  1.00 16.67 ?  70  ALA   B C    1 
ATOM   5041 O  O    . ALA   B 1 70  ? 48.860 -5.286  13.640  1.00 17.15 ?  70  ALA   B O    1 
ATOM   5042 C  CB   . ALA   B 1 70  ? 51.754 -6.413  12.544  1.00 16.24 ?  70  ALA   B CB   1 
ATOM   5043 H  H    . ALA   B 1 70  ? 50.711 -8.175  11.225  1.00 19.44 ?  70  ALA   B H    1 
ATOM   5044 H  HA   . ALA   B 1 70  ? 50.278 -7.324  13.626  1.00 19.41 ?  70  ALA   B HA   1 
ATOM   5045 H  HB1  . ALA   B 1 70  ? 51.944 -5.757  13.237  1.00 19.55 ?  70  ALA   B HB1  1 
ATOM   5046 H  HB2  . ALA   B 1 70  ? 52.387 -7.148  12.612  1.00 19.55 ?  70  ALA   B HB2  1 
ATOM   5047 H  HB3  . ALA   B 1 70  ? 51.828 -5.998  11.670  1.00 19.55 ?  70  ALA   B HB3  1 
ATOM   5048 N  N    . THR   B 1 71  ? 48.949 -5.453  11.400  1.00 16.77 ?  71  THR   B N    1 
ATOM   5049 C  CA   . THR   B 1 71  ? 48.046 -4.327  11.190  1.00 17.94 ?  71  THR   B CA   1 
ATOM   5050 C  C    . THR   B 1 71  ? 46.581 -4.709  11.390  1.00 18.54 ?  71  THR   B C    1 
ATOM   5051 O  O    . THR   B 1 71  ? 45.789 -3.901  11.895  1.00 20.25 ?  71  THR   B O    1 
ATOM   5052 C  CB   . THR   B 1 71  ? 48.248 -3.763  9.783   1.00 19.46 ?  71  THR   B CB   1 
ATOM   5053 O  OG1  . THR   B 1 71  ? 49.566 -3.215  9.675   1.00 21.37 ?  71  THR   B OG1  1 
ATOM   5054 C  CG2  . THR   B 1 71  ? 47.217 -2.685  9.472   1.00 20.17 ?  71  THR   B CG2  1 
ATOM   5055 H  H    . THR   B 1 71  ? 49.209 -5.846  10.679  1.00 20.18 ?  71  THR   B H    1 
ATOM   5056 H  HA   . THR   B 1 71  ? 48.269 -3.629  11.826  1.00 21.58 ?  71  THR   B HA   1 
ATOM   5057 H  HB   . THR   B 1 71  ? 48.158 -4.476  9.132   1.00 23.41 ?  71  THR   B HB   1 
ATOM   5058 H  HG1  . THR   B 1 71  ? 49.687 -2.887  8.906   1.00 25.70 ?  71  THR   B HG1  1 
ATOM   5059 H  HG21 . THR   B 1 71  ? 47.514 -2.150  8.717   1.00 24.26 ?  71  THR   B HG21 1 
ATOM   5060 H  HG22 . THR   B 1 71  ? 46.366 -3.089  9.256   1.00 24.26 ?  71  THR   B HG22 1 
ATOM   5061 H  HG23 . THR   B 1 71  ? 47.107 -2.100  10.241  1.00 24.26 ?  71  THR   B HG23 1 
ATOM   5062 N  N    . ASN   B 1 72  ? 46.198 -5.925  11.000  1.00 18.13 ?  72  ASN   B N    1 
ATOM   5063 C  CA   . ASN   B 1 72  ? 44.799 -6.298  10.865  1.00 18.57 ?  72  ASN   B CA   1 
ATOM   5064 C  C    . ASN   B 1 72  ? 44.326 -7.395  11.808  1.00 18.98 ?  72  ASN   B C    1 
ATOM   5065 O  O    . ASN   B 1 72  ? 43.109 -7.559  11.966  1.00 20.13 ?  72  ASN   B O    1 
ATOM   5066 C  CB   . ASN   B 1 72  ? 44.514 -6.731  9.420   1.00 18.95 ?  72  ASN   B CB   1 
ATOM   5067 C  CG   . ASN   B 1 72  ? 44.789 -5.622  8.420   1.00 20.39 ?  72  ASN   B CG   1 
ATOM   5068 O  OD1  . ASN   B 1 72  ? 45.813 -5.615  7.737   1.00 21.86 ?  72  ASN   B OD1  1 
ATOM   5069 N  ND2  . ASN   B 1 72  ? 43.891 -4.665  8.351   1.00 21.43 ?  72  ASN   B ND2  1 
ATOM   5070 H  H    . ASN   B 1 72  ? 46.748 -6.568  10.807  1.00 21.82 ?  72  ASN   B H    1 
ATOM   5071 H  HA   . ASN   B 1 72  ? 44.262 -5.515  11.044  1.00 22.33 ?  72  ASN   B HA   1 
ATOM   5072 H  HB2  . ASN   B 1 72  ? 45.081 -7.487  9.197   1.00 22.80 ?  72  ASN   B HB2  1 
ATOM   5073 H  HB3  . ASN   B 1 72  ? 43.582 -6.977  9.343   1.00 22.80 ?  72  ASN   B HB3  1 
ATOM   5074 H  HD21 . ASN   B 1 72  ? 44.000 -4.014  7.797   1.00 25.77 ?  72  ASN   B HD21 1 
ATOM   5075 H  HD22 . ASN   B 1 72  ? 43.187 -4.697  8.842   1.00 25.77 ?  72  ASN   B HD22 1 
ATOM   5076 N  N    . GLY   B 1 73  ? 45.225 -8.149  12.432  1.00 18.73 ?  73  GLY   B N    1 
ATOM   5077 C  CA   . GLY   B 1 73  ? 44.816 -9.285  13.224  1.00 18.41 ?  73  GLY   B CA   1 
ATOM   5078 C  C    . GLY   B 1 73  ? 44.474 -10.479 12.355  1.00 17.04 ?  73  GLY   B C    1 
ATOM   5079 O  O    . GLY   B 1 73  ? 44.479 -10.400 11.123  1.00 17.12 ?  73  GLY   B O    1 
ATOM   5080 H  H    . GLY   B 1 73  ? 46.076 -8.020  12.413  1.00 22.53 ?  73  GLY   B H    1 
ATOM   5081 H  HA2  . GLY   B 1 73  ? 45.530 -9.534  13.832  1.00 22.15 ?  73  GLY   B HA2  1 
ATOM   5082 H  HA3  . GLY   B 1 73  ? 44.032 -9.052  13.749  1.00 22.15 ?  73  GLY   B HA3  1 
ATOM   5083 N  N    . PRO   B 1 74  ? 44.160 -11.608 12.990  1.00 17.25 ?  74  PRO   B N    1 
ATOM   5084 C  CA   . PRO   B 1 74  ? 43.908 -12.839 12.238  1.00 16.76 ?  74  PRO   B CA   1 
ATOM   5085 C  C    . PRO   B 1 74  ? 42.613 -12.778 11.443  1.00 16.33 ?  74  PRO   B C    1 
ATOM   5086 O  O    . PRO   B 1 74  ? 41.673 -12.043 11.770  1.00 17.78 ?  74  PRO   B O    1 
ATOM   5087 C  CB   . PRO   B 1 74  ? 43.828 -13.910 13.332  1.00 17.66 ?  74  PRO   B CB   1 
ATOM   5088 C  CG   . PRO   B 1 74  ? 43.386 -13.161 14.547  1.00 19.05 ?  74  PRO   B CG   1 
ATOM   5089 C  CD   . PRO   B 1 74  ? 44.038 -11.810 14.443  1.00 18.81 ?  74  PRO   B CD   1 
ATOM   5090 H  HA   . PRO   B 1 74  ? 44.652 -13.031 11.641  1.00 20.16 ?  74  PRO   B HA   1 
ATOM   5091 H  HB2  . PRO   B 1 74  ? 43.177 -14.582 13.084  1.00 21.25 ?  74  PRO   B HB2  1 
ATOM   5092 H  HB3  . PRO   B 1 74  ? 44.703 -14.304 13.469  1.00 21.25 ?  74  PRO   B HB3  1 
ATOM   5093 H  HG2  . PRO   B 1 74  ? 42.420 -13.076 14.543  1.00 22.91 ?  74  PRO   B HG2  1 
ATOM   5094 H  HG3  . PRO   B 1 74  ? 43.687 -13.625 15.342  1.00 22.91 ?  74  PRO   B HG3  1 
ATOM   5095 H  HD2  . PRO   B 1 74  ? 43.468 -11.127 14.837  1.00 22.62 ?  74  PRO   B HD2  1 
ATOM   5096 H  HD3  . PRO   B 1 74  ? 44.915 -11.821 14.857  1.00 22.62 ?  74  PRO   B HD3  1 
ATOM   5097 N  N    . LEU   B 1 75  ? 42.587 -13.564 10.374  1.00 15.66 ?  75  LEU   B N    1 
ATOM   5098 C  CA   . LEU   B 1 75  ? 41.380 -13.785 9.603   1.00 16.02 ?  75  LEU   B CA   1 
ATOM   5099 C  C    . LEU   B 1 75  ? 40.396 -14.632 10.403  1.00 16.60 ?  75  LEU   B C    1 
ATOM   5100 O  O    . LEU   B 1 75  ? 40.728 -15.217 11.437  1.00 17.39 ?  75  LEU   B O    1 
ATOM   5101 C  CB   . LEU   B 1 75  ? 41.709 -14.517 8.303   1.00 15.87 ?  75  LEU   B CB   1 
ATOM   5102 C  CG   . LEU   B 1 75  ? 42.535 -13.739 7.276   1.00 17.49 ?  75  LEU   B CG   1 
ATOM   5103 C  CD1  . LEU   B 1 75  ? 42.773 -14.570 6.020   1.00 19.02 ?  75  LEU   B CD1  1 
ATOM   5104 C  CD2  . LEU   B 1 75  ? 41.889 -12.421 6.921   1.00 20.35 ?  75  LEU   B CD2  1 
ATOM   5105 H  H    . LEU   B 1 75  ? 43.270 -13.987 10.067  1.00 18.85 ?  75  LEU   B H    1 
ATOM   5106 H  HA   . LEU   B 1 75  ? 40.963 -12.937 9.391   1.00 19.28 ?  75  LEU   B HA   1 
ATOM   5107 H  HB2  . LEU   B 1 75  ? 42.212 -15.320 8.522   1.00 19.09 ?  75  LEU   B HB2  1 
ATOM   5108 H  HB3  . LEU   B 1 75  ? 40.879 -14.769 7.872   1.00 19.09 ?  75  LEU   B HB3  1 
ATOM   5109 H  HG   . LEU   B 1 75  ? 43.403 -13.542 7.662   1.00 21.05 ?  75  LEU   B HG   1 
ATOM   5110 H  HD11 . LEU   B 1 75  ? 43.306 -14.051 5.392   1.00 22.88 ?  75  LEU   B HD11 1 
ATOM   5111 H  HD12 . LEU   B 1 75  ? 43.251 -15.380 6.262   1.00 22.88 ?  75  LEU   B HD12 1 
ATOM   5112 H  HD13 . LEU   B 1 75  ? 41.920 -14.795 5.621   1.00 22.88 ?  75  LEU   B HD13 1 
ATOM   5113 H  HD21 . LEU   B 1 75  ? 42.360 -12.031 6.170   1.00 24.47 ?  75  LEU   B HD21 1 
ATOM   5114 H  HD22 . LEU   B 1 75  ? 40.962 -12.578 6.688   1.00 24.47 ?  75  LEU   B HD22 1 
ATOM   5115 H  HD23 . LEU   B 1 75  ? 41.942 -11.828 7.689   1.00 24.47 ?  75  LEU   B HD23 1 
ATOM   5116 N  N    . LYS   B 1 76  ? 39.162 -14.687 9.906   1.00 18.22 ?  76  LYS   B N    1 
ATOM   5117 C  CA   . LYS   B 1 76  ? 38.172 -15.639 10.388  1.00 19.76 ?  76  LYS   B CA   1 
ATOM   5118 C  C    . LYS   B 1 76  ? 38.284 -16.917 9.567   1.00 19.09 ?  76  LYS   B C    1 
ATOM   5119 O  O    . LYS   B 1 76  ? 38.558 -16.870 8.367   1.00 18.13 ?  76  LYS   B O    1 
ATOM   5120 C  CB   . LYS   B 1 76  ? 36.759 -15.077 10.197  1.00 20.88 ?  76  LYS   B CB   1 
ATOM   5121 C  CG   . LYS   B 1 76  ? 36.474 -13.723 10.860  1.00 22.36 ?  76  LYS   B CG   1 
ATOM   5122 C  CD   . LYS   B 1 76  ? 35.091 -13.182 10.455  1.00 23.64 ?  76  LYS   B CD   1 
ATOM   5123 C  CE   . LYS   B 1 76  ? 34.778 -11.855 11.128  1.00 24.81 ?  76  LYS   B CE   1 
ATOM   5124 N  NZ   . LYS   B 1 76  ? 33.542 -11.215 10.592  1.00 25.74 ?  76  LYS   B NZ   1 
ATOM   5125 H  H    . LYS   B 1 76  ? 38.875 -14.182 9.273   1.00 21.91 ?  76  LYS   B H    1 
ATOM   5126 H  HA   . LYS   B 1 76  ? 38.318 -15.845 11.325  1.00 23.76 ?  76  LYS   B HA   1 
ATOM   5127 H  HB2  . LYS   B 1 76  ? 36.598 -14.972 9.246   1.00 25.11 ?  76  LYS   B HB2  1 
ATOM   5128 H  HB3  . LYS   B 1 76  ? 36.124 -15.715 10.561  1.00 25.11 ?  76  LYS   B HB3  1 
ATOM   5129 H  HG2  . LYS   B 1 76  ? 36.490 -13.829 11.825  1.00 26.89 ?  76  LYS   B HG2  1 
ATOM   5130 H  HG3  . LYS   B 1 76  ? 37.148 -13.082 10.582  1.00 26.89 ?  76  LYS   B HG3  1 
ATOM   5131 H  HD2  . LYS   B 1 76  ? 35.073 -13.044 9.493   1.00 28.43 ?  76  LYS   B HD2  1 
ATOM   5132 H  HD3  . LYS   B 1 76  ? 34.409 -13.821 10.713  1.00 28.43 ?  76  LYS   B HD3  1 
ATOM   5133 H  HE2  . LYS   B 1 76  ? 34.651 -12.006 12.077  1.00 29.83 ?  76  LYS   B HE2  1 
ATOM   5134 H  HE3  . LYS   B 1 76  ? 35.519 -11.245 10.984  1.00 29.83 ?  76  LYS   B HE3  1 
ATOM   5135 H  HZ1  . LYS   B 1 76  ? 33.393 -10.442 11.011  1.00 30.94 ?  76  LYS   B HZ1  1 
ATOM   5136 H  HZ2  . LYS   B 1 76  ? 33.633 -11.056 9.721   1.00 30.94 ?  76  LYS   B HZ2  1 
ATOM   5137 H  HZ3  . LYS   B 1 76  ? 32.842 -11.749 10.717  1.00 30.94 ?  76  LYS   B HZ3  1 
ATOM   5138 N  N    . VAL   B 1 77  ? 38.060 -18.064 10.211  1.00 20.13 ?  77  VAL   B N    1 
ATOM   5139 C  CA   . VAL   B 1 77  ? 37.849 -19.287 9.447   1.00 19.97 ?  77  VAL   B CA   1 
ATOM   5140 C  C    . VAL   B 1 77  ? 36.657 -19.068 8.529   1.00 18.61 ?  77  VAL   B C    1 
ATOM   5141 O  O    . VAL   B 1 77  ? 35.591 -18.623 8.972   1.00 18.69 ?  77  VAL   B O    1 
ATOM   5142 C  CB   . VAL   B 1 77  ? 37.640 -20.483 10.387  1.00 21.66 ?  77  VAL   B CB   1 
ATOM   5143 C  CG1  . VAL   B 1 77  ? 37.314 -21.738 9.582   1.00 21.65 ?  77  VAL   B CG1  1 
ATOM   5144 C  CG2  . VAL   B 1 77  ? 38.878 -20.702 11.262  1.00 22.81 ?  77  VAL   B CG2  1 
ATOM   5145 H  H    . VAL   B 1 77  ? 38.023 -18.157 11.061  1.00 24.21 ?  77  VAL   B H    1 
ATOM   5146 H  HA   . VAL   B 1 77  ? 38.622 -19.462 8.894   1.00 24.02 ?  77  VAL   B HA   1 
ATOM   5147 H  HB   . VAL   B 1 77  ? 36.885 -20.302 10.968  1.00 26.05 ?  77  VAL   B HB   1 
ATOM   5148 H  HG11 . VAL   B 1 77  ? 37.329 -22.505 10.177  1.00 26.04 ?  77  VAL   B HG11 1 
ATOM   5149 H  HG12 . VAL   B 1 77  ? 36.428 -21.649 9.190   1.00 26.04 ?  77  VAL   B HG12 1 
ATOM   5150 H  HG13 . VAL   B 1 77  ? 37.974 -21.847 8.883   1.00 26.04 ?  77  VAL   B HG13 1 
ATOM   5151 H  HG21 . VAL   B 1 77  ? 38.739 -21.490 11.807  1.00 27.43 ?  77  VAL   B HG21 1 
ATOM   5152 H  HG22 . VAL   B 1 77  ? 39.648 -20.823 10.687  1.00 27.43 ?  77  VAL   B HG22 1 
ATOM   5153 H  HG23 . VAL   B 1 77  ? 39.000 -19.923 11.825  1.00 27.43 ?  77  VAL   B HG23 1 
ATOM   5154 N  N    . GLY   B 1 78  ? 36.836 -19.360 7.239   1.00 17.45 ?  78  GLY   B N    1 
ATOM   5155 C  CA   . GLY   B 1 78  ? 35.859 -19.042 6.225   1.00 17.53 ?  78  GLY   B CA   1 
ATOM   5156 C  C    . GLY   B 1 78  ? 36.096 -17.728 5.516   1.00 16.73 ?  78  GLY   B C    1 
ATOM   5157 O  O    . GLY   B 1 78  ? 35.405 -17.450 4.527   1.00 16.90 ?  78  GLY   B O    1 
ATOM   5158 H  H    . GLY   B 1 78  ? 37.528 -19.767 6.930   1.00 20.99 ?  78  GLY   B H    1 
ATOM   5159 H  HA2  . GLY   B 1 78  ? 35.857 -19.738 5.551   1.00 21.09 ?  78  GLY   B HA2  1 
ATOM   5160 H  HA3  . GLY   B 1 78  ? 34.977 -19.010 6.627   1.00 21.09 ?  78  GLY   B HA3  1 
ATOM   5161 N  N    . GLY   B 1 79  ? 37.042 -16.912 5.997   1.00 16.44 ?  79  GLY   B N    1 
ATOM   5162 C  CA   . GLY   B 1 79  ? 37.343 -15.622 5.411   1.00 16.14 ?  79  GLY   B CA   1 
ATOM   5163 C  C    . GLY   B 1 79  ? 38.572 -15.654 4.515   1.00 16.04 ?  79  GLY   B C    1 
ATOM   5164 O  O    . GLY   B 1 79  ? 39.184 -16.692 4.271   1.00 15.99 ?  79  GLY   B O    1 
ATOM   5165 H  H    . GLY   B 1 79  ? 37.529 -17.091 6.683   1.00 19.79 ?  79  GLY   B H    1 
ATOM   5166 H  HA2  . GLY   B 1 79  ? 36.588 -15.326 4.872   1.00 19.42 ?  79  GLY   B HA2  1 
ATOM   5167 H  HA3  . GLY   B 1 79  ? 37.486 -14.968 6.113   1.00 19.42 ?  79  GLY   B HA3  1 
ATOM   5168 N  N    . SER   B 1 80  ? 38.937 -14.464 4.038   1.00 15.68 ?  80  SER   B N    1 
ATOM   5169 C  CA   . SER   B 1 80  ? 40.045 -14.336 3.103   1.00 15.16 ?  80  SER   B CA   1 
ATOM   5170 C  C    . SER   B 1 80  ? 40.623 -12.930 3.161   1.00 14.96 ?  80  SER   B C    1 
ATOM   5171 O  O    . SER   B 1 80  ? 40.005 -11.994 3.680   1.00 15.96 ?  80  SER   B O    1 
ATOM   5172 C  CB   . SER   B 1 80  ? 39.614 -14.625 1.663   1.00 15.54 ?  80  SER   B CB   1 
ATOM   5173 O  OG   . SER   B 1 80  ? 38.760 -13.611 1.166   1.00 16.58 ?  80  SER   B OG   1 
ATOM   5174 H  H    . SER   B 1 80  ? 38.572 -13.718 4.252   1.00 18.87 ?  80  SER   B H    1 
ATOM   5175 H  HA   . SER   B 1 80  ? 40.742 -14.961 3.355   1.00 18.24 ?  80  SER   B HA   1 
ATOM   5176 H  HB2  . SER   B 1 80  ? 40.404 -14.675 1.103   1.00 18.71 ?  80  SER   B HB2  1 
ATOM   5177 H  HB3  . SER   B 1 80  ? 39.140 -15.470 1.645   1.00 18.71 ?  80  SER   B HB3  1 
ATOM   5178 H  HG   . SER   B 1 80  ? 38.075 -13.550 1.654   1.00 19.95 ?  80  SER   B HG   1 
ATOM   5179 N  N    . CYS   B 1 81  ? 41.811 -12.788 2.577   1.00 14.90 ?  81  CYS   B N    1 
ATOM   5180 C  CA   . CYS   B 1 81  ? 42.357 -11.477 2.271   1.00 14.99 ?  81  CYS   B CA   1 
ATOM   5181 C  C    . CYS   B 1 81  ? 43.135 -11.562 0.968   1.00 14.47 ?  81  CYS   B C    1 
ATOM   5182 O  O    . CYS   B 1 81  ? 43.654 -12.624 0.603   1.00 15.30 ?  81  CYS   B O    1 
ATOM   5183 C  CB   . CYS   B 1 81  ? 43.243 -10.928 3.398   1.00 15.82 ?  81  CYS   B CB   1 
ATOM   5184 S  SG   . CYS   B 1 81  ? 44.765 -11.857 3.645   1.00 14.80 ?  81  CYS   B SG   1 
ATOM   5185 H  H    . CYS   B 1 81  ? 42.329 -13.443 2.351   1.00 17.94 ?  81  CYS   B H    1 
ATOM   5186 H  HA   . CYS   B 1 81  ? 41.622 -10.857 2.136   1.00 18.04 ?  81  CYS   B HA   1 
ATOM   5187 H  HB2  . CYS   B 1 81  ? 43.484 -10.007 3.190   1.00 19.03 ?  81  CYS   B HB2  1 
ATOM   5188 H  HB3  . CYS   B 1 81  ? 42.737 -10.945 4.231   1.00 19.03 ?  81  CYS   B HB3  1 
ATOM   5189 H  HG   . CYS   B 1 81  ? 45.390 -11.358 4.550   1.00 17.82 ?  81  CYS   B HG   1 
ATOM   5190 N  N    . VAL   B 1 82  ? 43.235 -10.421 0.290   1.00 14.21 ?  82  VAL   B N    1 
ATOM   5191 C  CA   . VAL   B 1 82  ? 44.001 -10.291 -0.947  1.00 14.64 ?  82  VAL   B CA   1 
ATOM   5192 C  C    . VAL   B 1 82  ? 45.344 -9.655  -0.625  1.00 15.02 ?  82  VAL   B C    1 
ATOM   5193 O  O    . VAL   B 1 82  ? 45.398 -8.540  -0.085  1.00 15.86 ?  82  VAL   B O    1 
ATOM   5194 C  CB   . VAL   B 1 82  ? 43.256 -9.446  -1.991  1.00 15.68 ?  82  VAL   B CB   1 
ATOM   5195 C  CG1  . VAL   B 1 82  ? 44.089 -9.325  -3.259  1.00 16.64 ?  82  VAL   B CG1  1 
ATOM   5196 C  CG2  . VAL   B 1 82  ? 41.887 -10.042 -2.288  1.00 16.91 ?  82  VAL   B CG2  1 
ATOM   5197 H  H    . VAL   B 1 82  ? 42.851 -9.684  0.531   1.00 17.10 ?  82  VAL   B H    1 
ATOM   5198 H  HA   . VAL   B 1 82  ? 44.158 -11.170 -1.320  1.00 17.63 ?  82  VAL   B HA   1 
ATOM   5199 H  HB   . VAL   B 1 82  ? 43.124 -8.556  -1.640  1.00 18.87 ?  82  VAL   B HB   1 
ATOM   5200 H  HG11 . VAL   B 1 82  ? 43.525 -8.993  -3.975  1.00 20.02 ?  82  VAL   B HG11 1 
ATOM   5201 H  HG12 . VAL   B 1 82  ? 44.821 -8.711  -3.103  1.00 20.02 ?  82  VAL   B HG12 1 
ATOM   5202 H  HG13 . VAL   B 1 82  ? 44.435 -10.202 -3.495  1.00 20.02 ?  82  VAL   B HG13 1 
ATOM   5203 H  HG21 . VAL   B 1 82  ? 41.459 -9.518  -2.987  1.00 20.35 ?  82  VAL   B HG21 1 
ATOM   5204 H  HG22 . VAL   B 1 82  ? 41.995 -10.959 -2.583  1.00 20.35 ?  82  VAL   B HG22 1 
ATOM   5205 H  HG23 . VAL   B 1 82  ? 41.348 -10.014 -1.481  1.00 20.35 ?  82  VAL   B HG23 1 
ATOM   5206 N  N    . LEU   B 1 83  ? 46.419 -10.341 -0.997  1.00 14.55 ?  83  LEU   B N    1 
ATOM   5207 C  CA   . LEU   B 1 83  ? 47.773 -9.825  -0.876  1.00 14.99 ?  83  LEU   B CA   1 
ATOM   5208 C  C    . LEU   B 1 83  ? 48.474 -9.976  -2.224  1.00 14.79 ?  83  LEU   B C    1 
ATOM   5209 O  O    . LEU   B 1 83  ? 47.874 -10.404 -3.211  1.00 14.52 ?  83  LEU   B O    1 
ATOM   5210 C  CB   . LEU   B 1 83  ? 48.518 -10.502 0.279   1.00 15.57 ?  83  LEU   B CB   1 
ATOM   5211 C  CG   . LEU   B 1 83  ? 48.000 -10.141 1.678   1.00 16.14 ?  83  LEU   B CG   1 
ATOM   5212 C  CD1  . LEU   B 1 83  ? 48.638 -10.999 2.754   1.00 16.47 ?  83  LEU   B CD1  1 
ATOM   5213 C  CD2  . LEU   B 1 83  ? 48.185 -8.650  1.997   1.00 16.90 ?  83  LEU   B CD2  1 
ATOM   5214 H  H    . LEU   B 1 83  ? 46.381 -11.135 -1.337  1.00 17.51 ?  83  LEU   B H    1 
ATOM   5215 H  HA   . LEU   B 1 83  ? 47.723 -8.880  -0.686  1.00 18.04 ?  83  LEU   B HA   1 
ATOM   5216 H  HB2  . LEU   B 1 83  ? 48.445 -11.463 0.176   1.00 18.74 ?  83  LEU   B HB2  1 
ATOM   5217 H  HB3  . LEU   B 1 83  ? 49.453 -10.241 0.235   1.00 18.74 ?  83  LEU   B HB3  1 
ATOM   5218 H  HG   . LEU   B 1 83  ? 47.047 -10.319 1.698   1.00 19.42 ?  83  LEU   B HG   1 
ATOM   5219 H  HD11 . LEU   B 1 83  ? 48.278 -10.746 3.618   1.00 19.82 ?  83  LEU   B HD11 1 
ATOM   5220 H  HD12 . LEU   B 1 83  ? 48.430 -11.934 2.574   1.00 19.82 ?  83  LEU   B HD12 1 
ATOM   5221 H  HD13 . LEU   B 1 83  ? 49.596 -10.868 2.740   1.00 19.82 ?  83  LEU   B HD13 1 
ATOM   5222 H  HD21 . LEU   B 1 83  ? 47.971 -8.496  2.931   1.00 20.34 ?  83  LEU   B HD21 1 
ATOM   5223 H  HD22 . LEU   B 1 83  ? 49.101 -8.397  1.819   1.00 20.34 ?  83  LEU   B HD22 1 
ATOM   5224 H  HD23 . LEU   B 1 83  ? 47.584 -8.129  1.435   1.00 20.34 ?  83  LEU   B HD23 1 
ATOM   5225 N  N    . SER   B 1 84  ? 49.750 -9.602  -2.277  1.00 15.44 ?  84  SER   B N    1 
ATOM   5226 C  CA   . SER   B 1 84  ? 50.495 -9.741  -3.517  1.00 15.92 ?  84  SER   B CA   1 
ATOM   5227 C  C    . SER   B 1 84  ? 50.654 -11.211 -3.900  1.00 14.99 ?  84  SER   B C    1 
ATOM   5228 O  O    . SER   B 1 84  ? 50.763 -12.093 -3.047  1.00 14.65 ?  84  SER   B O    1 
ATOM   5229 C  CB   . SER   B 1 84  ? 51.887 -9.129  -3.369  1.00 17.08 ?  84  SER   B CB   1 
ATOM   5230 O  OG   . SER   B 1 84  ? 52.620 -9.357  -4.552  1.00 18.47 ?  84  SER   B OG   1 
ATOM   5231 H  H    . SER   B 1 84  ? 50.191 -9.262  -1.627  1.00 18.58 ?  84  SER   B H    1 
ATOM   5232 H  HA   . SER   B 1 84  ? 50.028 -9.283  -4.235  1.00 19.16 ?  84  SER   B HA   1 
ATOM   5233 H  HB2  . SER   B 1 84  ? 51.800 -8.174  -3.208  1.00 20.55 ?  84  SER   B HB2  1 
ATOM   5234 H  HB3  . SER   B 1 84  ? 52.345 -9.552  -2.626  1.00 20.55 ?  84  SER   B HB3  1 
ATOM   5235 H  HG   . SER   B 1 84  ? 53.390 -9.002  -4.479  1.00 22.22 ?  84  SER   B HG   1 
ATOM   5236 N  N    . GLY   B 1 85  ? 50.711 -11.458 -5.204  1.00 15.67 ?  85  GLY   B N    1 
ATOM   5237 C  CA   . GLY   B 1 85  ? 51.069 -12.755 -5.725  1.00 16.65 ?  85  GLY   B CA   1 
ATOM   5238 C  C    . GLY   B 1 85  ? 52.542 -12.933 -6.037  1.00 15.87 ?  85  GLY   B C    1 
ATOM   5239 O  O    . GLY   B 1 85  ? 52.927 -14.010 -6.497  1.00 16.26 ?  85  GLY   B O    1 
ATOM   5240 H  H    . GLY   B 1 85  ? 50.551 -10.878 -5.812  1.00 18.86 ?  85  GLY   B H    1 
ATOM   5241 H  HA2  . GLY   B 1 85  ? 50.820 -13.437 -5.077  1.00 20.04 ?  85  GLY   B HA2  1 
ATOM   5242 H  HA3  . GLY   B 1 85  ? 50.572 -12.920 -6.536  1.00 20.04 ?  85  GLY   B HA3  1 
ATOM   5243 N  N    . HIS   B 1 86  ? 53.389 -11.924 -5.822  1.00 15.99 ?  86  HIS   B N    1 
ATOM   5244 C  CA   . HIS   B 1 86  ? 54.854 -12.078 -5.904  1.00 15.83 ?  86  HIS   B CA   1 
ATOM   5245 C  C    . HIS   B 1 86  ? 55.238 -12.602 -7.286  1.00 15.91 ?  86  HIS   B C    1 
ATOM   5246 O  O    . HIS   B 1 86  ? 54.849 -11.999 -8.299  1.00 16.89 ?  86  HIS   B O    1 
ATOM   5247 C  CB   . HIS   B 1 86  ? 55.343 -12.899 -4.717  1.00 16.12 ?  86  HIS   B CB   1 
ATOM   5248 C  CG   . HIS   B 1 86  ? 55.017 -12.283 -3.397  1.00 16.06 ?  86  HIS   B CG   1 
ATOM   5249 N  ND1  . HIS   B 1 86  ? 55.839 -11.368 -2.779  1.00 17.60 ?  86  HIS   B ND1  1 
ATOM   5250 C  CD2  . HIS   B 1 86  ? 53.939 -12.428 -2.590  1.00 16.67 ?  86  HIS   B CD2  1 
ATOM   5251 C  CE1  . HIS   B 1 86  ? 55.282 -10.975 -1.646  1.00 17.05 ?  86  HIS   B CE1  1 
ATOM   5252 N  NE2  . HIS   B 1 86  ? 54.126 -11.601 -1.510  1.00 16.91 ?  86  HIS   B NE2  1 
ATOM   5253 H  H    . HIS   B 1 86  ? 53.138 -11.127 -5.629  1.00 19.24 ?  86  HIS   B H    1 
ATOM   5254 H  HA   . HIS   B 1 86  ? 55.252 -11.201 -5.817  1.00 19.06 ?  86  HIS   B HA   1 
ATOM   5255 H  HB2  . HIS   B 1 86  ? 54.936 -13.777 -4.748  1.00 19.40 ?  86  HIS   B HB2  1 
ATOM   5256 H  HB3  . HIS   B 1 86  ? 56.312 -12.985 -4.772  1.00 19.40 ?  86  HIS   B HB3  1 
ATOM   5257 H  HD2  . HIS   B 1 86  ? 53.201 -12.975 -2.747  1.00 20.06 ?  86  HIS   B HD2  1 
ATOM   5258 H  HE1  . HIS   B 1 86  ? 55.645 -10.371 -1.039  1.00 20.51 ?  86  HIS   B HE1  1 
ATOM   5259 H  HE2  . HIS   B 1 86  ? 53.584 -11.517 -0.845  1.00 20.35 ?  86  HIS   B HE2  1 
ATOM   5260 N  N    . ASN   B 1 87  ? 56.004 -13.689 -7.381  1.00 16.30 ?  87  ASN   B N    1 
ATOM   5261 C  CA   . ASN   B 1 87  ? 56.408 -14.265 -8.654  1.00 17.70 ?  87  ASN   B CA   1 
ATOM   5262 C  C    . ASN   B 1 87  ? 55.426 -15.304 -9.163  1.00 17.33 ?  87  ASN   B C    1 
ATOM   5263 O  O    . ASN   B 1 87  ? 55.747 -16.015 -10.120 1.00 18.71 ?  87  ASN   B O    1 
ATOM   5264 C  CB   . ASN   B 1 87  ? 57.802 -14.895 -8.534  1.00 19.04 ?  87  ASN   B CB   1 
ATOM   5265 C  CG   . ASN   B 1 87  ? 57.853 -16.006 -7.497  1.00 19.93 ?  87  ASN   B CG   1 
ATOM   5266 O  OD1  . ASN   B 1 87  ? 57.210 -15.923 -6.445  1.00 19.03 ?  87  ASN   B OD1  1 
ATOM   5267 N  ND2  . ASN   B 1 87  ? 58.614 -17.066 -7.798  1.00 21.22 ?  87  ASN   B ND2  1 
ATOM   5268 H  H    . ASN   B 1 87  ? 56.296 -14.124 -6.703  1.00 19.62 ?  87  ASN   B H    1 
ATOM   5269 H  HA   . ASN   B 1 87  ? 56.454 -13.567 -9.314  1.00 21.30 ?  87  ASN   B HA   1 
ATOM   5270 H  HB2  . ASN   B 1 87  ? 58.055 -15.274 -9.391  1.00 22.91 ?  87  ASN   B HB2  1 
ATOM   5271 H  HB3  . ASN   B 1 87  ? 58.433 -14.210 -8.272  1.00 22.91 ?  87  ASN   B HB3  1 
ATOM   5272 H  HD21 . ASN   B 1 87  ? 58.680 -17.721 -7.244  1.00 25.51 ?  87  ASN   B HD21 1 
ATOM   5273 H  HD22 . ASN   B 1 87  ? 59.042 -17.094 -8.546  1.00 25.51 ?  87  ASN   B HD22 1 
ATOM   5274 N  N    . LEU   B 1 88  ? 54.241 -15.405 -8.555  1.00 15.93 ?  88  LEU   B N    1 
ATOM   5275 C  CA   . LEU   B 1 88  ? 53.258 -16.428 -8.888  1.00 16.29 ?  88  LEU   B CA   1 
ATOM   5276 C  C    . LEU   B 1 88  ? 52.033 -15.901 -9.613  1.00 16.27 ?  88  LEU   B C    1 
ATOM   5277 O  O    . LEU   B 1 88  ? 51.437 -16.636 -10.410 1.00 18.30 ?  88  LEU   B O    1 
ATOM   5278 C  CB   . LEU   B 1 88  ? 52.769 -17.098 -7.603  1.00 17.42 ?  88  LEU   B CB   1 
ATOM   5279 C  CG   . LEU   B 1 88  ? 53.866 -17.786 -6.803  1.00 19.79 ?  88  LEU   B CG   1 
ATOM   5280 C  CD1  . LEU   B 1 88  ? 53.373 -18.093 -5.400  1.00 20.81 ?  88  LEU   B CD1  1 
ATOM   5281 C  CD2  . LEU   B 1 88  ? 54.285 -19.056 -7.516  1.00 22.05 ?  88  LEU   B CD2  1 
ATOM   5282 H  H    . LEU   B 1 88  ? 53.977 -14.879 -7.921  1.00 19.17 ?  88  LEU   B H    1 
ATOM   5283 H  HA   . LEU   B 1 88  ? 53.666 -17.099 -9.444  1.00 19.61 ?  88  LEU   B HA   1 
ATOM   5284 H  HB2  . LEU   B 1 88  ? 52.358 -16.433 -7.030  1.00 20.96 ?  88  LEU   B HB2  1 
ATOM   5285 H  HB3  . LEU   B 1 88  ? 52.108 -17.777 -7.835  1.00 20.96 ?  88  LEU   B HB3  1 
ATOM   5286 H  HG   . LEU   B 1 88  ? 54.634 -17.198 -6.737  1.00 23.81 ?  88  LEU   B HG   1 
ATOM   5287 H  HD11 . LEU   B 1 88  ? 53.971 -18.732 -4.988  1.00 25.03 ?  88  LEU   B HD11 1 
ATOM   5288 H  HD12 . LEU   B 1 88  ? 53.356 -17.271 -4.885  1.00 25.03 ?  88  LEU   B HD12 1 
ATOM   5289 H  HD13 . LEU   B 1 88  ? 52.478 -18.464 -5.458  1.00 25.03 ?  88  LEU   B HD13 1 
ATOM   5290 H  HD21 . LEU   B 1 88  ? 54.942 -19.518 -6.973  1.00 26.52 ?  88  LEU   B HD21 1 
ATOM   5291 H  HD22 . LEU   B 1 88  ? 53.505 -19.617 -7.644  1.00 26.52 ?  88  LEU   B HD22 1 
ATOM   5292 H  HD23 . LEU   B 1 88  ? 54.671 -18.822 -8.375  1.00 26.52 ?  88  LEU   B HD23 1 
ATOM   5293 N  N    . ALA   B 1 89  ? 51.625 -14.671 -9.328  1.00 15.74 ?  89  ALA   B N    1 
ATOM   5294 C  CA   . ALA   B 1 89  ? 50.340 -14.171 -9.791  1.00 15.45 ?  89  ALA   B CA   1 
ATOM   5295 C  C    . ALA   B 1 89  ? 50.307 -12.686 -9.490  1.00 15.45 ?  89  ALA   B C    1 
ATOM   5296 O  O    . ALA   B 1 89  ? 51.120 -12.178 -8.716  1.00 16.09 ?  89  ALA   B O    1 
ATOM   5297 C  CB   . ALA   B 1 89  ? 49.196 -14.866 -9.062  1.00 15.36 ?  89  ALA   B CB   1 
ATOM   5298 H  H    . ALA   B 1 89  ? 52.071 -14.095 -8.868  1.00 18.95 ?  89  ALA   B H    1 
ATOM   5299 H  HA   . ALA   B 1 89  ? 50.242 -14.304 -10.749 1.00 18.59 ?  89  ALA   B HA   1 
ATOM   5300 H  HB1  . ALA   B 1 89  ? 48.353 -14.529 -9.402  1.00 18.49 ?  89  ALA   B HB1  1 
ATOM   5301 H  HB2  . ALA   B 1 89  ? 49.261 -15.821 -9.226  1.00 18.49 ?  89  ALA   B HB2  1 
ATOM   5302 H  HB3  . ALA   B 1 89  ? 49.273 -14.686 -8.116  1.00 18.49 ?  89  ALA   B HB3  1 
ATOM   5303 N  N    . LYS   B 1 90  ? 49.342 -11.987 -10.082 1.00 16.20 ?  90  LYS   B N    1 
ATOM   5304 C  CA   . LYS   B 1 90  ? 49.153 -10.598 -9.680  1.00 16.56 ?  90  LYS   B CA   1 
ATOM   5305 C  C    . LYS   B 1 90  ? 48.816 -10.521 -8.195  1.00 15.75 ?  90  LYS   B C    1 
ATOM   5306 O  O    . LYS   B 1 90  ? 49.461 -9.779  -7.435  1.00 16.44 ?  90  LYS   B O    1 
ATOM   5307 C  CB   . LYS   B 1 90  ? 48.092 -9.927  -10.548 1.00 17.85 ?  90  LYS   B CB   1 
ATOM   5308 C  CG   . LYS   B 1 90  ? 47.750 -8.512  -10.129 1.00 18.03 ?  90  LYS   B CG   1 
ATOM   5309 C  CD   . LYS   B 1 90  ? 48.941 -7.594  -10.172 1.00 19.56 ?  90  LYS   B CD   1 
ATOM   5310 C  CE   . LYS   B 1 90  ? 48.471 -6.192  -9.875  1.00 20.76 ?  90  LYS   B CE   1 
ATOM   5311 N  NZ   . LYS   B 1 90  ? 49.590 -5.224  -9.850  1.00 19.76 ?  90  LYS   B NZ   1 
ATOM   5312 H  H    . LYS   B 1 90  ? 48.807 -12.279 -10.691 1.00 19.50 ?  90  LYS   B H    1 
ATOM   5313 H  HA   . LYS   B 1 90  ? 49.983 -10.123 -9.814  1.00 19.93 ?  90  LYS   B HA   1 
ATOM   5314 H  HB2  . LYS   B 1 90  ? 48.415 -9.890  -11.464 1.00 21.47 ?  90  LYS   B HB2  1 
ATOM   5315 H  HB3  . LYS   B 1 90  ? 47.277 -10.452 -10.514 1.00 21.47 ?  90  LYS   B HB3  1 
ATOM   5316 H  HG2  . LYS   B 1 90  ? 47.076 -8.160  -10.732 1.00 21.69 ?  90  LYS   B HG2  1 
ATOM   5317 H  HG3  . LYS   B 1 90  ? 47.402 -8.521  -9.221  1.00 21.69 ?  90  LYS   B HG3  1 
ATOM   5318 H  HD2  . LYS   B 1 90  ? 49.587 -7.853  -9.496  1.00 23.52 ?  90  LYS   B HD2  1 
ATOM   5319 H  HD3  . LYS   B 1 90  ? 49.340 -7.609  -11.055 1.00 23.52 ?  90  LYS   B HD3  1 
ATOM   5320 H  HE2  . LYS   B 1 90  ? 47.847 -5.908  -10.563 1.00 24.97 ?  90  LYS   B HE2  1 
ATOM   5321 H  HE3  . LYS   B 1 90  ? 48.041 -6.171  -9.006  1.00 24.97 ?  90  LYS   B HE3  1 
ATOM   5322 H  HZ1  . LYS   B 1 90  ? 49.283 -4.403  -9.675  1.00 23.77 ?  90  LYS   B HZ1  1 
ATOM   5323 H  HZ2  . LYS   B 1 90  ? 50.178 -5.449  -9.223  1.00 23.77 ?  90  LYS   B HZ2  1 
ATOM   5324 H  HZ3  . LYS   B 1 90  ? 50.001 -5.209  -10.641 1.00 23.77 ?  90  LYS   B HZ3  1 
ATOM   5325 N  N    . HIS   B 1 91  ? 47.843 -11.332 -7.759  1.00 14.38 ?  91  HIS   B N    1 
ATOM   5326 C  CA   . HIS   B 1 91  ? 47.381 -11.356 -6.385  1.00 14.22 ?  91  HIS   B CA   1 
ATOM   5327 C  C    . HIS   B 1 91  ? 47.388 -12.783 -5.868  1.00 13.94 ?  91  HIS   B C    1 
ATOM   5328 O  O    . HIS   B 1 91  ? 47.149 -13.742 -6.618  1.00 14.58 ?  91  HIS   B O    1 
ATOM   5329 C  CB   . HIS   B 1 91  ? 45.919 -10.880 -6.268  1.00 15.52 ?  91  HIS   B CB   1 
ATOM   5330 C  CG   . HIS   B 1 91  ? 45.702 -9.471  -6.700  1.00 18.97 ?  91  HIS   B CG   1 
ATOM   5331 N  ND1  . HIS   B 1 91  ? 46.314 -8.400  -6.086  1.00 21.13 ?  91  HIS   B ND1  1 
ATOM   5332 C  CD2  . HIS   B 1 91  ? 44.923 -8.953  -7.675  1.00 21.09 ?  91  HIS   B CD2  1 
ATOM   5333 C  CE1  . HIS   B 1 91  ? 45.932 -7.280  -6.674  1.00 22.16 ?  91  HIS   B CE1  1 
ATOM   5334 N  NE2  . HIS   B 1 91  ? 45.080 -7.588  -7.637  1.00 22.62 ?  91  HIS   B NE2  1 
ATOM   5335 H  H    . HIS   B 1 91  ? 47.432 -11.898 -8.261  1.00 17.31 ?  91  HIS   B H    1 
ATOM   5336 H  HA   . HIS   B 1 91  ? 47.945 -10.797 -5.822  1.00 17.12 ?  91  HIS   B HA   1 
ATOM   5337 H  HB2  . HIS   B 1 91  ? 45.358 -11.445 -6.823  1.00 18.68 ?  91  HIS   B HB2  1 
ATOM   5338 H  HB3  . HIS   B 1 91  ? 45.636 -10.950 -5.341  1.00 18.68 ?  91  HIS   B HB3  1 
ATOM   5339 H  HD1  . HIS   B 1 91  ? 46.868 -8.451  -5.426  1.00 25.41 ?  91  HIS   B HD1  1 
ATOM   5340 H  HD2  . HIS   B 1 91  ? 44.383 -9.423  -8.264  1.00 25.36 ?  91  HIS   B HD2  1 
ATOM   5341 H  HE1  . HIS   B 1 91  ? 46.214 -6.422  -6.444  1.00 26.64 ?  91  HIS   B HE1  1 
ATOM   5342 N  N    . CYS   B 1 92  ? 47.566 -12.911 -4.561  1.00 13.98 ?  92  CYS   B N    1 
ATOM   5343 C  CA   . CYS   B 1 92  ? 47.244 -14.145 -3.853  1.00 13.87 ?  92  CYS   B CA   1 
ATOM   5344 C  C    . CYS   B 1 92  ? 46.022 -13.903 -2.979  1.00 13.63 ?  92  CYS   B C    1 
ATOM   5345 O  O    . CYS   B 1 92  ? 46.020 -12.990 -2.141  1.00 14.80 ?  92  CYS   B O    1 
ATOM   5346 C  CB   . CYS   B 1 92  ? 48.415 -14.605 -2.994  1.00 13.84 ?  92  CYS   B CB   1 
ATOM   5347 S  SG   . CYS   B 1 92  ? 48.060 -16.136 -2.086  1.00 14.55 ?  92  CYS   B SG   1 
ATOM   5348 H  H    . CYS   B 1 92  ? 47.893 -12.293 -4.060  1.00 16.83 ?  92  CYS   B H    1 
ATOM   5349 H  HA   . CYS   B 1 92  ? 47.044 -14.840 -4.501  1.00 16.69 ?  92  CYS   B HA   1 
ATOM   5350 H  HB2  . CYS   B 1 92  ? 49.184 -14.761 -3.562  1.00 16.66 ?  92  CYS   B HB2  1 
ATOM   5351 H  HB3  . CYS   B 1 92  ? 48.616 -13.911 -2.346  1.00 16.66 ?  92  CYS   B HB3  1 
ATOM   5352 H  HG   . CYS   B 1 92  ? 49.035 -16.440 -1.463  1.00 17.51 ?  92  CYS   B HG   1 
ATOM   5353 N  N    . LEU   B 1 93  ? 44.990 -14.715 -3.180  1.00 13.45 ?  93  LEU   B N    1 
ATOM   5354 C  CA   . LEU   B 1 93  ? 43.810 -14.714 -2.325  1.00 13.73 ?  93  LEU   B CA   1 
ATOM   5355 C  C    . LEU   B 1 93  ? 44.035 -15.777 -1.258  1.00 12.85 ?  93  LEU   B C    1 
ATOM   5356 O  O    . LEU   B 1 93  ? 43.986 -16.978 -1.549  1.00 13.40 ?  93  LEU   B O    1 
ATOM   5357 C  CB   . LEU   B 1 93  ? 42.556 -15.010 -3.139  1.00 14.42 ?  93  LEU   B CB   1 
ATOM   5358 C  CG   . LEU   B 1 93  ? 41.257 -15.022 -2.330  1.00 14.96 ?  93  LEU   B CG   1 
ATOM   5359 C  CD1  . LEU   B 1 93  ? 40.896 -13.628 -1.844  1.00 15.57 ?  93  LEU   B CD1  1 
ATOM   5360 C  CD2  . LEU   B 1 93  ? 40.133 -15.622 -3.154  1.00 14.74 ?  93  LEU   B CD2  1 
ATOM   5361 H  H    . LEU   B 1 93  ? 44.955 -15.305 -3.816  1.00 16.20 ?  93  LEU   B H    1 
ATOM   5362 H  HA   . LEU   B 1 93  ? 43.716 -13.852 -1.900  1.00 16.53 ?  93  LEU   B HA   1 
ATOM   5363 H  HB2  . LEU   B 1 93  ? 42.463 -14.329 -3.825  1.00 17.36 ?  93  LEU   B HB2  1 
ATOM   5364 H  HB3  . LEU   B 1 93  ? 42.649 -15.880 -3.555  1.00 17.36 ?  93  LEU   B HB3  1 
ATOM   5365 H  HG   . LEU   B 1 93  ? 41.375 -15.583 -1.549  1.00 18.00 ?  93  LEU   B HG   1 
ATOM   5366 H  HD11 . LEU   B 1 93  ? 40.041 -13.658 -1.388  1.00 18.74 ?  93  LEU   B HD11 1 
ATOM   5367 H  HD12 . LEU   B 1 93  ? 41.585 -13.315 -1.236  1.00 18.74 ?  93  LEU   B HD12 1 
ATOM   5368 H  HD13 . LEU   B 1 93  ? 40.838 -13.030 -2.610  1.00 18.74 ?  93  LEU   B HD13 1 
ATOM   5369 H  HD21 . LEU   B 1 93  ? 39.314 -15.614 -2.632  1.00 17.75 ?  93  LEU   B HD21 1 
ATOM   5370 H  HD22 . LEU   B 1 93  ? 40.016 -15.105 -3.963  1.00 17.75 ?  93  LEU   B HD22 1 
ATOM   5371 H  HD23 . LEU   B 1 93  ? 40.363 -16.542 -3.381  1.00 17.75 ?  93  LEU   B HD23 1 
ATOM   5372 N  N    . HIS   B 1 94  ? 44.297 -15.350 -0.031  1.00 12.77 ?  94  HIS   B N    1 
ATOM   5373 C  CA   . HIS   B 1 94  ? 44.521 -16.256 1.090   1.00 12.99 ?  94  HIS   B CA   1 
ATOM   5374 C  C    . HIS   B 1 94  ? 43.158 -16.604 1.671   1.00 14.53 ?  94  HIS   B C    1 
ATOM   5375 O  O    . HIS   B 1 94  ? 42.483 -15.723 2.211   1.00 15.56 ?  94  HIS   B O    1 
ATOM   5376 C  CB   . HIS   B 1 94  ? 45.395 -15.586 2.148   1.00 13.46 ?  94  HIS   B CB   1 
ATOM   5377 C  CG   . HIS   B 1 94  ? 46.776 -15.280 1.678   1.00 13.65 ?  94  HIS   B CG   1 
ATOM   5378 N  ND1  . HIS   B 1 94  ? 47.803 -16.196 1.750   1.00 14.05 ?  94  HIS   B ND1  1 
ATOM   5379 C  CD2  . HIS   B 1 94  ? 47.289 -14.161 1.113   1.00 13.96 ?  94  HIS   B CD2  1 
ATOM   5380 C  CE1  . HIS   B 1 94  ? 48.895 -15.642 1.254   1.00 14.54 ?  94  HIS   B CE1  1 
ATOM   5381 N  NE2  . HIS   B 1 94  ? 48.610 -14.414 0.855   1.00 14.12 ?  94  HIS   B NE2  1 
ATOM   5382 H  H    . HIS   B 1 94  ? 44.351 -14.511 0.179   1.00 15.38 ?  94  HIS   B H    1 
ATOM   5383 H  HA   . HIS   B 1 94  ? 44.955 -17.061 0.777   1.00 15.64 ?  94  HIS   B HA   1 
ATOM   5384 H  HB2  . HIS   B 1 94  ? 44.979 -14.749 2.409   1.00 16.20 ?  94  HIS   B HB2  1 
ATOM   5385 H  HB3  . HIS   B 1 94  ? 45.462 -16.176 2.909   1.00 16.20 ?  94  HIS   B HB3  1 
ATOM   5386 H  HD2  . HIS   B 1 94  ? 46.831 -13.375 0.931   1.00 16.81 ?  94  HIS   B HD2  1 
ATOM   5387 H  HE1  . HIS   B 1 94  ? 49.726 -16.059 1.182   1.00 17.51 ?  94  HIS   B HE1  1 
ATOM   5388 H  HE2  . HIS   B 1 94  ? 49.167 -13.865 0.500   1.00 17.00 ?  94  HIS   B HE2  1 
ATOM   5389 N  N    . VAL   B 1 95  ? 42.726 -17.855 1.517   1.00 13.91 ?  95  VAL   B N    1 
ATOM   5390 C  CA   . VAL   B 1 95  ? 41.401 -18.294 1.952   1.00 14.22 ?  95  VAL   B CA   1 
ATOM   5391 C  C    . VAL   B 1 95  ? 41.570 -19.333 3.049   1.00 14.68 ?  95  VAL   B C    1 
ATOM   5392 O  O    . VAL   B 1 95  ? 42.342 -20.284 2.893   1.00 15.40 ?  95  VAL   B O    1 
ATOM   5393 C  CB   . VAL   B 1 95  ? 40.586 -18.904 0.796   1.00 14.00 ?  95  VAL   B CB   1 
ATOM   5394 C  CG1  . VAL   B 1 95  ? 39.223 -19.369 1.285   1.00 15.57 ?  95  VAL   B CG1  1 
ATOM   5395 C  CG2  . VAL   B 1 95  ? 40.452 -17.910 -0.336  1.00 14.14 ?  95  VAL   B CG2  1 
ATOM   5396 H  H    . VAL   B 1 95  ? 43.191 -18.482 1.149   1.00 16.74 ?  95  VAL   B H    1 
ATOM   5397 H  HA   . VAL   B 1 95  ? 40.909 -17.543 2.315   1.00 17.12 ?  95  VAL   B HA   1 
ATOM   5398 H  HB   . VAL   B 1 95  ? 41.058 -19.674 0.451   1.00 16.86 ?  95  VAL   B HB   1 
ATOM   5399 H  HG11 . VAL   B 1 95  ? 38.655 -19.542 0.516   1.00 18.74 ?  95  VAL   B HG11 1 
ATOM   5400 H  HG12 . VAL   B 1 95  ? 39.331 -20.182 1.802   1.00 18.74 ?  95  VAL   B HG12 1 
ATOM   5401 H  HG13 . VAL   B 1 95  ? 38.828 -18.674 1.834   1.00 18.74 ?  95  VAL   B HG13 1 
ATOM   5402 H  HG21 . VAL   B 1 95  ? 39.875 -18.289 -1.018  1.00 17.03 ?  95  VAL   B HG21 1 
ATOM   5403 H  HG22 . VAL   B 1 95  ? 40.056 -17.092 0.012   1.00 17.03 ?  95  VAL   B HG22 1 
ATOM   5404 H  HG23 . VAL   B 1 95  ? 41.327 -17.727 -0.701  1.00 17.03 ?  95  VAL   B HG23 1 
ATOM   5405 N  N    . VAL   B 1 96  ? 40.845 -19.159 4.148   1.00 14.88 ?  96  VAL   B N    1 
ATOM   5406 C  CA   . VAL   B 1 96  ? 40.931 -20.069 5.291   1.00 15.61 ?  96  VAL   B CA   1 
ATOM   5407 C  C    . VAL   B 1 96  ? 39.742 -21.025 5.244   1.00 16.71 ?  96  VAL   B C    1 
ATOM   5408 O  O    . VAL   B 1 96  ? 38.631 -20.667 5.641   1.00 16.66 ?  96  VAL   B O    1 
ATOM   5409 C  CB   . VAL   B 1 96  ? 40.974 -19.310 6.620   1.00 16.53 ?  96  VAL   B CB   1 
ATOM   5410 C  CG1  . VAL   B 1 96  ? 41.127 -20.293 7.777   1.00 16.78 ?  96  VAL   B CG1  1 
ATOM   5411 C  CG2  . VAL   B 1 96  ? 42.102 -18.296 6.625   1.00 16.32 ?  96  VAL   B CG2  1 
ATOM   5412 H  H    . VAL   B 1 96  ? 40.291 -18.515 4.263   1.00 17.91 ?  96  VAL   B H    1 
ATOM   5413 H  HA   . VAL   B 1 96  ? 41.746 -20.595 5.224   1.00 18.79 ?  96  VAL   B HA   1 
ATOM   5414 H  HB   . VAL   B 1 96  ? 40.139 -18.836 6.743   1.00 19.90 ?  96  VAL   B HB   1 
ATOM   5415 H  HG11 . VAL   B 1 96  ? 41.322 -19.800 8.590   1.00 20.19 ?  96  VAL   B HG11 1 
ATOM   5416 H  HG12 . VAL   B 1 96  ? 40.302 -20.793 7.886   1.00 20.19 ?  96  VAL   B HG12 1 
ATOM   5417 H  HG13 . VAL   B 1 96  ? 41.858 -20.903 7.581   1.00 20.19 ?  96  VAL   B HG13 1 
ATOM   5418 H  HG21 . VAL   B 1 96  ? 42.155 -17.881 7.502   1.00 19.63 ?  96  VAL   B HG21 1 
ATOM   5419 H  HG22 . VAL   B 1 96  ? 42.937 -18.744 6.421   1.00 19.63 ?  96  VAL   B HG22 1 
ATOM   5420 H  HG23 . VAL   B 1 96  ? 41.920 -17.617 5.953   1.00 19.63 ?  96  VAL   B HG23 1 
ATOM   5421 N  N    . GLY   B 1 97  ? 39.971 -22.254 4.779   1.00 16.63 ?  97  GLY   B N    1 
ATOM   5422 C  CA   . GLY   B 1 97  ? 39.008 -23.317 4.945   1.00 17.71 ?  97  GLY   B CA   1 
ATOM   5423 C  C    . GLY   B 1 97  ? 39.153 -23.925 6.322   1.00 19.35 ?  97  GLY   B C    1 
ATOM   5424 O  O    . GLY   B 1 97  ? 40.190 -23.781 6.979   1.00 19.60 ?  97  GLY   B O    1 
ATOM   5425 H  H    . GLY   B 1 97  ? 40.686 -22.484 4.351   1.00 20.02 ?  97  GLY   B H    1 
ATOM   5426 H  HA2  . GLY   B 1 97  ? 38.114 -22.957 4.845   1.00 21.30 ?  97  GLY   B HA2  1 
ATOM   5427 H  HA3  . GLY   B 1 97  ? 39.154 -24.000 4.274   1.00 21.30 ?  97  GLY   B HA3  1 
ATOM   5428 N  N    . PRO   B 1 98  ? 38.117 -24.615 6.790   1.00 20.43 ?  98  PRO   B N    1 
ATOM   5429 C  CA   . PRO   B 1 98  ? 38.224 -25.309 8.078   1.00 21.32 ?  98  PRO   B CA   1 
ATOM   5430 C  C    . PRO   B 1 98  ? 39.252 -26.427 8.027   1.00 21.24 ?  98  PRO   B C    1 
ATOM   5431 O  O    . PRO   B 1 98  ? 39.356 -27.153 7.039   1.00 21.22 ?  98  PRO   B O    1 
ATOM   5432 C  CB   . PRO   B 1 98  ? 36.810 -25.857 8.307   1.00 21.13 ?  98  PRO   B CB   1 
ATOM   5433 C  CG   . PRO   B 1 98  ? 36.207 -25.947 6.955   1.00 20.80 ?  98  PRO   B CG   1 
ATOM   5434 C  CD   . PRO   B 1 98  ? 36.785 -24.788 6.184   1.00 20.30 ?  98  PRO   B CD   1 
ATOM   5435 H  HA   . PRO   B 1 98  ? 38.456 -24.693 8.784   1.00 25.64 ?  98  PRO   B HA   1 
ATOM   5436 H  HB2  . PRO   B 1 98  ? 36.862 -26.736 8.719   1.00 25.41 ?  98  PRO   B HB2  1 
ATOM   5437 H  HB3  . PRO   B 1 98  ? 36.313 -25.245 8.865   1.00 25.41 ?  98  PRO   B HB3  1 
ATOM   5438 H  HG2  . PRO   B 1 98  ? 36.454 -26.795 6.547   1.00 25.02 ?  98  PRO   B HG2  1 
ATOM   5439 H  HG3  . PRO   B 1 98  ? 35.245 -25.869 7.026   1.00 25.02 ?  98  PRO   B HG3  1 
ATOM   5440 H  HD2  . PRO   B 1 98  ? 36.866 -25.018 5.243   1.00 24.41 ?  98  PRO   B HD2  1 
ATOM   5441 H  HD3  . PRO   B 1 98  ? 36.254 -23.994 6.316   1.00 24.41 ?  98  PRO   B HD3  1 
ATOM   5442 N  N    . ASN   B 1 99  ? 40.024 -26.545 9.105   1.00 23.04 ?  99  ASN   B N    1 
ATOM   5443 C  CA   . ASN   B 1 99  ? 41.017 -27.607 9.272   1.00 24.38 ?  99  ASN   B CA   1 
ATOM   5444 C  C    . ASN   B 1 99  ? 40.413 -28.680 10.172  1.00 27.44 ?  99  ASN   B C    1 
ATOM   5445 O  O    . ASN   B 1 99  ? 40.378 -28.531 11.396  1.00 28.60 ?  99  ASN   B O    1 
ATOM   5446 C  CB   . ASN   B 1 99  ? 42.289 -27.040 9.892   1.00 24.38 ?  99  ASN   B CB   1 
ATOM   5447 C  CG   . ASN   B 1 99  ? 43.439 -28.031 9.886   1.00 24.72 ?  99  ASN   B CG   1 
ATOM   5448 O  OD1  . ASN   B 1 99  ? 43.250 -29.218 10.109  1.00 25.34 ?  99  ASN   B OD1  1 
ATOM   5449 N  ND2  . ASN   B 1 99  ? 44.636 -27.543 9.623   1.00 24.59 ?  99  ASN   B ND2  1 
ATOM   5450 H  H    . ASN   B 1 99  ? 39.992 -26.007 9.770   1.00 27.71 ?  99  ASN   B H    1 
ATOM   5451 H  HA   . ASN   B 1 99  ? 41.229 -28.011 8.416   1.00 29.31 ?  99  ASN   B HA   1 
ATOM   5452 H  HB2  . ASN   B 1 99  ? 42.560 -26.264 9.391   1.00 29.31 ?  99  ASN   B HB2  1 
ATOM   5453 H  HB3  . ASN   B 1 99  ? 42.101 -26.797 10.816  1.00 29.31 ?  99  ASN   B HB3  1 
ATOM   5454 H  HD21 . ASN   B 1 99  ? 45.317 -28.061 9.608   1.00 29.57 ?  99  ASN   B HD21 1 
ATOM   5455 H  HD22 . ASN   B 1 99  ? 44.724 -26.702 9.467   1.00 29.57 ?  99  ASN   B HD22 1 
ATOM   5456 N  N    . VAL   B 1 100 ? 39.951 -29.774 9.563   1.00 30.19 ?  100 VAL   B N    1 
ATOM   5457 C  CA   . VAL   B 1 100 ? 39.329 -30.844 10.338  1.00 33.19 ?  100 VAL   B CA   1 
ATOM   5458 C  C    . VAL   B 1 100 ? 40.344 -31.501 11.266  1.00 34.37 ?  100 VAL   B C    1 
ATOM   5459 O  O    . VAL   B 1 100 ? 39.990 -31.961 12.359  1.00 34.87 ?  100 VAL   B O    1 
ATOM   5460 C  CB   . VAL   B 1 100 ? 38.636 -31.850 9.400   1.00 34.98 ?  100 VAL   B CB   1 
ATOM   5461 C  CG1  . VAL   B 1 100 ? 38.196 -33.089 10.162  1.00 35.53 ?  100 VAL   B CG1  1 
ATOM   5462 C  CG2  . VAL   B 1 100 ? 37.440 -31.188 8.723   1.00 35.49 ?  100 VAL   B CG2  1 
ATOM   5463 H  H    . VAL   B 1 100 ? 39.985 -29.917 8.718   1.00 36.28 ?  100 VAL   B H    1 
ATOM   5464 H  HA   . VAL   B 1 100 ? 38.634 -30.455 10.895  1.00 39.88 ?  100 VAL   B HA   1 
ATOM   5465 H  HB   . VAL   B 1 100 ? 39.259 -32.128 8.711   1.00 42.04 ?  100 VAL   B HB   1 
ATOM   5466 H  HG11 . VAL   B 1 100 ? 37.571 -33.590 9.612   1.00 42.69 ?  100 VAL   B HG11 1 
ATOM   5467 H  HG12 . VAL   B 1 100 ? 38.972 -33.637 10.357  1.00 42.69 ?  100 VAL   B HG12 1 
ATOM   5468 H  HG13 . VAL   B 1 100 ? 37.763 -32.817 10.986  1.00 42.69 ?  100 VAL   B HG13 1 
ATOM   5469 H  HG21 . VAL   B 1 100 ? 37.009 -31.834 8.142   1.00 42.65 ?  100 VAL   B HG21 1 
ATOM   5470 H  HG22 . VAL   B 1 100 ? 36.818 -30.890 9.405   1.00 42.65 ?  100 VAL   B HG22 1 
ATOM   5471 H  HG23 . VAL   B 1 100 ? 37.752 -30.431 8.205   1.00 42.65 ?  100 VAL   B HG23 1 
ATOM   5472 N  N    A ASN   B 1 101 ? 41.615 -31.556 10.863  0.66 34.49 ?  101 ASN   B N    1 
ATOM   5473 N  N    B ASN   B 1 101 ? 41.610 -31.570 10.847  0.34 35.17 ?  101 ASN   B N    1 
ATOM   5474 C  CA   A ASN   B 1 101 ? 42.645 -32.086 11.751  0.66 35.33 ?  101 ASN   B CA   1 
ATOM   5475 C  CA   B ASN   B 1 101 ? 42.662 -32.087 11.715  0.34 36.25 ?  101 ASN   B CA   1 
ATOM   5476 C  C    A ASN   B 1 101 ? 42.844 -31.221 12.989  0.66 37.38 ?  101 ASN   B C    1 
ATOM   5477 C  C    B ASN   B 1 101 ? 42.889 -31.212 12.940  0.34 37.96 ?  101 ASN   B C    1 
ATOM   5478 O  O    A ASN   B 1 101 ? 43.489 -31.673 13.943  0.66 37.72 ?  101 ASN   B O    1 
ATOM   5479 O  O    B ASN   B 1 101 ? 43.608 -31.630 13.855  0.34 38.00 ?  101 ASN   B O    1 
ATOM   5480 C  CB   A ASN   B 1 101 ? 43.969 -32.251 11.001  0.66 34.49 ?  101 ASN   B CB   1 
ATOM   5481 C  CB   B ASN   B 1 101 ? 43.967 -32.253 10.929  0.34 35.67 ?  101 ASN   B CB   1 
ATOM   5482 C  CG   A ASN   B 1 101 ? 43.929 -33.385 9.994   0.66 33.83 ?  101 ASN   B CG   1 
ATOM   5483 C  CG   B ASN   B 1 101 ? 43.896 -33.379 9.914   0.34 35.26 ?  101 ASN   B CG   1 
ATOM   5484 O  OD1  A ASN   B 1 101 ? 43.236 -34.379 10.195  0.66 34.13 ?  101 ASN   B OD1  1 
ATOM   5485 O  OD1  B ASN   B 1 101 ? 43.178 -34.359 10.108  0.34 35.27 ?  101 ASN   B OD1  1 
ATOM   5486 N  ND2  A ASN   B 1 101 ? 44.672 -33.239 8.904   0.66 33.23 ?  101 ASN   B ND2  1 
ATOM   5487 N  ND2  B ASN   B 1 101 ? 44.645 -33.244 8.826   0.34 34.95 ?  101 ASN   B ND2  1 
ATOM   5488 H  H    A ASN   B 1 101 ? 41.897 -31.303 10.093  0.66 41.44 ?  101 ASN   B H    1 
ATOM   5489 H  H    B ASN   B 1 101 ? 41.875 -31.333 10.066  0.34 42.25 ?  101 ASN   B H    1 
ATOM   5490 H  HA   A ASN   B 1 101 ? 42.368 -32.966 12.049  0.66 42.45 ?  101 ASN   B HA   1 
ATOM   5491 H  HA   B ASN   B 1 101 ? 42.397 -32.962 12.029  0.34 43.56 ?  101 ASN   B HA   1 
ATOM   5492 H  HB2  A ASN   B 1 101 ? 44.170 -31.433 10.525  0.66 41.44 ?  101 ASN   B HB2  1 
ATOM   5493 H  HB2  B ASN   B 1 101 ? 44.161 -31.433 10.451  0.34 42.86 ?  101 ASN   B HB2  1 
ATOM   5494 H  HB3  A ASN   B 1 101 ? 44.672 -32.444 11.643  0.66 41.44 ?  101 ASN   B HB3  1 
ATOM   5495 H  HB3  B ASN   B 1 101 ? 44.685 -32.454 11.549  0.34 42.86 ?  101 ASN   B HB3  1 
ATOM   5496 H  HD21 A ASN   B 1 101 ? 44.681 -33.855 8.304   0.66 39.93 ?  101 ASN   B HD21 1 
ATOM   5497 H  HD21 B ASN   B 1 101 ? 44.640 -33.856 8.221   0.34 42.00 ?  101 ASN   B HD21 1 
ATOM   5498 H  HD22 A ASN   B 1 101 ? 45.142 -32.527 8.798   0.66 39.93 ?  101 ASN   B HD22 1 
ATOM   5499 H  HD22 B ASN   B 1 101 ? 45.135 -32.544 8.726   0.34 42.00 ?  101 ASN   B HD22 1 
ATOM   5500 N  N    A LYS   B 1 102 ? 42.321 -29.995 12.990  0.66 39.73 ?  102 LYS   B N    1 
ATOM   5501 N  N    B LYS   B 1 102 ? 42.305 -30.014 12.977  0.34 39.93 ?  102 LYS   B N    1 
ATOM   5502 C  CA   A LYS   B 1 102 ? 42.274 -29.145 14.171  0.66 42.12 ?  102 LYS   B CA   1 
ATOM   5503 C  CA   B LYS   B 1 102 ? 42.284 -29.177 14.170  0.34 41.87 ?  102 LYS   B CA   1 
ATOM   5504 C  C    A LYS   B 1 102 ? 40.893 -29.123 14.815  0.66 41.96 ?  102 LYS   B C    1 
ATOM   5505 C  C    B LYS   B 1 102 ? 40.901 -29.127 14.809  0.34 41.83 ?  102 LYS   B C    1 
ATOM   5506 O  O    A LYS   B 1 102 ? 40.644 -28.292 15.694  0.66 41.77 ?  102 LYS   B O    1 
ATOM   5507 O  O    B LYS   B 1 102 ? 40.660 -28.286 15.681  0.34 41.82 ?  102 LYS   B O    1 
ATOM   5508 C  CB   A LYS   B 1 102 ? 42.685 -27.715 13.816  0.66 44.65 ?  102 LYS   B CB   1 
ATOM   5509 C  CB   B LYS   B 1 102 ? 42.762 -27.761 13.843  0.34 43.58 ?  102 LYS   B CB   1 
ATOM   5510 C  CG   A LYS   B 1 102 ? 44.147 -27.532 13.456  0.66 47.06 ?  102 LYS   B CG   1 
ATOM   5511 C  CG   B LYS   B 1 102 ? 44.231 -27.663 13.464  0.34 45.29 ?  102 LYS   B CG   1 
ATOM   5512 C  CD   A LYS   B 1 102 ? 44.411 -26.082 13.080  0.66 48.78 ?  102 LYS   B CD   1 
ATOM   5513 C  CD   B LYS   B 1 102 ? 44.603 -26.235 13.099  0.34 46.48 ?  102 LYS   B CD   1 
ATOM   5514 C  CE   A LYS   B 1 102 ? 45.877 -25.817 12.798  0.66 50.18 ?  102 LYS   B CE   1 
ATOM   5515 C  CE   B LYS   B 1 102 ? 46.091 -26.091 12.829  0.34 47.58 ?  102 LYS   B CE   1 
ATOM   5516 N  NZ   A LYS   B 1 102 ? 46.101 -24.396 12.403  0.66 50.87 ?  102 LYS   B NZ   1 
ATOM   5517 N  NZ   B LYS   B 1 102 ? 46.446 -24.699 12.431  0.34 48.12 ?  102 LYS   B NZ   1 
ATOM   5518 H  H    A LYS   B 1 102 ? 41.983 -29.626 12.293  0.66 47.73 ?  102 LYS   B H    1 
ATOM   5519 H  H    B LYS   B 1 102 ? 41.904 -29.659 12.306  0.34 47.97 ?  102 LYS   B H    1 
ATOM   5520 H  HA   A LYS   B 1 102 ? 42.904 -29.481 14.826  0.66 50.60 ?  102 LYS   B HA   1 
ATOM   5521 H  HA   B LYS   B 1 102 ? 42.896 -29.548 14.822  0.34 50.30 ?  102 LYS   B HA   1 
ATOM   5522 H  HB2  A LYS   B 1 102 ? 42.158 -27.423 13.057  0.66 53.63 ?  102 LYS   B HB2  1 
ATOM   5523 H  HB2  B LYS   B 1 102 ? 42.243 -27.421 13.099  0.34 52.36 ?  102 LYS   B HB2  1 
ATOM   5524 H  HB3  A LYS   B 1 102 ? 42.500 -27.143 14.578  0.66 53.63 ?  102 LYS   B HB3  1 
ATOM   5525 H  HB3  B LYS   B 1 102 ? 42.623 -27.199 14.622  0.34 52.36 ?  102 LYS   B HB3  1 
ATOM   5526 H  HG2  A LYS   B 1 102 ? 44.702 -27.758 14.219  0.66 56.53 ?  102 LYS   B HG2  1 
ATOM   5527 H  HG2  B LYS   B 1 102 ? 44.779 -27.938 14.217  0.34 54.41 ?  102 LYS   B HG2  1 
ATOM   5528 H  HG3  A LYS   B 1 102 ? 44.368 -28.093 12.696  0.66 56.53 ?  102 LYS   B HG3  1 
ATOM   5529 H  HG3  B LYS   B 1 102 ? 44.405 -28.230 12.696  0.34 54.41 ?  102 LYS   B HG3  1 
ATOM   5530 H  HD2  A LYS   B 1 102 ? 43.905 -25.865 12.281  0.66 58.60 ?  102 LYS   B HD2  1 
ATOM   5531 H  HD2  B LYS   B 1 102 ? 44.122 -25.975 12.297  0.34 55.84 ?  102 LYS   B HD2  1 
ATOM   5532 H  HD3  A LYS   B 1 102 ? 44.136 -25.509 13.813  0.66 58.60 ?  102 LYS   B HD3  1 
ATOM   5533 H  HD3  B LYS   B 1 102 ? 44.369 -25.646 13.834  0.34 55.84 ?  102 LYS   B HD3  1 
ATOM   5534 H  HE2  A LYS   B 1 102 ? 46.396 -25.996 13.598  0.66 60.27 ?  102 LYS   B HE2  1 
ATOM   5535 H  HE2  B LYS   B 1 102 ? 46.585 -26.312 13.634  0.34 57.16 ?  102 LYS   B HE2  1 
ATOM   5536 H  HE3  A LYS   B 1 102 ? 46.172 -26.386 12.070  0.66 60.27 ?  102 LYS   B HE3  1 
ATOM   5537 H  HE3  B LYS   B 1 102 ? 46.344 -26.687 12.107  0.34 57.16 ?  102 LYS   B HE3  1 
ATOM   5538 H  HZ1  A LYS   B 1 102 ? 46.964 -24.257 12.241  0.66 61.10 ?  102 LYS   B HZ1  1 
ATOM   5539 H  HZ1  B LYS   B 1 102 ? 47.321 -24.640 12.279  0.34 57.80 ?  102 LYS   B HZ1  1 
ATOM   5540 H  HZ2  A LYS   B 1 102 ? 45.634 -24.208 11.668  0.66 61.10 ?  102 LYS   B HZ2  1 
ATOM   5541 H  HZ2  B LYS   B 1 102 ? 46.007 -24.474 11.690  0.34 57.80 ?  102 LYS   B HZ2  1 
ATOM   5542 H  HZ3  A LYS   B 1 102 ? 45.838 -23.854 13.058  0.66 61.10 ?  102 LYS   B HZ3  1 
ATOM   5543 H  HZ3  B LYS   B 1 102 ? 46.227 -24.132 13.081  0.34 57.80 ?  102 LYS   B HZ3  1 
ATOM   5544 N  N    . GLY   B 1 103 ? 39.987 -30.002 14.390  1.00 41.93 ?  103 GLY   B N    1 
ATOM   5545 C  CA   . GLY   B 1 103 ? 38.658 -30.069 14.961  1.00 42.19 ?  103 GLY   B CA   1 
ATOM   5546 C  C    . GLY   B 1 103 ? 37.676 -29.038 14.450  1.00 42.24 ?  103 GLY   B C    1 
ATOM   5547 O  O    . GLY   B 1 103 ? 36.530 -29.021 14.917  1.00 42.36 ?  103 GLY   B O    1 
ATOM   5548 H  H    A GLY   B 1 103 ? 40.126 -30.573 13.763  0.66 50.37 ?  103 GLY   B H    1 
ATOM   5549 H  H    B GLY   B 1 103 ? 40.122 -30.576 13.765  0.34 50.37 ?  103 GLY   B H    1 
ATOM   5550 H  HA2  . GLY   B 1 103 ? 38.289 -30.951 14.789  1.00 50.68 ?  103 GLY   B HA2  1 
ATOM   5551 H  HA3  . GLY   B 1 103 ? 38.722 -29.956 15.921  1.00 50.68 ?  103 GLY   B HA3  1 
ATOM   5552 N  N    . GLU   B 1 104 ? 38.075 -28.185 13.510  1.00 41.35 ?  104 GLU   B N    1 
ATOM   5553 C  CA   . GLU   B 1 104 ? 37.208 -27.115 13.042  1.00 40.24 ?  104 GLU   B CA   1 
ATOM   5554 C  C    . GLU   B 1 104 ? 36.020 -27.675 12.261  1.00 40.20 ?  104 GLU   B C    1 
ATOM   5555 O  O    . GLU   B 1 104 ? 36.048 -28.796 11.743  1.00 40.27 ?  104 GLU   B O    1 
ATOM   5556 C  CB   . GLU   B 1 104 ? 38.010 -26.114 12.210  1.00 39.08 ?  104 GLU   B CB   1 
ATOM   5557 C  CG   . GLU   B 1 104 ? 39.103 -25.435 13.025  1.00 37.77 ?  104 GLU   B CG   1 
ATOM   5558 C  CD   . GLU   B 1 104 ? 40.030 -24.567 12.195  1.00 36.23 ?  104 GLU   B CD   1 
ATOM   5559 O  OE1  . GLU   B 1 104 ? 39.996 -24.662 10.951  1.00 34.96 ?  104 GLU   B OE1  1 
ATOM   5560 O  OE2  . GLU   B 1 104 ? 40.798 -23.787 12.796  1.00 36.20 -1 104 GLU   B OE2  1 
ATOM   5561 H  H    . GLU   B 1 104 ? 38.848 -28.201 13.135  1.00 49.67 ?  104 GLU   B H    1 
ATOM   5562 H  HA   . GLU   B 1 104 ? 36.857 -26.642 13.810  1.00 48.34 ?  104 GLU   B HA   1 
ATOM   5563 H  HB2  . GLU   B 1 104 ? 38.429 -26.579 11.469  1.00 46.96 ?  104 GLU   B HB2  1 
ATOM   5564 H  HB3  . GLU   B 1 104 ? 37.411 -25.427 11.877  1.00 46.96 ?  104 GLU   B HB3  1 
ATOM   5565 H  HG2  . GLU   B 1 104 ? 38.689 -24.870 13.696  1.00 45.38 ?  104 GLU   B HG2  1 
ATOM   5566 H  HG3  . GLU   B 1 104 ? 39.643 -26.117 13.456  1.00 45.38 ?  104 GLU   B HG3  1 
ATOM   5567 N  N    A ASP   B 1 105 ? 34.963 -26.867 12.184  0.66 40.15 ?  105 ASP   B N    1 
ATOM   5568 N  N    B ASP   B 1 105 ? 34.965 -26.867 12.169  0.34 40.49 ?  105 ASP   B N    1 
ATOM   5569 C  CA   A ASP   B 1 105 ? 33.688 -27.308 11.634  0.66 39.99 ?  105 ASP   B CA   1 
ATOM   5570 C  CA   B ASP   B 1 105 ? 33.703 -27.317 11.594  0.34 40.40 ?  105 ASP   B CA   1 
ATOM   5571 C  C    A ASP   B 1 105 ? 33.760 -27.345 10.112  0.66 38.07 ?  105 ASP   B C    1 
ATOM   5572 C  C    B ASP   B 1 105 ? 33.801 -27.337 10.072  0.34 39.00 ?  105 ASP   B C    1 
ATOM   5573 O  O    A ASP   B 1 105 ? 33.994 -26.316 9.469   0.66 37.29 ?  105 ASP   B O    1 
ATOM   5574 O  O    B ASP   B 1 105 ? 34.044 -26.301 9.444   0.34 38.86 ?  105 ASP   B O    1 
ATOM   5575 C  CB   A ASP   B 1 105 ? 32.580 -26.359 12.085  0.66 41.58 ?  105 ASP   B CB   1 
ATOM   5576 C  CB   B ASP   B 1 105 ? 32.563 -26.406 12.044  0.34 41.60 ?  105 ASP   B CB   1 
ATOM   5577 C  CG   A ASP   B 1 105 ? 31.210 -26.800 11.611  0.66 42.91 ?  105 ASP   B CG   1 
ATOM   5578 C  CG   B ASP   B 1 105 ? 31.212 -26.871 11.537  0.34 42.48 ?  105 ASP   B CG   1 
ATOM   5579 O  OD1  A ASP   B 1 105 ? 31.086 -27.948 11.136  0.66 43.08 ?  105 ASP   B OD1  1 
ATOM   5580 O  OD1  B ASP   B 1 105 ? 31.120 -28.017 11.048  0.34 42.72 ?  105 ASP   B OD1  1 
ATOM   5581 O  OD2  A ASP   B 1 105 ? 30.260 -25.992 11.701  0.66 43.69 -1 105 ASP   B OD2  1 
ATOM   5582 O  OD2  B ASP   B 1 105 ? 30.243 -26.087 11.618  0.34 42.94 -1 105 ASP   B OD2  1 
ATOM   5583 H  H    A ASP   B 1 105 ? 34.962 -26.047 12.444  0.66 48.23 ?  105 ASP   B H    1 
ATOM   5584 H  H    B ASP   B 1 105 ? 34.957 -26.047 12.428  0.34 48.65 ?  105 ASP   B H    1 
ATOM   5585 H  HA   A ASP   B 1 105 ? 33.481 -28.200 11.957  0.66 48.05 ?  105 ASP   B HA   1 
ATOM   5586 H  HA   B ASP   B 1 105 ? 33.511 -28.217 11.898  0.34 48.53 ?  105 ASP   B HA   1 
ATOM   5587 H  HB2  A ASP   B 1 105 ? 32.584 -26.306 13.057  0.66 49.95 ?  105 ASP   B HB2  1 
ATOM   5588 H  HB2  B ASP   B 1 105 ? 32.537 -26.387 13.016  0.34 49.97 ?  105 ASP   B HB2  1 
ATOM   5589 H  HB3  A ASP   B 1 105 ? 32.738 -25.482 11.706  0.66 49.95 ?  105 ASP   B HB3  1 
ATOM   5590 H  HB3  B ASP   B 1 105 ? 32.709 -25.514 11.699  0.34 49.97 ?  105 ASP   B HB3  1 
ATOM   5591 N  N    A ILE   B 1 106 ? 33.541 -28.531 9.540   0.66 37.22 ?  106 ILE   B N    1 
ATOM   5592 N  N    B ILE   B 1 106 ? 33.605 -28.520 9.485   0.34 37.95 ?  106 ILE   B N    1 
ATOM   5593 C  CA   A ILE   B 1 106 ? 33.540 -28.697 8.092   0.66 36.14 ?  106 ILE   B CA   1 
ATOM   5594 C  CA   B ILE   B 1 106 ? 33.610 -28.673 8.035   0.34 36.81 ?  106 ILE   B CA   1 
ATOM   5595 C  C    A ILE   B 1 106 ? 32.452 -27.866 7.423   0.66 34.85 ?  106 ILE   B C    1 
ATOM   5596 C  C    B ILE   B 1 106 ? 32.504 -27.862 7.375   0.34 35.58 ?  106 ILE   B C    1 
ATOM   5597 O  O    A ILE   B 1 106 ? 32.537 -27.592 6.220   0.66 34.49 ?  106 ILE   B O    1 
ATOM   5598 O  O    B ILE   B 1 106 ? 32.571 -27.590 6.172   0.34 35.52 ?  106 ILE   B O    1 
ATOM   5599 C  CB   A ILE   B 1 106 ? 33.406 -30.198 7.749   0.66 36.46 ?  106 ILE   B CB   1 
ATOM   5600 C  CB   B ILE   B 1 106 ? 33.505 -30.173 7.676   0.34 37.00 ?  106 ILE   B CB   1 
ATOM   5601 C  CG1  A ILE   B 1 106 ? 33.645 -30.448 6.258   0.66 36.74 ?  106 ILE   B CG1  1 
ATOM   5602 C  CG1  B ILE   B 1 106 ? 33.748 -30.401 6.181   0.34 37.26 ?  106 ILE   B CG1  1 
ATOM   5603 C  CG2  A ILE   B 1 106 ? 32.037 -30.720 8.162   0.66 36.88 ?  106 ILE   B CG2  1 
ATOM   5604 C  CG2  B ILE   B 1 106 ? 32.144 -30.726 8.078   0.34 37.20 ?  106 ILE   B CG2  1 
ATOM   5605 C  CD1  A ILE   B 1 106 ? 35.019 -30.035 5.785   0.66 36.81 ?  106 ILE   B CD1  1 
ATOM   5606 C  CD1  B ILE   B 1 106 ? 35.096 -29.916 5.705   0.34 37.36 ?  106 ILE   B CD1  1 
ATOM   5607 H  H    A ILE   B 1 106 ? 33.400 -29.258 9.975   0.66 44.72 ?  106 ILE   B H    1 
ATOM   5608 H  H    B ILE   B 1 106 ? 33.477 -29.253 9.910   0.34 45.60 ?  106 ILE   B H    1 
ATOM   5609 H  HA   A ILE   B 1 106 ? 34.389 -28.389 7.749   0.66 43.43 ?  106 ILE   B HA   1 
ATOM   5610 H  HA   B ILE   B 1 106 ? 34.454 -28.341 7.697   0.34 44.22 ?  106 ILE   B HA   1 
ATOM   5611 H  HB   A ILE   B 1 106 ? 34.079 -30.682 8.249   0.66 43.80 ?  106 ILE   B HB   1 
ATOM   5612 H  HB   B ILE   B 1 106 ? 34.185 -30.654 8.170   0.34 44.45 ?  106 ILE   B HB   1 
ATOM   5613 H  HG12 A ILE   B 1 106 ? 33.549 -31.399 6.083   0.66 44.14 ?  106 ILE   B HG12 1 
ATOM   5614 H  HG12 B ILE   B 1 106 ? 33.699 -31.354 5.999   0.34 44.77 ?  106 ILE   B HG12 1 
ATOM   5615 H  HG13 A ILE   B 1 106 ? 32.991 -29.954 5.742   0.66 44.14 ?  106 ILE   B HG13 1 
ATOM   5616 H  HG13 B ILE   B 1 106 ? 33.067 -29.936 5.673   0.34 44.77 ?  106 ILE   B HG13 1 
ATOM   5617 H  HG21 A ILE   B 1 106 ? 32.031 -31.686 8.076   0.66 44.31 ?  106 ILE   B HG21 1 
ATOM   5618 H  HG21 B ILE   B 1 106 ? 32.157 -31.692 7.989   0.34 44.70 ?  106 ILE   B HG21 1 
ATOM   5619 H  HG22 A ILE   B 1 106 ? 31.868 -30.470 9.084   0.66 44.31 ?  106 ILE   B HG22 1 
ATOM   5620 H  HG22 B ILE   B 1 106 ? 31.965 -30.483 9.000   0.34 44.70 ?  106 ILE   B HG22 1 
ATOM   5621 H  HG23 A ILE   B 1 106 ? 31.360 -30.333 7.585   0.66 44.31 ?  106 ILE   B HG23 1 
ATOM   5622 H  HG23 B ILE   B 1 106 ? 31.463 -30.350 7.498   0.34 44.70 ?  106 ILE   B HG23 1 
ATOM   5623 H  HD11 A ILE   B 1 106 ? 35.185 -30.429 4.916   0.66 44.23 ?  106 ILE   B HD11 1 
ATOM   5624 H  HD11 B ILE   B 1 106 ? 35.281 -30.308 4.839   0.34 44.89 ?  106 ILE   B HD11 1 
ATOM   5625 H  HD12 A ILE   B 1 106 ? 35.053 -29.067 5.721   0.66 44.23 ?  106 ILE   B HD12 1 
ATOM   5626 H  HD12 B ILE   B 1 106 ? 35.075 -28.949 5.633   0.34 44.89 ?  106 ILE   B HD12 1 
ATOM   5627 H  HD13 A ILE   B 1 106 ? 35.680 -30.349 6.422   0.66 44.23 ?  106 ILE   B HD13 1 
ATOM   5628 H  HD13 B ILE   B 1 106 ? 35.772 -30.189 6.344   0.34 44.89 ?  106 ILE   B HD13 1 
ATOM   5629 N  N    A GLN   B 1 107 ? 31.429 -27.450 8.173   0.66 34.04 ?  107 GLN   B N    1 
ATOM   5630 N  N    B GLN   B 1 107 ? 31.480 -27.465 8.135   0.34 34.49 ?  107 GLN   B N    1 
ATOM   5631 C  CA   A GLN   B 1 107 ? 30.342 -26.672 7.587   0.66 33.53 ?  107 GLN   B CA   1 
ATOM   5632 C  CA   B GLN   B 1 107 ? 30.376 -26.703 7.561   0.34 33.56 ?  107 GLN   B CA   1 
ATOM   5633 C  C    A GLN   B 1 107 ? 30.817 -25.323 7.065   0.66 30.74 ?  107 GLN   B C    1 
ATOM   5634 C  C    B GLN   B 1 107 ? 30.820 -25.332 7.065   0.34 30.88 ?  107 GLN   B C    1 
ATOM   5635 O  O    A GLN   B 1 107 ? 30.179 -24.761 6.169   0.66 30.36 ?  107 GLN   B O    1 
ATOM   5636 O  O    B GLN   B 1 107 ? 30.159 -24.760 6.193   0.34 30.66 ?  107 GLN   B O    1 
ATOM   5637 C  CB   A GLN   B 1 107 ? 29.227 -26.474 8.621   0.66 36.15 ?  107 GLN   B CB   1 
ATOM   5638 C  CB   B GLN   B 1 107 ? 29.255 -26.555 8.594   0.34 35.35 ?  107 GLN   B CB   1 
ATOM   5639 C  CG   A GLN   B 1 107 ? 27.893 -26.006 8.045   0.66 38.71 ?  107 GLN   B CG   1 
ATOM   5640 C  CG   B GLN   B 1 107 ? 27.904 -26.152 8.015   0.34 37.14 ?  107 GLN   B CG   1 
ATOM   5641 C  CD   A GLN   B 1 107 ? 27.802 -24.497 7.912   0.66 40.59 ?  107 GLN   B CD   1 
ATOM   5642 C  CD   B GLN   B 1 107 ? 27.743 -24.649 7.880   0.34 38.48 ?  107 GLN   B CD   1 
ATOM   5643 O  OE1  A GLN   B 1 107 ? 28.624 -23.762 8.462   0.66 41.31 ?  107 GLN   B OE1  1 
ATOM   5644 O  OE1  B GLN   B 1 107 ? 28.490 -23.875 8.478   0.34 38.99 ?  107 GLN   B OE1  1 
ATOM   5645 N  NE2  A GLN   B 1 107 ? 26.795 -24.027 7.182   0.66 41.24 ?  107 GLN   B NE2  1 
ATOM   5646 N  NE2  B GLN   B 1 107 ? 26.759 -24.229 7.091   0.34 38.94 ?  107 GLN   B NE2  1 
ATOM   5647 H  H    A GLN   B 1 107 ? 31.343 -27.597 9.015   0.66 40.90 ?  107 GLN   B H    1 
ATOM   5648 H  H    B GLN   B 1 107 ? 31.404 -27.619 8.977   0.34 41.44 ?  107 GLN   B H    1 
ATOM   5649 H  HA   A GLN   B 1 107 ? 29.967 -27.168 6.842   0.66 40.29 ?  107 GLN   B HA   1 
ATOM   5650 H  HA   B GLN   B 1 107 ? 30.017 -27.196 6.807   0.34 40.33 ?  107 GLN   B HA   1 
ATOM   5651 H  HB2  A GLN   B 1 107 ? 29.070 -27.316 9.067   0.66 43.43 ?  107 GLN   B HB2  1 
ATOM   5652 H  HB2  B GLN   B 1 107 ? 29.136 -27.405 9.042   0.34 42.48 ?  107 GLN   B HB2  1 
ATOM   5653 H  HB3  A GLN   B 1 107 ? 29.517 -25.810 9.267   0.66 43.43 ?  107 GLN   B HB3  1 
ATOM   5654 H  HB3  B GLN   B 1 107 ? 29.514 -25.879 9.239   0.34 42.48 ?  107 GLN   B HB3  1 
ATOM   5655 H  HG2  A GLN   B 1 107 ? 27.775 -26.389 7.162   0.66 46.51 ?  107 GLN   B HG2  1 
ATOM   5656 H  HG2  B GLN   B 1 107 ? 27.805 -26.542 7.133   0.34 44.62 ?  107 GLN   B HG2  1 
ATOM   5657 H  HG3  A GLN   B 1 107 ? 27.175 -26.302 8.631   0.66 46.51 ?  107 GLN   B HG3  1 
ATOM   5658 H  HG3  B GLN   B 1 107 ? 27.200 -26.479 8.601   0.34 44.62 ?  107 GLN   B HG3  1 
ATOM   5659 H  HE21 A GLN   B 1 107 ? 26.240 -24.571 6.812   0.66 49.54 ?  107 GLN   B HE21 1 
ATOM   5660 H  HE21 B GLN   B 1 107 ? 26.257 -24.800 6.688   0.34 46.78 ?  107 GLN   B HE21 1 
ATOM   5661 H  HE22 A GLN   B 1 107 ? 26.697 -23.179 7.080   0.66 49.54 ?  107 GLN   B HE22 1 
ATOM   5662 H  HE22 B GLN   B 1 107 ? 26.624 -23.387 6.984   0.34 46.78 ?  107 GLN   B HE22 1 
ATOM   5663 N  N    . LEU   B 1 108 ? 31.925 -24.799 7.592   1.00 28.53 ?  108 LEU   B N    1 
ATOM   5664 C  CA   . LEU   B 1 108 ? 32.446 -23.502 7.163   1.00 24.97 ?  108 LEU   B CA   1 
ATOM   5665 C  C    . LEU   B 1 108 ? 33.101 -23.541 5.791   1.00 21.29 ?  108 LEU   B C    1 
ATOM   5666 O  O    . LEU   B 1 108 ? 33.543 -22.490 5.304   1.00 20.54 ?  108 LEU   B O    1 
ATOM   5667 C  CB   . LEU   B 1 108 ? 33.435 -22.968 8.199   1.00 25.56 ?  108 LEU   B CB   1 
ATOM   5668 C  CG   . LEU   B 1 108 ? 32.815 -22.430 9.490   1.00 27.36 ?  108 LEU   B CG   1 
ATOM   5669 C  CD1  . LEU   B 1 108 ? 33.826 -22.439 10.618  1.00 28.24 ?  108 LEU   B CD1  1 
ATOM   5670 C  CD2  . LEU   B 1 108 ? 32.279 -21.024 9.272   1.00 27.82 ?  108 LEU   B CD2  1 
ATOM   5671 H  H    A LEU   B 1 108 ? 32.385 -25.173 8.211   0.66 34.29 ?  108 LEU   B H    1 
ATOM   5672 H  H    B LEU   B 1 108 ? 32.384 -25.169 8.214   0.34 34.29 ?  108 LEU   B H    1 
ATOM   5673 H  HA   . LEU   B 1 108 ? 31.709 -22.877 7.114   1.00 30.02 ?  108 LEU   B HA   1 
ATOM   5674 H  HB2  . LEU   B 1 108 ? 34.037 -23.685 8.447   1.00 30.72 ?  108 LEU   B HB2  1 
ATOM   5675 H  HB3  . LEU   B 1 108 ? 33.938 -22.244 7.799   1.00 30.72 ?  108 LEU   B HB3  1 
ATOM   5676 H  HG   . LEU   B 1 108 ? 32.070 -22.996 9.749   1.00 32.88 ?  108 LEU   B HG   1 
ATOM   5677 H  HD11 . LEU   B 1 108 ? 33.386 -22.167 11.439  1.00 33.94 ?  108 LEU   B HD11 1 
ATOM   5678 H  HD12 . LEU   B 1 108 ? 34.183 -23.335 10.714  1.00 33.94 ?  108 LEU   B HD12 1 
ATOM   5679 H  HD13 . LEU   B 1 108 ? 34.540 -21.818 10.405  1.00 33.94 ?  108 LEU   B HD13 1 
ATOM   5680 H  HD21 . LEU   B 1 108 ? 31.889 -20.701 10.100  1.00 33.44 ?  108 LEU   B HD21 1 
ATOM   5681 H  HD22 . LEU   B 1 108 ? 33.011 -20.446 9.004   1.00 33.44 ?  108 LEU   B HD22 1 
ATOM   5682 H  HD23 . LEU   B 1 108 ? 31.604 -21.047 8.576   1.00 33.44 ?  108 LEU   B HD23 1 
ATOM   5683 N  N    . LEU   B 1 109 ? 33.164 -24.712 5.160   1.00 20.30 ?  109 LEU   B N    1 
ATOM   5684 C  CA   . LEU   B 1 109 ? 33.797 -24.822 3.853   1.00 18.94 ?  109 LEU   B CA   1 
ATOM   5685 C  C    . LEU   B 1 109 ? 33.033 -24.047 2.788   1.00 18.38 ?  109 LEU   B C    1 
ATOM   5686 O  O    . LEU   B 1 109 ? 33.649 -23.474 1.883   1.00 18.16 ?  109 LEU   B O    1 
ATOM   5687 C  CB   . LEU   B 1 109 ? 33.922 -26.298 3.477   1.00 18.63 ?  109 LEU   B CB   1 
ATOM   5688 C  CG   . LEU   B 1 109 ? 34.706 -26.655 2.218   1.00 17.96 ?  109 LEU   B CG   1 
ATOM   5689 C  CD1  . LEU   B 1 109 ? 36.074 -25.994 2.217   1.00 17.72 ?  109 LEU   B CD1  1 
ATOM   5690 C  CD2  . LEU   B 1 109 ? 34.846 -28.170 2.129   1.00 18.98 ?  109 LEU   B CD2  1 
ATOM   5691 H  H    . LEU   B 1 109 ? 32.856 -25.453 5.462   1.00 24.42 ?  109 LEU   B H    1 
ATOM   5692 H  HA   . LEU   B 1 109 ? 34.694 -24.453 3.902   1.00 22.79 ?  109 LEU   B HA   1 
ATOM   5693 H  HB2  . LEU   B 1 109 ? 34.350 -26.763 4.212   1.00 22.41 ?  109 LEU   B HB2  1 
ATOM   5694 H  HB3  . LEU   B 1 109 ? 33.024 -26.656 3.361   1.00 22.41 ?  109 LEU   B HB3  1 
ATOM   5695 H  HG   . LEU   B 1 109 ? 34.212 -26.362 1.433   1.00 21.61 ?  109 LEU   B HG   1 
ATOM   5696 H  HD11 . LEU   B 1 109 ? 36.604 -26.366 1.495   1.00 21.32 ?  109 LEU   B HD11 1 
ATOM   5697 H  HD12 . LEU   B 1 109 ? 35.958 -25.042 2.088   1.00 21.32 ?  109 LEU   B HD12 1 
ATOM   5698 H  HD13 . LEU   B 1 109 ? 36.505 -26.169 3.068   1.00 21.32 ?  109 LEU   B HD13 1 
ATOM   5699 H  HD21 . LEU   B 1 109 ? 35.424 -28.392 1.382   1.00 22.83 ?  109 LEU   B HD21 1 
ATOM   5700 H  HD22 . LEU   B 1 109 ? 35.229 -28.501 2.954   1.00 22.83 ?  109 LEU   B HD22 1 
ATOM   5701 H  HD23 . LEU   B 1 109 ? 33.967 -28.566 1.992   1.00 22.83 ?  109 LEU   B HD23 1 
ATOM   5702 N  N    . LYS   B 1 110 ? 31.698 -24.020 2.861   1.00 18.31 ?  110 LYS   B N    1 
ATOM   5703 C  CA   . LYS   B 1 110 ? 30.944 -23.267 1.862   1.00 18.56 ?  110 LYS   B CA   1 
ATOM   5704 C  C    . LYS   B 1 110 ? 31.270 -21.776 1.950   1.00 18.04 ?  110 LYS   B C    1 
ATOM   5705 O  O    . LYS   B 1 110 ? 31.528 -21.126 0.932   1.00 18.00 ?  110 LYS   B O    1 
ATOM   5706 C  CB   . LYS   B 1 110 ? 29.443 -23.528 2.007   1.00 19.31 ?  110 LYS   B CB   1 
ATOM   5707 C  CG   . LYS   B 1 110 ? 28.625 -22.887 0.893   1.00 19.38 ?  110 LYS   B CG   1 
ATOM   5708 C  CD   . LYS   B 1 110 ? 27.165 -23.356 0.924   1.00 19.28 ?  110 LYS   B CD   1 
ATOM   5709 C  CE   . LYS   B 1 110 ? 26.380 -22.815 -0.261  1.00 19.88 ?  110 LYS   B CE   1 
ATOM   5710 N  NZ   . LYS   B 1 110 ? 26.734 -23.509 -1.520  1.00 19.77 ?  110 LYS   B NZ   1 
ATOM   5711 H  H    . LYS   B 1 110 ? 31.224 -24.419 3.452   1.00 22.03 ?  110 LYS   B H    1 
ATOM   5712 H  HA   . LYS   B 1 110 ? 31.205 -23.571 0.978   1.00 22.33 ?  110 LYS   B HA   1 
ATOM   5713 H  HB2  . LYS   B 1 110 ? 29.286 -24.490 1.977   1.00 23.22 ?  110 LYS   B HB2  1 
ATOM   5714 H  HB3  . LYS   B 1 110 ? 29.137 -23.171 2.852   1.00 23.22 ?  110 LYS   B HB3  1 
ATOM   5715 H  HG2  . LYS   B 1 110 ? 28.632 -21.925 1.005   1.00 23.31 ?  110 LYS   B HG2  1 
ATOM   5716 H  HG3  . LYS   B 1 110 ? 29.000 -23.131 0.034   1.00 23.31 ?  110 LYS   B HG3  1 
ATOM   5717 H  HD2  . LYS   B 1 110 ? 27.136 -24.327 0.889   1.00 23.19 ?  110 LYS   B HD2  1 
ATOM   5718 H  HD3  . LYS   B 1 110 ? 26.741 -23.041 1.739   1.00 23.19 ?  110 LYS   B HD3  1 
ATOM   5719 H  HE2  . LYS   B 1 110 ? 25.432 -22.939 -0.101  1.00 23.91 ?  110 LYS   B HE2  1 
ATOM   5720 H  HE3  . LYS   B 1 110 ? 26.582 -21.872 -0.369  1.00 23.91 ?  110 LYS   B HE3  1 
ATOM   5721 H  HZ1  . LYS   B 1 110 ? 26.263 -23.175 -2.195  1.00 23.78 ?  110 LYS   B HZ1  1 
ATOM   5722 H  HZ2  . LYS   B 1 110 ? 27.601 -23.409 -1.691  1.00 23.78 ?  110 LYS   B HZ2  1 
ATOM   5723 H  HZ3  . LYS   B 1 110 ? 26.555 -24.381 -1.446  1.00 23.78 ?  110 LYS   B HZ3  1 
ATOM   5724 N  N    . SER   B 1 111 ? 31.301 -21.231 3.170   1.00 18.50 ?  111 SER   B N    1 
ATOM   5725 C  CA   . SER   B 1 111 ? 31.682 -19.830 3.349   1.00 17.72 ?  111 SER   B CA   1 
ATOM   5726 C  C    . SER   B 1 111 ? 33.061 -19.565 2.759   1.00 17.09 ?  111 SER   B C    1 
ATOM   5727 O  O    . SER   B 1 111 ? 33.284 -18.530 2.110   1.00 17.56 ?  111 SER   B O    1 
ATOM   5728 C  CB   . SER   B 1 111 ? 31.683 -19.481 4.837   1.00 18.85 ?  111 SER   B CB   1 
ATOM   5729 O  OG   . SER   B 1 111 ? 30.377 -19.469 5.388   1.00 20.31 ?  111 SER   B OG   1 
ATOM   5730 H  H    . SER   B 1 111 ? 31.116 -21.654 3.897   1.00 22.25 ?  111 SER   B H    1 
ATOM   5731 H  HA   . SER   B 1 111 ? 31.037 -19.264 2.902   1.00 21.32 ?  111 SER   B HA   1 
ATOM   5732 H  HB2  . SER   B 1 111 ? 32.211 -20.143 5.312   1.00 22.67 ?  111 SER   B HB2  1 
ATOM   5733 H  HB3  . SER   B 1 111 ? 32.079 -18.605 4.948   1.00 22.67 ?  111 SER   B HB3  1 
ATOM   5734 H  HG   . SER   B 1 111 ? 30.418 -19.268 6.207   1.00 24.43 ?  111 SER   B HG   1 
ATOM   5735 N  N    . ALA   B 1 112 ? 34.005 -20.477 2.991   1.00 17.05 ?  112 ALA   B N    1 
ATOM   5736 C  CA   . ALA   B 1 112 ? 35.349 -20.300 2.452   1.00 16.66 ?  112 ALA   B CA   1 
ATOM   5737 C  C    . ALA   B 1 112 ? 35.323 -20.215 0.929   1.00 16.34 ?  112 ALA   B C    1 
ATOM   5738 O  O    . ALA   B 1 112 ? 35.946 -19.329 0.332   1.00 17.07 ?  112 ALA   B O    1 
ATOM   5739 C  CB   . ALA   B 1 112 ? 36.250 -21.439 2.927   1.00 17.14 ?  112 ALA   B CB   1 
ATOM   5740 H  H    . ALA   B 1 112 ? 33.892 -21.198 3.461   1.00 20.52 ?  112 ALA   B H    1 
ATOM   5741 H  HA   . ALA   B 1 112 ? 35.710 -19.470 2.792   1.00 20.04 ?  112 ALA   B HA   1 
ATOM   5742 H  HB1  . ALA   B 1 112 ? 37.142 -21.300 2.563   1.00 20.63 ?  112 ALA   B HB1  1 
ATOM   5743 H  HB2  . ALA   B 1 112 ? 36.290 -21.429 3.897   1.00 20.63 ?  112 ALA   B HB2  1 
ATOM   5744 H  HB3  . ALA   B 1 112 ? 35.893 -22.281 2.616   1.00 20.63 ?  112 ALA   B HB3  1 
ATOM   5745 N  N    . TYR   B 1 113 ? 34.590 -21.123 0.279   1.00 16.01 ?  113 TYR   B N    1 
ATOM   5746 C  CA   . TYR   B 1 113 ? 34.517 -21.089 -1.178  1.00 16.22 ?  113 TYR   B CA   1 
ATOM   5747 C  C    . TYR   B 1 113 ? 33.810 -19.840 -1.700  1.00 15.96 ?  113 TYR   B C    1 
ATOM   5748 O  O    . TYR   B 1 113 ? 34.072 -19.419 -2.832  1.00 15.83 ?  113 TYR   B O    1 
ATOM   5749 C  CB   . TYR   B 1 113 ? 33.841 -22.351 -1.714  1.00 16.31 ?  113 TYR   B CB   1 
ATOM   5750 C  CG   . TYR   B 1 113 ? 34.806 -23.496 -1.960  1.00 16.53 ?  113 TYR   B CG   1 
ATOM   5751 C  CD1  . TYR   B 1 113 ? 35.818 -23.393 -2.910  1.00 17.35 ?  113 TYR   B CD1  1 
ATOM   5752 C  CD2  . TYR   B 1 113 ? 34.702 -24.684 -1.250  1.00 17.08 ?  113 TYR   B CD2  1 
ATOM   5753 C  CE1  . TYR   B 1 113 ? 36.701 -24.428 -3.135  1.00 17.60 ?  113 TYR   B CE1  1 
ATOM   5754 C  CE2  . TYR   B 1 113 ? 35.583 -25.733 -1.474  1.00 17.76 ?  113 TYR   B CE2  1 
ATOM   5755 C  CZ   . TYR   B 1 113 ? 36.574 -25.603 -2.422  1.00 17.77 ?  113 TYR   B CZ   1 
ATOM   5756 O  OH   . TYR   B 1 113 ? 37.457 -26.620 -2.669  1.00 18.67 ?  113 TYR   B OH   1 
ATOM   5757 H  H    . TYR   B 1 113 ? 34.129 -21.753 0.651   1.00 19.27 ?  113 TYR   B H    1 
ATOM   5758 H  HA   . TYR   B 1 113 ? 35.415 -21.072 -1.523  1.00 19.52 ?  113 TYR   B HA   1 
ATOM   5759 H  HB2  . TYR   B 1 113 ? 33.178 -22.660 -1.069  1.00 19.63 ?  113 TYR   B HB2  1 
ATOM   5760 H  HB3  . TYR   B 1 113 ? 33.401 -22.147 -2.555  1.00 19.63 ?  113 TYR   B HB3  1 
ATOM   5761 H  HD1  . TYR   B 1 113 ? 35.904 -22.602 -3.392  1.00 20.87 ?  113 TYR   B HD1  1 
ATOM   5762 H  HD2  . TYR   B 1 113 ? 34.026 -24.773 -0.618  1.00 20.55 ?  113 TYR   B HD2  1 
ATOM   5763 H  HE1  . TYR   B 1 113 ? 37.366 -24.339 -3.774  1.00 21.18 ?  113 TYR   B HE1  1 
ATOM   5764 H  HE2  . TYR   B 1 113 ? 35.489 -26.525 -0.994  1.00 21.36 ?  113 TYR   B HE2  1 
ATOM   5765 H  HH   . TYR   B 1 113 ? 37.272 -27.283 -2.186  1.00 22.46 ?  113 TYR   B HH   1 
ATOM   5766 N  N    . GLU   B 1 114 ? 32.876 -19.270 -0.927  1.00 16.05 ?  114 GLU   B N    1 
ATOM   5767 C  CA   . GLU   B 1 114 ? 32.187 -18.063 -1.377  1.00 16.50 ?  114 GLU   B CA   1 
ATOM   5768 C  C    . GLU   B 1 114 ? 33.164 -16.935 -1.672  1.00 16.53 ?  114 GLU   B C    1 
ATOM   5769 O  O    . GLU   B 1 114 ? 32.878 -16.078 -2.509  1.00 16.64 ?  114 GLU   B O    1 
ATOM   5770 C  CB   . GLU   B 1 114 ? 31.127 -17.636 -0.358  1.00 16.88 ?  114 GLU   B CB   1 
ATOM   5771 C  CG   . GLU   B 1 114 ? 29.912 -18.548 -0.447  1.00 16.99 ?  114 GLU   B CG   1 
ATOM   5772 C  CD   . GLU   B 1 114 ? 28.895 -18.374 0.665   1.00 17.02 ?  114 GLU   B CD   1 
ATOM   5773 O  OE1  . GLU   B 1 114 ? 29.188 -17.774 1.717   1.00 17.63 ?  114 GLU   B OE1  1 
ATOM   5774 O  OE2  . GLU   B 1 114 ? 27.778 -18.908 0.501   1.00 17.98 -1 114 GLU   B OE2  1 
ATOM   5775 H  H    . GLU   B 1 114 ? 32.615 -19.575 -0.163  1.00 19.32 ?  114 GLU   B H    1 
ATOM   5776 H  HA   . GLU   B 1 114 ? 31.726 -18.262 -2.202  1.00 19.85 ?  114 GLU   B HA   1 
ATOM   5777 H  HB2  . GLU   B 1 114 ? 31.495 -17.700 0.540   1.00 20.31 ?  114 GLU   B HB2  1 
ATOM   5778 H  HB3  . GLU   B 1 114 ? 30.846 -16.728 -0.544  1.00 20.31 ?  114 GLU   B HB3  1 
ATOM   5779 H  HG2  . GLU   B 1 114 ? 29.457 -18.369 -1.281  1.00 20.44 ?  114 GLU   B HG2  1 
ATOM   5780 H  HG3  . GLU   B 1 114 ? 30.215 -19.466 -0.426  1.00 20.44 ?  114 GLU   B HG3  1 
ATOM   5781 N  N    . ASN   B 1 115 ? 34.337 -16.926 -1.029  1.00 16.05 ?  115 ASN   B N    1 
ATOM   5782 C  CA   . ASN   B 1 115 ? 35.323 -15.892 -1.335  1.00 15.33 ?  115 ASN   B CA   1 
ATOM   5783 C  C    . ASN   B 1 115 ? 35.724 -15.920 -2.802  1.00 15.10 ?  115 ASN   B C    1 
ATOM   5784 O  O    . ASN   B 1 115 ? 36.123 -14.882 -3.355  1.00 15.63 ?  115 ASN   B O    1 
ATOM   5785 C  CB   . ASN   B 1 115 ? 36.568 -16.053 -0.457  1.00 15.98 ?  115 ASN   B CB   1 
ATOM   5786 C  CG   . ASN   B 1 115 ? 36.300 -15.799 1.017   1.00 16.44 ?  115 ASN   B CG   1 
ATOM   5787 O  OD1  . ASN   B 1 115 ? 36.310 -14.651 1.475   1.00 18.72 ?  115 ASN   B OD1  1 
ATOM   5788 N  ND2  . ASN   B 1 115 ? 36.101 -16.872 1.780   1.00 16.62 ?  115 ASN   B ND2  1 
ATOM   5789 H  H    . ASN   B 1 115 ? 34.582 -17.488 -0.421  1.00 19.32 ?  115 ASN   B H    1 
ATOM   5790 H  HA   . ASN   B 1 115 ? 34.943 -15.022 -1.144  1.00 18.45 ?  115 ASN   B HA   1 
ATOM   5791 H  HB2  . ASN   B 1 115 ? 36.911 -16.957 -0.551  1.00 19.24 ?  115 ASN   B HB2  1 
ATOM   5792 H  HB3  . ASN   B 1 115 ? 37.247 -15.417 -0.747  1.00 19.24 ?  115 ASN   B HB3  1 
ATOM   5793 H  HD21 . ASN   B 1 115 ? 35.952 -16.778 2.619   1.00 20.00 ?  115 ASN   B HD21 1 
ATOM   5794 H  HD22 . ASN   B 1 115 ? 36.110 -17.659 1.429   1.00 20.00 ?  115 ASN   B HD22 1 
ATOM   5795 N  N    . PHE   B 1 116 ? 35.714 -17.106 -3.427  1.00 15.10 ?  116 PHE   B N    1 
ATOM   5796 C  CA   . PHE   B 1 116 ? 36.144 -17.198 -4.817  1.00 15.57 ?  116 PHE   B CA   1 
ATOM   5797 C  C    . PHE   B 1 116 ? 35.241 -16.378 -5.730  1.00 15.19 ?  116 PHE   B C    1 
ATOM   5798 O  O    . PHE   B 1 116 ? 35.674 -15.949 -6.803  1.00 15.81 ?  116 PHE   B O    1 
ATOM   5799 C  CB   . PHE   B 1 116 ? 36.114 -18.640 -5.344  1.00 14.89 ?  116 PHE   B CB   1 
ATOM   5800 C  CG   . PHE   B 1 116 ? 37.178 -19.597 -4.785  1.00 14.82 ?  116 PHE   B CG   1 
ATOM   5801 C  CD1  . PHE   B 1 116 ? 37.803 -19.413 -3.560  1.00 15.27 ?  116 PHE   B CD1  1 
ATOM   5802 C  CD2  . PHE   B 1 116 ? 37.505 -20.733 -5.521  1.00 15.14 ?  116 PHE   B CD2  1 
ATOM   5803 C  CE1  . PHE   B 1 116 ? 38.739 -20.343 -3.099  1.00 15.54 ?  116 PHE   B CE1  1 
ATOM   5804 C  CE2  . PHE   B 1 116 ? 38.435 -21.657 -5.066  1.00 15.15 ?  116 PHE   B CE2  1 
ATOM   5805 C  CZ   . PHE   B 1 116 ? 39.044 -21.470 -3.860  1.00 14.92 ?  116 PHE   B CZ   1 
ATOM   5806 H  H    . PHE   B 1 116 ? 35.455 -17.848 -3.077  1.00 18.18 ?  116 PHE   B H    1 
ATOM   5807 H  HA   . PHE   B 1 116 ? 37.050 -16.865 -4.895  1.00 18.74 ?  116 PHE   B HA   1 
ATOM   5808 H  HB2  . PHE   B 1 116 ? 35.238 -19.020 -5.137  1.00 17.93 ?  116 PHE   B HB2  1 
ATOM   5809 H  HB3  . PHE   B 1 116 ? 36.223 -18.615 -6.308  1.00 17.93 ?  116 PHE   B HB3  1 
ATOM   5810 H  HD1  . PHE   B 1 116 ? 37.585 -18.672 -3.039  1.00 18.38 ?  116 PHE   B HD1  1 
ATOM   5811 H  HD2  . PHE   B 1 116 ? 37.089 -20.879 -6.341  1.00 18.23 ?  116 PHE   B HD2  1 
ATOM   5812 H  HE1  . PHE   B 1 116 ? 39.152 -20.214 -2.276  1.00 18.70 ?  116 PHE   B HE1  1 
ATOM   5813 H  HE2  . PHE   B 1 116 ? 38.635 -22.397 -5.585  1.00 18.23 ?  116 PHE   B HE2  1 
ATOM   5814 H  HZ   . PHE   B 1 116 ? 39.673 -22.079 -3.558  1.00 17.96 ?  116 PHE   B HZ   1 
ATOM   5815 N  N    . ASN   B 1 117 ? 33.973 -16.179 -5.347  1.00 16.08 ?  117 ASN   B N    1 
ATOM   5816 C  CA   . ASN   B 1 117 ? 33.023 -15.479 -6.211  1.00 16.36 ?  117 ASN   B CA   1 
ATOM   5817 C  C    . ASN   B 1 117 ? 33.335 -13.998 -6.370  1.00 16.58 ?  117 ASN   B C    1 
ATOM   5818 O  O    . ASN   B 1 117 ? 32.730 -13.345 -7.223  1.00 17.94 ?  117 ASN   B O    1 
ATOM   5819 C  CB   . ASN   B 1 117 ? 31.599 -15.700 -5.704  1.00 17.10 ?  117 ASN   B CB   1 
ATOM   5820 C  CG   . ASN   B 1 117 ? 31.138 -17.106 -5.962  1.00 17.02 ?  117 ASN   B CG   1 
ATOM   5821 O  OD1  . ASN   B 1 117 ? 31.502 -17.696 -6.980  1.00 17.77 ?  117 ASN   B OD1  1 
ATOM   5822 N  ND2  . ASN   B 1 117 ? 30.398 -17.680 -5.026  1.00 16.60 ?  117 ASN   B ND2  1 
ATOM   5823 H  H    . ASN   B 1 117 ? 33.647 -16.438 -4.592  1.00 19.35 ?  117 ASN   B H    1 
ATOM   5824 H  HA   . ASN   B 1 117 ? 33.075 -15.881 -7.088  1.00 19.69 ?  117 ASN   B HA   1 
ATOM   5825 H  HB2  . ASN   B 1 117 ? 31.568 -15.538 -4.745  1.00 20.58 ?  117 ASN   B HB2  1 
ATOM   5826 H  HB3  . ASN   B 1 117 ? 30.999 -15.085 -6.162  1.00 20.58 ?  117 ASN   B HB3  1 
ATOM   5827 H  HD21 . ASN   B 1 117 ? 30.111 -18.484 -5.137  1.00 19.98 ?  117 ASN   B HD21 1 
ATOM   5828 H  HD22 . ASN   B 1 117 ? 30.168 -17.235 -4.327  1.00 19.98 ?  117 ASN   B HD22 1 
ATOM   5829 N  N    . GLN   B 1 118 ? 34.269 -13.469 -5.595  1.00 16.26 ?  118 GLN   B N    1 
ATOM   5830 C  CA   . GLN   B 1 118 ? 34.692 -12.087 -5.737  1.00 16.89 ?  118 GLN   B CA   1 
ATOM   5831 C  C    . GLN   B 1 118 ? 35.760 -11.898 -6.809  1.00 17.12 ?  118 GLN   B C    1 
ATOM   5832 O  O    . GLN   B 1 118 ? 36.242 -10.774 -6.980  1.00 18.43 ?  118 GLN   B O    1 
ATOM   5833 C  CB   . GLN   B 1 118 ? 35.162 -11.550 -4.378  1.00 17.23 ?  118 GLN   B CB   1 
ATOM   5834 C  CG   . GLN   B 1 118 ? 34.079 -11.593 -3.304  1.00 17.45 ?  118 GLN   B CG   1 
ATOM   5835 C  CD   . GLN   B 1 118 ? 32.914 -10.684 -3.627  1.00 17.65 ?  118 GLN   B CD   1 
ATOM   5836 O  OE1  . GLN   B 1 118 ? 33.108 -9.547  -4.078  1.00 18.54 ?  118 GLN   B OE1  1 
ATOM   5837 N  NE2  . GLN   B 1 118 ? 31.701 -11.171 -3.405  1.00 18.23 ?  118 GLN   B NE2  1 
ATOM   5838 H  H    . GLN   B 1 118 ? 34.681 -13.890 -4.971  1.00 19.57 ?  118 GLN   B H    1 
ATOM   5839 H  HA   . GLN   B 1 118 ? 33.926 -11.556 -6.013  1.00 20.33 ?  118 GLN   B HA   1 
ATOM   5840 H  HB2  . GLN   B 1 118 ? 35.910 -12.079 -4.069  1.00 20.73 ?  118 GLN   B HB2  1 
ATOM   5841 H  HB3  . GLN   B 1 118 ? 35.435 -10.620 -4.480  1.00 20.73 ?  118 GLN   B HB3  1 
ATOM   5842 H  HG2  . GLN   B 1 118 ? 33.743 -12.503 -3.232  1.00 20.99 ?  118 GLN   B HG2  1 
ATOM   5843 H  HG3  . GLN   B 1 118 ? 34.455 -11.310 -2.459  1.00 20.99 ?  118 GLN   B HG3  1 
ATOM   5844 H  HE21 . GLN   B 1 118 ? 31.608 -11.968 -3.083  1.00 21.93 ?  118 GLN   B HE21 1 
ATOM   5845 H  HE22 . GLN   B 1 118 ? 31.011 -10.696 -3.575  1.00 21.93 ?  118 GLN   B HE22 1 
ATOM   5846 N  N    . HIS   B 1 119 ? 36.118 -12.957 -7.541  1.00 16.27 ?  119 HIS   B N    1 
ATOM   5847 C  CA   . HIS   B 1 119 ? 37.171 -12.903 -8.548  1.00 16.65 ?  119 HIS   B CA   1 
ATOM   5848 C  C    . HIS   B 1 119 ? 36.690 -13.641 -9.780  1.00 16.77 ?  119 HIS   B C    1 
ATOM   5849 O  O    . HIS   B 1 119 ? 36.172 -14.752 -9.666  1.00 16.86 ?  119 HIS   B O    1 
ATOM   5850 C  CB   . HIS   B 1 119 ? 38.448 -13.532 -7.993  1.00 16.64 ?  119 HIS   B CB   1 
ATOM   5851 C  CG   . HIS   B 1 119 ? 38.918 -12.844 -6.755  1.00 17.49 ?  119 HIS   B CG   1 
ATOM   5852 N  ND1  . HIS   B 1 119 ? 39.705 -11.712 -6.788  1.00 18.67 ?  119 HIS   B ND1  1 
ATOM   5853 C  CD2  . HIS   B 1 119 ? 38.630 -13.066 -5.452  1.00 18.39 ?  119 HIS   B CD2  1 
ATOM   5854 C  CE1  . HIS   B 1 119 ? 39.922 -11.299 -5.554  1.00 19.76 ?  119 HIS   B CE1  1 
ATOM   5855 N  NE2  . HIS   B 1 119 ? 39.270 -12.093 -4.725  1.00 19.58 ?  119 HIS   B NE2  1 
ATOM   5856 H  H    . HIS   B 1 119 ? 35.748 -13.732 -7.476  1.00 19.58 ?  119 HIS   B H    1 
ATOM   5857 H  HA   . HIS   B 1 119 ? 37.352 -11.976 -8.785  1.00 20.03 ?  119 HIS   B HA   1 
ATOM   5858 H  HB2  . HIS   B 1 119 ? 38.277 -14.462 -7.776  1.00 20.02 ?  119 HIS   B HB2  1 
ATOM   5859 H  HB3  . HIS   B 1 119 ? 39.151 -13.469 -8.660  1.00 20.02 ?  119 HIS   B HB3  1 
ATOM   5860 H  HD2  . HIS   B 1 119 ? 38.110 -13.758 -5.111  1.00 22.13 ?  119 HIS   B HD2  1 
ATOM   5861 H  HE1  . HIS   B 1 119 ? 40.449 -10.572 -5.310  1.00 23.76 ?  119 HIS   B HE1  1 
ATOM   5862 H  HE2  . HIS   B 1 119 ? 39.279 -12.034 -3.867  1.00 23.55 ?  119 HIS   B HE2  1 
ATOM   5863 N  N    A GLU   B 1 120 ? 36.848 -13.029 -10.953 0.66 17.09 ?  120 GLU   B N    1 
ATOM   5864 N  N    B GLU   B 1 120 ? 36.855 -13.031 -10.955 0.34 17.30 ?  120 GLU   B N    1 
ATOM   5865 C  CA   A GLU   B 1 120 ? 36.256 -13.611 -12.153 0.66 18.89 ?  120 GLU   B CA   1 
ATOM   5866 C  CA   B GLU   B 1 120 ? 36.261 -13.603 -12.161 0.34 18.70 ?  120 GLU   B CA   1 
ATOM   5867 C  C    A GLU   B 1 120 ? 36.938 -14.910 -12.564 0.66 17.70 ?  120 GLU   B C    1 
ATOM   5868 C  C    B GLU   B 1 120 ? 36.945 -14.897 -12.588 0.34 17.59 ?  120 GLU   B C    1 
ATOM   5869 O  O    A GLU   B 1 120 ? 36.278 -15.799 -13.113 0.66 18.09 ?  120 GLU   B O    1 
ATOM   5870 O  O    B GLU   B 1 120 ? 36.295 -15.768 -13.177 0.34 17.56 ?  120 GLU   B O    1 
ATOM   5871 C  CB   A GLU   B 1 120 ? 36.254 -12.597 -13.299 0.66 23.13 ?  120 GLU   B CB   1 
ATOM   5872 C  CB   B GLU   B 1 120 ? 36.266 -12.579 -13.297 0.34 21.93 ?  120 GLU   B CB   1 
ATOM   5873 C  CG   A GLU   B 1 120 ? 35.229 -11.484 -13.114 0.66 27.12 ?  120 GLU   B CG   1 
ATOM   5874 C  CG   B GLU   B 1 120 ? 35.359 -11.381 -13.042 0.34 25.02 ?  120 GLU   B CG   1 
ATOM   5875 C  CD   A GLU   B 1 120 ? 35.094 -10.581 -14.324 0.66 30.86 ?  120 GLU   B CD   1 
ATOM   5876 C  CD   B GLU   B 1 120 ? 35.224 -10.472 -14.250 0.34 28.02 ?  120 GLU   B CD   1 
ATOM   5877 O  OE1  A GLU   B 1 120 ? 36.121 -10.275 -14.967 0.66 32.54 ?  120 GLU   B OE1  1 
ATOM   5878 O  OE1  B GLU   B 1 120 ? 36.098 -10.529 -15.141 0.34 29.43 ?  120 GLU   B OE1  1 
ATOM   5879 O  OE2  A GLU   B 1 120 ? 33.950 -10.181 -14.629 0.66 33.31 -1 120 GLU   B OE2  1 
ATOM   5880 O  OE2  B GLU   B 1 120 ? 34.245 -9.697  -14.307 0.34 29.63 -1 120 GLU   B OE2  1 
ATOM   5881 H  H    A GLU   B 1 120 ? 37.266 -12.284 -11.074 0.66 20.56 ?  120 GLU   B H    1 
ATOM   5882 H  H    B GLU   B 1 120 ? 37.288 -12.295 -11.076 0.34 20.82 ?  120 GLU   B H    1 
ATOM   5883 H  HA   A GLU   B 1 120 ? 35.332 -13.821 -11.959 0.66 22.72 ?  120 GLU   B HA   1 
ATOM   5884 H  HA   B GLU   B 1 120 ? 35.337 -13.815 -11.970 0.34 22.49 ?  120 GLU   B HA   1 
ATOM   5885 H  HB2  A GLU   B 1 120 ? 37.129 -12.186 -13.361 0.66 27.81 ?  120 GLU   B HB2  1 
ATOM   5886 H  HB2  B GLU   B 1 120 ? 37.167 -12.247 -13.419 0.34 26.38 ?  120 GLU   B HB2  1 
ATOM   5887 H  HB3  A GLU   B 1 120 ? 36.045 -13.058 -14.126 0.66 27.81 ?  120 GLU   B HB3  1 
ATOM   5888 H  HB3  B GLU   B 1 120 ? 35.961 -13.014 -14.109 0.34 26.38 ?  120 GLU   B HB3  1 
ATOM   5889 H  HG2  A GLU   B 1 120 ? 34.357 -11.878 -12.960 0.66 32.60 ?  120 GLU   B HG2  1 
ATOM   5890 H  HG2  B GLU   B 1 120 ? 34.475 -11.702 -12.796 0.34 30.08 ?  120 GLU   B HG2  1 
ATOM   5891 H  HG3  A GLU   B 1 120 ? 35.486 -10.938 -12.357 0.66 32.60 ?  120 GLU   B HG3  1 
ATOM   5892 H  HG3  B GLU   B 1 120 ? 35.731 -10.851 -12.322 0.34 30.08 ?  120 GLU   B HG3  1 
ATOM   5893 N  N    . VAL   B 1 121 ? 38.239 -15.044 -12.310 1.00 17.03 ?  121 VAL   B N    1 
ATOM   5894 C  CA   . VAL   B 1 121 ? 38.984 -16.256 -12.652 1.00 16.24 ?  121 VAL   B CA   1 
ATOM   5895 C  C    . VAL   B 1 121 ? 40.096 -16.455 -11.632 1.00 15.74 ?  121 VAL   B C    1 
ATOM   5896 O  O    . VAL   B 1 121 ? 40.773 -15.494 -11.247 1.00 16.33 ?  121 VAL   B O    1 
ATOM   5897 C  CB   . VAL   B 1 121 ? 39.503 -16.219 -14.109 1.00 18.38 ?  121 VAL   B CB   1 
ATOM   5898 C  CG1  . VAL   B 1 121 ? 40.382 -14.996 -14.350 1.00 19.58 ?  121 VAL   B CG1  1 
ATOM   5899 C  CG2  . VAL   B 1 121 ? 40.245 -17.506 -14.451 1.00 20.22 ?  121 VAL   B CG2  1 
ATOM   5900 H  H    A VAL   B 1 121 ? 38.725 -14.436 -11.943 0.66 20.49 ?  121 VAL   B H    1 
ATOM   5901 H  H    B VAL   B 1 121 ? 38.721 -14.444 -11.926 0.34 20.49 ?  121 VAL   B H    1 
ATOM   5902 H  HA   . VAL   B 1 121 ? 38.375 -17.011 -12.584 1.00 19.55 ?  121 VAL   B HA   1 
ATOM   5903 H  HB   . VAL   B 1 121 ? 38.740 -16.156 -14.709 1.00 22.11 ?  121 VAL   B HB   1 
ATOM   5904 H  HG11 . VAL   B 1 121 ? 40.685 -15.005 -15.272 1.00 23.55 ?  121 VAL   B HG11 1 
ATOM   5905 H  HG12 . VAL   B 1 121 ? 39.862 -14.196 -14.180 1.00 23.55 ?  121 VAL   B HG12 1 
ATOM   5906 H  HG13 . VAL   B 1 121 ? 41.143 -15.034 -13.752 1.00 23.55 ?  121 VAL   B HG13 1 
ATOM   5907 H  HG21 . VAL   B 1 121 ? 40.443 -17.514 -15.402 1.00 24.32 ?  121 VAL   B HG21 1 
ATOM   5908 H  HG22 . VAL   B 1 121 ? 41.073 -17.540 -13.944 1.00 24.32 ?  121 VAL   B HG22 1 
ATOM   5909 H  HG23 . VAL   B 1 121 ? 39.687 -18.266 -14.225 1.00 24.32 ?  121 VAL   B HG23 1 
ATOM   5910 N  N    . LEU   B 1 122 ? 40.279 -17.706 -11.196 1.00 15.37 ?  122 LEU   B N    1 
ATOM   5911 C  CA   . LEU   B 1 122 ? 41.264 -18.051 -10.174 1.00 15.18 ?  122 LEU   B CA   1 
ATOM   5912 C  C    . LEU   B 1 122 ? 41.922 -19.385 -10.492 1.00 14.91 ?  122 LEU   B C    1 
ATOM   5913 O  O    . LEU   B 1 122 ? 41.260 -20.319 -10.975 1.00 15.98 ?  122 LEU   B O    1 
ATOM   5914 C  CB   . LEU   B 1 122 ? 40.620 -18.276 -8.794  1.00 16.62 ?  122 LEU   B CB   1 
ATOM   5915 C  CG   . LEU   B 1 122 ? 39.577 -17.266 -8.312  1.00 16.72 ?  122 LEU   B CG   1 
ATOM   5916 C  CD1  . LEU   B 1 122 ? 38.196 -17.663 -8.804  1.00 17.73 ?  122 LEU   B CD1  1 
ATOM   5917 C  CD2  . LEU   B 1 122 ? 39.600 -17.148 -6.803  1.00 16.57 ?  122 LEU   B CD2  1 
ATOM   5918 H  H    . LEU   B 1 122 ? 39.833 -18.387 -11.476 1.00 18.49 ?  122 LEU   B H    1 
ATOM   5919 H  HA   . LEU   B 1 122 ? 41.940 -17.360 -10.101 1.00 18.28 ?  122 LEU   B HA   1 
ATOM   5920 H  HB2  . LEU   B 1 122 ? 40.183 -19.139 -8.807  1.00 20.00 ?  122 LEU   B HB2  1 
ATOM   5921 H  HB3  . LEU   B 1 122 ? 41.326 -18.285 -8.132  1.00 20.00 ?  122 LEU   B HB3  1 
ATOM   5922 H  HG   . LEU   B 1 122 ? 39.789 -16.389 -8.679  1.00 20.12 ?  122 LEU   B HG   1 
ATOM   5923 H  HD11 . LEU   B 1 122 ? 37.546 -17.038 -8.447  1.00 21.33 ?  122 LEU   B HD11 1 
ATOM   5924 H  HD12 . LEU   B 1 122 ? 38.186 -17.628 -9.774  1.00 21.33 ?  122 LEU   B HD12 1 
ATOM   5925 H  HD13 . LEU   B 1 122 ? 38.001 -18.558 -8.499  1.00 21.33 ?  122 LEU   B HD13 1 
ATOM   5926 H  HD21 . LEU   B 1 122 ? 38.915 -16.521 -6.521  1.00 19.94 ?  122 LEU   B HD21 1 
ATOM   5927 H  HD22 . LEU   B 1 122 ? 39.426 -18.021 -6.416  1.00 19.94 ?  122 LEU   B HD22 1 
ATOM   5928 H  HD23 . LEU   B 1 122 ? 40.473 -16.831 -6.520  1.00 19.94 ?  122 LEU   B HD23 1 
ATOM   5929 N  N    . LEU   B 1 123 ? 43.211 -19.491 -10.138 1.00 14.14 ?  123 LEU   B N    1 
ATOM   5930 C  CA   . LEU   B 1 123 ? 43.913 -20.766 -10.010 1.00 14.61 ?  123 LEU   B CA   1 
ATOM   5931 C  C    . LEU   B 1 123 ? 43.884 -21.150 -8.537  1.00 14.45 ?  123 LEU   B C    1 
ATOM   5932 O  O    . LEU   B 1 123 ? 44.236 -20.322 -7.688  1.00 14.74 ?  123 LEU   B O    1 
ATOM   5933 C  CB   . LEU   B 1 123 ? 45.363 -20.589 -10.465 1.00 15.23 ?  123 LEU   B CB   1 
ATOM   5934 C  CG   . LEU   B 1 123 ? 46.304 -21.768 -10.231 1.00 15.19 ?  123 LEU   B CG   1 
ATOM   5935 C  CD1  . LEU   B 1 123 ? 45.875 -23.005 -11.018 1.00 16.62 ?  123 LEU   B CD1  1 
ATOM   5936 C  CD2  . LEU   B 1 123 ? 47.704 -21.349 -10.607 1.00 16.16 ?  123 LEU   B CD2  1 
ATOM   5937 H  H    . LEU   B 1 123 ? 43.710 -18.809 -9.952  1.00 17.02 ?  123 LEU   B H    1 
ATOM   5938 H  HA   . LEU   B 1 123 ? 43.473 -21.453 -10.537 1.00 17.59 ?  123 LEU   B HA   1 
ATOM   5939 H  HB2  . LEU   B 1 123 ? 45.354 -20.410 -11.418 1.00 18.33 ?  123 LEU   B HB2  1 
ATOM   5940 H  HB3  . LEU   B 1 123 ? 45.734 -19.830 -9.996  1.00 18.33 ?  123 LEU   B HB3  1 
ATOM   5941 H  HG   . LEU   B 1 123 ? 46.299 -22.003 -9.291  1.00 18.29 ?  123 LEU   B HG   1 
ATOM   5942 H  HD11 . LEU   B 1 123 ? 46.507 -23.724 -10.852 1.00 20.00 ?  123 LEU   B HD11 1 
ATOM   5943 H  HD12 . LEU   B 1 123 ? 44.987 -23.280 -10.728 1.00 20.00 ?  123 LEU   B HD12 1 
ATOM   5944 H  HD13 . LEU   B 1 123 ? 45.858 -22.793 -11.964 1.00 20.00 ?  123 LEU   B HD13 1 
ATOM   5945 H  HD21 . LEU   B 1 123 ? 48.306 -22.095 -10.471 1.00 19.44 ?  123 LEU   B HD21 1 
ATOM   5946 H  HD22 . LEU   B 1 123 ? 47.713 -21.081 -11.540 1.00 19.44 ?  123 LEU   B HD22 1 
ATOM   5947 H  HD23 . LEU   B 1 123 ? 47.967 -20.602 -10.047 1.00 19.44 ?  123 LEU   B HD23 1 
ATOM   5948 N  N    . ALA   B 1 124 ? 43.445 -22.377 -8.220  1.00 14.18 ?  124 ALA   B N    1 
ATOM   5949 C  CA   . ALA   B 1 124 ? 43.195 -22.681 -6.818  1.00 14.10 ?  124 ALA   B CA   1 
ATOM   5950 C  C    . ALA   B 1 124 ? 43.469 -24.146 -6.492  1.00 13.73 ?  124 ALA   B C    1 
ATOM   5951 O  O    . ALA   B 1 124 ? 43.322 -25.027 -7.351  1.00 14.50 ?  124 ALA   B O    1 
ATOM   5952 C  CB   . ALA   B 1 124 ? 41.741 -22.368 -6.449  1.00 14.81 ?  124 ALA   B CB   1 
ATOM   5953 H  H    . ALA   B 1 124 ? 43.270 -23.013 -8.779  1.00 17.07 ?  124 ALA   B H    1 
ATOM   5954 H  HA   . ALA   B 1 124 ? 43.774 -22.135 -6.278  1.00 16.98 ?  124 ALA   B HA   1 
ATOM   5955 H  HB1  . ALA   B 1 124 ? 41.593 -22.581 -5.515  1.00 17.82 ?  124 ALA   B HB1  1 
ATOM   5956 H  HB2  . ALA   B 1 124 ? 41.574 -21.423 -6.603  1.00 17.82 ?  124 ALA   B HB2  1 
ATOM   5957 H  HB3  . ALA   B 1 124 ? 41.145 -22.899 -7.006  1.00 17.82 ?  124 ALA   B HB3  1 
ATOM   5958 N  N    . PRO   B 1 125 ? 43.768 -24.441 -5.230  1.00 14.25 ?  125 PRO   B N    1 
ATOM   5959 C  CA   . PRO   B 1 125 ? 43.705 -25.808 -4.708  1.00 15.15 ?  125 PRO   B CA   1 
ATOM   5960 C  C    . PRO   B 1 125 ? 42.309 -26.071 -4.148  1.00 15.53 ?  125 PRO   B C    1 
ATOM   5961 O  O    . PRO   B 1 125 ? 41.520 -25.149 -3.947  1.00 15.64 ?  125 PRO   B O    1 
ATOM   5962 C  CB   . PRO   B 1 125 ? 44.699 -25.738 -3.543  1.00 15.94 ?  125 PRO   B CB   1 
ATOM   5963 C  CG   . PRO   B 1 125 ? 44.467 -24.347 -2.977  1.00 16.01 ?  125 PRO   B CG   1 
ATOM   5964 C  CD   . PRO   B 1 125 ? 44.103 -23.475 -4.172  1.00 14.73 ?  125 PRO   B CD   1 
ATOM   5965 H  HA   . PRO   B 1 125 ? 43.972 -26.481 -5.359  1.00 18.24 ?  125 PRO   B HA   1 
ATOM   5966 H  HB2  . PRO   B 1 125 ? 44.487 -26.418 -2.881  1.00 19.18 ?  125 PRO   B HB2  1 
ATOM   5967 H  HB3  . PRO   B 1 125 ? 45.606 -25.836 -3.866  1.00 19.18 ?  125 PRO   B HB3  1 
ATOM   5968 H  HG2  . PRO   B 1 125 ? 43.735 -24.364 -2.341  1.00 19.26 ?  125 PRO   B HG2  1 
ATOM   5969 H  HG3  . PRO   B 1 125 ? 45.279 -24.023 -2.553  1.00 19.26 ?  125 PRO   B HG3  1 
ATOM   5970 H  HD2  . PRO   B 1 125 ? 43.342 -22.916 -3.975  1.00 17.74 ?  125 PRO   B HD2  1 
ATOM   5971 H  HD3  . PRO   B 1 125 ? 44.875 -22.936 -4.442  1.00 17.74 ?  125 PRO   B HD3  1 
ATOM   5972 N  N    . LEU   B 1 126 ? 42.036 -27.344 -3.850  1.00 15.81 ?  126 LEU   B N    1 
ATOM   5973 C  CA   . LEU   B 1 126 ? 40.812 -27.702 -3.140  1.00 16.82 ?  126 LEU   B CA   1 
ATOM   5974 C  C    . LEU   B 1 126 ? 40.939 -27.316 -1.673  1.00 16.92 ?  126 LEU   B C    1 
ATOM   5975 O  O    . LEU   B 1 126 ? 41.848 -27.775 -0.976  1.00 19.66 ?  126 LEU   B O    1 
ATOM   5976 C  CB   . LEU   B 1 126 ? 40.547 -29.199 -3.261  1.00 18.10 ?  126 LEU   B CB   1 
ATOM   5977 C  CG   . LEU   B 1 126 ? 40.026 -29.705 -4.604  1.00 19.02 ?  126 LEU   B CG   1 
ATOM   5978 C  CD1  . LEU   B 1 126 ? 40.043 -31.210 -4.628  1.00 20.67 ?  126 LEU   B CD1  1 
ATOM   5979 C  CD2  . LEU   B 1 126 ? 38.620 -29.198 -4.873  1.00 19.00 ?  126 LEU   B CD2  1 
ATOM   5980 H  H    . LEU   B 1 126 ? 42.547 -28.013 -4.031  1.00 19.03 ?  126 LEU   B H    1 
ATOM   5981 H  HA   . LEU   B 1 126 ? 40.063 -27.215 -3.521  1.00 20.24 ?  126 LEU   B HA   1 
ATOM   5982 H  HB2  . LEU   B 1 126 ? 41.373 -29.664 -3.084  1.00 21.78 ?  126 LEU   B HB2  1 
ATOM   5983 H  HB3  . LEU   B 1 126 ? 39.887 -29.440 -2.594  1.00 21.78 ?  126 LEU   B HB3  1 
ATOM   5984 H  HG   . LEU   B 1 126 ? 40.604 -29.378 -5.315  1.00 22.88 ?  126 LEU   B HG   1 
ATOM   5985 H  HD11 . LEU   B 1 126 ? 39.704 -31.516 -5.485  1.00 24.85 ?  126 LEU   B HD11 1 
ATOM   5986 H  HD12 . LEU   B 1 126 ? 40.951 -31.519 -4.500  1.00 24.85 ?  126 LEU   B HD12 1 
ATOM   5987 H  HD13 . LEU   B 1 126 ? 39.474 -31.541 -3.913  1.00 24.85 ?  126 LEU   B HD13 1 
ATOM   5988 H  HD21 . LEU   B 1 126 ? 38.288 -29.603 -5.692  1.00 22.85 ?  126 LEU   B HD21 1 
ATOM   5989 H  HD22 . LEU   B 1 126 ? 38.046 -29.448 -4.130  1.00 22.85 ?  126 LEU   B HD22 1 
ATOM   5990 H  HD23 . LEU   B 1 126 ? 38.635 -28.233 -4.967  1.00 22.85 ?  126 LEU   B HD23 1 
ATOM   5991 N  N    . LEU   B 1 127 ? 40.008 -26.495 -1.194  1.00 16.85 ?  127 LEU   B N    1 
ATOM   5992 C  CA   . LEU   B 1 127 ? 40.069 -26.006 0.174   1.00 17.13 ?  127 LEU   B CA   1 
ATOM   5993 C  C    . LEU   B 1 127 ? 39.797 -27.126 1.172   1.00 17.39 ?  127 LEU   B C    1 
ATOM   5994 O  O    . LEU   B 1 127 ? 38.983 -28.025 0.940   1.00 18.19 ?  127 LEU   B O    1 
ATOM   5995 C  CB   . LEU   B 1 127 ? 39.058 -24.876 0.388   1.00 17.55 ?  127 LEU   B CB   1 
ATOM   5996 C  CG   . LEU   B 1 127 ? 39.235 -23.627 -0.480  1.00 17.97 ?  127 LEU   B CG   1 
ATOM   5997 C  CD1  . LEU   B 1 127 ? 38.115 -22.651 -0.186  1.00 17.81 ?  127 LEU   B CD1  1 
ATOM   5998 C  CD2  . LEU   B 1 127 ? 40.605 -22.977 -0.268  1.00 18.51 ?  127 LEU   B CD2  1 
ATOM   5999 H  H    . LEU   B 1 127 ? 39.328 -26.199 -1.639  1.00 20.27 ?  127 LEU   B H    1 
ATOM   6000 H  HA   . LEU   B 1 127 ? 40.956 -25.652 0.345   1.00 20.61 ?  127 LEU   B HA   1 
ATOM   6001 H  HB2  . LEU   B 1 127 ? 38.169 -25.227 0.212   1.00 21.12 ?  127 LEU   B HB2  1 
ATOM   6002 H  HB3  . LEU   B 1 127 ? 39.108 -24.592 1.315   1.00 21.12 ?  127 LEU   B HB3  1 
ATOM   6003 H  HG   . LEU   B 1 127 ? 39.157 -23.882 -1.409  1.00 21.62 ?  127 LEU   B HG   1 
ATOM   6004 H  HD11 . LEU   B 1 127 ? 38.240 -21.854 -0.731  1.00 21.42 ?  127 LEU   B HD11 1 
ATOM   6005 H  HD12 . LEU   B 1 127 ? 37.262 -23.061 -0.396  1.00 21.42 ?  127 LEU   B HD12 1 
ATOM   6006 H  HD13 . LEU   B 1 127 ? 38.141 -22.407 0.755   1.00 21.42 ?  127 LEU   B HD13 1 
ATOM   6007 H  HD21 . LEU   B 1 127 ? 40.637 -22.144 -0.760  1.00 22.26 ?  127 LEU   B HD21 1 
ATOM   6008 H  HD22 . LEU   B 1 127 ? 40.731 -22.810 0.679   1.00 22.26 ?  127 LEU   B HD22 1 
ATOM   6009 H  HD23 . LEU   B 1 127 ? 41.289 -23.583 -0.591  1.00 22.26 ?  127 LEU   B HD23 1 
ATOM   6010 N  N    . SER   B 1 128 ? 40.470 -27.037 2.310   1.00 17.82 ?  128 SER   B N    1 
ATOM   6011 C  CA   . SER   B 1 128 ? 40.333 -27.949 3.430   1.00 18.33 ?  128 SER   B CA   1 
ATOM   6012 C  C    . SER   B 1 128 ? 40.804 -29.360 3.105   1.00 19.87 ?  128 SER   B C    1 
ATOM   6013 O  O    . SER   B 1 128 ? 40.682 -30.245 3.951   1.00 21.54 ?  128 SER   B O    1 
ATOM   6014 C  CB   . SER   B 1 128 ? 38.909 -27.929 3.987   1.00 18.59 ?  128 SER   B CB   1 
ATOM   6015 O  OG   . SER   B 1 128 ? 38.640 -26.653 4.560   1.00 19.23 ?  128 SER   B OG   1 
ATOM   6016 H  H    . SER   B 1 128 ? 41.047 -26.404 2.470   1.00 21.43 ?  128 SER   B H    1 
ATOM   6017 H  HA   . SER   B 1 128 ? 40.911 -27.637 4.138   1.00 22.05 ?  128 SER   B HA   1 
ATOM   6018 H  HB2  . SER   B 1 128 ? 38.282 -28.094 3.258   1.00 22.37 ?  128 SER   B HB2  1 
ATOM   6019 H  HB3  . SER   B 1 128 ? 38.822 -28.614 4.660   1.00 22.37 ?  128 SER   B HB3  1 
ATOM   6020 H  HG   . SER   B 1 128 ? 39.178 -26.504 5.184   1.00 23.13 ?  128 SER   B HG   1 
ATOM   6021 N  N    . ALA   B 1 129 ? 41.393 -29.580 1.927   1.00 20.85 ?  129 ALA   B N    1 
ATOM   6022 C  CA   . ALA   B 1 129 ? 41.930 -30.883 1.551   1.00 21.69 ?  129 ALA   B CA   1 
ATOM   6023 C  C    . ALA   B 1 129 ? 43.329 -31.078 2.130   1.00 20.81 ?  129 ALA   B C    1 
ATOM   6024 O  O    . ALA   B 1 129 ? 43.900 -30.187 2.773   1.00 20.72 ?  129 ALA   B O    1 
ATOM   6025 C  CB   . ALA   B 1 129 ? 41.962 -31.027 0.030   1.00 23.55 ?  129 ALA   B CB   1 
ATOM   6026 H  H    . ALA   B 1 129 ? 41.485 -28.975 1.321   1.00 25.07 ?  129 ALA   B H    1 
ATOM   6027 H  HA   . ALA   B 1 129 ? 41.349 -31.573 1.902   1.00 26.09 ?  129 ALA   B HA   1 
ATOM   6028 H  HB1  . ALA   B 1 129 ? 42.315 -31.903 -0.198  1.00 28.31 ?  129 ALA   B HB1  1 
ATOM   6029 H  HB2  . ALA   B 1 129 ? 41.060 -30.937 -0.320  1.00 28.31 ?  129 ALA   B HB2  1 
ATOM   6030 H  HB3  . ALA   B 1 129 ? 42.530 -30.336 -0.346  1.00 28.31 ?  129 ALA   B HB3  1 
ATOM   6031 N  N    . GLY   B 1 130 ? 43.889 -32.266 1.887   1.00 20.45 ?  130 GLY   B N    1 
ATOM   6032 C  CA   . GLY   B 1 130 ? 45.278 -32.513 2.231   1.00 20.80 ?  130 GLY   B CA   1 
ATOM   6033 C  C    . GLY   B 1 130 ? 45.507 -32.426 3.722   1.00 20.51 ?  130 GLY   B C    1 
ATOM   6034 O  O    . GLY   B 1 130 ? 44.817 -33.073 4.522   1.00 21.52 ?  130 GLY   B O    1 
ATOM   6035 H  H    . GLY   B 1 130 ? 43.487 -32.936 1.518   1.00 24.60 ?  130 GLY   B H    1 
ATOM   6036 H  HA2  . GLY   B 1 130 ? 45.533 -33.400 1.930   1.00 25.02 ?  130 GLY   B HA2  1 
ATOM   6037 H  HA3  . GLY   B 1 130 ? 45.839 -31.861 1.791   1.00 25.02 ?  130 GLY   B HA3  1 
ATOM   6038 N  N    . ILE   B 1 131 ? 46.498 -31.611 4.101   1.00 21.01 ?  131 ILE   B N    1 
ATOM   6039 C  CA   . ILE   B 1 131 ? 46.879 -31.478 5.500   1.00 21.76 ?  131 ILE   B CA   1 
ATOM   6040 C  C    . ILE   B 1 131 ? 45.785 -30.857 6.347   1.00 21.30 ?  131 ILE   B C    1 
ATOM   6041 O  O    . ILE   B 1 131 ? 45.884 -30.889 7.576   1.00 23.16 ?  131 ILE   B O    1 
ATOM   6042 C  CB   . ILE   B 1 131 ? 48.201 -30.693 5.660   1.00 23.45 ?  131 ILE   B CB   1 
ATOM   6043 C  CG1  . ILE   B 1 131 ? 48.001 -29.213 5.306   1.00 24.04 ?  131 ILE   B CG1  1 
ATOM   6044 C  CG2  . ILE   B 1 131 ? 49.299 -31.307 4.797   1.00 24.30 ?  131 ILE   B CG2  1 
ATOM   6045 C  CD1  . ILE   B 1 131 ? 49.224 -28.350 5.545   1.00 24.93 ?  131 ILE   B CD1  1 
ATOM   6046 H  H    . ILE   B 1 131 ? 46.961 -31.124 3.568   1.00 25.27 ?  131 ILE   B H    1 
ATOM   6047 H  HA   . ILE   B 1 131 ? 47.035 -32.364 5.857   1.00 26.16 ?  131 ILE   B HA   1 
ATOM   6048 H  HB   . ILE   B 1 131 ? 48.476 -30.747 6.588   1.00 28.19 ?  131 ILE   B HB   1 
ATOM   6049 H  HG12 . ILE   B 1 131 ? 47.767 -29.146 4.368   1.00 28.90 ?  131 ILE   B HG12 1 
ATOM   6050 H  HG13 . ILE   B 1 131 ? 47.283 -28.845 5.849   1.00 28.90 ?  131 ILE   B HG13 1 
ATOM   6051 H  HG21 . ILE   B 1 131 ? 50.147 -30.910 5.040   1.00 29.21 ?  131 ILE   B HG21 1 
ATOM   6052 H  HG22 . ILE   B 1 131 ? 49.318 -32.261 4.951   1.00 29.21 ?  131 ILE   B HG22 1 
ATOM   6053 H  HG23 . ILE   B 1 131 ? 49.100 -31.125 3.864   1.00 29.21 ?  131 ILE   B HG23 1 
ATOM   6054 H  HD11 . ILE   B 1 131 ? 48.984 -27.420 5.405   1.00 29.98 ?  131 ILE   B HD11 1 
ATOM   6055 H  HD12 . ILE   B 1 131 ? 49.526 -28.479 6.458   1.00 29.98 ?  131 ILE   B HD12 1 
ATOM   6056 H  HD13 . ILE   B 1 131 ? 49.920 -28.611 4.925   1.00 29.98 ?  131 ILE   B HD13 1 
ATOM   6057 N  N    . PHE   B 1 132 ? 44.748 -30.287 5.728   1.00 20.72 ?  132 PHE   B N    1 
ATOM   6058 C  CA   . PHE   B 1 132 ? 43.608 -29.764 6.471   1.00 21.18 ?  132 PHE   B CA   1 
ATOM   6059 C  C    . PHE   B 1 132 ? 42.585 -30.841 6.832   1.00 23.17 ?  132 PHE   B C    1 
ATOM   6060 O  O    . PHE   B 1 132 ? 41.700 -30.571 7.651   1.00 24.76 ?  132 PHE   B O    1 
ATOM   6061 C  CB   . PHE   B 1 132 ? 42.925 -28.651 5.672   1.00 20.00 ?  132 PHE   B CB   1 
ATOM   6062 C  CG   . PHE   B 1 132 ? 43.611 -27.309 5.771   1.00 19.85 ?  132 PHE   B CG   1 
ATOM   6063 C  CD1  . PHE   B 1 132 ? 44.929 -27.143 5.373   1.00 20.69 ?  132 PHE   B CD1  1 
ATOM   6064 C  CD2  . PHE   B 1 132 ? 42.914 -26.202 6.233   1.00 19.44 ?  132 PHE   B CD2  1 
ATOM   6065 C  CE1  . PHE   B 1 132 ? 45.544 -25.903 5.460   1.00 20.60 ?  132 PHE   B CE1  1 
ATOM   6066 C  CE2  . PHE   B 1 132 ? 43.522 -24.958 6.321   1.00 19.55 ?  132 PHE   B CE2  1 
ATOM   6067 C  CZ   . PHE   B 1 132 ? 44.839 -24.812 5.931   1.00 20.16 ?  132 PHE   B CZ   1 
ATOM   6068 H  H    . PHE   B 1 132 ? 44.683 -30.195 4.878   1.00 24.92 ?  132 PHE   B H    1 
ATOM   6069 H  HA   . PHE   B 1 132 ? 43.934 -29.375 7.298   1.00 25.47 ?  132 PHE   B HA   1 
ATOM   6070 H  HB2  . PHE   B 1 132 ? 42.908 -28.912 4.741   1.00 24.05 ?  132 PHE   B HB2  1 
ATOM   6071 H  HB3  . PHE   B 1 132 ? 42.017 -28.550 6.003   1.00 24.05 ?  132 PHE   B HB3  1 
ATOM   6072 H  HD1  . PHE   B 1 132 ? 45.414 -27.877 5.061   1.00 24.88 ?  132 PHE   B HD1  1 
ATOM   6073 H  HD2  . PHE   B 1 132 ? 42.028 -26.302 6.498   1.00 23.38 ?  132 PHE   B HD2  1 
ATOM   6074 H  HE1  . PHE   B 1 132 ? 46.431 -25.809 5.201   1.00 24.78 ?  132 PHE   B HE1  1 
ATOM   6075 H  HE2  . PHE   B 1 132 ? 43.044 -24.226 6.639   1.00 23.52 ?  132 PHE   B HE2  1 
ATOM   6076 H  HZ   . PHE   B 1 132 ? 45.249 -23.977 5.991   1.00 24.25 ?  132 PHE   B HZ   1 
ATOM   6077 N  N    . GLY   B 1 133 ? 42.662 -32.036 6.232   1.00 23.10 ?  133 GLY   B N    1 
ATOM   6078 C  CA   . GLY   B 1 133 ? 41.955 -33.201 6.742   1.00 23.54 ?  133 GLY   B CA   1 
ATOM   6079 C  C    . GLY   B 1 133 ? 40.549 -33.451 6.230   1.00 24.57 ?  133 GLY   B C    1 
ATOM   6080 O  O    . GLY   B 1 133 ? 39.943 -34.448 6.637   1.00 26.16 ?  133 GLY   B O    1 
ATOM   6081 H  H    . GLY   B 1 133 ? 43.122 -32.191 5.522   1.00 27.78 ?  133 GLY   B H    1 
ATOM   6082 H  HA2  . GLY   B 1 133 ? 42.482 -33.992 6.539   1.00 28.31 ?  133 GLY   B HA2  1 
ATOM   6083 H  HA3  . GLY   B 1 133 ? 41.906 -33.129 7.710   1.00 28.31 ?  133 GLY   B HA3  1 
ATOM   6084 N  N    . ALA   B 1 134 ? 40.002 -32.600 5.366   1.00 23.83 ?  134 ALA   B N    1 
ATOM   6085 C  CA   . ALA   B 1 134 ? 38.672 -32.879 4.846   1.00 23.26 ?  134 ALA   B CA   1 
ATOM   6086 C  C    . ALA   B 1 134 ? 38.744 -33.850 3.673   1.00 22.82 ?  134 ALA   B C    1 
ATOM   6087 O  O    . ALA   B 1 134 ? 39.792 -34.041 3.048   1.00 23.12 ?  134 ALA   B O    1 
ATOM   6088 C  CB   . ALA   B 1 134 ? 37.981 -31.593 4.401   1.00 23.33 ?  134 ALA   B CB   1 
ATOM   6089 H  H    . ALA   B 1 134 ? 40.372 -31.874 5.080   1.00 28.65 ?  134 ALA   B H    1 
ATOM   6090 H  HA   . ALA   B 1 134 ? 38.137 -33.281 5.549   1.00 27.96 ?  134 ALA   B HA   1 
ATOM   6091 H  HB1  . ALA   B 1 134 ? 37.083 -31.810 4.107   1.00 28.05 ?  134 ALA   B HB1  1 
ATOM   6092 H  HB2  . ALA   B 1 134 ? 37.947 -30.978 5.149   1.00 28.05 ?  134 ALA   B HB2  1 
ATOM   6093 H  HB3  . ALA   B 1 134 ? 38.485 -31.202 3.672   1.00 28.05 ?  134 ALA   B HB3  1 
ATOM   6094 N  N    . ASP   B 1 135 ? 37.605 -34.464 3.382   1.00 22.86 ?  135 ASP   B N    1 
ATOM   6095 C  CA   . ASP   B 1 135 ? 37.494 -35.352 2.237   1.00 23.53 ?  135 ASP   B CA   1 
ATOM   6096 C  C    . ASP   B 1 135 ? 37.591 -34.517 0.967   1.00 22.23 ?  135 ASP   B C    1 
ATOM   6097 O  O    . ASP   B 1 135 ? 36.736 -33.647 0.742   1.00 22.06 ?  135 ASP   B O    1 
ATOM   6098 C  CB   . ASP   B 1 135 ? 36.154 -36.077 2.292   1.00 25.17 ?  135 ASP   B CB   1 
ATOM   6099 C  CG   . ASP   B 1 135 ? 35.996 -37.110 1.191   1.00 26.70 ?  135 ASP   B CG   1 
ATOM   6100 O  OD1  . ASP   B 1 135 ? 36.845 -37.149 0.277   1.00 26.93 ?  135 ASP   B OD1  1 
ATOM   6101 O  OD2  . ASP   B 1 135 ? 35.030 -37.905 1.248   1.00 28.96 -1 135 ASP   B OD2  1 
ATOM   6102 H  H    . ASP   B 1 135 ? 36.880 -34.374 3.835   1.00 27.48 ?  135 ASP   B H    1 
ATOM   6103 H  HA   . ASP   B 1 135 ? 38.211 -36.005 2.268   1.00 28.29 ?  135 ASP   B HA   1 
ATOM   6104 H  HB2  . ASP   B 1 135 ? 36.081 -36.526 3.147   1.00 30.26 ?  135 ASP   B HB2  1 
ATOM   6105 H  HB3  . ASP   B 1 135 ? 35.446 -35.423 2.196   1.00 30.26 ?  135 ASP   B HB3  1 
ATOM   6106 N  N    . PRO   B 1 136 ? 38.604 -34.721 0.125   1.00 22.24 ?  136 PRO   B N    1 
ATOM   6107 C  CA   . PRO   B 1 136 ? 38.702 -33.905 -1.097  1.00 21.35 ?  136 PRO   B CA   1 
ATOM   6108 C  C    . PRO   B 1 136 ? 37.514 -34.067 -2.023  1.00 20.72 ?  136 PRO   B C    1 
ATOM   6109 O  O    . PRO   B 1 136 ? 37.186 -33.128 -2.754  1.00 20.37 ?  136 PRO   B O    1 
ATOM   6110 C  CB   . PRO   B 1 136 ? 40.009 -34.390 -1.740  1.00 21.88 ?  136 PRO   B CB   1 
ATOM   6111 C  CG   . PRO   B 1 136 ? 40.205 -35.780 -1.182  1.00 23.09 ?  136 PRO   B CG   1 
ATOM   6112 C  CD   . PRO   B 1 136 ? 39.688 -35.715 0.220   1.00 22.87 ?  136 PRO   B CD   1 
ATOM   6113 H  HA   . PRO   B 1 136 ? 38.793 -32.970 -0.873  1.00 25.67 ?  136 PRO   B HA   1 
ATOM   6114 H  HB2  . PRO   B 1 136 ? 39.917 -34.419 -2.706  1.00 26.31 ?  136 PRO   B HB2  1 
ATOM   6115 H  HB3  . PRO   B 1 136 ? 40.740 -33.810 -1.480  1.00 26.31 ?  136 PRO   B HB3  1 
ATOM   6116 H  HG2  . PRO   B 1 136 ? 39.694 -36.424 -1.701  1.00 27.76 ?  136 PRO   B HG2  1 
ATOM   6117 H  HG3  . PRO   B 1 136 ? 41.148 -36.013 -1.185  1.00 27.76 ?  136 PRO   B HG3  1 
ATOM   6118 H  HD2  . PRO   B 1 136 ? 39.333 -36.574 0.496   1.00 27.50 ?  136 PRO   B HD2  1 
ATOM   6119 H  HD3  . PRO   B 1 136 ? 40.380 -35.404 0.829   1.00 27.50 ?  136 PRO   B HD3  1 
ATOM   6120 N  N    . ILE   B 1 137 ? 36.866 -35.237 -2.026  1.00 21.03 ?  137 ILE   B N    1 
ATOM   6121 C  CA   . ILE   B 1 137 ? 35.646 -35.408 -2.811  1.00 21.18 ?  137 ILE   B CA   1 
ATOM   6122 C  C    . ILE   B 1 137 ? 34.575 -34.437 -2.334  1.00 20.49 ?  137 ILE   B C    1 
ATOM   6123 O  O    . ILE   B 1 137 ? 33.854 -33.830 -3.137  1.00 20.58 ?  137 ILE   B O    1 
ATOM   6124 C  CB   . ILE   B 1 137 ? 35.175 -36.877 -2.746  1.00 22.69 ?  137 ILE   B CB   1 
ATOM   6125 C  CG1  . ILE   B 1 137 ? 36.180 -37.784 -3.460  1.00 24.60 ?  137 ILE   B CG1  1 
ATOM   6126 C  CG2  . ILE   B 1 137 ? 33.781 -37.035 -3.349  1.00 23.42 ?  137 ILE   B CG2  1 
ATOM   6127 C  CD1  . ILE   B 1 137 ? 35.908 -39.265 -3.283  1.00 26.50 ?  137 ILE   B CD1  1 
ATOM   6128 H  H    . ILE   B 1 137 ? 37.109 -35.939 -1.590  1.00 25.29 ?  137 ILE   B H    1 
ATOM   6129 H  HA   . ILE   B 1 137 ? 35.837 -35.206 -3.740  1.00 25.47 ?  137 ILE   B HA   1 
ATOM   6130 H  HB   . ILE   B 1 137 ? 35.132 -37.145 -1.818  1.00 27.28 ?  137 ILE   B HB   1 
ATOM   6131 H  HG12 . ILE   B 1 137 ? 36.156 -37.601 -4.412  1.00 29.57 ?  137 ILE   B HG12 1 
ATOM   6132 H  HG13 . ILE   B 1 137 ? 37.066 -37.612 -3.112  1.00 29.57 ?  137 ILE   B HG13 1 
ATOM   6133 H  HG21 . ILE   B 1 137 ? 33.554 -37.982 -3.400  1.00 28.16 ?  137 ILE   B HG21 1 
ATOM   6134 H  HG22 . ILE   B 1 137 ? 33.133 -36.587 -2.784  1.00 28.16 ?  137 ILE   B HG22 1 
ATOM   6135 H  HG23 . ILE   B 1 137 ? 33.771 -36.653 -4.238  1.00 28.16 ?  137 ILE   B HG23 1 
ATOM   6136 H  HD11 . ILE   B 1 137 ? 36.610 -39.762 -3.728  1.00 31.86 ?  137 ILE   B HD11 1 
ATOM   6137 H  HD12 . ILE   B 1 137 ? 35.901 -39.479 -2.335  1.00 31.86 ?  137 ILE   B HD12 1 
ATOM   6138 H  HD13 . ILE   B 1 137 ? 35.051 -39.491 -3.679  1.00 31.86 ?  137 ILE   B HD13 1 
ATOM   6139 N  N    . HIS   B 1 138 ? 34.446 -34.284 -1.016  1.00 20.57 ?  138 HIS   B N    1 
ATOM   6140 C  CA   . HIS   B 1 138 ? 33.491 -33.321 -0.483  1.00 21.05 ?  138 HIS   B CA   1 
ATOM   6141 C  C    . HIS   B 1 138 ? 33.899 -31.893 -0.818  1.00 20.73 ?  138 HIS   B C    1 
ATOM   6142 O  O    . HIS   B 1 138 ? 33.046 -31.054 -1.132  1.00 21.29 ?  138 HIS   B O    1 
ATOM   6143 C  CB   . HIS   B 1 138 ? 33.374 -33.484 1.025   1.00 22.35 ?  138 HIS   B CB   1 
ATOM   6144 C  CG   . HIS   B 1 138 ? 32.443 -32.502 1.652   1.00 23.78 ?  138 HIS   B CG   1 
ATOM   6145 N  ND1  . HIS   B 1 138 ? 31.100 -32.449 1.342   1.00 24.92 ?  138 HIS   B ND1  1 
ATOM   6146 C  CD2  . HIS   B 1 138 ? 32.664 -31.506 2.541   1.00 24.27 ?  138 HIS   B CD2  1 
ATOM   6147 C  CE1  . HIS   B 1 138 ? 30.531 -31.478 2.031   1.00 25.19 ?  138 HIS   B CE1  1 
ATOM   6148 N  NE2  . HIS   B 1 138 ? 31.457 -30.895 2.770   1.00 24.57 ?  138 HIS   B NE2  1 
ATOM   6149 H  H    . HIS   B 1 138 ? 34.894 -34.720 -0.423  1.00 24.74 ?  138 HIS   B H    1 
ATOM   6150 H  HA   . HIS   B 1 138 ? 32.620 -33.492 -0.872  1.00 25.32 ?  138 HIS   B HA   1 
ATOM   6151 H  HB2  . HIS   B 1 138 ? 33.039 -34.377 1.222   1.00 26.88 ?  138 HIS   B HB2  1 
ATOM   6152 H  HB3  . HIS   B 1 138 ? 34.247 -33.367 1.427   1.00 26.88 ?  138 HIS   B HB3  1 
ATOM   6153 H  HD1  . HIS   B 1 138 ? 30.697 -32.978 0.795   1.00 29.96 ?  138 HIS   B HD1  1 
ATOM   6154 H  HD2  . HIS   B 1 138 ? 33.469 -31.288 2.945   1.00 29.18 ?  138 HIS   B HD2  1 
ATOM   6155 H  HE1  . HIS   B 1 138 ? 29.625 -31.253 2.006   1.00 30.28 ?  138 HIS   B HE1  1 
ATOM   6156 N  N    . SER   B 1 139 ? 35.191 -31.582 -0.737  1.00 19.97 ?  139 SER   B N    1 
ATOM   6157 C  CA   . SER   B 1 139 ? 35.621 -30.228 -1.058  1.00 19.14 ?  139 SER   B CA   1 
ATOM   6158 C  C    . SER   B 1 139 ? 35.303 -29.890 -2.504  1.00 18.40 ?  139 SER   B C    1 
ATOM   6159 O  O    . SER   B 1 139 ? 34.858 -28.776 -2.802  1.00 18.83 ?  139 SER   B O    1 
ATOM   6160 C  CB   . SER   B 1 139 ? 37.116 -30.092 -0.792  1.00 19.86 ?  139 SER   B CB   1 
ATOM   6161 O  OG   . SER   B 1 139 ? 37.535 -28.756 -0.999  1.00 19.85 ?  139 SER   B OG   1 
ATOM   6162 H  H    . SER   B 1 139 ? 35.817 -32.118 -0.502  1.00 24.02 ?  139 SER   B H    1 
ATOM   6163 H  HA   . SER   B 1 139 ? 35.146 -29.597 -0.495  1.00 23.02 ?  139 SER   B HA   1 
ATOM   6164 H  HB2  . SER   B 1 139 ? 37.294 -30.343 0.127   1.00 23.89 ?  139 SER   B HB2  1 
ATOM   6165 H  HB3  . SER   B 1 139 ? 37.601 -30.664 -1.399  1.00 23.89 ?  139 SER   B HB3  1 
ATOM   6166 H  HG   . SER   B 1 139 ? 38.361 -28.682 -0.835  1.00 23.87 ?  139 SER   B HG   1 
ATOM   6167 N  N    . LEU   B 1 140 ? 35.503 -30.841 -3.415  1.00 18.26 ?  140 LEU   B N    1 
ATOM   6168 C  CA   . LEU   B 1 140 ? 35.146 -30.603 -4.808  1.00 18.34 ?  140 LEU   B CA   1 
ATOM   6169 C  C    . LEU   B 1 140 ? 33.643 -30.371 -4.950  1.00 18.60 ?  140 LEU   B C    1 
ATOM   6170 O  O    . LEU   B 1 140 ? 33.209 -29.488 -5.695  1.00 19.05 ?  140 LEU   B O    1 
ATOM   6171 C  CB   . LEU   B 1 140 ? 35.619 -31.769 -5.677  1.00 18.06 ?  140 LEU   B CB   1 
ATOM   6172 C  CG   . LEU   B 1 140 ? 35.261 -31.662 -7.151  1.00 18.79 ?  140 LEU   B CG   1 
ATOM   6173 C  CD1  . LEU   B 1 140 ? 35.836 -30.391 -7.733  1.00 19.39 ?  140 LEU   B CD1  1 
ATOM   6174 C  CD2  . LEU   B 1 140 ? 35.748 -32.893 -7.896  1.00 19.53 ?  140 LEU   B CD2  1 
ATOM   6175 H  H    . LEU   B 1 140 ? 35.840 -31.615 -3.258  1.00 21.97 ?  140 LEU   B H    1 
ATOM   6176 H  HA   . LEU   B 1 140 ? 35.599 -29.803 -5.113  1.00 22.06 ?  140 LEU   B HA   1 
ATOM   6177 H  HB2  . LEU   B 1 140 ? 36.588 -31.824 -5.619  1.00 21.72 ?  140 LEU   B HB2  1 
ATOM   6178 H  HB3  . LEU   B 1 140 ? 35.227 -32.587 -5.343  1.00 21.72 ?  140 LEU   B HB3  1 
ATOM   6179 H  HG   . LEU   B 1 140 ? 34.296 -31.616 -7.240  1.00 22.60 ?  140 LEU   B HG   1 
ATOM   6180 H  HD11 . LEU   B 1 140 ? 35.754 -30.420 -8.696  1.00 23.33 ?  140 LEU   B HD11 1 
ATOM   6181 H  HD12 . LEU   B 1 140 ? 35.342 -29.628 -7.383  1.00 23.33 ?  140 LEU   B HD12 1 
ATOM   6182 H  HD13 . LEU   B 1 140 ? 36.770 -30.321 -7.479  1.00 23.33 ?  140 LEU   B HD13 1 
ATOM   6183 H  HD21 . LEU   B 1 140 ? 35.506 -32.803 -8.831  1.00 23.49 ?  140 LEU   B HD21 1 
ATOM   6184 H  HD22 . LEU   B 1 140 ? 36.707 -32.954 -7.802  1.00 23.49 ?  140 LEU   B HD22 1 
ATOM   6185 H  HD23 . LEU   B 1 140 ? 35.320 -33.672 -7.514  1.00 23.49 ?  140 LEU   B HD23 1 
ATOM   6186 N  N    . ARG   B 1 141 ? 32.833 -31.167 -4.245  1.00 18.74 ?  141 ARG   B N    1 
ATOM   6187 C  CA   . ARG   B 1 141 ? 31.383 -30.987 -4.245  1.00 19.65 ?  141 ARG   B CA   1 
ATOM   6188 C  C    . ARG   B 1 141 ? 31.003 -29.576 -3.818  1.00 19.11 ?  141 ARG   B C    1 
ATOM   6189 O  O    . ARG   B 1 141 ? 30.205 -28.901 -4.481  1.00 19.82 ?  141 ARG   B O    1 
ATOM   6190 C  CB   . ARG   B 1 141 ? 30.785 -32.019 -3.281  1.00 20.43 ?  141 ARG   B CB   1 
ATOM   6191 C  CG   . ARG   B 1 141 ? 29.312 -31.910 -2.999  1.00 22.57 ?  141 ARG   B CG   1 
ATOM   6192 C  CD   . ARG   B 1 141 ? 28.546 -32.558 -4.087  1.00 24.46 ?  141 ARG   B CD   1 
ATOM   6193 N  NE   . ARG   B 1 141 ? 28.254 -31.635 -5.171  1.00 24.66 ?  141 ARG   B NE   1 
ATOM   6194 C  CZ   . ARG   B 1 141 ? 28.238 -31.963 -6.455  1.00 24.42 ?  141 ARG   B CZ   1 
ATOM   6195 N  NH1  . ARG   B 1 141 ? 28.646 -33.152 -6.872  1.00 24.01 ?  141 ARG   B NH1  1 
ATOM   6196 N  NH2  . ARG   B 1 141 ? 27.794 -31.080 -7.343  1.00 25.95 ?  141 ARG   B NH2  1 
ATOM   6197 H  H    . ARG   B 1 141 ? 33.107 -31.817 -3.757  1.00 22.55 ?  141 ARG   B H    1 
ATOM   6198 H  HA   . ARG   B 1 141 ? 31.033 -31.145 -5.134  1.00 23.63 ?  141 ARG   B HA   1 
ATOM   6199 H  HB2  . ARG   B 1 141 ? 30.961 -32.901 -3.642  1.00 24.57 ?  141 ARG   B HB2  1 
ATOM   6200 H  HB3  . ARG   B 1 141 ? 31.245 -31.931 -2.432  1.00 24.57 ?  141 ARG   B HB3  1 
ATOM   6201 H  HG2  . ARG   B 1 141 ? 29.115 -32.356 -2.165  1.00 27.14 ?  141 ARG   B HG2  1 
ATOM   6202 H  HG3  . ARG   B 1 141 ? 29.050 -30.973 -2.949  1.00 27.14 ?  141 ARG   B HG3  1 
ATOM   6203 H  HD2  . ARG   B 1 141 ? 29.062 -33.302 -4.440  1.00 29.41 ?  141 ARG   B HD2  1 
ATOM   6204 H  HD3  . ARG   B 1 141 ? 27.710 -32.883 -3.729  1.00 29.41 ?  141 ARG   B HD3  1 
ATOM   6205 H  HE   . ARG   B 1 141 ? 28.089 -30.813 -4.962  1.00 29.65 ?  141 ARG   B HE   1 
ATOM   6206 H  HH11 . ARG   B 1 141 ? 28.925 -33.739 -6.310  1.00 28.87 ?  141 ARG   B HH11 1 
ATOM   6207 H  HH12 . ARG   B 1 141 ? 28.630 -33.336 -7.709  1.00 28.87 ?  141 ARG   B HH12 1 
ATOM   6208 H  HH21 . ARG   B 1 141 ? 27.533 -30.299 -7.084  1.00 31.20 ?  141 ARG   B HH21 1 
ATOM   6209 H  HH22 . ARG   B 1 141 ? 27.794 -31.272 -8.181  1.00 31.20 ?  141 ARG   B HH22 1 
ATOM   6210 N  N    . VAL   B 1 142 ? 31.542 -29.130 -2.686  1.00 19.24 ?  142 VAL   B N    1 
ATOM   6211 C  CA   . VAL   B 1 142 ? 31.207 -27.794 -2.207  1.00 18.32 ?  142 VAL   B CA   1 
ATOM   6212 C  C    . VAL   B 1 142 ? 31.688 -26.739 -3.197  1.00 18.55 ?  142 VAL   B C    1 
ATOM   6213 O  O    . VAL   B 1 142 ? 30.985 -25.763 -3.476  1.00 19.15 ?  142 VAL   B O    1 
ATOM   6214 C  CB   . VAL   B 1 142 ? 31.755 -27.564 -0.786  1.00 18.70 ?  142 VAL   B CB   1 
ATOM   6215 C  CG1  . VAL   B 1 142 ? 31.437 -26.142 -0.321  1.00 18.59 ?  142 VAL   B CG1  1 
ATOM   6216 C  CG2  . VAL   B 1 142 ? 31.192 -28.581 0.186   1.00 19.55 ?  142 VAL   B CG2  1 
ATOM   6217 H  H    . VAL   B 1 142 ? 32.083 -29.572 -2.185  1.00 23.14 ?  142 VAL   B H    1 
ATOM   6218 H  HA   . VAL   B 1 142 ? 30.245 -27.721 -2.155  1.00 22.04 ?  142 VAL   B HA   1 
ATOM   6219 H  HB   . VAL   B 1 142 ? 32.719 -27.664 -0.797  1.00 22.50 ?  142 VAL   B HB   1 
ATOM   6220 H  HG11 . VAL   B 1 142 ? 31.617 -26.073 0.628   1.00 22.37 ?  142 VAL   B HG11 1 
ATOM   6221 H  HG12 . VAL   B 1 142 ? 31.998 -25.517 -0.809  1.00 22.37 ?  142 VAL   B HG12 1 
ATOM   6222 H  HG13 . VAL   B 1 142 ? 30.502 -25.955 -0.496  1.00 22.37 ?  142 VAL   B HG13 1 
ATOM   6223 H  HG21 . VAL   B 1 142 ? 31.526 -28.385 1.076   1.00 23.51 ?  142 VAL   B HG21 1 
ATOM   6224 H  HG22 . VAL   B 1 142 ? 30.225 -28.526 0.176   1.00 23.51 ?  142 VAL   B HG22 1 
ATOM   6225 H  HG23 . VAL   B 1 142 ? 31.477 -29.468 -0.086  1.00 23.51 ?  142 VAL   B HG23 1 
ATOM   6226 N  N    . CYS   B 1 143 ? 32.875 -26.938 -3.771  1.00 18.12 ?  143 CYS   B N    1 
ATOM   6227 C  CA   . CYS   B 1 143 ? 33.367 -26.001 -4.776  1.00 18.07 ?  143 CYS   B CA   1 
ATOM   6228 C  C    . CYS   B 1 143 ? 32.366 -25.859 -5.918  1.00 18.13 ?  143 CYS   B C    1 
ATOM   6229 O  O    . CYS   B 1 143 ? 31.962 -24.750 -6.285  1.00 18.44 ?  143 CYS   B O    1 
ATOM   6230 C  CB   . CYS   B 1 143 ? 34.719 -26.486 -5.308  1.00 18.66 ?  143 CYS   B CB   1 
ATOM   6231 S  SG   . CYS   B 1 143 ? 35.462 -25.380 -6.528  1.00 18.60 ?  143 CYS   B SG   1 
ATOM   6232 H  H    . CYS   B 1 143 ? 33.412 -27.587 -3.594  1.00 21.80 ?  143 CYS   B H    1 
ATOM   6233 H  HA   . CYS   B 1 143 ? 33.498 -25.125 -4.372  1.00 21.74 ?  143 CYS   B HA   1 
ATOM   6234 H  HB2  . CYS   B 1 143 ? 35.341 -26.570 -4.567  1.00 22.45 ?  143 CYS   B HB2  1 
ATOM   6235 H  HB3  . CYS   B 1 143 ? 34.595 -27.351 -5.726  1.00 22.45 ?  143 CYS   B HB3  1 
ATOM   6236 H  HG   . CYS   B 1 143 ? 36.542 -25.809 -6.840  1.00 22.37 ?  143 CYS   B HG   1 
ATOM   6237 N  N    . VAL   B 1 144 ? 31.958 -26.987 -6.500  1.00 18.88 ?  144 VAL   B N    1 
ATOM   6238 C  CA   . VAL   B 1 144 ? 31.048 -26.937 -7.639  1.00 20.04 ?  144 VAL   B CA   1 
ATOM   6239 C  C    . VAL   B 1 144 ? 29.702 -26.333 -7.264  1.00 20.56 ?  144 VAL   B C    1 
ATOM   6240 O  O    . VAL   B 1 144 ? 29.090 -25.618 -8.069  1.00 21.58 ?  144 VAL   B O    1 
ATOM   6241 C  CB   . VAL   B 1 144 ? 30.897 -28.345 -8.226  1.00 21.92 ?  144 VAL   B CB   1 
ATOM   6242 C  CG1  . VAL   B 1 144 ? 29.600 -28.487 -9.032  1.00 24.34 ?  144 VAL   B CG1  1 
ATOM   6243 C  CG2  . VAL   B 1 144 ? 32.123 -28.718 -9.054  1.00 22.53 ?  144 VAL   B CG2  1 
ATOM   6244 H  H    . VAL   B 1 144 ? 32.190 -27.778 -6.257  1.00 22.71 ?  144 VAL   B H    1 
ATOM   6245 H  HA   . VAL   B 1 144 ? 31.430 -26.372 -8.323  1.00 24.11 ?  144 VAL   B HA   1 
ATOM   6246 H  HB   . VAL   B 1 144 ? 30.843 -28.979 -7.493  1.00 26.36 ?  144 VAL   B HB   1 
ATOM   6247 H  HG11 . VAL   B 1 144 ? 29.675 -29.271 -9.602  1.00 29.26 ?  144 VAL   B HG11 1 
ATOM   6248 H  HG12 . VAL   B 1 144 ? 28.856 -28.596 -8.422  1.00 29.26 ?  144 VAL   B HG12 1 
ATOM   6249 H  HG13 . VAL   B 1 144 ? 29.479 -27.696 -9.577  1.00 29.26 ?  144 VAL   B HG13 1 
ATOM   6250 H  HG21 . VAL   B 1 144 ? 32.008 -29.612 -9.407  1.00 27.10 ?  144 VAL   B HG21 1 
ATOM   6251 H  HG22 . VAL   B 1 144 ? 32.212 -28.082 -9.785  1.00 27.10 ?  144 VAL   B HG22 1 
ATOM   6252 H  HG23 . VAL   B 1 144 ? 32.907 -28.679 -8.487  1.00 27.10 ?  144 VAL   B HG23 1 
ATOM   6253 N  N    . ASP   B 1 145 ? 29.239 -26.570 -6.042  1.00 21.10 ?  145 ASP   B N    1 
ATOM   6254 C  CA   . ASP   B 1 145 ? 27.933 -26.097 -5.611  1.00 21.56 ?  145 ASP   B CA   1 
ATOM   6255 C  C    . ASP   B 1 145 ? 27.963 -24.675 -5.080  1.00 21.19 ?  145 ASP   B C    1 
ATOM   6256 O  O    . ASP   B 1 145 ? 26.906 -24.139 -4.739  1.00 22.48 ?  145 ASP   B O    1 
ATOM   6257 C  CB   . ASP   B 1 145 ? 27.355 -27.014 -4.524  1.00 23.06 ?  145 ASP   B CB   1 
ATOM   6258 C  CG   . ASP   B 1 145 ? 26.995 -28.390 -5.037  1.00 24.31 ?  145 ASP   B CG   1 
ATOM   6259 O  OD1  . ASP   B 1 145 ? 26.890 -28.579 -6.268  1.00 24.45 ?  145 ASP   B OD1  1 
ATOM   6260 O  OD2  . ASP   B 1 145 ? 26.815 -29.281 -4.189  1.00 26.59 -1 145 ASP   B OD2  1 
ATOM   6261 H  H    . ASP   B 1 145 ? 29.671 -27.000 -5.433  1.00 25.38 ?  145 ASP   B H    1 
ATOM   6262 H  HA   . ASP   B 1 145 ? 27.331 -26.095 -6.363  1.00 25.92 ?  145 ASP   B HA   1 
ATOM   6263 H  HB2  . ASP   B 1 145 ? 28.008 -27.127 -3.824  1.00 27.73 ?  145 ASP   B HB2  1 
ATOM   6264 H  HB3  . ASP   B 1 145 ? 26.548 -26.602 -4.166  1.00 27.73 ?  145 ASP   B HB3  1 
ATOM   6265 N  N    . THR   B 1 146 ? 29.133 -24.051 -5.006  1.00 19.37 ?  146 THR   B N    1 
ATOM   6266 C  CA   . THR   B 1 146 ? 29.272 -22.730 -4.405  1.00 18.87 ?  146 THR   B CA   1 
ATOM   6267 C  C    . THR   B 1 146 ? 29.906 -21.710 -5.332  1.00 18.43 ?  146 THR   B C    1 
ATOM   6268 O  O    . THR   B 1 146 ? 29.448 -20.552 -5.388  1.00 18.20 ?  146 THR   B O    1 
ATOM   6269 C  CB   . THR   B 1 146 ? 30.100 -22.835 -3.118  1.00 18.69 ?  146 THR   B CB   1 
ATOM   6270 O  OG1  . THR   B 1 146 ? 29.519 -23.829 -2.265  1.00 19.34 ?  146 THR   B OG1  1 
ATOM   6271 C  CG2  . THR   B 1 146 ? 30.171 -21.487 -2.395  1.00 19.06 ?  146 THR   B CG2  1 
ATOM   6272 H  H    . THR   B 1 146 ? 29.878 -24.367 -5.305  1.00 23.30 ?  146 THR   B H    1 
ATOM   6273 H  HA   . THR   B 1 146 ? 28.404 -22.389 -4.160  1.00 22.70 ?  146 THR   B HA   1 
ATOM   6274 H  HB   . THR   B 1 146 ? 31.012 -23.096 -3.333  1.00 22.48 ?  146 THR   B HB   1 
ATOM   6275 H  HG1  . THR   B 1 146 ? 29.560 -24.588 -2.636  1.00 23.26 ?  146 THR   B HG1  1 
ATOM   6276 H  HG21 . THR   B 1 146 ? 30.527 -21.599 -1.500  1.00 22.93 ?  146 THR   B HG21 1 
ATOM   6277 H  HG22 . THR   B 1 146 ? 30.746 -20.874 -2.884  1.00 22.93 ?  146 THR   B HG22 1 
ATOM   6278 H  HG23 . THR   B 1 146 ? 29.283 -21.099 -2.332  1.00 22.93 ?  146 THR   B HG23 1 
ATOM   6279 N  N    . VAL   B 1 147 ? 30.964 -22.092 -6.044  1.00 17.51 ?  147 VAL   B N    1 
ATOM   6280 C  CA   . VAL   B 1 147 ? 31.688 -21.146 -6.883  1.00 17.26 ?  147 VAL   B CA   1 
ATOM   6281 C  C    . VAL   B 1 147 ? 30.965 -21.014 -8.211  1.00 17.99 ?  147 VAL   B C    1 
ATOM   6282 O  O    . VAL   B 1 147 ? 30.597 -22.018 -8.837  1.00 18.84 ?  147 VAL   B O    1 
ATOM   6283 C  CB   . VAL   B 1 147 ? 33.144 -21.592 -7.084  1.00 17.13 ?  147 VAL   B CB   1 
ATOM   6284 C  CG1  . VAL   B 1 147 ? 33.895 -20.563 -7.919  1.00 16.62 ?  147 VAL   B CG1  1 
ATOM   6285 C  CG2  . VAL   B 1 147 ? 33.820 -21.799 -5.742  1.00 17.00 ?  147 VAL   B CG2  1 
ATOM   6286 H  H    . VAL   B 1 147 ? 31.284 -22.890 -6.063  1.00 21.07 ?  147 VAL   B H    1 
ATOM   6287 H  HA   . VAL   B 1 147 ? 31.701 -20.275 -6.459  1.00 20.77 ?  147 VAL   B HA   1 
ATOM   6288 H  HB   . VAL   B 1 147 ? 33.158 -22.436 -7.565  1.00 20.61 ?  147 VAL   B HB   1 
ATOM   6289 H  HG11 . VAL   B 1 147 ? 34.845 -20.767 -7.896  1.00 20.00 ?  147 VAL   B HG11 1 
ATOM   6290 H  HG12 . VAL   B 1 147 ? 33.578 -20.596 -8.836  1.00 20.00 ?  147 VAL   B HG12 1 
ATOM   6291 H  HG13 . VAL   B 1 147 ? 33.742 -19.679 -7.548  1.00 20.00 ?  147 VAL   B HG13 1 
ATOM   6292 H  HG21 . VAL   B 1 147 ? 34.761 -21.981 -5.887  1.00 20.46 ?  147 VAL   B HG21 1 
ATOM   6293 H  HG22 . VAL   B 1 147 ? 33.715 -20.995 -5.211  1.00 20.46 ?  147 VAL   B HG22 1 
ATOM   6294 H  HG23 . VAL   B 1 147 ? 33.403 -22.550 -5.292  1.00 20.46 ?  147 VAL   B HG23 1 
ATOM   6295 N  N    . ARG   B 1 148 ? 30.737 -19.765 -8.627  1.00 17.82 ?  148 ARG   B N    1 
ATOM   6296 C  CA   . ARG   B 1 148 ? 30.114 -19.455 -9.904  1.00 17.62 ?  148 ARG   B CA   1 
ATOM   6297 C  C    . ARG   B 1 148 ? 31.068 -18.774 -10.870 1.00 17.36 ?  148 ARG   B C    1 
ATOM   6298 O  O    . ARG   B 1 148 ? 30.796 -18.763 -12.074 1.00 19.01 ?  148 ARG   B O    1 
ATOM   6299 C  CB   . ARG   B 1 148 ? 28.873 -18.572 -9.696  1.00 17.88 ?  148 ARG   B CB   1 
ATOM   6300 C  CG   . ARG   B 1 148 ? 27.817 -19.261 -8.850  1.00 18.73 ?  148 ARG   B CG   1 
ATOM   6301 C  CD   . ARG   B 1 148 ? 26.608 -18.374 -8.554  1.00 19.37 ?  148 ARG   B CD   1 
ATOM   6302 N  NE   . ARG   B 1 148 ? 26.986 -17.173 -7.819  1.00 19.04 ?  148 ARG   B NE   1 
ATOM   6303 C  CZ   . ARG   B 1 148 ? 27.275 -17.140 -6.525  1.00 18.64 ?  148 ARG   B CZ   1 
ATOM   6304 N  NH1  . ARG   B 1 148 ? 27.204 -18.228 -5.769  1.00 18.41 ?  148 ARG   B NH1  1 
ATOM   6305 N  NH2  . ARG   B 1 148 ? 27.687 -15.995 -5.982  1.00 18.35 ?  148 ARG   B NH2  1 
ATOM   6306 H  H    . ARG   B 1 148 ? 30.946 -19.061 -8.173  1.00 21.44 ?  148 ARG   B H    1 
ATOM   6307 H  HA   . ARG   B 1 148 ? 29.822 -20.280 -10.318 1.00 21.19 ?  148 ARG   B HA   1 
ATOM   6308 H  HB2  . ARG   B 1 148 ? 29.140 -17.756 -9.245  1.00 21.51 ?  148 ARG   B HB2  1 
ATOM   6309 H  HB3  . ARG   B 1 148 ? 28.485 -18.366 -10.560 1.00 21.51 ?  148 ARG   B HB3  1 
ATOM   6310 H  HG2  . ARG   B 1 148 ? 27.505 -20.049 -9.324  1.00 22.54 ?  148 ARG   B HG2  1 
ATOM   6311 H  HG3  . ARG   B 1 148 ? 28.215 -19.521 -8.005  1.00 22.54 ?  148 ARG   B HG3  1 
ATOM   6312 H  HD2  . ARG   B 1 148 ? 26.203 -18.103 -9.390  1.00 23.30 ?  148 ARG   B HD2  1 
ATOM   6313 H  HD3  . ARG   B 1 148 ? 25.976 -18.873 -8.016  1.00 23.30 ?  148 ARG   B HD3  1 
ATOM   6314 H  HE   . ARG   B 1 148 ? 27.046 -16.438 -8.259  1.00 22.90 ?  148 ARG   B HE   1 
ATOM   6315 H  HH11 . ARG   B 1 148 ? 26.939 -18.975 -6.110  1.00 22.15 ?  148 ARG   B HH11 1 
ATOM   6316 H  HH12 . ARG   B 1 148 ? 27.387 -18.184 -4.931  1.00 22.15 ?  148 ARG   B HH12 1 
ATOM   6317 H  HH21 . ARG   B 1 148 ? 27.749 -15.287 -6.463  1.00 22.07 ?  148 ARG   B HH21 1 
ATOM   6318 H  HH22 . ARG   B 1 148 ? 27.876 -15.959 -5.142  1.00 22.07 ?  148 ARG   B HH22 1 
ATOM   6319 N  N    . THR   B 1 149 ? 32.170 -18.212 -10.373 1.00 17.46 ?  149 THR   B N    1 
ATOM   6320 C  CA   . THR   B 1 149 ? 33.220 -17.652 -11.209 1.00 17.52 ?  149 THR   B CA   1 
ATOM   6321 C  C    . THR   B 1 149 ? 34.102 -18.789 -11.723 1.00 17.22 ?  149 THR   B C    1 
ATOM   6322 O  O    . THR   B 1 149 ? 33.902 -19.959 -11.389 1.00 17.69 ?  149 THR   B O    1 
ATOM   6323 C  CB   . THR   B 1 149 ? 33.984 -16.597 -10.418 1.00 17.91 ?  149 THR   B CB   1 
ATOM   6324 O  OG1  . THR   B 1 149 ? 34.432 -17.182 -9.195  1.00 17.87 ?  149 THR   B OG1  1 
ATOM   6325 C  CG2  . THR   B 1 149 ? 33.084 -15.385 -10.138 1.00 18.18 ?  149 THR   B CG2  1 
ATOM   6326 H  H    . THR   B 1 149 ? 32.319 -18.136 -9.530  1.00 21.01 ?  149 THR   B H    1 
ATOM   6327 H  HA   . THR   B 1 149 ? 32.812 -17.213 -11.971 1.00 21.08 ?  149 THR   B HA   1 
ATOM   6328 H  HB   . THR   B 1 149 ? 34.751 -16.303 -10.923 1.00 21.55 ?  149 THR   B HB   1 
ATOM   6329 H  HG1  . THR   B 1 149 ? 34.833 -16.607 -8.724  1.00 21.50 ?  149 THR   B HG1  1 
ATOM   6330 H  HG21 . THR   B 1 149 ? 33.577 -14.710 -9.649  1.00 21.87 ?  149 THR   B HG21 1 
ATOM   6331 H  HG22 . THR   B 1 149 ? 32.774 -15.004 -10.976 1.00 21.87 ?  149 THR   B HG22 1 
ATOM   6332 H  HG23 . THR   B 1 149 ? 32.312 -15.655 -9.614  1.00 21.87 ?  149 THR   B HG23 1 
ATOM   6333 N  N    . ASN   B 1 150 ? 35.066 -18.464 -12.572 1.00 17.03 ?  150 ASN   B N    1 
ATOM   6334 C  CA   . ASN   B 1 150 ? 35.835 -19.486 -13.274 1.00 17.14 ?  150 ASN   B CA   1 
ATOM   6335 C  C    . ASN   B 1 150 ? 37.002 -19.934 -12.401 1.00 16.96 ?  150 ASN   B C    1 
ATOM   6336 O  O    . ASN   B 1 150 ? 37.948 -19.174 -12.180 1.00 17.39 ?  150 ASN   B O    1 
ATOM   6337 C  CB   . ASN   B 1 150 ? 36.301 -18.953 -14.623 1.00 19.27 ?  150 ASN   B CB   1 
ATOM   6338 C  CG   . ASN   B 1 150 ? 35.155 -18.758 -15.582 1.00 21.49 ?  150 ASN   B CG   1 
ATOM   6339 O  OD1  . ASN   B 1 150 ? 34.266 -19.595 -15.660 1.00 22.24 ?  150 ASN   B OD1  1 
ATOM   6340 N  ND2  . ASN   B 1 150 ? 35.154 -17.647 -16.299 1.00 23.06 ?  150 ASN   B ND2  1 
ATOM   6341 H  H    . ASN   B 1 150 ? 35.302 -17.654 -12.758 1.00 20.49 ?  150 ASN   B H    1 
ATOM   6342 H  HA   . ASN   B 1 150 ? 35.258 -20.253 -13.435 1.00 20.62 ?  150 ASN   B HA   1 
ATOM   6343 H  HB2  . ASN   B 1 150 ? 36.730 -18.091 -14.488 1.00 23.18 ?  150 ASN   B HB2  1 
ATOM   6344 H  HB3  . ASN   B 1 150 ? 36.921 -19.580 -15.014 1.00 23.18 ?  150 ASN   B HB3  1 
ATOM   6345 H  HD21 . ASN   B 1 150 ? 34.517 -17.492 -16.860 1.00 27.73 ?  150 ASN   B HD21 1 
ATOM   6346 H  HD22 . ASN   B 1 150 ? 35.791 -17.075 -16.212 1.00 27.73 ?  150 ASN   B HD22 1 
ATOM   6347 N  N    . VAL   B 1 151 ? 36.939 -21.168 -11.902 1.00 17.00 ?  151 VAL   B N    1 
ATOM   6348 C  CA   . VAL   B 1 151 ? 37.961 -21.702 -11.010 1.00 16.90 ?  151 VAL   B CA   1 
ATOM   6349 C  C    . VAL   B 1 151 ? 38.662 -22.878 -11.683 1.00 16.62 ?  151 VAL   B C    1 
ATOM   6350 O  O    . VAL   B 1 151 ? 38.017 -23.820 -12.167 1.00 17.45 ?  151 VAL   B O    1 
ATOM   6351 C  CB   . VAL   B 1 151 ? 37.405 -22.038 -9.608  1.00 17.26 ?  151 VAL   B CB   1 
ATOM   6352 C  CG1  . VAL   B 1 151 ? 36.237 -23.024 -9.680  1.00 18.26 ?  151 VAL   B CG1  1 
ATOM   6353 C  CG2  . VAL   B 1 151 ? 38.512 -22.550 -8.694  1.00 17.43 ?  151 VAL   B CG2  1 
ATOM   6354 H  H    . VAL   B 1 151 ? 36.295 -21.720 -12.067 1.00 20.46 ?  151 VAL   B H    1 
ATOM   6355 H  HA   . VAL   B 1 151 ? 38.626 -21.008 -10.878 1.00 20.34 ?  151 VAL   B HA   1 
ATOM   6356 H  HB   . VAL   B 1 151 ? 37.059 -21.218 -9.212  1.00 20.77 ?  151 VAL   B HB   1 
ATOM   6357 H  HG11 . VAL   B 1 151 ? 35.922 -23.206 -8.778  1.00 21.97 ?  151 VAL   B HG11 1 
ATOM   6358 H  HG12 . VAL   B 1 151 ? 35.519 -22.631 -10.203 1.00 21.97 ?  151 VAL   B HG12 1 
ATOM   6359 H  HG13 . VAL   B 1 151 ? 36.540 -23.843 -10.096 1.00 21.97 ?  151 VAL   B HG13 1 
ATOM   6360 H  HG21 . VAL   B 1 151 ? 38.161 -22.629 -7.791  1.00 20.97 ?  151 VAL   B HG21 1 
ATOM   6361 H  HG22 . VAL   B 1 151 ? 38.805 -23.418 -9.010  1.00 20.97 ?  151 VAL   B HG22 1 
ATOM   6362 H  HG23 . VAL   B 1 151 ? 39.247 -21.921 -8.708  1.00 20.97 ?  151 VAL   B HG23 1 
ATOM   6363 N  N    . TYR   B 1 152 ? 39.991 -22.786 -11.727 1.00 15.89 ?  152 TYR   B N    1 
ATOM   6364 C  CA   . TYR   B 1 152 ? 40.888 -23.775 -12.312 1.00 16.42 ?  152 TYR   B CA   1 
ATOM   6365 C  C    . TYR   B 1 152 ? 41.618 -24.446 -11.154 1.00 16.18 ?  152 TYR   B C    1 
ATOM   6366 O  O    . TYR   B 1 152 ? 42.477 -23.828 -10.515 1.00 16.27 ?  152 TYR   B O    1 
ATOM   6367 C  CB   . TYR   B 1 152 ? 41.853 -23.070 -13.271 1.00 17.19 ?  152 TYR   B CB   1 
ATOM   6368 C  CG   . TYR   B 1 152 ? 41.174 -22.612 -14.545 1.00 18.03 ?  152 TYR   B CG   1 
ATOM   6369 C  CD1  . TYR   B 1 152 ? 40.517 -21.385 -14.616 1.00 18.45 ?  152 TYR   B CD1  1 
ATOM   6370 C  CD2  . TYR   B 1 152 ? 41.171 -23.421 -15.671 1.00 19.14 ?  152 TYR   B CD2  1 
ATOM   6371 C  CE1  . TYR   B 1 152 ? 39.874 -20.987 -15.780 1.00 19.67 ?  152 TYR   B CE1  1 
ATOM   6372 C  CE2  . TYR   B 1 152 ? 40.537 -23.035 -16.832 1.00 20.09 ?  152 TYR   B CE2  1 
ATOM   6373 C  CZ   . TYR   B 1 152 ? 39.894 -21.814 -16.888 1.00 20.40 ?  152 TYR   B CZ   1 
ATOM   6374 O  OH   . TYR   B 1 152 ? 39.268 -21.442 -18.054 1.00 22.41 ?  152 TYR   B OH   1 
ATOM   6375 H  H    . TYR   B 1 152 ? 40.422 -22.113 -11.400 1.00 19.12 ?  152 TYR   B H    1 
ATOM   6376 H  HA   . TYR   B 1 152 ? 40.373 -24.437 -12.805 1.00 19.76 ?  152 TYR   B HA   1 
ATOM   6377 H  HB2  . TYR   B 1 152 ? 42.220 -22.288 -12.829 1.00 20.68 ?  152 TYR   B HB2  1 
ATOM   6378 H  HB3  . TYR   B 1 152 ? 42.566 -23.679 -13.513 1.00 20.68 ?  152 TYR   B HB3  1 
ATOM   6379 H  HD1  . TYR   B 1 152 ? 40.494 -20.828 -13.871 1.00 22.19 ?  152 TYR   B HD1  1 
ATOM   6380 H  HD2  . TYR   B 1 152 ? 41.598 -24.245 -15.639 1.00 23.02 ?  152 TYR   B HD2  1 
ATOM   6381 H  HE1  . TYR   B 1 152 ? 39.438 -20.164 -15.819 1.00 23.66 ?  152 TYR   B HE1  1 
ATOM   6382 H  HE2  . TYR   B 1 152 ? 40.551 -23.589 -17.576 1.00 24.16 ?  152 TYR   B HE2  1 
ATOM   6383 H  HH   . TYR   B 1 152 ? 39.369 -22.041 -18.635 1.00 26.95 ?  152 TYR   B HH   1 
ATOM   6384 N  N    . LEU   B 1 153 ? 41.237 -25.693 -10.865 1.00 15.88 ?  153 LEU   B N    1 
ATOM   6385 C  CA   . LEU   B 1 153 ? 41.749 -26.439 -9.723  1.00 15.47 ?  153 LEU   B CA   1 
ATOM   6386 C  C    . LEU   B 1 153 ? 42.979 -27.241 -10.118 1.00 15.85 ?  153 LEU   B C    1 
ATOM   6387 O  O    . LEU   B 1 153 ? 42.965 -27.966 -11.115 1.00 16.94 ?  153 LEU   B O    1 
ATOM   6388 C  CB   . LEU   B 1 153 ? 40.678 -27.399 -9.193  1.00 16.24 ?  153 LEU   B CB   1 
ATOM   6389 C  CG   . LEU   B 1 153 ? 39.421 -26.745 -8.617  1.00 16.89 ?  153 LEU   B CG   1 
ATOM   6390 C  CD1  . LEU   B 1 153 ? 38.324 -27.773 -8.448  1.00 17.86 ?  153 LEU   B CD1  1 
ATOM   6391 C  CD2  . LEU   B 1 153 ? 39.737 -26.079 -7.282  1.00 17.09 ?  153 LEU   B CD2  1 
ATOM   6392 H  H    . LEU   B 1 153 ? 40.647 -26.133 -11.325 1.00 19.11 ?  153 LEU   B H    1 
ATOM   6393 H  HA   . LEU   B 1 153 ? 41.982 -25.814 -9.021  1.00 18.62 ?  153 LEU   B HA   1 
ATOM   6394 H  HB2  . LEU   B 1 153 ? 40.399 -27.976 -9.917  1.00 19.54 ?  153 LEU   B HB2  1 
ATOM   6395 H  HB3  . LEU   B 1 153 ? 41.076 -27.932 -8.486  1.00 19.54 ?  153 LEU   B HB3  1 
ATOM   6396 H  HG   . LEU   B 1 153 ? 39.106 -26.054 -9.227  1.00 20.32 ?  153 LEU   B HG   1 
ATOM   6397 H  HD11 . LEU   B 1 153 ? 37.514 -27.319 -8.160  1.00 21.48 ?  153 LEU   B HD11 1 
ATOM   6398 H  HD12 . LEU   B 1 153 ? 38.175 -28.209 -9.296  1.00 21.48 ?  153 LEU   B HD12 1 
ATOM   6399 H  HD13 . LEU   B 1 153 ? 38.601 -28.413 -7.779  1.00 21.48 ?  153 LEU   B HD13 1 
ATOM   6400 H  HD21 . LEU   B 1 153 ? 38.925 -25.704 -6.909  1.00 20.57 ?  153 LEU   B HD21 1 
ATOM   6401 H  HD22 . LEU   B 1 153 ? 40.103 -26.744 -6.677  1.00 20.57 ?  153 LEU   B HD22 1 
ATOM   6402 H  HD23 . LEU   B 1 153 ? 40.390 -25.372 -7.424  1.00 20.57 ?  153 LEU   B HD23 1 
ATOM   6403 N  N    . ALA   B 1 154 ? 44.030 -27.128 -9.315  1.00 15.01 ?  154 ALA   B N    1 
ATOM   6404 C  CA   . ALA   B 1 154 ? 45.256 -27.892 -9.500  1.00 16.38 ?  154 ALA   B CA   1 
ATOM   6405 C  C    . ALA   B 1 154 ? 45.326 -28.968 -8.426  1.00 17.36 ?  154 ALA   B C    1 
ATOM   6406 O  O    . ALA   B 1 154 ? 45.264 -28.668 -7.226  1.00 18.69 ?  154 ALA   B O    1 
ATOM   6407 C  CB   . ALA   B 1 154 ? 46.483 -26.986 -9.435  1.00 16.97 ?  154 ALA   B CB   1 
ATOM   6408 H  H    . ALA   B 1 154 ? 44.044 -26.601 -8.633  1.00 18.06 ?  154 ALA   B H    1 
ATOM   6409 H  HA   . ALA   B 1 154 ? 45.234 -28.318 -10.366 1.00 19.71 ?  154 ALA   B HA   1 
ATOM   6410 H  HB1  . ALA   B 1 154 ? 47.279 -27.527 -9.560  1.00 20.42 ?  154 ALA   B HB1  1 
ATOM   6411 H  HB2  . ALA   B 1 154 ? 46.425 -26.318 -10.138 1.00 20.42 ?  154 ALA   B HB2  1 
ATOM   6412 H  HB3  . ALA   B 1 154 ? 46.514 -26.549 -8.568  1.00 20.42 ?  154 ALA   B HB3  1 
ATOM   6413 N  N    . VAL   B 1 155 ? 45.447 -30.217 -8.860  1.00 16.98 ?  155 VAL   B N    1 
ATOM   6414 C  CA   . VAL   B 1 155 ? 45.551 -31.366 -7.968  1.00 17.63 ?  155 VAL   B CA   1 
ATOM   6415 C  C    . VAL   B 1 155 ? 46.886 -32.043 -8.249  1.00 17.58 ?  155 VAL   B C    1 
ATOM   6416 O  O    . VAL   B 1 155 ? 47.120 -32.529 -9.363  1.00 19.30 ?  155 VAL   B O    1 
ATOM   6417 C  CB   . VAL   B 1 155 ? 44.389 -32.353 -8.158  1.00 18.68 ?  155 VAL   B CB   1 
ATOM   6418 C  CG1  . VAL   B 1 155 ? 44.585 -33.565 -7.265  1.00 18.77 ?  155 VAL   B CG1  1 
ATOM   6419 C  CG2  . VAL   B 1 155 ? 43.052 -31.669 -7.871  1.00 19.32 ?  155 VAL   B CG2  1 
ATOM   6420 H  H    . VAL   B 1 155 ? 45.479 -30.430 -9.696  1.00 20.43 ?  155 VAL   B H    1 
ATOM   6421 H  HA   . VAL   B 1 155 ? 45.544 -31.063 -7.050  1.00 21.21 ?  155 VAL   B HA   1 
ATOM   6422 H  HB   . VAL   B 1 155 ? 44.371 -32.653 -9.081  1.00 22.47 ?  155 VAL   B HB   1 
ATOM   6423 H  HG11 . VAL   B 1 155 ? 43.750 -34.062 -7.218  1.00 22.58 ?  155 VAL   B HG11 1 
ATOM   6424 H  HG12 . VAL   B 1 155 ? 45.279 -34.129 -7.641  1.00 22.58 ?  155 VAL   B HG12 1 
ATOM   6425 H  HG13 . VAL   B 1 155 ? 44.839 -33.268 -6.378  1.00 22.58 ?  155 VAL   B HG13 1 
ATOM   6426 H  HG21 . VAL   B 1 155 ? 42.335 -32.317 -7.965  1.00 23.24 ?  155 VAL   B HG21 1 
ATOM   6427 H  HG22 . VAL   B 1 155 ? 43.063 -31.320 -6.964  1.00 23.24 ?  155 VAL   B HG22 1 
ATOM   6428 H  HG23 . VAL   B 1 155 ? 42.922 -30.941 -8.501  1.00 23.24 ?  155 VAL   B HG23 1 
ATOM   6429 N  N    . PHE   B 1 156 ? 47.753 -32.078 -7.238  1.00 18.01 ?  156 PHE   B N    1 
ATOM   6430 C  CA   . PHE   B 1 156 ? 49.131 -32.532 -7.438  1.00 18.91 ?  156 PHE   B CA   1 
ATOM   6431 C  C    . PHE   B 1 156 ? 49.224 -34.032 -7.723  1.00 20.42 ?  156 PHE   B C    1 
ATOM   6432 O  O    . PHE   B 1 156 ? 49.947 -34.457 -8.633  1.00 22.40 ?  156 PHE   B O    1 
ATOM   6433 C  CB   . PHE   B 1 156 ? 49.963 -32.165 -6.212  1.00 19.05 ?  156 PHE   B CB   1 
ATOM   6434 C  CG   . PHE   B 1 156 ? 51.382 -32.635 -6.275  1.00 19.52 ?  156 PHE   B CG   1 
ATOM   6435 C  CD1  . PHE   B 1 156 ? 52.269 -32.091 -7.186  1.00 20.57 ?  156 PHE   B CD1  1 
ATOM   6436 C  CD2  . PHE   B 1 156 ? 51.836 -33.603 -5.402  1.00 20.29 ?  156 PHE   B CD2  1 
ATOM   6437 C  CE1  . PHE   B 1 156 ? 53.584 -32.514 -7.234  1.00 21.06 ?  156 PHE   B CE1  1 
ATOM   6438 C  CE2  . PHE   B 1 156 ? 53.146 -34.032 -5.446  1.00 21.36 ?  156 PHE   B CE2  1 
ATOM   6439 C  CZ   . PHE   B 1 156 ? 54.015 -33.491 -6.366  1.00 21.22 ?  156 PHE   B CZ   1 
ATOM   6440 H  H    . PHE   B 1 156 ? 47.566 -31.852 -6.430  1.00 21.67 ?  156 PHE   B H    1 
ATOM   6441 H  HA   . PHE   B 1 156 ? 49.500 -32.065 -8.200  1.00 22.75 ?  156 PHE   B HA   1 
ATOM   6442 H  HB2  . PHE   B 1 156 ? 49.972 -31.198 -6.130  1.00 22.92 ?  156 PHE   B HB2  1 
ATOM   6443 H  HB3  . PHE   B 1 156 ? 49.553 -32.558 -5.427  1.00 22.92 ?  156 PHE   B HB3  1 
ATOM   6444 H  HD1  . PHE   B 1 156 ? 51.978 -31.429 -7.775  1.00 24.74 ?  156 PHE   B HD1  1 
ATOM   6445 H  HD2  . PHE   B 1 156 ? 51.243 -33.972 -4.787  1.00 24.40 ?  156 PHE   B HD2  1 
ATOM   6446 H  HE1  . PHE   B 1 156 ? 54.175 -32.147 -7.853  1.00 25.33 ?  156 PHE   B HE1  1 
ATOM   6447 H  HE2  . PHE   B 1 156 ? 53.437 -34.695 -4.858  1.00 25.69 ?  156 PHE   B HE2  1 
ATOM   6448 H  HZ   . PHE   B 1 156 ? 54.903 -33.782 -6.392  1.00 25.52 ?  156 PHE   B HZ   1 
ATOM   6449 N  N    . ASP   B 1 157 ? 48.551 -34.855 -6.927  1.00 20.47 ?  157 ASP   B N    1 
ATOM   6450 C  CA   . ASP   B 1 157 ? 48.692 -36.303 -7.029  1.00 21.79 ?  157 ASP   B CA   1 
ATOM   6451 C  C    . ASP   B 1 157 ? 47.777 -36.845 -8.122  1.00 22.14 ?  157 ASP   B C    1 
ATOM   6452 O  O    . ASP   B 1 157 ? 46.553 -36.732 -8.023  1.00 21.93 ?  157 ASP   B O    1 
ATOM   6453 C  CB   . ASP   B 1 157 ? 48.322 -36.917 -5.685  1.00 23.37 ?  157 ASP   B CB   1 
ATOM   6454 C  CG   . ASP   B 1 157 ? 48.468 -38.419 -5.669  1.00 25.24 ?  157 ASP   B CG   1 
ATOM   6455 O  OD1  . ASP   B 1 157 ? 48.837 -39.005 -6.712  1.00 25.79 ?  157 ASP   B OD1  1 
ATOM   6456 O  OD2  . ASP   B 1 157 ? 48.217 -39.007 -4.602  1.00 27.29 -1 157 ASP   B OD2  1 
ATOM   6457 H  H    . ASP   B 1 157 ? 48.015 -34.600 -6.310  1.00 24.62 ?  157 ASP   B H    1 
ATOM   6458 H  HA   . ASP   B 1 157 ? 49.614 -36.541 -7.236  1.00 26.20 ?  157 ASP   B HA   1 
ATOM   6459 H  HB2  . ASP   B 1 157 ? 48.892 -36.536 -4.996  1.00 28.10 ?  157 ASP   B HB2  1 
ATOM   6460 H  HB3  . ASP   B 1 157 ? 47.392 -36.709 -5.487  1.00 28.10 ?  157 ASP   B HB3  1 
ATOM   6461 N  N    . LYS   B 1 158 ? 48.367 -37.480 -9.140  1.00 23.10 ?  158 LYS   B N    1 
ATOM   6462 C  CA   . LYS   B 1 158 ? 47.581 -38.100 -10.210 1.00 24.10 ?  158 LYS   B CA   1 
ATOM   6463 C  C    . LYS   B 1 158 ? 46.531 -39.068 -9.663  1.00 24.67 ?  158 LYS   B C    1 
ATOM   6464 O  O    . LYS   B 1 158 ? 45.420 -39.167 -10.203 1.00 24.78 ?  158 LYS   B O    1 
ATOM   6465 C  CB   . LYS   B 1 158 ? 48.523 -38.824 -11.180 1.00 26.08 ?  158 LYS   B CB   1 
ATOM   6466 C  CG   . LYS   B 1 158 ? 47.839 -39.744 -12.184 1.00 28.59 ?  158 LYS   B CG   1 
ATOM   6467 C  CD   . LYS   B 1 158 ? 47.001 -38.979 -13.189 1.00 30.81 ?  158 LYS   B CD   1 
ATOM   6468 C  CE   . LYS   B 1 158 ? 46.373 -39.924 -14.203 1.00 33.09 ?  158 LYS   B CE   1 
ATOM   6469 N  NZ   . LYS   B 1 158 ? 45.307 -39.266 -15.010 1.00 33.75 ?  158 LYS   B NZ   1 
ATOM   6470 H  H    . LYS   B 1 158 ? 49.221 -37.572 -9.231  1.00 27.78 ?  158 LYS   B H    1 
ATOM   6471 H  HA   . LYS   B 1 158 ? 47.124 -37.402 -10.706 1.00 28.97 ?  158 LYS   B HA   1 
ATOM   6472 H  HB2  . LYS   B 1 158 ? 49.017 -38.158 -11.688 1.00 31.36 ?  158 LYS   B HB2  1 
ATOM   6473 H  HB3  . LYS   B 1 158 ? 49.143 -39.362 -10.666 1.00 31.36 ?  158 LYS   B HB3  1 
ATOM   6474 H  HG2  . LYS   B 1 158 ? 48.521 -40.226 -12.676 1.00 34.36 ?  158 LYS   B HG2  1 
ATOM   6475 H  HG3  . LYS   B 1 158 ? 47.264 -40.377 -11.724 1.00 34.36 ?  158 LYS   B HG3  1 
ATOM   6476 H  HD2  . LYS   B 1 158 ? 46.289 -38.508 -12.728 1.00 37.03 ?  158 LYS   B HD2  1 
ATOM   6477 H  HD3  . LYS   B 1 158 ? 47.565 -38.351 -13.669 1.00 37.03 ?  158 LYS   B HD3  1 
ATOM   6478 H  HE2  . LYS   B 1 158 ? 47.058 -40.238 -14.812 1.00 39.76 ?  158 LYS   B HE2  1 
ATOM   6479 H  HE3  . LYS   B 1 158 ? 45.978 -40.677 -13.736 1.00 39.76 ?  158 LYS   B HE3  1 
ATOM   6480 H  HZ1  . LYS   B 1 158 ? 44.960 -39.845 -15.590 1.00 40.56 ?  158 LYS   B HZ1  1 
ATOM   6481 H  HZ2  . LYS   B 1 158 ? 44.659 -38.970 -14.475 1.00 40.56 ?  158 LYS   B HZ2  1 
ATOM   6482 H  HZ3  . LYS   B 1 158 ? 45.648 -38.576 -15.458 1.00 40.56 ?  158 LYS   B HZ3  1 
ATOM   6483 N  N    . ASN   B 1 159 ? 46.863 -39.805 -8.604  1.00 24.82 ?  159 ASN   B N    1 
ATOM   6484 C  CA   . ASN   B 1 159 ? 45.909 -40.779 -8.082  1.00 25.09 ?  159 ASN   B CA   1 
ATOM   6485 C  C    . ASN   B 1 159 ? 44.721 -40.105 -7.394  1.00 23.98 ?  159 ASN   B C    1 
ATOM   6486 O  O    . ASN   B 1 159 ? 43.585 -40.595 -7.496  1.00 24.85 ?  159 ASN   B O    1 
ATOM   6487 C  CB   . ASN   B 1 159 ? 46.626 -41.773 -7.173  1.00 26.24 ?  159 ASN   B CB   1 
ATOM   6488 C  CG   . ASN   B 1 159 ? 47.616 -42.634 -7.932  1.00 29.00 ?  159 ASN   B CG   1 
ATOM   6489 O  OD1  . ASN   B 1 159 ? 47.336 -43.083 -9.047  1.00 29.13 ?  159 ASN   B OD1  1 
ATOM   6490 N  ND2  . ASN   B 1 159 ? 48.791 -42.854 -7.340  1.00 30.25 ?  159 ASN   B ND2  1 
ATOM   6491 H  H    . ASN   B 1 159 ? 47.605 -39.745 -8.179  1.00 29.84 ?  159 ASN   B H    1 
ATOM   6492 H  HA   . ASN   B 1 159 ? 45.565 -41.283 -8.836  1.00 30.17 ?  159 ASN   B HA   1 
ATOM   6493 H  HB2  . ASN   B 1 159 ? 47.117 -41.294 -6.491  1.00 31.54 ?  159 ASN   B HB2  1 
ATOM   6494 H  HB3  . ASN   B 1 159 ? 45.977 -42.366 -6.776  1.00 31.54 ?  159 ASN   B HB3  1 
ATOM   6495 H  HD21 . ASN   B 1 159 ? 49.395 -43.330 -7.730  1.00 36.35 ?  159 ASN   B HD21 1 
ATOM   6496 H  HD22 . ASN   B 1 159 ? 48.948 -42.525 -6.559  1.00 36.35 ?  159 ASN   B HD22 1 
ATOM   6497 N  N    . LEU   B 1 160 ? 44.939 -38.970 -6.723  1.00 23.11 ?  160 LEU   B N    1 
ATOM   6498 C  CA   . LEU   B 1 160 ? 43.809 -38.232 -6.179  1.00 22.23 ?  160 LEU   B CA   1 
ATOM   6499 C  C    . LEU   B 1 160 ? 43.018 -37.566 -7.293  1.00 21.95 ?  160 LEU   B C    1 
ATOM   6500 O  O    . LEU   B 1 160 ? 41.783 -37.563 -7.265  1.00 21.84 ?  160 LEU   B O    1 
ATOM   6501 C  CB   . LEU   B 1 160 ? 44.278 -37.202 -5.153  1.00 21.63 ?  160 LEU   B CB   1 
ATOM   6502 C  CG   . LEU   B 1 160 ? 43.150 -36.307 -4.629  1.00 20.93 ?  160 LEU   B CG   1 
ATOM   6503 C  CD1  . LEU   B 1 160 ? 42.053 -37.160 -4.009  1.00 21.88 ?  160 LEU   B CD1  1 
ATOM   6504 C  CD2  . LEU   B 1 160 ? 43.686 -35.305 -3.626  1.00 21.19 ?  160 LEU   B CD2  1 
ATOM   6505 H  H    . LEU   B 1 160 ? 45.714 -38.619 -6.581  1.00 27.78 ?  160 LEU   B H    1 
ATOM   6506 H  HA   . LEU   B 1 160 ? 43.223 -38.860 -5.729  1.00 26.73 ?  160 LEU   B HA   1 
ATOM   6507 H  HB2  . LEU   B 1 160 ? 44.670 -37.674 -4.397  1.00 26.02 ?  160 LEU   B HB2  1 
ATOM   6508 H  HB3  . LEU   B 1 160 ? 44.951 -36.636 -5.567  1.00 26.02 ?  160 LEU   B HB3  1 
ATOM   6509 H  HG   . LEU   B 1 160 ? 42.770 -35.813 -5.369  1.00 25.17 ?  160 LEU   B HG   1 
ATOM   6510 H  HD11 . LEU   B 1 160 ? 41.444 -36.582 -3.530  1.00 26.31 ?  160 LEU   B HD11 1 
ATOM   6511 H  HD12 . LEU   B 1 160 ? 41.578 -37.632 -4.713  1.00 26.31 ?  160 LEU   B HD12 1 
ATOM   6512 H  HD13 . LEU   B 1 160 ? 42.455 -37.799 -3.397  1.00 26.31 ?  160 LEU   B HD13 1 
ATOM   6513 H  HD21 . LEU   B 1 160 ? 42.962 -34.728 -3.349  1.00 25.48 ?  160 LEU   B HD21 1 
ATOM   6514 H  HD22 . LEU   B 1 160 ? 44.042 -35.786 -2.862  1.00 25.48 ?  160 LEU   B HD22 1 
ATOM   6515 H  HD23 . LEU   B 1 160 ? 44.388 -34.784 -4.047  1.00 25.48 ?  160 LEU   B HD23 1 
ATOM   6516 N  N    . TYR   B 1 161 ? 43.710 -37.006 -8.290  1.00 22.09 ?  161 TYR   B N    1 
ATOM   6517 C  CA   . TYR   B 1 161 ? 43.028 -36.434 -9.448  1.00 21.76 ?  161 TYR   B CA   1 
ATOM   6518 C  C    . TYR   B 1 161 ? 42.072 -37.449 -10.065 1.00 21.88 ?  161 TYR   B C    1 
ATOM   6519 O  O    . TYR   B 1 161 ? 40.899 -37.149 -10.313 1.00 22.25 ?  161 TYR   B O    1 
ATOM   6520 C  CB   . TYR   B 1 161 ? 44.065 -35.965 -10.479 1.00 22.00 ?  161 TYR   B CB   1 
ATOM   6521 C  CG   . TYR   B 1 161 ? 43.478 -35.495 -11.793 1.00 22.19 ?  161 TYR   B CG   1 
ATOM   6522 C  CD1  . TYR   B 1 161 ? 43.104 -34.168 -11.968 1.00 22.35 ?  161 TYR   B CD1  1 
ATOM   6523 C  CD2  . TYR   B 1 161 ? 43.284 -36.375 -12.855 1.00 22.53 ?  161 TYR   B CD2  1 
ATOM   6524 C  CE1  . TYR   B 1 161 ? 42.565 -33.730 -13.155 1.00 22.97 ?  161 TYR   B CE1  1 
ATOM   6525 C  CE2  . TYR   B 1 161 ? 42.742 -35.941 -14.052 1.00 23.46 ?  161 TYR   B CE2  1 
ATOM   6526 C  CZ   . TYR   B 1 161 ? 42.383 -34.616 -14.194 1.00 23.74 ?  161 TYR   B CZ   1 
ATOM   6527 O  OH   . TYR   B 1 161 ? 41.843 -34.176 -15.380 1.00 25.96 ?  161 TYR   B OH   1 
ATOM   6528 H  H    . TYR   B 1 161 ? 44.567 -36.955 -8.323  1.00 26.56 ?  161 TYR   B H    1 
ATOM   6529 H  HA   . TYR   B 1 161 ? 42.513 -35.661 -9.162  1.00 26.17 ?  161 TYR   B HA   1 
ATOM   6530 H  HB2  . TYR   B 1 161 ? 44.565 -35.226 -10.100 1.00 26.46 ?  161 TYR   B HB2  1 
ATOM   6531 H  HB3  . TYR   B 1 161 ? 44.663 -36.702 -10.671 1.00 26.46 ?  161 TYR   B HB3  1 
ATOM   6532 H  HD1  . TYR   B 1 161 ? 43.223 -33.561 -11.272 1.00 26.88 ?  161 TYR   B HD1  1 
ATOM   6533 H  HD2  . TYR   B 1 161 ? 43.518 -37.270 -12.762 1.00 27.09 ?  161 TYR   B HD2  1 
ATOM   6534 H  HE1  . TYR   B 1 161 ? 42.323 -32.832 -13.253 1.00 27.62 ?  161 TYR   B HE1  1 
ATOM   6535 H  HE2  . TYR   B 1 161 ? 42.613 -36.535 -14.754 1.00 28.21 ?  161 TYR   B HE2  1 
ATOM   6536 H  HH   . TYR   B 1 161 ? 41.758 -34.819 -15.915 1.00 31.21 ?  161 TYR   B HH   1 
ATOM   6537 N  N    . ASP   B 1 162 ? 42.563 -38.666 -10.314 1.00 22.30 ?  162 ASP   B N    1 
ATOM   6538 C  CA   . ASP   B 1 162 ? 41.724 -39.695 -10.918 1.00 22.61 ?  162 ASP   B CA   1 
ATOM   6539 C  C    . ASP   B 1 162 ? 40.533 -40.035 -10.031 1.00 21.96 ?  162 ASP   B C    1 
ATOM   6540 O  O    . ASP   B 1 162 ? 39.420 -40.246 -10.530 1.00 22.91 ?  162 ASP   B O    1 
ATOM   6541 C  CB   . ASP   B 1 162 ? 42.546 -40.959 -11.179 1.00 23.55 ?  162 ASP   B CB   1 
ATOM   6542 C  CG   . ASP   B 1 162 ? 43.528 -40.803 -12.324 1.00 24.77 ?  162 ASP   B CG   1 
ATOM   6543 O  OD1  . ASP   B 1 162 ? 43.383 -39.868 -13.133 1.00 25.61 ?  162 ASP   B OD1  1 
ATOM   6544 O  OD2  . ASP   B 1 162 ? 44.435 -41.651 -12.429 1.00 26.24 -1 162 ASP   B OD2  1 
ATOM   6545 H  H    . ASP   B 1 162 ? 43.366 -38.908 -10.152 1.00 26.81 ?  162 ASP   B H    1 
ATOM   6546 H  HA   . ASP   B 1 162 ? 41.382 -39.374 -11.766 1.00 27.19 ?  162 ASP   B HA   1 
ATOM   6547 H  HB2  . ASP   B 1 162 ? 43.054 -41.173 -10.382 1.00 28.31 ?  162 ASP   B HB2  1 
ATOM   6548 H  HB3  . ASP   B 1 162 ? 41.946 -41.685 -11.399 1.00 28.31 ?  162 ASP   B HB3  1 
ATOM   6549 N  N    . LYS   B 1 163 ? 40.743 -40.110 -8.713  1.00 21.38 ?  163 LYS   B N    1 
ATOM   6550 C  CA   . LYS   B 1 163 ? 39.625 -40.392 -7.817  1.00 22.41 ?  163 LYS   B CA   1 
ATOM   6551 C  C    . LYS   B 1 163 ? 38.589 -39.274 -7.865  1.00 21.13 ?  163 LYS   B C    1 
ATOM   6552 O  O    . LYS   B 1 163 ? 37.376 -39.532 -7.840  1.00 21.89 ?  163 LYS   B O    1 
ATOM   6553 C  CB   . LYS   B 1 163 ? 40.116 -40.578 -6.385  1.00 25.95 ?  163 LYS   B CB   1 
ATOM   6554 C  CG   . LYS   B 1 163 ? 39.042 -41.121 -5.466  1.00 30.96 ?  163 LYS   B CG   1 
ATOM   6555 C  CD   . LYS   B 1 163 ? 39.524 -41.281 -4.037  1.00 36.52 ?  163 LYS   B CD   1 
ATOM   6556 C  CE   . LYS   B 1 163 ? 38.444 -41.926 -3.178  1.00 41.52 ?  163 LYS   B CE   1 
ATOM   6557 N  NZ   . LYS   B 1 163 ? 38.613 -41.624 -1.729  1.00 44.36 ?  163 LYS   B NZ   1 
ATOM   6558 H  H    . LYS   B 1 163 ? 41.504 -40.005 -8.326  1.00 25.71 ?  163 LYS   B H    1 
ATOM   6559 H  HA   . LYS   B 1 163 ? 39.196 -41.210 -8.097  1.00 26.95 ?  163 LYS   B HA   1 
ATOM   6560 H  HB2  . LYS   B 1 163 ? 40.857 -41.203 -6.385  1.00 31.19 ?  163 LYS   B HB2  1 
ATOM   6561 H  HB3  . LYS   B 1 163 ? 40.405 -39.720 -6.035  1.00 31.19 ?  163 LYS   B HB3  1 
ATOM   6562 H  HG2  . LYS   B 1 163 ? 38.288 -40.512 -5.461  1.00 37.21 ?  163 LYS   B HG2  1 
ATOM   6563 H  HG3  . LYS   B 1 163 ? 38.762 -41.993 -5.789  1.00 37.21 ?  163 LYS   B HG3  1 
ATOM   6564 H  HD2  . LYS   B 1 163 ? 40.309 -41.854 -4.024  1.00 43.88 ?  163 LYS   B HD2  1 
ATOM   6565 H  HD3  . LYS   B 1 163 ? 39.735 -40.410 -3.668  1.00 43.88 ?  163 LYS   B HD3  1 
ATOM   6566 H  HE2  . LYS   B 1 163 ? 37.573 -41.606 -3.460  1.00 49.88 ?  163 LYS   B HE2  1 
ATOM   6567 H  HE3  . LYS   B 1 163 ? 38.488 -42.888 -3.288  1.00 49.88 ?  163 LYS   B HE3  1 
ATOM   6568 H  HZ1  . LYS   B 1 163 ? 37.964 -42.014 -1.260  1.00 53.29 ?  163 LYS   B HZ1  1 
ATOM   6569 H  HZ2  . LYS   B 1 163 ? 39.398 -41.929 -1.445  1.00 53.29 ?  163 LYS   B HZ2  1 
ATOM   6570 H  HZ3  . LYS   B 1 163 ? 38.577 -40.745 -1.595  1.00 53.29 ?  163 LYS   B HZ3  1 
ATOM   6571 N  N    . LEU   B 1 164 ? 39.050 -38.022 -7.928  1.00 19.86 ?  164 LEU   B N    1 
ATOM   6572 C  CA   . LEU   B 1 164 ? 38.139 -36.882 -7.989  1.00 19.67 ?  164 LEU   B CA   1 
ATOM   6573 C  C    . LEU   B 1 164 ? 37.353 -36.871 -9.297  1.00 20.38 ?  164 LEU   B C    1 
ATOM   6574 O  O    . LEU   B 1 164 ? 36.129 -36.672 -9.299  1.00 21.39 ?  164 LEU   B O    1 
ATOM   6575 C  CB   . LEU   B 1 164 ? 38.933 -35.585 -7.819  1.00 18.89 ?  164 LEU   B CB   1 
ATOM   6576 C  CG   . LEU   B 1 164 ? 39.486 -35.323 -6.420  1.00 19.61 ?  164 LEU   B CG   1 
ATOM   6577 C  CD1  . LEU   B 1 164 ? 40.559 -34.252 -6.473  1.00 19.59 ?  164 LEU   B CD1  1 
ATOM   6578 C  CD2  . LEU   B 1 164 ? 38.379 -34.899 -5.476  1.00 20.83 ?  164 LEU   B CD2  1 
ATOM   6579 H  H    . LEU   B 1 164 ? 39.889 -37.807 -7.933  1.00 23.89 ?  164 LEU   B H    1 
ATOM   6580 H  HA   . LEU   B 1 164 ? 37.510 -36.946 -7.261  1.00 23.65 ?  164 LEU   B HA   1 
ATOM   6581 H  HB2  . LEU   B 1 164 ? 39.690 -35.600 -8.426  1.00 22.73 ?  164 LEU   B HB2  1 
ATOM   6582 H  HB3  . LEU   B 1 164 ? 38.356 -34.839 -8.041  1.00 22.73 ?  164 LEU   B HB3  1 
ATOM   6583 H  HG   . LEU   B 1 164 ? 39.891 -36.133 -6.073  1.00 23.59 ?  164 LEU   B HG   1 
ATOM   6584 H  HD11 . LEU   B 1 164 ? 40.896 -34.088 -5.574  1.00 23.56 ?  164 LEU   B HD11 1 
ATOM   6585 H  HD12 . LEU   B 1 164 ? 41.289 -34.556 -7.041  1.00 23.56 ?  164 LEU   B HD12 1 
ATOM   6586 H  HD13 . LEU   B 1 164 ? 40.182 -33.435 -6.834  1.00 23.56 ?  164 LEU   B HD13 1 
ATOM   6587 H  HD21 . LEU   B 1 164 ? 38.759 -34.692 -4.609  1.00 25.06 ?  164 LEU   B HD21 1 
ATOM   6588 H  HD22 . LEU   B 1 164 ? 37.938 -34.113 -5.839  1.00 25.06 ?  164 LEU   B HD22 1 
ATOM   6589 H  HD23 . LEU   B 1 164 ? 37.742 -35.626 -5.393  1.00 25.06 ?  164 LEU   B HD23 1 
ATOM   6590 N  N    . VAL   B 1 165 ? 38.042 -37.055 -10.423 1.00 22.29 ?  165 VAL   B N    1 
ATOM   6591 C  CA   . VAL   B 1 165 ? 37.377 -36.994 -11.720 1.00 23.77 ?  165 VAL   B CA   1 
ATOM   6592 C  C    . VAL   B 1 165 ? 36.448 -38.189 -11.896 1.00 26.23 ?  165 VAL   B C    1 
ATOM   6593 O  O    . VAL   B 1 165 ? 35.269 -38.041 -12.243 1.00 27.98 ?  165 VAL   B O    1 
ATOM   6594 C  CB   . VAL   B 1 165 ? 38.412 -36.922 -12.855 1.00 24.55 ?  165 VAL   B CB   1 
ATOM   6595 C  CG1  . VAL   B 1 165 ? 37.730 -37.057 -14.191 1.00 25.56 ?  165 VAL   B CG1  1 
ATOM   6596 C  CG2  . VAL   B 1 165 ? 39.170 -35.617 -12.787 1.00 24.13 ?  165 VAL   B CG2  1 
ATOM   6597 H  H    . VAL   B 1 165 ? 38.890 -37.223 -10.461 1.00 26.80 ?  165 VAL   B H    1 
ATOM   6598 H  HA   . VAL   B 1 165 ? 36.844 -36.189 -11.758 1.00 28.58 ?  165 VAL   B HA   1 
ATOM   6599 H  HB   . VAL   B 1 165 ? 39.055 -37.643 -12.760 1.00 29.51 ?  165 VAL   B HB   1 
ATOM   6600 H  HG11 . VAL   B 1 165 ? 38.324 -36.742 -14.886 1.00 30.72 ?  165 VAL   B HG11 1 
ATOM   6601 H  HG12 . VAL   B 1 165 ? 37.521 -37.995 -14.340 1.00 30.72 ?  165 VAL   B HG12 1 
ATOM   6602 H  HG13 . VAL   B 1 165 ? 36.915 -36.535 -14.184 1.00 30.72 ?  165 VAL   B HG13 1 
ATOM   6603 H  HG21 . VAL   B 1 165 ? 39.803 -35.578 -13.523 1.00 29.01 ?  165 VAL   B HG21 1 
ATOM   6604 H  HG22 . VAL   B 1 165 ? 38.538 -34.881 -12.860 1.00 29.01 ?  165 VAL   B HG22 1 
ATOM   6605 H  HG23 . VAL   B 1 165 ? 39.641 -35.564 -11.942 1.00 29.01 ?  165 VAL   B HG23 1 
ATOM   6606 N  N    . SER   B 1 166 ? 36.975 -39.397 -11.665 1.00 26.89 ?  166 SER   B N    1 
ATOM   6607 C  CA   . SER   B 1 166 ? 36.222 -40.610 -11.957 1.00 27.36 ?  166 SER   B CA   1 
ATOM   6608 C  C    . SER   B 1 166 ? 34.967 -40.709 -11.105 1.00 26.81 ?  166 SER   B C    1 
ATOM   6609 O  O    . SER   B 1 166 ? 33.991 -41.324 -11.531 1.00 27.69 ?  166 SER   B O    1 
ATOM   6610 C  CB   . SER   B 1 166 ? 37.102 -41.861 -11.812 1.00 28.17 ?  166 SER   B CB   1 
ATOM   6611 O  OG   . SER   B 1 166 ? 37.480 -42.081 -10.464 1.00 28.01 ?  166 SER   B OG   1 
ATOM   6612 H  H    . SER   B 1 166 ? 37.762 -39.533 -11.351 1.00 32.32 ?  166 SER   B H    1 
ATOM   6613 H  HA   . SER   B 1 166 ? 35.928 -40.577 -12.876 1.00 32.89 ?  166 SER   B HA   1 
ATOM   6614 H  HB2  . SER   B 1 166 ? 36.606 -42.631 -12.129 1.00 33.86 ?  166 SER   B HB2  1 
ATOM   6615 H  HB3  . SER   B 1 166 ? 37.901 -41.741 -12.354 1.00 33.86 ?  166 SER   B HB3  1 
ATOM   6616 H  HG   . SER   B 1 166 ? 37.923 -41.422 -10.186 1.00 33.66 ?  166 SER   B HG   1 
ATOM   6617 N  N    . SER   B 1 167 ? 34.953 -40.100 -9.922  1.00 24.55 ?  167 SER   B N    1 
ATOM   6618 C  CA   . SER   B 1 167 ? 33.796 -40.160 -9.035  1.00 24.35 ?  167 SER   B CA   1 
ATOM   6619 C  C    . SER   B 1 167 ? 32.889 -38.936 -9.120  1.00 24.08 ?  167 SER   B C    1 
ATOM   6620 O  O    . SER   B 1 167 ? 31.817 -38.938 -8.507  1.00 24.70 ?  167 SER   B O    1 
ATOM   6621 C  CB   . SER   B 1 167 ? 34.241 -40.339 -7.580  1.00 24.61 ?  167 SER   B CB   1 
ATOM   6622 O  OG   . SER   B 1 167 ? 34.897 -39.172 -7.117  1.00 24.66 ?  167 SER   B OG   1 
ATOM   6623 H  H    . SER   B 1 167 ? 35.596 -39.635 -9.611  1.00 29.51 ?  167 SER   B H    1 
ATOM   6624 H  HA   . SER   B 1 167 ? 33.253 -40.927 -9.272  1.00 29.27 ?  167 SER   B HA   1 
ATOM   6625 H  HB2  . SER   B 1 167 ? 33.458 -40.509 -7.027  1.00 29.58 ?  167 SER   B HB2  1 
ATOM   6626 H  HB3  . SER   B 1 167 ? 34.846 -41.099 -7.531  1.00 29.58 ?  167 SER   B HB3  1 
ATOM   6627 H  HG   . SER   B 1 167 ? 35.579 -39.030 -7.585  1.00 29.65 ?  167 SER   B HG   1 
ATOM   6628 N  N    . PHE   B 1 168 ? 33.276 -37.892 -9.854  1.00 24.37 ?  168 PHE   B N    1 
ATOM   6629 C  CA   . PHE   B 1 168 ? 32.444 -36.689 -9.899  1.00 23.83 ?  168 PHE   B CA   1 
ATOM   6630 C  C    . PHE   B 1 168 ? 31.138 -36.941 -10.642 1.00 21.48 ?  168 PHE   B C    1 
ATOM   6631 O  O    . PHE   B 1 168 ? 30.100 -36.330 -10.320 1.00 22.16 ?  168 PHE   B O    1 
ATOM   6632 C  CB   . PHE   B 1 168 ? 33.198 -35.538 -10.561 1.00 24.69 ?  168 PHE   B CB   1 
ATOM   6633 C  CG   . PHE   B 1 168 ? 32.361 -34.307 -10.753 1.00 24.47 ?  168 PHE   B CG   1 
ATOM   6634 C  CD1  . PHE   B 1 168 ? 31.982 -33.543 -9.662  1.00 25.40 ?  168 PHE   B CD1  1 
ATOM   6635 C  CD2  . PHE   B 1 168 ? 31.940 -33.925 -12.014 1.00 23.64 ?  168 PHE   B CD2  1 
ATOM   6636 C  CE1  . PHE   B 1 168 ? 31.202 -32.412 -9.823  1.00 25.22 ?  168 PHE   B CE1  1 
ATOM   6637 C  CE2  . PHE   B 1 168 ? 31.167 -32.786 -12.190 1.00 24.78 ?  168 PHE   B CE2  1 
ATOM   6638 C  CZ   . PHE   B 1 168 ? 30.792 -32.029 -11.091 1.00 24.94 ?  168 PHE   B CZ   1 
ATOM   6639 H  H    . PHE   B 1 168 ? 33.995 -37.854 -10.325 1.00 29.29 ?  168 PHE   B H    1 
ATOM   6640 H  HA   . PHE   B 1 168 ? 32.222 -36.422 -8.995  1.00 28.65 ?  168 PHE   B HA   1 
ATOM   6641 H  HB2  . PHE   B 1 168 ? 33.953 -35.294 -10.003 1.00 29.68 ?  168 PHE   B HB2  1 
ATOM   6642 H  HB3  . PHE   B 1 168 ? 33.507 -35.818 -11.434 1.00 29.68 ?  168 PHE   B HB3  1 
ATOM   6643 H  HD1  . PHE   B 1 168 ? 32.255 -33.797 -8.812  1.00 30.54 ?  168 PHE   B HD1  1 
ATOM   6644 H  HD2  . PHE   B 1 168 ? 32.188 -34.427 -12.754 1.00 28.42 ?  168 PHE   B HD2  1 
ATOM   6645 H  HE1  . PHE   B 1 168 ? 30.955 -31.910 -9.083  1.00 30.32 ?  168 PHE   B HE1  1 
ATOM   6646 H  HE2  . PHE   B 1 168 ? 30.889 -32.543 -13.044 1.00 29.80 ?  168 PHE   B HE2  1 
ATOM   6647 H  HZ   . PHE   B 1 168 ? 30.265 -31.272 -11.206 1.00 29.98 ?  168 PHE   B HZ   1 
ATOM   6648 N  N    . LEU   B 1 169 ? 31.175 -37.808 -11.648 1.00 20.94 ?  169 LEU   B N    1 
ATOM   6649 C  CA   . LEU   B 1 169 ? 29.990 -38.136 -12.427 1.00 22.44 ?  169 LEU   B CA   1 
ATOM   6650 C  C    . LEU   B 1 169 ? 29.992 -39.585 -12.897 1.00 25.22 ?  169 LEU   B C    1 
ATOM   6651 O  O    . LEU   B 1 169 ? 29.078 -40.022 -13.595 1.00 27.36 ?  169 LEU   B O    1 
ATOM   6652 C  CB   . LEU   B 1 169 ? 29.899 -37.218 -13.643 1.00 23.26 ?  169 LEU   B CB   1 
ATOM   6653 C  CG   . LEU   B 1 169 ? 28.618 -36.397 -13.789 1.00 25.68 ?  169 LEU   B CG   1 
ATOM   6654 C  CD1  . LEU   B 1 169 ? 28.513 -35.895 -15.209 1.00 26.28 ?  169 LEU   B CD1  1 
ATOM   6655 C  CD2  . LEU   B 1 169 ? 27.378 -37.190 -13.404 1.00 25.41 ?  169 LEU   B CD2  1 
ATOM   6656 O  OXT  . LEU   B 1 169 ? 30.908 -40.342 -12.600 1.00 26.49 -1 169 LEU   B OXT  1 
ATOM   6657 H  H    . LEU   B 1 169 ? 31.887 -38.219 -11.909 1.00 25.19 ?  169 LEU   B H    1 
ATOM   6658 H  HA   . LEU   B 1 169 ? 29.214 -37.998 -11.869 1.00 26.98 ?  169 LEU   B HA   1 
ATOM   6659 H  HB2  . LEU   B 1 169 ? 30.638 -36.589 -13.610 1.00 27.97 ?  169 LEU   B HB2  1 
ATOM   6660 H  HB3  . LEU   B 1 169 ? 29.977 -37.761 -14.443 1.00 27.97 ?  169 LEU   B HB3  1 
ATOM   6661 H  HG   . LEU   B 1 169 ? 28.671 -35.624 -13.203 1.00 30.87 ?  169 LEU   B HG   1 
ATOM   6662 H  HD11 . LEU   B 1 169 ? 27.723 -35.338 -15.286 1.00 31.59 ?  169 LEU   B HD11 1 
ATOM   6663 H  HD12 . LEU   B 1 169 ? 29.306 -35.378 -15.417 1.00 31.59 ?  169 LEU   B HD12 1 
ATOM   6664 H  HD13 . LEU   B 1 169 ? 28.444 -36.655 -15.805 1.00 31.59 ?  169 LEU   B HD13 1 
ATOM   6665 H  HD21 . LEU   B 1 169 ? 26.606 -36.809 -13.844 1.00 30.55 ?  169 LEU   B HD21 1 
ATOM   6666 H  HD22 . LEU   B 1 169 ? 27.495 -38.115 -13.683 1.00 30.55 ?  169 LEU   B HD22 1 
ATOM   6667 H  HD23 . LEU   B 1 169 ? 27.266 -37.151 -12.442 1.00 30.55 ?  169 LEU   B HD23 1 
HETATM 6668 N  N2   B A1BBY C 2 .   ? 14.825 -0.291  4.133   0.17 15.88 ?  201 A1BBY A N2   1 
HETATM 6669 C  C3   B A1BBY C 2 .   ? 13.953 -0.319  1.123   0.17 19.26 ?  201 A1BBY A C3   1 
HETATM 6670 C  C6   B A1BBY C 2 .   ? 14.886 -0.041  5.474   0.17 15.53 ?  201 A1BBY A C6   1 
HETATM 6671 C  C9   B A1BBY C 2 .   ? 15.530 3.430   3.374   0.17 14.97 ?  201 A1BBY A C9   1 
HETATM 6672 C  C1   B A1BBY C 2 .   ? 13.898 -2.445  -0.345  0.17 20.32 ?  201 A1BBY A C1   1 
HETATM 6673 C  C10  B A1BBY C 2 .   ? 15.700 4.228   4.484   0.17 14.59 ?  201 A1BBY A C10  1 
HETATM 6674 C  C2   B A1BBY C 2 .   ? 14.613 -1.115  -0.041  0.17 20.10 ?  201 A1BBY A C2   1 
HETATM 6675 C  C4   B A1BBY C 2 .   ? 13.216 -1.374  1.961   0.17 19.43 ?  201 A1BBY A C4   1 
HETATM 6676 C  C5   B A1BBY C 2 .   ? 15.006 0.769   3.261   0.17 16.13 ?  201 A1BBY A C5   1 
HETATM 6677 C  C7   B A1BBY C 2 .   ? 15.305 2.146   5.212   0.17 14.64 ?  201 A1BBY A C7   1 
HETATM 6678 C  C8   B A1BBY C 2 .   ? 15.274 2.087   3.793   0.17 15.08 ?  201 A1BBY A C8   1 
HETATM 6679 N  N1   B A1BBY C 2 .   ? 14.950 0.498   1.908   0.17 17.83 ?  201 A1BBY A N1   1 
HETATM 6680 N  N3   B A1BBY C 2 .   ? 15.113 1.118   6.070   0.17 14.84 ?  201 A1BBY A N3   1 
HETATM 6681 N  N4   B A1BBY C 2 .   ? 15.564 3.446   5.645   0.17 14.73 ?  201 A1BBY A N4   1 
HETATM 6682 O  O1   B A1BBY C 2 .   ? 15.943 -1.349  0.304   0.17 20.66 ?  201 A1BBY A O1   1 
HETATM 6683 H  H2   B A1BBY C 2 .   ? 13.185 0.371   0.673   0.17 23.16 ?  201 A1BBY A H2   1 
HETATM 6684 H  H11  B A1BBY C 2 .   ? 14.735 -0.877  6.191   0.17 18.69 ?  201 A1BBY A H11  1 
HETATM 6685 H  H12  B A1BBY C 2 .   ? 15.585 3.802   2.364   0.17 18.01 ?  201 A1BBY A H12  1 
HETATM 6686 H  H3   B A1BBY C 2 .   ? 14.222 -2.851  -1.242  0.17 24.44 ?  201 A1BBY A H3   1 
HETATM 6687 H  H4   B A1BBY C 2 .   ? 12.818 -2.363  -0.462  0.17 24.44 ?  201 A1BBY A H4   1 
HETATM 6688 H  H5   B A1BBY C 2 .   ? 14.092 -3.227  0.385   0.17 24.44 ?  201 A1BBY A H5   1 
HETATM 6689 H  H13  B A1BBY C 2 .   ? 15.903 5.287   4.620   0.17 17.57 ?  201 A1BBY A H13  1 
HETATM 6690 H  H1   B A1BBY C 2 .   ? 14.552 -0.534  -0.947  0.17 24.18 ?  201 A1BBY A H1   1 
HETATM 6691 H  H8   B A1BBY C 2 .   ? 13.792 -2.245  2.138   0.17 23.37 ?  201 A1BBY A H8   1 
HETATM 6692 H  H7   B A1BBY C 2 .   ? 12.284 -1.762  1.534   0.17 23.37 ?  201 A1BBY A H7   1 
HETATM 6693 H  H9   B A1BBY C 2 .   ? 12.972 -1.022  2.895   0.17 23.37 ?  201 A1BBY A H9   1 
HETATM 6694 H  H10  B A1BBY C 2 .   ? 15.683 0.901   1.361   0.17 21.45 ?  201 A1BBY A H10  1 
HETATM 6695 H  H14  B A1BBY C 2 .   ? 15.632 3.736   6.600   0.17 17.73 ?  201 A1BBY A H14  1 
HETATM 6696 H  H6   B A1BBY C 2 .   ? 16.455 -1.357  -0.515  0.17 24.85 ?  201 A1BBY A H6   1 
HETATM 6697 O  O1   C A1BBZ D 3 .   ? 12.697 -0.066  -0.771  0.17 19.80 ?  202 A1BBZ A O1   1 
HETATM 6698 C  C1   C A1BBZ D 3 .   ? 13.776 -2.238  -0.562  0.17 19.59 ?  202 A1BBZ A C1   1 
HETATM 6699 C  C2   C A1BBZ D 3 .   ? 13.800 -0.725  -0.178  0.17 19.44 ?  202 A1BBZ A C2   1 
HETATM 6700 C  C3   C A1BBZ D 3 .   ? 13.707 -0.481  1.430   0.17 18.66 ?  202 A1BBZ A C3   1 
HETATM 6701 C  C4   C A1BBZ D 3 .   ? 13.374 -1.866  2.137   0.17 18.42 ?  202 A1BBZ A C4   1 
HETATM 6702 C  C5   C A1BBZ D 3 .   ? 15.041 0.594   3.443   0.17 16.71 ?  202 A1BBZ A C5   1 
HETATM 6703 C  C6   C A1BBZ D 3 .   ? 14.962 -0.057  5.753   0.17 16.49 ?  202 A1BBZ A C6   1 
HETATM 6704 C  C7   C A1BBZ D 3 .   ? 15.348 2.103   5.327   0.17 15.55 ?  202 A1BBZ A C7   1 
HETATM 6705 C  C8   C A1BBZ D 3 .   ? 15.294 1.960   3.883   0.17 15.81 ?  202 A1BBZ A C8   1 
HETATM 6706 C  C10  C A1BBZ D 3 .   ? 15.712 4.173   4.458   0.17 15.43 ?  202 A1BBZ A C10  1 
HETATM 6707 C  C9   C A1BBZ D 3 .   ? 15.534 3.315   3.364   0.17 15.75 ?  202 A1BBZ A C9   1 
HETATM 6708 N  N1   C A1BBZ D 3 .   ? 14.937 0.174   2.058   0.17 18.07 ?  202 A1BBZ A N1   1 
HETATM 6709 N  N2   C A1BBZ D 3 .   ? 14.880 -0.377  4.409   0.17 16.61 ?  202 A1BBZ A N2   1 
HETATM 6710 N  N3   C A1BBZ D 3 .   ? 15.194 1.150   6.309   0.17 15.98 ?  202 A1BBZ A N3   1 
HETATM 6711 N  N4   C A1BBZ D 3 .   ? 15.598 3.428   5.606   0.17 15.52 ?  202 A1BBZ A N4   1 
HETATM 6712 H  H6   C A1BBZ D 3 .   ? 12.914 0.202   -1.680  0.17 23.81 ?  202 A1BBZ A H6   1 
HETATM 6713 H  H5   C A1BBZ D 3 .   ? 13.994 -2.400  -1.624  0.17 23.56 ?  202 A1BBZ A H5   1 
HETATM 6714 H  H3   C A1BBZ D 3 .   ? 12.789 -2.716  -0.389  0.17 23.56 ?  202 A1BBZ A H3   1 
HETATM 6715 H  H4   C A1BBZ D 3 .   ? 14.517 -2.843  -0.006  0.17 23.56 ?  202 A1BBZ A H4   1 
HETATM 6716 H  H1   C A1BBZ D 3 .   ? 14.753 -0.277  -0.568  0.17 23.38 ?  202 A1BBZ A H1   1 
HETATM 6717 H  H2   C A1BBZ D 3 .   ? 12.834 0.178   1.605   0.17 22.45 ?  202 A1BBZ A H2   1 
HETATM 6718 H  H8   C A1BBZ D 3 .   ? 14.217 -2.601  2.125   0.17 22.16 ?  202 A1BBZ A H8   1 
HETATM 6719 H  H7   C A1BBZ D 3 .   ? 12.510 -2.409  1.707   0.17 22.16 ?  202 A1BBZ A H7   1 
HETATM 6720 H  H9   C A1BBZ D 3 .   ? 13.139 -1.744  3.199   0.17 22.16 ?  202 A1BBZ A H9   1 
HETATM 6721 H  H11  C A1BBZ D 3 .   ? 14.830 -0.864  6.510   0.17 19.85 ?  202 A1BBZ A H11  1 
HETATM 6722 H  H13  C A1BBZ D 3 .   ? 15.908 5.250   4.584   0.17 18.57 ?  202 A1BBZ A H13  1 
HETATM 6723 H  H12  C A1BBZ D 3 .   ? 15.582 3.690   2.346   0.17 18.96 ?  202 A1BBZ A H12  1 
HETATM 6724 H  H10  C A1BBZ D 3 .   ? 15.722 0.325   1.429   0.17 21.74 ?  202 A1BBZ A H10  1 
HETATM 6725 H  H14  C A1BBZ D 3 .   ? 15.681 3.806   6.568   0.17 18.68 ?  202 A1BBZ A H14  1 
HETATM 6726 CL CL   B CL    E 4 .   ? 15.796 2.681   -0.833  0.34 16.54 ?  203 CL    A CL   1 
HETATM 6727 O  O    . HOH   F 5 .   ? 18.603 -2.314  -16.357 1.00 47.66 ?  301 HOH   A O    1 
HETATM 6728 O  O    . HOH   F 5 .   ? 4.748  3.814   0.680   1.00 29.27 ?  302 HOH   A O    1 
HETATM 6729 O  O    . HOH   F 5 .   ? 6.922  -8.162  11.842  1.00 24.50 ?  303 HOH   A O    1 
HETATM 6730 O  O    . HOH   F 5 .   ? 14.823 -4.643  20.472  1.00 44.99 ?  304 HOH   A O    1 
HETATM 6731 O  O    . HOH   F 5 .   ? 15.927 2.227   24.757  1.00 44.55 ?  305 HOH   A O    1 
HETATM 6732 O  O    . HOH   F 5 .   ? 8.084  -21.572 3.949   1.00 49.85 ?  306 HOH   A O    1 
HETATM 6733 O  O    . HOH   F 5 .   ? 7.930  -12.545 -0.808  1.00 28.40 ?  307 HOH   A O    1 
HETATM 6734 O  O    . HOH   F 5 .   ? 34.304 -1.890  12.528  1.00 35.83 ?  308 HOH   A O    1 
HETATM 6735 O  O    . HOH   F 5 .   ? -0.448 -3.110  3.103   1.00 39.70 ?  309 HOH   A O    1 
HETATM 6736 O  O    . HOH   F 5 .   ? 26.855 11.386  1.609   1.00 19.42 ?  310 HOH   A O    1 
HETATM 6737 O  O    . HOH   F 5 .   ? 28.916 0.436   -9.743  1.00 26.62 ?  311 HOH   A O    1 
HETATM 6738 O  O    . HOH   F 5 .   ? 11.755 -10.920 -10.048 1.00 44.52 ?  312 HOH   A O    1 
HETATM 6739 O  O    . HOH   F 5 .   ? 15.174 -12.273 18.538  1.00 33.32 ?  313 HOH   A O    1 
HETATM 6740 O  O    . HOH   F 5 .   ? 14.046 -4.418  -11.852 1.00 35.31 ?  314 HOH   A O    1 
HETATM 6741 O  O    . HOH   F 5 .   ? 10.530 -0.449  1.753   1.00 40.11 ?  315 HOH   A O    1 
HETATM 6742 O  O    . HOH   F 5 .   ? 0.671  -4.635  0.147   1.00 34.59 ?  316 HOH   A O    1 
HETATM 6743 O  O    . HOH   F 5 .   ? 9.248  -10.123 19.279  1.00 46.48 ?  317 HOH   A O    1 
HETATM 6744 O  O    . HOH   F 5 .   ? 30.238 -13.307 -8.532  1.00 30.63 ?  318 HOH   A O    1 
HETATM 6745 O  O    . HOH   F 5 .   ? 42.407 10.524  4.981   1.00 22.90 ?  319 HOH   A O    1 
HETATM 6746 O  O    . HOH   F 5 .   ? 19.907 -12.492 -8.994  1.00 30.06 ?  320 HOH   A O    1 
HETATM 6747 O  O    . HOH   F 5 .   ? 8.908  -11.997 17.294  1.00 43.13 ?  321 HOH   A O    1 
HETATM 6748 O  O    . HOH   F 5 .   ? 14.913 3.876   17.602  1.00 44.32 ?  322 HOH   A O    1 
HETATM 6749 O  O    . HOH   F 5 .   ? 34.047 -1.034  -8.838  1.00 31.23 ?  323 HOH   A O    1 
HETATM 6750 O  O    . HOH   F 5 .   ? 27.528 -6.262  -14.026 1.00 43.48 ?  324 HOH   A O    1 
HETATM 6751 O  O    . HOH   F 5 .   ? 22.739 12.482  1.572   1.00 18.74 ?  325 HOH   A O    1 
HETATM 6752 O  O    . HOH   F 5 .   ? 16.990 -19.278 4.799   1.00 19.74 ?  326 HOH   A O    1 
HETATM 6753 O  O    . HOH   F 5 .   ? 11.946 0.272   14.744  1.00 36.32 ?  327 HOH   A O    1 
HETATM 6754 O  O    . HOH   F 5 .   ? 38.214 10.264  7.069   1.00 56.34 ?  328 HOH   A O    1 
HETATM 6755 O  O    . HOH   F 5 .   ? 18.917 -22.032 6.905   1.00 36.33 ?  329 HOH   A O    1 
HETATM 6756 O  O    . HOH   F 5 .   ? 43.348 7.713   2.705   1.00 33.12 ?  330 HOH   A O    1 
HETATM 6757 O  O    . HOH   F 5 .   ? 9.864  -21.394 5.650   1.00 22.04 ?  331 HOH   A O    1 
HETATM 6758 O  O    . HOH   F 5 .   ? 37.499 2.824   10.237  1.00 26.23 ?  332 HOH   A O    1 
HETATM 6759 O  O    A HOH   F 5 .   ? 17.489 -1.735  0.399   0.83 25.58 ?  333 HOH   A O    1 
HETATM 6760 O  O    . HOH   F 5 .   ? 3.609  -9.508  9.776   1.00 35.99 ?  334 HOH   A O    1 
HETATM 6761 O  O    . HOH   F 5 .   ? 28.213 -6.323  19.501  1.00 44.18 ?  335 HOH   A O    1 
HETATM 6762 O  O    . HOH   F 5 .   ? 31.082 -18.082 7.740   1.00 24.30 ?  336 HOH   A O    1 
HETATM 6763 O  O    . HOH   F 5 .   ? 26.505 -19.358 -1.819  1.00 18.63 ?  337 HOH   A O    1 
HETATM 6764 O  O    . HOH   F 5 .   ? 17.181 -18.123 14.912  1.00 27.13 ?  338 HOH   A O    1 
HETATM 6765 O  O    . HOH   F 5 .   ? 27.298 13.771  2.843   1.00 32.89 ?  339 HOH   A O    1 
HETATM 6766 O  O    . HOH   F 5 .   ? 10.266 -22.200 -1.273  1.00 55.02 ?  340 HOH   A O    1 
HETATM 6767 O  O    . HOH   F 5 .   ? 18.661 -19.363 13.533  1.00 45.19 ?  341 HOH   A O    1 
HETATM 6768 O  O    . HOH   F 5 .   ? 44.296 7.202   6.413   1.00 28.58 ?  342 HOH   A O    1 
HETATM 6769 O  O    A HOH   F 5 .   ? 14.628 -3.678  3.052   0.66 19.74 ?  343 HOH   A O    1 
HETATM 6770 O  O    . HOH   F 5 .   ? 13.578 -15.270 -7.535  1.00 28.43 ?  344 HOH   A O    1 
HETATM 6771 O  O    . HOH   F 5 .   ? 36.254 -5.138  -0.539  1.00 33.43 ?  345 HOH   A O    1 
HETATM 6772 O  O    . HOH   F 5 .   ? 28.316 -0.107  -13.380 1.00 45.77 ?  346 HOH   A O    1 
HETATM 6773 O  O    . HOH   F 5 .   ? 38.547 5.008   7.030   1.00 18.07 ?  347 HOH   A O    1 
HETATM 6774 O  O    . HOH   F 5 .   ? 6.421  -5.607  11.092  1.00 23.80 ?  348 HOH   A O    1 
HETATM 6775 O  O    A HOH   F 5 .   ? 14.748 -14.008 16.636  0.66 20.86 ?  349 HOH   A O    1 
HETATM 6776 O  O    . HOH   F 5 .   ? 22.199 -19.239 11.303  1.00 40.99 ?  350 HOH   A O    1 
HETATM 6777 O  O    . HOH   F 5 .   ? 37.217 -2.812  9.647   1.00 42.35 ?  351 HOH   A O    1 
HETATM 6778 O  O    . HOH   F 5 .   ? 14.349 -21.251 -4.244  1.00 30.96 ?  352 HOH   A O    1 
HETATM 6779 O  O    . HOH   F 5 .   ? 42.488 4.264   5.466   1.00 34.78 ?  353 HOH   A O    1 
HETATM 6780 O  O    . HOH   F 5 .   ? 20.635 -19.773 -5.072  1.00 30.44 ?  354 HOH   A O    1 
HETATM 6781 O  O    . HOH   F 5 .   ? 21.289 -2.400  -2.225  1.00 20.04 ?  355 HOH   A O    1 
HETATM 6782 O  O    . HOH   F 5 .   ? 39.761 -1.038  -5.111  1.00 24.34 ?  356 HOH   A O    1 
HETATM 6783 O  O    . HOH   F 5 .   ? 17.125 -17.857 -5.086  1.00 30.32 ?  357 HOH   A O    1 
HETATM 6784 O  O    . HOH   F 5 .   ? 18.494 9.388   8.932   1.00 24.87 ?  358 HOH   A O    1 
HETATM 6785 O  O    . HOH   F 5 .   ? 35.773 -12.636 6.761   1.00 19.65 ?  359 HOH   A O    1 
HETATM 6786 O  O    A HOH   F 5 .   ? 14.259 0.550   6.753   0.66 27.08 ?  360 HOH   A O    1 
HETATM 6787 O  O    . HOH   F 5 .   ? 21.180 10.095  14.922  1.00 38.23 ?  361 HOH   A O    1 
HETATM 6788 O  O    . HOH   F 5 .   ? 10.964 1.680   12.509  1.00 27.92 ?  362 HOH   A O    1 
HETATM 6789 O  O    . HOH   F 5 .   ? 18.968 -0.726  -1.753  1.00 17.87 ?  363 HOH   A O    1 
HETATM 6790 O  O    B HOH   F 5 .   ? 15.108 -3.000  3.488   0.34 21.79 ?  364 HOH   A O    1 
HETATM 6791 O  O    . HOH   F 5 .   ? 30.788 3.049   8.256   1.00 15.66 ?  365 HOH   A O    1 
HETATM 6792 O  O    . HOH   F 5 .   ? 24.039 -2.122  -2.107  1.00 14.76 ?  366 HOH   A O    1 
HETATM 6793 O  O    . HOH   F 5 .   ? 24.398 3.550   -1.824  1.00 18.23 ?  367 HOH   A O    1 
HETATM 6794 O  O    . HOH   F 5 .   ? 31.899 -9.369  -6.739  1.00 26.79 ?  368 HOH   A O    1 
HETATM 6795 O  O    . HOH   F 5 .   ? 24.655 -17.509 12.737  1.00 27.36 ?  369 HOH   A O    1 
HETATM 6796 O  O    . HOH   F 5 .   ? 33.642 -7.168  4.306   1.00 20.39 ?  370 HOH   A O    1 
HETATM 6797 O  O    . HOH   F 5 .   ? 31.109 -13.940 -2.511  1.00 18.56 ?  371 HOH   A O    1 
HETATM 6798 O  O    . HOH   F 5 .   ? 21.884 -21.925 8.367   1.00 32.31 ?  372 HOH   A O    1 
HETATM 6799 O  O    . HOH   F 5 .   ? 13.329 -1.434  -6.637  1.00 21.67 ?  373 HOH   A O    1 
HETATM 6800 O  O    . HOH   F 5 .   ? 27.445 -10.629 14.048  1.00 21.19 ?  374 HOH   A O    1 
HETATM 6801 O  O    . HOH   F 5 .   ? 31.681 8.173   14.832  1.00 27.80 ?  375 HOH   A O    1 
HETATM 6802 O  O    . HOH   F 5 .   ? 24.625 2.029   -7.079  1.00 23.90 ?  376 HOH   A O    1 
HETATM 6803 O  O    . HOH   F 5 .   ? 43.942 8.465   -3.057  1.00 31.89 ?  377 HOH   A O    1 
HETATM 6804 O  O    . HOH   F 5 .   ? 37.302 11.964  4.925   1.00 29.77 ?  378 HOH   A O    1 
HETATM 6805 O  O    . HOH   F 5 .   ? 21.794 -13.831 -8.189  1.00 44.72 ?  379 HOH   A O    1 
HETATM 6806 O  O    . HOH   F 5 .   ? 22.225 5.288   19.056  1.00 47.60 ?  380 HOH   A O    1 
HETATM 6807 O  O    . HOH   F 5 .   ? 15.526 11.900  7.907   1.00 34.06 ?  381 HOH   A O    1 
HETATM 6808 O  O    . HOH   F 5 .   ? 22.574 -11.940 21.759  1.00 42.21 ?  382 HOH   A O    1 
HETATM 6809 O  O    . HOH   F 5 .   ? 25.735 -0.777  -7.353  1.00 20.71 ?  383 HOH   A O    1 
HETATM 6810 O  O    . HOH   F 5 .   ? 37.531 -2.131  5.835   1.00 28.13 ?  384 HOH   A O    1 
HETATM 6811 O  O    . HOH   F 5 .   ? 23.466 11.348  4.077   1.00 16.28 ?  385 HOH   A O    1 
HETATM 6812 O  O    . HOH   F 5 .   ? 31.821 -7.294  -9.847  1.00 23.85 ?  386 HOH   A O    1 
HETATM 6813 O  O    . HOH   F 5 .   ? 33.524 -16.884 8.109   1.00 23.89 ?  387 HOH   A O    1 
HETATM 6814 O  O    . HOH   F 5 .   ? 23.993 -15.684 -9.145  1.00 35.23 ?  388 HOH   A O    1 
HETATM 6815 O  O    . HOH   F 5 .   ? 24.201 -7.797  14.367  1.00 21.16 ?  389 HOH   A O    1 
HETATM 6816 O  O    . HOH   F 5 .   ? 30.884 -15.689 2.640   1.00 18.51 ?  390 HOH   A O    1 
HETATM 6817 O  O    . HOH   F 5 .   ? 16.497 -22.083 0.983   1.00 28.75 ?  391 HOH   A O    1 
HETATM 6818 O  O    . HOH   F 5 .   ? 13.985 -5.025  17.318  1.00 27.39 ?  392 HOH   A O    1 
HETATM 6819 O  O    . HOH   F 5 .   ? 5.207  2.687   5.126   1.00 34.30 ?  393 HOH   A O    1 
HETATM 6820 O  O    . HOH   F 5 .   ? 15.221 -21.619 14.097  1.00 21.87 ?  394 HOH   A O    1 
HETATM 6821 O  O    . HOH   F 5 .   ? 26.935 4.145   -0.649  1.00 16.06 ?  395 HOH   A O    1 
HETATM 6822 O  O    . HOH   F 5 .   ? 6.702  -3.398  12.809  1.00 33.57 ?  396 HOH   A O    1 
HETATM 6823 O  O    . HOH   F 5 .   ? 32.746 -9.275  5.885   1.00 23.34 ?  397 HOH   A O    1 
HETATM 6824 O  O    . HOH   F 5 .   ? 14.472 -0.439  -12.129 1.00 28.43 ?  398 HOH   A O    1 
HETATM 6825 O  O    . HOH   F 5 .   ? 20.068 4.604   -7.440  1.00 23.90 ?  399 HOH   A O    1 
HETATM 6826 O  O    . HOH   F 5 .   ? 30.657 1.856   16.621  1.00 27.48 ?  400 HOH   A O    1 
HETATM 6827 O  O    . HOH   F 5 .   ? 20.533 -20.026 2.736   1.00 22.68 ?  401 HOH   A O    1 
HETATM 6828 O  O    . HOH   F 5 .   ? 27.322 2.257   18.647  1.00 37.29 ?  402 HOH   A O    1 
HETATM 6829 O  O    . HOH   F 5 .   ? 23.945 -20.286 -1.361  1.00 22.13 ?  403 HOH   A O    1 
HETATM 6830 O  O    B HOH   F 5 .   ? 21.207 2.895   -0.008  0.34 14.92 ?  404 HOH   A O    1 
HETATM 6831 O  O    . HOH   F 5 .   ? 32.690 -4.252  -9.838  1.00 31.50 ?  405 HOH   A O    1 
HETATM 6832 O  O    . HOH   F 5 .   ? 30.919 6.211   -12.263 1.00 30.46 ?  406 HOH   A O    1 
HETATM 6833 O  O    . HOH   F 5 .   ? 14.045 -23.091 7.285   1.00 23.17 ?  407 HOH   A O    1 
HETATM 6834 O  O    . HOH   F 5 .   ? 40.910 -8.231  -6.814  1.00 38.07 ?  408 HOH   A O    1 
HETATM 6835 O  O    . HOH   F 5 .   ? 16.281 16.695  8.594   1.00 28.84 ?  409 HOH   A O    1 
HETATM 6836 O  O    . HOH   F 5 .   ? 38.069 -1.304  -1.906  1.00 22.07 ?  410 HOH   A O    1 
HETATM 6837 O  O    . HOH   F 5 .   ? 24.094 3.980   -4.895  1.00 27.24 ?  411 HOH   A O    1 
HETATM 6838 O  O    . HOH   F 5 .   ? 30.351 -12.986 13.407  1.00 23.94 ?  412 HOH   A O    1 
HETATM 6839 O  O    . HOH   F 5 .   ? 16.046 6.930   2.843   1.00 22.93 ?  413 HOH   A O    1 
HETATM 6840 O  O    A HOH   F 5 .   ? 21.336 3.138   -0.390  0.66 16.28 ?  414 HOH   A O    1 
HETATM 6841 O  O    . HOH   F 5 .   ? 7.650  -6.252  -6.586  1.00 40.64 ?  415 HOH   A O    1 
HETATM 6842 O  O    . HOH   F 5 .   ? 35.108 -5.244  -3.116  1.00 21.19 ?  416 HOH   A O    1 
HETATM 6843 O  O    A HOH   F 5 .   ? 15.787 -0.967  5.225   0.66 29.10 ?  417 HOH   A O    1 
HETATM 6844 O  O    . HOH   F 5 .   ? 21.239 -9.213  21.286  1.00 43.72 ?  418 HOH   A O    1 
HETATM 6845 O  O    . HOH   F 5 .   ? 14.452 -24.741 11.484  1.00 36.07 ?  419 HOH   A O    1 
HETATM 6846 O  O    . HOH   F 5 .   ? 27.935 0.800   -7.154  1.00 18.09 ?  420 HOH   A O    1 
HETATM 6847 O  O    . HOH   F 5 .   ? 15.221 -7.980  -9.888  1.00 25.57 ?  421 HOH   A O    1 
HETATM 6848 O  O    . HOH   F 5 .   ? 41.704 1.433   5.037   1.00 38.27 ?  422 HOH   A O    1 
HETATM 6849 O  O    . HOH   F 5 .   ? 32.463 -10.637 3.219   1.00 34.36 ?  423 HOH   A O    1 
HETATM 6850 O  O    . HOH   F 5 .   ? 11.777 -10.835 16.866  1.00 28.60 ?  424 HOH   A O    1 
HETATM 6851 O  O    . HOH   F 5 .   ? -0.638 -8.473  2.155   1.00 43.94 ?  425 HOH   A O    1 
HETATM 6852 O  O    A HOH   F 5 .   ? 28.569 -10.661 -13.947 0.66 34.45 ?  426 HOH   A O    1 
HETATM 6853 O  O    . HOH   F 5 .   ? 30.044 -10.131 13.023  1.00 27.67 ?  427 HOH   A O    1 
HETATM 6854 O  O    . HOH   F 5 .   ? 16.211 -14.256 20.117  1.00 42.07 ?  428 HOH   A O    1 
HETATM 6855 O  O    . HOH   F 5 .   ? 36.751 -4.962  5.345   1.00 25.52 ?  429 HOH   A O    1 
HETATM 6856 O  O    . HOH   F 5 .   ? 10.396 -13.743 -1.744  1.00 21.58 ?  430 HOH   A O    1 
HETATM 6857 O  O    . HOH   F 5 .   ? 22.630 8.121   18.343  1.00 52.40 ?  431 HOH   A O    1 
HETATM 6858 O  O    . HOH   F 5 .   ? 27.005 -3.291  19.382  1.00 38.93 ?  432 HOH   A O    1 
HETATM 6859 O  O    . HOH   F 5 .   ? 37.723 -8.832  -3.529  1.00 26.55 ?  433 HOH   A O    1 
HETATM 6860 O  O    B HOH   F 5 .   ? 22.639 5.568   -1.902  0.34 20.85 ?  434 HOH   A O    1 
HETATM 6861 O  O    A HOH   F 5 .   ? 18.852 2.013   -0.794  0.66 15.25 ?  435 HOH   A O    1 
HETATM 6862 O  O    . HOH   F 5 .   ? 45.068 -0.557  3.013   1.00 42.01 ?  436 HOH   A O    1 
HETATM 6863 O  O    . HOH   F 5 .   ? 9.489  -16.277 -2.054  1.00 43.95 ?  437 HOH   A O    1 
HETATM 6864 O  O    . HOH   F 5 .   ? 21.479 -14.753 17.927  1.00 44.97 ?  438 HOH   A O    1 
HETATM 6865 O  O    . HOH   F 5 .   ? 23.400 -20.942 1.315   1.00 23.41 ?  439 HOH   A O    1 
HETATM 6866 O  O    . HOH   F 5 .   ? 23.485 -8.096  16.996  1.00 26.60 ?  440 HOH   A O    1 
HETATM 6867 O  O    . HOH   F 5 .   ? 23.242 7.621   -3.270  1.00 26.52 ?  441 HOH   A O    1 
HETATM 6868 O  O    . HOH   F 5 .   ? 20.550 -17.779 24.780  1.00 44.87 ?  442 HOH   A O    1 
HETATM 6869 O  O    . HOH   F 5 .   ? 34.442 -8.077  -0.618  1.00 34.95 ?  443 HOH   A O    1 
HETATM 6870 O  O    . HOH   F 5 .   ? 18.394 -16.123 16.297  1.00 35.39 ?  444 HOH   A O    1 
HETATM 6871 O  O    A HOH   F 5 .   ? 16.247 2.924   -1.487  0.66 16.60 ?  445 HOH   A O    1 
HETATM 6872 O  O    . HOH   F 5 .   ? 31.317 -12.781 -0.016  1.00 21.94 ?  446 HOH   A O    1 
HETATM 6873 O  O    . HOH   F 5 .   ? 18.493 4.983   -15.132 1.00 57.25 ?  447 HOH   A O    1 
HETATM 6874 O  O    . HOH   F 5 .   ? 30.553 14.720  2.701   1.00 23.62 ?  448 HOH   A O    1 
HETATM 6875 O  O    . HOH   F 5 .   ? -1.494 -5.018  7.611   1.00 46.35 ?  449 HOH   A O    1 
HETATM 6876 O  O    A HOH   F 5 .   ? 19.293 -11.048 24.116  0.66 37.12 ?  450 HOH   A O    1 
HETATM 6877 O  O    A HOH   F 5 .   ? 14.015 -0.363  3.415   0.66 29.71 ?  451 HOH   A O    1 
HETATM 6878 O  O    . HOH   F 5 .   ? 27.623 6.895   -6.521  1.00 36.27 ?  452 HOH   A O    1 
HETATM 6879 O  O    B HOH   F 5 .   ? 18.714 1.551   -0.444  0.34 16.16 ?  453 HOH   A O    1 
HETATM 6880 O  O    . HOH   F 5 .   ? 32.404 -15.865 10.797  1.00 32.27 ?  454 HOH   A O    1 
HETATM 6881 O  O    . HOH   F 5 .   ? 29.767 -16.058 10.724  1.00 34.98 ?  455 HOH   A O    1 
HETATM 6882 O  O    . HOH   F 5 .   ? 29.817 -2.012  -12.724 1.00 53.19 ?  456 HOH   A O    1 
HETATM 6883 O  O    . HOH   F 5 .   ? 25.442 8.277   -4.899  1.00 27.34 ?  457 HOH   A O    1 
HETATM 6884 O  O    . HOH   F 5 .   ? 19.924 -17.371 -5.037  1.00 26.73 ?  458 HOH   A O    1 
HETATM 6885 O  O    . HOH   F 5 .   ? 24.863 5.556   20.742  1.00 54.47 ?  459 HOH   A O    1 
HETATM 6886 O  O    . HOH   F 5 .   ? 18.681 10.760  11.255  1.00 35.34 ?  460 HOH   A O    1 
HETATM 6887 O  O    . HOH   F 5 .   ? 24.596 14.509  7.718   1.00 36.82 ?  461 HOH   A O    1 
HETATM 6888 O  O    . HOH   F 5 .   ? 23.265 -22.429 -3.194  1.00 39.20 ?  462 HOH   A O    1 
HETATM 6889 O  O    . HOH   F 5 .   ? 21.958 5.184   -6.069  1.00 33.52 ?  463 HOH   A O    1 
HETATM 6890 O  O    . HOH   F 5 .   ? 26.917 11.613  -1.316  1.00 32.54 ?  464 HOH   A O    1 
HETATM 6891 O  O    . HOH   F 5 .   ? 15.727 -21.536 3.602   1.00 24.05 ?  465 HOH   A O    1 
HETATM 6892 O  O    . HOH   F 5 .   ? 12.398 1.643   17.224  1.00 42.34 ?  466 HOH   A O    1 
HETATM 6893 O  O    . HOH   F 5 .   ? 23.465 13.678  5.565   1.00 21.87 ?  467 HOH   A O    1 
HETATM 6894 O  O    . HOH   F 5 .   ? 39.653 -6.999  -3.546  1.00 51.02 ?  468 HOH   A O    1 
HETATM 6895 O  O    . HOH   F 5 .   ? 27.418 -11.470 16.476  1.00 44.31 ?  469 HOH   A O    1 
HETATM 6896 O  O    . HOH   F 5 .   ? 11.024 -14.994 -6.028  1.00 36.72 ?  470 HOH   A O    1 
HETATM 6897 O  O    . HOH   F 5 .   ? 11.950 -13.368 16.372  1.00 52.41 ?  471 HOH   A O    1 
HETATM 6898 O  O    . HOH   F 5 .   ? 18.051 -16.230 -8.842  1.00 40.30 ?  472 HOH   A O    1 
HETATM 6899 O  O    . HOH   F 5 .   ? 25.873 10.774  -3.735  1.00 26.93 ?  473 HOH   A O    1 
HETATM 6900 O  O    . HOH   F 5 .   ? 23.142 11.832  -4.045  1.00 22.90 ?  474 HOH   A O    1 
HETATM 6901 O  O    . HOH   F 5 .   ? 17.319 -18.691 19.834  1.00 43.23 ?  475 HOH   A O    1 
HETATM 6902 O  O    . HOH   F 5 .   ? 35.139 7.466   12.218  1.00 53.99 ?  476 HOH   A O    1 
HETATM 6903 O  O    . HOH   F 5 .   ? 28.810 8.979   17.540  1.00 40.59 ?  477 HOH   A O    1 
HETATM 6904 O  O    . HOH   F 5 .   ? 28.674 -8.028  -15.249 1.00 56.10 ?  478 HOH   A O    1 
HETATM 6905 O  O    . HOH   F 5 .   ? 15.753 -17.172 -6.985  1.00 33.68 ?  479 HOH   A O    1 
HETATM 6906 O  O    . HOH   F 5 .   ? 41.133 -3.956  -0.409  1.00 36.42 ?  480 HOH   A O    1 
HETATM 6907 O  O    . HOH   F 5 .   ? 44.475 10.357  -1.720  1.00 32.53 ?  481 HOH   A O    1 
HETATM 6908 O  O    . HOH   F 5 .   ? 30.855 0.755   19.095  1.00 44.19 ?  482 HOH   A O    1 
HETATM 6909 O  O    . HOH   F 5 .   ? 14.052 -10.277 -10.934 1.00 30.09 ?  483 HOH   A O    1 
HETATM 6910 O  O    . HOH   F 5 .   ? 16.833 -20.593 16.083  1.00 31.05 ?  484 HOH   A O    1 
HETATM 6911 O  O    . HOH   F 5 .   ? 23.252 -12.905 19.221  1.00 44.99 ?  485 HOH   A O    1 
HETATM 6912 O  O    . HOH   F 5 .   ? 16.038 -6.605  -11.856 1.00 46.87 ?  486 HOH   A O    1 
HETATM 6913 O  O    . HOH   F 5 .   ? 39.179 2.401   7.315   1.00 32.66 ?  487 HOH   A O    1 
HETATM 6914 O  O    . HOH   F 5 .   ? 41.759 9.554   -3.833  1.00 33.57 ?  488 HOH   A O    1 
HETATM 6915 O  O    . HOH   F 5 .   ? 31.481 -0.603  -10.598 1.00 33.97 ?  489 HOH   A O    1 
HETATM 6916 O  O    . HOH   F 5 .   ? 8.152  -3.128  -5.720  1.00 54.14 ?  490 HOH   A O    1 
HETATM 6917 O  O    . HOH   F 5 .   ? 18.492 -23.250 1.878   1.00 45.45 ?  491 HOH   A O    1 
HETATM 6918 O  O    . HOH   F 5 .   ? 14.074 -25.327 8.853   1.00 33.66 ?  492 HOH   A O    1 
HETATM 6919 O  O    . HOH   F 5 .   ? 40.561 -0.279  -7.785  1.00 35.92 ?  493 HOH   A O    1 
HETATM 6920 O  O    . HOH   F 5 .   ? 16.192 -23.358 5.705   1.00 29.77 ?  494 HOH   A O    1 
HETATM 6921 O  O    . HOH   F 5 .   ? 20.034 -22.389 4.228   1.00 33.96 ?  495 HOH   A O    1 
HETATM 6922 O  O    . HOH   F 5 .   ? 28.828 -4.803  -12.463 1.00 45.71 ?  496 HOH   A O    1 
HETATM 6923 O  O    . HOH   F 5 .   ? 30.754 -5.820  -11.791 1.00 50.42 ?  497 HOH   A O    1 
HETATM 6924 O  O    B HOH   F 5 .   ? 14.762 7.886   4.831   0.34 31.84 ?  498 HOH   A O    1 
HETATM 6925 O  O    . HOH   F 5 .   ? 37.388 -6.634  7.565   1.00 26.08 ?  499 HOH   A O    1 
HETATM 6926 O  O    . HOH   F 5 .   ? 39.493 -0.033  6.656   1.00 33.07 ?  500 HOH   A O    1 
HETATM 6927 O  O    . HOH   F 5 .   ? 28.983 14.481  0.905   1.00 48.97 ?  501 HOH   A O    1 
HETATM 6928 O  O    . HOH   F 5 .   ? 30.611 5.789   -14.774 1.00 35.47 ?  502 HOH   A O    1 
HETATM 6929 O  O    . HOH   F 5 .   ? 37.995 13.966  6.668   1.00 39.05 ?  503 HOH   A O    1 
HETATM 6930 O  O    . HOH   F 5 .   ? 20.472 -16.163 -7.424  1.00 30.00 ?  504 HOH   A O    1 
HETATM 6931 O  O    . HOH   F 5 .   ? 36.435 -6.442  10.228  1.00 49.85 ?  505 HOH   A O    1 
HETATM 6932 O  O    . HOH   F 5 .   ? 22.033 -24.018 4.491   1.00 26.84 ?  506 HOH   A O    1 
HETATM 6933 O  O    . HOH   F 5 .   ? 17.257 -6.777  -14.182 1.00 43.65 ?  507 HOH   A O    1 
HETATM 6934 O  O    A HOH   F 5 .   ? 14.826 8.628   4.839   0.66 36.98 ?  508 HOH   A O    1 
HETATM 6935 O  O    . HOH   F 5 .   ? 24.030 8.962   -7.230  1.00 39.84 ?  509 HOH   A O    1 
HETATM 6936 O  O    . HOH   F 5 .   ? 16.472 -21.109 18.673  1.00 40.13 ?  510 HOH   A O    1 
HETATM 6937 O  O    . HOH   F 5 .   ? 15.832 -12.130 27.247  1.00 41.68 ?  511 HOH   A O    1 
HETATM 6938 O  O    . HOH   F 5 .   ? 14.663 -22.716 19.753  1.00 33.37 ?  512 HOH   A O    1 
HETATM 6939 O  O    . HOH   G 5 .   ? 29.916 -22.457 5.482   1.00 24.88 ?  201 HOH   B O    1 
HETATM 6940 O  O    . HOH   G 5 .   ? 41.739 -35.939 -17.095 1.00 36.45 ?  202 HOH   B O    1 
HETATM 6941 O  O    . HOH   G 5 .   ? 27.805 -29.211 -1.923  1.00 33.68 ?  203 HOH   B O    1 
HETATM 6942 O  O    . HOH   G 5 .   ? 30.037 -26.273 4.142   1.00 31.87 ?  204 HOH   B O    1 
HETATM 6943 O  O    . HOH   G 5 .   ? 56.657 -30.735 -7.804  1.00 35.88 ?  205 HOH   B O    1 
HETATM 6944 O  O    . HOH   G 5 .   ? 31.091 -28.764 4.418   1.00 33.48 ?  206 HOH   B O    1 
HETATM 6945 O  O    . HOH   G 5 .   ? 59.133 -18.653 6.862   1.00 41.21 ?  207 HOH   B O    1 
HETATM 6946 O  O    . HOH   G 5 .   ? 48.096 -6.909  15.508  1.00 34.13 ?  208 HOH   B O    1 
HETATM 6947 O  O    . HOH   G 5 .   ? 27.820 -41.603 -15.228 1.00 36.24 ?  209 HOH   B O    1 
HETATM 6948 O  O    . HOH   G 5 .   ? 41.399 -7.769  5.391   1.00 42.64 ?  210 HOH   B O    1 
HETATM 6949 O  O    . HOH   G 5 .   ? 30.256 -41.000 -8.094  1.00 22.40 ?  211 HOH   B O    1 
HETATM 6950 O  O    . HOH   G 5 .   ? 34.967 -24.718 13.684  1.00 44.30 ?  212 HOH   B O    1 
HETATM 6951 O  O    . HOH   G 5 .   ? 47.480 -7.398  -3.963  1.00 44.53 ?  213 HOH   B O    1 
HETATM 6952 O  O    . HOH   G 5 .   ? 54.530 -9.415  -8.606  1.00 21.51 ?  214 HOH   B O    1 
HETATM 6953 O  O    . HOH   G 5 .   ? 53.020 -13.470 -20.384 1.00 39.45 ?  215 HOH   B O    1 
HETATM 6954 O  O    . HOH   G 5 .   ? 50.210 -3.334  7.133   1.00 34.44 ?  216 HOH   B O    1 
HETATM 6955 O  O    . HOH   G 5 .   ? 34.594 -36.451 -7.170  1.00 22.88 ?  217 HOH   B O    1 
HETATM 6956 O  O    . HOH   G 5 .   ? 56.333 -19.706 7.307   1.00 33.58 ?  218 HOH   B O    1 
HETATM 6957 O  O    . HOH   G 5 .   ? 38.142 -39.425 -0.198  1.00 42.73 ?  219 HOH   B O    1 
HETATM 6958 O  O    . HOH   G 5 .   ? 58.196 -12.918 8.385   1.00 32.16 ?  220 HOH   B O    1 
HETATM 6959 O  O    . HOH   G 5 .   ? 41.509 -39.151 -14.910 1.00 26.61 ?  221 HOH   B O    1 
HETATM 6960 O  O    . HOH   G 5 .   ? 57.135 -26.870 -7.606  1.00 38.31 ?  222 HOH   B O    1 
HETATM 6961 O  O    . HOH   G 5 .   ? 57.354 -16.246 -12.269 1.00 21.13 ?  223 HOH   B O    1 
HETATM 6962 O  O    . HOH   G 5 .   ? 46.950 -29.592 9.683   1.00 36.88 ?  224 HOH   B O    1 
HETATM 6963 O  O    . HOH   G 5 .   ? 49.470 -22.764 -19.815 1.00 50.86 ?  225 HOH   B O    1 
HETATM 6964 O  O    . HOH   G 5 .   ? 44.406 -7.271  2.077   1.00 33.31 ?  226 HOH   B O    1 
HETATM 6965 O  O    . HOH   G 5 .   ? 48.568 -36.502 -15.448 1.00 50.48 ?  227 HOH   B O    1 
HETATM 6966 O  O    . HOH   G 5 .   ? 35.088 -8.019  -3.035  1.00 21.52 ?  228 HOH   B O    1 
HETATM 6967 O  O    . HOH   G 5 .   ? 38.515 -11.060 -2.334  1.00 22.71 ?  229 HOH   B O    1 
HETATM 6968 O  O    . HOH   G 5 .   ? 44.541 -27.652 -0.673  1.00 26.06 ?  230 HOH   B O    1 
HETATM 6969 O  O    . HOH   G 5 .   ? 41.361 -9.635  12.984  1.00 24.05 ?  231 HOH   B O    1 
HETATM 6970 O  O    . HOH   G 5 .   ? 50.749 -12.976 -0.479  1.00 15.45 ?  232 HOH   B O    1 
HETATM 6971 O  O    . HOH   G 5 .   ? 50.739 -6.066  0.199   1.00 28.87 ?  233 HOH   B O    1 
HETATM 6972 O  O    . HOH   G 5 .   ? 51.547 -13.846 10.936  1.00 34.12 ?  234 HOH   B O    1 
HETATM 6973 O  O    . HOH   G 5 .   ? 37.071 -19.824 -18.141 1.00 43.45 ?  235 HOH   B O    1 
HETATM 6974 O  O    . HOH   G 5 .   ? 51.658 -6.476  4.340   1.00 22.90 ?  236 HOH   B O    1 
HETATM 6975 O  O    . HOH   G 5 .   ? 39.540 -11.150 0.250   1.00 20.21 ?  237 HOH   B O    1 
HETATM 6976 O  O    . HOH   G 5 .   ? 29.818 -34.057 -0.469  1.00 39.93 ?  238 HOH   B O    1 
HETATM 6977 O  O    . HOH   G 5 .   ? 45.202 -35.026 6.816   1.00 46.92 ?  239 HOH   B O    1 
HETATM 6978 O  O    . HOH   G 5 .   ? 40.671 -16.049 14.053  1.00 23.90 ?  240 HOH   B O    1 
HETATM 6979 O  O    . HOH   G 5 .   ? 58.188 -10.671 -4.019  1.00 22.74 ?  241 HOH   B O    1 
HETATM 6980 O  O    . HOH   G 5 .   ? 42.612 -25.370 2.729   1.00 19.80 ?  242 HOH   B O    1 
HETATM 6981 O  O    . HOH   G 5 .   ? 57.639 -24.339 -3.790  1.00 23.70 ?  243 HOH   B O    1 
HETATM 6982 O  O    . HOH   G 5 .   ? 32.843 -43.809 -11.244 1.00 28.38 ?  244 HOH   B O    1 
HETATM 6983 O  O    . HOH   G 5 .   ? 55.395 -16.497 -14.320 1.00 35.39 ?  245 HOH   B O    1 
HETATM 6984 O  O    . HOH   G 5 .   ? 27.070 -31.836 -9.890  1.00 25.10 ?  246 HOH   B O    1 
HETATM 6985 O  O    . HOH   G 5 .   ? 28.423 -19.704 -13.109 1.00 29.78 ?  247 HOH   B O    1 
HETATM 6986 O  O    . HOH   G 5 .   ? 42.662 -22.850 3.859   1.00 16.28 ?  248 HOH   B O    1 
HETATM 6987 O  O    . HOH   G 5 .   ? 25.478 -25.957 -1.261  1.00 37.46 ?  249 HOH   B O    1 
HETATM 6988 O  O    . HOH   G 5 .   ? 43.041 -43.218 -8.180  1.00 34.88 ?  250 HOH   B O    1 
HETATM 6989 O  O    . HOH   G 5 .   ? 29.748 -25.194 -10.721 1.00 22.57 ?  251 HOH   B O    1 
HETATM 6990 O  O    . HOH   G 5 .   ? 38.969 -11.975 12.348  1.00 40.22 ?  252 HOH   B O    1 
HETATM 6991 O  O    . HOH   G 5 .   ? 46.371 -1.518  13.176  1.00 29.37 ?  253 HOH   B O    1 
HETATM 6992 O  O    . HOH   G 5 .   ? 57.753 -24.504 4.975   1.00 42.77 ?  254 HOH   B O    1 
HETATM 6993 O  O    . HOH   G 5 .   ? 31.783 -17.988 -14.543 1.00 34.86 ?  255 HOH   B O    1 
HETATM 6994 O  O    . HOH   G 5 .   ? 44.824 -43.606 -10.505 1.00 32.63 ?  256 HOH   B O    1 
HETATM 6995 O  O    . HOH   G 5 .   ? 39.319 -10.804 6.086   1.00 27.47 ?  257 HOH   B O    1 
HETATM 6996 O  O    . HOH   G 5 .   ? 40.392 -12.761 -11.543 1.00 19.31 ?  258 HOH   B O    1 
HETATM 6997 O  O    . HOH   G 5 .   ? 48.040 -22.791 5.781   1.00 21.91 ?  259 HOH   B O    1 
HETATM 6998 O  O    . HOH   G 5 .   ? 30.565 -42.267 -10.612 1.00 34.03 ?  260 HOH   B O    1 
HETATM 6999 O  O    . HOH   G 5 .   ? 28.214 -34.373 -9.349  1.00 25.34 ?  261 HOH   B O    1 
HETATM 7000 O  O    . HOH   G 5 .   ? 50.969 -39.958 -8.251  1.00 35.88 ?  262 HOH   B O    1 
HETATM 7001 O  O    . HOH   G 5 .   ? 46.623 -31.253 -4.814  1.00 28.80 ?  263 HOH   B O    1 
HETATM 7002 O  O    . HOH   G 5 .   ? 43.176 -32.376 -17.066 1.00 29.57 ?  264 HOH   B O    1 
HETATM 7003 O  O    . HOH   G 5 .   ? 34.249 -18.406 11.424  1.00 30.16 ?  265 HOH   B O    1 
HETATM 7004 O  O    . HOH   G 5 .   ? 47.091 -34.002 -4.678  1.00 22.94 ?  266 HOH   B O    1 
HETATM 7005 O  O    . HOH   G 5 .   ? 27.640 -26.721 -15.664 1.00 36.10 ?  267 HOH   B O    1 
HETATM 7006 O  O    . HOH   G 5 .   ? 43.407 -15.778 -12.215 1.00 17.59 ?  268 HOH   B O    1 
HETATM 7007 O  O    . HOH   G 5 .   ? 41.945 -23.495 9.275   1.00 26.40 ?  269 HOH   B O    1 
HETATM 7008 O  O    . HOH   G 5 .   ? 42.368 -9.941  9.303   1.00 23.56 ?  270 HOH   B O    1 
HETATM 7009 O  O    . HOH   G 5 .   ? 49.350 -28.694 -6.865  1.00 19.26 ?  271 HOH   B O    1 
HETATM 7010 O  O    . HOH   G 5 .   ? 56.940 -8.606  8.395   1.00 21.50 ?  272 HOH   B O    1 
HETATM 7011 O  O    . HOH   G 5 .   ? 49.648 -0.447  10.257  1.00 32.88 ?  273 HOH   B O    1 
HETATM 7012 O  O    . HOH   G 5 .   ? 57.472 -9.184  1.335   1.00 21.63 ?  274 HOH   B O    1 
HETATM 7013 O  O    . HOH   G 5 .   ? 59.786 -15.285 8.118   1.00 37.17 ?  275 HOH   B O    1 
HETATM 7014 O  O    . HOH   G 5 .   ? 28.424 -30.937 -14.693 1.00 37.36 ?  276 HOH   B O    1 
HETATM 7015 O  O    . HOH   G 5 .   ? 56.171 -23.621 -14.769 1.00 30.91 ?  277 HOH   B O    1 
HETATM 7016 O  O    . HOH   G 5 .   ? 42.444 -34.696 3.822   1.00 29.93 ?  278 HOH   B O    1 
HETATM 7017 O  O    . HOH   G 5 .   ? 57.151 -12.066 12.302  1.00 39.73 ?  279 HOH   B O    1 
HETATM 7018 O  O    . HOH   G 5 .   ? 48.428 -25.043 3.080   1.00 17.91 ?  280 HOH   B O    1 
HETATM 7019 O  O    . HOH   G 5 .   ? 48.714 -20.005 5.898   1.00 17.37 ?  281 HOH   B O    1 
HETATM 7020 O  O    . HOH   G 5 .   ? 42.925 -20.261 -20.679 1.00 40.65 ?  282 HOH   B O    1 
HETATM 7021 O  O    . HOH   G 5 .   ? 27.994 -22.877 -8.003  1.00 22.99 ?  283 HOH   B O    1 
HETATM 7022 O  O    . HOH   G 5 .   ? 45.300 -33.413 -15.870 1.00 30.59 ?  284 HOH   B O    1 
HETATM 7023 O  O    . HOH   G 5 .   ? 41.166 -5.493  11.525  1.00 49.12 ?  285 HOH   B O    1 
HETATM 7024 O  O    . HOH   G 5 .   ? 34.477 -12.721 2.554   1.00 26.23 ?  286 HOH   B O    1 
HETATM 7025 O  O    . HOH   G 5 .   ? 34.964 -33.335 -19.229 1.00 38.41 ?  287 HOH   B O    1 
HETATM 7026 O  O    . HOH   G 5 .   ? 47.961 -24.535 -17.828 1.00 39.28 ?  288 HOH   B O    1 
HETATM 7027 O  O    . HOH   G 5 .   ? 45.862 -40.342 -3.619  1.00 33.00 ?  289 HOH   B O    1 
HETATM 7028 O  O    . HOH   G 5 .   ? 52.563 -35.663 -8.680  1.00 33.00 ?  290 HOH   B O    1 
HETATM 7029 O  O    . HOH   G 5 .   ? 52.479 -10.400 12.961  1.00 24.90 ?  291 HOH   B O    1 
HETATM 7030 O  O    . HOH   G 5 .   ? 36.059 -43.433 -8.348  1.00 41.10 ?  292 HOH   B O    1 
HETATM 7031 O  O    . HOH   G 5 .   ? 33.551 -15.340 -13.961 1.00 25.51 ?  293 HOH   B O    1 
HETATM 7032 O  O    . HOH   G 5 .   ? 52.950 -15.971 -12.777 1.00 26.73 ?  294 HOH   B O    1 
HETATM 7033 O  O    . HOH   G 5 .   ? 53.666 -12.561 -22.226 1.00 36.27 ?  295 HOH   B O    1 
HETATM 7034 O  O    . HOH   G 5 .   ? 49.886 -24.781 5.783   1.00 39.13 ?  296 HOH   B O    1 
HETATM 7035 O  O    . HOH   G 5 .   ? 42.739 -12.245 -18.485 1.00 30.02 ?  297 HOH   B O    1 
HETATM 7036 O  O    . HOH   G 5 .   ? 57.484 -21.820 3.574   1.00 35.00 ?  298 HOH   B O    1 
HETATM 7037 O  O    . HOH   G 5 .   ? 51.214 -37.614 -9.713  1.00 31.69 ?  299 HOH   B O    1 
HETATM 7038 O  O    . HOH   G 5 .   ? 35.091 -33.590 4.563   1.00 35.92 ?  300 HOH   B O    1 
HETATM 7039 O  O    . HOH   G 5 .   ? 37.467 -17.939 13.061  1.00 38.78 ?  301 HOH   B O    1 
HETATM 7040 O  O    . HOH   G 5 .   ? 25.992 -21.490 -3.495  1.00 21.02 ?  302 HOH   B O    1 
HETATM 7041 O  O    . HOH   G 5 .   ? 62.812 -20.110 -0.772  1.00 41.50 ?  303 HOH   B O    1 
HETATM 7042 O  O    . HOH   G 5 .   ? 51.659 -6.069  -7.965  1.00 41.04 ?  304 HOH   B O    1 
HETATM 7043 O  O    . HOH   G 5 .   ? 44.666 -27.461 2.017   1.00 24.27 ?  305 HOH   B O    1 
HETATM 7044 O  O    . HOH   G 5 .   ? 37.848 -10.266 -10.785 1.00 21.35 ?  306 HOH   B O    1 
HETATM 7045 O  O    . HOH   G 5 .   ? 36.858 -12.748 -1.459  1.00 30.26 ?  307 HOH   B O    1 
HETATM 7046 O  O    . HOH   G 5 .   ? 62.707 -13.533 4.764   1.00 28.15 ?  308 HOH   B O    1 
HETATM 7047 O  O    . HOH   G 5 .   ? 53.446 -30.234 4.499   1.00 24.97 ?  309 HOH   B O    1 
HETATM 7048 O  O    . HOH   G 5 .   ? 44.111 -29.319 -4.573  1.00 24.91 ?  310 HOH   B O    1 
HETATM 7049 O  O    . HOH   G 5 .   ? 38.420 -9.404  -13.328 1.00 31.14 ?  311 HOH   B O    1 
HETATM 7050 O  O    . HOH   G 5 .   ? 43.218 -21.422 10.670  1.00 20.65 ?  312 HOH   B O    1 
HETATM 7051 O  O    . HOH   G 5 .   ? 33.779 -31.089 11.013  1.00 39.26 ?  313 HOH   B O    1 
HETATM 7052 O  O    . HOH   G 5 .   ? 42.419 -9.815  -14.903 1.00 40.60 ?  314 HOH   B O    1 
HETATM 7053 O  O    . HOH   G 5 .   ? 48.570 -12.040 -14.333 1.00 29.02 ?  315 HOH   B O    1 
HETATM 7054 O  O    . HOH   G 5 .   ? 32.890 -34.663 -5.829  1.00 22.10 ?  316 HOH   B O    1 
HETATM 7055 O  O    . HOH   G 5 .   ? 44.701 -24.561 9.607   1.00 26.06 ?  317 HOH   B O    1 
HETATM 7056 O  O    . HOH   G 5 .   ? 37.085 -30.561 -20.981 1.00 36.84 ?  318 HOH   B O    1 
HETATM 7057 O  O    . HOH   G 5 .   ? 41.771 -8.057  1.385   1.00 23.66 ?  319 HOH   B O    1 
HETATM 7058 O  O    . HOH   G 5 .   ? 52.511 -29.240 -13.124 1.00 28.36 ?  320 HOH   B O    1 
HETATM 7059 O  O    . HOH   G 5 .   ? 48.079 -32.644 -16.626 1.00 47.61 ?  321 HOH   B O    1 
HETATM 7060 O  O    . HOH   G 5 .   ? 26.375 -21.065 -6.240  1.00 21.98 ?  322 HOH   B O    1 
HETATM 7061 O  O    . HOH   G 5 .   ? 37.261 -35.651 7.228   1.00 36.05 ?  323 HOH   B O    1 
HETATM 7062 O  O    . HOH   G 5 .   ? 38.344 -12.688 7.823   1.00 22.13 ?  324 HOH   B O    1 
HETATM 7063 O  O    . HOH   G 5 .   ? 51.401 -33.002 -10.821 1.00 44.69 ?  325 HOH   B O    1 
HETATM 7064 O  O    . HOH   G 5 .   ? 40.281 -10.860 -9.611  1.00 21.43 ?  326 HOH   B O    1 
HETATM 7065 O  O    . HOH   G 5 .   ? 36.757 -12.384 4.246   1.00 20.77 ?  327 HOH   B O    1 
HETATM 7066 O  O    . HOH   G 5 .   ? 47.239 -24.459 8.122   1.00 32.25 ?  328 HOH   B O    1 
HETATM 7067 O  O    . HOH   G 5 .   ? 43.152 -34.577 0.059   1.00 25.06 ?  329 HOH   B O    1 
HETATM 7068 O  O    . HOH   G 5 .   ? 38.412 -12.238 -16.208 1.00 50.12 ?  330 HOH   B O    1 
HETATM 7069 O  O    . HOH   G 5 .   ? 59.966 -17.331 -10.559 1.00 38.17 ?  331 HOH   B O    1 
HETATM 7070 O  O    . HOH   G 5 .   ? 47.504 -27.453 1.942   1.00 20.21 ?  332 HOH   B O    1 
HETATM 7071 O  O    . HOH   G 5 .   ? 44.113 -1.670  7.600   1.00 49.87 ?  333 HOH   B O    1 
HETATM 7072 O  O    . HOH   G 5 .   ? 42.788 -43.461 -14.340 1.00 43.98 ?  334 HOH   B O    1 
HETATM 7073 O  O    . HOH   G 5 .   ? 27.887 -14.733 -9.527  1.00 36.15 ?  335 HOH   B O    1 
HETATM 7074 O  O    . HOH   G 5 .   ? 43.478 -15.405 18.074  1.00 29.35 ?  336 HOH   B O    1 
HETATM 7075 O  O    . HOH   G 5 .   ? 28.923 -42.854 -12.303 1.00 40.65 ?  337 HOH   B O    1 
HETATM 7076 O  O    . HOH   G 5 .   ? 46.907 -19.822 12.236  1.00 32.29 ?  338 HOH   B O    1 
HETATM 7077 O  O    . HOH   G 5 .   ? 41.391 -24.645 15.751  1.00 46.82 ?  339 HOH   B O    1 
HETATM 7078 O  O    . HOH   G 5 .   ? 37.112 -15.188 -16.514 1.00 43.10 ?  340 HOH   B O    1 
HETATM 7079 O  O    . HOH   G 5 .   ? 37.064 -45.115 -9.617  1.00 38.63 ?  341 HOH   B O    1 
HETATM 7080 O  O    . HOH   G 5 .   ? 45.759 -36.276 -16.033 1.00 39.77 ?  342 HOH   B O    1 
HETATM 7081 O  O    . HOH   G 5 .   ? 39.628 -23.577 -20.427 1.00 36.11 ?  343 HOH   B O    1 
HETATM 7082 O  O    . HOH   G 5 .   ? 34.459 -10.340 7.598   1.00 25.23 ?  344 HOH   B O    1 
HETATM 7083 O  O    . HOH   G 5 .   ? 39.847 -44.216 -11.190 1.00 46.41 ?  345 HOH   B O    1 
HETATM 7084 O  O    . HOH   G 5 .   ? 33.014 -14.680 1.019   1.00 24.11 ?  346 HOH   B O    1 
HETATM 7085 O  O    . HOH   G 5 .   ? 38.641 -22.517 14.983  1.00 45.95 ?  347 HOH   B O    1 
HETATM 7086 O  O    . HOH   G 5 .   ? 40.438 -43.447 -9.136  1.00 26.94 ?  348 HOH   B O    1 
HETATM 7087 O  O    . HOH   G 5 .   ? 55.612 -8.230  10.815  1.00 26.21 ?  349 HOH   B O    1 
HETATM 7088 O  O    . HOH   G 5 .   ? 62.494 -20.160 -4.897  1.00 42.41 ?  350 HOH   B O    1 
HETATM 7089 O  O    . HOH   G 5 .   ? 27.850 -26.590 -0.534  1.00 32.75 ?  351 HOH   B O    1 
HETATM 7090 O  O    . HOH   G 5 .   ? 33.770 -9.392  -8.912  1.00 35.44 ?  352 HOH   B O    1 
HETATM 7091 O  O    . HOH   G 5 .   ? 34.022 -7.866  11.447  1.00 41.13 ?  353 HOH   B O    1 
HETATM 7092 O  O    . HOH   G 5 .   ? 44.227 -37.382 -17.744 1.00 39.50 ?  354 HOH   B O    1 
HETATM 7093 O  O    . HOH   G 5 .   ? 23.282 -23.677 6.789   1.00 35.81 ?  355 HOH   B O    1 
HETATM 7094 O  O    . HOH   G 5 .   ? 36.104 -8.552  -9.761  1.00 36.76 ?  356 HOH   B O    1 
HETATM 7095 O  O    . HOH   G 5 .   ? 56.650 -7.274  2.995   1.00 29.30 ?  357 HOH   B O    1 
HETATM 7096 O  O    . HOH   G 5 .   ? 56.859 -21.610 -16.402 1.00 42.50 ?  358 HOH   B O    1 
HETATM 7097 O  O    . HOH   G 5 .   ? 61.499 -19.854 1.739   1.00 39.00 ?  359 HOH   B O    1 
HETATM 7098 O  O    . HOH   G 5 .   ? 40.306 -8.787  9.815   1.00 38.31 ?  360 HOH   B O    1 
HETATM 7099 O  O    . HOH   G 5 .   ? 27.151 -25.921 -11.288 1.00 38.14 ?  361 HOH   B O    1 
HETATM 7100 O  O    . HOH   G 5 .   ? 43.178 -12.710 -21.165 1.00 40.22 ?  362 HOH   B O    1 
HETATM 7101 O  O    . HOH   G 5 .   ? 48.352 -26.472 8.715   1.00 44.18 ?  363 HOH   B O    1 
HETATM 7102 O  O    . HOH   G 5 .   ? 40.300 -11.328 -14.003 1.00 38.20 ?  364 HOH   B O    1 
HETATM 7103 O  O    . HOH   G 5 .   ? 36.231 -8.684  8.895   1.00 37.39 ?  365 HOH   B O    1 
HETATM 7104 O  O    . HOH   G 5 .   ? 32.706 -23.721 14.024  1.00 36.13 ?  366 HOH   B O    1 
HETATM 7105 O  O    . HOH   G 5 .   ? 54.221 -5.751  2.868   1.00 38.73 ?  367 HOH   B O    1 
HETATM 7106 O  O    . HOH   G 5 .   ? 39.916 -6.991  7.754   1.00 39.61 ?  368 HOH   B O    1 
HETATM 7107 O  O    . HOH   G 5 .   ? 41.853 -10.040 -17.410 1.00 56.47 ?  369 HOH   B O    1 
HETATM 7108 O  O    . HOH   G 5 .   ? 52.026 -12.984 13.300  1.00 28.36 ?  370 HOH   B O    1 
HETATM 7109 O  O    . HOH   G 5 .   ? 59.034 -10.391 9.174   1.00 40.60 ?  371 HOH   B O    1 
HETATM 7110 O  O    . HOH   G 5 .   ? 55.993 -7.695  -0.610  1.00 34.85 ?  372 HOH   B O    1 
HETATM 7111 O  O    . HOH   G 5 .   ? 63.084 -12.307 6.933   1.00 36.63 ?  373 HOH   B O    1 
HETATM 7112 O  O    . HOH   G 5 .   ? 41.835 -6.787  -4.872  1.00 49.78 ?  374 HOH   B O    1 
HETATM 7113 O  O    . HOH   G 5 .   ? 36.570 -22.924 13.276  1.00 35.53 ?  375 HOH   B O    1 
HETATM 7114 O  O    . HOH   G 5 .   ? 38.021 -10.495 9.973   1.00 30.11 ?  376 HOH   B O    1 
HETATM 7115 O  O    . HOH   G 5 .   ? 42.624 -16.965 -23.185 1.00 40.74 ?  377 HOH   B O    1 
HETATM 7116 O  O    . HOH   G 5 .   ? 40.112 -7.583  3.125   1.00 36.52 ?  378 HOH   B O    1 
HETATM 7117 O  O    . HOH   G 5 .   ? 44.099 -5.585  -3.412  1.00 44.31 ?  379 HOH   B O    1 
HETATM 7118 O  O    . HOH   G 5 .   ? 39.594 -13.982 15.597  1.00 47.18 ?  380 HOH   B O    1 
HETATM 7119 O  O    . HOH   G 5 .   ? 46.777 -5.412  2.863   1.00 45.01 ?  381 HOH   B O    1 
HETATM 7120 O  O    . HOH   G 5 .   ? 25.862 -18.937 -11.859 1.00 41.37 ?  382 HOH   B O    1 
HETATM 7121 O  O    . HOH   G 5 .   ? 52.913 -29.875 7.260   1.00 28.18 ?  383 HOH   B O    1 
HETATM 7122 O  O    . HOH   G 5 .   ? 60.515 -22.248 2.916   1.00 47.66 ?  384 HOH   B O    1 
HETATM 7123 O  O    . HOH   G 5 .   ? 35.444 -33.706 7.336   1.00 45.58 ?  385 HOH   B O    1 
HETATM 7124 O  O    . HOH   G 5 .   ? 23.236 -23.782 1.443   1.00 34.84 ?  386 HOH   B O    1 
HETATM 7125 O  O    . HOH   G 5 .   ? 23.952 -20.866 -7.679  1.00 33.63 ?  387 HOH   B O    1 
HETATM 7126 O  O    . HOH   G 5 .   ? 35.274 -20.415 13.241  1.00 35.51 ?  388 HOH   B O    1 
HETATM 7127 O  O    . HOH   G 5 .   ? 40.934 -9.705  15.768  1.00 52.12 ?  389 HOH   B O    1 
HETATM 7128 O  O    . HOH   G 5 .   ? 40.767 -6.620  -0.897  1.00 26.39 ?  390 HOH   B O    1 
HETATM 7129 O  O    . HOH   G 5 .   ? 44.218 -31.646 -3.750  1.00 41.98 ?  391 HOH   B O    1 
HETATM 7130 O  O    . HOH   G 5 .   ? 28.147 -27.091 2.308   1.00 32.42 ?  392 HOH   B O    1 
HETATM 7131 O  O    . HOH   G 5 .   ? 26.683 -28.051 -13.504 1.00 43.31 ?  393 HOH   B O    1 
HETATM 7132 O  O    . HOH   G 5 .   ? 50.712 -30.855 8.649   1.00 33.81 ?  394 HOH   B O    1 
HETATM 7133 O  O    . HOH   G 5 .   ? 24.631 -20.682 -10.477 1.00 41.46 ?  395 HOH   B O    1 
HETATM 7134 O  O    . HOH   G 5 .   ? 26.785 -30.656 -12.580 1.00 34.72 ?  396 HOH   B O    1 
HETATM 7135 O  O    . HOH   G 5 .   ? 34.408 -33.536 9.572   1.00 41.78 ?  397 HOH   B O    1 
HETATM 7136 O  O    . HOH   G 5 .   ? 45.816 -20.049 15.200  1.00 43.92 ?  398 HOH   B O    1 
HETATM 7137 O  O    . HOH   G 5 .   ? 57.639 -6.439  -2.348  1.00 35.18 ?  399 HOH   B O    1 
HETATM 7138 O  O    . HOH   G 5 .   ? 40.810 -11.856 -22.295 1.00 42.09 ?  400 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   A VAL   A 3   ? 0.5208 0.5331 0.5976 -0.0197 -0.0612 0.1239  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.5092 0.5118 0.5721 -0.0129 -0.0410 0.0608  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.5168 0.5287 0.5936 -0.0203 -0.0593 0.1242  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.5058 0.5079 0.5681 -0.0128 -0.0395 0.0606  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.5038 0.5219 0.5745 -0.0252 -0.0527 0.1251  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.4952 0.4990 0.5500 -0.0153 -0.0365 0.0602  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.5063 0.5211 0.5805 -0.0220 -0.0493 0.1282  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.4968 0.4995 0.5534 -0.0129 -0.0353 0.0617  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.5225 0.5293 0.5984 -0.0180 -0.0566 0.1253  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.5105 0.5109 0.5762 -0.0111 -0.0383 0.0616  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.5257 0.5315 0.6050 -0.0175 -0.0532 0.1264  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.5132 0.5135 0.5814 -0.0105 -0.0370 0.0618  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.5219 0.5263 0.6049 -0.0157 -0.0547 0.1266  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.5104 0.5096 0.5816 -0.0099 -0.0376 0.0627  3   VAL   A CG2 
31   N  N   A ASN   A 4   ? 0.4858 0.5152 0.5383 -0.0325 -0.0424 0.1224  4   ASN   A N   
32   N  N   B ASN   A 4   ? 0.4810 0.4885 0.5211 -0.0196 -0.0319 0.0574  4   ASN   A N   
33   C  CA  A ASN   A 4   ? 0.4699 0.5078 0.4968 -0.0421 -0.0303 0.1150  4   ASN   A CA  
34   C  CA  B ASN   A 4   ? 0.4683 0.4782 0.4886 -0.0250 -0.0268 0.0525  4   ASN   A CA  
35   C  C   A ASN   A 4   ? 0.4454 0.4979 0.4714 -0.0546 -0.0096 0.0964  4   ASN   A C   
36   C  C   B ASN   A 4   ? 0.4511 0.4650 0.4687 -0.0298 -0.0161 0.0430  4   ASN   A C   
37   O  O   A ASN   A 4   ? 0.4478 0.4996 0.4663 -0.0548 -0.0114 0.1014  4   ASN   A O   
38   O  O   B ASN   A 4   ? 0.4550 0.4665 0.4677 -0.0297 -0.0172 0.0447  4   ASN   A O   
39   C  CB  A ASN   A 4   ? 0.4782 0.5112 0.4773 -0.0403 -0.0386 0.1240  4   ASN   A CB  
40   C  CB  B ASN   A 4   ? 0.4735 0.4818 0.4732 -0.0256 -0.0319 0.0556  4   ASN   A CB  
41   C  CG  A ASN   A 4   ? 0.4864 0.5118 0.4583 -0.0415 -0.0411 0.1363  4   ASN   A CG  
42   C  CG  B ASN   A 4   ? 0.4789 0.4848 0.4605 -0.0272 -0.0334 0.0600  4   ASN   A CG  
43   O  OD1 A ASN   A 4   ? 0.4932 0.5100 0.4492 -0.0412 -0.0414 0.1411  4   ASN   A OD1 
44   O  OD1 B ASN   A 4   ? 0.4829 0.4854 0.4524 -0.0277 -0.0326 0.0625  4   ASN   A OD1 
45   N  ND2 A ASN   A 4   ? 0.4853 0.5129 0.4500 -0.0415 -0.0428 0.1469  4   ASN   A ND2 
46   N  ND2 B ASN   A 4   ? 0.4789 0.4861 0.4547 -0.0277 -0.0343 0.0633  4   ASN   A ND2 
59   N  N   A SER   A 5   ? 0.4184 0.4833 0.4514 -0.0678 0.0076  0.0750  5   SER   A N   
60   N  N   B SER   A 5   ? 0.4294 0.4474 0.4500 -0.0351 -0.0070 0.0326  5   SER   A N   
61   C  CA  A SER   A 5   ? 0.3914 0.4716 0.4317 -0.0747 0.0221  0.0551  5   SER   A CA  
62   C  CA  B SER   A 5   ? 0.4075 0.4299 0.4298 -0.0373 0.0016  0.0223  5   SER   A CA  
63   C  C   A SER   A 5   ? 0.3588 0.4473 0.3933 -0.0806 0.0351  0.0499  5   SER   A C   
64   C  C   B SER   A 5   ? 0.3806 0.4047 0.3901 -0.0394 0.0090  0.0211  5   SER   A C   
65   O  O   A SER   A 5   ? 0.3708 0.4570 0.3934 -0.0687 0.0415  0.0469  5   SER   A O   
66   O  O   B SER   A 5   ? 0.3852 0.4081 0.3930 -0.0337 0.0107  0.0191  5   SER   A O   
67   C  CB  A SER   A 5   ? 0.3974 0.4816 0.4433 -0.0738 0.0271  0.0431  5   SER   A CB  
68   C  CB  B SER   A 5   ? 0.4129 0.4355 0.4400 -0.0365 0.0031  0.0146  5   SER   A CB  
69   O  OG  A SER   A 5   ? 0.4018 0.4901 0.4560 -0.0704 0.0328  0.0391  5   SER   A OG  
70   O  OG  B SER   A 5   ? 0.4166 0.4393 0.4492 -0.0339 0.0048  0.0112  5   SER   A OG  
81   N  N   A PHE   A 6   ? 0.3095 0.4092 0.3650 -0.0951 0.0448  0.0547  6   PHE   A N   
82   N  N   B PHE   A 6   ? 0.3472 0.3738 0.3536 -0.0452 0.0177  0.0263  6   PHE   A N   
83   C  CA  A PHE   A 6   ? 0.2689 0.3709 0.3345 -0.1031 0.0444  0.0623  6   PHE   A CA  
84   C  CA  B PHE   A 6   ? 0.3174 0.3429 0.3171 -0.0513 0.0241  0.0315  6   PHE   A CA  
85   C  C   A PHE   A 6   ? 0.2641 0.3694 0.3361 -0.1044 0.0506  0.0602  6   PHE   A C   
86   C  C   B PHE   A 6   ? 0.3068 0.3384 0.3108 -0.0464 0.0350  0.0280  6   PHE   A C   
87   O  O   A PHE   A 6   ? 0.2719 0.3801 0.3555 -0.1090 0.0657  0.0715  6   PHE   A O   
88   O  O   B PHE   A 6   ? 0.3068 0.3411 0.3144 -0.0497 0.0370  0.0276  6   PHE   A O   
89   C  CB  A PHE   A 6   ? 0.2471 0.3421 0.3121 -0.1006 0.0341  0.0695  6   PHE   A CB  
90   C  CB  B PHE   A 6   ? 0.3039 0.3206 0.2913 -0.0573 0.0163  0.0376  6   PHE   A CB  
91   C  CG  A PHE   A 6   ? 0.2298 0.3179 0.2920 -0.0969 0.0253  0.0645  6   PHE   A CG  
92   C  CG  B PHE   A 6   ? 0.2895 0.3011 0.2718 -0.0643 0.0121  0.0414  6   PHE   A CG  
93   C  CD1 A PHE   A 6   ? 0.2265 0.3042 0.2843 -0.0860 0.0160  0.0560  6   PHE   A CD1 
94   C  CD1 B PHE   A 6   ? 0.2820 0.2895 0.2637 -0.0686 0.0073  0.0418  6   PHE   A CD1 
95   C  CD2 A PHE   A 6   ? 0.2369 0.3187 0.2899 -0.0794 0.0260  0.0617  6   PHE   A CD2 
96   C  CD2 B PHE   A 6   ? 0.2886 0.2972 0.2603 -0.0592 0.0130  0.0401  6   PHE   A CD2 
97   C  CE1 A PHE   A 6   ? 0.2257 0.2973 0.2894 -0.0809 0.0198  0.0517  6   PHE   A CE1 
98   C  CE1 B PHE   A 6   ? 0.2779 0.2840 0.2630 -0.0693 0.0078  0.0416  6   PHE   A CE1 
99   C  CE2 A PHE   A 6   ? 0.2387 0.3093 0.2883 -0.0770 0.0300  0.0588  6   PHE   A CE2 
100  C  CE2 B PHE   A 6   ? 0.2847 0.2893 0.2615 -0.0629 0.0145  0.0395  6   PHE   A CE2 
101  C  CZ  A PHE   A 6   ? 0.2357 0.2989 0.2940 -0.0819 0.0208  0.0528  6   PHE   A CZ  
102  C  CZ  B PHE   A 6   ? 0.2809 0.2844 0.2611 -0.0678 0.0109  0.0410  6   PHE   A CZ  
121  N  N   A SER   A 7   ? 0.2480 0.3563 0.3129 -0.0986 0.0457  0.0480  7   SER   A N   
122  N  N   B SER   A 7   ? 0.2966 0.3309 0.3093 -0.0379 0.0389  0.0225  7   SER   A N   
123  C  CA  A SER   A 7   ? 0.2495 0.3475 0.3031 -0.0885 0.0417  0.0249  7   SER   A CA  
124  C  CA  B SER   A 7   ? 0.2947 0.3261 0.3087 -0.0305 0.0303  0.0091  7   SER   A CA  
125  C  C   A SER   A 7   ? 0.2321 0.3109 0.2858 -0.0903 0.0511  0.0156  7   SER   A C   
126  C  C   B SER   A 7   ? 0.2799 0.3080 0.2906 -0.0311 0.0293  0.0058  7   SER   A C   
127  O  O   A SER   A 7   ? 0.2345 0.2909 0.2913 -0.0921 0.0486  0.0105  7   SER   A O   
128  O  O   B SER   A 7   ? 0.2873 0.3092 0.2841 -0.0315 0.0236  0.0048  7   SER   A O   
129  C  CB  A SER   A 7   ? 0.2688 0.3715 0.3131 -0.0710 0.0305  0.0213  7   SER   A CB  
130  C  CB  B SER   A 7   ? 0.3065 0.3382 0.3264 -0.0228 0.0267  0.0026  7   SER   A CB  
131  O  OG  A SER   A 7   ? 0.2899 0.3988 0.3303 -0.0543 0.0302  0.0221  7   SER   A OG  
132  O  OG  B SER   A 7   ? 0.3154 0.3472 0.3391 -0.0174 0.0219  0.0007  7   SER   A OG  
143  N  N   A GLY   A 8   ? 0.2217 0.2867 0.2853 -0.0902 0.0514  0.0024  8   GLY   A N   
144  N  N   B GLY   A 8   ? 0.2617 0.2906 0.2703 -0.0294 0.0369  0.0067  8   GLY   A N   
145  C  CA  A GLY   A 8   ? 0.2147 0.2663 0.2730 -0.0725 0.0511  -0.0008 8   GLY   A CA  
146  C  CA  B GLY   A 8   ? 0.2427 0.2740 0.2632 -0.0263 0.0392  0.0060  8   GLY   A CA  
147  C  C   A GLY   A 8   ? 0.2076 0.2472 0.2716 -0.0493 0.0318  -0.0093 8   GLY   A C   
148  C  C   B GLY   A 8   ? 0.2241 0.2580 0.2437 -0.0218 0.0387  0.0056  8   GLY   A C   
149  O  O   A GLY   A 8   ? 0.2022 0.2522 0.2764 -0.0290 0.0377  -0.0254 8   GLY   A O   
150  O  O   B GLY   A 8   ? 0.2215 0.2611 0.2464 -0.0170 0.0470  -0.0070 8   GLY   A O   
157  N  N   A TYR   A 9   ? 0.1944 0.2172 0.2613 -0.0477 0.0255  0.0058  9   TYR   A N   
158  N  N   B TYR   A 9   ? 0.2050 0.2353 0.2384 -0.0196 0.0302  0.0186  9   TYR   A N   
159  C  CA  A TYR   A 9   ? 0.1841 0.1974 0.2432 -0.0355 0.0168  0.0123  9   TYR   A CA  
160  C  CA  B TYR   A 9   ? 0.1894 0.2112 0.2317 -0.0142 0.0375  0.0169  9   TYR   A CA  
161  C  C   A TYR   A 9   ? 0.1964 0.1820 0.2280 -0.0213 0.0249  0.0262  9   TYR   A C   
162  C  C   B TYR   A 9   ? 0.1858 0.1925 0.2157 -0.0040 0.0375  0.0116  9   TYR   A C   
163  O  O   A TYR   A 9   ? 0.2169 0.1946 0.2378 -0.0296 0.0337  0.0103  9   TYR   A O   
164  O  O   B TYR   A 9   ? 0.1945 0.1929 0.2248 0.0007  0.0326  0.0067  9   TYR   A O   
165  C  CB  A TYR   A 9   ? 0.1774 0.2013 0.2624 -0.0218 0.0223  0.0085  9   TYR   A CB  
166  C  CB  B TYR   A 9   ? 0.1902 0.2162 0.2465 -0.0140 0.0343  0.0164  9   TYR   A CB  
167  C  CG  A TYR   A 9   ? 0.1670 0.1992 0.2749 -0.0060 0.0376  0.0149  9   TYR   A CG  
168  C  CG  B TYR   A 9   ? 0.1920 0.2199 0.2549 -0.0190 0.0364  0.0163  9   TYR   A CG  
169  C  CD1 A TYR   A 9   ? 0.1583 0.1953 0.2906 -0.0093 0.0374  0.0196  9   TYR   A CD1 
170  C  CD1 B TYR   A 9   ? 0.1932 0.2163 0.2615 -0.0261 0.0430  0.0154  9   TYR   A CD1 
171  C  CD2 A TYR   A 9   ? 0.1710 0.2026 0.2843 -0.0082 0.0270  0.0245  9   TYR   A CD2 
172  C  CD2 B TYR   A 9   ? 0.1869 0.2178 0.2544 -0.0254 0.0300  0.0262  9   TYR   A CD2 
173  C  CE1 A TYR   A 9   ? 0.1678 0.1969 0.2984 -0.0084 0.0343  0.0184  9   TYR   A CE1 
174  C  CE1 B TYR   A 9   ? 0.1965 0.2134 0.2621 -0.0238 0.0456  0.0202  9   TYR   A CE1 
175  C  CE2 A TYR   A 9   ? 0.1785 0.2039 0.2987 -0.0145 0.0243  0.0207  9   TYR   A CE2 
176  C  CE2 B TYR   A 9   ? 0.1905 0.2187 0.2552 -0.0240 0.0328  0.0295  9   TYR   A CE2 
177  C  CZ  A TYR   A 9   ? 0.1737 0.2025 0.3086 -0.0191 0.0372  0.0103  9   TYR   A CZ  
178  C  CZ  B TYR   A 9   ? 0.1925 0.2125 0.2650 -0.0205 0.0462  0.0299  9   TYR   A CZ  
179  O  OH  A TYR   A 9   ? 0.1859 0.2095 0.3440 -0.0366 0.0390  0.0072  9   TYR   A OH  
180  O  OH  B TYR   A 9   ? 0.1930 0.2122 0.2808 -0.0241 0.0567  0.0344  9   TYR   A OH  
199  N  N   A LEU   A 10  ? 0.1820 0.1662 0.2419 -0.0185 0.0223  0.0287  10  LEU   A N   
200  N  N   B LEU   A 10  ? 0.1763 0.1853 0.2040 -0.0077 0.0387  0.0074  10  LEU   A N   
201  C  CA  A LEU   A 10  ? 0.1737 0.1659 0.2464 -0.0185 0.0235  0.0296  10  LEU   A CA  
202  C  CA  B LEU   A 10  ? 0.1693 0.1795 0.2072 -0.0070 0.0368  0.0013  10  LEU   A CA  
203  C  C   A LEU   A 10  ? 0.1683 0.1591 0.2489 -0.0189 0.0226  0.0323  10  LEU   A C   
204  C  C   B LEU   A 10  ? 0.1596 0.1689 0.1921 -0.0138 0.0399  0.0134  10  LEU   A C   
205  O  O   A LEU   A 10  ? 0.1729 0.1643 0.2395 -0.0174 0.0322  0.0332  10  LEU   A O   
206  O  O   B LEU   A 10  ? 0.1599 0.1664 0.1905 -0.0157 0.0409  0.0171  10  LEU   A O   
207  C  CB  A LEU   A 10  ? 0.1790 0.1703 0.2657 -0.0218 0.0247  0.0378  10  LEU   A CB  
208  C  CB  B LEU   A 10  ? 0.1744 0.1881 0.2225 -0.0086 0.0247  0.0021  10  LEU   A CB  
209  C  CG  A LEU   A 10  ? 0.2044 0.1846 0.3039 -0.0238 0.0068  0.0374  10  LEU   A CG  
210  C  CG  B LEU   A 10  ? 0.1860 0.1981 0.2496 -0.0066 0.0119  0.0052  10  LEU   A CG  
211  C  CD1 A LEU   A 10  ? 0.2186 0.1970 0.3186 -0.0293 0.0157  0.0303  10  LEU   A CD1 
212  C  CD1 B LEU   A 10  ? 0.1980 0.2025 0.2675 -0.0172 0.0104  0.0069  10  LEU   A CD1 
213  C  CD2 A LEU   A 10  ? 0.2287 0.2011 0.3137 -0.0198 0.0214  0.0186  10  LEU   A CD2 
214  C  CD2 B LEU   A 10  ? 0.2019 0.2117 0.2569 0.0015  0.0097  0.0009  10  LEU   A CD2 
237  N  N   A LYS   A 11  ? 0.1664 0.1570 0.2549 -0.0201 0.0358  0.0232  11  LYS   A N   
238  N  N   B LYS   A 11  ? 0.1695 0.1713 0.1974 -0.0233 0.0337  0.0082  11  LYS   A N   
239  C  CA  A LYS   A 11  ? 0.1628 0.1669 0.2598 -0.0226 0.0203  0.0169  11  LYS   A CA  
240  C  CA  B LYS   A 11  ? 0.1743 0.1676 0.1947 -0.0236 0.0279  0.0136  11  LYS   A CA  
241  C  C   A LYS   A 11  ? 0.1541 0.1654 0.2675 -0.0265 0.0216  0.0029  11  LYS   A C   
242  C  C   B LYS   A 11  ? 0.1656 0.1597 0.2012 -0.0216 0.0191  0.0070  11  LYS   A C   
243  O  O   A LYS   A 11  ? 0.1572 0.1861 0.2881 -0.0458 0.0272  -0.0012 11  LYS   A O   
244  O  O   B LYS   A 11  ? 0.1656 0.1529 0.2318 -0.0173 0.0203  -0.0101 11  LYS   A O   
245  C  CB  A LYS   A 11  ? 0.1604 0.1662 0.2509 -0.0245 0.0128  0.0145  11  LYS   A CB  
246  C  CB  B LYS   A 11  ? 0.1907 0.1682 0.1990 -0.0182 0.0207  0.0111  11  LYS   A CB  
247  C  CG  A LYS   A 11  ? 0.1733 0.1618 0.2548 -0.0240 0.0094  0.0318  11  LYS   A CG  
248  C  CG  B LYS   A 11  ? 0.2053 0.1718 0.1935 -0.0116 0.0171  0.0015  11  LYS   A CG  
249  C  CD  A LYS   A 11  ? 0.1890 0.1689 0.2500 -0.0180 0.0056  0.0280  11  LYS   A CD  
250  C  CD  B LYS   A 11  ? 0.2152 0.1740 0.1886 -0.0078 0.0230  0.0034  11  LYS   A CD  
251  C  CE  A LYS   A 11  ? 0.1929 0.1637 0.2634 -0.0097 0.0069  0.0233  11  LYS   A CE  
252  C  CE  B LYS   A 11  ? 0.2183 0.1694 0.1761 -0.0046 0.0222  0.0068  11  LYS   A CE  
253  N  NZ  A LYS   A 11  ? 0.1887 0.1592 0.2644 -0.0011 0.0065  0.0112  11  LYS   A NZ  
254  N  NZ  B LYS   A 11  ? 0.2189 0.1694 0.1643 0.0049  0.0180  0.0213  11  LYS   A NZ  
281  N  N   A LEU   A 12  ? 0.1489 0.1573 0.2635 -0.0265 0.0221  0.0020  12  LEU   A N   
282  N  N   B LEU   A 12  ? 0.1521 0.1711 0.1998 -0.0057 0.0095  -0.0035 12  LEU   A N   
283  C  CA  A LEU   A 12  ? 0.1475 0.1620 0.2610 -0.0228 0.0136  0.0137  12  LEU   A CA  
284  C  CA  B LEU   A 12  ? 0.1560 0.1838 0.2085 0.0027  0.0234  -0.0009 12  LEU   A CA  
285  C  C   A LEU   A 12  ? 0.1491 0.1535 0.2634 -0.0229 0.0157  0.0188  12  LEU   A C   
286  C  C   B LEU   A 12  ? 0.1615 0.1798 0.2047 -0.0006 0.0290  0.0013  12  LEU   A C   
287  O  O   A LEU   A 12  ? 0.1466 0.1515 0.2681 -0.0156 0.0285  0.0159  12  LEU   A O   
288  O  O   B LEU   A 12  ? 0.1738 0.1824 0.1910 0.0007  0.0282  0.0029  12  LEU   A O   
289  C  CB  A LEU   A 12  ? 0.1591 0.1626 0.2717 -0.0188 0.0097  0.0268  12  LEU   A CB  
290  C  CB  B LEU   A 12  ? 0.1652 0.2022 0.2211 0.0099  0.0399  -0.0030 12  LEU   A CB  
291  C  CG  A LEU   A 12  ? 0.1553 0.1793 0.2833 -0.0056 0.0162  0.0239  12  LEU   A CG  
292  C  CG  B LEU   A 12  ? 0.1657 0.2113 0.2427 0.0148  0.0519  0.0059  12  LEU   A CG  
293  C  CD1 A LEU   A 12  ? 0.1644 0.1943 0.2862 0.0125  0.0289  0.0517  12  LEU   A CD1 
294  C  CD1 B LEU   A 12  ? 0.1620 0.2268 0.2510 0.0278  0.0709  0.0163  12  LEU   A CD1 
295  C  CD2 A LEU   A 12  ? 0.1614 0.1864 0.2801 -0.0110 0.0068  0.0144  12  LEU   A CD2 
296  C  CD2 B LEU   A 12  ? 0.1674 0.2149 0.2399 0.0171  0.0423  -0.0066 12  LEU   A CD2 
319  N  N   A THR   A 13  ? 0.1485 0.1538 0.2910 -0.0226 0.0089  0.0165  13  THR   A N   
320  N  N   B THR   A 13  ? 0.1565 0.1767 0.2135 -0.0066 0.0288  -0.0046 13  THR   A N   
321  C  CA  A THR   A 13  ? 0.1518 0.1587 0.3093 -0.0161 0.0168  0.0278  13  THR   A CA  
322  C  CA  B THR   A 13  ? 0.1616 0.1781 0.2365 -0.0155 0.0246  0.0045  13  THR   A CA  
323  C  C   A THR   A 13  ? 0.1546 0.1667 0.3266 -0.0201 0.0174  0.0356  13  THR   A C   
324  C  C   B THR   A 13  ? 0.1661 0.1923 0.2447 -0.0260 0.0210  0.0269  13  THR   A C   
325  O  O   A THR   A 13  ? 0.1568 0.1692 0.3238 -0.0085 0.0149  0.0343  13  THR   A O   
326  O  O   B THR   A 13  ? 0.1609 0.1994 0.2379 -0.0449 0.0212  0.0482  13  THR   A O   
327  C  CB  A THR   A 13  ? 0.1586 0.1684 0.3139 -0.0074 0.0126  0.0368  13  THR   A CB  
328  C  CB  B THR   A 13  ? 0.1587 0.1758 0.2486 -0.0036 0.0281  0.0066  13  THR   A CB  
329  O  OG1 A THR   A 13  ? 0.1657 0.1559 0.3284 -0.0177 0.0052  0.0470  13  THR   A OG1 
330  O  OG1 B THR   A 13  ? 0.1460 0.1792 0.2666 -0.0019 0.0416  0.0234  13  THR   A OG1 
331  C  CG2 A THR   A 13  ? 0.1605 0.1748 0.3158 -0.0038 0.0149  0.0175  13  THR   A CG2 
332  C  CG2 B THR   A 13  ? 0.1518 0.1703 0.2393 0.0061  0.0265  0.0010  13  THR   A CG2 
347  N  N   A ASP   A 14  ? 0.1572 0.1691 0.3398 -0.0276 0.0086  0.0695  14  ASP   A N   
348  N  N   B ASP   A 14  ? 0.1721 0.1994 0.2656 -0.0210 0.0120  0.0374  14  ASP   A N   
349  C  CA  A ASP   A 14  ? 0.1653 0.1885 0.3413 -0.0306 -0.0040 0.0828  14  ASP   A CA  
350  C  CA  B ASP   A 14  ? 0.1794 0.2126 0.2659 -0.0128 0.0043  0.0441  14  ASP   A CA  
351  C  C   A ASP   A 14  ? 0.1640 0.1852 0.3313 -0.0247 -0.0064 0.0811  14  ASP   A C   
352  C  C   B ASP   A 14  ? 0.1668 0.2021 0.2556 -0.0087 0.0046  0.0488  14  ASP   A C   
353  O  O   A ASP   A 14  ? 0.1656 0.1928 0.3344 -0.0323 -0.0086 0.0889  14  ASP   A O   
354  O  O   B ASP   A 14  ? 0.1616 0.2021 0.2616 -0.0019 -0.0014 0.0466  14  ASP   A O   
355  C  CB  A ASP   A 14  ? 0.1785 0.2137 0.3627 -0.0326 -0.0092 0.1019  14  ASP   A CB  
356  C  CB  B ASP   A 14  ? 0.1951 0.2354 0.2855 -0.0035 -0.0019 0.0467  14  ASP   A CB  
357  C  CG  A ASP   A 14  ? 0.2098 0.2620 0.4064 -0.0298 -0.0090 0.0923  14  ASP   A CG  
358  C  CG  B ASP   A 14  ? 0.2064 0.2639 0.3125 0.0020  -0.0051 0.0409  14  ASP   A CG  
359  O  OD1 A ASP   A 14  ? 0.2381 0.2849 0.4274 -0.0155 -0.0155 0.1005  14  ASP   A OD1 
360  O  OD1 B ASP   A 14  ? 0.2162 0.2789 0.3140 0.0207  -0.0213 0.0535  14  ASP   A OD1 
361  O  OD2 A ASP   A 14  ? 0.2301 0.2919 0.4347 -0.0247 -0.0175 0.0495  14  ASP   A OD2 
362  O  OD2 B ASP   A 14  ? 0.2086 0.2782 0.3271 -0.0069 0.0001  0.0200  14  ASP   A OD2 
371  N  N   A ASN   A 15  ? 0.1570 0.1706 0.3492 -0.0236 -0.0059 0.0734  15  ASN   A N   
372  N  N   B ASN   A 15  ? 0.1640 0.1933 0.2641 -0.0181 0.0035  0.0562  15  ASN   A N   
373  C  CA  A ASN   A 15  ? 0.1583 0.1664 0.3617 -0.0291 -0.0018 0.0566  15  ASN   A CA  
374  C  CA  B ASN   A 15  ? 0.1627 0.1853 0.2683 -0.0190 -0.0005 0.0485  15  ASN   A CA  
375  C  C   A ASN   A 15  ? 0.1547 0.1656 0.3668 -0.0225 0.0064  0.0386  15  ASN   A C   
376  C  C   B ASN   A 15  ? 0.1602 0.1756 0.2648 -0.0176 0.0077  0.0437  15  ASN   A C   
377  O  O   A ASN   A 15  ? 0.1584 0.1671 0.4080 -0.0212 -0.0098 0.0439  15  ASN   A O   
378  O  O   B ASN   A 15  ? 0.1616 0.1860 0.2842 -0.0162 0.0069  0.0461  15  ASN   A O   
379  C  CB  A ASN   A 15  ? 0.1510 0.1600 0.3457 -0.0149 -0.0025 0.0614  15  ASN   A CB  
380  C  CB  B ASN   A 15  ? 0.1580 0.1821 0.2613 -0.0030 -0.0085 0.0500  15  ASN   A CB  
381  C  CG  A ASN   A 15  ? 0.1403 0.1647 0.3608 -0.0102 -0.0059 0.0498  15  ASN   A CG  
382  C  CG  B ASN   A 15  ? 0.1480 0.1770 0.2725 0.0065  -0.0101 0.0481  15  ASN   A CG  
383  O  OD1 A ASN   A 15  ? 0.1379 0.1751 0.3777 -0.0198 -0.0097 0.0599  15  ASN   A OD1 
384  O  OD1 B ASN   A 15  ? 0.1478 0.1730 0.2908 0.0085  -0.0132 0.0532  15  ASN   A OD1 
385  N  ND2 A ASN   A 15  ? 0.1456 0.1800 0.3639 -0.0264 -0.0111 0.0473  15  ASN   A ND2 
386  N  ND2 B ASN   A 15  ? 0.1469 0.1786 0.2756 0.0061  -0.0079 0.0469  15  ASN   A ND2 
399  N  N   A VAL   A 16  ? 0.1545 0.1619 0.3240 -0.0085 0.0176  0.0363  16  VAL   A N   
400  N  N   B VAL   A 16  ? 0.1599 0.1566 0.2481 -0.0106 0.0091  0.0439  16  VAL   A N   
401  C  CA  A VAL   A 16  ? 0.1492 0.1531 0.2851 -0.0135 0.0160  0.0198  16  VAL   A CA  
402  C  CA  B VAL   A 16  ? 0.1628 0.1524 0.2111 -0.0081 0.0175  0.0344  16  VAL   A CA  
403  C  C   A VAL   A 16  ? 0.1518 0.1570 0.2607 -0.0199 0.0073  0.0127  16  VAL   A C   
404  C  C   B VAL   A 16  ? 0.1582 0.1655 0.1938 -0.0193 0.0128  0.0199  16  VAL   A C   
405  O  O   A VAL   A 16  ? 0.1356 0.1560 0.2585 -0.0193 0.0167  0.0161  16  VAL   A O   
406  O  O   B VAL   A 16  ? 0.1523 0.1648 0.1885 -0.0282 0.0070  0.0149  16  VAL   A O   
407  C  CB  A VAL   A 16  ? 0.1570 0.1532 0.2660 0.0109  0.0397  0.0231  16  VAL   A CB  
408  C  CB  B VAL   A 16  ? 0.1823 0.1530 0.1918 0.0086  0.0342  0.0190  16  VAL   A CB  
409  C  CG1 A VAL   A 16  ? 0.1859 0.1556 0.2654 0.0104  0.0251  0.0131  16  VAL   A CG1 
410  C  CG1 B VAL   A 16  ? 0.1925 0.1432 0.1877 0.0095  0.0278  0.0075  16  VAL   A CG1 
411  C  CG2 A VAL   A 16  ? 0.1545 0.1819 0.2729 0.0199  0.0556  0.0326  16  VAL   A CG2 
412  C  CG2 B VAL   A 16  ? 0.1880 0.1707 0.1867 0.0163  0.0544  0.0126  16  VAL   A CG2 
431  N  N   A TYR   A 17  ? 0.1576 0.1472 0.2364 -0.0135 0.0201  0.0182  17  TYR   A N   
432  N  N   B TYR   A 17  ? 0.1620 0.1681 0.1857 -0.0250 0.0202  0.0237  17  TYR   A N   
433  C  CA  A TYR   A 17  ? 0.1646 0.1542 0.2189 -0.0151 0.0173  0.0090  17  TYR   A CA  
434  C  CA  B TYR   A 17  ? 0.1651 0.1709 0.1683 -0.0300 0.0203  0.0213  17  TYR   A CA  
435  C  C   A TYR   A 17  ? 0.1648 0.1471 0.2304 -0.0158 0.0181  0.0075  17  TYR   A C   
436  C  C   B TYR   A 17  ? 0.1560 0.1701 0.1603 -0.0313 0.0151  0.0201  17  TYR   A C   
437  O  O   A TYR   A 17  ? 0.1525 0.1573 0.2376 -0.0263 0.0083  0.0200  17  TYR   A O   
438  O  O   B TYR   A 17  ? 0.1448 0.1731 0.1589 -0.0329 0.0071  0.0188  17  TYR   A O   
439  C  CB  A TYR   A 17  ? 0.1705 0.1713 0.2134 -0.0231 0.0110  0.0261  17  TYR   A CB  
440  C  CB  B TYR   A 17  ? 0.1854 0.1722 0.1755 -0.0299 0.0095  0.0115  17  TYR   A CB  
441  C  CG  A TYR   A 17  ? 0.1801 0.1834 0.2128 -0.0258 0.0078  0.0283  17  TYR   A CG  
442  C  CG  B TYR   A 17  ? 0.2073 0.1790 0.1788 -0.0347 0.0010  0.0039  17  TYR   A CG  
443  C  CD1 A TYR   A 17  ? 0.1893 0.1929 0.2174 -0.0142 0.0048  0.0119  17  TYR   A CD1 
444  C  CD1 B TYR   A 17  ? 0.2190 0.1880 0.1826 -0.0314 0.0018  0.0132  17  TYR   A CD1 
445  C  CD2 A TYR   A 17  ? 0.1871 0.1884 0.2139 -0.0376 0.0080  0.0296  17  TYR   A CD2 
446  C  CD2 B TYR   A 17  ? 0.2223 0.1849 0.1861 -0.0421 0.0027  -0.0002 17  TYR   A CD2 
447  C  CE1 A TYR   A 17  ? 0.2030 0.1941 0.2205 -0.0212 0.0046  0.0113  17  TYR   A CE1 
448  C  CE1 B TYR   A 17  ? 0.2284 0.1899 0.2027 -0.0352 0.0039  0.0214  17  TYR   A CE1 
449  C  CE2 A TYR   A 17  ? 0.2035 0.1822 0.2125 -0.0371 0.0082  0.0108  17  TYR   A CE2 
450  C  CE2 B TYR   A 17  ? 0.2366 0.1883 0.1943 -0.0448 -0.0028 0.0054  17  TYR   A CE2 
451  C  CZ  A TYR   A 17  ? 0.2104 0.1850 0.2217 -0.0247 -0.0010 0.0167  17  TYR   A CZ  
452  C  CZ  B TYR   A 17  ? 0.2387 0.1882 0.2028 -0.0411 -0.0001 0.0232  17  TYR   A CZ  
453  O  OH  A TYR   A 17  ? 0.2280 0.1933 0.2421 -0.0232 0.0059  0.0152  17  TYR   A OH  
454  O  OH  B TYR   A 17  ? 0.2515 0.1859 0.2167 -0.0382 0.0043  0.0312  17  TYR   A OH  
473  N  N   A ILE   A 18  ? 0.1631 0.1544 0.2173 -0.0186 0.0343  0.0203  18  ILE   A N   
474  N  N   B ILE   A 18  ? 0.1535 0.1687 0.1601 -0.0296 0.0228  0.0199  18  ILE   A N   
475  C  CA  A ILE   A 18  ? 0.1648 0.1547 0.2220 -0.0181 0.0300  0.0092  18  ILE   A CA  
476  C  CA  B ILE   A 18  ? 0.1549 0.1688 0.1507 -0.0182 0.0243  0.0139  18  ILE   A CA  
477  C  C   A ILE   A 18  ? 0.1677 0.1646 0.2209 -0.0255 0.0246  0.0173  18  ILE   A C   
478  C  C   B ILE   A 18  ? 0.1566 0.1829 0.1525 -0.0158 0.0196  0.0066  18  ILE   A C   
479  O  O   A ILE   A 18  ? 0.1663 0.1777 0.2281 -0.0297 0.0353  0.0231  18  ILE   A O   
480  O  O   B ILE   A 18  ? 0.1573 0.1879 0.1539 -0.0179 0.0310  -0.0023 18  ILE   A O   
481  C  CB  A ILE   A 18  ? 0.1823 0.1637 0.2115 -0.0025 0.0199  0.0236  18  ILE   A CB  
482  C  CB  B ILE   A 18  ? 0.1612 0.1655 0.1350 -0.0099 0.0204  0.0210  18  ILE   A CB  
483  C  CG1 A ILE   A 18  ? 0.1862 0.1742 0.2022 0.0090  -0.0017 0.0124  18  ILE   A CG1 
484  C  CG1 B ILE   A 18  ? 0.1671 0.1685 0.1314 -0.0091 0.0146  0.0297  18  ILE   A CG1 
485  C  CG2 A ILE   A 18  ? 0.1788 0.1643 0.2184 -0.0005 0.0244  0.0201  18  ILE   A CG2 
486  C  CG2 B ILE   A 18  ? 0.1632 0.1742 0.1484 -0.0191 0.0151  0.0185  18  ILE   A CG2 
487  C  CD1 A ILE   A 18  ? 0.2063 0.1932 0.2274 0.0077  -0.0012 0.0062  18  ILE   A CD1 
488  C  CD1 B ILE   A 18  ? 0.1789 0.1710 0.1355 -0.0103 0.0036  0.0147  18  ILE   A CD1 
511  N  N   A LYS   A 19  ? 0.1691 0.1701 0.2379 -0.0174 0.0315  0.0218  19  LYS   A N   
512  N  N   B LYS   A 19  ? 0.1579 0.1957 0.1672 -0.0065 0.0178  0.0031  19  LYS   A N   
513  C  CA  A LYS   A 19  ? 0.1769 0.1786 0.2492 -0.0175 0.0352  0.0182  19  LYS   A CA  
514  C  CA  B LYS   A 19  ? 0.1726 0.2126 0.1938 0.0033  0.0223  0.0003  19  LYS   A CA  
515  C  C   A LYS   A 19  ? 0.1704 0.1822 0.2806 -0.0049 0.0342  0.0386  19  LYS   A C   
516  C  C   B LYS   A 19  ? 0.1724 0.2181 0.2245 0.0116  0.0207  0.0081  19  LYS   A C   
517  O  O   A LYS   A 19  ? 0.1572 0.1737 0.2822 -0.0030 0.0302  0.0427  19  LYS   A O   
518  O  O   B LYS   A 19  ? 0.1768 0.2167 0.2235 0.0152  0.0164  0.0065  19  LYS   A O   
519  C  CB  A LYS   A 19  ? 0.1897 0.1873 0.2592 -0.0182 0.0470  0.0086  19  LYS   A CB  
520  C  CB  B LYS   A 19  ? 0.1803 0.2242 0.1950 0.0022  0.0270  -0.0161 19  LYS   A CB  
521  C  CG  A LYS   A 19  ? 0.2265 0.2060 0.2650 -0.0124 0.0454  -0.0024 19  LYS   A CG  
522  C  CG  B LYS   A 19  ? 0.2016 0.2387 0.2039 0.0025  0.0308  -0.0271 19  LYS   A CG  
523  C  CD  A LYS   A 19  ? 0.2544 0.2218 0.2690 -0.0124 0.0440  -0.0048 19  LYS   A CD  
524  C  CD  B LYS   A 19  ? 0.2196 0.2495 0.2068 0.0006  0.0310  -0.0318 19  LYS   A CD  
525  C  CE  A LYS   A 19  ? 0.2768 0.2360 0.2625 -0.0234 0.0383  -0.0141 19  LYS   A CE  
526  C  CE  B LYS   A 19  ? 0.2288 0.2602 0.2139 0.0019  0.0184  -0.0312 19  LYS   A CE  
527  N  NZ  A LYS   A 19  ? 0.2922 0.2464 0.2692 -0.0392 0.0384  -0.0211 19  LYS   A NZ  
528  N  NZ  B LYS   A 19  ? 0.2392 0.2676 0.2200 -0.0014 0.0183  -0.0326 19  LYS   A NZ  
555  N  N   A ASN   A 20  ? 0.1880 0.1987 0.3338 -0.0094 0.0504  0.0666  20  ASN   A N   
556  N  N   B ASN   A 20  ? 0.1756 0.2313 0.2706 0.0122  0.0311  0.0213  20  ASN   A N   
557  C  CA  A ASN   A 20  ? 0.2009 0.2195 0.3638 0.0206  0.0583  0.0766  20  ASN   A CA  
558  C  CA  B ASN   A 20  ? 0.1747 0.2430 0.2951 0.0224  0.0402  0.0321  20  ASN   A CA  
559  C  C   A ASN   A 20  ? 0.2157 0.2235 0.3692 0.0248  0.0607  0.0656  20  ASN   A C   
560  C  C   B ASN   A 20  ? 0.1891 0.2358 0.3033 0.0128  0.0533  0.0425  20  ASN   A C   
561  O  O   A ASN   A 20  ? 0.2299 0.2235 0.3669 0.0279  0.0607  0.0615  20  ASN   A O   
562  O  O   B ASN   A 20  ? 0.2006 0.2364 0.3129 0.0135  0.0462  0.0550  20  ASN   A O   
563  C  CB  A ASN   A 20  ? 0.2108 0.2277 0.3943 0.0254  0.0688  0.1014  20  ASN   A CB  
564  C  CB  B ASN   A 20  ? 0.1657 0.2540 0.3135 0.0327  0.0379  0.0358  20  ASN   A CB  
565  C  CG  A ASN   A 20  ? 0.2256 0.2294 0.4257 0.0303  0.0787  0.1090  20  ASN   A CG  
566  C  CG  B ASN   A 20  ? 0.1635 0.2626 0.3390 0.0426  0.0315  0.0294  20  ASN   A CG  
567  O  OD1 A ASN   A 20  ? 0.2574 0.2441 0.4670 0.0306  0.0729  0.0854  20  ASN   A OD1 
568  O  OD1 B ASN   A 20  ? 0.1638 0.2673 0.3642 0.0400  0.0385  0.0156  20  ASN   A OD1 
569  N  ND2 A ASN   A 20  ? 0.2377 0.2219 0.4386 0.0302  0.0681  0.1266  20  ASN   A ND2 
570  N  ND2 B ASN   A 20  ? 0.1804 0.2661 0.3505 0.0421  0.0220  0.0359  20  ASN   A ND2 
583  N  N   A ALA   A 21  ? 0.2144 0.2217 0.3779 0.0263  0.0479  0.0522  21  ALA   A N   
584  N  N   B ALA   A 21  ? 0.1945 0.2285 0.3061 -0.0011 0.0553  0.0374  21  ALA   A N   
585  C  CA  A ALA   A 21  ? 0.2183 0.2201 0.3633 0.0221  0.0409  0.0572  21  ALA   A CA  
586  C  CA  B ALA   A 21  ? 0.2028 0.2195 0.2983 -0.0149 0.0645  0.0436  21  ALA   A CA  
587  C  C   A ALA   A 21  ? 0.2175 0.2235 0.3561 0.0126  0.0497  0.0477  21  ALA   A C   
588  C  C   B ALA   A 21  ? 0.1995 0.2087 0.2899 -0.0186 0.0725  0.0328  21  ALA   A C   
589  O  O   A ALA   A 21  ? 0.2229 0.2287 0.3756 0.0097  0.0678  0.0356  21  ALA   A O   
590  O  O   B ALA   A 21  ? 0.1965 0.2038 0.3099 -0.0202 0.0763  0.0157  21  ALA   A O   
591  C  CB  A ALA   A 21  ? 0.2316 0.2197 0.3708 0.0226  0.0265  0.0605  21  ALA   A CB  
592  C  CB  B ALA   A 21  ? 0.2154 0.2226 0.3046 -0.0213 0.0577  0.0492  21  ALA   A CB  
603  N  N   A ASP   A 22  ? 0.2118 0.2195 0.3360 0.0109  0.0500  0.0552  22  ASP   A N   
604  N  N   B ASP   A 22  ? 0.2010 0.2029 0.2730 -0.0155 0.0757  0.0369  22  ASP   A N   
605  C  CA  A ASP   A 22  ? 0.2135 0.2190 0.3174 0.0087  0.0397  0.0458  22  ASP   A CA  
606  C  CA  B ASP   A 22  ? 0.2055 0.2021 0.2625 -0.0111 0.0641  0.0256  22  ASP   A CA  
607  C  C   A ASP   A 22  ? 0.2000 0.2176 0.2735 -0.0025 0.0381  0.0319  22  ASP   A C   
608  C  C   B ASP   A 22  ? 0.1847 0.1914 0.2289 -0.0218 0.0646  0.0083  22  ASP   A C   
609  O  O   A ASP   A 22  ? 0.2096 0.2315 0.2695 -0.0106 0.0385  0.0194  22  ASP   A O   
610  O  O   B ASP   A 22  ? 0.1819 0.1898 0.2385 -0.0207 0.0591  -0.0080 22  ASP   A O   
611  C  CB  A ASP   A 22  ? 0.2424 0.2220 0.3602 0.0087  0.0352  0.0323  22  ASP   A CB  
612  C  CB  B ASP   A 22  ? 0.2231 0.2135 0.2877 0.0060  0.0572  0.0173  22  ASP   A CB  
613  C  CG  A ASP   A 22  ? 0.2600 0.2190 0.4033 -0.0018 0.0162  0.0308  22  ASP   A CG  
614  C  CG  B ASP   A 22  ? 0.2346 0.2175 0.3151 0.0156  0.0517  0.0186  22  ASP   A CG  
615  O  OD1 A ASP   A 22  ? 0.2614 0.2054 0.4153 -0.0375 -0.0069 0.0515  22  ASP   A OD1 
616  O  OD1 B ASP   A 22  ? 0.2293 0.2123 0.3201 0.0176  0.0517  0.0200  22  ASP   A OD1 
617  O  OD2 A ASP   A 22  ? 0.2785 0.2330 0.4310 0.0198  0.0173  0.0155  22  ASP   A OD2 
618  O  OD2 B ASP   A 22  ? 0.2447 0.2301 0.3160 0.0182  0.0604  0.0128  22  ASP   A OD2 
627  N  N   A ILE   A 23  ? 0.1981 0.2048 0.2608 0.0002  0.0453  0.0293  23  ILE   A N   
628  N  N   B ILE   A 23  ? 0.1811 0.1901 0.2138 -0.0174 0.0560  0.0059  23  ILE   A N   
629  C  CA  A ILE   A 23  ? 0.1912 0.1892 0.2476 -0.0065 0.0493  0.0242  23  ILE   A CA  
630  C  CA  B ILE   A 23  ? 0.1758 0.1964 0.1881 -0.0208 0.0474  0.0012  23  ILE   A CA  
631  C  C   A ILE   A 23  ? 0.1950 0.2107 0.2498 -0.0059 0.0636  0.0064  23  ILE   A C   
632  C  C   B ILE   A 23  ? 0.1873 0.2010 0.1934 -0.0263 0.0444  -0.0136 23  ILE   A C   
633  O  O   A ILE   A 23  ? 0.2002 0.2201 0.2642 -0.0073 0.0510  0.0069  23  ILE   A O   
634  O  O   B ILE   A 23  ? 0.1868 0.2004 0.2068 -0.0169 0.0323  -0.0206 23  ILE   A O   
635  C  CB  A ILE   A 23  ? 0.2132 0.1841 0.2289 -0.0016 0.0418  0.0139  23  ILE   A CB  
636  C  CB  B ILE   A 23  ? 0.1760 0.1926 0.1817 -0.0086 0.0375  0.0081  23  ILE   A CB  
637  C  CG1 A ILE   A 23  ? 0.2149 0.1869 0.2266 -0.0013 0.0299  0.0021  23  ILE   A CG1 
638  C  CG1 B ILE   A 23  ? 0.1720 0.1814 0.1791 -0.0097 0.0251  0.0020  23  ILE   A CG1 
639  C  CG2 A ILE   A 23  ? 0.2210 0.1845 0.2245 -0.0072 0.0514  0.0110  23  ILE   A CG2 
640  C  CG2 B ILE   A 23  ? 0.1785 0.1922 0.1831 0.0013  0.0371  0.0115  23  ILE   A CG2 
641  C  CD1 A ILE   A 23  ? 0.2199 0.1853 0.2319 -0.0034 0.0249  -0.0014 23  ILE   A CD1 
642  C  CD1 B ILE   A 23  ? 0.1675 0.1752 0.1816 -0.0044 0.0219  0.0049  23  ILE   A CD1 
665  N  N   A VAL   A 24  ? 0.2035 0.2199 0.2581 -0.0111 0.0638  0.0040  24  VAL   A N   
666  N  N   B VAL   A 24  ? 0.1987 0.2088 0.2051 -0.0372 0.0507  -0.0197 24  VAL   A N   
667  C  CA  A VAL   A 24  ? 0.2222 0.2319 0.2794 -0.0154 0.0465  -0.0008 24  VAL   A CA  
668  C  CA  B VAL   A 24  ? 0.2147 0.2158 0.2264 -0.0475 0.0477  -0.0260 24  VAL   A CA  
669  C  C   A VAL   A 24  ? 0.2317 0.2515 0.2799 -0.0246 0.0426  -0.0113 24  VAL   A C   
670  C  C   B VAL   A 24  ? 0.2148 0.2343 0.2367 -0.0479 0.0505  -0.0324 24  VAL   A C   
671  O  O   A VAL   A 24  ? 0.2434 0.2476 0.2999 -0.0252 0.0531  -0.0124 24  VAL   A O   
672  O  O   B VAL   A 24  ? 0.2235 0.2416 0.2566 -0.0447 0.0485  -0.0212 24  VAL   A O   
673  C  CB  A VAL   A 24  ? 0.2202 0.2298 0.2955 -0.0154 0.0492  0.0082  24  VAL   A CB  
674  C  CB  B VAL   A 24  ? 0.2216 0.2143 0.2398 -0.0552 0.0447  -0.0242 24  VAL   A CB  
675  C  CG1 A VAL   A 24  ? 0.2257 0.2395 0.2908 -0.0071 0.0415  -0.0006 24  VAL   A CG1 
676  C  CG1 B VAL   A 24  ? 0.2340 0.2161 0.2516 -0.0508 0.0390  -0.0232 24  VAL   A CG1 
677  C  CG2 A VAL   A 24  ? 0.2241 0.2341 0.2979 -0.0028 0.0612  0.0087  24  VAL   A CG2 
678  C  CG2 B VAL   A 24  ? 0.2245 0.2165 0.2340 -0.0569 0.0440  -0.0296 24  VAL   A CG2 
697  N  N   A GLU   A 25  ? 0.2423 0.2882 0.2858 -0.0317 0.0464  -0.0239 25  GLU   A N   
698  N  N   B GLU   A 25  ? 0.2174 0.2453 0.2390 -0.0506 0.0662  -0.0415 25  GLU   A N   
699  C  CA  A GLU   A 25  ? 0.2638 0.3201 0.2930 -0.0312 0.0527  -0.0250 25  GLU   A CA  
700  C  CA  B GLU   A 25  ? 0.2305 0.2593 0.2498 -0.0546 0.0628  -0.0414 25  GLU   A CA  
701  C  C   A GLU   A 25  ? 0.2440 0.3243 0.2580 -0.0441 0.0699  -0.0198 25  GLU   A C   
702  C  C   B GLU   A 25  ? 0.2255 0.2680 0.2438 -0.0575 0.0720  -0.0405 25  GLU   A C   
703  O  O   A GLU   A 25  ? 0.2487 0.3344 0.2720 -0.0404 0.0764  -0.0213 25  GLU   A O   
704  O  O   B GLU   A 25  ? 0.2294 0.2729 0.2410 -0.0569 0.0839  -0.0514 25  GLU   A O   
705  C  CB  A GLU   A 25  ? 0.2896 0.3386 0.3198 -0.0251 0.0538  -0.0235 25  GLU   A CB  
706  C  CB  B GLU   A 25  ? 0.2436 0.2644 0.2759 -0.0572 0.0602  -0.0391 25  GLU   A CB  
707  C  CG  A GLU   A 25  ? 0.3163 0.3563 0.3705 -0.0248 0.0401  -0.0247 25  GLU   A CG  
708  C  CG  B GLU   A 25  ? 0.2654 0.2719 0.3092 -0.0566 0.0427  -0.0435 25  GLU   A CG  
709  C  CD  A GLU   A 25  ? 0.3356 0.3703 0.4167 -0.0313 0.0299  -0.0261 25  GLU   A CD  
710  C  CD  B GLU   A 25  ? 0.2801 0.2758 0.3469 -0.0592 0.0248  -0.0452 25  GLU   A CD  
711  O  OE1 A GLU   A 25  ? 0.3425 0.3729 0.4218 -0.0321 0.0167  -0.0392 25  GLU   A OE1 
712  O  OE1 B GLU   A 25  ? 0.2866 0.2751 0.3629 -0.0540 0.0195  -0.0424 25  GLU   A OE1 
713  O  OE2 A GLU   A 25  ? 0.3433 0.3798 0.4528 -0.0364 0.0211  -0.0300 25  GLU   A OE2 
714  O  OE2 B GLU   A 25  ? 0.2914 0.2800 0.3621 -0.0619 0.0155  -0.0456 25  GLU   A OE2 
727  N  N   A GLU   A 26  ? 0.2305 0.3180 0.2479 -0.0639 0.0802  -0.0243 26  GLU   A N   
728  N  N   B GLU   A 26  ? 0.2281 0.2726 0.2418 -0.0574 0.0709  -0.0410 26  GLU   A N   
729  C  CA  A GLU   A 26  ? 0.2415 0.3163 0.2491 -0.0857 0.0756  -0.0078 26  GLU   A CA  
730  C  CA  B GLU   A 26  ? 0.2368 0.2740 0.2399 -0.0505 0.0692  -0.0372 26  GLU   A CA  
731  C  C   A GLU   A 26  ? 0.2371 0.3043 0.2270 -0.0899 0.0642  -0.0035 26  GLU   A C   
732  C  C   B GLU   A 26  ? 0.2313 0.2758 0.2259 -0.0460 0.0608  -0.0215 26  GLU   A C   
733  O  O   A GLU   A 26  ? 0.2450 0.2988 0.2162 -0.1035 0.0700  -0.0050 26  GLU   A O   
734  O  O   B GLU   A 26  ? 0.2284 0.2729 0.2200 -0.0435 0.0658  -0.0242 26  GLU   A O   
735  C  CB  A GLU   A 26  ? 0.2690 0.3233 0.2848 -0.0953 0.0606  0.0008  26  GLU   A CB  
736  C  CB  B GLU   A 26  ? 0.2477 0.2745 0.2608 -0.0508 0.0647  -0.0434 26  GLU   A CB  
737  C  CG  A GLU   A 26  ? 0.2920 0.3383 0.3370 -0.1005 0.0599  0.0028  26  GLU   A CG  
738  C  CG  B GLU   A 26  ? 0.2581 0.2705 0.2739 -0.0597 0.0787  -0.0402 26  GLU   A CG  
739  C  CD  A GLU   A 26  ? 0.3018 0.3571 0.3804 -0.1063 0.0801  0.0117  26  GLU   A CD  
740  C  CD  B GLU   A 26  ? 0.2659 0.2620 0.2908 -0.0764 0.0987  -0.0316 26  GLU   A CD  
741  O  OE1 A GLU   A 26  ? 0.2983 0.3850 0.4006 -0.0995 0.0987  0.0032  26  GLU   A OE1 
742  O  OE1 B GLU   A 26  ? 0.2680 0.2686 0.3118 -0.0742 0.1115  -0.0377 26  GLU   A OE1 
743  O  OE2 A GLU   A 26  ? 0.3238 0.3646 0.3816 -0.1036 0.0760  0.0137  26  GLU   A OE2 
744  O  OE2 B GLU   A 26  ? 0.2734 0.2593 0.2689 -0.0853 0.1097  -0.0354 26  GLU   A OE2 
757  N  N   A ALA   A 27  ? 0.2211 0.2934 0.2338 -0.0938 0.0551  0.0089  27  ALA   A N   
758  N  N   B ALA   A 27  ? 0.2254 0.2798 0.2217 -0.0428 0.0586  0.0023  27  ALA   A N   
759  C  CA  A ALA   A 27  ? 0.2294 0.2920 0.2338 -0.0929 0.0419  0.0116  27  ALA   A CA  
760  C  CA  B ALA   A 27  ? 0.2305 0.2881 0.2243 -0.0374 0.0498  0.0137  27  ALA   A CA  
761  C  C   A ALA   A 27  ? 0.2544 0.3013 0.2496 -0.1029 0.0372  0.0027  27  ALA   A C   
762  C  C   B ALA   A 27  ? 0.2434 0.3024 0.2393 -0.0353 0.0393  0.0150  27  ALA   A C   
763  O  O   A ALA   A 27  ? 0.2604 0.2907 0.2726 -0.1049 0.0312  0.0028  27  ALA   A O   
764  O  O   B ALA   A 27  ? 0.2425 0.2994 0.2565 -0.0341 0.0350  0.0183  27  ALA   A O   
765  C  CB  A ALA   A 27  ? 0.2138 0.2817 0.2347 -0.0918 0.0299  0.0132  27  ALA   A CB  
766  C  CB  B ALA   A 27  ? 0.2229 0.2840 0.2206 -0.0426 0.0533  0.0155  27  ALA   A CB  
777  N  N   A LYS   A 28  ? 0.2845 0.3323 0.2622 -0.0899 0.0392  -0.0084 28  LYS   A N   
778  N  N   B LYS   A 28  ? 0.2629 0.3214 0.2508 -0.0291 0.0316  0.0060  28  LYS   A N   
779  C  CA  A LYS   A 28  ? 0.3145 0.3626 0.2824 -0.0774 0.0479  -0.0178 28  LYS   A CA  
780  C  CA  B LYS   A 28  ? 0.2858 0.3435 0.2695 -0.0235 0.0258  -0.0001 28  LYS   A CA  
781  C  C   A LYS   A 28  ? 0.3296 0.3835 0.2878 -0.0787 0.0647  -0.0063 28  LYS   A C   
782  C  C   B LYS   A 28  ? 0.3055 0.3635 0.2770 -0.0344 0.0339  0.0029  28  LYS   A C   
783  O  O   A LYS   A 28  ? 0.3371 0.3845 0.3078 -0.0691 0.0608  0.0079  28  LYS   A O   
784  O  O   B LYS   A 28  ? 0.3102 0.3604 0.2781 -0.0346 0.0283  0.0064  28  LYS   A O   
785  C  CB  A LYS   A 28  ? 0.3308 0.3758 0.3127 -0.0621 0.0413  -0.0282 28  LYS   A CB  
786  C  CB  B LYS   A 28  ? 0.2937 0.3480 0.2829 -0.0087 0.0149  -0.0074 28  LYS   A CB  
787  C  CG  A LYS   A 28  ? 0.3453 0.3862 0.3453 -0.0477 0.0455  -0.0320 28  LYS   A CG  
788  C  CG  B LYS   A 28  ? 0.2999 0.3521 0.3041 -0.0022 0.0124  -0.0119 28  LYS   A CG  
789  C  CD  A LYS   A 28  ? 0.3534 0.3984 0.3788 -0.0390 0.0524  -0.0382 28  LYS   A CD  
790  C  CD  B LYS   A 28  ? 0.3064 0.3574 0.3199 0.0040  0.0135  -0.0197 28  LYS   A CD  
791  C  CE  A LYS   A 28  ? 0.3553 0.4018 0.4088 -0.0381 0.0597  -0.0377 28  LYS   A CE  
792  C  CE  B LYS   A 28  ? 0.3128 0.3596 0.3306 0.0043  0.0187  -0.0240 28  LYS   A CE  
793  N  NZ  A LYS   A 28  ? 0.3584 0.4011 0.4200 -0.0340 0.0666  -0.0321 28  LYS   A NZ  
794  N  NZ  B LYS   A 28  ? 0.3175 0.3600 0.3393 0.0049  0.0192  -0.0233 28  LYS   A NZ  
821  N  N   A LYS   A 29  ? 0.3341 0.4069 0.2915 -0.0912 0.0892  0.0019  29  LYS   A N   
822  N  N   B LYS   A 29  ? 0.3184 0.3869 0.2968 -0.0492 0.0527  0.0071  29  LYS   A N   
823  C  CA  A LYS   A 29  ? 0.3468 0.4323 0.3165 -0.0990 0.0986  0.0152  29  LYS   A CA  
824  C  CA  B LYS   A 29  ? 0.3368 0.4097 0.3222 -0.0643 0.0620  0.0135  29  LYS   A CA  
825  C  C   A LYS   A 29  ? 0.3465 0.4285 0.3029 -0.1077 0.0846  0.0224  29  LYS   A C   
826  C  C   B LYS   A 29  ? 0.3406 0.4168 0.3116 -0.0880 0.0690  0.0232  29  LYS   A C   
827  O  O   A LYS   A 29  ? 0.3515 0.4324 0.3103 -0.1126 0.0899  0.0287  29  LYS   A O   
828  O  O   B LYS   A 29  ? 0.3456 0.4215 0.3256 -0.0878 0.0669  0.0232  29  LYS   A O   
829  C  CB  A LYS   A 29  ? 0.3588 0.4568 0.3667 -0.0929 0.1090  0.0122  29  LYS   A CB  
830  C  CB  B LYS   A 29  ? 0.3482 0.4219 0.3656 -0.0566 0.0634  0.0094  29  LYS   A CB  
831  C  CG  A LYS   A 29  ? 0.3764 0.4758 0.4167 -0.0827 0.1128  0.0032  29  LYS   A CG  
832  C  CG  B LYS   A 29  ? 0.3584 0.4303 0.4010 -0.0511 0.0626  0.0036  29  LYS   A CG  
833  C  CD  A LYS   A 29  ? 0.3900 0.4917 0.4612 -0.0728 0.1143  -0.0037 29  LYS   A CD  
834  C  CD  B LYS   A 29  ? 0.3667 0.4365 0.4349 -0.0491 0.0596  -0.0014 29  LYS   A CD  
835  C  CE  A LYS   A 29  ? 0.3978 0.4990 0.4969 -0.0681 0.1166  -0.0024 29  LYS   A CE  
836  C  CE  B LYS   A 29  ? 0.3719 0.4408 0.4559 -0.0474 0.0613  -0.0023 29  LYS   A CE  
837  N  NZ  A LYS   A 29  ? 0.3995 0.5027 0.5157 -0.0656 0.1151  -0.0008 29  LYS   A NZ  
838  N  NZ  B LYS   A 29  ? 0.3731 0.4423 0.4686 -0.0460 0.0629  -0.0004 29  LYS   A NZ  
865  N  N   . VAL   A 30  ? 0.3386 0.4171 0.2968 -0.1132 0.0785  0.0286  30  VAL   A N   
866  C  CA  . VAL   A 30  ? 0.3420 0.4070 0.2838 -0.1324 0.0547  0.0409  30  VAL   A CA  
867  C  C   . VAL   A 30  ? 0.3466 0.3976 0.2568 -0.1386 0.0523  0.0402  30  VAL   A C   
868  O  O   . VAL   A 30  ? 0.3586 0.3981 0.2664 -0.1357 0.0553  0.0417  30  VAL   A O   
869  C  CB  . VAL   A 30  ? 0.3419 0.4026 0.2951 -0.1437 0.0335  0.0446  30  VAL   A CB  
870  C  CG1 . VAL   A 30  ? 0.3522 0.4056 0.2996 -0.1377 0.0182  0.0524  30  VAL   A CG1 
871  C  CG2 . VAL   A 30  ? 0.3392 0.3988 0.3179 -0.1530 0.0358  0.0511  30  VAL   A CG2 
882  N  N   . LYS   A 31  ? 0.3383 0.3800 0.2598 -0.1503 0.0362  0.0346  31  LYS   A N   
883  C  CA  . LYS   A 31  ? 0.3573 0.3851 0.2846 -0.1317 0.0155  0.0418  31  LYS   A CA  
884  C  C   . LYS   A 31  ? 0.3313 0.3628 0.2387 -0.1148 0.0014  0.0623  31  LYS   A C   
885  O  O   . LYS   A 31  ? 0.3385 0.3698 0.2467 -0.1068 -0.0104 0.0672  31  LYS   A O   
886  C  CB  . LYS   A 31  ? 0.3971 0.4092 0.3714 -0.1291 0.0053  0.0214  31  LYS   A CB  
887  C  CG  . LYS   A 31  ? 0.4397 0.4416 0.4713 -0.1149 -0.0078 0.0113  31  LYS   A CG  
888  C  CD  . LYS   A 31  ? 0.4729 0.4621 0.5562 -0.1042 -0.0225 -0.0003 31  LYS   A CD  
889  C  CE  . LYS   A 31  ? 0.4888 0.4678 0.6218 -0.0979 -0.0338 -0.0124 31  LYS   A CE  
890  N  NZ  . LYS   A 31  ? 0.4986 0.4806 0.6493 -0.0953 -0.0384 -0.0180 31  LYS   A NZ  
904  N  N   . PRO   A 32  ? 0.2976 0.3288 0.2279 -0.1124 0.0008  0.0631  32  PRO   A N   
905  C  CA  . PRO   A 32  ? 0.2882 0.3123 0.2438 -0.1040 -0.0121 0.0782  32  PRO   A CA  
906  C  C   . PRO   A 32  ? 0.2798 0.3041 0.2550 -0.0905 -0.0099 0.0809  32  PRO   A C   
907  O  O   . PRO   A 32  ? 0.2773 0.2967 0.2614 -0.0897 -0.0319 0.0753  32  PRO   A O   
908  C  CB  . PRO   A 32  ? 0.2829 0.3155 0.2407 -0.1017 -0.0172 0.0750  32  PRO   A CB  
909  C  CG  . PRO   A 32  ? 0.2869 0.3223 0.2402 -0.0922 -0.0208 0.0539  32  PRO   A CG  
910  C  CD  . PRO   A 32  ? 0.2880 0.3261 0.2247 -0.1002 -0.0113 0.0482  32  PRO   A CD  
918  N  N   . THR   A 33  ? 0.2832 0.2998 0.2488 -0.0857 -0.0087 0.0810  33  THR   A N   
919  C  CA  . THR   A 33  ? 0.2829 0.2959 0.2445 -0.0702 -0.0219 0.0782  33  THR   A CA  
920  C  C   . THR   A 33  ? 0.2544 0.2738 0.2360 -0.0635 -0.0219 0.0702  33  THR   A C   
921  O  O   . THR   A 33  ? 0.2522 0.2741 0.2392 -0.0597 -0.0311 0.0711  33  THR   A O   
922  C  CB  . THR   A 33  ? 0.3095 0.3171 0.2586 -0.0493 -0.0325 0.0899  33  THR   A CB  
923  O  OG1 . THR   A 33  ? 0.3338 0.3252 0.2815 -0.0331 -0.0338 0.1050  33  THR   A OG1 
924  C  CG2 . THR   A 33  ? 0.3114 0.3307 0.2634 -0.0359 -0.0319 0.0859  33  THR   A CG2 
932  N  N   . VAL   A 34  ? 0.2210 0.2515 0.2327 -0.0616 -0.0101 0.0606  34  VAL   A N   
933  C  CA  . VAL   A 34  ? 0.2042 0.2259 0.2288 -0.0453 -0.0057 0.0527  34  VAL   A CA  
934  C  C   . VAL   A 34  ? 0.1944 0.2096 0.2412 -0.0373 -0.0035 0.0526  34  VAL   A C   
935  O  O   . VAL   A 34  ? 0.1886 0.2075 0.2626 -0.0445 0.0002  0.0576  34  VAL   A O   
936  C  CB  . VAL   A 34  ? 0.2066 0.2213 0.2500 -0.0400 -0.0033 0.0405  34  VAL   A CB  
937  C  CG1 . VAL   A 34  ? 0.2143 0.2201 0.2582 -0.0354 0.0009  0.0273  34  VAL   A CG1 
938  C  CG2 . VAL   A 34  ? 0.2086 0.2345 0.2668 -0.0371 -0.0034 0.0379  34  VAL   A CG2 
948  N  N   . VAL   A 35  ? 0.1777 0.1950 0.2558 -0.0382 0.0000  0.0437  35  VAL   A N   
949  C  CA  . VAL   A 35  ? 0.1708 0.1894 0.2504 -0.0281 0.0144  0.0464  35  VAL   A CA  
950  C  C   . VAL   A 35  ? 0.1583 0.1807 0.2508 -0.0257 0.0262  0.0349  35  VAL   A C   
951  O  O   . VAL   A 35  ? 0.1557 0.1809 0.2592 -0.0276 0.0189  0.0336  35  VAL   A O   
952  C  CB  . VAL   A 35  ? 0.1739 0.1931 0.2602 -0.0226 0.0186  0.0326  35  VAL   A CB  
953  C  CG1 . VAL   A 35  ? 0.1914 0.1911 0.2526 -0.0200 0.0130  0.0205  35  VAL   A CG1 
954  C  CG2 . VAL   A 35  ? 0.1800 0.1892 0.2798 -0.0179 0.0186  0.0166  35  VAL   A CG2 
964  N  N   . VAL   A 36  ? 0.1399 0.1655 0.2416 -0.0233 0.0291  0.0341  36  VAL   A N   
965  C  CA  . VAL   A 36  ? 0.1413 0.1565 0.2556 -0.0090 0.0219  0.0276  36  VAL   A CA  
966  C  C   . VAL   A 36  ? 0.1391 0.1575 0.2692 -0.0215 0.0118  0.0364  36  VAL   A C   
967  O  O   . VAL   A 36  ? 0.1513 0.1526 0.2818 -0.0129 0.0208  0.0290  36  VAL   A O   
968  C  CB  . VAL   A 36  ? 0.1426 0.1466 0.2552 -0.0135 0.0184  0.0283  36  VAL   A CB  
969  C  CG1 . VAL   A 36  ? 0.1554 0.1520 0.2748 -0.0198 0.0100  0.0170  36  VAL   A CG1 
970  C  CG2 . VAL   A 36  ? 0.1447 0.1585 0.2850 -0.0175 -0.0038 0.0394  36  VAL   A CG2 
980  N  N   . ASN   A 37  ? 0.1402 0.1470 0.2365 -0.0087 0.0020  0.0303  37  ASN   A N   
981  C  CA  . ASN   A 37  ? 0.1385 0.1462 0.2207 -0.0009 -0.0012 0.0228  37  ASN   A CA  
982  C  C   . ASN   A 37  ? 0.1260 0.1371 0.2322 -0.0060 0.0153  0.0315  37  ASN   A C   
983  O  O   . ASN   A 37  ? 0.1412 0.1513 0.2346 -0.0011 0.0156  0.0149  37  ASN   A O   
984  C  CB  . ASN   A 37  ? 0.1412 0.1436 0.2115 -0.0005 0.0102  0.0230  37  ASN   A CB  
985  C  CG  . ASN   A 37  ? 0.1392 0.1413 0.2396 0.0028  0.0134  0.0209  37  ASN   A CG  
986  O  OD1 . ASN   A 37  ? 0.1384 0.1453 0.2566 -0.0016 0.0093  0.0177  37  ASN   A OD1 
987  N  ND2 . ASN   A 37  ? 0.1451 0.1384 0.2560 -0.0017 0.0098  0.0329  37  ASN   A ND2 
994  N  N   A ALA   A 38  ? 0.1321 0.1504 0.2488 -0.0049 0.0183  0.0132  38  ALA   A N   
995  N  N   B ALA   A 38  ? 0.1349 0.1477 0.2238 -0.0078 0.0132  0.0211  38  ALA   A N   
996  C  CA  A ALA   A 38  ? 0.1325 0.1457 0.2380 -0.0019 -0.0042 -0.0023 38  ALA   A CA  
997  C  CA  B ALA   A 38  ? 0.1395 0.1514 0.2100 -0.0045 -0.0028 0.0098  38  ALA   A CA  
998  C  C   A ALA   A 38  ? 0.1363 0.1465 0.2449 0.0028  -0.0008 -0.0018 38  ALA   A C   
999  C  C   B ALA   A 38  ? 0.1385 0.1537 0.2090 -0.0002 -0.0086 0.0003  38  ALA   A C   
1000 O  O   A ALA   A 38  ? 0.1366 0.1308 0.2506 0.0039  -0.0091 -0.0075 38  ALA   A O   
1001 O  O   B ALA   A 38  ? 0.1232 0.1424 0.2141 -0.0053 -0.0175 -0.0039 38  ALA   A O   
1002 C  CB  A ALA   A 38  ? 0.1368 0.1600 0.2579 -0.0140 -0.0037 0.0009  38  ALA   A CB  
1003 C  CB  B ALA   A 38  ? 0.1493 0.1538 0.2094 -0.0057 -0.0068 0.0069  38  ALA   A CB  
1014 N  N   A ALA   A 39  ? 0.1379 0.1434 0.2451 0.0014  0.0100  0.0210  39  ALA   A N   
1015 N  N   B ALA   A 39  ? 0.1514 0.1529 0.2044 -0.0034 -0.0084 0.0023  39  ALA   A N   
1016 C  CA  A ALA   A 39  ? 0.1280 0.1347 0.2318 0.0022  0.0180  0.0164  39  ALA   A CA  
1017 C  CA  B ALA   A 39  ? 0.1630 0.1537 0.1960 -0.0054 -0.0021 -0.0039 39  ALA   A CA  
1018 C  C   A ALA   A 39  ? 0.1205 0.1410 0.2307 0.0004  0.0038  0.0174  39  ALA   A C   
1019 C  C   B ALA   A 39  ? 0.1559 0.1501 0.1806 -0.0029 0.0061  0.0004  39  ALA   A C   
1020 O  O   A ALA   A 39  ? 0.1438 0.1508 0.2334 -0.0031 0.0087  0.0185  39  ALA   A O   
1021 O  O   B ALA   A 39  ? 0.1659 0.1552 0.1836 0.0003  -0.0031 0.0024  39  ALA   A O   
1022 C  CB  A ALA   A 39  ? 0.1299 0.1306 0.2433 0.0084  -0.0044 0.0089  39  ALA   A CB  
1023 C  CB  B ALA   A 39  ? 0.1780 0.1549 0.2027 0.0028  -0.0094 -0.0192 39  ALA   A CB  
1034 N  N   A ASN   A 40  ? 0.1408 0.1396 0.2389 -0.0017 0.0119  0.0152  40  ASN   A N   
1035 N  N   B ASN   A 40  ? 0.1591 0.1464 0.1802 -0.0058 0.0323  0.0063  40  ASN   A N   
1036 C  CA  A ASN   A 40  ? 0.1552 0.1468 0.2477 0.0011  0.0101  0.0161  40  ASN   A CA  
1037 C  CA  B ASN   A 40  ? 0.1651 0.1448 0.1929 -0.0020 0.0313  0.0033  40  ASN   A CA  
1038 C  C   A ASN   A 40  ? 0.1555 0.1410 0.2594 0.0025  0.0166  0.0235  40  ASN   A C   
1039 C  C   B ASN   A 40  ? 0.1645 0.1444 0.1977 -0.0069 0.0401  0.0134  40  ASN   A C   
1040 O  O   A ASN   A 40  ? 0.1496 0.1395 0.2712 -0.0043 0.0175  0.0372  40  ASN   A O   
1041 O  O   B ASN   A 40  ? 0.1559 0.1431 0.1999 -0.0192 0.0408  0.0196  40  ASN   A O   
1042 C  CB  A ASN   A 40  ? 0.1629 0.1551 0.2499 0.0069  -0.0066 0.0171  40  ASN   A CB  
1043 C  CB  B ASN   A 40  ? 0.1793 0.1498 0.2218 0.0011  0.0101  0.0020  40  ASN   A CB  
1044 C  CG  A ASN   A 40  ? 0.1658 0.1567 0.2580 0.0082  0.0016  0.0278  40  ASN   A CG  
1045 C  CG  B ASN   A 40  ? 0.1872 0.1530 0.2534 -0.0012 0.0055  0.0067  40  ASN   A CG  
1046 O  OD1 A ASN   A 40  ? 0.1754 0.1532 0.2964 0.0004  0.0017  0.0267  40  ASN   A OD1 
1047 O  OD1 B ASN   A 40  ? 0.1940 0.1557 0.2769 -0.0033 0.0038  0.0019  40  ASN   A OD1 
1048 N  ND2 A ASN   A 40  ? 0.1571 0.1751 0.2413 0.0133  0.0071  0.0157  40  ASN   A ND2 
1049 N  ND2 B ASN   A 40  ? 0.1866 0.1673 0.2630 -0.0051 0.0041  0.0052  40  ASN   A ND2 
1062 N  N   A VAL   A 41  ? 0.1565 0.1451 0.2629 0.0070  0.0213  0.0258  41  VAL   A N   
1063 N  N   B VAL   A 41  ? 0.1651 0.1425 0.1965 -0.0038 0.0487  0.0193  41  VAL   A N   
1064 C  CA  A VAL   A 41  ? 0.1552 0.1509 0.2577 0.0034  0.0258  0.0234  41  VAL   A CA  
1065 C  CA  B VAL   A 41  ? 0.1706 0.1495 0.2091 -0.0029 0.0477  0.0194  41  VAL   A CA  
1066 C  C   A VAL   A 41  ? 0.1586 0.1517 0.2457 0.0069  0.0320  0.0329  41  VAL   A C   
1067 C  C   B VAL   A 41  ? 0.1641 0.1469 0.2268 0.0015  0.0402  0.0260  41  VAL   A C   
1068 O  O   A VAL   A 41  ? 0.1580 0.1419 0.2244 0.0073  0.0367  0.0301  41  VAL   A O   
1069 O  O   B VAL   A 41  ? 0.1647 0.1333 0.2315 -0.0022 0.0444  0.0223  41  VAL   A O   
1070 C  CB  A VAL   A 41  ? 0.1647 0.1575 0.2467 0.0023  0.0263  0.0215  41  VAL   A CB  
1071 C  CB  B VAL   A 41  ? 0.1781 0.1575 0.2008 -0.0104 0.0506  0.0178  41  VAL   A CB  
1072 C  CG1 A VAL   A 41  ? 0.1739 0.1724 0.2648 0.0022  0.0178  0.0140  41  VAL   A CG1 
1073 C  CG1 B VAL   A 41  ? 0.1953 0.1647 0.2179 -0.0119 0.0502  0.0111  41  VAL   A CG1 
1074 C  CG2 A VAL   A 41  ? 0.1729 0.1612 0.2234 0.0053  0.0346  0.0036  41  VAL   A CG2 
1075 C  CG2 B VAL   A 41  ? 0.1745 0.1644 0.2030 -0.0123 0.0453  0.0090  41  VAL   A CG2 
1094 N  N   . TYR   A 42  ? 0.1480 0.1482 0.2556 0.0011  0.0328  0.0313  42  TYR   A N   
1095 C  CA  . TYR   A 42  ? 0.1484 0.1398 0.2506 -0.0040 0.0395  0.0353  42  TYR   A CA  
1096 C  C   . TYR   A 42  ? 0.1404 0.1416 0.2471 -0.0056 0.0224  0.0332  42  TYR   A C   
1097 O  O   . TYR   A 42  ? 0.1481 0.1472 0.2653 -0.0140 0.0209  0.0165  42  TYR   A O   
1098 C  CB  . TYR   A 42  ? 0.1789 0.1510 0.2228 0.0011  0.0388  0.0303  42  TYR   A CB  
1099 C  CG  . TYR   A 42  ? 0.1974 0.1577 0.2167 -0.0053 0.0287  0.0372  42  TYR   A CG  
1100 C  CD1 . TYR   A 42  ? 0.2009 0.1698 0.2361 -0.0076 0.0263  0.0361  42  TYR   A CD1 
1101 C  CD2 . TYR   A 42  ? 0.2141 0.1780 0.2417 -0.0053 0.0142  0.0277  42  TYR   A CD2 
1102 C  CE1 . TYR   A 42  ? 0.2103 0.1795 0.2402 -0.0153 0.0283  0.0222  42  TYR   A CE1 
1103 C  CE2 . TYR   A 42  ? 0.2262 0.1919 0.2550 -0.0158 0.0157  0.0273  42  TYR   A CE2 
1104 C  CZ  . TYR   A 42  ? 0.2327 0.1958 0.2509 -0.0171 0.0323  0.0285  42  TYR   A CZ  
1105 O  OH  . TYR   A 42  ? 0.2468 0.2126 0.2919 -0.0337 0.0381  0.0189  42  TYR   A OH  
1116 N  N   A LEU   A 43  ? 0.1405 0.1369 0.2497 -0.0106 0.0196  0.0126  43  LEU   A N   
1117 N  N   B LEU   A 43  ? 0.1542 0.1468 0.2203 -0.0095 0.0105  0.0197  43  LEU   A N   
1118 C  CA  A LEU   A 43  ? 0.1312 0.1362 0.2550 -0.0093 0.0242  0.0197  43  LEU   A CA  
1119 C  CA  B LEU   A 43  ? 0.1631 0.1521 0.2084 -0.0089 -0.0003 0.0201  43  LEU   A CA  
1120 C  C   A LEU   A 43  ? 0.1301 0.1408 0.2550 -0.0009 0.0110  0.0164  43  LEU   A C   
1121 C  C   B LEU   A 43  ? 0.1728 0.1636 0.2030 -0.0099 -0.0105 0.0211  43  LEU   A C   
1122 O  O   A LEU   A 43  ? 0.1403 0.1451 0.2836 0.0087  -0.0020 0.0201  43  LEU   A O   
1123 O  O   B LEU   A 43  ? 0.1846 0.1642 0.2131 -0.0129 -0.0133 0.0223  43  LEU   A O   
1124 C  CB  A LEU   A 43  ? 0.1410 0.1399 0.2694 -0.0137 0.0193  0.0214  43  LEU   A CB  
1125 C  CB  B LEU   A 43  ? 0.1632 0.1457 0.2091 -0.0088 -0.0048 0.0182  43  LEU   A CB  
1126 C  CG  A LEU   A 43  ? 0.1503 0.1406 0.2640 -0.0004 0.0107  0.0170  43  LEU   A CG  
1127 C  CG  B LEU   A 43  ? 0.1626 0.1411 0.2036 -0.0079 -0.0088 0.0120  43  LEU   A CG  
1128 C  CD1 A LEU   A 43  ? 0.1543 0.1449 0.2673 0.0010  0.0146  0.0213  43  LEU   A CD1 
1129 C  CD1 B LEU   A 43  ? 0.1638 0.1403 0.2028 -0.0011 -0.0075 0.0107  43  LEU   A CD1 
1130 C  CD2 A LEU   A 43  ? 0.1582 0.1376 0.2497 -0.0017 0.0262  0.0137  43  LEU   A CD2 
1131 C  CD2 B LEU   A 43  ? 0.1669 0.1382 0.1903 -0.0208 -0.0092 0.0190  43  LEU   A CD2 
1154 N  N   A LYS   A 44  ? 0.1329 0.1354 0.2481 0.0007  0.0139  0.0122  44  LYS   A N   
1155 N  N   B LYS   A 44  ? 0.1748 0.1721 0.2010 -0.0072 -0.0116 0.0213  44  LYS   A N   
1156 C  CA  A LYS   A 44  ? 0.1467 0.1370 0.2587 -0.0062 0.0241  0.0179  44  LYS   A CA  
1157 C  CA  B LYS   A 44  ? 0.1852 0.1819 0.2124 -0.0084 -0.0030 0.0195  44  LYS   A CA  
1158 C  C   A LYS   A 44  ? 0.1323 0.1291 0.2495 0.0001  0.0172  0.0157  44  LYS   A C   
1159 C  C   B LYS   A 44  ? 0.1760 0.1757 0.1998 -0.0101 -0.0045 0.0139  44  LYS   A C   
1160 O  O   A LYS   A 44  ? 0.1411 0.1442 0.2650 0.0014  0.0099  0.0054  44  LYS   A O   
1161 O  O   B LYS   A 44  ? 0.1825 0.1754 0.2019 -0.0196 -0.0071 0.0061  44  LYS   A O   
1162 C  CB  A LYS   A 44  ? 0.1742 0.1532 0.2927 -0.0157 0.0323  0.0195  44  LYS   A CB  
1163 C  CB  B LYS   A 44  ? 0.2038 0.2004 0.2546 -0.0040 0.0110  0.0220  44  LYS   A CB  
1164 C  CG  A LYS   A 44  ? 0.2126 0.1855 0.3446 -0.0249 0.0453  0.0243  44  LYS   A CG  
1165 C  CG  B LYS   A 44  ? 0.2208 0.2244 0.3016 0.0024  0.0114  0.0262  44  LYS   A CG  
1166 C  CD  A LYS   A 44  ? 0.2542 0.2400 0.4095 -0.0246 0.0330  0.0238  44  LYS   A CD  
1167 C  CD  B LYS   A 44  ? 0.2411 0.2599 0.3522 0.0000  -0.0050 0.0229  44  LYS   A CD  
1168 C  CE  A LYS   A 44  ? 0.2752 0.2728 0.4562 -0.0192 0.0297  0.0189  44  LYS   A CE  
1169 C  CE  B LYS   A 44  ? 0.2527 0.2847 0.3877 -0.0079 -0.0120 0.0204  44  LYS   A CE  
1170 N  NZ  A LYS   A 44  ? 0.2779 0.2869 0.4794 -0.0101 0.0345  0.0198  44  LYS   A NZ  
1171 N  NZ  B LYS   A 44  ? 0.2615 0.2993 0.4089 -0.0187 -0.0113 0.0196  44  LYS   A NZ  
1198 N  N   A HIS   A 45  ? 0.1251 0.1334 0.2467 0.0014  0.0072  0.0248  45  HIS   A N   
1199 N  N   B HIS   A 45  ? 0.1695 0.1745 0.1969 -0.0094 -0.0119 0.0179  45  HIS   A N   
1200 C  CA  A HIS   A 45  ? 0.1320 0.1368 0.2408 -0.0028 0.0045  0.0291  45  HIS   A CA  
1201 C  CA  B HIS   A 45  ? 0.1631 0.1720 0.2046 -0.0121 -0.0130 0.0144  45  HIS   A CA  
1202 C  C   A HIS   A 45  ? 0.1369 0.1462 0.2483 -0.0024 -0.0046 0.0318  45  HIS   A C   
1203 C  C   B HIS   A 45  ? 0.1623 0.1793 0.2224 -0.0106 -0.0135 0.0091  45  HIS   A C   
1204 O  O   A HIS   A 45  ? 0.1301 0.1468 0.2517 0.0036  -0.0057 0.0169  45  HIS   A O   
1205 O  O   B HIS   A 45  ? 0.1668 0.1809 0.2479 -0.0036 -0.0163 0.0027  45  HIS   A O   
1206 C  CB  A HIS   A 45  ? 0.1370 0.1372 0.2347 0.0005  0.0039  0.0236  45  HIS   A CB  
1207 C  CB  B HIS   A 45  ? 0.1558 0.1641 0.1960 -0.0086 -0.0141 0.0116  45  HIS   A CB  
1208 C  CG  A HIS   A 45  ? 0.1360 0.1327 0.2419 -0.0007 0.0044  0.0144  45  HIS   A CG  
1209 C  CG  B HIS   A 45  ? 0.1440 0.1586 0.1948 -0.0035 -0.0097 0.0161  45  HIS   A CG  
1210 N  ND1 A HIS   A 45  ? 0.1286 0.1348 0.2576 0.0009  0.0120  0.0163  45  HIS   A ND1 
1211 N  ND1 B HIS   A 45  ? 0.1388 0.1585 0.2066 -0.0014 -0.0121 0.0296  45  HIS   A ND1 
1212 C  CD2 A HIS   A 45  ? 0.1414 0.1371 0.2498 -0.0015 -0.0039 0.0231  45  HIS   A CD2 
1213 C  CD2 B HIS   A 45  ? 0.1364 0.1517 0.1901 0.0025  -0.0091 0.0171  45  HIS   A CD2 
1214 C  CE1 A HIS   A 45  ? 0.1383 0.1391 0.2577 -0.0110 0.0147  0.0311  45  HIS   A CE1 
1215 C  CE1 B HIS   A 45  ? 0.1351 0.1459 0.1976 -0.0055 -0.0068 0.0219  45  HIS   A CE1 
1216 N  NE2 A HIS   A 45  ? 0.1414 0.1469 0.2550 -0.0036 0.0109  0.0337  45  HIS   A NE2 
1217 N  NE2 B HIS   A 45  ? 0.1324 0.1513 0.1916 -0.0030 -0.0072 0.0186  45  HIS   A NE2 
1232 N  N   A GLY   A 46  ? 0.1453 0.1601 0.2735 0.0077  -0.0184 0.0293  46  GLY   A N   
1233 N  N   B GLY   A 46  ? 0.1621 0.1808 0.2236 -0.0105 -0.0118 0.0143  46  GLY   A N   
1234 C  CA  A GLY   A 46  ? 0.1448 0.1671 0.2719 0.0145  -0.0165 0.0351  46  GLY   A CA  
1235 C  CA  B GLY   A 46  ? 0.1571 0.1825 0.2103 -0.0072 -0.0055 0.0224  46  GLY   A CA  
1236 C  C   A GLY   A 46  ? 0.1528 0.1603 0.2630 0.0222  -0.0145 0.0422  46  GLY   A C   
1237 C  C   B GLY   A 46  ? 0.1520 0.1758 0.1959 -0.0019 0.0048  0.0286  46  GLY   A C   
1238 O  O   A GLY   A 46  ? 0.1624 0.1520 0.2484 0.0182  -0.0357 0.0351  46  GLY   A O   
1239 O  O   B GLY   A 46  ? 0.1559 0.1810 0.1926 -0.0027 -0.0034 0.0290  46  GLY   A O   
1246 N  N   A GLY   A 47  ? 0.1435 0.1690 0.2600 0.0201  -0.0071 0.0384  47  GLY   A N   
1247 N  N   B GLY   A 47  ? 0.1544 0.1701 0.1826 0.0012  0.0125  0.0280  47  GLY   A N   
1248 C  CA  A GLY   A 47  ? 0.1476 0.1753 0.2414 0.0239  -0.0032 0.0175  47  GLY   A CA  
1249 C  CA  B GLY   A 47  ? 0.1498 0.1706 0.1726 0.0025  0.0134  0.0196  47  GLY   A CA  
1250 C  C   A GLY   A 47  ? 0.1531 0.1636 0.2307 0.0178  -0.0026 0.0164  47  GLY   A C   
1251 C  C   B GLY   A 47  ? 0.1430 0.1582 0.1545 0.0096  0.0191  0.0130  47  GLY   A C   
1252 O  O   A GLY   A 47  ? 0.1514 0.1559 0.2460 0.0241  -0.0002 0.0313  47  GLY   A O   
1253 O  O   B GLY   A 47  ? 0.1434 0.1495 0.1666 0.0228  0.0097  0.0333  47  GLY   A O   
1260 N  N   A GLY   A 48  ? 0.1526 0.1719 0.2276 0.0233  -0.0061 0.0094  48  GLY   A N   
1261 N  N   B GLY   A 48  ? 0.1435 0.1651 0.1429 0.0024  0.0224  0.0012  48  GLY   A N   
1262 C  CA  A GLY   A 48  ? 0.1497 0.1687 0.2203 0.0033  -0.0063 0.0052  48  GLY   A CA  
1263 C  CA  B GLY   A 48  ? 0.1460 0.1577 0.1197 -0.0001 0.0256  0.0005  48  GLY   A CA  
1264 C  C   A GLY   A 48  ? 0.1455 0.1600 0.2222 -0.0112 -0.0006 0.0144  48  GLY   A C   
1265 C  C   B GLY   A 48  ? 0.1508 0.1542 0.1321 -0.0097 0.0156  0.0136  48  GLY   A C   
1266 O  O   A GLY   A 48  ? 0.1501 0.1589 0.2157 -0.0048 0.0050  0.0242  48  GLY   A O   
1267 O  O   B GLY   A 48  ? 0.1638 0.1531 0.1189 -0.0097 0.0283  0.0120  48  GLY   A O   
1274 N  N   A VAL   A 49  ? 0.1453 0.1515 0.2599 -0.0135 -0.0077 0.0130  49  VAL   A N   
1275 N  N   B VAL   A 49  ? 0.1470 0.1493 0.1582 -0.0078 -0.0042 0.0096  49  VAL   A N   
1276 C  CA  A VAL   A 49  ? 0.1533 0.1481 0.2623 -0.0195 -0.0104 0.0174  49  VAL   A CA  
1277 C  CA  B VAL   A 49  ? 0.1395 0.1542 0.1697 -0.0013 -0.0107 0.0095  49  VAL   A CA  
1278 C  C   A VAL   A 49  ? 0.1441 0.1423 0.2549 -0.0129 -0.0126 0.0161  49  VAL   A C   
1279 C  C   B VAL   A 49  ? 0.1388 0.1436 0.1761 0.0108  -0.0030 -0.0031 49  VAL   A C   
1280 O  O   A VAL   A 49  ? 0.1478 0.1519 0.2723 -0.0211 -0.0070 0.0139  49  VAL   A O   
1281 O  O   B VAL   A 49  ? 0.1354 0.1478 0.1863 0.0207  0.0010  0.0049  49  VAL   A O   
1282 C  CB  A VAL   A 49  ? 0.1745 0.1515 0.2861 -0.0115 -0.0087 0.0130  49  VAL   A CB  
1283 C  CB  B VAL   A 49  ? 0.1377 0.1555 0.1803 0.0032  -0.0130 0.0101  49  VAL   A CB  
1284 C  CG1 A VAL   A 49  ? 0.1855 0.1456 0.2874 -0.0076 -0.0004 0.0167  49  VAL   A CG1 
1285 C  CG1 B VAL   A 49  ? 0.1230 0.1530 0.1837 0.0188  -0.0196 0.0136  49  VAL   A CG1 
1286 C  CG2 A VAL   A 49  ? 0.1899 0.1594 0.3202 -0.0290 -0.0109 0.0023  49  VAL   A CG2 
1287 C  CG2 B VAL   A 49  ? 0.1486 0.1560 0.1974 -0.0001 -0.0050 0.0118  49  VAL   A CG2 
1306 N  N   A ALA   A 50  ? 0.1362 0.1373 0.2527 -0.0123 -0.0281 0.0244  50  ALA   A N   
1307 N  N   B ALA   A 50  ? 0.1436 0.1410 0.1800 0.0102  -0.0044 -0.0099 50  ALA   A N   
1308 C  CA  A ALA   A 50  ? 0.1383 0.1420 0.2605 -0.0147 -0.0103 0.0178  50  ALA   A CA  
1309 C  CA  B ALA   A 50  ? 0.1448 0.1335 0.1827 0.0010  -0.0021 -0.0167 50  ALA   A CA  
1310 C  C   A ALA   A 50  ? 0.1339 0.1440 0.2444 -0.0168 -0.0088 0.0131  50  ALA   A C   
1311 C  C   B ALA   A 50  ? 0.1456 0.1310 0.1810 0.0070  -0.0040 -0.0110 50  ALA   A C   
1312 O  O   A ALA   A 50  ? 0.1346 0.1479 0.2585 -0.0088 -0.0120 0.0181  50  ALA   A O   
1313 O  O   B ALA   A 50  ? 0.1516 0.1328 0.1847 0.0176  -0.0000 -0.0032 50  ALA   A O   
1314 C  CB  A ALA   A 50  ? 0.1346 0.1471 0.2795 -0.0142 -0.0058 0.0112  50  ALA   A CB  
1315 C  CB  B ALA   A 50  ? 0.1485 0.1294 0.1831 0.0007  0.0100  -0.0298 50  ALA   A CB  
1326 N  N   A GLY   A 51  ? 0.1381 0.1410 0.2423 -0.0020 -0.0170 0.0134  51  GLY   A N   
1327 N  N   B GLY   A 51  ? 0.1426 0.1299 0.1885 0.0090  -0.0171 -0.0106 51  GLY   A N   
1328 C  CA  A GLY   A 51  ? 0.1519 0.1346 0.2490 -0.0040 -0.0170 0.0084  51  GLY   A CA  
1329 C  CA  B GLY   A 51  ? 0.1505 0.1298 0.1799 0.0128  -0.0285 -0.0123 51  GLY   A CA  
1330 C  C   A GLY   A 51  ? 0.1377 0.1488 0.2456 -0.0000 -0.0080 -0.0068 51  GLY   A C   
1331 C  C   B GLY   A 51  ? 0.1408 0.1416 0.1818 0.0216  -0.0170 -0.0204 51  GLY   A C   
1332 O  O   A GLY   A 51  ? 0.1423 0.1645 0.2473 -0.0004 -0.0126 -0.0060 51  GLY   A O   
1333 O  O   B GLY   A 51  ? 0.1425 0.1502 0.1927 0.0212  -0.0089 -0.0154 51  GLY   A O   
1340 N  N   A ALA   A 52  ? 0.1423 0.1584 0.2445 -0.0039 -0.0019 -0.0006 52  ALA   A N   
1341 N  N   B ALA   A 52  ? 0.1493 0.1511 0.1837 0.0176  0.0021  -0.0298 52  ALA   A N   
1342 C  CA  A ALA   A 52  ? 0.1486 0.1661 0.2498 -0.0065 0.0002  0.0006  52  ALA   A CA  
1343 C  CA  B ALA   A 52  ? 0.1512 0.1600 0.1878 0.0070  0.0057  -0.0174 52  ALA   A CA  
1344 C  C   A ALA   A 52  ? 0.1400 0.1702 0.2376 -0.0132 0.0161  0.0105  52  ALA   A C   
1345 C  C   B ALA   A 52  ? 0.1428 0.1603 0.1771 -0.0066 0.0081  -0.0143 52  ALA   A C   
1346 O  O   A ALA   A 52  ? 0.1460 0.1763 0.2481 -0.0020 0.0108  0.0089  52  ALA   A O   
1347 O  O   B ALA   A 52  ? 0.1492 0.1632 0.1931 -0.0086 0.0022  -0.0222 52  ALA   A O   
1348 C  CB  A ALA   A 52  ? 0.1474 0.1807 0.2728 -0.0110 -0.0004 0.0074  52  ALA   A CB  
1349 C  CB  B ALA   A 52  ? 0.1503 0.1744 0.2052 0.0032  -0.0055 -0.0067 52  ALA   A CB  
1360 N  N   A LEU   A 53  ? 0.1366 0.1713 0.2352 -0.0126 0.0160  0.0208  53  LEU   A N   
1361 N  N   B LEU   A 53  ? 0.1381 0.1608 0.1638 -0.0044 0.0009  -0.0037 53  LEU   A N   
1362 C  CA  A LEU   A 53  ? 0.1526 0.1723 0.2318 -0.0161 0.0088  0.0185  53  LEU   A CA  
1363 C  CA  B LEU   A 53  ? 0.1462 0.1650 0.1538 -0.0025 -0.0129 0.0030  53  LEU   A CA  
1364 C  C   A LEU   A 53  ? 0.1506 0.1687 0.2282 0.0029  0.0061  0.0120  53  LEU   A C   
1365 C  C   B LEU   A 53  ? 0.1453 0.1657 0.1668 0.0036  -0.0051 0.0009  53  LEU   A C   
1366 O  O   A LEU   A 53  ? 0.1671 0.1727 0.2404 -0.0182 0.0031  -0.0052 53  LEU   A O   
1367 O  O   B LEU   A 53  ? 0.1480 0.1680 0.1747 -0.0053 -0.0060 -0.0109 53  LEU   A O   
1368 C  CB  A LEU   A 53  ? 0.1611 0.1726 0.2388 -0.0256 0.0141  0.0224  53  LEU   A CB  
1369 C  CB  B LEU   A 53  ? 0.1506 0.1644 0.1434 -0.0121 -0.0200 0.0089  53  LEU   A CB  
1370 C  CG  A LEU   A 53  ? 0.1759 0.1730 0.2476 -0.0234 0.0032  0.0112  53  LEU   A CG  
1371 C  CG  B LEU   A 53  ? 0.1591 0.1654 0.1556 -0.0120 -0.0191 0.0141  53  LEU   A CG  
1372 C  CD1 A LEU   A 53  ? 0.1670 0.1775 0.2484 -0.0020 -0.0090 0.0088  53  LEU   A CD1 
1373 C  CD1 B LEU   A 53  ? 0.1657 0.1655 0.1642 -0.0125 -0.0193 -0.0087 53  LEU   A CD1 
1374 C  CD2 A LEU   A 53  ? 0.2052 0.1892 0.2515 -0.0274 -0.0135 0.0048  53  LEU   A CD2 
1375 C  CD2 B LEU   A 53  ? 0.1689 0.1727 0.1622 -0.0157 -0.0228 0.0189  53  LEU   A CD2 
1398 N  N   A ASN   A 54  ? 0.1335 0.1572 0.2534 -0.0018 -0.0080 0.0114  54  ASN   A N   
1399 N  N   B ASN   A 54  ? 0.1391 0.1612 0.1876 -0.0005 -0.0131 -0.0049 54  ASN   A N   
1400 C  CA  A ASN   A 54  ? 0.1284 0.1497 0.2649 -0.0023 0.0008  0.0096  54  ASN   A CA  
1401 C  CA  B ASN   A 54  ? 0.1392 0.1609 0.2073 -0.0038 -0.0017 -0.0040 54  ASN   A CA  
1402 C  C   A ASN   A 54  ? 0.1372 0.1592 0.2640 -0.0043 0.0121  0.0048  54  ASN   A C   
1403 C  C   B ASN   A 54  ? 0.1453 0.1626 0.2254 -0.0099 0.0061  0.0017  54  ASN   A C   
1404 O  O   A ASN   A 54  ? 0.1431 0.1676 0.2675 -0.0031 -0.0051 0.0021  54  ASN   A O   
1405 O  O   B ASN   A 54  ? 0.1521 0.1621 0.2200 -0.0166 -0.0032 0.0121  54  ASN   A O   
1406 C  CB  A ASN   A 54  ? 0.1333 0.1456 0.2730 -0.0077 -0.0040 0.0046  54  ASN   A CB  
1407 C  CB  B ASN   A 54  ? 0.1415 0.1620 0.2051 0.0059  -0.0036 -0.0075 54  ASN   A CB  
1408 C  CG  A ASN   A 54  ? 0.1379 0.1481 0.2797 -0.0073 0.0015  0.0096  54  ASN   A CG  
1409 C  CG  B ASN   A 54  ? 0.1367 0.1623 0.1986 0.0076  -0.0003 -0.0157 54  ASN   A CG  
1410 O  OD1 A ASN   A 54  ? 0.1396 0.1448 0.2899 -0.0091 -0.0073 0.0363  54  ASN   A OD1 
1411 O  OD1 B ASN   A 54  ? 0.1250 0.1573 0.1887 0.0041  0.0009  -0.0300 54  ASN   A OD1 
1412 N  ND2 A ASN   A 54  ? 0.1397 0.1526 0.2851 -0.0144 -0.0075 0.0169  54  ASN   A ND2 
1413 N  ND2 B ASN   A 54  ? 0.1467 0.1677 0.2071 0.0029  -0.0116 0.0019  54  ASN   A ND2 
1426 N  N   . LYS   A 55  ? 0.1414 0.1581 0.2479 -0.0008 0.0014  -0.0038 55  LYS   A N   
1427 C  CA  . LYS   A 55  ? 0.1497 0.1754 0.2565 0.0029  -0.0108 -0.0126 55  LYS   A CA  
1428 C  C   . LYS   A 55  ? 0.1446 0.1826 0.2506 -0.0089 -0.0121 -0.0117 55  LYS   A C   
1429 O  O   . LYS   A 55  ? 0.1550 0.2010 0.2738 -0.0018 -0.0129 -0.0185 55  LYS   A O   
1430 C  CB  . LYS   A 55  ? 0.1548 0.1785 0.2774 0.0111  -0.0035 -0.0172 55  LYS   A CB  
1431 C  CG  . LYS   A 55  ? 0.1690 0.2001 0.2799 0.0229  -0.0222 -0.0253 55  LYS   A CG  
1432 C  CD  . LYS   A 55  ? 0.1827 0.2067 0.2816 0.0303  -0.0119 -0.0246 55  LYS   A CD  
1433 C  CE  . LYS   A 55  ? 0.2103 0.2391 0.2921 0.0438  -0.0230 -0.0148 55  LYS   A CE  
1434 N  NZ  . LYS   A 55  ? 0.2209 0.2487 0.3039 0.0461  -0.0218 -0.0092 55  LYS   A NZ  
1449 N  N   . ALA   A 56  ? 0.1520 0.1931 0.2427 -0.0152 0.0010  -0.0129 56  ALA   A N   
1450 C  CA  . ALA   A 56  ? 0.1636 0.2189 0.2413 -0.0193 0.0093  -0.0096 56  ALA   A CA  
1451 C  C   . ALA   A 56  ? 0.1695 0.2286 0.2256 -0.0143 0.0151  -0.0171 56  ALA   A C   
1452 O  O   . ALA   A 56  ? 0.1742 0.2559 0.2284 -0.0075 0.0225  -0.0102 56  ALA   A O   
1453 C  CB  . ALA   A 56  ? 0.1722 0.2337 0.2606 -0.0260 0.0111  -0.0003 56  ALA   A CB  
1459 N  N   . THR   A 57  ? 0.1524 0.1998 0.2184 -0.0131 0.0148  -0.0079 57  THR   A N   
1460 C  CA  . THR   A 57  ? 0.1620 0.1953 0.2242 -0.0178 0.0012  0.0009  57  THR   A CA  
1461 C  C   . THR   A 57  ? 0.1566 0.2019 0.2340 -0.0098 -0.0013 -0.0139 57  THR   A C   
1462 O  O   . THR   A 57  ? 0.1545 0.2067 0.2558 -0.0201 -0.0009 -0.0307 57  THR   A O   
1463 C  CB  . THR   A 57  ? 0.1577 0.1893 0.2298 -0.0136 0.0071  0.0074  57  THR   A CB  
1464 O  OG1 . THR   A 57  ? 0.1536 0.1864 0.2312 -0.0070 -0.0008 -0.0050 57  THR   A OG1 
1465 C  CG2 . THR   A 57  ? 0.1569 0.1968 0.2251 -0.0120 0.0003  0.0109  57  THR   A CG2 
1473 N  N   . ASN   A 58  ? 0.1587 0.1921 0.2530 -0.0118 0.0005  -0.0202 58  ASN   A N   
1474 C  CA  . ASN   A 58  ? 0.1807 0.1949 0.2741 -0.0117 0.0037  -0.0204 58  ASN   A CA  
1475 C  C   . ASN   A 58  ? 0.1563 0.1786 0.2611 -0.0046 -0.0035 -0.0230 58  ASN   A C   
1476 O  O   . ASN   A 58  ? 0.1610 0.1848 0.2693 -0.0104 -0.0015 -0.0280 58  ASN   A O   
1477 C  CB  . ASN   A 58  ? 0.2251 0.2138 0.2929 -0.0190 0.0278  -0.0225 58  ASN   A CB  
1478 C  CG  . ASN   A 58  ? 0.2652 0.2402 0.3446 -0.0136 0.0395  -0.0090 58  ASN   A CG  
1479 O  OD1 . ASN   A 58  ? 0.2877 0.2337 0.3896 0.0222  0.0620  -0.0128 58  ASN   A OD1 
1480 N  ND2 . ASN   A 58  ? 0.2789 0.2466 0.3562 -0.0068 0.0371  -0.0137 58  ASN   A ND2 
1487 N  N   . ASN   A 59  ? 0.1460 0.1691 0.2508 -0.0078 -0.0140 -0.0130 59  ASN   A N   
1488 C  CA  . ASN   A 59  ? 0.1463 0.1511 0.2395 -0.0053 -0.0051 -0.0000 59  ASN   A CA  
1489 C  C   . ASN   A 59  ? 0.1514 0.1544 0.2388 -0.0069 -0.0120 0.0107  59  ASN   A C   
1490 O  O   . ASN   A 59  ? 0.1491 0.1553 0.2362 -0.0078 -0.0022 0.0091  59  ASN   A O   
1491 C  CB  . ASN   A 59  ? 0.1539 0.1515 0.2462 0.0017  -0.0049 -0.0167 59  ASN   A CB  
1492 C  CG  . ASN   A 59  ? 0.1537 0.1565 0.2437 -0.0033 -0.0158 0.0029  59  ASN   A CG  
1493 O  OD1 . ASN   A 59  ? 0.1675 0.1616 0.2256 -0.0144 -0.0252 0.0054  59  ASN   A OD1 
1494 N  ND2 . ASN   A 59  ? 0.1621 0.1553 0.2584 -0.0140 -0.0167 0.0123  59  ASN   A ND2 
1501 N  N   . ALA   A 60  ? 0.1436 0.1643 0.2357 -0.0041 -0.0019 0.0106  60  ALA   A N   
1502 C  CA  . ALA   A 60  ? 0.1463 0.1591 0.2399 -0.0027 -0.0053 0.0102  60  ALA   A CA  
1503 C  C   . ALA   A 60  ? 0.1477 0.1499 0.2536 -0.0004 -0.0120 0.0050  60  ALA   A C   
1504 O  O   . ALA   A 60  ? 0.1400 0.1567 0.2713 -0.0056 -0.0126 -0.0054 60  ALA   A O   
1505 C  CB  . ALA   A 60  ? 0.1504 0.1711 0.2520 -0.0015 -0.0036 -0.0035 60  ALA   A CB  
1511 N  N   . MET   A 61  ? 0.1443 0.1489 0.2471 -0.0152 0.0022  0.0030  61  MET   A N   
1512 C  CA  . MET   A 61  ? 0.1392 0.1463 0.2536 -0.0131 -0.0053 0.0123  61  MET   A CA  
1513 C  C   . MET   A 61  ? 0.1343 0.1416 0.2597 -0.0123 -0.0110 0.0051  61  MET   A C   
1514 O  O   . MET   A 61  ? 0.1389 0.1448 0.2653 -0.0049 0.0026  0.0143  61  MET   A O   
1515 C  CB  . MET   A 61  ? 0.1522 0.1487 0.2433 -0.0123 -0.0006 0.0084  61  MET   A CB  
1516 C  CG  . MET   A 61  ? 0.1510 0.1551 0.2642 -0.0106 -0.0031 0.0098  61  MET   A CG  
1517 S  SD  . MET   A 61  ? 0.1511 0.1615 0.2576 -0.0137 -0.0001 -0.0055 61  MET   A SD  
1518 C  CE  . MET   A 61  ? 0.1759 0.1833 0.3233 -0.0110 0.0234  -0.0117 61  MET   A CE  
1528 N  N   . GLN   A 62  ? 0.1392 0.1407 0.2517 -0.0128 -0.0094 0.0062  62  GLN   A N   
1529 C  CA  . GLN   A 62  ? 0.1364 0.1387 0.2698 -0.0066 0.0052  0.0229  62  GLN   A CA  
1530 C  C   . GLN   A 62  ? 0.1415 0.1204 0.2712 -0.0025 -0.0002 0.0157  62  GLN   A C   
1531 O  O   . GLN   A 62  ? 0.1438 0.1452 0.2527 -0.0048 0.0037  0.0053  62  GLN   A O   
1532 C  CB  . GLN   A 62  ? 0.1311 0.1435 0.2674 -0.0008 0.0168  0.0199  62  GLN   A CB  
1533 C  CG  . GLN   A 62  ? 0.1358 0.1430 0.2599 -0.0089 0.0035  0.0367  62  GLN   A CG  
1534 C  CD  . GLN   A 62  ? 0.1493 0.1392 0.2627 -0.0045 0.0057  0.0187  62  GLN   A CD  
1535 O  OE1 . GLN   A 62  ? 0.1512 0.1575 0.2708 -0.0042 -0.0004 0.0080  62  GLN   A OE1 
1536 N  NE2 . GLN   A 62  ? 0.1528 0.1487 0.2614 0.0022  0.0041  0.0083  62  GLN   A NE2 
1545 N  N   . VAL   A 63  ? 0.1361 0.1388 0.2772 -0.0078 0.0064  -0.0100 63  VAL   A N   
1546 C  CA  . VAL   A 63  ? 0.1382 0.1480 0.2856 -0.0097 0.0035  0.0009  63  VAL   A CA  
1547 C  C   . VAL   A 63  ? 0.1299 0.1524 0.2685 -0.0181 -0.0159 -0.0053 63  VAL   A C   
1548 O  O   . VAL   A 63  ? 0.1315 0.1545 0.2830 -0.0162 -0.0079 -0.0013 63  VAL   A O   
1549 C  CB  . VAL   A 63  ? 0.1526 0.1647 0.3158 -0.0163 -0.0046 -0.0192 63  VAL   A CB  
1550 C  CG1 . VAL   A 63  ? 0.1623 0.1837 0.3365 -0.0166 -0.0112 -0.0492 63  VAL   A CG1 
1551 C  CG2 . VAL   A 63  ? 0.1583 0.1702 0.3158 -0.0144 0.0080  -0.0283 63  VAL   A CG2 
1561 N  N   . GLU   A 64  ? 0.1326 0.1612 0.2594 -0.0102 -0.0107 0.0047  64  GLU   A N   
1562 C  CA  . GLU   A 64  ? 0.1339 0.1565 0.2745 -0.0120 -0.0129 0.0073  64  GLU   A CA  
1563 C  C   . GLU   A 64  ? 0.1330 0.1513 0.2602 -0.0150 0.0011  0.0158  64  GLU   A C   
1564 O  O   . GLU   A 64  ? 0.1393 0.1525 0.2633 -0.0051 0.0021  0.0090  64  GLU   A O   
1565 C  CB  . GLU   A 64  ? 0.1411 0.1635 0.2857 -0.0083 -0.0020 0.0086  64  GLU   A CB  
1566 C  CG  . GLU   A 64  ? 0.1492 0.1727 0.2827 -0.0076 -0.0053 0.0160  64  GLU   A CG  
1567 C  CD  . GLU   A 64  ? 0.1590 0.1815 0.2904 -0.0213 0.0019  0.0100  64  GLU   A CD  
1568 O  OE1 . GLU   A 64  ? 0.1615 0.1959 0.2966 -0.0234 0.0064  0.0152  64  GLU   A OE1 
1569 O  OE2 . GLU   A 64  ? 0.1761 0.1798 0.2931 -0.0243 -0.0096 0.0120  64  GLU   A OE2 
1576 N  N   . SER   A 65  ? 0.1263 0.1539 0.2596 -0.0061 -0.0121 0.0130  65  SER   A N   
1577 C  CA  . SER   A 65  ? 0.1359 0.1463 0.2557 -0.0045 -0.0108 0.0132  65  SER   A CA  
1578 C  C   . SER   A 65  ? 0.1389 0.1468 0.2567 -0.0067 -0.0178 0.0192  65  SER   A C   
1579 O  O   . SER   A 65  ? 0.1467 0.1493 0.2758 -0.0013 0.0097  0.0103  65  SER   A O   
1580 C  CB  . SER   A 65  ? 0.1338 0.1418 0.2636 -0.0088 -0.0078 0.0224  65  SER   A CB  
1581 O  OG  . SER   A 65  ? 0.1349 0.1530 0.2609 -0.0091 -0.0060 0.0205  65  SER   A OG  
1587 N  N   . ASP   A 66  ? 0.1370 0.1429 0.2675 -0.0029 0.0118  0.0202  66  ASP   A N   
1588 C  CA  . ASP   A 66  ? 0.1522 0.1545 0.2766 0.0025  0.0058  0.0247  66  ASP   A CA  
1589 C  C   . ASP   A 66  ? 0.1465 0.1518 0.2767 -0.0097 0.0003  0.0282  66  ASP   A C   
1590 O  O   . ASP   A 66  ? 0.1557 0.1616 0.2893 -0.0057 0.0187  0.0204  66  ASP   A O   
1591 C  CB  . ASP   A 66  ? 0.1616 0.1582 0.3058 0.0108  0.0110  0.0430  66  ASP   A CB  
1592 C  CG  . ASP   A 66  ? 0.1901 0.1763 0.3126 0.0029  -0.0015 0.0631  66  ASP   A CG  
1593 O  OD1 . ASP   A 66  ? 0.1903 0.2032 0.2969 -0.0085 -0.0023 0.0618  66  ASP   A OD1 
1594 O  OD2 . ASP   A 66  ? 0.2069 0.1999 0.3811 0.0263  -0.0141 0.0321  66  ASP   A OD2 
1599 N  N   . ASP   A 67  ? 0.1436 0.1513 0.2843 -0.0072 0.0029  0.0281  67  ASP   A N   
1600 C  CA  . ASP   A 67  ? 0.1433 0.1714 0.2908 0.0065  0.0030  0.0335  67  ASP   A CA  
1601 C  C   . ASP   A 67  ? 0.1474 0.1683 0.2927 0.0030  0.0087  0.0364  67  ASP   A C   
1602 O  O   . ASP   A 67  ? 0.1457 0.1763 0.2890 -0.0011 0.0217  0.0333  67  ASP   A O   
1603 C  CB  . ASP   A 67  ? 0.1456 0.1811 0.3157 -0.0067 -0.0142 0.0359  67  ASP   A CB  
1604 C  CG  . ASP   A 67  ? 0.1475 0.1940 0.3587 -0.0181 -0.0253 0.0512  67  ASP   A CG  
1605 O  OD1 . ASP   A 67  ? 0.1587 0.2116 0.4100 -0.0194 -0.0271 0.0633  67  ASP   A OD1 
1606 O  OD2 . ASP   A 67  ? 0.1468 0.2023 0.3551 -0.0020 -0.0183 0.0459  67  ASP   A OD2 
1611 N  N   . TYR   A 68  ? 0.1465 0.1528 0.2921 0.0019  0.0106  0.0399  68  TYR   A N   
1612 C  CA  . TYR   A 68  ? 0.1611 0.1510 0.2680 0.0022  0.0251  0.0371  68  TYR   A CA  
1613 C  C   . TYR   A 68  ? 0.1479 0.1533 0.2723 -0.0009 0.0331  0.0246  68  TYR   A C   
1614 O  O   . TYR   A 68  ? 0.1537 0.1650 0.2874 0.0109  0.0232  0.0309  68  TYR   A O   
1615 C  CB  . TYR   A 68  ? 0.1636 0.1520 0.2859 0.0080  0.0439  0.0418  68  TYR   A CB  
1616 C  CG  . TYR   A 68  ? 0.1692 0.1662 0.3008 0.0073  0.0394  0.0355  68  TYR   A CG  
1617 C  CD1 . TYR   A 68  ? 0.1768 0.1759 0.3333 -0.0176 0.0394  0.0007  68  TYR   A CD1 
1618 C  CD2 . TYR   A 68  ? 0.1948 0.1732 0.3191 0.0158  0.0499  0.0403  68  TYR   A CD2 
1619 C  CE1 . TYR   A 68  ? 0.1778 0.1876 0.3519 -0.0149 0.0585  -0.0056 68  TYR   A CE1 
1620 C  CE2 . TYR   A 68  ? 0.1965 0.1687 0.3500 -0.0000 0.0677  0.0061  68  TYR   A CE2 
1621 C  CZ  . TYR   A 68  ? 0.1851 0.1763 0.3703 -0.0108 0.0595  -0.0133 68  TYR   A CZ  
1622 O  OH  . TYR   A 68  ? 0.2108 0.1795 0.4104 -0.0174 0.0324  -0.0417 68  TYR   A OH  
1632 N  N   . ILE   A 69  ? 0.1403 0.1487 0.2639 0.0032  0.0219  0.0247  69  ILE   A N   
1633 C  CA  . ILE   A 69  ? 0.1511 0.1471 0.2717 0.0072  0.0161  0.0174  69  ILE   A CA  
1634 C  C   . ILE   A 69  ? 0.1484 0.1528 0.2747 0.0056  0.0166  0.0309  69  ILE   A C   
1635 O  O   . ILE   A 69  ? 0.1531 0.1654 0.2729 0.0031  0.0166  0.0317  69  ILE   A O   
1636 C  CB  . ILE   A 69  ? 0.1547 0.1588 0.2651 0.0052  0.0073  0.0104  69  ILE   A CB  
1637 C  CG1 . ILE   A 69  ? 0.1622 0.1773 0.2865 0.0049  0.0078  -0.0027 69  ILE   A CG1 
1638 C  CG2 . ILE   A 69  ? 0.1752 0.1897 0.2626 0.0134  -0.0071 -0.0132 69  ILE   A CG2 
1639 C  CD1 . ILE   A 69  ? 0.1636 0.1915 0.3024 -0.0091 0.0156  -0.0029 69  ILE   A CD1 
1651 N  N   . ALA   A 70  ? 0.1600 0.1534 0.2920 -0.0057 0.0202  0.0373  70  ALA   A N   
1652 C  CA  . ALA   A 70  ? 0.1649 0.1659 0.3027 -0.0172 0.0383  0.0395  70  ALA   A CA  
1653 C  C   . ALA   A 70  ? 0.1654 0.1861 0.2978 -0.0136 0.0366  0.0335  70  ALA   A C   
1654 O  O   . ALA   A 70  ? 0.1833 0.2170 0.3138 0.0097  0.0452  0.0536  70  ALA   A O   
1655 C  CB  . ALA   A 70  ? 0.1712 0.1621 0.3197 -0.0190 0.0229  0.0403  70  ALA   A CB  
1661 N  N   . THR   A 71  ? 0.1530 0.1832 0.2840 -0.0070 0.0289  0.0333  71  THR   A N   
1662 C  CA  . THR   A 71  ? 0.1648 0.2085 0.3048 0.0092  0.0177  0.0369  71  THR   A CA  
1663 C  C   . THR   A 71  ? 0.1531 0.1926 0.3336 0.0126  0.0189  0.0329  71  THR   A C   
1664 O  O   . THR   A 71  ? 0.1581 0.2128 0.3940 0.0108  0.0290  -0.0020 71  THR   A O   
1665 C  CB  . THR   A 71  ? 0.1950 0.2422 0.3334 0.0178  -0.0091 0.0463  71  THR   A CB  
1666 O  OG1 . THR   A 71  ? 0.2207 0.2597 0.3604 0.0076  -0.0387 0.0321  71  THR   A OG1 
1667 C  CG2 . THR   A 71  ? 0.2038 0.2616 0.3532 0.0302  -0.0255 0.0685  71  THR   A CG2 
1675 N  N   . ASN   A 72  ? 0.1580 0.1743 0.3091 0.0134  0.0196  0.0351  72  ASN   A N   
1676 C  CA  . ASN   A 72  ? 0.1524 0.1724 0.3170 0.0180  0.0242  0.0311  72  ASN   A CA  
1677 C  C   . ASN   A 72  ? 0.1730 0.1778 0.2995 0.0130  0.0453  0.0275  72  ASN   A C   
1678 O  O   . ASN   A 72  ? 0.1902 0.1716 0.3296 0.0214  0.0445  0.0167  72  ASN   A O   
1679 C  CB  . ASN   A 72  ? 0.1782 0.1914 0.3011 0.0096  0.0277  0.0474  72  ASN   A CB  
1680 C  CG  . ASN   A 72  ? 0.1970 0.2010 0.3115 0.0179  0.0280  0.0396  72  ASN   A CG  
1681 O  OD1 . ASN   A 72  ? 0.2248 0.2377 0.3323 0.0320  0.0442  0.0408  72  ASN   A OD1 
1682 N  ND2 . ASN   A 72  ? 0.2187 0.1987 0.3227 0.0526  0.0148  0.0354  72  ASN   A ND2 
1689 N  N   . GLY   A 73  ? 0.1754 0.1733 0.2850 0.0021  0.0494  0.0208  73  GLY   A N   
1690 C  CA  . GLY   A 73  ? 0.1782 0.1677 0.2885 -0.0077 0.0473  0.0170  73  GLY   A CA  
1691 C  C   . GLY   A 73  ? 0.1837 0.1606 0.2736 0.0077  0.0488  0.0326  73  GLY   A C   
1692 O  O   . GLY   A 73  ? 0.1774 0.1644 0.2898 0.0183  0.0368  0.0366  73  GLY   A O   
1696 N  N   . PRO   A 74  ? 0.1923 0.1605 0.2671 -0.0089 0.0493  0.0166  74  PRO   A N   
1697 C  CA  . PRO   A 74  ? 0.1868 0.1616 0.2662 0.0011  0.0394  0.0180  74  PRO   A CA  
1698 C  C   . PRO   A 74  ? 0.1781 0.1422 0.2875 -0.0021 0.0199  0.0216  74  PRO   A C   
1699 O  O   . PRO   A 74  ? 0.1824 0.1472 0.3213 0.0084  0.0292  0.0122  74  PRO   A O   
1700 C  CB  . PRO   A 74  ? 0.2017 0.1973 0.2958 0.0047  0.0407  0.0319  74  PRO   A CB  
1701 C  CG  . PRO   A 74  ? 0.2370 0.2400 0.3294 -0.0191 0.0259  0.0227  74  PRO   A CG  
1702 C  CD  . PRO   A 74  ? 0.2151 0.2077 0.2852 -0.0126 0.0344  0.0149  74  PRO   A CD  
1710 N  N   . LEU   A 75  ? 0.1758 0.1420 0.2685 0.0012  0.0197  0.0110  75  LEU   A N   
1711 C  CA  . LEU   A 75  ? 0.1732 0.1460 0.2515 -0.0011 0.0123  0.0207  75  LEU   A CA  
1712 C  C   . LEU   A 75  ? 0.1814 0.1591 0.2577 0.0005  0.0043  0.0226  75  LEU   A C   
1713 O  O   . LEU   A 75  ? 0.2164 0.1763 0.2399 0.0067  0.0019  0.0151  75  LEU   A O   
1714 C  CB  . LEU   A 75  ? 0.1795 0.1507 0.2608 -0.0008 0.0227  0.0213  75  LEU   A CB  
1715 C  CG  . LEU   A 75  ? 0.1967 0.1836 0.2537 -0.0307 0.0259  0.0086  75  LEU   A CG  
1716 C  CD1 . LEU   A 75  ? 0.2162 0.2358 0.2576 -0.0308 0.0209  -0.0043 75  LEU   A CD1 
1717 C  CD2 . LEU   A 75  ? 0.2229 0.2266 0.2849 -0.0083 0.0159  0.0091  75  LEU   A CD2 
1729 N  N   . LYS   A 76  ? 0.1795 0.1579 0.2678 -0.0119 0.0031  0.0047  76  LYS   A N   
1730 C  CA  . LYS   A 76  ? 0.1726 0.1794 0.2884 -0.0139 0.0097  0.0016  76  LYS   A CA  
1731 C  C   . LYS   A 76  ? 0.1719 0.1641 0.2588 0.0010  0.0180  0.0092  76  LYS   A C   
1732 O  O   . LYS   A 76  ? 0.1796 0.1477 0.2664 -0.0004 0.0247  0.0247  76  LYS   A O   
1733 C  CB  . LYS   A 76  ? 0.1748 0.1999 0.3163 0.0017  0.0132  -0.0166 76  LYS   A CB  
1734 C  CG  . LYS   A 76  ? 0.1909 0.1952 0.3477 0.0098  0.0093  -0.0189 76  LYS   A CG  
1735 C  CD  . LYS   A 76  ? 0.1935 0.1953 0.3846 0.0130  0.0117  -0.0174 76  LYS   A CD  
1736 C  CE  . LYS   A 76  ? 0.2123 0.2142 0.4264 0.0043  0.0140  -0.0276 76  LYS   A CE  
1737 N  NZ  . LYS   A 76  ? 0.2161 0.2006 0.4549 -0.0196 0.0109  -0.0388 76  LYS   A NZ  
1751 N  N   . VAL   A 77  ? 0.1921 0.1707 0.2376 -0.0036 0.0201  0.0056  77  VAL   A N   
1752 C  CA  . VAL   A 77  ? 0.1918 0.1693 0.2454 0.0045  0.0159  0.0113  77  VAL   A CA  
1753 C  C   . VAL   A 77  ? 0.1779 0.1644 0.2590 0.0038  0.0180  0.0106  77  VAL   A C   
1754 O  O   . VAL   A 77  ? 0.1840 0.1760 0.2512 0.0024  0.0344  -0.0065 77  VAL   A O   
1755 C  CB  . VAL   A 77  ? 0.2139 0.1922 0.2461 -0.0059 0.0175  0.0092  77  VAL   A CB  
1756 C  CG1 . VAL   A 77  ? 0.2093 0.1956 0.2576 0.0035  0.0143  -0.0001 77  VAL   A CG1 
1757 C  CG2 . VAL   A 77  ? 0.2367 0.2113 0.2703 -0.0142 0.0010  0.0166  77  VAL   A CG2 
1767 N  N   . GLY   A 78  ? 0.1687 0.1555 0.2560 0.0048  0.0277  0.0137  78  GLY   A N   
1768 C  CA  . GLY   A 78  ? 0.1702 0.1645 0.2648 0.0003  0.0330  0.0146  78  GLY   A CA  
1769 C  C   . GLY   A 78  ? 0.1551 0.1577 0.2768 -0.0050 0.0263  0.0222  78  GLY   A C   
1770 O  O   . GLY   A 78  ? 0.1594 0.1615 0.2987 -0.0003 0.0156  0.0379  78  GLY   A O   
1774 N  N   . GLY   A 79  ? 0.1583 0.1514 0.2680 -0.0023 0.0208  0.0266  79  GLY   A N   
1775 C  CA  . GLY   A 79  ? 0.1605 0.1547 0.2697 -0.0065 0.0272  0.0261  79  GLY   A CA  
1776 C  C   . GLY   A 79  ? 0.1527 0.1424 0.2620 -0.0053 0.0188  0.0210  79  GLY   A C   
1777 O  O   . GLY   A 79  ? 0.1597 0.1444 0.2882 0.0152  0.0206  0.0153  79  GLY   A O   
1781 N  N   . SER   A 80  ? 0.1512 0.1637 0.2745 -0.0137 0.0248  0.0082  80  SER   A N   
1782 C  CA  . SER   A 80  ? 0.1426 0.1553 0.2717 -0.0076 0.0132  0.0157  80  SER   A CA  
1783 C  C   . SER   A 80  ? 0.1423 0.1525 0.2828 -0.0069 0.0181  0.0311  80  SER   A C   
1784 O  O   . SER   A 80  ? 0.1399 0.1719 0.2981 0.0077  0.0161  0.0112  80  SER   A O   
1785 C  CB  . SER   A 80  ? 0.1511 0.1486 0.2951 -0.0122 0.0182  0.0125  80  SER   A CB  
1786 O  OG  . SER   A 80  ? 0.1742 0.1557 0.3175 0.0012  0.0104  0.0306  80  SER   A OG  
1792 N  N   . CYS   A 81  ? 0.1395 0.1454 0.2903 0.0017  0.0088  0.0337  81  CYS   A N   
1793 C  CA  . CYS   A 81  ? 0.1393 0.1602 0.2800 -0.0096 -0.0011 0.0391  81  CYS   A CA  
1794 C  C   . CYS   A 81  ? 0.1375 0.1485 0.2831 -0.0112 0.0049  0.0484  81  CYS   A C   
1795 O  O   . CYS   A 81  ? 0.1367 0.1797 0.2932 -0.0009 0.0052  0.0482  81  CYS   A O   
1796 C  CB  . CYS   A 81  ? 0.1430 0.1729 0.2956 -0.0151 0.0034  0.0417  81  CYS   A CB  
1797 S  SG  . CYS   A 81  ? 0.1597 0.1535 0.2544 -0.0143 -0.0031 0.0200  81  CYS   A SG  
1803 N  N   . VAL   A 82  ? 0.1376 0.1605 0.2879 -0.0044 0.0057  0.0414  82  VAL   A N   
1804 C  CA  . VAL   A 82  ? 0.1477 0.1726 0.2771 -0.0097 0.0103  0.0514  82  VAL   A CA  
1805 C  C   . VAL   A 82  ? 0.1504 0.1721 0.2838 -0.0071 -0.0034 0.0498  82  VAL   A C   
1806 O  O   . VAL   A 82  ? 0.1515 0.1774 0.3034 -0.0044 0.0073  0.0272  82  VAL   A O   
1807 C  CB  . VAL   A 82  ? 0.1781 0.1904 0.2706 -0.0065 0.0029  0.0580  82  VAL   A CB  
1808 C  CG1 . VAL   A 82  ? 0.2018 0.1978 0.2821 0.0042  0.0089  0.0413  82  VAL   A CG1 
1809 C  CG2 . VAL   A 82  ? 0.1868 0.1912 0.3007 -0.0093 0.0048  0.0520  82  VAL   A CG2 
1819 N  N   . LEU   A 83  ? 0.1477 0.1720 0.2675 -0.0191 -0.0130 0.0314  83  LEU   A N   
1820 C  CA  . LEU   A 83  ? 0.1519 0.1733 0.2578 -0.0152 -0.0127 0.0245  83  LEU   A CA  
1821 C  C   . LEU   A 83  ? 0.1582 0.1775 0.2574 -0.0166 -0.0136 0.0251  83  LEU   A C   
1822 O  O   . LEU   A 83  ? 0.1614 0.1817 0.2714 -0.0190 -0.0062 0.0397  83  LEU   A O   
1823 C  CB  . LEU   A 83  ? 0.1669 0.1728 0.2513 -0.0161 -0.0233 0.0360  83  LEU   A CB  
1824 C  CG  . LEU   A 83  ? 0.1707 0.1823 0.2604 -0.0134 -0.0047 0.0232  83  LEU   A CG  
1825 C  CD1 . LEU   A 83  ? 0.1841 0.1836 0.2507 -0.0185 -0.0009 0.0311  83  LEU   A CD1 
1826 C  CD2 . LEU   A 83  ? 0.1677 0.1919 0.2812 -0.0120 0.0149  0.0305  83  LEU   A CD2 
1838 N  N   . SER   A 84  ? 0.1748 0.1863 0.2447 -0.0191 -0.0082 0.0477  84  SER   A N   
1839 C  CA  . SER   A 84  ? 0.1842 0.1938 0.2260 -0.0219 -0.0092 0.0342  84  SER   A CA  
1840 C  C   . SER   A 84  ? 0.1881 0.1952 0.2320 -0.0307 -0.0017 0.0357  84  SER   A C   
1841 O  O   . SER   A 84  ? 0.1762 0.1946 0.2249 -0.0240 -0.0041 0.0336  84  SER   A O   
1842 C  CB  . SER   A 84  ? 0.1970 0.2125 0.2371 -0.0213 -0.0221 0.0297  84  SER   A CB  
1843 O  OG  . SER   A 84  ? 0.2009 0.2351 0.2586 -0.0258 -0.0311 0.0172  84  SER   A OG  
1849 N  N   . GLY   A 85  ? 0.1987 0.2169 0.2149 -0.0336 0.0119  0.0324  85  GLY   A N   
1850 C  CA  . GLY   A 85  ? 0.2042 0.2221 0.2349 -0.0333 0.0127  0.0147  85  GLY   A CA  
1851 C  C   . GLY   A 85  ? 0.2025 0.2315 0.2348 -0.0379 0.0077  0.0140  85  GLY   A C   
1852 O  O   . GLY   A 85  ? 0.2041 0.2396 0.2534 -0.0480 0.0254  -0.0062 85  GLY   A O   
1856 N  N   . HIS   A 86  ? 0.2040 0.2224 0.2234 -0.0326 -0.0020 0.0246  86  HIS   A N   
1857 C  CA  . HIS   A 86  ? 0.2209 0.2418 0.2113 -0.0404 -0.0110 0.0228  86  HIS   A CA  
1858 C  C   . HIS   A 86  ? 0.2485 0.2561 0.2104 -0.0433 0.0028  0.0157  86  HIS   A C   
1859 O  O   . HIS   A 86  ? 0.2558 0.2737 0.2216 -0.0396 0.0156  0.0128  86  HIS   A O   
1860 C  CB  . HIS   A 86  ? 0.2175 0.2349 0.2174 -0.0292 -0.0116 0.0216  86  HIS   A CB  
1861 C  CG  . HIS   A 86  ? 0.2026 0.2193 0.2407 -0.0232 -0.0058 0.0261  86  HIS   A CG  
1862 N  ND1 . HIS   A 86  ? 0.2030 0.2089 0.2716 -0.0312 -0.0015 0.0186  86  HIS   A ND1 
1863 C  CD2 . HIS   A 86  ? 0.2030 0.2188 0.2276 -0.0100 -0.0002 0.0231  86  HIS   A CD2 
1864 C  CE1 . HIS   A 86  ? 0.1961 0.2084 0.2535 -0.0261 0.0132  0.0213  86  HIS   A CE1 
1865 N  NE2 . HIS   A 86  ? 0.1997 0.2014 0.2363 -0.0054 0.0134  0.0351  86  HIS   A NE2 
1873 N  N   . ASN   A 87  ? 0.2592 0.2624 0.2072 -0.0435 0.0239  -0.0038 87  ASN   A N   
1874 C  CA  . ASN   A 87  ? 0.2806 0.2692 0.2182 -0.0405 0.0403  -0.0033 87  ASN   A CA  
1875 C  C   . ASN   A 87  ? 0.2748 0.2840 0.2402 -0.0398 0.0456  0.0038  87  ASN   A C   
1876 O  O   . ASN   A 87  ? 0.3012 0.3023 0.2704 -0.0557 0.0746  0.0007  87  ASN   A O   
1877 C  CB  . ASN   A 87  ? 0.2995 0.2687 0.2307 -0.0316 0.0339  -0.0059 87  ASN   A CB  
1878 C  CG  . ASN   A 87  ? 0.3137 0.2734 0.2293 -0.0197 0.0447  0.0073  87  ASN   A CG  
1879 O  OD1 . ASN   A 87  ? 0.3252 0.2672 0.2352 -0.0025 0.0336  0.0136  87  ASN   A OD1 
1880 N  ND2 . ASN   A 87  ? 0.3211 0.2942 0.2483 -0.0205 0.0526  0.0087  87  ASN   A ND2 
1887 N  N   . LEU   A 88  ? 0.2463 0.2739 0.2461 -0.0385 0.0341  0.0112  88  LEU   A N   
1888 C  CA  . LEU   A 88  ? 0.2236 0.2548 0.2553 -0.0429 0.0401  0.0169  88  LEU   A CA  
1889 C  C   . LEU   A 88  ? 0.2185 0.2590 0.2653 -0.0431 0.0380  0.0291  88  LEU   A C   
1890 O  O   . LEU   A 88  ? 0.2126 0.2607 0.2824 -0.0359 0.0419  0.0435  88  LEU   A O   
1891 C  CB  . LEU   A 88  ? 0.2244 0.2524 0.2547 -0.0437 0.0147  0.0219  88  LEU   A CB  
1892 C  CG  . LEU   A 88  ? 0.2439 0.2605 0.2701 -0.0474 0.0067  0.0194  88  LEU   A CG  
1893 C  CD1 . LEU   A 88  ? 0.2547 0.2745 0.2718 -0.0472 0.0009  0.0089  88  LEU   A CD1 
1894 C  CD2 . LEU   A 88  ? 0.2609 0.2719 0.3089 -0.0378 0.0152  0.0170  88  LEU   A CD2 
1906 N  N   . ALA   A 89  ? 0.2200 0.2578 0.2524 -0.0395 0.0305  0.0223  89  ALA   A N   
1907 C  CA  . ALA   A 89  ? 0.2142 0.2614 0.2431 -0.0277 0.0078  0.0344  89  ALA   A CA  
1908 C  C   . ALA   A 89  ? 0.2157 0.2674 0.2422 -0.0290 -0.0075 0.0483  89  ALA   A C   
1909 O  O   . ALA   A 89  ? 0.2129 0.2613 0.2679 -0.0384 -0.0032 0.0267  89  ALA   A O   
1910 C  CB  . ALA   A 89  ? 0.2070 0.2595 0.2557 -0.0112 -0.0039 0.0224  89  ALA   A CB  
1916 N  N   . LYS   A 90  ? 0.2288 0.2777 0.2463 -0.0412 -0.0074 0.0530  90  LYS   A N   
1917 C  CA  . LYS   A 90  ? 0.2462 0.2941 0.2584 -0.0349 -0.0079 0.0480  90  LYS   A CA  
1918 C  C   . LYS   A 90  ? 0.2239 0.2741 0.2447 -0.0384 -0.0155 0.0374  90  LYS   A C   
1919 O  O   . LYS   A 90  ? 0.2226 0.2994 0.2667 -0.0410 -0.0308 0.0172  90  LYS   A O   
1920 C  CB  . LYS   A 90  ? 0.2777 0.3303 0.2963 -0.0345 -0.0067 0.0682  90  LYS   A CB  
1921 C  CG  . LYS   A 90  ? 0.3275 0.3704 0.3776 -0.0335 -0.0047 0.0796  90  LYS   A CG  
1922 C  CD  . LYS   A 90  ? 0.3591 0.3974 0.4502 -0.0337 0.0007  0.0963  90  LYS   A CD  
1923 C  CE  . LYS   A 90  ? 0.3873 0.4105 0.5235 -0.0322 0.0082  0.0969  90  LYS   A CE  
1924 N  NZ  . LYS   A 90  ? 0.4409 0.4409 0.5592 -0.0337 0.0183  0.0883  90  LYS   A NZ  
1938 N  N   . HIS   A 91  ? 0.2147 0.2379 0.2115 -0.0312 -0.0171 0.0460  91  HIS   A N   
1939 C  CA  . HIS   A 91  ? 0.2013 0.2139 0.2184 -0.0255 -0.0211 0.0451  91  HIS   A CA  
1940 C  C   . HIS   A 91  ? 0.1812 0.2047 0.2208 -0.0238 -0.0108 0.0497  91  HIS   A C   
1941 O  O   . HIS   A 91  ? 0.1678 0.2170 0.2468 -0.0227 -0.0031 0.0470  91  HIS   A O   
1942 C  CB  . HIS   A 91  ? 0.2155 0.2335 0.2557 -0.0047 -0.0353 0.0392  91  HIS   A CB  
1943 C  CG  . HIS   A 91  ? 0.2635 0.2873 0.3016 0.0044  -0.0565 0.0267  91  HIS   A CG  
1944 N  ND1 . HIS   A 91  ? 0.2763 0.3160 0.3278 0.0142  -0.0719 0.0069  91  HIS   A ND1 
1945 C  CD2 . HIS   A 91  ? 0.2867 0.3145 0.3192 0.0102  -0.0659 0.0305  91  HIS   A CD2 
1946 C  CE1 . HIS   A 91  ? 0.2865 0.3262 0.3367 0.0189  -0.0765 0.0217  91  HIS   A CE1 
1947 N  NE2 . HIS   A 91  ? 0.2967 0.3281 0.3348 0.0218  -0.0792 0.0230  91  HIS   A NE2 
1955 N  N   . CYS   A 92  ? 0.1761 0.1940 0.2299 -0.0189 -0.0096 0.0487  92  CYS   A N   
1956 C  CA  . CYS   A 92  ? 0.1663 0.1829 0.2389 -0.0165 0.0086  0.0447  92  CYS   A CA  
1957 C  C   . CYS   A 92  ? 0.1503 0.1775 0.2585 -0.0162 0.0044  0.0393  92  CYS   A C   
1958 O  O   . CYS   A 92  ? 0.1497 0.1739 0.2704 -0.0200 -0.0033 0.0322  92  CYS   A O   
1959 C  CB  . CYS   A 92  ? 0.1667 0.1792 0.2556 -0.0137 0.0040  0.0307  92  CYS   A CB  
1960 S  SG  . CYS   A 92  ? 0.1598 0.1625 0.2300 -0.0178 -0.0023 0.0227  92  CYS   A SG  
1966 N  N   . LEU   A 93  ? 0.1471 0.1525 0.2692 -0.0192 0.0165  0.0356  93  LEU   A N   
1967 C  CA  . LEU   A 93  ? 0.1355 0.1526 0.2784 -0.0122 0.0023  0.0369  93  LEU   A CA  
1968 C  C   . LEU   A 93  ? 0.1373 0.1353 0.2882 -0.0102 0.0052  0.0299  93  LEU   A C   
1969 O  O   . LEU   A 93  ? 0.1348 0.1504 0.2716 -0.0105 0.0052  0.0177  93  LEU   A O   
1970 C  CB  . LEU   A 93  ? 0.1421 0.1546 0.2797 -0.0109 -0.0074 0.0449  93  LEU   A CB  
1971 C  CG  . LEU   A 93  ? 0.1505 0.1557 0.2831 -0.0071 0.0055  0.0415  93  LEU   A CG  
1972 C  CD1 . LEU   A 93  ? 0.1623 0.1549 0.3125 -0.0109 0.0081  0.0309  93  LEU   A CD1 
1973 C  CD2 . LEU   A 93  ? 0.1648 0.1500 0.2878 -0.0071 0.0014  0.0332  93  LEU   A CD2 
1985 N  N   . HIS   A 94  ? 0.1318 0.1388 0.2628 -0.0058 0.0024  0.0353  94  HIS   A N   
1986 C  CA  . HIS   A 94  ? 0.1349 0.1391 0.2632 -0.0069 -0.0065 0.0335  94  HIS   A CA  
1987 C  C   . HIS   A 94  ? 0.1330 0.1311 0.2687 -0.0073 0.0007  0.0175  94  HIS   A C   
1988 O  O   . HIS   A 94  ? 0.1344 0.1520 0.2993 -0.0021 0.0005  0.0047  94  HIS   A O   
1989 C  CB  . HIS   A 94  ? 0.1295 0.1366 0.2767 -0.0090 -0.0114 0.0295  94  HIS   A CB  
1990 C  CG  . HIS   A 94  ? 0.1379 0.1348 0.2648 -0.0099 -0.0035 0.0310  94  HIS   A CG  
1991 N  ND1 . HIS   A 94  ? 0.1351 0.1323 0.2717 -0.0082 0.0096  0.0277  94  HIS   A ND1 
1992 C  CD2 . HIS   A 94  ? 0.1479 0.1504 0.2696 -0.0155 -0.0018 0.0246  94  HIS   A CD2 
1993 C  CE1 . HIS   A 94  ? 0.1429 0.1408 0.2668 -0.0109 -0.0072 0.0260  94  HIS   A CE1 
1994 N  NE2 . HIS   A 94  ? 0.1460 0.1432 0.2417 -0.0137 -0.0086 0.0144  94  HIS   A NE2 
2002 N  N   . VAL   A 95  ? 0.1304 0.1304 0.2470 -0.0056 0.0100  0.0145  95  VAL   A N   
2003 C  CA  . VAL   A 95  ? 0.1395 0.1380 0.2478 -0.0117 0.0059  0.0178  95  VAL   A CA  
2004 C  C   . VAL   A 95  ? 0.1381 0.1405 0.2343 -0.0178 0.0120  0.0171  95  VAL   A C   
2005 O  O   . VAL   A 95  ? 0.1437 0.1481 0.2442 0.0091  0.0116  0.0123  95  VAL   A O   
2006 C  CB  . VAL   A 95  ? 0.1414 0.1393 0.2671 -0.0165 0.0080  0.0223  95  VAL   A CB  
2007 C  CG1 . VAL   A 95  ? 0.1569 0.1471 0.2673 -0.0183 0.0010  0.0101  95  VAL   A CG1 
2008 C  CG2 . VAL   A 95  ? 0.1427 0.1471 0.2799 -0.0173 0.0091  0.0351  95  VAL   A CG2 
2018 N  N   A VAL   A 96  ? 0.1340 0.1374 0.2384 -0.0083 0.0028  0.0165  96  VAL   A N   
2019 N  N   B VAL   A 96  ? 0.1444 0.1498 0.2069 -0.0113 0.0044  0.0213  96  VAL   A N   
2020 C  CA  A VAL   A 96  ? 0.1434 0.1391 0.2466 -0.0064 0.0036  0.0219  96  VAL   A CA  
2021 C  CA  B VAL   A 96  ? 0.1573 0.1624 0.1924 -0.0122 0.0013  0.0227  96  VAL   A CA  
2022 C  C   A VAL   A 96  ? 0.1439 0.1437 0.2667 -0.0077 0.0120  0.0227  96  VAL   A C   
2023 C  C   B VAL   A 96  ? 0.1621 0.1647 0.1971 -0.0040 0.0081  0.0211  96  VAL   A C   
2024 O  O   A VAL   A 96  ? 0.1513 0.1469 0.2922 -0.0099 0.0224  0.0023  96  VAL   A O   
2025 O  O   B VAL   A 96  ? 0.1643 0.1611 0.1955 -0.0030 0.0160  0.0112  96  VAL   A O   
2026 C  CB  A VAL   A 96  ? 0.1500 0.1413 0.2502 -0.0018 0.0203  0.0168  96  VAL   A CB  
2027 C  CB  B VAL   A 96  ? 0.1605 0.1648 0.1887 -0.0163 0.0083  0.0172  96  VAL   A CB  
2028 C  CG1 A VAL   A 96  ? 0.1575 0.1529 0.2388 -0.0003 0.0155  0.0197  96  VAL   A CG1 
2029 C  CG1 B VAL   A 96  ? 0.1662 0.1699 0.1822 -0.0130 0.0064  0.0165  96  VAL   A CG1 
2030 C  CG2 A VAL   A 96  ? 0.1469 0.1338 0.2593 0.0017  0.0306  0.0106  96  VAL   A CG2 
2031 C  CG2 B VAL   A 96  ? 0.1546 0.1654 0.1878 -0.0186 0.0072  0.0140  96  VAL   A CG2 
2050 N  N   A GLY   A 97  ? 0.1436 0.1379 0.2555 -0.0107 0.0099  0.0207  97  GLY   A N   
2051 N  N   B GLY   A 97  ? 0.1672 0.1673 0.2072 -0.0041 0.0033  0.0187  97  GLY   A N   
2052 C  CA  A GLY   A 97  ? 0.1457 0.1588 0.2469 -0.0089 0.0125  0.0119  97  GLY   A CA  
2053 C  CA  B GLY   A 97  ? 0.1785 0.1751 0.2103 0.0004  0.0044  0.0163  97  GLY   A CA  
2054 C  C   A GLY   A 97  ? 0.1477 0.1961 0.2281 -0.0179 0.0115  0.0146  97  GLY   A C   
2055 C  C   B GLY   A 97  ? 0.1857 0.1882 0.2080 0.0006  0.0039  0.0180  97  GLY   A C   
2056 O  O   A GLY   A 97  ? 0.1557 0.1915 0.2454 -0.0248 0.0082  0.0186  97  GLY   A O   
2057 O  O   B GLY   A 97  ? 0.1884 0.1864 0.2178 0.0033  0.0038  0.0148  97  GLY   A O   
2064 N  N   A PRO   A 98  ? 0.1570 0.2097 0.2039 -0.0051 -0.0028 0.0126  98  PRO   A N   
2065 N  N   B PRO   A 98  ? 0.1914 0.1838 0.2012 0.0053  0.0007  0.0269  98  PRO   A N   
2066 C  CA  A PRO   A 98  ? 0.1661 0.2327 0.1964 -0.0195 -0.0019 0.0087  98  PRO   A CA  
2067 C  CA  B PRO   A 98  ? 0.2010 0.1935 0.2060 -0.0027 -0.0001 0.0221  98  PRO   A CA  
2068 C  C   A PRO   A 98  ? 0.1718 0.2381 0.2019 -0.0325 -0.0095 0.0127  98  PRO   A C   
2069 C  C   B PRO   A 98  ? 0.2217 0.1894 0.2036 -0.0062 0.0022  0.0244  98  PRO   A C   
2070 O  O   A PRO   A 98  ? 0.1628 0.2040 0.2250 -0.0236 0.0029  0.0061  98  PRO   A O   
2071 O  O   B PRO   A 98  ? 0.2175 0.1821 0.2220 -0.0085 0.0164  0.0164  98  PRO   A O   
2072 C  CB  A PRO   A 98  ? 0.1742 0.2403 0.1932 0.0057  -0.0098 -0.0080 98  PRO   A CB  
2073 C  CB  B PRO   A 98  ? 0.2002 0.1993 0.2120 0.0040  -0.0060 0.0194  98  PRO   A CB  
2074 C  CG  A PRO   A 98  ? 0.1685 0.2312 0.2036 0.0109  -0.0158 -0.0102 98  PRO   A CG  
2075 C  CG  B PRO   A 98  ? 0.2054 0.1964 0.2044 0.0062  -0.0097 0.0233  98  PRO   A CG  
2076 C  CD  A PRO   A 98  ? 0.1627 0.2179 0.2017 0.0028  -0.0163 -0.0047 98  PRO   A CD  
2077 C  CD  B PRO   A 98  ? 0.1949 0.1831 0.1929 0.0082  -0.0104 0.0290  98  PRO   A CD  
2092 N  N   A ASN   A 99  ? 0.1783 0.2789 0.1870 -0.0383 -0.0110 0.0438  99  ASN   A N   
2093 N  N   B ASN   A 99  ? 0.2449 0.1875 0.1894 0.0077  -0.0048 0.0388  99  ASN   A N   
2094 C  CA  A ASN   A 99  ? 0.1921 0.2978 0.1966 -0.0399 -0.0109 0.0525  99  ASN   A CA  
2095 C  CA  B ASN   A 99  ? 0.2699 0.1808 0.1872 0.0216  -0.0141 0.0346  99  ASN   A CA  
2096 C  C   A ASN   A 99  ? 0.2052 0.3225 0.1949 -0.0392 -0.0022 0.0579  99  ASN   A C   
2097 C  C   B ASN   A 99  ? 0.2836 0.1707 0.1923 0.0370  -0.0163 0.0226  99  ASN   A C   
2098 O  O   A ASN   A 99  ? 0.2146 0.3315 0.1963 -0.0161 -0.0053 0.0538  99  ASN   A O   
2099 O  O   B ASN   A 99  ? 0.2841 0.1399 0.1822 0.0539  -0.0161 0.0207  99  ASN   A O   
2100 C  CB  A ASN   A 99  ? 0.1971 0.2891 0.2176 -0.0390 -0.0196 0.0512  99  ASN   A CB  
2101 C  CB  B ASN   A 99  ? 0.2804 0.1880 0.1980 0.0245  -0.0234 0.0323  99  ASN   A CB  
2102 C  CG  A ASN   A 99  ? 0.2014 0.2792 0.2391 -0.0350 -0.0262 0.0442  99  ASN   A CG  
2103 C  CG  B ASN   A 99  ? 0.2845 0.1936 0.2071 0.0261  -0.0192 0.0200  99  ASN   A CG  
2104 O  OD1 A ASN   A 99  ? 0.1925 0.2818 0.2227 -0.0223 -0.0154 0.0466  99  ASN   A OD1 
2105 O  OD1 B ASN   A 99  ? 0.2894 0.2018 0.1933 0.0197  -0.0084 0.0255  99  ASN   A OD1 
2106 N  ND2 A ASN   A 99  ? 0.2108 0.2550 0.2648 -0.0441 -0.0450 0.0581  99  ASN   A ND2 
2107 N  ND2 B ASN   A 99  ? 0.2809 0.1911 0.2151 0.0388  -0.0250 0.0046  99  ASN   A ND2 
2120 N  N   A VAL   A 100 ? 0.2233 0.3396 0.1970 -0.0571 -0.0129 0.0586  100 VAL   A N   
2121 N  N   B VAL   A 100 ? 0.2982 0.2066 0.2081 0.0325  -0.0265 0.0242  100 VAL   A N   
2122 C  CA  A VAL   A 100 ? 0.2545 0.3622 0.2288 -0.0599 -0.0228 0.0617  100 VAL   A CA  
2123 C  CA  B VAL   A 100 ? 0.3133 0.2262 0.2318 0.0291  -0.0315 0.0049  100 VAL   A CA  
2124 C  C   A VAL   A 100 ? 0.2734 0.3826 0.2469 -0.0729 -0.0206 0.0857  100 VAL   A C   
2125 C  C   B VAL   A 100 ? 0.3182 0.2188 0.2375 0.0443  -0.0340 -0.0055 100 VAL   A C   
2126 O  O   A VAL   A 100 ? 0.2828 0.3933 0.2656 -0.0679 -0.0114 0.0900  100 VAL   A O   
2127 O  O   B VAL   A 100 ? 0.3183 0.2117 0.2419 0.0371  -0.0454 -0.0176 100 VAL   A O   
2128 C  CB  A VAL   A 100 ? 0.2725 0.3672 0.2546 -0.0528 -0.0261 0.0516  100 VAL   A CB  
2129 C  CB  B VAL   A 100 ? 0.3213 0.2483 0.2467 0.0202  -0.0333 -0.0014 100 VAL   A CB  
2130 C  CG1 A VAL   A 100 ? 0.2740 0.3705 0.2694 -0.0518 -0.0261 0.0456  100 VAL   A CG1 
2131 C  CG1 B VAL   A 100 ? 0.3231 0.2464 0.2534 0.0141  -0.0332 -0.0026 100 VAL   A CG1 
2132 C  CG2 A VAL   A 100 ? 0.2862 0.3703 0.2557 -0.0501 -0.0209 0.0520  100 VAL   A CG2 
2133 C  CG2 B VAL   A 100 ? 0.3223 0.2626 0.2465 0.0206  -0.0347 -0.0041 100 VAL   A CG2 
2152 N  N   A ASN   A 101 ? 0.2844 0.3874 0.2586 -0.0889 -0.0307 0.1086  101 ASN   A N   
2153 N  N   B ASN   A 101 ? 0.3288 0.2247 0.2507 0.0506  -0.0272 -0.0070 101 ASN   A N   
2154 C  CA  A ASN   A 101 ? 0.3156 0.3897 0.2727 -0.0962 -0.0366 0.1199  101 ASN   A CA  
2155 C  CA  B ASN   A 101 ? 0.3388 0.2454 0.2620 0.0573  -0.0223 0.0016  101 ASN   A CA  
2156 C  C   A ASN   A 101 ? 0.3479 0.4222 0.3084 -0.0943 -0.0144 0.1345  101 ASN   A C   
2157 C  C   B ASN   A 101 ? 0.3532 0.2736 0.2851 0.0480  -0.0142 0.0064  101 ASN   A C   
2158 O  O   A ASN   A 101 ? 0.3636 0.4229 0.3330 -0.0916 -0.0216 0.1291  101 ASN   A O   
2159 O  O   B ASN   A 101 ? 0.3512 0.2728 0.2858 0.0469  -0.0180 0.0142  101 ASN   A O   
2160 C  CB  A ASN   A 101 ? 0.3155 0.3599 0.2508 -0.1010 -0.0649 0.1062  101 ASN   A CB  
2161 C  CB  B ASN   A 101 ? 0.3337 0.2467 0.2680 0.0666  -0.0292 -0.0017 101 ASN   A CB  
2162 C  CG  A ASN   A 101 ? 0.3197 0.3317 0.2417 -0.1000 -0.0750 0.0824  101 ASN   A CG  
2163 C  CG  B ASN   A 101 ? 0.3291 0.2618 0.2800 0.0640  -0.0346 -0.0020 101 ASN   A CG  
2164 O  OD1 A ASN   A 101 ? 0.3097 0.3243 0.2577 -0.0828 -0.0854 0.0664  101 ASN   A OD1 
2165 O  OD1 B ASN   A 101 ? 0.3398 0.2751 0.2966 0.0528  -0.0324 -0.0010 101 ASN   A OD1 
2166 N  ND2 A ASN   A 101 ? 0.3310 0.3208 0.2472 -0.1066 -0.0777 0.0799  101 ASN   A ND2 
2167 N  ND2 B ASN   A 101 ? 0.3178 0.2648 0.2810 0.0720  -0.0318 -0.0030 101 ASN   A ND2 
2180 N  N   A LYS   A 102 ? 0.3586 0.4579 0.3325 -0.0944 -0.0001 0.1351  102 LYS   A N   
2181 N  N   B LYS   A 102 ? 0.3679 0.2967 0.3131 0.0443  -0.0004 0.0060  102 LYS   A N   
2182 C  CA  A LYS   A 102 ? 0.3754 0.4890 0.3468 -0.0865 -0.0028 0.1211  102 LYS   A CA  
2183 C  CA  B LYS   A 102 ? 0.3827 0.3303 0.3314 0.0336  0.0085  0.0000  102 LYS   A CA  
2184 C  C   A LYS   A 102 ? 0.3816 0.5106 0.3372 -0.0728 -0.0068 0.1064  102 LYS   A C   
2185 C  C   B LYS   A 102 ? 0.3818 0.3423 0.3230 0.0289  0.0126  0.0088  102 LYS   A C   
2186 O  O   A LYS   A 102 ? 0.3820 0.5192 0.3413 -0.0675 -0.0145 0.1048  102 LYS   A O   
2187 O  O   B LYS   A 102 ? 0.3825 0.3432 0.3214 0.0305  0.0204  0.0148  102 LYS   A O   
2188 C  CB  A LYS   A 102 ? 0.3884 0.4954 0.3684 -0.0899 -0.0020 0.1182  102 LYS   A CB  
2189 C  CB  B LYS   A 102 ? 0.3949 0.3487 0.3676 0.0290  0.0137  -0.0136 102 LYS   A CB  
2190 C  CG  A LYS   A 102 ? 0.3982 0.4988 0.3964 -0.0921 -0.0047 0.1093  102 LYS   A CG  
2191 C  CG  B LYS   A 102 ? 0.4040 0.3645 0.4014 0.0263  0.0195  -0.0253 102 LYS   A CG  
2192 C  CD  A LYS   A 102 ? 0.4069 0.5022 0.4269 -0.0950 -0.0116 0.0969  102 LYS   A CD  
2193 C  CD  B LYS   A 102 ? 0.4110 0.3784 0.4323 0.0216  0.0269  -0.0286 102 LYS   A CD  
2194 C  CE  A LYS   A 102 ? 0.4132 0.5029 0.4438 -0.0996 -0.0171 0.0896  102 LYS   A CE  
2195 C  CE  B LYS   A 102 ? 0.4155 0.3881 0.4589 0.0163  0.0309  -0.0320 102 LYS   A CE  
2196 N  NZ  A LYS   A 102 ? 0.4175 0.5040 0.4592 -0.1046 -0.0126 0.0844  102 LYS   A NZ  
2197 N  NZ  B LYS   A 102 ? 0.4190 0.3946 0.4705 0.0130  0.0280  -0.0346 102 LYS   A NZ  
2224 N  N   A GLY   A 103 ? 0.3826 0.5247 0.3370 -0.0621 -0.0100 0.0809  103 GLY   A N   
2225 N  N   B GLY   A 103 ? 0.3792 0.3544 0.3217 0.0282  0.0094  0.0035  103 GLY   A N   
2226 C  CA  A GLY   A 103 ? 0.3842 0.5325 0.3357 -0.0513 -0.0075 0.0636  103 GLY   A CA  
2227 C  CA  B GLY   A 103 ? 0.3756 0.3595 0.3278 0.0319  0.0049  0.0086  103 GLY   A CA  
2228 C  C   A GLY   A 103 ? 0.3769 0.5373 0.3289 -0.0421 -0.0020 0.0469  103 GLY   A C   
2229 C  C   B GLY   A 103 ? 0.3736 0.3656 0.3336 0.0339  -0.0041 0.0121  103 GLY   A C   
2230 O  O   A GLY   A 103 ? 0.3818 0.5409 0.3536 -0.0305 -0.0019 0.0382  103 GLY   A O   
2231 O  O   B GLY   A 103 ? 0.3786 0.3691 0.3454 0.0367  -0.0042 0.0105  103 GLY   A O   
2238 N  N   A GLU   A 104 ? 0.3581 0.5337 0.2880 -0.0522 0.0085  0.0449  104 GLU   A N   
2239 N  N   B GLU   A 104 ? 0.3649 0.3635 0.3292 0.0326  -0.0136 0.0237  104 GLU   A N   
2240 C  CA  A GLU   A 104 ? 0.3345 0.5232 0.2516 -0.0690 0.0155  0.0349  104 GLU   A CA  
2241 C  CA  B GLU   A 104 ? 0.3583 0.3628 0.3239 0.0224  -0.0192 0.0235  104 GLU   A CA  
2242 C  C   A GLU   A 104 ? 0.3320 0.5259 0.2559 -0.0702 0.0181  0.0060  104 GLU   A C   
2243 C  C   B GLU   A 104 ? 0.3459 0.3657 0.3314 0.0218  -0.0250 0.0137  104 GLU   A C   
2244 O  O   A GLU   A 104 ? 0.3243 0.5208 0.2390 -0.0755 0.0209  -0.0018 104 GLU   A O   
2245 O  O   B GLU   A 104 ? 0.3458 0.3596 0.3291 0.0178  -0.0279 0.0154  104 GLU   A O   
2246 C  CB  A GLU   A 104 ? 0.3022 0.5066 0.2197 -0.0831 0.0163  0.0540  104 GLU   A CB  
2247 C  CB  B GLU   A 104 ? 0.3646 0.3596 0.3228 0.0142  -0.0153 0.0279  104 GLU   A CB  
2248 C  CG  A GLU   A 104 ? 0.2788 0.4906 0.2156 -0.0848 0.0048  0.0720  104 GLU   A CG  
2249 C  CG  B GLU   A 104 ? 0.3700 0.3603 0.3234 0.0065  -0.0127 0.0276  104 GLU   A CG  
2250 C  CD  A GLU   A 104 ? 0.2544 0.4768 0.1994 -0.0844 -0.0048 0.0865  104 GLU   A CD  
2251 C  CD  B GLU   A 104 ? 0.3699 0.3542 0.3235 -0.0002 -0.0130 0.0315  104 GLU   A CD  
2252 O  OE1 A GLU   A 104 ? 0.2403 0.4722 0.1874 -0.0835 -0.0111 0.0956  104 GLU   A OE1 
2253 O  OE1 B GLU   A 104 ? 0.3705 0.3526 0.3289 -0.0028 -0.0066 0.0312  104 GLU   A OE1 
2254 O  OE2 A GLU   A 104 ? 0.2562 0.4694 0.2260 -0.0850 0.0052  0.1037  104 GLU   A OE2 
2255 O  OE2 B GLU   A 104 ? 0.3706 0.3533 0.3186 -0.0063 -0.0209 0.0271  104 GLU   A OE2 
2268 N  N   A ASP   A 105 ? 0.3355 0.5329 0.2860 -0.0675 0.0183  -0.0180 105 ASP   A N   
2269 N  N   B ASP   A 105 ? 0.3381 0.3732 0.3489 0.0210  -0.0253 0.0005  105 ASP   A N   
2270 C  CA  A ASP   A 105 ? 0.3374 0.5357 0.3221 -0.0606 0.0218  -0.0509 105 ASP   A CA  
2271 C  CA  B ASP   A 105 ? 0.3298 0.3791 0.3723 0.0196  -0.0245 -0.0179 105 ASP   A CA  
2272 C  C   A ASP   A 105 ? 0.3024 0.5179 0.2919 -0.0739 0.0191  -0.0729 105 ASP   A C   
2273 C  C   B ASP   A 105 ? 0.3270 0.3770 0.3578 0.0039  -0.0241 -0.0315 105 ASP   A C   
2274 O  O   A ASP   A 105 ? 0.2822 0.5178 0.2492 -0.0795 0.0219  -0.0850 105 ASP   A O   
2275 O  O   B ASP   A 105 ? 0.3233 0.3876 0.3516 -0.0002 -0.0246 -0.0334 105 ASP   A O   
2276 C  CB  A ASP   A 105 ? 0.3670 0.5511 0.3872 -0.0438 0.0260  -0.0585 105 ASP   A CB  
2277 C  CB  B ASP   A 105 ? 0.3267 0.3820 0.4055 0.0291  -0.0234 -0.0261 105 ASP   A CB  
2278 C  CG  A ASP   A 105 ? 0.3906 0.5616 0.4406 -0.0308 0.0292  -0.0639 105 ASP   A CG  
2279 C  CG  B ASP   A 105 ? 0.3238 0.3816 0.4285 0.0351  -0.0229 -0.0354 105 ASP   A CG  
2280 O  OD1 A ASP   A 105 ? 0.3948 0.5679 0.4502 -0.0345 0.0310  -0.0704 105 ASP   A OD1 
2281 O  OD1 B ASP   A 105 ? 0.3189 0.3745 0.4448 0.0333  -0.0244 -0.0393 105 ASP   A OD1 
2282 O  OD2 A ASP   A 105 ? 0.4064 0.5630 0.4677 -0.0223 0.0340  -0.0603 105 ASP   A OD2 
2283 O  OD2 B ASP   A 105 ? 0.3209 0.3834 0.4415 0.0413  -0.0195 -0.0376 105 ASP   A OD2 
2292 N  N   A ILE   A 106 ? 0.2841 0.4947 0.3085 -0.0846 0.0076  -0.0840 106 ILE   A N   
2293 N  N   B ILE   A 106 ? 0.3274 0.3661 0.3556 -0.0072 -0.0229 -0.0358 106 ILE   A N   
2294 C  CA  A ILE   A 106 ? 0.2543 0.4650 0.3069 -0.1019 -0.0061 -0.0943 106 ILE   A CA  
2295 C  CA  B ILE   A 106 ? 0.3234 0.3531 0.3552 -0.0207 -0.0254 -0.0406 106 ILE   A CA  
2296 C  C   A ILE   A 106 ? 0.2432 0.4316 0.3246 -0.1277 0.0029  -0.1175 106 ILE   A C   
2297 C  C   B ILE   A 106 ? 0.3220 0.3478 0.3433 -0.0209 -0.0169 -0.0274 106 ILE   A C   
2298 O  O   A ILE   A 106 ? 0.2247 0.4191 0.3311 -0.1398 0.0254  -0.1322 106 ILE   A O   
2299 O  O   B ILE   A 106 ? 0.3170 0.3523 0.3471 -0.0226 -0.0206 -0.0220 106 ILE   A O   
2300 C  CB  A ILE   A 106 ? 0.2550 0.4714 0.3164 -0.0822 -0.0189 -0.0696 106 ILE   A CB  
2301 C  CB  B ILE   A 106 ? 0.3236 0.3493 0.3462 -0.0311 -0.0361 -0.0535 106 ILE   A CB  
2302 C  CG1 A ILE   A 106 ? 0.2423 0.4781 0.3283 -0.0674 -0.0262 -0.0457 106 ILE   A CG1 
2303 C  CG1 B ILE   A 106 ? 0.3213 0.3486 0.3440 -0.0347 -0.0411 -0.0653 106 ILE   A CG1 
2304 C  CG2 A ILE   A 106 ? 0.2636 0.4690 0.3165 -0.0747 -0.0230 -0.0723 106 ILE   A CG2 
2305 C  CG2 B ILE   A 106 ? 0.3261 0.3478 0.3448 -0.0313 -0.0384 -0.0545 106 ILE   A CG2 
2306 C  CD1 A ILE   A 106 ? 0.2399 0.4798 0.3377 -0.0543 -0.0237 -0.0337 106 ILE   A CD1 
2307 C  CD1 B ILE   A 106 ? 0.3190 0.3473 0.3443 -0.0378 -0.0446 -0.0672 106 ILE   A CD1 
2330 N  N   A GLN   A 107 ? 0.2597 0.4082 0.3635 -0.1208 0.0281  -0.1196 107 GLN   A N   
2331 N  N   B GLN   A 107 ? 0.3252 0.3323 0.3536 -0.0187 -0.0009 -0.0154 107 GLN   A N   
2332 C  CA  A GLN   A 107 ? 0.2843 0.3846 0.4208 -0.1035 0.0459  -0.1100 107 GLN   A CA  
2333 C  CA  B GLN   A 107 ? 0.3296 0.3272 0.3720 -0.0213 0.0132  -0.0109 107 GLN   A CA  
2334 C  C   A GLN   A 107 ? 0.2511 0.3230 0.4087 -0.0962 0.0611  -0.0926 107 GLN   A C   
2335 C  C   B GLN   A 107 ? 0.3022 0.2961 0.3454 -0.0177 0.0266  -0.0075 107 GLN   A C   
2336 O  O   A GLN   A 107 ? 0.2693 0.3097 0.4612 -0.0978 0.0652  -0.0831 107 GLN   A O   
2337 O  O   B GLN   A 107 ? 0.3031 0.2957 0.3496 -0.0146 0.0338  -0.0145 107 GLN   A O   
2338 C  CB  A GLN   A 107 ? 0.3280 0.4111 0.4906 -0.1040 0.0405  -0.1117 107 GLN   A CB  
2339 C  CB  B GLN   A 107 ? 0.3563 0.3558 0.4322 -0.0296 0.0119  -0.0151 107 GLN   A CB  
2340 C  CG  A GLN   A 107 ? 0.3627 0.4385 0.5702 -0.1034 0.0356  -0.1050 107 GLN   A CG  
2341 C  CG  B GLN   A 107 ? 0.3785 0.3810 0.4917 -0.0367 0.0099  -0.0149 107 GLN   A CG  
2342 C  CD  A GLN   A 107 ? 0.3917 0.4601 0.6378 -0.1044 0.0388  -0.0924 107 GLN   A CD  
2343 C  CD  B GLN   A 107 ? 0.3952 0.4029 0.5401 -0.0427 0.0126  -0.0140 107 GLN   A CD  
2344 O  OE1 A GLN   A 107 ? 0.4066 0.4671 0.6694 -0.1019 0.0413  -0.0888 107 GLN   A OE1 
2345 O  OE1 B GLN   A 107 ? 0.4028 0.4119 0.5639 -0.0446 0.0128  -0.0177 107 GLN   A OE1 
2346 N  NE2 A GLN   A 107 ? 0.4058 0.4699 0.6579 -0.1107 0.0373  -0.0916 107 GLN   A NE2 
2347 N  NE2 B GLN   A 107 ? 0.3984 0.4114 0.5585 -0.0463 0.0139  -0.0126 107 GLN   A NE2 
2364 N  N   A LEU   A 108 ? 0.2032 0.2703 0.3496 -0.0843 0.0543  -0.0929 108 LEU   A N   
2365 N  N   B LEU   A 108 ? 0.2746 0.2670 0.3148 -0.0195 0.0304  -0.0052 108 LEU   A N   
2366 C  CA  A LEU   A 108 ? 0.1913 0.2202 0.3215 -0.0475 0.0369  -0.0501 108 LEU   A CA  
2367 C  CA  B LEU   A 108 ? 0.2470 0.2371 0.2955 -0.0133 0.0293  -0.0027 108 LEU   A CA  
2368 C  C   A LEU   A 108 ? 0.1821 0.1715 0.3192 -0.0226 0.0327  -0.0044 108 LEU   A C   
2369 C  C   B LEU   A 108 ? 0.2130 0.1969 0.2987 -0.0053 0.0271  0.0075  108 LEU   A C   
2370 O  O   A LEU   A 108 ? 0.1757 0.1582 0.3511 -0.0102 0.0458  0.0050  108 LEU   A O   
2371 O  O   B LEU   A 108 ? 0.2143 0.1923 0.3038 -0.0019 0.0324  0.0077  108 LEU   A O   
2372 C  CB  A LEU   A 108 ? 0.2001 0.2283 0.3059 -0.0450 0.0375  -0.0463 108 LEU   A CB  
2373 C  CB  B LEU   A 108 ? 0.2541 0.2505 0.2839 -0.0182 0.0340  -0.0084 108 LEU   A CB  
2374 C  CG  A LEU   A 108 ? 0.2195 0.2459 0.3208 -0.0335 0.0374  -0.0406 108 LEU   A CG  
2375 C  CG  B LEU   A 108 ? 0.2609 0.2630 0.2902 -0.0256 0.0325  -0.0143 108 LEU   A CG  
2376 C  CD1 A LEU   A 108 ? 0.2345 0.2510 0.3248 -0.0410 0.0402  -0.0359 108 LEU   A CD1 
2377 C  CD1 B LEU   A 108 ? 0.2661 0.2652 0.2911 -0.0308 0.0313  -0.0150 108 LEU   A CD1 
2378 C  CD2 A LEU   A 108 ? 0.2272 0.2632 0.3430 -0.0159 0.0413  -0.0348 108 LEU   A CD2 
2379 C  CD2 B LEU   A 108 ? 0.2652 0.2728 0.3008 -0.0243 0.0323  -0.0130 108 LEU   A CD2 
2402 N  N   . LEU   A 109 ? 0.1787 0.1738 0.3111 0.0011  0.0226  0.0127  109 LEU   A N   
2403 C  CA  . LEU   A 109 ? 0.1694 0.1613 0.3173 0.0078  0.0056  0.0161  109 LEU   A CA  
2404 C  C   . LEU   A 109 ? 0.1499 0.1458 0.3112 -0.0061 0.0010  0.0056  109 LEU   A C   
2405 O  O   . LEU   A 109 ? 0.1588 0.1424 0.3212 -0.0073 -0.0049 0.0094  109 LEU   A O   
2406 C  CB  . LEU   A 109 ? 0.1707 0.1785 0.3428 0.0067  0.0016  0.0341  109 LEU   A CB  
2407 C  CG  . LEU   A 109 ? 0.1618 0.1855 0.3586 0.0037  0.0038  0.0350  109 LEU   A CG  
2408 C  CD1 . LEU   A 109 ? 0.1671 0.1734 0.3706 -0.0012 0.0180  0.0227  109 LEU   A CD1 
2409 C  CD2 . LEU   A 109 ? 0.1666 0.1996 0.3752 0.0038  -0.0051 0.0448  109 LEU   A CD2 
2422 N  N   . LYS   A 110 ? 0.1548 0.1492 0.3157 -0.0091 -0.0026 0.0160  110 LYS   A N   
2423 C  CA  . LYS   A 110 ? 0.1518 0.1449 0.3169 -0.0131 -0.0007 0.0177  110 LYS   A CA  
2424 C  C   . LYS   A 110 ? 0.1577 0.1417 0.3009 -0.0154 0.0031  0.0136  110 LYS   A C   
2425 O  O   . LYS   A 110 ? 0.1503 0.1429 0.3261 -0.0062 0.0039  0.0011  110 LYS   A O   
2426 C  CB  . LYS   A 110 ? 0.1640 0.1554 0.3365 -0.0062 -0.0082 0.0074  110 LYS   A CB  
2427 C  CG  . LYS   A 110 ? 0.1711 0.1488 0.3445 -0.0073 -0.0116 0.0041  110 LYS   A CG  
2428 C  CD  . LYS   A 110 ? 0.1716 0.1581 0.3527 -0.0119 -0.0039 -0.0019 110 LYS   A CD  
2429 C  CE  . LYS   A 110 ? 0.1743 0.1622 0.3803 -0.0203 0.0115  -0.0112 110 LYS   A CE  
2430 N  NZ  . LYS   A 110 ? 0.1694 0.1661 0.3977 -0.0168 0.0239  -0.0078 110 LYS   A NZ  
2444 N  N   . SER   A 111 ? 0.1601 0.1418 0.3086 -0.0108 -0.0024 0.0198  111 SER   A N   
2445 C  CA  . SER   A 111 ? 0.1478 0.1470 0.3231 -0.0103 0.0105  0.0091  111 SER   A CA  
2446 C  C   . SER   A 111 ? 0.1434 0.1458 0.3334 -0.0095 0.0241  0.0112  111 SER   A C   
2447 O  O   . SER   A 111 ? 0.1547 0.1356 0.3502 -0.0071 0.0195  0.0103  111 SER   A O   
2448 C  CB  . SER   A 111 ? 0.1679 0.1670 0.3390 -0.0094 0.0161  -0.0112 111 SER   A CB  
2449 O  OG  . SER   A 111 ? 0.2104 0.1735 0.3337 0.0022  0.0005  -0.0163 111 SER   A OG  
2455 N  N   . ALA   A 112 ? 0.1477 0.1396 0.3313 -0.0040 0.0222  0.0073  112 ALA   A N   
2456 C  CA  . ALA   A 112 ? 0.1498 0.1404 0.3321 -0.0056 0.0363  0.0052  112 ALA   A CA  
2457 C  C   . ALA   A 112 ? 0.1450 0.1371 0.3410 -0.0040 0.0259  0.0065  112 ALA   A C   
2458 O  O   . ALA   A 112 ? 0.1483 0.1346 0.3424 -0.0117 0.0257  0.0217  112 ALA   A O   
2459 C  CB  . ALA   A 112 ? 0.1572 0.1395 0.3300 -0.0088 0.0235  0.0124  112 ALA   A CB  
2465 N  N   . TYR   A 113 ? 0.1317 0.1407 0.3458 -0.0027 0.0224  0.0191  113 TYR   A N   
2466 C  CA  . TYR   A 113 ? 0.1362 0.1401 0.3232 -0.0056 0.0268  0.0243  113 TYR   A CA  
2467 C  C   . TYR   A 113 ? 0.1325 0.1413 0.3232 -0.0151 0.0230  0.0109  113 TYR   A C   
2468 O  O   . TYR   A 113 ? 0.1404 0.1413 0.3337 -0.0057 0.0243  0.0032  113 TYR   A O   
2469 C  CB  . TYR   A 113 ? 0.1369 0.1472 0.3200 -0.0017 0.0066  0.0297  113 TYR   A CB  
2470 C  CG  . TYR   A 113 ? 0.1454 0.1538 0.3138 -0.0194 0.0263  0.0370  113 TYR   A CG  
2471 C  CD1 . TYR   A 113 ? 0.1445 0.1674 0.3070 -0.0072 0.0287  0.0488  113 TYR   A CD1 
2472 C  CD2 . TYR   A 113 ? 0.1509 0.1558 0.3134 -0.0130 0.0175  0.0430  113 TYR   A CD2 
2473 C  CE1 . TYR   A 113 ? 0.1506 0.1724 0.3130 -0.0041 0.0222  0.0461  113 TYR   A CE1 
2474 C  CE2 . TYR   A 113 ? 0.1533 0.1725 0.2977 -0.0095 0.0187  0.0447  113 TYR   A CE2 
2475 C  CZ  . TYR   A 113 ? 0.1431 0.1752 0.3048 -0.0035 0.0279  0.0542  113 TYR   A CZ  
2476 O  OH  . TYR   A 113 ? 0.1387 0.1814 0.3320 0.0102  0.0133  0.0584  113 TYR   A OH  
2486 N  N   . GLU   A 114 ? 0.1333 0.1369 0.3291 -0.0138 0.0200  0.0239  114 GLU   A N   
2487 C  CA  . GLU   A 114 ? 0.1396 0.1298 0.3385 0.0038  0.0095  0.0272  114 GLU   A CA  
2488 C  C   . GLU   A 114 ? 0.1339 0.1375 0.3329 -0.0060 0.0187  0.0199  114 GLU   A C   
2489 O  O   . GLU   A 114 ? 0.1476 0.1392 0.3300 -0.0047 0.0058  0.0221  114 GLU   A O   
2490 C  CB  . GLU   A 114 ? 0.1407 0.1363 0.3435 -0.0076 0.0135  0.0255  114 GLU   A CB  
2491 C  CG  . GLU   A 114 ? 0.1432 0.1361 0.3615 -0.0029 0.0165  0.0127  114 GLU   A CG  
2492 C  CD  . GLU   A 114 ? 0.1551 0.1338 0.3756 -0.0069 0.0029  0.0080  114 GLU   A CD  
2493 O  OE1 . GLU   A 114 ? 0.1490 0.1373 0.3812 -0.0124 0.0111  0.0006  114 GLU   A OE1 
2494 O  OE2 . GLU   A 114 ? 0.1737 0.1408 0.3756 -0.0116 0.0059  -0.0049 114 GLU   A OE2 
2501 N  N   . ASN   A 115 ? 0.1359 0.1408 0.3245 -0.0123 0.0257  0.0199  115 ASN   A N   
2502 C  CA  . ASN   A 115 ? 0.1415 0.1481 0.3337 -0.0124 0.0216  0.0302  115 ASN   A CA  
2503 C  C   . ASN   A 115 ? 0.1498 0.1449 0.3481 -0.0069 0.0266  0.0327  115 ASN   A C   
2504 O  O   . ASN   A 115 ? 0.1488 0.1491 0.3595 -0.0137 0.0311  0.0296  115 ASN   A O   
2505 C  CB  . ASN   A 115 ? 0.1581 0.1481 0.3213 -0.0171 0.0194  0.0197  115 ASN   A CB  
2506 C  CG  . ASN   A 115 ? 0.1577 0.1645 0.3134 -0.0225 0.0217  0.0101  115 ASN   A CG  
2507 O  OD1 . ASN   A 115 ? 0.1518 0.2600 0.3373 -0.0127 0.0251  0.0194  115 ASN   A OD1 
2508 N  ND2 . ASN   A 115 ? 0.1586 0.1457 0.3100 -0.0210 0.0337  0.0187  115 ASN   A ND2 
2515 N  N   . PHE   A 116 ? 0.1390 0.1371 0.3557 -0.0004 0.0221  0.0291  116 PHE   A N   
2516 C  CA  . PHE   A 116 ? 0.1418 0.1478 0.3346 -0.0039 0.0221  0.0265  116 PHE   A CA  
2517 C  C   . PHE   A 116 ? 0.1406 0.1574 0.3182 -0.0099 0.0208  0.0327  116 PHE   A C   
2518 O  O   . PHE   A 116 ? 0.1405 0.1634 0.3185 0.0016  0.0237  0.0459  116 PHE   A O   
2519 C  CB  . PHE   A 116 ? 0.1364 0.1421 0.3538 0.0014  0.0309  0.0217  116 PHE   A CB  
2520 C  CG  . PHE   A 116 ? 0.1396 0.1406 0.3279 -0.0103 0.0267  0.0079  116 PHE   A CG  
2521 C  CD1 . PHE   A 116 ? 0.1421 0.1390 0.3257 -0.0134 0.0200  0.0177  116 PHE   A CD1 
2522 C  CD2 . PHE   A 116 ? 0.1521 0.1500 0.3228 -0.0106 0.0244  0.0136  116 PHE   A CD2 
2523 C  CE1 . PHE   A 116 ? 0.1446 0.1458 0.3300 -0.0229 0.0215  0.0171  116 PHE   A CE1 
2524 C  CE2 . PHE   A 116 ? 0.1405 0.1509 0.3327 -0.0069 0.0241  0.0121  116 PHE   A CE2 
2525 C  CZ  . PHE   A 116 ? 0.1487 0.1301 0.3258 -0.0030 0.0215  0.0230  116 PHE   A CZ  
2535 N  N   . ASN   A 117 ? 0.1406 0.1482 0.3337 -0.0111 0.0175  0.0293  117 ASN   A N   
2536 C  CA  . ASN   A 117 ? 0.1451 0.1481 0.3352 -0.0012 0.0168  0.0414  117 ASN   A CA  
2537 C  C   . ASN   A 117 ? 0.1469 0.1631 0.3403 -0.0048 0.0210  0.0351  117 ASN   A C   
2538 O  O   . ASN   A 117 ? 0.1568 0.1644 0.3903 -0.0042 0.0072  0.0450  117 ASN   A O   
2539 C  CB  . ASN   A 117 ? 0.1454 0.1558 0.3356 -0.0061 0.0099  0.0515  117 ASN   A CB  
2540 C  CG  . ASN   A 117 ? 0.1421 0.1504 0.3434 -0.0040 0.0202  0.0524  117 ASN   A CG  
2541 O  OD1 . ASN   A 117 ? 0.1454 0.1718 0.3552 -0.0136 0.0221  0.0417  117 ASN   A OD1 
2542 N  ND2 . ASN   A 117 ? 0.1385 0.1502 0.3417 -0.0007 0.0106  0.0444  117 ASN   A ND2 
2549 N  N   . GLN   A 118 ? 0.1380 0.1598 0.3276 -0.0140 0.0133  0.0430  118 GLN   A N   
2550 C  CA  . GLN   A 118 ? 0.1544 0.1722 0.3443 -0.0169 0.0104  0.0364  118 GLN   A CA  
2551 C  C   . GLN   A 118 ? 0.1538 0.1817 0.3333 -0.0243 0.0089  0.0405  118 GLN   A C   
2552 O  O   . GLN   A 118 ? 0.1581 0.2023 0.3464 -0.0119 0.0031  0.0300  118 GLN   A O   
2553 C  CB  . GLN   A 118 ? 0.1548 0.1731 0.3426 -0.0072 0.0347  0.0401  118 GLN   A CB  
2554 C  CG  . GLN   A 118 ? 0.1430 0.1746 0.3474 -0.0032 0.0232  0.0401  118 GLN   A CG  
2555 C  CD  . GLN   A 118 ? 0.1457 0.1783 0.3624 -0.0040 0.0228  0.0405  118 GLN   A CD  
2556 O  OE1 . GLN   A 118 ? 0.1449 0.1912 0.3790 -0.0059 0.0118  0.0281  118 GLN   A OE1 
2557 N  NE2 . GLN   A 118 ? 0.1517 0.1712 0.3644 -0.0007 0.0253  0.0423  118 GLN   A NE2 
2566 N  N   . HIS   A 119 ? 0.1600 0.1825 0.3075 -0.0114 0.0179  0.0518  119 HIS   A N   
2567 C  CA  . HIS   A 119 ? 0.1696 0.1849 0.2999 -0.0083 0.0155  0.0519  119 HIS   A CA  
2568 C  C   . HIS   A 119 ? 0.1802 0.1946 0.2891 -0.0151 0.0193  0.0633  119 HIS   A C   
2569 O  O   . HIS   A 119 ? 0.1795 0.2016 0.3095 -0.0290 0.0063  0.0607  119 HIS   A O   
2570 C  CB  . HIS   A 119 ? 0.1667 0.1730 0.3270 -0.0090 0.0252  0.0482  119 HIS   A CB  
2571 C  CG  . HIS   A 119 ? 0.1718 0.1838 0.3637 -0.0042 0.0259  0.0451  119 HIS   A CG  
2572 N  ND1 . HIS   A 119 ? 0.1861 0.2020 0.4056 -0.0166 0.0243  0.0381  119 HIS   A ND1 
2573 C  CD2 . HIS   A 119 ? 0.1862 0.1907 0.3665 0.0016  0.0447  0.0597  119 HIS   A CD2 
2574 C  CE1 . HIS   A 119 ? 0.1806 0.2040 0.3983 -0.0183 0.0372  0.0558  119 HIS   A CE1 
2575 N  NE2 . HIS   A 119 ? 0.1951 0.1961 0.3889 -0.0112 0.0554  0.0646  119 HIS   A NE2 
2583 N  N   . GLU   A 120 ? 0.1889 0.2227 0.2985 -0.0166 0.0040  0.0879  120 GLU   A N   
2584 C  CA  . GLU   A 120 ? 0.2061 0.2523 0.3235 -0.0107 -0.0019 0.1218  120 GLU   A CA  
2585 C  C   . GLU   A 120 ? 0.1859 0.2352 0.3088 -0.0200 0.0069  0.1124  120 GLU   A C   
2586 O  O   . GLU   A 120 ? 0.1859 0.2276 0.3296 -0.0119 -0.0030 0.1134  120 GLU   A O   
2587 C  CB  . GLU   A 120 ? 0.2533 0.3069 0.3635 0.0074  -0.0099 0.1503  120 GLU   A CB  
2588 C  CG  . GLU   A 120 ? 0.3094 0.3453 0.4340 0.0201  -0.0043 0.1448  120 GLU   A CG  
2589 C  CD  . GLU   A 120 ? 0.3738 0.3891 0.4903 0.0322  0.0016  0.1350  120 GLU   A CD  
2590 O  OE1 . GLU   A 120 ? 0.4249 0.4114 0.5187 0.0323  0.0002  0.1270  120 GLU   A OE1 
2591 O  OE2 . GLU   A 120 ? 0.4199 0.4194 0.5350 0.0314  -0.0004 0.1335  120 GLU   A OE2 
2598 N  N   . VAL   A 121 ? 0.1801 0.2360 0.2917 -0.0228 0.0204  0.0906  121 VAL   A N   
2599 C  CA  . VAL   A 121 ? 0.1945 0.2361 0.2832 -0.0184 0.0225  0.0841  121 VAL   A CA  
2600 C  C   . VAL   A 121 ? 0.1806 0.2211 0.2801 -0.0285 0.0201  0.0704  121 VAL   A C   
2601 O  O   . VAL   A 121 ? 0.1837 0.2279 0.2937 -0.0388 0.0041  0.0666  121 VAL   A O   
2602 C  CB  . VAL   A 121 ? 0.2328 0.2720 0.2911 -0.0071 0.0299  0.0682  121 VAL   A CB  
2603 C  CG1 . VAL   A 121 ? 0.2357 0.2857 0.2822 -0.0039 0.0250  0.0684  121 VAL   A CG1 
2604 C  CG2 . VAL   A 121 ? 0.2557 0.2952 0.3194 -0.0204 0.0304  0.0550  121 VAL   A CG2 
2614 N  N   . LEU   A 122 ? 0.1669 0.1982 0.2763 -0.0232 0.0167  0.0652  122 LEU   A N   
2615 C  CA  . LEU   A 122 ? 0.1681 0.1816 0.2791 -0.0285 0.0292  0.0624  122 LEU   A CA  
2616 C  C   . LEU   A 122 ? 0.1680 0.1850 0.2948 -0.0301 0.0083  0.0523  122 LEU   A C   
2617 O  O   . LEU   A 122 ? 0.1638 0.1997 0.3196 -0.0349 -0.0008 0.0691  122 LEU   A O   
2618 C  CB  . LEU   A 122 ? 0.1968 0.1897 0.3036 -0.0173 0.0133  0.0631  122 LEU   A CB  
2619 C  CG  . LEU   A 122 ? 0.1990 0.2014 0.2927 -0.0127 0.0365  0.0450  122 LEU   A CG  
2620 C  CD1 . LEU   A 122 ? 0.2130 0.1955 0.2830 -0.0222 0.0380  0.0521  122 LEU   A CD1 
2621 C  CD2 . LEU   A 122 ? 0.1924 0.1897 0.2721 -0.0101 0.0419  0.0460  122 LEU   A CD2 
2633 N  N   A LEU   A 123 ? 0.1590 0.1799 0.2884 -0.0260 0.0021  0.0473  123 LEU   A N   
2634 N  N   B LEU   A 123 ? 0.1655 0.1723 0.2634 -0.0311 0.0080  0.0451  123 LEU   A N   
2635 C  CA  A LEU   A 123 ? 0.1640 0.1845 0.2720 -0.0280 0.0023  0.0479  123 LEU   A CA  
2636 C  CA  B LEU   A 123 ? 0.1708 0.1690 0.2362 -0.0334 0.0118  0.0473  123 LEU   A CA  
2637 C  C   A LEU   A 123 ? 0.1574 0.1766 0.2672 -0.0199 0.0172  0.0539  123 LEU   A C   
2638 C  C   B LEU   A 123 ? 0.1703 0.1599 0.2253 -0.0222 0.0120  0.0452  123 LEU   A C   
2639 O  O   A LEU   A 123 ? 0.1450 0.1823 0.2865 -0.0218 0.0133  0.0492  123 LEU   A O   
2640 O  O   B LEU   A 123 ? 0.1650 0.1578 0.2397 -0.0233 0.0013  0.0394  123 LEU   A O   
2641 C  CB  A LEU   A 123 ? 0.1737 0.1985 0.2800 -0.0271 0.0097  0.0571  123 LEU   A CB  
2642 C  CB  B LEU   A 123 ? 0.1763 0.1708 0.2365 -0.0381 0.0252  0.0573  123 LEU   A CB  
2643 C  CG  A LEU   A 123 ? 0.1784 0.2195 0.2792 -0.0192 0.0133  0.0425  123 LEU   A CG  
2644 C  CG  B LEU   A 123 ? 0.1825 0.1806 0.2383 -0.0300 0.0273  0.0439  123 LEU   A CG  
2645 C  CD1 A LEU   A 123 ? 0.1854 0.2261 0.2860 -0.0079 0.0124  0.0324  123 LEU   A CD1 
2646 C  CD1 B LEU   A 123 ? 0.1872 0.1859 0.2393 -0.0261 0.0229  0.0329  123 LEU   A CD1 
2647 C  CD2 A LEU   A 123 ? 0.1862 0.2283 0.2864 -0.0228 0.0042  0.0409  123 LEU   A CD2 
2648 C  CD2 B LEU   A 123 ? 0.1883 0.1818 0.2387 -0.0271 0.0279  0.0471  123 LEU   A CD2 
2671 N  N   A ALA   A 124 ? 0.1572 0.1632 0.2649 -0.0210 0.0146  0.0420  124 ALA   A N   
2672 N  N   B ALA   A 124 ? 0.1680 0.1545 0.2101 -0.0181 0.0175  0.0371  124 ALA   A N   
2673 C  CA  A ALA   A 124 ? 0.1402 0.1436 0.2796 -0.0062 0.0187  0.0427  124 ALA   A CA  
2674 C  CA  B ALA   A 124 ? 0.1658 0.1434 0.2211 -0.0160 0.0143  0.0336  124 ALA   A CA  
2675 C  C   A ALA   A 124 ? 0.1382 0.1396 0.2713 -0.0069 0.0319  0.0310  124 ALA   A C   
2676 C  C   B ALA   A 124 ? 0.1607 0.1396 0.2250 -0.0106 0.0202  0.0316  124 ALA   A C   
2677 O  O   A ALA   A 124 ? 0.1340 0.1576 0.2767 -0.0046 0.0285  0.0347  124 ALA   A O   
2678 O  O   B ALA   A 124 ? 0.1606 0.1357 0.2427 0.0028  0.0135  0.0306  124 ALA   A O   
2679 C  CB  A ALA   A 124 ? 0.1375 0.1198 0.2930 0.0021  0.0020  0.0390  124 ALA   A CB  
2680 C  CB  B ALA   A 124 ? 0.1786 0.1428 0.2226 -0.0101 0.0040  0.0195  124 ALA   A CB  
2691 N  N   A PRO   A 125 ? 0.1301 0.1443 0.2612 0.0007  0.0294  0.0228  125 PRO   A N   
2692 N  N   B PRO   A 125 ? 0.1440 0.1325 0.2110 0.0009  0.0201  0.0275  125 PRO   A N   
2693 C  CA  A PRO   A 125 ? 0.1384 0.1596 0.2683 0.0016  0.0255  0.0290  125 PRO   A CA  
2694 C  CA  B PRO   A 125 ? 0.1423 0.1440 0.2113 0.0030  0.0279  0.0286  125 PRO   A CA  
2695 C  C   A PRO   A 125 ? 0.1394 0.1653 0.2558 -0.0146 0.0281  0.0351  125 PRO   A C   
2696 C  C   B PRO   A 125 ? 0.1417 0.1569 0.2198 0.0036  0.0239  0.0297  125 PRO   A C   
2697 O  O   A PRO   A 125 ? 0.1506 0.1562 0.2497 -0.0169 0.0274  0.0288  125 PRO   A O   
2698 O  O   B PRO   A 125 ? 0.1440 0.1571 0.2258 0.0048  0.0124  0.0345  125 PRO   A O   
2699 C  CB  A PRO   A 125 ? 0.1561 0.1614 0.2813 -0.0108 0.0324  0.0261  125 PRO   A CB  
2700 C  CB  B PRO   A 125 ? 0.1356 0.1350 0.2127 -0.0014 0.0191  0.0280  125 PRO   A CB  
2701 C  CG  A PRO   A 125 ? 0.1692 0.1545 0.2919 -0.0042 0.0151  0.0273  125 PRO   A CG  
2702 C  CG  B PRO   A 125 ? 0.1249 0.1239 0.2037 0.0014  0.0148  0.0199  125 PRO   A CG  
2703 C  CD  A PRO   A 125 ? 0.1485 0.1538 0.2741 -0.0050 0.0240  0.0281  125 PRO   A CD  
2704 C  CD  B PRO   A 125 ? 0.1275 0.1097 0.2057 -0.0041 0.0212  0.0187  125 PRO   A CD  
2719 N  N   A LEU   A 126 ? 0.1354 0.1879 0.2771 -0.0050 0.0131  0.0453  126 LEU   A N   
2720 N  N   B LEU   A 126 ? 0.1458 0.1782 0.2341 0.0107  0.0153  0.0334  126 LEU   A N   
2721 C  CA  A LEU   A 126 ? 0.1410 0.1779 0.2699 -0.0110 -0.0062 0.0601  126 LEU   A CA  
2722 C  CA  B LEU   A 126 ? 0.1526 0.1801 0.2336 0.0035  0.0040  0.0459  126 LEU   A CA  
2723 C  C   A LEU   A 126 ? 0.1496 0.1766 0.2633 -0.0030 -0.0045 0.0493  126 LEU   A C   
2724 C  C   B LEU   A 126 ? 0.1462 0.1739 0.2239 0.0005  -0.0013 0.0441  126 LEU   A C   
2725 O  O   A LEU   A 126 ? 0.1561 0.1804 0.2635 0.0089  0.0056  0.0553  126 LEU   A O   
2726 O  O   B LEU   A 126 ? 0.1399 0.1664 0.2057 -0.0070 -0.0088 0.0532  126 LEU   A O   
2727 C  CB  A LEU   A 126 ? 0.1445 0.1740 0.2709 -0.0041 -0.0015 0.0622  126 LEU   A CB  
2728 C  CB  B LEU   A 126 ? 0.1629 0.1907 0.2353 0.0011  0.0143  0.0436  126 LEU   A CB  
2729 C  CG  A LEU   A 126 ? 0.1408 0.1814 0.2932 0.0069  0.0080  0.0511  126 LEU   A CG  
2730 C  CG  B LEU   A 126 ? 0.1627 0.1881 0.2412 0.0071  0.0179  0.0254  126 LEU   A CG  
2731 C  CD1 A LEU   A 126 ? 0.1408 0.1951 0.3018 0.0043  0.0154  0.0521  126 LEU   A CD1 
2732 C  CD1 B LEU   A 126 ? 0.1667 0.1840 0.2454 0.0043  0.0066  0.0156  126 LEU   A CD1 
2733 C  CD2 A LEU   A 126 ? 0.1588 0.1786 0.2922 -0.0041 0.0151  0.0370  126 LEU   A CD2 
2734 C  CD2 B LEU   A 126 ? 0.1561 0.1907 0.2521 0.0133  0.0195  0.0242  126 LEU   A CD2 
2757 N  N   A LEU   A 127 ? 0.1539 0.1702 0.2629 -0.0070 0.0157  0.0475  127 LEU   A N   
2758 N  N   B LEU   A 127 ? 0.1398 0.1724 0.2105 0.0057  0.0119  0.0537  127 LEU   A N   
2759 C  CA  A LEU   A 127 ? 0.1583 0.1688 0.2557 -0.0078 0.0033  0.0352  127 LEU   A CA  
2760 C  CA  B LEU   A 127 ? 0.1353 0.1727 0.2015 0.0094  0.0032  0.0444  127 LEU   A CA  
2761 C  C   A LEU   A 127 ? 0.1568 0.1574 0.2481 -0.0145 0.0027  0.0267  127 LEU   A C   
2762 C  C   B LEU   A 127 ? 0.1349 0.1643 0.2110 0.0100  -0.0003 0.0302  127 LEU   A C   
2763 O  O   A LEU   A 127 ? 0.1584 0.1617 0.2845 -0.0251 0.0063  0.0334  127 LEU   A O   
2764 O  O   B LEU   A 127 ? 0.1364 0.1593 0.2359 0.0120  0.0072  0.0463  127 LEU   A O   
2765 C  CB  A LEU   A 127 ? 0.1661 0.1689 0.2576 -0.0002 0.0112  0.0375  127 LEU   A CB  
2766 C  CB  B LEU   A 127 ? 0.1339 0.1870 0.2090 0.0077  0.0039  0.0347  127 LEU   A CB  
2767 C  CG  A LEU   A 127 ? 0.1641 0.1637 0.2559 0.0019  0.0011  0.0349  127 LEU   A CG  
2768 C  CG  B LEU   A 127 ? 0.1415 0.2032 0.2055 0.0110  0.0058  0.0404  127 LEU   A CG  
2769 C  CD1 A LEU   A 127 ? 0.1713 0.1609 0.2737 0.0052  -0.0056 0.0197  127 LEU   A CD1 
2770 C  CD1 B LEU   A 127 ? 0.1456 0.2084 0.2218 0.0127  0.0089  0.0394  127 LEU   A CD1 
2771 C  CD2 A LEU   A 127 ? 0.1682 0.1579 0.2741 0.0084  -0.0070 0.0325  127 LEU   A CD2 
2772 C  CD2 B LEU   A 127 ? 0.1525 0.2167 0.2137 0.0072  -0.0084 0.0337  127 LEU   A CD2 
2795 N  N   A SER   A 128 ? 0.1602 0.1528 0.2301 -0.0181 0.0034  0.0263  128 SER   A N   
2796 N  N   B SER   A 128 ? 0.1422 0.1605 0.2069 -0.0027 -0.0056 0.0148  128 SER   A N   
2797 C  CA  A SER   A 128 ? 0.1676 0.1605 0.2081 -0.0107 0.0066  0.0248  128 SER   A CA  
2798 C  CA  B SER   A 128 ? 0.1528 0.1587 0.1932 -0.0101 -0.0032 0.0114  128 SER   A CA  
2799 C  C   A SER   A 128 ? 0.1722 0.1664 0.1995 0.0014  0.0113  0.0268  128 SER   A C   
2800 C  C   B SER   A 128 ? 0.1568 0.1649 0.1949 -0.0050 -0.0115 0.0184  128 SER   A C   
2801 O  O   A SER   A 128 ? 0.1811 0.1793 0.1955 0.0043  0.0169  0.0218  128 SER   A O   
2802 O  O   B SER   A 128 ? 0.1625 0.1650 0.1974 -0.0107 -0.0069 0.0328  128 SER   A O   
2803 C  CB  A SER   A 128 ? 0.1627 0.1607 0.2167 -0.0070 0.0056  0.0307  128 SER   A CB  
2804 C  CB  B SER   A 128 ? 0.1630 0.1615 0.2051 -0.0083 0.0039  0.0053  128 SER   A CB  
2805 O  OG  A SER   A 128 ? 0.1639 0.1593 0.2416 -0.0065 0.0054  0.0085  128 SER   A OG  
2806 O  OG  B SER   A 128 ? 0.1674 0.1659 0.2174 -0.0018 0.0108  0.0062  128 SER   A OG  
2817 N  N   A ALA   A 129 ? 0.1641 0.1699 0.2064 -0.0047 -0.0001 0.0391  129 ALA   A N   
2818 N  N   B ALA   A 129 ? 0.1498 0.1725 0.1937 0.0014  -0.0276 0.0160  129 ALA   A N   
2819 C  CA  A ALA   A 129 ? 0.1584 0.1640 0.2336 -0.0026 0.0029  0.0263  129 ALA   A CA  
2820 C  CA  B ALA   A 129 ? 0.1508 0.1746 0.2048 0.0008  -0.0243 0.0051  129 ALA   A CA  
2821 C  C   A ALA   A 129 ? 0.1689 0.1555 0.2697 -0.0104 -0.0115 0.0077  129 ALA   A C   
2822 C  C   B ALA   A 129 ? 0.1647 0.1745 0.2174 0.0024  -0.0201 0.0026  129 ALA   A C   
2823 O  O   A ALA   A 129 ? 0.1702 0.1662 0.2822 -0.0128 -0.0130 0.0259  129 ALA   A O   
2824 O  O   B ALA   A 129 ? 0.1637 0.1814 0.2191 0.0029  -0.0174 0.0124  129 ALA   A O   
2825 C  CB  A ALA   A 129 ? 0.1552 0.1727 0.2253 0.0041  0.0028  0.0218  129 ALA   A CB  
2826 C  CB  B ALA   A 129 ? 0.1531 0.1814 0.2020 -0.0013 -0.0113 0.0024  129 ALA   A CB  
2837 N  N   A GLY   A 130 ? 0.1766 0.1571 0.2990 -0.0095 -0.0071 0.0024  130 GLY   A N   
2838 N  N   B GLY   A 130 ? 0.1776 0.1696 0.2299 0.0070  -0.0036 0.0084  130 GLY   A N   
2839 C  CA  A GLY   A 130 ? 0.1924 0.1693 0.3034 -0.0009 -0.0108 0.0080  130 GLY   A CA  
2840 C  CA  B GLY   A 130 ? 0.1889 0.1730 0.2193 0.0087  0.0136  0.0131  130 GLY   A CA  
2841 C  C   A GLY   A 130 ? 0.1866 0.1699 0.2820 0.0034  -0.0180 0.0055  130 GLY   A C   
2842 C  C   B GLY   A 130 ? 0.1901 0.1713 0.2012 0.0099  0.0266  -0.0003 130 GLY   A C   
2843 O  O   A GLY   A 130 ? 0.1891 0.1647 0.3141 0.0061  -0.0370 0.0015  130 GLY   A O   
2844 O  O   B GLY   A 130 ? 0.1972 0.1643 0.2018 0.0128  0.0198  -0.0093 130 GLY   A O   
2851 N  N   A ILE   A 131 ? 0.1857 0.1646 0.2338 -0.0081 -0.0133 0.0219  131 ILE   A N   
2852 N  N   B ILE   A 131 ? 0.1931 0.1714 0.1908 0.0048  0.0265  -0.0076 131 ILE   A N   
2853 C  CA  A ILE   A 131 ? 0.2047 0.1554 0.2054 -0.0093 -0.0142 0.0206  131 ILE   A CA  
2854 C  CA  B ILE   A 131 ? 0.1977 0.1703 0.1829 -0.0066 0.0209  -0.0184 131 ILE   A CA  
2855 C  C   A ILE   A 131 ? 0.1926 0.1561 0.2090 -0.0076 -0.0077 0.0242  131 ILE   A C   
2856 C  C   B ILE   A 131 ? 0.1865 0.1569 0.1823 -0.0054 0.0170  -0.0132 131 ILE   A C   
2857 O  O   A ILE   A 131 ? 0.2011 0.1578 0.2078 0.0029  -0.0121 0.0235  131 ILE   A O   
2858 O  O   B ILE   A 131 ? 0.1848 0.1347 0.1968 -0.0068 0.0099  -0.0237 131 ILE   A O   
2859 C  CB  A ILE   A 131 ? 0.2322 0.1730 0.1919 -0.0210 -0.0156 0.0106  131 ILE   A CB  
2860 C  CB  B ILE   A 131 ? 0.2061 0.1855 0.1938 -0.0190 0.0294  -0.0265 131 ILE   A CB  
2861 C  CG1 A ILE   A 131 ? 0.2426 0.2095 0.2069 -0.0395 -0.0133 0.0114  131 ILE   A CG1 
2862 C  CG1 B ILE   A 131 ? 0.2103 0.2085 0.1842 -0.0296 0.0307  -0.0336 131 ILE   A CG1 
2863 C  CG2 A ILE   A 131 ? 0.2477 0.1648 0.2030 -0.0218 0.0015  0.0067  131 ILE   A CG2 
2864 C  CG2 B ILE   A 131 ? 0.2125 0.1814 0.2100 -0.0172 0.0396  -0.0265 131 ILE   A CG2 
2865 C  CD1 A ILE   A 131 ? 0.2526 0.2286 0.2268 -0.0537 -0.0090 -0.0005 131 ILE   A CD1 
2866 C  CD1 B ILE   A 131 ? 0.2111 0.2191 0.1861 -0.0397 0.0350  -0.0332 131 ILE   A CD1 
2889 N  N   A PHE   A 132 ? 0.1843 0.1542 0.2217 -0.0040 -0.0169 0.0220  132 PHE   A N   
2890 N  N   B PHE   A 132 ? 0.1867 0.1636 0.1783 -0.0051 0.0154  -0.0054 132 PHE   A N   
2891 C  CA  A PHE   A 132 ? 0.1928 0.1574 0.2266 -0.0112 -0.0172 0.0132  132 PHE   A CA  
2892 C  CA  B PHE   A 132 ? 0.1970 0.1702 0.1746 -0.0004 0.0135  -0.0125 132 PHE   A CA  
2893 C  C   A PHE   A 132 ? 0.2134 0.1647 0.2464 -0.0183 -0.0250 0.0267  132 PHE   A C   
2894 C  C   B PHE   A 132 ? 0.2100 0.1791 0.1781 -0.0015 0.0106  -0.0143 132 PHE   A C   
2895 O  O   A PHE   A 132 ? 0.2320 0.1661 0.2601 -0.0147 -0.0317 0.0140  132 PHE   A O   
2896 O  O   B PHE   A 132 ? 0.2184 0.1855 0.1757 -0.0016 0.0124  -0.0265 132 PHE   A O   
2897 C  CB  A PHE   A 132 ? 0.1837 0.1546 0.1954 -0.0100 -0.0211 0.0139  132 PHE   A CB  
2898 C  CB  B PHE   A 132 ? 0.1940 0.1639 0.1645 0.0020  0.0191  -0.0262 132 PHE   A CB  
2899 C  CG  A PHE   A 132 ? 0.1843 0.1542 0.2014 0.0010  -0.0141 0.0247  132 PHE   A CG  
2900 C  CG  B PHE   A 132 ? 0.1942 0.1584 0.1718 0.0047  0.0162  -0.0204 132 PHE   A CG  
2901 C  CD1 A PHE   A 132 ? 0.1820 0.1788 0.2069 0.0033  -0.0081 0.0046  132 PHE   A CD1 
2902 C  CD1 B PHE   A 132 ? 0.1978 0.1727 0.1822 0.0030  0.0203  -0.0236 132 PHE   A CD1 
2903 C  CD2 A PHE   A 132 ? 0.1918 0.1664 0.2221 0.0077  -0.0192 0.0134  132 PHE   A CD2 
2904 C  CD2 B PHE   A 132 ? 0.1941 0.1530 0.1710 0.0088  0.0158  -0.0346 132 PHE   A CD2 
2905 C  CE1 A PHE   A 132 ? 0.1847 0.1888 0.2306 0.0110  -0.0185 0.0017  132 PHE   A CE1 
2906 C  CE1 B PHE   A 132 ? 0.1979 0.1782 0.1847 0.0084  0.0203  -0.0286 132 PHE   A CE1 
2907 C  CE2 A PHE   A 132 ? 0.1895 0.1739 0.2434 0.0138  -0.0164 0.0093  132 PHE   A CE2 
2908 C  CE2 B PHE   A 132 ? 0.1945 0.1640 0.1836 0.0153  0.0254  -0.0320 132 PHE   A CE2 
2909 C  CZ  A PHE   A 132 ? 0.1815 0.1800 0.2397 0.0087  -0.0258 0.0066  132 PHE   A CZ  
2910 C  CZ  B PHE   A 132 ? 0.1920 0.1696 0.1900 0.0129  0.0270  -0.0336 132 PHE   A CZ  
2929 N  N   A GLY   A 133 ? 0.2242 0.1798 0.2465 -0.0125 -0.0405 0.0224  133 GLY   A N   
2930 N  N   B GLY   A 133 ? 0.2133 0.1865 0.1845 -0.0005 -0.0120 0.0006  133 GLY   A N   
2931 C  CA  A GLY   A 133 ? 0.2332 0.1903 0.2541 -0.0129 -0.0385 0.0172  133 GLY   A CA  
2932 C  CA  B GLY   A 133 ? 0.2190 0.1974 0.1970 -0.0012 -0.0139 0.0027  133 GLY   A CA  
2933 C  C   A GLY   A 133 ? 0.2285 0.1955 0.2502 -0.0164 -0.0406 0.0075  133 GLY   A C   
2934 C  C   B GLY   A 133 ? 0.2153 0.2026 0.1993 0.0042  -0.0191 -0.0046 133 GLY   A C   
2935 O  O   A GLY   A 133 ? 0.2437 0.2093 0.2672 -0.0206 -0.0438 -0.0198 133 GLY   A O   
2936 O  O   B GLY   A 133 ? 0.2189 0.2034 0.2003 0.0088  -0.0242 -0.0227 133 GLY   A O   
2943 N  N   A ALA   A 134 ? 0.2125 0.1813 0.2489 -0.0229 -0.0390 0.0082  134 ALA   A N   
2944 N  N   B ALA   A 134 ? 0.2098 0.2051 0.2147 0.0022  -0.0184 0.0011  134 ALA   A N   
2945 C  CA  A ALA   A 134 ? 0.1987 0.1802 0.2635 -0.0243 -0.0354 0.0052  134 ALA   A CA  
2946 C  CA  B ALA   A 134 ? 0.2053 0.2072 0.2305 0.0073  -0.0234 0.0072  134 ALA   A CA  
2947 C  C   A ALA   A 134 ? 0.1996 0.2010 0.2752 -0.0217 -0.0182 0.0123  134 ALA   A C   
2948 C  C   B ALA   A 134 ? 0.2028 0.2090 0.2444 0.0051  -0.0149 0.0127  134 ALA   A C   
2949 O  O   A ALA   A 134 ? 0.2145 0.2111 0.2948 -0.0180 -0.0055 0.0126  134 ALA   A O   
2950 O  O   B ALA   A 134 ? 0.2074 0.2132 0.2520 0.0044  -0.0053 0.0112  134 ALA   A O   
2951 C  CB  A ALA   A 134 ? 0.2056 0.1678 0.2822 -0.0187 -0.0390 -0.0039 134 ALA   A CB  
2952 C  CB  B ALA   A 134 ? 0.2104 0.2069 0.2428 0.0136  -0.0281 0.0046  134 ALA   A CB  
2963 N  N   A ASP   A 135 ? 0.2026 0.2121 0.2831 -0.0278 -0.0178 0.0281  135 ASP   A N   
2964 N  N   B ASP   A 135 ? 0.2073 0.2155 0.2576 -0.0023 -0.0176 0.0199  135 ASP   A N   
2965 C  CA  A ASP   A 135 ? 0.1988 0.2263 0.2955 -0.0392 -0.0282 0.0388  135 ASP   A CA  
2966 C  CA  B ASP   A 135 ? 0.2039 0.2219 0.2744 -0.0046 -0.0207 0.0236  135 ASP   A CA  
2967 C  C   A ASP   A 135 ? 0.1817 0.2106 0.3018 -0.0254 -0.0282 0.0531  135 ASP   A C   
2968 C  C   B ASP   A 135 ? 0.1989 0.2148 0.2721 -0.0003 -0.0186 0.0259  135 ASP   A C   
2969 O  O   A ASP   A 135 ? 0.1797 0.1964 0.3260 -0.0218 -0.0180 0.0572  135 ASP   A O   
2970 O  O   B ASP   A 135 ? 0.1957 0.2038 0.2814 0.0023  -0.0169 0.0326  135 ASP   A O   
2971 C  CB  A ASP   A 135 ? 0.2226 0.2680 0.3191 -0.0633 -0.0417 0.0262  135 ASP   A CB  
2972 C  CB  B ASP   A 135 ? 0.2105 0.2405 0.3014 -0.0114 -0.0259 0.0280  135 ASP   A CB  
2973 C  CG  A ASP   A 135 ? 0.2424 0.3074 0.3428 -0.0748 -0.0569 0.0279  135 ASP   A CG  
2974 C  CG  B ASP   A 135 ? 0.2142 0.2577 0.3316 -0.0095 -0.0270 0.0382  135 ASP   A CG  
2975 O  OD1 A ASP   A 135 ? 0.2411 0.3312 0.3214 -0.0803 -0.0742 0.0463  135 ASP   A OD1 
2976 O  OD1 B ASP   A 135 ? 0.2140 0.2724 0.3393 -0.0121 -0.0274 0.0488  135 ASP   A OD1 
2977 O  OD2 A ASP   A 135 ? 0.2657 0.3278 0.3693 -0.0693 -0.0593 0.0327  135 ASP   A OD2 
2978 O  OD2 B ASP   A 135 ? 0.2156 0.2610 0.3464 0.0010  -0.0275 0.0444  135 ASP   A OD2 
2987 N  N   A PRO   A 136 ? 0.1692 0.2085 0.3009 -0.0073 -0.0189 0.0725  136 PRO   A N   
2988 N  N   B PRO   A 136 ? 0.1996 0.2178 0.2707 0.0022  -0.0115 0.0296  136 PRO   A N   
2989 C  CA  A PRO   A 136 ? 0.1699 0.2016 0.3168 -0.0034 -0.0068 0.0685  136 PRO   A CA  
2990 C  CA  B PRO   A 136 ? 0.1976 0.2218 0.2703 -0.0032 -0.0069 0.0314  136 PRO   A CA  
2991 C  C   A PRO   A 136 ? 0.1473 0.1973 0.3307 -0.0036 -0.0017 0.0625  136 PRO   A C   
2992 C  C   B PRO   A 136 ? 0.1895 0.2190 0.2711 -0.0085 -0.0028 0.0340  136 PRO   A C   
2993 O  O   A PRO   A 136 ? 0.1328 0.1942 0.3479 -0.0026 -0.0024 0.0715  136 PRO   A O   
2994 O  O   B PRO   A 136 ? 0.1858 0.2084 0.2721 -0.0069 -0.0008 0.0327  136 PRO   A O   
2995 C  CB  A PRO   A 136 ? 0.1907 0.2059 0.3245 0.0083  -0.0170 0.0684  136 PRO   A CB  
2996 C  CB  B PRO   A 136 ? 0.2066 0.2268 0.2732 0.0035  -0.0115 0.0306  136 PRO   A CB  
2997 C  CG  A PRO   A 136 ? 0.2049 0.2166 0.3304 0.0177  -0.0107 0.0693  136 PRO   A CG  
2998 C  CG  B PRO   A 136 ? 0.2157 0.2276 0.2749 0.0108  -0.0114 0.0357  136 PRO   A CG  
2999 C  CD  A PRO   A 136 ? 0.1876 0.2164 0.3079 0.0164  -0.0042 0.0881  136 PRO   A CD  
3000 C  CD  B PRO   A 136 ? 0.2088 0.2222 0.2729 0.0116  -0.0063 0.0367  136 PRO   A CD  
3015 N  N   A ILE   A 137 ? 0.1441 0.1939 0.3377 -0.0069 -0.0079 0.0728  137 ILE   A N   
3016 N  N   B ILE   A 137 ? 0.1863 0.2206 0.2753 -0.0074 -0.0083 0.0376  137 ILE   A N   
3017 C  CA  A ILE   A 137 ? 0.1458 0.2044 0.3319 -0.0127 -0.0239 0.0767  137 ILE   A CA  
3018 C  CA  B ILE   A 137 ? 0.1885 0.2302 0.2748 -0.0071 -0.0083 0.0374  137 ILE   A CA  
3019 C  C   A ILE   A 137 ? 0.1526 0.2024 0.3348 -0.0196 -0.0157 0.0600  137 ILE   A C   
3020 C  C   B ILE   A 137 ? 0.1840 0.2268 0.2746 -0.0101 0.0011  0.0362  137 ILE   A C   
3021 O  O   A ILE   A 137 ? 0.1541 0.1830 0.3515 -0.0292 -0.0125 0.0458  137 ILE   A O   
3022 O  O   B ILE   A 137 ? 0.1801 0.2225 0.2866 -0.0146 0.0008  0.0410  137 ILE   A O   
3023 C  CB  A ILE   A 137 ? 0.1578 0.2305 0.3414 -0.0210 -0.0316 0.0660  137 ILE   A CB  
3024 C  CB  B ILE   A 137 ? 0.2008 0.2440 0.2858 -0.0077 -0.0163 0.0333  137 ILE   A CB  
3025 C  CG1 A ILE   A 137 ? 0.1722 0.2663 0.3681 -0.0051 -0.0305 0.0630  137 ILE   A CG1 
3026 C  CG1 B ILE   A 137 ? 0.2105 0.2606 0.3047 0.0003  -0.0218 0.0346  137 ILE   A CG1 
3027 C  CG2 A ILE   A 137 ? 0.1722 0.2281 0.3458 -0.0308 -0.0392 0.0518  137 ILE   A CG2 
3028 C  CG2 B ILE   A 137 ? 0.2104 0.2449 0.2853 -0.0107 -0.0196 0.0305  137 ILE   A CG2 
3029 C  CD1 A ILE   A 137 ? 0.1954 0.2888 0.3863 0.0013  -0.0271 0.0536  137 ILE   A CD1 
3030 C  CD1 B ILE   A 137 ? 0.2210 0.2706 0.3179 0.0030  -0.0230 0.0342  137 ILE   A CD1 
3053 N  N   A HIS   A 138 ? 0.1537 0.2210 0.3396 -0.0112 0.0042  0.0497  138 HIS   A N   
3054 N  N   B HIS   A 138 ? 0.1776 0.2275 0.2816 -0.0099 0.0096  0.0285  138 HIS   A N   
3055 C  CA  A HIS   A 138 ? 0.1590 0.2300 0.3221 -0.0133 0.0035  0.0453  138 HIS   A CA  
3056 C  CA  B HIS   A 138 ? 0.1685 0.2212 0.2787 -0.0114 0.0061  0.0239  138 HIS   A CA  
3057 C  C   A HIS   A 138 ? 0.1539 0.2188 0.3235 -0.0142 -0.0038 0.0463  138 HIS   A C   
3058 C  C   B HIS   A 138 ? 0.1577 0.2132 0.2921 -0.0111 0.0055  0.0382  138 HIS   A C   
3059 O  O   A HIS   A 138 ? 0.1618 0.2207 0.3364 -0.0078 0.0015  0.0476  138 HIS   A O   
3060 O  O   B HIS   A 138 ? 0.1625 0.2125 0.2950 -0.0086 0.0080  0.0448  138 HIS   A O   
3061 C  CB  A HIS   A 138 ? 0.1920 0.2479 0.3252 -0.0177 -0.0128 0.0295  138 HIS   A CB  
3062 C  CB  B HIS   A 138 ? 0.1706 0.2210 0.2736 -0.0136 0.0014  0.0002  138 HIS   A CB  
3063 C  CG  A HIS   A 138 ? 0.2167 0.2605 0.3253 -0.0289 -0.0183 0.0129  138 HIS   A CG  
3064 C  CG  B HIS   A 138 ? 0.1730 0.2184 0.2724 -0.0206 -0.0067 -0.0263 138 HIS   A CG  
3065 N  ND1 A HIS   A 138 ? 0.2286 0.2708 0.3293 -0.0322 -0.0189 0.0010  138 HIS   A ND1 
3066 N  ND1 B HIS   A 138 ? 0.1772 0.2230 0.2763 -0.0197 -0.0073 -0.0440 138 HIS   A ND1 
3067 C  CD2 A HIS   A 138 ? 0.2252 0.2684 0.3230 -0.0292 -0.0179 0.0176  138 HIS   A CD2 
3068 C  CD2 B HIS   A 138 ? 0.1665 0.2166 0.2673 -0.0213 -0.0064 -0.0322 138 HIS   A CD2 
3069 C  CE1 A HIS   A 138 ? 0.2323 0.2740 0.3300 -0.0318 -0.0179 0.0065  138 HIS   A CE1 
3070 C  CE1 B HIS   A 138 ? 0.1752 0.2239 0.2789 -0.0201 -0.0003 -0.0443 138 HIS   A CE1 
3071 N  NE2 A HIS   A 138 ? 0.2318 0.2728 0.3218 -0.0323 -0.0118 0.0097  138 HIS   A NE2 
3072 N  NE2 B HIS   A 138 ? 0.1682 0.2199 0.2739 -0.0226 -0.0007 -0.0461 138 HIS   A NE2 
3087 N  N   . SER   A 139 ? 0.1439 0.2078 0.3169 -0.0061 0.0032  0.0495  139 SER   A N   
3088 C  CA  . SER   A 139 ? 0.1491 0.1967 0.3350 -0.0004 0.0129  0.0615  139 SER   A CA  
3089 C  C   . SER   A 139 ? 0.1430 0.1870 0.3420 -0.0033 0.0033  0.0554  139 SER   A C   
3090 O  O   . SER   A 139 ? 0.1400 0.1767 0.3626 -0.0150 -0.0040 0.0674  139 SER   A O   
3091 C  CB  . SER   A 139 ? 0.1514 0.1949 0.3258 -0.0123 0.0029  0.0610  139 SER   A CB  
3092 O  OG  . SER   A 139 ? 0.1573 0.1929 0.3247 -0.0179 -0.0134 0.0677  139 SER   A OG  
3099 N  N   . LEU   A 140 ? 0.1418 0.1999 0.3279 -0.0025 0.0134  0.0639  140 LEU   A N   
3100 C  CA  . LEU   A 140 ? 0.1395 0.1918 0.3372 0.0006  0.0048  0.0662  140 LEU   A CA  
3101 C  C   . LEU   A 140 ? 0.1304 0.1977 0.3572 -0.0054 0.0073  0.0573  140 LEU   A C   
3102 O  O   . LEU   A 140 ? 0.1448 0.1893 0.3790 -0.0080 0.0015  0.0584  140 LEU   A O   
3103 C  CB  . LEU   A 140 ? 0.1481 0.2026 0.3416 -0.0048 0.0166  0.0639  140 LEU   A CB  
3104 C  CG  . LEU   A 140 ? 0.1488 0.2207 0.3416 -0.0177 0.0135  0.0756  140 LEU   A CG  
3105 C  CD1 . LEU   A 140 ? 0.1580 0.2195 0.3625 -0.0181 0.0064  0.0771  140 LEU   A CD1 
3106 C  CD2 . LEU   A 140 ? 0.1478 0.2353 0.3454 -0.0144 0.0117  0.0701  140 LEU   A CD2 
3118 N  N   . ARG   A 141 ? 0.1492 0.2006 0.3499 -0.0144 0.0053  0.0470  141 ARG   A N   
3119 C  CA  . ARG   A 141 ? 0.1638 0.2163 0.3455 -0.0233 -0.0112 0.0372  141 ARG   A CA  
3120 C  C   . ARG   A 141 ? 0.1584 0.1976 0.3374 -0.0185 -0.0109 0.0412  141 ARG   A C   
3121 O  O   . ARG   A 141 ? 0.1498 0.1976 0.3560 -0.0228 0.0024  0.0395  141 ARG   A O   
3122 C  CB  . ARG   A 141 ? 0.1807 0.2434 0.3509 -0.0339 -0.0200 0.0200  141 ARG   A CB  
3123 C  CG  . ARG   A 141 ? 0.2202 0.2756 0.3716 -0.0477 -0.0097 0.0159  141 ARG   A CG  
3124 C  CD  . ARG   A 141 ? 0.2595 0.3033 0.3967 -0.0606 0.0024  0.0220  141 ARG   A CD  
3125 N  NE  . ARG   A 141 ? 0.2471 0.3241 0.4217 -0.0594 -0.0051 0.0242  141 ARG   A NE  
3126 C  CZ  . ARG   A 141 ? 0.2382 0.3398 0.4218 -0.0737 -0.0168 0.0249  141 ARG   A CZ  
3127 N  NH1 . ARG   A 141 ? 0.2186 0.3423 0.4144 -0.0935 -0.0106 0.0024  141 ARG   A NH1 
3128 N  NH2 . ARG   A 141 ? 0.2416 0.3582 0.4450 -0.0468 -0.0345 0.0277  141 ARG   A NH2 
3142 N  N   . VAL   A 142 ? 0.1472 0.1831 0.3314 -0.0095 -0.0035 0.0255  142 VAL   A N   
3143 C  CA  . VAL   A 142 ? 0.1538 0.1761 0.3203 -0.0113 0.0185  0.0236  142 VAL   A CA  
3144 C  C   . VAL   A 142 ? 0.1342 0.1756 0.3196 -0.0191 0.0085  0.0317  142 VAL   A C   
3145 O  O   . VAL   A 142 ? 0.1471 0.1698 0.3492 -0.0016 0.0040  0.0293  142 VAL   A O   
3146 C  CB  . VAL   A 142 ? 0.1608 0.1991 0.3172 -0.0138 0.0196  0.0287  142 VAL   A CB  
3147 C  CG1 . VAL   A 142 ? 0.1560 0.1810 0.3200 -0.0198 0.0221  0.0196  142 VAL   A CG1 
3148 C  CG2 . VAL   A 142 ? 0.1722 0.2131 0.3247 -0.0006 0.0220  0.0301  142 VAL   A CG2 
3158 N  N   . CYS   A 143 ? 0.1459 0.1756 0.3129 -0.0199 0.0081  0.0456  143 CYS   A N   
3159 C  CA  . CYS   A 143 ? 0.1455 0.1738 0.3325 -0.0135 0.0180  0.0556  143 CYS   A CA  
3160 C  C   . CYS   A 143 ? 0.1410 0.1657 0.3481 -0.0110 0.0112  0.0571  143 CYS   A C   
3161 O  O   . CYS   A 143 ? 0.1402 0.1680 0.3544 -0.0094 0.0053  0.0461  143 CYS   A O   
3162 C  CB  . CYS   A 143 ? 0.1545 0.1807 0.3383 -0.0050 0.0168  0.0722  143 CYS   A CB  
3163 S  SG  . CYS   A 143 ? 0.1677 0.1815 0.3190 0.0024  0.0143  0.0413  143 CYS   A SG  
3169 N  N   . VAL   A 144 ? 0.1453 0.1745 0.3773 -0.0084 0.0116  0.0618  144 VAL   A N   
3170 C  CA  . VAL   A 144 ? 0.1506 0.1853 0.4003 -0.0084 0.0220  0.0527  144 VAL   A CA  
3171 C  C   . VAL   A 144 ? 0.1521 0.1749 0.3820 -0.0188 -0.0071 0.0403  144 VAL   A C   
3172 O  O   . VAL   A 144 ? 0.1707 0.1732 0.3885 -0.0094 -0.0136 0.0601  144 VAL   A O   
3173 C  CB  . VAL   A 144 ? 0.1718 0.2092 0.4364 -0.0053 0.0462  0.0559  144 VAL   A CB  
3174 C  CG1 . VAL   A 144 ? 0.1835 0.2257 0.4664 -0.0143 0.0424  0.0525  144 VAL   A CG1 
3175 C  CG2 . VAL   A 144 ? 0.1543 0.2195 0.4337 -0.0111 0.0544  0.0719  144 VAL   A CG2 
3185 N  N   . ASP   A 145 ? 0.1453 0.1744 0.3877 -0.0243 -0.0015 0.0314  145 ASP   A N   
3186 C  CA  . ASP   A 145 ? 0.1681 0.1857 0.3930 -0.0272 -0.0024 0.0285  145 ASP   A CA  
3187 C  C   . ASP   A 145 ? 0.1580 0.1743 0.3927 -0.0194 -0.0026 0.0171  145 ASP   A C   
3188 O  O   . ASP   A 145 ? 0.1786 0.1726 0.4275 -0.0162 -0.0156 -0.0026 145 ASP   A O   
3189 C  CB  . ASP   A 145 ? 0.1837 0.2180 0.4050 -0.0316 -0.0172 0.0303  145 ASP   A CB  
3190 C  CG  . ASP   A 145 ? 0.2033 0.2570 0.4266 -0.0535 -0.0156 0.0429  145 ASP   A CG  
3191 O  OD1 . ASP   A 145 ? 0.1903 0.2737 0.4422 -0.0668 -0.0133 0.0479  145 ASP   A OD1 
3192 O  OD2 . ASP   A 145 ? 0.2228 0.2796 0.4398 -0.0713 -0.0367 0.0349  145 ASP   A OD2 
3197 N  N   . THR   A 146 ? 0.1512 0.1627 0.3593 -0.0181 -0.0022 0.0182  146 THR   A N   
3198 C  CA  . THR   A 146 ? 0.1504 0.1478 0.3395 -0.0093 0.0076  0.0183  146 THR   A CA  
3199 C  C   . THR   A 146 ? 0.1453 0.1443 0.3601 0.0005  0.0167  0.0285  146 THR   A C   
3200 O  O   . THR   A 146 ? 0.1536 0.1619 0.3774 0.0081  0.0068  0.0253  146 THR   A O   
3201 C  CB  . THR   A 146 ? 0.1515 0.1570 0.3408 -0.0046 0.0073  0.0269  146 THR   A CB  
3202 O  OG1 . THR   A 146 ? 0.1502 0.1736 0.3597 0.0003  0.0001  0.0268  146 THR   A OG1 
3203 C  CG2 . THR   A 146 ? 0.1411 0.1581 0.3585 -0.0124 0.0046  0.0234  146 THR   A CG2 
3211 N  N   . VAL   A 147 ? 0.1428 0.1482 0.3589 -0.0032 0.0138  0.0232  147 VAL   A N   
3212 C  CA  . VAL   A 147 ? 0.1452 0.1523 0.3535 -0.0115 0.0373  0.0317  147 VAL   A CA  
3213 C  C   . VAL   A 147 ? 0.1496 0.1524 0.3628 -0.0148 0.0282  0.0536  147 VAL   A C   
3214 O  O   . VAL   A 147 ? 0.1505 0.1607 0.3727 -0.0151 0.0123  0.0536  147 VAL   A O   
3215 C  CB  . VAL   A 147 ? 0.1626 0.1533 0.3323 -0.0125 0.0333  0.0288  147 VAL   A CB  
3216 C  CG1 . VAL   A 147 ? 0.1935 0.1631 0.3251 -0.0040 0.0222  0.0393  147 VAL   A CG1 
3217 C  CG2 . VAL   A 147 ? 0.1709 0.1520 0.3349 -0.0056 0.0211  0.0274  147 VAL   A CG2 
3227 N  N   . ARG   A 148 ? 0.1492 0.1627 0.3780 -0.0137 0.0211  0.0679  148 ARG   A N   
3228 C  CA  . ARG   A 148 ? 0.1542 0.1636 0.3738 -0.0152 0.0010  0.0708  148 ARG   A CA  
3229 C  C   . ARG   A 148 ? 0.1569 0.1616 0.3518 -0.0182 0.0091  0.0840  148 ARG   A C   
3230 O  O   . ARG   A 148 ? 0.1864 0.1773 0.3820 -0.0236 0.0159  0.0747  148 ARG   A O   
3231 C  CB  . ARG   A 148 ? 0.1577 0.1639 0.3752 -0.0099 0.0071  0.0592  148 ARG   A CB  
3232 C  CG  . ARG   A 148 ? 0.1811 0.1718 0.3844 -0.0059 0.0338  0.0534  148 ARG   A CG  
3233 C  CD  . ARG   A 148 ? 0.1960 0.1662 0.4090 -0.0076 0.0569  0.0687  148 ARG   A CD  
3234 N  NE  . ARG   A 148 ? 0.1818 0.1685 0.4214 0.0027  0.0566  0.0732  148 ARG   A NE  
3235 C  CZ  . ARG   A 148 ? 0.1841 0.1529 0.3948 0.0036  0.0510  0.0708  148 ARG   A CZ  
3236 N  NH1 . ARG   A 148 ? 0.1942 0.1512 0.4068 -0.0115 0.0541  0.0478  148 ARG   A NH1 
3237 N  NH2 . ARG   A 148 ? 0.1754 0.1721 0.3948 0.0108  0.0498  0.0681  148 ARG   A NH2 
3251 N  N   . THR   A 149 ? 0.1584 0.1756 0.3509 -0.0115 0.0053  0.0741  149 THR   A N   
3252 C  CA  . THR   A 149 ? 0.1637 0.1841 0.3435 -0.0121 0.0012  0.0676  149 THR   A CA  
3253 C  C   . THR   A 149 ? 0.1625 0.1877 0.3344 -0.0209 0.0183  0.0761  149 THR   A C   
3254 O  O   . THR   A 149 ? 0.1617 0.1929 0.3302 -0.0209 0.0086  0.0687  149 THR   A O   
3255 C  CB  . THR   A 149 ? 0.1683 0.1914 0.3534 -0.0193 0.0116  0.0605  149 THR   A CB  
3256 O  OG1 . THR   A 149 ? 0.1668 0.1812 0.3706 -0.0234 0.0225  0.0644  149 THR   A OG1 
3257 C  CG2 . THR   A 149 ? 0.1625 0.1969 0.3515 -0.0216 0.0013  0.0416  149 THR   A CG2 
3265 N  N   . ASN   A 150 ? 0.1615 0.1832 0.3219 -0.0142 0.0093  0.0794  150 ASN   A N   
3266 C  CA  . ASN   A 150 ? 0.1826 0.2022 0.3197 -0.0213 0.0175  0.0665  150 ASN   A CA  
3267 C  C   . ASN   A 150 ? 0.1557 0.1939 0.3233 -0.0276 0.0031  0.0648  150 ASN   A C   
3268 O  O   . ASN   A 150 ? 0.1604 0.2038 0.3518 -0.0216 -0.0043 0.0602  150 ASN   A O   
3269 C  CB  . ASN   A 150 ? 0.2363 0.2303 0.3310 -0.0315 0.0427  0.0799  150 ASN   A CB  
3270 C  CG  . ASN   A 150 ? 0.3001 0.2740 0.3868 -0.0260 0.0061  0.0803  150 ASN   A CG  
3271 O  OD1 . ASN   A 150 ? 0.3235 0.2799 0.4041 -0.0329 -0.0014 0.0975  150 ASN   A OD1 
3272 N  ND2 . ASN   A 150 ? 0.3393 0.3045 0.4180 -0.0249 -0.0057 0.0673  150 ASN   A ND2 
3279 N  N   . VAL   A 151 ? 0.1640 0.1761 0.3353 -0.0241 -0.0025 0.0717  151 VAL   A N   
3280 C  CA  . VAL   A 151 ? 0.1704 0.1740 0.3213 -0.0252 0.0091  0.0596  151 VAL   A CA  
3281 C  C   . VAL   A 151 ? 0.1626 0.1710 0.3198 -0.0274 0.0102  0.0711  151 VAL   A C   
3282 O  O   . VAL   A 151 ? 0.1716 0.1819 0.3655 -0.0298 0.0085  0.0701  151 VAL   A O   
3283 C  CB  . VAL   A 151 ? 0.1984 0.1869 0.3087 -0.0191 0.0122  0.0517  151 VAL   A CB  
3284 C  CG1 . VAL   A 151 ? 0.1909 0.2157 0.3182 -0.0122 0.0047  0.0335  151 VAL   A CG1 
3285 C  CG2 . VAL   A 151 ? 0.2123 0.1848 0.3035 -0.0070 0.0160  0.0468  151 VAL   A CG2 
3295 N  N   A TYR   A 152 ? 0.1610 0.1667 0.3176 -0.0237 0.0066  0.0714  152 TYR   A N   
3296 N  N   B TYR   A 152 ? 0.1680 0.1780 0.2840 -0.0215 0.0042  0.0621  152 TYR   A N   
3297 C  CA  A TYR   A 152 ? 0.1634 0.1807 0.2891 -0.0186 0.0115  0.0642  152 TYR   A CA  
3298 C  CA  B TYR   A 152 ? 0.1764 0.1938 0.2444 -0.0156 0.0004  0.0455  152 TYR   A CA  
3299 C  C   A TYR   A 152 ? 0.1596 0.1648 0.2779 -0.0230 0.0229  0.0584  152 TYR   A C   
3300 C  C   B TYR   A 152 ? 0.1752 0.1868 0.2197 -0.0216 0.0072  0.0407  152 TYR   A C   
3301 O  O   A TYR   A 152 ? 0.1635 0.1607 0.3129 -0.0301 0.0208  0.0479  152 TYR   A O   
3302 O  O   B TYR   A 152 ? 0.1765 0.1847 0.2377 -0.0260 -0.0029 0.0402  152 TYR   A O   
3303 C  CB  A TYR   A 152 ? 0.1715 0.1899 0.2804 -0.0212 0.0199  0.0821  152 TYR   A CB  
3304 C  CB  B TYR   A 152 ? 0.1885 0.2055 0.2425 -0.0080 0.0016  0.0433  152 TYR   A CB  
3305 C  CG  A TYR   A 152 ? 0.1806 0.2070 0.2734 -0.0300 0.0248  0.0848  152 TYR   A CG  
3306 C  CG  B TYR   A 152 ? 0.2059 0.2146 0.2441 -0.0141 0.0096  0.0455  152 TYR   A CG  
3307 C  CD1 A TYR   A 152 ? 0.1852 0.2144 0.2875 -0.0282 0.0311  0.0834  152 TYR   A CD1 
3308 C  CD1 B TYR   A 152 ? 0.2104 0.2122 0.2442 -0.0228 0.0255  0.0555  152 TYR   A CD1 
3309 C  CD2 A TYR   A 152 ? 0.1775 0.2196 0.2773 -0.0361 0.0226  0.0662  152 TYR   A CD2 
3310 C  CD2 B TYR   A 152 ? 0.2079 0.2162 0.2468 -0.0234 0.0084  0.0358  152 TYR   A CD2 
3311 C  CE1 A TYR   A 152 ? 0.1948 0.2255 0.2857 -0.0265 0.0279  0.0948  152 TYR   A CE1 
3312 C  CE1 B TYR   A 152 ? 0.2201 0.2103 0.2530 -0.0341 0.0211  0.0567  152 TYR   A CE1 
3313 C  CE2 A TYR   A 152 ? 0.1890 0.2317 0.2749 -0.0296 0.0436  0.0774  152 TYR   A CE2 
3314 C  CE2 B TYR   A 152 ? 0.2193 0.2174 0.2562 -0.0342 0.0149  0.0409  152 TYR   A CE2 
3315 C  CZ  A TYR   A 152 ? 0.2003 0.2379 0.2837 -0.0240 0.0367  0.0985  152 TYR   A CZ  
3316 C  CZ  B TYR   A 152 ? 0.2252 0.2115 0.2657 -0.0472 0.0166  0.0501  152 TYR   A CZ  
3317 O  OH  A TYR   A 152 ? 0.2142 0.2633 0.3151 -0.0141 0.0396  0.1122  152 TYR   A OH  
3318 O  OH  B TYR   A 152 ? 0.2361 0.2197 0.2862 -0.0669 0.0197  0.0530  152 TYR   A OH  
3337 N  N   A LEU   A 153 ? 0.1563 0.1602 0.2690 -0.0258 0.0296  0.0447  153 LEU   A N   
3338 N  N   B LEU   A 153 ? 0.1750 0.1810 0.2021 -0.0205 0.0176  0.0306  153 LEU   A N   
3339 C  CA  A LEU   A 153 ? 0.1507 0.1512 0.2688 -0.0060 0.0205  0.0363  153 LEU   A CA  
3340 C  CA  B LEU   A 153 ? 0.1687 0.1711 0.1763 -0.0033 0.0183  0.0044  153 LEU   A CA  
3341 C  C   A LEU   A 153 ? 0.1478 0.1470 0.2764 -0.0121 0.0367  0.0276  153 LEU   A C   
3342 C  C   B LEU   A 153 ? 0.1728 0.1808 0.1758 0.0028  0.0203  0.0120  153 LEU   A C   
3343 O  O   A LEU   A 153 ? 0.1557 0.1577 0.2832 -0.0191 0.0479  0.0186  153 LEU   A O   
3344 O  O   B LEU   A 153 ? 0.1728 0.1931 0.1701 0.0033  0.0184  0.0162  153 LEU   A O   
3345 C  CB  A LEU   A 153 ? 0.1514 0.1385 0.2669 -0.0124 0.0132  0.0260  153 LEU   A CB  
3346 C  CB  B LEU   A 153 ? 0.1613 0.1669 0.1711 -0.0003 0.0103  -0.0087 153 LEU   A CB  
3347 C  CG  A LEU   A 153 ? 0.1487 0.1511 0.2574 -0.0151 0.0278  0.0181  153 LEU   A CG  
3348 C  CG  B LEU   A 153 ? 0.1625 0.1651 0.1664 0.0037  0.0063  -0.0059 153 LEU   A CG  
3349 C  CD1 A LEU   A 153 ? 0.1487 0.1446 0.2652 -0.0020 0.0249  0.0174  153 LEU   A CD1 
3350 C  CD1 B LEU   A 153 ? 0.1638 0.1601 0.1703 0.0183  0.0075  -0.0042 153 LEU   A CD1 
3351 C  CD2 A LEU   A 153 ? 0.1609 0.1695 0.2413 -0.0210 0.0228  0.0009  153 LEU   A CD2 
3352 C  CD2 B LEU   A 153 ? 0.1688 0.1744 0.1624 -0.0022 0.0014  -0.0161 153 LEU   A CD2 
3375 N  N   A ALA   A 154 ? 0.1431 0.1476 0.2907 -0.0099 0.0423  0.0251  154 ALA   A N   
3376 N  N   B ALA   A 154 ? 0.1737 0.1824 0.2044 0.0050  0.0391  0.0218  154 ALA   A N   
3377 C  CA  A ALA   A 154 ? 0.1578 0.1589 0.2959 0.0014  0.0493  0.0328  154 ALA   A CA  
3378 C  CA  B ALA   A 154 ? 0.1727 0.1900 0.2239 0.0012  0.0489  0.0263  154 ALA   A CA  
3379 C  C   A ALA   A 154 ? 0.1669 0.1685 0.3166 0.0112  0.0447  0.0527  154 ALA   A C   
3380 C  C   B ALA   A 154 ? 0.1791 0.1974 0.2304 -0.0081 0.0434  0.0399  154 ALA   A C   
3381 O  O   A ALA   A 154 ? 0.1742 0.1624 0.3224 0.0108  0.0388  0.0490  154 ALA   A O   
3382 O  O   B ALA   A 154 ? 0.1824 0.1931 0.2245 -0.0133 0.0376  0.0425  154 ALA   A O   
3383 C  CB  A ALA   A 154 ? 0.1674 0.1580 0.2926 0.0147  0.0553  0.0253  154 ALA   A CB  
3384 C  CB  B ALA   A 154 ? 0.1644 0.1880 0.2414 0.0008  0.0507  0.0139  154 ALA   A CB  
3395 N  N   A VAL   A 155 ? 0.1745 0.1852 0.3436 0.0290  0.0357  0.0883  155 VAL   A N   
3396 N  N   B VAL   A 155 ? 0.1845 0.2067 0.2613 -0.0082 0.0339  0.0521  155 VAL   A N   
3397 C  CA  A VAL   A 155 ? 0.1865 0.2076 0.3490 0.0363  0.0276  0.0986  155 VAL   A CA  
3398 C  CA  B VAL   A 155 ? 0.1890 0.2109 0.2675 -0.0133 0.0295  0.0530  155 VAL   A CA  
3399 C  C   A VAL   A 155 ? 0.1916 0.2155 0.3729 0.0511  0.0279  0.1019  155 VAL   A C   
3400 C  C   B VAL   A 155 ? 0.1970 0.2136 0.2775 -0.0265 0.0312  0.0500  155 VAL   A C   
3401 O  O   A VAL   A 155 ? 0.1944 0.2228 0.4126 0.0644  0.0274  0.0806  155 VAL   A O   
3402 O  O   B VAL   A 155 ? 0.1956 0.2122 0.2892 -0.0288 0.0423  0.0462  155 VAL   A O   
3403 C  CB  A VAL   A 155 ? 0.1912 0.2201 0.3279 0.0432  0.0153  0.0910  155 VAL   A CB  
3404 C  CB  B VAL   A 155 ? 0.1861 0.2124 0.2680 0.0046  0.0227  0.0442  155 VAL   A CB  
3405 C  CG1 A VAL   A 155 ? 0.2079 0.2265 0.3340 0.0481  0.0083  0.0918  155 VAL   A CG1 
3406 C  CG1 B VAL   A 155 ? 0.1856 0.2122 0.2708 0.0126  0.0219  0.0340  155 VAL   A CG1 
3407 C  CG2 A VAL   A 155 ? 0.1928 0.2279 0.3229 0.0512  -0.0039 0.0807  155 VAL   A CG2 
3408 C  CG2 B VAL   A 155 ? 0.1841 0.2179 0.2718 0.0182  0.0169  0.0405  155 VAL   A CG2 
3427 N  N   A PHE   A 156 ? 0.2022 0.2172 0.3729 0.0559  0.0473  0.1124  156 PHE   A N   
3428 N  N   B PHE   A 156 ? 0.2127 0.2198 0.2935 -0.0332 0.0239  0.0469  156 PHE   A N   
3429 C  CA  A PHE   A 156 ? 0.2323 0.2190 0.3817 0.0584  0.0437  0.1161  156 PHE   A CA  
3430 C  CA  B PHE   A 156 ? 0.2286 0.2260 0.3023 -0.0309 0.0105  0.0369  156 PHE   A CA  
3431 C  C   A PHE   A 156 ? 0.2400 0.2258 0.3743 0.0704  0.0462  0.1181  156 PHE   A C   
3432 C  C   B PHE   A 156 ? 0.2377 0.2297 0.3135 -0.0261 0.0179  0.0368  156 PHE   A C   
3433 O  O   A PHE   A 156 ? 0.2511 0.2463 0.3929 0.0556  0.0547  0.0985  156 PHE   A O   
3434 O  O   B PHE   A 156 ? 0.2409 0.2407 0.3232 -0.0182 0.0309  0.0532  156 PHE   A O   
3435 C  CB  A PHE   A 156 ? 0.2625 0.2197 0.3821 0.0518  0.0294  0.1178  156 PHE   A CB  
3436 C  CB  B PHE   A 156 ? 0.2389 0.2302 0.3075 -0.0248 -0.0082 0.0241  156 PHE   A CB  
3437 C  CG  A PHE   A 156 ? 0.2899 0.2306 0.3980 0.0515  0.0028  0.1030  156 PHE   A CG  
3438 C  CG  B PHE   A 156 ? 0.2500 0.2403 0.3208 -0.0112 -0.0262 0.0128  156 PHE   A CG  
3439 C  CD1 A PHE   A 156 ? 0.3041 0.2392 0.3965 0.0489  0.0069  0.0943  156 PHE   A CD1 
3440 C  CD1 B PHE   A 156 ? 0.2550 0.2484 0.3227 0.0028  -0.0312 0.0089  156 PHE   A CD1 
3441 C  CD2 A PHE   A 156 ? 0.3044 0.2366 0.4038 0.0577  -0.0151 0.1109  156 PHE   A CD2 
3442 C  CD2 B PHE   A 156 ? 0.2571 0.2454 0.3306 -0.0057 -0.0270 0.0092  156 PHE   A CD2 
3443 C  CE1 A PHE   A 156 ? 0.3178 0.2473 0.4115 0.0487  0.0107  0.0893  156 PHE   A CE1 
3444 C  CE1 B PHE   A 156 ? 0.2564 0.2536 0.3266 0.0066  -0.0267 0.0017  156 PHE   A CE1 
3445 C  CE2 A PHE   A 156 ? 0.3243 0.2484 0.4083 0.0566  -0.0090 0.0957  156 PHE   A CE2 
3446 C  CE2 B PHE   A 156 ? 0.2597 0.2500 0.3337 -0.0032 -0.0302 0.0037  156 PHE   A CE2 
3447 C  CZ  A PHE   A 156 ? 0.3284 0.2538 0.4158 0.0561  0.0064  0.0794  156 PHE   A CZ  
3448 C  CZ  B PHE   A 156 ? 0.2603 0.2540 0.3330 0.0054  -0.0266 -0.0013 156 PHE   A CZ  
3467 N  N   A ASP   A 157 ? 0.2466 0.2263 0.3570 0.0652  0.0451  0.1325  157 ASP   A N   
3468 N  N   B ASP   A 157 ? 0.2466 0.2292 0.3144 -0.0399 0.0084  0.0271  157 ASP   A N   
3469 C  CA  A ASP   A 157 ? 0.2590 0.2447 0.3619 0.0662  0.0400  0.1382  157 ASP   A CA  
3470 C  CA  B ASP   A 157 ? 0.2535 0.2304 0.3023 -0.0476 0.0027  0.0022  157 ASP   A CA  
3471 C  C   A ASP   A 157 ? 0.2259 0.2615 0.3758 0.0747  0.0397  0.1451  157 ASP   A C   
3472 C  C   B ASP   A 157 ? 0.2399 0.2085 0.2959 -0.0582 0.0056  -0.0211 157 ASP   A C   
3473 O  O   A ASP   A 157 ? 0.2108 0.2667 0.3852 0.0733  0.0458  0.1431  157 ASP   A O   
3474 O  O   B ASP   A 157 ? 0.2249 0.1980 0.2976 -0.0597 0.0109  -0.0303 157 ASP   A O   
3475 C  CB  A ASP   A 157 ? 0.2929 0.2594 0.3725 0.0687  0.0457  0.1092  157 ASP   A CB  
3476 C  CB  B ASP   A 157 ? 0.2682 0.2521 0.3083 -0.0421 0.0070  -0.0019 157 ASP   A CB  
3477 C  CG  A ASP   A 157 ? 0.3177 0.2647 0.3881 0.0838  0.0243  0.1096  157 ASP   A CG  
3478 C  CG  B ASP   A 157 ? 0.2776 0.2707 0.3176 -0.0343 -0.0018 -0.0107 157 ASP   A CG  
3479 O  OD1 A ASP   A 157 ? 0.3517 0.2762 0.4088 0.0799  0.0035  0.1031  157 ASP   A OD1 
3480 O  OD1 B ASP   A 157 ? 0.2781 0.2911 0.3324 -0.0286 -0.0037 -0.0155 157 ASP   A OD1 
3481 O  OD2 A ASP   A 157 ? 0.3042 0.2611 0.4014 0.0845  0.0343  0.1231  157 ASP   A OD2 
3482 O  OD2 B ASP   A 157 ? 0.2857 0.2731 0.3147 -0.0305 0.0018  -0.0113 157 ASP   A OD2 
3491 N  N   A LYS   A 158 ? 0.2267 0.2837 0.4005 0.0755  0.0410  0.1365  158 LYS   A N   
3492 N  N   B LYS   A 158 ? 0.2458 0.2078 0.3059 -0.0598 0.0018  -0.0273 158 LYS   A N   
3493 C  CA  A LYS   A 158 ? 0.2221 0.3132 0.4106 0.0733  0.0571  0.1246  158 LYS   A CA  
3494 C  CA  B LYS   A 158 ? 0.2528 0.2074 0.3121 -0.0574 0.0170  -0.0184 158 LYS   A CA  
3495 C  C   A LYS   A 158 ? 0.1942 0.3212 0.4073 0.0778  0.0486  0.1395  158 LYS   A C   
3496 C  C   B LYS   A 158 ? 0.2359 0.1917 0.3106 -0.0671 0.0107  -0.0123 158 LYS   A C   
3497 O  O   A LYS   A 158 ? 0.1842 0.3180 0.4128 0.0712  0.0693  0.1422  158 LYS   A O   
3498 O  O   B LYS   A 158 ? 0.2357 0.1737 0.3172 -0.0707 0.0192  -0.0047 158 LYS   A O   
3499 C  CB  A LYS   A 158 ? 0.2458 0.3293 0.4306 0.0707  0.0878  0.1196  158 LYS   A CB  
3500 C  CB  B LYS   A 158 ? 0.2730 0.2282 0.3369 -0.0446 0.0274  -0.0130 158 LYS   A CB  
3501 C  CG  A LYS   A 158 ? 0.2647 0.3471 0.4596 0.0664  0.1093  0.1139  158 LYS   A CG  
3502 C  CG  B LYS   A 158 ? 0.2913 0.2477 0.3623 -0.0367 0.0392  -0.0087 158 LYS   A CG  
3503 C  CD  A LYS   A 158 ? 0.2735 0.3654 0.4807 0.0636  0.1283  0.1143  158 LYS   A CD  
3504 C  CD  B LYS   A 158 ? 0.3016 0.2632 0.3863 -0.0339 0.0547  -0.0062 158 LYS   A CD  
3505 C  CE  A LYS   A 158 ? 0.2829 0.3766 0.5066 0.0565  0.1360  0.1215  158 LYS   A CE  
3506 C  CE  B LYS   A 158 ? 0.3122 0.2728 0.4068 -0.0366 0.0661  -0.0062 158 LYS   A CE  
3507 N  NZ  A LYS   A 158 ? 0.2850 0.3807 0.5203 0.0559  0.1394  0.1275  158 LYS   A NZ  
3508 N  NZ  B LYS   A 158 ? 0.3162 0.2784 0.4183 -0.0330 0.0727  -0.0077 158 LYS   A NZ  
3535 N  N   A ASN   A 159 ? 0.1912 0.3303 0.4276 0.0789  0.0234  0.1475  159 ASN   A N   
3536 N  N   B ASN   A 159 ? 0.2229 0.2052 0.3091 -0.0718 -0.0069 0.0009  159 ASN   A N   
3537 C  CA  A ASN   A 159 ? 0.1981 0.3364 0.4303 0.0659  0.0078  0.1564  159 ASN   A CA  
3538 C  CA  B ASN   A 159 ? 0.2170 0.2273 0.3240 -0.0513 -0.0158 0.0288  159 ASN   A CA  
3539 C  C   A ASN   A 159 ? 0.1822 0.3320 0.4181 0.0502  0.0140  0.1444  159 ASN   A C   
3540 C  C   B ASN   A 159 ? 0.1971 0.2215 0.3013 -0.0484 -0.0219 0.0410  159 ASN   A C   
3541 O  O   A ASN   A 159 ? 0.1669 0.3104 0.4302 0.0530  -0.0054 0.1267  159 ASN   A O   
3542 O  O   B ASN   A 159 ? 0.1964 0.2268 0.3012 -0.0516 -0.0184 0.0441  159 ASN   A O   
3543 C  CB  A ASN   A 159 ? 0.2172 0.3454 0.4719 0.0657  0.0051  0.1629  159 ASN   A CB  
3544 C  CB  B ASN   A 159 ? 0.2401 0.2583 0.3662 -0.0345 -0.0125 0.0414  159 ASN   A CB  
3545 C  CG  A ASN   A 159 ? 0.2459 0.3599 0.5299 0.0654  0.0105  0.1556  159 ASN   A CG  
3546 C  CG  B ASN   A 159 ? 0.2664 0.2889 0.4025 -0.0189 -0.0071 0.0492  159 ASN   A CG  
3547 O  OD1 A ASN   A 159 ? 0.2588 0.3793 0.5626 0.0574  0.0212  0.1477  159 ASN   A OD1 
3548 O  OD1 B ASN   A 159 ? 0.2761 0.3063 0.4155 -0.0134 -0.0065 0.0509  159 ASN   A OD1 
3549 N  ND2 A ASN   A 159 ? 0.2544 0.3589 0.5494 0.0720  0.0045  0.1524  159 ASN   A ND2 
3550 N  ND2 B ASN   A 159 ? 0.2745 0.2957 0.4202 -0.0151 -0.0003 0.0523  159 ASN   A ND2 
3563 N  N   A LEU   A 160 ? 0.1765 0.3337 0.3941 0.0478  0.0122  0.1597  160 LEU   A N   
3564 N  N   B LEU   A 160 ? 0.1807 0.2266 0.2863 -0.0369 -0.0302 0.0688  160 LEU   A N   
3565 C  CA  A LEU   A 160 ? 0.1827 0.3339 0.3682 0.0367  0.0287  0.1554  160 LEU   A CA  
3566 C  CA  B LEU   A 160 ? 0.1745 0.2466 0.2812 -0.0164 -0.0030 0.0902  160 LEU   A CA  
3567 C  C   A LEU   A 160 ? 0.1675 0.3383 0.3667 0.0284  0.0387  0.1478  160 LEU   A C   
3568 C  C   B LEU   A 160 ? 0.1662 0.2647 0.2805 0.0081  0.0103  0.0956  160 LEU   A C   
3569 O  O   A LEU   A 160 ? 0.1650 0.3483 0.4058 0.0243  0.0436  0.1445  160 LEU   A O   
3570 O  O   B LEU   A 160 ? 0.1664 0.2668 0.2951 0.0076  0.0065  0.1065  160 LEU   A O   
3571 C  CB  A LEU   A 160 ? 0.1988 0.3298 0.3546 0.0310  0.0397  0.1496  160 LEU   A CB  
3572 C  CB  B LEU   A 160 ? 0.1777 0.2508 0.2786 -0.0114 0.0068  0.0927  160 LEU   A CB  
3573 C  CG  A LEU   A 160 ? 0.2185 0.3336 0.3486 0.0197  0.0384  0.1254  160 LEU   A CG  
3574 C  CG  B LEU   A 160 ? 0.1836 0.2639 0.2808 -0.0020 0.0102  0.0868  160 LEU   A CG  
3575 C  CD1 A LEU   A 160 ? 0.2370 0.3364 0.3528 0.0149  0.0297  0.1065  160 LEU   A CD1 
3576 C  CD1 B LEU   A 160 ? 0.1908 0.2682 0.2820 0.0025  0.0082  0.0898  160 LEU   A CD1 
3577 C  CD2 A LEU   A 160 ? 0.2198 0.3270 0.3325 0.0189  0.0507  0.1294  160 LEU   A CD2 
3578 C  CD2 B LEU   A 160 ? 0.1842 0.2653 0.2773 0.0063  0.0180  0.0798  160 LEU   A CD2 
3601 N  N   A TYR   A 161 ? 0.1666 0.3291 0.3439 0.0279  0.0295  0.1511  161 TYR   A N   
3602 N  N   B TYR   A 161 ? 0.1607 0.2815 0.2637 0.0269  0.0152  0.1038  161 TYR   A N   
3603 C  CA  A TYR   A 161 ? 0.1672 0.3225 0.3358 0.0153  0.0257  0.1419  161 TYR   A CA  
3604 C  CA  B TYR   A 161 ? 0.1662 0.2893 0.2693 0.0382  0.0224  0.1046  161 TYR   A CA  
3605 C  C   A TYR   A 161 ? 0.1612 0.3435 0.3535 0.0076  0.0225  0.1341  161 TYR   A C   
3606 C  C   B TYR   A 161 ? 0.1702 0.3072 0.2822 0.0393  0.0262  0.1007  161 TYR   A C   
3607 O  O   A TYR   A 161 ? 0.1448 0.3514 0.3686 0.0007  0.0201  0.1428  161 TYR   A O   
3608 O  O   B TYR   A 161 ? 0.1664 0.3147 0.2896 0.0359  0.0269  0.1067  161 TYR   A O   
3609 C  CB  A TYR   A 161 ? 0.1786 0.3031 0.3382 0.0073  0.0271  0.1219  161 TYR   A CB  
3610 C  CB  B TYR   A 161 ? 0.1694 0.2822 0.2721 0.0474  0.0294  0.0990  161 TYR   A CB  
3611 C  CG  A TYR   A 161 ? 0.1825 0.2871 0.3298 -0.0040 0.0193  0.0975  161 TYR   A CG  
3612 C  CG  B TYR   A 161 ? 0.1716 0.2796 0.2667 0.0478  0.0336  0.0896  161 TYR   A CG  
3613 C  CD1 A TYR   A 161 ? 0.1709 0.2718 0.3276 -0.0172 0.0157  0.0862  161 TYR   A CD1 
3614 C  CD1 B TYR   A 161 ? 0.1766 0.2807 0.2694 0.0480  0.0337  0.0906  161 TYR   A CD1 
3615 C  CD2 A TYR   A 161 ? 0.1911 0.2900 0.3353 -0.0074 0.0149  0.0852  161 TYR   A CD2 
3616 C  CD2 B TYR   A 161 ? 0.1681 0.2773 0.2678 0.0476  0.0341  0.0803  161 TYR   A CD2 
3617 C  CE1 A TYR   A 161 ? 0.1790 0.2517 0.3215 -0.0323 0.0055  0.0872  161 TYR   A CE1 
3618 C  CE1 B TYR   A 161 ? 0.1759 0.2804 0.2693 0.0421  0.0361  0.0903  161 TYR   A CE1 
3619 C  CE2 A TYR   A 161 ? 0.1876 0.2741 0.3364 -0.0188 0.0137  0.0816  161 TYR   A CE2 
3620 C  CE2 B TYR   A 161 ? 0.1735 0.2815 0.2656 0.0446  0.0298  0.0754  161 TYR   A CE2 
3621 C  CZ  A TYR   A 161 ? 0.1925 0.2524 0.3187 -0.0272 0.0028  0.0839  161 TYR   A CZ  
3622 C  CZ  B TYR   A 161 ? 0.1829 0.2809 0.2687 0.0426  0.0310  0.0847  161 TYR   A CZ  
3623 O  OH  A TYR   A 161 ? 0.2058 0.2278 0.3235 -0.0234 -0.0010 0.0907  161 TYR   A OH  
3624 O  OH  B TYR   A 161 ? 0.1957 0.2800 0.2858 0.0358  0.0238  0.0861  161 TYR   A OH  
3643 N  N   A ASP   A 162 ? 0.1656 0.3543 0.3655 0.0089  0.0338  0.1319  162 ASP   A N   
3644 N  N   B ASP   A 162 ? 0.1736 0.3157 0.2921 0.0430  0.0322  0.0975  162 ASP   A N   
3645 C  CA  A ASP   A 162 ? 0.1604 0.3707 0.3710 -0.0005 0.0377  0.1259  162 ASP   A CA  
3646 C  CA  B ASP   A 162 ? 0.1768 0.3264 0.3047 0.0414  0.0392  0.0903  162 ASP   A CA  
3647 C  C   A ASP   A 162 ? 0.1487 0.3812 0.3658 -0.0118 0.0320  0.1254  162 ASP   A C   
3648 C  C   B ASP   A 162 ? 0.1770 0.3326 0.2989 0.0428  0.0330  0.0845  162 ASP   A C   
3649 O  O   A ASP   A 162 ? 0.1478 0.3863 0.4017 -0.0264 0.0259  0.1147  162 ASP   A O   
3650 O  O   B ASP   A 162 ? 0.1806 0.3373 0.3213 0.0437  0.0362  0.0778  162 ASP   A O   
3651 C  CB  A ASP   A 162 ? 0.1756 0.3844 0.3784 0.0077  0.0421  0.1159  162 ASP   A CB  
3652 C  CB  B ASP   A 162 ? 0.1759 0.3358 0.3231 0.0387  0.0523  0.0815  162 ASP   A CB  
3653 C  CG  A ASP   A 162 ? 0.1861 0.3980 0.3932 0.0186  0.0450  0.0991  162 ASP   A CG  
3654 C  CG  B ASP   A 162 ? 0.1787 0.3503 0.3408 0.0349  0.0592  0.0708  162 ASP   A CG  
3655 O  OD1 A ASP   A 162 ? 0.1929 0.4134 0.4163 0.0190  0.0615  0.0834  162 ASP   A OD1 
3656 O  OD1 B ASP   A 162 ? 0.1765 0.3585 0.3566 0.0334  0.0599  0.0680  162 ASP   A OD1 
3657 O  OD2 A ASP   A 162 ? 0.1896 0.3959 0.4032 0.0193  0.0513  0.0947  162 ASP   A OD2 
3658 O  OD2 B ASP   A 162 ? 0.1846 0.3548 0.3555 0.0353  0.0667  0.0646  162 ASP   A OD2 
3667 N  N   A LYS   A 163 ? 0.1613 0.3860 0.3633 -0.0068 -0.0035 0.1236  163 LYS   A N   
3668 N  N   B LYS   A 163 ? 0.1860 0.3339 0.3034 0.0370  0.0092  0.0807  163 LYS   A N   
3669 C  CA  A LYS   A 163 ? 0.1756 0.3909 0.3550 -0.0087 -0.0183 0.1077  163 LYS   A CA  
3670 C  CA  B LYS   A 163 ? 0.1973 0.3324 0.2985 0.0264  0.0025  0.0686  163 LYS   A CA  
3671 C  C   A LYS   A 163 ? 0.1709 0.3679 0.3530 -0.0200 0.0009  0.0828  163 LYS   A C   
3672 C  C   B LYS   A 163 ? 0.1904 0.3166 0.2741 0.0144  0.0099  0.0632  163 LYS   A C   
3673 O  O   A LYS   A 163 ? 0.1724 0.3916 0.3705 -0.0260 0.0065  0.0825  163 LYS   A O   
3674 O  O   B LYS   A 163 ? 0.1914 0.3204 0.2839 -0.0010 0.0105  0.0573  163 LYS   A O   
3675 C  CB  A LYS   A 163 ? 0.2144 0.4178 0.3854 0.0037  -0.0369 0.1010  163 LYS   A CB  
3676 C  CB  B LYS   A 163 ? 0.2279 0.3469 0.3320 0.0282  -0.0045 0.0579  163 LYS   A CB  
3677 C  CG  A LYS   A 163 ? 0.2654 0.4429 0.4300 0.0027  -0.0251 0.0978  163 LYS   A CG  
3678 C  CG  B LYS   A 163 ? 0.2595 0.3578 0.3741 0.0223  0.0022  0.0489  163 LYS   A CG  
3679 C  CD  A LYS   A 163 ? 0.2978 0.4615 0.4774 0.0021  -0.0173 0.0955  163 LYS   A CD  
3680 C  CD  B LYS   A 163 ? 0.2844 0.3681 0.4172 0.0156  0.0073  0.0435  163 LYS   A CD  
3681 C  CE  A LYS   A 163 ? 0.3128 0.4709 0.5143 0.0005  -0.0135 0.0936  163 LYS   A CE  
3682 C  CE  B LYS   A 163 ? 0.2972 0.3758 0.4488 0.0084  0.0096  0.0403  163 LYS   A CE  
3683 N  NZ  A LYS   A 163 ? 0.3487 0.4781 0.5352 -0.0025 -0.0154 0.0951  163 LYS   A NZ  
3684 N  NZ  B LYS   A 163 ? 0.3106 0.3818 0.4697 0.0038  0.0050  0.0372  163 LYS   A NZ  
3711 N  N   A LEU   A 164 ? 0.1588 0.3256 0.3277 -0.0284 0.0031  0.0664  164 LEU   A N   
3712 N  N   B LEU   A 164 ? 0.1744 0.2852 0.2512 0.0122  0.0142  0.0620  164 LEU   A N   
3713 C  CA  A LEU   A 164 ? 0.1615 0.2879 0.3117 -0.0402 0.0262  0.0546  164 LEU   A CA  
3714 C  CA  B LEU   A 164 ? 0.1709 0.2586 0.2345 -0.0030 0.0165  0.0466  164 LEU   A CA  
3715 C  C   A LEU   A 164 ? 0.1702 0.2682 0.3029 -0.0468 0.0367  0.0368  164 LEU   A C   
3716 C  C   B LEU   A 164 ? 0.1765 0.2380 0.2299 -0.0135 0.0159  0.0249  164 LEU   A C   
3717 O  O   A LEU   A 164 ? 0.1907 0.2781 0.3098 -0.0434 0.0489  0.0026  164 LEU   A O   
3718 O  O   B LEU   A 164 ? 0.1726 0.2237 0.2423 -0.0240 0.0303  0.0131  164 LEU   A O   
3719 C  CB  A LEU   A 164 ? 0.1632 0.2841 0.3186 -0.0461 0.0195  0.0674  164 LEU   A CB  
3720 C  CB  B LEU   A 164 ? 0.1628 0.2530 0.2336 -0.0003 0.0189  0.0517  164 LEU   A CB  
3721 C  CG  A LEU   A 164 ? 0.1692 0.2906 0.3305 -0.0375 0.0174  0.0818  164 LEU   A CG  
3722 C  CG  B LEU   A 164 ? 0.1626 0.2542 0.2342 0.0036  0.0134  0.0621  164 LEU   A CG  
3723 C  CD1 A LEU   A 164 ? 0.1707 0.2942 0.3353 -0.0270 0.0168  0.0848  164 LEU   A CD1 
3724 C  CD1 B LEU   A 164 ? 0.1549 0.2475 0.2333 0.0095  0.0203  0.0683  164 LEU   A CD1 
3725 C  CD2 A LEU   A 164 ? 0.1715 0.2938 0.3184 -0.0230 -0.0000 0.0798  164 LEU   A CD2 
3726 C  CD2 B LEU   A 164 ? 0.1604 0.2602 0.2309 0.0068  0.0070  0.0607  164 LEU   A CD2 
3749 N  N   A VAL   A 165 ? 0.1581 0.2593 0.2775 -0.0226 0.0323  0.0507  165 VAL   A N   
3750 N  N   B VAL   A 165 ? 0.1697 0.2291 0.2131 -0.0213 0.0123  0.0188  165 VAL   A N   
3751 C  CA  A VAL   A 165 ? 0.1642 0.2524 0.2475 -0.0299 0.0366  0.0510  165 VAL   A CA  
3752 C  CA  B VAL   A 165 ? 0.1789 0.2309 0.2120 -0.0119 0.0182  0.0098  165 VAL   A CA  
3753 C  C   A VAL   A 165 ? 0.1668 0.2663 0.2654 -0.0231 0.0262  0.0369  165 VAL   A C   
3754 C  C   B VAL   A 165 ? 0.1686 0.2366 0.2100 -0.0026 0.0247  -0.0013 165 VAL   A C   
3755 O  O   A VAL   A 165 ? 0.1612 0.2542 0.2854 -0.0226 0.0236  0.0353  165 VAL   A O   
3756 O  O   B VAL   A 165 ? 0.1638 0.2343 0.2209 0.0009  0.0254  -0.0059 165 VAL   A O   
3757 C  CB  A VAL   A 165 ? 0.1760 0.2444 0.2447 -0.0300 0.0393  0.0367  165 VAL   A CB  
3758 C  CB  B VAL   A 165 ? 0.2005 0.2309 0.2253 -0.0119 0.0107  0.0013  165 VAL   A CB  
3759 C  CG1 A VAL   A 165 ? 0.1883 0.2467 0.2534 -0.0300 0.0332  0.0334  165 VAL   A CG1 
3760 C  CG1 B VAL   A 165 ? 0.2110 0.2356 0.2341 -0.0190 0.0041  -0.0040 165 VAL   A CG1 
3761 C  CG2 A VAL   A 165 ? 0.1917 0.2427 0.2525 -0.0208 0.0283  0.0269  165 VAL   A CG2 
3762 C  CG2 B VAL   A 165 ? 0.2107 0.2296 0.2244 -0.0069 0.0035  -0.0087 165 VAL   A CG2 
3781 N  N   A SER   A 166 ? 0.1735 0.2956 0.2757 -0.0123 0.0265  0.0328  166 SER   A N   
3782 N  N   B SER   A 166 ? 0.1577 0.2456 0.2133 0.0032  0.0197  -0.0007 166 SER   A N   
3783 C  CA  A SER   A 166 ? 0.1761 0.3295 0.2846 -0.0170 0.0329  0.0191  166 SER   A CA  
3784 C  CA  B SER   A 166 ? 0.1658 0.2647 0.2184 0.0104  0.0216  0.0000  166 SER   A CA  
3785 C  C   A SER   A 166 ? 0.1665 0.3628 0.2935 -0.0248 0.0262  -0.0001 166 SER   A C   
3786 C  C   B SER   A 166 ? 0.1738 0.2743 0.2229 0.0219  0.0086  -0.0160 166 SER   A C   
3787 O  O   A SER   A 166 ? 0.1779 0.3740 0.3247 -0.0392 0.0199  -0.0294 166 SER   A O   
3788 O  O   B SER   A 166 ? 0.1881 0.2848 0.2388 0.0151  0.0112  -0.0369 166 SER   A O   
3789 C  CB  A SER   A 166 ? 0.2022 0.3385 0.3121 -0.0240 0.0330  0.0182  166 SER   A CB  
3790 C  CB  B SER   A 166 ? 0.1685 0.2754 0.2285 0.0205  0.0294  0.0132  166 SER   A CB  
3791 O  OG  A SER   A 166 ? 0.2336 0.3516 0.3444 -0.0341 0.0251  0.0261  166 SER   A OG  
3792 O  OG  B SER   A 166 ? 0.1626 0.2811 0.2511 0.0260  0.0182  0.0298  166 SER   A OG  
3803 N  N   A SER   A 167 ? 0.1687 0.3836 0.2834 0.0076  0.0127  0.0058  167 SER   A N   
3804 N  N   B SER   A 167 ? 0.1840 0.2820 0.2174 0.0367  -0.0052 -0.0120 167 SER   A N   
3805 C  CA  A SER   A 167 ? 0.1995 0.3969 0.2795 0.0223  0.0017  0.0045  167 SER   A CA  
3806 C  CA  B SER   A 167 ? 0.2014 0.2923 0.2304 0.0444  0.0123  -0.0220 167 SER   A CA  
3807 C  C   A SER   A 167 ? 0.2017 0.4075 0.2744 0.0304  0.0120  -0.0022 167 SER   A C   
3808 C  C   B SER   A 167 ? 0.2118 0.2988 0.2431 0.0487  0.0262  -0.0282 167 SER   A C   
3809 O  O   A SER   A 167 ? 0.2110 0.4158 0.2620 0.0303  0.0233  0.0080  167 SER   A O   
3810 O  O   B SER   A 167 ? 0.2206 0.2969 0.2521 0.0556  0.0260  -0.0479 167 SER   A O   
3811 C  CB  A SER   A 167 ? 0.2090 0.3962 0.2913 0.0333  0.0121  0.0135  167 SER   A CB  
3812 C  CB  B SER   A 167 ? 0.2138 0.3003 0.2403 0.0405  0.0145  -0.0214 167 SER   A CB  
3813 O  OG  A SER   A 167 ? 0.2211 0.3911 0.2980 0.0401  0.0224  0.0217  167 SER   A OG  
3814 O  OG  B SER   A 167 ? 0.2192 0.3034 0.2409 0.0376  0.0250  -0.0292 167 SER   A OG  
3825 N  N   A PHE   A 168 ? 0.1923 0.4054 0.2821 0.0402  0.0075  -0.0146 168 PHE   A N   
3826 N  N   B PHE   A 168 ? 0.2147 0.3083 0.2594 0.0428  0.0221  -0.0124 168 PHE   A N   
3827 C  CA  A PHE   A 168 ? 0.1925 0.3957 0.2984 0.0311  0.0143  -0.0218 168 PHE   A CA  
3828 C  CA  B PHE   A 168 ? 0.2182 0.3217 0.2767 0.0324  0.0066  0.0062  168 PHE   A CA  
3829 C  C   A PHE   A 168 ? 0.2289 0.4195 0.3487 0.0085  0.0319  -0.0391 168 PHE   A C   
3830 C  C   B PHE   A 168 ? 0.2276 0.3334 0.3076 0.0186  0.0004  0.0009  168 PHE   A C   
3831 O  O   A PHE   A 168 ? 0.2332 0.4219 0.3693 -0.0077 0.0393  -0.0463 168 PHE   A O   
3832 O  O   B PHE   A 168 ? 0.2222 0.3294 0.3055 0.0136  0.0125  0.0072  168 PHE   A O   
3833 C  CB  A PHE   A 168 ? 0.1800 0.3616 0.2768 0.0170  0.0017  -0.0071 168 PHE   A CB  
3834 C  CB  B PHE   A 168 ? 0.2133 0.3223 0.2639 0.0376  0.0097  0.0248  168 PHE   A CB  
3835 C  CG  A PHE   A 168 ? 0.1655 0.3303 0.2587 -0.0027 0.0062  0.0031  168 PHE   A CG  
3836 C  CG  B PHE   A 168 ? 0.2112 0.3242 0.2639 0.0353  0.0233  0.0395  168 PHE   A CG  
3837 C  CD1 A PHE   A 168 ? 0.1686 0.3202 0.2530 -0.0110 -0.0037 0.0082  168 PHE   A CD1 
3838 C  CD1 B PHE   A 168 ? 0.2124 0.3234 0.2601 0.0321  0.0341  0.0453  168 PHE   A CD1 
3839 C  CD2 A PHE   A 168 ? 0.1511 0.3131 0.2474 -0.0062 0.0289  0.0067  168 PHE   A CD2 
3840 C  CD2 B PHE   A 168 ? 0.2122 0.3258 0.2622 0.0354  0.0350  0.0427  168 PHE   A CD2 
3841 C  CE1 A PHE   A 168 ? 0.1633 0.3103 0.2380 -0.0170 -0.0079 0.0075  168 PHE   A CE1 
3842 C  CE1 B PHE   A 168 ? 0.2133 0.3203 0.2603 0.0344  0.0379  0.0546  168 PHE   A CE1 
3843 C  CE2 A PHE   A 168 ? 0.1597 0.3017 0.2490 -0.0102 0.0183  0.0090  168 PHE   A CE2 
3844 C  CE2 B PHE   A 168 ? 0.2159 0.3239 0.2668 0.0375  0.0400  0.0495  168 PHE   A CE2 
3845 C  CZ  A PHE   A 168 ? 0.1649 0.3045 0.2390 -0.0175 0.0018  0.0124  168 PHE   A CZ  
3846 C  CZ  B PHE   A 168 ? 0.2153 0.3213 0.2638 0.0348  0.0397  0.0550  168 PHE   A CZ  
3865 N  N   A LEU   A 169 ? 0.2798 0.4377 0.4053 -0.0053 0.0282  -0.0524 169 LEU   A N   
3866 N  N   B LEU   A 169 ? 0.2600 0.3542 0.3401 0.0028  -0.0196 -0.0079 169 LEU   A N   
3867 C  CA  A LEU   A 169 ? 0.3507 0.4610 0.4760 -0.0112 0.0015  -0.0573 169 LEU   A CA  
3868 C  CA  B LEU   A 169 ? 0.2906 0.3713 0.3816 -0.0016 -0.0311 -0.0203 169 LEU   A CA  
3869 C  C   A LEU   A 169 ? 0.3757 0.4687 0.5097 -0.0220 -0.0083 -0.0521 169 LEU   A C   
3870 C  C   B LEU   A 169 ? 0.2914 0.3724 0.3812 -0.0046 -0.0278 -0.0228 169 LEU   A C   
3871 O  O   A LEU   A 169 ? 0.3895 0.4781 0.5260 -0.0323 -0.0062 -0.0501 169 LEU   A O   
3872 O  O   B LEU   A 169 ? 0.2910 0.3710 0.3901 -0.0077 -0.0232 -0.0291 169 LEU   A O   
3873 C  CB  A LEU   A 169 ? 0.3934 0.4765 0.5078 -0.0123 -0.0080 -0.0649 169 LEU   A CB  
3874 C  CB  B LEU   A 169 ? 0.3139 0.3844 0.4155 -0.0063 -0.0421 -0.0293 169 LEU   A CB  
3875 C  CG  A LEU   A 169 ? 0.4234 0.4883 0.5252 -0.0153 -0.0145 -0.0727 169 LEU   A CG  
3876 C  CG  B LEU   A 169 ? 0.3327 0.3954 0.4349 -0.0110 -0.0519 -0.0376 169 LEU   A CG  
3877 C  CD1 A LEU   A 169 ? 0.4375 0.4939 0.5396 -0.0141 -0.0139 -0.0729 169 LEU   A CD1 
3878 C  CD1 B LEU   A 169 ? 0.3438 0.3988 0.4510 -0.0115 -0.0529 -0.0394 169 LEU   A CD1 
3879 C  CD2 A LEU   A 169 ? 0.4350 0.4899 0.5338 -0.0189 -0.0159 -0.0762 169 LEU   A CD2 
3880 C  CD2 B LEU   A 169 ? 0.3363 0.3983 0.4483 -0.0138 -0.0546 -0.0413 169 LEU   A CD2 
3881 O  OXT A LEU   A 169 ? 0.3804 0.4663 0.5208 -0.0206 -0.0057 -0.0531 169 LEU   A OXT 
3882 O  OXT B LEU   A 169 ? 0.2863 0.3737 0.3801 -0.0062 -0.0313 -0.0195 169 LEU   A OXT 
3905 N  N   . SER   B 1   ? 0.3456 0.3334 0.3741 -0.0930 -0.0645 0.0253  1   SER   B N   
3906 C  CA  . SER   B 1   ? 0.3331 0.3460 0.3615 -0.1038 -0.0788 0.0218  1   SER   B CA  
3907 C  C   . SER   B 1   ? 0.3084 0.3539 0.3689 -0.1017 -0.0878 0.0429  1   SER   B C   
3908 O  O   . SER   B 1   ? 0.3230 0.3564 0.3668 -0.0908 -0.0860 0.0396  1   SER   B O   
3909 C  CB  . SER   B 1   ? 0.3454 0.3436 0.3972 -0.1059 -0.0636 -0.0070 1   SER   B CB  
3910 O  OG  . SER   B 1   ? 0.3692 0.3575 0.4450 -0.1010 -0.0327 -0.0251 1   SER   B OG  
3918 N  N   A MET   B 2   ? 0.2941 0.3509 0.3817 -0.1124 -0.0792 0.0680  2   MET   B N   
3919 N  N   B MET   B 2   ? 0.3027 0.3537 0.3698 -0.0989 -0.0795 0.0619  2   MET   B N   
3920 C  CA  A MET   B 2   ? 0.2918 0.3581 0.3943 -0.0941 -0.0755 0.0835  2   MET   B CA  
3921 C  CA  B MET   B 2   ? 0.2979 0.3551 0.3700 -0.0841 -0.0760 0.0786  2   MET   B CA  
3922 C  C   A MET   B 2   ? 0.2621 0.3477 0.3670 -0.0748 -0.0879 0.1051  2   MET   B C   
3923 C  C   B MET   B 2   ? 0.2673 0.3414 0.3499 -0.0784 -0.0810 0.1009  2   MET   B C   
3924 O  O   A MET   B 2   ? 0.2593 0.3604 0.3813 -0.0571 -0.1050 0.1063  2   MET   B O   
3925 O  O   B MET   B 2   ? 0.2656 0.3493 0.3559 -0.0721 -0.0871 0.0999  2   MET   B O   
3926 C  CB  A MET   B 2   ? 0.3263 0.3871 0.4599 -0.0744 -0.0571 0.0624  2   MET   B CB  
3927 C  CB  B MET   B 2   ? 0.3251 0.3734 0.4050 -0.0664 -0.0677 0.0671  2   MET   B CB  
3928 C  CG  A MET   B 2   ? 0.3549 0.4134 0.5360 -0.0543 -0.0389 0.0521  2   MET   B CG  
3929 C  CG  B MET   B 2   ? 0.3453 0.3875 0.4483 -0.0484 -0.0611 0.0619  2   MET   B CG  
3930 S  SD  A MET   B 2   ? 0.3807 0.4407 0.6067 -0.0335 -0.0148 0.0396  2   MET   B SD  
3931 S  SD  B MET   B 2   ? 0.3598 0.4003 0.4861 -0.0313 -0.0554 0.0525  2   MET   B SD  
3932 C  CE  A MET   B 2   ? 0.3777 0.4473 0.6091 -0.0327 -0.0063 0.0397  2   MET   B CE  
3933 C  CE  B MET   B 2   ? 0.3578 0.4008 0.4851 -0.0328 -0.0532 0.0511  2   MET   B CE  
3952 N  N   . VAL   B 3   ? 0.2378 0.3151 0.3366 -0.0876 -0.0779 0.1241  3   VAL   B N   
3953 C  CA  . VAL   B 3   ? 0.2348 0.2788 0.3378 -0.0734 -0.0764 0.1044  3   VAL   B CA  
3954 C  C   . VAL   B 3   ? 0.2204 0.2635 0.3072 -0.0620 -0.0713 0.0934  3   VAL   B C   
3955 O  O   . VAL   B 3   ? 0.2247 0.2744 0.3034 -0.0718 -0.0843 0.1000  3   VAL   B O   
3956 C  CB  . VAL   B 3   ? 0.2462 0.2718 0.3814 -0.0799 -0.0854 0.0805  3   VAL   B CB  
3957 C  CG1 . VAL   B 3   ? 0.2568 0.2572 0.3997 -0.0842 -0.0867 0.0880  3   VAL   B CG1 
3958 C  CG2 . VAL   B 3   ? 0.2445 0.2773 0.3924 -0.0776 -0.0649 0.0884  3   VAL   B CG2 
3969 N  N   . ASN   B 4   ? 0.2047 0.2348 0.2855 -0.0642 -0.0636 0.0844  4   ASN   B N   
3970 C  CA  . ASN   B 4   ? 0.2064 0.2369 0.2611 -0.0636 -0.0579 0.0560  4   ASN   B CA  
3971 C  C   . ASN   B 4   ? 0.2012 0.2545 0.2679 -0.0633 -0.0521 0.0434  4   ASN   B C   
3972 O  O   . ASN   B 4   ? 0.1972 0.2563 0.2885 -0.0589 -0.0435 0.0373  4   ASN   B O   
3973 C  CB  . ASN   B 4   ? 0.2161 0.2277 0.2400 -0.0630 -0.0654 0.0463  4   ASN   B CB  
3974 C  CG  . ASN   B 4   ? 0.2214 0.2026 0.2386 -0.0613 -0.0546 0.0435  4   ASN   B CG  
3975 O  OD1 . ASN   B 4   ? 0.2256 0.1900 0.2452 -0.0558 -0.0472 0.0384  4   ASN   B OD1 
3976 N  ND2 . ASN   B 4   ? 0.2434 0.2170 0.2372 -0.0453 -0.0443 0.0308  4   ASN   B ND2 
3983 N  N   . SER   B 5   ? 0.2133 0.2724 0.2744 -0.0684 -0.0541 0.0245  5   SER   B N   
3984 C  CA  . SER   B 5   ? 0.2472 0.3071 0.2945 -0.0728 -0.0330 0.0278  5   SER   B CA  
3985 C  C   . SER   B 5   ? 0.2809 0.3124 0.3121 -0.0979 -0.0163 0.0398  5   SER   B C   
3986 O  O   . SER   B 5   ? 0.3075 0.3027 0.3448 -0.0815 0.0279  0.0367  5   SER   B O   
3987 C  CB  . SER   B 5   ? 0.2622 0.3314 0.3155 -0.0625 -0.0142 0.0367  5   SER   B CB  
3988 O  OG  . SER   B 5   ? 0.3113 0.3698 0.3703 -0.0433 -0.0065 0.0508  5   SER   B OG  
3994 N  N   . PHE   B 6   ? 0.3096 0.3470 0.3169 -0.1086 -0.0016 0.0573  6   PHE   B N   
3995 C  CA  . PHE   B 6   ? 0.3286 0.3629 0.2879 -0.1337 0.0075  0.0423  6   PHE   B CA  
3996 C  C   . PHE   B 6   ? 0.3819 0.4010 0.3403 -0.1390 0.0309  0.0108  6   PHE   B C   
3997 O  O   . PHE   B 6   ? 0.3942 0.4301 0.3660 -0.1275 0.0283  0.0010  6   PHE   B O   
3998 C  CB  . PHE   B 6   ? 0.3035 0.3463 0.2712 -0.1307 -0.0161 0.0444  6   PHE   B CB  
3999 C  CG  . PHE   B 6   ? 0.2704 0.3182 0.2646 -0.1283 -0.0292 0.0455  6   PHE   B CG  
4000 C  CD1 . PHE   B 6   ? 0.2715 0.2890 0.2404 -0.1228 -0.0449 0.0321  6   PHE   B CD1 
4001 C  CD2 . PHE   B 6   ? 0.2500 0.3142 0.2564 -0.1080 -0.0241 0.0682  6   PHE   B CD2 
4002 C  CE1 . PHE   B 6   ? 0.2656 0.2621 0.2521 -0.1072 -0.0407 0.0366  6   PHE   B CE1 
4003 C  CE2 . PHE   B 6   ? 0.2496 0.2908 0.2733 -0.0991 -0.0146 0.0715  6   PHE   B CE2 
4004 C  CZ  . PHE   B 6   ? 0.2521 0.2667 0.2653 -0.0957 -0.0324 0.0520  6   PHE   B CZ  
4014 N  N   . SER   B 7   ? 0.4288 0.3917 0.3723 -0.1605 0.0546  -0.0133 7   SER   B N   
4015 C  CA  . SER   B 7   ? 0.4741 0.4016 0.4298 -0.1603 0.0740  -0.0257 7   SER   B CA  
4016 C  C   . SER   B 7   ? 0.4865 0.3891 0.4075 -0.1742 0.0873  -0.0451 7   SER   B C   
4017 O  O   . SER   B 7   ? 0.5052 0.3781 0.4129 -0.1893 0.0907  -0.0478 7   SER   B O   
4018 C  CB  . SER   B 7   ? 0.4937 0.4106 0.5071 -0.1535 0.0933  -0.0109 7   SER   B CB  
4019 O  OG  . SER   B 7   ? 0.5113 0.4384 0.5564 -0.1492 0.0981  0.0017  7   SER   B OG  
4025 N  N   . GLY   B 8   ? 0.4838 0.3839 0.3931 -0.1600 0.0912  -0.0535 8   GLY   B N   
4026 C  CA  . GLY   B 8   ? 0.4738 0.3679 0.3750 -0.1578 0.0922  -0.0465 8   GLY   B CA  
4027 C  C   . GLY   B 8   ? 0.4680 0.3423 0.3571 -0.1651 0.0907  -0.0409 8   GLY   B C   
4028 O  O   . GLY   B 8   ? 0.4872 0.3531 0.3666 -0.1563 0.0960  -0.0575 8   GLY   B O   
4032 N  N   . TYR   B 9   ? 0.4539 0.3218 0.3337 -0.1607 0.0622  -0.0494 9   TYR   B N   
4033 C  CA  . TYR   B 9   ? 0.4380 0.2911 0.3052 -0.1532 0.0401  -0.0473 9   TYR   B CA  
4034 C  C   . TYR   B 9   ? 0.4301 0.2893 0.3070 -0.1459 0.0077  -0.0346 9   TYR   B C   
4035 O  O   . TYR   B 9   ? 0.4279 0.3061 0.3499 -0.1405 0.0149  -0.0342 9   TYR   B O   
4036 C  CB  . TYR   B 9   ? 0.4380 0.2673 0.2938 -0.1459 0.0409  -0.0479 9   TYR   B CB  
4037 C  CG  . TYR   B 9   ? 0.4282 0.2447 0.2830 -0.1527 0.0356  -0.0493 9   TYR   B CG  
4038 C  CD1 . TYR   B 9   ? 0.4230 0.2466 0.2856 -0.1576 0.0353  -0.0441 9   TYR   B CD1 
4039 C  CD2 . TYR   B 9   ? 0.4165 0.2434 0.2770 -0.1455 0.0390  -0.0556 9   TYR   B CD2 
4040 C  CE1 . TYR   B 9   ? 0.4090 0.2600 0.2807 -0.1550 0.0466  -0.0517 9   TYR   B CE1 
4041 C  CE2 . TYR   B 9   ? 0.4071 0.2473 0.2793 -0.1439 0.0391  -0.0601 9   TYR   B CE2 
4042 C  CZ  . TYR   B 9   ? 0.3982 0.2611 0.2854 -0.1479 0.0448  -0.0710 9   TYR   B CZ  
4043 O  OH  . TYR   B 9   ? 0.3828 0.2681 0.2925 -0.1427 0.0610  -0.0837 9   TYR   B OH  
4053 N  N   . LEU   B 10  ? 0.4215 0.2604 0.2861 -0.1478 -0.0124 -0.0243 10  LEU   B N   
4054 C  CA  . LEU   B 10  ? 0.4233 0.2510 0.2842 -0.1466 -0.0405 -0.0046 10  LEU   B CA  
4055 C  C   . LEU   B 10  ? 0.4126 0.2460 0.2812 -0.1336 -0.0654 -0.0071 10  LEU   B C   
4056 O  O   . LEU   B 10  ? 0.4047 0.2503 0.2814 -0.1233 -0.0691 -0.0029 10  LEU   B O   
4057 C  CB  . LEU   B 10  ? 0.4386 0.2468 0.3020 -0.1450 -0.0458 0.0087  10  LEU   B CB  
4058 C  CG  . LEU   B 10  ? 0.4496 0.2554 0.3169 -0.1339 -0.0618 0.0106  10  LEU   B CG  
4059 C  CD1 . LEU   B 10  ? 0.4552 0.2582 0.3358 -0.1221 -0.0609 0.0018  10  LEU   B CD1 
4060 C  CD2 . LEU   B 10  ? 0.4476 0.2560 0.3347 -0.1464 -0.0582 0.0230  10  LEU   B CD2 
4072 N  N   . LYS   B 11  ? 0.4169 0.2624 0.3048 -0.1270 -0.0748 -0.0050 11  LYS   B N   
4073 C  CA  . LYS   B 11  ? 0.4299 0.2860 0.3459 -0.1046 -0.0700 -0.0080 11  LYS   B CA  
4074 C  C   . LYS   B 11  ? 0.4045 0.2569 0.3528 -0.1229 -0.0727 -0.0251 11  LYS   B C   
4075 O  O   . LYS   B 11  ? 0.4174 0.2686 0.3846 -0.1390 -0.0739 -0.0547 11  LYS   B O   
4076 C  CB  . LYS   B 11  ? 0.4548 0.3300 0.4007 -0.0751 -0.0589 -0.0125 11  LYS   B CB  
4077 C  CG  . LYS   B 11  ? 0.4754 0.3613 0.4611 -0.0518 -0.0597 -0.0259 11  LYS   B CG  
4078 C  CD  . LYS   B 11  ? 0.4884 0.3839 0.5067 -0.0331 -0.0569 -0.0342 11  LYS   B CD  
4079 C  CE  . LYS   B 11  ? 0.4987 0.4021 0.5447 -0.0191 -0.0451 -0.0343 11  LYS   B CE  
4080 N  NZ  . LYS   B 11  ? 0.5069 0.4124 0.5666 -0.0104 -0.0355 -0.0290 11  LYS   B NZ  
4094 N  N   . LEU   B 12  ? 0.3655 0.2363 0.3364 -0.1163 -0.0866 -0.0261 12  LEU   B N   
4095 C  CA  . LEU   B 12  ? 0.3396 0.2131 0.3459 -0.1017 -0.0692 -0.0115 12  LEU   B CA  
4096 C  C   . LEU   B 12  ? 0.3220 0.2256 0.3645 -0.1057 -0.0847 0.0095  12  LEU   B C   
4097 O  O   . LEU   B 12  ? 0.3184 0.2311 0.3817 -0.1163 -0.1103 0.0135  12  LEU   B O   
4098 C  CB  . LEU   B 12  ? 0.3354 0.1931 0.3378 -0.0742 -0.0574 -0.0064 12  LEU   B CB  
4099 C  CG  . LEU   B 12  ? 0.3359 0.1848 0.3300 -0.0688 -0.0347 -0.0120 12  LEU   B CG  
4100 C  CD1 . LEU   B 12  ? 0.3398 0.1871 0.3243 -0.0485 -0.0274 -0.0039 12  LEU   B CD1 
4101 C  CD2 . LEU   B 12  ? 0.3414 0.1886 0.3327 -0.0737 -0.0316 -0.0294 12  LEU   B CD2 
4113 N  N   . THR   B 13  ? 0.3081 0.2357 0.3618 -0.1103 -0.0840 -0.0011 13  THR   B N   
4114 C  CA  . THR   B 13  ? 0.2919 0.2460 0.3727 -0.1199 -0.1100 0.0100  13  THR   B CA  
4115 C  C   . THR   B 13  ? 0.3318 0.2625 0.3866 -0.1242 -0.1153 0.0040  13  THR   B C   
4116 O  O   . THR   B 13  ? 0.3606 0.2684 0.3968 -0.1169 -0.0999 0.0007  13  THR   B O   
4117 C  CB  . THR   B 13  ? 0.2703 0.2515 0.3792 -0.1028 -0.1107 0.0244  13  THR   B CB  
4118 O  OG1 . THR   B 13  ? 0.2540 0.2430 0.3946 -0.0965 -0.1030 0.0246  13  THR   B OG1 
4119 C  CG2 . THR   B 13  ? 0.2827 0.2563 0.3692 -0.0924 -0.1040 0.0250  13  THR   B CG2 
4127 N  N   A ASP   B 14  ? 0.3451 0.2765 0.3936 -0.1224 -0.1281 0.0134  14  ASP   B N   
4128 N  N   B ASP   B 14  ? 0.3409 0.2730 0.3856 -0.1181 -0.1121 0.0124  14  ASP   B N   
4129 C  CA  A ASP   B 14  ? 0.3545 0.2892 0.4107 -0.1196 -0.1206 0.0266  14  ASP   B CA  
4130 C  CA  B ASP   B 14  ? 0.3454 0.2804 0.3937 -0.1123 -0.1028 0.0229  14  ASP   B CA  
4131 C  C   A ASP   B 14  ? 0.3402 0.2687 0.3806 -0.1241 -0.1102 0.0329  14  ASP   B C   
4132 C  C   B ASP   B 14  ? 0.3312 0.2614 0.3705 -0.1137 -0.1045 0.0297  14  ASP   B C   
4133 O  O   A ASP   B 14  ? 0.3668 0.2885 0.3883 -0.1239 -0.1004 0.0478  14  ASP   B O   
4134 O  O   B ASP   B 14  ? 0.3455 0.2653 0.3715 -0.1141 -0.1001 0.0352  14  ASP   B O   
4135 C  CB  A ASP   B 14  ? 0.3732 0.3252 0.4649 -0.1044 -0.1203 0.0267  14  ASP   B CB  
4136 C  CB  B ASP   B 14  ? 0.3611 0.3080 0.4345 -0.0995 -0.0919 0.0228  14  ASP   B CB  
4137 C  CG  A ASP   B 14  ? 0.3931 0.3569 0.5168 -0.0875 -0.1181 0.0157  14  ASP   B CG  
4138 C  CG  B ASP   B 14  ? 0.3769 0.3322 0.4687 -0.0844 -0.0827 0.0176  14  ASP   B CG  
4139 O  OD1 A ASP   B 14  ? 0.4024 0.3664 0.5336 -0.0834 -0.1225 0.0035  14  ASP   B OD1 
4140 O  OD1 B ASP   B 14  ? 0.3824 0.3438 0.4824 -0.0752 -0.0810 0.0115  14  ASP   B OD1 
4141 O  OD2 A ASP   B 14  ? 0.3955 0.3766 0.5472 -0.0829 -0.1134 0.0214  14  ASP   B OD2 
4142 O  OD2 B ASP   B 14  ? 0.3809 0.3394 0.4875 -0.0854 -0.0785 0.0231  14  ASP   B OD2 
4151 N  N   . ASN   B 15  ? 0.3063 0.2405 0.3635 -0.1040 -0.1133 0.0309  15  ASN   B N   
4152 C  CA  . ASN   B 15  ? 0.2462 0.2100 0.3462 -0.0743 -0.1020 0.0266  15  ASN   B CA  
4153 C  C   . ASN   B 15  ? 0.2228 0.1928 0.3303 -0.0523 -0.0809 0.0270  15  ASN   B C   
4154 O  O   . ASN   B 15  ? 0.2051 0.1815 0.3409 -0.0500 -0.0782 0.0156  15  ASN   B O   
4155 C  CB  . ASN   B 15  ? 0.2299 0.2021 0.3584 -0.0473 -0.0971 0.0258  15  ASN   B CB  
4156 C  CG  . ASN   B 15  ? 0.2076 0.1922 0.3759 -0.0470 -0.0609 0.0356  15  ASN   B CG  
4157 O  OD1 . ASN   B 15  ? 0.2142 0.2238 0.4050 -0.0660 -0.0561 0.0475  15  ASN   B OD1 
4158 N  ND2 . ASN   B 15  ? 0.2002 0.1661 0.3568 -0.0266 -0.0199 0.0051  15  ASN   B ND2 
4166 N  N   . VAL   B 16  ? 0.2247 0.1791 0.3212 -0.0563 -0.0855 0.0280  16  VAL   B N   
4167 C  CA  . VAL   B 16  ? 0.2308 0.1779 0.3247 -0.0494 -0.0801 -0.0028 16  VAL   B CA  
4168 C  C   . VAL   B 16  ? 0.2323 0.1991 0.3135 -0.0721 -0.0779 0.0099  16  VAL   B C   
4169 O  O   . VAL   B 16  ? 0.2370 0.2163 0.3412 -0.0696 -0.0805 -0.0012 16  VAL   B O   
4170 C  CB  . VAL   B 16  ? 0.2242 0.1667 0.3374 -0.0299 -0.0572 -0.0011 16  VAL   B CB  
4171 C  CG1 . VAL   B 16  ? 0.2383 0.1631 0.3350 -0.0146 -0.0413 0.0142  16  VAL   B CG1 
4172 C  CG2 . VAL   B 16  ? 0.2221 0.1669 0.3505 -0.0209 -0.0266 -0.0069 16  VAL   B CG2 
4182 N  N   . TYR   B 17  ? 0.2520 0.2211 0.3037 -0.0797 -0.0669 0.0032  17  TYR   B N   
4183 C  CA  . TYR   B 17  ? 0.2634 0.2276 0.2881 -0.0922 -0.0715 0.0215  17  TYR   B CA  
4184 C  C   . TYR   B 17  ? 0.2516 0.1946 0.2911 -0.0880 -0.0441 0.0107  17  TYR   B C   
4185 O  O   . TYR   B 17  ? 0.2352 0.2037 0.3115 -0.0680 -0.0437 -0.0360 17  TYR   B O   
4186 C  CB  . TYR   B 17  ? 0.2919 0.2847 0.3047 -0.0902 -0.0768 0.0492  17  TYR   B CB  
4187 C  CG  . TYR   B 17  ? 0.3211 0.3548 0.3402 -0.0863 -0.0866 0.0576  17  TYR   B CG  
4188 C  CD1 . TYR   B 17  ? 0.3376 0.3814 0.3633 -0.0855 -0.0970 0.0666  17  TYR   B CD1 
4189 C  CD2 . TYR   B 17  ? 0.3451 0.3885 0.3684 -0.0731 -0.0853 0.0600  17  TYR   B CD2 
4190 C  CE1 . TYR   B 17  ? 0.3575 0.4007 0.3818 -0.0743 -0.1098 0.0653  17  TYR   B CE1 
4191 C  CE2 . TYR   B 17  ? 0.3621 0.4029 0.3858 -0.0605 -0.1026 0.0692  17  TYR   B CE2 
4192 C  CZ  . TYR   B 17  ? 0.3731 0.4104 0.3962 -0.0605 -0.1107 0.0636  17  TYR   B CZ  
4193 O  OH  . TYR   B 17  ? 0.3857 0.4385 0.4074 -0.0468 -0.1190 0.0652  17  TYR   B OH  
4203 N  N   . ILE   B 18  ? 0.2639 0.1981 0.2650 -0.0793 -0.0280 0.0111  18  ILE   B N   
4204 C  CA  . ILE   B 18  ? 0.2659 0.1941 0.2785 -0.0775 -0.0123 -0.0176 18  ILE   B CA  
4205 C  C   . ILE   B 18  ? 0.2755 0.2062 0.2768 -0.0875 -0.0065 -0.0356 18  ILE   B C   
4206 O  O   . ILE   B 18  ? 0.2915 0.2179 0.2960 -0.0806 -0.0090 -0.0403 18  ILE   B O   
4207 C  CB  . ILE   B 18  ? 0.2634 0.1934 0.2893 -0.0809 -0.0206 -0.0155 18  ILE   B CB  
4208 C  CG1 . ILE   B 18  ? 0.2532 0.2017 0.3008 -0.0818 -0.0033 -0.0185 18  ILE   B CG1 
4209 C  CG2 . ILE   B 18  ? 0.2651 0.1987 0.2944 -0.0818 -0.0358 -0.0039 18  ILE   B CG2 
4210 C  CD1 . ILE   B 18  ? 0.2571 0.2272 0.3101 -0.0778 -0.0192 0.0064  18  ILE   B CD1 
4222 N  N   . LYS   B 19  ? 0.2811 0.2075 0.2851 -0.0656 0.0402  -0.0534 19  LYS   B N   
4223 C  CA  . LYS   B 19  ? 0.2804 0.2019 0.3071 -0.0697 0.0276  -0.0540 19  LYS   B CA  
4224 C  C   . LYS   B 19  ? 0.2569 0.1951 0.3246 -0.0538 0.0320  -0.0628 19  LYS   B C   
4225 O  O   . LYS   B 19  ? 0.2449 0.1999 0.3181 -0.0456 0.0274  -0.0525 19  LYS   B O   
4226 C  CB  . LYS   B 19  ? 0.3144 0.2245 0.3162 -0.0720 0.0375  -0.0514 19  LYS   B CB  
4227 C  CG  . LYS   B 19  ? 0.3491 0.2348 0.3456 -0.0852 0.0405  -0.0518 19  LYS   B CG  
4228 C  CD  . LYS   B 19  ? 0.3823 0.2540 0.3555 -0.0927 0.0568  -0.0397 19  LYS   B CD  
4229 C  CE  . LYS   B 19  ? 0.4122 0.2792 0.3678 -0.0914 0.0561  -0.0343 19  LYS   B CE  
4230 N  NZ  . LYS   B 19  ? 0.4377 0.2979 0.3772 -0.0893 0.0619  -0.0316 19  LYS   B NZ  
4244 N  N   . ASN   B 20  ? 0.2623 0.2010 0.3520 -0.0479 0.0485  -0.0668 20  ASN   B N   
4245 C  CA  . ASN   B 20  ? 0.2586 0.2107 0.3816 -0.0411 0.0648  -0.0870 20  ASN   B CA  
4246 C  C   . ASN   B 20  ? 0.2551 0.2353 0.3741 -0.0476 0.0707  -0.1012 20  ASN   B C   
4247 O  O   . ASN   B 20  ? 0.2835 0.2755 0.3851 -0.0637 0.0773  -0.0997 20  ASN   B O   
4248 C  CB  . ASN   B 20  ? 0.2828 0.2171 0.4120 -0.0116 0.0592  -0.0884 20  ASN   B CB  
4249 C  CG  . ASN   B 20  ? 0.3093 0.2244 0.4332 0.0195  0.0563  -0.1028 20  ASN   B CG  
4250 O  OD1 . ASN   B 20  ? 0.3452 0.2549 0.4621 0.0341  0.0500  -0.1028 20  ASN   B OD1 
4251 N  ND2 . ASN   B 20  ? 0.2930 0.2219 0.4381 0.0232  0.0441  -0.1004 20  ASN   B ND2 
4258 N  N   . ALA   B 21  ? 0.2550 0.2225 0.3739 -0.0503 0.0642  -0.0814 21  ALA   B N   
4259 C  CA  . ALA   B 21  ? 0.2554 0.2372 0.3737 -0.0527 0.0601  -0.0672 21  ALA   B CA  
4260 C  C   . ALA   B 21  ? 0.2526 0.2122 0.3603 -0.0410 0.0578  -0.0422 21  ALA   B C   
4261 O  O   . ALA   B 21  ? 0.2529 0.1908 0.3767 -0.0525 0.0558  -0.0430 21  ALA   B O   
4262 C  CB  . ALA   B 21  ? 0.2619 0.2686 0.3796 -0.0752 0.0703  -0.0479 21  ALA   B CB  
4268 N  N   . ASP   B 22  ? 0.2354 0.1933 0.3482 -0.0399 0.0464  -0.0360 22  ASP   B N   
4269 C  CA  . ASP   B 22  ? 0.2243 0.1864 0.3422 -0.0202 0.0332  -0.0266 22  ASP   B CA  
4270 C  C   . ASP   B 22  ? 0.2121 0.1832 0.3202 -0.0290 0.0270  -0.0175 22  ASP   B C   
4271 O  O   . ASP   B 22  ? 0.2133 0.1866 0.3139 -0.0189 0.0223  -0.0231 22  ASP   B O   
4272 C  CB  . ASP   B 22  ? 0.2316 0.1976 0.3752 -0.0072 0.0329  -0.0191 22  ASP   B CB  
4273 C  CG  . ASP   B 22  ? 0.2306 0.2192 0.4121 0.0012  0.0177  -0.0166 22  ASP   B CG  
4274 O  OD1 . ASP   B 22  ? 0.2373 0.2076 0.4150 -0.0118 -0.0005 -0.0150 22  ASP   B OD1 
4275 O  OD2 . ASP   B 22  ? 0.2376 0.2514 0.4502 0.0135  0.0026  -0.0332 22  ASP   B OD2 
4280 N  N   . ILE   B 23  ? 0.2114 0.1760 0.3058 -0.0305 0.0035  0.0130  23  ILE   B N   
4281 C  CA  . ILE   B 23  ? 0.1982 0.1689 0.2806 -0.0278 -0.0095 0.0072  23  ILE   B CA  
4282 C  C   . ILE   B 23  ? 0.1951 0.1732 0.2658 -0.0218 -0.0166 -0.0024 23  ILE   B C   
4283 O  O   . ILE   B 23  ? 0.1818 0.1645 0.2501 -0.0228 -0.0101 0.0039  23  ILE   B O   
4284 C  CB  . ILE   B 23  ? 0.1940 0.1791 0.2852 -0.0364 -0.0125 0.0217  23  ILE   B CB  
4285 C  CG1 . ILE   B 23  ? 0.1856 0.1939 0.2899 -0.0198 -0.0078 0.0306  23  ILE   B CG1 
4286 C  CG2 . ILE   B 23  ? 0.1979 0.2007 0.2924 -0.0324 -0.0045 0.0253  23  ILE   B CG2 
4287 C  CD1 . ILE   B 23  ? 0.1922 0.2053 0.2914 -0.0175 -0.0086 0.0240  23  ILE   B CD1 
4299 N  N   . VAL   B 24  ? 0.1951 0.1696 0.2659 -0.0204 -0.0180 0.0003  24  VAL   B N   
4300 C  CA  . VAL   B 24  ? 0.1934 0.1715 0.2776 -0.0133 -0.0218 0.0023  24  VAL   B CA  
4301 C  C   . VAL   B 24  ? 0.1977 0.1824 0.2850 -0.0151 -0.0106 0.0027  24  VAL   B C   
4302 O  O   . VAL   B 24  ? 0.1811 0.1938 0.2851 -0.0205 -0.0070 0.0165  24  VAL   B O   
4303 C  CB  . VAL   B 24  ? 0.1987 0.1917 0.2795 -0.0019 -0.0261 0.0068  24  VAL   B CB  
4304 C  CG1 . VAL   B 24  ? 0.1879 0.1961 0.2882 -0.0152 -0.0189 -0.0024 24  VAL   B CG1 
4305 C  CG2 . VAL   B 24  ? 0.2145 0.2159 0.2611 0.0031  -0.0294 -0.0023 24  VAL   B CG2 
4315 N  N   . GLU   B 25  ? 0.2131 0.1902 0.2845 -0.0202 -0.0068 0.0013  25  GLU   B N   
4316 C  CA  . GLU   B 25  ? 0.2216 0.2258 0.3045 -0.0158 0.0099  -0.0048 25  GLU   B CA  
4317 C  C   . GLU   B 25  ? 0.2188 0.2213 0.2681 -0.0256 0.0136  0.0005  25  GLU   B C   
4318 O  O   . GLU   B 25  ? 0.2232 0.2301 0.2886 -0.0282 0.0204  0.0038  25  GLU   B O   
4319 C  CB  . GLU   B 25  ? 0.2552 0.2843 0.3845 0.0082  0.0219  0.0006  25  GLU   B CB  
4320 C  CG  . GLU   B 25  ? 0.2960 0.3350 0.4733 0.0202  0.0158  -0.0055 25  GLU   B CG  
4321 C  CD  . GLU   B 25  ? 0.3351 0.3873 0.5422 0.0209  0.0130  -0.0076 25  GLU   B CD  
4322 O  OE1 . GLU   B 25  ? 0.3457 0.4311 0.5792 0.0291  0.0181  -0.0064 25  GLU   B OE1 
4323 O  OE2 . GLU   B 25  ? 0.3469 0.4178 0.5746 0.0211  0.0103  -0.0150 25  GLU   B OE2 
4330 N  N   A GLU   B 26  ? 0.2143 0.2138 0.2469 -0.0408 0.0086  0.0010  26  GLU   B N   
4331 N  N   B GLU   B 26  ? 0.2080 0.2156 0.2483 -0.0394 0.0032  0.0024  26  GLU   B N   
4332 C  CA  A GLU   B 26  ? 0.2151 0.2281 0.2547 -0.0454 -0.0045 0.0027  26  GLU   B CA  
4333 C  CA  B GLU   B 26  ? 0.2025 0.2175 0.2480 -0.0449 -0.0121 0.0036  26  GLU   B CA  
4334 C  C   A GLU   B 26  ? 0.2000 0.2193 0.2466 -0.0356 -0.0006 0.0126  26  GLU   B C   
4335 C  C   B GLU   B 26  ? 0.1943 0.2114 0.2398 -0.0362 -0.0019 0.0138  26  GLU   B C   
4336 O  O   A GLU   B 26  ? 0.2149 0.2338 0.2607 -0.0244 0.0003  0.0171  26  GLU   B O   
4337 O  O   B GLU   B 26  ? 0.2048 0.2203 0.2416 -0.0290 -0.0012 0.0173  26  GLU   B O   
4338 C  CB  A GLU   B 26  ? 0.2520 0.2535 0.2707 -0.0502 0.0035  0.0171  26  GLU   B CB  
4339 C  CB  B GLU   B 26  ? 0.2183 0.2261 0.2657 -0.0531 -0.0257 0.0067  26  GLU   B CB  
4340 C  CG  A GLU   B 26  ? 0.2969 0.2866 0.3025 -0.0518 0.0258  0.0101  26  GLU   B CG  
4341 C  CG  B GLU   B 26  ? 0.2400 0.2405 0.2925 -0.0591 -0.0261 -0.0051 26  GLU   B CG  
4342 C  CD  A GLU   B 26  ? 0.3216 0.3006 0.3188 -0.0715 0.0606  0.0068  26  GLU   B CD  
4343 C  CD  B GLU   B 26  ? 0.2423 0.2374 0.3059 -0.0793 -0.0260 -0.0210 26  GLU   B CD  
4344 O  OE1 A GLU   B 26  ? 0.3379 0.3003 0.3312 -0.0803 0.0943  0.0311  26  GLU   B OE1 
4345 O  OE1 B GLU   B 26  ? 0.2436 0.2382 0.3320 -0.1039 -0.0073 -0.0323 26  GLU   B OE1 
4346 O  OE2 A GLU   B 26  ? 0.3255 0.3108 0.3377 -0.0773 0.0643  0.0071  26  GLU   B OE2 
4347 O  OE2 B GLU   B 26  ? 0.2418 0.2368 0.3060 -0.0735 -0.0246 -0.0118 26  GLU   B OE2 
4360 N  N   . ALA   B 27  ? 0.1807 0.2002 0.2512 -0.0341 0.0035  0.0206  27  ALA   B N   
4361 C  CA  . ALA   B 27  ? 0.1820 0.1992 0.2698 -0.0251 -0.0170 0.0351  27  ALA   B CA  
4362 C  C   . ALA   B 27  ? 0.1823 0.2086 0.2911 -0.0272 -0.0068 0.0470  27  ALA   B C   
4363 O  O   . ALA   B 27  ? 0.1865 0.2165 0.3009 -0.0186 -0.0112 0.0482  27  ALA   B O   
4364 C  CB  . ALA   B 27  ? 0.1944 0.1918 0.2723 -0.0262 -0.0143 0.0303  27  ALA   B CB  
4371 N  N   . LYS   B 28  ? 0.1789 0.2258 0.3282 -0.0302 0.0042  0.0613  28  LYS   B N   
4372 C  CA  . LYS   B 28  ? 0.2063 0.2672 0.3330 -0.0155 0.0432  0.0883  28  LYS   B CA  
4373 C  C   . LYS   B 28  ? 0.2450 0.2927 0.3164 -0.0003 0.0514  0.0842  28  LYS   B C   
4374 O  O   . LYS   B 28  ? 0.2589 0.3039 0.3336 0.0013  0.0638  0.0912  28  LYS   B O   
4375 C  CB  . LYS   B 28  ? 0.2328 0.3182 0.3581 0.0019  0.0726  0.1050  28  LYS   B CB  
4376 C  CG  . LYS   B 28  ? 0.2563 0.3779 0.4052 0.0091  0.0816  0.1069  28  LYS   B CG  
4377 C  CD  . LYS   B 28  ? 0.2906 0.4250 0.4488 0.0133  0.1038  0.1113  28  LYS   B CD  
4378 C  CE  . LYS   B 28  ? 0.3582 0.4798 0.4884 0.0200  0.1066  0.1118  28  LYS   B CE  
4379 N  NZ  . LYS   B 28  ? 0.3994 0.5450 0.5247 0.0266  0.1055  0.1134  28  LYS   B NZ  
4393 N  N   A LYS   B 29  ? 0.2654 0.3120 0.3191 0.0131  0.0454  0.0712  29  LYS   B N   
4394 N  N   B LYS   B 29  ? 0.2659 0.3117 0.3196 0.0032  0.0433  0.0723  29  LYS   B N   
4395 C  CA  A LYS   B 29  ? 0.2992 0.3360 0.3474 0.0089  0.0428  0.0591  29  LYS   B CA  
4396 C  CA  B LYS   B 29  ? 0.2910 0.3309 0.3422 0.0000  0.0375  0.0612  29  LYS   B CA  
4397 C  C   A LYS   B 29  ? 0.2920 0.3306 0.3252 0.0037  0.0369  0.0641  29  LYS   B C   
4398 C  C   B LYS   B 29  ? 0.2843 0.3233 0.3204 -0.0031 0.0335  0.0638  29  LYS   B C   
4399 O  O   A LYS   B 29  ? 0.3087 0.3532 0.3415 0.0097  0.0405  0.0697  29  LYS   B O   
4400 O  O   B LYS   B 29  ? 0.2952 0.3350 0.3251 0.0020  0.0376  0.0682  29  LYS   B O   
4401 C  CB  A LYS   B 29  ? 0.3452 0.3648 0.4159 0.0023  0.0438  0.0429  29  LYS   B CB  
4402 C  CB  B LYS   B 29  ? 0.3234 0.3559 0.4007 -0.0038 0.0354  0.0479  29  LYS   B CB  
4403 C  CG  A LYS   B 29  ? 0.3860 0.3893 0.4836 -0.0048 0.0445  0.0354  29  LYS   B CG  
4404 C  CG  B LYS   B 29  ? 0.3507 0.3771 0.4575 -0.0072 0.0329  0.0388  29  LYS   B CG  
4405 C  CD  A LYS   B 29  ? 0.4125 0.4059 0.5423 -0.0113 0.0524  0.0259  29  LYS   B CD  
4406 C  CD  B LYS   B 29  ? 0.3717 0.3925 0.5060 -0.0105 0.0352  0.0290  29  LYS   B CD  
4407 C  CE  A LYS   B 29  ? 0.4275 0.4172 0.5857 -0.0164 0.0611  0.0191  29  LYS   B CE  
4408 C  CE  B LYS   B 29  ? 0.3874 0.4028 0.5431 -0.0138 0.0389  0.0217  29  LYS   B CE  
4409 N  NZ  A LYS   B 29  ? 0.4396 0.4273 0.6034 -0.0179 0.0629  0.0170  29  LYS   B NZ  
4410 N  NZ  B LYS   B 29  ? 0.3971 0.4111 0.5582 -0.0154 0.0394  0.0188  29  LYS   B NZ  
4437 N  N   . VAL   B 30  ? 0.2636 0.3028 0.3063 -0.0143 0.0221  0.0635  30  VAL   B N   
4438 C  CA  . VAL   B 30  ? 0.2444 0.2805 0.3130 -0.0298 -0.0113 0.0651  30  VAL   B CA  
4439 C  C   . VAL   B 30  ? 0.2180 0.2623 0.2845 -0.0342 -0.0232 0.0688  30  VAL   B C   
4440 O  O   . VAL   B 30  ? 0.2253 0.2734 0.2942 -0.0262 -0.0218 0.0816  30  VAL   B O   
4441 C  CB  . VAL   B 30  ? 0.2472 0.2740 0.3444 -0.0507 -0.0330 0.0811  30  VAL   B CB  
4442 C  CG1 . VAL   B 30  ? 0.2606 0.3009 0.3554 -0.0431 -0.0371 0.0671  30  VAL   B CG1 
4443 C  CG2 . VAL   B 30  ? 0.2592 0.2679 0.3582 -0.0641 -0.0366 0.0640  30  VAL   B CG2 
4454 N  N   A LYS   B 31  ? 0.2005 0.2367 0.2976 -0.0535 -0.0325 0.0736  31  LYS   B N   
4455 N  N   B LYS   B 31  ? 0.2194 0.2494 0.2824 -0.0396 -0.0294 0.0608  31  LYS   B N   
4456 C  CA  A LYS   B 31  ? 0.1847 0.2386 0.3229 -0.0579 -0.0249 0.0748  31  LYS   B CA  
4457 C  CA  B LYS   B 31  ? 0.2194 0.2464 0.2912 -0.0391 -0.0303 0.0536  31  LYS   B CA  
4458 C  C   A LYS   B 31  ? 0.1830 0.2047 0.3034 -0.0493 -0.0325 0.0639  31  LYS   B C   
4459 C  C   B LYS   B 31  ? 0.2081 0.2121 0.2759 -0.0397 -0.0383 0.0491  31  LYS   B C   
4460 O  O   A LYS   B 31  ? 0.1799 0.2117 0.3282 -0.0455 -0.0263 0.0717  31  LYS   B O   
4461 O  O   B LYS   B 31  ? 0.2082 0.2147 0.2773 -0.0381 -0.0375 0.0537  31  LYS   B O   
4462 C  CB  A LYS   B 31  ? 0.1970 0.2892 0.3670 -0.0520 0.0015  0.0834  31  LYS   B CB  
4463 C  CB  B LYS   B 31  ? 0.2372 0.2789 0.3243 -0.0317 -0.0203 0.0496  31  LYS   B CB  
4464 C  CG  A LYS   B 31  ? 0.2235 0.3312 0.4159 -0.0512 0.0135  0.0837  31  LYS   B CG  
4465 C  CG  B LYS   B 31  ? 0.2568 0.3038 0.3627 -0.0296 -0.0143 0.0427  31  LYS   B CG  
4466 C  CD  A LYS   B 31  ? 0.2474 0.3643 0.4591 -0.0429 0.0057  0.0782  31  LYS   B CD  
4467 C  CD  B LYS   B 31  ? 0.2746 0.3277 0.3977 -0.0276 -0.0144 0.0367  31  LYS   B CD  
4468 C  CE  A LYS   B 31  ? 0.2598 0.3843 0.4972 -0.0351 -0.0077 0.0714  31  LYS   B CE  
4469 C  CE  B LYS   B 31  ? 0.2892 0.3429 0.4280 -0.0268 -0.0170 0.0315  31  LYS   B CE  
4470 N  NZ  A LYS   B 31  ? 0.2858 0.4161 0.5154 -0.0246 -0.0156 0.0582  31  LYS   B NZ  
4471 N  NZ  B LYS   B 31  ? 0.3029 0.3537 0.4417 -0.0238 -0.0204 0.0232  31  LYS   B NZ  
4498 N  N   . PRO   B 32  ? 0.2006 0.1830 0.2729 -0.0438 -0.0456 0.0439  32  PRO   B N   
4499 C  CA  . PRO   B 32  ? 0.2113 0.1798 0.2573 -0.0440 -0.0419 0.0328  32  PRO   B CA  
4500 C  C   . PRO   B 32  ? 0.2200 0.1673 0.2534 -0.0499 -0.0589 0.0362  32  PRO   B C   
4501 O  O   . PRO   B 32  ? 0.2293 0.1673 0.2824 -0.0524 -0.0730 0.0359  32  PRO   B O   
4502 C  CB  . PRO   B 32  ? 0.2257 0.1704 0.2596 -0.0553 -0.0386 0.0304  32  PRO   B CB  
4503 C  CG  . PRO   B 32  ? 0.2395 0.1600 0.2559 -0.0448 -0.0526 0.0413  32  PRO   B CG  
4504 C  CD  . PRO   B 32  ? 0.2243 0.1731 0.2613 -0.0370 -0.0742 0.0252  32  PRO   B CD  
4512 N  N   . THR   B 33  ? 0.2205 0.1577 0.2432 -0.0507 -0.0577 0.0307  33  THR   B N   
4513 C  CA  . THR   B 33  ? 0.2191 0.1651 0.2585 -0.0487 -0.0494 0.0373  33  THR   B CA  
4514 C  C   . THR   B 33  ? 0.2174 0.1573 0.2470 -0.0469 -0.0463 0.0242  33  THR   B C   
4515 O  O   . THR   B 33  ? 0.2391 0.1662 0.2383 -0.0598 -0.0538 0.0265  33  THR   B O   
4516 C  CB  . THR   B 33  ? 0.2324 0.1797 0.2607 -0.0355 -0.0444 0.0374  33  THR   B CB  
4517 O  OG1 . THR   B 33  ? 0.2151 0.1867 0.2671 -0.0419 -0.0543 0.0462  33  THR   B OG1 
4518 C  CG2 . THR   B 33  ? 0.2590 0.1892 0.2704 -0.0270 -0.0434 0.0310  33  THR   B CG2 
4526 N  N   . VAL   B 34  ? 0.2021 0.1541 0.2327 -0.0457 -0.0417 0.0208  34  VAL   B N   
4527 C  CA  . VAL   B 34  ? 0.1923 0.1522 0.2458 -0.0438 -0.0371 0.0162  34  VAL   B CA  
4528 C  C   . VAL   B 34  ? 0.1725 0.1506 0.2416 -0.0376 -0.0278 0.0139  34  VAL   B C   
4529 O  O   . VAL   B 34  ? 0.1913 0.1561 0.2326 -0.0339 -0.0389 0.0213  34  VAL   B O   
4530 C  CB  . VAL   B 34  ? 0.2016 0.1673 0.2499 -0.0163 -0.0316 0.0166  34  VAL   B CB  
4531 C  CG1 . VAL   B 34  ? 0.1894 0.1827 0.2405 -0.0184 -0.0105 -0.0122 34  VAL   B CG1 
4532 C  CG2 . VAL   B 34  ? 0.2022 0.1721 0.2698 -0.0199 -0.0396 0.0165  34  VAL   B CG2 
4542 N  N   . VAL   B 35  ? 0.1687 0.1449 0.2209 -0.0348 -0.0153 0.0114  35  VAL   B N   
4543 C  CA  . VAL   B 35  ? 0.1621 0.1438 0.2263 -0.0269 -0.0083 0.0064  35  VAL   B CA  
4544 C  C   . VAL   B 35  ? 0.1466 0.1422 0.2189 -0.0196 -0.0184 0.0071  35  VAL   B C   
4545 O  O   . VAL   B 35  ? 0.1541 0.1469 0.2012 -0.0285 -0.0052 -0.0044 35  VAL   B O   
4546 C  CB  . VAL   B 35  ? 0.1577 0.1630 0.2515 -0.0271 -0.0052 0.0007  35  VAL   B CB  
4547 C  CG1 . VAL   B 35  ? 0.1500 0.1734 0.2610 -0.0348 -0.0080 -0.0051 35  VAL   B CG1 
4548 C  CG2 . VAL   B 35  ? 0.1603 0.1669 0.2605 -0.0193 -0.0014 0.0017  35  VAL   B CG2 
4558 N  N   . VAL   B 36  ? 0.1498 0.1481 0.2268 -0.0173 -0.0176 0.0048  36  VAL   B N   
4559 C  CA  . VAL   B 36  ? 0.1462 0.1345 0.2298 -0.0140 -0.0064 0.0055  36  VAL   B CA  
4560 C  C   . VAL   B 36  ? 0.1410 0.1431 0.2258 -0.0118 -0.0015 0.0061  36  VAL   B C   
4561 O  O   . VAL   B 36  ? 0.1532 0.1566 0.2225 -0.0186 0.0005  -0.0061 36  VAL   B O   
4562 C  CB  . VAL   B 36  ? 0.1500 0.1430 0.2359 -0.0247 -0.0057 0.0019  36  VAL   B CB  
4563 C  CG1 . VAL   B 36  ? 0.1469 0.1605 0.2347 -0.0195 -0.0080 0.0096  36  VAL   B CG1 
4564 C  CG2 . VAL   B 36  ? 0.1529 0.1527 0.2488 -0.0252 -0.0140 0.0131  36  VAL   B CG2 
4574 N  N   . ASN   B 37  ? 0.1471 0.1435 0.2258 -0.0042 -0.0062 0.0092  37  ASN   B N   
4575 C  CA  . ASN   B 37  ? 0.1493 0.1461 0.2370 -0.0070 -0.0140 0.0096  37  ASN   B CA  
4576 C  C   . ASN   B 37  ? 0.1491 0.1472 0.2445 0.0003  -0.0099 0.0024  37  ASN   B C   
4577 O  O   . ASN   B 37  ? 0.1658 0.1569 0.2141 -0.0090 0.0006  0.0117  37  ASN   B O   
4578 C  CB  . ASN   B 37  ? 0.1500 0.1509 0.2342 -0.0102 -0.0161 -0.0026 37  ASN   B CB  
4579 C  CG  . ASN   B 37  ? 0.1588 0.1535 0.2348 -0.0030 -0.0250 0.0076  37  ASN   B CG  
4580 O  OD1 . ASN   B 37  ? 0.1695 0.1529 0.2507 0.0083  -0.0179 0.0052  37  ASN   B OD1 
4581 N  ND2 . ASN   B 37  ? 0.1597 0.1503 0.2351 -0.0043 -0.0214 0.0144  37  ASN   B ND2 
4588 N  N   . ALA   B 38  ? 0.1692 0.1442 0.2411 0.0048  -0.0116 -0.0020 38  ALA   B N   
4589 C  CA  . ALA   B 38  ? 0.1841 0.1451 0.2453 -0.0065 -0.0043 0.0160  38  ALA   B CA  
4590 C  C   . ALA   B 38  ? 0.1792 0.1408 0.2344 -0.0044 -0.0003 0.0134  38  ALA   B C   
4591 O  O   . ALA   B 38  ? 0.1932 0.1515 0.2374 0.0043  -0.0012 0.0159  38  ALA   B O   
4592 C  CB  . ALA   B 38  ? 0.2067 0.1623 0.2618 -0.0168 0.0052  0.0132  38  ALA   B CB  
4598 N  N   . ALA   B 39  ? 0.1778 0.1449 0.2303 0.0055  -0.0079 0.0118  39  ALA   B N   
4599 C  CA  . ALA   B 39  ? 0.1860 0.1510 0.2326 0.0084  -0.0057 0.0170  39  ALA   B CA  
4600 C  C   . ALA   B 39  ? 0.2011 0.1522 0.2187 0.0130  -0.0129 0.0114  39  ALA   B C   
4601 O  O   . ALA   B 39  ? 0.2096 0.1594 0.2347 -0.0042 -0.0157 0.0127  39  ALA   B O   
4602 C  CB  . ALA   B 39  ? 0.1708 0.1560 0.2372 0.0030  0.0000  0.0140  39  ALA   B CB  
4608 N  N   . ASN   B 40  ? 0.2005 0.1736 0.2157 0.0090  -0.0121 0.0011  40  ASN   B N   
4609 C  CA  . ASN   B 40  ? 0.2115 0.1813 0.2265 0.0131  -0.0164 0.0007  40  ASN   B CA  
4610 C  C   . ASN   B 40  ? 0.2201 0.1759 0.2191 0.0145  -0.0184 0.0020  40  ASN   B C   
4611 O  O   . ASN   B 40  ? 0.2123 0.1628 0.2399 0.0157  -0.0170 0.0111  40  ASN   B O   
4612 C  CB  . ASN   B 40  ? 0.2245 0.1798 0.2414 0.0201  -0.0249 0.0179  40  ASN   B CB  
4613 C  CG  . ASN   B 40  ? 0.2322 0.1841 0.2733 0.0185  -0.0351 0.0231  40  ASN   B CG  
4614 O  OD1 . ASN   B 40  ? 0.2334 0.1763 0.3386 0.0079  -0.0419 0.0302  40  ASN   B OD1 
4615 N  ND2 . ASN   B 40  ? 0.2311 0.1827 0.2640 0.0175  -0.0236 0.0297  40  ASN   B ND2 
4622 N  N   . VAL   B 41  ? 0.2344 0.1809 0.2180 0.0210  0.0038  0.0020  41  VAL   B N   
4623 C  CA  . VAL   B 41  ? 0.2450 0.1894 0.2213 0.0133  0.0047  -0.0004 41  VAL   B CA  
4624 C  C   . VAL   B 41  ? 0.2414 0.1864 0.2257 0.0258  0.0001  0.0007  41  VAL   B C   
4625 O  O   . VAL   B 41  ? 0.2230 0.1909 0.2275 0.0257  0.0033  -0.0046 41  VAL   B O   
4626 C  CB  . VAL   B 41  ? 0.2623 0.2020 0.2348 -0.0046 0.0280  -0.0119 41  VAL   B CB  
4627 C  CG1 . VAL   B 41  ? 0.2622 0.1973 0.2414 -0.0095 0.0433  -0.0242 41  VAL   B CG1 
4628 C  CG2 . VAL   B 41  ? 0.2670 0.2231 0.2442 -0.0191 0.0211  -0.0091 41  VAL   B CG2 
4638 N  N   . TYR   B 42  ? 0.2552 0.1823 0.2107 0.0280  -0.0147 0.0086  42  TYR   B N   
4639 C  CA  . TYR   B 42  ? 0.2531 0.1896 0.2139 0.0314  -0.0284 -0.0010 42  TYR   B CA  
4640 C  C   . TYR   B 42  ? 0.2289 0.1803 0.2294 0.0319  -0.0302 -0.0058 42  TYR   B C   
4641 O  O   . TYR   B 42  ? 0.2284 0.1907 0.2577 0.0206  -0.0297 -0.0079 42  TYR   B O   
4642 C  CB  . TYR   B 42  ? 0.2657 0.2186 0.2200 0.0236  -0.0265 0.0051  42  TYR   B CB  
4643 C  CG  . TYR   B 42  ? 0.2540 0.2324 0.2155 0.0110  -0.0259 0.0133  42  TYR   B CG  
4644 C  CD1 . TYR   B 42  ? 0.2349 0.2310 0.1995 -0.0010 -0.0171 0.0169  42  TYR   B CD1 
4645 C  CD2 . TYR   B 42  ? 0.2596 0.2395 0.2337 0.0038  -0.0163 0.0205  42  TYR   B CD2 
4646 C  CE1 . TYR   B 42  ? 0.2332 0.2391 0.2028 -0.0013 -0.0118 0.0072  42  TYR   B CE1 
4647 C  CE2 . TYR   B 42  ? 0.2462 0.2447 0.2270 0.0035  0.0089  0.0316  42  TYR   B CE2 
4648 C  CZ  . TYR   B 42  ? 0.2426 0.2554 0.2161 0.0218  0.0080  0.0106  42  TYR   B CZ  
4649 O  OH  . TYR   B 42  ? 0.2692 0.2907 0.2576 0.0378  0.0213  0.0184  42  TYR   B OH  
4659 N  N   . LEU   B 43  ? 0.2132 0.1618 0.2223 0.0217  -0.0210 -0.0051 43  LEU   B N   
4660 C  CA  . LEU   B 43  ? 0.2087 0.1681 0.2103 0.0091  -0.0186 0.0046  43  LEU   B CA  
4661 C  C   . LEU   B 43  ? 0.2133 0.1674 0.2126 0.0110  -0.0174 0.0009  43  LEU   B C   
4662 O  O   . LEU   B 43  ? 0.2102 0.1707 0.2292 0.0101  -0.0311 0.0003  43  LEU   B O   
4663 C  CB  . LEU   B 43  ? 0.1992 0.1621 0.2267 0.0010  -0.0183 0.0011  43  LEU   B CB  
4664 C  CG  . LEU   B 43  ? 0.2001 0.1583 0.2249 -0.0029 -0.0270 0.0045  43  LEU   B CG  
4665 C  CD1 . LEU   B 43  ? 0.2036 0.1664 0.2484 -0.0054 -0.0347 -0.0089 43  LEU   B CD1 
4666 C  CD2 . LEU   B 43  ? 0.2023 0.1651 0.2292 -0.0100 -0.0301 0.0002  43  LEU   B CD2 
4678 N  N   . LYS   B 44  ? 0.2147 0.1652 0.2096 0.0189  -0.0027 -0.0005 44  LYS   B N   
4679 C  CA  . LYS   B 44  ? 0.2249 0.1731 0.2241 0.0154  -0.0069 0.0083  44  LYS   B CA  
4680 C  C   . LYS   B 44  ? 0.2129 0.1747 0.2164 0.0203  -0.0124 -0.0039 44  LYS   B C   
4681 O  O   . LYS   B 44  ? 0.2391 0.1740 0.2564 0.0146  -0.0086 -0.0050 44  LYS   B O   
4682 C  CB  . LYS   B 44  ? 0.2539 0.1991 0.2430 0.0215  -0.0234 0.0028  44  LYS   B CB  
4683 C  CG  . LYS   B 44  ? 0.2991 0.2321 0.2797 0.0135  -0.0494 0.0022  44  LYS   B CG  
4684 C  CD  . LYS   B 44  ? 0.3311 0.2532 0.3306 -0.0010 -0.0674 -0.0003 44  LYS   B CD  
4685 C  CE  . LYS   B 44  ? 0.3579 0.2865 0.3938 -0.0144 -0.0666 0.0097  44  LYS   B CE  
4686 N  NZ  . LYS   B 44  ? 0.3738 0.2990 0.4200 -0.0193 -0.0642 0.0184  44  LYS   B NZ  
4700 N  N   . HIS   B 45  ? 0.1989 0.1789 0.2239 0.0175  -0.0149 0.0109  45  HIS   B N   
4701 C  CA  . HIS   B 45  ? 0.1998 0.1782 0.2340 0.0102  -0.0000 -0.0032 45  HIS   B CA  
4702 C  C   . HIS   B 45  ? 0.2199 0.1967 0.2650 0.0215  -0.0125 -0.0095 45  HIS   B C   
4703 O  O   . HIS   B 45  ? 0.2347 0.2263 0.3085 0.0536  0.0120  0.0015  45  HIS   B O   
4704 C  CB  . HIS   B 45  ? 0.1899 0.1807 0.2396 0.0030  -0.0126 -0.0042 45  HIS   B CB  
4705 C  CG  . HIS   B 45  ? 0.1872 0.1727 0.2237 -0.0087 -0.0187 0.0000  45  HIS   B CG  
4706 N  ND1 . HIS   B 45  ? 0.1951 0.1684 0.2293 0.0014  -0.0339 -0.0125 45  HIS   B ND1 
4707 C  CD2 . HIS   B 45  ? 0.1920 0.1733 0.2162 -0.0063 -0.0164 0.0012  45  HIS   B CD2 
4708 C  CE1 . HIS   B 45  ? 0.1933 0.1523 0.2303 -0.0025 -0.0354 -0.0195 45  HIS   B CE1 
4709 N  NE2 . HIS   B 45  ? 0.2037 0.1639 0.2341 -0.0020 -0.0176 -0.0094 45  HIS   B NE2 
4717 N  N   . GLY   B 46  ? 0.2264 0.1877 0.3013 0.0216  -0.0433 -0.0070 46  GLY   B N   
4718 C  CA  . GLY   B 46  ? 0.2539 0.2008 0.3398 0.0200  -0.0515 -0.0114 46  GLY   B CA  
4719 C  C   . GLY   B 46  ? 0.2679 0.2232 0.3808 0.0255  -0.0469 -0.0001 46  GLY   B C   
4720 O  O   . GLY   B 46  ? 0.2773 0.2499 0.4622 0.0328  -0.0347 -0.0255 46  GLY   B O   
4724 N  N   . GLY   B 47  ? 0.2589 0.2251 0.3555 0.0020  -0.0244 0.0129  47  GLY   B N   
4725 C  CA  . GLY   B 47  ? 0.2332 0.1966 0.3144 -0.0017 -0.0158 0.0199  47  GLY   B CA  
4726 C  C   . GLY   B 47  ? 0.2157 0.1896 0.2811 -0.0058 -0.0039 0.0186  47  GLY   B C   
4727 O  O   . GLY   B 47  ? 0.2266 0.1759 0.2754 -0.0058 -0.0165 0.0216  47  GLY   B O   
4731 N  N   . GLY   B 48  ? 0.1940 0.1835 0.2811 -0.0027 -0.0176 0.0167  48  GLY   B N   
4732 C  CA  . GLY   B 48  ? 0.1895 0.1796 0.2808 -0.0198 -0.0117 0.0107  48  GLY   B CA  
4733 C  C   . GLY   B 48  ? 0.1818 0.1681 0.2743 -0.0082 -0.0054 0.0022  48  GLY   B C   
4734 O  O   . GLY   B 48  ? 0.1723 0.1667 0.3005 -0.0091 -0.0191 0.0040  48  GLY   B O   
4738 N  N   . VAL   B 49  ? 0.1816 0.1789 0.2610 0.0051  0.0035  -0.0027 49  VAL   B N   
4739 C  CA  . VAL   B 49  ? 0.1777 0.1875 0.2570 0.0068  -0.0184 -0.0098 49  VAL   B CA  
4740 C  C   . VAL   B 49  ? 0.1662 0.1717 0.2444 0.0086  -0.0103 -0.0093 49  VAL   B C   
4741 O  O   . VAL   B 49  ? 0.1782 0.1819 0.2594 -0.0003 -0.0151 -0.0089 49  VAL   B O   
4742 C  CB  . VAL   B 49  ? 0.1803 0.2040 0.2722 -0.0009 -0.0342 -0.0101 49  VAL   B CB  
4743 C  CG1 . VAL   B 49  ? 0.1792 0.2162 0.2586 0.0027  -0.0483 -0.0190 49  VAL   B CG1 
4744 C  CG2 . VAL   B 49  ? 0.1988 0.2214 0.2939 -0.0064 -0.0336 -0.0016 49  VAL   B CG2 
4754 N  N   . ALA   B 50  ? 0.1700 0.1638 0.2448 -0.0040 -0.0030 -0.0019 50  ALA   B N   
4755 C  CA  . ALA   B 50  ? 0.1650 0.1554 0.2424 -0.0006 -0.0081 -0.0009 50  ALA   B CA  
4756 C  C   . ALA   B 50  ? 0.1731 0.1637 0.2407 0.0037  -0.0149 -0.0021 50  ALA   B C   
4757 O  O   . ALA   B 50  ? 0.1730 0.1599 0.2348 0.0051  -0.0093 -0.0030 50  ALA   B O   
4758 C  CB  . ALA   B 50  ? 0.1740 0.1551 0.2302 -0.0052 -0.0090 0.0001  50  ALA   B CB  
4764 N  N   . GLY   B 51  ? 0.1737 0.1727 0.2527 0.0120  -0.0218 -0.0020 51  GLY   B N   
4765 C  CA  . GLY   B 51  ? 0.1778 0.1788 0.2622 0.0198  -0.0258 0.0059  51  GLY   B CA  
4766 C  C   . GLY   B 51  ? 0.1771 0.1737 0.2631 0.0231  -0.0077 -0.0038 51  GLY   B C   
4767 O  O   . GLY   B 51  ? 0.1713 0.1851 0.2771 0.0155  -0.0086 -0.0145 51  GLY   B O   
4771 N  N   . ALA   B 52  ? 0.1736 0.1681 0.2471 0.0140  -0.0019 -0.0015 52  ALA   B N   
4772 C  CA  . ALA   B 52  ? 0.1781 0.1716 0.2579 0.0121  -0.0025 -0.0029 52  ALA   B CA  
4773 C  C   . ALA   B 52  ? 0.1657 0.1637 0.2529 0.0017  -0.0029 -0.0035 52  ALA   B C   
4774 O  O   . ALA   B 52  ? 0.1618 0.1702 0.2866 0.0070  0.0007  -0.0083 52  ALA   B O   
4775 C  CB  . ALA   B 52  ? 0.1890 0.1739 0.2623 0.0016  0.0041  -0.0090 52  ALA   B CB  
4781 N  N   . LEU   B 53  ? 0.1589 0.1670 0.2398 0.0099  0.0097  -0.0034 53  LEU   B N   
4782 C  CA  . LEU   B 53  ? 0.1574 0.1763 0.2475 0.0109  -0.0034 -0.0089 53  LEU   B CA  
4783 C  C   . LEU   B 53  ? 0.1641 0.1666 0.2338 0.0090  -0.0006 -0.0045 53  LEU   B C   
4784 O  O   . LEU   B 53  ? 0.1725 0.1783 0.2403 -0.0012 -0.0043 0.0076  53  LEU   B O   
4785 C  CB  . LEU   B 53  ? 0.1566 0.1763 0.2611 0.0093  -0.0005 0.0097  53  LEU   B CB  
4786 C  CG  . LEU   B 53  ? 0.1585 0.1924 0.2504 0.0014  -0.0024 0.0154  53  LEU   B CG  
4787 C  CD1 . LEU   B 53  ? 0.1697 0.2112 0.2660 0.0151  -0.0087 0.0078  53  LEU   B CD1 
4788 C  CD2 . LEU   B 53  ? 0.1762 0.2224 0.2793 -0.0096 -0.0186 -0.0133 53  LEU   B CD2 
4800 N  N   . ASN   B 54  ? 0.1670 0.1559 0.2234 0.0054  -0.0031 -0.0010 54  ASN   B N   
4801 C  CA  . ASN   B 54  ? 0.1691 0.1691 0.2379 0.0021  0.0037  -0.0106 54  ASN   B CA  
4802 C  C   . ASN   B 54  ? 0.1653 0.1746 0.2821 0.0028  -0.0002 -0.0116 54  ASN   B C   
4803 O  O   . ASN   B 54  ? 0.1618 0.1814 0.2866 -0.0009 0.0026  -0.0219 54  ASN   B O   
4804 C  CB  . ASN   B 54  ? 0.1763 0.1799 0.2464 0.0004  0.0097  -0.0059 54  ASN   B CB  
4805 C  CG  . ASN   B 54  ? 0.1770 0.1874 0.2678 0.0056  -0.0072 -0.0044 54  ASN   B CG  
4806 O  OD1 . ASN   B 54  ? 0.1687 0.1843 0.2798 0.0004  -0.0187 -0.0132 54  ASN   B OD1 
4807 N  ND2 . ASN   B 54  ? 0.1862 0.2046 0.2857 0.0063  -0.0366 -0.0030 54  ASN   B ND2 
4814 N  N   . LYS   B 55  ? 0.1663 0.1815 0.2919 0.0137  -0.0044 -0.0063 55  LYS   B N   
4815 C  CA  . LYS   B 55  ? 0.1756 0.1918 0.2999 0.0219  0.0001  0.0045  55  LYS   B CA  
4816 C  C   . LYS   B 55  ? 0.1684 0.1901 0.2927 0.0110  0.0036  -0.0039 55  LYS   B C   
4817 O  O   . LYS   B 55  ? 0.1655 0.2142 0.3002 0.0103  0.0022  -0.0100 55  LYS   B O   
4818 C  CB  . LYS   B 55  ? 0.1930 0.2073 0.3405 0.0357  0.0031  0.0070  55  LYS   B CB  
4819 C  CG  . LYS   B 55  ? 0.2328 0.2410 0.3984 0.0384  0.0143  0.0082  55  LYS   B CG  
4820 C  CD  . LYS   B 55  ? 0.2770 0.2603 0.4603 0.0443  0.0298  0.0199  55  LYS   B CD  
4821 C  CE  . LYS   B 55  ? 0.3003 0.2683 0.5035 0.0469  0.0530  0.0238  55  LYS   B CE  
4822 N  NZ  . LYS   B 55  ? 0.3086 0.2799 0.5331 0.0398  0.0485  0.0363  55  LYS   B NZ  
4836 N  N   . ALA   B 56  ? 0.1645 0.1977 0.2823 0.0096  0.0077  -0.0052 56  ALA   B N   
4837 C  CA  . ALA   B 56  ? 0.1773 0.2177 0.2784 -0.0015 0.0106  -0.0043 56  ALA   B CA  
4838 C  C   . ALA   B 56  ? 0.1762 0.2109 0.2732 -0.0040 0.0087  -0.0016 56  ALA   B C   
4839 O  O   . ALA   B 56  ? 0.1843 0.2184 0.2848 0.0047  0.0283  0.0071  56  ALA   B O   
4840 C  CB  . ALA   B 56  ? 0.1885 0.2352 0.2758 -0.0246 0.0071  -0.0094 56  ALA   B CB  
4846 N  N   . THR   B 57  ? 0.1671 0.2026 0.2811 -0.0049 0.0172  -0.0090 57  THR   B N   
4847 C  CA  . THR   B 57  ? 0.1730 0.2007 0.2817 -0.0038 0.0248  -0.0097 57  THR   B CA  
4848 C  C   . THR   B 57  ? 0.1716 0.2052 0.3045 0.0000  0.0201  -0.0099 57  THR   B C   
4849 O  O   . THR   B 57  ? 0.1850 0.2008 0.3149 -0.0201 0.0138  -0.0140 57  THR   B O   
4850 C  CB  . THR   B 57  ? 0.1791 0.1787 0.2688 0.0028  0.0189  0.0029  57  THR   B CB  
4851 O  OG1 . THR   B 57  ? 0.1787 0.1670 0.3113 -0.0025 0.0117  -0.0101 57  THR   B OG1 
4852 C  CG2 . THR   B 57  ? 0.1752 0.1797 0.2597 0.0010  0.0256  -0.0022 57  THR   B CG2 
4860 N  N   . ASN   B 58  ? 0.1623 0.2235 0.3211 -0.0101 0.0035  -0.0328 58  ASN   B N   
4861 C  CA  . ASN   B 58  ? 0.1832 0.2613 0.3454 -0.0256 0.0255  -0.0316 58  ASN   B CA  
4862 C  C   . ASN   B 58  ? 0.1700 0.2453 0.3122 -0.0194 -0.0005 -0.0249 58  ASN   B C   
4863 O  O   . ASN   B 58  ? 0.1707 0.2554 0.3252 -0.0245 -0.0012 -0.0306 58  ASN   B O   
4864 C  CB  . ASN   B 58  ? 0.2451 0.3144 0.4463 -0.0370 0.0741  -0.0229 58  ASN   B CB  
4865 C  CG  . ASN   B 58  ? 0.3855 0.3996 0.5737 -0.0374 0.1000  0.0047  58  ASN   B CG  
4866 O  OD1 . ASN   B 58  ? 0.4293 0.4326 0.6207 -0.0332 0.1067  0.0096  58  ASN   B OD1 
4867 N  ND2 . ASN   B 58  ? 0.4793 0.4793 0.6157 -0.0398 0.1101  0.0130  58  ASN   B ND2 
4874 N  N   . ASN   B 59  ? 0.1745 0.2305 0.2962 -0.0200 -0.0094 -0.0128 59  ASN   B N   
4875 C  CA  . ASN   B 59  ? 0.1721 0.2267 0.2924 -0.0139 -0.0211 -0.0024 59  ASN   B CA  
4876 C  C   . ASN   B 59  ? 0.1673 0.2143 0.2818 -0.0203 -0.0188 -0.0168 59  ASN   B C   
4877 O  O   . ASN   B 59  ? 0.1712 0.2110 0.2838 -0.0143 -0.0056 -0.0137 59  ASN   B O   
4878 C  CB  . ASN   B 59  ? 0.1822 0.2426 0.3006 0.0025  -0.0368 -0.0012 59  ASN   B CB  
4879 C  CG  . ASN   B 59  ? 0.1973 0.2556 0.3134 0.0041  -0.0517 0.0031  59  ASN   B CG  
4880 O  OD1 . ASN   B 59  ? 0.1947 0.2583 0.3341 0.0043  -0.0470 0.0111  59  ASN   B OD1 
4881 N  ND2 . ASN   B 59  ? 0.2081 0.2687 0.3257 -0.0052 -0.0604 -0.0059 59  ASN   B ND2 
4888 N  N   . ALA   B 60  ? 0.1673 0.2015 0.2734 -0.0143 -0.0083 -0.0082 60  ALA   B N   
4889 C  CA  . ALA   B 60  ? 0.1734 0.1964 0.2854 -0.0107 -0.0033 -0.0063 60  ALA   B CA  
4890 C  C   . ALA   B 60  ? 0.1701 0.1775 0.2790 -0.0066 -0.0117 0.0112  60  ALA   B C   
4891 O  O   . ALA   B 60  ? 0.1798 0.1788 0.2884 -0.0089 0.0003  -0.0077 60  ALA   B O   
4892 C  CB  . ALA   B 60  ? 0.1904 0.1945 0.3019 -0.0145 0.0006  -0.0109 60  ALA   B CB  
4898 N  N   . MET   B 61  ? 0.1674 0.1680 0.2600 -0.0080 -0.0067 0.0095  61  MET   B N   
4899 C  CA  . MET   B 61  ? 0.1577 0.1667 0.2499 -0.0084 -0.0146 0.0049  61  MET   B CA  
4900 C  C   . MET   B 61  ? 0.1673 0.1565 0.2578 -0.0134 -0.0144 0.0020  61  MET   B C   
4901 O  O   . MET   B 61  ? 0.1737 0.1645 0.2430 -0.0041 -0.0144 -0.0169 61  MET   B O   
4902 C  CB  . MET   B 61  ? 0.1522 0.1782 0.2650 0.0008  -0.0098 0.0021  61  MET   B CB  
4903 C  CG  . MET   B 61  ? 0.1515 0.1719 0.2650 -0.0082 -0.0048 0.0021  61  MET   B CG  
4904 S  SD  . MET   B 61  ? 0.1672 0.1709 0.2368 -0.0064 -0.0083 -0.0119 61  MET   B SD  
4905 C  CE  . MET   B 61  ? 0.1731 0.2035 0.2822 -0.0292 -0.0157 -0.0181 61  MET   B CE  
4915 N  N   . GLN   B 62  ? 0.1688 0.1680 0.2594 -0.0072 -0.0196 0.0039  62  GLN   B N   
4916 C  CA  . GLN   B 62  ? 0.1743 0.1726 0.2613 -0.0000 -0.0233 -0.0043 62  GLN   B CA  
4917 C  C   . GLN   B 62  ? 0.1814 0.1768 0.2610 -0.0001 -0.0335 -0.0141 62  GLN   B C   
4918 O  O   . GLN   B 62  ? 0.1905 0.1763 0.2563 0.0040  -0.0288 -0.0249 62  GLN   B O   
4919 C  CB  . GLN   B 62  ? 0.1833 0.1715 0.2660 0.0107  -0.0142 0.0023  62  GLN   B CB  
4920 C  CG  . GLN   B 62  ? 0.1923 0.1862 0.2833 0.0061  -0.0221 -0.0132 62  GLN   B CG  
4921 C  CD  . GLN   B 62  ? 0.1834 0.1837 0.2652 0.0051  -0.0382 -0.0031 62  GLN   B CD  
4922 O  OE1 . GLN   B 62  ? 0.1902 0.1780 0.2604 0.0048  -0.0462 -0.0104 62  GLN   B OE1 
4923 N  NE2 . GLN   B 62  ? 0.1893 0.1911 0.2496 0.0131  -0.0354 -0.0146 62  GLN   B NE2 
4932 N  N   . VAL   B 63  ? 0.1804 0.1772 0.2744 -0.0015 -0.0304 -0.0148 63  VAL   B N   
4933 C  CA  . VAL   B 63  ? 0.1901 0.1783 0.2796 -0.0084 -0.0352 -0.0085 63  VAL   B CA  
4934 C  C   . VAL   B 63  ? 0.1921 0.1733 0.2607 -0.0176 -0.0401 -0.0191 63  VAL   B C   
4935 O  O   . VAL   B 63  ? 0.2001 0.1769 0.2730 -0.0137 -0.0531 -0.0169 63  VAL   B O   
4936 C  CB  . VAL   B 63  ? 0.1883 0.1985 0.3063 -0.0096 -0.0314 -0.0063 63  VAL   B CB  
4937 C  CG1 . VAL   B 63  ? 0.1900 0.2056 0.3168 -0.0251 -0.0212 -0.0145 63  VAL   B CG1 
4938 C  CG2 . VAL   B 63  ? 0.1900 0.2088 0.3114 -0.0064 -0.0374 -0.0162 63  VAL   B CG2 
4948 N  N   . GLU   B 64  ? 0.1824 0.1680 0.2678 -0.0081 -0.0351 -0.0119 64  GLU   B N   
4949 C  CA  . GLU   B 64  ? 0.1808 0.1614 0.2527 -0.0175 -0.0396 -0.0048 64  GLU   B CA  
4950 C  C   . GLU   B 64  ? 0.1772 0.1580 0.2429 -0.0077 -0.0347 -0.0146 64  GLU   B C   
4951 O  O   . GLU   B 64  ? 0.1865 0.1714 0.2383 -0.0095 -0.0398 -0.0106 64  GLU   B O   
4952 C  CB  . GLU   B 64  ? 0.1824 0.1730 0.2479 -0.0120 -0.0300 -0.0035 64  GLU   B CB  
4953 C  CG  . GLU   B 64  ? 0.1918 0.1717 0.2680 -0.0169 -0.0250 -0.0099 64  GLU   B CG  
4954 C  CD  . GLU   B 64  ? 0.1954 0.1829 0.2749 -0.0304 -0.0368 -0.0025 64  GLU   B CD  
4955 O  OE1 . GLU   B 64  ? 0.1971 0.2020 0.2782 -0.0418 -0.0266 -0.0187 64  GLU   B OE1 
4956 O  OE2 . GLU   B 64  ? 0.2136 0.1913 0.2721 -0.0425 -0.0485 -0.0122 64  GLU   B OE2 
4963 N  N   . SER   B 65  ? 0.1780 0.1589 0.2294 -0.0090 -0.0246 -0.0111 65  SER   B N   
4964 C  CA  . SER   B 65  ? 0.1782 0.1593 0.2282 0.0019  -0.0349 -0.0151 65  SER   B CA  
4965 C  C   . SER   B 65  ? 0.1887 0.1654 0.2315 0.0111  -0.0416 -0.0166 65  SER   B C   
4966 O  O   . SER   B 65  ? 0.1864 0.1663 0.2298 -0.0017 -0.0319 -0.0155 65  SER   B O   
4967 C  CB  . SER   B 65  ? 0.1856 0.1679 0.2417 -0.0054 -0.0276 -0.0144 65  SER   B CB  
4968 O  OG  . SER   B 65  ? 0.1851 0.1687 0.2386 -0.0040 -0.0278 -0.0188 65  SER   B OG  
4974 N  N   . ASP   B 66  ? 0.1968 0.1701 0.2267 0.0074  -0.0429 -0.0249 66  ASP   B N   
4975 C  CA  . ASP   B 66  ? 0.2012 0.1740 0.2246 0.0127  -0.0493 -0.0223 66  ASP   B CA  
4976 C  C   . ASP   B 66  ? 0.2050 0.1809 0.2533 -0.0064 -0.0439 -0.0207 66  ASP   B C   
4977 O  O   . ASP   B 66  ? 0.1999 0.1846 0.2560 0.0092  -0.0350 -0.0219 66  ASP   B O   
4978 C  CB  . ASP   B 66  ? 0.2240 0.1936 0.2525 0.0151  -0.0549 -0.0182 66  ASP   B CB  
4979 C  CG  . ASP   B 66  ? 0.2514 0.2013 0.2710 0.0197  -0.0545 -0.0029 66  ASP   B CG  
4980 O  OD1 . ASP   B 66  ? 0.2793 0.2012 0.2844 0.0115  -0.0480 0.0075  66  ASP   B OD1 
4981 O  OD2 . ASP   B 66  ? 0.2681 0.2256 0.3187 0.0481  -0.0640 -0.0087 66  ASP   B OD2 
4986 N  N   . ASP   B 67  ? 0.1987 0.1737 0.2457 -0.0084 -0.0404 -0.0208 67  ASP   B N   
4987 C  CA  . ASP   B 67  ? 0.1995 0.1666 0.2608 -0.0012 -0.0351 -0.0083 67  ASP   B CA  
4988 C  C   . ASP   B 67  ? 0.1985 0.1656 0.2618 0.0024  -0.0314 -0.0073 67  ASP   B C   
4989 O  O   . ASP   B 67  ? 0.2002 0.1766 0.2664 -0.0016 -0.0252 -0.0102 67  ASP   B O   
4990 C  CB  . ASP   B 67  ? 0.2009 0.1723 0.2909 -0.0127 -0.0460 -0.0124 67  ASP   B CB  
4991 C  CG  . ASP   B 67  ? 0.2420 0.1820 0.3087 -0.0125 -0.0677 -0.0110 67  ASP   B CG  
4992 O  OD1 . ASP   B 67  ? 0.2760 0.1869 0.3226 -0.0094 -0.0785 -0.0089 67  ASP   B OD1 
4993 O  OD2 . ASP   B 67  ? 0.2581 0.1939 0.3288 0.0028  -0.0712 -0.0052 67  ASP   B OD2 
4998 N  N   . TYR   B 68  ? 0.1924 0.1631 0.2695 0.0021  -0.0439 -0.0168 68  TYR   B N   
4999 C  CA  . TYR   B 68  ? 0.1917 0.1825 0.2798 0.0122  -0.0390 -0.0271 68  TYR   B CA  
5000 C  C   . TYR   B 68  ? 0.1891 0.1804 0.2516 0.0100  -0.0405 -0.0264 68  TYR   B C   
5001 O  O   . TYR   B 68  ? 0.2006 0.1906 0.2557 0.0108  -0.0380 -0.0415 68  TYR   B O   
5002 C  CB  . TYR   B 68  ? 0.1922 0.2020 0.2720 0.0053  -0.0415 -0.0222 68  TYR   B CB  
5003 C  CG  . TYR   B 68  ? 0.2027 0.2187 0.2774 0.0079  -0.0335 -0.0434 68  TYR   B CG  
5004 C  CD1 . TYR   B 68  ? 0.2075 0.2211 0.2851 -0.0038 -0.0347 -0.0558 68  TYR   B CD1 
5005 C  CD2 . TYR   B 68  ? 0.2064 0.2442 0.2882 0.0137  -0.0417 -0.0510 68  TYR   B CD2 
5006 C  CE1 . TYR   B 68  ? 0.2137 0.2367 0.2995 0.0081  -0.0273 -0.0601 68  TYR   B CE1 
5007 C  CE2 . TYR   B 68  ? 0.2051 0.2574 0.3031 0.0152  -0.0276 -0.0668 68  TYR   B CE2 
5008 C  CZ  . TYR   B 68  ? 0.1990 0.2470 0.3194 0.0125  -0.0226 -0.0588 68  TYR   B CZ  
5009 O  OH  . TYR   B 68  ? 0.1958 0.2639 0.3523 0.0020  -0.0176 -0.0358 68  TYR   B OH  
5019 N  N   . ILE   B 69  ? 0.1846 0.1726 0.2504 0.0103  -0.0315 -0.0299 69  ILE   B N   
5020 C  CA  . ILE   B 69  ? 0.1872 0.1842 0.2584 0.0095  -0.0385 -0.0304 69  ILE   B CA  
5021 C  C   . ILE   B 69  ? 0.1900 0.1824 0.2307 0.0115  -0.0488 -0.0199 69  ILE   B C   
5022 O  O   . ILE   B 69  ? 0.2002 0.1837 0.2249 0.0066  -0.0269 -0.0167 69  ILE   B O   
5023 C  CB  . ILE   B 69  ? 0.1951 0.1779 0.2776 0.0012  -0.0106 -0.0374 69  ILE   B CB  
5024 C  CG1 . ILE   B 69  ? 0.1979 0.1798 0.2750 -0.0012 -0.0092 -0.0445 69  ILE   B CG1 
5025 C  CG2 . ILE   B 69  ? 0.2142 0.1924 0.2904 -0.0023 -0.0119 -0.0361 69  ILE   B CG2 
5026 C  CD1 . ILE   B 69  ? 0.2020 0.1943 0.2868 -0.0120 -0.0052 -0.0400 69  ILE   B CD1 
5038 N  N   . ALA   B 70  ? 0.1901 0.1757 0.2480 0.0134  -0.0400 -0.0250 70  ALA   B N   
5039 C  CA  . ALA   B 70  ? 0.1955 0.1743 0.2429 0.0035  -0.0382 -0.0228 70  ALA   B CA  
5040 C  C   . ALA   B 70  ? 0.2036 0.1774 0.2525 -0.0035 -0.0382 -0.0266 70  ALA   B C   
5041 O  O   . ALA   B 70  ? 0.2084 0.1784 0.2647 0.0033  -0.0374 -0.0292 70  ALA   B O   
5042 C  CB  . ALA   B 70  ? 0.1988 0.1857 0.2327 0.0011  -0.0408 -0.0251 70  ALA   B CB  
5048 N  N   . THR   B 71  ? 0.2134 0.1742 0.2498 0.0053  -0.0503 -0.0212 71  THR   B N   
5049 C  CA  . THR   B 71  ? 0.2244 0.1866 0.2705 0.0119  -0.0561 -0.0272 71  THR   B CA  
5050 C  C   . THR   B 71  ? 0.2142 0.1870 0.3033 0.0269  -0.0603 -0.0479 71  THR   B C   
5051 O  O   . THR   B 71  ? 0.2277 0.1931 0.3486 0.0353  -0.0602 -0.0591 71  THR   B O   
5052 C  CB  . THR   B 71  ? 0.2430 0.2038 0.2925 0.0064  -0.0672 -0.0128 71  THR   B CB  
5053 O  OG1 . THR   B 71  ? 0.2524 0.2212 0.3385 -0.0125 -0.0735 0.0034  71  THR   B OG1 
5054 C  CG2 . THR   B 71  ? 0.2606 0.1975 0.3083 0.0105  -0.0563 -0.0123 71  THR   B CG2 
5062 N  N   . ASN   B 72  ? 0.2066 0.1895 0.2929 0.0161  -0.0614 -0.0629 72  ASN   B N   
5063 C  CA  . ASN   B 72  ? 0.2063 0.2032 0.2960 0.0224  -0.0358 -0.0685 72  ASN   B CA  
5064 C  C   . ASN   B 72  ? 0.2002 0.2128 0.3081 0.0087  -0.0181 -0.0629 72  ASN   B C   
5065 O  O   . ASN   B 72  ? 0.2074 0.2267 0.3306 0.0083  -0.0104 -0.0693 72  ASN   B O   
5066 C  CB  . ASN   B 72  ? 0.2064 0.2134 0.3003 0.0181  -0.0483 -0.0531 72  ASN   B CB  
5067 C  CG  . ASN   B 72  ? 0.2263 0.2291 0.3192 0.0362  -0.0569 -0.0359 72  ASN   B CG  
5068 O  OD1 . ASN   B 72  ? 0.2571 0.2521 0.3212 0.0210  -0.0503 -0.0465 72  ASN   B OD1 
5069 N  ND2 . ASN   B 72  ? 0.2326 0.2380 0.3435 0.0498  -0.0547 -0.0017 72  ASN   B ND2 
5076 N  N   . GLY   B 73  ? 0.2049 0.2163 0.2904 0.0018  -0.0277 -0.0574 73  GLY   B N   
5077 C  CA  . GLY   B 73  ? 0.2076 0.2160 0.2761 -0.0024 -0.0182 -0.0482 73  GLY   B CA  
5078 C  C   . GLY   B 73  ? 0.1962 0.2101 0.2413 0.0087  -0.0175 -0.0368 73  GLY   B C   
5079 O  O   . GLY   B 73  ? 0.1936 0.2049 0.2520 0.0093  -0.0138 -0.0264 73  GLY   B O   
5083 N  N   . PRO   B 74  ? 0.2022 0.2205 0.2327 0.0103  -0.0209 -0.0207 74  PRO   B N   
5084 C  CA  . PRO   B 74  ? 0.2029 0.2161 0.2178 0.0144  -0.0164 -0.0098 74  PRO   B CA  
5085 C  C   . PRO   B 74  ? 0.1872 0.2055 0.2277 0.0084  -0.0108 -0.0050 74  PRO   B C   
5086 O  O   . PRO   B 74  ? 0.1958 0.2041 0.2757 0.0108  -0.0147 -0.0149 74  PRO   B O   
5087 C  CB  . PRO   B 74  ? 0.2168 0.2304 0.2238 0.0119  -0.0155 -0.0093 74  PRO   B CB  
5088 C  CG  . PRO   B 74  ? 0.2357 0.2439 0.2441 0.0157  -0.0173 -0.0016 74  PRO   B CG  
5089 C  CD  . PRO   B 74  ? 0.2346 0.2353 0.2447 0.0141  -0.0131 -0.0062 74  PRO   B CD  
5097 N  N   . LEU   B 75  ? 0.1908 0.1974 0.2069 0.0091  -0.0147 -0.0075 75  LEU   B N   
5098 C  CA  . LEU   B 75  ? 0.1998 0.2066 0.2022 0.0029  -0.0109 0.0061  75  LEU   B CA  
5099 C  C   . LEU   B 75  ? 0.2136 0.2141 0.2030 0.0014  0.0032  0.0135  75  LEU   B C   
5100 O  O   . LEU   B 75  ? 0.2293 0.2116 0.2200 -0.0040 -0.0073 0.0163  75  LEU   B O   
5101 C  CB  . LEU   B 75  ? 0.2068 0.2096 0.1864 -0.0168 -0.0131 0.0212  75  LEU   B CB  
5102 C  CG  . LEU   B 75  ? 0.2375 0.2245 0.2027 -0.0324 -0.0004 0.0103  75  LEU   B CG  
5103 C  CD1 . LEU   B 75  ? 0.2661 0.2415 0.2149 -0.0392 0.0106  0.0011  75  LEU   B CD1 
5104 C  CD2 . LEU   B 75  ? 0.2723 0.2448 0.2561 -0.0237 0.0044  0.0051  75  LEU   B CD2 
5116 N  N   . LYS   B 76  ? 0.2144 0.2384 0.2393 0.0004  0.0192  0.0255  76  LYS   B N   
5117 C  CA  . LYS   B 76  ? 0.2259 0.2489 0.2759 -0.0114 0.0382  0.0246  76  LYS   B CA  
5118 C  C   . LYS   B 76  ? 0.2249 0.2363 0.2640 -0.0103 0.0348  0.0373  76  LYS   B C   
5119 O  O   . LYS   B 76  ? 0.2208 0.2090 0.2589 -0.0126 0.0239  0.0363  76  LYS   B O   
5120 C  CB  . LYS   B 76  ? 0.2330 0.2551 0.3052 -0.0191 0.0518  0.0032  76  LYS   B CB  
5121 C  CG  . LYS   B 76  ? 0.2369 0.2757 0.3372 -0.0130 0.0398  -0.0096 76  LYS   B CG  
5122 C  CD  . LYS   B 76  ? 0.2400 0.2830 0.3753 -0.0129 0.0303  -0.0269 76  LYS   B CD  
5123 C  CE  . LYS   B 76  ? 0.2396 0.3020 0.4011 -0.0091 0.0173  -0.0294 76  LYS   B CE  
5124 N  NZ  . LYS   B 76  ? 0.2397 0.3122 0.4260 -0.0112 -0.0018 -0.0325 76  LYS   B NZ  
5138 N  N   . VAL   B 77  ? 0.2370 0.2494 0.2785 -0.0081 0.0299  0.0460  77  VAL   B N   
5139 C  CA  . VAL   B 77  ? 0.2391 0.2363 0.2835 -0.0068 0.0329  0.0713  77  VAL   B CA  
5140 C  C   . VAL   B 77  ? 0.2201 0.2090 0.2780 0.0069  0.0568  0.0530  77  VAL   B C   
5141 O  O   . VAL   B 77  ? 0.2282 0.2014 0.2804 0.0192  0.0549  0.0471  77  VAL   B O   
5142 C  CB  . VAL   B 77  ? 0.2601 0.2447 0.3181 -0.0117 0.0410  0.0837  77  VAL   B CB  
5143 C  CG1 . VAL   B 77  ? 0.2655 0.2276 0.3296 -0.0238 0.0455  0.0959  77  VAL   B CG1 
5144 C  CG2 . VAL   B 77  ? 0.2808 0.2635 0.3224 -0.0091 0.0211  0.0846  77  VAL   B CG2 
5154 N  N   . GLY   B 78  ? 0.2044 0.1903 0.2681 0.0067  0.0390  0.0405  78  GLY   B N   
5155 C  CA  . GLY   B 78  ? 0.2056 0.1907 0.2698 0.0106  0.0490  0.0373  78  GLY   B CA  
5156 C  C   . GLY   B 78  ? 0.1914 0.1781 0.2660 0.0060  0.0356  0.0322  78  GLY   B C   
5157 O  O   . GLY   B 78  ? 0.1848 0.1726 0.2847 0.0084  0.0362  0.0409  78  GLY   B O   
5161 N  N   . GLY   B 79  ? 0.1849 0.1794 0.2605 0.0029  0.0276  0.0144  79  GLY   B N   
5162 C  CA  . GLY   B 79  ? 0.1834 0.1745 0.2552 0.0051  0.0126  0.0135  79  GLY   B CA  
5163 C  C   . GLY   B 79  ? 0.1732 0.1699 0.2663 0.0155  0.0165  0.0167  79  GLY   B C   
5164 O  O   . GLY   B 79  ? 0.1748 0.1672 0.2658 0.0069  0.0318  0.0375  79  GLY   B O   
5168 N  N   . SER   B 80  ? 0.1674 0.1621 0.2663 0.0043  0.0165  0.0154  80  SER   B N   
5169 C  CA  . SER   B 80  ? 0.1586 0.1633 0.2540 -0.0013 0.0023  0.0154  80  SER   B CA  
5170 C  C   . SER   B 80  ? 0.1618 0.1549 0.2516 0.0030  -0.0038 0.0185  80  SER   B C   
5171 O  O   . SER   B 80  ? 0.1663 0.1580 0.2822 0.0042  0.0067  0.0167  80  SER   B O   
5172 C  CB  . SER   B 80  ? 0.1560 0.1692 0.2653 -0.0085 0.0051  0.0204  80  SER   B CB  
5173 O  OG  . SER   B 80  ? 0.1663 0.1851 0.2786 -0.0088 -0.0050 0.0184  80  SER   B OG  
5179 N  N   . CYS   B 81  ? 0.1562 0.1445 0.2656 -0.0031 -0.0035 0.0023  81  CYS   B N   
5180 C  CA  . CYS   B 81  ? 0.1625 0.1449 0.2621 0.0020  -0.0121 0.0048  81  CYS   B CA  
5181 C  C   . CYS   B 81  ? 0.1608 0.1465 0.2426 -0.0021 -0.0020 0.0031  81  CYS   B C   
5182 O  O   . CYS   B 81  ? 0.1721 0.1453 0.2639 0.0032  0.0001  0.0054  81  CYS   B O   
5183 C  CB  . CYS   B 81  ? 0.1801 0.1556 0.2652 -0.0068 -0.0092 -0.0001 81  CYS   B CB  
5184 S  SG  . CYS   B 81  ? 0.1847 0.1720 0.2058 -0.0080 -0.0176 -0.0036 81  CYS   B SG  
5190 N  N   . VAL   B 82  ? 0.1619 0.1413 0.2366 -0.0026 -0.0075 0.0086  82  VAL   B N   
5191 C  CA  . VAL   B 82  ? 0.1795 0.1413 0.2356 -0.0081 -0.0085 0.0176  82  VAL   B CA  
5192 C  C   . VAL   B 82  ? 0.1808 0.1358 0.2542 -0.0112 -0.0156 0.0079  82  VAL   B C   
5193 O  O   . VAL   B 82  ? 0.1866 0.1382 0.2776 -0.0130 -0.0093 -0.0068 82  VAL   B O   
5194 C  CB  . VAL   B 82  ? 0.1818 0.1592 0.2546 -0.0060 -0.0146 0.0215  82  VAL   B CB  
5195 C  CG1 . VAL   B 82  ? 0.1924 0.1856 0.2540 -0.0050 -0.0267 0.0243  82  VAL   B CG1 
5196 C  CG2 . VAL   B 82  ? 0.1898 0.1715 0.2813 -0.0181 -0.0250 0.0191  82  VAL   B CG2 
5206 N  N   . LEU   B 83  ? 0.1610 0.1333 0.2586 -0.0215 -0.0190 -0.0046 83  LEU   B N   
5207 C  CA  . LEU   B 83  ? 0.1633 0.1501 0.2560 -0.0175 -0.0159 0.0028  83  LEU   B CA  
5208 C  C   . LEU   B 83  ? 0.1625 0.1461 0.2534 -0.0209 -0.0129 0.0026  83  LEU   B C   
5209 O  O   . LEU   B 83  ? 0.1597 0.1597 0.2323 -0.0287 -0.0154 0.0090  83  LEU   B O   
5210 C  CB  . LEU   B 83  ? 0.1689 0.1607 0.2619 -0.0217 -0.0183 -0.0101 83  LEU   B CB  
5211 C  CG  . LEU   B 83  ? 0.1920 0.1764 0.2447 -0.0213 -0.0124 -0.0103 83  LEU   B CG  
5212 C  CD1 . LEU   B 83  ? 0.2102 0.1807 0.2348 -0.0074 -0.0235 -0.0054 83  LEU   B CD1 
5213 C  CD2 . LEU   B 83  ? 0.2169 0.1804 0.2450 -0.0145 -0.0130 -0.0256 83  LEU   B CD2 
5225 N  N   . SER   B 84  ? 0.1722 0.1542 0.2602 -0.0335 -0.0170 0.0059  84  SER   B N   
5226 C  CA  . SER   B 84  ? 0.1775 0.1783 0.2490 -0.0328 -0.0170 0.0162  84  SER   B CA  
5227 C  C   . SER   B 84  ? 0.1657 0.2034 0.2005 -0.0345 -0.0327 0.0118  84  SER   B C   
5228 O  O   . SER   B 84  ? 0.1701 0.1893 0.1973 -0.0319 -0.0121 -0.0019 84  SER   B O   
5229 C  CB  . SER   B 84  ? 0.1858 0.1801 0.2829 -0.0374 0.0042  0.0148  84  SER   B CB  
5230 O  OG  . SER   B 84  ? 0.1803 0.1957 0.3258 -0.0456 0.0068  0.0182  84  SER   B OG  
5236 N  N   . GLY   B 85  ? 0.1644 0.2148 0.2160 -0.0385 -0.0300 0.0205  85  GLY   B N   
5237 C  CA  . GLY   B 85  ? 0.1742 0.2241 0.2344 -0.0391 -0.0075 0.0037  85  GLY   B CA  
5238 C  C   . GLY   B 85  ? 0.1687 0.2091 0.2251 -0.0458 -0.0036 0.0072  85  GLY   B C   
5239 O  O   . GLY   B 85  ? 0.1823 0.2076 0.2280 -0.0555 0.0107  -0.0216 85  GLY   B O   
5243 N  N   . HIS   B 86  ? 0.1611 0.1986 0.2479 -0.0426 -0.0153 0.0109  86  HIS   B N   
5244 C  CA  . HIS   B 86  ? 0.1619 0.1958 0.2440 -0.0384 -0.0244 0.0186  86  HIS   B CA  
5245 C  C   . HIS   B 86  ? 0.1649 0.2055 0.2340 -0.0479 -0.0079 0.0288  86  HIS   B C   
5246 O  O   . HIS   B 86  ? 0.1838 0.2122 0.2458 -0.0369 -0.0021 0.0257  86  HIS   B O   
5247 C  CB  . HIS   B 86  ? 0.1733 0.1964 0.2428 -0.0313 -0.0328 0.0106  86  HIS   B CB  
5248 C  CG  . HIS   B 86  ? 0.1732 0.2045 0.2326 -0.0208 -0.0242 -0.0099 86  HIS   B CG  
5249 N  ND1 . HIS   B 86  ? 0.1853 0.2315 0.2517 -0.0310 -0.0217 -0.0227 86  HIS   B ND1 
5250 C  CD2 . HIS   B 86  ? 0.1806 0.2069 0.2458 -0.0174 -0.0171 -0.0051 86  HIS   B CD2 
5251 C  CE1 . HIS   B 86  ? 0.1950 0.2200 0.2327 -0.0152 -0.0004 -0.0354 86  HIS   B CE1 
5252 N  NE2 . HIS   B 86  ? 0.1934 0.2096 0.2398 -0.0098 -0.0115 -0.0169 86  HIS   B NE2 
5260 N  N   . ASN   B 87  ? 0.1623 0.2214 0.2357 -0.0401 -0.0044 0.0239  87  ASN   B N   
5261 C  CA  . ASN   B 87  ? 0.1809 0.2363 0.2554 -0.0468 0.0298  0.0102  87  ASN   B CA  
5262 C  C   . ASN   B 87  ? 0.1996 0.2151 0.2436 -0.0411 0.0392  0.0024  87  ASN   B C   
5263 O  O   . ASN   B 87  ? 0.2300 0.2154 0.2656 -0.0304 0.0665  -0.0017 87  ASN   B O   
5264 C  CB  . ASN   B 87  ? 0.1780 0.2601 0.2855 -0.0491 0.0333  0.0140  87  ASN   B CB  
5265 C  CG  . ASN   B 87  ? 0.1945 0.2762 0.2864 -0.0090 0.0413  0.0296  87  ASN   B CG  
5266 O  OD1 . ASN   B 87  ? 0.1869 0.2633 0.2729 -0.0001 0.0571  0.0472  87  ASN   B OD1 
5267 N  ND2 . ASN   B 87  ? 0.2260 0.2819 0.2982 0.0014  0.0379  0.0112  87  ASN   B ND2 
5274 N  N   . LEU   B 88  ? 0.1884 0.2007 0.2161 -0.0437 0.0084  0.0030  88  LEU   B N   
5275 C  CA  . LEU   B 88  ? 0.2086 0.1941 0.2164 -0.0411 0.0012  -0.0018 88  LEU   B CA  
5276 C  C   . LEU   B 88  ? 0.2037 0.1771 0.2373 -0.0526 0.0027  0.0025  88  LEU   B C   
5277 O  O   . LEU   B 88  ? 0.2289 0.1878 0.2786 -0.0397 -0.0248 -0.0143 88  LEU   B O   
5278 C  CB  . LEU   B 88  ? 0.2258 0.2015 0.2346 -0.0557 -0.0148 0.0054  88  LEU   B CB  
5279 C  CG  . LEU   B 88  ? 0.2656 0.2305 0.2560 -0.0481 -0.0309 0.0111  88  LEU   B CG  
5280 C  CD1 . LEU   B 88  ? 0.2757 0.2581 0.2569 -0.0578 -0.0247 0.0371  88  LEU   B CD1 
5281 C  CD2 . LEU   B 88  ? 0.2997 0.2415 0.2968 -0.0126 -0.0477 -0.0169 88  LEU   B CD2 
5293 N  N   . ALA   B 89  ? 0.1859 0.1822 0.2300 -0.0514 0.0288  0.0025  89  ALA   B N   
5294 C  CA  . ALA   B 89  ? 0.1818 0.1792 0.2260 -0.0464 0.0147  0.0114  89  ALA   B CA  
5295 C  C   . ALA   B 89  ? 0.1882 0.1822 0.2166 -0.0534 0.0219  -0.0018 89  ALA   B C   
5296 O  O   . ALA   B 89  ? 0.1726 0.1947 0.2438 -0.0530 0.0165  -0.0314 89  ALA   B O   
5297 C  CB  . ALA   B 89  ? 0.1691 0.1780 0.2366 -0.0460 -0.0033 0.0205  89  ALA   B CB  
5303 N  N   . LYS   B 90  ? 0.2205 0.1700 0.2250 -0.0614 -0.0119 0.0026  90  LYS   B N   
5304 C  CA  . LYS   B 90  ? 0.2308 0.1703 0.2280 -0.0594 -0.0015 0.0104  90  LYS   B CA  
5305 C  C   . LYS   B 90  ? 0.2123 0.1540 0.2320 -0.0527 -0.0052 0.0004  90  LYS   B C   
5306 O  O   . LYS   B 90  ? 0.2143 0.1777 0.2328 -0.0622 0.0044  0.0059  90  LYS   B O   
5307 C  CB  . LYS   B 90  ? 0.2508 0.1734 0.2540 -0.0528 0.0009  0.0108  90  LYS   B CB  
5308 C  CG  . LYS   B 90  ? 0.2461 0.1874 0.2515 -0.0397 0.0147  0.0099  90  LYS   B CG  
5309 C  CD  . LYS   B 90  ? 0.2703 0.1981 0.2747 -0.0155 0.0270  -0.0072 90  LYS   B CD  
5310 C  CE  . LYS   B 90  ? 0.2823 0.2071 0.2995 -0.0203 0.0295  -0.0185 90  LYS   B CE  
5311 N  NZ  . LYS   B 90  ? 0.2774 0.2021 0.2714 -0.0275 0.0467  -0.0164 90  LYS   B NZ  
5325 N  N   . HIS   B 91  ? 0.1891 0.1490 0.2083 -0.0367 -0.0119 0.0186  91  HIS   B N   
5326 C  CA  . HIS   B 91  ? 0.1786 0.1455 0.2164 -0.0323 -0.0181 0.0058  91  HIS   B CA  
5327 C  C   . HIS   B 91  ? 0.1682 0.1506 0.2110 -0.0399 -0.0163 0.0224  91  HIS   B C   
5328 O  O   . HIS   B 91  ? 0.1776 0.1567 0.2197 -0.0407 -0.0242 0.0065  91  HIS   B O   
5329 C  CB  . HIS   B 91  ? 0.1941 0.1455 0.2501 -0.0137 -0.0132 0.0194  91  HIS   B CB  
5330 C  CG  . HIS   B 91  ? 0.2371 0.1681 0.3155 -0.0049 0.0249  0.0298  91  HIS   B CG  
5331 N  ND1 . HIS   B 91  ? 0.2621 0.1755 0.3650 -0.0082 0.0294  0.0126  91  HIS   B ND1 
5332 C  CD2 . HIS   B 91  ? 0.2494 0.1995 0.3523 0.0081  0.0133  0.0557  91  HIS   B CD2 
5333 C  CE1 . HIS   B 91  ? 0.2686 0.1912 0.3822 0.0119  0.0268  0.0123  91  HIS   B CE1 
5334 N  NE2 . HIS   B 91  ? 0.2686 0.2113 0.3795 0.0214  0.0249  0.0523  91  HIS   B NE2 
5342 N  N   . CYS   B 92  ? 0.1641 0.1534 0.2138 -0.0334 -0.0153 0.0100  92  CYS   B N   
5343 C  CA  . CYS   B 92  ? 0.1626 0.1520 0.2122 -0.0253 -0.0135 0.0012  92  CYS   B CA  
5344 C  C   . CYS   B 92  ? 0.1570 0.1422 0.2188 -0.0174 -0.0079 0.0116  92  CYS   B C   
5345 O  O   . CYS   B 92  ? 0.1678 0.1497 0.2449 -0.0214 -0.0049 0.0027  92  CYS   B O   
5346 C  CB  . CYS   B 92  ? 0.1712 0.1529 0.2018 -0.0231 -0.0125 -0.0090 92  CYS   B CB  
5347 S  SG  . CYS   B 92  ? 0.1607 0.1564 0.2356 -0.0172 -0.0157 0.0089  92  CYS   B SG  
5353 N  N   . LEU   B 93  ? 0.1450 0.1460 0.2201 -0.0213 -0.0123 0.0027  93  LEU   B N   
5354 C  CA  . LEU   B 93  ? 0.1474 0.1502 0.2240 -0.0110 -0.0172 0.0076  93  LEU   B CA  
5355 C  C   . LEU   B 93  ? 0.1474 0.1455 0.1953 -0.0042 -0.0125 0.0083  93  LEU   B C   
5356 O  O   . LEU   B 93  ? 0.1564 0.1431 0.2096 -0.0104 -0.0053 0.0013  93  LEU   B O   
5357 C  CB  . LEU   B 93  ? 0.1482 0.1525 0.2471 -0.0078 -0.0103 0.0064  93  LEU   B CB  
5358 C  CG  . LEU   B 93  ? 0.1477 0.1588 0.2618 -0.0136 0.0012  0.0196  93  LEU   B CG  
5359 C  CD1 . LEU   B 93  ? 0.1554 0.1660 0.2703 0.0007  0.0026  0.0094  93  LEU   B CD1 
5360 C  CD2 . LEU   B 93  ? 0.1523 0.1439 0.2639 -0.0061 -0.0150 0.0100  93  LEU   B CD2 
5372 N  N   . HIS   B 94  ? 0.1526 0.1442 0.1885 -0.0099 -0.0164 0.0098  94  HIS   B N   
5373 C  CA  . HIS   B 94  ? 0.1605 0.1365 0.1965 -0.0062 -0.0082 0.0100  94  HIS   B CA  
5374 C  C   . HIS   B 94  ? 0.1559 0.1407 0.2553 -0.0078 -0.0072 0.0250  94  HIS   B C   
5375 O  O   . HIS   B 94  ? 0.1531 0.1532 0.2850 -0.0040 0.0117  0.0100  94  HIS   B O   
5376 C  CB  . HIS   B 94  ? 0.1592 0.1468 0.2053 -0.0007 0.0011  0.0059  94  HIS   B CB  
5377 C  CG  . HIS   B 94  ? 0.1637 0.1395 0.2155 -0.0117 -0.0225 0.0048  94  HIS   B CG  
5378 N  ND1 . HIS   B 94  ? 0.1666 0.1428 0.2244 -0.0093 -0.0191 0.0033  94  HIS   B ND1 
5379 C  CD2 . HIS   B 94  ? 0.1654 0.1491 0.2159 -0.0027 -0.0164 0.0062  94  HIS   B CD2 
5380 C  CE1 . HIS   B 94  ? 0.1733 0.1439 0.2354 -0.0121 -0.0177 0.0134  94  HIS   B CE1 
5381 N  NE2 . HIS   B 94  ? 0.1616 0.1568 0.2180 -0.0156 -0.0100 0.0122  94  HIS   B NE2 
5389 N  N   . VAL   B 95  ? 0.1465 0.1391 0.2428 -0.0022 -0.0036 0.0109  95  VAL   B N   
5390 C  CA  . VAL   B 95  ? 0.1523 0.1535 0.2347 -0.0070 0.0046  0.0277  95  VAL   B CA  
5391 C  C   . VAL   B 95  ? 0.1634 0.1498 0.2445 -0.0035 0.0242  0.0288  95  VAL   B C   
5392 O  O   . VAL   B 95  ? 0.1679 0.1480 0.2693 0.0059  0.0027  0.0288  95  VAL   B O   
5393 C  CB  . VAL   B 95  ? 0.1543 0.1451 0.2326 -0.0054 -0.0094 0.0162  95  VAL   B CB  
5394 C  CG1 . VAL   B 95  ? 0.1710 0.1582 0.2625 -0.0100 0.0082  0.0122  95  VAL   B CG1 
5395 C  CG2 . VAL   B 95  ? 0.1600 0.1424 0.2350 0.0021  -0.0197 0.0132  95  VAL   B CG2 
5405 N  N   . VAL   B 96  ? 0.1767 0.1542 0.2347 0.0019  0.0093  0.0334  96  VAL   B N   
5406 C  CA  . VAL   B 96  ? 0.1969 0.1649 0.2314 0.0031  0.0150  0.0342  96  VAL   B CA  
5407 C  C   . VAL   B 96  ? 0.2101 0.1712 0.2535 0.0017  0.0153  0.0379  96  VAL   B C   
5408 O  O   . VAL   B 96  ? 0.2041 0.1675 0.2613 -0.0056 0.0238  0.0119  96  VAL   B O   
5409 C  CB  . VAL   B 96  ? 0.2001 0.1843 0.2438 0.0103  0.0184  0.0137  96  VAL   B CB  
5410 C  CG1 . VAL   B 96  ? 0.1983 0.1942 0.2449 0.0235  0.0281  0.0118  96  VAL   B CG1 
5411 C  CG2 . VAL   B 96  ? 0.2004 0.1807 0.2388 0.0111  0.0209  0.0032  96  VAL   B CG2 
5421 N  N   . GLY   B 97  ? 0.2192 0.1693 0.2434 0.0017  -0.0017 0.0410  97  GLY   B N   
5422 C  CA  . GLY   B 97  ? 0.2445 0.1806 0.2477 0.0042  0.0161  0.0409  97  GLY   B CA  
5423 C  C   . GLY   B 97  ? 0.2784 0.1952 0.2616 0.0177  0.0301  0.0444  97  GLY   B C   
5424 O  O   . GLY   B 97  ? 0.2925 0.1949 0.2573 0.0110  0.0237  0.0295  97  GLY   B O   
5428 N  N   . PRO   B 98  ? 0.2982 0.2018 0.2763 0.0201  0.0542  0.0589  98  PRO   B N   
5429 C  CA  . PRO   B 98  ? 0.3098 0.2218 0.2784 0.0390  0.0607  0.0578  98  PRO   B CA  
5430 C  C   . PRO   B 98  ? 0.3241 0.2144 0.2685 0.0635  0.0738  0.0740  98  PRO   B C   
5431 O  O   . PRO   B 98  ? 0.3149 0.2157 0.2756 0.0462  0.0738  0.0692  98  PRO   B O   
5432 C  CB  . PRO   B 98  ? 0.2991 0.2269 0.2766 0.0292  0.0715  0.0537  98  PRO   B CB  
5433 C  CG  . PRO   B 98  ? 0.2974 0.2086 0.2844 0.0212  0.0641  0.0806  98  PRO   B CG  
5434 C  CD  . PRO   B 98  ? 0.2868 0.1946 0.2898 0.0266  0.0707  0.0702  98  PRO   B CD  
5442 N  N   . ASN   B 99  ? 0.3298 0.2405 0.3052 0.0930  0.0854  0.0728  99  ASN   B N   
5443 C  CA  . ASN   B 99  ? 0.3464 0.2589 0.3210 0.1033  0.0720  0.0906  99  ASN   B CA  
5444 C  C   . ASN   B 99  ? 0.3722 0.3048 0.3657 0.1048  0.0785  0.1162  99  ASN   B C   
5445 O  O   . ASN   B 99  ? 0.3846 0.3260 0.3759 0.1107  0.0748  0.1295  99  ASN   B O   
5446 C  CB  . ASN   B 99  ? 0.3571 0.2543 0.3149 0.1010  0.0624  0.0717  99  ASN   B CB  
5447 C  CG  . ASN   B 99  ? 0.3611 0.2609 0.3174 0.0966  0.0543  0.0603  99  ASN   B CG  
5448 O  OD1 . ASN   B 99  ? 0.3538 0.2663 0.3427 0.1101  0.0575  0.0626  99  ASN   B OD1 
5449 N  ND2 . ASN   B 99  ? 0.3598 0.2516 0.3229 0.0956  0.0318  0.0614  99  ASN   B ND2 
5456 N  N   . VAL   B 100 ? 0.4051 0.3305 0.4116 0.0789  0.0850  0.1359  100 VAL   B N   
5457 C  CA  . VAL   B 100 ? 0.4459 0.3633 0.4519 0.0608  0.0674  0.1537  100 VAL   B CA  
5458 C  C   . VAL   B 100 ? 0.4848 0.3934 0.4275 0.0586  0.0424  0.1583  100 VAL   B C   
5459 O  O   . VAL   B 100 ? 0.4864 0.4057 0.4327 0.0582  0.0589  0.1561  100 VAL   B O   
5460 C  CB  . VAL   B 100 ? 0.4492 0.3682 0.5119 0.0361  0.0656  0.1732  100 VAL   B CB  
5461 C  CG1 . VAL   B 100 ? 0.4495 0.3703 0.5302 0.0248  0.0609  0.1810  100 VAL   B CG1 
5462 C  CG2 . VAL   B 100 ? 0.4518 0.3698 0.5271 0.0309  0.0692  0.1804  100 VAL   B CG2 
5472 N  N   A ASN   B 101 ? 0.5025 0.3950 0.4130 0.0650  0.0214  0.1669  101 ASN   B N   
5473 N  N   B ASN   B 101 ? 0.5019 0.4127 0.4215 0.0509  0.0276  0.1401  101 ASN   B N   
5474 C  CA  A ASN   B 101 ? 0.5221 0.4022 0.4181 0.0654  0.0097  0.1582  101 ASN   B CA  
5475 C  CA  B ASN   B 101 ? 0.5193 0.4328 0.4254 0.0419  0.0179  0.1157  101 ASN   B CA  
5476 C  C   A ASN   B 101 ? 0.5504 0.4385 0.4315 0.0522  0.0121  0.1436  101 ASN   B C   
5477 C  C   B ASN   B 101 ? 0.5419 0.4606 0.4399 0.0341  0.0163  0.1058  101 ASN   B C   
5478 O  O   A ASN   B 101 ? 0.5494 0.4412 0.4424 0.0552  0.0179  0.1317  101 ASN   B O   
5479 O  O   B ASN   B 101 ? 0.5399 0.4607 0.4432 0.0352  0.0189  0.1001  101 ASN   B O   
5480 C  CB  A ASN   B 101 ? 0.5161 0.3825 0.4117 0.0706  0.0070  0.1428  101 ASN   B CB  
5481 C  CB  B ASN   B 101 ? 0.5149 0.4275 0.4129 0.0395  0.0136  0.0965  101 ASN   B CB  
5482 C  CG  A ASN   B 101 ? 0.5063 0.3641 0.4148 0.0782  -0.0041 0.1335  101 ASN   B CG  
5483 C  CG  B ASN   B 101 ? 0.5091 0.4223 0.4085 0.0384  0.0069  0.0814  101 ASN   B CG  
5484 O  OD1 A ASN   B 101 ? 0.5049 0.3641 0.4278 0.0738  0.0002  0.1309  101 ASN   B OD1 
5485 O  OD1 B ASN   B 101 ? 0.5073 0.4217 0.4110 0.0371  0.0072  0.0775  101 ASN   B OD1 
5486 N  ND2 A ASN   B 101 ? 0.4998 0.3497 0.4130 0.0857  -0.0133 0.1280  101 ASN   B ND2 
5487 N  ND2 B ASN   B 101 ? 0.5061 0.4179 0.4040 0.0385  0.0030  0.0743  101 ASN   B ND2 
5500 N  N   A LYS   B 102 ? 0.5789 0.4737 0.4568 0.0368  0.0127  0.1309  102 LYS   B N   
5501 N  N   B LYS   B 102 ? 0.5659 0.4885 0.4626 0.0267  0.0126  0.1000  102 LYS   B N   
5502 C  CA  A LYS   B 102 ? 0.6043 0.5086 0.4875 0.0217  0.0150  0.1114  102 LYS   B CA  
5503 C  CA  B LYS   B 102 ? 0.5874 0.5140 0.4895 0.0199  0.0101  0.0921  102 LYS   B CA  
5504 C  C   A LYS   B 102 ? 0.6048 0.5157 0.4739 0.0228  0.0141  0.1187  102 LYS   B C   
5505 C  C   B LYS   B 102 ? 0.5955 0.5191 0.4749 0.0212  0.0121  0.1079  102 LYS   B C   
5506 O  O   A LYS   B 102 ? 0.6090 0.5165 0.4615 0.0231  0.0093  0.1238  102 LYS   B O   
5507 O  O   B LYS   B 102 ? 0.5982 0.5208 0.4702 0.0200  0.0093  0.1126  102 LYS   B O   
5508 C  CB  A LYS   B 102 ? 0.6256 0.5335 0.5373 0.0085  0.0230  0.0790  102 LYS   B CB  
5509 C  CB  B LYS   B 102 ? 0.5977 0.5312 0.5272 0.0138  0.0089  0.0657  102 LYS   B CB  
5510 C  CG  A LYS   B 102 ? 0.6417 0.5523 0.5942 -0.0000 0.0289  0.0466  102 LYS   B CG  
5511 C  CG  B LYS   B 102 ? 0.6050 0.5442 0.5718 0.0100  0.0068  0.0402  102 LYS   B CG  
5512 C  CD  A LYS   B 102 ? 0.6537 0.5667 0.6331 -0.0064 0.0335  0.0207  102 LYS   B CD  
5513 C  CD  B LYS   B 102 ? 0.6108 0.5544 0.6010 0.0069  0.0054  0.0189  102 LYS   B CD  
5514 C  CE  A LYS   B 102 ? 0.6605 0.5756 0.6706 -0.0117 0.0390  0.0037  102 LYS   B CE  
5515 C  CE  B LYS   B 102 ? 0.6146 0.5614 0.6319 0.0044  0.0058  0.0045  102 LYS   B CE  
5516 N  NZ  A LYS   B 102 ? 0.6640 0.5801 0.6886 -0.0141 0.0429  -0.0073 102 LYS   B NZ  
5517 N  NZ  B LYS   B 102 ? 0.6173 0.5659 0.6451 0.0028  0.0067  -0.0031 102 LYS   B NZ  
5544 N  N   . GLY   B 103 ? 0.5981 0.5193 0.4757 0.0241  0.0174  0.1165  103 GLY   B N   
5545 C  CA  . GLY   B 103 ? 0.5936 0.5213 0.4880 0.0335  0.0310  0.1186  103 GLY   B CA  
5546 C  C   . GLY   B 103 ? 0.5844 0.5202 0.5003 0.0389  0.0445  0.1150  103 GLY   B C   
5547 O  O   . GLY   B 103 ? 0.5883 0.5249 0.4964 0.0335  0.0486  0.1237  103 GLY   B O   
5552 N  N   . GLU   B 104 ? 0.5684 0.5102 0.4924 0.0487  0.0575  0.0916  104 GLU   B N   
5553 C  CA  . GLU   B 104 ? 0.5498 0.4969 0.4822 0.0615  0.0655  0.0679  104 GLU   B CA  
5554 C  C   . GLU   B 104 ? 0.5458 0.4954 0.4861 0.0303  0.1058  0.0624  104 GLU   B C   
5555 O  O   . GLU   B 104 ? 0.5405 0.4889 0.5005 0.0248  0.1082  0.0640  104 GLU   B O   
5556 C  CB  . GLU   B 104 ? 0.5360 0.4811 0.4680 0.1052  0.0298  0.0472  104 GLU   B CB  
5557 C  CG  . GLU   B 104 ? 0.5202 0.4663 0.4485 0.1430  -0.0105 0.0256  104 GLU   B CG  
5558 C  CD  . GLU   B 104 ? 0.5042 0.4512 0.4213 0.1754  -0.0365 0.0043  104 GLU   B CD  
5559 O  OE1 . GLU   B 104 ? 0.4918 0.4351 0.4015 0.1982  -0.0324 -0.0084 104 GLU   B OE1 
5560 O  OE2 . GLU   B 104 ? 0.4991 0.4540 0.4223 0.1797  -0.0533 -0.0122 104 GLU   B OE2 
5567 N  N   A ASP   B 105 ? 0.5453 0.4960 0.4841 0.0192  0.1438  0.0610  105 ASP   B N   
5568 N  N   B ASP   B 105 ? 0.5440 0.4998 0.4947 0.0194  0.1090  0.0553  105 ASP   B N   
5569 C  CA  A ASP   B 105 ? 0.5434 0.4911 0.4850 0.0115  0.1760  0.0488  105 ASP   B CA  
5570 C  CA  B ASP   B 105 ? 0.5395 0.4996 0.4958 0.0106  0.1111  0.0412  105 ASP   B CA  
5571 C  C   A ASP   B 105 ? 0.5252 0.4649 0.4565 0.0001  0.1879  0.0441  105 ASP   B C   
5572 C  C   B ASP   B 105 ? 0.5229 0.4834 0.4755 0.0024  0.1097  0.0330  105 ASP   B C   
5573 O  O   A ASP   B 105 ? 0.5198 0.4608 0.4361 0.0040  0.2044  0.0513  105 ASP   B O   
5574 O  O   B ASP   B 105 ? 0.5224 0.4830 0.4712 0.0034  0.1122  0.0359  105 ASP   B O   
5575 C  CB  A ASP   B 105 ? 0.5530 0.5061 0.5207 0.0197  0.1957  0.0352  105 ASP   B CB  
5576 C  CB  B ASP   B 105 ? 0.5469 0.5108 0.5229 0.0123  0.1150  0.0320  105 ASP   B CB  
5577 C  CG  A ASP   B 105 ? 0.5585 0.5130 0.5590 0.0258  0.2065  0.0244  105 ASP   B CG  
5578 C  CG  B ASP   B 105 ? 0.5507 0.5164 0.5469 0.0131  0.1153  0.0248  105 ASP   B CG  
5579 O  OD1 A ASP   B 105 ? 0.5591 0.5150 0.5628 0.0191  0.2197  0.0293  105 ASP   B OD1 
5580 O  OD1 B ASP   B 105 ? 0.5522 0.5184 0.5525 0.0091  0.1176  0.0261  105 ASP   B OD1 
5581 O  OD2 A ASP   B 105 ? 0.5590 0.5140 0.5871 0.0372  0.2018  0.0113  105 ASP   B OD2 
5582 O  OD2 B ASP   B 105 ? 0.5505 0.5174 0.5635 0.0175  0.1125  0.0185  105 ASP   B OD2 
5591 N  N   A ILE   B 106 ? 0.5107 0.4418 0.4617 -0.0106 0.1772  0.0377  106 ILE   B N   
5592 N  N   B ILE   B 106 ? 0.5056 0.4661 0.4702 -0.0036 0.1025  0.0248  106 ILE   B N   
5593 C  CA  A ILE   B 106 ? 0.4936 0.4205 0.4592 -0.0236 0.1746  0.0298  106 ILE   B CA  
5594 C  CA  B ILE   B 106 ? 0.4884 0.4507 0.4594 -0.0094 0.0988  0.0156  106 ILE   B CA  
5595 C  C   A ILE   B 106 ? 0.4655 0.4101 0.4485 -0.0234 0.1677  0.0220  106 ILE   B C   
5596 C  C   B ILE   B 106 ? 0.4659 0.4377 0.4482 -0.0091 0.0985  0.0108  106 ILE   B C   
5597 O  O   A ILE   B 106 ? 0.4629 0.4018 0.4458 -0.0269 0.1769  0.0261  106 ILE   B O   
5598 O  O   B ILE   B 106 ? 0.4669 0.4359 0.4467 -0.0110 0.1009  0.0115  106 ILE   B O   
5599 C  CB  A ILE   B 106 ? 0.5048 0.4140 0.4664 -0.0363 0.1745  0.0299  106 ILE   B CB  
5600 C  CB  B ILE   B 106 ? 0.4942 0.4503 0.4613 -0.0150 0.0951  0.0111  106 ILE   B CB  
5601 C  CG1 A ILE   B 106 ? 0.5115 0.4125 0.4720 -0.0433 0.1710  0.0290  106 ILE   B CG1 
5602 C  CG1 B ILE   B 106 ? 0.4992 0.4522 0.4644 -0.0185 0.0910  0.0084  106 ILE   B CG1 
5603 C  CG2 A ILE   B 106 ? 0.5065 0.4137 0.4810 -0.0369 0.1757  0.0302  106 ILE   B CG2 
5604 C  CG2 B ILE   B 106 ? 0.4943 0.4502 0.4690 -0.0147 0.0953  0.0095  106 ILE   B CG2 
5605 C  CD1 A ILE   B 106 ? 0.5163 0.4137 0.4686 -0.0465 0.1678  0.0293  106 ILE   B CD1 
5606 C  CD1 B ILE   B 106 ? 0.5029 0.4544 0.4624 -0.0203 0.0878  0.0066  106 ILE   B CD1 
5629 N  N   A GLN   B 107 ? 0.4370 0.4082 0.4482 -0.0260 0.1585  0.0177  107 GLN   B N   
5630 N  N   B GLN   B 107 ? 0.4412 0.4262 0.4431 -0.0095 0.0988  0.0085  107 GLN   B N   
5631 C  CA  A GLN   B 107 ? 0.4124 0.4055 0.4561 -0.0225 0.1352  0.0221  107 GLN   B CA  
5632 C  CA  B GLN   B 107 ? 0.4174 0.4138 0.4441 -0.0071 0.0936  0.0124  107 GLN   B CA  
5633 C  C   A GLN   B 107 ? 0.3741 0.3796 0.4143 -0.0088 0.1168  0.0156  107 GLN   B C   
5634 C  C   B GLN   B 107 ? 0.3809 0.3860 0.4063 0.0005  0.0982  0.0135  107 GLN   B C   
5635 O  O   A GLN   B 107 ? 0.3596 0.3779 0.4161 -0.0044 0.1027  -0.0019 107 GLN   B O   
5636 O  O   B GLN   B 107 ? 0.3763 0.3857 0.4028 0.0030  0.0915  0.0048  107 GLN   B O   
5637 C  CB  A GLN   B 107 ? 0.4321 0.4323 0.5090 -0.0238 0.1188  0.0261  107 GLN   B CB  
5638 C  CB  B GLN   B 107 ? 0.4314 0.4299 0.4819 -0.0082 0.0804  0.0130  107 GLN   B CB  
5639 C  CG  A GLN   B 107 ? 0.4506 0.4557 0.5645 -0.0201 0.0965  0.0288  107 GLN   B CG  
5640 C  CG  B GLN   B 107 ? 0.4438 0.4440 0.5233 -0.0065 0.0647  0.0138  107 GLN   B CG  
5641 C  CD  A GLN   B 107 ? 0.4634 0.4725 0.6062 -0.0172 0.0811  0.0330  107 GLN   B CD  
5642 C  CD  B GLN   B 107 ? 0.4527 0.4545 0.5547 -0.0047 0.0531  0.0149  107 GLN   B CD  
5643 O  OE1 A GLN   B 107 ? 0.4666 0.4807 0.6223 -0.0109 0.0804  0.0322  107 GLN   B OE1 
5644 O  OE1 B GLN   B 107 ? 0.4554 0.4593 0.5667 -0.0021 0.0529  0.0155  107 GLN   B OE1 
5645 N  NE2 A GLN   B 107 ? 0.4698 0.4765 0.6206 -0.0180 0.0731  0.0376  107 GLN   B NE2 
5646 N  NE2 B GLN   B 107 ? 0.4565 0.4574 0.5656 -0.0044 0.0475  0.0158  107 GLN   B NE2 
5663 N  N   . LEU   B 108 ? 0.3457 0.3587 0.3794 0.0095  0.1102  0.0219  108 LEU   B N   
5664 C  CA  . LEU   B 108 ? 0.2992 0.3162 0.3333 0.0259  0.1009  0.0461  108 LEU   B CA  
5665 C  C   . LEU   B 108 ? 0.2277 0.2502 0.3310 0.0295  0.0810  0.0409  108 LEU   B C   
5666 O  O   . LEU   B 108 ? 0.2182 0.2288 0.3334 0.0359  0.0656  0.0442  108 LEU   B O   
5667 C  CB  . LEU   B 108 ? 0.3176 0.3347 0.3187 0.0300  0.0966  0.0674  108 LEU   B CB  
5668 C  CG  . LEU   B 108 ? 0.3386 0.3617 0.3391 0.0326  0.0927  0.0509  108 LEU   B CG  
5669 C  CD1 . LEU   B 108 ? 0.3557 0.3763 0.3408 0.0242  0.0907  0.0473  108 LEU   B CD1 
5670 C  CD2 . LEU   B 108 ? 0.3456 0.3704 0.3410 0.0471  0.0845  0.0398  108 LEU   B CD2 
5683 N  N   . LEU   B 109 ? 0.2075 0.2205 0.3434 0.0109  0.0645  0.0356  109 LEU   B N   
5684 C  CA  . LEU   B 109 ? 0.1768 0.1692 0.3738 0.0009  0.0543  0.0395  109 LEU   B CA  
5685 C  C   . LEU   B 109 ? 0.1645 0.1521 0.3816 0.0009  0.0518  0.0283  109 LEU   B C   
5686 O  O   . LEU   B 109 ? 0.1666 0.1446 0.3789 0.0077  0.0450  0.0422  109 LEU   B O   
5687 C  CB  . LEU   B 109 ? 0.1825 0.1574 0.3678 -0.0050 0.0442  0.0401  109 LEU   B CB  
5688 C  CG  . LEU   B 109 ? 0.1884 0.1510 0.3432 -0.0009 0.0320  0.0243  109 LEU   B CG  
5689 C  CD1 . LEU   B 109 ? 0.1892 0.1616 0.3226 0.0048  0.0378  0.0243  109 LEU   B CD1 
5690 C  CD2 . LEU   B 109 ? 0.2023 0.1574 0.3615 0.0066  0.0186  0.0406  109 LEU   B CD2 
5702 N  N   . LYS   B 110 ? 0.1656 0.1503 0.3798 -0.0096 0.0521  0.0151  110 LYS   B N   
5703 C  CA  . LYS   B 110 ? 0.1637 0.1503 0.3911 -0.0050 0.0363  0.0184  110 LYS   B CA  
5704 C  C   . LYS   B 110 ? 0.1551 0.1549 0.3753 -0.0010 0.0434  0.0195  110 LYS   B C   
5705 O  O   . LYS   B 110 ? 0.1563 0.1511 0.3765 -0.0035 0.0319  0.0046  110 LYS   B O   
5706 C  CB  . LYS   B 110 ? 0.1642 0.1438 0.4256 -0.0042 0.0401  0.0234  110 LYS   B CB  
5707 C  CG  . LYS   B 110 ? 0.1691 0.1480 0.4194 -0.0104 0.0321  0.0386  110 LYS   B CG  
5708 C  CD  . LYS   B 110 ? 0.1716 0.1514 0.4093 -0.0157 0.0174  0.0319  110 LYS   B CD  
5709 C  CE  . LYS   B 110 ? 0.1721 0.1618 0.4213 -0.0122 0.0113  0.0178  110 LYS   B CE  
5710 N  NZ  . LYS   B 110 ? 0.1707 0.1773 0.4032 -0.0030 0.0166  0.0224  110 LYS   B NZ  
5724 N  N   . SER   B 111 ? 0.1634 0.1561 0.3832 -0.0082 0.0390  0.0225  111 SER   B N   
5725 C  CA  . SER   B 111 ? 0.1678 0.1566 0.3490 -0.0051 0.0431  0.0283  111 SER   B CA  
5726 C  C   . SER   B 111 ? 0.1631 0.1521 0.3341 -0.0046 0.0399  0.0118  111 SER   B C   
5727 O  O   . SER   B 111 ? 0.1560 0.1563 0.3550 -0.0125 0.0297  0.0079  111 SER   B O   
5728 C  CB  . SER   B 111 ? 0.1794 0.1747 0.3620 0.0042  0.0512  0.0354  111 SER   B CB  
5729 O  OG  . SER   B 111 ? 0.1978 0.2043 0.3698 0.0105  0.0631  0.0564  111 SER   B OG  
5735 N  N   . ALA   B 112 ? 0.1564 0.1572 0.3343 -0.0011 0.0396  0.0141  112 ALA   B N   
5736 C  CA  . ALA   B 112 ? 0.1535 0.1629 0.3165 -0.0058 0.0201  0.0103  112 ALA   B CA  
5737 C  C   . ALA   B 112 ? 0.1401 0.1573 0.3233 -0.0053 0.0214  0.0019  112 ALA   B C   
5738 O  O   . ALA   B 112 ? 0.1476 0.1538 0.3471 -0.0105 0.0215  0.0048  112 ALA   B O   
5739 C  CB  . ALA   B 112 ? 0.1562 0.1720 0.3232 -0.0047 0.0235  0.0224  112 ALA   B CB  
5745 N  N   . TYR   B 113 ? 0.1426 0.1421 0.3237 -0.0073 0.0250  0.0077  113 TYR   B N   
5746 C  CA  . TYR   B 113 ? 0.1427 0.1450 0.3287 -0.0102 0.0217  0.0064  113 TYR   B CA  
5747 C  C   . TYR   B 113 ? 0.1356 0.1325 0.3383 -0.0115 0.0252  0.0110  113 TYR   B C   
5748 O  O   . TYR   B 113 ? 0.1414 0.1411 0.3188 -0.0084 0.0133  0.0021  113 TYR   B O   
5749 C  CB  . TYR   B 113 ? 0.1491 0.1361 0.3345 -0.0071 0.0277  0.0104  113 TYR   B CB  
5750 C  CG  . TYR   B 113 ? 0.1482 0.1367 0.3430 -0.0107 0.0165  0.0208  113 TYR   B CG  
5751 C  CD1 . TYR   B 113 ? 0.1555 0.1492 0.3545 -0.0058 0.0187  0.0260  113 TYR   B CD1 
5752 C  CD2 . TYR   B 113 ? 0.1617 0.1354 0.3518 -0.0052 0.0016  0.0217  113 TYR   B CD2 
5753 C  CE1 . TYR   B 113 ? 0.1622 0.1464 0.3602 -0.0055 0.0271  0.0114  113 TYR   B CE1 
5754 C  CE2 . TYR   B 113 ? 0.1684 0.1363 0.3700 -0.0039 0.0109  0.0221  113 TYR   B CE2 
5755 C  CZ  . TYR   B 113 ? 0.1604 0.1386 0.3761 0.0007  0.0143  0.0151  113 TYR   B CZ  
5756 O  OH  . TYR   B 113 ? 0.1680 0.1318 0.4094 0.0069  0.0369  0.0199  113 TYR   B OH  
5766 N  N   . GLU   B 114 ? 0.1383 0.1267 0.3448 -0.0075 0.0181  0.0067  114 GLU   B N   
5767 C  CA  . GLU   B 114 ? 0.1394 0.1292 0.3582 -0.0010 0.0101  0.0037  114 GLU   B CA  
5768 C  C   . GLU   B 114 ? 0.1401 0.1359 0.3519 -0.0057 0.0173  0.0074  114 GLU   B C   
5769 O  O   . GLU   B 114 ? 0.1406 0.1361 0.3555 -0.0029 -0.0055 0.0162  114 GLU   B O   
5770 C  CB  . GLU   B 114 ? 0.1473 0.1314 0.3626 -0.0010 0.0219  0.0164  114 GLU   B CB  
5771 C  CG  . GLU   B 114 ? 0.1507 0.1341 0.3607 -0.0060 0.0113  0.0104  114 GLU   B CG  
5772 C  CD  . GLU   B 114 ? 0.1413 0.1398 0.3654 -0.0087 0.0112  0.0203  114 GLU   B CD  
5773 O  OE1 . GLU   B 114 ? 0.1451 0.1554 0.3692 -0.0066 0.0208  0.0213  114 GLU   B OE1 
5774 O  OE2 . GLU   B 114 ? 0.1427 0.1610 0.3794 -0.0178 0.0086  0.0209  114 GLU   B OE2 
5781 N  N   . ASN   B 115 ? 0.1435 0.1322 0.3343 -0.0061 0.0074  0.0172  115 ASN   B N   
5782 C  CA  . ASN   B 115 ? 0.1454 0.1349 0.3022 -0.0106 0.0083  0.0131  115 ASN   B CA  
5783 C  C   . ASN   B 115 ? 0.1396 0.1323 0.3018 -0.0114 -0.0033 -0.0072 115 ASN   B C   
5784 O  O   . ASN   B 115 ? 0.1477 0.1391 0.3069 -0.0174 0.0019  0.0015  115 ASN   B O   
5785 C  CB  . ASN   B 115 ? 0.1583 0.1498 0.2992 -0.0095 0.0099  0.0046  115 ASN   B CB  
5786 C  CG  . ASN   B 115 ? 0.1720 0.1543 0.2982 -0.0058 0.0087  -0.0069 115 ASN   B CG  
5787 O  OD1 . ASN   B 115 ? 0.2186 0.1693 0.3233 -0.0041 0.0230  -0.0004 115 ASN   B OD1 
5788 N  ND2 . ASN   B 115 ? 0.1632 0.1620 0.3063 -0.0140 0.0236  0.0099  115 ASN   B ND2 
5795 N  N   . PHE   B 116 ? 0.1426 0.1368 0.2944 -0.0084 0.0013  -0.0100 116 PHE   B N   
5796 C  CA  . PHE   B 116 ? 0.1463 0.1374 0.3078 -0.0132 0.0002  -0.0038 116 PHE   B CA  
5797 C  C   . PHE   B 116 ? 0.1466 0.1204 0.3100 -0.0117 -0.0054 0.0064  116 PHE   B C   
5798 O  O   . PHE   B 116 ? 0.1488 0.1427 0.3093 -0.0089 -0.0147 0.0165  116 PHE   B O   
5799 C  CB  . PHE   B 116 ? 0.1390 0.1359 0.2910 -0.0057 -0.0084 0.0053  116 PHE   B CB  
5800 C  CG  . PHE   B 116 ? 0.1348 0.1396 0.2887 -0.0130 -0.0100 0.0068  116 PHE   B CG  
5801 C  CD1 . PHE   B 116 ? 0.1432 0.1440 0.2931 -0.0029 0.0069  0.0039  116 PHE   B CD1 
5802 C  CD2 . PHE   B 116 ? 0.1465 0.1485 0.2804 -0.0100 0.0018  0.0048  116 PHE   B CD2 
5803 C  CE1 . PHE   B 116 ? 0.1535 0.1461 0.2908 -0.0094 -0.0096 0.0005  116 PHE   B CE1 
5804 C  CE2 . PHE   B 116 ? 0.1441 0.1500 0.2815 -0.0060 -0.0053 0.0063  116 PHE   B CE2 
5805 C  CZ  . PHE   B 116 ? 0.1419 0.1447 0.2805 -0.0076 -0.0075 0.0081  116 PHE   B CZ  
5815 N  N   . ASN   B 117 ? 0.1462 0.1374 0.3274 -0.0072 -0.0087 0.0106  117 ASN   B N   
5816 C  CA  . ASN   B 117 ? 0.1510 0.1360 0.3346 -0.0038 -0.0077 0.0029  117 ASN   B CA  
5817 C  C   . ASN   B 117 ? 0.1498 0.1284 0.3518 -0.0132 -0.0129 0.0068  117 ASN   B C   
5818 O  O   . ASN   B 117 ? 0.1572 0.1388 0.3857 -0.0106 -0.0467 0.0237  117 ASN   B O   
5819 C  CB  . ASN   B 117 ? 0.1540 0.1413 0.3545 -0.0088 -0.0028 -0.0021 117 ASN   B CB  
5820 C  CG  . ASN   B 117 ? 0.1476 0.1441 0.3551 -0.0013 -0.0050 -0.0029 117 ASN   B CG  
5821 O  OD1 . ASN   B 117 ? 0.1687 0.1439 0.3625 -0.0226 -0.0058 -0.0012 117 ASN   B OD1 
5822 N  ND2 . ASN   B 117 ? 0.1482 0.1543 0.3283 -0.0055 -0.0053 -0.0062 117 ASN   B ND2 
5829 N  N   . GLN   B 118 ? 0.1531 0.1297 0.3352 -0.0153 -0.0154 0.0052  118 GLN   B N   
5830 C  CA  . GLN   B 118 ? 0.1570 0.1417 0.3431 -0.0089 -0.0102 0.0092  118 GLN   B CA  
5831 C  C   . GLN   B 118 ? 0.1592 0.1406 0.3505 -0.0093 -0.0220 0.0143  118 GLN   B C   
5832 O  O   . GLN   B 118 ? 0.1799 0.1374 0.3830 -0.0146 -0.0065 0.0155  118 GLN   B O   
5833 C  CB  . GLN   B 118 ? 0.1652 0.1413 0.3480 -0.0019 -0.0171 0.0070  118 GLN   B CB  
5834 C  CG  . GLN   B 118 ? 0.1720 0.1440 0.3470 0.0008  -0.0081 -0.0060 118 GLN   B CG  
5835 C  CD  . GLN   B 118 ? 0.1774 0.1370 0.3560 -0.0019 -0.0078 -0.0149 118 GLN   B CD  
5836 O  OE1 . GLN   B 118 ? 0.1843 0.1408 0.3791 -0.0034 0.0118  0.0048  118 GLN   B OE1 
5837 N  NE2 . GLN   B 118 ? 0.1851 0.1442 0.3632 -0.0020 -0.0149 0.0045  118 GLN   B NE2 
5846 N  N   . HIS   B 119 ? 0.1674 0.1433 0.3076 -0.0160 -0.0312 0.0266  119 HIS   B N   
5847 C  CA  . HIS   B 119 ? 0.1797 0.1542 0.2986 -0.0087 -0.0282 0.0226  119 HIS   B CA  
5848 C  C   . HIS   B 119 ? 0.1898 0.1650 0.2824 -0.0125 -0.0485 0.0309  119 HIS   B C   
5849 O  O   . HIS   B 119 ? 0.1875 0.1528 0.3005 -0.0386 -0.0423 0.0224  119 HIS   B O   
5850 C  CB  . HIS   B 119 ? 0.1842 0.1592 0.2890 -0.0081 -0.0260 0.0166  119 HIS   B CB  
5851 C  CG  . HIS   B 119 ? 0.1856 0.1878 0.2911 -0.0020 -0.0487 0.0016  119 HIS   B CG  
5852 N  ND1 . HIS   B 119 ? 0.1938 0.2037 0.3118 -0.0035 -0.0616 -0.0178 119 HIS   B ND1 
5853 C  CD2 . HIS   B 119 ? 0.2058 0.2134 0.2797 0.0333  -0.0583 -0.0054 119 HIS   B CD2 
5854 C  CE1 . HIS   B 119 ? 0.2162 0.2204 0.3141 0.0203  -0.0653 -0.0253 119 HIS   B CE1 
5855 N  NE2 . HIS   B 119 ? 0.2225 0.2335 0.2880 0.0315  -0.0609 -0.0328 119 HIS   B NE2 
5863 N  N   A GLU   B 120 ? 0.2098 0.1603 0.2791 -0.0247 -0.0696 0.0420  120 GLU   B N   
5864 N  N   B GLU   B 120 ? 0.2100 0.1735 0.2738 -0.0183 -0.0564 0.0332  120 GLU   B N   
5865 C  CA  A GLU   B 120 ? 0.2426 0.1759 0.2991 -0.0237 -0.0778 0.0533  120 GLU   B CA  
5866 C  CA  B GLU   B 120 ? 0.2357 0.1897 0.2850 -0.0177 -0.0626 0.0376  120 GLU   B CA  
5867 C  C   A GLU   B 120 ? 0.2174 0.1623 0.2927 -0.0367 -0.0693 0.0510  120 GLU   B C   
5868 C  C   B GLU   B 120 ? 0.2185 0.1752 0.2744 -0.0287 -0.0620 0.0404  120 GLU   B C   
5869 O  O   A GLU   B 120 ? 0.2043 0.1754 0.3077 -0.0413 -0.0804 0.0470  120 GLU   B O   
5870 O  O   B GLU   B 120 ? 0.2126 0.1822 0.2725 -0.0285 -0.0670 0.0405  120 GLU   B O   
5871 C  CB  A GLU   B 120 ? 0.3027 0.2206 0.3555 -0.0077 -0.0865 0.0631  120 GLU   B CB  
5872 C  CB  B GLU   B 120 ? 0.2782 0.2246 0.3307 -0.0047 -0.0654 0.0390  120 GLU   B CB  
5873 C  CG  A GLU   B 120 ? 0.3445 0.2661 0.4198 0.0012  -0.0966 0.0660  120 GLU   B CG  
5874 C  CG  B GLU   B 120 ? 0.3095 0.2591 0.3820 0.0042  -0.0691 0.0402  120 GLU   B CG  
5875 C  CD  A GLU   B 120 ? 0.3740 0.3089 0.4897 -0.0028 -0.0971 0.0688  120 GLU   B CD  
5876 C  CD  B GLU   B 120 ? 0.3361 0.2940 0.4345 0.0059  -0.0649 0.0394  120 GLU   B CD  
5877 O  OE1 A GLU   B 120 ? 0.3898 0.3281 0.5186 -0.0098 -0.0893 0.0790  120 GLU   B OE1 
5878 O  OE1 B GLU   B 120 ? 0.3505 0.3080 0.4596 0.0038  -0.0615 0.0398  120 GLU   B OE1 
5879 O  OE2 A GLU   B 120 ? 0.3962 0.3356 0.5341 -0.0065 -0.0981 0.0539  120 GLU   B OE2 
5880 O  OE2 B GLU   B 120 ? 0.3530 0.3133 0.4593 0.0054  -0.0662 0.0367  120 GLU   B OE2 
5893 N  N   . VAL   B 121 ? 0.2058 0.1628 0.2785 -0.0386 -0.0580 0.0360  121 VAL   B N   
5894 C  CA  . VAL   B 121 ? 0.1956 0.1745 0.2471 -0.0322 -0.0481 0.0448  121 VAL   B CA  
5895 C  C   . VAL   B 121 ? 0.1903 0.1647 0.2430 -0.0385 -0.0370 0.0368  121 VAL   B C   
5896 O  O   . VAL   B 121 ? 0.1982 0.1659 0.2565 -0.0463 -0.0456 0.0278  121 VAL   B O   
5897 C  CB  . VAL   B 121 ? 0.2208 0.2160 0.2616 -0.0271 -0.0522 0.0359  121 VAL   B CB  
5898 C  CG1 . VAL   B 121 ? 0.2245 0.2216 0.2977 -0.0404 -0.0340 0.0146  121 VAL   B CG1 
5899 C  CG2 . VAL   B 121 ? 0.2528 0.2475 0.2681 -0.0150 -0.0513 0.0350  121 VAL   B CG2 
5910 N  N   . LEU   B 122 ? 0.1815 0.1599 0.2425 -0.0331 -0.0413 0.0301  122 LEU   B N   
5911 C  CA  . LEU   B 122 ? 0.1638 0.1702 0.2430 -0.0336 -0.0271 0.0269  122 LEU   B CA  
5912 C  C   . LEU   B 122 ? 0.1640 0.1568 0.2459 -0.0418 -0.0208 0.0277  122 LEU   B C   
5913 O  O   . LEU   B 122 ? 0.1753 0.1588 0.2733 -0.0472 -0.0345 0.0218  122 LEU   B O   
5914 C  CB  . LEU   B 122 ? 0.1785 0.1850 0.2681 -0.0093 -0.0269 0.0193  122 LEU   B CB  
5915 C  CG  . LEU   B 122 ? 0.1708 0.1902 0.2744 -0.0234 -0.0128 0.0236  122 LEU   B CG  
5916 C  CD1 . LEU   B 122 ? 0.1831 0.2139 0.2766 -0.0288 -0.0173 0.0248  122 LEU   B CD1 
5917 C  CD2 . LEU   B 122 ? 0.1751 0.1815 0.2732 -0.0193 -0.0107 0.0164  122 LEU   B CD2 
5929 N  N   . LEU   B 123 ? 0.1628 0.1477 0.2269 -0.0297 -0.0208 0.0190  123 LEU   B N   
5930 C  CA  . LEU   B 123 ? 0.1692 0.1463 0.2397 -0.0317 -0.0241 0.0162  123 LEU   B CA  
5931 C  C   . LEU   B 123 ? 0.1607 0.1458 0.2425 -0.0360 -0.0256 0.0109  123 LEU   B C   
5932 O  O   . LEU   B 123 ? 0.1747 0.1459 0.2395 -0.0371 -0.0225 0.0034  123 LEU   B O   
5933 C  CB  . LEU   B 123 ? 0.1798 0.1573 0.2415 -0.0317 -0.0233 0.0005  123 LEU   B CB  
5934 C  CG  . LEU   B 123 ? 0.1675 0.1540 0.2558 -0.0248 -0.0191 0.0030  123 LEU   B CG  
5935 C  CD1 . LEU   B 123 ? 0.1828 0.1647 0.2841 -0.0334 -0.0147 -0.0057 123 LEU   B CD1 
5936 C  CD2 . LEU   B 123 ? 0.1829 0.1690 0.2620 -0.0251 -0.0083 0.0215  123 LEU   B CD2 
5948 N  N   . ALA   B 124 ? 0.1540 0.1463 0.2385 -0.0239 -0.0172 0.0107  124 ALA   B N   
5949 C  CA  . ALA   B 124 ? 0.1514 0.1441 0.2403 -0.0169 -0.0178 0.0092  124 ALA   B CA  
5950 C  C   . ALA   B 124 ? 0.1471 0.1453 0.2294 -0.0311 -0.0250 0.0196  124 ALA   B C   
5951 O  O   . ALA   B 124 ? 0.1589 0.1452 0.2468 -0.0220 -0.0286 0.0120  124 ALA   B O   
5952 C  CB  . ALA   B 124 ? 0.1564 0.1499 0.2563 -0.0098 -0.0151 0.0011  124 ALA   B CB  
5958 N  N   . PRO   B 125 ? 0.1645 0.1439 0.2330 -0.0175 -0.0214 0.0243  125 PRO   B N   
5959 C  CA  . PRO   B 125 ? 0.1656 0.1505 0.2595 -0.0220 -0.0234 0.0333  125 PRO   B CA  
5960 C  C   . PRO   B 125 ? 0.1538 0.1452 0.2910 -0.0174 -0.0139 0.0192  125 PRO   B C   
5961 O  O   . PRO   B 125 ? 0.1598 0.1401 0.2942 -0.0134 -0.0120 0.0219  125 PRO   B O   
5962 C  CB  . PRO   B 125 ? 0.1701 0.1681 0.2674 -0.0230 -0.0343 0.0330  125 PRO   B CB  
5963 C  CG  . PRO   B 125 ? 0.1822 0.1721 0.2539 -0.0330 -0.0305 0.0155  125 PRO   B CG  
5964 C  CD  . PRO   B 125 ? 0.1751 0.1557 0.2290 -0.0347 -0.0234 0.0134  125 PRO   B CD  
5972 N  N   . LEU   B 126 ? 0.1594 0.1409 0.3006 -0.0182 0.0114  0.0266  126 LEU   B N   
5973 C  CA  . LEU   B 126 ? 0.1739 0.1500 0.3151 -0.0082 0.0172  0.0360  126 LEU   B CA  
5974 C  C   . LEU   B 126 ? 0.1706 0.1688 0.3034 0.0097  0.0210  0.0404  126 LEU   B C   
5975 O  O   . LEU   B 126 ? 0.2032 0.2090 0.3350 0.0353  -0.0047 0.0064  126 LEU   B O   
5976 C  CB  . LEU   B 126 ? 0.1919 0.1591 0.3368 -0.0043 0.0264  0.0293  126 LEU   B CB  
5977 C  CG  . LEU   B 126 ? 0.2105 0.1632 0.3489 -0.0213 0.0262  0.0086  126 LEU   B CG  
5978 C  CD1 . LEU   B 126 ? 0.2243 0.1703 0.3906 -0.0274 0.0165  0.0129  126 LEU   B CD1 
5979 C  CD2 . LEU   B 126 ? 0.2123 0.1669 0.3427 -0.0290 0.0165  0.0047  126 LEU   B CD2 
5991 N  N   . LEU   B 127 ? 0.1703 0.1491 0.3207 0.0085  0.0220  0.0169  127 LEU   B N   
5992 C  CA  . LEU   B 127 ? 0.1685 0.1561 0.3260 -0.0041 0.0260  0.0276  127 LEU   B CA  
5993 C  C   . LEU   B 127 ? 0.1673 0.1434 0.3499 -0.0021 0.0277  0.0238  127 LEU   B C   
5994 O  O   . LEU   B 127 ? 0.1714 0.1457 0.3740 -0.0192 0.0240  0.0269  127 LEU   B O   
5995 C  CB  . LEU   B 127 ? 0.1787 0.1503 0.3380 -0.0061 0.0319  0.0372  127 LEU   B CB  
5996 C  CG  . LEU   B 127 ? 0.1889 0.1536 0.3402 -0.0005 0.0276  0.0278  127 LEU   B CG  
5997 C  CD1 . LEU   B 127 ? 0.2027 0.1497 0.3242 0.0111  0.0249  0.0218  127 LEU   B CD1 
5998 C  CD2 . LEU   B 127 ? 0.1842 0.1679 0.3511 -0.0174 0.0268  0.0387  127 LEU   B CD2 
6010 N  N   . SER   B 128 ? 0.1742 0.1523 0.3504 0.0038  0.0107  0.0196  128 SER   B N   
6011 C  CA  . SER   B 128 ? 0.1846 0.1591 0.3527 0.0084  -0.0019 0.0269  128 SER   B CA  
6012 C  C   . SER   B 128 ? 0.2019 0.1644 0.3889 0.0077  -0.0204 0.0160  128 SER   B C   
6013 O  O   . SER   B 128 ? 0.2198 0.1679 0.4308 0.0031  -0.0377 0.0336  128 SER   B O   
6014 C  CB  . SER   B 128 ? 0.1898 0.1612 0.3554 -0.0031 0.0093  0.0477  128 SER   B CB  
6015 O  OG  . SER   B 128 ? 0.1921 0.1798 0.3588 0.0117  0.0187  0.0633  128 SER   B OG  
6021 N  N   . ALA   B 129 ? 0.2110 0.1807 0.4004 0.0258  0.0016  0.0070  129 ALA   B N   
6022 C  CA  . ALA   B 129 ? 0.2272 0.1871 0.4099 0.0386  0.0007  -0.0041 129 ALA   B CA  
6023 C  C   . ALA   B 129 ? 0.2128 0.1804 0.3974 0.0299  0.0031  -0.0038 129 ALA   B C   
6024 O  O   . ALA   B 129 ? 0.2060 0.1848 0.3966 0.0262  -0.0121 -0.0094 129 ALA   B O   
6025 C  CB  . ALA   B 129 ? 0.2560 0.2116 0.4270 0.0283  0.0197  -0.0060 129 ALA   B CB  
6031 N  N   . GLY   B 130 ? 0.2123 0.1797 0.3851 0.0350  0.0206  -0.0066 130 GLY   B N   
6032 C  CA  . GLY   B 130 ? 0.2159 0.1911 0.3835 0.0303  0.0382  -0.0116 130 GLY   B CA  
6033 C  C   . GLY   B 130 ? 0.2204 0.1961 0.3628 0.0169  0.0290  -0.0081 130 GLY   B C   
6034 O  O   . GLY   B 130 ? 0.2286 0.2178 0.3713 0.0177  0.0146  0.0007  130 GLY   B O   
6038 N  N   . ILE   B 131 ? 0.2250 0.2025 0.3708 0.0309  0.0294  -0.0060 131 ILE   B N   
6039 C  CA  . ILE   B 131 ? 0.2551 0.2147 0.3568 0.0324  0.0203  0.0126  131 ILE   B CA  
6040 C  C   . ILE   B 131 ? 0.2643 0.2047 0.3402 0.0287  0.0264  0.0111  131 ILE   B C   
6041 O  O   . ILE   B 131 ? 0.2915 0.2296 0.3589 0.0275  0.0168  0.0182  131 ILE   B O   
6042 C  CB  . ILE   B 131 ? 0.2639 0.2487 0.3782 0.0298  0.0075  0.0186  131 ILE   B CB  
6043 C  CG1 . ILE   B 131 ? 0.2642 0.2627 0.3865 0.0034  0.0148  0.0174  131 ILE   B CG1 
6044 C  CG2 . ILE   B 131 ? 0.2755 0.2672 0.3805 0.0382  -0.0014 0.0147  131 ILE   B CG2 
6045 C  CD1 . ILE   B 131 ? 0.2761 0.2777 0.3936 -0.0171 0.0092  0.0156  131 ILE   B CD1 
6057 N  N   . PHE   B 132 ? 0.2546 0.1950 0.3376 0.0177  0.0375  0.0218  132 PHE   B N   
6058 C  CA  . PHE   B 132 ? 0.2606 0.1968 0.3474 0.0110  0.0531  0.0211  132 PHE   B CA  
6059 C  C   . PHE   B 132 ? 0.2940 0.2151 0.3712 0.0046  0.0645  0.0116  132 PHE   B C   
6060 O  O   . PHE   B 132 ? 0.3089 0.2495 0.3823 -0.0011 0.0821  0.0220  132 PHE   B O   
6061 C  CB  . PHE   B 132 ? 0.2371 0.2015 0.3212 0.0085  0.0602  0.0215  132 PHE   B CB  
6062 C  CG  . PHE   B 132 ? 0.2308 0.2057 0.3178 0.0097  0.0365  0.0260  132 PHE   B CG  
6063 C  CD1 . PHE   B 132 ? 0.2399 0.2041 0.3420 0.0073  0.0251  0.0170  132 PHE   B CD1 
6064 C  CD2 . PHE   B 132 ? 0.2261 0.2085 0.3039 0.0241  0.0379  0.0434  132 PHE   B CD2 
6065 C  CE1 . PHE   B 132 ? 0.2420 0.2025 0.3381 0.0054  0.0131  0.0209  132 PHE   B CE1 
6066 C  CE2 . PHE   B 132 ? 0.2302 0.2109 0.3018 0.0147  0.0302  0.0442  132 PHE   B CE2 
6067 C  CZ  . PHE   B 132 ? 0.2395 0.2066 0.3200 0.0124  0.0119  0.0452  132 PHE   B CZ  
6077 N  N   . GLY   B 133 ? 0.2997 0.1989 0.3792 -0.0067 0.0544  0.0274  133 GLY   B N   
6078 C  CA  . GLY   B 133 ? 0.2972 0.2150 0.3822 -0.0360 0.0482  0.0454  133 GLY   B CA  
6079 C  C   . GLY   B 133 ? 0.3068 0.2246 0.4020 -0.0561 0.0442  0.0534  133 GLY   B C   
6080 O  O   . GLY   B 133 ? 0.3268 0.2364 0.4307 -0.0667 0.0437  0.0684  133 GLY   B O   
6084 N  N   . ALA   B 134 ? 0.2951 0.2300 0.3804 -0.0543 0.0392  0.0299  134 ALA   B N   
6085 C  CA  . ALA   B 134 ? 0.2903 0.2264 0.3670 -0.0455 0.0481  0.0241  134 ALA   B CA  
6086 C  C   . ALA   B 134 ? 0.2877 0.2139 0.3653 -0.0323 0.0476  0.0391  134 ALA   B C   
6087 O  O   . ALA   B 134 ? 0.2828 0.2275 0.3683 -0.0165 0.0440  0.0383  134 ALA   B O   
6088 C  CB  . ALA   B 134 ? 0.2844 0.2264 0.3758 -0.0412 0.0420  0.0100  134 ALA   B CB  
6094 N  N   . ASP   B 135 ? 0.3030 0.1956 0.3699 -0.0326 0.0344  0.0397  135 ASP   B N   
6095 C  CA  . ASP   B 135 ? 0.3192 0.1936 0.3811 -0.0321 0.0236  0.0507  135 ASP   B CA  
6096 C  C   . ASP   B 135 ? 0.2867 0.1851 0.3729 -0.0146 0.0218  0.0525  135 ASP   B C   
6097 O  O   . ASP   B 135 ? 0.2739 0.1794 0.3847 -0.0160 0.0292  0.0448  135 ASP   B O   
6098 C  CB  . ASP   B 135 ? 0.3546 0.1972 0.4045 -0.0524 0.0235  0.0513  135 ASP   B CB  
6099 C  CG  . ASP   B 135 ? 0.3809 0.1976 0.4358 -0.0641 0.0225  0.0412  135 ASP   B CG  
6100 O  OD1 . ASP   B 135 ? 0.3869 0.1851 0.4513 -0.0427 0.0224  0.0408  135 ASP   B OD1 
6101 O  OD2 . ASP   B 135 ? 0.4006 0.2222 0.4774 -0.0764 0.0191  0.0196  135 ASP   B OD2 
6106 N  N   . PRO   B 136 ? 0.2706 0.1897 0.3848 0.0138  0.0008  0.0508  136 PRO   B N   
6107 C  CA  . PRO   B 136 ? 0.2401 0.1789 0.3922 0.0205  0.0021  0.0351  136 PRO   B CA  
6108 C  C   . PRO   B 136 ? 0.2114 0.1569 0.4191 0.0134  0.0055  0.0226  136 PRO   B C   
6109 O  O   . PRO   B 136 ? 0.1879 0.1533 0.4329 0.0064  -0.0015 0.0288  136 PRO   B O   
6110 C  CB  . PRO   B 136 ? 0.2479 0.2017 0.3817 0.0443  -0.0041 0.0206  136 PRO   B CB  
6111 C  CG  . PRO   B 136 ? 0.2738 0.2124 0.3911 0.0383  0.0085  0.0163  136 PRO   B CG  
6112 C  CD  . PRO   B 136 ? 0.2748 0.2036 0.3905 0.0406  0.0091  0.0394  136 PRO   B CD  
6120 N  N   . ILE   B 137 ? 0.2220 0.1460 0.4311 0.0125  0.0042  0.0165  137 ILE   B N   
6121 C  CA  . ILE   B 137 ? 0.2269 0.1420 0.4359 -0.0050 0.0126  0.0059  137 ILE   B CA  
6122 C  C   . ILE   B 137 ? 0.2176 0.1457 0.4152 -0.0141 0.0197  0.0092  137 ILE   B C   
6123 O  O   . ILE   B 137 ? 0.2073 0.1555 0.4190 -0.0149 0.0248  0.0100  137 ILE   B O   
6124 C  CB  . ILE   B 137 ? 0.2520 0.1584 0.4517 -0.0087 0.0205  0.0101  137 ILE   B CB  
6125 C  CG1 . ILE   B 137 ? 0.2726 0.1814 0.4806 -0.0005 0.0223  0.0085  137 ILE   B CG1 
6126 C  CG2 . ILE   B 137 ? 0.2606 0.1622 0.4672 -0.0416 0.0270  0.0124  137 ILE   B CG2 
6127 C  CD1 . ILE   B 137 ? 0.2883 0.2143 0.5042 0.0147  0.0109  0.0189  137 ILE   B CD1 
6139 N  N   . HIS   B 138 ? 0.2288 0.1454 0.4074 -0.0141 0.0315  0.0094  138 HIS   B N   
6140 C  CA  . HIS   B 138 ? 0.2401 0.1551 0.4048 -0.0130 0.0457  0.0225  138 HIS   B CA  
6141 C  C   . HIS   B 138 ? 0.2109 0.1575 0.4192 -0.0141 0.0340  0.0324  138 HIS   B C   
6142 O  O   . HIS   B 138 ? 0.1973 0.1606 0.4510 -0.0062 0.0447  0.0333  138 HIS   B O   
6143 C  CB  . HIS   B 138 ? 0.2752 0.1801 0.3939 -0.0178 0.0748  0.0197  138 HIS   B CB  
6144 C  CG  . HIS   B 138 ? 0.3049 0.1973 0.4014 -0.0229 0.0916  0.0302  138 HIS   B CG  
6145 N  ND1 . HIS   B 138 ? 0.3147 0.2140 0.4181 -0.0182 0.1039  0.0263  138 HIS   B ND1 
6146 C  CD2 . HIS   B 138 ? 0.3234 0.2081 0.3905 -0.0290 0.0946  0.0245  138 HIS   B CD2 
6147 C  CE1 . HIS   B 138 ? 0.3184 0.2236 0.4152 -0.0173 0.1026  0.0242  138 HIS   B CE1 
6148 N  NE2 . HIS   B 138 ? 0.3280 0.2059 0.3997 -0.0139 0.0970  0.0157  138 HIS   B NE2 
6156 N  N   . SER   B 139 ? 0.2023 0.1489 0.4075 -0.0092 0.0251  0.0213  139 SER   B N   
6157 C  CA  . SER   B 139 ? 0.1975 0.1448 0.3849 -0.0067 0.0285  0.0165  139 SER   B CA  
6158 C  C   . SER   B 139 ? 0.1703 0.1357 0.3932 -0.0102 0.0262  0.0083  139 SER   B C   
6159 O  O   . SER   B 139 ? 0.1752 0.1378 0.4025 -0.0026 0.0171  0.0170  139 SER   B O   
6160 C  CB  . SER   B 139 ? 0.2077 0.1469 0.4000 -0.0052 0.0165  0.0094  139 SER   B CB  
6161 O  OG  . SER   B 139 ? 0.2071 0.1403 0.4069 -0.0077 -0.0003 0.0260  139 SER   B OG  
6167 N  N   . LEU   B 140 ? 0.1782 0.1380 0.3778 -0.0163 0.0306  0.0163  140 LEU   B N   
6168 C  CA  . LEU   B 140 ? 0.1819 0.1380 0.3768 -0.0091 0.0233  0.0064  140 LEU   B CA  
6169 C  C   . LEU   B 140 ? 0.1719 0.1341 0.4005 -0.0070 0.0107  0.0008  140 LEU   B C   
6170 O  O   . LEU   B 140 ? 0.1689 0.1486 0.4062 -0.0055 -0.0033 0.0116  140 LEU   B O   
6171 C  CB  . LEU   B 140 ? 0.1888 0.1316 0.3657 -0.0158 0.0351  -0.0108 140 LEU   B CB  
6172 C  CG  . LEU   B 140 ? 0.1998 0.1402 0.3739 -0.0178 0.0254  0.0080  140 LEU   B CG  
6173 C  CD1 . LEU   B 140 ? 0.2049 0.1452 0.3867 -0.0226 0.0293  -0.0025 140 LEU   B CD1 
6174 C  CD2 . LEU   B 140 ? 0.2158 0.1475 0.3788 -0.0074 0.0203  -0.0038 140 LEU   B CD2 
6186 N  N   . ARG   B 141 ? 0.1675 0.1380 0.4067 -0.0143 0.0120  -0.0056 141 ARG   B N   
6187 C  CA  . ARG   B 141 ? 0.1676 0.1435 0.4355 -0.0171 0.0193  -0.0033 141 ARG   B CA  
6188 C  C   . ARG   B 141 ? 0.1576 0.1371 0.4312 -0.0162 0.0109  -0.0068 141 ARG   B C   
6189 O  O   . ARG   B 141 ? 0.1636 0.1396 0.4500 -0.0207 -0.0022 -0.0139 141 ARG   B O   
6190 C  CB  . ARG   B 141 ? 0.1857 0.1568 0.4336 -0.0355 0.0323  -0.0018 141 ARG   B CB  
6191 C  CG  . ARG   B 141 ? 0.2320 0.1846 0.4409 -0.0336 0.0334  0.0047  141 ARG   B CG  
6192 C  CD  . ARG   B 141 ? 0.2899 0.2086 0.4310 -0.0278 0.0222  -0.0138 141 ARG   B CD  
6193 N  NE  . ARG   B 141 ? 0.3137 0.2101 0.4131 -0.0518 0.0376  -0.0243 141 ARG   B NE  
6194 C  CZ  . ARG   B 141 ? 0.3279 0.2025 0.3973 -0.0535 0.0409  -0.0352 141 ARG   B CZ  
6195 N  NH1 . ARG   B 141 ? 0.3334 0.1905 0.3884 -0.0524 0.0301  -0.0371 141 ARG   B NH1 
6196 N  NH2 . ARG   B 141 ? 0.3626 0.2167 0.4068 -0.0462 0.0345  -0.0196 141 ARG   B NH2 
6210 N  N   . VAL   B 142 ? 0.1662 0.1391 0.4257 -0.0135 0.0179  -0.0114 142 VAL   B N   
6211 C  CA  . VAL   B 142 ? 0.1570 0.1397 0.3994 -0.0038 0.0262  -0.0011 142 VAL   B CA  
6212 C  C   . VAL   B 142 ? 0.1520 0.1391 0.4136 -0.0110 0.0072  0.0019  142 VAL   B C   
6213 O  O   . VAL   B 142 ? 0.1586 0.1382 0.4309 -0.0051 0.0184  -0.0016 142 VAL   B O   
6214 C  CB  . VAL   B 142 ? 0.1706 0.1574 0.3826 -0.0021 0.0227  0.0040  142 VAL   B CB  
6215 C  CG1 . VAL   B 142 ? 0.1708 0.1518 0.3837 0.0055  0.0233  -0.0011 142 VAL   B CG1 
6216 C  CG2 . VAL   B 142 ? 0.1986 0.1685 0.3755 0.0007  0.0246  -0.0003 142 VAL   B CG2 
6226 N  N   . CYS   B 143 ? 0.1499 0.1395 0.3991 -0.0074 -0.0025 0.0075  143 CYS   B N   
6227 C  CA  . CYS   B 143 ? 0.1503 0.1391 0.3972 -0.0132 -0.0006 0.0054  143 CYS   B CA  
6228 C  C   . CYS   B 143 ? 0.1481 0.1440 0.3966 -0.0133 -0.0050 0.0046  143 CYS   B C   
6229 O  O   . CYS   B 143 ? 0.1507 0.1495 0.4003 -0.0088 -0.0181 0.0070  143 CYS   B O   
6230 C  CB  . CYS   B 143 ? 0.1578 0.1493 0.4019 -0.0150 -0.0012 0.0030  143 CYS   B CB  
6231 S  SG  . CYS   B 143 ? 0.1605 0.1639 0.3822 -0.0098 -0.0045 0.0088  143 CYS   B SG  
6237 N  N   . VAL   B 144 ? 0.1569 0.1468 0.4136 -0.0174 -0.0145 -0.0119 144 VAL   B N   
6238 C  CA  . VAL   B 144 ? 0.1730 0.1542 0.4344 -0.0250 -0.0303 -0.0188 144 VAL   B CA  
6239 C  C   . VAL   B 144 ? 0.1694 0.1548 0.4571 -0.0172 -0.0329 0.0017  144 VAL   B C   
6240 O  O   . VAL   B 144 ? 0.1684 0.1777 0.4738 -0.0123 -0.0309 0.0256  144 VAL   B O   
6241 C  CB  . VAL   B 144 ? 0.1995 0.1722 0.4612 -0.0311 -0.0326 -0.0336 144 VAL   B CB  
6242 C  CG1 . VAL   B 144 ? 0.2256 0.2246 0.4746 -0.0356 -0.0242 -0.0270 144 VAL   B CG1 
6243 C  CG2 . VAL   B 144 ? 0.2216 0.1869 0.4477 -0.0176 -0.0432 -0.0488 144 VAL   B CG2 
6253 N  N   . ASP   B 145 ? 0.1667 0.1464 0.4887 -0.0210 -0.0137 -0.0103 145 ASP   B N   
6254 C  CA  . ASP   B 145 ? 0.1627 0.1516 0.5048 -0.0180 0.0038  -0.0050 145 ASP   B CA  
6255 C  C   . ASP   B 145 ? 0.1571 0.1575 0.4905 -0.0216 -0.0004 -0.0082 145 ASP   B C   
6256 O  O   . ASP   B 145 ? 0.1577 0.1733 0.5230 -0.0250 0.0037  -0.0180 145 ASP   B O   
6257 C  CB  . ASP   B 145 ? 0.1793 0.1634 0.5337 -0.0280 0.0092  -0.0011 145 ASP   B CB  
6258 C  CG  . ASP   B 145 ? 0.1927 0.1679 0.5632 -0.0319 0.0183  -0.0035 145 ASP   B CG  
6259 O  OD1 . ASP   B 145 ? 0.1923 0.1642 0.5723 -0.0316 -0.0186 -0.0043 145 ASP   B OD1 
6260 O  OD2 . ASP   B 145 ? 0.2222 0.1862 0.6021 -0.0461 0.0496  0.0065  145 ASP   B OD2 
6265 N  N   . THR   B 146 ? 0.1502 0.1415 0.4442 -0.0159 -0.0032 0.0013  146 THR   B N   
6266 C  CA  . THR   B 146 ? 0.1662 0.1367 0.4140 -0.0136 0.0103  0.0033  146 THR   B CA  
6267 C  C   . THR   B 146 ? 0.1546 0.1453 0.4006 -0.0093 -0.0001 0.0087  146 THR   B C   
6268 O  O   . THR   B 146 ? 0.1538 0.1398 0.3978 -0.0091 -0.0128 0.0058  146 THR   B O   
6269 C  CB  . THR   B 146 ? 0.1613 0.1427 0.4061 -0.0115 0.0232  0.0073  146 THR   B CB  
6270 O  OG1 . THR   B 146 ? 0.1587 0.1401 0.4361 -0.0110 0.0280  0.0232  146 THR   B OG1 
6271 C  CG2 . THR   B 146 ? 0.1728 0.1513 0.4000 -0.0171 0.0218  -0.0030 146 THR   B CG2 
6279 N  N   . VAL   B 147 ? 0.1494 0.1440 0.3719 -0.0083 0.0053  0.0157  147 VAL   B N   
6280 C  CA  . VAL   B 147 ? 0.1615 0.1366 0.3579 -0.0138 -0.0132 0.0098  147 VAL   B CA  
6281 C  C   . VAL   B 147 ? 0.1607 0.1420 0.3808 -0.0232 -0.0252 0.0023  147 VAL   B C   
6282 O  O   . VAL   B 147 ? 0.1732 0.1506 0.3919 -0.0281 -0.0589 0.0072  147 VAL   B O   
6283 C  CB  . VAL   B 147 ? 0.1613 0.1534 0.3362 -0.0122 -0.0062 0.0103  147 VAL   B CB  
6284 C  CG1 . VAL   B 147 ? 0.1610 0.1662 0.3045 -0.0144 -0.0152 0.0104  147 VAL   B CG1 
6285 C  CG2 . VAL   B 147 ? 0.1656 0.1508 0.3297 -0.0179 -0.0103 0.0095  147 VAL   B CG2 
6295 N  N   . ARG   B 148 ? 0.1586 0.1518 0.3666 -0.0149 -0.0311 0.0001  148 ARG   B N   
6296 C  CA  . ARG   B 148 ? 0.1669 0.1557 0.3468 -0.0151 -0.0483 -0.0099 148 ARG   B CA  
6297 C  C   . ARG   B 148 ? 0.1711 0.1570 0.3314 -0.0158 -0.0555 0.0129  148 ARG   B C   
6298 O  O   . ARG   B 148 ? 0.1919 0.1894 0.3408 -0.0371 -0.0653 0.0202  148 ARG   B O   
6299 C  CB  . ARG   B 148 ? 0.1680 0.1609 0.3503 -0.0120 -0.0457 -0.0225 148 ARG   B CB  
6300 C  CG  . ARG   B 148 ? 0.1724 0.1746 0.3648 -0.0228 -0.0461 -0.0325 148 ARG   B CG  
6301 C  CD  . ARG   B 148 ? 0.1815 0.1993 0.3551 -0.0005 -0.0419 -0.0382 148 ARG   B CD  
6302 N  NE  . ARG   B 148 ? 0.1732 0.1944 0.3558 0.0122  -0.0475 -0.0333 148 ARG   B NE  
6303 C  CZ  . ARG   B 148 ? 0.1714 0.1858 0.3509 0.0049  -0.0310 -0.0273 148 ARG   B CZ  
6304 N  NH1 . ARG   B 148 ? 0.1608 0.1904 0.3483 -0.0070 -0.0048 -0.0315 148 ARG   B NH1 
6305 N  NH2 . ARG   B 148 ? 0.1823 0.1645 0.3503 0.0084  -0.0286 -0.0164 148 ARG   B NH2 
6319 N  N   . THR   B 149 ? 0.1772 0.1497 0.3364 -0.0223 -0.0584 0.0179  149 THR   B N   
6320 C  CA  . THR   B 149 ? 0.1852 0.1582 0.3223 -0.0306 -0.0586 0.0260  149 THR   B CA  
6321 C  C   . THR   B 149 ? 0.1861 0.1555 0.3126 -0.0311 -0.0599 0.0262  149 THR   B C   
6322 O  O   . THR   B 149 ? 0.1940 0.1588 0.3193 -0.0340 -0.0380 0.0229  149 THR   B O   
6323 C  CB  . THR   B 149 ? 0.1945 0.1585 0.3277 -0.0366 -0.0545 0.0119  149 THR   B CB  
6324 O  OG1 . THR   B 149 ? 0.1968 0.1677 0.3145 -0.0418 -0.0578 0.0235  149 THR   B OG1 
6325 C  CG2 . THR   B 149 ? 0.2022 0.1572 0.3312 -0.0245 -0.0426 0.0201  149 THR   B CG2 
6333 N  N   . ASN   B 150 ? 0.1886 0.1613 0.2971 -0.0317 -0.0647 0.0250  150 ASN   B N   
6334 C  CA  . ASN   B 150 ? 0.1988 0.1789 0.2734 -0.0340 -0.0499 0.0125  150 ASN   B CA  
6335 C  C   . ASN   B 150 ? 0.1880 0.1678 0.2886 -0.0251 -0.0471 0.0117  150 ASN   B C   
6336 O  O   . ASN   B 150 ? 0.1877 0.1644 0.3088 -0.0386 -0.0561 0.0099  150 ASN   B O   
6337 C  CB  . ASN   B 150 ? 0.2298 0.2170 0.2854 -0.0448 -0.0558 0.0236  150 ASN   B CB  
6338 C  CG  . ASN   B 150 ? 0.2548 0.2555 0.3062 -0.0464 -0.0489 0.0392  150 ASN   B CG  
6339 O  OD1 . ASN   B 150 ? 0.2627 0.2713 0.3111 -0.0460 -0.0623 0.0322  150 ASN   B OD1 
6340 N  ND2 . ASN   B 150 ? 0.2688 0.2756 0.3318 -0.0477 -0.0579 0.0721  150 ASN   B ND2 
6347 N  N   . VAL   B 151 ? 0.1787 0.1696 0.2977 -0.0366 -0.0480 0.0241  151 VAL   B N   
6348 C  CA  . VAL   B 151 ? 0.1813 0.1683 0.2926 -0.0424 -0.0423 0.0196  151 VAL   B CA  
6349 C  C   . VAL   B 151 ? 0.1853 0.1641 0.2821 -0.0524 -0.0508 0.0022  151 VAL   B C   
6350 O  O   . VAL   B 151 ? 0.1999 0.1767 0.2864 -0.0429 -0.0411 0.0000  151 VAL   B O   
6351 C  CB  . VAL   B 151 ? 0.1983 0.1677 0.2900 -0.0184 -0.0375 0.0143  151 VAL   B CB  
6352 C  CG1 . VAL   B 151 ? 0.2089 0.1711 0.3138 -0.0314 -0.0231 -0.0043 151 VAL   B CG1 
6353 C  CG2 . VAL   B 151 ? 0.2079 0.1818 0.2724 -0.0024 -0.0332 0.0070  151 VAL   B CG2 
6363 N  N   . TYR   B 152 ? 0.1884 0.1486 0.2667 -0.0378 -0.0519 0.0097  152 TYR   B N   
6364 C  CA  . TYR   B 152 ? 0.1904 0.1701 0.2632 -0.0469 -0.0369 0.0098  152 TYR   B CA  
6365 C  C   . TYR   B 152 ? 0.1818 0.1546 0.2782 -0.0400 -0.0290 -0.0005 152 TYR   B C   
6366 O  O   . TYR   B 152 ? 0.1836 0.1504 0.2843 -0.0324 -0.0302 0.0057  152 TYR   B O   
6367 C  CB  . TYR   B 152 ? 0.2193 0.1967 0.2370 -0.0651 -0.0446 0.0228  152 TYR   B CB  
6368 C  CG  . TYR   B 152 ? 0.2411 0.2127 0.2314 -0.0865 -0.0490 0.0284  152 TYR   B CG  
6369 C  CD1 . TYR   B 152 ? 0.2472 0.2307 0.2230 -0.0829 -0.0535 0.0309  152 TYR   B CD1 
6370 C  CD2 . TYR   B 152 ? 0.2645 0.2397 0.2229 -0.0841 -0.0484 0.0254  152 TYR   B CD2 
6371 C  CE1 . TYR   B 152 ? 0.2649 0.2576 0.2249 -0.0743 -0.0547 0.0421  152 TYR   B CE1 
6372 C  CE2 . TYR   B 152 ? 0.2739 0.2669 0.2226 -0.0791 -0.0561 0.0144  152 TYR   B CE2 
6373 C  CZ  . TYR   B 152 ? 0.2699 0.2822 0.2229 -0.0661 -0.0627 0.0387  152 TYR   B CZ  
6374 O  OH  . TYR   B 152 ? 0.2774 0.3181 0.2559 -0.0518 -0.0593 0.0395  152 TYR   B OH  
6384 N  N   . LEU   B 153 ? 0.1801 0.1569 0.2665 -0.0402 -0.0273 -0.0007 153 LEU   B N   
6385 C  CA  . LEU   B 153 ? 0.1825 0.1478 0.2575 -0.0308 -0.0241 -0.0088 153 LEU   B CA  
6386 C  C   . LEU   B 153 ? 0.1898 0.1490 0.2634 -0.0311 -0.0201 -0.0122 153 LEU   B C   
6387 O  O   . LEU   B 153 ? 0.2065 0.1734 0.2638 -0.0323 -0.0249 -0.0292 153 LEU   B O   
6388 C  CB  . LEU   B 153 ? 0.1867 0.1498 0.2806 -0.0313 -0.0197 0.0036  153 LEU   B CB  
6389 C  CG  . LEU   B 153 ? 0.1786 0.1545 0.3085 -0.0346 -0.0177 0.0116  153 LEU   B CG  
6390 C  CD1 . LEU   B 153 ? 0.1891 0.1719 0.3175 -0.0378 -0.0038 0.0185  153 LEU   B CD1 
6391 C  CD2 . LEU   B 153 ? 0.1769 0.1626 0.3100 -0.0324 -0.0127 0.0224  153 LEU   B CD2 
6403 N  N   . ALA   B 154 ? 0.1752 0.1457 0.2492 -0.0142 -0.0136 -0.0158 154 ALA   B N   
6404 C  CA  . ALA   B 154 ? 0.1867 0.1588 0.2768 -0.0114 -0.0098 -0.0222 154 ALA   B CA  
6405 C  C   . ALA   B 154 ? 0.1978 0.1660 0.2957 0.0021  -0.0221 -0.0325 154 ALA   B C   
6406 O  O   . ALA   B 154 ? 0.2268 0.1630 0.3203 0.0038  -0.0241 -0.0128 154 ALA   B O   
6407 C  CB  . ALA   B 154 ? 0.1791 0.1785 0.2871 -0.0099 0.0066  -0.0286 154 ALA   B CB  
6413 N  N   . VAL   B 155 ? 0.1671 0.1604 0.3176 -0.0108 -0.0008 -0.0152 155 VAL   B N   
6414 C  CA  . VAL   B 155 ? 0.1664 0.1591 0.3445 -0.0114 -0.0009 -0.0059 155 VAL   B CA  
6415 C  C   . VAL   B 155 ? 0.1672 0.1610 0.3398 -0.0125 -0.0047 -0.0246 155 VAL   B C   
6416 O  O   . VAL   B 155 ? 0.1845 0.1868 0.3621 -0.0050 0.0016  -0.0465 155 VAL   B O   
6417 C  CB  . VAL   B 155 ? 0.1711 0.1721 0.3665 -0.0066 -0.0073 0.0128  155 VAL   B CB  
6418 C  CG1 . VAL   B 155 ? 0.1785 0.1698 0.3650 -0.0170 -0.0137 0.0164  155 VAL   B CG1 
6419 C  CG2 . VAL   B 155 ? 0.1657 0.1832 0.3853 -0.0109 -0.0174 0.0425  155 VAL   B CG2 
6429 N  N   . PHE   B 156 ? 0.1552 0.1700 0.3592 0.0083  0.0091  -0.0203 156 PHE   B N   
6430 C  CA  . PHE   B 156 ? 0.1662 0.1750 0.3773 0.0103  0.0079  -0.0210 156 PHE   B CA  
6431 C  C   . PHE   B 156 ? 0.1643 0.1871 0.4247 0.0128  -0.0042 -0.0235 156 PHE   B C   
6432 O  O   . PHE   B 156 ? 0.1912 0.2115 0.4485 0.0214  0.0066  -0.0404 156 PHE   B O   
6433 C  CB  . PHE   B 156 ? 0.1722 0.1783 0.3735 0.0099  -0.0000 -0.0146 156 PHE   B CB  
6434 C  CG  . PHE   B 156 ? 0.1713 0.1927 0.3776 0.0031  -0.0000 0.0028  156 PHE   B CG  
6435 C  CD1 . PHE   B 156 ? 0.1801 0.2150 0.3864 0.0085  0.0158  0.0258  156 PHE   B CD1 
6436 C  CD2 . PHE   B 156 ? 0.1831 0.2116 0.3762 0.0146  -0.0056 0.0125  156 PHE   B CD2 
6437 C  CE1 . PHE   B 156 ? 0.1792 0.2329 0.3881 0.0125  0.0120  0.0205  156 PHE   B CE1 
6438 C  CE2 . PHE   B 156 ? 0.1945 0.2369 0.3802 0.0206  -0.0076 0.0070  156 PHE   B CE2 
6439 C  CZ  . PHE   B 156 ? 0.1773 0.2361 0.3929 0.0237  -0.0074 0.0096  156 PHE   B CZ  
6449 N  N   . ASP   B 157 ? 0.1661 0.1787 0.4329 0.0172  -0.0194 -0.0174 157 ASP   B N   
6450 C  CA  . ASP   B 157 ? 0.1878 0.1935 0.4467 0.0207  -0.0129 -0.0301 157 ASP   B CA  
6451 C  C   . ASP   B 157 ? 0.1892 0.1913 0.4607 0.0083  -0.0167 -0.0476 157 ASP   B C   
6452 O  O   . ASP   B 157 ? 0.1669 0.1922 0.4739 0.0033  -0.0113 -0.0299 157 ASP   B O   
6453 C  CB  . ASP   B 157 ? 0.2205 0.2210 0.4465 0.0110  -0.0175 -0.0269 157 ASP   B CB  
6454 C  CG  . ASP   B 157 ? 0.2609 0.2382 0.4599 0.0102  -0.0122 -0.0271 157 ASP   B CG  
6455 O  OD1 . ASP   B 157 ? 0.2748 0.2252 0.4801 0.0252  -0.0078 -0.0113 157 ASP   B OD1 
6456 O  OD2 . ASP   B 157 ? 0.2965 0.2567 0.4836 0.0098  0.0022  -0.0282 157 ASP   B OD2 
6461 N  N   . LYS   B 158 ? 0.1940 0.2174 0.4664 0.0063  -0.0038 -0.0706 158 LYS   B N   
6462 C  CA  . LYS   B 158 ? 0.2042 0.2419 0.4695 -0.0014 0.0040  -0.0877 158 LYS   B CA  
6463 C  C   . LYS   B 158 ? 0.2121 0.2315 0.4938 -0.0063 -0.0055 -0.0758 158 LYS   B C   
6464 O  O   . LYS   B 158 ? 0.2157 0.2175 0.5083 -0.0116 0.0011  -0.0979 158 LYS   B O   
6465 C  CB  . LYS   B 158 ? 0.2338 0.2959 0.4613 0.0072  0.0090  -0.1103 158 LYS   B CB  
6466 C  CG  . LYS   B 158 ? 0.2803 0.3399 0.4659 0.0058  0.0073  -0.1297 158 LYS   B CG  
6467 C  CD  . LYS   B 158 ? 0.3016 0.3961 0.4729 0.0042  0.0118  -0.1319 158 LYS   B CD  
6468 C  CE  . LYS   B 158 ? 0.3205 0.4451 0.4917 0.0053  0.0098  -0.1230 158 LYS   B CE  
6469 N  NZ  . LYS   B 158 ? 0.3208 0.4643 0.4975 0.0048  0.0067  -0.1200 158 LYS   B NZ  
6483 N  N   . ASN   B 159 ? 0.2158 0.2093 0.5181 0.0054  -0.0029 -0.0613 159 ASN   B N   
6484 C  CA  . ASN   B 159 ? 0.2308 0.1908 0.5317 0.0232  -0.0217 -0.0531 159 ASN   B CA  
6485 C  C   . ASN   B 159 ? 0.2099 0.1687 0.5325 0.0115  -0.0404 -0.0356 159 ASN   B C   
6486 O  O   . ASN   B 159 ? 0.2061 0.1689 0.5693 -0.0060 -0.0473 -0.0141 159 ASN   B O   
6487 C  CB  . ASN   B 159 ? 0.2475 0.2029 0.5466 0.0369  -0.0442 -0.0525 159 ASN   B CB  
6488 C  CG  . ASN   B 159 ? 0.2848 0.2532 0.5639 0.0370  -0.0570 -0.0595 159 ASN   B CG  
6489 O  OD1 . ASN   B 159 ? 0.3002 0.2529 0.5536 0.0376  -0.0584 -0.0704 159 ASN   B OD1 
6490 N  ND2 . ASN   B 159 ? 0.3122 0.2678 0.5692 0.0387  -0.0618 -0.0538 159 ASN   B ND2 
6497 N  N   . LEU   B 160 ? 0.1868 0.1765 0.5146 0.0071  -0.0435 -0.0270 160 LEU   B N   
6498 C  CA  . LEU   B 160 ? 0.1811 0.1769 0.4868 0.0008  -0.0323 -0.0061 160 LEU   B CA  
6499 C  C   . LEU   B 160 ? 0.1810 0.1633 0.4896 -0.0050 -0.0188 -0.0128 160 LEU   B C   
6500 O  O   . LEU   B 160 ? 0.1653 0.1617 0.5026 -0.0053 -0.0153 -0.0101 160 LEU   B O   
6501 C  CB  . LEU   B 160 ? 0.1767 0.1951 0.4502 0.0016  -0.0379 0.0056  160 LEU   B CB  
6502 C  CG  . LEU   B 160 ? 0.1754 0.2058 0.4139 0.0034  -0.0357 0.0152  160 LEU   B CG  
6503 C  CD1 . LEU   B 160 ? 0.1935 0.2250 0.4127 -0.0006 -0.0187 0.0131  160 LEU   B CD1 
6504 C  CD2 . LEU   B 160 ? 0.1823 0.2117 0.4112 0.0191  -0.0277 0.0106  160 LEU   B CD2 
6516 N  N   . TYR   B 161 ? 0.1906 0.1680 0.4807 -0.0182 -0.0006 -0.0271 161 TYR   B N   
6517 C  CA  . TYR   B 161 ? 0.2049 0.1732 0.4487 -0.0334 0.0178  -0.0321 161 TYR   B CA  
6518 C  C   . TYR   B 161 ? 0.2152 0.1684 0.4478 -0.0302 0.0241  -0.0329 161 TYR   B C   
6519 O  O   . TYR   B 161 ? 0.2159 0.1757 0.4539 -0.0425 0.0271  -0.0358 161 TYR   B O   
6520 C  CB  . TYR   B 161 ? 0.2228 0.1911 0.4220 -0.0444 0.0233  -0.0422 161 TYR   B CB  
6521 C  CG  . TYR   B 161 ? 0.2518 0.1953 0.3959 -0.0530 0.0271  -0.0536 161 TYR   B CG  
6522 C  CD1 . TYR   B 161 ? 0.2624 0.1941 0.3929 -0.0614 0.0324  -0.0544 161 TYR   B CD1 
6523 C  CD2 . TYR   B 161 ? 0.2767 0.1966 0.3826 -0.0415 0.0163  -0.0476 161 TYR   B CD2 
6524 C  CE1 . TYR   B 161 ? 0.2812 0.2152 0.3763 -0.0664 0.0283  -0.0601 161 TYR   B CE1 
6525 C  CE2 . TYR   B 161 ? 0.2993 0.2198 0.3724 -0.0476 0.0270  -0.0465 161 TYR   B CE2 
6526 C  CZ  . TYR   B 161 ? 0.3038 0.2239 0.3745 -0.0608 0.0160  -0.0452 161 TYR   B CZ  
6527 O  OH  . TYR   B 161 ? 0.3336 0.2473 0.4056 -0.0634 0.0139  -0.0394 161 TYR   B OH  
6537 N  N   . ASP   B 162 ? 0.2223 0.1746 0.4502 -0.0356 0.0136  -0.0435 162 ASP   B N   
6538 C  CA  . ASP   B 162 ? 0.2253 0.1868 0.4471 -0.0322 0.0047  -0.0423 162 ASP   B CA  
6539 C  C   . ASP   B 162 ? 0.2160 0.1729 0.4454 -0.0259 0.0038  -0.0333 162 ASP   B C   
6540 O  O   . ASP   B 162 ? 0.2224 0.1785 0.4697 -0.0377 -0.0166 -0.0304 162 ASP   B O   
6541 C  CB  . ASP   B 162 ? 0.2367 0.2018 0.4561 -0.0254 0.0046  -0.0619 162 ASP   B CB  
6542 C  CG  . ASP   B 162 ? 0.2465 0.2244 0.4703 -0.0157 0.0016  -0.0768 162 ASP   B CG  
6543 O  OD1 . ASP   B 162 ? 0.2522 0.2474 0.4734 -0.0165 0.0069  -0.0596 162 ASP   B OD1 
6544 O  OD2 . ASP   B 162 ? 0.2538 0.2519 0.4911 0.0016  0.0009  -0.0815 162 ASP   B OD2 
6549 N  N   . LYS   B 163 ? 0.2143 0.1572 0.4407 -0.0263 -0.0011 -0.0110 163 LYS   B N   
6550 C  CA  . LYS   B 163 ? 0.2251 0.1733 0.4531 -0.0371 0.0092  -0.0005 163 LYS   B CA  
6551 C  C   . LYS   B 163 ? 0.1817 0.1692 0.4520 -0.0245 -0.0009 0.0129  163 LYS   B C   
6552 O  O   . LYS   B 163 ? 0.1766 0.1787 0.4764 -0.0243 -0.0023 0.0354  163 LYS   B O   
6553 C  CB  . LYS   B 163 ? 0.2838 0.2195 0.4825 -0.0307 -0.0009 0.0113  163 LYS   B CB  
6554 C  CG  . LYS   B 163 ? 0.3626 0.2886 0.5250 -0.0295 0.0105  0.0143  163 LYS   B CG  
6555 C  CD  . LYS   B 163 ? 0.4573 0.3619 0.5683 -0.0426 0.0138  0.0066  163 LYS   B CD  
6556 C  CE  . LYS   B 163 ? 0.5406 0.4365 0.6005 -0.0516 0.0165  0.0169  163 LYS   B CE  
6557 N  NZ  . LYS   B 163 ? 0.5761 0.4916 0.6177 -0.0573 0.0140  0.0215  163 LYS   B NZ  
6571 N  N   . LEU   B 164 ? 0.1687 0.1597 0.4264 -0.0178 -0.0049 0.0120  164 LEU   B N   
6572 C  CA  . LEU   B 164 ? 0.1767 0.1555 0.4150 -0.0204 -0.0105 0.0155  164 LEU   B CA  
6573 C  C   . LEU   B 164 ? 0.1934 0.1591 0.4220 -0.0298 -0.0247 0.0221  164 LEU   B C   
6574 O  O   . LEU   B 164 ? 0.1909 0.1831 0.4386 -0.0300 -0.0292 0.0225  164 LEU   B O   
6575 C  CB  . LEU   B 164 ? 0.1742 0.1551 0.3885 -0.0037 -0.0043 0.0107  164 LEU   B CB  
6576 C  CG  . LEU   B 164 ? 0.1815 0.1768 0.3869 -0.0153 -0.0003 0.0156  164 LEU   B CG  
6577 C  CD1 . LEU   B 164 ? 0.1890 0.1811 0.3742 -0.0206 -0.0178 0.0066  164 LEU   B CD1 
6578 C  CD2 . LEU   B 164 ? 0.1888 0.2065 0.3963 -0.0150 0.0194  0.0020  164 LEU   B CD2 
6590 N  N   . VAL   B 165 ? 0.2442 0.1667 0.4360 -0.0434 -0.0457 0.0191  165 VAL   B N   
6591 C  CA  . VAL   B 165 ? 0.2890 0.1826 0.4316 -0.0608 -0.0690 0.0154  165 VAL   B CA  
6592 C  C   . VAL   B 165 ? 0.3319 0.2010 0.4639 -0.0665 -0.0801 0.0247  165 VAL   B C   
6593 O  O   . VAL   B 165 ? 0.3622 0.2168 0.4840 -0.0689 -0.0775 0.0274  165 VAL   B O   
6594 C  CB  . VAL   B 165 ? 0.3166 0.1999 0.4163 -0.0338 -0.0458 -0.0128 165 VAL   B CB  
6595 C  CG1 . VAL   B 165 ? 0.3271 0.2109 0.4330 -0.0304 -0.0284 -0.0082 165 VAL   B CG1 
6596 C  CG2 . VAL   B 165 ? 0.3181 0.2039 0.3948 -0.0246 -0.0359 -0.0239 165 VAL   B CG2 
6606 N  N   . SER   B 166 ? 0.3383 0.1860 0.4973 -0.0689 -0.0942 -0.0003 166 SER   B N   
6607 C  CA  . SER   B 166 ? 0.3227 0.1903 0.5266 -0.0621 -0.0772 -0.0119 166 SER   B CA  
6608 C  C   . SER   B 166 ? 0.3008 0.2036 0.5142 -0.0647 -0.0724 0.0063  166 SER   B C   
6609 O  O   . SER   B 166 ? 0.2987 0.2123 0.5410 -0.0744 -0.0926 -0.0242 166 SER   B O   
6610 C  CB  . SER   B 166 ? 0.3180 0.1958 0.5565 -0.0430 -0.0688 -0.0089 166 SER   B CB  
6611 O  OG  . SER   B 166 ? 0.3044 0.1861 0.5737 -0.0332 -0.0716 -0.0016 166 SER   B OG  
6617 N  N   . SER   B 167 ? 0.2718 0.1867 0.4742 -0.0680 -0.0761 0.0311  167 SER   B N   
6618 C  CA  . SER   B 167 ? 0.2639 0.1940 0.4671 -0.0543 -0.0424 0.0396  167 SER   B CA  
6619 C  C   . SER   B 167 ? 0.2567 0.2081 0.4500 -0.0670 -0.0402 0.0605  167 SER   B C   
6620 O  O   . SER   B 167 ? 0.2544 0.2300 0.4542 -0.0692 -0.0388 0.0530  167 SER   B O   
6621 C  CB  . SER   B 167 ? 0.2452 0.2021 0.4877 -0.0479 -0.0154 0.0123  167 SER   B CB  
6622 O  OG  . SER   B 167 ? 0.2313 0.2054 0.5002 -0.0403 0.0120  0.0052  167 SER   B OG  
6628 N  N   . PHE   B 168 ? 0.2674 0.2123 0.4461 -0.0655 -0.0414 0.0559  168 PHE   B N   
6629 C  CA  . PHE   B 168 ? 0.2719 0.2138 0.4198 -0.0704 -0.0434 0.0423  168 PHE   B CA  
6630 C  C   . PHE   B 168 ? 0.2332 0.1986 0.3841 -0.0451 -0.0328 0.0257  168 PHE   B C   
6631 O  O   . PHE   B 168 ? 0.2659 0.1840 0.3921 -0.0164 -0.0447 0.0231  168 PHE   B O   
6632 C  CB  . PHE   B 168 ? 0.2984 0.2241 0.4156 -0.0883 -0.0544 0.0507  168 PHE   B CB  
6633 C  CG  . PHE   B 168 ? 0.3279 0.2097 0.3923 -0.0973 -0.0631 0.0276  168 PHE   B CG  
6634 C  CD1 . PHE   B 168 ? 0.3501 0.2155 0.3997 -0.0904 -0.0615 0.0319  168 PHE   B CD1 
6635 C  CD2 . PHE   B 168 ? 0.3255 0.1944 0.3782 -0.0965 -0.0652 0.0348  168 PHE   B CD2 
6636 C  CE1 . PHE   B 168 ? 0.3634 0.2161 0.3789 -0.0783 -0.0487 0.0460  168 PHE   B CE1 
6637 C  CE2 . PHE   B 168 ? 0.3521 0.2082 0.3814 -0.0725 -0.0605 0.0271  168 PHE   B CE2 
6638 C  CZ  . PHE   B 168 ? 0.3650 0.2017 0.3808 -0.0617 -0.0541 0.0585  168 PHE   B CZ  
6648 N  N   . LEU   B 169 ? 0.2261 0.1994 0.3704 -0.0079 -0.0149 0.0263  169 LEU   B N   
6649 C  CA  . LEU   B 169 ? 0.2467 0.2276 0.3784 -0.0023 -0.0071 -0.0135 169 LEU   B CA  
6650 C  C   . LEU   B 169 ? 0.2914 0.2469 0.4198 0.0087  -0.0119 -0.0512 169 LEU   B C   
6651 O  O   . LEU   B 169 ? 0.3163 0.2623 0.4610 0.0110  -0.0075 -0.0730 169 LEU   B O   
6652 C  CB  . LEU   B 169 ? 0.2483 0.2682 0.3674 -0.0080 -0.0096 0.0058  169 LEU   B CB  
6653 C  CG  . LEU   B 169 ? 0.2824 0.3145 0.3786 0.0063  0.0020  -0.0002 169 LEU   B CG  
6654 C  CD1 . LEU   B 169 ? 0.3041 0.3265 0.3679 0.0046  0.0004  0.0037  169 LEU   B CD1 
6655 C  CD2 . LEU   B 169 ? 0.2710 0.3266 0.3679 0.0211  0.0248  -0.0169 169 LEU   B CD2 
6656 O  OXT . LEU   B 169 ? 0.3194 0.2608 0.4263 0.0284  -0.0084 -0.0588 169 LEU   B OXT 
6668 N  N2  B A1BBY C .   ? 0.1956 0.2133 0.1944 -0.0297 -0.0057 0.0177  201 A1BBY A N2  
6669 C  C3  B A1BBY C .   ? 0.2371 0.2593 0.2352 -0.0149 -0.0197 -0.0033 201 A1BBY A C3  
6670 C  C6  B A1BBY C .   ? 0.1872 0.2130 0.1899 -0.0233 0.0037  0.0267  201 A1BBY A C6  
6671 C  C9  B A1BBY C .   ? 0.1638 0.2083 0.1964 -0.0181 0.0073  0.0341  201 A1BBY A C9  
6672 C  C1  B A1BBY C .   ? 0.2570 0.2689 0.2460 -0.0148 -0.0229 -0.0119 201 A1BBY A C1  
6673 C  C10 B A1BBY C .   ? 0.1534 0.2038 0.1972 -0.0182 0.0065  0.0458  201 A1BBY A C10 
6674 C  C2  B A1BBY C .   ? 0.2525 0.2676 0.2437 -0.0109 -0.0220 -0.0065 201 A1BBY A C2  
6675 C  C4  B A1BBY C .   ? 0.2395 0.2606 0.2379 -0.0131 -0.0292 -0.0122 201 A1BBY A C4  
6676 C  C5  B A1BBY C .   ? 0.1921 0.2210 0.1998 -0.0255 -0.0059 0.0161  201 A1BBY A C5  
6677 C  C7  B A1BBY C .   ? 0.1615 0.2039 0.1909 -0.0182 0.0099  0.0400  201 A1BBY A C7  
6678 C  C8  B A1BBY C .   ? 0.1702 0.2095 0.1935 -0.0202 0.0027  0.0295  201 A1BBY A C8  
6679 N  N1  B A1BBY C .   ? 0.2132 0.2428 0.2213 -0.0213 -0.0084 0.0101  201 A1BBY A N1  
6680 N  N3  B A1BBY C .   ? 0.1725 0.2069 0.1843 -0.0228 0.0171  0.0403  201 A1BBY A N3  
6681 N  N4  B A1BBY C .   ? 0.1563 0.2047 0.1988 -0.0128 0.0027  0.0412  201 A1BBY A N4  
6682 O  O1  B A1BBY C .   ? 0.2587 0.2722 0.2541 -0.0092 -0.0209 -0.0063 201 A1BBY A O1  
6697 O  O1  C A1BBZ D .   ? 0.2222 0.2738 0.2562 -0.0267 0.0058  -0.0151 202 A1BBZ A O1  
6698 C  C1  C A1BBZ D .   ? 0.2234 0.2739 0.2468 -0.0224 0.0116  -0.0100 202 A1BBZ A C1  
6699 C  C2  C A1BBZ D .   ? 0.2185 0.2720 0.2482 -0.0248 0.0122  -0.0036 202 A1BBZ A C2  
6700 C  C3  C A1BBZ D .   ? 0.2077 0.2674 0.2341 -0.0290 0.0234  0.0196  202 A1BBZ A C3  
6701 C  C4  C A1BBZ D .   ? 0.2122 0.2623 0.2255 -0.0310 0.0203  0.0306  202 A1BBZ A C4  
6702 C  C5  C A1BBZ D .   ? 0.1829 0.2495 0.2025 -0.0190 0.0115  0.0245  202 A1BBZ A C5  
6703 C  C6  C A1BBZ D .   ? 0.1832 0.2457 0.1979 -0.0123 0.0117  0.0235  202 A1BBZ A C6  
6704 C  C7  C A1BBZ D .   ? 0.1594 0.2364 0.1951 -0.0019 0.0155  0.0366  202 A1BBZ A C7  
6705 C  C8  C A1BBZ D .   ? 0.1663 0.2393 0.1953 -0.0068 0.0121  0.0337  202 A1BBZ A C8  
6706 C  C10 C A1BBZ D .   ? 0.1519 0.2354 0.1991 0.0001  0.0095  0.0414  202 A1BBZ A C10 
6707 C  C9  C A1BBZ D .   ? 0.1615 0.2381 0.1990 -0.0016 0.0125  0.0347  202 A1BBZ A C9  
6708 N  N1  C A1BBZ D .   ? 0.1944 0.2651 0.2271 -0.0255 0.0210  0.0233  202 A1BBZ A N1  
6709 N  N2  C A1BBZ D .   ? 0.1898 0.2451 0.1962 -0.0209 0.0066  0.0222  202 A1BBZ A N2  
6710 N  N3  C A1BBZ D .   ? 0.1719 0.2411 0.1940 -0.0062 0.0208  0.0334  202 A1BBZ A N3  
6711 N  N4  C A1BBZ D .   ? 0.1533 0.2363 0.2002 0.0048  0.0075  0.0368  202 A1BBZ A N4  
6726 CL CL  B CL    E .   ? 0.1845 0.1776 0.2665 -0.0155 0.0244  0.0121  203 CL    A CL  
6727 O  O   . HOH   F .   ? 0.7786 0.5845 0.4477 -0.1614 -0.0288 0.1991  301 HOH   A O   
6728 O  O   . HOH   F .   ? 0.4078 0.2734 0.4311 -0.0511 -0.0721 0.0161  302 HOH   A O   
6729 O  O   . HOH   F .   ? 0.2776 0.2796 0.3738 -0.0144 0.0458  0.0860  303 HOH   A O   
6730 O  O   . HOH   F .   ? 0.4528 0.7153 0.5414 -0.1267 0.1127  0.0054  304 HOH   A O   
6731 O  O   . HOH   F .   ? 0.5706 0.5987 0.5233 0.0851  -0.0625 0.0464  305 HOH   A O   
6732 O  O   . HOH   F .   ? 0.9352 0.3823 0.5766 -0.0325 -0.1251 0.1094  306 HOH   A O   
6733 O  O   . HOH   F .   ? 0.1767 0.5627 0.3398 -0.0081 0.0296  0.1232  307 HOH   A O   
6734 O  O   . HOH   F .   ? 0.5824 0.4534 0.3255 0.1057  -0.0810 0.0456  308 HOH   A O   
6735 O  O   . HOH   F .   ? 0.3143 0.6467 0.5476 0.1155  0.0700  0.1474  309 HOH   A O   
6736 O  O   . HOH   F .   ? 0.2247 0.2016 0.3116 0.0270  -0.0516 -0.0079 310 HOH   A O   
6737 O  O   . HOH   F .   ? 0.3472 0.4072 0.2569 -0.0357 0.0503  0.0748  311 HOH   A O   
6738 O  O   . HOH   F .   ? 0.5037 0.6517 0.5361 -0.1245 -0.1040 -0.0657 312 HOH   A O   
6739 O  O   . HOH   F .   ? 0.4443 0.2930 0.5287 -0.0924 0.0697  0.0480  313 HOH   A O   
6740 O  O   . HOH   F .   ? 0.5831 0.3693 0.3890 -0.1636 -0.1413 0.0697  314 HOH   A O   
6741 O  O   . HOH   F .   ? 0.8425 0.3014 0.3802 -0.0050 0.1395  0.0760  315 HOH   A O   
6742 O  O   . HOH   F .   ? 0.2853 0.6258 0.4029 0.0464  -0.0247 0.1125  316 HOH   A O   
6743 O  O   . HOH   F .   ? 0.6782 0.4545 0.6333 -0.0896 0.1792  0.1837  317 HOH   A O   
6744 O  O   . HOH   F .   ? 0.2197 0.5318 0.4122 0.1279  0.0169  0.0874  318 HOH   A O   
6745 O  O   . HOH   F .   ? 0.2162 0.2102 0.4438 -0.0583 0.0177  -0.0104 319 HOH   A O   
6746 O  O   . HOH   F .   ? 0.2193 0.3917 0.5312 -0.0493 0.0473  -0.1268 320 HOH   A O   
6747 O  O   . HOH   F .   ? 0.5590 0.4756 0.6042 -0.1673 0.0099  0.1234  321 HOH   A O   
6748 O  O   . HOH   F .   ? 0.4671 0.5632 0.6537 0.1664  0.0878  -0.0050 322 HOH   A O   
6749 O  O   . HOH   F .   ? 0.3711 0.5004 0.3151 -0.0689 0.0063  0.0533  323 HOH   A O   
6750 O  O   . HOH   F .   ? 0.4058 0.7509 0.4953 -0.1081 -0.0304 0.2008  324 HOH   A O   
6751 O  O   . HOH   F .   ? 0.1897 0.1894 0.3331 0.0079  -0.0362 0.0313  325 HOH   A O   
6752 O  O   . HOH   F .   ? 0.1928 0.1984 0.3588 -0.0296 0.0160  0.0577  326 HOH   A O   
6753 O  O   . HOH   F .   ? 0.4574 0.3231 0.5995 -0.0019 0.1623  -0.0036 327 HOH   A O   
6754 O  O   . HOH   F .   ? 0.7729 0.8558 0.5121 0.0835  -0.1100 -0.0540 328 HOH   A O   
6755 O  O   . HOH   F .   ? 0.5140 0.2197 0.6467 0.0765  0.0246  0.0244  329 HOH   A O   
6756 O  O   . HOH   F .   ? 0.2963 0.4780 0.4840 0.0542  0.0459  0.0953  330 HOH   A O   
6757 O  O   . HOH   F .   ? 0.2736 0.2294 0.3344 -0.0373 0.0487  -0.0016 331 HOH   A O   
6758 O  O   . HOH   F .   ? 0.2410 0.3405 0.4151 -0.0393 -0.0657 0.1070  332 HOH   A O   
6759 O  O   A HOH   F .   ? 0.4598 0.2314 0.2806 0.0010  0.0450  0.0298  333 HOH   A O   
6760 O  O   . HOH   F .   ? 0.2486 0.4968 0.6222 -0.0058 0.0807  0.2588  334 HOH   A O   
6761 O  O   . HOH   F .   ? 0.6516 0.6001 0.4268 -0.0416 0.0098  0.1054  335 HOH   A O   
6762 O  O   . HOH   F .   ? 0.2441 0.2471 0.4321 0.0290  0.0489  0.0374  336 HOH   A O   
6763 O  O   . HOH   F .   ? 0.1702 0.1666 0.3711 -0.0269 -0.0082 0.0160  337 HOH   A O   
6764 O  O   . HOH   F .   ? 0.2931 0.2540 0.4837 -0.0196 -0.0844 0.0874  338 HOH   A O   
6765 O  O   . HOH   F .   ? 0.5454 0.2322 0.4720 0.0573  -0.1277 0.0431  339 HOH   A O   
6766 O  O   . HOH   F .   ? 0.6748 0.7472 0.6684 -0.0801 0.1008  0.0441  340 HOH   A O   
6767 O  O   . HOH   F .   ? 0.6844 0.4052 0.6274 -0.1833 -0.0381 0.2300  341 HOH   A O   
6768 O  O   . HOH   F .   ? 0.2600 0.4424 0.3837 0.1031  -0.0607 -0.0206 342 HOH   A O   
6769 O  O   A HOH   F .   ? 0.1635 0.3187 0.2678 0.0626  0.0278  0.0734  343 HOH   A O   
6770 O  O   . HOH   F .   ? 0.3472 0.3308 0.4024 -0.0918 -0.0161 -0.0167 344 HOH   A O   
6771 O  O   . HOH   F .   ? 0.3631 0.4218 0.4852 -0.0568 0.1477  0.0042  345 HOH   A O   
6772 O  O   . HOH   F .   ? 0.5791 0.7030 0.4568 -0.1481 0.2039  0.0508  346 HOH   A O   
6773 O  O   . HOH   F .   ? 0.1722 0.2234 0.2909 -0.0050 -0.0190 0.0566  347 HOH   A O   
6774 O  O   . HOH   F .   ? 0.1956 0.3124 0.3961 -0.0177 0.0675  0.0915  348 HOH   A O   
6775 O  O   A HOH   F .   ? 0.2383 0.2659 0.2883 -0.0823 -0.0049 0.0593  349 HOH   A O   
6776 O  O   . HOH   F .   ? 0.6971 0.4328 0.4273 -0.0396 0.0205  0.1686  350 HOH   A O   
6777 O  O   . HOH   F .   ? 0.4192 0.7293 0.4604 -0.0561 -0.1337 0.0886  351 HOH   A O   
6778 O  O   . HOH   F .   ? 0.2915 0.3310 0.5538 -0.0699 -0.0727 -0.0404 352 HOH   A O   
6779 O  O   . HOH   F .   ? 0.3708 0.4564 0.4942 0.2020  0.0722  0.0715  353 HOH   A O   
6780 O  O   . HOH   F .   ? 0.2903 0.4349 0.4314 -0.0932 -0.0511 -0.0123 354 HOH   A O   
6781 O  O   . HOH   F .   ? 0.1670 0.1961 0.3984 0.0106  -0.0436 -0.0282 355 HOH   A O   
6782 O  O   . HOH   F .   ? 0.1992 0.2150 0.5105 0.0197  0.0863  0.0005  356 HOH   A O   
6783 O  O   . HOH   F .   ? 0.2605 0.4864 0.4052 -0.0558 0.0162  0.0443  357 HOH   A O   
6784 O  O   . HOH   F .   ? 0.2260 0.2822 0.4367 0.0330  0.0715  -0.0563 358 HOH   A O   
6785 O  O   . HOH   F .   ? 0.1662 0.2222 0.3584 0.0036  -0.0028 0.0279  359 HOH   A O   
6786 O  O   A HOH   F .   ? 0.2592 0.4938 0.2761 0.1220  -0.0036 -0.0097 360 HOH   A O   
6787 O  O   . HOH   F .   ? 0.4019 0.6671 0.3834 0.1784  0.0580  0.0066  361 HOH   A O   
6788 O  O   . HOH   F .   ? 0.2806 0.3733 0.4071 -0.0175 0.0603  -0.0047 362 HOH   A O   
6789 O  O   . HOH   F .   ? 0.1848 0.2112 0.2829 0.0069  -0.0298 -0.0041 363 HOH   A O   
6790 O  O   B HOH   F .   ? 0.2289 0.3430 0.2561 0.0514  -0.0750 -0.0144 364 HOH   A O   
6791 O  O   . HOH   F .   ? 0.1623 0.1747 0.2578 -0.0090 -0.0078 0.0079  365 HOH   A O   
6792 O  O   . HOH   F .   ? 0.1491 0.1499 0.2617 -0.0063 0.0177  0.0170  366 HOH   A O   
6793 O  O   . HOH   F .   ? 0.1945 0.1925 0.3055 0.0034  0.0078  0.0279  367 HOH   A O   
6794 O  O   . HOH   F .   ? 0.3923 0.2449 0.3805 0.1177  0.0754  0.0353  368 HOH   A O   
6795 O  O   . HOH   F .   ? 0.3316 0.3192 0.3887 0.0197  -0.0290 0.1049  369 HOH   A O   
6796 O  O   . HOH   F .   ? 0.1980 0.2073 0.3697 -0.0291 0.0182  0.0452  370 HOH   A O   
6797 O  O   . HOH   F .   ? 0.1773 0.1421 0.3857 -0.0149 0.0289  0.0004  371 HOH   A O   
6798 O  O   . HOH   F .   ? 0.4271 0.2552 0.5453 -0.1167 0.0812  0.0646  372 HOH   A O   
6799 O  O   . HOH   F .   ? 0.2413 0.2027 0.3795 -0.0111 -0.0850 -0.0107 373 HOH   A O   
6800 O  O   . HOH   F .   ? 0.2129 0.2691 0.3232 -0.0342 -0.0218 0.0646  374 HOH   A O   
6801 O  O   . HOH   F .   ? 0.3280 0.4208 0.3075 -0.1536 0.0083  -0.0721 375 HOH   A O   
6802 O  O   . HOH   F .   ? 0.2324 0.2217 0.4539 0.0105  -0.0709 0.0357  376 HOH   A O   
6803 O  O   . HOH   F .   ? 0.2763 0.5311 0.4043 0.0755  0.0752  0.2010  377 HOH   A O   
6804 O  O   . HOH   F .   ? 0.4532 0.2780 0.3999 -0.1556 0.1343  -0.0516 378 HOH   A O   
6805 O  O   . HOH   F .   ? 0.4020 0.6676 0.6294 -0.1315 0.0357  0.0489  379 HOH   A O   
6806 O  O   . HOH   F .   ? 0.7035 0.5659 0.5391 0.0888  0.1924  -0.0934 380 HOH   A O   
6807 O  O   . HOH   F .   ? 0.2636 0.4575 0.5731 0.0250  -0.0033 0.0969  381 HOH   A O   
6808 O  O   . HOH   F .   ? 0.4587 0.5253 0.6196 -0.1278 0.0024  0.1507  382 HOH   A O   
6809 O  O   . HOH   F .   ? 0.1873 0.2931 0.3066 -0.0254 0.0019  0.1000  383 HOH   A O   
6810 O  O   . HOH   F .   ? 0.2817 0.4165 0.3706 -0.0166 0.0659  -0.0372 384 HOH   A O   
6811 O  O   . HOH   F .   ? 0.1504 0.1583 0.3098 0.0002  -0.0108 0.0048  385 HOH   A O   
6812 O  O   . HOH   F .   ? 0.3224 0.3005 0.2831 0.0030  0.0501  0.0053  386 HOH   A O   
6813 O  O   . HOH   F .   ? 0.2337 0.3075 0.3664 0.0325  0.0616  0.1025  387 HOH   A O   
6814 O  O   . HOH   F .   ? 0.4810 0.2816 0.5760 0.0798  -0.0164 -0.0534 388 HOH   A O   
6815 O  O   . HOH   F .   ? 0.2809 0.2430 0.2802 -0.0806 0.0118  0.0485  389 HOH   A O   
6816 O  O   . HOH   F .   ? 0.1511 0.1908 0.3616 -0.0119 0.0201  0.0284  390 HOH   A O   
6817 O  O   . HOH   F .   ? 0.3176 0.2568 0.5179 -0.0756 -0.0166 -0.0080 391 HOH   A O   
6818 O  O   . HOH   F .   ? 0.2969 0.3181 0.4257 -0.0900 0.0693  0.0239  392 HOH   A O   
6819 O  O   . HOH   F .   ? 0.3727 0.3786 0.5519 0.1071  0.1201  0.0830  393 HOH   A O   
6820 O  O   . HOH   F .   ? 0.2087 0.2448 0.3774 -0.0001 -0.0054 0.0910  394 HOH   A O   
6821 O  O   . HOH   F .   ? 0.1754 0.1606 0.2741 -0.0230 0.0125  0.0097  395 HOH   A O   
6822 O  O   . HOH   F .   ? 0.3238 0.4406 0.5111 -0.0367 0.1184  0.0290  396 HOH   A O   
6823 O  O   . HOH   F .   ? 0.1913 0.2057 0.4899 0.0226  0.0842  0.0887  397 HOH   A O   
6824 O  O   . HOH   F .   ? 0.3919 0.3813 0.3072 -0.0913 -0.1068 0.0474  398 HOH   A O   
6825 O  O   . HOH   F .   ? 0.2714 0.2388 0.3979 0.0010  -0.0173 0.0547  399 HOH   A O   
6826 O  O   . HOH   F .   ? 0.3494 0.3203 0.3743 -0.0993 -0.1126 0.0603  400 HOH   A O   
6827 O  O   . HOH   F .   ? 0.2312 0.2040 0.4266 0.0073  -0.0096 0.0261  401 HOH   A O   
6828 O  O   . HOH   F .   ? 0.5516 0.6134 0.2520 -0.0315 0.1221  0.0515  402 HOH   A O   
6829 O  O   . HOH   F .   ? 0.1647 0.1861 0.4900 0.0004  0.0079  0.0292  403 HOH   A O   
6830 O  O   B HOH   F .   ? 0.1356 0.1314 0.3000 0.0386  -0.0168 -0.0021 404 HOH   A O   
6831 O  O   . HOH   F .   ? 0.2654 0.6818 0.2496 -0.0266 0.0308  -0.0203 405 HOH   A O   
6832 O  O   . HOH   F .   ? 0.4798 0.2815 0.3959 -0.0649 0.0748  0.0385  406 HOH   A O   
6833 O  O   . HOH   F .   ? 0.2923 0.2260 0.3621 -0.0190 0.0216  0.0593  407 HOH   A O   
6834 O  O   . HOH   F .   ? 0.2704 0.4056 0.7704 -0.0243 0.0476  -0.0207 408 HOH   A O   
6835 O  O   . HOH   F .   ? 0.3026 0.3859 0.4075 0.0822  -0.0383 -0.0979 409 HOH   A O   
6836 O  O   . HOH   F .   ? 0.2813 0.2306 0.3265 -0.0606 -0.0019 0.0771  410 HOH   A O   
6837 O  O   . HOH   F .   ? 0.2229 0.3033 0.5087 -0.0020 -0.0383 -0.0344 411 HOH   A O   
6838 O  O   . HOH   F .   ? 0.2362 0.3244 0.3491 -0.0172 -0.0409 0.0808  412 HOH   A O   
6839 O  O   . HOH   F .   ? 0.2212 0.2131 0.4369 0.0250  -0.0541 0.0179  413 HOH   A O   
6840 O  O   A HOH   F .   ? 0.1703 0.2163 0.2321 -0.0382 -0.0049 0.0025  414 HOH   A O   
6841 O  O   . HOH   F .   ? 0.3252 0.7349 0.4841 -0.0515 -0.0546 0.1826  415 HOH   A O   
6842 O  O   . HOH   F .   ? 0.3463 0.1549 0.3038 -0.0185 -0.0552 0.0150  416 HOH   A O   
6843 O  O   A HOH   F .   ? 0.3932 0.2493 0.4631 -0.0469 0.1043  0.0060  417 HOH   A O   
6844 O  O   . HOH   F .   ? 0.3764 0.6154 0.6694 -0.1716 0.0301  -0.1225 418 HOH   A O   
6845 O  O   . HOH   F .   ? 0.3717 0.3938 0.6048 0.1356  0.1333  0.0003  419 HOH   A O   
6846 O  O   . HOH   F .   ? 0.2228 0.1980 0.2665 -0.0040 0.0144  0.0399  420 HOH   A O   
6847 O  O   . HOH   F .   ? 0.2569 0.2928 0.4221 0.0055  -0.0115 -0.0686 421 HOH   A O   
6848 O  O   . HOH   F .   ? 0.4576 0.6325 0.3642 -0.0290 0.0286  0.1345  422 HOH   A O   
6849 O  O   . HOH   F .   ? 0.4361 0.2584 0.6109 -0.1084 -0.2377 0.1252  423 HOH   A O   
6850 O  O   . HOH   F .   ? 0.4321 0.3191 0.3355 -0.0367 -0.0193 0.0307  424 HOH   A O   
6851 O  O   . HOH   F .   ? 0.5593 0.5487 0.5616 -0.0462 -0.0644 0.0391  425 HOH   A O   
6852 O  O   A HOH   F .   ? 0.4159 0.5208 0.3721 0.1210  -0.0385 -0.0571 426 HOH   A O   
6853 O  O   . HOH   F .   ? 0.2030 0.3402 0.5080 -0.0204 -0.0165 0.0375  427 HOH   A O   
6854 O  O   . HOH   F .   ? 0.4825 0.5575 0.5584 -0.1919 -0.0520 -0.0960 428 HOH   A O   
6855 O  O   . HOH   F .   ? 0.2456 0.3648 0.3592 0.1189  0.0000  0.0360  429 HOH   A O   
6856 O  O   . HOH   F .   ? 0.1818 0.2439 0.3940 -0.0221 -0.0058 0.0752  430 HOH   A O   
6857 O  O   . HOH   F .   ? 0.6480 0.7896 0.5531 0.0444  0.2997  -0.0622 431 HOH   A O   
6858 O  O   . HOH   F .   ? 0.5600 0.5178 0.4013 -0.0166 -0.1462 0.0233  432 HOH   A O   
6859 O  O   . HOH   F .   ? 0.2030 0.2340 0.5716 -0.0279 -0.0661 0.0589  433 HOH   A O   
6860 O  O   B HOH   F .   ? 0.2304 0.3358 0.2261 0.1527  0.0460  0.0838  434 HOH   A O   
6861 O  O   A HOH   F .   ? 0.2211 0.1312 0.2270 -0.0135 0.0249  0.0062  435 HOH   A O   
6862 O  O   . HOH   F .   ? 0.6540 0.4176 0.5247 0.1206  -0.0735 0.1186  436 HOH   A O   
6863 O  O   . HOH   F .   ? 0.4556 0.4619 0.7526 0.0692  -0.1306 -0.1210 437 HOH   A O   
6864 O  O   . HOH   F .   ? 0.5218 0.4214 0.7654 0.0588  -0.1398 0.0743  438 HOH   A O   
6865 O  O   . HOH   F .   ? 0.2931 0.1965 0.3998 0.0252  -0.0087 0.0213  439 HOH   A O   
6866 O  O   . HOH   F .   ? 0.3899 0.3351 0.2856 -0.1202 0.0210  0.0255  440 HOH   A O   
6867 O  O   . HOH   F .   ? 0.2813 0.2727 0.4536 0.0516  0.0141  -0.0106 441 HOH   A O   
6868 O  O   . HOH   F .   ? 0.5144 0.6605 0.5298 0.0359  -0.0914 0.0108  442 HOH   A O   
6869 O  O   . HOH   F .   ? 0.4450 0.4113 0.4718 0.2520  -0.0525 -0.0125 443 HOH   A O   
6870 O  O   . HOH   F .   ? 0.3785 0.4942 0.4721 -0.1248 -0.0538 -0.1187 444 HOH   A O   
6871 O  O   A HOH   F .   ? 0.1991 0.1705 0.2612 0.0133  -0.0009 -0.0095 445 HOH   A O   
6872 O  O   . HOH   F .   ? 0.2254 0.2756 0.3327 0.0058  -0.0037 -0.0289 446 HOH   A O   
6873 O  O   . HOH   F .   ? 0.6916 0.9889 0.4948 0.1209  -0.1403 0.2623  447 HOH   A O   
6874 O  O   . HOH   F .   ? 0.2668 0.2184 0.4122 0.0002  0.0214  0.0165  448 HOH   A O   
6875 O  O   . HOH   F .   ? 0.6718 0.6202 0.4691 -0.0309 0.0339  0.2487  449 HOH   A O   
6876 O  O   A HOH   F .   ? 0.5191 0.5386 0.3528 -0.1208 -0.1387 -0.0134 450 HOH   A O   
6877 O  O   A HOH   F .   ? 0.5189 0.2244 0.3856 -0.0414 0.0220  0.0980  451 HOH   A O   
6878 O  O   . HOH   F .   ? 0.4739 0.4890 0.4153 0.0152  -0.0163 0.1166  452 HOH   A O   
6879 O  O   B HOH   F .   ? 0.1906 0.1998 0.2238 -0.0561 -0.0325 0.0602  453 HOH   A O   
6880 O  O   . HOH   F .   ? 0.3712 0.3884 0.4666 0.0239  0.0900  0.0328  454 HOH   A O   
6881 O  O   . HOH   F .   ? 0.4304 0.4496 0.4490 0.1096  0.1119  0.0799  455 HOH   A O   
6882 O  O   . HOH   F .   ? 0.8322 0.6218 0.5671 -0.0806 0.1760  0.1163  456 HOH   A O   
6883 O  O   . HOH   F .   ? 0.3111 0.3436 0.3843 0.1077  -0.0128 0.0590  457 HOH   A O   
6884 O  O   . HOH   F .   ? 0.3215 0.3053 0.3886 -0.0751 0.0206  -0.0609 458 HOH   A O   
6885 O  O   . HOH   F .   ? 0.7995 0.7409 0.5294 -0.0477 -0.0115 -0.0667 459 HOH   A O   
6886 O  O   . HOH   F .   ? 0.2966 0.4052 0.6410 0.0754  -0.0031 -0.1405 460 HOH   A O   
6887 O  O   . HOH   F .   ? 0.3455 0.5853 0.4684 0.0703  -0.0284 0.1354  461 HOH   A O   
6888 O  O   . HOH   F .   ? 0.3344 0.5727 0.5826 -0.1902 0.0415  -0.1757 462 HOH   A O   
6889 O  O   . HOH   F .   ? 0.2888 0.3441 0.6407 0.0325  -0.1164 0.0048  463 HOH   A O   
6890 O  O   . HOH   F .   ? 0.3473 0.4354 0.4535 -0.0812 -0.0328 -0.0408 464 HOH   A O   
6891 O  O   . HOH   F .   ? 0.2607 0.2836 0.3693 -0.0798 -0.0006 -0.0012 465 HOH   A O   
6892 O  O   . HOH   F .   ? 0.5897 0.5199 0.4991 -0.0158 0.0406  0.0636  466 HOH   A O   
6893 O  O   . HOH   F .   ? 0.2798 0.1978 0.3532 0.0226  -0.0952 -0.0205 467 HOH   A O   
6894 O  O   . HOH   F .   ? 0.7864 0.3763 0.7760 -0.0145 0.0109  0.2567  468 HOH   A O   
6895 O  O   . HOH   F .   ? 0.4576 0.7651 0.4608 -0.0513 -0.0459 0.2759  469 HOH   A O   
6896 O  O   . HOH   F .   ? 0.3835 0.5986 0.4132 0.0637  -0.0620 -0.0387 470 HOH   A O   
6897 O  O   . HOH   F .   ? 0.8038 0.6205 0.5670 -0.0616 0.0961  0.2472  471 HOH   A O   
6898 O  O   . HOH   F .   ? 0.4759 0.5364 0.5190 0.0575  0.0316  -0.0342 472 HOH   A O   
6899 O  O   . HOH   F .   ? 0.3450 0.2546 0.4237 -0.0110 0.0812  0.0088  473 HOH   A O   
6900 O  O   . HOH   F .   ? 0.2760 0.2651 0.3291 0.0555  -0.0188 -0.0184 474 HOH   A O   
6901 O  O   . HOH   F .   ? 0.6658 0.4718 0.5051 -0.1123 0.0787  -0.0516 475 HOH   A O   
6902 O  O   . HOH   F .   ? 0.6232 0.7085 0.7198 -0.1951 -0.1495 0.0623  476 HOH   A O   
6903 O  O   . HOH   F .   ? 0.4869 0.5451 0.5100 -0.2379 -0.0471 -0.0123 477 HOH   A O   
6904 O  O   . HOH   F .   ? 0.7284 0.7099 0.6931 0.1779  0.3021  -0.0881 478 HOH   A O   
6905 O  O   . HOH   F .   ? 0.4345 0.5032 0.3421 -0.0698 -0.0523 0.0399  479 HOH   A O   
6906 O  O   . HOH   F .   ? 0.5475 0.3614 0.4751 0.0719  -0.0061 -0.1016 480 HOH   A O   
6907 O  O   . HOH   F .   ? 0.3102 0.4241 0.5018 0.0002  0.0906  0.1006  481 HOH   A O   
6908 O  O   . HOH   F .   ? 0.8804 0.3934 0.4054 -0.0480 -0.1434 0.0862  482 HOH   A O   
6909 O  O   . HOH   F .   ? 0.4349 0.3869 0.3217 -0.0248 -0.0160 -0.0274 483 HOH   A O   
6910 O  O   . HOH   F .   ? 0.5015 0.3158 0.3625 -0.0836 -0.1296 0.0584  484 HOH   A O   
6911 O  O   . HOH   F .   ? 0.5683 0.7021 0.4390 -0.0471 0.1463  0.1677  485 HOH   A O   
6912 O  O   . HOH   F .   ? 0.6962 0.6196 0.4651 -0.0996 -0.0861 -0.0468 486 HOH   A O   
6913 O  O   . HOH   F .   ? 0.2725 0.2509 0.7175 -0.0057 -0.1087 0.0485  487 HOH   A O   
6914 O  O   . HOH   F .   ? 0.3028 0.5919 0.3807 0.1299  0.1133  0.2502  488 HOH   A O   
6915 O  O   . HOH   F .   ? 0.5241 0.4282 0.3383 -0.1368 0.1191  -0.0784 489 HOH   A O   
6916 O  O   . HOH   F .   ? 0.7388 0.7569 0.5613 0.1460  -0.1726 0.0343  490 HOH   A O   
6917 O  O   . HOH   F .   ? 0.5685 0.6136 0.5449 0.0837  -0.1082 0.0792  491 HOH   A O   
6918 O  O   . HOH   F .   ? 0.4450 0.3294 0.5047 -0.1094 0.0987  0.0563  492 HOH   A O   
6919 O  O   . HOH   F .   ? 0.4782 0.3616 0.5250 -0.0320 0.2540  0.0007  493 HOH   A O   
6920 O  O   . HOH   F .   ? 0.2768 0.2897 0.5646 0.0036  0.0978  -0.0213 494 HOH   A O   
6921 O  O   . HOH   F .   ? 0.3645 0.2302 0.6956 0.0119  0.0482  0.0719  495 HOH   A O   
6922 O  O   . HOH   F .   ? 0.7578 0.4637 0.5151 -0.1275 0.1669  -0.0453 496 HOH   A O   
6923 O  O   . HOH   F .   ? 0.3958 0.8652 0.6548 -0.1076 -0.0422 0.2591  497 HOH   A O   
6924 O  O   B HOH   F .   ? 0.2309 0.5887 0.3902 0.0281  0.0629  -0.0316 498 HOH   A O   
6925 O  O   . HOH   F .   ? 0.2561 0.3262 0.4085 0.0132  -0.0520 0.0869  499 HOH   A O   
6926 O  O   . HOH   F .   ? 0.2865 0.4374 0.5325 0.0050  -0.0731 0.0721  500 HOH   A O   
6927 O  O   . HOH   F .   ? 0.5370 0.7991 0.5247 0.0341  -0.0576 0.0370  501 HOH   A O   
6928 O  O   . HOH   F .   ? 0.6538 0.2855 0.4084 -0.0682 0.0996  0.0211  502 HOH   A O   
6929 O  O   . HOH   F .   ? 0.4721 0.3805 0.6313 -0.1745 -0.1279 0.2157  503 HOH   A O   
6930 O  O   . HOH   F .   ? 0.3028 0.4828 0.3542 -0.0383 -0.0349 -0.0342 504 HOH   A O   
6931 O  O   . HOH   F .   ? 0.6033 0.8077 0.4829 0.3568  -0.0010 0.1697  505 HOH   A O   
6932 O  O   . HOH   F .   ? 0.3114 0.2518 0.4565 -0.0072 0.0115  0.0538  506 HOH   A O   
6933 O  O   . HOH   F .   ? 0.5961 0.6014 0.4610 -0.0427 -0.0823 -0.1277 507 HOH   A O   
6934 O  O   A HOH   F .   ? 0.3792 0.7717 0.2542 0.1211  0.0320  0.0500  508 HOH   A O   
6935 O  O   . HOH   F .   ? 0.3133 0.8237 0.3765 0.0968  0.0092  -0.0138 509 HOH   A O   
6936 O  O   . HOH   F .   ? 0.5864 0.4324 0.5061 0.2006  0.0150  0.0562  510 HOH   A O   
6937 O  O   . HOH   F .   ? 0.4282 0.6049 0.5507 -0.0310 -0.1346 0.0308  511 HOH   A O   
6938 O  O   . HOH   F .   ? 0.2715 0.4191 0.5774 0.0102  -0.0537 0.2359  512 HOH   A O   
6939 O  O   . HOH   G .   ? 0.2462 0.2670 0.4322 0.0214  0.0852  0.0399  201 HOH   B O   
6940 O  O   . HOH   G .   ? 0.5301 0.4013 0.4536 0.0119  -0.0243 -0.0970 202 HOH   B O   
6941 O  O   . HOH   G .   ? 0.3893 0.2696 0.6209 -0.0089 0.0802  -0.0230 203 HOH   B O   
6942 O  O   . HOH   G .   ? 0.3278 0.2180 0.6651 -0.0233 0.1964  0.0374  204 HOH   B O   
6943 O  O   . HOH   G .   ? 0.3817 0.4548 0.5266 0.0856  -0.0027 0.0595  205 HOH   B O   
6944 O  O   . HOH   G .   ? 0.3884 0.3060 0.5776 -0.0489 0.2085  0.0251  206 HOH   B O   
6945 O  O   . HOH   G .   ? 0.3527 0.7447 0.4683 0.1588  0.0093  0.2518  207 HOH   B O   
6946 O  O   . HOH   G .   ? 0.2948 0.6499 0.3520 0.0049  -0.0082 -0.1398 208 HOH   B O   
6947 O  O   . HOH   G .   ? 0.3159 0.5731 0.4879 0.0085  0.1065  -0.1935 209 HOH   B O   
6948 O  O   . HOH   G .   ? 0.4589 0.6959 0.4652 0.3085  -0.0942 -0.0287 210 HOH   B O   
6949 O  O   . HOH   G .   ? 0.1989 0.2166 0.4355 -0.0275 -0.0065 -0.0069 211 HOH   B O   
6950 O  O   . HOH   G .   ? 0.8346 0.4548 0.3938 -0.0963 0.0422  0.0605  212 HOH   B O   
6951 O  O   . HOH   G .   ? 0.6053 0.4415 0.6451 0.0753  -0.0932 0.2622  213 HOH   B O   
6952 O  O   . HOH   G .   ? 0.2137 0.2515 0.3520 -0.0114 0.0173  -0.0308 214 HOH   B O   
6953 O  O   . HOH   G .   ? 0.4586 0.4181 0.6222 -0.0884 -0.0525 -0.1350 215 HOH   B O   
6954 O  O   . HOH   G .   ? 0.4153 0.4526 0.4408 0.1809  -0.0355 0.0589  216 HOH   B O   
6955 O  O   . HOH   G .   ? 0.2040 0.2401 0.4254 -0.0259 0.0255  -0.0281 217 HOH   B O   
6956 O  O   . HOH   G .   ? 0.3267 0.2793 0.6697 0.0828  -0.0979 0.0526  218 HOH   B O   
6957 O  O   . HOH   G .   ? 0.7790 0.3520 0.4925 0.1040  0.1277  -0.0061 219 HOH   B O   
6958 O  O   . HOH   G .   ? 0.3806 0.4602 0.3810 0.0162  -0.0902 0.0285  220 HOH   B O   
6959 O  O   . HOH   G .   ? 0.2476 0.2716 0.4918 -0.0334 0.0060  -0.0480 221 HOH   B O   
6960 O  O   . HOH   G .   ? 0.4490 0.3714 0.6353 -0.0849 -0.1417 -0.0559 222 HOH   B O   
6961 O  O   . HOH   G .   ? 0.2681 0.1999 0.3350 -0.0317 0.0820  0.0084  223 HOH   B O   
6962 O  O   . HOH   G .   ? 0.4377 0.4252 0.5385 0.1577  -0.0766 -0.0801 224 HOH   B O   
6963 O  O   . HOH   G .   ? 0.7166 0.6908 0.5250 0.2363  0.0079  -0.0287 225 HOH   B O   
6964 O  O   . HOH   G .   ? 0.3664 0.4553 0.4439 0.0335  0.0506  -0.1174 226 HOH   B O   
6965 O  O   . HOH   G .   ? 0.8628 0.5878 0.4674 0.1609  -0.0298 -0.1277 227 HOH   B O   
6966 O  O   . HOH   G .   ? 0.2280 0.1532 0.4364 0.0072  -0.0560 -0.0110 228 HOH   B O   
6967 O  O   . HOH   G .   ? 0.2641 0.2364 0.3626 0.0770  -0.0915 -0.0758 229 HOH   B O   
6968 O  O   . HOH   G .   ? 0.2348 0.4413 0.3142 -0.0468 -0.0114 0.0349  230 HOH   B O   
6969 O  O   . HOH   G .   ? 0.2814 0.2924 0.3402 0.0338  0.0210  -0.0779 231 HOH   B O   
6970 O  O   . HOH   G .   ? 0.1698 0.1651 0.2523 -0.0124 -0.0023 -0.0056 232 HOH   B O   
6971 O  O   . HOH   G .   ? 0.5087 0.2286 0.3597 -0.0125 -0.0695 0.0243  233 HOH   B O   
6972 O  O   . HOH   G .   ? 0.3179 0.6350 0.3434 -0.1412 -0.0054 -0.0989 234 HOH   B O   
6973 O  O   . HOH   G .   ? 0.5152 0.7156 0.4201 0.2728  0.0541  0.0311  235 HOH   B O   
6974 O  O   . HOH   G .   ? 0.3772 0.1925 0.3002 0.0176  -0.1072 0.0063  236 HOH   B O   
6975 O  O   . HOH   G .   ? 0.2508 0.2161 0.3010 -0.0430 -0.0176 0.0289  237 HOH   B O   
6976 O  O   . HOH   G .   ? 0.4595 0.4429 0.6147 -0.1654 0.0085  0.1372  238 HOH   B O   
6977 O  O   . HOH   G .   ? 0.7232 0.6337 0.4259 0.0626  0.0752  0.0573  239 HOH   B O   
6978 O  O   . HOH   G .   ? 0.3486 0.3097 0.2496 0.0216  0.0204  0.0057  240 HOH   B O   
6979 O  O   . HOH   G .   ? 0.2659 0.3426 0.2553 -0.0607 0.0319  0.0430  241 HOH   B O   
6980 O  O   . HOH   G .   ? 0.1735 0.1691 0.4097 -0.0010 -0.0033 0.0111  242 HOH   B O   
6981 O  O   . HOH   G .   ? 0.3054 0.2382 0.3569 0.0651  0.0549  -0.0282 243 HOH   B O   
6982 O  O   . HOH   G .   ? 0.2859 0.3789 0.4135 -0.1425 -0.0052 -0.0074 244 HOH   B O   
6983 O  O   . HOH   G .   ? 0.5664 0.3335 0.4447 -0.1585 -0.0229 0.0310  245 HOH   B O   
6984 O  O   . HOH   G .   ? 0.2215 0.2420 0.4900 0.0001  -0.0367 -0.0231 246 HOH   B O   
6985 O  O   . HOH   G .   ? 0.2861 0.4599 0.3853 -0.0891 -0.0755 -0.0172 247 HOH   B O   
6986 O  O   . HOH   G .   ? 0.1862 0.1566 0.2759 -0.0030 -0.0254 0.0116  248 HOH   B O   
6987 O  O   . HOH   G .   ? 0.5872 0.3752 0.4610 -0.2660 0.0355  0.0062  249 HOH   B O   
6988 O  O   . HOH   G .   ? 0.3549 0.2079 0.7625 -0.0244 -0.1233 -0.0276 250 HOH   B O   
6989 O  O   . HOH   G .   ? 0.1863 0.1936 0.4775 -0.0283 -0.0431 0.0443  251 HOH   B O   
6990 O  O   . HOH   G .   ? 0.3085 0.5783 0.6415 -0.0027 -0.0272 -0.1116 252 HOH   B O   
6991 O  O   . HOH   G .   ? 0.4039 0.2732 0.4388 0.0665  -0.1024 -0.0955 253 HOH   B O   
6992 O  O   . HOH   G .   ? 0.4506 0.6564 0.5180 0.3060  0.0070  -0.0788 254 HOH   B O   
6993 O  O   . HOH   G .   ? 0.3627 0.5101 0.4516 -0.0283 -0.1090 0.1680  255 HOH   B O   
6994 O  O   . HOH   G .   ? 0.4551 0.3497 0.4348 0.1194  -0.0139 -0.0468 256 HOH   B O   
6995 O  O   . HOH   G .   ? 0.3003 0.3719 0.3715 -0.0806 0.0258  0.0117  257 HOH   B O   
6996 O  O   . HOH   G .   ? 0.2478 0.1850 0.3009 -0.0415 -0.0560 0.0440  258 HOH   B O   
6997 O  O   . HOH   G .   ? 0.2861 0.2530 0.2934 0.0210  0.0152  -0.0242 259 HOH   B O   
6998 O  O   . HOH   G .   ? 0.5187 0.4205 0.3540 0.0091  -0.0181 -0.0412 260 HOH   B O   
6999 O  O   . HOH   G .   ? 0.2219 0.1594 0.5815 -0.0144 -0.0646 0.0028  261 HOH   B O   
7000 O  O   . HOH   G .   ? 0.3100 0.4967 0.5567 0.1608  -0.0673 -0.1519 262 HOH   B O   
7001 O  O   . HOH   G .   ? 0.2802 0.5528 0.2613 0.1728  -0.0013 -0.0200 263 HOH   B O   
7002 O  O   . HOH   G .   ? 0.4378 0.3247 0.3610 -0.0984 0.0115  -0.0325 264 HOH   B O   
7003 O  O   . HOH   G .   ? 0.3894 0.4416 0.3150 -0.0083 0.0756  0.0081  265 HOH   B O   
7004 O  O   . HOH   G .   ? 0.1974 0.2669 0.4075 0.0203  0.0048  -0.0210 266 HOH   B O   
7005 O  O   . HOH   G .   ? 0.3391 0.5117 0.5210 -0.1231 -0.1194 0.1299  267 HOH   B O   
7006 O  O   . HOH   G .   ? 0.2201 0.1900 0.2583 -0.0519 -0.0572 0.0207  268 HOH   B O   
7007 O  O   . HOH   G .   ? 0.4476 0.2856 0.2698 0.0931  -0.0137 -0.0133 269 HOH   B O   
7008 O  O   . HOH   G .   ? 0.2822 0.3005 0.3124 -0.0441 -0.1035 0.0301  270 HOH   B O   
7009 O  O   . HOH   G .   ? 0.2288 0.1805 0.3226 -0.0414 -0.0154 0.0121  271 HOH   B O   
7010 O  O   . HOH   G .   ? 0.2452 0.2664 0.3053 -0.0261 -0.0629 -0.0400 272 HOH   B O   
7011 O  O   . HOH   G .   ? 0.4587 0.2683 0.5225 -0.0229 -0.1165 -0.0034 273 HOH   B O   
7012 O  O   . HOH   G .   ? 0.2780 0.2126 0.3311 -0.0541 0.0289  -0.0125 274 HOH   B O   
7013 O  O   . HOH   G .   ? 0.3130 0.7657 0.3337 0.1101  -0.0463 -0.0841 275 HOH   B O   
7014 O  O   . HOH   G .   ? 0.2496 0.5709 0.5992 -0.0262 -0.0450 -0.1248 276 HOH   B O   
7015 O  O   . HOH   G .   ? 0.3398 0.4291 0.4056 0.0428  0.1162  0.0318  277 HOH   B O   
7016 O  O   . HOH   G .   ? 0.3943 0.2530 0.4900 0.0443  0.0493  0.0364  278 HOH   B O   
7017 O  O   . HOH   G .   ? 0.4635 0.5086 0.5372 -0.0313 -0.1419 0.0434  279 HOH   B O   
7018 O  O   . HOH   G .   ? 0.2073 0.1711 0.3023 -0.0046 0.0101  -0.0102 280 HOH   B O   
7019 O  O   . HOH   G .   ? 0.2018 0.2111 0.2473 -0.0077 -0.0195 -0.0003 281 HOH   B O   
7020 O  O   . HOH   G .   ? 0.5639 0.6868 0.2938 0.0904  -0.1137 0.0457  282 HOH   B O   
7021 O  O   . HOH   G .   ? 0.1763 0.1827 0.5146 -0.0146 0.0157  -0.0257 283 HOH   B O   
7022 O  O   . HOH   G .   ? 0.4592 0.3559 0.3474 -0.1283 0.0735  -0.1279 284 HOH   B O   
7023 O  O   . HOH   G .   ? 0.2975 0.7729 0.7958 0.1589  -0.0724 -0.1318 285 HOH   B O   
7024 O  O   . HOH   G .   ? 0.2609 0.3225 0.4134 -0.0296 0.0260  -0.0826 286 HOH   B O   
7025 O  O   . HOH   G .   ? 0.4946 0.4527 0.5123 0.0584  0.0651  0.0285  287 HOH   B O   
7026 O  O   . HOH   G .   ? 0.5264 0.4175 0.5487 -0.1250 0.0408  -0.1142 288 HOH   B O   
7027 O  O   . HOH   G .   ? 0.3426 0.3578 0.5534 -0.0427 -0.0707 0.1122  289 HOH   B O   
7028 O  O   . HOH   G .   ? 0.2339 0.3469 0.6731 0.0594  -0.0420 -0.1157 290 HOH   B O   
7029 O  O   . HOH   G .   ? 0.3794 0.2807 0.2861 0.0276  -0.0797 0.0004  291 HOH   B O   
7030 O  O   . HOH   G .   ? 0.4377 0.4543 0.6694 -0.0108 0.1001  -0.0605 292 HOH   B O   
7031 O  O   . HOH   G .   ? 0.3197 0.2985 0.3508 0.0244  -0.0912 0.0397  293 HOH   B O   
7032 O  O   . HOH   G .   ? 0.4365 0.3032 0.2760 -0.1525 0.0159  -0.0020 294 HOH   B O   
7033 O  O   . HOH   G .   ? 0.2343 0.6062 0.5377 -0.0868 -0.0430 0.0879  295 HOH   B O   
7034 O  O   . HOH   G .   ? 0.6793 0.4570 0.3503 0.3160  0.0974  0.0790  296 HOH   B O   
7035 O  O   . HOH   G .   ? 0.4558 0.3760 0.3088 0.0884  -0.0904 0.0502  297 HOH   B O   
7036 O  O   . HOH   G .   ? 0.3234 0.3479 0.6586 -0.0483 -0.1823 0.1725  298 HOH   B O   
7037 O  O   . HOH   G .   ? 0.2066 0.4426 0.5550 0.0500  -0.0121 -0.1515 299 HOH   B O   
7038 O  O   . HOH   G .   ? 0.4465 0.5136 0.4045 -0.2079 0.1169  -0.0444 300 HOH   B O   
7039 O  O   . HOH   G .   ? 0.4972 0.6310 0.3452 0.0423  0.1101  0.1837  301 HOH   B O   
7040 O  O   . HOH   G .   ? 0.1793 0.1666 0.4529 0.0040  -0.0031 0.0136  302 HOH   B O   
7041 O  O   . HOH   G .   ? 0.4452 0.5004 0.6313 0.0508  -0.0060 0.0550  303 HOH   B O   
7042 O  O   . HOH   G .   ? 0.5545 0.5716 0.4333 0.2393  -0.0681 -0.0218 304 HOH   B O   
7043 O  O   . HOH   G .   ? 0.3602 0.1683 0.3936 0.0344  0.0953  0.0264  305 HOH   B O   
7044 O  O   . HOH   G .   ? 0.2897 0.1710 0.3504 -0.0278 -0.0493 0.0300  306 HOH   B O   
7045 O  O   . HOH   G .   ? 0.4310 0.2425 0.4763 -0.1142 -0.1923 0.1098  307 HOH   B O   
7046 O  O   . HOH   G .   ? 0.2450 0.3270 0.4975 -0.0102 -0.0492 -0.0074 308 HOH   B O   
7047 O  O   . HOH   G .   ? 0.2573 0.1944 0.4970 0.0595  -0.0971 -0.0390 309 HOH   B O   
7048 O  O   . HOH   G .   ? 0.3433 0.2117 0.3914 0.0617  0.0913  0.0320  310 HOH   B O   
7049 O  O   . HOH   G .   ? 0.5527 0.2922 0.3383 0.0476  0.0330  0.0705  311 HOH   B O   
7050 O  O   . HOH   G .   ? 0.2903 0.1988 0.2954 -0.0053 0.0243  0.0289  312 HOH   B O   
7051 O  O   . HOH   G .   ? 0.6237 0.4556 0.4124 0.1108  0.1351  0.1771  313 HOH   B O   
7052 O  O   . HOH   G .   ? 0.4073 0.7545 0.3807 0.1874  -0.0200 0.1265  314 HOH   B O   
7053 O  O   . HOH   G .   ? 0.2398 0.2438 0.6190 -0.0592 0.0116  0.1171  315 HOH   B O   
7054 O  O   . HOH   G .   ? 0.1966 0.1965 0.4467 -0.0361 0.0141  0.0083  316 HOH   B O   
7055 O  O   . HOH   G .   ? 0.4203 0.2623 0.3077 0.0485  -0.0131 0.0300  317 HOH   B O   
7056 O  O   . HOH   G .   ? 0.6818 0.3797 0.3382 -0.0962 -0.0249 -0.0444 318 HOH   B O   
7057 O  O   . HOH   G .   ? 0.3342 0.2206 0.3443 0.0923  0.0589  0.0167  319 HOH   B O   
7058 O  O   . HOH   G .   ? 0.3552 0.3228 0.3997 -0.0532 0.1213  -0.0888 320 HOH   B O   
7059 O  O   . HOH   G .   ? 0.7342 0.5228 0.5518 0.1286  0.1046  -0.0461 321 HOH   B O   
7060 O  O   . HOH   G .   ? 0.1880 0.1833 0.4640 -0.0177 -0.0270 -0.0191 322 HOH   B O   
7061 O  O   . HOH   G .   ? 0.4792 0.3827 0.5079 -0.0904 0.0272  0.1037  323 HOH   B O   
7062 O  O   . HOH   G .   ? 0.1953 0.3149 0.3306 -0.0278 -0.0206 0.1023  324 HOH   B O   
7063 O  O   . HOH   G .   ? 0.3660 0.4553 0.8768 -0.0765 -0.1175 0.2542  325 HOH   B O   
7064 O  O   . HOH   G .   ? 0.2277 0.1924 0.3940 -0.0395 -0.0177 -0.0125 326 HOH   B O   
7065 O  O   . HOH   G .   ? 0.2123 0.2116 0.3653 0.0157  0.0297  0.0072  327 HOH   B O   
7066 O  O   . HOH   G .   ? 0.2898 0.2275 0.7078 -0.0248 -0.0008 0.0805  328 HOH   B O   
7067 O  O   . HOH   G .   ? 0.2265 0.3426 0.3829 0.0590  -0.0258 -0.0416 329 HOH   B O   
7068 O  O   . HOH   G .   ? 0.7013 0.8491 0.3540 0.0169  -0.0576 0.1168  330 HOH   B O   
7069 O  O   . HOH   G .   ? 0.4789 0.3703 0.6011 0.1500  0.2132  0.1973  331 HOH   B O   
7070 O  O   . HOH   G .   ? 0.1959 0.1728 0.3991 0.0066  -0.0139 0.0077  332 HOH   B O   
7071 O  O   . HOH   G .   ? 0.5465 0.6266 0.7217 0.1864  -0.0977 0.2621  333 HOH   B O   
7072 O  O   . HOH   G .   ? 0.5882 0.4654 0.6174 -0.0734 -0.1159 -0.1159 334 HOH   B O   
7073 O  O   . HOH   G .   ? 0.7540 0.2698 0.3499 -0.0029 -0.0454 -0.0073 335 HOH   B O   
7074 O  O   . HOH   G .   ? 0.4554 0.3811 0.2788 0.1292  -0.0567 -0.0423 336 HOH   B O   
7075 O  O   . HOH   G .   ? 0.2880 0.5225 0.7342 -0.0534 -0.0636 -0.0055 337 HOH   B O   
7076 O  O   . HOH   G .   ? 0.5654 0.3187 0.3428 0.0431  -0.1179 -0.0429 338 HOH   B O   
7077 O  O   . HOH   G .   ? 0.6091 0.5960 0.5737 -0.0972 -0.1134 0.1850  339 HOH   B O   
7078 O  O   . HOH   G .   ? 0.4603 0.7946 0.3829 -0.0617 -0.1028 0.1704  340 HOH   B O   
7079 O  O   . HOH   G .   ? 0.3872 0.6574 0.4230 -0.0912 -0.0840 -0.0375 341 HOH   B O   
7080 O  O   . HOH   G .   ? 0.6219 0.4569 0.4321 -0.0444 0.1329  -0.1374 342 HOH   B O   
7081 O  O   . HOH   G .   ? 0.4839 0.5331 0.3549 -0.0063 -0.1396 -0.0312 343 HOH   B O   
7082 O  O   . HOH   G .   ? 0.3081 0.2118 0.4388 0.0167  -0.0970 -0.0287 344 HOH   B O   
7083 O  O   . HOH   G .   ? 0.4678 0.7418 0.5538 0.0263  -0.0804 -0.0002 345 HOH   B O   
7084 O  O   . HOH   G .   ? 0.2226 0.2001 0.4935 -0.0195 0.0902  -0.0052 346 HOH   B O   
7085 O  O   . HOH   G .   ? 0.4920 0.6177 0.6363 -0.1263 0.0115  0.1703  347 HOH   B O   
7086 O  O   . HOH   G .   ? 0.3188 0.2476 0.4571 -0.0398 -0.0779 -0.0520 348 HOH   B O   
7087 O  O   . HOH   G .   ? 0.4148 0.2430 0.3382 -0.0784 -0.0216 -0.0483 349 HOH   B O   
7088 O  O   . HOH   G .   ? 0.4357 0.6016 0.5742 -0.0122 -0.0135 -0.1007 350 HOH   B O   
7089 O  O   . HOH   G .   ? 0.2769 0.3613 0.6059 -0.0298 0.0081  0.0345  351 HOH   B O   
7090 O  O   . HOH   G .   ? 0.2312 0.6738 0.4414 0.1378  -0.0496 -0.1172 352 HOH   B O   
7091 O  O   . HOH   G .   ? 0.5364 0.5684 0.4581 0.2084  -0.1118 0.0720  353 HOH   B O   
7092 O  O   . HOH   G .   ? 0.3848 0.5570 0.5592 -0.1971 -0.0057 -0.0472 354 HOH   B O   
7093 O  O   . HOH   G .   ? 0.5019 0.2855 0.5731 -0.1293 0.0945  0.0375  355 HOH   B O   
7094 O  O   . HOH   G .   ? 0.5661 0.3921 0.4383 0.0714  0.1259  -0.0240 356 HOH   B O   
7095 O  O   . HOH   G .   ? 0.3427 0.3053 0.4652 -0.0932 -0.0097 -0.0755 357 HOH   B O   
7096 O  O   . HOH   G .   ? 0.5523 0.4410 0.6215 0.0323  0.0787  0.0812  358 HOH   B O   
7097 O  O   . HOH   G .   ? 0.5951 0.4174 0.4692 0.0162  -0.1576 -0.0531 359 HOH   B O   
7098 O  O   . HOH   G .   ? 0.4127 0.7049 0.3378 0.2269  0.0603  0.1074  360 HOH   B O   
7099 O  O   . HOH   G .   ? 0.2586 0.4127 0.7778 -0.0976 -0.0758 -0.0459 361 HOH   B O   
7100 O  O   . HOH   G .   ? 0.5082 0.4780 0.5421 -0.0185 0.0095  0.0495  362 HOH   B O   
7101 O  O   . HOH   G .   ? 0.6226 0.5665 0.4896 -0.0849 -0.0594 -0.1189 363 HOH   B O   
7102 O  O   . HOH   G .   ? 0.7171 0.2470 0.4872 -0.0146 0.0199  0.0613  364 HOH   B O   
7103 O  O   . HOH   G .   ? 0.5072 0.4002 0.5131 0.0770  -0.1335 0.0493  365 HOH   B O   
7104 O  O   . HOH   G .   ? 0.5471 0.4540 0.3718 0.1301  -0.0031 0.0370  366 HOH   B O   
7105 O  O   . HOH   G .   ? 0.5742 0.3304 0.5668 -0.1546 -0.0851 0.0185  367 HOH   B O   
7106 O  O   . HOH   G .   ? 0.3704 0.5958 0.5387 0.2222  0.0875  0.1680  368 HOH   B O   
7107 O  O   . HOH   G .   ? 0.7506 0.8489 0.5462 0.2693  -0.1287 0.0581  369 HOH   B O   
7108 O  O   . HOH   G .   ? 0.3838 0.2876 0.4062 0.0412  -0.0968 -0.0151 370 HOH   B O   
7109 O  O   . HOH   G .   ? 0.5925 0.5849 0.3651 0.1663  -0.1442 0.0563  371 HOH   B O   
7110 O  O   . HOH   G .   ? 0.5489 0.4334 0.3421 -0.0764 -0.1001 -0.0827 372 HOH   B O   
7111 O  O   . HOH   G .   ? 0.4290 0.5027 0.4601 -0.0810 -0.0112 -0.0176 373 HOH   B O   
7112 O  O   . HOH   G .   ? 0.4889 0.7558 0.6468 0.1319  0.0735  0.2995  374 HOH   B O   
7113 O  O   . HOH   G .   ? 0.4002 0.6708 0.2790 -0.0431 0.0305  0.0644  375 HOH   B O   
7114 O  O   . HOH   G .   ? 0.2462 0.3796 0.5184 0.0185  -0.0491 -0.0550 376 HOH   B O   
7115 O  O   . HOH   G .   ? 0.5250 0.6220 0.4011 -0.1148 -0.0071 -0.1486 377 HOH   B O   
7116 O  O   . HOH   G .   ? 0.3328 0.4933 0.5616 0.0735  -0.0701 0.0302  378 HOH   B O   
7117 O  O   . HOH   G .   ? 0.8030 0.3958 0.4847 -0.1238 -0.0653 -0.0281 379 HOH   B O   
7118 O  O   . HOH   G .   ? 0.5222 0.6620 0.6084 -0.0219 0.1450  0.1951  380 HOH   B O   
7119 O  O   . HOH   G .   ? 0.8786 0.3904 0.4411 0.0851  0.2122  -0.0445 381 HOH   B O   
7120 O  O   . HOH   G .   ? 0.6491 0.4665 0.4560 -0.0798 -0.0279 -0.0651 382 HOH   B O   
7121 O  O   . HOH   G .   ? 0.3659 0.2969 0.4078 0.0074  0.0186  0.0267  383 HOH   B O   
7122 O  O   . HOH   G .   ? 0.4294 0.8673 0.5141 0.0850  0.1181  0.0937  384 HOH   B O   
7123 O  O   . HOH   G .   ? 0.7562 0.4632 0.5125 -0.0632 0.0712  -0.0080 385 HOH   B O   
7124 O  O   . HOH   G .   ? 0.5301 0.3001 0.4936 -0.1653 -0.0193 0.0361  386 HOH   B O   
7125 O  O   . HOH   G .   ? 0.2641 0.5031 0.5105 -0.1052 -0.0743 -0.0229 387 HOH   B O   
7126 O  O   . HOH   G .   ? 0.4841 0.4232 0.4420 -0.0052 0.0975  -0.0391 388 HOH   B O   
7127 O  O   . HOH   G .   ? 0.8685 0.6171 0.4947 0.1445  -0.0175 -0.0268 389 HOH   B O   
7128 O  O   . HOH   G .   ? 0.3954 0.2435 0.3638 0.0783  -0.0049 0.0219  390 HOH   B O   
7129 O  O   . HOH   G .   ? 0.5630 0.4417 0.5903 0.0753  0.1454  0.0936  391 HOH   B O   
7130 O  O   . HOH   G .   ? 0.4578 0.2392 0.5349 -0.0725 -0.0100 0.0597  392 HOH   B O   
7131 O  O   . HOH   G .   ? 0.2629 0.6141 0.7686 -0.1537 -0.0665 -0.0389 393 HOH   B O   
7132 O  O   . HOH   G .   ? 0.3598 0.4473 0.4776 -0.0014 0.0380  -0.0835 394 HOH   B O   
7133 O  O   . HOH   G .   ? 0.4633 0.6050 0.5068 0.1366  0.0213  -0.1357 395 HOH   B O   
7134 O  O   . HOH   G .   ? 0.2547 0.3047 0.7598 -0.0625 -0.0743 0.0123  396 HOH   B O   
7135 O  O   . HOH   G .   ? 0.5399 0.4946 0.5530 0.1556  0.1982  0.0954  397 HOH   B O   
7136 O  O   . HOH   G .   ? 0.4960 0.5433 0.6295 -0.0440 -0.1203 0.2973  398 HOH   B O   
7137 O  O   . HOH   G .   ? 0.5304 0.4713 0.3348 -0.2470 -0.0675 0.1159  399 HOH   B O   
7138 O  O   . HOH   G .   ? 0.6068 0.6047 0.3878 0.1733  -0.0730 -0.0606 400 HOH   B O   
# 
