data_7HDX
# 
_entry.id   7HDX 
# 
_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   7HDX         pdb_00007hdx 10.2210/pdb7hdx/pdb 
WWPDB D_1001407351 ?            ?                   
# 
_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                        7HDX 
_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 'trifluoroacetic acid'                                                    114.023   1   ?                      ? 
? ?                                                                                    
3 non-polymer syn '(2S)-4,4-dimethyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]pentan-1-ol' 248.324   1   ?                      ? 
? ?                                                                                    
4 non-polymer syn 'CHLORIDE ION'                                                            35.453    1   ?                      ? 
? ?                                                                                    
5 water       nat water                                                                     18.015    422 ?                      ? 
? ?                                                                                    
# 
_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 'trifluoroacetic acid'                                                    TFA   
3 '(2S)-4,4-dimethyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]pentan-1-ol' A1A86 
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 
A1A86 non-polymer         . '(2S)-4,4-dimethyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]pentan-1-ol' ? 'C13 H20 N4 O'   248.324 
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 
TFA   non-polymer         . 'trifluoroacetic acid'                                                    ? 'C2 H F3 O2'     114.023 
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 TFA   1   201 201  TFA   TFA A . 
D 3 A1A86 1   202 201  A1A86 LA1 A . 
E 4 CL    1   203 1    CL    CL  A . 
F 5 HOH   1   301 292  HOH   HOH A . 
F 5 HOH   2   302 229  HOH   HOH A . 
F 5 HOH   3   303 625  HOH   HOH A . 
F 5 HOH   4   304 196  HOH   HOH A . 
F 5 HOH   5   305 109  HOH   HOH A . 
F 5 HOH   6   306 1275 HOH   HOH A . 
F 5 HOH   7   307 153  HOH   HOH A . 
F 5 HOH   8   308 209  HOH   HOH A . 
F 5 HOH   9   309 76   HOH   HOH A . 
F 5 HOH   10  310 136  HOH   HOH A . 
F 5 HOH   11  311 18   HOH   HOH A . 
F 5 HOH   12  312 1289 HOH   HOH A . 
F 5 HOH   13  313 105  HOH   HOH A . 
F 5 HOH   14  314 281  HOH   HOH A . 
F 5 HOH   15  315 662  HOH   HOH A . 
F 5 HOH   16  316 337  HOH   HOH A . 
F 5 HOH   17  317 1295 HOH   HOH A . 
F 5 HOH   18  318 36   HOH   HOH A . 
F 5 HOH   19  319 409  HOH   HOH A . 
F 5 HOH   20  320 393  HOH   HOH A . 
F 5 HOH   21  321 247  HOH   HOH A . 
F 5 HOH   22  322 661  HOH   HOH A . 
F 5 HOH   23  323 1309 HOH   HOH A . 
F 5 HOH   24  324 225  HOH   HOH A . 
F 5 HOH   25  325 124  HOH   HOH A . 
F 5 HOH   26  326 192  HOH   HOH A . 
F 5 HOH   27  327 56   HOH   HOH A . 
F 5 HOH   28  328 164  HOH   HOH A . 
F 5 HOH   29  329 354  HOH   HOH A . 
F 5 HOH   30  330 140  HOH   HOH A . 
F 5 HOH   31  331 8    HOH   HOH A . 
F 5 HOH   32  332 151  HOH   HOH A . 
F 5 HOH   33  333 236  HOH   HOH A . 
F 5 HOH   34  334 15   HOH   HOH A . 
F 5 HOH   35  335 93   HOH   HOH A . 
F 5 HOH   36  336 469  HOH   HOH A . 
F 5 HOH   37  337 964  HOH   HOH A . 
F 5 HOH   38  338 13   HOH   HOH A . 
F 5 HOH   39  339 241  HOH   HOH A . 
F 5 HOH   40  340 92   HOH   HOH A . 
F 5 HOH   41  341 1300 HOH   HOH A . 
F 5 HOH   42  342 42   HOH   HOH A . 
F 5 HOH   43  343 21   HOH   HOH A . 
F 5 HOH   44  344 165  HOH   HOH A . 
F 5 HOH   45  345 195  HOH   HOH A . 
F 5 HOH   46  346 2    HOH   HOH A . 
F 5 HOH   47  347 162  HOH   HOH A . 
F 5 HOH   48  348 320  HOH   HOH A . 
F 5 HOH   49  349 1283 HOH   HOH A . 
F 5 HOH   50  350 630  HOH   HOH A . 
F 5 HOH   51  351 405  HOH   HOH A . 
F 5 HOH   52  352 19   HOH   HOH A . 
F 5 HOH   53  353 102  HOH   HOH A . 
F 5 HOH   54  354 66   HOH   HOH A . 
F 5 HOH   55  355 17   HOH   HOH A . 
F 5 HOH   56  356 939  HOH   HOH A . 
F 5 HOH   57  357 186  HOH   HOH A . 
F 5 HOH   58  358 139  HOH   HOH A . 
F 5 HOH   59  359 155  HOH   HOH A . 
F 5 HOH   60  360 138  HOH   HOH A . 
F 5 HOH   61  361 39   HOH   HOH A . 
F 5 HOH   62  362 396  HOH   HOH A . 
F 5 HOH   63  363 8    HOH   HOH A . 
F 5 HOH   64  364 218  HOH   HOH A . 
F 5 HOH   65  365 296  HOH   HOH A . 
F 5 HOH   66  366 148  HOH   HOH A . 
F 5 HOH   67  367 1301 HOH   HOH A . 
F 5 HOH   68  368 57   HOH   HOH A . 
F 5 HOH   69  369 46   HOH   HOH A . 
F 5 HOH   70  370 5    HOH   HOH A . 
F 5 HOH   71  371 1290 HOH   HOH A . 
F 5 HOH   72  372 461  HOH   HOH A . 
F 5 HOH   73  373 159  HOH   HOH A . 
F 5 HOH   74  374 169  HOH   HOH A . 
F 5 HOH   75  375 1310 HOH   HOH A . 
F 5 HOH   76  376 33   HOH   HOH A . 
F 5 HOH   77  377 366  HOH   HOH A . 
F 5 HOH   78  378 493  HOH   HOH A . 
F 5 HOH   79  379 45   HOH   HOH A . 
F 5 HOH   80  380 12   HOH   HOH A . 
F 5 HOH   81  381 27   HOH   HOH A . 
F 5 HOH   82  382 85   HOH   HOH A . 
F 5 HOH   83  383 134  HOH   HOH A . 
F 5 HOH   84  384 81   HOH   HOH A . 
F 5 HOH   85  385 49   HOH   HOH A . 
F 5 HOH   86  386 140  HOH   HOH A . 
F 5 HOH   87  387 116  HOH   HOH A . 
F 5 HOH   88  388 62   HOH   HOH A . 
F 5 HOH   89  389 86   HOH   HOH A . 
F 5 HOH   90  390 351  HOH   HOH A . 
F 5 HOH   91  391 78   HOH   HOH A . 
F 5 HOH   92  392 381  HOH   HOH A . 
F 5 HOH   93  393 6    HOH   HOH A . 
F 5 HOH   94  394 26   HOH   HOH A . 
F 5 HOH   95  395 35   HOH   HOH A . 
F 5 HOH   96  396 58   HOH   HOH A . 
F 5 HOH   97  397 74   HOH   HOH A . 
F 5 HOH   98  398 154  HOH   HOH A . 
F 5 HOH   99  399 1308 HOH   HOH A . 
F 5 HOH   100 400 132  HOH   HOH A . 
F 5 HOH   101 401 115  HOH   HOH A . 
F 5 HOH   102 402 199  HOH   HOH A . 
F 5 HOH   103 403 67   HOH   HOH A . 
F 5 HOH   104 404 83   HOH   HOH A . 
F 5 HOH   105 405 1    HOH   HOH A . 
F 5 HOH   106 406 121  HOH   HOH A . 
F 5 HOH   107 407 4    HOH   HOH A . 
F 5 HOH   108 408 1315 HOH   HOH A . 
F 5 HOH   109 409 303  HOH   HOH A . 
F 5 HOH   110 410 1313 HOH   HOH A . 
F 5 HOH   111 411 397  HOH   HOH A . 
F 5 HOH   112 412 3    HOH   HOH A . 
F 5 HOH   113 413 4    HOH   HOH A . 
F 5 HOH   114 414 34   HOH   HOH A . 
F 5 HOH   115 415 1068 HOH   HOH A . 
F 5 HOH   116 416 25   HOH   HOH A . 
F 5 HOH   117 417 68   HOH   HOH A . 
F 5 HOH   118 418 24   HOH   HOH A . 
F 5 HOH   119 419 156  HOH   HOH A . 
F 5 HOH   120 420 96   HOH   HOH A . 
F 5 HOH   121 421 125  HOH   HOH A . 
F 5 HOH   122 422 278  HOH   HOH A . 
F 5 HOH   123 423 53   HOH   HOH A . 
F 5 HOH   124 424 123  HOH   HOH A . 
F 5 HOH   125 425 95   HOH   HOH A . 
F 5 HOH   126 426 333  HOH   HOH A . 
F 5 HOH   127 427 1279 HOH   HOH A . 
F 5 HOH   128 428 1222 HOH   HOH A . 
F 5 HOH   129 429 122  HOH   HOH A . 
F 5 HOH   130 430 51   HOH   HOH A . 
F 5 HOH   131 431 70   HOH   HOH A . 
F 5 HOH   132 432 7    HOH   HOH A . 
F 5 HOH   133 433 582  HOH   HOH A . 
F 5 HOH   134 434 70   HOH   HOH A . 
F 5 HOH   135 435 952  HOH   HOH A . 
F 5 HOH   136 436 1189 HOH   HOH A . 
F 5 HOH   137 437 212  HOH   HOH A . 
F 5 HOH   138 438 12   HOH   HOH A . 
F 5 HOH   139 439 104  HOH   HOH A . 
F 5 HOH   140 440 71   HOH   HOH A . 
F 5 HOH   141 441 80   HOH   HOH A . 
F 5 HOH   142 442 40   HOH   HOH A . 
F 5 HOH   143 443 2    HOH   HOH A . 
F 5 HOH   144 444 94   HOH   HOH A . 
F 5 HOH   145 445 1286 HOH   HOH A . 
F 5 HOH   146 446 1296 HOH   HOH A . 
F 5 HOH   147 447 944  HOH   HOH A . 
F 5 HOH   148 448 1238 HOH   HOH A . 
F 5 HOH   149 449 576  HOH   HOH A . 
F 5 HOH   150 450 79   HOH   HOH A . 
F 5 HOH   151 451 97   HOH   HOH A . 
F 5 HOH   152 452 73   HOH   HOH A . 
F 5 HOH   153 453 16   HOH   HOH A . 
F 5 HOH   154 454 1094 HOH   HOH A . 
F 5 HOH   155 455 188  HOH   HOH A . 
F 5 HOH   156 456 330  HOH   HOH A . 
F 5 HOH   157 457 1119 HOH   HOH A . 
F 5 HOH   158 458 7    HOH   HOH A . 
F 5 HOH   159 459 107  HOH   HOH A . 
F 5 HOH   160 460 1134 HOH   HOH A . 
F 5 HOH   161 461 509  HOH   HOH A . 
F 5 HOH   162 462 163  HOH   HOH A . 
F 5 HOH   163 463 726  HOH   HOH A . 
F 5 HOH   164 464 756  HOH   HOH A . 
F 5 HOH   165 465 408  HOH   HOH A . 
F 5 HOH   166 466 361  HOH   HOH A . 
F 5 HOH   167 467 14   HOH   HOH A . 
F 5 HOH   168 468 126  HOH   HOH A . 
F 5 HOH   169 469 1307 HOH   HOH A . 
F 5 HOH   170 470 319  HOH   HOH A . 
F 5 HOH   171 471 63   HOH   HOH A . 
F 5 HOH   172 472 280  HOH   HOH A . 
F 5 HOH   173 473 250  HOH   HOH A . 
F 5 HOH   174 474 1276 HOH   HOH A . 
F 5 HOH   175 475 801  HOH   HOH A . 
F 5 HOH   176 476 556  HOH   HOH A . 
F 5 HOH   177 477 1287 HOH   HOH A . 
F 5 HOH   178 478 135  HOH   HOH A . 
F 5 HOH   179 479 342  HOH   HOH A . 
F 5 HOH   180 480 695  HOH   HOH A . 
F 5 HOH   181 481 370  HOH   HOH A . 
F 5 HOH   182 482 1306 HOH   HOH A . 
F 5 HOH   183 483 224  HOH   HOH A . 
F 5 HOH   184 484 674  HOH   HOH A . 
F 5 HOH   185 485 919  HOH   HOH A . 
F 5 HOH   186 486 11   HOH   HOH A . 
F 5 HOH   187 487 267  HOH   HOH A . 
F 5 HOH   188 488 202  HOH   HOH A . 
F 5 HOH   189 489 1299 HOH   HOH A . 
F 5 HOH   190 490 326  HOH   HOH A . 
F 5 HOH   191 491 1314 HOH   HOH A . 
F 5 HOH   192 492 521  HOH   HOH A . 
F 5 HOH   193 493 318  HOH   HOH A . 
F 5 HOH   194 494 309  HOH   HOH A . 
F 5 HOH   195 495 315  HOH   HOH A . 
F 5 HOH   196 496 805  HOH   HOH A . 
F 5 HOH   197 497 331  HOH   HOH A . 
F 5 HOH   198 498 263  HOH   HOH A . 
F 5 HOH   199 499 152  HOH   HOH A . 
F 5 HOH   200 500 711  HOH   HOH A . 
F 5 HOH   201 501 356  HOH   HOH A . 
F 5 HOH   202 502 941  HOH   HOH A . 
F 5 HOH   203 503 208  HOH   HOH A . 
F 5 HOH   204 504 1071 HOH   HOH A . 
F 5 HOH   205 505 180  HOH   HOH A . 
F 5 HOH   206 506 350  HOH   HOH A . 
F 5 HOH   207 507 363  HOH   HOH A . 
F 5 HOH   208 508 371  HOH   HOH A . 
F 5 HOH   209 509 9    HOH   HOH A . 
F 5 HOH   210 510 313  HOH   HOH A . 
F 5 HOH   211 511 1284 HOH   HOH A . 
F 5 HOH   212 512 10   HOH   HOH A . 
F 5 HOH   213 513 5    HOH   HOH A . 
F 5 HOH   214 514 429  HOH   HOH A . 
F 5 HOH   215 515 185  HOH   HOH A . 
F 5 HOH   216 516 376  HOH   HOH A . 
F 5 HOH   217 517 772  HOH   HOH A . 
F 5 HOH   218 518 6    HOH   HOH A . 
F 5 HOH   219 519 1074 HOH   HOH A . 
F 5 HOH   220 520 346  HOH   HOH A . 
F 5 HOH   221 521 1292 HOH   HOH A . 
F 5 HOH   222 522 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 900  HOH   HOH B . 
G 5 HOH   3   203 358  HOH   HOH B . 
G 5 HOH   4   204 1249 HOH   HOH B . 
G 5 HOH   5   205 364  HOH   HOH B . 
G 5 HOH   6   206 654  HOH   HOH B . 
G 5 HOH   7   207 120  HOH   HOH B . 
G 5 HOH   8   208 743  HOH   HOH B . 
G 5 HOH   9   209 758  HOH   HOH B . 
G 5 HOH   10  210 549  HOH   HOH B . 
G 5 HOH   11  211 452  HOH   HOH B . 
G 5 HOH   12  212 1140 HOH   HOH B . 
G 5 HOH   13  213 232  HOH   HOH B . 
G 5 HOH   14  214 353  HOH   HOH B . 
G 5 HOH   15  215 343  HOH   HOH B . 
G 5 HOH   16  216 332  HOH   HOH B . 
G 5 HOH   17  217 50   HOH   HOH B . 
G 5 HOH   18  218 131  HOH   HOH B . 
G 5 HOH   19  219 276  HOH   HOH B . 
G 5 HOH   20  220 398  HOH   HOH B . 
G 5 HOH   21  221 1278 HOH   HOH B . 
G 5 HOH   22  222 1312 HOH   HOH B . 
G 5 HOH   23  223 240  HOH   HOH B . 
G 5 HOH   24  224 264  HOH   HOH B . 
G 5 HOH   25  225 723  HOH   HOH B . 
G 5 HOH   26  226 444  HOH   HOH B . 
G 5 HOH   27  227 54   HOH   HOH B . 
G 5 HOH   28  228 82   HOH   HOH B . 
G 5 HOH   29  229 282  HOH   HOH B . 
G 5 HOH   30  230 75   HOH   HOH B . 
G 5 HOH   31  231 531  HOH   HOH B . 
G 5 HOH   32  232 128  HOH   HOH B . 
G 5 HOH   33  233 205  HOH   HOH B . 
G 5 HOH   34  234 325  HOH   HOH B . 
G 5 HOH   35  235 1    HOH   HOH B . 
G 5 HOH   36  236 129  HOH   HOH B . 
G 5 HOH   37  237 14   HOH   HOH B . 
G 5 HOH   38  238 181  HOH   HOH B . 
G 5 HOH   39  239 127  HOH   HOH B . 
G 5 HOH   40  240 110  HOH   HOH B . 
G 5 HOH   41  241 166  HOH   HOH B . 
G 5 HOH   42  242 252  HOH   HOH B . 
G 5 HOH   43  243 133  HOH   HOH B . 
G 5 HOH   44  244 272  HOH   HOH B . 
G 5 HOH   45  245 144  HOH   HOH B . 
G 5 HOH   46  246 60   HOH   HOH B . 
G 5 HOH   47  247 52   HOH   HOH B . 
G 5 HOH   48  248 69   HOH   HOH B . 
G 5 HOH   49  249 231  HOH   HOH B . 
G 5 HOH   50  250 31   HOH   HOH B . 
G 5 HOH   51  251 391  HOH   HOH B . 
G 5 HOH   52  252 10   HOH   HOH B . 
G 5 HOH   53  253 300  HOH   HOH B . 
G 5 HOH   54  254 9    HOH   HOH B . 
G 5 HOH   55  255 143  HOH   HOH B . 
G 5 HOH   56  256 47   HOH   HOH B . 
G 5 HOH   57  257 11   HOH   HOH B . 
G 5 HOH   58  258 59   HOH   HOH B . 
G 5 HOH   59  259 30   HOH   HOH B . 
G 5 HOH   60  260 72   HOH   HOH B . 
G 5 HOH   61  261 103  HOH   HOH B . 
G 5 HOH   62  262 221  HOH   HOH B . 
G 5 HOH   63  263 20   HOH   HOH B . 
G 5 HOH   64  264 77   HOH   HOH B . 
G 5 HOH   65  265 175  HOH   HOH B . 
G 5 HOH   66  266 302  HOH   HOH B . 
G 5 HOH   67  267 150  HOH   HOH B . 
G 5 HOH   68  268 147  HOH   HOH B . 
G 5 HOH   69  269 41   HOH   HOH B . 
G 5 HOH   70  270 347  HOH   HOH B . 
G 5 HOH   71  271 114  HOH   HOH B . 
G 5 HOH   72  272 172  HOH   HOH B . 
G 5 HOH   73  273 61   HOH   HOH B . 
G 5 HOH   74  274 271  HOH   HOH B . 
G 5 HOH   75  275 117  HOH   HOH B . 
G 5 HOH   76  276 84   HOH   HOH B . 
G 5 HOH   77  277 635  HOH   HOH B . 
G 5 HOH   78  278 242  HOH   HOH B . 
G 5 HOH   79  279 235  HOH   HOH B . 
G 5 HOH   80  280 243  HOH   HOH B . 
G 5 HOH   81  281 43   HOH   HOH B . 
G 5 HOH   82  282 88   HOH   HOH B . 
G 5 HOH   83  283 1106 HOH   HOH B . 
G 5 HOH   84  284 1277 HOH   HOH B . 
G 5 HOH   85  285 287  HOH   HOH B . 
G 5 HOH   86  286 13   HOH   HOH B . 
G 5 HOH   87  287 22   HOH   HOH B . 
G 5 HOH   88  288 416  HOH   HOH B . 
G 5 HOH   89  289 220  HOH   HOH B . 
G 5 HOH   90  290 1126 HOH   HOH B . 
G 5 HOH   91  291 1305 HOH   HOH B . 
G 5 HOH   92  292 89   HOH   HOH B . 
G 5 HOH   93  293 1066 HOH   HOH B . 
G 5 HOH   94  294 216  HOH   HOH B . 
G 5 HOH   95  295 99   HOH   HOH B . 
G 5 HOH   96  296 387  HOH   HOH B . 
G 5 HOH   97  297 137  HOH   HOH B . 
G 5 HOH   98  298 106  HOH   HOH B . 
G 5 HOH   99  299 142  HOH   HOH B . 
G 5 HOH   100 300 704  HOH   HOH B . 
G 5 HOH   101 301 299  HOH   HOH B . 
G 5 HOH   102 302 38   HOH   HOH B . 
G 5 HOH   103 303 141  HOH   HOH B . 
G 5 HOH   104 304 112  HOH   HOH B . 
G 5 HOH   105 305 160  HOH   HOH B . 
G 5 HOH   106 306 311  HOH   HOH B . 
G 5 HOH   107 307 1274 HOH   HOH B . 
G 5 HOH   108 308 32   HOH   HOH B . 
G 5 HOH   109 309 48   HOH   HOH B . 
G 5 HOH   110 310 118  HOH   HOH B . 
G 5 HOH   111 311 297  HOH   HOH B . 
G 5 HOH   112 312 215  HOH   HOH B . 
G 5 HOH   113 313 1291 HOH   HOH B . 
G 5 HOH   114 314 316  HOH   HOH B . 
G 5 HOH   115 315 341  HOH   HOH B . 
G 5 HOH   116 316 170  HOH   HOH B . 
G 5 HOH   117 317 37   HOH   HOH B . 
G 5 HOH   118 318 161  HOH   HOH B . 
G 5 HOH   119 319 100  HOH   HOH B . 
G 5 HOH   120 320 101  HOH   HOH B . 
G 5 HOH   121 321 28   HOH   HOH B . 
G 5 HOH   122 322 1285 HOH   HOH B . 
G 5 HOH   123 323 182  HOH   HOH B . 
G 5 HOH   124 324 177  HOH   HOH B . 
G 5 HOH   125 325 23   HOH   HOH B . 
G 5 HOH   126 326 334  HOH   HOH B . 
G 5 HOH   127 327 91   HOH   HOH B . 
G 5 HOH   128 328 29   HOH   HOH B . 
G 5 HOH   129 329 339  HOH   HOH B . 
G 5 HOH   130 330 44   HOH   HOH B . 
G 5 HOH   131 331 98   HOH   HOH B . 
G 5 HOH   132 332 1294 HOH   HOH B . 
G 5 HOH   133 333 197  HOH   HOH B . 
G 5 HOH   134 334 717  HOH   HOH B . 
G 5 HOH   135 335 207  HOH   HOH B . 
G 5 HOH   136 336 55   HOH   HOH B . 
G 5 HOH   137 337 234  HOH   HOH B . 
G 5 HOH   138 338 65   HOH   HOH B . 
G 5 HOH   139 339 619  HOH   HOH B . 
G 5 HOH   140 340 445  HOH   HOH B . 
G 5 HOH   141 341 1293 HOH   HOH B . 
G 5 HOH   142 342 178  HOH   HOH B . 
G 5 HOH   143 343 362  HOH   HOH B . 
G 5 HOH   144 344 90   HOH   HOH B . 
G 5 HOH   145 345 463  HOH   HOH B . 
G 5 HOH   146 346 960  HOH   HOH B . 
G 5 HOH   147 347 1304 HOH   HOH B . 
G 5 HOH   148 348 335  HOH   HOH B . 
G 5 HOH   149 349 304  HOH   HOH B . 
G 5 HOH   150 350 1046 HOH   HOH B . 
G 5 HOH   151 351 623  HOH   HOH B . 
G 5 HOH   152 352 191  HOH   HOH B . 
G 5 HOH   153 353 1280 HOH   HOH B . 
G 5 HOH   154 354 203  HOH   HOH B . 
G 5 HOH   155 355 290  HOH   HOH B . 
G 5 HOH   156 356 541  HOH   HOH B . 
G 5 HOH   157 357 479  HOH   HOH B . 
G 5 HOH   158 358 389  HOH   HOH B . 
G 5 HOH   159 359 87   HOH   HOH B . 
G 5 HOH   160 360 1077 HOH   HOH B . 
G 5 HOH   161 361 283  HOH   HOH B . 
G 5 HOH   162 362 1072 HOH   HOH B . 
G 5 HOH   163 363 718  HOH   HOH B . 
G 5 HOH   164 364 898  HOH   HOH B . 
G 5 HOH   165 365 615  HOH   HOH B . 
G 5 HOH   166 366 1316 HOH   HOH B . 
G 5 HOH   167 367 340  HOH   HOH B . 
G 5 HOH   168 368 1303 HOH   HOH B . 
G 5 HOH   169 369 291  HOH   HOH B . 
G 5 HOH   170 370 373  HOH   HOH B . 
G 5 HOH   171 371 667  HOH   HOH B . 
G 5 HOH   172 372 149  HOH   HOH B . 
G 5 HOH   173 373 190  HOH   HOH B . 
G 5 HOH   174 374 310  HOH   HOH B . 
G 5 HOH   175 375 431  HOH   HOH B . 
G 5 HOH   176 376 1173 HOH   HOH B . 
G 5 HOH   177 377 1163 HOH   HOH B . 
G 5 HOH   178 378 183  HOH   HOH B . 
G 5 HOH   179 379 1000 HOH   HOH B . 
G 5 HOH   180 380 418  HOH   HOH B . 
G 5 HOH   181 381 176  HOH   HOH B . 
G 5 HOH   182 382 424  HOH   HOH B . 
G 5 HOH   183 383 1311 HOH   HOH B . 
G 5 HOH   184 384 470  HOH   HOH B . 
G 5 HOH   185 385 248  HOH   HOH B . 
G 5 HOH   186 386 981  HOH   HOH B . 
G 5 HOH   187 387 491  HOH   HOH B . 
G 5 HOH   188 388 1298 HOH   HOH B . 
G 5 HOH   189 389 265  HOH   HOH B . 
G 5 HOH   190 390 184  HOH   HOH B . 
G 5 HOH   191 391 360  HOH   HOH B . 
G 5 HOH   192 392 355  HOH   HOH B . 
G 5 HOH   193 393 410  HOH   HOH B . 
G 5 HOH   194 394 314  HOH   HOH B . 
G 5 HOH   195 395 274  HOH   HOH B . 
G 5 HOH   196 396 566  HOH   HOH B . 
G 5 HOH   197 397 157  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           7HDX 
_cell.length_a           88.948 
_cell.length_b           88.948 
_cell.length_c           39.642 
_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                         7HDX 
_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          7HDX 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.16 
_exptl_crystal.density_percent_sol   43.07 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-20 
_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                     7HDX 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.470 
_reflns.d_resolution_high            1.080 
_reflns.number_obs                   132541 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.700 
_reflns.pdbx_Rmerge_I_obs            0.069 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        10.900 
_reflns.B_iso_Wilson_estimate        13.610 
_reflns.pdbx_redundancy              6.300 
_reflns.pdbx_Rrim_I_all              0.076 
_reflns.pdbx_Rpim_I_all              0.030 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     839453 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.080 1.100  ? 37934 6217 ? 1.969 ? ? ? 6.100 ? 0.700  ? ? ? ? ? ? 94.700 2.152 0.856 0.357 
1 2 5.920 44.470 ? 6033  889  ? 0.031 ? ? ? 6.800 ? 41.500 ? ? ? ? ? ? 99.800 0.033 0.013 0.999 
# 
_refine.entry_id                                 7HDX 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0800 
_refine.ls_d_res_low                             44.4700 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.6000 
_refine.ls_number_reflns_obs                     132419 
_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                          0.1575 
_refine.ls_R_factor_R_work                       0.1566 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1755 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8000 
_refine.ls_number_reflns_R_free                  6359 
_refine.ls_number_reflns_R_work                  126060 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.5718 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1700 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                66.270 
_refine.B_iso_min                                6.990 
_refine.pdbx_overall_phase_error                 21.2100 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0800 
_refine_hist.d_res_low                        44.4700 
_refine_hist.pdbx_number_atoms_ligand         46 
_refine_hist.number_atoms_solvent             422 
_refine_hist.number_atoms_total               3010 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           17.95 
_refine_hist.pdbx_B_iso_mean_solvent          31.42 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0800 1.0900  30 92.0000  3879 . 0.4438 0.4112 . 195 0.0000 4074 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 4167 . 0.4014 0.4025 . 211 0.0000 4378 . 'X-RAY DIFFRACTION' 
1.1100 1.1200  30 100.0000 4166 . 0.3827 0.3919 . 229 0.0000 4395 . 'X-RAY DIFFRACTION' 
1.1200 1.1300  30 100.0000 4280 . 0.3464 0.4056 . 170 0.0000 4450 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 4113 . 0.3173 0.3485 . 207 0.0000 4320 . 'X-RAY DIFFRACTION' 
1.1500 1.1600  30 100.0000 4238 . 0.2996 0.3465 . 203 0.0000 4441 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 4151 . 0.2690 0.2645 . 220 0.0000 4371 . 'X-RAY DIFFRACTION' 
1.1800 1.2000  30 100.0000 4216 . 0.2527 0.2560 . 216 0.0000 4432 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 100.0000 4157 . 0.2183 0.2633 . 233 0.0000 4390 . 'X-RAY DIFFRACTION' 
1.2200 1.2400  30 100.0000 4267 . 0.2099 0.2150 . 180 0.0000 4447 . 'X-RAY DIFFRACTION' 
1.2400 1.2600  30 100.0000 4136 . 0.2056 0.2222 . 218 0.0000 4354 . 'X-RAY DIFFRACTION' 
1.2600 1.2800  30 100.0000 4255 . 0.1971 0.2224 . 209 0.0000 4464 . 'X-RAY DIFFRACTION' 
1.2800 1.3100  30 100.0000 4158 . 0.1909 0.2059 . 193 0.0000 4351 . 'X-RAY DIFFRACTION' 
1.3100 1.3300  30 100.0000 4175 . 0.1923 0.2062 . 244 0.0000 4419 . 'X-RAY DIFFRACTION' 
1.3300 1.3600  30 100.0000 4165 . 0.1907 0.2173 . 233 0.0000 4398 . 'X-RAY DIFFRACTION' 
1.3600 1.3900  30 100.0000 4217 . 0.1759 0.2338 . 191 0.0000 4408 . 'X-RAY DIFFRACTION' 
1.3900 1.4300  30 100.0000 4244 . 0.1556 0.2113 . 207 0.0000 4451 . 'X-RAY DIFFRACTION' 
1.4300 1.4700  30 100.0000 4206 . 0.1428 0.1572 . 218 0.0000 4424 . 'X-RAY DIFFRACTION' 
1.4700 1.5100  30 100.0000 4202 . 0.1250 0.1542 . 200 0.0000 4402 . 'X-RAY DIFFRACTION' 
1.5100 1.5600  30 100.0000 4174 . 0.1184 0.1419 . 224 0.0000 4398 . 'X-RAY DIFFRACTION' 
1.5600 1.6100  30 100.0000 4227 . 0.1171 0.1570 . 220 0.0000 4447 . 'X-RAY DIFFRACTION' 
1.6100 1.6800  30 100.0000 4228 . 0.1229 0.1510 . 206 0.0000 4434 . 'X-RAY DIFFRACTION' 
1.6800 1.7500  30 100.0000 4253 . 0.1297 0.1549 . 183 0.0000 4436 . 'X-RAY DIFFRACTION' 
1.7500 1.8500  30 100.0000 4192 . 0.1292 0.1493 . 235 0.0000 4427 . 'X-RAY DIFFRACTION' 
1.8500 1.9600  30 100.0000 4242 . 0.1328 0.1399 . 215 0.0000 4457 . 'X-RAY DIFFRACTION' 
1.9600 2.1100  30 100.0000 4234 . 0.1345 0.1525 . 216 0.0000 4450 . 'X-RAY DIFFRACTION' 
2.1100 2.3300  30 100.0000 4208 . 0.1373 0.1426 . 249 0.0000 4457 . 'X-RAY DIFFRACTION' 
2.3300 2.6600  30 99.0000  4238 . 0.1413 0.1581 . 199 0.0000 4437 . 'X-RAY DIFFRACTION' 
2.6600 3.3600  30 100.0000 4292 . 0.1540 0.1755 . 208 0.0000 4500 . 'X-RAY DIFFRACTION' 
3.3600 44.4700 30 100.0000 4380 . 0.1497 0.1695 . 227 0.0000 4607 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDX 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003648' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDX 
_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 7HDX A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDX 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 7HDX SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDX MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDX SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDX 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 ? PHE A 168 ? ASP A 157 PHE A 168 1 ? 12 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HDX 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 15 ? B -143.38 13.43   
2 1 ALA A 21 ? B -170.60 149.24  
3 1 HIS A 86 ? ? 56.03   -132.67 
4 1 HIS B 86 ? ? 56.99   -126.39 
# 
_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 520 ? 5.98 . 
2 1 O ? A HOH 521 ? 6.04 . 
3 1 O ? A HOH 522 ? 7.64 . 
4 1 O ? B HOH 400 ? 6.35 . 
# 
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 
A1A86 N2   N  Y N 1   
A1A86 C3   C  N N 2   
A1A86 C6   C  N S 3   
A1A86 C9   C  Y N 4   
A1A86 C12  C  Y N 5   
A1A86 C1   C  N N 6   
A1A86 C10  C  Y N 7   
A1A86 C11  C  Y N 8   
A1A86 C13  C  Y N 9   
A1A86 C2   C  N N 10  
A1A86 C4   C  N N 11  
A1A86 C5   C  N N 12  
A1A86 C7   C  N N 13  
A1A86 C8   C  Y N 14  
A1A86 N1   N  N N 15  
A1A86 N3   N  Y N 16  
A1A86 N4   N  Y N 17  
A1A86 O1   O  N N 18  
A1A86 H7   H  N N 19  
A1A86 H6   H  N N 20  
A1A86 H5   H  N N 21  
A1A86 H1   H  N N 22  
A1A86 H17  H  N N 23  
A1A86 H18  H  N N 24  
A1A86 H2   H  N N 25  
A1A86 H4   H  N N 26  
A1A86 H3   H  N N 27  
A1A86 H19  H  N N 28  
A1A86 H9   H  N N 29  
A1A86 H8   H  N N 30  
A1A86 H10  H  N N 31  
A1A86 H12  H  N N 32  
A1A86 H11  H  N N 33  
A1A86 H13  H  N N 34  
A1A86 H14  H  N N 35  
A1A86 H16  H  N N 36  
A1A86 H20  H  N N 37  
A1A86 H15  H  N N 38  
ALA   N    N  N N 39  
ALA   CA   C  N S 40  
ALA   C    C  N N 41  
ALA   O    O  N N 42  
ALA   CB   C  N N 43  
ALA   OXT  O  N N 44  
ALA   H    H  N N 45  
ALA   H2   H  N N 46  
ALA   HA   H  N N 47  
ALA   HB1  H  N N 48  
ALA   HB2  H  N N 49  
ALA   HB3  H  N N 50  
ALA   HXT  H  N N 51  
ARG   N    N  N N 52  
ARG   CA   C  N S 53  
ARG   C    C  N N 54  
ARG   O    O  N N 55  
ARG   CB   C  N N 56  
ARG   CG   C  N N 57  
ARG   CD   C  N N 58  
ARG   NE   N  N N 59  
ARG   CZ   C  N N 60  
ARG   NH1  N  N N 61  
ARG   NH2  N  N N 62  
ARG   OXT  O  N N 63  
ARG   H    H  N N 64  
ARG   H2   H  N N 65  
ARG   HA   H  N N 66  
ARG   HB2  H  N N 67  
ARG   HB3  H  N N 68  
ARG   HG2  H  N N 69  
ARG   HG3  H  N N 70  
ARG   HD2  H  N N 71  
ARG   HD3  H  N N 72  
ARG   HE   H  N N 73  
ARG   HH11 H  N N 74  
ARG   HH12 H  N N 75  
ARG   HH21 H  N N 76  
ARG   HH22 H  N N 77  
ARG   HXT  H  N N 78  
ASN   N    N  N N 79  
ASN   CA   C  N S 80  
ASN   C    C  N N 81  
ASN   O    O  N N 82  
ASN   CB   C  N N 83  
ASN   CG   C  N N 84  
ASN   OD1  O  N N 85  
ASN   ND2  N  N N 86  
ASN   OXT  O  N N 87  
ASN   H    H  N N 88  
ASN   H2   H  N N 89  
ASN   HA   H  N N 90  
ASN   HB2  H  N N 91  
ASN   HB3  H  N N 92  
ASN   HD21 H  N N 93  
ASN   HD22 H  N N 94  
ASN   HXT  H  N N 95  
ASP   N    N  N N 96  
ASP   CA   C  N S 97  
ASP   C    C  N N 98  
ASP   O    O  N N 99  
ASP   CB   C  N N 100 
ASP   CG   C  N N 101 
ASP   OD1  O  N N 102 
ASP   OD2  O  N N 103 
ASP   OXT  O  N N 104 
ASP   H    H  N N 105 
ASP   H2   H  N N 106 
ASP   HA   H  N N 107 
ASP   HB2  H  N N 108 
ASP   HB3  H  N N 109 
ASP   HD2  H  N N 110 
ASP   HXT  H  N N 111 
CL    CL   CL N N 112 
CYS   N    N  N N 113 
CYS   CA   C  N R 114 
CYS   C    C  N N 115 
CYS   O    O  N N 116 
CYS   CB   C  N N 117 
CYS   SG   S  N N 118 
CYS   OXT  O  N N 119 
CYS   H    H  N N 120 
CYS   H2   H  N N 121 
CYS   HA   H  N N 122 
CYS   HB2  H  N N 123 
CYS   HB3  H  N N 124 
CYS   HG   H  N N 125 
CYS   HXT  H  N N 126 
GLN   N    N  N N 127 
GLN   CA   C  N S 128 
GLN   C    C  N N 129 
GLN   O    O  N N 130 
GLN   CB   C  N N 131 
GLN   CG   C  N N 132 
GLN   CD   C  N N 133 
GLN   OE1  O  N N 134 
GLN   NE2  N  N N 135 
GLN   OXT  O  N N 136 
GLN   H    H  N N 137 
GLN   H2   H  N N 138 
GLN   HA   H  N N 139 
GLN   HB2  H  N N 140 
GLN   HB3  H  N N 141 
GLN   HG2  H  N N 142 
GLN   HG3  H  N N 143 
GLN   HE21 H  N N 144 
GLN   HE22 H  N N 145 
GLN   HXT  H  N N 146 
GLU   N    N  N N 147 
GLU   CA   C  N S 148 
GLU   C    C  N N 149 
GLU   O    O  N N 150 
GLU   CB   C  N N 151 
GLU   CG   C  N N 152 
GLU   CD   C  N N 153 
GLU   OE1  O  N N 154 
GLU   OE2  O  N N 155 
GLU   OXT  O  N N 156 
GLU   H    H  N N 157 
GLU   H2   H  N N 158 
GLU   HA   H  N N 159 
GLU   HB2  H  N N 160 
GLU   HB3  H  N N 161 
GLU   HG2  H  N N 162 
GLU   HG3  H  N N 163 
GLU   HE2  H  N N 164 
GLU   HXT  H  N N 165 
GLY   N    N  N N 166 
GLY   CA   C  N N 167 
GLY   C    C  N N 168 
GLY   O    O  N N 169 
GLY   OXT  O  N N 170 
GLY   H    H  N N 171 
GLY   H2   H  N N 172 
GLY   HA2  H  N N 173 
GLY   HA3  H  N N 174 
GLY   HXT  H  N N 175 
HIS   N    N  N N 176 
HIS   CA   C  N S 177 
HIS   C    C  N N 178 
HIS   O    O  N N 179 
HIS   CB   C  N N 180 
HIS   CG   C  Y N 181 
HIS   ND1  N  Y N 182 
HIS   CD2  C  Y N 183 
HIS   CE1  C  Y N 184 
HIS   NE2  N  Y N 185 
HIS   OXT  O  N N 186 
HIS   H    H  N N 187 
HIS   H2   H  N N 188 
HIS   HA   H  N N 189 
HIS   HB2  H  N N 190 
HIS   HB3  H  N N 191 
HIS   HD1  H  N N 192 
HIS   HD2  H  N N 193 
HIS   HE1  H  N N 194 
HIS   HE2  H  N N 195 
HIS   HXT  H  N N 196 
HOH   O    O  N N 197 
HOH   H1   H  N N 198 
HOH   H2   H  N N 199 
ILE   N    N  N N 200 
ILE   CA   C  N S 201 
ILE   C    C  N N 202 
ILE   O    O  N N 203 
ILE   CB   C  N S 204 
ILE   CG1  C  N N 205 
ILE   CG2  C  N N 206 
ILE   CD1  C  N N 207 
ILE   OXT  O  N N 208 
ILE   H    H  N N 209 
ILE   H2   H  N N 210 
ILE   HA   H  N N 211 
ILE   HB   H  N N 212 
ILE   HG12 H  N N 213 
ILE   HG13 H  N N 214 
ILE   HG21 H  N N 215 
ILE   HG22 H  N N 216 
ILE   HG23 H  N N 217 
ILE   HD11 H  N N 218 
ILE   HD12 H  N N 219 
ILE   HD13 H  N N 220 
ILE   HXT  H  N N 221 
LEU   N    N  N N 222 
LEU   CA   C  N S 223 
LEU   C    C  N N 224 
LEU   O    O  N N 225 
LEU   CB   C  N N 226 
LEU   CG   C  N N 227 
LEU   CD1  C  N N 228 
LEU   CD2  C  N N 229 
LEU   OXT  O  N N 230 
LEU   H    H  N N 231 
LEU   H2   H  N N 232 
LEU   HA   H  N N 233 
LEU   HB2  H  N N 234 
LEU   HB3  H  N N 235 
LEU   HG   H  N N 236 
LEU   HD11 H  N N 237 
LEU   HD12 H  N N 238 
LEU   HD13 H  N N 239 
LEU   HD21 H  N N 240 
LEU   HD22 H  N N 241 
LEU   HD23 H  N N 242 
LEU   HXT  H  N N 243 
LYS   N    N  N N 244 
LYS   CA   C  N S 245 
LYS   C    C  N N 246 
LYS   O    O  N N 247 
LYS   CB   C  N N 248 
LYS   CG   C  N N 249 
LYS   CD   C  N N 250 
LYS   CE   C  N N 251 
LYS   NZ   N  N N 252 
LYS   OXT  O  N N 253 
LYS   H    H  N N 254 
LYS   H2   H  N N 255 
LYS   HA   H  N N 256 
LYS   HB2  H  N N 257 
LYS   HB3  H  N N 258 
LYS   HG2  H  N N 259 
LYS   HG3  H  N N 260 
LYS   HD2  H  N N 261 
LYS   HD3  H  N N 262 
LYS   HE2  H  N N 263 
LYS   HE3  H  N N 264 
LYS   HZ1  H  N N 265 
LYS   HZ2  H  N N 266 
LYS   HZ3  H  N N 267 
LYS   HXT  H  N N 268 
MET   N    N  N N 269 
MET   CA   C  N S 270 
MET   C    C  N N 271 
MET   O    O  N N 272 
MET   CB   C  N N 273 
MET   CG   C  N N 274 
MET   SD   S  N N 275 
MET   CE   C  N N 276 
MET   OXT  O  N N 277 
MET   H    H  N N 278 
MET   H2   H  N N 279 
MET   HA   H  N N 280 
MET   HB2  H  N N 281 
MET   HB3  H  N N 282 
MET   HG2  H  N N 283 
MET   HG3  H  N N 284 
MET   HE1  H  N N 285 
MET   HE2  H  N N 286 
MET   HE3  H  N N 287 
MET   HXT  H  N N 288 
PHE   N    N  N N 289 
PHE   CA   C  N S 290 
PHE   C    C  N N 291 
PHE   O    O  N N 292 
PHE   CB   C  N N 293 
PHE   CG   C  Y N 294 
PHE   CD1  C  Y N 295 
PHE   CD2  C  Y N 296 
PHE   CE1  C  Y N 297 
PHE   CE2  C  Y N 298 
PHE   CZ   C  Y N 299 
PHE   OXT  O  N N 300 
PHE   H    H  N N 301 
PHE   H2   H  N N 302 
PHE   HA   H  N N 303 
PHE   HB2  H  N N 304 
PHE   HB3  H  N N 305 
PHE   HD1  H  N N 306 
PHE   HD2  H  N N 307 
PHE   HE1  H  N N 308 
PHE   HE2  H  N N 309 
PHE   HZ   H  N N 310 
PHE   HXT  H  N N 311 
PRO   N    N  N N 312 
PRO   CA   C  N S 313 
PRO   C    C  N N 314 
PRO   O    O  N N 315 
PRO   CB   C  N N 316 
PRO   CG   C  N N 317 
PRO   CD   C  N N 318 
PRO   OXT  O  N N 319 
PRO   H    H  N N 320 
PRO   HA   H  N N 321 
PRO   HB2  H  N N 322 
PRO   HB3  H  N N 323 
PRO   HG2  H  N N 324 
PRO   HG3  H  N N 325 
PRO   HD2  H  N N 326 
PRO   HD3  H  N N 327 
PRO   HXT  H  N N 328 
SER   N    N  N N 329 
SER   CA   C  N S 330 
SER   C    C  N N 331 
SER   O    O  N N 332 
SER   CB   C  N N 333 
SER   OG   O  N N 334 
SER   OXT  O  N N 335 
SER   H    H  N N 336 
SER   H2   H  N N 337 
SER   HA   H  N N 338 
SER   HB2  H  N N 339 
SER   HB3  H  N N 340 
SER   HG   H  N N 341 
SER   HXT  H  N N 342 
TFA   C1   C  N N 343 
TFA   C2   C  N N 344 
TFA   O    O  N N 345 
TFA   F1   F  N N 346 
TFA   F2   F  N N 347 
TFA   F3   F  N N 348 
TFA   OXT  O  N N 349 
TFA   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TYR   N    N  N N 368 
TYR   CA   C  N S 369 
TYR   C    C  N N 370 
TYR   O    O  N N 371 
TYR   CB   C  N N 372 
TYR   CG   C  Y N 373 
TYR   CD1  C  Y N 374 
TYR   CD2  C  Y N 375 
TYR   CE1  C  Y N 376 
TYR   CE2  C  Y N 377 
TYR   CZ   C  Y N 378 
TYR   OH   O  N N 379 
TYR   OXT  O  N N 380 
TYR   H    H  N N 381 
TYR   H2   H  N N 382 
TYR   HA   H  N N 383 
TYR   HB2  H  N N 384 
TYR   HB3  H  N N 385 
TYR   HD1  H  N N 386 
TYR   HD2  H  N N 387 
TYR   HE1  H  N N 388 
TYR   HE2  H  N N 389 
TYR   HH   H  N N 390 
TYR   HXT  H  N N 391 
VAL   N    N  N N 392 
VAL   CA   C  N S 393 
VAL   C    C  N N 394 
VAL   O    O  N N 395 
VAL   CB   C  N N 396 
VAL   CG1  C  N N 397 
VAL   CG2  C  N N 398 
VAL   OXT  O  N N 399 
VAL   H    H  N N 400 
VAL   H2   H  N N 401 
VAL   HA   H  N N 402 
VAL   HB   H  N N 403 
VAL   HG11 H  N N 404 
VAL   HG12 H  N N 405 
VAL   HG13 H  N N 406 
VAL   HG21 H  N N 407 
VAL   HG22 H  N N 408 
VAL   HG23 H  N N 409 
VAL   HXT  H  N N 410 
# 
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 
A1A86 C4  C2   sing N N 1   
A1A86 C5  C2   sing N N 2   
A1A86 C5  C6   sing N N 3   
A1A86 C7  O1   sing N N 4   
A1A86 C7  C6   sing N N 5   
A1A86 C2  C1   sing N N 6   
A1A86 C2  C3   sing N N 7   
A1A86 C6  N1   sing N N 8   
A1A86 N1  C8   sing N N 9   
A1A86 C8  C11  doub Y N 10  
A1A86 C8  N2   sing Y N 11  
A1A86 C12 C11  sing Y N 12  
A1A86 C12 C13  doub Y N 13  
A1A86 C11 C10  sing Y N 14  
A1A86 N2  C9   doub Y N 15  
A1A86 C13 N4   sing Y N 16  
A1A86 C10 N4   sing Y N 17  
A1A86 C10 N3   doub Y N 18  
A1A86 C9  N3   sing Y N 19  
A1A86 C3  H7   sing N N 20  
A1A86 C3  H6   sing N N 21  
A1A86 C3  H5   sing N N 22  
A1A86 C6  H1   sing N N 23  
A1A86 C9  H17  sing N N 24  
A1A86 C12 H18  sing N N 25  
A1A86 C1  H2   sing N N 26  
A1A86 C1  H4   sing N N 27  
A1A86 C1  H3   sing N N 28  
A1A86 C13 H19  sing N N 29  
A1A86 C4  H9   sing N N 30  
A1A86 C4  H8   sing N N 31  
A1A86 C4  H10  sing N N 32  
A1A86 C5  H12  sing N N 33  
A1A86 C5  H11  sing N N 34  
A1A86 C7  H13  sing N N 35  
A1A86 C7  H14  sing N N 36  
A1A86 N1  H16  sing N N 37  
A1A86 N4  H20  sing N N 38  
A1A86 O1  H15  sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
GLN   N   CA   sing N N 122 
GLN   N   H    sing N N 123 
GLN   N   H2   sing N N 124 
GLN   CA  C    sing N N 125 
GLN   CA  CB   sing N N 126 
GLN   CA  HA   sing N N 127 
GLN   C   O    doub N N 128 
GLN   C   OXT  sing N N 129 
GLN   CB  CG   sing N N 130 
GLN   CB  HB2  sing N N 131 
GLN   CB  HB3  sing N N 132 
GLN   CG  CD   sing N N 133 
GLN   CG  HG2  sing N N 134 
GLN   CG  HG3  sing N N 135 
GLN   CD  OE1  doub N N 136 
GLN   CD  NE2  sing N N 137 
GLN   NE2 HE21 sing N N 138 
GLN   NE2 HE22 sing N N 139 
GLN   OXT HXT  sing N N 140 
GLU   N   CA   sing N N 141 
GLU   N   H    sing N N 142 
GLU   N   H2   sing N N 143 
GLU   CA  C    sing N N 144 
GLU   CA  CB   sing N N 145 
GLU   CA  HA   sing N N 146 
GLU   C   O    doub N N 147 
GLU   C   OXT  sing N N 148 
GLU   CB  CG   sing N N 149 
GLU   CB  HB2  sing N N 150 
GLU   CB  HB3  sing N N 151 
GLU   CG  CD   sing N N 152 
GLU   CG  HG2  sing N N 153 
GLU   CG  HG3  sing N N 154 
GLU   CD  OE1  doub N N 155 
GLU   CD  OE2  sing N N 156 
GLU   OE2 HE2  sing N N 157 
GLU   OXT HXT  sing N N 158 
GLY   N   CA   sing N N 159 
GLY   N   H    sing N N 160 
GLY   N   H2   sing N N 161 
GLY   CA  C    sing N N 162 
GLY   CA  HA2  sing N N 163 
GLY   CA  HA3  sing N N 164 
GLY   C   O    doub N N 165 
GLY   C   OXT  sing N N 166 
GLY   OXT HXT  sing N N 167 
HIS   N   CA   sing N N 168 
HIS   N   H    sing N N 169 
HIS   N   H2   sing N N 170 
HIS   CA  C    sing N N 171 
HIS   CA  CB   sing N N 172 
HIS   CA  HA   sing N N 173 
HIS   C   O    doub N N 174 
HIS   C   OXT  sing N N 175 
HIS   CB  CG   sing N N 176 
HIS   CB  HB2  sing N N 177 
HIS   CB  HB3  sing N N 178 
HIS   CG  ND1  sing Y N 179 
HIS   CG  CD2  doub Y N 180 
HIS   ND1 CE1  doub Y N 181 
HIS   ND1 HD1  sing N N 182 
HIS   CD2 NE2  sing Y N 183 
HIS   CD2 HD2  sing N N 184 
HIS   CE1 NE2  sing Y N 185 
HIS   CE1 HE1  sing N N 186 
HIS   NE2 HE2  sing N N 187 
HIS   OXT HXT  sing N N 188 
HOH   O   H1   sing N N 189 
HOH   O   H2   sing N N 190 
ILE   N   CA   sing N N 191 
ILE   N   H    sing N N 192 
ILE   N   H2   sing N N 193 
ILE   CA  C    sing N N 194 
ILE   CA  CB   sing N N 195 
ILE   CA  HA   sing N N 196 
ILE   C   O    doub N N 197 
ILE   C   OXT  sing N N 198 
ILE   CB  CG1  sing N N 199 
ILE   CB  CG2  sing N N 200 
ILE   CB  HB   sing N N 201 
ILE   CG1 CD1  sing N N 202 
ILE   CG1 HG12 sing N N 203 
ILE   CG1 HG13 sing N N 204 
ILE   CG2 HG21 sing N N 205 
ILE   CG2 HG22 sing N N 206 
ILE   CG2 HG23 sing N N 207 
ILE   CD1 HD11 sing N N 208 
ILE   CD1 HD12 sing N N 209 
ILE   CD1 HD13 sing N N 210 
ILE   OXT HXT  sing N N 211 
LEU   N   CA   sing N N 212 
LEU   N   H    sing N N 213 
LEU   N   H2   sing N N 214 
LEU   CA  C    sing N N 215 
LEU   CA  CB   sing N N 216 
LEU   CA  HA   sing N N 217 
LEU   C   O    doub N N 218 
LEU   C   OXT  sing N N 219 
LEU   CB  CG   sing N N 220 
LEU   CB  HB2  sing N N 221 
LEU   CB  HB3  sing N N 222 
LEU   CG  CD1  sing N N 223 
LEU   CG  CD2  sing N N 224 
LEU   CG  HG   sing N N 225 
LEU   CD1 HD11 sing N N 226 
LEU   CD1 HD12 sing N N 227 
LEU   CD1 HD13 sing N N 228 
LEU   CD2 HD21 sing N N 229 
LEU   CD2 HD22 sing N N 230 
LEU   CD2 HD23 sing N N 231 
LEU   OXT HXT  sing N N 232 
LYS   N   CA   sing N N 233 
LYS   N   H    sing N N 234 
LYS   N   H2   sing N N 235 
LYS   CA  C    sing N N 236 
LYS   CA  CB   sing N N 237 
LYS   CA  HA   sing N N 238 
LYS   C   O    doub N N 239 
LYS   C   OXT  sing N N 240 
LYS   CB  CG   sing N N 241 
LYS   CB  HB2  sing N N 242 
LYS   CB  HB3  sing N N 243 
LYS   CG  CD   sing N N 244 
LYS   CG  HG2  sing N N 245 
LYS   CG  HG3  sing N N 246 
LYS   CD  CE   sing N N 247 
LYS   CD  HD2  sing N N 248 
LYS   CD  HD3  sing N N 249 
LYS   CE  NZ   sing N N 250 
LYS   CE  HE2  sing N N 251 
LYS   CE  HE3  sing N N 252 
LYS   NZ  HZ1  sing N N 253 
LYS   NZ  HZ2  sing N N 254 
LYS   NZ  HZ3  sing N N 255 
LYS   OXT HXT  sing N N 256 
MET   N   CA   sing N N 257 
MET   N   H    sing N N 258 
MET   N   H2   sing N N 259 
MET   CA  C    sing N N 260 
MET   CA  CB   sing N N 261 
MET   CA  HA   sing N N 262 
MET   C   O    doub N N 263 
MET   C   OXT  sing N N 264 
MET   CB  CG   sing N N 265 
MET   CB  HB2  sing N N 266 
MET   CB  HB3  sing N N 267 
MET   CG  SD   sing N N 268 
MET   CG  HG2  sing N N 269 
MET   CG  HG3  sing N N 270 
MET   SD  CE   sing N N 271 
MET   CE  HE1  sing N N 272 
MET   CE  HE2  sing N N 273 
MET   CE  HE3  sing N N 274 
MET   OXT HXT  sing N N 275 
PHE   N   CA   sing N N 276 
PHE   N   H    sing N N 277 
PHE   N   H2   sing N N 278 
PHE   CA  C    sing N N 279 
PHE   CA  CB   sing N N 280 
PHE   CA  HA   sing N N 281 
PHE   C   O    doub N N 282 
PHE   C   OXT  sing N N 283 
PHE   CB  CG   sing N N 284 
PHE   CB  HB2  sing N N 285 
PHE   CB  HB3  sing N N 286 
PHE   CG  CD1  doub Y N 287 
PHE   CG  CD2  sing Y N 288 
PHE   CD1 CE1  sing Y N 289 
PHE   CD1 HD1  sing N N 290 
PHE   CD2 CE2  doub Y N 291 
PHE   CD2 HD2  sing N N 292 
PHE   CE1 CZ   doub Y N 293 
PHE   CE1 HE1  sing N N 294 
PHE   CE2 CZ   sing Y N 295 
PHE   CE2 HE2  sing N N 296 
PHE   CZ  HZ   sing N N 297 
PHE   OXT HXT  sing N N 298 
PRO   N   CA   sing N N 299 
PRO   N   CD   sing N N 300 
PRO   N   H    sing N N 301 
PRO   CA  C    sing N N 302 
PRO   CA  CB   sing N N 303 
PRO   CA  HA   sing N N 304 
PRO   C   O    doub N N 305 
PRO   C   OXT  sing N N 306 
PRO   CB  CG   sing N N 307 
PRO   CB  HB2  sing N N 308 
PRO   CB  HB3  sing N N 309 
PRO   CG  CD   sing N N 310 
PRO   CG  HG2  sing N N 311 
PRO   CG  HG3  sing N N 312 
PRO   CD  HD2  sing N N 313 
PRO   CD  HD3  sing N N 314 
PRO   OXT HXT  sing N N 315 
SER   N   CA   sing N N 316 
SER   N   H    sing N N 317 
SER   N   H2   sing N N 318 
SER   CA  C    sing N N 319 
SER   CA  CB   sing N N 320 
SER   CA  HA   sing N N 321 
SER   C   O    doub N N 322 
SER   C   OXT  sing N N 323 
SER   CB  OG   sing N N 324 
SER   CB  HB2  sing N N 325 
SER   CB  HB3  sing N N 326 
SER   OG  HG   sing N N 327 
SER   OXT HXT  sing N N 328 
TFA   C1  C2   sing N N 329 
TFA   C1  O    doub N N 330 
TFA   C1  OXT  sing N N 331 
TFA   C2  F1   sing N N 332 
TFA   C2  F2   sing N N 333 
TFA   C2  F3   sing N N 334 
TFA   OXT HXT  sing N N 335 
THR   N   CA   sing N N 336 
THR   N   H    sing N N 337 
THR   N   H2   sing N N 338 
THR   CA  C    sing N N 339 
THR   CA  CB   sing N N 340 
THR   CA  HA   sing N N 341 
THR   C   O    doub N N 342 
THR   C   OXT  sing N N 343 
THR   CB  OG1  sing N N 344 
THR   CB  CG2  sing N N 345 
THR   CB  HB   sing N N 346 
THR   OG1 HG1  sing N N 347 
THR   CG2 HG21 sing N N 348 
THR   CG2 HG22 sing N N 349 
THR   CG2 HG23 sing N N 350 
THR   OXT HXT  sing N N 351 
TYR   N   CA   sing N N 352 
TYR   N   H    sing N N 353 
TYR   N   H2   sing N N 354 
TYR   CA  C    sing N N 355 
TYR   CA  CB   sing N N 356 
TYR   CA  HA   sing N N 357 
TYR   C   O    doub N N 358 
TYR   C   OXT  sing N N 359 
TYR   CB  CG   sing N N 360 
TYR   CB  HB2  sing N N 361 
TYR   CB  HB3  sing N N 362 
TYR   CG  CD1  doub Y N 363 
TYR   CG  CD2  sing Y N 364 
TYR   CD1 CE1  sing Y N 365 
TYR   CD1 HD1  sing N N 366 
TYR   CD2 CE2  doub Y N 367 
TYR   CD2 HD2  sing N N 368 
TYR   CE1 CZ   doub Y N 369 
TYR   CE1 HE1  sing N N 370 
TYR   CE2 CZ   sing Y N 371 
TYR   CE2 HE2  sing N N 372 
TYR   CZ  OH   sing N N 373 
TYR   OH  HH   sing N N 374 
TYR   OXT HXT  sing N N 375 
VAL   N   CA   sing N N 376 
VAL   N   H    sing N N 377 
VAL   N   H2   sing N N 378 
VAL   CA  C    sing N N 379 
VAL   CA  CB   sing N N 380 
VAL   CA  HA   sing N N 381 
VAL   C   O    doub N N 382 
VAL   C   OXT  sing N N 383 
VAL   CB  CG1  sing N N 384 
VAL   CB  CG2  sing N N 385 
VAL   CB  HB   sing N N 386 
VAL   CG1 HG11 sing N N 387 
VAL   CG1 HG12 sing N N 388 
VAL   CG1 HG13 sing N N 389 
VAL   CG2 HG21 sing N N 390 
VAL   CG2 HG22 sing N N 391 
VAL   CG2 HG23 sing N N 392 
VAL   OXT HXT  sing N N 393 
# 
_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                    7HDX 
_atom_sites.fract_transf_matrix[1][1]   0.011243 
_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]   0.011243 
_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]   0.025226 
_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 
F  
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   ? 19.720 -16.313 22.252  0.74 51.22 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.627 -16.281 22.370  0.26 50.50 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.755 -15.236 22.446  0.74 50.81 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.692 -15.179 22.561  0.26 50.20 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.403 -13.886 22.155  0.74 49.22 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.362 -13.853 22.228  0.26 48.97 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.537 -13.632 22.560  0.74 49.37 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.478 -13.583 22.670  0.26 49.25 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.141 -15.280 23.862  0.74 51.66 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.124 -15.168 23.994  0.26 50.83 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.129 -14.155 24.045  0.74 51.87 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.144 -14.014 24.170  0.26 51.06 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.489 -16.633 24.113  0.74 51.96 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.454 -16.497 24.312  0.26 51.07 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 18.030 -15.349 21.815  0.74 60.98 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.946 -15.291 21.954  0.26 60.24 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.844 -15.160 24.519  0.74 61.99 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.851 -15.040 24.622  0.26 61.01 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.633 -14.309 24.865  0.74 62.26 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.663 -14.135 25.003  0.26 61.28 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.600 -13.309 24.100  0.74 62.26 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.636 -13.179 24.192  0.26 61.28 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.522 -14.150 23.289  0.74 62.26 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.521 -14.013 23.427  0.26 61.28 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 17.051 -16.617 24.979  0.74 62.36 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 17.045 -16.441 25.190  0.26 61.29 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.835 -16.802 23.416  0.74 62.36 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.776 -16.676 23.642  0.26 61.29 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.172 -17.321 24.100  0.74 62.36 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.124 -17.198 24.303  0.26 61.29 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.675 -13.028 21.440  1.00 47.00 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.133 -11.683 21.116  1.00 42.53 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 17.979 -10.707 21.332  1.00 39.17 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.856 -11.104 21.660  1.00 38.15 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.716 -11.602 19.697  1.00 41.28 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.709 -11.957 18.627  1.00 40.00 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.613 -11.397 18.580  1.00 39.26 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 19.077 -12.892 17.754  1.00 39.64 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.897 -13.211 21.121  0.74 56.40 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.922 -13.231 21.075  0.26 56.40 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.841 -11.442 21.728  1.00 51.04 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 20.020 -10.695 19.531  1.00 49.54 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.461 -12.218 19.625  1.00 49.54 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.543 -13.130 17.123  1.00 47.57 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.854 -13.259 17.818  1.00 47.57 ?  4   ASN   A HD22 1 
ATOM   46   N  N    . SER   A 1 5   ? 18.259 -9.417  21.139  1.00 36.32 ?  5   SER   A N    1 
ATOM   47   C  CA   . SER   A 1 5   ? 17.343 -8.349  21.520  1.00 34.01 ?  5   SER   A CA   1 
ATOM   48   C  C    . SER   A 1 5   ? 16.466 -7.853  20.371  1.00 30.76 ?  5   SER   A C    1 
ATOM   49   O  O    . SER   A 1 5   ? 15.747 -6.862  20.541  1.00 31.33 ?  5   SER   A O    1 
ATOM   50   C  CB   . SER   A 1 5   ? 18.118 -7.181  22.132  1.00 35.14 ?  5   SER   A CB   1 
ATOM   51   O  OG   . SER   A 1 5   ? 19.040 -6.643  21.201  1.00 35.75 ?  5   SER   A OG   1 
ATOM   52   H  H    . SER   A 1 5   ? 18.990 -9.135  20.781  1.00 43.59 ?  5   SER   A H    1 
ATOM   53   H  HA   . SER   A 1 5   ? 16.753 -8.687  22.208  1.00 40.82 ?  5   SER   A HA   1 
ATOM   54   H  HB2  . SER   A 1 5   ? 17.493 -6.486  22.392  1.00 42.18 ?  5   SER   A HB2  1 
ATOM   55   H  HB3  . SER   A 1 5   ? 18.604 -7.495  22.913  1.00 42.18 ?  5   SER   A HB3  1 
ATOM   56   H  HG   . SER   A 1 5   ? 19.461 -6.002  21.551  1.00 42.91 ?  5   SER   A HG   1 
ATOM   57   N  N    . PHE   A 1 6   ? 16.496 -8.511  19.215  1.00 26.73 ?  6   PHE   A N    1 
ATOM   58   C  CA   . PHE   A 1 6   ? 15.599 -8.135  18.128  1.00 22.81 ?  6   PHE   A CA   1 
ATOM   59   C  C    . PHE   A 1 6   ? 14.161 -8.497  18.493  1.00 23.77 ?  6   PHE   A C    1 
ATOM   60   O  O    . PHE   A 1 6   ? 13.888 -9.613  18.942  1.00 25.05 ?  6   PHE   A O    1 
ATOM   61   C  CB   . PHE   A 1 6   ? 16.004 -8.854  16.844  1.00 20.55 ?  6   PHE   A CB   1 
ATOM   62   C  CG   . PHE   A 1 6   ? 17.284 -8.339  16.237  1.00 19.39 ?  6   PHE   A CG   1 
ATOM   63   C  CD1  . PHE   A 1 6   ? 17.295 -7.165  15.508  1.00 19.33 ?  6   PHE   A CD1  1 
ATOM   64   C  CD2  . PHE   A 1 6   ? 18.469 -9.036  16.388  1.00 20.25 ?  6   PHE   A CD2  1 
ATOM   65   C  CE1  . PHE   A 1 6   ? 18.475 -6.686  14.948  1.00 19.90 ?  6   PHE   A CE1  1 
ATOM   66   C  CE2  . PHE   A 1 6   ? 19.645 -8.565  15.832  1.00 20.86 ?  6   PHE   A CE2  1 
ATOM   67   C  CZ   . PHE   A 1 6   ? 19.649 -7.389  15.110  1.00 20.36 ?  6   PHE   A CZ   1 
ATOM   68   H  H    . PHE   A 1 6   ? 17.016 -9.175  19.040  1.00 32.08 ?  6   PHE   A H    1 
ATOM   69   H  HA   . PHE   A 1 6   ? 15.651 -7.180  17.981  1.00 27.37 ?  6   PHE   A HA   1 
ATOM   70   H  HB2  . PHE   A 1 6   ? 16.127 -9.799  17.041  1.00 24.67 ?  6   PHE   A HB2  1 
ATOM   71   H  HB3  . PHE   A 1 6   ? 15.298 -8.747  16.190  1.00 24.67 ?  6   PHE   A HB3  1 
ATOM   72   H  HD1  . PHE   A 1 6   ? 16.507 -6.687  15.396  1.00 23.20 ?  6   PHE   A HD1  1 
ATOM   73   H  HD2  . PHE   A 1 6   ? 18.475 -9.829  16.879  1.00 24.30 ?  6   PHE   A HD2  1 
ATOM   74   H  HE1  . PHE   A 1 6   ? 18.476 -5.894  14.460  1.00 23.88 ?  6   PHE   A HE1  1 
ATOM   75   H  HE2  . PHE   A 1 6   ? 20.438 -9.042  15.947  1.00 25.04 ?  6   PHE   A HE2  1 
ATOM   76   H  HZ   . PHE   A 1 6   ? 20.440 -7.071  14.736  1.00 24.44 ?  6   PHE   A HZ   1 
ATOM   77   N  N    . SER   A 1 7   ? 13.235 -7.559  18.281  1.00 23.11 ?  7   SER   A N    1 
ATOM   78   C  CA   . SER   A 1 7   ? 11.868 -7.694  18.770  1.00 24.39 ?  7   SER   A CA   1 
ATOM   79   C  C    . SER   A 1 7   ? 10.864 -7.438  17.654  1.00 22.35 ?  7   SER   A C    1 
ATOM   80   O  O    . SER   A 1 7   ? 11.070 -6.559  16.810  1.00 22.53 ?  7   SER   A O    1 
ATOM   81   C  CB   . SER   A 1 7   ? 11.620 -6.710  19.922  1.00 27.60 ?  7   SER   A CB   1 
ATOM   82   O  OG   . SER   A 1 7   ? 10.300 -6.810  20.407  1.00 30.47 ?  7   SER   A OG   1 
ATOM   83   H  H    . SER   A 1 7   ? 13.379 -6.832  17.842  1.00 27.74 ?  7   SER   A H    1 
ATOM   84   H  HA   . SER   A 1 7   ? 11.731 -8.595  19.103  1.00 29.28 ?  7   SER   A HA   1 
ATOM   85   H  HB2  . SER   A 1 7   ? 12.239 -6.909  20.643  1.00 33.13 ?  7   SER   A HB2  1 
ATOM   86   H  HB3  . SER   A 1 7   ? 11.770 -5.807  19.601  1.00 33.13 ?  7   SER   A HB3  1 
ATOM   87   H  HG   . SER   A 1 7   ? 10.182 -6.267  21.039  1.00 36.57 ?  7   SER   A HG   1 
ATOM   88   N  N    . GLY   A 1 8   ? 9.772  -8.210  17.658  1.00 21.22 ?  8   GLY   A N    1 
ATOM   89   C  CA   . GLY   A 1 8   ? 8.681  -7.976  16.735  1.00 20.90 ?  8   GLY   A CA   1 
ATOM   90   C  C    . GLY   A 1 8   ? 8.888  -8.487  15.329  1.00 18.79 ?  8   GLY   A C    1 
ATOM   91   O  O    . GLY   A 1 8   ? 8.133  -8.098  14.429  1.00 19.08 ?  8   GLY   A O    1 
ATOM   92   H  H    . GLY   A 1 8   ? 9.641  -8.878  18.191  1.00 25.47 ?  8   GLY   A H    1 
ATOM   93   H  HA2  . GLY   A 1 8   ? 7.876  -8.391  17.091  1.00 25.08 ?  8   GLY   A HA2  1 
ATOM   94   H  HA3  . GLY   A 1 8   ? 8.517  -7.023  16.681  1.00 25.08 ?  8   GLY   A HA3  1 
ATOM   95   N  N    A TYR   A 1 9   ? 9.868  -9.361  15.108  0.74 17.53 ?  9   TYR   A N    1 
ATOM   96   N  N    B TYR   A 1 9   ? 9.885  -9.335  15.105  0.26 18.02 ?  9   TYR   A N    1 
ATOM   97   C  CA   A TYR   A 1 9   ? 10.138 -9.916  13.787  0.74 16.64 ?  9   TYR   A CA   1 
ATOM   98   C  CA   B TYR   A 1 9   ? 10.154 -9.843  13.770  0.26 17.29 ?  9   TYR   A CA   1 
ATOM   99   C  C    A TYR   A 1 9   ? 9.272  -11.140 13.520  0.74 16.15 ?  9   TYR   A C    1 
ATOM   100  C  C    B TYR   A 1 9   ? 9.269  -11.038 13.460  0.26 16.86 ?  9   TYR   A C    1 
ATOM   101  O  O    A TYR   A 1 9   ? 8.965  -11.923 14.422  0.74 18.01 ?  9   TYR   A O    1 
ATOM   102  O  O    B TYR   A 1 9   ? 9.003  -11.878 14.324  0.26 17.27 ?  9   TYR   A O    1 
ATOM   103  C  CB   A TYR   A 1 9   ? 11.621 -10.299 13.642  0.74 17.09 ?  9   TYR   A CB   1 
ATOM   104  C  CB   B TYR   A 1 9   ? 11.622 -10.246 13.633  0.26 17.30 ?  9   TYR   A CB   1 
ATOM   105  C  CG   A TYR   A 1 9   ? 12.529 -9.100  13.461  0.74 17.10 ?  9   TYR   A CG   1 
ATOM   106  C  CG   B TYR   A 1 9   ? 12.550 -9.067  13.453  0.26 17.23 ?  9   TYR   A CG   1 
ATOM   107  C  CD1  A TYR   A 1 9   ? 12.886 -8.314  14.545  0.74 17.91 ?  9   TYR   A CD1  1 
ATOM   108  C  CD1  B TYR   A 1 9   ? 12.853 -8.232  14.518  0.26 17.64 ?  9   TYR   A CD1  1 
ATOM   109  C  CD2  A TYR   A 1 9   ? 12.998 -8.742  12.205  0.74 16.58 ?  9   TYR   A CD2  1 
ATOM   110  C  CD2  B TYR   A 1 9   ? 13.108 -8.781  12.215  0.26 16.91 ?  9   TYR   A CD2  1 
ATOM   111  C  CE1  A TYR   A 1 9   ? 13.684 -7.196  14.389  0.74 18.19 ?  9   TYR   A CE1  1 
ATOM   112  C  CE1  B TYR   A 1 9   ? 13.690 -7.146  14.359  0.26 17.74 ?  9   TYR   A CE1  1 
ATOM   113  C  CE2  A TYR   A 1 9   ? 13.806 -7.629  12.032  0.74 16.65 ?  9   TYR   A CE2  1 
ATOM   114  C  CE2  B TYR   A 1 9   ? 13.945 -7.694  12.043  0.26 17.08 ?  9   TYR   A CE2  1 
ATOM   115  C  CZ   A TYR   A 1 9   ? 14.153 -6.861  13.130  0.74 17.56 ?  9   TYR   A CZ   1 
ATOM   116  C  CZ   B TYR   A 1 9   ? 14.236 -6.882  13.120  0.26 17.59 ?  9   TYR   A CZ   1 
ATOM   117  O  OH   A TYR   A 1 9   ? 14.937 -5.743  12.970  0.74 19.12 ?  9   TYR   A OH   1 
ATOM   118  O  OH   B TYR   A 1 9   ? 15.067 -5.798  12.958  0.26 18.48 ?  9   TYR   A OH   1 
ATOM   119  H  H    A TYR   A 1 9   ? 10.406 -9.644  15.718  0.74 21.04 ?  9   TYR   A H    1 
ATOM   120  H  H    B TYR   A 1 9   ? 10.422 -9.626  15.710  0.26 21.63 ?  9   TYR   A H    1 
ATOM   121  H  HA   A TYR   A 1 9   ? 9.939  -9.245  13.115  0.74 19.98 ?  9   TYR   A HA   1 
ATOM   122  H  HA   B TYR   A 1 9   ? 9.968  -9.150  13.123  0.26 20.75 ?  9   TYR   A HA   1 
ATOM   123  H  HB2  A TYR   A 1 9   ? 11.905 -10.778 14.438  0.74 20.52 ?  9   TYR   A HB2  1 
ATOM   124  H  HB2  B TYR   A 1 9   ? 11.900 -10.741 14.422  0.26 20.76 ?  9   TYR   A HB2  1 
ATOM   125  H  HB3  A TYR   A 1 9   ? 11.717 -10.867 12.862  0.74 20.52 ?  9   TYR   A HB3  1 
ATOM   126  H  HB3  B TYR   A 1 9   ? 11.693 -10.806 12.848  0.26 20.76 ?  9   TYR   A HB3  1 
ATOM   127  H  HD1  A TYR   A 1 9   ? 12.565 -8.536  15.393  0.74 21.50 ?  9   TYR   A HD1  1 
ATOM   128  H  HD1  B TYR   A 1 9   ? 12.484 -8.408  15.354  0.26 21.17 ?  9   TYR   A HD1  1 
ATOM   129  H  HD2  A TYR   A 1 9   ? 12.763 -9.256  11.467  0.74 19.90 ?  9   TYR   A HD2  1 
ATOM   130  H  HD2  B TYR   A 1 9   ? 12.915 -9.328  11.488  0.26 20.30 ?  9   TYR   A HD2  1 
ATOM   131  H  HE1  A TYR   A 1 9   ? 13.916 -6.679  15.128  0.74 21.84 ?  9   TYR   A HE1  1 
ATOM   132  H  HE1  B TYR   A 1 9   ? 13.883 -6.595  15.083  0.26 21.30 ?  9   TYR   A HE1  1 
ATOM   133  H  HE2  A TYR   A 1 9   ? 14.115 -7.400  11.185  0.74 19.99 ?  9   TYR   A HE2  1 
ATOM   134  H  HE2  B TYR   A 1 9   ? 14.316 -7.515  11.209  0.26 20.51 ?  9   TYR   A HE2  1 
ATOM   135  H  HH   A TYR   A 1 9   ? 15.069 -5.371  13.714  0.74 22.95 ?  9   TYR   A HH   1 
ATOM   136  H  HH   B TYR   A 1 9   ? 15.152 -5.391  13.689  0.26 22.19 ?  9   TYR   A HH   1 
ATOM   137  N  N    A LEU   A 1 10  ? 8.879  -11.290 12.261  0.74 15.22 ?  10  LEU   A N    1 
ATOM   138  N  N    B LEU   A 1 10  ? 8.811  -11.107 12.216  0.26 16.25 ?  10  LEU   A N    1 
ATOM   139  C  CA   A LEU   A 1 10  ? 8.278  -12.520 11.772  0.74 14.93 ?  10  LEU   A CA   1 
ATOM   140  C  CA   B LEU   A 1 10  ? 8.109  -12.279 11.719  0.26 15.82 ?  10  LEU   A CA   1 
ATOM   141  C  C    A LEU   A 1 10  ? 9.402  -13.441 11.312  0.74 14.46 ?  10  LEU   A C    1 
ATOM   142  C  C    B LEU   A 1 10  ? 9.150  -13.260 11.198  0.26 16.08 ?  10  LEU   A C    1 
ATOM   143  O  O    A LEU   A 1 10  ? 10.354 -12.992 10.670  0.74 13.18 ?  10  LEU   A O    1 
ATOM   144  O  O    B LEU   A 1 10  ? 9.974  -12.907 10.346  0.26 16.44 ?  10  LEU   A O    1 
ATOM   145  C  CB   A LEU   A 1 10  ? 7.350  -12.190 10.601  0.74 16.03 ?  10  LEU   A CB   1 
ATOM   146  C  CB   B LEU   A 1 10  ? 7.127  -11.884 10.620  0.26 15.69 ?  10  LEU   A CB   1 
ATOM   147  C  CG   A LEU   A 1 10  ? 6.632  -13.349 9.915   0.74 18.08 ?  10  LEU   A CG   1 
ATOM   148  C  CG   B LEU   A 1 10  ? 6.186  -12.991 10.147  0.26 16.02 ?  10  LEU   A CG   1 
ATOM   149  C  CD1  A LEU   A 1 10  ? 5.608  -13.970 10.848  0.74 20.35 ?  10  LEU   A CD1  1 
ATOM   150  C  CD1  B LEU   A 1 10  ? 4.865  -12.382 9.750   0.26 16.15 ?  10  LEU   A CD1  1 
ATOM   151  C  CD2  A LEU   A 1 10  ? 5.976  -12.914 8.599   0.74 20.21 ?  10  LEU   A CD2  1 
ATOM   152  C  CD2  B LEU   A 1 10  ? 6.777  -13.750 8.974   0.26 16.14 ?  10  LEU   A CD2  1 
ATOM   153  H  H    A LEU   A 1 10  ? 8.959  -10.681 11.653  0.74 18.27 ?  10  LEU   A H    1 
ATOM   154  H  H    B LEU   A 1 10  ? 8.900  -10.480 11.630  0.26 19.51 ?  10  LEU   A H    1 
ATOM   155  H  HA   A LEU   A 1 10  ? 7.773  -12.950 12.482  0.74 17.92 ?  10  LEU   A HA   1 
ATOM   156  H  HA   B LEU   A 1 10  ? 7.617  -12.697 12.442  0.26 18.99 ?  10  LEU   A HA   1 
ATOM   157  H  HB2  A LEU   A 1 10  ? 6.671  -11.581 10.923  0.74 19.24 ?  10  LEU   A HB2  1 
ATOM   158  H  HB2  B LEU   A 1 10  ? 6.577  -11.154 10.947  0.26 18.84 ?  10  LEU   A HB2  1 
ATOM   159  H  HB3  A LEU   A 1 10  ? 7.882  -11.746 9.922   0.74 19.24 ?  10  LEU   A HB3  1 
ATOM   160  H  HB3  B LEU   A 1 10  ? 7.632  -11.585 9.849   0.26 18.84 ?  10  LEU   A HB3  1 
ATOM   161  H  HG   A LEU   A 1 10  ? 7.283  -14.033 9.705   0.74 21.70 ?  10  LEU   A HG   1 
ATOM   162  H  HG   B LEU   A 1 10  ? 6.025  -13.613 10.875  0.26 19.24 ?  10  LEU   A HG   1 
ATOM   163  H  HD11 A LEU   A 1 10  ? 5.275  -14.789 10.449  0.74 24.43 ?  10  LEU   A HD11 1 
ATOM   164  H  HD11 B LEU   A 1 10  ? 4.305  -13.065 9.351   0.26 19.39 ?  10  LEU   A HD11 1 
ATOM   165  H  HD12 A LEU   A 1 10  ? 6.028  -14.164 11.700  0.74 24.43 ?  10  LEU   A HD12 1 
ATOM   166  H  HD12 B LEU   A 1 10  ? 4.435  -12.018 10.541  0.26 19.39 ?  10  LEU   A HD12 1 
ATOM   167  H  HD13 A LEU   A 1 10  ? 4.878  -13.344 10.978  0.74 24.43 ?  10  LEU   A HD13 1 
ATOM   168  H  HD13 B LEU   A 1 10  ? 5.027  -11.669 9.110   0.26 19.39 ?  10  LEU   A HD13 1 
ATOM   169  H  HD21 A LEU   A 1 10  ? 5.533  -13.679 8.203   0.74 24.26 ?  10  LEU   A HD21 1 
ATOM   170  H  HD21 B LEU   A 1 10  ? 6.113  -14.374 8.640   0.26 19.38 ?  10  LEU   A HD21 1 
ATOM   171  H  HD22 A LEU   A 1 10  ? 5.333  -12.213 8.783   0.74 24.26 ?  10  LEU   A HD22 1 
ATOM   172  H  HD22 B LEU   A 1 10  ? 7.015  -13.118 8.279   0.26 19.38 ?  10  LEU   A HD22 1 
ATOM   173  H  HD23 A LEU   A 1 10  ? 6.665  -12.583 8.001   0.74 24.26 ?  10  LEU   A HD23 1 
ATOM   174  H  HD23 B LEU   A 1 10  ? 7.561  -14.230 9.274   0.26 19.38 ?  10  LEU   A HD23 1 
ATOM   175  N  N    A LYS   A 1 11  ? 9.291  -14.727 11.652  0.74 15.22 ?  11  LYS   A N    1 
ATOM   176  N  N    B LYS   A 1 11  ? 9.129  -14.477 11.729  0.26 16.00 ?  11  LYS   A N    1 
ATOM   177  C  CA   A LYS   A 1 11  ? 10.304 -15.721 11.314  0.74 14.66 ?  11  LYS   A CA   1 
ATOM   178  C  CA   B LYS   A 1 11  ? 10.083 -15.505 11.337  0.26 15.34 ?  11  LYS   A CA   1 
ATOM   179  C  C    A LYS   A 1 11  ? 9.953  -16.314 9.956   0.74 15.02 ?  11  LYS   A C    1 
ATOM   180  C  C    B LYS   A 1 11  ? 9.656  -16.082 9.995   0.26 14.48 ?  11  LYS   A C    1 
ATOM   181  O  O    A LYS   A 1 11  ? 8.900  -16.939 9.809   0.74 17.19 ?  11  LYS   A O    1 
ATOM   182  O  O    B LYS   A 1 11  ? 8.529  -16.569 9.856   0.26 14.61 ?  11  LYS   A O    1 
ATOM   183  C  CB   A LYS   A 1 11  ? 10.328 -16.809 12.391  0.74 14.36 ?  11  LYS   A CB   1 
ATOM   184  C  CB   B LYS   A 1 11  ? 10.108 -16.597 12.403  0.26 15.38 ?  11  LYS   A CB   1 
ATOM   185  C  CG   A LYS   A 1 11  ? 11.353 -17.929 12.195  0.74 14.10 ?  11  LYS   A CG   1 
ATOM   186  C  CG   B LYS   A 1 11  ? 11.178 -17.659 12.213  0.26 15.42 ?  11  LYS   A CG   1 
ATOM   187  C  CD   A LYS   A 1 11  ? 11.437 -18.757 13.475  0.74 14.69 ?  11  LYS   A CD   1 
ATOM   188  C  CD   B LYS   A 1 11  ? 11.214 -18.592 13.413  0.26 15.43 ?  11  LYS   A CD   1 
ATOM   189  C  CE   A LYS   A 1 11  ? 12.426 -19.913 13.370  0.74 15.05 ?  11  LYS   A CE   1 
ATOM   190  C  CE   B LYS   A 1 11  ? 12.178 -19.748 13.204  0.26 15.48 ?  11  LYS   A CE   1 
ATOM   191  N  NZ   A LYS   A 1 11  ? 13.802 -19.457 13.038  0.74 15.32 ?  11  LYS   A NZ   1 
ATOM   192  N  NZ   B LYS   A 1 11  ? 13.599 -19.306 13.158  0.26 15.22 ?  11  LYS   A NZ   1 
ATOM   193  H  H    A LYS   A 1 11  ? 8.619  -15.050 12.083  0.74 18.27 ?  11  LYS   A H    1 
ATOM   194  H  H    B LYS   A 1 11  ? 8.565  -14.731 12.325  0.26 19.21 ?  11  LYS   A H    1 
ATOM   195  H  HA   A LYS   A 1 11  ? 11.176 -15.303 11.264  0.74 17.60 ?  11  LYS   A HA   1 
ATOM   196  H  HA   B LYS   A 1 11  ? 10.971 -15.120 11.251  0.26 18.42 ?  11  LYS   A HA   1 
ATOM   197  H  HB2  A LYS   A 1 11  ? 10.522 -16.387 13.244  0.74 17.24 ?  11  LYS   A HB2  1 
ATOM   198  H  HB2  B LYS   A 1 11  ? 10.258 -16.182 13.266  0.26 18.46 ?  11  LYS   A HB2  1 
ATOM   199  H  HB3  A LYS   A 1 11  ? 9.451  -17.222 12.429  0.74 17.24 ?  11  LYS   A HB3  1 
ATOM   200  H  HB3  B LYS   A 1 11  ? 9.248  -17.046 12.402  0.26 18.46 ?  11  LYS   A HB3  1 
ATOM   201  H  HG2  A LYS   A 1 11  ? 11.071 -18.504 11.465  0.74 16.93 ?  11  LYS   A HG2  1 
ATOM   202  H  HG2  B LYS   A 1 11  ? 10.978 -18.182 11.420  0.26 18.51 ?  11  LYS   A HG2  1 
ATOM   203  H  HG3  A LYS   A 1 11  ? 12.225 -17.544 12.012  0.74 16.93 ?  11  LYS   A HG3  1 
ATOM   204  H  HG3  B LYS   A 1 11  ? 12.046 -17.232 12.128  0.26 18.51 ?  11  LYS   A HG3  1 
ATOM   205  H  HD2  A LYS   A 1 11  ? 11.716 -18.182 14.203  0.74 17.64 ?  11  LYS   A HD2  1 
ATOM   206  H  HD2  B LYS   A 1 11  ? 11.499 -18.094 14.195  0.26 18.53 ?  11  LYS   A HD2  1 
ATOM   207  H  HD3  A LYS   A 1 11  ? 10.558 -19.127 13.665  0.74 17.64 ?  11  LYS   A HD3  1 
ATOM   208  H  HD3  B LYS   A 1 11  ? 10.326 -18.958 13.557  0.26 18.53 ?  11  LYS   A HD3  1 
ATOM   209  H  HE2  A LYS   A 1 11  ? 12.460 -20.377 14.221  0.74 18.06 ?  11  LYS   A HE2  1 
ATOM   210  H  HE2  B LYS   A 1 11  ? 12.081 -20.376 13.936  0.26 18.59 ?  11  LYS   A HE2  1 
ATOM   211  H  HE3  A LYS   A 1 11  ? 12.133 -20.518 12.672  0.74 18.06 ?  11  LYS   A HE3  1 
ATOM   212  H  HE3  B LYS   A 1 11  ? 11.970 -20.183 12.363  0.26 18.59 ?  11  LYS   A HE3  1 
ATOM   213  H  HZ1  A LYS   A 1 11  ? 14.339 -20.161 12.942  0.74 18.39 ?  11  LYS   A HZ1  1 
ATOM   214  H  HZ1  B LYS   A 1 11  ? 14.131 -20.010 13.035  0.26 18.27 ?  11  LYS   A HZ1  1 
ATOM   215  H  HZ2  A LYS   A 1 11  ? 13.795 -18.995 12.278  0.74 18.39 ?  11  LYS   A HZ2  1 
ATOM   216  H  HZ2  B LYS   A 1 11  ? 13.718 -18.733 12.488  0.26 18.27 ?  11  LYS   A HZ2  1 
ATOM   217  H  HZ3  A LYS   A 1 11  ? 14.118 -18.941 13.689  0.74 18.39 ?  11  LYS   A HZ3  1 
ATOM   218  H  HZ3  B LYS   A 1 11  ? 13.819 -18.909 13.923  0.26 18.27 ?  11  LYS   A HZ3  1 
ATOM   219  N  N    A LEU   A 1 12  ? 10.815 -16.113 8.961   0.74 14.36 ?  12  LEU   A N    1 
ATOM   220  N  N    B LEU   A 1 12  ? 10.547 -16.024 9.006   0.26 14.09 ?  12  LEU   A N    1 
ATOM   221  C  CA   A LEU   A 1 12  ? 10.582 -16.695 7.642   0.74 14.00 ?  12  LEU   A CA   1 
ATOM   222  C  CA   B LEU   A 1 12  ? 10.273 -16.561 7.678   0.26 13.90 ?  12  LEU   A CA   1 
ATOM   223  C  C    A LEU   A 1 12  ? 11.163 -18.099 7.515   0.74 13.97 ?  12  LEU   A C    1 
ATOM   224  C  C    B LEU   A 1 12  ? 10.873 -17.943 7.470   0.26 13.80 ?  12  LEU   A C    1 
ATOM   225  O  O    A LEU   A 1 12  ? 10.530 -18.976 6.918   0.74 14.60 ?  12  LEU   A O    1 
ATOM   226  O  O    B LEU   A 1 12  ? 10.224 -18.815 6.885   0.26 14.18 ?  12  LEU   A O    1 
ATOM   227  C  CB   A LEU   A 1 12  ? 11.170 -15.806 6.539   0.74 15.15 ?  12  LEU   A CB   1 
ATOM   228  C  CB   B LEU   A 1 12  ? 10.821 -15.621 6.600   0.26 14.27 ?  12  LEU   A CB   1 
ATOM   229  C  CG   A LEU   A 1 12  ? 10.476 -14.459 6.325   0.74 16.09 ?  12  LEU   A CG   1 
ATOM   230  C  CG   B LEU   A 1 12  ? 10.197 -14.230 6.487   0.26 14.22 ?  12  LEU   A CG   1 
ATOM   231  C  CD1  A LEU   A 1 12  ? 11.167 -13.693 5.209   0.74 16.92 ?  12  LEU   A CD1  1 
ATOM   232  C  CD1  B LEU   A 1 12  ? 10.972 -13.393 5.486   0.26 14.29 ?  12  LEU   A CD1  1 
ATOM   233  C  CD2  A LEU   A 1 12  ? 8.994  -14.646 6.017   0.74 17.38 ?  12  LEU   A CD2  1 
ATOM   234  C  CD2  B LEU   A 1 12  ? 8.742  -14.330 6.071   0.26 14.63 ?  12  LEU   A CD2  1 
ATOM   235  H  H    A LEU   A 1 12  ? 11.540 -15.647 9.024   0.74 17.23 ?  12  LEU   A H    1 
ATOM   236  H  H    B LEU   A 1 12  ? 11.331 -15.676 9.083   0.26 16.91 ?  12  LEU   A H    1 
ATOM   237  H  HA   A LEU   A 1 12  ? 9.628  -16.760 7.500   0.74 16.80 ?  12  LEU   A HA   1 
ATOM   238  H  HA   B LEU   A 1 12  ? 9.312  -16.628 7.558   0.26 16.69 ?  12  LEU   A HA   1 
ATOM   239  H  HB2  A LEU   A 1 12  ? 12.097 -15.623 6.754   0.74 18.18 ?  12  LEU   A HB2  1 
ATOM   240  H  HB2  B LEU   A 1 12  ? 11.766 -15.494 6.765   0.26 17.13 ?  12  LEU   A HB2  1 
ATOM   241  H  HB3  A LEU   A 1 12  ? 11.122 -16.291 5.701   0.74 18.18 ?  12  LEU   A HB3  1 
ATOM   242  H  HB3  B LEU   A 1 12  ? 10.701 -16.052 5.740   0.26 17.13 ?  12  LEU   A HB3  1 
ATOM   243  H  HG   A LEU   A 1 12  ? 10.552 -13.932 7.134   0.74 19.32 ?  12  LEU   A HG   1 
ATOM   244  H  HG   B LEU   A 1 12  ? 10.238 -13.784 7.349   0.26 17.08 ?  12  LEU   A HG   1 
ATOM   245  H  HD11 A LEU   A 1 12  ? 10.723 -12.840 5.085   0.74 20.32 ?  12  LEU   A HD11 1 
ATOM   246  H  HD11 B LEU   A 1 12  ? 10.558 -12.518 5.415   0.26 17.16 ?  12  LEU   A HD11 1 
ATOM   247  H  HD12 A LEU   A 1 12  ? 12.097 -13.547 5.452   0.74 20.32 ?  12  LEU   A HD12 1 
ATOM   248  H  HD12 B LEU   A 1 12  ? 11.888 -13.300 5.794   0.26 17.16 ?  12  LEU   A HD12 1 
ATOM   249  H  HD13 A LEU   A 1 12  ? 11.120 -14.212 4.390   0.74 20.32 ?  12  LEU   A HD13 1 
ATOM   250  H  HD13 B LEU   A 1 12  ? 10.957 -13.837 4.624   0.26 17.16 ?  12  LEU   A HD13 1 
ATOM   251  H  HD21 A LEU   A 1 12  ? 8.631  -13.808 5.690   0.74 20.87 ?  12  LEU   A HD21 1 
ATOM   252  H  HD21 B LEU   A 1 12  ? 8.392  -13.439 5.926   0.26 17.57 ?  12  LEU   A HD21 1 
ATOM   253  H  HD22 A LEU   A 1 12  ? 8.898  -15.335 5.341   0.74 20.87 ?  12  LEU   A HD22 1 
ATOM   254  H  HD22 B LEU   A 1 12  ? 8.687  -14.846 5.250   0.26 17.57 ?  12  LEU   A HD22 1 
ATOM   255  H  HD23 A LEU   A 1 12  ? 8.536  -14.911 6.829   0.74 20.87 ?  12  LEU   A HD23 1 
ATOM   256  H  HD23 B LEU   A 1 12  ? 8.245  -14.774 6.774   0.26 17.57 ?  12  LEU   A HD23 1 
ATOM   257  N  N    A THR   A 1 13  ? 12.370 -18.317 8.033   0.74 14.43 ?  13  THR   A N    1 
ATOM   258  N  N    B THR   A 1 13  ? 12.109 -18.150 7.915   0.26 14.28 ?  13  THR   A N    1 
ATOM   259  C  CA   A THR   A 1 13  ? 13.048 -19.607 7.944   0.74 13.80 ?  13  THR   A CA   1 
ATOM   260  C  CA   B THR   A 1 13  ? 12.785 -19.437 7.810   0.26 14.80 ?  13  THR   A CA   1 
ATOM   261  C  C    A THR   A 1 13  ? 13.824 -19.830 9.232   0.74 14.15 ?  13  THR   A C    1 
ATOM   262  C  C    B THR   A 1 13  ? 13.542 -19.688 9.110   0.26 15.14 ?  13  THR   A C    1 
ATOM   263  O  O    A THR   A 1 13  ? 13.757 -19.032 10.171  0.74 13.83 ?  13  THR   A O    1 
ATOM   264  O  O    B THR   A 1 13  ? 13.356 -18.990 10.112  0.26 15.67 ?  13  THR   A O    1 
ATOM   265  C  CB   A THR   A 1 13  ? 14.006 -19.680 6.749   0.74 14.92 ?  13  THR   A CB   1 
ATOM   266  C  CB   B THR   A 1 13  ? 13.737 -19.476 6.606   0.26 14.65 ?  13  THR   A CB   1 
ATOM   267  O  OG1  A THR   A 1 13  ? 15.094 -18.786 6.987   0.74 14.41 ?  13  THR   A OG1  1 
ATOM   268  O  OG1  B THR   A 1 13  ? 14.787 -18.524 6.801   0.26 14.71 ?  13  THR   A OG1  1 
ATOM   269  C  CG2  A THR   A 1 13  ? 13.328 -19.317 5.432   0.74 16.12 ?  13  THR   A CG2  1 
ATOM   270  C  CG2  B THR   A 1 13  ? 13.012 -19.169 5.303   0.26 15.01 ?  13  THR   A CG2  1 
ATOM   271  H  H    A THR   A 1 13  ? 12.829 -17.718 8.442   0.74 17.32 ?  13  THR   A H    1 
ATOM   272  H  H    B THR   A 1 13  ? 12.588 -17.540 8.280   0.26 17.14 ?  13  THR   A H    1 
ATOM   273  H  HA   A THR   A 1 13  ? 12.392 -20.315 7.852   0.74 16.57 ?  13  THR   A HA   1 
ATOM   274  H  HA   B THR   A 1 13  ? 12.123 -20.138 7.698   0.26 17.76 ?  13  THR   A HA   1 
ATOM   275  H  HB   A THR   A 1 13  ? 14.351 -20.585 6.668   0.74 17.92 ?  13  THR   A HB   1 
ATOM   276  H  HB   B THR   A 1 13  ? 14.121 -20.364 6.532   0.26 17.59 ?  13  THR   A HB   1 
ATOM   277  H  HG1  A THR   A 1 13  ? 15.733 -19.198 7.352   0.74 17.30 ?  13  THR   A HG1  1 
ATOM   278  H  HG1  B THR   A 1 13  ? 15.319 -18.543 6.151   0.26 17.66 ?  13  THR   A HG1  1 
ATOM   279  H  HG21 A THR   A 1 13  ? 13.949 -19.442 4.692   0.74 19.35 ?  13  THR   A HG21 1 
ATOM   280  H  HG21 B THR   A 1 13  ? 13.624 -19.273 4.554   0.26 18.02 ?  13  THR   A HG21 1 
ATOM   281  H  HG22 A THR   A 1 13  ? 12.558 -19.890 5.288   0.74 19.35 ?  13  THR   A HG22 1 
ATOM   282  H  HG22 B THR   A 1 13  ? 12.268 -19.778 5.187   0.26 18.02 ?  13  THR   A HG22 1 
ATOM   283  H  HG23 A THR   A 1 13  ? 13.040 -18.395 5.446   0.74 19.35 ?  13  THR   A HG23 1 
ATOM   284  H  HG23 B THR   A 1 13  ? 12.681 -18.260 5.314   0.26 18.02 ?  13  THR   A HG23 1 
ATOM   285  N  N    A ASP   A 1 14  ? 14.611 -20.907 9.254   0.74 14.28 ?  14  ASP   A N    1 
ATOM   286  N  N    B ASP   A 1 14  ? 14.419 -20.693 9.078   0.26 15.48 ?  14  ASP   A N    1 
ATOM   287  C  CA   A ASP   A 1 14  ? 15.473 -21.167 10.397  0.74 15.15 ?  14  ASP   A CA   1 
ATOM   288  C  CA   B ASP   A 1 14  ? 15.227 -21.047 10.239  0.26 15.37 ?  14  ASP   A CA   1 
ATOM   289  C  C    A ASP   A 1 14  ? 16.290 -19.931 10.782  0.74 14.66 ?  14  ASP   A C    1 
ATOM   290  C  C    B ASP   A 1 14  ? 16.200 -19.943 10.637  0.26 14.63 ?  14  ASP   A C    1 
ATOM   291  O  O    A ASP   A 1 14  ? 16.457 -19.633 11.972  0.74 15.96 ?  14  ASP   A O    1 
ATOM   292  O  O    B ASP   A 1 14  ? 16.667 -19.929 11.782  0.26 15.02 ?  14  ASP   A O    1 
ATOM   293  C  CB   A ASP   A 1 14  ? 16.404 -22.340 10.086  0.74 18.48 ?  14  ASP   A CB   1 
ATOM   294  C  CB   B ASP   A 1 14  ? 16.032 -22.306 9.920   0.26 16.79 ?  14  ASP   A CB   1 
ATOM   295  C  CG   A ASP   A 1 14  ? 17.386 -22.594 11.201  0.74 23.14 ?  14  ASP   A CG   1 
ATOM   296  C  CG   B ASP   A 1 14  ? 16.910 -22.754 11.076  0.26 18.17 ?  14  ASP   A CG   1 
ATOM   297  O  OD1  A ASP   A 1 14  ? 16.943 -23.020 12.289  0.74 24.71 ?  14  ASP   A OD1  1 
ATOM   298  O  OD1  B ASP   A 1 14  ? 16.363 -23.115 12.141  0.26 18.49 ?  14  ASP   A OD1  1 
ATOM   299  O  OD2  A ASP   A 1 14  ? 18.592 -22.338 10.996  0.74 25.36 -1 14  ASP   A OD2  1 
ATOM   300  O  OD2  B ASP   A 1 14  ? 18.148 -22.762 10.913  0.26 19.25 -1 14  ASP   A OD2  1 
ATOM   301  H  H    A ASP   A 1 14  ? 14.681 -21.483 8.615   0.74 17.15 ?  14  ASP   A H    1 
ATOM   302  H  H    B ASP   A 1 14  ? 14.562 -21.182 8.388   0.26 18.58 ?  14  ASP   A H    1 
ATOM   303  H  HA   A ASP   A 1 14  ? 14.925 -21.423 11.159  0.74 18.18 ?  14  ASP   A HA   1 
ATOM   304  H  HA   B ASP   A 1 14  ? 14.634 -21.240 10.986  0.26 18.45 ?  14  ASP   A HA   1 
ATOM   305  H  HB2  A ASP   A 1 14  ? 15.865 -23.147 9.927   0.74 22.19 ?  14  ASP   A HB2  1 
ATOM   306  H  HB2  B ASP   A 1 14  ? 15.419 -23.025 9.713   0.26 20.15 ?  14  ASP   A HB2  1 
ATOM   307  H  HB3  A ASP   A 1 14  ? 16.923 -22.144 9.293   0.74 22.19 ?  14  ASP   A HB3  1 
ATOM   308  H  HB3  B ASP   A 1 14  ? 16.601 -22.123 9.154   0.26 20.15 ?  14  ASP   A HB3  1 
ATOM   309  N  N    A ASN   A 1 15  ? 16.808 -19.193 9.789   0.74 13.95 ?  15  ASN   A N    1 
ATOM   310  N  N    B ASN   A 1 15  ? 16.535 -19.029 9.716   0.26 13.91 ?  15  ASN   A N    1 
ATOM   311  C  CA   A ASN   A 1 15  ? 17.787 -18.137 10.046  0.74 15.01 ?  15  ASN   A CA   1 
ATOM   312  C  CA   B ASN   A 1 15  ? 17.558 -18.026 9.989   0.26 14.03 ?  15  ASN   A CA   1 
ATOM   313  C  C    A ASN   A 1 15  ? 17.380 -16.732 9.597   0.74 15.01 ?  15  ASN   A C    1 
ATOM   314  C  C    B ASN   A 1 15  ? 17.254 -16.662 9.374   0.26 13.92 ?  15  ASN   A C    1 
ATOM   315  O  O    A ASN   A 1 15  ? 18.071 -15.775 9.966   0.74 15.16 ?  15  ASN   A O    1 
ATOM   316  O  O    B ASN   A 1 15  ? 18.157 -15.817 9.312   0.26 14.41 ?  15  ASN   A O    1 
ATOM   317  C  CB   A ASN   A 1 15  ? 19.157 -18.501 9.434   0.74 14.87 ?  15  ASN   A CB   1 
ATOM   318  C  CB   B ASN   A 1 15  ? 18.922 -18.512 9.483   0.26 13.99 ?  15  ASN   A CB   1 
ATOM   319  C  CG   A ASN   A 1 15  ? 19.115 -18.593 7.928   0.74 15.46 ?  15  ASN   A CG   1 
ATOM   320  C  CG   B ASN   A 1 15  ? 18.975 -18.623 7.974   0.26 13.99 ?  15  ASN   A CG   1 
ATOM   321  O  OD1  A ASN   A 1 15  ? 18.363 -19.393 7.367   0.74 17.30 ?  15  ASN   A OD1  1 
ATOM   322  O  OD1  B ASN   A 1 15  ? 18.314 -19.478 7.381   0.26 14.60 ?  15  ASN   A OD1  1 
ATOM   323  N  ND2  A ASN   A 1 15  ? 19.902 -17.755 7.258   0.74 15.33 ?  15  ASN   A ND2  1 
ATOM   324  N  ND2  B ASN   A 1 15  ? 19.764 -17.759 7.343   0.26 13.68 ?  15  ASN   A ND2  1 
ATOM   325  H  H    A ASN   A 1 15  ? 16.601 -19.290 8.965   0.74 16.75 ?  15  ASN   A H    1 
ATOM   326  H  H    B ASN   A 1 15  ? 16.188 -18.977 8.934   0.26 16.70 ?  15  ASN   A H    1 
ATOM   327  H  HA   A ASN   A 1 15  ? 17.927 -18.094 11.004  0.74 18.02 ?  15  ASN   A HA   1 
ATOM   328  H  HA   B ASN   A 1 15  ? 17.632 -17.916 10.952  0.26 16.85 ?  15  ASN   A HA   1 
ATOM   329  H  HB2  A ASN   A 1 15  ? 19.806 -17.823 9.679   0.74 17.85 ?  15  ASN   A HB2  1 
ATOM   330  H  HB2  B ASN   A 1 15  ? 19.602 -17.880 9.763   0.26 16.79 ?  15  ASN   A HB2  1 
ATOM   331  H  HB3  A ASN   A 1 15  ? 19.441 -19.367 9.780   0.74 17.85 ?  15  ASN   A HB3  1 
ATOM   332  H  HB3  B ASN   A 1 15  ? 19.103 -19.386 9.856   0.26 16.79 ?  15  ASN   A HB3  1 
ATOM   333  H  HD21 A ASN   A 1 15  ? 19.911 -17.767 6.397   0.74 18.41 ?  15  ASN   A HD21 1 
ATOM   334  H  HD21 B ASN   A 1 15  ? 19.827 -17.779 6.485   0.26 16.42 ?  15  ASN   A HD21 1 
ATOM   335  H  HD22 A ASN   A 1 15  ? 20.408 -17.201 7.683   0.74 18.41 ?  15  ASN   A HD22 1 
ATOM   336  H  HD22 B ASN   A 1 15  ? 20.213 -17.178 7.792   0.26 16.42 ?  15  ASN   A HD22 1 
ATOM   337  N  N    A VAL   A 1 16  ? 16.293 -16.566 8.840   0.74 14.48 ?  16  VAL   A N    1 
ATOM   338  N  N    B VAL   A 1 16  ? 16.032 -16.419 8.909   0.26 13.54 ?  16  VAL   A N    1 
ATOM   339  C  CA   A VAL   A 1 16  ? 15.900 -15.265 8.293   0.74 14.65 ?  16  VAL   A CA   1 
ATOM   340  C  CA   B VAL   A 1 16  ? 15.652 -15.150 8.300   0.26 13.58 ?  16  VAL   A CA   1 
ATOM   341  C  C    A VAL   A 1 16  ? 14.625 -14.785 8.972   0.74 13.22 ?  16  VAL   A C    1 
ATOM   342  C  C    B VAL   A 1 16  ? 14.421 -14.607 9.014   0.26 13.50 ?  16  VAL   A C    1 
ATOM   343  O  O    A VAL   A 1 16  ? 13.631 -15.523 9.052   0.74 13.78 ?  16  VAL   A O    1 
ATOM   344  O  O    B VAL   A 1 16  ? 13.407 -15.305 9.136   0.26 13.54 ?  16  VAL   A O    1 
ATOM   345  C  CB   A VAL   A 1 16  ? 15.709 -15.312 6.767   0.74 15.06 ?  16  VAL   A CB   1 
ATOM   346  C  CB   B VAL   A 1 16  ? 15.385 -15.302 6.789   0.26 13.87 ?  16  VAL   A CB   1 
ATOM   347  C  CG1  A VAL   A 1 16  ? 15.274 -13.941 6.235   0.74 15.61 ?  16  VAL   A CG1  1 
ATOM   348  C  CG1  B VAL   A 1 16  ? 14.950 -13.979 6.187   0.26 14.32 ?  16  VAL   A CG1  1 
ATOM   349  C  CG2  A VAL   A 1 16  ? 16.984 -15.779 6.077   0.74 15.46 ?  16  VAL   A CG2  1 
ATOM   350  C  CG2  B VAL   A 1 16  ? 16.629 -15.829 6.081   0.26 14.38 ?  16  VAL   A CG2  1 
ATOM   351  H  H    A VAL   A 1 16  ? 15.765 -17.205 8.629   0.74 17.39 ?  16  VAL   A H    1 
ATOM   352  H  H    B VAL   A 1 16  ? 15.401 -16.997 8.926   0.26 16.25 ?  16  VAL   A H    1 
ATOM   353  H  HA   A VAL   A 1 16  ? 16.600 -14.620 8.485   0.74 17.59 ?  16  VAL   A HA   1 
ATOM   354  H  HA   B VAL   A 1 16  ? 16.369 -14.509 8.416   0.26 16.30 ?  16  VAL   A HA   1 
ATOM   355  H  HB   A VAL   A 1 16  ? 15.009 -15.950 6.564   0.74 18.08 ?  16  VAL   A HB   1 
ATOM   356  H  HB   B VAL   A 1 16  ? 14.671 -15.945 6.659   0.26 16.65 ?  16  VAL   A HB   1 
ATOM   357  H  HG11 A VAL   A 1 16  ? 15.360 -13.942 5.270   0.74 18.74 ?  16  VAL   A HG11 1 
ATOM   358  H  HG11 B VAL   A 1 16  ? 14.972 -14.055 5.222   0.26 17.20 ?  16  VAL   A HG11 1 
ATOM   359  H  HG12 A VAL   A 1 16  ? 14.347 -13.786 6.483   0.74 18.74 ?  16  VAL   A HG12 1 
ATOM   360  H  HG12 B VAL   A 1 16  ? 14.049 -13.780 6.484   0.26 17.20 ?  16  VAL   A HG12 1 
ATOM   361  H  HG13 A VAL   A 1 16  ? 15.841 -13.259 6.620   0.74 18.74 ?  16  VAL   A HG13 1 
ATOM   362  H  HG13 B VAL   A 1 16  ? 15.559 -13.286 6.480   0.26 17.20 ?  16  VAL   A HG13 1 
ATOM   363  H  HG21 A VAL   A 1 16  ? 16.856 -15.726 5.118   0.74 18.56 ?  16  VAL   A HG21 1 
ATOM   364  H  HG21 B VAL   A 1 16  ? 16.472 -15.830 5.124   0.26 17.26 ?  16  VAL   A HG21 1 
ATOM   365  H  HG22 A VAL   A 1 16  ? 17.717 -15.210 6.348   0.74 18.56 ?  16  VAL   A HG22 1 
ATOM   366  H  HG22 B VAL   A 1 16  ? 17.381 -15.253 6.292   0.26 17.26 ?  16  VAL   A HG22 1 
ATOM   367  H  HG23 A VAL   A 1 16  ? 17.163 -16.697 6.337   0.74 18.56 ?  16  VAL   A HG23 1 
ATOM   368  H  HG23 B VAL   A 1 16  ? 16.810 -16.733 6.387   0.26 17.26 ?  16  VAL   A HG23 1 
ATOM   369  N  N    A TYR   A 1 17  ? 14.645 -13.523 9.394   0.74 13.05 ?  17  TYR   A N    1 
ATOM   370  N  N    B TYR   A 1 17  ? 14.510 -13.356 9.462   0.26 13.83 ?  17  TYR   A N    1 
ATOM   371  C  CA   A TYR   A 1 17  ? 13.560 -12.849 10.083  0.74 13.11 ?  17  TYR   A CA   1 
ATOM   372  C  CA   B TYR   A 1 17  ? 13.443 -12.667 10.172  0.26 14.25 ?  17  TYR   A CA   1 
ATOM   373  C  C    A TYR   A 1 17  ? 13.278 -11.527 9.376   0.74 14.30 ?  17  TYR   A C    1 
ATOM   374  C  C    B TYR   A 1 17  ? 13.188 -11.329 9.490   0.26 14.28 ?  17  TYR   A C    1 
ATOM   375  O  O    A TYR   A 1 17  ? 14.176 -10.932 8.781   0.74 14.72 ?  17  TYR   A O    1 
ATOM   376  O  O    B TYR   A 1 17  ? 14.063 -10.786 8.812   0.26 14.31 ?  17  TYR   A O    1 
ATOM   377  C  CB   A TYR   A 1 17  ? 13.959 -12.582 11.544  0.74 14.20 ?  17  TYR   A CB   1 
ATOM   378  C  CB   B TYR   A 1 17  ? 13.821 -12.434 11.642  0.26 14.75 ?  17  TYR   A CB   1 
ATOM   379  C  CG   A TYR   A 1 17  ? 14.144 -13.851 12.351  0.74 15.44 ?  17  TYR   A CG   1 
ATOM   380  C  CG   B TYR   A 1 17  ? 14.077 -13.705 12.428  0.26 15.37 ?  17  TYR   A CG   1 
ATOM   381  C  CD1  A TYR   A 1 17  ? 15.311 -14.602 12.255  0.74 16.33 ?  17  TYR   A CD1  1 
ATOM   382  C  CD1  B TYR   A 1 17  ? 15.271 -14.403 12.292  0.26 15.83 ?  17  TYR   A CD1  1 
ATOM   383  C  CD2  A TYR   A 1 17  ? 13.147 -14.303 13.200  0.74 15.89 ?  17  TYR   A CD2  1 
ATOM   384  C  CD2  B TYR   A 1 17  ? 13.127 -14.201 13.312  0.26 15.81 ?  17  TYR   A CD2  1 
ATOM   385  C  CE1  A TYR   A 1 17  ? 15.474 -15.776 12.986  0.74 17.23 ?  17  TYR   A CE1  1 
ATOM   386  C  CE1  B TYR   A 1 17  ? 15.509 -15.566 13.007  0.26 16.46 ?  17  TYR   A CE1  1 
ATOM   387  C  CE2  A TYR   A 1 17  ? 13.298 -15.471 13.934  0.74 16.84 ?  17  TYR   A CE2  1 
ATOM   388  C  CE2  B TYR   A 1 17  ? 13.356 -15.364 14.034  0.26 16.37 ?  17  TYR   A CE2  1 
ATOM   389  C  CZ   A TYR   A 1 17  ? 14.461 -16.203 13.828  0.74 17.10 ?  17  TYR   A CZ   1 
ATOM   390  C  CZ   B TYR   A 1 17  ? 14.550 -16.039 13.878  0.26 16.72 ?  17  TYR   A CZ   1 
ATOM   391  O  OH   A TYR   A 1 17  ? 14.582 -17.359 14.572  0.74 17.98 ?  17  TYR   A OH   1 
ATOM   392  O  OH   B TYR   A 1 17  ? 14.776 -17.192 14.597  0.26 17.41 ?  17  TYR   A OH   1 
ATOM   393  H  H    A TYR   A 1 17  ? 15.327 -13.009 9.279   0.74 15.67 ?  17  TYR   A H    1 
ATOM   394  H  H    B TYR   A 1 17  ? 15.208 -12.863 9.353   0.26 16.61 ?  17  TYR   A H    1 
ATOM   395  H  HA   A TYR   A 1 17  ? 12.759 -13.399 10.064  0.74 15.74 ?  17  TYR   A HA   1 
ATOM   396  H  HA   B TYR   A 1 17  ? 12.630 -13.193 10.136  0.26 17.11 ?  17  TYR   A HA   1 
ATOM   397  H  HB2  A TYR   A 1 17  ? 14.796 -12.091 11.552  0.74 17.05 ?  17  TYR   A HB2  1 
ATOM   398  H  HB2  B TYR   A 1 17  ? 14.624 -11.892 11.676  0.26 17.71 ?  17  TYR   A HB2  1 
ATOM   399  H  HB3  A TYR   A 1 17  ? 13.264 -12.054 11.964  0.74 17.05 ?  17  TYR   A HB3  1 
ATOM   400  H  HB3  B TYR   A 1 17  ? 13.096 -11.965 12.074  0.26 17.71 ?  17  TYR   A HB3  1 
ATOM   401  H  HD1  A TYR   A 1 17  ? 15.993 -14.316 11.686  0.74 19.60 ?  17  TYR   A HD1  1 
ATOM   402  H  HD1  B TYR   A 1 17  ? 15.919 -14.087 11.706  0.26 19.00 ?  17  TYR   A HD1  1 
ATOM   403  H  HD2  A TYR   A 1 17  ? 12.357 -13.815 13.275  0.74 19.07 ?  17  TYR   A HD2  1 
ATOM   404  H  HD2  B TYR   A 1 17  ? 12.319 -13.749 13.420  0.26 18.98 ?  17  TYR   A HD2  1 
ATOM   405  H  HE1  A TYR   A 1 17  ? 16.264 -16.268 12.915  0.74 20.69 ?  17  TYR   A HE1  1 
ATOM   406  H  HE1  B TYR   A 1 17  ? 16.313 -16.025 12.905  0.26 19.77 ?  17  TYR   A HE1  1 
ATOM   407  H  HE2  A TYR   A 1 17  ? 12.619 -15.755 14.501  0.74 20.21 ?  17  TYR   A HE2  1 
ATOM   408  H  HE2  B TYR   A 1 17  ? 12.709 -15.686 14.622  0.26 19.65 ?  17  TYR   A HE2  1 
ATOM   409  H  HH   A TYR   A 1 17  ? 13.846 -17.538 14.936  0.74 21.59 ?  17  TYR   A HH   1 
ATOM   410  H  HH   B TYR   A 1 17  ? 15.531 -17.510 14.410  0.26 20.90 ?  17  TYR   A HH   1 
ATOM   411  N  N    A ILE   A 1 18  ? 12.032 -11.040 9.440   0.74 14.24 ?  18  ILE   A N    1 
ATOM   412  N  N    B ILE   A 1 18  ? 11.987 -10.782 9.677   0.26 13.12 ?  18  ILE   A N    1 
ATOM   413  C  CA   A ILE   A 1 18  ? 11.637 -9.842  8.691   0.74 14.49 ?  18  ILE   A CA   1 
ATOM   414  C  CA   B ILE   A 1 18  ? 11.598 -9.554  8.979   0.26 12.15 ?  18  ILE   A CA   1 
ATOM   415  C  C    A ILE   A 1 18  ? 10.649 -8.990  9.485   0.74 14.20 ?  18  ILE   A C    1 
ATOM   416  C  C    B ILE   A 1 18  ? 10.706 -8.712  9.879   0.26 11.91 ?  18  ILE   A C    1 
ATOM   417  O  O    A ILE   A 1 18  ? 9.820  -9.509  10.237  0.74 14.87 ?  18  ILE   A O    1 
ATOM   418  O  O    B ILE   A 1 18  ? 9.879  -9.238  10.628  0.26 12.06 ?  18  ILE   A O    1 
ATOM   419  C  CB   A ILE   A 1 18  ? 11.080 -10.227 7.299   0.74 14.04 ?  18  ILE   A CB   1 
ATOM   420  C  CB   B ILE   A 1 18  ? 10.914 -9.862  7.631   0.26 11.77 ?  18  ILE   A CB   1 
ATOM   421  C  CG1  A ILE   A 1 18  ? 11.035 -9.010  6.369   0.74 14.24 ?  18  ILE   A CG1  1 
ATOM   422  C  CG1  B ILE   A 1 18  ? 10.676 -8.574  6.840   0.26 12.43 ?  18  ILE   A CG1  1 
ATOM   423  C  CG2  A ILE   A 1 18  ? 9.715  -10.931 7.428   0.74 14.72 ?  18  ILE   A CG2  1 
ATOM   424  C  CG2  B ILE   A 1 18  ? 9.609  -10.623 7.847   0.26 11.89 ?  18  ILE   A CG2  1 
ATOM   425  C  CD1  A ILE   A 1 18  ? 10.752 -9.367  4.933   0.74 15.56 ?  18  ILE   A CD1  1 
ATOM   426  C  CD1  B ILE   A 1 18  ? 10.311 -8.821  5.392   0.26 13.40 ?  18  ILE   A CD1  1 
ATOM   427  H  H    A ILE   A 1 18  ? 11.399 -11.393 9.902   0.74 17.10 ?  18  ILE   A H    1 
ATOM   428  H  H    B ILE   A 1 18  ? 11.382 -11.099 10.204  0.26 15.75 ?  18  ILE   A H    1 
ATOM   429  H  HA   A ILE   A 1 18  ? 12.429 -9.306  8.540   0.74 17.40 ?  18  ILE   A HA   1 
ATOM   430  H  HA   B ILE   A 1 18  ? 12.398 -9.039  8.797   0.26 14.59 ?  18  ILE   A HA   1 
ATOM   431  H  HB   A ILE   A 1 18  ? 11.697 -10.863 6.902   0.74 16.86 ?  18  ILE   A HB   1 
ATOM   432  H  HB   B ILE   A 1 18  ? 11.510 -10.421 7.119   0.26 14.13 ?  18  ILE   A HB   1 
ATOM   433  H  HG12 A ILE   A 1 18  ? 10.343 -8.405  6.666   0.74 17.10 ?  18  ILE   A HG12 1 
ATOM   434  H  HG12 B ILE   A 1 18  ? 9.950  -8.077  7.249   0.26 14.92 ?  18  ILE   A HG12 1 
ATOM   435  H  HG13 A ILE   A 1 18  ? 11.899 -8.562  6.391   0.74 17.10 ?  18  ILE   A HG13 1 
ATOM   436  H  HG13 B ILE   A 1 18  ? 11.487 -8.039  6.854   0.26 14.92 ?  18  ILE   A HG13 1 
ATOM   437  H  HG21 A ILE   A 1 18  ? 9.472  -11.311 6.566   0.74 17.67 ?  18  ILE   A HG21 1 
ATOM   438  H  HG21 B ILE   A 1 18  ? 9.262  -10.899 6.983   0.26 14.27 ?  18  ILE   A HG21 1 
ATOM   439  H  HG22 A ILE   A 1 18  ? 9.786  -11.634 8.090   0.74 17.67 ?  18  ILE   A HG22 1 
ATOM   440  H  HG22 B ILE   A 1 18  ? 9.786  -11.402 8.395   0.26 14.27 ?  18  ILE   A HG22 1 
ATOM   441  H  HG23 A ILE   A 1 18  ? 9.047  -10.283 7.700   0.74 17.67 ?  18  ILE   A HG23 1 
ATOM   442  H  HG23 B ILE   A 1 18  ? 8.969  -10.044 8.290   0.26 14.27 ?  18  ILE   A HG23 1 
ATOM   443  H  HD11 A ILE   A 1 18  ? 10.790 -8.559  4.392   0.74 18.67 ?  18  ILE   A HD11 1 
ATOM   444  H  HD11 B ILE   A 1 18  ? 10.238 -7.969  4.934   0.26 16.09 ?  18  ILE   A HD11 1 
ATOM   445  H  HD12 A ILE   A 1 18  ? 11.416 -10.000 4.624   0.74 18.67 ?  18  ILE   A HD12 1 
ATOM   446  H  HD12 B ILE   A 1 18  ? 11.005 -9.360  4.981   0.26 16.09 ?  18  ILE   A HD12 1 
ATOM   447  H  HD13 A ILE   A 1 18  ? 9.866  -9.757  4.875   0.74 18.67 ?  18  ILE   A HD13 1 
ATOM   448  H  HD13 B ILE   A 1 18  ? 9.463  -9.290  5.356   0.26 16.09 ?  18  ILE   A HD13 1 
ATOM   449  N  N    A LYS   A 1 19  ? 10.737 -7.667  9.295   0.74 14.49 ?  19  LYS   A N    1 
ATOM   450  N  N    B LYS   A 1 19  ? 10.880 -7.393  9.793   0.26 12.41 ?  19  LYS   A N    1 
ATOM   451  C  CA   A LYS   A 1 19  ? 9.919  -6.699  10.024  0.74 14.72 ?  19  LYS   A CA   1 
ATOM   452  C  CA   B LYS   A 1 19  ? 10.116 -6.453  10.598  0.26 13.19 ?  19  LYS   A CA   1 
ATOM   453  C  C    A LYS   A 1 19  ? 9.747  -5.438  9.180   0.74 14.92 ?  19  LYS   A C    1 
ATOM   454  C  C    B LYS   A 1 19  ? 9.866  -5.202  9.772   0.26 14.04 ?  19  LYS   A C    1 
ATOM   455  O  O    A LYS   A 1 19  ? 10.651 -5.049  8.436   0.74 14.58 ?  19  LYS   A O    1 
ATOM   456  O  O    B LYS   A 1 19  ? 10.748 -4.752  9.037   0.26 13.67 ?  19  LYS   A O    1 
ATOM   457  C  CB   A LYS   A 1 19  ? 10.596 -6.343  11.358  0.74 16.41 ?  19  LYS   A CB   1 
ATOM   458  C  CB   B LYS   A 1 19  ? 10.884 -6.079  11.872  0.26 13.51 ?  19  LYS   A CB   1 
ATOM   459  C  CG   A LYS   A 1 19  ? 9.876  -5.350  12.265  0.74 18.02 ?  19  LYS   A CG   1 
ATOM   460  C  CG   B LYS   A 1 19  ? 10.170 -5.134  12.822  0.26 14.21 ?  19  LYS   A CG   1 
ATOM   461  C  CD   A LYS   A 1 19  ? 10.746 -5.057  13.490  0.74 20.29 ?  19  LYS   A CD   1 
ATOM   462  C  CD   B LYS   A 1 19  ? 11.104 -4.774  13.968  0.26 14.69 ?  19  LYS   A CD   1 
ATOM   463  C  CE   A LYS   A 1 19  ? 10.089 -4.122  14.490  0.74 21.42 ?  19  LYS   A CE   1 
ATOM   464  C  CE   B LYS   A 1 19  ? 10.432 -3.943  15.040  0.26 15.62 ?  19  LYS   A CE   1 
ATOM   465  N  NZ   A LYS   A 1 19  ? 10.999 -3.867  15.646  0.74 21.64 ?  19  LYS   A NZ   1 
ATOM   466  N  NZ   B LYS   A 1 19  ? 11.320 -3.838  16.232  0.26 16.33 ?  19  LYS   A NZ   1 
ATOM   467  H  H    A LYS   A 1 19  ? 11.281 -7.304  8.741   0.74 17.40 ?  19  LYS   A H    1 
ATOM   468  H  H    B LYS   A 1 19  ? 11.448 -7.010  9.268   0.26 14.90 ?  19  LYS   A H    1 
ATOM   469  H  HA   A LYS   A 1 19  ? 9.046  -7.085  10.207  0.74 17.67 ?  19  LYS   A HA   1 
ATOM   470  H  HA   B LYS   A 1 19  ? 9.267  -6.841  10.850  0.26 15.84 ?  19  LYS   A HA   1 
ATOM   471  H  HB2  A LYS   A 1 19  ? 10.702 -7.163  11.870  0.74 19.71 ?  19  LYS   A HB2  1 
ATOM   472  H  HB2  B LYS   A 1 19  ? 11.071 -6.890  12.372  0.26 16.22 ?  19  LYS   A HB2  1 
ATOM   473  H  HB3  A LYS   A 1 19  ? 11.467 -5.974  11.164  0.74 19.71 ?  19  LYS   A HB3  1 
ATOM   474  H  HB3  B LYS   A 1 19  ? 11.719 -5.654  11.623  0.26 16.22 ?  19  LYS   A HB3  1 
ATOM   475  H  HG2  A LYS   A 1 19  ? 9.726  -4.519  11.788  0.74 21.64 ?  19  LYS   A HG2  1 
ATOM   476  H  HG2  B LYS   A 1 19  ? 9.926  -4.318  12.358  0.26 17.06 ?  19  LYS   A HG2  1 
ATOM   477  H  HG3  A LYS   A 1 19  ? 9.035  -5.727  12.568  0.74 21.64 ?  19  LYS   A HG3  1 
ATOM   478  H  HG3  B LYS   A 1 19  ? 9.384  -5.567  13.190  0.26 17.06 ?  19  LYS   A HG3  1 
ATOM   479  H  HD2  A LYS   A 1 19  ? 10.939 -5.891  13.946  0.74 24.36 ?  19  LYS   A HD2  1 
ATOM   480  H  HD2  B LYS   A 1 19  ? 11.422 -5.591  14.382  0.26 17.63 ?  19  LYS   A HD2  1 
ATOM   481  H  HD3  A LYS   A 1 19  ? 11.574 -4.644  13.196  0.74 24.36 ?  19  LYS   A HD3  1 
ATOM   482  H  HD3  B LYS   A 1 19  ? 11.853 -4.266  13.618  0.26 17.63 ?  19  LYS   A HD3  1 
ATOM   483  H  HE2  A LYS   A 1 19  ? 9.897  -3.271  14.062  0.74 25.71 ?  19  LYS   A HE2  1 
ATOM   484  H  HE2  B LYS   A 1 19  ? 10.262 -3.049  14.701  0.26 18.75 ?  19  LYS   A HE2  1 
ATOM   485  H  HE3  A LYS   A 1 19  ? 9.274  -4.524  14.827  0.74 25.71 ?  19  LYS   A HE3  1 
ATOM   486  H  HE3  B LYS   A 1 19  ? 9.602  -4.367  15.309  0.26 18.75 ?  19  LYS   A HE3  1 
ATOM   487  H  HZ1  A LYS   A 1 19  ? 10.605 -3.326  16.232  0.74 25.98 ?  19  LYS   A HZ1  1 
ATOM   488  H  HZ1  B LYS   A 1 19  ? 10.919 -3.365  16.870  0.26 19.60 ?  19  LYS   A HZ1  1 
ATOM   489  H  HZ2  A LYS   A 1 19  ? 11.199 -4.635  16.049  0.74 25.98 ?  19  LYS   A HZ2  1 
ATOM   490  H  HZ2  B LYS   A 1 19  ? 11.503 -4.650  16.546  0.26 19.60 ?  19  LYS   A HZ2  1 
ATOM   491  H  HZ3  A LYS   A 1 19  ? 11.752 -3.486  15.363  0.74 25.98 ?  19  LYS   A HZ3  1 
ATOM   492  H  HZ3  B LYS   A 1 19  ? 12.082 -3.435  16.009  0.26 19.60 ?  19  LYS   A HZ3  1 
ATOM   493  N  N    A ASN   A 1 20  ? 8.581  -4.794  9.299   0.74 16.32 ?  20  ASN   A N    1 
ATOM   494  N  N    B ASN   A 1 20  ? 8.660  -4.652  9.886   0.26 15.29 ?  20  ASN   A N    1 
ATOM   495  C  CA   A ASN   A 1 20  ? 8.371  -3.464  8.724   0.74 18.02 ?  20  ASN   A CA   1 
ATOM   496  C  CA   B ASN   A 1 20  ? 8.370  -3.347  9.306   0.26 16.62 ?  20  ASN   A CA   1 
ATOM   497  C  C    A ASN   A 1 20  ? 8.977  -2.452  9.688   0.74 18.31 ?  20  ASN   A C    1 
ATOM   498  C  C    B ASN   A 1 20  ? 9.036  -2.286  10.170  0.26 16.80 ?  20  ASN   A C    1 
ATOM   499  O  O    A ASN   A 1 20  ? 8.425  -2.215  10.768  0.74 20.28 ?  20  ASN   A O    1 
ATOM   500  O  O    B ASN   A 1 20  ? 8.578  -2.001  11.280  0.26 17.48 ?  20  ASN   A O    1 
ATOM   501  C  CB   A ASN   A 1 20  ? 6.875  -3.215  8.514   0.74 18.56 ?  20  ASN   A CB   1 
ATOM   502  C  CB   B ASN   A 1 20  ? 6.863  -3.123  9.233   0.26 17.29 ?  20  ASN   A CB   1 
ATOM   503  C  CG   A ASN   A 1 20  ? 6.543  -1.764  8.142   0.74 20.23 ?  20  ASN   A CG   1 
ATOM   504  C  CG   B ASN   A 1 20  ? 6.501  -1.682  8.933   0.26 18.14 ?  20  ASN   A CG   1 
ATOM   505  O  OD1  A ASN   A 1 20  ? 5.566  -1.197  8.639   0.74 22.37 ?  20  ASN   A OD1  1 
ATOM   506  O  OD1  B ASN   A 1 20  ? 5.684  -1.078  9.628   0.26 19.06 ?  20  ASN   A OD1  1 
ATOM   507  N  ND2  A ASN   A 1 20  ? 7.338  -1.168  7.260   0.74 20.24 ?  20  ASN   A ND2  1 
ATOM   508  N  ND2  B ASN   A 1 20  ? 7.114  -1.119  7.896   0.26 18.18 ?  20  ASN   A ND2  1 
ATOM   509  H  H    A ASN   A 1 20  ? 7.897  -5.120  9.704   0.74 19.59 ?  20  ASN   A H    1 
ATOM   510  H  H    B ASN   A 1 20  ? 8.001  -5.014  10.293  0.26 18.36 ?  20  ASN   A H    1 
ATOM   511  H  HA   A ASN   A 1 20  ? 8.828  -3.401  7.875   0.74 21.63 ?  20  ASN   A HA   1 
ATOM   512  H  HA   B ASN   A 1 20  ? 8.738  -3.297  8.410   0.26 19.95 ?  20  ASN   A HA   1 
ATOM   513  H  HB2  A ASN   A 1 20  ? 6.567  -3.784  7.794   0.74 22.29 ?  20  ASN   A HB2  1 
ATOM   514  H  HB2  B ASN   A 1 20  ? 6.493  -3.677  8.528   0.26 20.76 ?  20  ASN   A HB2  1 
ATOM   515  H  HB3  A ASN   A 1 20  ? 6.406  -3.435  9.334   0.74 22.29 ?  20  ASN   A HB3  1 
ATOM   516  H  HB3  B ASN   A 1 20  ? 6.465  -3.362  10.084  0.26 20.76 ?  20  ASN   A HB3  1 
ATOM   517  H  HD21 A ASN   A 1 20  ? 7.182  -0.354  7.032   0.74 24.29 ?  20  ASN   A HD21 1 
ATOM   518  H  HD21 B ASN   A 1 20  ? 6.945  -0.303  7.688   0.26 21.83 ?  20  ASN   A HD21 1 
ATOM   519  H  HD22 A ASN   A 1 20  ? 8.004  -1.592  6.927   0.74 24.29 ?  20  ASN   A HD22 1 
ATOM   520  H  HD22 B ASN   A 1 20  ? 7.683  -1.571  7.436   0.26 21.83 ?  20  ASN   A HD22 1 
ATOM   521  N  N    A ALA   A 1 21  ? 10.119 -1.867  9.319   0.74 19.16 ?  21  ALA   A N    1 
ATOM   522  N  N    B ALA   A 1 21  ? 10.130 -1.718  9.674   0.26 17.02 ?  21  ALA   A N    1 
ATOM   523  C  CA   A ALA   A 1 21  ? 10.811 -0.974  10.239  0.74 19.25 ?  21  ALA   A CA   1 
ATOM   524  C  CA   B ALA   A 1 21  ? 10.856 -0.700  10.417  0.26 16.84 ?  21  ALA   A CA   1 
ATOM   525  C  C    A ALA   A 1 21  ? 11.778 -0.076  9.483   0.74 18.86 ?  21  ALA   A C    1 
ATOM   526  C  C    B ALA   A 1 21  ? 11.906 -0.081  9.513   0.26 16.47 ?  21  ALA   A C    1 
ATOM   527  O  O    A ALA   A 1 21  ? 12.203 -0.384  8.366   0.74 18.84 ?  21  ALA   A O    1 
ATOM   528  O  O    B ALA   A 1 21  ? 12.437 -0.738  8.613   0.26 16.72 ?  21  ALA   A O    1 
ATOM   529  C  CB   A ALA   A 1 21  ? 11.559 -1.758  11.320  0.74 20.95 ?  21  ALA   A CB   1 
ATOM   530  C  CB   B ALA   A 1 21  ? 11.541 -1.292  11.654  0.26 17.37 ?  21  ALA   A CB   1 
ATOM   531  H  H    A ALA   A 1 21  ? 10.501 -1.965  8.556   0.74 23.00 ?  21  ALA   A H    1 
ATOM   532  H  H    B ALA   A 1 21  ? 10.467 -1.908  8.910   0.26 20.43 ?  21  ALA   A H    1 
ATOM   533  H  HA   A ALA   A 1 21  ? 10.155 -0.408  10.680  0.74 23.11 ?  21  ALA   A HA   1 
ATOM   534  H  HA   B ALA   A 1 21  ? 10.239 -0.007  10.705  0.26 20.22 ?  21  ALA   A HA   1 
ATOM   535  H  HB1  A ALA   A 1 21  ? 11.982 -1.131  11.925  0.74 25.15 ?  21  ALA   A HB1  1 
ATOM   536  H  HB1  B ALA   A 1 21  ? 12.022 -0.585  12.113  0.26 20.85 ?  21  ALA   A HB1  1 
ATOM   537  H  HB2  A ALA   A 1 21  ? 10.922 -2.308  11.807  0.74 25.15 ?  21  ALA   A HB2  1 
ATOM   538  H  HB2  B ALA   A 1 21  ? 10.870 -1.672  12.238  0.26 20.85 ?  21  ALA   A HB2  1 
ATOM   539  H  HB3  A ALA   A 1 21  ? 12.225 -2.319  10.898  0.74 25.15 ?  21  ALA   A HB3  1 
ATOM   540  H  HB3  B ALA   A 1 21  ? 12.163 -1.980  11.367  0.26 20.85 ?  21  ALA   A HB3  1 
ATOM   541  N  N    A ASP   A 1 22  ? 12.103 1.052   10.119  0.74 19.27 ?  22  ASP   A N    1 
ATOM   542  N  N    B ASP   A 1 22  ? 12.189 1.193   9.765   0.26 16.44 ?  22  ASP   A N    1 
ATOM   543  C  CA   A ASP   A 1 22  ? 13.133 1.976   9.654   0.74 18.97 ?  22  ASP   A CA   1 
ATOM   544  C  CA   B ASP   A 1 22  ? 13.363 1.838   9.199   0.26 16.47 ?  22  ASP   A CA   1 
ATOM   545  C  C    A ASP   A 1 22  ? 14.467 1.505   10.222  0.74 17.53 ?  22  ASP   A C    1 
ATOM   546  C  C    B ASP   A 1 22  ? 14.603 1.199   9.809   0.26 15.19 ?  22  ASP   A C    1 
ATOM   547  O  O    A ASP   A 1 22  ? 14.668 1.520   11.441  0.74 18.33 ?  22  ASP   A O    1 
ATOM   548  O  O    B ASP   A 1 22  ? 14.713 1.090   11.034  0.26 15.12 ?  22  ASP   A O    1 
ATOM   549  C  CB   A ASP   A 1 22  ? 12.803 3.382   10.148  0.74 20.46 ?  22  ASP   A CB   1 
ATOM   550  C  CB   B ASP   A 1 22  ? 13.322 3.322   9.562   0.26 17.48 ?  22  ASP   A CB   1 
ATOM   551  C  CG   A ASP   A 1 22  ? 13.826 4.428   9.718   0.74 22.46 ?  22  ASP   A CG   1 
ATOM   552  C  CG   B ASP   A 1 22  ? 14.349 4.144   8.819   0.26 17.80 ?  22  ASP   A CG   1 
ATOM   553  O  OD1  A ASP   A 1 22  ? 14.917 4.067   9.242   0.74 23.47 ?  22  ASP   A OD1  1 
ATOM   554  O  OD1  B ASP   A 1 22  ? 15.328 3.567   8.306   0.26 17.32 ?  22  ASP   A OD1  1 
ATOM   555  O  OD2  A ASP   A 1 22  ? 13.527 5.635   9.863   0.74 24.76 -1 22  ASP   A OD2  1 
ATOM   556  O  OD2  B ASP   A 1 22  ? 14.180 5.379   8.762   0.26 18.32 -1 22  ASP   A OD2  1 
ATOM   557  H  H    A ASP   A 1 22  ? 11.706 1.318   10.836  0.74 23.13 ?  22  ASP   A H    1 
ATOM   558  H  H    B ASP   A 1 22  ? 11.708 1.708   10.263  0.26 19.74 ?  22  ASP   A H    1 
ATOM   559  H  HA   A ASP   A 1 22  ? 13.173 1.965   8.682   0.74 22.78 ?  22  ASP   A HA   1 
ATOM   560  H  HA   B ASP   A 1 22  ? 13.376 1.733   8.231   0.26 19.78 ?  22  ASP   A HA   1 
ATOM   561  H  HB2  A ASP   A 1 22  ? 11.941 3.640   9.796   0.74 24.56 ?  22  ASP   A HB2  1 
ATOM   562  H  HB2  B ASP   A 1 22  ? 12.450 3.681   9.350   0.26 20.98 ?  22  ASP   A HB2  1 
ATOM   563  H  HB3  A ASP   A 1 22  ? 12.778 3.366   11.118  0.74 24.56 ?  22  ASP   A HB3  1 
ATOM   564  H  HB3  B ASP   A 1 22  ? 13.499 3.413   10.509  0.26 20.98 ?  22  ASP   A HB3  1 
ATOM   565  N  N    A ILE   A 1 23  ? 15.377 1.091   9.337   0.74 17.44 ?  23  ILE   A N    1 
ATOM   566  N  N    B ILE   A 1 23  ? 15.534 0.754   8.959   0.26 14.95 ?  23  ILE   A N    1 
ATOM   567  C  CA   A ILE   A 1 23  ? 16.632 0.477   9.768   0.74 16.44 ?  23  ILE   A CA   1 
ATOM   568  C  CA   B ILE   A 1 23  ? 16.755 0.143   9.479   0.26 14.91 ?  23  ILE   A CA   1 
ATOM   569  C  C    A ILE   A 1 23  ? 17.442 1.414   10.658  0.74 16.17 ?  23  ILE   A C    1 
ATOM   570  C  C    B ILE   A 1 23  ? 17.504 1.122   10.372  0.26 15.34 ?  23  ILE   A C    1 
ATOM   571  O  O    A ILE   A 1 23  ? 18.158 0.962   11.559  0.74 16.72 ?  23  ILE   A O    1 
ATOM   572  O  O    B ILE   A 1 23  ? 18.174 0.718   11.330  0.26 15.72 ?  23  ILE   A O    1 
ATOM   573  C  CB   A ILE   A 1 23  ? 17.424 -0.025  8.541   0.74 15.23 ?  23  ILE   A CB   1 
ATOM   574  C  CB   B ILE   A 1 23  ? 17.641 -0.415  8.344   0.26 14.55 ?  23  ILE   A CB   1 
ATOM   575  C  CG1  A ILE   A 1 23  ? 18.572 -0.940  8.981   0.74 15.22 ?  23  ILE   A CG1  1 
ATOM   576  C  CG1  B ILE   A 1 23  ? 18.678 -1.385  8.922   0.26 13.98 ?  23  ILE   A CG1  1 
ATOM   577  C  CG2  A ILE   A 1 23  ? 17.915 1.148   7.689   0.74 15.66 ?  23  ILE   A CG2  1 
ATOM   578  C  CG2  B ILE   A 1 23  ? 18.326 0.711   7.569   0.26 14.59 ?  23  ILE   A CG2  1 
ATOM   579  C  CD1  A ILE   A 1 23  ? 19.285 -1.631  7.830   0.74 15.40 ?  23  ILE   A CD1  1 
ATOM   580  C  CD1  B ILE   A 1 23  ? 19.655 -1.924  7.901   0.26 13.63 ?  23  ILE   A CD1  1 
ATOM   581  H  H    A ILE   A 1 23  ? 15.287 1.153   8.486   0.74 20.94 ?  23  ILE   A H    1 
ATOM   582  H  H    B ILE   A 1 23  ? 15.484 0.794   8.106   0.26 17.95 ?  23  ILE   A H    1 
ATOM   583  H  HA   A ILE   A 1 23  ? 16.415 -0.306  10.299  0.74 19.74 ?  23  ILE   A HA   1 
ATOM   584  H  HA   B ILE   A 1 23  ? 16.499 -0.610  10.031  0.26 17.90 ?  23  ILE   A HA   1 
ATOM   585  H  HB   A ILE   A 1 23  ? 16.822 -0.556  7.994   0.74 18.28 ?  23  ILE   A HB   1 
ATOM   586  H  HB   B ILE   A 1 23  ? 17.077 -0.910  7.730   0.26 17.47 ?  23  ILE   A HB   1 
ATOM   587  H  HG12 A ILE   A 1 23  ? 19.227 -0.414  9.461   0.74 18.28 ?  23  ILE   A HG12 1 
ATOM   588  H  HG12 B ILE   A 1 23  ? 19.190 -0.929  9.607   0.26 16.79 ?  23  ILE   A HG12 1 
ATOM   589  H  HG13 A ILE   A 1 23  ? 18.216 -1.632  9.562   0.74 18.28 ?  23  ILE   A HG13 1 
ATOM   590  H  HG13 B ILE   A 1 23  ? 18.214 -2.145  9.312   0.26 16.79 ?  23  ILE   A HG13 1 
ATOM   591  H  HG21 A ILE   A 1 23  ? 18.276 0.804   6.855   0.74 18.80 ?  23  ILE   A HG21 1 
ATOM   592  H  HG21 B ILE   A 1 23  ? 18.671 0.354   6.732   0.26 17.52 ?  23  ILE   A HG21 1 
ATOM   593  H  HG22 A ILE   A 1 23  ? 17.165 1.736   7.503   0.74 18.80 ?  23  ILE   A HG22 1 
ATOM   594  H  HG22 B ILE   A 1 23  ? 17.677 1.406   7.386   0.26 17.52 ?  23  ILE   A HG22 1 
ATOM   595  H  HG23 A ILE   A 1 23  ? 18.601 1.628   8.174   0.74 18.80 ?  23  ILE   A HG23 1 
ATOM   596  H  HG23 B ILE   A 1 23  ? 19.054 1.067   8.101   0.26 17.52 ?  23  ILE   A HG23 1 
ATOM   597  H  HD11 A ILE   A 1 23  ? 19.948 -2.239  8.191   0.74 18.49 ?  23  ILE   A HD11 1 
ATOM   598  H  HD11 B ILE   A 1 23  ? 20.163 -2.648  8.302   0.26 16.37 ?  23  ILE   A HD11 1 
ATOM   599  H  HD12 A ILE   A 1 23  ? 18.635 -2.122  7.305   0.74 18.49 ?  23  ILE   A HD12 1 
ATOM   600  H  HD12 B ILE   A 1 23  ? 19.161 -2.251  7.135   0.26 16.37 ?  23  ILE   A HD12 1 
ATOM   601  H  HD13 A ILE   A 1 23  ? 19.717 -0.959  7.280   0.74 18.49 ?  23  ILE   A HD13 1 
ATOM   602  H  HD13 B ILE   A 1 23  ? 20.255 -1.211  7.630   0.26 16.37 ?  23  ILE   A HD13 1 
ATOM   603  N  N    A VAL   A 1 24  ? 17.334 2.724   10.439  0.74 17.07 ?  24  VAL   A N    1 
ATOM   604  N  N    B VAL   A 1 24  ? 17.396 2.419   10.082  0.26 16.21 ?  24  VAL   A N    1 
ATOM   605  C  CA   A VAL   A 1 24  ? 18.025 3.684   11.298  0.74 18.54 ?  24  VAL   A CA   1 
ATOM   606  C  CA   B VAL   A 1 24  ? 18.000 3.434   10.940  0.26 17.46 ?  24  VAL   A CA   1 
ATOM   607  C  C    A VAL   A 1 24  ? 17.503 3.588   12.727  0.74 19.46 ?  24  VAL   A C    1 
ATOM   608  C  C    B VAL   A 1 24  ? 17.388 3.381   12.334  0.26 18.31 ?  24  VAL   A C    1 
ATOM   609  O  O    A VAL   A 1 24  ? 18.275 3.479   13.688  0.74 19.32 ?  24  VAL   A O    1 
ATOM   610  O  O    B VAL   A 1 24  ? 18.095 3.473   13.345  0.26 18.64 ?  24  VAL   A O    1 
ATOM   611  C  CB   A VAL   A 1 24  ? 17.869 5.107   10.737  0.74 19.66 ?  24  VAL   A CB   1 
ATOM   612  C  CB   B VAL   A 1 24  ? 17.848 4.825   10.296  0.26 18.24 ?  24  VAL   A CB   1 
ATOM   613  C  CG1  A VAL   A 1 24  ? 18.358 6.133   11.745  0.74 20.92 ?  24  VAL   A CG1  1 
ATOM   614  C  CG1  B VAL   A 1 24  ? 18.426 5.899   11.201  0.26 18.89 ?  24  VAL   A CG1  1 
ATOM   615  C  CG2  A VAL   A 1 24  ? 18.615 5.238   9.420   0.74 20.69 ?  24  VAL   A CG2  1 
ATOM   616  C  CG2  B VAL   A 1 24  ? 18.508 4.855   8.923   0.26 18.18 ?  24  VAL   A CG2  1 
ATOM   617  H  H    A VAL   A 1 24  ? 16.873 3.073   9.808   0.74 20.49 ?  24  VAL   A H    1 
ATOM   618  H  H    B VAL   A 1 24  ? 16.980 2.732   9.401   0.26 19.46 ?  24  VAL   A H    1 
ATOM   619  H  HA   A VAL   A 1 24  ? 18.970 3.470   11.310  0.74 22.25 ?  24  VAL   A HA   1 
ATOM   620  H  HA   B VAL   A 1 24  ? 18.947 3.250   11.025  0.26 20.97 ?  24  VAL   A HA   1 
ATOM   621  H  HB   A VAL   A 1 24  ? 16.929 5.276   10.562  0.74 23.60 ?  24  VAL   A HB   1 
ATOM   622  H  HB   B VAL   A 1 24  ? 16.905 5.013   10.172  0.26 21.90 ?  24  VAL   A HB   1 
ATOM   623  H  HG11 A VAL   A 1 24  ? 18.542 6.963   11.281  0.74 25.11 ?  24  VAL   A HG11 1 
ATOM   624  H  HG11 B VAL   A 1 24  ? 18.512 6.723   10.695  0.26 22.68 ?  24  VAL   A HG11 1 
ATOM   625  H  HG12 A VAL   A 1 24  ? 17.667 6.272   12.411  0.74 25.11 ?  24  VAL   A HG12 1 
ATOM   626  H  HG12 B VAL   A 1 24  ? 17.828 6.036   11.952  0.26 22.68 ?  24  VAL   A HG12 1 
ATOM   627  H  HG13 A VAL   A 1 24  ? 19.167 5.801   12.164  0.74 25.11 ?  24  VAL   A HG13 1 
ATOM   628  H  HG13 B VAL   A 1 24  ? 19.297 5.613   11.515  0.26 22.68 ?  24  VAL   A HG13 1 
ATOM   629  H  HG21 A VAL   A 1 24  ? 18.506 6.140   9.080   0.74 24.84 ?  24  VAL   A HG21 1 
ATOM   630  H  HG21 B VAL   A 1 24  ? 18.295 5.697   8.491   0.26 21.83 ?  24  VAL   A HG21 1 
ATOM   631  H  HG22 A VAL   A 1 24  ? 19.557 5.054   9.570   0.74 24.84 ?  24  VAL   A HG22 1 
ATOM   632  H  HG22 B VAL   A 1 24  ? 19.468 4.776   9.033   0.26 21.83 ?  24  VAL   A HG22 1 
ATOM   633  H  HG23 A VAL   A 1 24  ? 18.254 4.600   8.782   0.74 24.84 ?  24  VAL   A HG23 1 
ATOM   634  H  HG23 B VAL   A 1 24  ? 18.173 4.119   8.386   0.26 21.83 ?  24  VAL   A HG23 1 
ATOM   635  N  N    A GLU   A 1 25  ? 16.180 3.641   12.887  0.74 20.15 ?  25  GLU   A N    1 
ATOM   636  N  N    B GLU   A 1 25  ? 16.063 3.228   12.411  0.26 18.76 ?  25  GLU   A N    1 
ATOM   637  C  CA   A GLU   A 1 25  ? 15.592 3.558   14.220  0.74 21.62 ?  25  GLU   A CA   1 
ATOM   638  C  CA   B GLU   A 1 25  ? 15.398 3.177   13.709  0.26 19.90 ?  25  GLU   A CA   1 
ATOM   639  C  C    A GLU   A 1 25  ? 15.830 2.187   14.840  0.74 20.63 ?  25  GLU   A C    1 
ATOM   640  C  C    B GLU   A 1 25  ? 15.657 1.860   14.435  0.26 20.00 ?  25  GLU   A C    1 
ATOM   641  O  O    A GLU   A 1 25  ? 16.102 2.083   16.042  0.74 21.53 ?  25  GLU   A O    1 
ATOM   642  O  O    B GLU   A 1 25  ? 15.743 1.844   15.668  0.26 20.65 ?  25  GLU   A O    1 
ATOM   643  C  CB   A GLU   A 1 25  ? 14.101 3.891   14.154  0.74 24.47 ?  25  GLU   A CB   1 
ATOM   644  C  CB   B GLU   A 1 25  ? 13.898 3.427   13.542  0.26 21.04 ?  25  GLU   A CB   1 
ATOM   645  C  CG   A GLU   A 1 25  ? 13.834 5.334   13.748  0.74 27.77 ?  25  GLU   A CG   1 
ATOM   646  C  CG   B GLU   A 1 25  ? 13.559 4.861   13.164  0.26 22.62 ?  25  GLU   A CG   1 
ATOM   647  C  CD   A GLU   A 1 25  ? 14.589 6.327   14.618  0.74 30.46 ?  25  GLU   A CD   1 
ATOM   648  C  CD   B GLU   A 1 25  ? 14.016 5.858   14.209  0.26 23.79 ?  25  GLU   A CD   1 
ATOM   649  O  OE1  A GLU   A 1 25  ? 14.597 6.147   15.855  0.74 31.56 ?  25  GLU   A OE1  1 
ATOM   650  O  OE1  B GLU   A 1 25  ? 13.931 5.538   15.414  0.26 24.37 ?  25  GLU   A OE1  1 
ATOM   651  O  OE2  A GLU   A 1 25  ? 15.199 7.268   14.065  0.74 31.80 -1 25  GLU   A OE2  1 
ATOM   652  O  OE2  B GLU   A 1 25  ? 14.468 6.956   13.825  0.26 24.37 -1 25  GLU   A OE2  1 
ATOM   653  H  H    A GLU   A 1 25  ? 15.611 3.732   12.249  0.74 24.18 ?  25  GLU   A H    1 
ATOM   654  H  H    B GLU   A 1 25  ? 15.537 3.165   11.734  0.26 22.52 ?  25  GLU   A H    1 
ATOM   655  H  HA   A GLU   A 1 25  ? 16.020 4.209   14.793  0.74 25.95 ?  25  GLU   A HA   1 
ATOM   656  H  HA   B GLU   A 1 25  ? 15.753 3.887   14.263  0.26 23.89 ?  25  GLU   A HA   1 
ATOM   657  H  HB2  A GLU   A 1 25  ? 13.672 3.315   13.501  0.74 29.37 ?  25  GLU   A HB2  1 
ATOM   658  H  HB2  B GLU   A 1 25  ? 13.558 2.850   12.841  0.26 25.25 ?  25  GLU   A HB2  1 
ATOM   659  H  HB3  A GLU   A 1 25  ? 13.702 3.752   15.028  0.74 29.37 ?  25  GLU   A HB3  1 
ATOM   660  H  HB3  B GLU   A 1 25  ? 13.451 3.229   14.379  0.26 25.25 ?  25  GLU   A HB3  1 
ATOM   661  H  HG2  A GLU   A 1 25  ? 14.127 5.464   12.833  0.74 33.33 ?  25  GLU   A HG2  1 
ATOM   662  H  HG2  B GLU   A 1 25  ? 13.996 5.082   12.325  0.26 27.15 ?  25  GLU   A HG2  1 
ATOM   663  H  HG3  A GLU   A 1 25  ? 12.878 5.510   13.817  0.74 33.33 ?  25  GLU   A HG3  1 
ATOM   664  H  HG3  B GLU   A 1 25  ? 12.599 4.952   13.074  0.26 27.15 ?  25  GLU   A HG3  1 
ATOM   665  N  N    A GLU   A 1 26  ? 15.755 1.126   14.034  0.74 20.07 ?  26  GLU   A N    1 
ATOM   666  N  N    B GLU   A 1 26  ? 15.778 0.751   13.701  0.26 19.52 ?  26  GLU   A N    1 
ATOM   667  C  CA   A GLU   A 1 26  ? 16.069 -0.206  14.539  0.74 20.25 ?  26  GLU   A CA   1 
ATOM   668  C  CA   B GLU   A 1 26  ? 16.128 -0.516  14.339  0.26 19.18 ?  26  GLU   A CA   1 
ATOM   669  C  C    A GLU   A 1 26  ? 17.502 -0.270  15.051  0.74 19.17 ?  26  GLU   A C    1 
ATOM   670  C  C    B GLU   A 1 26  ? 17.533 -0.470  14.927  0.26 18.64 ?  26  GLU   A C    1 
ATOM   671  O  O    A GLU   A 1 26  ? 17.757 -0.757  16.159  0.74 19.35 ?  26  GLU   A O    1 
ATOM   672  O  O    B GLU   A 1 26  ? 17.791 -1.056  15.984  0.26 18.81 ?  26  GLU   A O    1 
ATOM   673  C  CB   A GLU   A 1 26  ? 15.847 -1.249  13.442  0.74 21.89 ?  26  GLU   A CB   1 
ATOM   674  C  CB   B GLU   A 1 26  ? 16.022 -1.667  13.335  0.26 19.32 ?  26  GLU   A CB   1 
ATOM   675  C  CG   A GLU   A 1 26  ? 14.416 -1.690  13.257  0.74 24.81 ?  26  GLU   A CG   1 
ATOM   676  C  CG   B GLU   A 1 26  ? 14.643 -2.267  13.199  0.26 18.71 ?  26  GLU   A CG   1 
ATOM   677  C  CD   A GLU   A 1 26  ? 13.863 -2.436  14.449  0.74 26.51 ?  26  GLU   A CD   1 
ATOM   678  C  CD   B GLU   A 1 26  ? 14.190 -2.923  14.484  0.26 17.40 ?  26  GLU   A CD   1 
ATOM   679  O  OE1  A GLU   A 1 26  ? 14.482 -3.430  14.889  0.74 26.59 ?  26  GLU   A OE1  1 
ATOM   680  O  OE1  B GLU   A 1 26  ? 14.544 -4.099  14.742  0.26 17.11 ?  26  GLU   A OE1  1 
ATOM   681  O  OE2  A GLU   A 1 26  ? 12.804 -2.010  14.945  0.74 28.44 -1 26  GLU   A OE2  1 
ATOM   682  O  OE2  B GLU   A 1 26  ? 13.498 -2.245  15.255  0.26 16.50 -1 26  GLU   A OE2  1 
ATOM   683  H  H    A GLU   A 1 26  ? 15.538 1.155   13.202  0.74 24.10 ?  26  GLU   A H    1 
ATOM   684  H  H    B GLU   A 1 26  ? 15.657 0.706   12.851  0.26 23.44 ?  26  GLU   A H    1 
ATOM   685  H  HA   A GLU   A 1 26  ? 15.477 -0.412  15.275  0.74 24.31 ?  26  GLU   A HA   1 
ATOM   686  H  HA   B GLU   A 1 26  ? 15.509 -0.684  15.065  0.26 23.02 ?  26  GLU   A HA   1 
ATOM   687  H  HB2  A GLU   A 1 26  ? 16.145 -0.875  12.595  0.74 26.28 ?  26  GLU   A HB2  1 
ATOM   688  H  HB2  B GLU   A 1 26  ? 16.289 -1.346  12.464  0.26 23.20 ?  26  GLU   A HB2  1 
ATOM   689  H  HB3  A GLU   A 1 26  ? 16.377 -2.034  13.651  0.74 26.28 ?  26  GLU   A HB3  1 
ATOM   690  H  HB3  B GLU   A 1 26  ? 16.618 -2.379  13.620  0.26 23.20 ?  26  GLU   A HB3  1 
ATOM   691  H  HG2  A GLU   A 1 26  ? 13.858 -0.913  13.147  0.74 29.78 ?  26  GLU   A HG2  1 
ATOM   692  H  HG2  B GLU   A 1 26  ? 14.014 -1.563  12.945  0.26 22.46 ?  26  GLU   A HG2  1 
ATOM   693  H  HG3  A GLU   A 1 26  ? 14.361 -2.262  12.475  0.74 29.78 ?  26  GLU   A HG3  1 
ATOM   694  H  HG3  B GLU   A 1 26  ? 14.653 -2.956  12.522  0.26 22.46 ?  26  GLU   A HG3  1 
ATOM   695  N  N    . ALA   A 1 27  ? 18.455 0.218   14.253  1.00 18.03 ?  27  ALA   A N    1 
ATOM   696  C  CA   . ALA   A 1 27  ? 19.850 0.217   14.689  1.00 18.11 ?  27  ALA   A CA   1 
ATOM   697  C  C    . ALA   A 1 27  ? 20.021 1.006   15.980  1.00 19.61 ?  27  ALA   A C    1 
ATOM   698  O  O    . ALA   A 1 27  ? 20.675 0.541   16.921  1.00 19.78 ?  27  ALA   A O    1 
ATOM   699  C  CB   . ALA   A 1 27  ? 20.747 0.777   13.582  1.00 17.61 ?  27  ALA   A CB   1 
ATOM   700  H  H    A ALA   A 1 27  ? 18.322 0.549   13.468  0.74 21.65 ?  27  ALA   A H    1 
ATOM   701  H  H    B ALA   A 1 27  ? 18.301 0.685   13.545  0.26 21.65 ?  27  ALA   A H    1 
ATOM   702  H  HA   . ALA   A 1 27  ? 20.124 -0.697  14.857  1.00 21.75 ?  27  ALA   A HA   1 
ATOM   703  H  HB1  . ALA   A 1 27  ? 21.670 0.770   13.888  1.00 21.14 ?  27  ALA   A HB1  1 
ATOM   704  H  HB2  . ALA   A 1 27  ? 20.660 0.225   12.789  1.00 21.14 ?  27  ALA   A HB2  1 
ATOM   705  H  HB3  . ALA   A 1 27  ? 20.476 1.688   13.381  1.00 21.14 ?  27  ALA   A HB3  1 
ATOM   706  N  N    A LYS   A 1 28  ? 19.429 2.201   16.049  0.74 20.83 ?  28  LYS   A N    1 
ATOM   707  N  N    B LYS   A 1 28  ? 19.426 2.200   16.052  0.26 21.83 ?  28  LYS   A N    1 
ATOM   708  C  CA   A LYS   A 1 28  ? 19.569 3.020   17.248  0.74 24.11 ?  28  LYS   A CA   1 
ATOM   709  C  CA   B LYS   A 1 28  ? 19.566 3.022   17.251  0.26 24.58 ?  28  LYS   A CA   1 
ATOM   710  C  C    A LYS   A 1 28  ? 19.027 2.312   18.483  0.74 25.23 ?  28  LYS   A C    1 
ATOM   711  C  C    B LYS   A 1 28  ? 19.020 2.320   18.487  0.26 25.25 ?  28  LYS   A C    1 
ATOM   712  O  O    A LYS   A 1 28  ? 19.586 2.462   19.575  0.74 27.51 ?  28  LYS   A O    1 
ATOM   713  O  O    B LYS   A 1 28  ? 19.557 2.496   19.586  0.26 26.44 ?  28  LYS   A O    1 
ATOM   714  C  CB   A LYS   A 1 28  ? 18.905 4.384   17.045  0.74 26.07 ?  28  LYS   A CB   1 
ATOM   715  C  CB   B LYS   A 1 28  ? 18.884 4.378   17.051  0.26 26.45 ?  28  LYS   A CB   1 
ATOM   716  C  CG   A LYS   A 1 28  ? 19.749 5.336   16.206  0.74 28.50 ?  28  LYS   A CG   1 
ATOM   717  C  CG   B LYS   A 1 28  ? 19.662 5.321   16.145  0.26 28.29 ?  28  LYS   A CG   1 
ATOM   718  C  CD   A LYS   A 1 28  ? 19.239 6.764   16.267  0.74 31.47 ?  28  LYS   A CD   1 
ATOM   719  C  CD   B LYS   A 1 28  ? 19.166 6.756   16.246  0.26 30.11 ?  28  LYS   A CD   1 
ATOM   720  C  CE   A LYS   A 1 28  ? 17.951 6.915   15.491  0.74 33.38 ?  28  LYS   A CE   1 
ATOM   721  C  CE   B LYS   A 1 28  ? 17.827 6.936   15.556  0.26 31.35 ?  28  LYS   A CE   1 
ATOM   722  N  NZ   A LYS   A 1 28  ? 17.473 8.325   15.497  0.74 34.52 ?  28  LYS   A NZ   1 
ATOM   723  N  NZ   B LYS   A 1 28  ? 17.419 8.368   15.515  0.26 32.01 ?  28  LYS   A NZ   1 
ATOM   724  H  H    A LYS   A 1 28  ? 18.954 2.552   15.426  0.74 25.01 ?  28  LYS   A H    1 
ATOM   725  H  H    B LYS   A 1 28  ? 18.948 2.550   15.431  0.26 26.21 ?  28  LYS   A H    1 
ATOM   726  H  HA   A LYS   A 1 28  ? 20.509 3.180   17.407  0.74 28.94 ?  28  LYS   A HA   1 
ATOM   727  H  HA   B LYS   A 1 28  ? 20.505 3.187   17.407  0.26 29.50 ?  28  LYS   A HA   1 
ATOM   728  H  HB2  A LYS   A 1 28  ? 18.058 4.263   16.591  0.74 31.29 ?  28  LYS   A HB2  1 
ATOM   729  H  HB2  B LYS   A 1 28  ? 18.012 4.238   16.651  0.26 31.75 ?  28  LYS   A HB2  1 
ATOM   730  H  HB3  A LYS   A 1 28  ? 18.761 4.802   17.909  0.74 31.29 ?  28  LYS   A HB3  1 
ATOM   731  H  HB3  B LYS   A 1 28  ? 18.786 4.812   17.913  0.26 31.75 ?  28  LYS   A HB3  1 
ATOM   732  H  HG2  A LYS   A 1 28  ? 20.661 5.328   16.536  0.74 34.21 ?  28  LYS   A HG2  1 
ATOM   733  H  HG2  B LYS   A 1 28  ? 20.598 5.307   16.400  0.26 33.95 ?  28  LYS   A HG2  1 
ATOM   734  H  HG3  A LYS   A 1 28  ? 19.727 5.048   15.280  0.74 34.21 ?  28  LYS   A HG3  1 
ATOM   735  H  HG3  B LYS   A 1 28  ? 19.562 5.032   15.225  0.26 33.95 ?  28  LYS   A HG3  1 
ATOM   736  H  HD2  A LYS   A 1 28  ? 19.070 7.006   17.191  0.74 37.77 ?  28  LYS   A HD2  1 
ATOM   737  H  HD2  B LYS   A 1 28  ? 19.059 6.992   17.182  0.26 36.14 ?  28  LYS   A HD2  1 
ATOM   738  H  HD3  A LYS   A 1 28  ? 19.901 7.358   15.879  0.74 37.77 ?  28  LYS   A HD3  1 
ATOM   739  H  HD3  B LYS   A 1 28  ? 19.808 7.347   15.823  0.26 36.14 ?  28  LYS   A HD3  1 
ATOM   740  H  HE2  A LYS   A 1 28  ? 18.101 6.647   14.571  0.74 40.06 ?  28  LYS   A HE2  1 
ATOM   741  H  HE2  B LYS   A 1 28  ? 17.892 6.613   14.643  0.26 37.63 ?  28  LYS   A HE2  1 
ATOM   742  H  HE3  A LYS   A 1 28  ? 17.267 6.359   15.896  0.74 40.06 ?  28  LYS   A HE3  1 
ATOM   743  H  HE3  B LYS   A 1 28  ? 17.148 6.441   16.039  0.26 37.63 ?  28  LYS   A HE3  1 
ATOM   744  H  HZ1  A LYS   A 1 28  ? 16.716 8.391   15.035  0.74 41.43 ?  28  LYS   A HZ1  1 
ATOM   745  H  HZ1  B LYS   A 1 28  ? 16.634 8.450   15.106  0.26 38.42 ?  28  LYS   A HZ1  1 
ATOM   746  H  HZ2  A LYS   A 1 28  ? 17.328 8.593   16.333  0.74 41.43 ?  28  LYS   A HZ2  1 
ATOM   747  H  HZ2  B LYS   A 1 28  ? 17.350 8.688   16.343  0.26 38.42 ?  28  LYS   A HZ2  1 
ATOM   748  H  HZ3  A LYS   A 1 28  ? 18.086 8.855   15.126  0.74 41.43 ?  28  LYS   A HZ3  1 
ATOM   749  H  HZ3  B LYS   A 1 28  ? 18.027 8.845   15.072  0.26 38.42 ?  28  LYS   A HZ3  1 
ATOM   750  N  N    . LYS   A 1 29  ? 17.965 1.520   18.332  1.00 24.94 ?  29  LYS   A N    1 
ATOM   751  C  CA   . LYS   A 1 29  ? 17.372 0.831   19.476  1.00 27.06 ?  29  LYS   A CA   1 
ATOM   752  C  C    . LYS   A 1 29  ? 18.178 -0.402  19.873  1.00 26.68 ?  29  LYS   A C    1 
ATOM   753  O  O    . LYS   A 1 29  ? 18.438 -0.629  21.061  1.00 28.55 ?  29  LYS   A O    1 
ATOM   754  C  CB   . LYS   A 1 29  ? 15.934 0.429   19.143  1.00 30.49 ?  29  LYS   A CB   1 
ATOM   755  C  CG   . LYS   A 1 29  ? 15.183 -0.225  20.293  1.00 33.97 ?  29  LYS   A CG   1 
ATOM   756  C  CD   . LYS   A 1 29  ? 14.812 0.794   21.358  1.00 36.97 ?  29  LYS   A CD   1 
ATOM   757  C  CE   . LYS   A 1 29  ? 13.956 0.174   22.453  1.00 39.04 ?  29  LYS   A CE   1 
ATOM   758  N  NZ   . LYS   A 1 29  ? 13.540 1.179   23.471  1.00 40.31 ?  29  LYS   A NZ   1 
ATOM   759  H  H    A LYS   A 1 29  ? 17.573 1.364   17.583  0.74 29.93 ?  29  LYS   A H    1 
ATOM   760  H  H    B LYS   A 1 29  ? 17.572 1.365   17.583  0.26 29.93 ?  29  LYS   A H    1 
ATOM   761  H  HA   . LYS   A 1 29  ? 17.349 1.433   20.235  1.00 32.48 ?  29  LYS   A HA   1 
ATOM   762  H  HB2  . LYS   A 1 29  ? 15.441 1.223   18.888  1.00 36.60 ?  29  LYS   A HB2  1 
ATOM   763  H  HB3  . LYS   A 1 29  ? 15.948 -0.201  18.407  1.00 36.60 ?  29  LYS   A HB3  1 
ATOM   764  H  HG2  . LYS   A 1 29  ? 14.363 -0.622  19.956  1.00 40.78 ?  29  LYS   A HG2  1 
ATOM   765  H  HG3  . LYS   A 1 29  ? 15.736 -0.909  20.705  1.00 40.78 ?  29  LYS   A HG3  1 
ATOM   766  H  HD2  . LYS   A 1 29  ? 15.621 1.141   21.765  1.00 44.37 ?  29  LYS   A HD2  1 
ATOM   767  H  HD3  . LYS   A 1 29  ? 14.307 1.514   20.948  1.00 44.37 ?  29  LYS   A HD3  1 
ATOM   768  H  HE2  . LYS   A 1 29  ? 13.156 -0.205  22.056  1.00 46.85 ?  29  LYS   A HE2  1 
ATOM   769  H  HE3  . LYS   A 1 29  ? 14.466 -0.519  22.902  1.00 46.85 ?  29  LYS   A HE3  1 
ATOM   770  H  HZ1  . LYS   A 1 29  ? 13.041 0.789   24.097  1.00 48.38 ?  29  LYS   A HZ1  1 
ATOM   771  H  HZ2  . LYS   A 1 29  ? 14.257 1.539   23.855  1.00 48.38 ?  29  LYS   A HZ2  1 
ATOM   772  H  HZ3  . LYS   A 1 29  ? 13.064 1.824   23.084  1.00 48.38 ?  29  LYS   A HZ3  1 
ATOM   773  N  N    . VAL   A 1 30  ? 18.563 -1.217  18.895  1.00 25.60 ?  30  VAL   A N    1 
ATOM   774  C  CA   . VAL   A 1 30  ? 19.195 -2.500  19.176  1.00 24.73 ?  30  VAL   A CA   1 
ATOM   775  C  C    . VAL   A 1 30  ? 20.704 -2.379  19.392  1.00 23.71 ?  30  VAL   A C    1 
ATOM   776  O  O    . VAL   A 1 30  ? 21.275 -3.136  20.183  1.00 24.19 ?  30  VAL   A O    1 
ATOM   777  C  CB   . VAL   A 1 30  ? 18.873 -3.479  18.033  1.00 25.70 ?  30  VAL   A CB   1 
ATOM   778  C  CG1  . VAL   A 1 30  ? 19.612 -4.793  18.223  1.00 26.07 ?  30  VAL   A CG1  1 
ATOM   779  C  CG2  . VAL   A 1 30  ? 17.366 -3.710  17.934  1.00 26.66 ?  30  VAL   A CG2  1 
ATOM   780  H  H    . VAL   A 1 30  ? 18.465 -1.055  18.056  1.00 30.73 ?  30  VAL   A H    1 
ATOM   781  H  HA   . VAL   A 1 30  ? 18.810 -2.864  19.987  1.00 29.68 ?  30  VAL   A HA   1 
ATOM   782  H  HB   . VAL   A 1 30  ? 19.171 -3.091  17.195  1.00 30.85 ?  30  VAL   A HB   1 
ATOM   783  H  HG11 . VAL   A 1 30  ? 19.214 -5.461  17.642  1.00 31.29 ?  30  VAL   A HG11 1 
ATOM   784  H  HG12 . VAL   A 1 30  ? 20.545 -4.671  17.994  1.00 31.29 ?  30  VAL   A HG12 1 
ATOM   785  H  HG13 . VAL   A 1 30  ? 19.527 -5.070  19.149  1.00 31.29 ?  30  VAL   A HG13 1 
ATOM   786  H  HG21 . VAL   A 1 30  ? 17.191 -4.366  17.241  1.00 32.00 ?  30  VAL   A HG21 1 
ATOM   787  H  HG22 . VAL   A 1 30  ? 17.040 -4.036  18.788  1.00 32.00 ?  30  VAL   A HG22 1 
ATOM   788  H  HG23 . VAL   A 1 30  ? 16.930 -2.872  17.712  1.00 32.00 ?  30  VAL   A HG23 1 
ATOM   789  N  N    . LYS   A 1 31  ? 21.359 -1.441  18.717  1.00 21.98 ?  31  LYS   A N    1 
ATOM   790  C  CA   . LYS   A 1 31  ? 22.816 -1.364  18.670  1.00 23.13 ?  31  LYS   A CA   1 
ATOM   791  C  C    . LYS   A 1 31  ? 23.407 -2.731  18.315  1.00 20.37 ?  31  LYS   A C    1 
ATOM   792  O  O    . LYS   A 1 31  ? 24.168 -3.310  19.096  1.00 21.70 ?  31  LYS   A O    1 
ATOM   793  C  CB   . LYS   A 1 31  ? 23.396 -0.839  19.976  1.00 28.56 ?  31  LYS   A CB   1 
ATOM   794  C  CG   . LYS   A 1 31  ? 22.741 0.443   20.460  1.00 35.38 ?  31  LYS   A CG   1 
ATOM   795  C  CD   . LYS   A 1 31  ? 23.772 1.499   20.836  1.00 40.64 ?  31  LYS   A CD   1 
ATOM   796  C  CE   . LYS   A 1 31  ? 23.174 2.556   21.756  1.00 43.99 ?  31  LYS   A CE   1 
ATOM   797  N  NZ   . LYS   A 1 31  ? 21.997 3.246   21.159  1.00 45.59 ?  31  LYS   A NZ   1 
ATOM   798  H  H    . LYS   A 1 31  ? 20.975 -0.811  18.274  1.00 26.39 ?  31  LYS   A H    1 
ATOM   799  H  HA   . LYS   A 1 31  ? 23.068 -0.747  17.969  1.00 27.76 ?  31  LYS   A HA   1 
ATOM   800  H  HB2  . LYS   A 1 31  ? 23.281 -1.512  20.662  1.00 34.28 ?  31  LYS   A HB2  1 
ATOM   801  H  HB3  . LYS   A 1 31  ? 24.343 -0.660  19.847  1.00 34.28 ?  31  LYS   A HB3  1 
ATOM   802  H  HG2  . LYS   A 1 31  ? 22.185 0.804   19.752  1.00 42.47 ?  31  LYS   A HG2  1 
ATOM   803  H  HG3  . LYS   A 1 31  ? 22.205 0.251   21.244  1.00 42.47 ?  31  LYS   A HG3  1 
ATOM   804  H  HD2  . LYS   A 1 31  ? 24.512 1.076   21.300  1.00 48.78 ?  31  LYS   A HD2  1 
ATOM   805  H  HD3  . LYS   A 1 31  ? 24.089 1.939   20.031  1.00 48.78 ?  31  LYS   A HD3  1 
ATOM   806  H  HE2  . LYS   A 1 31  ? 22.887 2.131   22.579  1.00 52.79 ?  31  LYS   A HE2  1 
ATOM   807  H  HE3  . LYS   A 1 31  ? 23.848 3.226   21.947  1.00 52.79 ?  31  LYS   A HE3  1 
ATOM   808  H  HZ1  . LYS   A 1 31  ? 21.683 3.858   21.725  1.00 54.72 ?  31  LYS   A HZ1  1 
ATOM   809  H  HZ2  . LYS   A 1 31  ? 22.231 3.647   20.400  1.00 54.72 ?  31  LYS   A HZ2  1 
ATOM   810  H  HZ3  . LYS   A 1 31  ? 21.353 2.656   20.987  1.00 54.72 ?  31  LYS   A HZ3  1 
ATOM   811  N  N    . PRO   A 1 32  ? 23.064 -3.272  17.150  1.00 17.93 ?  32  PRO   A N    1 
ATOM   812  C  CA   . PRO   A 1 32  ? 23.538 -4.607  16.789  1.00 18.30 ?  32  PRO   A CA   1 
ATOM   813  C  C    . PRO   A 1 32  ? 25.040 -4.619  16.571  1.00 18.03 ?  32  PRO   A C    1 
ATOM   814  O  O    . PRO   A 1 32  ? 25.681 -3.588  16.355  1.00 18.48 ?  32  PRO   A O    1 
ATOM   815  C  CB   . PRO   A 1 32  ? 22.799 -4.893  15.478  1.00 18.64 ?  32  PRO   A CB   1 
ATOM   816  C  CG   . PRO   A 1 32  ? 22.610 -3.536  14.874  1.00 17.62 ?  32  PRO   A CG   1 
ATOM   817  C  CD   . PRO   A 1 32  ? 22.313 -2.648  16.049  1.00 17.07 ?  32  PRO   A CD   1 
ATOM   818  H  HA   . PRO   A 1 32  ? 23.292 -5.265  17.461  1.00 21.97 ?  32  PRO   A HA   1 
ATOM   819  H  HB2  . PRO   A 1 32  ? 23.343 -5.460  14.905  1.00 22.38 ?  32  PRO   A HB2  1 
ATOM   820  H  HB3  . PRO   A 1 32  ? 21.943 -5.317  15.666  1.00 22.38 ?  32  PRO   A HB3  1 
ATOM   821  H  HG2  . PRO   A 1 32  ? 23.423 -3.267  14.425  1.00 21.15 ?  32  PRO   A HG2  1 
ATOM   822  H  HG3  . PRO   A 1 32  ? 21.861 -3.559  14.257  1.00 21.15 ?  32  PRO   A HG3  1 
ATOM   823  H  HD2  . PRO   A 1 32  ? 22.644 -1.754  15.875  1.00 20.49 ?  32  PRO   A HD2  1 
ATOM   824  H  HD3  . PRO   A 1 32  ? 21.366 -2.652  16.241  1.00 20.49 ?  32  PRO   A HD3  1 
ATOM   825  N  N    . THR   A 1 33  ? 25.598 -5.830  16.607  1.00 18.13 ?  33  THR   A N    1 
ATOM   826  C  CA   . THR   A 1 33  ? 27.009 -5.992  16.285  1.00 18.33 ?  33  THR   A CA   1 
ATOM   827  C  C    . THR   A 1 33  ? 27.300 -5.527  14.863  1.00 16.52 ?  33  THR   A C    1 
ATOM   828  O  O    . THR   A 1 33  ? 28.336 -4.894  14.609  1.00 17.11 ?  33  THR   A O    1 
ATOM   829  C  CB   . THR   A 1 33  ? 27.421 -7.452  16.486  1.00 19.88 ?  33  THR   A CB   1 
ATOM   830  O  OG1  . THR   A 1 33  ? 27.126 -7.846  17.831  1.00 22.44 ?  33  THR   A OG1  1 
ATOM   831  C  CG2  . THR   A 1 33  ? 28.910 -7.636  16.234  1.00 22.07 ?  33  THR   A CG2  1 
ATOM   832  H  H    . THR   A 1 33  ? 25.188 -6.563  16.801  1.00 21.76 ?  33  THR   A H    1 
ATOM   833  H  HA   . THR   A 1 33  ? 27.536 -5.450  16.886  1.00 22.00 ?  33  THR   A HA   1 
ATOM   834  H  HB   . THR   A 1 33  ? 26.930 -8.022  15.867  1.00 23.87 ?  33  THR   A HB   1 
ATOM   835  H  HG1  . THR   A 1 33  ? 27.545 -7.351  18.370  1.00 26.94 ?  33  THR   A HG1  1 
ATOM   836  H  HG21 . THR   A 1 33  ? 29.185 -8.524  16.513  1.00 26.49 ?  33  THR   A HG21 1 
ATOM   837  H  HG22 . THR   A 1 33  ? 29.106 -7.527  15.292  1.00 26.49 ?  33  THR   A HG22 1 
ATOM   838  H  HG23 . THR   A 1 33  ? 29.411 -6.979  16.741  1.00 26.49 ?  33  THR   A HG23 1 
ATOM   839  N  N    . VAL   A 1 34  ? 26.397 -5.827  13.925  1.00 14.81 ?  34  VAL   A N    1 
ATOM   840  C  CA   . VAL   A 1 34  ? 26.579 -5.485  12.519  1.00 13.92 ?  34  VAL   A CA   1 
ATOM   841  C  C    . VAL   A 1 34  ? 25.278 -4.923  11.957  1.00 13.39 ?  34  VAL   A C    1 
ATOM   842  O  O    . VAL   A 1 34  ? 24.236 -5.591  12.009  1.00 14.26 ?  34  VAL   A O    1 
ATOM   843  C  CB   . VAL   A 1 34  ? 27.022 -6.689  11.668  1.00 14.74 ?  34  VAL   A CB   1 
ATOM   844  C  CG1  . VAL   A 1 34  ? 27.187 -6.270  10.214  1.00 14.94 ?  34  VAL   A CG1  1 
ATOM   845  C  CG2  . VAL   A 1 34  ? 28.308 -7.307  12.209  1.00 16.32 ?  34  VAL   A CG2  1 
ATOM   846  H  H    . VAL   A 1 34  ? 25.649 -6.228  14.086  1.00 17.78 ?  34  VAL   A H    1 
ATOM   847  H  HA   . VAL   A 1 34  ? 27.259 -4.797  12.440  1.00 16.71 ?  34  VAL   A HA   1 
ATOM   848  H  HB   . VAL   A 1 34  ? 26.330 -7.368  11.704  1.00 17.69 ?  34  VAL   A HB   1 
ATOM   849  H  HG11 . VAL   A 1 34  ? 27.703 -6.946  9.748   1.00 17.94 ?  34  VAL   A HG11 1 
ATOM   850  H  HG12 . VAL   A 1 34  ? 26.314 -6.180  9.805   1.00 17.94 ?  34  VAL   A HG12 1 
ATOM   851  H  HG13 . VAL   A 1 34  ? 27.659 -5.420  10.183  1.00 17.94 ?  34  VAL   A HG13 1 
ATOM   852  H  HG21 . VAL   A 1 34  ? 28.569 -8.048  11.636  1.00 19.59 ?  34  VAL   A HG21 1 
ATOM   853  H  HG22 . VAL   A 1 34  ? 29.006 -6.636  12.218  1.00 19.59 ?  34  VAL   A HG22 1 
ATOM   854  H  HG23 . VAL   A 1 34  ? 28.150 -7.633  13.111  1.00 19.59 ?  34  VAL   A HG23 1 
ATOM   855  N  N    . VAL   A 1 35  ? 25.335 -3.707  11.419  1.00 12.85 ?  35  VAL   A N    1 
ATOM   856  C  CA   . VAL   A 1 35  ? 24.308 -3.185  10.523  1.00 12.07 ?  35  VAL   A CA   1 
ATOM   857  C  C    . VAL   A 1 35  ? 24.861 -3.188  9.101   1.00 11.85 ?  35  VAL   A C    1 
ATOM   858  O  O    . VAL   A 1 35  ? 26.017 -2.803  8.875   1.00 12.68 ?  35  VAL   A O    1 
ATOM   859  C  CB   . VAL   A 1 35  ? 23.790 -1.787  10.934  1.00 13.14 ?  35  VAL   A CB   1 
ATOM   860  C  CG1  . VAL   A 1 35  ? 24.872 -0.698  10.811  1.00 14.04 ?  35  VAL   A CG1  1 
ATOM   861  C  CG2  . VAL   A 1 35  ? 22.557 -1.425  10.117  1.00 13.94 ?  35  VAL   A CG2  1 
ATOM   862  H  H    . VAL   A 1 35  ? 25.972 -3.148  11.559  1.00 15.43 ?  35  VAL   A H    1 
ATOM   863  H  HA   . VAL   A 1 35  ? 23.544 -3.789  10.541  1.00 14.49 ?  35  VAL   A HA   1 
ATOM   864  H  HB   . VAL   A 1 35  ? 23.515 -1.822  11.860  1.00 15.77 ?  35  VAL   A HB   1 
ATOM   865  H  HG11 . VAL   A 1 35  ? 24.530 0.139   11.169  1.00 16.85 ?  35  VAL   A HG11 1 
ATOM   866  H  HG12 . VAL   A 1 35  ? 25.658 -0.970  11.318  1.00 16.85 ?  35  VAL   A HG12 1 
ATOM   867  H  HG13 . VAL   A 1 35  ? 25.113 -0.579  9.878   1.00 16.85 ?  35  VAL   A HG13 1 
ATOM   868  H  HG21 . VAL   A 1 35  ? 22.211 -0.578  10.428  1.00 16.73 ?  35  VAL   A HG21 1 
ATOM   869  H  HG22 . VAL   A 1 35  ? 22.812 -1.353  9.179   1.00 16.73 ?  35  VAL   A HG22 1 
ATOM   870  H  HG23 . VAL   A 1 35  ? 21.893 -2.121  10.224  1.00 16.73 ?  35  VAL   A HG23 1 
ATOM   871  N  N    . VAL   A 1 36  ? 24.042 -3.647  8.144   1.00 11.27 ?  36  VAL   A N    1 
ATOM   872  C  CA   . VAL   A 1 36  ? 24.414 -3.664  6.730   1.00 10.74 ?  36  VAL   A CA   1 
ATOM   873  C  C    . VAL   A 1 36  ? 23.953 -2.366  6.081   1.00 11.14 ?  36  VAL   A C    1 
ATOM   874  O  O    . VAL   A 1 36  ? 22.795 -1.962  6.234   1.00 11.77 ?  36  VAL   A O    1 
ATOM   875  C  CB   . VAL   A 1 36  ? 23.805 -4.882  6.011   1.00 11.06 ?  36  VAL   A CB   1 
ATOM   876  C  CG1  . VAL   A 1 36  ? 24.097 -4.827  4.526   1.00 11.69 ?  36  VAL   A CG1  1 
ATOM   877  C  CG2  . VAL   A 1 36  ? 24.341 -6.182  6.604   1.00 12.72 ?  36  VAL   A CG2  1 
ATOM   878  H  H    . VAL   A 1 36  ? 23.250 -3.963  8.296   1.00 13.54 ?  36  VAL   A H    1 
ATOM   879  H  HA   . VAL   A 1 36  ? 25.380 -3.725  6.657   1.00 12.90 ?  36  VAL   A HA   1 
ATOM   880  H  HB   . VAL   A 1 36  ? 22.840 -4.871  6.131   1.00 13.27 ?  36  VAL   A HB   1 
ATOM   881  H  HG11 . VAL   A 1 36  ? 23.920 -5.699  4.139   1.00 14.03 ?  36  VAL   A HG11 1 
ATOM   882  H  HG12 . VAL   A 1 36  ? 23.528 -4.161  4.111   1.00 14.03 ?  36  VAL   A HG12 1 
ATOM   883  H  HG13 . VAL   A 1 36  ? 25.031 -4.595  4.398   1.00 14.03 ?  36  VAL   A HG13 1 
ATOM   884  H  HG21 . VAL   A 1 36  ? 23.951 -6.935  6.128   1.00 15.28 ?  36  VAL   A HG21 1 
ATOM   885  H  HG22 . VAL   A 1 36  ? 25.307 -6.200  6.509   1.00 15.28 ?  36  VAL   A HG22 1 
ATOM   886  H  HG23 . VAL   A 1 36  ? 24.102 -6.230  7.544   1.00 15.28 ?  36  VAL   A HG23 1 
ATOM   887  N  N    . ASN   A 1 37  ? 24.855 -1.721  5.343   1.00 10.49 ?  37  ASN   A N    1 
ATOM   888  C  CA   . ASN   A 1 37  ? 24.525 -0.608  4.474   1.00 10.49 ?  37  ASN   A CA   1 
ATOM   889  C  C    . ASN   A 1 37  ? 24.388 -1.078  3.031   1.00 11.04 ?  37  ASN   A C    1 
ATOM   890  O  O    . ASN   A 1 37  ? 25.184 -1.893  2.542   1.00 11.47 ?  37  ASN   A O    1 
ATOM   891  C  CB   . ASN   A 1 37  ? 25.614 0.462   4.546   1.00 11.65 ?  37  ASN   A CB   1 
ATOM   892  C  CG   . ASN   A 1 37  ? 25.276 1.678   3.706   1.00 11.63 ?  37  ASN   A CG   1 
ATOM   893  O  OD1  . ASN   A 1 37  ? 24.101 2.032   3.537   1.00 11.94 ?  37  ASN   A OD1  1 
ATOM   894  N  ND2  . ASN   A 1 37  ? 26.317 2.338   3.172   1.00 11.48 ?  37  ASN   A ND2  1 
ATOM   895  H  H    . ASN   A 1 37  ? 25.696 -1.922  5.336   1.00 12.59 ?  37  ASN   A H    1 
ATOM   896  H  HA   . ASN   A 1 37  ? 23.693 -0.207  4.761   1.00 12.60 ?  37  ASN   A HA   1 
ATOM   897  H  HB2  . ASN   A 1 37  ? 25.721 0.754   5.470   1.00 13.99 ?  37  ASN   A HB2  1 
ATOM   898  H  HB3  . ASN   A 1 37  ? 26.457 0.086   4.228   1.00 13.99 ?  37  ASN   A HB3  1 
ATOM   899  H  HD21 . ASN   A 1 37  ? 26.181 3.035   2.684   1.00 13.78 ?  37  ASN   A HD21 1 
ATOM   900  H  HD22 . ASN   A 1 37  ? 27.122 2.073   3.310   1.00 13.78 ?  37  ASN   A HD22 1 
ATOM   901  N  N    . ALA   A 1 38  ? 23.405 -0.500  2.338   1.00 11.26 ?  38  ALA   A N    1 
ATOM   902  C  CA   . ALA   A 1 38  ? 23.207 -0.687  0.900   1.00 11.26 ?  38  ALA   A CA   1 
ATOM   903  C  C    . ALA   A 1 38  ? 24.105 0.318   0.186   1.00 11.96 ?  38  ALA   A C    1 
ATOM   904  O  O    . ALA   A 1 38  ? 23.679 1.397   -0.232  1.00 11.87 ?  38  ALA   A O    1 
ATOM   905  C  CB   . ALA   A 1 38  ? 21.739 -0.478  0.544   1.00 13.28 ?  38  ALA   A CB   1 
ATOM   906  H  H    . ALA   A 1 38  ? 22.836 0.035   2.694   1.00 13.52 ?  38  ALA   A H    1 
ATOM   907  H  HA   . ALA   A 1 38  ? 23.473 -1.588  0.648   1.00 13.52 ?  38  ALA   A HA   1 
ATOM   908  H  HB1  . ALA   A 1 38  ? 21.573 -0.844  -0.336  1.00 15.94 ?  38  ALA   A HB1  1 
ATOM   909  H  HB2  . ALA   A 1 38  ? 21.186 -0.933  1.203   1.00 15.94 ?  38  ALA   A HB2  1 
ATOM   910  H  HB3  . ALA   A 1 38  ? 21.550 0.469   0.553   1.00 15.94 ?  38  ALA   A HB3  1 
ATOM   911  N  N    A ALA   A 1 39  ? 25.375 -0.056  0.054   0.74 11.70 ?  39  ALA   A N    1 
ATOM   912  N  N    B ALA   A 1 39  ? 25.378 -0.042  0.073   0.26 11.90 ?  39  ALA   A N    1 
ATOM   913  C  CA   A ALA   A 1 39  ? 26.428 0.818   -0.440  0.74 11.55 ?  39  ALA   A CA   1 
ATOM   914  C  CA   B ALA   A 1 39  ? 26.401 0.874   -0.404  0.26 12.10 ?  39  ALA   A CA   1 
ATOM   915  C  C    A ALA   A 1 39  ? 26.539 0.780   -1.963  0.74 11.17 ?  39  ALA   A C    1 
ATOM   916  C  C    B ALA   A 1 39  ? 26.598 0.746   -1.911  0.26 11.70 ?  39  ALA   A C    1 
ATOM   917  O  O    A ALA   A 1 39  ? 26.005 -0.109  -2.634  0.74 11.80 ?  39  ALA   A O    1 
ATOM   918  O  O    B ALA   A 1 39  ? 26.248 -0.262  -2.530  0.26 11.28 ?  39  ALA   A O    1 
ATOM   919  C  CB   A ALA   A 1 39  ? 27.757 0.373   0.168   0.74 12.56 ?  39  ALA   A CB   1 
ATOM   920  C  CB   B ALA   A 1 39  ? 27.722 0.595   0.313   0.26 12.69 ?  39  ALA   A CB   1 
ATOM   921  H  H    A ALA   A 1 39  ? 25.656 -0.846  0.256   0.74 14.05 ?  39  ALA   A H    1 
ATOM   922  H  H    B ALA   A 1 39  ? 25.678 -0.827  0.268   0.26 14.28 ?  39  ALA   A H    1 
ATOM   923  H  HA   A ALA   A 1 39  ? 26.244 1.729   -0.161  0.74 13.87 ?  39  ALA   A HA   1 
ATOM   924  H  HA   B ALA   A 1 39  ? 26.133 1.781   -0.209  0.26 14.53 ?  39  ALA   A HA   1 
ATOM   925  H  HB1  A ALA   A 1 39  ? 28.460 0.955   -0.158  0.74 15.08 ?  39  ALA   A HB1  1 
ATOM   926  H  HB1  B ALA   A 1 39  ? 28.395 1.211   -0.015  0.26 15.23 ?  39  ALA   A HB1  1 
ATOM   927  H  HB2  A ALA   A 1 39  ? 27.699 0.434   1.135   0.74 15.08 ?  39  ALA   A HB2  1 
ATOM   928  H  HB2  B ALA   A 1 39  ? 27.596 0.720   1.267   0.26 15.23 ?  39  ALA   A HB2  1 
ATOM   929  H  HB3  A ALA   A 1 39  ? 27.934 -0.543  -0.095  0.74 15.08 ?  39  ALA   A HB3  1 
ATOM   930  H  HB3  B ALA   A 1 39  ? 27.995 -0.319  0.134   0.26 15.23 ?  39  ALA   A HB3  1 
ATOM   931  N  N    A ASN   A 1 40  ? 27.235 1.783   -2.504  0.74 11.81 ?  40  ASN   A N    1 
ATOM   932  N  N    B ASN   A 1 40  ? 27.166 1.800   -2.500  0.26 12.18 ?  40  ASN   A N    1 
ATOM   933  C  CA   A ASN   A 1 40  ? 27.776 1.731   -3.856  0.74 11.70 ?  40  ASN   A CA   1 
ATOM   934  C  CA   B ASN   A 1 40  ? 27.640 1.758   -3.873  0.26 12.62 ?  40  ASN   A CA   1 
ATOM   935  C  C    A ASN   A 1 40  ? 29.301 1.630   -3.788  0.74 10.89 ?  40  ASN   A C    1 
ATOM   936  C  C    B ASN   A 1 40  ? 29.158 1.608   -3.884  0.26 12.55 ?  40  ASN   A C    1 
ATOM   937  O  O    A ASN   A 1 40  ? 29.906 1.749   -2.718  0.74 11.10 ?  40  ASN   A O    1 
ATOM   938  O  O    B ASN   A 1 40  ? 29.822 1.625   -2.845  0.26 12.89 ?  40  ASN   A O    1 
ATOM   939  C  CB   A ASN   A 1 40  ? 27.288 2.920   -4.709  0.74 12.74 ?  40  ASN   A CB   1 
ATOM   940  C  CB   B ASN   A 1 40  ? 27.188 2.990   -4.662  0.26 12.97 ?  40  ASN   A CB   1 
ATOM   941  C  CG   A ASN   A 1 40  ? 27.673 4.271   -4.135  0.74 14.16 ?  40  ASN   A CG   1 
ATOM   942  C  CG   B ASN   A 1 40  ? 27.573 4.290   -3.994  0.26 13.93 ?  40  ASN   A CG   1 
ATOM   943  O  OD1  A ASN   A 1 40  ? 28.839 4.519   -3.825  0.74 15.94 ?  40  ASN   A OD1  1 
ATOM   944  O  OD1  B ASN   A 1 40  ? 28.751 4.644   -3.928  0.26 14.19 ?  40  ASN   A OD1  1 
ATOM   945  N  ND2  A ASN   A 1 40  ? 26.683 5.158   -3.998  0.74 13.87 ?  40  ASN   A ND2  1 
ATOM   946  N  ND2  B ASN   A 1 40  ? 26.575 5.017   -3.505  0.26 14.18 ?  40  ASN   A ND2  1 
ATOM   947  H  H    A ASN   A 1 40  ? 27.409 2.513   -2.092  0.74 14.18 ?  40  ASN   A H    1 
ATOM   948  H  H    B ASN   A 1 40  ? 27.290 2.557   -2.110  0.26 14.63 ?  40  ASN   A H    1 
ATOM   949  H  HA   A ASN   A 1 40  ? 27.452 0.923   -4.284  0.74 14.05 ?  40  ASN   A HA   1 
ATOM   950  H  HA   B ASN   A 1 40  ? 27.272 0.973   -4.309  0.26 15.15 ?  40  ASN   A HA   1 
ATOM   951  H  HB2  A ASN   A 1 40  ? 27.673 2.844   -5.599  0.74 15.30 ?  40  ASN   A HB2  1 
ATOM   952  H  HB2  B ASN   A 1 40  ? 27.601 2.970   -5.541  0.26 15.57 ?  40  ASN   A HB2  1 
ATOM   953  H  HB3  A ASN   A 1 40  ? 26.320 2.889   -4.769  0.74 15.30 ?  40  ASN   A HB3  1 
ATOM   954  H  HB3  B ASN   A 1 40  ? 26.225 2.968   -4.750  0.26 15.57 ?  40  ASN   A HB3  1 
ATOM   955  H  HD21 A ASN   A 1 40  ? 26.849 5.941   -3.682  0.74 16.65 ?  40  ASN   A HD21 1 
ATOM   956  H  HD21 B ASN   A 1 40  ? 26.740 5.764   -3.116  0.26 17.03 ?  40  ASN   A HD21 1 
ATOM   957  H  HD22 A ASN   A 1 40  ? 25.883 4.941   -4.216  0.74 16.65 ?  40  ASN   A HD22 1 
ATOM   958  H  HD22 B ASN   A 1 40  ? 25.765 4.735   -3.574  0.26 17.03 ?  40  ASN   A HD22 1 
ATOM   959  N  N    A VAL   A 1 41  ? 29.926 1.369   -4.940  0.74 11.32 ?  41  VAL   A N    1 
ATOM   960  N  N    B VAL   A 1 41  ? 29.713 1.454   -5.086  0.26 12.55 ?  41  VAL   A N    1 
ATOM   961  C  CA   A VAL   A 1 41  ? 31.358 1.071   -4.961  0.74 11.53 ?  41  VAL   A CA   1 
ATOM   962  C  CA   B VAL   A 1 41  ? 31.137 1.154   -5.205  0.26 12.54 ?  41  VAL   A CA   1 
ATOM   963  C  C    A VAL   A 1 41  ? 32.214 2.236   -4.503  0.74 12.74 ?  41  VAL   A C    1 
ATOM   964  C  C    B VAL   A 1 41  ? 32.000 2.280   -4.654  0.26 12.77 ?  41  VAL   A C    1 
ATOM   965  O  O    A VAL   A 1 41  ? 33.370 2.024   -4.119  0.74 13.50 ?  41  VAL   A O    1 
ATOM   966  O  O    B VAL   A 1 41  ? 33.102 2.029   -4.152  0.26 12.78 ?  41  VAL   A O    1 
ATOM   967  C  CB   A VAL   A 1 41  ? 31.839 0.558   -6.341  0.74 12.14 ?  41  VAL   A CB   1 
ATOM   968  C  CB   B VAL   A 1 41  ? 31.509 0.794   -6.657  0.26 13.06 ?  41  VAL   A CB   1 
ATOM   969  C  CG1  A VAL   A 1 41  ? 31.130 -0.738  -6.723  0.74 13.81 ?  41  VAL   A CG1  1 
ATOM   970  C  CG1  B VAL   A 1 41  ? 30.947 -0.571  -7.023  0.26 13.73 ?  41  VAL   A CG1  1 
ATOM   971  C  CG2  A VAL   A 1 41  ? 31.696 1.635   -7.425  0.74 12.84 ?  41  VAL   A CG2  1 
ATOM   972  C  CG2  B VAL   A 1 41  ? 31.021 1.869   -7.622  0.26 13.30 ?  41  VAL   A CG2  1 
ATOM   973  H  H    A VAL   A 1 41  ? 29.548 1.342   -5.710  0.74 13.59 ?  41  VAL   A H    1 
ATOM   974  H  H    B VAL   A 1 41  ? 29.286 1.508   -5.831  0.26 15.07 ?  41  VAL   A H    1 
ATOM   975  H  HA   A VAL   A 1 41  ? 31.521 0.350   -4.332  0.74 13.84 ?  41  VAL   A HA   1 
ATOM   976  H  HA   B VAL   A 1 41  ? 31.320 0.374   -4.663  0.26 15.06 ?  41  VAL   A HA   1 
ATOM   977  H  HB   A VAL   A 1 41  ? 32.786 0.349   -6.272  0.74 14.58 ?  41  VAL   A HB   1 
ATOM   978  H  HB   B VAL   A 1 41  ? 32.474 0.746   -6.727  0.26 15.68 ?  41  VAL   A HB   1 
ATOM   979  H  HG11 A VAL   A 1 41  ? 31.474 -1.047  -7.575  0.74 16.59 ?  41  VAL   A HG11 1 
ATOM   980  H  HG11 B VAL   A 1 41  ? 31.187 -0.774  -7.938  0.26 16.49 ?  41  VAL   A HG11 1 
ATOM   981  H  HG12 A VAL   A 1 41  ? 31.293 -1.401  -6.036  0.74 16.59 ?  41  VAL   A HG12 1 
ATOM   982  H  HG12 B VAL   A 1 41  ? 31.323 -1.236  -6.425  0.26 16.49 ?  41  VAL   A HG12 1 
ATOM   983  H  HG13 A VAL   A 1 41  ? 30.178 -0.562  -6.795  0.74 16.59 ?  41  VAL   A HG13 1 
ATOM   984  H  HG13 B VAL   A 1 41  ? 29.982 -0.550  -6.928  0.26 16.49 ?  41  VAL   A HG13 1 
ATOM   985  H  HG21 A VAL   A 1 41  ? 31.915 1.248   -8.289  0.74 15.41 ?  41  VAL   A HG21 1 
ATOM   986  H  HG21 B VAL   A 1 41  ? 31.432 1.721   -8.487  0.26 15.97 ?  41  VAL   A HG21 1 
ATOM   987  H  HG22 A VAL   A 1 41  ? 30.784 1.960   -7.431  0.74 15.41 ?  41  VAL   A HG22 1 
ATOM   988  H  HG22 B VAL   A 1 41  ? 30.056 1.814   -7.703  0.26 15.97 ?  41  VAL   A HG22 1 
ATOM   989  H  HG23 A VAL   A 1 41  ? 32.307 2.365   -7.230  0.74 15.41 ?  41  VAL   A HG23 1 
ATOM   990  H  HG23 B VAL   A 1 41  ? 31.277 2.738   -7.279  0.26 15.97 ?  41  VAL   A HG23 1 
ATOM   991  N  N    A TYR   A 1 42  ? 31.689 3.462   -4.563  0.74 12.27 ?  42  TYR   A N    1 
ATOM   992  N  N    B TYR   A 1 42  ? 31.528 3.525   -4.730  0.26 12.73 ?  42  TYR   A N    1 
ATOM   993  C  CA   A TYR   A 1 42  ? 32.421 4.656   -4.156  0.74 12.05 ?  42  TYR   A CA   1 
ATOM   994  C  CA   B TYR   A 1 42  ? 32.311 4.679   -4.299  0.26 13.02 ?  42  TYR   A CA   1 
ATOM   995  C  C    A TYR   A 1 42  ? 32.171 5.016   -2.699  0.74 11.86 ?  42  TYR   A C    1 
ATOM   996  C  C    B TYR   A 1 42  ? 32.023 5.085   -2.858  0.26 12.64 ?  42  TYR   A C    1 
ATOM   997  O  O    A TYR   A 1 42  ? 32.775 5.969   -2.194  0.74 12.72 ?  42  TYR   A O    1 
ATOM   998  O  O    B TYR   A 1 42  ? 32.531 6.117   -2.405  0.26 12.66 ?  42  TYR   A O    1 
ATOM   999  C  CB   A TYR   A 1 42  ? 32.047 5.836   -5.072  0.74 13.19 ?  42  TYR   A CB   1 
ATOM   1000 C  CB   B TYR   A 1 42  ? 32.063 5.873   -5.227  0.26 14.02 ?  42  TYR   A CB   1 
ATOM   1001 C  CG   A TYR   A 1 42  ? 32.247 5.515   -6.542  0.74 14.68 ?  42  TYR   A CG   1 
ATOM   1002 C  CG   B TYR   A 1 42  ? 32.200 5.553   -6.698  0.26 14.88 ?  42  TYR   A CG   1 
ATOM   1003 C  CD1  A TYR   A 1 42  ? 33.516 5.318   -7.062  0.74 15.39 ?  42  TYR   A CD1  1 
ATOM   1004 C  CD1  B TYR   A 1 42  ? 33.445 5.331   -7.273  0.26 14.90 ?  42  TYR   A CD1  1 
ATOM   1005 C  CD2  A TYR   A 1 42  ? 31.165 5.382   -7.404  0.74 16.57 ?  42  TYR   A CD2  1 
ATOM   1006 C  CD2  B TYR   A 1 42  ? 31.082 5.479   -7.515  0.26 15.65 ?  42  TYR   A CD2  1 
ATOM   1007 C  CE1  A TYR   A 1 42  ? 33.708 5.015   -8.395  0.74 16.36 ?  42  TYR   A CE1  1 
ATOM   1008 C  CE1  B TYR   A 1 42  ? 33.567 5.040   -8.621  0.26 15.48 ?  42  TYR   A CE1  1 
ATOM   1009 C  CE2  A TYR   A 1 42  ? 31.347 5.078   -8.745  0.74 17.18 ?  42  TYR   A CE2  1 
ATOM   1010 C  CE2  B TYR   A 1 42  ? 31.195 5.189   -8.860  0.26 16.02 ?  42  TYR   A CE2  1 
ATOM   1011 C  CZ   A TYR   A 1 42  ? 32.626 4.893   -9.233  0.74 17.36 ?  42  TYR   A CZ   1 
ATOM   1012 C  CZ   B TYR   A 1 42  ? 32.438 4.970   -9.408  0.26 16.13 ?  42  TYR   A CZ   1 
ATOM   1013 O  OH   A TYR   A 1 42  ? 32.826 4.587   -10.561 0.74 18.58 ?  42  TYR   A OH   1 
ATOM   1014 O  OH   B TYR   A 1 42  ? 32.545 4.682   -10.749 0.26 16.82 ?  42  TYR   A OH   1 
ATOM   1015 H  H    A TYR   A 1 42  ? 30.895 3.628   -4.848  0.74 14.74 ?  42  TYR   A H    1 
ATOM   1016 H  H    B TYR   A 1 42  ? 30.745 3.729   -5.025  0.26 15.29 ?  42  TYR   A H    1 
ATOM   1017 H  HA   A TYR   A 1 42  ? 33.371 4.492   -4.266  0.74 14.47 ?  42  TYR   A HA   1 
ATOM   1018 H  HA   B TYR   A 1 42  ? 33.250 4.454   -4.360  0.26 15.63 ?  42  TYR   A HA   1 
ATOM   1019 H  HB2  A TYR   A 1 42  ? 31.111 6.061   -4.937  0.74 15.84 ?  42  TYR   A HB2  1 
ATOM   1020 H  HB2  B TYR   A 1 42  ? 31.164 6.203   -5.080  0.26 16.83 ?  42  TYR   A HB2  1 
ATOM   1021 H  HB3  A TYR   A 1 42  ? 32.604 6.601   -4.853  0.74 15.84 ?  42  TYR   A HB3  1 
ATOM   1022 H  HB3  B TYR   A 1 42  ? 32.707 6.570   -5.016  0.26 16.83 ?  42  TYR   A HB3  1 
ATOM   1023 H  HD1  A TYR   A 1 42  ? 34.252 5.397   -6.501  0.74 18.48 ?  42  TYR   A HD1  1 
ATOM   1024 H  HD1  B TYR   A 1 42  ? 34.208 5.375   -6.742  0.26 17.89 ?  42  TYR   A HD1  1 
ATOM   1025 H  HD2  A TYR   A 1 42  ? 30.303 5.513   -7.077  0.74 19.89 ?  42  TYR   A HD2  1 
ATOM   1026 H  HD2  B TYR   A 1 42  ? 30.241 5.627   -7.148  0.26 18.79 ?  42  TYR   A HD2  1 
ATOM   1027 H  HE1  A TYR   A 1 42  ? 34.566 4.886   -8.725  0.74 19.65 ?  42  TYR   A HE1  1 
ATOM   1028 H  HE1  B TYR   A 1 42  ? 34.407 4.890   -8.992  0.26 18.58 ?  42  TYR   A HE1  1 
ATOM   1029 H  HE2  A TYR   A 1 42  ? 30.612 5.001   -9.313  0.74 20.63 ?  42  TYR   A HE2  1 
ATOM   1030 H  HE2  B TYR   A 1 42  ? 30.436 5.143   -9.394  0.26 19.23 ?  42  TYR   A HE2  1 
ATOM   1031 H  HH   A TYR   A 1 42  ? 33.646 4.495   -10.715 0.74 22.30 ?  42  TYR   A HH   1 
ATOM   1032 H  HH   B TYR   A 1 42  ? 31.783 4.671   -11.101 0.26 20.19 ?  42  TYR   A HH   1 
ATOM   1033 N  N    A LEU   A 1 43  ? 31.324 4.249   -2.009  0.74 11.62 ?  43  LEU   A N    1 
ATOM   1034 N  N    B LEU   A 1 43  ? 31.228 4.296   -2.134  0.26 12.60 ?  43  LEU   A N    1 
ATOM   1035 C  CA   A LEU   A 1 43  ? 30.869 4.595   -0.663  0.74 11.30 ?  43  LEU   A CA   1 
ATOM   1036 C  CA   B LEU   A 1 43  ? 30.813 4.625   -0.769  0.26 12.43 ?  43  LEU   A CA   1 
ATOM   1037 C  C    A LEU   A 1 43  ? 30.391 6.045   -0.567  0.74 11.24 ?  43  LEU   A C    1 
ATOM   1038 C  C    B LEU   A 1 43  ? 30.333 6.070   -0.657  0.26 13.13 ?  43  LEU   A C    1 
ATOM   1039 O  O    A LEU   A 1 43  ? 30.664 6.753   0.409   0.74 12.83 ?  43  LEU   A O    1 
ATOM   1040 O  O    B LEU   A 1 43  ? 30.628 6.775   0.312   0.26 13.67 ?  43  LEU   A O    1 
ATOM   1041 C  CB   A LEU   A 1 43  ? 31.922 4.278   0.396   0.74 12.66 ?  43  LEU   A CB   1 
ATOM   1042 C  CB   B LEU   A 1 43  ? 31.906 4.315   0.255   0.26 12.44 ?  43  LEU   A CB   1 
ATOM   1043 C  CG   A LEU   A 1 43  ? 32.424 2.826   0.482   0.74 12.98 ?  43  LEU   A CG   1 
ATOM   1044 C  CG   B LEU   A 1 43  ? 32.417 2.871   0.325   0.26 12.68 ?  43  LEU   A CG   1 
ATOM   1045 C  CD1  A LEU   A 1 43  ? 33.467 2.706   1.579   0.74 14.09 ?  43  LEU   A CD1  1 
ATOM   1046 C  CD1  B LEU   A 1 43  ? 33.461 2.739   1.425   0.26 13.38 ?  43  LEU   A CD1  1 
ATOM   1047 C  CD2  A LEU   A 1 43  ? 31.285 1.854   0.735   0.74 13.24 ?  43  LEU   A CD2  1 
ATOM   1048 C  CD2  B LEU   A 1 43  ? 31.278 1.885   0.546   0.26 12.49 ?  43  LEU   A CD2  1 
ATOM   1049 H  H    A LEU   A 1 43  ? 30.993 3.511   -2.307  0.74 13.95 ?  43  LEU   A H    1 
ATOM   1050 H  H    B LEU   A 1 43  ? 30.910 3.552   -2.417  0.26 15.13 ?  43  LEU   A H    1 
ATOM   1051 H  HA   A LEU   A 1 43  ? 30.100 4.035   -0.465  0.74 13.56 ?  43  LEU   A HA   1 
ATOM   1052 H  HA   B LEU   A 1 43  ? 30.055 4.066   -0.549  0.26 14.92 ?  43  LEU   A HA   1 
ATOM   1053 H  HB2  A LEU   A 1 43  ? 32.692 4.840   0.237   0.74 15.20 ?  43  LEU   A HB2  1 
ATOM   1054 H  HB2  B LEU   A 1 43  ? 32.669 4.879   0.064   0.26 14.94 ?  43  LEU   A HB2  1 
ATOM   1055 H  HB3  A LEU   A 1 43  ? 31.542 4.491   1.265   0.74 15.20 ?  43  LEU   A HB3  1 
ATOM   1056 H  HB3  B LEU   A 1 43  ? 31.560 4.533   1.136   0.26 14.94 ?  43  LEU   A HB3  1 
ATOM   1057 H  HG   A LEU   A 1 43  ? 32.848 2.586   -0.359  0.74 15.58 ?  43  LEU   A HG   1 
ATOM   1058 H  HG   B LEU   A 1 43  ? 32.845 2.649   -0.517  0.26 15.23 ?  43  LEU   A HG   1 
ATOM   1059 H  HD11 A LEU   A 1 43  ? 33.779 1.788   1.620   0.74 16.92 ?  43  LEU   A HD11 1 
ATOM   1060 H  HD11 B LEU   A 1 43  ? 33.775 1.822   1.454   0.26 16.07 ?  43  LEU   A HD11 1 
ATOM   1061 H  HD12 A LEU   A 1 43  ? 34.208 3.299   1.377   0.74 16.92 ?  43  LEU   A HD12 1 
ATOM   1062 H  HD12 B LEU   A 1 43  ? 34.201 3.336   1.232   0.26 16.07 ?  43  LEU   A HD12 1 
ATOM   1063 H  HD13 A LEU   A 1 43  ? 33.063 2.956   2.425   0.74 16.92 ?  43  LEU   A HD13 1 
ATOM   1064 H  HD13 B LEU   A 1 43  ? 33.056 2.977   2.274   0.26 16.07 ?  43  LEU   A HD13 1 
ATOM   1065 H  HD21 A LEU   A 1 43  ? 31.653 0.965   0.868   0.74 15.90 ?  43  LEU   A HD21 1 
ATOM   1066 H  HD21 B LEU   A 1 43  ? 31.651 0.999   0.686   0.26 15.00 ?  43  LEU   A HD21 1 
ATOM   1067 H  HD22 A LEU   A 1 43  ? 30.804 2.134   1.528   0.74 15.90 ?  43  LEU   A HD22 1 
ATOM   1068 H  HD22 B LEU   A 1 43  ? 30.772 2.158   1.327   0.26 15.00 ?  43  LEU   A HD22 1 
ATOM   1069 H  HD23 A LEU   A 1 43  ? 30.694 1.855   -0.032  0.74 15.90 ?  43  LEU   A HD23 1 
ATOM   1070 H  HD23 B LEU   A 1 43  ? 30.706 1.882   -0.237  0.26 15.00 ?  43  LEU   A HD23 1 
ATOM   1071 N  N    A LYS   A 1 44  ? 29.669 6.493   -1.596  0.74 11.49 ?  44  LYS   A N    1 
ATOM   1072 N  N    B LYS   A 1 44  ? 29.586 6.516   -1.664  0.26 13.70 ?  44  LYS   A N    1 
ATOM   1073 C  CA   A LYS   A 1 44  ? 29.010 7.797   -1.595  0.74 12.06 ?  44  LYS   A CA   1 
ATOM   1074 C  CA   B LYS   A 1 44  ? 28.940 7.825   -1.640  0.26 14.20 ?  44  LYS   A CA   1 
ATOM   1075 C  C    A LYS   A 1 44  ? 27.578 7.599   -1.109  0.74 11.86 ?  44  LYS   A C    1 
ATOM   1076 C  C    B LYS   A 1 44  ? 27.524 7.639   -1.127  0.26 12.84 ?  44  LYS   A C    1 
ATOM   1077 O  O    A LYS   A 1 44  ? 26.722 7.094   -1.839  0.74 13.39 ?  44  LYS   A O    1 
ATOM   1078 O  O    B LYS   A 1 44  ? 26.636 7.182   -1.850  0.26 13.22 ?  44  LYS   A O    1 
ATOM   1079 C  CB   A LYS   A 1 44  ? 29.060 8.413   -2.986  0.74 14.96 ?  44  LYS   A CB   1 
ATOM   1080 C  CB   B LYS   A 1 44  ? 28.989 8.477   -3.019  0.26 16.67 ?  44  LYS   A CB   1 
ATOM   1081 C  CG   A LYS   A 1 44  ? 30.443 8.880   -3.403  0.74 18.81 ?  44  LYS   A CG   1 
ATOM   1082 C  CG   B LYS   A 1 44  ? 30.396 8.876   -3.467  0.26 19.13 ?  44  LYS   A CG   1 
ATOM   1083 C  CD   A LYS   A 1 44  ? 31.059 9.835   -2.390  0.74 23.37 ?  44  LYS   A CD   1 
ATOM   1084 C  CD   B LYS   A 1 44  ? 31.236 9.414   -2.299  0.26 21.67 ?  44  LYS   A CD   1 
ATOM   1085 C  CE   A LYS   A 1 44  ? 32.412 10.328  -2.869  0.74 26.00 ?  44  LYS   A CE   1 
ATOM   1086 C  CE   B LYS   A 1 44  ? 31.677 10.836  -2.506  0.26 22.85 ?  44  LYS   A CE   1 
ATOM   1087 N  NZ   A LYS   A 1 44  ? 33.262 10.832  -1.757  0.74 27.04 ?  44  LYS   A NZ   1 
ATOM   1088 N  NZ   B LYS   A 1 44  ? 32.765 10.945  -3.502  0.26 23.51 ?  44  LYS   A NZ   1 
ATOM   1089 H  H    A LYS   A 1 44  ? 29.525 6.035   -2.313  0.74 13.80 ?  44  LYS   A H    1 
ATOM   1090 H  H    B LYS   A 1 44  ? 29.434 6.075   -2.384  0.26 16.45 ?  44  LYS   A H    1 
ATOM   1091 H  HA   A LYS   A 1 44  ? 29.452 8.379   -0.961  0.74 14.49 ?  44  LYS   A HA   1 
ATOM   1092 H  HA   B LYS   A 1 44  ? 29.360 8.382   -0.969  0.26 17.05 ?  44  LYS   A HA   1 
ATOM   1093 H  HB2  A LYS   A 1 44  ? 28.759 7.756   -3.631  0.74 17.96 ?  44  LYS   A HB2  1 
ATOM   1094 H  HB2  B LYS   A 1 44  ? 28.639 7.849   -3.676  0.26 20.01 ?  44  LYS   A HB2  1 
ATOM   1095 H  HB3  A LYS   A 1 44  ? 28.467 9.184   -3.005  0.74 17.96 ?  44  LYS   A HB3  1 
ATOM   1096 H  HB3  B LYS   A 1 44  ? 28.446 9.281   -3.016  0.26 20.01 ?  44  LYS   A HB3  1 
ATOM   1097 H  HG2  A LYS   A 1 44  ? 31.026 8.112   -3.489  0.74 22.58 ?  44  LYS   A HG2  1 
ATOM   1098 H  HG2  B LYS   A 1 44  ? 30.846 8.098   -3.843  0.26 22.97 ?  44  LYS   A HG2  1 
ATOM   1099 H  HG3  A LYS   A 1 44  ? 30.379 9.348   -4.252  0.74 22.58 ?  44  LYS   A HG3  1 
ATOM   1100 H  HG3  B LYS   A 1 44  ? 30.335 9.577   -4.141  0.26 22.97 ?  44  LYS   A HG3  1 
ATOM   1101 H  HD2  A LYS   A 1 44  ? 30.473 10.594  -2.263  0.74 28.06 ?  44  LYS   A HD2  1 
ATOM   1102 H  HD2  B LYS   A 1 44  ? 30.744 9.436   -1.468  0.26 26.01 ?  44  LYS   A HD2  1 
ATOM   1103 H  HD3  A LYS   A 1 44  ? 31.199 9.367   -1.549  0.74 28.06 ?  44  LYS   A HD3  1 
ATOM   1104 H  HD3  B LYS   A 1 44  ? 32.006 8.841   -2.200  0.26 26.01 ?  44  LYS   A HD3  1 
ATOM   1105 H  HE2  A LYS   A 1 44  ? 32.886 9.596   -3.297  0.74 31.21 ?  44  LYS   A HE2  1 
ATOM   1106 H  HE2  B LYS   A 1 44  ? 30.917 11.359  -2.811  0.26 27.43 ?  44  LYS   A HE2  1 
ATOM   1107 H  HE3  A LYS   A 1 44  ? 32.281 11.052  -3.498  0.74 31.21 ?  44  LYS   A HE3  1 
ATOM   1108 H  HE3  B LYS   A 1 44  ? 31.993 11.180  -1.655  0.26 27.43 ?  44  LYS   A HE3  1 
ATOM   1109 H  HZ1  A LYS   A 1 44  ? 34.043 11.114  -2.074  0.74 32.45 ?  44  LYS   A HZ1  1 
ATOM   1110 H  HZ1  B LYS   A 1 44  ? 33.003 11.796  -3.592  0.26 28.22 ?  44  LYS   A HZ1  1 
ATOM   1111 H  HZ2  A LYS   A 1 44  ? 32.854 11.511  -1.348  0.74 32.45 ?  44  LYS   A HZ2  1 
ATOM   1112 H  HZ2  B LYS   A 1 44  ? 33.469 10.472  -3.233  0.26 28.22 ?  44  LYS   A HZ2  1 
ATOM   1113 H  HZ3  A LYS   A 1 44  ? 33.405 10.184  -1.164  0.74 32.45 ?  44  LYS   A HZ3  1 
ATOM   1114 H  HZ3  B LYS   A 1 44  ? 32.489 10.634  -4.288  0.26 28.22 ?  44  LYS   A HZ3  1 
ATOM   1115 N  N    . HIS   A 1 45  ? 27.322 7.995   0.139   1.00 11.74 ?  45  HIS   A N    1 
ATOM   1116 C  CA   . HIS   A 1 45  ? 26.084 7.662   0.840   1.00 12.36 ?  45  HIS   A CA   1 
ATOM   1117 C  C    . HIS   A 1 45  ? 25.077 8.802   0.685   1.00 12.72 ?  45  HIS   A C    1 
ATOM   1118 O  O    . HIS   A 1 45  ? 24.769 9.537   1.624   1.00 14.42 ?  45  HIS   A O    1 
ATOM   1119 C  CB   . HIS   A 1 45  ? 26.393 7.397   2.305   1.00 12.44 ?  45  HIS   A CB   1 
ATOM   1120 C  CG   . HIS   A 1 45  ? 27.509 6.425   2.521   1.00 11.77 ?  45  HIS   A CG   1 
ATOM   1121 N  ND1  . HIS   A 1 45  ? 27.499 5.139   2.020   1.00 11.91 ?  45  HIS   A ND1  1 
ATOM   1122 C  CD2  . HIS   A 1 45  ? 28.678 6.566   3.192   1.00 12.05 ?  45  HIS   A CD2  1 
ATOM   1123 C  CE1  . HIS   A 1 45  ? 28.619 4.538   2.377   1.00 11.22 ?  45  HIS   A CE1  1 
ATOM   1124 N  NE2  . HIS   A 1 45  ? 29.351 5.373   3.094   1.00 11.80 ?  45  HIS   A NE2  1 
ATOM   1125 H  H    A HIS   A 1 45  ? 27.866 8.470   0.612   0.74 14.09 ?  45  HIS   A H    1 
ATOM   1126 H  H    B HIS   A 1 45  ? 27.890 8.428   0.624   0.26 14.09 ?  45  HIS   A H    1 
ATOM   1127 H  HA   . HIS   A 1 45  ? 25.700 6.860   0.455   1.00 14.84 ?  45  HIS   A HA   1 
ATOM   1128 H  HB2  . HIS   A 1 45  ? 26.639 8.234   2.729   1.00 14.94 ?  45  HIS   A HB2  1 
ATOM   1129 H  HB3  . HIS   A 1 45  ? 25.597 7.039   2.735   1.00 14.94 ?  45  HIS   A HB3  1 
ATOM   1130 H  HD2  . HIS   A 1 45  ? 28.971 7.332   3.639   1.00 14.47 ?  45  HIS   A HD2  1 
ATOM   1131 H  HE1  . HIS   A 1 45  ? 28.851 3.664   2.175   1.00 13.47 ?  45  HIS   A HE1  1 
ATOM   1132 H  HE2  . HIS   A 1 45  ? 30.125 5.206   3.435   1.00 14.17 ?  45  HIS   A HE2  1 
ATOM   1133 N  N    A GLY   A 1 46  ? 24.472 8.869   -0.500  0.74 13.82 ?  46  GLY   A N    1 
ATOM   1134 N  N    B GLY   A 1 46  ? 24.608 8.994   -0.546  0.26 13.22 ?  46  GLY   A N    1 
ATOM   1135 C  CA   A GLY   A 1 46  ? 23.629 10.000  -0.839  0.74 14.08 ?  46  GLY   A CA   1 
ATOM   1136 C  CA   B GLY   A 1 46  ? 23.877 10.212  -0.866  0.26 13.14 ?  46  GLY   A CA   1 
ATOM   1137 C  C    A GLY   A 1 46  ? 22.148 9.838   -0.559  0.74 14.34 ?  46  GLY   A C    1 
ATOM   1138 C  C    B GLY   A 1 46  ? 22.387 10.159  -0.590  0.26 12.83 ?  46  GLY   A C    1 
ATOM   1139 O  O    A GLY   A 1 46  ? 21.469 10.810  -0.206  0.74 14.79 ?  46  GLY   A O    1 
ATOM   1140 O  O    B GLY   A 1 46  ? 21.755 11.181  -0.305  0.26 13.45 ?  46  GLY   A O    1 
ATOM   1141 H  H    A GLY   A 1 46  ? 24.534 8.274   -1.118  0.74 16.59 ?  46  GLY   A H    1 
ATOM   1142 H  H    B GLY   A 1 46  ? 24.698 8.446   -1.201  0.26 15.87 ?  46  GLY   A H    1 
ATOM   1143 H  HA2  A GLY   A 1 46  ? 23.933 10.778  -0.346  0.74 16.91 ?  46  GLY   A HA2  1 
ATOM   1144 H  HA2  B GLY   A 1 46  ? 24.254 10.949  -0.356  0.26 15.78 ?  46  GLY   A HA2  1 
ATOM   1145 H  HA3  A GLY   A 1 46  ? 23.724 10.191  -1.784  0.74 16.91 ?  46  GLY   A HA3  1 
ATOM   1146 H  HA3  B GLY   A 1 46  ? 23.992 10.411  -1.807  0.26 15.78 ?  46  GLY   A HA3  1 
ATOM   1147 N  N    A GLY   A 1 47  ? 21.623 8.627   -0.724  0.74 14.22 ?  47  GLY   A N    1 
ATOM   1148 N  N    B GLY   A 1 47  ? 21.819 8.966   -0.693  0.26 12.60 ?  47  GLY   A N    1 
ATOM   1149 C  CA   A GLY   A 1 47  ? 20.190 8.420   -0.655  0.74 14.54 ?  47  GLY   A CA   1 
ATOM   1150 C  CA   B GLY   A 1 47  ? 20.406 8.755   -0.489  0.26 13.01 ?  47  GLY   A CA   1 
ATOM   1151 C  C    A GLY   A 1 47  ? 19.857 6.992   -0.284  0.74 13.41 ?  47  GLY   A C    1 
ATOM   1152 C  C    B GLY   A 1 47  ? 20.126 7.283   -0.271  0.26 13.07 ?  47  GLY   A C    1 
ATOM   1153 O  O    A GLY   A 1 47  ? 20.737 6.157   -0.066  0.74 13.45 ?  47  GLY   A O    1 
ATOM   1154 O  O    B GLY   A 1 47  ? 21.042 6.474   -0.109  0.26 13.28 ?  47  GLY   A O    1 
ATOM   1155 H  H    A GLY   A 1 47  ? 22.076 7.906   -0.863  0.74 17.07 ?  47  GLY   A H    1 
ATOM   1156 H  H    B GLY   A 1 47  ? 22.248 8.257   -0.885  0.26 15.13 ?  47  GLY   A H    1 
ATOM   1157 H  HA2  A GLY   A 1 47  ? 19.799 9.019   0.004   0.74 17.45 ?  47  GLY   A HA2  1 
ATOM   1158 H  HA2  B GLY   A 1 47  ? 20.096 9.253   0.285   0.26 15.62 ?  47  GLY   A HA2  1 
ATOM   1159 H  HA3  A GLY   A 1 47  ? 19.791 8.614   -1.520  0.74 17.45 ?  47  GLY   A HA3  1 
ATOM   1160 H  HA3  B GLY   A 1 47  ? 19.914 9.059   -1.269  0.26 15.62 ?  47  GLY   A HA3  1 
ATOM   1161 N  N    A GLY   A 1 48  ? 18.557 6.719   -0.220  0.74 13.98 ?  48  GLY   A N    1 
ATOM   1162 N  N    B GLY   A 1 48  ? 18.841 6.943   -0.270  0.26 13.03 ?  48  GLY   A N    1 
ATOM   1163 C  CA   A GLY   A 1 48  ? 18.106 5.419   0.221   0.74 13.56 ?  48  GLY   A CA   1 
ATOM   1164 C  CA   B GLY   A 1 48  ? 18.442 5.567   -0.035  0.26 13.35 ?  48  GLY   A CA   1 
ATOM   1165 C  C    A GLY   A 1 48  ? 18.619 5.108   1.614   0.74 12.41 ?  48  GLY   A C    1 
ATOM   1166 C  C    B GLY   A 1 48  ? 18.810 5.110   1.368   0.26 13.08 ?  48  GLY   A C    1 
ATOM   1167 O  O    A GLY   A 1 48  ? 18.842 5.997   2.444   0.74 13.94 ?  48  GLY   A O    1 
ATOM   1168 O  O    B GLY   A 1 48  ? 18.768 5.875   2.337   0.26 13.73 ?  48  GLY   A O    1 
ATOM   1169 H  H    A GLY   A 1 48  ? 17.920 7.272   -0.403  0.74 16.78 ?  48  GLY   A H    1 
ATOM   1170 H  H    B GLY   A 1 48  ? 18.191 7.490   -0.395  0.26 15.64 ?  48  GLY   A H    1 
ATOM   1171 H  HA2  A GLY   A 1 48  ? 17.136 5.385   0.231   0.74 16.28 ?  48  GLY   A HA2  1 
ATOM   1172 H  HA2  B GLY   A 1 48  ? 17.482 5.481   -0.159  0.26 16.03 ?  48  GLY   A HA2  1 
ATOM   1173 H  HA3  A GLY   A 1 48  ? 18.435 4.737   -0.385  0.74 16.28 ?  48  GLY   A HA3  1 
ATOM   1174 H  HA3  B GLY   A 1 48  ? 18.886 4.984   -0.672  0.26 16.03 ?  48  GLY   A HA3  1 
ATOM   1175 N  N    A VAL   A 1 49  ? 18.829 3.815   1.872   0.74 10.87 ?  49  VAL   A N    1 
ATOM   1176 N  N    B VAL   A 1 49  ? 19.178 3.830   1.477   0.26 12.51 ?  49  VAL   A N    1 
ATOM   1177 C  CA   A VAL   A 1 49  ? 19.349 3.376   3.166   0.74 11.33 ?  49  VAL   A CA   1 
ATOM   1178 C  CA   B VAL   A 1 49  ? 19.626 3.286   2.759   0.26 12.04 ?  49  VAL   A CA   1 
ATOM   1179 C  C    A VAL   A 1 49  ? 20.672 4.062   3.485   0.74 10.88 ?  49  VAL   A C    1 
ATOM   1180 C  C    B VAL   A 1 49  ? 20.882 4.009   3.234   0.26 11.61 ?  49  VAL   A C    1 
ATOM   1181 O  O    A VAL   A 1 49  ? 20.900 4.505   4.616   0.74 11.07 ?  49  VAL   A O    1 
ATOM   1182 O  O    B VAL   A 1 49  ? 21.005 4.375   4.407   0.26 11.59 ?  49  VAL   A O    1 
ATOM   1183 C  CB   A VAL   A 1 49  ? 19.491 1.842   3.178   0.74 12.39 ?  49  VAL   A CB   1 
ATOM   1184 C  CB   B VAL   A 1 49  ? 19.862 1.767   2.648   0.26 11.67 ?  49  VAL   A CB   1 
ATOM   1185 C  CG1  A VAL   A 1 49  ? 20.257 1.374   4.409   0.74 13.66 ?  49  VAL   A CG1  1 
ATOM   1186 C  CG1  B VAL   A 1 49  ? 20.660 1.255   3.847   0.26 10.98 ?  49  VAL   A CG1  1 
ATOM   1187 C  CG2  A VAL   A 1 49  ? 18.116 1.177   3.111   0.74 15.23 ?  49  VAL   A CG2  1 
ATOM   1188 C  CG2  B VAL   A 1 49  ? 18.546 1.010   2.525   0.26 12.23 ?  49  VAL   A CG2  1 
ATOM   1189 H  H    A VAL   A 1 49  ? 18.669 3.170   1.321   0.74 13.05 ?  49  VAL   A H    1 
ATOM   1190 H  H    B VAL   A 1 49  ? 19.170 3.260   0.832   0.26 15.02 ?  49  VAL   A H    1 
ATOM   1191 H  HA   A VAL   A 1 49  ? 18.716 3.617   3.861   0.74 13.60 ?  49  VAL   A HA   1 
ATOM   1192 H  HA   B VAL   A 1 49  ? 18.928 3.427   3.420   0.26 14.46 ?  49  VAL   A HA   1 
ATOM   1193 H  HB   A VAL   A 1 49  ? 19.995 1.565   2.396   0.74 14.88 ?  49  VAL   A HB   1 
ATOM   1194 H  HB   B VAL   A 1 49  ? 20.381 1.595   1.851   0.26 14.02 ?  49  VAL   A HB   1 
ATOM   1195 H  HG11 A VAL   A 1 49  ? 20.099 0.428   4.536   0.74 16.40 ?  49  VAL   A HG11 1 
ATOM   1196 H  HG11 B VAL   A 1 49  ? 20.560 0.292   3.900   0.26 13.18 ?  49  VAL   A HG11 1 
ATOM   1197 H  HG12 A VAL   A 1 49  ? 21.202 1.540   4.278   0.74 16.40 ?  49  VAL   A HG12 1 
ATOM   1198 H  HG12 B VAL   A 1 49  ? 21.595 1.483   3.729   0.26 13.18 ?  49  VAL   A HG12 1 
ATOM   1199 H  HG13 A VAL   A 1 49  ? 19.936 1.869   5.182   0.74 16.40 ?  49  VAL   A HG13 1 
ATOM   1200 H  HG13 B VAL   A 1 49  ? 20.313 1.667   4.653   0.26 13.18 ?  49  VAL   A HG13 1 
ATOM   1201 H  HG21 A VAL   A 1 49  ? 18.231 0.215   3.128   0.74 18.28 ?  49  VAL   A HG21 1 
ATOM   1202 H  HG21 B VAL   A 1 49  ? 18.736 0.076   2.340   0.26 14.69 ?  49  VAL   A HG21 1 
ATOM   1203 H  HG22 A VAL   A 1 49  ? 17.592 1.464   3.875   0.74 18.28 ?  49  VAL   A HG22 1 
ATOM   1204 H  HG22 B VAL   A 1 49  ? 18.060 1.089   3.360   0.26 14.69 ?  49  VAL   A HG22 1 
ATOM   1205 H  HG23 A VAL   A 1 49  ? 17.679 1.445   2.288   0.74 18.28 ?  49  VAL   A HG23 1 
ATOM   1206 H  HG23 B VAL   A 1 49  ? 18.030 1.392   1.799   0.26 14.69 ?  49  VAL   A HG23 1 
ATOM   1207 N  N    A ALA   A 1 50  ? 21.571 4.140   2.503   0.74 10.85 ?  50  ALA   A N    1 
ATOM   1208 N  N    B ALA   A 1 50  ? 21.844 4.204   2.330   0.26 11.32 ?  50  ALA   A N    1 
ATOM   1209 C  CA   A ALA   A 1 50  ? 22.904 4.687   2.762   0.74 11.14 ?  50  ALA   A CA   1 
ATOM   1210 C  CA   B ALA   A 1 50  ? 23.108 4.821   2.723   0.26 10.75 ?  50  ALA   A CA   1 
ATOM   1211 C  C    A ALA   A 1 50  ? 22.834 6.144   3.191   0.74 11.15 ?  50  ALA   A C    1 
ATOM   1212 C  C    B ALA   A 1 50  ? 22.921 6.276   3.135   0.26 10.44 ?  50  ALA   A C    1 
ATOM   1213 O  O    A ALA   A 1 50  ? 23.476 6.544   4.170   0.74 11.84 ?  50  ALA   A O    1 
ATOM   1214 O  O    B ALA   A 1 50  ? 23.513 6.726   4.124   0.26 10.83 ?  50  ALA   A O    1 
ATOM   1215 C  CB   A ALA   A 1 50  ? 23.771 4.541   1.515   0.74 10.74 ?  50  ALA   A CB   1 
ATOM   1216 C  CB   B ALA   A 1 50  ? 24.119 4.715   1.583   0.26 10.78 ?  50  ALA   A CB   1 
ATOM   1217 H  H    A ALA   A 1 50  ? 21.445 3.883   1.692   0.74 13.03 ?  50  ALA   A H    1 
ATOM   1218 H  H    B ALA   A 1 50  ? 21.792 3.980   1.502   0.26 13.59 ?  50  ALA   A H    1 
ATOM   1219 H  HA   A ALA   A 1 50  ? 23.323 4.189   3.482   0.74 13.38 ?  50  ALA   A HA   1 
ATOM   1220 H  HA   B ALA   A 1 50  ? 23.465 4.344   3.484   0.26 12.91 ?  50  ALA   A HA   1 
ATOM   1221 H  HB1  A ALA   A 1 50  ? 24.652 4.907   1.697   0.74 12.90 ?  50  ALA   A HB1  1 
ATOM   1222 H  HB1  B ALA   A 1 50  ? 24.963 5.089   1.875   0.26 12.95 ?  50  ALA   A HB1  1 
ATOM   1223 H  HB2  A ALA   A 1 50  ? 23.845 3.600   1.291   0.74 12.90 ?  50  ALA   A HB2  1 
ATOM   1224 H  HB2  B ALA   A 1 50  ? 24.235 3.779   1.353   0.26 12.95 ?  50  ALA   A HB2  1 
ATOM   1225 H  HB3  A ALA   A 1 50  ? 23.356 5.025   0.786   0.74 12.90 ?  50  ALA   A HB3  1 
ATOM   1226 H  HB3  B ALA   A 1 50  ? 23.785 5.204   0.815   0.26 12.95 ?  50  ALA   A HB3  1 
ATOM   1227 N  N    A GLY   A 1 51  ? 22.049 6.952   2.476   0.74 11.58 ?  51  GLY   A N    1 
ATOM   1228 N  N    B GLY   A 1 51  ? 22.105 7.026   2.394   0.26 10.93 ?  51  GLY   A N    1 
ATOM   1229 C  CA   A GLY   A 1 51  ? 21.898 8.343   2.876   0.74 12.08 ?  51  GLY   A CA   1 
ATOM   1230 C  CA   B GLY   A 1 51  ? 21.900 8.424   2.736   0.26 11.47 ?  51  GLY   A CA   1 
ATOM   1231 C  C    A GLY   A 1 51  ? 21.309 8.470   4.267   0.74 11.42 ?  51  GLY   A C    1 
ATOM   1232 C  C    B GLY   A 1 51  ? 21.252 8.595   4.096   0.26 11.82 ?  51  GLY   A C    1 
ATOM   1233 O  O    A GLY   A 1 51  ? 21.722 9.331   5.049   0.74 12.30 ?  51  GLY   A O    1 
ATOM   1234 O  O    B GLY   A 1 51  ? 21.629 9.482   4.865   0.26 12.25 ?  51  GLY   A O    1 
ATOM   1235 H  H    A GLY   A 1 51  ? 21.615 6.717   1.771   0.74 13.91 ?  51  GLY   A H    1 
ATOM   1236 H  H    B GLY   A 1 51  ? 21.667 6.753   1.706   0.26 13.13 ?  51  GLY   A H    1 
ATOM   1237 H  HA2  A GLY   A 1 51  ? 22.764 8.779   2.861   0.74 14.50 ?  51  GLY   A HA2  1 
ATOM   1238 H  HA2  B GLY   A 1 51  ? 22.755 8.881   2.750   0.26 13.77 ?  51  GLY   A HA2  1 
ATOM   1239 H  HA3  A GLY   A 1 51  ? 21.316 8.793   2.241   0.74 14.50 ?  51  GLY   A HA3  1 
ATOM   1240 H  HA3  B GLY   A 1 51  ? 21.339 8.845   2.067   0.26 13.77 ?  51  GLY   A HA3  1 
ATOM   1241 N  N    A ALA   A 1 52  ? 20.351 7.595   4.602   0.74 11.18 ?  52  ALA   A N    1 
ATOM   1242 N  N    B ALA   A 1 52  ? 20.272 7.742   4.413   0.26 11.88 ?  52  ALA   A N    1 
ATOM   1243 C  CA   A ALA   A 1 52  ? 19.718 7.638   5.915   0.74 11.66 ?  52  ALA   A CA   1 
ATOM   1244 C  CA   B ALA   A 1 52  ? 19.610 7.829   5.710   0.26 12.24 ?  52  ALA   A CA   1 
ATOM   1245 C  C    A ALA   A 1 52  ? 20.689 7.231   7.024   0.74 10.91 ?  52  ALA   A C    1 
ATOM   1246 C  C    B ALA   A 1 52  ? 20.530 7.373   6.837   0.26 12.64 ?  52  ALA   A C    1 
ATOM   1247 O  O    A ALA   A 1 52  ? 20.787 7.906   8.056   0.74 12.33 ?  52  ALA   A O    1 
ATOM   1248 O  O    B ALA   A 1 52  ? 20.569 7.999   7.903   0.26 13.28 ?  52  ALA   A O    1 
ATOM   1249 C  CB   A ALA   A 1 52  ? 18.480 6.736   5.904   0.74 13.50 ?  52  ALA   A CB   1 
ATOM   1250 C  CB   B ALA   A 1 52  ? 18.320 7.009   5.693   0.26 12.67 ?  52  ALA   A CB   1 
ATOM   1251 H  H    A ALA   A 1 52  ? 20.073 6.956   4.092   0.74 13.43 ?  52  ALA   A H    1 
ATOM   1252 H  H    B ALA   A 1 52  ? 19.987 7.110   3.905   0.26 14.26 ?  52  ALA   A H    1 
ATOM   1253 H  HA   A ALA   A 1 52  ? 19.427 8.544   6.088   0.74 14.00 ?  52  ALA   A HA   1 
ATOM   1254 H  HA   B ALA   A 1 52  ? 19.373 8.752   5.877   0.26 14.69 ?  52  ALA   A HA   1 
ATOM   1255 H  HB1  A ALA   A 1 52  ? 18.056 6.774   6.777   0.74 16.21 ?  52  ALA   A HB1  1 
ATOM   1256 H  HB1  B ALA   A 1 52  ? 17.893 7.077   6.562   0.26 15.21 ?  52  ALA   A HB1  1 
ATOM   1257 H  HB2  A ALA   A 1 52  ? 17.861 7.057   5.226   0.74 16.21 ?  52  ALA   A HB2  1 
ATOM   1258 H  HB2  B ALA   A 1 52  ? 17.732 7.361   5.008   0.26 15.21 ?  52  ALA   A HB2  1 
ATOM   1259 H  HB3  A ALA   A 1 52  ? 18.747 5.828   5.704   0.74 16.21 ?  52  ALA   A HB3  1 
ATOM   1260 H  HB3  B ALA   A 1 52  ? 18.535 6.083   5.502   0.26 15.21 ?  52  ALA   A HB3  1 
ATOM   1261 N  N    A LEU   A 1 53  ? 21.410 6.121   6.841   0.74 10.82 ?  53  LEU   A N    1 
ATOM   1262 N  N    B LEU   A 1 53  ? 21.275 6.285   6.629   0.26 12.76 ?  53  LEU   A N    1 
ATOM   1263 C  CA   A LEU   A 1 53  ? 22.396 5.729   7.846   0.74 11.43 ?  53  LEU   A CA   1 
ATOM   1264 C  CA   B LEU   A 1 53  ? 22.191 5.818   7.664   0.26 12.97 ?  53  LEU   A CA   1 
ATOM   1265 C  C    A LEU   A 1 53  ? 23.443 6.818   8.026   0.74 10.87 ?  53  LEU   A C    1 
ATOM   1266 C  C    B LEU   A 1 53  ? 23.271 6.857   7.939   0.26 12.77 ?  53  LEU   A C    1 
ATOM   1267 O  O    A LEU   A 1 53  ? 23.803 7.171   9.156   0.74 12.41 ?  53  LEU   A O    1 
ATOM   1268 O  O    B LEU   A 1 53  ? 23.532 7.208   9.096   0.26 13.07 ?  53  LEU   A O    1 
ATOM   1269 C  CB   A LEU   A 1 53  ? 23.075 4.415   7.464   0.74 11.55 ?  53  LEU   A CB   1 
ATOM   1270 C  CB   B LEU   A 1 53  ? 22.804 4.471   7.265   0.26 13.24 ?  53  LEU   A CB   1 
ATOM   1271 C  CG   A LEU   A 1 53  ? 22.248 3.127   7.527   0.74 12.17 ?  53  LEU   A CG   1 
ATOM   1272 C  CG   B LEU   A 1 53  ? 21.896 3.243   7.401   0.26 13.12 ?  53  LEU   A CG   1 
ATOM   1273 C  CD1  A LEU   A 1 53  ? 23.012 1.992   6.870   0.74 13.09 ?  53  LEU   A CD1  1 
ATOM   1274 C  CD1  B LEU   A 1 53  ? 22.575 2.018   6.816   0.26 12.81 ?  53  LEU   A CD1  1 
ATOM   1275 C  CD2  A LEU   A 1 53  ? 21.887 2.742   8.952   0.74 13.64 ?  53  LEU   A CD2  1 
ATOM   1276 C  CD2  B LEU   A 1 53  ? 21.527 2.981   8.854   0.26 13.74 ?  53  LEU   A CD2  1 
ATOM   1277 H  H    A LEU   A 1 53  ? 21.340 5.587   6.167   0.74 12.99 ?  53  LEU   A H    1 
ATOM   1278 H  H    B LEU   A 1 53  ? 21.273 5.812   5.913   0.26 15.33 ?  53  LEU   A H    1 
ATOM   1279 H  HA   A LEU   A 1 53  ? 21.943 5.597   8.697   0.74 13.72 ?  53  LEU   A HA   1 
ATOM   1280 H  HA   B LEU   A 1 53  ? 21.699 5.690   8.487   0.26 15.57 ?  53  LEU   A HA   1 
ATOM   1281 H  HB2  A LEU   A 1 53  ? 23.397 4.501   6.552   0.74 13.87 ?  53  LEU   A HB2  1 
ATOM   1282 H  HB2  B LEU   A 1 53  ? 23.076 4.519   6.335   0.26 15.90 ?  53  LEU   A HB2  1 
ATOM   1283 H  HB3  A LEU   A 1 53  ? 23.833 4.289   8.055   0.74 13.87 ?  53  LEU   A HB3  1 
ATOM   1284 H  HB3  B LEU   A 1 53  ? 23.583 4.305   7.818   0.26 15.90 ?  53  LEU   A HB3  1 
ATOM   1285 H  HG   A LEU   A 1 53  ? 21.426 3.250   7.025   0.74 14.61 ?  53  LEU   A HG   1 
ATOM   1286 H  HG   B LEU   A 1 53  ? 21.075 3.393   6.902   0.26 15.76 ?  53  LEU   A HG   1 
ATOM   1287 H  HD11 A LEU   A 1 53  ? 22.480 1.179   6.917   0.74 15.71 ?  53  LEU   A HD11 1 
ATOM   1288 H  HD11 B LEU   A 1 53  ? 21.991 1.250   6.920   0.26 15.39 ?  53  LEU   A HD11 1 
ATOM   1289 H  HD12 A LEU   A 1 53  ? 23.184 2.216   5.941   0.74 15.71 ?  53  LEU   A HD12 1 
ATOM   1290 H  HD12 B LEU   A 1 53  ? 22.754 2.173   5.875   0.26 15.39 ?  53  LEU   A HD12 1 
ATOM   1291 H  HD13 A LEU   A 1 53  ? 23.852 1.861   7.338   0.74 15.71 ?  53  LEU   A HD13 1 
ATOM   1292 H  HD13 B LEU   A 1 53  ? 23.409 1.865   7.290   0.26 15.39 ?  53  LEU   A HD13 1 
ATOM   1293 H  HD21 A LEU   A 1 53  ? 21.380 1.911   8.939   0.74 16.38 ?  53  LEU   A HD21 1 
ATOM   1294 H  HD21 B LEU   A 1 53  ? 20.572 2.831   8.915   0.26 16.50 ?  53  LEU   A HD21 1 
ATOM   1295 H  HD22 A LEU   A 1 53  ? 22.699 2.624   9.465   0.74 16.38 ?  53  LEU   A HD22 1 
ATOM   1296 H  HD22 B LEU   A 1 53  ? 22.003 2.192   9.159   0.26 16.50 ?  53  LEU   A HD22 1 
ATOM   1297 H  HD23 A LEU   A 1 53  ? 21.346 3.448   9.339   0.74 16.38 ?  53  LEU   A HD23 1 
ATOM   1298 H  HD23 B LEU   A 1 53  ? 21.780 3.744   9.393   0.26 16.50 ?  53  LEU   A HD23 1 
ATOM   1299 N  N    A ASN   A 1 54  ? 23.934 7.384   6.922   0.74 10.87 ?  54  ASN   A N    1 
ATOM   1300 N  N    B ASN   A 1 54  ? 23.883 7.396   6.881   0.26 12.57 ?  54  ASN   A N    1 
ATOM   1301 C  CA   A ASN   A 1 54  ? 24.982 8.390   7.046   0.74 11.29 ?  54  ASN   A CA   1 
ATOM   1302 C  CA   B ASN   A 1 54  ? 24.959 8.363   7.076   0.26 12.48 ?  54  ASN   A CA   1 
ATOM   1303 C  C    A ASN   A 1 54  ? 24.469 9.631   7.773   0.74 11.40 ?  54  ASN   A C    1 
ATOM   1304 C  C    B ASN   A 1 54  ? 24.454 9.611   7.795   0.26 12.15 ?  54  ASN   A C    1 
ATOM   1305 O  O    A ASN   A 1 54  ? 25.159 10.193  8.634   0.74 11.72 ?  54  ASN   A O    1 
ATOM   1306 O  O    B ASN   A 1 54  ? 25.137 10.154  8.672   0.26 12.31 ?  54  ASN   A O    1 
ATOM   1307 C  CB   A ASN   A 1 54  ? 25.532 8.769   5.680   0.74 11.45 ?  54  ASN   A CB   1 
ATOM   1308 C  CB   B ASN   A 1 54  ? 25.591 8.736   5.737   0.26 12.43 ?  54  ASN   A CB   1 
ATOM   1309 C  CG   A ASN   A 1 54  ? 26.562 9.854   5.790   0.74 12.18 ?  54  ASN   A CG   1 
ATOM   1310 C  CG   B ASN   A 1 54  ? 26.596 9.857   5.876   0.26 12.30 ?  54  ASN   A CG   1 
ATOM   1311 O  OD1  A ASN   A 1 54  ? 27.550 9.703   6.511   0.74 12.54 ?  54  ASN   A OD1  1 
ATOM   1312 O  OD1  B ASN   A 1 54  ? 27.643 9.689   6.502   0.26 12.26 ?  54  ASN   A OD1  1 
ATOM   1313 N  ND2  A ASN   A 1 54  ? 26.335 10.961  5.110   0.74 13.12 ?  54  ASN   A ND2  1 
ATOM   1314 N  ND2  B ASN   A 1 54  ? 26.282 11.010  5.304   0.26 12.47 ?  54  ASN   A ND2  1 
ATOM   1315 H  H    A ASN   A 1 54  ? 23.676 7.207   6.120   0.74 13.05 ?  54  ASN   A H    1 
ATOM   1316 H  H    B ASN   A 1 54  ? 23.685 7.231   6.059   0.26 15.09 ?  54  ASN   A H    1 
ATOM   1317 H  HA   A ASN   A 1 54  ? 25.703 8.014   7.568   0.74 13.56 ?  54  ASN   A HA   1 
ATOM   1318 H  HA   B ASN   A 1 54  ? 25.648 7.958   7.624   0.26 14.98 ?  54  ASN   A HA   1 
ATOM   1319 H  HB2  A ASN   A 1 54  ? 25.947 7.986   5.277   0.74 13.75 ?  54  ASN   A HB2  1 
ATOM   1320 H  HB2  B ASN   A 1 54  ? 26.050 7.960   5.373   0.26 14.92 ?  54  ASN   A HB2  1 
ATOM   1321 H  HB3  A ASN   A 1 54  ? 24.806 9.085   5.119   0.74 13.75 ?  54  ASN   A HB3  1 
ATOM   1322 H  HB3  B ASN   A 1 54  ? 24.896 9.026   5.125   0.26 14.92 ?  54  ASN   A HB3  1 
ATOM   1323 H  HD21 A ASN   A 1 54  ? 26.895 11.614  5.150   0.74 15.76 ?  54  ASN   A HD21 1 
ATOM   1324 H  HD21 B ASN   A 1 54  ? 26.821 11.679  5.360   0.26 14.97 ?  54  ASN   A HD21 1 
ATOM   1325 H  HD22 A ASN   A 1 54  ? 25.624 11.034  4.635   0.74 15.76 ?  54  ASN   A HD22 1 
ATOM   1326 H  HD22 B ASN   A 1 54  ? 25.539 11.093  4.879   0.26 14.97 ?  54  ASN   A HD22 1 
ATOM   1327 N  N    . LYS   A 1 55  ? 23.259 10.085  7.431   1.00 11.92 ?  55  LYS   A N    1 
ATOM   1328 C  CA   . LYS   A 1 55  ? 22.674 11.241  8.107   1.00 12.71 ?  55  LYS   A CA   1 
ATOM   1329 C  C    . LYS   A 1 55  ? 22.583 10.998  9.610   1.00 12.27 ?  55  LYS   A C    1 
ATOM   1330 O  O    . LYS   A 1 55  ? 22.880 11.889  10.413  1.00 13.61 ?  55  LYS   A O    1 
ATOM   1331 C  CB   . LYS   A 1 55  ? 21.302 11.546  7.498   1.00 13.58 ?  55  LYS   A CB   1 
ATOM   1332 C  CG   . LYS   A 1 55  ? 20.555 12.708  8.128   1.00 15.18 ?  55  LYS   A CG   1 
ATOM   1333 C  CD   . LYS   A 1 55  ? 19.226 12.941  7.404   1.00 16.61 ?  55  LYS   A CD   1 
ATOM   1334 C  CE   . LYS   A 1 55  ? 18.377 14.021  8.062   1.00 18.46 ?  55  LYS   A CE   1 
ATOM   1335 N  NZ   . LYS   A 1 55  ? 17.037 14.173  7.405   1.00 19.92 ?  55  LYS   A NZ   1 
ATOM   1336 H  H    A LYS   A 1 55  ? 22.758 9.737   6.823   0.74 14.31 ?  55  LYS   A H    1 
ATOM   1337 H  H    B LYS   A 1 55  ? 22.768 9.751   6.808   0.26 14.31 ?  55  LYS   A H    1 
ATOM   1338 H  HA   . LYS   A 1 55  ? 23.247 12.009  7.962   1.00 15.26 ?  55  LYS   A HA   1 
ATOM   1339 H  HB2  . LYS   A 1 55  ? 21.425 11.752  6.558   1.00 16.30 ?  55  LYS   A HB2  1 
ATOM   1340 H  HB3  . LYS   A 1 55  ? 20.747 10.755  7.586   1.00 16.30 ?  55  LYS   A HB3  1 
ATOM   1341 H  HG2  . LYS   A 1 55  ? 20.369 12.498  9.060   1.00 18.22 ?  55  LYS   A HG2  1 
ATOM   1342 H  HG3  . LYS   A 1 55  ? 21.096 13.507  8.064   1.00 18.22 ?  55  LYS   A HG3  1 
ATOM   1343 H  HD2  . LYS   A 1 55  ? 19.414 13.218  6.494   1.00 19.95 ?  55  LYS   A HD2  1 
ATOM   1344 H  HD3  . LYS   A 1 55  ? 18.719 12.116  7.404   1.00 19.95 ?  55  LYS   A HD3  1 
ATOM   1345 H  HE2  . LYS   A 1 55  ? 18.231 13.789  8.992   1.00 22.16 ?  55  LYS   A HE2  1 
ATOM   1346 H  HE3  . LYS   A 1 55  ? 18.838 14.872  8.000   1.00 22.16 ?  55  LYS   A HE3  1 
ATOM   1347 H  HZ1  . LYS   A 1 55  ? 16.469 14.579  7.960   1.00 23.91 ?  55  LYS   A HZ1  1 
ATOM   1348 H  HZ2  . LYS   A 1 55  ? 17.109 14.661  6.665   1.00 23.91 ?  55  LYS   A HZ2  1 
ATOM   1349 H  HZ3  . LYS   A 1 55  ? 16.705 13.373  7.195   1.00 23.91 ?  55  LYS   A HZ3  1 
ATOM   1350 N  N    . ALA   A 1 56  ? 22.216 9.782   10.010  1.00 13.19 ?  56  ALA   A N    1 
ATOM   1351 C  CA   . ALA   A 1 56  ? 22.082 9.461   11.425  1.00 14.30 ?  56  ALA   A CA   1 
ATOM   1352 C  C    . ALA   A 1 56  ? 23.426 9.502   12.153  1.00 14.32 ?  56  ALA   A C    1 
ATOM   1353 O  O    . ALA   A 1 56  ? 23.455 9.704   13.371  1.00 15.38 ?  56  ALA   A O    1 
ATOM   1354 C  CB   . ALA   A 1 56  ? 21.414 8.093   11.583  1.00 15.09 ?  56  ALA   A CB   1 
ATOM   1355 H  H    . ALA   A 1 56  ? 22.034 9.129   9.478   1.00 15.84 ?  56  ALA   A H    1 
ATOM   1356 H  HA   . ALA   A 1 56  ? 21.503 10.113  11.840  1.00 17.17 ?  56  ALA   A HA   1 
ATOM   1357 H  HB1  . ALA   A 1 56  ? 21.326 7.890   12.531  1.00 18.12 ?  56  ALA   A HB1  1 
ATOM   1358 H  HB2  . ALA   A 1 56  ? 20.532 8.120   11.174  1.00 18.12 ?  56  ALA   A HB2  1 
ATOM   1359 H  HB3  . ALA   A 1 56  ? 21.957 7.416   11.152  1.00 18.12 ?  56  ALA   A HB3  1 
ATOM   1360 N  N    . THR   A 1 57  ? 24.538 9.300   11.441  1.00 13.04 ?  57  THR   A N    1 
ATOM   1361 C  CA   . THR   A 1 57  ? 25.883 9.436   12.013  1.00 13.18 ?  57  THR   A CA   1 
ATOM   1362 C  C    . THR   A 1 57  ? 26.427 10.860  11.935  1.00 13.55 ?  57  THR   A C    1 
ATOM   1363 O  O    . THR   A 1 57  ? 27.612 11.080  12.215  1.00 14.00 ?  57  THR   A O    1 
ATOM   1364 C  CB   . THR   A 1 57  ? 26.901 8.492   11.339  1.00 12.57 ?  57  THR   A CB   1 
ATOM   1365 O  OG1  . THR   A 1 57  ? 27.264 8.983   10.036  1.00 12.96 ?  57  THR   A OG1  1 
ATOM   1366 C  CG2  . THR   A 1 57  ? 26.372 7.080   11.240  1.00 13.28 ?  57  THR   A CG2  1 
ATOM   1367 H  H    . THR   A 1 57  ? 24.540 9.057   10.612  1.00 15.65 ?  57  THR   A H    1 
ATOM   1368 H  HA   . THR   A 1 57  ? 25.838 9.179   12.952  1.00 15.82 ?  57  THR   A HA   1 
ATOM   1369 H  HB   . THR   A 1 57  ? 27.700 8.455   11.892  1.00 15.10 ?  57  THR   A HB   1 
ATOM   1370 H  HG1  . THR   A 1 57  ? 26.571 9.031   9.555   1.00 15.56 ?  57  THR   A HG1  1 
ATOM   1371 H  HG21 . THR   A 1 57  ? 27.059 6.484   10.906  1.00 15.94 ?  57  THR   A HG21 1 
ATOM   1372 H  HG22 . THR   A 1 57  ? 26.081 6.765   12.113  1.00 15.94 ?  57  THR   A HG22 1 
ATOM   1373 H  HG23 . THR   A 1 57  ? 25.612 7.050   10.634  1.00 15.94 ?  57  THR   A HG23 1 
ATOM   1374 N  N    . ASN   A 1 58  ? 25.611 11.822  11.520  1.00 13.89 ?  58  ASN   A N    1 
ATOM   1375 C  CA   . ASN   A 1 58  ? 26.074 13.207  11.423  1.00 15.08 ?  58  ASN   A CA   1 
ATOM   1376 C  C    . ASN   A 1 58  ? 27.235 13.339  10.432  1.00 14.12 ?  58  ASN   A C    1 
ATOM   1377 O  O    . ASN   A 1 58  ? 28.130 14.176  10.602  1.00 14.47 ?  58  ASN   A O    1 
ATOM   1378 C  CB   . ASN   A 1 58  ? 26.430 13.765  12.813  1.00 17.81 ?  58  ASN   A CB   1 
ATOM   1379 C  CG   . ASN   A 1 58  ? 26.765 15.242  12.800  1.00 22.77 ?  58  ASN   A CG   1 
ATOM   1380 O  OD1  . ASN   A 1 58  ? 26.121 16.034  12.119  1.00 24.91 ?  58  ASN   A OD1  1 
ATOM   1381 N  ND2  . ASN   A 1 58  ? 27.773 15.622  13.579  1.00 24.47 ?  58  ASN   A ND2  1 
ATOM   1382 H  H    . ASN   A 1 58  ? 24.792 11.696  11.281  1.00 16.67 ?  58  ASN   A H    1 
ATOM   1383 H  HA   . ASN   A 1 58  ? 25.340 13.735  11.084  1.00 18.11 ?  58  ASN   A HA   1 
ATOM   1384 H  HB2  . ASN   A 1 58  ? 25.672 13.628  13.412  1.00 21.38 ?  58  ASN   A HB2  1 
ATOM   1385 H  HB3  . ASN   A 1 58  ? 27.203 13.291  13.160  1.00 21.38 ?  58  ASN   A HB3  1 
ATOM   1386 H  HD21 . ASN   A 1 58  ? 27.998 16.452  13.613  1.00 29.37 ?  58  ASN   A HD21 1 
ATOM   1387 H  HD22 . ASN   A 1 58  ? 28.198 15.041  14.046  1.00 29.37 ?  58  ASN   A HD22 1 
ATOM   1388 N  N    . ASN   A 1 59  ? 27.211 12.524  9.375   1.00 12.69 ?  59  ASN   A N    1 
ATOM   1389 C  CA   . ASN   A 1 59  ? 28.189 12.492  8.284   1.00 12.68 ?  59  ASN   A CA   1 
ATOM   1390 C  C    . ASN   A 1 59  ? 29.507 11.814  8.677   1.00 12.48 ?  59  ASN   A C    1 
ATOM   1391 O  O    . ASN   A 1 59  ? 30.434 11.781  7.849   1.00 12.62 ?  59  ASN   A O    1 
ATOM   1392 C  CB   . ASN   A 1 59  ? 28.472 13.883  7.680   1.00 12.57 ?  59  ASN   A CB   1 
ATOM   1393 C  CG   . ASN   A 1 59  ? 28.824 13.823  6.211   1.00 13.22 ?  59  ASN   A CG   1 
ATOM   1394 O  OD1  . ASN   A 1 59  ? 28.132 13.184  5.412   1.00 13.17 ?  59  ASN   A OD1  1 
ATOM   1395 N  ND2  . ASN   A 1 59  ? 29.913 14.493  5.839   1.00 14.32 ?  59  ASN   A ND2  1 
ATOM   1396 H  H    . ASN   A 1 59  ? 26.590 11.936  9.257   1.00 15.23 ?  59  ASN   A H    1 
ATOM   1397 H  HA   . ASN   A 1 59  ? 27.811 11.960  7.572   1.00 15.23 ?  59  ASN   A HA   1 
ATOM   1398 H  HB2  . ASN   A 1 59  ? 27.685 14.440  7.770   1.00 15.09 ?  59  ASN   A HB2  1 
ATOM   1399 H  HB3  . ASN   A 1 59  ? 29.222 14.288  8.143   1.00 15.09 ?  59  ASN   A HB3  1 
ATOM   1400 H  HD21 . ASN   A 1 59  ? 30.160 14.488  5.013   1.00 17.19 ?  59  ASN   A HD21 1 
ATOM   1401 H  HD22 . ASN   A 1 59  ? 30.377 14.921  6.422   1.00 17.19 ?  59  ASN   A HD22 1 
ATOM   1402 N  N    . ALA   A 1 60  ? 29.630 11.254  9.882   1.00 12.68 ?  60  ALA   A N    1 
ATOM   1403 C  CA   . ALA   A 1 60  ? 30.878 10.586  10.226  1.00 12.17 ?  60  ALA   A CA   1 
ATOM   1404 C  C    . ALA   A 1 60  ? 31.104 9.353   9.353   1.00 13.00 ?  60  ALA   A C    1 
ATOM   1405 O  O    . ALA   A 1 60  ? 32.249 9.019   9.016   1.00 13.10 ?  60  ALA   A O    1 
ATOM   1406 C  CB   . ALA   A 1 60  ? 30.885 10.204  11.706  1.00 12.85 ?  60  ALA   A CB   1 
ATOM   1407 H  H    . ALA   A 1 60  ? 29.029 11.251  10.501  1.00 15.22 ?  60  ALA   A H    1 
ATOM   1408 H  HA   . ALA   A 1 60  ? 31.617 11.201  10.080  1.00 14.61 ?  60  ALA   A HA   1 
ATOM   1409 H  HB1  . ALA   A 1 60  ? 31.719 9.763   11.920  1.00 15.43 ?  60  ALA   A HB1  1 
ATOM   1410 H  HB2  . ALA   A 1 60  ? 30.789 11.009  12.245  1.00 15.43 ?  60  ALA   A HB2  1 
ATOM   1411 H  HB3  . ALA   A 1 60  ? 30.139 9.606   11.881  1.00 15.43 ?  60  ALA   A HB3  1 
ATOM   1412 N  N    . MET   A 1 61  ? 30.032 8.646   8.974   1.00 12.60 ?  61  MET   A N    1 
ATOM   1413 C  CA   . MET   A 1 61  ? 30.177 7.510   8.065   1.00 12.27 ?  61  MET   A CA   1 
ATOM   1414 C  C    . MET   A 1 61  ? 30.803 7.946   6.739   1.00 11.86 ?  61  MET   A C    1 
ATOM   1415 O  O    . MET   A 1 61  ? 31.691 7.270   6.210   1.00 12.08 ?  61  MET   A O    1 
ATOM   1416 C  CB   . MET   A 1 61  ? 28.813 6.839   7.860   1.00 11.73 ?  61  MET   A CB   1 
ATOM   1417 C  CG   . MET   A 1 61  ? 28.813 5.695   6.873   1.00 11.79 ?  61  MET   A CG   1 
ATOM   1418 S  SD   . MET   A 1 61  ? 27.186 4.941   6.658   1.00 13.50 ?  61  MET   A SD   1 
ATOM   1419 C  CE   . MET   A 1 61  ? 27.001 4.080   8.214   1.00 15.10 ?  61  MET   A CE   1 
ATOM   1420 H  H    . MET   A 1 61  ? 29.224 8.808   9.216   1.00 15.12 ?  61  MET   A H    1 
ATOM   1421 H  HA   . MET   A 1 61  ? 30.762 6.854   8.478   1.00 14.73 ?  61  MET   A HA   1 
ATOM   1422 H  HB2  . MET   A 1 61  ? 28.509 6.490   8.709   1.00 14.09 ?  61  MET   A HB2  1 
ATOM   1423 H  HB3  . MET   A 1 61  ? 28.188 7.502   7.532   1.00 14.09 ?  61  MET   A HB3  1 
ATOM   1424 H  HG2  . MET   A 1 61  ? 29.099 6.012   6.002   1.00 14.16 ?  61  MET   A HG2  1 
ATOM   1425 H  HG3  . MET   A 1 61  ? 29.419 5.001   7.185   1.00 14.16 ?  61  MET   A HG3  1 
ATOM   1426 H  HE1  . MET   A 1 61  ? 26.152 3.604   8.216   1.00 18.13 ?  61  MET   A HE1  1 
ATOM   1427 H  HE2  . MET   A 1 61  ? 27.731 3.451   8.319   1.00 18.13 ?  61  MET   A HE2  1 
ATOM   1428 H  HE3  . MET   A 1 61  ? 27.013 4.726   8.940   1.00 18.13 ?  61  MET   A HE3  1 
ATOM   1429 N  N    . GLN   A 1 62  ? 30.357 9.079   6.188   1.00 11.90 ?  62  GLN   A N    1 
ATOM   1430 C  CA   . GLN   A 1 62  ? 30.915 9.565   4.928   1.00 11.77 ?  62  GLN   A CA   1 
ATOM   1431 C  C    . GLN   A 1 62  ? 32.387 9.937   5.074   1.00 11.50 ?  62  GLN   A C    1 
ATOM   1432 O  O    . GLN   A 1 62  ? 33.202 9.614   4.201   1.00 12.34 ?  62  GLN   A O    1 
ATOM   1433 C  CB   . GLN   A 1 62  ? 30.110 10.756  4.399   1.00 12.97 ?  62  GLN   A CB   1 
ATOM   1434 C  CG   . GLN   A 1 62  ? 30.500 11.118  2.978   1.00 12.54 ?  62  GLN   A CG   1 
ATOM   1435 C  CD   . GLN   A 1 62  ? 30.152 9.993   2.022   1.00 12.33 ?  62  GLN   A CD   1 
ATOM   1436 O  OE1  . GLN   A 1 62  ? 28.972 9.695   1.807   1.00 13.01 ?  62  GLN   A OE1  1 
ATOM   1437 N  NE2  . GLN   A 1 62  ? 31.163 9.319   1.490   1.00 12.77 ?  62  GLN   A NE2  1 
ATOM   1438 H  H    . GLN   A 1 62  ? 29.733 9.569   6.515   1.00 14.28 ?  62  GLN   A H    1 
ATOM   1439 H  HA   . GLN   A 1 62  ? 30.861 8.851   4.271   1.00 14.13 ?  62  GLN   A HA   1 
ATOM   1440 H  HB2  . GLN   A 1 62  ? 29.166 10.533  4.409   1.00 15.57 ?  62  GLN   A HB2  1 
ATOM   1441 H  HB3  . GLN   A 1 62  ? 30.277 11.527  4.967   1.00 15.57 ?  62  GLN   A HB3  1 
ATOM   1442 H  HG2  . GLN   A 1 62  ? 30.012 11.908  2.704   1.00 15.06 ?  62  GLN   A HG2  1 
ATOM   1443 H  HG3  . GLN   A 1 62  ? 31.456 11.279  2.934   1.00 15.06 ?  62  GLN   A HG3  1 
ATOM   1444 H  HE21 . GLN   A 1 62  ? 31.974 9.545   1.672   1.00 15.33 ?  62  GLN   A HE21 1 
ATOM   1445 H  HE22 . GLN   A 1 62  ? 31.012 8.666   0.951   1.00 15.33 ?  62  GLN   A HE22 1 
ATOM   1446 N  N    . VAL   A 1 63  ? 32.750 10.615  6.170   1.00 12.49 ?  63  VAL   A N    1 
ATOM   1447 C  CA   . VAL   A 1 63  ? 34.145 11.009  6.382   1.00 13.33 ?  63  VAL   A CA   1 
ATOM   1448 C  C    . VAL   A 1 63  ? 35.042 9.776   6.444   1.00 12.42 ?  63  VAL   A C    1 
ATOM   1449 O  O    . VAL   A 1 63  ? 36.089 9.706   5.788   1.00 13.30 ?  63  VAL   A O    1 
ATOM   1450 C  CB   . VAL   A 1 63  ? 34.266 11.872  7.650   1.00 15.04 ?  63  VAL   A CB   1 
ATOM   1451 C  CG1  . VAL   A 1 63  ? 35.726 12.137  7.996   1.00 16.55 ?  63  VAL   A CG1  1 
ATOM   1452 C  CG2  . VAL   A 1 63  ? 33.522 13.194  7.462   1.00 15.79 ?  63  VAL   A CG2  1 
ATOM   1453 H  H    . VAL   A 1 63  ? 32.206 10.856  6.797   1.00 14.99 ?  63  VAL   A H    1 
ATOM   1454 H  HA   . VAL   A 1 63  ? 34.429 11.550  5.627   1.00 16.00 ?  63  VAL   A HA   1 
ATOM   1455 H  HB   . VAL   A 1 63  ? 33.856 11.400  8.394   1.00 18.06 ?  63  VAL   A HB   1 
ATOM   1456 H  HG11 . VAL   A 1 63  ? 35.767 12.862  8.636   1.00 19.86 ?  63  VAL   A HG11 1 
ATOM   1457 H  HG12 . VAL   A 1 63  ? 36.110 11.334  8.377   1.00 19.86 ?  63  VAL   A HG12 1 
ATOM   1458 H  HG13 . VAL   A 1 63  ? 36.197 12.382  7.185   1.00 19.86 ?  63  VAL   A HG13 1 
ATOM   1459 H  HG21 . VAL   A 1 63  ? 33.616 13.726  8.267   1.00 18.96 ?  63  VAL   A HG21 1 
ATOM   1460 H  HG22 . VAL   A 1 63  ? 33.902 13.664  6.705   1.00 18.96 ?  63  VAL   A HG22 1 
ATOM   1461 H  HG23 . VAL   A 1 63  ? 32.582 13.008  7.298   1.00 18.96 ?  63  VAL   A HG23 1 
ATOM   1462 N  N    . GLU   A 1 64  ? 34.618 8.764   7.210   1.00 12.57 ?  64  GLU   A N    1 
ATOM   1463 C  CA   . GLU   A 1 64  ? 35.386 7.527   7.298   1.00 12.41 ?  64  GLU   A CA   1 
ATOM   1464 C  C    . GLU   A 1 64  ? 35.466 6.838   5.939   1.00 12.08 ?  64  GLU   A C    1 
ATOM   1465 O  O    . GLU   A 1 64  ? 36.511 6.289   5.561   1.00 12.73 ?  64  GLU   A O    1 
ATOM   1466 C  CB   . GLU   A 1 64  ? 34.715 6.617   8.327   1.00 13.18 ?  64  GLU   A CB   1 
ATOM   1467 C  CG   . GLU   A 1 64  ? 35.354 5.261   8.455   1.00 13.83 ?  64  GLU   A CG   1 
ATOM   1468 C  CD   . GLU   A 1 64  ? 34.474 4.273   9.189   1.00 14.69 ?  64  GLU   A CD   1 
ATOM   1469 O  OE1  . GLU   A 1 64  ? 33.230 4.367   9.060   1.00 15.75 ?  64  GLU   A OE1  1 
ATOM   1470 O  OE2  . GLU   A 1 64  ? 35.024 3.390   9.888   1.00 15.36 -1 64  GLU   A OE2  1 
ATOM   1471 H  H    . GLU   A 1 64  ? 33.888 8.773   7.677   1.00 15.09 ?  64  GLU   A H    1 
ATOM   1472 H  HA   . GLU   A 1 64  ? 36.282 7.737   7.602   1.00 14.90 ?  64  GLU   A HA   1 
ATOM   1473 H  HB2  . GLU   A 1 64  ? 34.758 7.053   9.200   1.00 15.82 ?  64  GLU   A HB2  1 
ATOM   1474 H  HB3  . GLU   A 1 64  ? 33.788 6.498   8.074   1.00 15.82 ?  64  GLU   A HB3  1 
ATOM   1475 H  HG2  . GLU   A 1 64  ? 35.533 4.899   7.572   1.00 16.61 ?  64  GLU   A HG2  1 
ATOM   1476 H  HG3  . GLU   A 1 64  ? 36.183 5.351   8.949   1.00 16.61 ?  64  GLU   A HG3  1 
ATOM   1477 N  N    . SER   A 1 65  ? 34.350 6.837   5.203   1.00 12.28 ?  65  SER   A N    1 
ATOM   1478 C  CA   . SER   A 1 65  ? 34.297 6.176   3.901   1.00 12.02 ?  65  SER   A CA   1 
ATOM   1479 C  C    . SER   A 1 65  ? 35.221 6.847   2.892   1.00 12.24 ?  65  SER   A C    1 
ATOM   1480 O  O    . SER   A 1 65  ? 35.863 6.171   2.080   1.00 13.28 ?  65  SER   A O    1 
ATOM   1481 C  CB   . SER   A 1 65  ? 32.854 6.186   3.374   1.00 11.99 ?  65  SER   A CB   1 
ATOM   1482 O  OG   . SER   A 1 65  ? 32.018 5.359   4.172   1.00 12.36 ?  65  SER   A OG   1 
ATOM   1483 H  H    . SER   A 1 65  ? 33.612 7.215   5.439   1.00 14.75 ?  65  SER   A H    1 
ATOM   1484 H  HA   . SER   A 1 65  ? 34.579 5.253   4.002   1.00 14.44 ?  65  SER   A HA   1 
ATOM   1485 H  HB2  . SER   A 1 65  ? 32.515 7.092   3.398   1.00 14.39 ?  65  SER   A HB2  1 
ATOM   1486 H  HB3  . SER   A 1 65  ? 32.852 5.851   2.466   1.00 14.39 ?  65  SER   A HB3  1 
ATOM   1487 H  HG   . SER   A 1 65  ? 32.019 5.638   4.972   1.00 14.84 ?  65  SER   A HG   1 
ATOM   1488 N  N    . ASP   A 1 66  ? 35.306 8.176   2.926   1.00 12.04 ?  66  ASP   A N    1 
ATOM   1489 C  CA   . ASP   A 1 66  ? 36.161 8.885   1.978   1.00 12.78 ?  66  ASP   A CA   1 
ATOM   1490 C  C    . ASP   A 1 66  ? 37.626 8.534   2.201   1.00 12.72 ?  66  ASP   A C    1 
ATOM   1491 O  O    . ASP   A 1 66  ? 38.395 8.383   1.243   1.00 14.47 ?  66  ASP   A O    1 
ATOM   1492 C  CB   . ASP   A 1 66  ? 35.937 10.393  2.096   1.00 14.88 ?  66  ASP   A CB   1 
ATOM   1493 C  CG   . ASP   A 1 66  ? 34.604 10.848  1.505   1.00 17.18 ?  66  ASP   A CG   1 
ATOM   1494 O  OD1  . ASP   A 1 66  ? 33.917 10.049  0.843   1.00 17.04 ?  66  ASP   A OD1  1 
ATOM   1495 O  OD2  . ASP   A 1 66  ? 34.265 12.035  1.684   1.00 20.64 -1 66  ASP   A OD2  1 
ATOM   1496 H  H    . ASP   A 1 66  ? 34.870 8.685   3.477   1.00 14.45 ?  66  ASP   A H    1 
ATOM   1497 H  HA   . ASP   A 1 66  ? 35.917 8.614   1.080   1.00 15.34 ?  66  ASP   A HA   1 
ATOM   1498 H  HB2  . ASP   A 1 66  ? 35.946 10.643  3.031   1.00 17.86 ?  66  ASP   A HB2  1 
ATOM   1499 H  HB3  . ASP   A 1 66  ? 36.651 10.849  1.622   1.00 17.86 ?  66  ASP   A HB3  1 
ATOM   1500 N  N    . ASP   A 1 67  ? 38.038 8.400   3.463   1.00 13.55 ?  67  ASP   A N    1 
ATOM   1501 C  CA   . ASP   A 1 67  ? 39.395 7.950   3.750   1.00 14.74 ?  67  ASP   A CA   1 
ATOM   1502 C  C    . ASP   A 1 67  ? 39.613 6.515   3.279   1.00 14.00 ?  67  ASP   A C    1 
ATOM   1503 O  O    . ASP   A 1 67  ? 40.660 6.198   2.710   1.00 14.82 ?  67  ASP   A O    1 
ATOM   1504 C  CB   . ASP   A 1 67  ? 39.681 8.097   5.244   1.00 15.40 ?  67  ASP   A CB   1 
ATOM   1505 C  CG   . ASP   A 1 67  ? 40.967 7.414   5.661   1.00 16.77 ?  67  ASP   A CG   1 
ATOM   1506 O  OD1  . ASP   A 1 67  ? 42.039 8.064   5.541   1.00 19.95 ?  67  ASP   A OD1  1 
ATOM   1507 O  OD2  . ASP   A 1 67  ? 40.898 6.242   6.117   1.00 16.06 -1 67  ASP   A OD2  1 
ATOM   1508 H  H    . ASP   A 1 67  ? 37.560 8.564   4.156   1.00 16.26 ?  67  ASP   A H    1 
ATOM   1509 H  HA   . ASP   A 1 67  ? 40.021 8.519   3.269   1.00 17.70 ?  67  ASP   A HA   1 
ATOM   1510 H  HB2  . ASP   A 1 67  ? 39.760 9.037   5.461   1.00 18.49 ?  67  ASP   A HB2  1 
ATOM   1511 H  HB3  . ASP   A 1 67  ? 38.953 7.697   5.744   1.00 18.49 ?  67  ASP   A HB3  1 
ATOM   1512 N  N    . TYR   A 1 68  ? 38.629 5.630   3.493   1.00 14.07 ?  68  TYR   A N    1 
ATOM   1513 C  CA   . TYR   A 1 68  ? 38.740 4.251   3.007   1.00 13.82 ?  68  TYR   A CA   1 
ATOM   1514 C  C    . TYR   A 1 68  ? 38.973 4.209   1.494   1.00 13.10 ?  68  TYR   A C    1 
ATOM   1515 O  O    . TYR   A 1 68  ? 39.847 3.480   1.006   1.00 14.06 ?  68  TYR   A O    1 
ATOM   1516 C  CB   . TYR   A 1 68  ? 37.484 3.441   3.381   1.00 14.20 ?  68  TYR   A CB   1 
ATOM   1517 C  CG   . TYR   A 1 68  ? 37.502 2.050   2.754   1.00 15.31 ?  68  TYR   A CG   1 
ATOM   1518 C  CD1  . TYR   A 1 68  ? 37.031 1.845   1.459   1.00 16.79 ?  68  TYR   A CD1  1 
ATOM   1519 C  CD2  . TYR   A 1 68  ? 38.050 0.967   3.422   1.00 17.71 ?  68  TYR   A CD2  1 
ATOM   1520 C  CE1  . TYR   A 1 68  ? 37.087 0.617   0.858   1.00 18.94 ?  68  TYR   A CE1  1 
ATOM   1521 C  CE2  . TYR   A 1 68  ? 38.114 -0.294  2.815   1.00 18.51 ?  68  TYR   A CE2  1 
ATOM   1522 C  CZ   . TYR   A 1 68  ? 37.638 -0.446  1.539   1.00 19.43 ?  68  TYR   A CZ   1 
ATOM   1523 O  OH   . TYR   A 1 68  ? 37.711 -1.669  0.929   1.00 22.06 ?  68  TYR   A OH   1 
ATOM   1524 H  H    . TYR   A 1 68  ? 37.893 5.805   3.908   1.00 16.89 ?  68  TYR   A H    1 
ATOM   1525 H  HA   . TYR   A 1 68  ? 39.501 3.833   3.436   1.00 16.59 ?  68  TYR   A HA   1 
ATOM   1526 H  HB2  . TYR   A 1 68  ? 37.444 3.333   4.344   1.00 17.05 ?  68  TYR   A HB2  1 
ATOM   1527 H  HB3  . TYR   A 1 68  ? 36.693 3.906   3.063   1.00 17.05 ?  68  TYR   A HB3  1 
ATOM   1528 H  HD1  . TYR   A 1 68  ? 36.670 2.568   0.987   1.00 20.16 ?  68  TYR   A HD1  1 
ATOM   1529 H  HD2  . TYR   A 1 68  ? 38.391 1.082   4.277   1.00 21.26 ?  68  TYR   A HD2  1 
ATOM   1530 H  HE1  . TYR   A 1 68  ? 36.766 0.506   -0.010  1.00 22.74 ?  68  TYR   A HE1  1 
ATOM   1531 H  HE2  . TYR   A 1 68  ? 38.486 -1.016  3.260   1.00 22.22 ?  68  TYR   A HE2  1 
ATOM   1532 H  HH   . TYR   A 1 68  ? 38.059 -2.227  1.447   1.00 26.48 ?  68  TYR   A HH   1 
ATOM   1533 N  N    . ILE   A 1 69  ? 38.166 4.955   0.729   1.00 12.91 ?  69  ILE   A N    1 
ATOM   1534 C  CA   . ILE   A 1 69  ? 38.312 4.960   -0.727  1.00 13.58 ?  69  ILE   A CA   1 
ATOM   1535 C  C    . ILE   A 1 69  ? 39.645 5.581   -1.153  1.00 13.11 ?  69  ILE   A C    1 
ATOM   1536 O  O    . ILE   A 1 69  ? 40.301 5.088   -2.079  1.00 13.22 ?  69  ILE   A O    1 
ATOM   1537 C  CB   . ILE   A 1 69  ? 37.110 5.661   -1.390  1.00 14.42 ?  69  ILE   A CB   1 
ATOM   1538 C  CG1  . ILE   A 1 69  ? 35.800 4.915   -1.104  1.00 14.94 ?  69  ILE   A CG1  1 
ATOM   1539 C  CG2  . ILE   A 1 69  ? 37.365 5.851   -2.892  1.00 15.91 ?  69  ILE   A CG2  1 
ATOM   1540 C  CD1  . ILE   A 1 69  ? 35.615 3.641   -1.896  1.00 15.77 ?  69  ILE   A CD1  1 
ATOM   1541 H  H    . ILE   A 1 69  ? 37.541 5.468   1.031   1.00 15.50 ?  69  ILE   A H    1 
ATOM   1542 H  HA   . ILE   A 1 69  ? 38.313 4.039   -1.027  1.00 16.30 ?  69  ILE   A HA   1 
ATOM   1543 H  HB   . ILE   A 1 69  ? 37.033 6.540   -0.995  1.00 17.31 ?  69  ILE   A HB   1 
ATOM   1544 H  HG12 . ILE   A 1 69  ? 35.773 4.681   -0.160  1.00 17.94 ?  69  ILE   A HG12 1 
ATOM   1545 H  HG13 . ILE   A 1 69  ? 35.057 5.503   -1.311  1.00 17.94 ?  69  ILE   A HG13 1 
ATOM   1546 H  HG21 . ILE   A 1 69  ? 36.520 6.041   -3.333  1.00 19.10 ?  69  ILE   A HG21 1 
ATOM   1547 H  HG22 . ILE   A 1 69  ? 37.972 6.601   -3.019  1.00 19.10 ?  69  ILE   A HG22 1 
ATOM   1548 H  HG23 . ILE   A 1 69  ? 37.754 5.044   -3.257  1.00 19.10 ?  69  ILE   A HG23 1 
ATOM   1549 H  HD11 . ILE   A 1 69  ? 34.825 3.181   -1.572  1.00 18.93 ?  69  ILE   A HD11 1 
ATOM   1550 H  HD12 . ILE   A 1 69  ? 35.503 3.866   -2.833  1.00 18.93 ?  69  ILE   A HD12 1 
ATOM   1551 H  HD13 . ILE   A 1 69  ? 36.395 3.079   -1.779  1.00 18.93 ?  69  ILE   A HD13 1 
ATOM   1552 N  N    . ALA   A 1 70  ? 40.071 6.659   -0.495  1.00 13.56 ?  70  ALA   A N    1 
ATOM   1553 C  CA   . ALA   A 1 70  ? 41.352 7.259   -0.846  1.00 14.71 ?  70  ALA   A CA   1 
ATOM   1554 C  C    . ALA   A 1 70  ? 42.496 6.267   -0.684  1.00 15.47 ?  70  ALA   A C    1 
ATOM   1555 O  O    . ALA   A 1 70  ? 43.460 6.305   -1.451  1.00 17.37 ?  70  ALA   A O    1 
ATOM   1556 C  CB   . ALA   A 1 70  ? 41.612 8.500   0.006   1.00 15.54 ?  70  ALA   A CB   1 
ATOM   1557 H  H    . ALA   A 1 70  ? 39.641 7.057   0.136   1.00 16.29 ?  70  ALA   A H    1 
ATOM   1558 H  HA   . ALA   A 1 70  ? 41.324 7.543   -1.777  1.00 17.66 ?  70  ALA   A HA   1 
ATOM   1559 H  HB1  . ALA   A 1 70  ? 42.474 8.880   -0.246  1.00 18.66 ?  70  ALA   A HB1  1 
ATOM   1560 H  HB2  . ALA   A 1 70  ? 40.911 9.148   -0.148  1.00 18.66 ?  70  ALA   A HB2  1 
ATOM   1561 H  HB3  . ALA   A 1 70  ? 41.631 8.242   0.941   1.00 18.66 ?  70  ALA   A HB3  1 
ATOM   1562 N  N    . THR   A 1 71  ? 42.405 5.380   0.302   1.00 14.90 ?  71  THR   A N    1 
ATOM   1563 C  CA   . THR   A 1 71  ? 43.453 4.393   0.540   1.00 16.84 ?  71  THR   A CA   1 
ATOM   1564 C  C    . THR   A 1 71  ? 43.314 3.175   -0.362  1.00 16.35 ?  71  THR   A C    1 
ATOM   1565 O  O    . THR   A 1 71  ? 44.315 2.669   -0.888  1.00 18.44 ?  71  THR   A O    1 
ATOM   1566 C  CB   . THR   A 1 71  ? 43.400 3.946   1.998   1.00 18.57 ?  71  THR   A CB   1 
ATOM   1567 O  OG1  . THR   A 1 71  ? 43.671 5.070   2.842   1.00 20.20 ?  71  THR   A OG1  1 
ATOM   1568 C  CG2  . THR   A 1 71  ? 44.401 2.825   2.270   1.00 20.16 ?  71  THR   A CG2  1 
ATOM   1569 H  H    . THR   A 1 71  ? 41.738 5.322   0.836   1.00 17.89 ?  71  THR   A H    1 
ATOM   1570 H  HA   . THR   A 1 71  ? 44.316 4.797   0.369   1.00 20.22 ?  71  THR   A HA   1 
ATOM   1571 H  HB   . THR   A 1 71  ? 42.506 3.605   2.185   1.00 22.29 ?  71  THR   A HB   1 
ATOM   1572 H  HG1  . THR   A 1 71  ? 43.086 5.665   2.706   1.00 24.24 ?  71  THR   A HG1  1 
ATOM   1573 H  HG21 . THR   A 1 71  ? 44.543 2.739   3.224   1.00 24.20 ?  71  THR   A HG21 1 
ATOM   1574 H  HG22 . THR   A 1 71  ? 44.070 1.981   1.924   1.00 24.20 ?  71  THR   A HG22 1 
ATOM   1575 H  HG23 . THR   A 1 71  ? 45.250 3.029   1.843   1.00 24.20 ?  71  THR   A HG23 1 
ATOM   1576 N  N    . ASN   A 1 72  ? 42.087 2.673   -0.534  1.00 15.47 ?  72  ASN   A N    1 
ATOM   1577 C  CA   . ASN   A 1 72  ? 41.871 1.349   -1.105  1.00 15.69 ?  72  ASN   A CA   1 
ATOM   1578 C  C    . ASN   A 1 72  ? 41.266 1.342   -2.496  1.00 16.05 ?  72  ASN   A C    1 
ATOM   1579 O  O    . ASN   A 1 72  ? 41.281 0.295   -3.146  1.00 16.72 ?  72  ASN   A O    1 
ATOM   1580 C  CB   . ASN   A 1 72  ? 40.984 0.514   -0.174  1.00 15.82 ?  72  ASN   A CB   1 
ATOM   1581 C  CG   . ASN   A 1 72  ? 41.598 0.341   1.188   1.00 17.01 ?  72  ASN   A CG   1 
ATOM   1582 O  OD1  . ASN   A 1 72  ? 41.159 0.940   2.169   1.00 19.69 ?  72  ASN   A OD1  1 
ATOM   1583 N  ND2  . ASN   A 1 72  ? 42.638 -0.458  1.254   1.00 17.96 ?  72  ASN   A ND2  1 
ATOM   1584 H  H    . ASN   A 1 72  ? 41.362 3.083   -0.331  1.00 18.57 ?  72  ASN   A H    1 
ATOM   1585 H  HA   . ASN   A 1 72  ? 42.727 0.898   -1.170  1.00 18.84 ?  72  ASN   A HA   1 
ATOM   1586 H  HB2  . ASN   A 1 72  ? 40.129 0.953   -0.067  1.00 18.99 ?  72  ASN   A HB2  1 
ATOM   1587 H  HB3  . ASN   A 1 72  ? 40.861 -0.371  -0.559  1.00 18.99 ?  72  ASN   A HB3  1 
ATOM   1588 H  HD21 . ASN   A 1 72  ? 43.033 -0.585  2.008   1.00 21.56 ?  72  ASN   A HD21 1 
ATOM   1589 H  HD22 . ASN   A 1 72  ? 42.921 -0.855  0.547   1.00 21.56 ?  72  ASN   A HD22 1 
ATOM   1590 N  N    . GLY   A 1 73  ? 40.705 2.449   -2.956  1.00 15.59 ?  73  GLY   A N    1 
ATOM   1591 C  CA   . GLY   A 1 73  ? 39.972 2.461   -4.196  1.00 15.41 ?  73  GLY   A CA   1 
ATOM   1592 C  C    . GLY   A 1 73  ? 38.582 1.877   -4.035  1.00 13.88 ?  73  GLY   A C    1 
ATOM   1593 O  O    . GLY   A 1 73  ? 38.198 1.399   -2.962  1.00 14.47 ?  73  GLY   A O    1 
ATOM   1594 H  H    . GLY   A 1 73  ? 40.739 3.219   -2.563  1.00 18.72 ?  73  GLY   A H    1 
ATOM   1595 H  HA2  . GLY   A 1 73  ? 39.886 3.376   -4.512  1.00 18.50 ?  73  GLY   A HA2  1 
ATOM   1596 H  HA3  . GLY   A 1 73  ? 40.448 1.946   -4.863  1.00 18.50 ?  73  GLY   A HA3  1 
ATOM   1597 N  N    . PRO   A 1 74  ? 37.802 1.905   -5.112  1.00 14.45 ?  74  PRO   A N    1 
ATOM   1598 C  CA   . PRO   A 1 74  ? 36.402 1.470   -5.026  1.00 14.33 ?  74  PRO   A CA   1 
ATOM   1599 C  C    . PRO   A 1 74  ? 36.253 -0.019  -4.725  1.00 13.97 ?  74  PRO   A C    1 
ATOM   1600 O  O    . PRO   A 1 74  ? 37.132 -0.839  -5.004  1.00 15.14 ?  74  PRO   A O    1 
ATOM   1601 C  CB   . PRO   A 1 74  ? 35.838 1.800   -6.415  1.00 16.21 ?  74  PRO   A CB   1 
ATOM   1602 C  CG   . PRO   A 1 74  ? 36.809 2.766   -7.033  1.00 19.78 ?  74  PRO   A CG   1 
ATOM   1603 C  CD   . PRO   A 1 74  ? 38.145 2.425   -6.446  1.00 16.36 ?  74  PRO   A CD   1 
ATOM   1604 H  HA   . PRO   A 1 74  ? 35.921 1.989   -4.359  1.00 17.21 ?  74  PRO   A HA   1 
ATOM   1605 H  HB2  . PRO   A 1 74  ? 35.778 0.990   -6.947  1.00 19.46 ?  74  PRO   A HB2  1 
ATOM   1606 H  HB3  . PRO   A 1 74  ? 34.960 2.212   -6.328  1.00 19.46 ?  74  PRO   A HB3  1 
ATOM   1607 H  HG2  . PRO   A 1 74  ? 36.823 2.652   -7.997  1.00 23.75 ?  74  PRO   A HG2  1 
ATOM   1608 H  HG3  . PRO   A 1 74  ? 36.560 3.676   -6.803  1.00 23.75 ?  74  PRO   A HG3  1 
ATOM   1609 H  HD2  . PRO   A 1 74  ? 38.585 1.739   -6.973  1.00 19.64 ?  74  PRO   A HD2  1 
ATOM   1610 H  HD3  . PRO   A 1 74  ? 38.695 3.224   -6.378  1.00 19.64 ?  74  PRO   A HD3  1 
ATOM   1611 N  N    . LEU   A 1 75  ? 35.099 -0.351  -4.146  1.00 13.32 ?  75  LEU   A N    1 
ATOM   1612 C  CA   . LEU   A 1 75  ? 34.700 -1.742  -3.987  1.00 12.76 ?  75  LEU   A CA   1 
ATOM   1613 C  C    . LEU   A 1 75  ? 34.312 -2.330  -5.340  1.00 13.49 ?  75  LEU   A C    1 
ATOM   1614 O  O    . LEU   A 1 75  ? 34.188 -1.621  -6.340  1.00 14.73 ?  75  LEU   A O    1 
ATOM   1615 C  CB   . LEU   A 1 75  ? 33.511 -1.855  -3.033  1.00 12.96 ?  75  LEU   A CB   1 
ATOM   1616 C  CG   . LEU   A 1 75  ? 33.727 -1.446  -1.578  1.00 14.60 ?  75  LEU   A CG   1 
ATOM   1617 C  CD1  . LEU   A 1 75  ? 32.441 -1.616  -0.769  1.00 16.54 ?  75  LEU   A CD1  1 
ATOM   1618 C  CD2  . LEU   A 1 75  ? 34.870 -2.180  -0.936  1.00 18.68 ?  75  LEU   A CD2  1 
ATOM   1619 H  H    . LEU   A 1 75  ? 34.523 0.218   -3.846  1.00 15.99 ?  75  LEU   A H    1 
ATOM   1620 H  HA   . LEU   A 1 75  ? 35.441 -2.247  -3.636  1.00 15.31 ?  75  LEU   A HA   1 
ATOM   1621 H  HB2  . LEU   A 1 75  ? 32.791 -1.306  -3.383  1.00 15.56 ?  75  LEU   A HB2  1 
ATOM   1622 H  HB3  . LEU   A 1 75  ? 33.225 -2.784  -3.030  1.00 15.56 ?  75  LEU   A HB3  1 
ATOM   1623 H  HG   . LEU   A 1 75  ? 33.957 -0.503  -1.568  1.00 17.53 ?  75  LEU   A HG   1 
ATOM   1624 H  HD11 . LEU   A 1 75  ? 32.610 -1.341  0.147   1.00 19.86 ?  75  LEU   A HD11 1 
ATOM   1625 H  HD12 . LEU   A 1 75  ? 31.751 -1.052  -1.157  1.00 19.86 ?  75  LEU   A HD12 1 
ATOM   1626 H  HD13 . LEU   A 1 75  ? 32.169 -2.542  -0.796  1.00 19.86 ?  75  LEU   A HD13 1 
ATOM   1627 H  HD21 . LEU   A 1 75  ? 34.915 -1.935  -0.000  1.00 22.42 ?  75  LEU   A HD21 1 
ATOM   1628 H  HD22 . LEU   A 1 75  ? 34.723 -3.134  -1.025  1.00 22.42 ?  75  LEU   A HD22 1 
ATOM   1629 H  HD23 . LEU   A 1 75  ? 35.699 -1.933  -1.382  1.00 22.42 ?  75  LEU   A HD23 1 
ATOM   1630 N  N    . LYS   A 1 76  ? 34.115 -3.647  -5.356  1.00 13.20 ?  76  LYS   A N    1 
ATOM   1631 C  CA   . LYS   A 1 76  ? 33.513 -4.352  -6.481  1.00 13.71 ?  76  LYS   A CA   1 
ATOM   1632 C  C    . LYS   A 1 76  ? 32.003 -4.446  -6.280  1.00 13.37 ?  76  LYS   A C    1 
ATOM   1633 O  O    . LYS   A 1 76  ? 31.528 -4.590  -5.155  1.00 13.28 ?  76  LYS   A O    1 
ATOM   1634 C  CB   . LYS   A 1 76  ? 34.055 -5.789  -6.563  1.00 16.23 ?  76  LYS   A CB   1 
ATOM   1635 C  CG   . LYS   A 1 76  ? 35.565 -5.897  -6.685  1.00 18.12 ?  76  LYS   A CG   1 
ATOM   1636 C  CD   . LYS   A 1 76  ? 36.060 -7.336  -6.578  1.00 19.35 ?  76  LYS   A CD   1 
ATOM   1637 C  CE   . LYS   A 1 76  ? 37.569 -7.393  -6.747  1.00 22.05 ?  76  LYS   A CE   1 
ATOM   1638 N  NZ   . LYS   A 1 76  ? 38.118 -8.753  -6.584  1.00 22.76 ?  76  LYS   A NZ   1 
ATOM   1639 H  H    . LYS   A 1 76  ? 34.342 -4.168  -4.707  1.00 15.85 ?  76  LYS   A H    1 
ATOM   1640 H  HA   . LYS   A 1 76  ? 33.701 -3.883  -7.312  1.00 16.47 ?  76  LYS   A HA   1 
ATOM   1641 H  HB2  . LYS   A 1 76  ? 33.785 -6.261  -5.762  1.00 19.48 ?  76  LYS   A HB2  1 
ATOM   1642 H  HB3  . LYS   A 1 76  ? 33.663 -6.215  -7.342  1.00 19.48 ?  76  LYS   A HB3  1 
ATOM   1643 H  HG2  . LYS   A 1 76  ? 35.841 -5.547  -7.546  1.00 21.76 ?  76  LYS   A HG2  1 
ATOM   1644 H  HG3  . LYS   A 1 76  ? 35.979 -5.385  -5.971  1.00 21.76 ?  76  LYS   A HG3  1 
ATOM   1645 H  HD2  . LYS   A 1 76  ? 35.830 -7.695  -5.704  1.00 23.23 ?  76  LYS   A HD2  1 
ATOM   1646 H  HD3  . LYS   A 1 76  ? 35.649 -7.873  -7.279  1.00 23.23 ?  76  LYS   A HD3  1 
ATOM   1647 H  HE2  . LYS   A 1 76  ? 37.796 -7.078  -7.635  1.00 26.47 ?  76  LYS   A HE2  1 
ATOM   1648 H  HE3  . LYS   A 1 76  ? 37.978 -6.821  -6.078  1.00 26.47 ?  76  LYS   A HE3  1 
ATOM   1649 H  HZ1  . LYS   A 1 76  ? 39.001 -8.743  -6.691  1.00 27.32 ?  76  LYS   A HZ1  1 
ATOM   1650 H  HZ2  . LYS   A 1 76  ? 37.928 -9.067  -5.773  1.00 27.32 ?  76  LYS   A HZ2  1 
ATOM   1651 H  HZ3  . LYS   A 1 76  ? 37.762 -9.302  -7.193  1.00 27.32 ?  76  LYS   A HZ3  1 
ATOM   1652 N  N    . VAL   A 1 77  ? 31.248 -4.404  -7.382  1.00 13.74 ?  77  VAL   A N    1 
ATOM   1653 C  CA   . VAL   A 1 77  ? 29.839 -4.795  -7.298  1.00 13.17 ?  77  VAL   A CA   1 
ATOM   1654 C  C    . VAL   A 1 77  ? 29.771 -6.251  -6.862  1.00 12.63 ?  77  VAL   A C    1 
ATOM   1655 O  O    . VAL   A 1 77  ? 30.428 -7.117  -7.446  1.00 13.64 ?  77  VAL   A O    1 
ATOM   1656 C  CB   . VAL   A 1 77  ? 29.114 -4.568  -8.634  1.00 14.50 ?  77  VAL   A CB   1 
ATOM   1657 C  CG1  . VAL   A 1 77  ? 27.651 -5.009  -8.525  1.00 15.32 ?  77  VAL   A CG1  1 
ATOM   1658 C  CG2  . VAL   A 1 77  ? 29.201 -3.105  -9.056  1.00 15.83 ?  77  VAL   A CG2  1 
ATOM   1659 H  H    . VAL   A 1 77  ? 31.517 -4.150  -8.161  1.00 16.49 ?  77  VAL   A H    1 
ATOM   1660 H  HA   . VAL   A 1 77  ? 29.400 -4.254  -6.623  1.00 15.81 ?  77  VAL   A HA   1 
ATOM   1661 H  HB   . VAL   A 1 77  ? 29.540 -5.105  -9.320  1.00 17.40 ?  77  VAL   A HB   1 
ATOM   1662 H  HG11 . VAL   A 1 77  ? 27.173 -4.704  -9.310  1.00 18.39 ?  77  VAL   A HG11 1 
ATOM   1663 H  HG12 . VAL   A 1 77  ? 27.616 -5.978  -8.473  1.00 18.39 ?  77  VAL   A HG12 1 
ATOM   1664 H  HG13 . VAL   A 1 77  ? 27.264 -4.618  -7.727  1.00 18.39 ?  77  VAL   A HG13 1 
ATOM   1665 H  HG21 . VAL   A 1 77  ? 28.689 -2.982  -9.871  1.00 19.01 ?  77  VAL   A HG21 1 
ATOM   1666 H  HG22 . VAL   A 1 77  ? 28.837 -2.551  -8.349  1.00 19.01 ?  77  VAL   A HG22 1 
ATOM   1667 H  HG23 . VAL   A 1 77  ? 30.130 -2.876  -9.213  1.00 19.01 ?  77  VAL   A HG23 1 
ATOM   1668 N  N    . GLY   A 1 78  ? 29.004 -6.516  -5.809  1.00 12.58 ?  78  GLY   A N    1 
ATOM   1669 C  CA   . GLY   A 1 78  ? 28.980 -7.812  -5.168  1.00 13.17 ?  78  GLY   A CA   1 
ATOM   1670 C  C    . GLY   A 1 78  ? 29.895 -7.913  -3.970  1.00 12.56 ?  78  GLY   A C    1 
ATOM   1671 O  O    . GLY   A 1 78  ? 29.824 -8.911  -3.236  1.00 13.27 ?  78  GLY   A O    1 
ATOM   1672 H  H    . GLY   A 1 78  ? 28.469 -5.944  -5.451  1.00 15.10 ?  78  GLY   A H    1 
ATOM   1673 H  HA2  . GLY   A 1 78  ? 28.075 -8.009  -4.880  1.00 15.81 ?  78  GLY   A HA2  1 
ATOM   1674 H  HA3  . GLY   A 1 78  ? 29.244 -8.492  -5.813  1.00 15.81 ?  78  GLY   A HA3  1 
ATOM   1675 N  N    . GLY   A 1 79  ? 30.738 -6.898  -3.744  1.00 12.85 ?  79  GLY   A N    1 
ATOM   1676 C  CA   . GLY   A 1 79  ? 31.713 -6.918  -2.677  1.00 13.19 ?  79  GLY   A CA   1 
ATOM   1677 C  C    . GLY   A 1 79  ? 31.269 -6.127  -1.453  1.00 12.39 ?  79  GLY   A C    1 
ATOM   1678 O  O    . GLY   A 1 79  ? 30.148 -5.632  -1.357  1.00 12.40 ?  79  GLY   A O    1 
ATOM   1679 H  H    . GLY   A 1 79  ? 30.758 -6.176  -4.212  1.00 15.42 ?  79  GLY   A H    1 
ATOM   1680 H  HA2  . GLY   A 1 79  ? 31.869 -7.844  -2.409  1.00 15.84 ?  79  GLY   A HA2  1 
ATOM   1681 H  HA3  . GLY   A 1 79  ? 32.550 -6.556  -3.003  1.00 15.84 ?  79  GLY   A HA3  1 
ATOM   1682 N  N    . SER   A 1 80  ? 32.180 -6.043  -0.485  1.00 12.41 ?  80  SER   A N    1 
ATOM   1683 C  CA   . SER   A 1 80  ? 31.862 -5.417  0.788   1.00 11.64 ?  80  SER   A CA   1 
ATOM   1684 C  C    . SER   A 1 80  ? 33.138 -4.977  1.485   1.00 12.22 ?  80  SER   A C    1 
ATOM   1685 O  O    . SER   A 1 80  ? 34.244 -5.422  1.155   1.00 13.55 ?  80  SER   A O    1 
ATOM   1686 C  CB   . SER   A 1 80  ? 31.090 -6.373  1.706   1.00 12.57 ?  80  SER   A CB   1 
ATOM   1687 O  OG   . SER   A 1 80  ? 31.919 -7.424  2.180   1.00 14.97 ?  80  SER   A OG   1 
ATOM   1688 H  H    . SER   A 1 80  ? 32.992 -6.340  -0.543  1.00 14.90 ?  80  SER   A H    1 
ATOM   1689 H  HA   . SER   A 1 80  ? 31.316 -4.634  0.616   1.00 13.98 ?  80  SER   A HA   1 
ATOM   1690 H  HB2  . SER   A 1 80  ? 30.751 -5.874  2.461   1.00 15.10 ?  80  SER   A HB2  1 
ATOM   1691 H  HB3  . SER   A 1 80  ? 30.354 -6.759  1.204   1.00 15.10 ?  80  SER   A HB3  1 
ATOM   1692 H  HG   . SER   A 1 80  ? 32.228 -7.859  1.528   1.00 17.97 ?  80  SER   A HG   1 
ATOM   1693 N  N    . CYS   A 1 81  ? 32.953 -4.133  2.495   1.00 12.03 ?  81  CYS   A N    1 
ATOM   1694 C  CA   . CYS   A 1 81  ? 34.001 -3.842  3.460   1.00 12.49 ?  81  CYS   A CA   1 
ATOM   1695 C  C    . CYS   A 1 81  ? 33.361 -3.591  4.819   1.00 12.10 ?  81  CYS   A C    1 
ATOM   1696 O  O    . CYS   A 1 81  ? 32.198 -3.178  4.910   1.00 13.00 ?  81  CYS   A O    1 
ATOM   1697 C  CB   . CYS   A 1 81  ? 34.870 -2.654  3.036   1.00 12.86 ?  81  CYS   A CB   1 
ATOM   1698 S  SG   . CYS   A 1 81  ? 33.995 -1.057  3.075   1.00 13.30 ?  81  CYS   A SG   1 
ATOM   1699 H  H    . CYS   A 1 81  ? 32.218 -3.709  2.646   1.00 14.45 ?  81  CYS   A H    1 
ATOM   1700 H  HA   . CYS   A 1 81  ? 34.576 -4.622  3.542   1.00 15.00 ?  81  CYS   A HA   1 
ATOM   1701 H  HB2  . CYS   A 1 81  ? 35.635 -2.597  3.637   1.00 15.44 ?  81  CYS   A HB2  1 
ATOM   1702 H  HB3  . CYS   A 1 81  ? 35.187 -2.807  2.128   1.00 15.44 ?  81  CYS   A HB3  1 
ATOM   1703 H  HG   . CYS   A 1 81  ? 34.750 -0.190  2.729   1.00 15.97 ?  81  CYS   A HG   1 
ATOM   1704 N  N    . VAL   A 1 82  ? 34.134 -3.858  5.875   1.00 12.08 ?  82  VAL   A N    1 
ATOM   1705 C  CA   . VAL   A 1 82  ? 33.707 -3.609  7.248   1.00 12.50 ?  82  VAL   A CA   1 
ATOM   1706 C  C    . VAL   A 1 82  ? 34.313 -2.301  7.726   1.00 13.32 ?  82  VAL   A C    1 
ATOM   1707 O  O    . VAL   A 1 82  ? 35.541 -2.137  7.713   1.00 13.91 ?  82  VAL   A O    1 
ATOM   1708 C  CB   . VAL   A 1 82  ? 34.122 -4.750  8.189   1.00 14.12 ?  82  VAL   A CB   1 
ATOM   1709 C  CG1  . VAL   A 1 82  ? 33.655 -4.466  9.605   1.00 15.56 ?  82  VAL   A CG1  1 
ATOM   1710 C  CG2  . VAL   A 1 82  ? 33.571 -6.058  7.698   1.00 15.23 ?  82  VAL   A CG2  1 
ATOM   1711 H  H    . VAL   A 1 82  ? 34.921 -4.209  5.817   1.00 14.51 ?  82  VAL   A H    1 
ATOM   1712 H  HA   . VAL   A 1 82  ? 32.738 -3.526  7.270   1.00 15.00 ?  82  VAL   A HA   1 
ATOM   1713 H  HB   . VAL   A 1 82  ? 35.088 -4.811  8.199   1.00 16.96 ?  82  VAL   A HB   1 
ATOM   1714 H  HG11 . VAL   A 1 82  ? 33.747 -5.272  10.135  1.00 18.68 ?  82  VAL   A HG11 1 
ATOM   1715 H  HG12 . VAL   A 1 82  ? 34.195 -3.756  9.987   1.00 18.68 ?  82  VAL   A HG12 1 
ATOM   1716 H  HG13 . VAL   A 1 82  ? 32.721 -4.193  9.584   1.00 18.68 ?  82  VAL   A HG13 1 
ATOM   1717 H  HG21 . VAL   A 1 82  ? 33.785 -6.752  8.340   1.00 18.28 ?  82  VAL   A HG21 1 
ATOM   1718 H  HG22 . VAL   A 1 82  ? 32.607 -5.982  7.605   1.00 18.28 ?  82  VAL   A HG22 1 
ATOM   1719 H  HG23 . VAL   A 1 82  ? 33.968 -6.268  6.838   1.00 18.28 ?  82  VAL   A HG23 1 
ATOM   1720 N  N    . LEU   A 1 83  ? 33.462 -1.383  8.166   1.00 12.75 ?  83  LEU   A N    1 
ATOM   1721 C  CA   . LEU   A 1 83  ? 33.889 -0.121  8.748   1.00 12.34 ?  83  LEU   A CA   1 
ATOM   1722 C  C    . LEU   A 1 83  ? 33.161 0.064   10.079  1.00 12.54 ?  83  LEU   A C    1 
ATOM   1723 O  O    . LEU   A 1 83  ? 32.443 -0.827  10.549  1.00 13.17 ?  83  LEU   A O    1 
ATOM   1724 C  CB   . LEU   A 1 83  ? 33.662 1.038   7.765   1.00 13.24 ?  83  LEU   A CB   1 
ATOM   1725 C  CG   . LEU   A 1 83  ? 34.524 1.035   6.499   1.00 13.47 ?  83  LEU   A CG   1 
ATOM   1726 C  CD1  . LEU   A 1 83  ? 34.091 2.093   5.508   1.00 14.51 ?  83  LEU   A CD1  1 
ATOM   1727 C  CD2  . LEU   A 1 83  ? 36.000 1.240   6.860   1.00 14.90 ?  83  LEU   A CD2  1 
ATOM   1728 H  H    . LEU   A 1 83  ? 32.604 -1.475  8.143   1.00 15.31 ?  83  LEU   A H    1 
ATOM   1729 H  HA   . LEU   A 1 83  ? 34.834 -0.167  8.943   1.00 14.81 ?  83  LEU   A HA   1 
ATOM   1730 H  HB2  . LEU   A 1 83  ? 32.736 1.020   7.481   1.00 15.90 ?  83  LEU   A HB2  1 
ATOM   1731 H  HB3  . LEU   A 1 83  ? 33.838 1.869   8.231   1.00 15.90 ?  83  LEU   A HB3  1 
ATOM   1732 H  HG   . LEU   A 1 83  ? 34.445 0.170   6.068   1.00 16.17 ?  83  LEU   A HG   1 
ATOM   1733 H  HD11 . LEU   A 1 83  ? 34.667 2.045   4.724   1.00 17.42 ?  83  LEU   A HD11 1 
ATOM   1734 H  HD12 . LEU   A 1 83  ? 33.172 1.925   5.250   1.00 17.42 ?  83  LEU   A HD12 1 
ATOM   1735 H  HD13 . LEU   A 1 83  ? 34.168 2.966   5.920   1.00 17.42 ?  83  LEU   A HD13 1 
ATOM   1736 H  HD21 . LEU   A 1 83  ? 36.516 1.341   6.041   1.00 17.89 ?  83  LEU   A HD21 1 
ATOM   1737 H  HD22 . LEU   A 1 83  ? 36.088 2.037   7.404   1.00 17.89 ?  83  LEU   A HD22 1 
ATOM   1738 H  HD23 . LEU   A 1 83  ? 36.320 0.466   7.352   1.00 17.89 ?  83  LEU   A HD23 1 
ATOM   1739 N  N    . SER   A 1 84  ? 33.377 1.212   10.715  1.00 13.21 ?  84  SER   A N    1 
ATOM   1740 C  CA   . SER   A 1 84  ? 32.727 1.471   11.992  1.00 12.90 ?  84  SER   A CA   1 
ATOM   1741 C  C    . SER   A 1 84  ? 31.209 1.557   11.848  1.00 12.97 ?  84  SER   A C    1 
ATOM   1742 O  O    . SER   A 1 84  ? 30.682 2.028   10.840  1.00 13.40 ?  84  SER   A O    1 
ATOM   1743 C  CB   . SER   A 1 84  ? 33.226 2.796   12.567  1.00 14.41 ?  84  SER   A CB   1 
ATOM   1744 O  OG   . SER   A 1 84  ? 32.587 3.081   13.799  1.00 15.13 ?  84  SER   A OG   1 
ATOM   1745 H  H    . SER   A 1 84  ? 33.882 1.851   10.430  1.00 15.86 ?  84  SER   A H    1 
ATOM   1746 H  HA   . SER   A 1 84  ? 32.944 0.761   12.613  1.00 15.49 ?  84  SER   A HA   1 
ATOM   1747 H  HB2  . SER   A 1 84  ? 34.182 2.737   12.712  1.00 17.30 ?  84  SER   A HB2  1 
ATOM   1748 H  HB3  . SER   A 1 84  ? 33.030 3.507   11.936  1.00 17.30 ?  84  SER   A HB3  1 
ATOM   1749 H  HG   . SER   A 1 84  ? 32.870 3.816   14.105  1.00 18.16 ?  84  SER   A HG   1 
ATOM   1750 N  N    . GLY   A 1 85  ? 30.506 1.136   12.898  1.00 13.60 ?  85  GLY   A N    1 
ATOM   1751 C  CA   . GLY   A 1 85  ? 29.080 1.368   12.996  1.00 14.58 ?  85  GLY   A CA   1 
ATOM   1752 C  C    . GLY   A 1 85  ? 28.701 2.687   13.631  1.00 14.07 ?  85  GLY   A C    1 
ATOM   1753 O  O    . GLY   A 1 85  ? 27.512 2.991   13.745  1.00 14.96 ?  85  GLY   A O    1 
ATOM   1754 H  H    . GLY   A 1 85  ? 30.842 0.720   13.573  1.00 16.33 ?  85  GLY   A H    1 
ATOM   1755 H  HA2  . GLY   A 1 85  ? 28.698 1.340   12.104  1.00 17.51 ?  85  GLY   A HA2  1 
ATOM   1756 H  HA3  . GLY   A 1 85  ? 28.681 0.652   13.513  1.00 17.51 ?  85  GLY   A HA3  1 
ATOM   1757 N  N    . HIS   A 1 86  ? 29.682 3.468   14.073  1.00 13.41 ?  86  HIS   A N    1 
ATOM   1758 C  CA   . HIS   A 1 86  ? 29.465 4.809   14.639  1.00 14.90 ?  86  HIS   A CA   1 
ATOM   1759 C  C    . HIS   A 1 86  ? 28.487 4.690   15.803  1.00 16.02 ?  86  HIS   A C    1 
ATOM   1760 O  O    . HIS   A 1 86  ? 28.681 3.811   16.658  1.00 17.23 ?  86  HIS   A O    1 
ATOM   1761 C  CB   . HIS   A 1 86  ? 29.086 5.783   13.528  1.00 14.63 ?  86  HIS   A CB   1 
ATOM   1762 C  CG   . HIS   A 1 86  ? 30.147 5.894   12.493  1.00 14.14 ?  86  HIS   A CG   1 
ATOM   1763 N  ND1  . HIS   A 1 86  ? 31.240 6.724   12.638  1.00 15.59 ?  86  HIS   A ND1  1 
ATOM   1764 C  CD2  . HIS   A 1 86  ? 30.335 5.210   11.343  1.00 14.28 ?  86  HIS   A CD2  1 
ATOM   1765 C  CE1  . HIS   A 1 86  ? 32.036 6.571   11.595  1.00 15.76 ?  86  HIS   A CE1  1 
ATOM   1766 N  NE2  . HIS   A 1 86  ? 31.513 5.657   10.798  1.00 15.40 ?  86  HIS   A NE2  1 
ATOM   1767 H  H    . HIS   A 1 86  ? 30.507 3.235   14.070  1.00 16.10 ?  86  HIS   A H    1 
ATOM   1768 H  HA   . HIS   A 1 86  ? 30.305 5.118   15.006  1.00 17.88 ?  86  HIS   A HA   1 
ATOM   1769 H  HB2  . HIS   A 1 86  ? 28.269 5.485   13.098  1.00 17.56 ?  86  HIS   A HB2  1 
ATOM   1770 H  HB3  . HIS   A 1 86  ? 28.949 6.670   13.912  1.00 17.56 ?  86  HIS   A HB3  1 
ATOM   1771 H  HD2  . HIS   A 1 86  ? 29.771 4.558   10.985  1.00 17.15 ?  86  HIS   A HD2  1 
ATOM   1772 H  HE1  . HIS   A 1 86  ? 32.827 7.032   11.438  1.00 18.92 ?  86  HIS   A HE1  1 
ATOM   1773 H  HE2  . HIS   A 1 86  ? 31.853 5.385   10.053  1.00 18.49 ?  86  HIS   A HE2  1 
ATOM   1774 N  N    . ASN   A 1 87  ? 27.467 5.537   15.877  1.00 16.90 ?  87  ASN   A N    1 
ATOM   1775 C  CA   . ASN   A 1 87  ? 26.479 5.523   16.940  1.00 17.63 ?  87  ASN   A CA   1 
ATOM   1776 C  C    . ASN   A 1 87  ? 25.354 4.523   16.695  1.00 18.90 ?  87  ASN   A C    1 
ATOM   1777 O  O    . ASN   A 1 87  ? 24.426 4.461   17.506  1.00 22.20 ?  87  ASN   A O    1 
ATOM   1778 C  CB   . ASN   A 1 87  ? 25.892 6.932   17.100  1.00 18.98 ?  87  ASN   A CB   1 
ATOM   1779 C  CG   . ASN   A 1 87  ? 25.354 7.498   15.789  1.00 19.20 ?  87  ASN   A CG   1 
ATOM   1780 O  OD1  . ASN   A 1 87  ? 25.978 7.383   14.739  1.00 20.34 ?  87  ASN   A OD1  1 
ATOM   1781 N  ND2  . ASN   A 1 87  ? 24.198 8.130   15.855  1.00 20.40 ?  87  ASN   A ND2  1 
ATOM   1782 H  H    . ASN   A 1 87  ? 27.324 6.154   15.296  1.00 20.29 ?  87  ASN   A H    1 
ATOM   1783 H  HA   . ASN   A 1 87  ? 26.912 5.281   17.776  1.00 21.16 ?  87  ASN   A HA   1 
ATOM   1784 H  HB2  . ASN   A 1 87  ? 25.161 6.897   17.742  1.00 22.78 ?  87  ASN   A HB2  1 
ATOM   1785 H  HB3  . ASN   A 1 87  ? 26.586 7.526   17.425  1.00 22.78 ?  87  ASN   A HB3  1 
ATOM   1786 H  HD21 . ASN   A 1 87  ? 23.853 8.460   15.143  1.00 24.49 ?  87  ASN   A HD21 1 
ATOM   1787 H  HD22 . ASN   A 1 87  ? 23.785 8.198   16.608  1.00 24.49 ?  87  ASN   A HD22 1 
ATOM   1788 N  N    . LEU   A 1 88  ? 25.416 3.733   15.623  1.00 17.59 ?  88  LEU   A N    1 
ATOM   1789 C  CA   . LEU   A 1 88  ? 24.310 2.862   15.231  1.00 17.87 ?  88  LEU   A CA   1 
ATOM   1790 C  C    . LEU   A 1 88  ? 24.533 1.389   15.528  1.00 17.36 ?  88  LEU   A C    1 
ATOM   1791 O  O    . LEU   A 1 88  ? 23.560 0.658   15.712  1.00 18.81 ?  88  LEU   A O    1 
ATOM   1792 C  CB   . LEU   A 1 88  ? 24.048 3.006   13.728  1.00 18.51 ?  88  LEU   A CB   1 
ATOM   1793 C  CG   . LEU   A 1 88  ? 23.777 4.423   13.226  1.00 20.33 ?  88  LEU   A CG   1 
ATOM   1794 C  CD1  . LEU   A 1 88  ? 23.618 4.426   11.715  1.00 20.77 ?  88  LEU   A CD1  1 
ATOM   1795 C  CD2  . LEU   A 1 88  ? 22.547 5.019   13.900  1.00 22.07 ?  88  LEU   A CD2  1 
ATOM   1796 H  H    . LEU   A 1 88  ? 26.099 3.684   15.105  1.00 21.11 ?  88  LEU   A H    1 
ATOM   1797 H  HA   . LEU   A 1 88  ? 23.510 3.147   15.700  1.00 21.46 ?  88  LEU   A HA   1 
ATOM   1798 H  HB2  . LEU   A 1 88  ? 24.822 2.676   13.249  1.00 22.22 ?  88  LEU   A HB2  1 
ATOM   1799 H  HB3  . LEU   A 1 88  ? 23.273 2.469   13.503  1.00 22.22 ?  88  LEU   A HB3  1 
ATOM   1800 H  HG   . LEU   A 1 88  ? 24.535 4.985   13.443  1.00 24.41 ?  88  LEU   A HG   1 
ATOM   1801 H  HD11 . LEU   A 1 88  ? 23.449 5.335   11.415  1.00 24.94 ?  88  LEU   A HD11 1 
ATOM   1802 H  HD12 . LEU   A 1 88  ? 24.435 4.093   11.310  1.00 24.94 ?  88  LEU   A HD12 1 
ATOM   1803 H  HD13 . LEU   A 1 88  ? 22.872 3.855   11.473  1.00 24.94 ?  88  LEU   A HD13 1 
ATOM   1804 H  HD21 . LEU   A 1 88  ? 22.346 5.875   13.490  1.00 26.49 ?  88  LEU   A HD21 1 
ATOM   1805 H  HD22 . LEU   A 1 88  ? 21.800 4.412   13.785  1.00 26.49 ?  88  LEU   A HD22 1 
ATOM   1806 H  HD23 . LEU   A 1 88  ? 22.734 5.140   14.844  1.00 26.49 ?  88  LEU   A HD23 1 
ATOM   1807 N  N    . ALA   A 1 89  ? 25.781 0.942   15.562  1.00 15.66 ?  89  ALA   A N    1 
ATOM   1808 C  CA   . ALA   A 1 89  ? 26.127 -0.470  15.664  1.00 15.72 ?  89  ALA   A CA   1 
ATOM   1809 C  C    . ALA   A 1 89  ? 27.611 -0.529  15.986  1.00 16.20 ?  89  ALA   A C    1 
ATOM   1810 O  O    . ALA   A 1 89  ? 28.320 0.472   15.873  1.00 17.36 ?  89  ALA   A O    1 
ATOM   1811 C  CB   . ALA   A 1 89  ? 25.867 -1.195  14.341  1.00 15.87 ?  89  ALA   A CB   1 
ATOM   1812 H  H    . ALA   A 1 89  ? 26.466 1.460   15.522  1.00 18.80 ?  89  ALA   A H    1 
ATOM   1813 H  HA   . ALA   A 1 89  ? 25.617 -0.890  16.377  1.00 18.88 ?  89  ALA   A HA   1 
ATOM   1814 H  HB1  . ALA   A 1 89  ? 26.124 -2.125  14.439  1.00 19.05 ?  89  ALA   A HB1  1 
ATOM   1815 H  HB2  . ALA   A 1 89  ? 24.923 -1.134  14.125  1.00 19.05 ?  89  ALA   A HB2  1 
ATOM   1816 H  HB3  . ALA   A 1 89  ? 26.394 -0.776  13.644  1.00 19.05 ?  89  ALA   A HB3  1 
ATOM   1817 N  N    . LYS   A 1 90  ? 28.096 -1.712  16.366  1.00 16.59 ?  90  LYS   A N    1 
ATOM   1818 C  CA   . LYS   A 1 90  ? 29.540 -1.861  16.507  1.00 17.53 ?  90  LYS   A CA   1 
ATOM   1819 C  C    . LYS   A 1 90  ? 30.232 -1.670  15.162  1.00 16.22 ?  90  LYS   A C    1 
ATOM   1820 O  O    . LYS   A 1 90  ? 31.167 -0.864  15.034  1.00 18.28 ?  90  LYS   A O    1 
ATOM   1821 C  CB   . LYS   A 1 90  ? 29.885 -3.226  17.103  1.00 20.15 ?  90  LYS   A CB   1 
ATOM   1822 C  CG   . LYS   A 1 90  ? 31.370 -3.389  17.410  1.00 24.88 ?  90  LYS   A CG   1 
ATOM   1823 C  CD   . LYS   A 1 90  ? 31.617 -4.616  18.270  1.00 29.84 ?  90  LYS   A CD   1 
ATOM   1824 C  CE   . LYS   A 1 90  ? 33.019 -4.629  18.857  1.00 33.32 ?  90  LYS   A CE   1 
ATOM   1825 N  NZ   . LYS   A 1 90  ? 34.057 -4.988  17.855  1.00 35.60 ?  90  LYS   A NZ   1 
ATOM   1826 H  H    . LYS   A 1 90  ? 27.630 -2.409  16.538  1.00 19.91 ?  90  LYS   A H    1 
ATOM   1827 H  HA   . LYS   A 1 90  ? 29.869 -1.176  17.108  1.00 21.04 ?  90  LYS   A HA   1 
ATOM   1828 H  HB2  . LYS   A 1 90  ? 29.390 -3.334  17.930  1.00 24.19 ?  90  LYS   A HB2  1 
ATOM   1829 H  HB3  . LYS   A 1 90  ? 29.629 -3.915  16.471  1.00 24.19 ?  90  LYS   A HB3  1 
ATOM   1830 H  HG2  . LYS   A 1 90  ? 31.861 -3.489  16.580  1.00 29.86 ?  90  LYS   A HG2  1 
ATOM   1831 H  HG3  . LYS   A 1 90  ? 31.684 -2.607  17.893  1.00 29.86 ?  90  LYS   A HG3  1 
ATOM   1832 H  HD2  . LYS   A 1 90  ? 30.981 -4.625  19.004  1.00 35.81 ?  90  LYS   A HD2  1 
ATOM   1833 H  HD3  . LYS   A 1 90  ? 31.508 -5.413  17.726  1.00 35.81 ?  90  LYS   A HD3  1 
ATOM   1834 H  HE2  . LYS   A 1 90  ? 33.226 -3.746  19.201  1.00 40.00 ?  90  LYS   A HE2  1 
ATOM   1835 H  HE3  . LYS   A 1 90  ? 33.056 -5.281  19.574  1.00 40.00 ?  90  LYS   A HE3  1 
ATOM   1836 H  HZ1  . LYS   A 1 90  ? 34.861 -4.994  18.240  1.00 42.73 ?  90  LYS   A HZ1  1 
ATOM   1837 H  HZ2  . LYS   A 1 90  ? 33.891 -5.796  17.521  1.00 42.73 ?  90  LYS   A HZ2  1 
ATOM   1838 H  HZ3  . LYS   A 1 90  ? 34.059 -4.394  17.193  1.00 42.73 ?  90  LYS   A HZ3  1 
ATOM   1839 N  N    . HIS   A 1 91  ? 29.760 -2.379  14.138  1.00 14.34 ?  91  HIS   A N    1 
ATOM   1840 C  CA   . HIS   A 1 91  ? 30.341 -2.357  12.808  1.00 13.74 ?  91  HIS   A CA   1 
ATOM   1841 C  C    . HIS   A 1 91  ? 29.255 -2.082  11.787  1.00 12.38 ?  91  HIS   A C    1 
ATOM   1842 O  O    . HIS   A 1 91  ? 28.090 -2.447  11.983  1.00 13.79 ?  91  HIS   A O    1 
ATOM   1843 C  CB   . HIS   A 1 91  ? 30.941 -3.725  12.442  1.00 16.52 ?  91  HIS   A CB   1 
ATOM   1844 C  CG   . HIS   A 1 91  ? 31.923 -4.251  13.438  1.00 21.93 ?  91  HIS   A CG   1 
ATOM   1845 N  ND1  . HIS   A 1 91  ? 33.210 -3.770  13.542  1.00 24.51 ?  91  HIS   A ND1  1 
ATOM   1846 C  CD2  . HIS   A 1 91  ? 31.812 -5.233  14.363  1.00 24.16 ?  91  HIS   A CD2  1 
ATOM   1847 C  CE1  . HIS   A 1 91  ? 33.849 -4.429  14.493  1.00 25.02 ?  91  HIS   A CE1  1 
ATOM   1848 N  NE2  . HIS   A 1 91  ? 33.021 -5.322  15.008  1.00 25.50 ?  91  HIS   A NE2  1 
ATOM   1849 H  H    . HIS   A 1 91  ? 29.074 -2.902  14.195  1.00 17.21 ?  91  HIS   A H    1 
ATOM   1850 H  HA   . HIS   A 1 91  ? 31.031 -1.678  12.746  1.00 16.49 ?  91  HIS   A HA   1 
ATOM   1851 H  HB2  . HIS   A 1 91  ? 30.223 -4.373  12.369  1.00 19.83 ?  91  HIS   A HB2  1 
ATOM   1852 H  HB3  . HIS   A 1 91  ? 31.399 -3.649  11.589  1.00 19.83 ?  91  HIS   A HB3  1 
ATOM   1853 H  HD1  . HIS   A 1 91  ? 33.548 -3.140  13.060  1.00 29.42 ?  91  HIS   A HD1  1 
ATOM   1854 H  HD2  . HIS   A 1 91  ? 31.061 -5.748  14.534  1.00 29.00 ?  91  HIS   A HD2  1 
ATOM   1855 H  HE1  . HIS   A 1 91  ? 34.733 -4.284  14.755  1.00 30.03 ?  91  HIS   A HE1  1 
ATOM   1856 N  N    . CYS   A 1 92  ? 29.649 -1.489  10.664  1.00 12.15 ?  92  CYS   A N    1 
ATOM   1857 C  CA   . CYS   A 1 92  ? 28.796 -1.426  9.484   1.00 11.89 ?  92  CYS   A CA   1 
ATOM   1858 C  C    . CYS   A 1 92  ? 29.450 -2.236  8.376   1.00 12.05 ?  92  CYS   A C    1 
ATOM   1859 O  O    . CYS   A 1 92  ? 30.613 -1.988  8.018   1.00 12.96 ?  92  CYS   A O    1 
ATOM   1860 C  CB   . CYS   A 1 92  ? 28.570 0.017   9.029   1.00 13.28 ?  92  CYS   A CB   1 
ATOM   1861 S  SG   . CYS   A 1 92  ? 27.587 0.143   7.519   1.00 12.27 ?  92  CYS   A SG   1 
ATOM   1862 H  H    . CYS   A 1 92  ? 30.418 -1.104  10.555  1.00 14.59 ?  92  CYS   A H    1 
ATOM   1863 H  HA   . CYS   A 1 92  ? 27.932 -1.815  9.690   1.00 14.27 ?  92  CYS   A HA   1 
ATOM   1864 H  HB2  . CYS   A 1 92  ? 28.104 0.502   9.729   1.00 15.95 ?  92  CYS   A HB2  1 
ATOM   1865 H  HB3  . CYS   A 1 92  ? 29.431 0.432   8.859   1.00 15.95 ?  92  CYS   A HB3  1 
ATOM   1866 H  HG   . CYS   A 1 92  ? 27.454 1.297   7.233   1.00 14.74 ?  92  CYS   A HG   1 
ATOM   1867 N  N    . LEU   A 1 93  ? 28.720 -3.218  7.862   1.00 11.59 ?  93  LEU   A N    1 
ATOM   1868 C  CA   . LEU   A 1 93  ? 29.132 -3.971  6.688   1.00 10.60 ?  93  LEU   A CA   1 
ATOM   1869 C  C    . LEU   A 1 93  ? 28.526 -3.288  5.467   1.00 10.78 ?  93  LEU   A C    1 
ATOM   1870 O  O    . LEU   A 1 93  ? 27.305 -3.347  5.247   1.00 11.18 ?  93  LEU   A O    1 
ATOM   1871 C  CB   . LEU   A 1 93  ? 28.661 -5.420  6.803   1.00 11.42 ?  93  LEU   A CB   1 
ATOM   1872 C  CG   . LEU   A 1 93  ? 29.041 -6.305  5.622   1.00 12.13 ?  93  LEU   A CG   1 
ATOM   1873 C  CD1  . LEU   A 1 93  ? 30.550 -6.563  5.602   1.00 12.63 ?  93  LEU   A CD1  1 
ATOM   1874 C  CD2  . LEU   A 1 93  ? 28.257 -7.624  5.629   1.00 12.98 ?  93  LEU   A CD2  1 
ATOM   1875 H  H    . LEU   A 1 93  ? 27.964 -3.468  8.189   1.00 13.92 ?  93  LEU   A H    1 
ATOM   1876 H  HA   . LEU   A 1 93  ? 30.096 -3.956  6.614   1.00 12.73 ?  93  LEU   A HA   1 
ATOM   1877 H  HB2  . LEU   A 1 93  ? 29.055 -5.809  7.605   1.00 13.71 ?  93  LEU   A HB2  1 
ATOM   1878 H  HB3  . LEU   A 1 93  ? 27.696 -5.430  6.880   1.00 13.71 ?  93  LEU   A HB3  1 
ATOM   1879 H  HG   . LEU   A 1 93  ? 28.824 -5.839  4.805   1.00 14.57 ?  93  LEU   A HG   1 
ATOM   1880 H  HD11 . LEU   A 1 93  ? 30.763 -7.166  4.875   1.00 15.16 ?  93  LEU   A HD11 1 
ATOM   1881 H  HD12 . LEU   A 1 93  ? 31.021 -5.722  5.484   1.00 15.16 ?  93  LEU   A HD12 1 
ATOM   1882 H  HD13 . LEU   A 1 93  ? 30.817 -6.967  6.450   1.00 15.16 ?  93  LEU   A HD13 1 
ATOM   1883 H  HD21 . LEU   A 1 93  ? 28.533 -8.157  4.861   1.00 15.59 ?  93  LEU   A HD21 1 
ATOM   1884 H  HD22 . LEU   A 1 93  ? 28.450 -8.107  6.447   1.00 15.59 ?  93  LEU   A HD22 1 
ATOM   1885 H  HD23 . LEU   A 1 93  ? 27.311 -7.430  5.570   1.00 15.59 ?  93  LEU   A HD23 1 
ATOM   1886 N  N    . HIS   A 1 94  ? 29.373 -2.593  4.706   1.00 10.90 ?  94  HIS   A N    1 
ATOM   1887 C  CA   . HIS   A 1 94  ? 28.943 -1.906  3.493   1.00 11.25 ?  94  HIS   A CA   1 
ATOM   1888 C  C    . HIS   A 1 94  ? 28.950 -2.932  2.377   1.00 10.97 ?  94  HIS   A C    1 
ATOM   1889 O  O    . HIS   A 1 94  ? 30.006 -3.469  2.033   1.00 12.29 ?  94  HIS   A O    1 
ATOM   1890 C  CB   . HIS   A 1 94  ? 29.896 -0.758  3.161   1.00 11.56 ?  94  HIS   A CB   1 
ATOM   1891 C  CG   . HIS   A 1 94  ? 29.893 0.337   4.178   1.00 11.26 ?  94  HIS   A CG   1 
ATOM   1892 N  ND1  . HIS   A 1 94  ? 29.022 1.407   4.123   1.00 11.53 ?  94  HIS   A ND1  1 
ATOM   1893 C  CD2  . HIS   A 1 94  ? 30.635 0.507   5.298   1.00 12.09 ?  94  HIS   A CD2  1 
ATOM   1894 C  CE1  . HIS   A 1 94  ? 29.252 2.197   5.156   1.00 11.22 ?  94  HIS   A CE1  1 
ATOM   1895 N  NE2  . HIS   A 1 94  ? 30.208 1.666   5.894   1.00 12.04 ?  94  HIS   A NE2  1 
ATOM   1896 H  H    . HIS   A 1 94  ? 30.217 -2.516  4.868   1.00 13.09 ?  94  HIS   A H    1 
ATOM   1897 H  HA   . HIS   A 1 94  ? 28.042 -1.559  3.604   1.00 13.51 ?  94  HIS   A HA   1 
ATOM   1898 H  HB2  . HIS   A 1 94  ? 30.794 -1.103  3.100   1.00 13.88 ?  94  HIS   A HB2  1 
ATOM   1899 H  HB3  . HIS   A 1 94  ? 29.630 -0.367  2.311   1.00 13.88 ?  94  HIS   A HB3  1 
ATOM   1900 H  HD2  . HIS   A 1 94  ? 31.302 -0.058  5.611   1.00 14.51 ?  94  HIS   A HD2  1 
ATOM   1901 H  HE1  . HIS   A 1 94  ? 28.791 2.984   5.345   1.00 13.47 ?  94  HIS   A HE1  1 
ATOM   1902 H  HE2  . HIS   A 1 94  ? 30.526 2.009   6.617   1.00 14.46 ?  94  HIS   A HE2  1 
ATOM   1903 N  N    . VAL   A 1 95  ? 27.779 -3.247  1.829   1.00 11.10 ?  95  VAL   A N    1 
ATOM   1904 C  CA   . VAL   A 1 95  ? 27.632 -4.280  0.808   1.00 11.21 ?  95  VAL   A CA   1 
ATOM   1905 C  C    . VAL   A 1 95  ? 27.074 -3.653  -0.457  1.00 10.44 ?  95  VAL   A C    1 
ATOM   1906 O  O    . VAL   A 1 95  ? 26.071 -2.931  -0.403  1.00 11.76 ?  95  VAL   A O    1 
ATOM   1907 C  CB   . VAL   A 1 95  ? 26.717 -5.431  1.267   1.00 11.75 ?  95  VAL   A CB   1 
ATOM   1908 C  CG1  . VAL   A 1 95  ? 26.596 -6.460  0.157   1.00 12.78 ?  95  VAL   A CG1  1 
ATOM   1909 C  CG2  . VAL   A 1 95  ? 27.248 -6.046  2.551   1.00 11.70 ?  95  VAL   A CG2  1 
ATOM   1910 H  H    . VAL   A 1 95  ? 27.034 -2.863  2.032   1.00 13.33 ?  95  VAL   A H    1 
ATOM   1911 H  HA   . VAL   A 1 95  ? 28.503 -4.654  0.602   1.00 13.46 ?  95  VAL   A HA   1 
ATOM   1912 H  HB   . VAL   A 1 95  ? 25.835 -5.083  1.447   1.00 14.11 ?  95  VAL   A HB   1 
ATOM   1913 H  HG11 . VAL   A 1 95  ? 26.233 -7.286  0.526   1.00 15.34 ?  95  VAL   A HG11 1 
ATOM   1914 H  HG12 . VAL   A 1 95  ? 26.000 -6.124  -0.531  1.00 15.34 ?  95  VAL   A HG12 1 
ATOM   1915 H  HG13 . VAL   A 1 95  ? 27.474 -6.634  -0.220  1.00 15.34 ?  95  VAL   A HG13 1 
ATOM   1916 H  HG21 . VAL   A 1 95  ? 26.701 -6.815  2.785   1.00 14.04 ?  95  VAL   A HG21 1 
ATOM   1917 H  HG22 . VAL   A 1 95  ? 28.167 -6.320  2.421   1.00 14.04 ?  95  VAL   A HG22 1 
ATOM   1918 H  HG23 . VAL   A 1 95  ? 27.197 -5.383  3.261   1.00 14.04 ?  95  VAL   A HG23 1 
ATOM   1919 N  N    . VAL   A 1 96  ? 27.726 -3.928  -1.594  1.00 10.66 ?  96  VAL   A N    1 
ATOM   1920 C  CA   . VAL   A 1 96  ? 27.312 -3.373  -2.878  1.00 11.38 ?  96  VAL   A CA   1 
ATOM   1921 C  C    . VAL   A 1 96  ? 26.505 -4.424  -3.630  1.00 11.52 ?  96  VAL   A C    1 
ATOM   1922 O  O    . VAL   A 1 96  ? 27.064 -5.354  -4.217  1.00 12.60 ?  96  VAL   A O    1 
ATOM   1923 C  CB   . VAL   A 1 96  ? 28.504 -2.901  -3.711  1.00 11.91 ?  96  VAL   A CB   1 
ATOM   1924 C  CG1  . VAL   A 1 96  ? 28.009 -2.267  -4.992  1.00 11.77 ?  96  VAL   A CG1  1 
ATOM   1925 C  CG2  . VAL   A 1 96  ? 29.372 -1.949  -2.919  1.00 12.44 ?  96  VAL   A CG2  1 
ATOM   1926 H  H    . VAL   A 1 96  ? 28.427 -4.439  -1.643  1.00 12.80 ?  96  VAL   A H    1 
ATOM   1927 H  HA   . VAL   A 1 96  ? 26.739 -2.611  -2.716  1.00 13.67 ?  96  VAL   A HA   1 
ATOM   1928 H  HB   . VAL   A 1 96  ? 29.047 -3.667  -3.950  1.00 14.30 ?  96  VAL   A HB   1 
ATOM   1929 H  HG11 . VAL   A 1 96  ? 28.747 -1.804  -5.417  1.00 14.13 ?  96  VAL   A HG11 1 
ATOM   1930 H  HG12 . VAL   A 1 96  ? 27.667 -2.956  -5.577  1.00 14.13 ?  96  VAL   A HG12 1 
ATOM   1931 H  HG13 . VAL   A 1 96  ? 27.306 -1.631  -4.775  1.00 14.13 ?  96  VAL   A HG13 1 
ATOM   1932 H  HG21 . VAL   A 1 96  ? 30.066 -1.599  -3.496  1.00 14.94 ?  96  VAL   A HG21 1 
ATOM   1933 H  HG22 . VAL   A 1 96  ? 28.820 -1.225  -2.583  1.00 14.94 ?  96  VAL   A HG22 1 
ATOM   1934 H  HG23 . VAL   A 1 96  ? 29.770 -2.430  -2.175  1.00 14.94 ?  96  VAL   A HG23 1 
ATOM   1935 N  N    . GLY   A 1 97  ? 25.187 -4.249  -3.674  1.00 11.76 ?  97  GLY   A N    1 
ATOM   1936 C  CA   . GLY   A 1 97  ? 24.384 -5.028  -4.587  1.00 12.24 ?  97  GLY   A CA   1 
ATOM   1937 C  C    . GLY   A 1 97  ? 24.365 -4.380  -5.959  1.00 12.19 ?  97  GLY   A C    1 
ATOM   1938 O  O    . GLY   A 1 97  ? 24.634 -3.185  -6.101  1.00 13.05 ?  97  GLY   A O    1 
ATOM   1939 H  H    . GLY   A 1 97  ? 24.738 -3.687  -3.185  1.00 14.12 ?  97  GLY   A H    1 
ATOM   1940 H  HA2  . GLY   A 1 97  ? 24.753 -5.918  -4.655  1.00 14.70 ?  97  GLY   A HA2  1 
ATOM   1941 H  HA3  . GLY   A 1 97  ? 23.474 -5.087  -4.256  1.00 14.70 ?  97  GLY   A HA3  1 
ATOM   1942 N  N    . PRO   A 1 98  ? 24.033 -5.141  -6.999  1.00 12.52 ?  98  PRO   A N    1 
ATOM   1943 C  CA   . PRO   A 1 98  ? 23.900 -4.538  -8.330  1.00 13.90 ?  98  PRO   A CA   1 
ATOM   1944 C  C    . PRO   A 1 98  ? 22.792 -3.492  -8.383  1.00 14.32 ?  98  PRO   A C    1 
ATOM   1945 O  O    . PRO   A 1 98  ? 21.713 -3.652  -7.802  1.00 14.34 ?  98  PRO   A O    1 
ATOM   1946 C  CB   . PRO   A 1 98  ? 23.585 -5.733  -9.236  1.00 14.30 ?  98  PRO   A CB   1 
ATOM   1947 C  CG   . PRO   A 1 98  ? 23.008 -6.766  -8.323  1.00 14.27 ?  98  PRO   A CG   1 
ATOM   1948 C  CD   . PRO   A 1 98  ? 23.728 -6.585  -7.007  1.00 12.86 ?  98  PRO   A CD   1 
ATOM   1949 H  HA   . PRO   A 1 98  ? 24.740 -4.133  -8.598  1.00 16.69 ?  98  PRO   A HA   1 
ATOM   1950 H  HB2  . PRO   A 1 98  ? 22.937 -5.463  -9.905  1.00 17.17 ?  98  PRO   A HB2  1 
ATOM   1951 H  HB3  . PRO   A 1 98  ? 24.400 -6.049  -9.646  1.00 17.17 ?  98  PRO   A HB3  1 
ATOM   1952 H  HG2  . PRO   A 1 98  ? 22.055 -6.611  -8.213  1.00 17.14 ?  98  PRO   A HG2  1 
ATOM   1953 H  HG3  . PRO   A 1 98  ? 23.174 -7.648  -8.684  1.00 17.14 ?  98  PRO   A HG3  1 
ATOM   1954 H  HD2  . PRO   A 1 98  ? 23.147 -6.814  -6.261  1.00 15.45 ?  98  PRO   A HD2  1 
ATOM   1955 H  HD3  . PRO   A 1 98  ? 24.549 -7.103  -6.988  1.00 15.45 ?  98  PRO   A HD3  1 
ATOM   1956 N  N    A ASN   A 1 99  ? 23.082 -2.386  -9.068  0.74 15.18 ?  99  ASN   A N    1 
ATOM   1957 N  N    B ASN   A 1 99  ? 23.073 -2.428  -9.125  0.26 15.58 ?  99  ASN   A N    1 
ATOM   1958 C  CA   A ASN   A 1 99  ? 22.113 -1.313  -9.284  0.74 16.32 ?  99  ASN   A CA   1 
ATOM   1959 C  CA   B ASN   A 1 99  ? 22.097 -1.396  -9.431  0.26 16.94 ?  99  ASN   A CA   1 
ATOM   1960 C  C    A ASN   A 1 99  ? 21.568 -1.470  -10.703 0.74 17.33 ?  99  ASN   A C    1 
ATOM   1961 C  C    B ASN   A 1 99  ? 21.446 -1.732  -10.768 0.26 17.97 ?  99  ASN   A C    1 
ATOM   1962 O  O    A ASN   A 1 99  ? 22.241 -1.148  -11.688 0.74 18.54 ?  99  ASN   A O    1 
ATOM   1963 O  O    B ASN   A 1 99  ? 22.133 -1.831  -11.793 0.26 17.37 ?  99  ASN   A O    1 
ATOM   1964 C  CB   A ASN   A 1 99  ? 22.756 0.054   -9.060  0.74 16.98 ?  99  ASN   A CB   1 
ATOM   1965 C  CB   B ASN   A 1 99  ? 22.802 -0.045  -9.508  0.26 17.36 ?  99  ASN   A CB   1 
ATOM   1966 C  CG   A ASN   A 1 99  ? 21.734 1.192   -9.027  0.74 17.80 ?  99  ASN   A CG   1 
ATOM   1967 C  CG   B ASN   A 1 99  ? 21.837 1.112   -9.606  0.26 18.17 ?  99  ASN   A CG   1 
ATOM   1968 O  OD1  A ASN   A 1 99  ? 20.715 1.149   -9.715  0.74 19.04 ?  99  ASN   A OD1  1 
ATOM   1969 O  OD1  B ASN   A 1 99  ? 20.845 1.046   -10.329 0.26 18.10 ?  99  ASN   A OD1  1 
ATOM   1970 N  ND2  A ASN   A 1 99  ? 22.022 2.224   -8.234  0.74 18.09 ?  99  ASN   A ND2  1 
ATOM   1971 N  ND2  B ASN   A 1 99  ? 22.120 2.181   -8.870  0.26 18.61 ?  99  ASN   A ND2  1 
ATOM   1972 H  H    A ASN   A 1 99  ? 23.852 -2.225  -9.412  0.74 18.22 ?  99  ASN   A H    1 
ATOM   1973 H  H    B ASN   A 1 99  ? 23.847 -2.279  -9.467  0.26 18.70 ?  99  ASN   A H    1 
ATOM   1974 H  HA   A ASN   A 1 99  ? 21.375 -1.410  -8.655  0.74 19.59 ?  99  ASN   A HA   1 
ATOM   1975 H  HA   B ASN   A 1 99  ? 21.413 -1.363  -8.742  0.26 20.34 ?  99  ASN   A HA   1 
ATOM   1976 H  HB2  A ASN   A 1 99  ? 23.225 0.052   -8.211  0.74 20.38 ?  99  ASN   A HB2  1 
ATOM   1977 H  HB2  B ASN   A 1 99  ? 23.336 0.074   -8.710  0.26 20.84 ?  99  ASN   A HB2  1 
ATOM   1978 H  HB3  A ASN   A 1 99  ? 23.380 0.229   -9.782  0.74 20.38 ?  99  ASN   A HB3  1 
ATOM   1979 H  HB3  B ASN   A 1 99  ? 23.371 -0.034  -10.291 0.26 20.84 ?  99  ASN   A HB3  1 
ATOM   1980 H  HD21 A ASN   A 1 99  ? 21.487 2.898   -8.185  0.74 21.72 ?  99  ASN   A HD21 1 
ATOM   1981 H  HD21 B ASN   A 1 99  ? 21.601 2.865   -8.883  0.26 22.33 ?  99  ASN   A HD21 1 
ATOM   1982 H  HD22 A ASN   A 1 99  ? 22.748 2.222   -7.771  0.74 21.72 ?  99  ASN   A HD22 1 
ATOM   1983 H  HD22 B ASN   A 1 99  ? 22.826 2.187   -8.375  0.26 22.33 ?  99  ASN   A HD22 1 
ATOM   1984 N  N    A VAL   A 1 100 ? 20.343 -1.997  -10.801 0.74 18.27 ?  100 VAL   A N    1 
ATOM   1985 N  N    B VAL   A 1 100 ? 20.124 -1.916  -10.755 0.26 19.39 ?  100 VAL   A N    1 
ATOM   1986 C  CA   A VAL   A 1 100 ? 19.705 -2.196  -12.098 0.74 20.96 ?  100 VAL   A CA   1 
ATOM   1987 C  CA   B VAL   A 1 100 ? 19.411 -2.274  -11.978 0.26 21.16 ?  100 VAL   A CA   1 
ATOM   1988 C  C    A VAL   A 1 100 ? 19.602 -0.881  -12.860 0.74 21.33 ?  100 VAL   A C    1 
ATOM   1989 C  C    B VAL   A 1 100 ? 19.281 -1.078  -12.906 0.26 22.64 ?  100 VAL   A C    1 
ATOM   1990 O  O    A VAL   A 1 100 ? 19.688 -0.862  -14.094 0.74 22.80 ?  100 VAL   A O    1 
ATOM   1991 O  O    B VAL   A 1 100 ? 19.280 -1.236  -14.134 0.26 23.06 ?  100 VAL   A O    1 
ATOM   1992 C  CB   A VAL   A 1 100 ? 18.337 -2.886  -11.912 0.74 23.21 ?  100 VAL   A CB   1 
ATOM   1993 C  CB   B VAL   A 1 100 ? 18.046 -2.895  -11.638 0.26 21.81 ?  100 VAL   A CB   1 
ATOM   1994 C  CG1  A VAL   A 1 100 ? 17.623 -3.059  -13.247 0.74 24.13 ?  100 VAL   A CG1  1 
ATOM   1995 C  CG1  B VAL   A 1 100 ? 17.317 -3.315  -12.908 0.26 22.03 ?  100 VAL   A CG1  1 
ATOM   1996 C  CG2  A VAL   A 1 100 ? 18.533 -4.231  -11.240 0.74 23.68 ?  100 VAL   A CG2  1 
ATOM   1997 C  CG2  B VAL   A 1 100 ? 18.243 -4.076  -10.720 0.26 22.43 ?  100 VAL   A CG2  1 
ATOM   1998 H  H    A VAL   A 1 100 ? 19.867 -2.256  -10.131 0.74 21.93 ?  100 VAL   A H    1 
ATOM   1999 H  H    B VAL   A 1 100 ? 19.628 -1.849  -10.057 0.26 23.27 ?  100 VAL   A H    1 
ATOM   2000 H  HA   A VAL   A 1 100 ? 20.256 -2.793  -12.627 0.74 25.16 ?  100 VAL   A HA   1 
ATOM   2001 H  HA   B VAL   A 1 100 ? 19.925 -2.943  -12.449 0.26 25.40 ?  100 VAL   A HA   1 
ATOM   2002 H  HB   A VAL   A 1 100 ? 17.776 -2.339  -11.339 0.74 27.86 ?  100 VAL   A HB   1 
ATOM   2003 H  HB   B VAL   A 1 100 ? 17.501 -2.234  -11.181 0.26 26.18 ?  100 VAL   A HB   1 
ATOM   2004 H  HG11 A VAL   A 1 100 ? 16.852 -3.636  -13.119 0.74 28.96 ?  100 VAL   A HG11 1 
ATOM   2005 H  HG11 B VAL   A 1 100 ? 16.533 -3.830  -12.663 0.26 26.45 ?  100 VAL   A HG11 1 
ATOM   2006 H  HG12 A VAL   A 1 100 ? 17.334 -2.192  -13.569 0.74 28.96 ?  100 VAL   A HG12 1 
ATOM   2007 H  HG12 B VAL   A 1 100 ? 17.050 -2.524  -13.403 0.26 26.45 ?  100 VAL   A HG12 1 
ATOM   2008 H  HG13 A VAL   A 1 100 ? 18.235 -3.464  -13.882 0.74 28.96 ?  100 VAL   A HG13 1 
ATOM   2009 H  HG13 B VAL   A 1 100 ? 17.912 -3.859  -13.448 0.26 26.45 ?  100 VAL   A HG13 1 
ATOM   2010 H  HG21 A VAL   A 1 100 ? 17.686 -4.705  -11.225 0.74 28.42 ?  100 VAL   A HG21 1 
ATOM   2011 H  HG21 B VAL   A 1 100 ? 17.405 -4.549  -10.636 0.26 26.92 ?  100 VAL   A HG21 1 
ATOM   2012 H  HG22 A VAL   A 1 100 ? 19.188 -4.742  -11.742 0.74 28.42 ?  100 VAL   A HG22 1 
ATOM   2013 H  HG22 B VAL   A 1 100 ? 18.919 -4.658  -11.104 0.26 26.92 ?  100 VAL   A HG22 1 
ATOM   2014 H  HG23 A VAL   A 1 100 ? 18.848 -4.091  -10.334 0.74 28.42 ?  100 VAL   A HG23 1 
ATOM   2015 H  HG23 B VAL   A 1 100 ? 18.536 -3.755  -9.854  0.26 26.92 ?  100 VAL   A HG23 1 
ATOM   2016 N  N    A ASN   A 1 101 ? 19.419 0.234   -12.153 0.74 22.61 ?  101 ASN   A N    1 
ATOM   2017 N  N    B ASN   A 1 101 ? 19.163 0.129   -12.353 0.26 24.07 ?  101 ASN   A N    1 
ATOM   2018 C  CA   A ASN   A 1 101 ? 19.363 1.537   -12.813 0.74 24.75 ?  101 ASN   A CA   1 
ATOM   2019 C  CA   B ASN   A 1 101 ? 19.175 1.347   -13.152 0.26 25.21 ?  101 ASN   A CA   1 
ATOM   2020 C  C    A ASN   A 1 101 ? 20.716 1.990   -13.361 0.74 26.96 ?  101 ASN   A C    1 
ATOM   2021 C  C    B ASN   A 1 101 ? 20.579 1.723   -13.634 0.26 27.03 ?  101 ASN   A C    1 
ATOM   2022 O  O    A ASN   A 1 101 ? 20.775 3.040   -14.016 0.74 29.65 ?  101 ASN   A O    1 
ATOM   2023 O  O    B ASN   A 1 101 ? 20.813 2.882   -14.001 0.26 27.90 ?  101 ASN   A O    1 
ATOM   2024 C  CB   A ASN   A 1 101 ? 18.762 2.576   -11.865 0.74 24.32 ?  101 ASN   A CB   1 
ATOM   2025 C  CB   B ASN   A 1 101 ? 18.533 2.498   -12.372 0.26 24.49 ?  101 ASN   A CB   1 
ATOM   2026 C  CG   A ASN   A 1 101 ? 17.361 2.198   -11.404 0.74 23.48 ?  101 ASN   A CG   1 
ATOM   2027 C  CG   B ASN   A 1 101 ? 17.343 2.047   -11.542 0.26 23.60 ?  101 ASN   A CG   1 
ATOM   2028 O  OD1  A ASN   A 1 101 ? 16.559 1.675   -12.182 0.74 24.14 ?  101 ASN   A OD1  1 
ATOM   2029 O  OD1  B ASN   A 1 101 ? 16.332 1.591   -12.079 0.26 23.18 ?  101 ASN   A OD1  1 
ATOM   2030 N  ND2  A ASN   A 1 101 ? 17.062 2.453   -10.135 0.74 23.37 ?  101 ASN   A ND2  1 
ATOM   2031 N  ND2  B ASN   A 1 101 ? 17.458 2.174   -10.224 0.26 23.44 ?  101 ASN   A ND2  1 
ATOM   2032 H  H    A ASN   A 1 101 ? 19.315 0.260   -11.300 0.74 27.14 ?  101 ASN   A H    1 
ATOM   2033 H  H    B ASN   A 1 101 ? 19.061 0.265   -11.508 0.26 28.90 ?  101 ASN   A H    1 
ATOM   2034 H  HA   A ASN   A 1 101 ? 18.760 1.462   -13.565 0.74 29.71 ?  101 ASN   A HA   1 
ATOM   2035 H  HA   B ASN   A 1 101 ? 18.636 1.200   -13.942 0.26 30.26 ?  101 ASN   A HA   1 
ATOM   2036 H  HB2  A ASN   A 1 101 ? 19.326 2.661   -11.080 0.74 29.19 ?  101 ASN   A HB2  1 
ATOM   2037 H  HB2  B ASN   A 1 101 ? 19.188 2.883   -11.772 0.26 29.39 ?  101 ASN   A HB2  1 
ATOM   2038 H  HB3  A ASN   A 1 101 ? 18.711 3.432   -12.326 0.74 29.19 ?  101 ASN   A HB3  1 
ATOM   2039 H  HB3  B ASN   A 1 101 ? 18.219 3.169   -12.999 0.26 29.39 ?  101 ASN   A HB3  1 
ATOM   2040 H  HD21 A ASN   A 1 101 ? 16.281 2.261   -9.831  0.74 28.05 ?  101 ASN   A HD21 1 
ATOM   2041 H  HD21 B ASN   A 1 101 ? 16.811 1.933   -9.709  0.26 28.14 ?  101 ASN   A HD21 1 
ATOM   2042 H  HD22 A ASN   A 1 101 ? 17.646 2.816   -9.618  0.74 28.05 ?  101 ASN   A HD22 1 
ATOM   2043 H  HD22 B ASN   A 1 101 ? 18.177 2.500   -9.885  0.26 28.14 ?  101 ASN   A HD22 1 
ATOM   2044 N  N    A LYS   A 1 102 ? 21.788 1.229   -13.121 0.74 28.12 ?  102 LYS   A N    1 
ATOM   2045 N  N    B LYS   A 1 102 ? 21.504 0.758   -13.641 0.26 27.79 ?  102 LYS   A N    1 
ATOM   2046 C  CA   A LYS   A 1 102 ? 23.065 1.414   -13.801 0.74 29.13 ?  102 LYS   A CA   1 
ATOM   2047 C  CA   B LYS   A 1 102 ? 22.847 0.938   -14.168 0.26 28.22 ?  102 LYS   A CA   1 
ATOM   2048 C  C    A LYS   A 1 102 ? 23.367 0.304   -14.799 0.74 29.67 ?  102 LYS   A C    1 
ATOM   2049 C  C    B LYS   A 1 102 ? 23.239 -0.196  -15.103 0.26 27.72 ?  102 LYS   A C    1 
ATOM   2050 O  O    A LYS   A 1 102 ? 24.453 0.303   -15.387 0.74 30.57 ?  102 LYS   A O    1 
ATOM   2051 O  O    B LYS   A 1 102 ? 24.348 -0.179  -15.646 0.26 27.95 ?  102 LYS   A O    1 
ATOM   2052 C  CB   A LYS   A 1 102 ? 24.215 1.484   -12.788 0.74 30.12 ?  102 LYS   A CB   1 
ATOM   2053 C  CB   B LYS   A 1 102 ? 23.872 0.998   -13.025 0.26 29.19 ?  102 LYS   A CB   1 
ATOM   2054 C  CG   A LYS   A 1 102 ? 24.087 2.582   -11.754 0.74 30.82 ?  102 LYS   A CG   1 
ATOM   2055 C  CG   B LYS   A 1 102 ? 24.025 2.366   -12.385 0.26 29.99 ?  102 LYS   A CG   1 
ATOM   2056 C  CD   A LYS   A 1 102 ? 25.244 2.528   -10.764 0.74 31.80 ?  102 LYS   A CD   1 
ATOM   2057 C  CD   B LYS   A 1 102 ? 25.011 2.334   -11.225 0.26 30.93 ?  102 LYS   A CD   1 
ATOM   2058 C  CE   A LYS   A 1 102 ? 25.159 3.654   -9.746  0.74 32.79 ?  102 LYS   A CE   1 
ATOM   2059 C  CE   B LYS   A 1 102 ? 25.351 3.740   -10.758 0.26 31.66 ?  102 LYS   A CE   1 
ATOM   2060 N  NZ   A LYS   A 1 102 ? 26.260 3.577   -8.739  0.74 33.23 ?  102 LYS   A NZ   1 
ATOM   2061 N  NZ   B LYS   A 1 102 ? 25.564 3.811   -9.286  0.26 32.02 ?  102 LYS   A NZ   1 
ATOM   2062 H  H    A LYS   A 1 102 ? 21.800 0.582   -12.551 0.74 33.75 ?  102 LYS   A H    1 
ATOM   2063 H  H    B LYS   A 1 102 ? 21.370 -0.040  -13.352 0.26 33.35 ?  102 LYS   A H    1 
ATOM   2064 H  HA   A LYS   A 1 102 ? 23.045 2.250   -14.288 0.74 34.97 ?  102 LYS   A HA   1 
ATOM   2065 H  HA   B LYS   A 1 102 ? 22.889 1.777   -14.654 0.26 33.88 ?  102 LYS   A HA   1 
ATOM   2066 H  HB2  A LYS   A 1 102 ? 24.265 0.637   -12.316 0.74 36.15 ?  102 LYS   A HB2  1 
ATOM   2067 H  HB2  B LYS   A 1 102 ? 23.596 0.375   -12.336 0.26 35.03 ?  102 LYS   A HB2  1 
ATOM   2068 H  HB3  A LYS   A 1 102 ? 25.045 1.632   -13.272 0.74 36.15 ?  102 LYS   A HB3  1 
ATOM   2069 H  HB3  B LYS   A 1 102 ? 24.739 0.737   -13.370 0.26 35.03 ?  102 LYS   A HB3  1 
ATOM   2070 H  HG2  A LYS   A 1 102 ? 24.100 3.444   -12.197 0.74 37.00 ?  102 LYS   A HG2  1 
ATOM   2071 H  HG2  B LYS   A 1 102 ? 24.356 2.993   -13.047 0.26 35.99 ?  102 LYS   A HG2  1 
ATOM   2072 H  HG3  A LYS   A 1 102 ? 23.258 2.464   -11.264 0.74 37.00 ?  102 LYS   A HG3  1 
ATOM   2073 H  HG3  B LYS   A 1 102 ? 23.165 2.659   -12.045 0.26 35.99 ?  102 LYS   A HG3  1 
ATOM   2074 H  HD2  A LYS   A 1 102 ? 25.218 1.682   -10.288 0.74 38.17 ?  102 LYS   A HD2  1 
ATOM   2075 H  HD2  B LYS   A 1 102 ? 24.618 1.853   -10.479 0.26 37.13 ?  102 LYS   A HD2  1 
ATOM   2076 H  HD3  A LYS   A 1 102 ? 26.081 2.613   -11.248 0.74 38.17 ?  102 LYS   A HD3  1 
ATOM   2077 H  HD3  B LYS   A 1 102 ? 25.831 1.899   -11.510 0.26 37.13 ?  102 LYS   A HD3  1 
ATOM   2078 H  HE2  A LYS   A 1 102 ? 25.227 4.505   -10.209 0.74 39.36 ?  102 LYS   A HE2  1 
ATOM   2079 H  HE2  B LYS   A 1 102 ? 26.168 4.030   -11.195 0.26 38.00 ?  102 LYS   A HE2  1 
ATOM   2080 H  HE3  A LYS   A 1 102 ? 24.311 3.596   -9.279  0.74 39.36 ?  102 LYS   A HE3  1 
ATOM   2081 H  HE3  B LYS   A 1 102 ? 24.622 4.336   -10.988 0.26 38.00 ?  102 LYS   A HE3  1 
ATOM   2082 H  HZ1  A LYS   A 1 102 ? 26.186 4.245   -8.158  0.74 39.88 ?  102 LYS   A HZ1  1 
ATOM   2083 H  HZ1  B LYS   A 1 102 ? 25.760 4.645   -9.047  0.26 38.44 ?  102 LYS   A HZ1  1 
ATOM   2084 H  HZ2  A LYS   A 1 102 ? 26.214 2.804   -8.300  0.74 39.88 ?  102 LYS   A HZ2  1 
ATOM   2085 H  HZ2  B LYS   A 1 102 ? 24.825 3.555   -8.860  0.26 38.44 ?  102 LYS   A HZ2  1 
ATOM   2086 H  HZ3  A LYS   A 1 102 ? 27.048 3.631   -9.147  0.74 39.88 ?  102 LYS   A HZ3  1 
ATOM   2087 H  HZ3  B LYS   A 1 102 ? 26.234 3.276   -9.049  0.26 38.44 ?  102 LYS   A HZ3  1 
ATOM   2088 N  N    A GLY   A 1 103 ? 22.455 -0.648  -14.990 0.74 29.74 ?  103 GLY   A N    1 
ATOM   2089 N  N    B GLY   A 1 103 ? 22.372 -1.188  -15.285 0.26 27.27 ?  103 GLY   A N    1 
ATOM   2090 C  CA   A GLY   A 1 103 ? 22.682 -1.736  -15.922 0.74 29.49 ?  103 GLY   A CA   1 
ATOM   2091 C  CA   B GLY   A 1 103 ? 22.660 -2.339  -16.108 0.26 26.56 ?  103 GLY   A CA   1 
ATOM   2092 C  C    A GLY   A 1 103 ? 23.533 -2.873  -15.401 0.74 29.32 ?  103 GLY   A C    1 
ATOM   2093 C  C    B GLY   A 1 103 ? 23.470 -3.418  -15.427 0.26 25.54 ?  103 GLY   A C    1 
ATOM   2094 O  O    A GLY   A 1 103 ? 24.146 -3.586  -16.201 0.74 30.60 ?  103 GLY   A O    1 
ATOM   2095 O  O    B GLY   A 1 103 ? 23.767 -4.439  -16.062 0.26 24.92 ?  103 GLY   A O    1 
ATOM   2096 H  H    A GLY   A 1 103 ? 21.698 -0.691  -14.586 0.74 35.69 ?  103 GLY   A H    1 
ATOM   2097 H  H    B GLY   A 1 103 ? 21.599 -1.211  -14.919 0.26 32.73 ?  103 GLY   A H    1 
ATOM   2098 H  HA2  A GLY   A 1 103 ? 21.824 -2.101  -16.195 0.74 35.40 ?  103 GLY   A HA2  1 
ATOM   2099 H  HA2  B GLY   A 1 103 ? 21.820 -2.727  -16.400 0.26 31.88 ?  103 GLY   A HA2  1 
ATOM   2100 H  HA3  A GLY   A 1 103 ? 23.120 -1.386  -16.713 0.74 35.40 ?  103 GLY   A HA3  1 
ATOM   2101 H  HA3  B GLY   A 1 103 ? 23.147 -2.049  -16.891 0.26 31.88 ?  103 GLY   A HA3  1 
ATOM   2102 N  N    A GLU   A 1 104 ? 23.586 -3.076  -14.089 0.74 26.86 ?  104 GLU   A N    1 
ATOM   2103 N  N    B GLU   A 1 104 ? 23.832 -3.233  -14.161 0.26 25.30 ?  104 GLU   A N    1 
ATOM   2104 C  CA   A GLU   A 1 104 ? 24.466 -4.073  -13.494 0.74 24.69 ?  104 GLU   A CA   1 
ATOM   2105 C  CA   B GLU   A 1 104 ? 24.681 -4.195  -13.475 0.26 25.05 ?  104 GLU   A CA   1 
ATOM   2106 C  C    A GLU   A 1 104 ? 23.784 -5.436  -13.393 0.74 24.97 ?  104 GLU   A C    1 
ATOM   2107 C  C    B GLU   A 1 104 ? 23.949 -5.522  -13.293 0.26 25.80 ?  104 GLU   A C    1 
ATOM   2108 O  O    A GLU   A 1 104 ? 22.557 -5.541  -13.296 0.74 26.07 ?  104 GLU   A O    1 
ATOM   2109 O  O    B GLU   A 1 104 ? 22.774 -5.562  -12.916 0.26 25.56 ?  104 GLU   A O    1 
ATOM   2110 C  CB   A GLU   A 1 104 ? 24.972 -3.581  -12.134 0.74 22.90 ?  104 GLU   A CB   1 
ATOM   2111 C  CB   B GLU   A 1 104 ? 25.137 -3.617  -12.135 0.26 24.42 ?  104 GLU   A CB   1 
ATOM   2112 C  CG   A GLU   A 1 104 ? 25.889 -2.364  -12.301 0.74 22.84 ?  104 GLU   A CG   1 
ATOM   2113 C  CG   B GLU   A 1 104 ? 25.893 -2.301  -12.298 0.26 24.28 ?  104 GLU   A CG   1 
ATOM   2114 C  CD   A GLU   A 1 104 ? 26.224 -1.601  -11.026 0.74 21.46 ?  104 GLU   A CD   1 
ATOM   2115 C  CD   B GLU   A 1 104 ? 26.355 -1.701  -10.983 0.26 23.96 ?  104 GLU   A CD   1 
ATOM   2116 O  OE1  A GLU   A 1 104 ? 25.663 -1.888  -9.951  0.74 20.23 ?  104 GLU   A OE1  1 
ATOM   2117 O  OE1  B GLU   A 1 104 ? 25.862 -2.124  -9.918  0.26 23.60 ?  104 GLU   A OE1  1 
ATOM   2118 O  OE2  A GLU   A 1 104 ? 27.065 -0.675  -11.125 0.74 22.71 -1 104 GLU   A OE2  1 
ATOM   2119 O  OE2  B GLU   A 1 104 ? 27.217 -0.797  -11.018 0.26 24.41 -1 104 GLU   A OE2  1 
ATOM   2120 H  H    A GLU   A 1 104 ? 23.120 -2.639  -13.515 0.74 32.24 ?  104 GLU   A H    1 
ATOM   2121 H  H    B GLU   A 1 104 ? 23.596 -2.559  -13.676 0.26 30.36 ?  104 GLU   A H    1 
ATOM   2122 H  HA   A GLU   A 1 104 ? 25.237 -4.182  -14.069 0.74 29.63 ?  104 GLU   A HA   1 
ATOM   2123 H  HA   B GLU   A 1 104 ? 25.474 -4.356  -14.012 0.26 30.07 ?  104 GLU   A HA   1 
ATOM   2124 H  HB2  A GLU   A 1 104 ? 24.214 -3.327  -11.586 0.74 27.48 ?  104 GLU   A HB2  1 
ATOM   2125 H  HB2  B GLU   A 1 104 ? 24.362 -3.446  -11.577 0.26 29.32 ?  104 GLU   A HB2  1 
ATOM   2126 H  HB3  A GLU   A 1 104 ? 25.474 -4.293  -11.707 0.74 27.48 ?  104 GLU   A HB3  1 
ATOM   2127 H  HB3  B GLU   A 1 104 ? 25.731 -4.247  -11.697 0.26 29.32 ?  104 GLU   A HB3  1 
ATOM   2128 H  HG2  A GLU   A 1 104 ? 26.724 -2.664  -12.688 0.74 27.41 ?  104 GLU   A HG2  1 
ATOM   2129 H  HG2  B GLU   A 1 104 ? 26.675 -2.454  -12.853 0.26 29.14 ?  104 GLU   A HG2  1 
ATOM   2130 H  HG3  A GLU   A 1 104 ? 25.458 -1.736  -12.898 0.74 27.41 ?  104 GLU   A HG3  1 
ATOM   2131 H  HG3  B GLU   A 1 104 ? 25.311 -1.652  -12.725 0.26 29.14 ?  104 GLU   A HG3  1 
ATOM   2132 N  N    A ASP   A 1 105 ? 24.606 -6.485  -13.410 0.74 25.52 ?  105 ASP   A N    1 
ATOM   2133 N  N    B ASP   A 1 105 ? 24.661 -6.612  -13.570 0.26 26.90 ?  105 ASP   A N    1 
ATOM   2134 C  CA   A ASP   A 1 105 ? 24.126 -7.854  -13.563 0.74 26.83 ?  105 ASP   A CA   1 
ATOM   2135 C  CA   B ASP   A 1 105 ? 24.062 -7.939  -13.611 0.26 27.91 ?  105 ASP   A CA   1 
ATOM   2136 C  C    A ASP   A 1 105 ? 23.434 -8.328  -12.287 0.74 24.30 ?  105 ASP   A C    1 
ATOM   2137 C  C    B ASP   A 1 105 ? 23.383 -8.275  -12.288 0.26 27.32 ?  105 ASP   A C    1 
ATOM   2138 O  O    A ASP   A 1 105 ? 24.070 -8.451  -11.237 0.74 22.02 ?  105 ASP   A O    1 
ATOM   2139 O  O    B ASP   A 1 105 ? 24.005 -8.224  -11.224 0.26 27.03 ?  105 ASP   A O    1 
ATOM   2140 C  CB   A ASP   A 1 105 ? 25.316 -8.755  -13.891 0.74 30.60 ?  105 ASP   A CB   1 
ATOM   2141 C  CB   B ASP   A 1 105 ? 25.157 -8.962  -13.916 0.26 29.32 ?  105 ASP   A CB   1 
ATOM   2142 C  CG   A ASP   A 1 105 ? 24.912 -10.177 -14.191 0.74 33.82 ?  105 ASP   A CG   1 
ATOM   2143 C  CG   B ASP   A 1 105 ? 24.663 -10.393 -13.848 0.26 30.49 ?  105 ASP   A CG   1 
ATOM   2144 O  OD1  A ASP   A 1 105 ? 23.697 -10.440 -14.289 0.74 34.02 ?  105 ASP   A OD1  1 
ATOM   2145 O  OD1  B ASP   A 1 105 ? 23.435 -10.614 -13.922 0.26 30.66 ?  105 ASP   A OD1  1 
ATOM   2146 O  OD2  A ASP   A 1 105 ? 25.822 -11.029 -14.333 0.74 36.15 -1 105 ASP   A OD2  1 
ATOM   2147 O  OD2  B ASP   A 1 105 ? 25.511 -11.300 -13.717 0.26 31.47 -1 105 ASP   A OD2  1 
ATOM   2148 H  H    A ASP   A 1 105 ? 25.462 -6.428  -13.326 0.74 30.64 ?  105 ASP   A H    1 
ATOM   2149 H  H    B ASP   A 1 105 ? 25.501 -6.608  -13.735 0.26 32.29 ?  105 ASP   A H    1 
ATOM   2150 H  HA   A ASP   A 1 105 ? 23.492 -7.901  -14.292 0.74 32.20 ?  105 ASP   A HA   1 
ATOM   2151 H  HA   B ASP   A 1 105 ? 23.398 -7.977  -14.314 0.26 33.50 ?  105 ASP   A HA   1 
ATOM   2152 H  HB2  A ASP   A 1 105 ? 25.769 -8.407  -14.675 0.74 36.73 ?  105 ASP   A HB2  1 
ATOM   2153 H  HB2  B ASP   A 1 105 ? 25.489 -8.807  -14.815 0.26 35.19 ?  105 ASP   A HB2  1 
ATOM   2154 H  HB3  A ASP   A 1 105 ? 25.923 -8.771  -13.137 0.74 36.73 ?  105 ASP   A HB3  1 
ATOM   2155 H  HB3  B ASP   A 1 105 ? 25.880 -8.852  -13.276 0.26 35.19 ?  105 ASP   A HB3  1 
ATOM   2156 N  N    A ILE   A 1 106 ? 22.134 -8.619  -12.385 0.74 24.35 ?  106 ILE   A N    1 
ATOM   2157 N  N    B ILE   A 1 106 ? 22.096 -8.628  -12.363 0.26 27.05 ?  106 ILE   A N    1 
ATOM   2158 C  CA   A ILE   A 1 106 ? 21.366 -9.041  -11.219 0.74 23.89 ?  106 ILE   A CA   1 
ATOM   2159 C  CA   B ILE   A 1 106 ? 21.353 -8.994  -11.163 0.26 26.50 ?  106 ILE   A CA   1 
ATOM   2160 C  C    A ILE   A 1 106 ? 21.905 -10.327 -10.620 0.74 23.06 ?  106 ILE   A C    1 
ATOM   2161 C  C    B ILE   A 1 106 ? 21.865 -10.295 -10.562 0.26 25.76 ?  106 ILE   A C    1 
ATOM   2162 O  O    A ILE   A 1 106 ? 21.698 -10.579 -9.428  0.74 22.30 ?  106 ILE   A O    1 
ATOM   2163 O  O    B ILE   A 1 106 ? 21.640 -10.552 -9.373  0.26 25.43 ?  106 ILE   A O    1 
ATOM   2164 C  CB   A ILE   A 1 106 ? 19.862 -9.151  -11.562 0.74 26.24 ?  106 ILE   A CB   1 
ATOM   2165 C  CB   B ILE   A 1 106 ? 19.836 -9.040  -11.446 0.26 27.12 ?  106 ILE   A CB   1 
ATOM   2166 C  CG1  A ILE   A 1 106 ? 19.018 -9.243  -10.287 0.74 27.45 ?  106 ILE   A CG1  1 
ATOM   2167 C  CG1  B ILE   A 1 106 ? 19.037 -9.078  -10.138 0.26 27.41 ?  106 ILE   A CG1  1 
ATOM   2168 C  CG2  A ILE   A 1 106 ? 19.601 -10.359 -12.444 0.74 27.23 ?  106 ILE   A CG2  1 
ATOM   2169 C  CG2  B ILE   A 1 106 ? 19.487 -10.246 -12.304 0.26 27.47 ?  106 ILE   A CG2  1 
ATOM   2170 C  CD1  A ILE   A 1 106 ? 19.102 -8.013  -9.410  0.74 27.94 ?  106 ILE   A CD1  1 
ATOM   2171 C  CD1  B ILE   A 1 106 ? 19.364 -7.947  -9.182  0.26 27.49 ?  106 ILE   A CD1  1 
ATOM   2172 H  H    A ILE   A 1 106 ? 21.681 -8.573  -13.107 0.74 29.23 ?  106 ILE   A H    1 
ATOM   2173 H  H    B ILE   A 1 106 ? 21.635 -8.655  -13.086 0.26 32.47 ?  106 ILE   A H    1 
ATOM   2174 H  HA   A ILE   A 1 106 ? 21.464 -8.370  -10.536 0.74 28.67 ?  106 ILE   A HA   1 
ATOM   2175 H  HA   B ILE   A 1 106 ? 21.508 -8.306  -10.506 0.26 31.80 ?  106 ILE   A HA   1 
ATOM   2176 H  HB   A ILE   A 1 106 ? 19.603 -8.354  -12.047 0.74 31.50 ?  106 ILE   A HB   1 
ATOM   2177 H  HB   B ILE   A 1 106 ? 19.588 -8.238  -11.931 0.26 32.55 ?  106 ILE   A HB   1 
ATOM   2178 H  HG12 A ILE   A 1 106 ? 18.089 -9.362  -10.537 0.74 32.94 ?  106 ILE   A HG12 1 
ATOM   2179 H  HG12 B ILE   A 1 106 ? 18.090 -9.019  -10.347 0.26 32.90 ?  106 ILE   A HG12 1 
ATOM   2180 H  HG13 A ILE   A 1 106 ? 19.317 -10.002 -9.763  0.74 32.94 ?  106 ILE   A HG13 1 
ATOM   2181 H  HG13 B ILE   A 1 106 ? 19.219 -9.913  -9.682  0.26 32.90 ?  106 ILE   A HG13 1 
ATOM   2182 H  HG21 A ILE   A 1 106 ? 18.713 -10.282 -12.825 0.74 32.68 ?  106 ILE   A HG21 1 
ATOM   2183 H  HG21 B ILE   A 1 106 ? 18.581 -10.146 -12.636 0.26 32.97 ?  106 ILE   A HG21 1 
ATOM   2184 H  HG22 A ILE   A 1 106 ? 20.264 -10.380 -13.150 0.74 32.68 ?  106 ILE   A HG22 1 
ATOM   2185 H  HG22 B ILE   A 1 106 ? 20.109 -10.292 -13.046 0.26 32.97 ?  106 ILE   A HG22 1 
ATOM   2186 H  HG23 A ILE   A 1 106 ? 19.663 -11.164 -11.907 0.74 32.68 ?  106 ILE   A HG23 1 
ATOM   2187 H  HG23 B ILE   A 1 106 ? 19.554 -11.050 -11.764 0.26 32.97 ?  106 ILE   A HG23 1 
ATOM   2188 H  HD11 A ILE   A 1 106 ? 18.371 -8.030  -8.774  0.74 33.54 ?  106 ILE   A HD11 1 
ATOM   2189 H  HD11 B ILE   A 1 106 ? 18.639 -7.851  -8.548  0.26 33.00 ?  106 ILE   A HD11 1 
ATOM   2190 H  HD12 A ILE   A 1 106 ? 19.950 -8.016  -8.939  0.74 33.54 ?  106 ILE   A HD12 1 
ATOM   2191 H  HD12 B ILE   A 1 106 ? 20.188 -8.159  -8.713  0.26 33.00 ?  106 ILE   A HD12 1 
ATOM   2192 H  HD13 A ILE   A 1 106 ? 19.035 -7.222  -9.969  0.74 33.54 ?  106 ILE   A HD13 1 
ATOM   2193 H  HD13 B ILE   A 1 106 ? 19.472 -7.128  -9.690  0.26 33.00 ?  106 ILE   A HD13 1 
ATOM   2194 N  N    A GLN   A 1 107 ? 22.607 -11.146 -11.416 0.74 23.70 ?  107 GLN   A N    1 
ATOM   2195 N  N    B GLN   A 1 107 ? 22.556 -11.125 -11.350 0.26 25.58 ?  107 GLN   A N    1 
ATOM   2196 C  CA   A GLN   A 1 107 ? 23.243 -12.349 -10.890 0.74 26.53 ?  107 GLN   A CA   1 
ATOM   2197 C  CA   B GLN   A 1 107 ? 23.159 -12.334 -10.803 0.26 25.65 ?  107 GLN   A CA   1 
ATOM   2198 C  C    A GLN   A 1 107 ? 24.226 -12.026 -9.775  0.74 24.37 ?  107 GLN   A C    1 
ATOM   2199 C  C    B GLN   A 1 107 ? 24.205 -12.018 -9.743  0.26 23.35 ?  107 GLN   A C    1 
ATOM   2200 O  O    A GLN   A 1 107 ? 24.484 -12.877 -8.919  0.74 26.74 ?  107 GLN   A O    1 
ATOM   2201 O  O    B GLN   A 1 107 ? 24.507 -12.878 -8.909  0.26 24.42 ?  107 GLN   A O    1 
ATOM   2202 C  CB   A GLN   A 1 107 ? 23.962 -13.104 -12.017 0.74 30.89 ?  107 GLN   A CB   1 
ATOM   2203 C  CB   B GLN   A 1 107 ? 23.772 -13.181 -11.922 0.26 27.89 ?  107 GLN   A CB   1 
ATOM   2204 C  CG   A GLN   A 1 107 ? 23.109 -13.331 -13.259 0.74 36.31 ?  107 GLN   A CG   1 
ATOM   2205 C  CG   B GLN   A 1 107 ? 22.770 -13.644 -12.969 0.26 30.38 ?  107 GLN   A CG   1 
ATOM   2206 C  CD   A GLN   A 1 107 ? 21.846 -14.117 -12.969 0.74 40.30 ?  107 GLN   A CD   1 
ATOM   2207 C  CD   B GLN   A 1 107 ? 21.657 -14.488 -12.378 0.26 32.50 ?  107 GLN   A CD   1 
ATOM   2208 O  OE1  A GLN   A 1 107 ? 21.894 -15.194 -12.371 0.74 42.32 ?  107 GLN   A OE1  1 
ATOM   2209 O  OE1  B GLN   A 1 107 ? 21.871 -15.243 -11.428 0.26 33.25 ?  107 GLN   A OE1  1 
ATOM   2210 N  NE2  A GLN   A 1 107 ? 20.705 -13.580 -13.388 0.74 41.50 ?  107 GLN   A NE2  1 
ATOM   2211 N  NE2  B GLN   A 1 107 ? 20.457 -14.359 -12.934 0.26 33.15 ?  107 GLN   A NE2  1 
ATOM   2212 H  H    A GLN   A 1 107 ? 22.735 -11.023 -12.256 0.74 28.45 ?  107 GLN   A H    1 
ATOM   2213 H  H    B GLN   A 1 107 ? 22.687 -11.009 -12.191 0.26 30.71 ?  107 GLN   A H    1 
ATOM   2214 H  HA   A GLN   A 1 107 ? 22.569 -12.942 -10.526 0.74 31.85 ?  107 GLN   A HA   1 
ATOM   2215 H  HA   B GLN   A 1 107 ? 22.469 -12.864 -10.381 0.26 30.79 ?  107 GLN   A HA   1 
ATOM   2216 H  HB2  A GLN   A 1 107 ? 24.746 -12.599 -12.287 0.74 37.08 ?  107 GLN   A HB2  1 
ATOM   2217 H  HB2  B GLN   A 1 107 ? 24.457 -12.666 -12.371 0.26 33.48 ?  107 GLN   A HB2  1 
ATOM   2218 H  HB3  A GLN   A 1 107 ? 24.237 -13.978 -11.690 0.74 37.08 ?  107 GLN   A HB3  1 
ATOM   2219 H  HB3  B GLN   A 1 107 ? 24.170 -13.972 -11.531 0.26 33.48 ?  107 GLN   A HB3  1 
ATOM   2220 H  HG2  A GLN   A 1 107 ? 22.847 -12.475 -13.631 0.74 43.58 ?  107 GLN   A HG2  1 
ATOM   2221 H  HG2  B GLN   A 1 107 ? 22.368 -12.867 -13.389 0.26 36.47 ?  107 GLN   A HG2  1 
ATOM   2222 H  HG3  A GLN   A 1 107 ? 23.627 -13.827 -13.911 0.74 43.58 ?  107 GLN   A HG3  1 
ATOM   2223 H  HG3  B GLN   A 1 107 ? 23.231 -14.179 -13.635 0.26 36.47 ?  107 GLN   A HG3  1 
ATOM   2224 H  HE21 A GLN   A 1 107 ? 20.710 -12.828 -13.804 0.74 49.80 ?  107 GLN   A HE21 1 
ATOM   2225 H  HE21 B GLN   A 1 107 ? 20.346 -13.819 -13.595 0.26 39.79 ?  107 GLN   A HE21 1 
ATOM   2226 H  HE22 A GLN   A 1 107 ? 19.961 -13.989 -13.248 0.74 49.80 ?  107 GLN   A HE22 1 
ATOM   2227 H  HE22 B GLN   A 1 107 ? 19.792 -14.814 -12.635 0.26 39.79 ?  107 GLN   A HE22 1 
ATOM   2228 N  N    . LEU   A 1 108 ? 24.753 -10.801 -9.743  1.00 19.92 ?  108 LEU   A N    1 
ATOM   2229 C  CA   . LEU   A 1 108 ? 25.680 -10.405 -8.695  1.00 17.29 ?  108 LEU   A CA   1 
ATOM   2230 C  C    . LEU   A 1 108 ? 24.990 -10.242 -7.351  1.00 15.26 ?  108 LEU   A C    1 
ATOM   2231 O  O    . LEU   A 1 108 ? 25.678 -10.084 -6.342  1.00 15.98 ?  108 LEU   A O    1 
ATOM   2232 C  CB   . LEU   A 1 108 ? 26.414 -9.111  -9.085  1.00 16.41 ?  108 LEU   A CB   1 
ATOM   2233 C  CG   . LEU   A 1 108 ? 27.415 -9.304  -10.227 1.00 18.61 ?  108 LEU   A CG   1 
ATOM   2234 C  CD1  . LEU   A 1 108 ? 27.894 -7.976  -10.791 1.00 19.83 ?  108 LEU   A CD1  1 
ATOM   2235 C  CD2  . LEU   A 1 108 ? 28.607 -10.128 -9.763  1.00 20.93 ?  108 LEU   A CD2  1 
ATOM   2236 H  H    A LEU   A 1 108 ? 24.578 -10.183 -10.310 0.74 23.91 ?  108 LEU   A H    1 
ATOM   2237 H  H    B LEU   A 1 108 ? 24.601 -10.196 -10.331 0.26 23.91 ?  108 LEU   A H    1 
ATOM   2238 H  HA   . LEU   A 1 108 ? 26.346 -11.100 -8.592  1.00 20.75 ?  108 LEU   A HA   1 
ATOM   2239 H  HB2  . LEU   A 1 108 ? 25.765 -8.450  -9.373  1.00 19.70 ?  108 LEU   A HB2  1 
ATOM   2240 H  HB3  . LEU   A 1 108 ? 26.904 -8.778  -8.316  1.00 19.70 ?  108 LEU   A HB3  1 
ATOM   2241 H  HG   . LEU   A 1 108 ? 26.984 -9.794  -10.946 1.00 22.34 ?  108 LEU   A HG   1 
ATOM   2242 H  HD11 . LEU   A 1 108 ? 28.501 -8.144  -11.532 1.00 23.81 ?  108 LEU   A HD11 1 
ATOM   2243 H  HD12 . LEU   A 1 108 ? 27.128 -7.470  -11.101 1.00 23.81 ?  108 LEU   A HD12 1 
ATOM   2244 H  HD13 . LEU   A 1 108 ? 28.356 -7.484  -10.093 1.00 23.81 ?  108 LEU   A HD13 1 
ATOM   2245 H  HD21 . LEU   A 1 108 ? 29.298 -10.092 -10.441 1.00 25.12 ?  108 LEU   A HD21 1 
ATOM   2246 H  HD22 . LEU   A 1 108 ? 28.938 -9.756  -8.931  1.00 25.12 ?  108 LEU   A HD22 1 
ATOM   2247 H  HD23 . LEU   A 1 108 ? 28.323 -11.045 -9.626  1.00 25.12 ?  108 LEU   A HD23 1 
ATOM   2248 N  N    . LEU   A 1 109 ? 23.656 -10.310 -7.306  1.00 14.24 ?  109 LEU   A N    1 
ATOM   2249 C  CA   . LEU   A 1 109 ? 22.968 -10.172 -6.034  1.00 13.84 ?  109 LEU   A CA   1 
ATOM   2250 C  C    . LEU   A 1 109 ? 23.316 -11.325 -5.099  1.00 13.22 ?  109 LEU   A C    1 
ATOM   2251 O  O    . LEU   A 1 109 ? 23.469 -11.130 -3.890  1.00 13.26 ?  109 LEU   A O    1 
ATOM   2252 C  CB   . LEU   A 1 109 ? 21.460 -10.084 -6.276  1.00 14.46 ?  109 LEU   A CB   1 
ATOM   2253 C  CG   . LEU   A 1 109 ? 20.580 -9.790  -5.067  1.00 14.82 ?  109 LEU   A CG   1 
ATOM   2254 C  CD1  . LEU   A 1 109 ? 21.036 -8.538  -4.345  1.00 14.88 ?  109 LEU   A CD1  1 
ATOM   2255 C  CD2  . LEU   A 1 109 ? 19.111 -9.664  -5.495  1.00 15.81 ?  109 LEU   A CD2  1 
ATOM   2256 H  H    . LEU   A 1 109 ? 23.143 -10.432 -7.983  1.00 17.10 ?  109 LEU   A H    1 
ATOM   2257 H  HA   . LEU   A 1 109 ? 23.258 -9.350  -5.610  1.00 16.62 ?  109 LEU   A HA   1 
ATOM   2258 H  HB2  . LEU   A 1 109 ? 21.302 -9.377  -6.919  1.00 17.36 ?  109 LEU   A HB2  1 
ATOM   2259 H  HB3  . LEU   A 1 109 ? 21.163 -10.927 -6.644  1.00 17.36 ?  109 LEU   A HB3  1 
ATOM   2260 H  HG   . LEU   A 1 109 ? 20.641 -10.530 -4.446  1.00 17.79 ?  109 LEU   A HG   1 
ATOM   2261 H  HD11 . LEU   A 1 109 ? 20.371 -8.290  -3.684  1.00 17.87 ?  109 LEU   A HD11 1 
ATOM   2262 H  HD12 . LEU   A 1 109 ? 21.885 -8.714  -3.909  1.00 17.87 ?  109 LEU   A HD12 1 
ATOM   2263 H  HD13 . LEU   A 1 109 ? 21.140 -7.818  -4.991  1.00 17.87 ?  109 LEU   A HD13 1 
ATOM   2264 H  HD21 . LEU   A 1 109 ? 18.579 -9.370  -4.734  1.00 18.98 ?  109 LEU   A HD21 1 
ATOM   2265 H  HD22 . LEU   A 1 109 ? 19.038 -9.014  -6.212  1.00 18.98 ?  109 LEU   A HD22 1 
ATOM   2266 H  HD23 . LEU   A 1 109 ? 18.790 -10.529 -5.802  1.00 18.98 ?  109 LEU   A HD23 1 
ATOM   2267 N  N    . LYS   A 1 110 ? 23.457 -12.537 -5.640  1.00 13.18 ?  110 LYS   A N    1 
ATOM   2268 C  CA   . LYS   A 1 110 ? 23.834 -13.657 -4.781  1.00 13.67 ?  110 LYS   A CA   1 
ATOM   2269 C  C    . LYS   A 1 110 ? 25.228 -13.450 -4.186  1.00 12.72 ?  110 LYS   A C    1 
ATOM   2270 O  O    . LYS   A 1 110 ? 25.434 -13.653 -2.988  1.00 12.16 ?  110 LYS   A O    1 
ATOM   2271 C  CB   . LYS   A 1 110 ? 23.724 -14.984 -5.538  1.00 14.60 ?  110 LYS   A CB   1 
ATOM   2272 C  CG   . LYS   A 1 110 ? 23.953 -16.200 -4.635  1.00 14.63 ?  110 LYS   A CG   1 
ATOM   2273 C  CD   . LYS   A 1 110 ? 23.720 -17.528 -5.348  1.00 15.31 ?  110 LYS   A CD   1 
ATOM   2274 C  CE   . LYS   A 1 110 ? 23.837 -18.713 -4.392  1.00 16.33 ?  110 LYS   A CE   1 
ATOM   2275 N  NZ   . LYS   A 1 110 ? 22.659 -18.816 -3.480  1.00 16.57 ?  110 LYS   A NZ   1 
ATOM   2276 H  H    . LYS   A 1 110 ? 23.349 -12.732 -6.468  1.00 15.82 ?  110 LYS   A H    1 
ATOM   2277 H  HA   . LYS   A 1 110 ? 23.210 -13.697 -4.040  1.00 16.42 ?  110 LYS   A HA   1 
ATOM   2278 H  HB2  . LYS   A 1 110 ? 22.831 -15.056 -5.916  1.00 17.53 ?  110 LYS   A HB2  1 
ATOM   2279 H  HB3  . LYS   A 1 110 ? 24.386 -15.004 -6.243  1.00 17.53 ?  110 LYS   A HB3  1 
ATOM   2280 H  HG2  . LYS   A 1 110 ? 24.869 -16.186 -4.316  1.00 17.56 ?  110 LYS   A HG2  1 
ATOM   2281 H  HG3  . LYS   A 1 110 ? 23.341 -16.151 -3.882  1.00 17.56 ?  110 LYS   A HG3  1 
ATOM   2282 H  HD2  . LYS   A 1 110 ? 22.827 -17.535 -5.727  1.00 18.38 ?  110 LYS   A HD2  1 
ATOM   2283 H  HD3  . LYS   A 1 110 ? 24.383 -17.634 -6.048  1.00 18.38 ?  110 LYS   A HD3  1 
ATOM   2284 H  HE2  . LYS   A 1 110 ? 23.900 -19.532 -4.906  1.00 19.61 ?  110 LYS   A HE2  1 
ATOM   2285 H  HE3  . LYS   A 1 110 ? 24.637 -18.600 -3.847  1.00 19.61 ?  110 LYS   A HE3  1 
ATOM   2286 H  HZ1  . LYS   A 1 110 ? 22.756 -19.510 -2.934  1.00 19.89 ?  110 LYS   A HZ1  1 
ATOM   2287 H  HZ2  . LYS   A 1 110 ? 22.587 -18.072 -2.993  1.00 19.89 ?  110 LYS   A HZ2  1 
ATOM   2288 H  HZ3  . LYS   A 1 110 ? 21.916 -18.920 -3.957  1.00 19.89 ?  110 LYS   A HZ3  1 
ATOM   2289 N  N    . SER   A 1 111 ? 26.185 -13.002 -5.003  1.00 12.95 ?  111 SER   A N    1 
ATOM   2290 C  CA   . SER   A 1 111 ? 27.518 -12.696 -4.488  1.00 12.98 ?  111 SER   A CA   1 
ATOM   2291 C  C    . SER   A 1 111 ? 27.458 -11.650 -3.383  1.00 12.39 ?  111 SER   A C    1 
ATOM   2292 O  O    . SER   A 1 111 ? 28.143 -11.767 -2.366  1.00 12.87 ?  111 SER   A O    1 
ATOM   2293 C  CB   . SER   A 1 111 ? 28.410 -12.214 -5.626  1.00 14.45 ?  111 SER   A CB   1 
ATOM   2294 O  OG   . SER   A 1 111 ? 28.487 -13.192 -6.647  1.00 16.32 ?  111 SER   A OG   1 
ATOM   2295 H  H    . SER   A 1 111 ? 26.088 -12.873 -5.848  1.00 15.55 ?  111 SER   A H    1 
ATOM   2296 H  HA   . SER   A 1 111 ? 27.912 -13.505 -4.124  1.00 15.59 ?  111 SER   A HA   1 
ATOM   2297 H  HB2  . SER   A 1 111 ? 28.034 -11.404 -6.004  1.00 17.35 ?  111 SER   A HB2  1 
ATOM   2298 H  HB3  . SER   A 1 111 ? 29.300 -12.033 -5.277  1.00 17.35 ?  111 SER   A HB3  1 
ATOM   2299 H  HG   . SER   A 1 111 ? 29.002 -12.918 -7.263  1.00 19.60 ?  111 SER   A HG   1 
ATOM   2300 N  N    . ALA   A 1 112 ? 26.610 -10.636 -3.552  1.00 12.88 ?  112 ALA   A N    1 
ATOM   2301 C  CA   . ALA   A 1 112 ? 26.470 -9.604  -2.529  1.00 12.05 ?  112 ALA   A CA   1 
ATOM   2302 C  C    . ALA   A 1 112 ? 25.993 -10.194 -1.206  1.00 11.66 ?  112 ALA   A C    1 
ATOM   2303 O  O    . ALA   A 1 112 ? 26.547 -9.898  -0.141  1.00 12.10 ?  112 ALA   A O    1 
ATOM   2304 C  CB   . ALA   A 1 112 ? 25.507 -8.521  -3.022  1.00 12.96 ?  112 ALA   A CB   1 
ATOM   2305 H  H    . ALA   A 1 112 ? 26.115 -10.520 -4.245  1.00 15.46 ?  112 ALA   A H    1 
ATOM   2306 H  HA   . ALA   A 1 112 ? 27.330 -9.185  -2.378  1.00 14.47 ?  112 ALA   A HA   1 
ATOM   2307 H  HB1  . ALA   A 1 112 ? 25.419 -7.837  -2.335  1.00 15.56 ?  112 ALA   A HB1  1 
ATOM   2308 H  HB2  . ALA   A 1 112 ? 25.856 -8.127  -3.834  1.00 15.56 ?  112 ALA   A HB2  1 
ATOM   2309 H  HB3  . ALA   A 1 112 ? 24.638 -8.921  -3.194  1.00 15.56 ?  112 ALA   A HB3  1 
ATOM   2310 N  N    . TYR   A 1 113 ? 24.955 -11.035 -1.250  1.00 12.26 ?  113 TYR   A N    1 
ATOM   2311 C  CA   . TYR   A 1 113 ? 24.447 -11.653 -0.026  1.00 11.57 ?  113 TYR   A CA   1 
ATOM   2312 C  C    . TYR   A 1 113 ? 25.442 -12.612 0.618   1.00 11.77 ?  113 TYR   A C    1 
ATOM   2313 O  O    . TYR   A 1 113 ? 25.408 -12.799 1.838   1.00 12.53 ?  113 TYR   A O    1 
ATOM   2314 C  CB   . TYR   A 1 113 ? 23.126 -12.371 -0.304  1.00 12.86 ?  113 TYR   A CB   1 
ATOM   2315 C  CG   . TYR   A 1 113 ? 21.905 -11.485 -0.205  1.00 11.94 ?  113 TYR   A CG   1 
ATOM   2316 C  CD1  . TYR   A 1 113 ? 21.551 -10.893 1.001   1.00 12.81 ?  113 TYR   A CD1  1 
ATOM   2317 C  CD2  . TYR   A 1 113 ? 21.089 -11.244 -1.310  1.00 12.78 ?  113 TYR   A CD2  1 
ATOM   2318 C  CE1  . TYR   A 1 113 ? 20.425 -10.105 1.112   1.00 12.86 ?  113 TYR   A CE1  1 
ATOM   2319 C  CE2  . TYR   A 1 113 ? 19.947 -10.433 -1.210  1.00 12.77 ?  113 TYR   A CE2  1 
ATOM   2320 C  CZ   . TYR   A 1 113 ? 19.623 -9.869  0.006   1.00 12.62 ?  113 TYR   A CZ   1 
ATOM   2321 O  OH   . TYR   A 1 113 ? 18.504 -9.073  0.148   1.00 13.68 ?  113 TYR   A OH   1 
ATOM   2322 H  H    . TYR   A 1 113 ? 24.531 -11.258 -1.967  1.00 14.72 ?  113 TYR   A H    1 
ATOM   2323 H  HA   . TYR   A 1 113 ? 24.270 -10.949 0.617   1.00 13.90 ?  113 TYR   A HA   1 
ATOM   2324 H  HB2  . TYR   A 1 113 ? 23.148 -12.733 -1.202  1.00 15.44 ?  113 TYR   A HB2  1 
ATOM   2325 H  HB3  . TYR   A 1 113 ? 23.022 -13.090 0.338   1.00 15.44 ?  113 TYR   A HB3  1 
ATOM   2326 H  HD1  . TYR   A 1 113 ? 22.083 -11.054 1.755   1.00 15.37 ?  113 TYR   A HD1  1 
ATOM   2327 H  HD2  . TYR   A 1 113 ? 21.302 -11.630 -2.124  1.00 15.34 ?  113 TYR   A HD2  1 
ATOM   2328 H  HE1  . TYR   A 1 113 ? 20.212 -9.718  1.934   1.00 15.45 ?  113 TYR   A HE1  1 
ATOM   2329 H  HE2  . TYR   A 1 113 ? 19.411 -10.282 -1.955  1.00 15.33 ?  113 TYR   A HE2  1 
ATOM   2330 H  HH   . TYR   A 1 113 ? 18.110 -9.002  -0.597  1.00 16.43 ?  113 TYR   A HH   1 
ATOM   2331 N  N    . GLU   A 1 114 ? 26.340 -13.223 -0.166  1.00 11.68 ?  114 GLU   A N    1 
ATOM   2332 C  CA   . GLU   A 1 114 ? 27.346 -14.110 0.427   1.00 11.49 ?  114 GLU   A CA   1 
ATOM   2333 C  C    . GLU   A 1 114 ? 28.198 -13.398 1.481   1.00 11.53 ?  114 GLU   A C    1 
ATOM   2334 O  O    . GLU   A 1 114 ? 28.688 -14.038 2.427   1.00 12.27 ?  114 GLU   A O    1 
ATOM   2335 C  CB   . GLU   A 1 114 ? 28.202 -14.760 -0.665  1.00 11.59 ?  114 GLU   A CB   1 
ATOM   2336 C  CG   . GLU   A 1 114 ? 27.435 -15.794 -1.462  1.00 12.25 ?  114 GLU   A CG   1 
ATOM   2337 C  CD   . GLU   A 1 114 ? 28.159 -16.331 -2.689  1.00 12.81 ?  114 GLU   A CD   1 
ATOM   2338 O  OE1  . GLU   A 1 114 ? 29.119 -15.700 -3.181  1.00 13.51 ?  114 GLU   A OE1  1 
ATOM   2339 O  OE2  . GLU   A 1 114 ? 27.723 -17.395 -3.177  1.00 14.22 -1 114 GLU   A OE2  1 
ATOM   2340 H  H    . GLU   A 1 114 ? 26.388 -13.138 -1.029  1.00 14.03 ?  114 GLU   A H    1 
ATOM   2341 H  HA   . GLU   A 1 114 ? 26.880 -14.824 0.875   1.00 13.79 ?  114 GLU   A HA   1 
ATOM   2342 H  HB2  . GLU   A 1 114 ? 28.516 -14.077 -1.284  1.00 13.92 ?  114 GLU   A HB2  1 
ATOM   2343 H  HB3  . GLU   A 1 114 ? 28.963 -15.203 -0.255  1.00 13.92 ?  114 GLU   A HB3  1 
ATOM   2344 H  HG2  . GLU   A 1 114 ? 27.249 -16.553 -0.891  1.00 14.71 ?  114 GLU   A HG2  1 
ATOM   2345 H  HG3  . GLU   A 1 114 ? 26.602 -15.402 -1.765  1.00 14.71 ?  114 GLU   A HG3  1 
ATOM   2346 N  N    . ASN   A 1 115 ? 28.397 -12.081 1.348   1.00 11.44 ?  115 ASN   A N    1 
ATOM   2347 C  CA   . ASN   A 1 115 ? 29.147 -11.352 2.365   1.00 12.15 ?  115 ASN   A CA   1 
ATOM   2348 C  C    . ASN   A 1 115 ? 28.520 -11.502 3.746   1.00 11.62 ?  115 ASN   A C    1 
ATOM   2349 O  O    . ASN   A 1 115 ? 29.224 -11.423 4.758   1.00 12.48 ?  115 ASN   A O    1 
ATOM   2350 C  CB   . ASN   A 1 115 ? 29.260 -9.875  1.991   1.00 12.22 ?  115 ASN   A CB   1 
ATOM   2351 C  CG   . ASN   A 1 115 ? 30.055 -9.663  0.724   1.00 13.27 ?  115 ASN   A CG   1 
ATOM   2352 O  OD1  . ASN   A 1 115 ? 31.277 -9.807  0.719   1.00 16.13 ?  115 ASN   A OD1  1 
ATOM   2353 N  ND2  . ASN   A 1 115 ? 29.374 -9.339  -0.360  1.00 12.57 ?  115 ASN   A ND2  1 
ATOM   2354 H  H    . ASN   A 1 115 ? 28.103 -11.592 0.699   1.00 13.73 ?  115 ASN   A H    1 
ATOM   2355 H  HA   . ASN   A 1 115 ? 30.040 -11.720 2.410   1.00 14.59 ?  115 ASN   A HA   1 
ATOM   2356 H  HB2  . ASN   A 1 115 ? 28.371 -9.514  1.865   1.00 14.68 ?  115 ASN   A HB2  1 
ATOM   2357 H  HB3  . ASN   A 1 115 ? 29.711 -9.406  2.714   1.00 14.68 ?  115 ASN   A HB3  1 
ATOM   2358 H  HD21 . ASN   A 1 115 ? 29.788 -9.212  -1.099  1.00 15.10 ?  115 ASN   A HD21 1 
ATOM   2359 H  HD22 . ASN   A 1 115 ? 28.518 -9.260  -0.323  1.00 15.10 ?  115 ASN   A HD22 1 
ATOM   2360 N  N    . PHE   A 1 116 ? 27.193 -11.668 3.820   1.00 11.97 ?  116 PHE   A N    1 
ATOM   2361 C  CA   . PHE   A 1 116 ? 26.545 -11.753 5.127   1.00 11.82 ?  116 PHE   A CA   1 
ATOM   2362 C  C    . PHE   A 1 116 ? 27.027 -12.985 5.901   1.00 12.64 ?  116 PHE   A C    1 
ATOM   2363 O  O    . PHE   A 1 116 ? 26.956 -13.021 7.134   1.00 12.60 ?  116 PHE   A O    1 
ATOM   2364 C  CB   . PHE   A 1 116 ? 25.016 -11.885 4.993   1.00 12.26 ?  116 PHE   A CB   1 
ATOM   2365 C  CG   . PHE   A 1 116 ? 24.259 -10.634 4.536   1.00 11.42 ?  116 PHE   A CG   1 
ATOM   2366 C  CD1  . PHE   A 1 116 ? 24.845 -9.632  3.783   1.00 11.74 ?  116 PHE   A CD1  1 
ATOM   2367 C  CD2  . PHE   A 1 116 ? 22.905 -10.522 4.858   1.00 12.26 ?  116 PHE   A CD2  1 
ATOM   2368 C  CE1  . PHE   A 1 116 ? 24.076 -8.539  3.373   1.00 12.09 ?  116 PHE   A CE1  1 
ATOM   2369 C  CE2  . PHE   A 1 116 ? 22.144 -9.437  4.461   1.00 12.64 ?  116 PHE   A CE2  1 
ATOM   2370 C  CZ   . PHE   A 1 116 ? 22.719 -8.442  3.713   1.00 12.39 ?  116 PHE   A CZ   1 
ATOM   2371 H  H    . PHE   A 1 116 ? 26.659 -11.726 3.149   1.00 14.37 ?  116 PHE   A H    1 
ATOM   2372 H  HA   . PHE   A 1 116 ? 26.738 -10.962 5.653   1.00 14.19 ?  116 PHE   A HA   1 
ATOM   2373 H  HB2  . PHE   A 1 116 ? 24.824 -12.585 4.352   1.00 14.73 ?  116 PHE   A HB2  1 
ATOM   2374 H  HB3  . PHE   A 1 116 ? 24.652 -12.138 5.860   1.00 14.73 ?  116 PHE   A HB3  1 
ATOM   2375 H  HD1  . PHE   A 1 116 ? 25.740 -9.695  3.544   1.00 14.10 ?  116 PHE   A HD1  1 
ATOM   2376 H  HD2  . PHE   A 1 116 ? 22.503 -11.198 5.364   1.00 14.72 ?  116 PHE   A HD2  1 
ATOM   2377 H  HE1  . PHE   A 1 116 ? 24.472 -7.866  2.869   1.00 14.51 ?  116 PHE   A HE1  1 
ATOM   2378 H  HE2  . PHE   A 1 116 ? 21.241 -9.389  4.700   1.00 15.17 ?  116 PHE   A HE2  1 
ATOM   2379 H  HZ   . PHE   A 1 116 ? 22.214 -7.707  3.448   1.00 14.87 ?  116 PHE   A HZ   1 
ATOM   2380 N  N    . ASN   A 1 117 ? 27.476 -14.020 5.190   1.00 12.51 ?  117 ASN   A N    1 
ATOM   2381 C  CA   . ASN   A 1 117 ? 27.840 -15.272 5.847   1.00 13.62 ?  117 ASN   A CA   1 
ATOM   2382 C  C    . ASN   A 1 117 ? 29.103 -15.158 6.678   1.00 13.57 ?  117 ASN   A C    1 
ATOM   2383 O  O    . ASN   A 1 117 ? 29.410 -16.084 7.436   1.00 14.45 ?  117 ASN   A O    1 
ATOM   2384 C  CB   . ASN   A 1 117 ? 27.949 -16.396 4.817   1.00 13.64 ?  117 ASN   A CB   1 
ATOM   2385 C  CG   . ASN   A 1 117 ? 26.592 -16.808 4.298   1.00 13.89 ?  117 ASN   A CG   1 
ATOM   2386 O  OD1  . ASN   A 1 117 ? 25.624 -16.824 5.056   1.00 14.21 ?  117 ASN   A OD1  1 
ATOM   2387 N  ND2  . ASN   A 1 117 ? 26.504 -17.087 3.013   1.00 13.38 ?  117 ASN   A ND2  1 
ATOM   2388 H  H    . ASN   A 1 117 ? 27.558 -14.020 4.329   1.00 15.02 ?  117 ASN   A H    1 
ATOM   2389 H  HA   . ASN   A 1 117 ? 27.117 -15.508 6.448   1.00 16.35 ?  117 ASN   A HA   1 
ATOM   2390 H  HB2  . ASN   A 1 117 ? 28.482 -16.097 4.063   1.00 16.38 ?  117 ASN   A HB2  1 
ATOM   2391 H  HB3  . ASN   A 1 117 ? 28.359 -17.169 5.232   1.00 16.38 ?  117 ASN   A HB3  1 
ATOM   2392 H  HD21 . ASN   A 1 117 ? 25.745 -17.315 2.673   1.00 16.06 ?  117 ASN   A HD21 1 
ATOM   2393 H  HD22 . ASN   A 1 117 ? 27.202 -17.050 2.511   1.00 16.06 ?  117 ASN   A HD22 1 
ATOM   2394 N  N    . GLN   A 1 118 ? 29.827 -14.051 6.560   1.00 13.31 ?  118 GLN   A N    1 
ATOM   2395 C  CA   . GLN   A 1 118 ? 31.007 -13.827 7.379   1.00 13.80 ?  118 GLN   A CA   1 
ATOM   2396 C  C    . GLN   A 1 118 ? 30.657 -13.264 8.750   1.00 13.03 ?  118 GLN   A C    1 
ATOM   2397 O  O    . GLN   A 1 118 ? 31.567 -12.993 9.541   1.00 15.62 ?  118 GLN   A O    1 
ATOM   2398 C  CB   . GLN   A 1 118 ? 31.989 -12.918 6.639   1.00 14.13 ?  118 GLN   A CB   1 
ATOM   2399 C  CG   . GLN   A 1 118 ? 32.504 -13.490 5.326   1.00 13.92 ?  118 GLN   A CG   1 
ATOM   2400 C  CD   . GLN   A 1 118 ? 33.310 -14.763 5.506   1.00 14.40 ?  118 GLN   A CD   1 
ATOM   2401 O  OE1  . GLN   A 1 118 ? 34.151 -14.850 6.400   1.00 15.01 ?  118 GLN   A OE1  1 
ATOM   2402 N  NE2  . GLN   A 1 118 ? 33.026 -15.772 4.671   1.00 14.97 ?  118 GLN   A NE2  1 
ATOM   2403 H  H    . GLN   A 1 118 ? 29.647 -13.407 6.012   1.00 15.98 ?  118 GLN   A H    1 
ATOM   2404 H  HA   . GLN   A 1 118 ? 31.440 -14.685 7.513   1.00 16.57 ?  118 GLN   A HA   1 
ATOM   2405 H  HB2  . GLN   A 1 118 ? 31.544 -12.078 6.444   1.00 16.96 ?  118 GLN   A HB2  1 
ATOM   2406 H  HB3  . GLN   A 1 118 ? 32.750 -12.759 7.217   1.00 16.96 ?  118 GLN   A HB3  1 
ATOM   2407 H  HG2  . GLN   A 1 118 ? 31.753 -13.687 4.746   1.00 16.71 ?  118 GLN   A HG2  1 
ATOM   2408 H  HG3  . GLN   A 1 118 ? 33.083 -12.832 4.903   1.00 16.71 ?  118 GLN   A HG3  1 
ATOM   2409 H  HE21 . GLN   A 1 118 ? 32.425 -15.672 4.060   1.00 17.97 ?  118 GLN   A HE21 1 
ATOM   2410 H  HE22 . GLN   A 1 118 ? 33.449 -16.518 4.734   1.00 17.97 ?  118 GLN   A HE22 1 
ATOM   2411 N  N    . HIS   A 1 119 ? 29.365 -13.101 9.058   1.00 13.03 ?  119 HIS   A N    1 
ATOM   2412 C  CA   . HIS   A 1 119 ? 28.913 -12.504 10.311  1.00 14.26 ?  119 HIS   A CA   1 
ATOM   2413 C  C    . HIS   A 1 119 ? 27.772 -13.319 10.895  1.00 14.93 ?  119 HIS   A C    1 
ATOM   2414 O  O    . HIS   A 1 119 ? 26.815 -13.646 10.188  1.00 15.57 ?  119 HIS   A O    1 
ATOM   2415 C  CB   . HIS   A 1 119 ? 28.480 -11.056 10.075  1.00 14.38 ?  119 HIS   A CB   1 
ATOM   2416 C  CG   . HIS   A 1 119 ? 29.573 -10.238 9.482   1.00 15.83 ?  119 HIS   A CG   1 
ATOM   2417 N  ND1  . HIS   A 1 119 ? 30.539 -9.626  10.249  1.00 18.87 ?  119 HIS   A ND1  1 
ATOM   2418 C  CD2  . HIS   A 1 119 ? 29.915 -10.021 8.192   1.00 16.47 ?  119 HIS   A CD2  1 
ATOM   2419 C  CE1  . HIS   A 1 119 ? 31.412 -9.033  9.455   1.00 19.04 ?  119 HIS   A CE1  1 
ATOM   2420 N  NE2  . HIS   A 1 119 ? 31.068 -9.275  8.202   1.00 18.64 ?  119 HIS   A NE2  1 
ATOM   2421 H  H    . HIS   A 1 119 ? 28.712 -13.342 8.543   1.00 15.65 ?  119 HIS   A H    1 
ATOM   2422 H  HA   . HIS   A 1 119 ? 29.645 -12.510 10.945  1.00 17.11 ?  119 HIS   A HA   1 
ATOM   2423 H  HB2  . HIS   A 1 119 ? 27.725 -11.049 9.466   1.00 17.27 ?  119 HIS   A HB2  1 
ATOM   2424 H  HB3  . HIS   A 1 119 ? 28.227 -10.664 10.926  1.00 17.27 ?  119 HIS   A HB3  1 
ATOM   2425 H  HD1  . HIS   A 1 119 ? 30.560 -9.625  11.112  1.00 22.66 ?  119 HIS   A HD1  1 
ATOM   2426 H  HD2  . HIS   A 1 119 ? 29.465 -10.333 7.443   1.00 19.77 ?  119 HIS   A HD2  1 
ATOM   2427 H  HE1  . HIS   A 1 119 ? 32.143 -8.533  9.736   1.00 22.86 ?  119 HIS   A HE1  1 
ATOM   2428 N  N    . GLU   A 1 120 ? 27.880 -13.638 12.186  1.00 15.69 ?  120 GLU   A N    1 
ATOM   2429 C  CA   . GLU   A 1 120 ? 26.939 -14.574 12.794  1.00 17.36 ?  120 GLU   A CA   1 
ATOM   2430 C  C    . GLU   A 1 120 ? 25.522 -14.010 12.858  1.00 15.81 ?  120 GLU   A C    1 
ATOM   2431 O  O    . GLU   A 1 120 ? 24.545 -14.764 12.728  1.00 15.78 ?  120 GLU   A O    1 
ATOM   2432 C  CB   . GLU   A 1 120 ? 27.432 -14.987 14.183  1.00 23.53 ?  120 GLU   A CB   1 
ATOM   2433 C  CG   . GLU   A 1 120 ? 28.595 -15.968 14.160  1.00 32.44 ?  120 GLU   A CG   1 
ATOM   2434 C  CD   . GLU   A 1 120 ? 28.784 -16.671 15.490  1.00 41.85 ?  120 GLU   A CD   1 
ATOM   2435 O  OE1  . GLU   A 1 120 ? 28.365 -16.112 16.528  1.00 43.68 ?  120 GLU   A OE1  1 
ATOM   2436 O  OE2  . GLU   A 1 120 ? 29.349 -17.785 15.499  1.00 48.88 -1 120 GLU   A OE2  1 
ATOM   2437 H  H    . GLU   A 1 120 ? 28.490 -13.339 12.720  1.00 18.83 ?  120 GLU   A H    1 
ATOM   2438 H  HA   . GLU   A 1 120 ? 26.910 -15.377 12.255  1.00 20.84 ?  120 GLU   A HA   1 
ATOM   2439 H  HB2  . GLU   A 1 120 ? 27.730 -14.200 14.665  1.00 28.24 ?  120 GLU   A HB2  1 
ATOM   2440 H  HB3  . GLU   A 1 120 ? 26.705 -15.412 14.665  1.00 28.24 ?  120 GLU   A HB3  1 
ATOM   2441 H  HG2  . GLU   A 1 120 ? 28.436 -16.634 13.470  1.00 38.94 ?  120 GLU   A HG2  1 
ATOM   2442 H  HG3  . GLU   A 1 120 ? 29.416 -15.488 13.974  1.00 38.94 ?  120 GLU   A HG3  1 
ATOM   2443 N  N    . VAL   A 1 121 ? 25.388 -12.701 13.084  1.00 15.37 ?  121 VAL   A N    1 
ATOM   2444 C  CA   . VAL   A 1 121 ? 24.091 -12.039 13.202  1.00 15.35 ?  121 VAL   A CA   1 
ATOM   2445 C  C    . VAL   A 1 121 ? 24.193 -10.657 12.569  1.00 14.01 ?  121 VAL   A C    1 
ATOM   2446 O  O    . VAL   A 1 121 ? 25.165 -9.934  12.809  1.00 14.72 ?  121 VAL   A O    1 
ATOM   2447 C  CB   . VAL   A 1 121 ? 23.657 -11.891 14.679  1.00 18.48 ?  121 VAL   A CB   1 
ATOM   2448 C  CG1  . VAL   A 1 121 ? 22.306 -11.194 14.778  1.00 18.91 ?  121 VAL   A CG1  1 
ATOM   2449 C  CG2  . VAL   A 1 121 ? 23.617 -13.229 15.390  1.00 21.13 ?  121 VAL   A CG2  1 
ATOM   2450 H  H    . VAL   A 1 121 ? 26.056 -12.163 13.186  1.00 18.45 ?  121 VAL   A H    1 
ATOM   2451 H  HA   . VAL   A 1 121 ? 23.422 -12.558 12.732  1.00 18.43 ?  121 VAL   A HA   1 
ATOM   2452 H  HB   . VAL   A 1 121 ? 24.303 -11.336 15.139  1.00 22.19 ?  121 VAL   A HB   1 
ATOM   2453 H  HG11 . VAL   A 1 121 ? 21.967 -11.287 15.683  1.00 22.70 ?  121 VAL   A HG11 1 
ATOM   2454 H  HG12 . VAL   A 1 121 ? 22.415 -10.253 14.564  1.00 22.70 ?  121 VAL   A HG12 1 
ATOM   2455 H  HG13 . VAL   A 1 121 ? 21.689 -11.607 14.152  1.00 22.70 ?  121 VAL   A HG13 1 
ATOM   2456 H  HG21 . VAL   A 1 121 ? 23.280 -13.097 16.295  1.00 25.36 ?  121 VAL   A HG21 1 
ATOM   2457 H  HG22 . VAL   A 1 121 ? 23.020 -13.827 14.908  1.00 25.36 ?  121 VAL   A HG22 1 
ATOM   2458 H  HG23 . VAL   A 1 121 ? 24.507 -13.602 15.421  1.00 25.36 ?  121 VAL   A HG23 1 
ATOM   2459 N  N    . LEU   A 1 122 ? 23.179 -10.265 11.793  1.00 13.66 ?  122 LEU   A N    1 
ATOM   2460 C  CA   . LEU   A 1 122 ? 23.181 -8.964  11.129  1.00 13.95 ?  122 LEU   A CA   1 
ATOM   2461 C  C    . LEU   A 1 122 ? 21.784 -8.366  11.099  1.00 13.08 ?  122 LEU   A C    1 
ATOM   2462 O  O    . LEU   A 1 122 ? 20.794 -9.085  10.937  1.00 14.54 ?  122 LEU   A O    1 
ATOM   2463 C  CB   . LEU   A 1 122 ? 23.610 -9.061  9.661   1.00 14.96 ?  122 LEU   A CB   1 
ATOM   2464 C  CG   . LEU   A 1 122 ? 24.817 -9.904  9.283   1.00 14.78 ?  122 LEU   A CG   1 
ATOM   2465 C  CD1  . LEU   A 1 122 ? 24.403 -11.348 9.052   1.00 15.73 ?  122 LEU   A CD1  1 
ATOM   2466 C  CD2  . LEU   A 1 122 ? 25.468 -9.305  8.045   1.00 14.23 ?  122 LEU   A CD2  1 
ATOM   2467 H  H    . LEU   A 1 122 ? 22.477 -10.742 11.629  1.00 16.41 ?  122 LEU   A H    1 
ATOM   2468 H  HA   . LEU   A 1 122 ? 23.777 -8.355  11.595  1.00 16.75 ?  122 LEU   A HA   1 
ATOM   2469 H  HB2  . LEU   A 1 122 ? 22.869 -9.417  9.158   1.00 17.96 ?  122 LEU   A HB2  1 
ATOM   2470 H  HB3  . LEU   A 1 122 ? 23.799 -8.160  9.351   1.00 17.96 ?  122 LEU   A HB3  1 
ATOM   2471 H  HG   . LEU   A 1 122 ? 25.477 -9.877  9.997   1.00 17.74 ?  122 LEU   A HG   1 
ATOM   2472 H  HD11 . LEU   A 1 122 ? 25.179 -11.862 8.777   1.00 18.88 ?  122 LEU   A HD11 1 
ATOM   2473 H  HD12 . LEU   A 1 122 ? 24.045 -11.706 9.877   1.00 18.88 ?  122 LEU   A HD12 1 
ATOM   2474 H  HD13 . LEU   A 1 122 ? 23.727 -11.374 8.356   1.00 18.88 ?  122 LEU   A HD13 1 
ATOM   2475 H  HD21 . LEU   A 1 122 ? 26.204 -9.871  7.760   1.00 17.09 ?  122 LEU   A HD21 1 
ATOM   2476 H  HD22 . LEU   A 1 122 ? 24.806 -9.248  7.335   1.00 17.09 ?  122 LEU   A HD22 1 
ATOM   2477 H  HD23 . LEU   A 1 122 ? 25.801 -8.415  8.252   1.00 17.09 ?  122 LEU   A HD23 1 
ATOM   2478 N  N    . LEU   A 1 123 ? 21.724 -7.035  11.207  1.00 12.92 ?  123 LEU   A N    1 
ATOM   2479 C  CA   . LEU   A 1 123 ? 20.557 -6.234  10.836  1.00 13.03 ?  123 LEU   A CA   1 
ATOM   2480 C  C    . LEU   A 1 123 ? 20.793 -5.701  9.433   1.00 12.40 ?  123 LEU   A C    1 
ATOM   2481 O  O    . LEU   A 1 123 ? 21.845 -5.107  9.180   1.00 12.89 ?  123 LEU   A O    1 
ATOM   2482 C  CB   . LEU   A 1 123 ? 20.398 -5.056  11.802  1.00 13.50 ?  123 LEU   A CB   1 
ATOM   2483 C  CG   . LEU   A 1 123 ? 19.352 -3.988  11.462  1.00 14.03 ?  123 LEU   A CG   1 
ATOM   2484 C  CD1  . LEU   A 1 123 ? 17.950 -4.567  11.463  1.00 14.97 ?  123 LEU   A CD1  1 
ATOM   2485 C  CD2  . LEU   A 1 123 ? 19.461 -2.829  12.448  1.00 15.35 ?  123 LEU   A CD2  1 
ATOM   2486 H  H    . LEU   A 1 123 ? 22.382 -6.553  11.506  1.00 15.52 ?  123 LEU   A H    1 
ATOM   2487 H  HA   . LEU   A 1 123 ? 19.757 -6.779  10.856  1.00 15.65 ?  123 LEU   A HA   1 
ATOM   2488 H  HB2  . LEU   A 1 123 ? 20.152 -5.409  12.677  1.00 16.21 ?  123 LEU   A HB2  1 
ATOM   2489 H  HB3  . LEU   A 1 123 ? 21.248 -4.601  11.876  1.00 16.21 ?  123 LEU   A HB3  1 
ATOM   2490 H  HG   . LEU   A 1 123 ? 19.531 -3.631  10.577  1.00 16.85 ?  123 LEU   A HG   1 
ATOM   2491 H  HD11 . LEU   A 1 123 ? 17.308 -3.858  11.300  1.00 17.97 ?  123 LEU   A HD11 1 
ATOM   2492 H  HD12 . LEU   A 1 123 ? 17.886 -5.238  10.765  1.00 17.97 ?  123 LEU   A HD12 1 
ATOM   2493 H  HD13 . LEU   A 1 123 ? 17.777 -4.975  12.328  1.00 17.97 ?  123 LEU   A HD13 1 
ATOM   2494 H  HD21 . LEU   A 1 123 ? 18.798 -2.158  12.228  1.00 18.43 ?  123 LEU   A HD21 1 
ATOM   2495 H  HD22 . LEU   A 1 123 ? 19.303 -3.167  13.347  1.00 18.43 ?  123 LEU   A HD22 1 
ATOM   2496 H  HD23 . LEU   A 1 123 ? 20.351 -2.449  12.393  1.00 18.43 ?  123 LEU   A HD23 1 
ATOM   2497 N  N    . ALA   A 1 124 ? 19.833 -5.880  8.526   1.00 12.10 ?  124 ALA   A N    1 
ATOM   2498 C  CA   . ALA   A 1 124 ? 20.106 -5.591  7.125   1.00 12.18 ?  124 ALA   A CA   1 
ATOM   2499 C  C    . ALA   A 1 124 ? 18.866 -5.111  6.390   1.00 12.46 ?  124 ALA   A C    1 
ATOM   2500 O  O    . ALA   A 1 124 ? 17.736 -5.475  6.750   1.00 13.12 ?  124 ALA   A O    1 
ATOM   2501 C  CB   . ALA   A 1 124 ? 20.687 -6.816  6.406   1.00 12.79 ?  124 ALA   A CB   1 
ATOM   2502 H  H    . ALA   A 1 124 ? 19.038 -6.169  8.692   1.00 14.53 ?  124 ALA   A H    1 
ATOM   2503 H  HA   . ALA   A 1 124 ? 20.773 -4.891  7.090   1.00 14.62 ?  124 ALA   A HA   1 
ATOM   2504 H  HB1  . ALA   A 1 124 ? 20.861 -6.586  5.477   1.00 15.36 ?  124 ALA   A HB1  1 
ATOM   2505 H  HB2  . ALA   A 1 124 ? 21.521 -7.071  6.838   1.00 15.36 ?  124 ALA   A HB2  1 
ATOM   2506 H  HB3  . ALA   A 1 124 ? 20.054 -7.545  6.453   1.00 15.36 ?  124 ALA   A HB3  1 
ATOM   2507 N  N    . PRO   A 1 125 ? 19.052 -4.370  5.301   1.00 12.23 ?  125 PRO   A N    1 
ATOM   2508 C  CA   . PRO   A 1 125 ? 17.983 -4.104  4.344   1.00 12.85 ?  125 PRO   A CA   1 
ATOM   2509 C  C    . PRO   A 1 125 ? 18.014 -5.164  3.247   1.00 13.23 ?  125 PRO   A C    1 
ATOM   2510 O  O    . PRO   A 1 125 ? 18.968 -5.934  3.119   1.00 12.82 ?  125 PRO   A O    1 
ATOM   2511 C  CB   . PRO   A 1 125 ? 18.419 -2.752  3.764   1.00 12.62 ?  125 PRO   A CB   1 
ATOM   2512 C  CG   . PRO   A 1 125 ? 19.901 -2.915  3.642   1.00 12.77 ?  125 PRO   A CG   1 
ATOM   2513 C  CD   . PRO   A 1 125 ? 20.316 -3.722  4.875   1.00 12.57 ?  125 PRO   A CD   1 
ATOM   2514 H  HA   . PRO   A 1 125 ? 17.109 -4.054  4.767   1.00 15.43 ?  125 PRO   A HA   1 
ATOM   2515 H  HB2  . PRO   A 1 125 ? 17.999 -2.611  2.896   1.00 15.15 ?  125 PRO   A HB2  1 
ATOM   2516 H  HB3  . PRO   A 1 125 ? 18.187 -2.038  4.380   1.00 15.15 ?  125 PRO   A HB3  1 
ATOM   2517 H  HG2  . PRO   A 1 125 ? 20.108 -3.403  2.825   1.00 15.33 ?  125 PRO   A HG2  1 
ATOM   2518 H  HG3  . PRO   A 1 125 ? 20.325 -2.045  3.635   1.00 15.33 ?  125 PRO   A HG3  1 
ATOM   2519 H  HD2  . PRO   A 1 125 ? 20.986 -4.386  4.636   1.00 15.09 ?  125 PRO   A HD2  1 
ATOM   2520 H  HD3  . PRO   A 1 125 ? 20.642 -3.128  5.571   1.00 15.09 ?  125 PRO   A HD3  1 
ATOM   2521 N  N    . LEU   A 1 126 ? 16.979 -5.148  2.412   1.00 13.46 ?  126 LEU   A N    1 
ATOM   2522 C  CA   . LEU   A 1 126 ? 16.983 -5.976  1.211   1.00 12.91 ?  126 LEU   A CA   1 
ATOM   2523 C  C    . LEU   A 1 126 ? 17.922 -5.383  0.164   1.00 12.41 ?  126 LEU   A C    1 
ATOM   2524 O  O    . LEU   A 1 126 ? 17.708 -4.270  -0.325  1.00 13.99 ?  126 LEU   A O    1 
ATOM   2525 C  CB   . LEU   A 1 126 ? 15.573 -6.116  0.647   1.00 14.37 ?  126 LEU   A CB   1 
ATOM   2526 C  CG   . LEU   A 1 126 ? 14.635 -7.061  1.408   1.00 15.79 ?  126 LEU   A CG   1 
ATOM   2527 C  CD1  . LEU   A 1 126 ? 13.206 -6.923  0.903   1.00 17.63 ?  126 LEU   A CD1  1 
ATOM   2528 C  CD2  . LEU   A 1 126 ? 15.118 -8.495  1.272   1.00 16.70 ?  126 LEU   A CD2  1 
ATOM   2529 H  H    . LEU   A 1 126 ? 16.274 -4.664  2.507   1.00 16.16 ?  126 LEU   A H    1 
ATOM   2530 H  HA   . LEU   A 1 126 ? 17.309 -6.859  1.438   1.00 15.50 ?  126 LEU   A HA   1 
ATOM   2531 H  HB2  . LEU   A 1 126 ? 15.154 -5.242  0.644   1.00 17.25 ?  126 LEU   A HB2  1 
ATOM   2532 H  HB3  . LEU   A 1 126 ? 15.636 -6.447  -0.263  1.00 17.25 ?  126 LEU   A HB3  1 
ATOM   2533 H  HG   . LEU   A 1 126 ? 14.648 -6.832  2.352   1.00 18.95 ?  126 LEU   A HG   1 
ATOM   2534 H  HD11 . LEU   A 1 126 ? 12.638 -7.531  1.396   1.00 21.17 ?  126 LEU   A HD11 1 
ATOM   2535 H  HD12 . LEU   A 1 126 ? 12.918 -6.009  1.034   1.00 21.17 ?  126 LEU   A HD12 1 
ATOM   2536 H  HD13 . LEU   A 1 126 ? 13.190 -7.144  -0.043  1.00 21.17 ?  126 LEU   A HD13 1 
ATOM   2537 H  HD21 . LEU   A 1 126 ? 14.441 -9.090  1.618   1.00 20.05 ?  126 LEU   A HD21 1 
ATOM   2538 H  HD22 . LEU   A 1 126 ? 15.283 -8.681  0.334   1.00 20.05 ?  126 LEU   A HD22 1 
ATOM   2539 H  HD23 . LEU   A 1 126 ? 15.943 -8.599  1.777   1.00 20.05 ?  126 LEU   A HD23 1 
ATOM   2540 N  N    . LEU   A 1 127 ? 18.965 -6.124  -0.182  1.00 12.89 ?  127 LEU   A N    1 
ATOM   2541 C  CA   . LEU   A 1 127 ? 19.943 -5.618  -1.129  1.00 12.61 ?  127 LEU   A CA   1 
ATOM   2542 C  C    . LEU   A 1 127 ? 19.332 -5.441  -2.512  1.00 11.39 ?  127 LEU   A C    1 
ATOM   2543 O  O    . LEU   A 1 127 ? 18.498 -6.243  -2.965  1.00 12.51 ?  127 LEU   A O    1 
ATOM   2544 C  CB   . LEU   A 1 127 ? 21.129 -6.575  -1.220  1.00 14.03 ?  127 LEU   A CB   1 
ATOM   2545 C  CG   . LEU   A 1 127 ? 21.922 -6.812  0.061   1.00 14.74 ?  127 LEU   A CG   1 
ATOM   2546 C  CD1  . LEU   A 1 127 ? 23.036 -7.802  -0.195  1.00 15.14 ?  127 LEU   A CD1  1 
ATOM   2547 C  CD2  . LEU   A 1 127 ? 22.494 -5.521  0.577   1.00 16.45 ?  127 LEU   A CD2  1 
ATOM   2548 H  H    . LEU   A 1 127 ? 19.134 -6.912  0.119   1.00 15.47 ?  127 LEU   A H    1 
ATOM   2549 H  HA   . LEU   A 1 127 ? 20.268 -4.752  -0.822  1.00 15.14 ?  127 LEU   A HA   1 
ATOM   2550 H  HB2  . LEU   A 1 127 ? 20.800 -7.432  -1.522  1.00 16.84 ?  127 LEU   A HB2  1 
ATOM   2551 H  HB3  . LEU   A 1 127 ? 21.750 -6.219  -1.879  1.00 16.84 ?  127 LEU   A HB3  1 
ATOM   2552 H  HG   . LEU   A 1 127 ? 21.334 -7.180  0.742   1.00 17.70 ?  127 LEU   A HG   1 
ATOM   2553 H  HD11 . LEU   A 1 127 ? 23.531 -7.944  0.631   1.00 18.18 ?  127 LEU   A HD11 1 
ATOM   2554 H  HD12 . LEU   A 1 127 ? 22.655 -8.640  -0.497  1.00 18.18 ?  127 LEU   A HD12 1 
ATOM   2555 H  HD13 . LEU   A 1 127 ? 23.629 -7.443  -0.874  1.00 18.18 ?  127 LEU   A HD13 1 
ATOM   2556 H  HD21 . LEU   A 1 127 ? 23.099 -5.715  1.310   1.00 19.75 ?  127 LEU   A HD21 1 
ATOM   2557 H  HD22 . LEU   A 1 127 ? 22.977 -5.084  -0.143  1.00 19.75 ?  127 LEU   A HD22 1 
ATOM   2558 H  HD23 . LEU   A 1 127 ? 21.771 -4.954  0.883   1.00 19.75 ?  127 LEU   A HD23 1 
ATOM   2559 N  N    . SER   A 1 128 ? 19.784 -4.395  -3.194  1.00 11.76 ?  128 SER   A N    1 
ATOM   2560 C  CA   . SER   A 1 128 ? 19.390 -4.022  -4.544  1.00 11.89 ?  128 SER   A CA   1 
ATOM   2561 C  C    . SER   A 1 128 ? 17.936 -3.568  -4.650  1.00 12.57 ?  128 SER   A C    1 
ATOM   2562 O  O    . SER   A 1 128 ? 17.491 -3.236  -5.755  1.00 13.79 ?  128 SER   A O    1 
ATOM   2563 C  CB   . SER   A 1 128 ? 19.719 -5.087  -5.602  1.00 12.16 ?  128 SER   A CB   1 
ATOM   2564 O  OG   . SER   A 1 128 ? 21.119 -5.324  -5.682  1.00 13.03 ?  128 SER   A OG   1 
ATOM   2565 H  H    . SER   A 1 128 ? 20.374 -3.854  -2.866  1.00 14.12 ?  128 SER   A H    1 
ATOM   2566 H  HA   . SER   A 1 128 ? 19.918 -3.246  -4.774  1.00 14.27 ?  128 SER   A HA   1 
ATOM   2567 H  HB2  . SER   A 1 128 ? 19.263 -5.907  -5.373  1.00 14.60 ?  128 SER   A HB2  1 
ATOM   2568 H  HB3  . SER   A 1 128 ? 19.401 -4.763  -6.467  1.00 14.60 ?  128 SER   A HB3  1 
ATOM   2569 H  HG   . SER   A 1 128 ? 21.516 -4.608  -5.878  1.00 15.65 ?  128 SER   A HG   1 
ATOM   2570 N  N    . ALA   A 1 129 ? 17.200 -3.495  -3.542  1.00 13.62 ?  129 ALA   A N    1 
ATOM   2571 C  CA   . ALA   A 1 129 ? 15.836 -2.987  -3.547  1.00 14.01 ?  129 ALA   A CA   1 
ATOM   2572 C  C    . ALA   A 1 129 ? 15.847 -1.454  -3.502  1.00 14.01 ?  129 ALA   A C    1 
ATOM   2573 O  O    . ALA   A 1 129 ? 16.893 -0.802  -3.582  1.00 13.85 ?  129 ALA   A O    1 
ATOM   2574 C  CB   . ALA   A 1 129 ? 15.045 -3.615  -2.396  1.00 16.20 ?  129 ALA   A CB   1 
ATOM   2575 H  H    . ALA   A 1 129 ? 17.474 -3.730  -2.757  1.00 16.35 ?  129 ALA   A H    1 
ATOM   2576 H  HA   . ALA   A 1 129 ? 15.410 -3.254  -4.372  1.00 16.82 ?  129 ALA   A HA   1 
ATOM   2577 H  HB1  . ALA   A 1 129 ? 14.180 -3.177  -2.325  1.00 19.45 ?  129 ALA   A HB1  1 
ATOM   2578 H  HB2  . ALA   A 1 129 ? 14.917 -4.560  -2.576  1.00 19.45 ?  129 ALA   A HB2  1 
ATOM   2579 H  HB3  . ALA   A 1 129 ? 15.536 -3.504  -1.566  1.00 19.45 ?  129 ALA   A HB3  1 
ATOM   2580 N  N    . GLY   A 1 130 ? 14.659 -0.867  -3.408  1.00 14.57 ?  130 GLY   A N    1 
ATOM   2581 C  CA   . GLY   A 1 130 ? 14.576 0.582   -3.350  1.00 14.91 ?  130 GLY   A CA   1 
ATOM   2582 C  C    . GLY   A 1 130 ? 15.165 1.208   -4.595  1.00 14.45 ?  130 GLY   A C    1 
ATOM   2583 O  O    . GLY   A 1 130 ? 14.928 0.751   -5.719  1.00 14.65 ?  130 GLY   A O    1 
ATOM   2584 H  H    . GLY   A 1 130 ? 13.902 -1.276  -3.386  1.00 17.49 ?  130 GLY   A H    1 
ATOM   2585 H  HA2  . GLY   A 1 130 ? 13.647 0.859   -3.259  1.00 17.90 ?  130 GLY   A HA2  1 
ATOM   2586 H  HA3  . GLY   A 1 130 ? 15.074 0.907   -2.585  1.00 17.90 ?  130 GLY   A HA3  1 
ATOM   2587 N  N    . ILE   A 1 131 ? 15.976 2.254   -4.392  1.00 14.22 ?  131 ILE   A N    1 
ATOM   2588 C  CA   . ILE   A 1 131 ? 16.539 3.019   -5.502  1.00 14.19 ?  131 ILE   A CA   1 
ATOM   2589 C  C    . ILE   A 1 131 ? 17.560 2.244   -6.319  1.00 13.77 ?  131 ILE   A C    1 
ATOM   2590 O  O    . ILE   A 1 131 ? 17.984 2.742   -7.370  1.00 14.55 ?  131 ILE   A O    1 
ATOM   2591 C  CB   . ILE   A 1 131 ? 17.124 4.374   -5.052  1.00 16.11 ?  131 ILE   A CB   1 
ATOM   2592 C  CG1  . ILE   A 1 131 ? 18.366 4.179   -4.178  1.00 17.82 ?  131 ILE   A CG1  1 
ATOM   2593 C  CG2  . ILE   A 1 131 ? 16.065 5.182   -4.327  1.00 16.17 ?  131 ILE   A CG2  1 
ATOM   2594 C  CD1  . ILE   A 1 131 ? 18.990 5.500   -3.712  1.00 19.77 ?  131 ILE   A CD1  1 
ATOM   2595 H  H    . ILE   A 1 131 ? 16.207 2.538   -3.617  1.00 17.07 ?  131 ILE   A H    1 
ATOM   2596 H  HA   . ILE   A 1 131 ? 15.815 3.223   -6.108  1.00 17.03 ?  131 ILE   A HA   1 
ATOM   2597 H  HB   . ILE   A 1 131 ? 17.385 4.864   -5.845  1.00 19.34 ?  131 ILE   A HB   1 
ATOM   2598 H  HG12 . ILE   A 1 131 ? 18.126 3.671   -3.390  1.00 21.39 ?  131 ILE   A HG12 1 
ATOM   2599 H  HG13 . ILE   A 1 131 ? 19.044 3.704   -4.685  1.00 21.39 ?  131 ILE   A HG13 1 
ATOM   2600 H  HG21 . ILE   A 1 131 ? 16.379 6.093   -4.222  1.00 19.41 ?  131 ILE   A HG21 1 
ATOM   2601 H  HG22 . ILE   A 1 131 ? 15.249 5.174   -4.853  1.00 19.41 ?  131 ILE   A HG22 1 
ATOM   2602 H  HG23 . ILE   A 1 131 ? 15.902 4.783   -3.459  1.00 19.41 ?  131 ILE   A HG23 1 
ATOM   2603 H  HD11 . ILE   A 1 131 ? 19.844 5.319   -3.288  1.00 23.74 ?  131 ILE   A HD11 1 
ATOM   2604 H  HD12 . ILE   A 1 131 ? 19.121 6.081   -4.479  1.00 23.74 ?  131 ILE   A HD12 1 
ATOM   2605 H  HD13 . ILE   A 1 131 ? 18.393 5.929   -3.075  1.00 23.74 ?  131 ILE   A HD13 1 
ATOM   2606 N  N    . PHE   A 1 132 ? 17.979 1.052   -5.870  1.00 13.72 ?  132 PHE   A N    1 
ATOM   2607 C  CA   . PHE   A 1 132 ? 18.835 0.198   -6.692  1.00 13.45 ?  132 PHE   A CA   1 
ATOM   2608 C  C    . PHE   A 1 132 ? 18.067 -0.561  -7.777  1.00 13.91 ?  132 PHE   A C    1 
ATOM   2609 O  O    . PHE   A 1 132 ? 18.696 -1.189  -8.634  1.00 15.38 ?  132 PHE   A O    1 
ATOM   2610 C  CB   . PHE   A 1 132 ? 19.644 -0.782  -5.834  1.00 13.04 ?  132 PHE   A CB   1 
ATOM   2611 C  CG   . PHE   A 1 132 ? 20.865 -0.171  -5.166  1.00 13.05 ?  132 PHE   A CG   1 
ATOM   2612 C  CD1  . PHE   A 1 132 ? 20.746 0.858   -4.245  1.00 13.96 ?  132 PHE   A CD1  1 
ATOM   2613 C  CD2  . PHE   A 1 132 ? 22.125 -0.687  -5.415  1.00 14.03 ?  132 PHE   A CD2  1 
ATOM   2614 C  CE1  . PHE   A 1 132 ? 21.866 1.391   -3.623  1.00 14.87 ?  132 PHE   A CE1  1 
ATOM   2615 C  CE2  . PHE   A 1 132 ? 23.248 -0.155  -4.796  1.00 14.54 ?  132 PHE   A CE2  1 
ATOM   2616 C  CZ   . PHE   A 1 132 ? 23.111 0.885   -3.893  1.00 14.51 ?  132 PHE   A CZ   1 
ATOM   2617 H  H    . PHE   A 1 132 ? 17.784 0.722   -5.098  1.00 16.48 ?  132 PHE   A H    1 
ATOM   2618 H  HA   . PHE   A 1 132 ? 19.477 0.768   -7.139  1.00 16.15 ?  132 PHE   A HA   1 
ATOM   2619 H  HB2  . PHE   A 1 132 ? 19.072 -1.133  -5.130  1.00 15.66 ?  132 PHE   A HB2  1 
ATOM   2620 H  HB3  . PHE   A 1 132 ? 19.949 -1.516  -6.396  1.00 15.66 ?  132 PHE   A HB3  1 
ATOM   2621 H  HD1  . PHE   A 1 132 ? 19.906 1.206   -4.057  1.00 16.77 ?  132 PHE   A HD1  1 
ATOM   2622 H  HD2  . PHE   A 1 132 ? 22.228 -1.394  -6.022  1.00 16.85 ?  132 PHE   A HD2  1 
ATOM   2623 H  HE1  . PHE   A 1 132 ? 21.775 2.093   -3.020  1.00 17.86 ?  132 PHE   A HE1  1 
ATOM   2624 H  HE2  . PHE   A 1 132 ? 24.092 -0.506  -4.983  1.00 17.46 ?  132 PHE   A HE2  1 
ATOM   2625 H  HZ   . PHE   A 1 132 ? 23.864 1.243   -3.480  1.00 17.42 ?  132 PHE   A HZ   1 
ATOM   2626 N  N    . GLY   A 1 133 ? 16.739 -0.525  -7.768  1.00 14.41 ?  133 GLY   A N    1 
ATOM   2627 C  CA   . GLY   A 1 133 ? 15.971 -0.898  -8.937  1.00 15.33 ?  133 GLY   A CA   1 
ATOM   2628 C  C    . GLY   A 1 133 ? 15.564 -2.347  -9.085  1.00 15.36 ?  133 GLY   A C    1 
ATOM   2629 O  O    . GLY   A 1 133 ? 14.865 -2.660  -10.056 1.00 17.12 ?  133 GLY   A O    1 
ATOM   2630 H  H    . GLY   A 1 133 ? 16.264 -0.283  -7.091  1.00 17.30 ?  133 GLY   A H    1 
ATOM   2631 H  HA2  . GLY   A 1 133 ? 15.151 -0.398  -8.929  1.00 18.40 ?  133 GLY   A HA2  1 
ATOM   2632 H  HA3  . GLY   A 1 133 ? 16.471 -0.643  -9.732  1.00 18.40 ?  133 GLY   A HA3  1 
ATOM   2633 N  N    . ALA   A 1 134 ? 15.971 -3.237  -8.185  1.00 15.04 ?  134 ALA   A N    1 
ATOM   2634 C  CA   . ALA   A 1 134 ? 15.628 -4.641  -8.340  1.00 14.94 ?  134 ALA   A CA   1 
ATOM   2635 C  C    . ALA   A 1 134 ? 14.273 -4.935  -7.701  1.00 15.28 ?  134 ALA   A C    1 
ATOM   2636 O  O    . ALA   A 1 134 ? 13.736 -4.145  -6.920  1.00 17.37 ?  134 ALA   A O    1 
ATOM   2637 C  CB   . ALA   A 1 134 ? 16.703 -5.547  -7.740  1.00 16.14 ?  134 ALA   A CB   1 
ATOM   2638 H  H    . ALA   A 1 134 ? 16.444 -3.052  -7.484  1.00 18.05 ?  134 ALA   A H    1 
ATOM   2639 H  HA   . ALA   A 1 134 ? 15.564 -4.841  -9.286  1.00 17.93 ?  134 ALA   A HA   1 
ATOM   2640 H  HB1  . ALA   A 1 134 ? 16.450 -6.471  -7.882  1.00 19.38 ?  134 ALA   A HB1  1 
ATOM   2641 H  HB2  . ALA   A 1 134 ? 17.551 -5.365  -8.180  1.00 19.38 ?  134 ALA   A HB2  1 
ATOM   2642 H  HB3  . ALA   A 1 134 ? 16.779 -5.364  -6.791  1.00 19.38 ?  134 ALA   A HB3  1 
ATOM   2643 N  N    . ASP   A 1 135 ? 13.720 -6.089  -8.056  1.00 16.75 ?  135 ASP   A N    1 
ATOM   2644 C  CA   . ASP   A 1 135 ? 12.454 -6.548  -7.490  1.00 18.16 ?  135 ASP   A CA   1 
ATOM   2645 C  C    . ASP   A 1 135 ? 12.689 -7.005  -6.057  1.00 17.12 ?  135 ASP   A C    1 
ATOM   2646 O  O    . ASP   A 1 135 ? 13.452 -7.958  -5.842  1.00 17.03 ?  135 ASP   A O    1 
ATOM   2647 C  CB   . ASP   A 1 135 ? 11.944 -7.716  -8.330  1.00 21.55 ?  135 ASP   A CB   1 
ATOM   2648 C  CG   . ASP   A 1 135 ? 10.675 -8.362  -7.767  1.00 25.42 ?  135 ASP   A CG   1 
ATOM   2649 O  OD1  . ASP   A 1 135 ? 10.100 -7.851  -6.782  1.00 25.27 ?  135 ASP   A OD1  1 
ATOM   2650 O  OD2  . ASP   A 1 135 ? 10.248 -9.395  -8.335  1.00 29.84 -1 135 ASP   A OD2  1 
ATOM   2651 H  H    . ASP   A 1 135 ? 14.062 -6.631  -8.630  1.00 20.11 ?  135 ASP   A H    1 
ATOM   2652 H  HA   . ASP   A 1 135 ? 11.803 -5.828  -7.517  1.00 21.80 ?  135 ASP   A HA   1 
ATOM   2653 H  HB2  . ASP   A 1 135 ? 11.754 -7.398  -9.224  1.00 25.86 ?  135 ASP   A HB2  1 
ATOM   2654 H  HB3  . ASP   A 1 135 ? 12.627 -8.402  -8.356  1.00 25.86 ?  135 ASP   A HB3  1 
ATOM   2655 N  N    . PRO   A 1 136 ? 12.067 -6.378  -5.056  1.00 16.59 ?  136 PRO   A N    1 
ATOM   2656 C  CA   . PRO   A 1 136 ? 12.305 -6.801  -3.664  1.00 16.84 ?  136 PRO   A CA   1 
ATOM   2657 C  C    . PRO   A 1 136 ? 11.876 -8.229  -3.362  1.00 15.79 ?  136 PRO   A C    1 
ATOM   2658 O  O    . PRO   A 1 136 ? 12.475 -8.860  -2.481  1.00 15.03 ?  136 PRO   A O    1 
ATOM   2659 C  CB   . PRO   A 1 136 ? 11.510 -5.770  -2.846  1.00 18.33 ?  136 PRO   A CB   1 
ATOM   2660 C  CG   . PRO   A 1 136 ? 10.479 -5.260  -3.795  1.00 20.23 ?  136 PRO   A CG   1 
ATOM   2661 C  CD   . PRO   A 1 136 ? 11.119 -5.257  -5.142  1.00 19.05 ?  136 PRO   A CD   1 
ATOM   2662 H  HA   . PRO   A 1 136 ? 13.247 -6.705  -3.444  1.00 20.22 ?  136 PRO   A HA   1 
ATOM   2663 H  HB2  . PRO   A 1 136 ? 11.094 -6.201  -2.086  1.00 22.00 ?  136 PRO   A HB2  1 
ATOM   2664 H  HB3  . PRO   A 1 136 ? 12.099 -5.051  -2.557  1.00 22.00 ?  136 PRO   A HB3  1 
ATOM   2665 H  HG2  . PRO   A 1 136 ? 9.713  -5.849  -3.793  1.00 24.28 ?  136 PRO   A HG2  1 
ATOM   2666 H  HG3  . PRO   A 1 136 ? 10.222 -4.358  -3.549  1.00 24.28 ?  136 PRO   A HG3  1 
ATOM   2667 H  HD2  . PRO   A 1 136 ? 10.452 -5.435  -5.831  1.00 22.87 ?  136 PRO   A HD2  1 
ATOM   2668 H  HD3  . PRO   A 1 136 ? 11.581 -4.421  -5.306  1.00 22.87 ?  136 PRO   A HD3  1 
ATOM   2669 N  N    . ILE   A 1 137 ? 10.860 -8.754  -4.052  1.00 16.00 ?  137 ILE   A N    1 
ATOM   2670 C  CA   . ILE   A 1 137 ? 10.485 -10.151 -3.844  1.00 16.56 ?  137 ILE   A CA   1 
ATOM   2671 C  C    . ILE   A 1 137 ? 11.639 -11.057 -4.237  1.00 16.24 ?  137 ILE   A C    1 
ATOM   2672 O  O    . ILE   A 1 137 ? 11.954 -12.030 -3.540  1.00 16.33 ?  137 ILE   A O    1 
ATOM   2673 C  CB   . ILE   A 1 137 ? 9.194  -10.487 -4.616  1.00 18.74 ?  137 ILE   A CB   1 
ATOM   2674 C  CG1  . ILE   A 1 137 ? 8.033  -9.627  -4.109  1.00 21.73 ?  137 ILE   A CG1  1 
ATOM   2675 C  CG2  . ILE   A 1 137 ? 8.864  -11.980 -4.501  1.00 19.49 ?  137 ILE   A CG2  1 
ATOM   2676 C  CD1  . ILE   A 1 137 ? 6.740  -9.818  -4.879  1.00 24.26 ?  137 ILE   A CD1  1 
ATOM   2677 H  H    . ILE   A 1 137 ? 10.382 -8.329  -4.631  1.00 19.21 ?  137 ILE   A H    1 
ATOM   2678 H  HA   . ILE   A 1 137 ? 10.310 -10.285 -2.903  1.00 19.88 ?  137 ILE   A HA   1 
ATOM   2679 H  HB   . ILE   A 1 137 ? 9.333  -10.276 -5.551  1.00 22.50 ?  137 ILE   A HB   1 
ATOM   2680 H  HG12 . ILE   A 1 137 ? 7.863  -9.844  -3.179  1.00 26.09 ?  137 ILE   A HG12 1 
ATOM   2681 H  HG13 . ILE   A 1 137 ? 8.281  -8.687  -4.181  1.00 26.09 ?  137 ILE   A HG13 1 
ATOM   2682 H  HG21 . ILE   A 1 137 ? 7.990  -12.149 -4.880  1.00 23.39 ?  137 ILE   A HG21 1 
ATOM   2683 H  HG22 . ILE   A 1 137 ? 9.533  -12.483 -4.984  1.00 23.39 ?  137 ILE   A HG22 1 
ATOM   2684 H  HG23 . ILE   A 1 137 ? 8.871  -12.226 -3.564  1.00 23.39 ?  137 ILE   A HG23 1 
ATOM   2685 H  HD11 . ILE   A 1 137 ? 6.052  -10.135 -4.271  1.00 29.12 ?  137 ILE   A HD11 1 
ATOM   2686 H  HD12 . ILE   A 1 137 ? 6.483  -8.968  -5.261  1.00 29.12 ?  137 ILE   A HD12 1 
ATOM   2687 H  HD13 . ILE   A 1 137 ? 6.880  -10.464 -5.589  1.00 29.12 ?  137 ILE   A HD13 1 
ATOM   2688 N  N    . HIS   A 1 138 ? 12.297 -10.736 -5.354  1.00 16.06 ?  138 HIS   A N    1 
ATOM   2689 C  CA   . HIS   A 1 138 ? 13.459 -11.502 -5.781  1.00 16.13 ?  138 HIS   A CA   1 
ATOM   2690 C  C    . HIS   A 1 138 ? 14.599 -11.372 -4.778  1.00 15.43 ?  138 HIS   A C    1 
ATOM   2691 O  O    . HIS   A 1 138 ? 15.258 -12.363 -4.434  1.00 15.30 ?  138 HIS   A O    1 
ATOM   2692 C  CB   . HIS   A 1 138 ? 13.887 -11.041 -7.173  1.00 16.69 ?  138 HIS   A CB   1 
ATOM   2693 C  CG   . HIS   A 1 138 ? 15.137 -11.701 -7.654  1.00 17.59 ?  138 HIS   A CG   1 
ATOM   2694 N  ND1  . HIS   A 1 138 ? 15.225 -13.060 -7.868  1.00 18.69 ?  138 HIS   A ND1  1 
ATOM   2695 C  CD2  . HIS   A 1 138 ? 16.361 -11.196 -7.935  1.00 17.87 ?  138 HIS   A CD2  1 
ATOM   2696 C  CE1  . HIS   A 1 138 ? 16.444 -13.362 -8.274  1.00 19.35 ?  138 HIS   A CE1  1 
ATOM   2697 N  NE2  . HIS   A 1 138 ? 17.155 -12.249 -8.320  1.00 18.11 ?  138 HIS   A NE2  1 
ATOM   2698 H  H    . HIS   A 1 138 ? 12.082 -10.084 -5.882  1.00 19.28 ?  138 HIS   A H    1 
ATOM   2699 H  HA   . HIS   A 1 138 ? 13.211 -12.435 -5.841  1.00 19.36 ?  138 HIS   A HA   1 
ATOM   2700 H  HB2  . HIS   A 1 138 ? 13.173 -11.248 -7.806  1.00 20.03 ?  138 HIS   A HB2  1 
ATOM   2701 H  HB3  . HIS   A 1 138 ? 14.038 -10.084 -7.158  1.00 20.03 ?  138 HIS   A HB3  1 
ATOM   2702 H  HD1  . HIS   A 1 138 ? 14.578 -13.625 -7.759  1.00 22.44 ?  138 HIS   A HD1  1 
ATOM   2703 H  HD2  . HIS   A 1 138 ? 16.608 -10.305 -7.883  1.00 21.45 ?  138 HIS   A HD2  1 
ATOM   2704 H  HE1  . HIS   A 1 138 ? 16.748 -14.215 -8.485  1.00 23.22 ?  138 HIS   A HE1  1 
ATOM   2705 N  N    . SER   A 1 139 ? 14.855 -10.157 -4.297  1.00 14.65 ?  139 SER   A N    1 
ATOM   2706 C  CA   . SER   A 1 139 ? 15.925 -9.966  -3.327  1.00 13.99 ?  139 SER   A CA   1 
ATOM   2707 C  C    . SER   A 1 139 ? 15.706 -10.804 -2.073  1.00 13.78 ?  139 SER   A C    1 
ATOM   2708 O  O    . SER   A 1 139 ? 16.653 -11.395 -1.542  1.00 14.21 ?  139 SER   A O    1 
ATOM   2709 C  CB   . SER   A 1 139 ? 16.068 -8.486  -2.982  1.00 14.59 ?  139 SER   A CB   1 
ATOM   2710 O  OG   . SER   A 1 139 ? 17.142 -8.318  -2.078  1.00 14.60 ?  139 SER   A OG   1 
ATOM   2711 H  H    . SER   A 1 139 ? 14.428 -9.439  -4.510  1.00 17.58 ?  139 SER   A H    1 
ATOM   2712 H  HA   . SER   A 1 139 ? 16.761 -10.247 -3.727  1.00 16.79 ?  139 SER   A HA   1 
ATOM   2713 H  HB2  . SER   A 1 139 ? 16.258 -7.979  -3.790  1.00 17.52 ?  139 SER   A HB2  1 
ATOM   2714 H  HB3  . SER   A 1 139 ? 15.245 -8.166  -2.576  1.00 17.52 ?  139 SER   A HB3  1 
ATOM   2715 H  HG   . SER   A 1 139 ? 17.222 -7.501  -1.870  1.00 17.53 ?  139 SER   A HG   1 
ATOM   2716 N  N    . LEU   A 1 140 ? 14.471 -10.862 -1.576  1.00 14.06 ?  140 LEU   A N    1 
ATOM   2717 C  CA   . LEU   A 1 140 ? 14.187 -11.684 -0.402  1.00 13.79 ?  140 LEU   A CA   1 
ATOM   2718 C  C    . LEU   A 1 140 ? 14.451 -13.159 -0.684  1.00 13.78 ?  140 LEU   A C    1 
ATOM   2719 O  O    . LEU   A 1 140 ? 14.993 -13.880 0.168   1.00 14.57 ?  140 LEU   A O    1 
ATOM   2720 C  CB   . LEU   A 1 140 ? 12.742 -11.484 0.043   1.00 14.36 ?  140 LEU   A CB   1 
ATOM   2721 C  CG   . LEU   A 1 140 ? 12.317 -12.337 1.235   1.00 14.53 ?  140 LEU   A CG   1 
ATOM   2722 C  CD1  . LEU   A 1 140 ? 13.207 -12.147 2.461   1.00 14.79 ?  140 LEU   A CD1  1 
ATOM   2723 C  CD2  . LEU   A 1 140 ? 10.861 -12.044 1.575   1.00 15.96 ?  140 LEU   A CD2  1 
ATOM   2724 H  H    . LEU   A 1 140 ? 13.792 -10.431 -1.886  1.00 16.88 ?  140 LEU   A H    1 
ATOM   2725 H  HA   . LEU   A 1 140 ? 14.767 -11.408 0.326   1.00 16.56 ?  140 LEU   A HA   1 
ATOM   2726 H  HB2  . LEU   A 1 140 ? 12.620 -10.558 0.290   1.00 17.25 ?  140 LEU   A HB2  1 
ATOM   2727 H  HB3  . LEU   A 1 140 ? 12.160 -11.709 -0.698  1.00 17.25 ?  140 LEU   A HB3  1 
ATOM   2728 H  HG   . LEU   A 1 140 ? 12.363 -13.273 0.983   1.00 17.45 ?  140 LEU   A HG   1 
ATOM   2729 H  HD11 . LEU   A 1 140 ? 12.829 -12.644 3.206   1.00 17.76 ?  140 LEU   A HD11 1 
ATOM   2730 H  HD12 . LEU   A 1 140 ? 14.094 -12.487 2.259   1.00 17.76 ?  140 LEU   A HD12 1 
ATOM   2731 H  HD13 . LEU   A 1 140 ? 13.251 -11.207 2.678   1.00 17.76 ?  140 LEU   A HD13 1 
ATOM   2732 H  HD21 . LEU   A 1 140 ? 10.591 -12.593 2.335   1.00 19.17 ?  140 LEU   A HD21 1 
ATOM   2733 H  HD22 . LEU   A 1 140 ? 10.763 -11.107 1.801   1.00 19.17 ?  140 LEU   A HD22 1 
ATOM   2734 H  HD23 . LEU   A 1 140 ? 10.301 -12.260 0.809   1.00 19.17 ?  140 LEU   A HD23 1 
ATOM   2735 N  N    . ARG   A 1 141 ? 14.083 -13.624 -1.878  1.00 14.72 ?  141 ARG   A N    1 
ATOM   2736 C  CA   . ARG   A 1 141 ? 14.319 -15.021 -2.243  1.00 15.34 ?  141 ARG   A CA   1 
ATOM   2737 C  C    . ARG   A 1 141 ? 15.811 -15.335 -2.269  1.00 14.49 ?  141 ARG   A C    1 
ATOM   2738 O  O    . ARG   A 1 141 ? 16.256 -16.357 -1.728  1.00 14.73 ?  141 ARG   A O    1 
ATOM   2739 C  CB   . ARG   A 1 141 ? 13.684 -15.294 -3.609  1.00 17.17 ?  141 ARG   A CB   1 
ATOM   2740 C  CG   . ARG   A 1 141 ? 13.702 -16.732 -4.065  1.00 20.67 ?  141 ARG   A CG   1 
ATOM   2741 C  CD   . ARG   A 1 141 ? 12.656 -17.511 -3.336  1.00 23.64 ?  141 ARG   A CD   1 
ATOM   2742 N  NE   . ARG   A 1 141 ? 13.256 -18.301 -2.278  1.00 24.44 ?  141 ARG   A NE   1 
ATOM   2743 C  CZ   . ARG   A 1 141 ? 12.571 -18.866 -1.293  1.00 24.90 ?  141 ARG   A CZ   1 
ATOM   2744 N  NH1  . ARG   A 1 141 ? 11.281 -18.627 -1.122  1.00 24.10 ?  141 ARG   A NH1  1 
ATOM   2745 N  NH2  . ARG   A 1 141 ? 13.201 -19.683 -0.455  1.00 26.61 ?  141 ARG   A NH2  1 
ATOM   2746 H  H    . ARG   A 1 141 ? 13.700 -13.155 -2.491  1.00 17.67 ?  141 ARG   A H    1 
ATOM   2747 H  HA   . ARG   A 1 141 ? 13.901 -15.596 -1.587  1.00 18.42 ?  141 ARG   A HA   1 
ATOM   2748 H  HB2  . ARG   A 1 141 ? 12.758 -15.002 -3.582  1.00 20.62 ?  141 ARG   A HB2  1 
ATOM   2749 H  HB3  . ARG   A 1 141 ? 14.160 -14.776 -4.274  1.00 20.62 ?  141 ARG   A HB3  1 
ATOM   2750 H  HG2  . ARG   A 1 141 ? 13.514 -16.777 -5.016  1.00 24.81 ?  141 ARG   A HG2  1 
ATOM   2751 H  HG3  . ARG   A 1 141 ? 14.571 -17.128 -3.875  1.00 24.81 ?  141 ARG   A HG3  1 
ATOM   2752 H  HD2  . ARG   A 1 141 ? 12.016 -16.903 -2.930  1.00 28.37 ?  141 ARG   A HD2  1 
ATOM   2753 H  HD3  . ARG   A 1 141 ? 12.204 -18.106 -3.955  1.00 28.37 ?  141 ARG   A HD3  1 
ATOM   2754 H  HE   . ARG   A 1 141 ? 14.084 -18.514 -2.359  1.00 29.34 ?  141 ARG   A HE   1 
ATOM   2755 H  HH11 . ARG   A 1 141 ? 10.860 -18.107 -1.662  1.00 28.93 ?  141 ARG   A HH11 1 
ATOM   2756 H  HH12 . ARG   A 1 141 ? 10.857 -18.999 -0.471  1.00 28.93 ?  141 ARG   A HH12 1 
ATOM   2757 H  HH21 . ARG   A 1 141 ? 14.039 -19.843 -0.557  1.00 31.94 ?  141 ARG   A HH21 1 
ATOM   2758 H  HH22 . ARG   A 1 141 ? 12.771 -20.046 0.197   1.00 31.94 ?  141 ARG   A HH22 1 
ATOM   2759 N  N    . VAL   A 1 142 ? 16.604 -14.462 -2.897  1.00 13.55 ?  142 VAL   A N    1 
ATOM   2760 C  CA   . VAL   A 1 142 ? 18.047 -14.679 -2.931  1.00 13.86 ?  142 VAL   A CA   1 
ATOM   2761 C  C    . VAL   A 1 142 ? 18.621 -14.670 -1.519  1.00 12.90 ?  142 VAL   A C    1 
ATOM   2762 O  O    . VAL   A 1 142 ? 19.484 -15.490 -1.175  1.00 14.24 ?  142 VAL   A O    1 
ATOM   2763 C  CB   . VAL   A 1 142 ? 18.738 -13.659 -3.853  1.00 14.08 ?  142 VAL   A CB   1 
ATOM   2764 C  CG1  . VAL   A 1 142 ? 20.254 -13.879 -3.834  1.00 14.58 ?  142 VAL   A CG1  1 
ATOM   2765 C  CG2  . VAL   A 1 142 ? 18.212 -13.771 -5.273  1.00 15.38 ?  142 VAL   A CG2  1 
ATOM   2766 H  H    . VAL   A 1 142 ? 16.336 -13.745 -3.304  1.00 16.26 ?  142 VAL   A H    1 
ATOM   2767 H  HA   . VAL   A 1 142 ? 18.216 -15.551 -3.305  1.00 16.64 ?  142 VAL   A HA   1 
ATOM   2768 H  HB   . VAL   A 1 142 ? 18.570 -12.755 -3.533  1.00 16.90 ?  142 VAL   A HB   1 
ATOM   2769 H  HG11 . VAL   A 1 142 ? 20.660 -13.380 -4.562  1.00 17.51 ?  142 VAL   A HG11 1 
ATOM   2770 H  HG12 . VAL   A 1 142 ? 20.616 -13.568 -2.986  1.00 17.51 ?  142 VAL   A HG12 1 
ATOM   2771 H  HG13 . VAL   A 1 142 ? 20.438 -14.825 -3.943  1.00 17.51 ?  142 VAL   A HG13 1 
ATOM   2772 H  HG21 . VAL   A 1 142 ? 18.694 -13.146 -5.842  1.00 18.47 ?  142 VAL   A HG21 1 
ATOM   2773 H  HG22 . VAL   A 1 142 ? 18.357 -14.678 -5.589  1.00 18.47 ?  142 VAL   A HG22 1 
ATOM   2774 H  HG23 . VAL   A 1 142 ? 17.270 -13.563 -5.276  1.00 18.47 ?  142 VAL   A HG23 1 
ATOM   2775 N  N    . CYS   A 1 143 ? 18.148 -13.748 -0.676  1.00 13.08 ?  143 CYS   A N    1 
ATOM   2776 C  CA   . CYS   A 1 143 ? 18.620 -13.695 0.703   1.00 13.33 ?  143 CYS   A CA   1 
ATOM   2777 C  C    . CYS   A 1 143 ? 18.393 -15.036 1.390   1.00 13.48 ?  143 CYS   A C    1 
ATOM   2778 O  O    . CYS   A 1 143 ? 19.309 -15.621 1.968   1.00 13.14 ?  143 CYS   A O    1 
ATOM   2779 C  CB   . CYS   A 1 143 ? 17.869 -12.598 1.456   1.00 14.02 ?  143 CYS   A CB   1 
ATOM   2780 S  SG   . CYS   A 1 143 ? 18.382 -12.413 3.169   1.00 14.25 ?  143 CYS   A SG   1 
ATOM   2781 H  H    . CYS   A 1 143 ? 17.557 -13.153 -0.878  1.00 15.71 ?  143 CYS   A H    1 
ATOM   2782 H  HA   . CYS   A 1 143 ? 19.568 -13.498 0.716   1.00 16.01 ?  143 CYS   A HA   1 
ATOM   2783 H  HB2  . CYS   A 1 143 ? 18.016 -11.756 1.003   1.00 16.83 ?  143 CYS   A HB2  1 
ATOM   2784 H  HB3  . CYS   A 1 143 ? 16.925 -12.813 1.449   1.00 16.83 ?  143 CYS   A HB3  1 
ATOM   2785 H  HG   . CYS   A 1 143 ? 17.780 -11.490 3.647   1.00 17.11 ?  143 CYS   A HG   1 
ATOM   2786 N  N    . VAL   A 1 144 ? 17.159 -15.543 1.325   1.00 13.93 ?  144 VAL   A N    1 
ATOM   2787 C  CA   . VAL   A 1 144 ? 16.812 -16.780 2.019   1.00 15.59 ?  144 VAL   A CA   1 
ATOM   2788 C  C    . VAL   A 1 144 ? 17.621 -17.953 1.490   1.00 15.29 ?  144 VAL   A C    1 
ATOM   2789 O  O    . VAL   A 1 144 ? 18.003 -18.851 2.252   1.00 15.94 ?  144 VAL   A O    1 
ATOM   2790 C  CB   . VAL   A 1 144 ? 15.293 -17.021 1.911   1.00 18.74 ?  144 VAL   A CB   1 
ATOM   2791 C  CG1  . VAL   A 1 144 ? 14.929 -18.464 2.220   1.00 21.37 ?  144 VAL   A CG1  1 
ATOM   2792 C  CG2  . VAL   A 1 144 ? 14.549 -16.037 2.821   1.00 18.86 ?  144 VAL   A CG2  1 
ATOM   2793 H  H    . VAL   A 1 144 ? 16.506 -15.188 0.886   1.00 16.73 ?  144 VAL   A H    1 
ATOM   2794 H  HA   . VAL   A 1 144 ? 17.021 -16.679 2.956   1.00 18.71 ?  144 VAL   A HA   1 
ATOM   2795 H  HB   . VAL   A 1 144 ? 15.009 -16.841 1.000   1.00 22.50 ?  144 VAL   A HB   1 
ATOM   2796 H  HG11 . VAL   A 1 144 ? 13.975 -18.520 2.391   1.00 25.65 ?  144 VAL   A HG11 1 
ATOM   2797 H  HG12 . VAL   A 1 144 ? 15.158 -19.020 1.459   1.00 25.65 ?  144 VAL   A HG12 1 
ATOM   2798 H  HG13 . VAL   A 1 144 ? 15.421 -18.753 3.004   1.00 25.65 ?  144 VAL   A HG13 1 
ATOM   2799 H  HG21 . VAL   A 1 144 ? 13.592 -16.112 2.665   1.00 22.64 ?  144 VAL   A HG21 1 
ATOM   2800 H  HG22 . VAL   A 1 144 ? 14.744 -16.245 3.749   1.00 22.64 ?  144 VAL   A HG22 1 
ATOM   2801 H  HG23 . VAL   A 1 144 ? 14.840 -15.131 2.619   1.00 22.64 ?  144 VAL   A HG23 1 
ATOM   2802 N  N    . ASP   A 1 145 ? 17.886 -17.974 0.187   1.00 15.27 ?  145 ASP   A N    1 
ATOM   2803 C  CA   . ASP   A 1 145 ? 18.615 -19.075 -0.437  1.00 15.99 ?  145 ASP   A CA   1 
ATOM   2804 C  C    . ASP   A 1 145 ? 20.137 -18.920 -0.398  1.00 15.05 ?  145 ASP   A C    1 
ATOM   2805 O  O    . ASP   A 1 145 ? 20.843 -19.814 -0.874  1.00 17.32 ?  145 ASP   A O    1 
ATOM   2806 C  CB   . ASP   A 1 145 ? 18.160 -19.247 -1.891  1.00 17.49 ?  145 ASP   A CB   1 
ATOM   2807 C  CG   . ASP   A 1 145 ? 16.693 -19.652 -2.008  1.00 19.14 ?  145 ASP   A CG   1 
ATOM   2808 O  OD1  . ASP   A 1 145 ? 16.132 -20.194 -1.032  1.00 19.83 ?  145 ASP   A OD1  1 
ATOM   2809 O  OD2  . ASP   A 1 145 ? 16.099 -19.416 -3.077  1.00 21.02 -1 145 ASP   A OD2  1 
ATOM   2810 H  H    . ASP   A 1 145 ? 17.640 -17.360 -0.367  1.00 18.33 ?  145 ASP   A H    1 
ATOM   2811 H  HA   . ASP   A 1 145 ? 18.392 -19.892 0.034   1.00 19.19 ?  145 ASP   A HA   1 
ATOM   2812 H  HB2  . ASP   A 1 145 ? 18.283 -18.408 -2.361  1.00 21.00 ?  145 ASP   A HB2  1 
ATOM   2813 H  HB3  . ASP   A 1 145 ? 18.693 -19.943 -2.305  1.00 21.00 ?  145 ASP   A HB3  1 
ATOM   2814 N  N    . THR   A 1 146 ? 20.664 -17.828 0.147   1.00 13.50 ?  146 THR   A N    1 
ATOM   2815 C  CA   . THR   A 1 146 ? 22.106 -17.581 0.158   1.00 12.89 ?  146 THR   A CA   1 
ATOM   2816 C  C    . THR   A 1 146 ? 22.672 -17.399 1.555   1.00 12.74 ?  146 THR   A C    1 
ATOM   2817 O  O    . THR   A 1 146 ? 23.747 -17.931 1.856   1.00 14.00 ?  146 THR   A O    1 
ATOM   2818 C  CB   . THR   A 1 146 ? 22.432 -16.343 -0.692  1.00 12.96 ?  146 THR   A CB   1 
ATOM   2819 O  OG1  . THR   A 1 146 ? 21.892 -16.514 -2.006  1.00 13.97 ?  146 THR   A OG1  1 
ATOM   2820 C  CG2  . THR   A 1 146 ? 23.934 -16.120 -0.786  1.00 13.70 ?  146 THR   A CG2  1 
ATOM   2821 H  H    . THR   A 1 146 ? 20.203 -17.196 0.512   1.00 16.20 ?  146 THR   A H    1 
ATOM   2822 H  HA   . THR   A 1 146 ? 22.558 -18.332 -0.245  1.00 15.48 ?  146 THR   A HA   1 
ATOM   2823 H  HB   . THR   A 1 146 ? 22.040 -15.554 -0.283  1.00 15.56 ?  146 THR   A HB   1 
ATOM   2824 H  HG1  . THR   A 1 146 ? 21.057 -16.574 -1.962  1.00 16.77 ?  146 THR   A HG1  1 
ATOM   2825 H  HG21 . THR   A 1 146 ? 24.127 -15.454 -1.469  1.00 16.45 ?  146 THR   A HG21 1 
ATOM   2826 H  HG22 . THR   A 1 146 ? 24.280 -15.803 0.062   1.00 16.45 ?  146 THR   A HG22 1 
ATOM   2827 H  HG23 . THR   A 1 146 ? 24.377 -16.947 -1.023  1.00 16.45 ?  146 THR   A HG23 1 
ATOM   2828 N  N    . VAL   A 1 147 ? 21.980 -16.643 2.404   1.00 12.98 ?  147 VAL   A N    1 
ATOM   2829 C  CA   . VAL   A 1 147 ? 22.468 -16.341 3.743   1.00 12.92 ?  147 VAL   A CA   1 
ATOM   2830 C  C    . VAL   A 1 147 ? 22.143 -17.510 4.662   1.00 13.79 ?  147 VAL   A C    1 
ATOM   2831 O  O    . VAL   A 1 147 ? 21.001 -17.998 4.700   1.00 13.90 ?  147 VAL   A O    1 
ATOM   2832 C  CB   . VAL   A 1 147 ? 21.858 -15.022 4.255   1.00 13.75 ?  147 VAL   A CB   1 
ATOM   2833 C  CG1  . VAL   A 1 147 ? 22.397 -14.697 5.635   1.00 15.32 ?  147 VAL   A CG1  1 
ATOM   2834 C  CG2  . VAL   A 1 147 ? 22.136 -13.884 3.270   1.00 13.87 ?  147 VAL   A CG2  1 
ATOM   2835 H  H    . VAL   A 1 147 ? 21.211 -16.290 2.226   1.00 15.59 ?  147 VAL   A H    1 
ATOM   2836 H  HA   . VAL   A 1 147 ? 23.432 -16.236 3.710   1.00 15.51 ?  147 VAL   A HA   1 
ATOM   2837 H  HB   . VAL   A 1 147 ? 20.899 -15.126 4.328   1.00 16.51 ?  147 VAL   A HB   1 
ATOM   2838 H  HG11 . VAL   A 1 147 ? 22.134 -13.799 5.872   1.00 18.39 ?  147 VAL   A HG11 1 
ATOM   2839 H  HG12 . VAL   A 1 147 ? 22.031 -15.332 6.273   1.00 18.39 ?  147 VAL   A HG12 1 
ATOM   2840 H  HG13 . VAL   A 1 147 ? 23.366 -14.768 5.619   1.00 18.39 ?  147 VAL   A HG13 1 
ATOM   2841 H  HG21 . VAL   A 1 147 ? 21.821 -13.050 3.654   1.00 16.65 ?  147 VAL   A HG21 1 
ATOM   2842 H  HG22 . VAL   A 1 147 ? 23.089 -13.832 3.104   1.00 16.65 ?  147 VAL   A HG22 1 
ATOM   2843 H  HG23 . VAL   A 1 147 ? 21.665 -14.062 2.440   1.00 16.65 ?  147 VAL   A HG23 1 
ATOM   2844 N  N    . ARG   A 1 148 ? 23.163 -17.998 5.363   1.00 14.31 ?  148 ARG   A N    1 
ATOM   2845 C  CA   . ARG   A 1 148 ? 23.038 -19.078 6.325   1.00 14.03 ?  148 ARG   A CA   1 
ATOM   2846 C  C    . ARG   A 1 148 ? 23.172 -18.608 7.765   1.00 14.31 ?  148 ARG   A C    1 
ATOM   2847 O  O    . ARG   A 1 148 ? 22.752 -19.333 8.679   1.00 16.11 ?  148 ARG   A O    1 
ATOM   2848 C  CB   . ARG   A 1 148 ? 24.085 -20.166 6.036   1.00 14.24 ?  148 ARG   A CB   1 
ATOM   2849 C  CG   . ARG   A 1 148 ? 23.885 -20.826 4.686   1.00 16.22 ?  148 ARG   A CG   1 
ATOM   2850 C  CD   . ARG   A 1 148 ? 24.976 -21.844 4.360   1.00 16.91 ?  148 ARG   A CD   1 
ATOM   2851 N  NE   . ARG   A 1 148 ? 26.318 -21.269 4.381   1.00 16.68 ?  148 ARG   A NE   1 
ATOM   2852 C  CZ   . ARG   A 1 148 ? 26.828 -20.517 3.414   1.00 16.17 ?  148 ARG   A CZ   1 
ATOM   2853 N  NH1  . ARG   A 1 148 ? 26.146 -20.258 2.309   1.00 16.90 ?  148 ARG   A NH1  1 
ATOM   2854 N  NH2  . ARG   A 1 148 ? 28.052 -20.000 3.563   1.00 16.41 ?  148 ARG   A NH2  1 
ATOM   2855 H  H    . ARG   A 1 148 ? 23.968 -17.708 5.279   1.00 17.19 ?  148 ARG   A H    1 
ATOM   2856 H  HA   . ARG   A 1 148 ? 22.163 -19.482 6.228   1.00 16.84 ?  148 ARG   A HA   1 
ATOM   2857 H  HB2  . ARG   A 1 148 ? 24.967 -19.777 6.049   1.00 17.09 ?  148 ARG   A HB2  1 
ATOM   2858 H  HB3  . ARG   A 1 148 ? 24.013 -20.862 6.712   1.00 17.09 ?  148 ARG   A HB3  1 
ATOM   2859 H  HG2  . ARG   A 1 148 ? 23.031 -21.285 4.681   1.00 19.48 ?  148 ARG   A HG2  1 
ATOM   2860 H  HG3  . ARG   A 1 148 ? 23.896 -20.139 4.000   1.00 19.48 ?  148 ARG   A HG3  1 
ATOM   2861 H  HD2  . ARG   A 1 148 ? 24.949 -22.558 5.012   1.00 20.30 ?  148 ARG   A HD2  1 
ATOM   2862 H  HD3  . ARG   A 1 148 ? 24.818 -22.201 3.470   1.00 20.30 ?  148 ARG   A HD3  1 
ATOM   2863 H  HE   . ARG   A 1 148 ? 26.813 -21.425 5.066   1.00 20.03 ?  148 ARG   A HE   1 
ATOM   2864 H  HH11 . ARG   A 1 148 ? 25.355 -20.572 2.204   1.00 20.29 ?  148 ARG   A HH11 1 
ATOM   2865 H  HH12 . ARG   A 1 148 ? 26.492 -19.755 1.698   1.00 20.29 ?  148 ARG   A HH12 1 
ATOM   2866 H  HH21 . ARG   A 1 148 ? 28.501 -20.156 4.279   1.00 19.70 ?  148 ARG   A HH21 1 
ATOM   2867 H  HH22 . ARG   A 1 148 ? 28.391 -19.501 2.946   1.00 19.70 ?  148 ARG   A HH22 1 
ATOM   2868 N  N    . THR   A 1 149 ? 23.713 -17.411 7.978   1.00 14.30 ?  149 THR   A N    1 
ATOM   2869 C  CA   . THR   A 1 149 ? 23.793 -16.808 9.296   1.00 14.34 ?  149 THR   A CA   1 
ATOM   2870 C  C    . THR   A 1 149 ? 22.466 -16.122 9.609   1.00 14.56 ?  149 THR   A C    1 
ATOM   2871 O  O    . THR   A 1 149 ? 21.543 -16.102 8.791   1.00 14.68 ?  149 THR   A O    1 
ATOM   2872 C  CB   . THR   A 1 149 ? 24.995 -15.872 9.355   1.00 15.36 ?  149 THR   A CB   1 
ATOM   2873 O  OG1  . THR   A 1 149 ? 24.874 -14.925 8.292   1.00 15.23 ?  149 THR   A OG1  1 
ATOM   2874 C  CG2  . THR   A 1 149 ? 26.300 -16.686 9.221   1.00 16.37 ?  149 THR   A CG2  1 
ATOM   2875 H  H    . THR   A 1 149 ? 24.058 -16.919 7.355   1.00 17.17 ?  149 THR   A H    1 
ATOM   2876 H  HA   . THR   A 1 149 ? 23.919 -17.512 9.949   1.00 17.22 ?  149 THR   A HA   1 
ATOM   2877 H  HB   . THR   A 1 149 ? 24.999 -15.416 10.208  1.00 18.44 ?  149 THR   A HB   1 
ATOM   2878 H  HG1  . THR   A 1 149 ? 25.529 -14.395 8.303   1.00 18.29 ?  149 THR   A HG1  1 
ATOM   2879 H  HG21 . THR   A 1 149 ? 27.064 -16.098 9.286   1.00 19.65 ?  149 THR   A HG21 1 
ATOM   2880 H  HG22 . THR   A 1 149 ? 26.350 -17.354 9.924   1.00 19.65 ?  149 THR   A HG22 1 
ATOM   2881 H  HG23 . THR   A 1 149 ? 26.322 -17.140 8.360   1.00 19.65 ?  149 THR   A HG23 1 
ATOM   2882 N  N    . ASN   A 1 150 ? 22.356 -15.570 10.810  1.00 14.29 ?  150 ASN   A N    1 
ATOM   2883 C  CA   . ASN   A 1 150 ? 21.081 -15.052 11.299  1.00 14.88 ?  150 ASN   A CA   1 
ATOM   2884 C  C    . ASN   A 1 150 ? 20.900 -13.610 10.843  1.00 14.57 ?  150 ASN   A C    1 
ATOM   2885 O  O    . ASN   A 1 150 ? 21.640 -12.708 11.266  1.00 15.50 ?  150 ASN   A O    1 
ATOM   2886 C  CB   . ASN   A 1 150 ? 21.019 -15.182 12.815  1.00 17.78 ?  150 ASN   A CB   1 
ATOM   2887 C  CG   . ASN   A 1 150 ? 20.905 -16.614 13.254  1.00 22.12 ?  150 ASN   A CG   1 
ATOM   2888 O  OD1  . ASN   A 1 150 ? 20.263 -17.418 12.584  1.00 23.79 ?  150 ASN   A OD1  1 
ATOM   2889 N  ND2  . ASN   A 1 150 ? 21.542 -16.952 14.367  1.00 25.20 ?  150 ASN   A ND2  1 
ATOM   2890 H  H    . ASN   A 1 150 ? 23.010 -15.473 11.360  1.00 17.16 ?  150 ASN   A H    1 
ATOM   2891 H  HA   . ASN   A 1 150 ? 20.362 -15.583 10.920  1.00 17.87 ?  150 ASN   A HA   1 
ATOM   2892 H  HB2  . ASN   A 1 150 ? 21.827 -14.814 13.200  1.00 21.34 ?  150 ASN   A HB2  1 
ATOM   2893 H  HB3  . ASN   A 1 150 ? 20.241 -14.707 13.143  1.00 21.34 ?  150 ASN   A HB3  1 
ATOM   2894 H  HD21 . ASN   A 1 150 ? 21.508 -17.766 14.660  1.00 30.24 ?  150 ASN   A HD21 1 
ATOM   2895 H  HD22 . ASN   A 1 150 ? 21.982 -16.362 14.811  1.00 30.24 ?  150 ASN   A HD22 1 
ATOM   2896 N  N    . VAL   A 1 151 ? 19.909 -13.381 9.989   1.00 14.29 ?  151 VAL   A N    1 
ATOM   2897 C  CA   . VAL   A 1 151 ? 19.699 -12.071 9.396   1.00 13.96 ?  151 VAL   A CA   1 
ATOM   2898 C  C    . VAL   A 1 151 ? 18.321 -11.547 9.776   1.00 13.61 ?  151 VAL   A C    1 
ATOM   2899 O  O    . VAL   A 1 151 ? 17.312 -12.263 9.651   1.00 15.26 ?  151 VAL   A O    1 
ATOM   2900 C  CB   . VAL   A 1 151 ? 19.964 -12.061 7.877   1.00 15.96 ?  151 VAL   A CB   1 
ATOM   2901 C  CG1  . VAL   A 1 151 ? 19.107 -13.060 7.140   1.00 17.07 ?  151 VAL   A CG1  1 
ATOM   2902 C  CG2  . VAL   A 1 151 ? 19.807 -10.641 7.310   1.00 15.85 ?  151 VAL   A CG2  1 
ATOM   2903 H  H    . VAL   A 1 151 ? 19.345 -13.974 9.735   1.00 17.16 ?  151 VAL   A H    1 
ATOM   2904 H  HA   . VAL   A 1 151 ? 20.341 -11.457 9.786   1.00 16.76 ?  151 VAL   A HA   1 
ATOM   2905 H  HB   . VAL   A 1 151 ? 20.889 -12.321 7.733   1.00 19.17 ?  151 VAL   A HB   1 
ATOM   2906 H  HG11 . VAL   A 1 151 ? 19.304 -13.012 6.188   1.00 20.50 ?  151 VAL   A HG11 1 
ATOM   2907 H  HG12 . VAL   A 1 151 ? 19.306 -13.954 7.467   1.00 20.50 ?  151 VAL   A HG12 1 
ATOM   2908 H  HG13 . VAL   A 1 151 ? 18.172 -12.856 7.291   1.00 20.50 ?  151 VAL   A HG13 1 
ATOM   2909 H  HG21 . VAL   A 1 151 ? 20.100 -10.638 6.379   1.00 19.03 ?  151 VAL   A HG21 1 
ATOM   2910 H  HG22 . VAL   A 1 151 ? 18.878 -10.375 7.360   1.00 19.03 ?  151 VAL   A HG22 1 
ATOM   2911 H  HG23 . VAL   A 1 151 ? 20.359 -10.030 7.823   1.00 19.03 ?  151 VAL   A HG23 1 
ATOM   2912 N  N    A TYR   A 1 152 ? 18.301 -10.299 10.245  0.74 13.59 ?  152 TYR   A N    1 
ATOM   2913 N  N    B TYR   A 1 152 ? 18.290 -10.294 10.235  0.26 13.99 ?  152 TYR   A N    1 
ATOM   2914 C  CA   A TYR   A 1 152 ? 17.104 -9.563  10.629  0.74 13.39 ?  152 TYR   A CA   1 
ATOM   2915 C  CA   B TYR   A 1 152 ? 17.078 -9.594  10.641  0.26 14.21 ?  152 TYR   A CA   1 
ATOM   2916 C  C    A TYR   A 1 152 ? 16.896 -8.462  9.598   0.74 13.57 ?  152 TYR   A C    1 
ATOM   2917 C  C    B TYR   A 1 152 ? 16.867 -8.435  9.677   0.26 13.47 ?  152 TYR   A C    1 
ATOM   2918 O  O    A TYR   A 1 152 ? 17.676 -7.504  9.538   0.74 13.35 ?  152 TYR   A O    1 
ATOM   2919 O  O    B TYR   A 1 152 ? 17.597 -7.440  9.723   0.26 13.53 ?  152 TYR   A O    1 
ATOM   2920 C  CB   A TYR   A 1 152 ? 17.278 -9.018  12.045  0.74 14.28 ?  152 TYR   A CB   1 
ATOM   2921 C  CB   B TYR   A 1 152 ? 17.214 -9.100  12.078  0.26 15.40 ?  152 TYR   A CB   1 
ATOM   2922 C  CG   A TYR   A 1 152 ? 17.228 -10.148 13.045  0.74 15.40 ?  152 TYR   A CG   1 
ATOM   2923 C  CG   B TYR   A 1 152 ? 17.173 -10.227 13.080  0.26 16.32 ?  152 TYR   A CG   1 
ATOM   2924 C  CD1  A TYR   A 1 152 ? 18.354 -10.914 13.313  0.74 16.85 ?  152 TYR   A CD1  1 
ATOM   2925 C  CD1  B TYR   A 1 152 ? 18.313 -10.960 13.375  0.26 16.98 ?  152 TYR   A CD1  1 
ATOM   2926 C  CD2  A TYR   A 1 152 ? 16.038 -10.495 13.675  0.74 15.67 ?  152 TYR   A CD2  1 
ATOM   2927 C  CD2  B TYR   A 1 152 ? 15.988 -10.573 13.714  0.26 16.66 ?  152 TYR   A CD2  1 
ATOM   2928 C  CE1  A TYR   A 1 152 ? 18.310 -11.974 14.196  0.74 17.85 ?  152 TYR   A CE1  1 
ATOM   2929 C  CE1  B TYR   A 1 152 ? 18.278 -12.002 14.280  0.26 17.67 ?  152 TYR   A CE1  1 
ATOM   2930 C  CE2  A TYR   A 1 152 ? 15.981 -11.561 14.566  0.74 16.93 ?  152 TYR   A CE2  1 
ATOM   2931 C  CE2  B TYR   A 1 152 ? 15.942 -11.616 14.622  0.26 17.25 ?  152 TYR   A CE2  1 
ATOM   2932 C  CZ   A TYR   A 1 152 ? 17.123 -12.295 14.821  0.74 17.53 ?  152 TYR   A CZ   1 
ATOM   2933 C  CZ   B TYR   A 1 152 ? 17.091 -12.327 14.901  0.26 17.86 ?  152 TYR   A CZ   1 
ATOM   2934 O  OH   A TYR   A 1 152 ? 17.078 -13.360 15.699  0.74 20.06 ?  152 TYR   A OH   1 
ATOM   2935 O  OH   B TYR   A 1 152 ? 17.051 -13.368 15.803  0.26 19.26 ?  152 TYR   A OH   1 
ATOM   2936 H  H    A TYR   A 1 152 ? 19.016 -9.828  10.344  0.74 16.32 ?  152 TYR   A H    1 
ATOM   2937 H  H    B TYR   A 1 152 ? 18.996 -9.806  10.317  0.26 16.80 ?  152 TYR   A H    1 
ATOM   2938 H  HA   A TYR   A 1 152 ? 16.336 -10.157 10.615  0.74 16.08 ?  152 TYR   A HA   1 
ATOM   2939 H  HA   B TYR   A 1 152 ? 16.316 -10.188 10.581  0.26 17.06 ?  152 TYR   A HA   1 
ATOM   2940 H  HB2  A TYR   A 1 152 ? 18.139 -8.579  12.121  0.74 17.15 ?  152 TYR   A HB2  1 
ATOM   2941 H  HB2  B TYR   A 1 152 ? 18.064 -8.643  12.174  0.26 18.49 ?  152 TYR   A HB2  1 
ATOM   2942 H  HB3  A TYR   A 1 152 ? 16.560 -8.398  12.246  0.74 17.15 ?  152 TYR   A HB3  1 
ATOM   2943 H  HB3  B TYR   A 1 152 ? 16.488 -8.490  12.277  0.26 18.49 ?  152 TYR   A HB3  1 
ATOM   2944 H  HD1  A TYR   A 1 152 ? 19.156 -10.705 12.891  0.74 20.23 ?  152 TYR   A HD1  1 
ATOM   2945 H  HD1  B TYR   A 1 152 ? 19.115 -10.745 12.954  0.26 20.39 ?  152 TYR   A HD1  1 
ATOM   2946 H  HD2  A TYR   A 1 152 ? 15.266 -10.004 13.501  0.74 18.81 ?  152 TYR   A HD2  1 
ATOM   2947 H  HD2  B TYR   A 1 152 ? 15.211 -10.095 13.524  0.26 20.00 ?  152 TYR   A HD2  1 
ATOM   2948 H  HE1  A TYR   A 1 152 ? 19.075 -12.473 14.370  0.74 21.43 ?  152 TYR   A HE1  1 
ATOM   2949 H  HE1  B TYR   A 1 152 ? 19.050 -12.483 14.470  0.26 21.21 ?  152 TYR   A HE1  1 
ATOM   2950 H  HE2  A TYR   A 1 152 ? 15.180 -11.780 14.988  0.74 20.33 ?  152 TYR   A HE2  1 
ATOM   2951 H  HE2  B TYR   A 1 152 ? 15.141 -11.835 15.042  0.26 20.71 ?  152 TYR   A HE2  1 
ATOM   2952 H  HH   A TYR   A 1 152 ? 16.298 -13.445 16.010  0.74 24.08 ?  152 TYR   A HH   1 
ATOM   2953 H  HH   B TYR   A 1 152 ? 16.272 -13.451 16.109  0.26 23.12 ?  152 TYR   A HH   1 
ATOM   2954 N  N    A LEU   A 1 153 ? 15.874 -8.628  8.759   0.74 13.85 ?  153 LEU   A N    1 
ATOM   2955 N  N    B LEU   A 1 153 ? 15.873 -8.573  8.804   0.26 13.04 ?  153 LEU   A N    1 
ATOM   2956 C  CA   A LEU   A 1 153 ? 15.615 -7.753  7.621   0.74 13.48 ?  153 LEU   A CA   1 
ATOM   2957 C  CA   B LEU   A 1 153 ? 15.605 -7.597  7.758   0.26 12.72 ?  153 LEU   A CA   1 
ATOM   2958 C  C    A LEU   A 1 153 ? 14.610 -6.676  7.999   0.74 14.00 ?  153 LEU   A C    1 
ATOM   2959 C  C    B LEU   A 1 153 ? 14.628 -6.546  8.265   0.26 12.95 ?  153 LEU   A C    1 
ATOM   2960 O  O    A LEU   A 1 153 ? 13.490 -6.984  8.424   0.74 15.24 ?  153 LEU   A O    1 
ATOM   2961 O  O    B LEU   A 1 153 ? 13.564 -6.881  8.795   0.26 13.41 ?  153 LEU   A O    1 
ATOM   2962 C  CB   A LEU   A 1 153 ? 15.055 -8.554  6.446   0.74 13.77 ?  153 LEU   A CB   1 
ATOM   2963 C  CB   B LEU   A 1 153 ? 15.015 -8.294  6.530   0.26 12.99 ?  153 LEU   A CB   1 
ATOM   2964 C  CG   A LEU   A 1 153 ? 15.997 -9.571  5.807   0.74 14.18 ?  153 LEU   A CG   1 
ATOM   2965 C  CG   B LEU   A 1 153 ? 15.923 -9.295  5.816   0.26 12.34 ?  153 LEU   A CG   1 
ATOM   2966 C  CD1  A LEU   A 1 153 ? 15.252 -10.413 4.796   0.74 14.37 ?  153 LEU   A CD1  1 
ATOM   2967 C  CD1  B LEU   A 1 153 ? 15.116 -10.183 4.887   0.26 12.58 ?  153 LEU   A CD1  1 
ATOM   2968 C  CD2  A LEU   A 1 153 ? 17.189 -8.875  5.152   0.74 14.46 ?  153 LEU   A CD2  1 
ATOM   2969 C  CD2  B LEU   A 1 153 ? 17.003 -8.568  5.038   0.26 12.48 ?  153 LEU   A CD2  1 
ATOM   2970 H  H    A LEU   A 1 153 ? 15.295 -9.268  8.829   0.74 16.62 ?  153 LEU   A H    1 
ATOM   2971 H  H    B LEU   A 1 153 ? 15.324 -9.235  8.801   0.26 15.65 ?  153 LEU   A H    1 
ATOM   2972 H  HA   A LEU   A 1 153 ? 16.439 -7.325  7.351   0.74 16.19 ?  153 LEU   A HA   1 
ATOM   2973 H  HA   B LEU   A 1 153 ? 16.428 -7.161  7.502   0.26 15.28 ?  153 LEU   A HA   1 
ATOM   2974 H  HB2  A LEU   A 1 153 ? 14.267 -9.027  6.754   0.74 16.53 ?  153 LEU   A HB2  1 
ATOM   2975 H  HB2  B LEU   A 1 153 ? 14.218 -8.771  6.805   0.26 15.59 ?  153 LEU   A HB2  1 
ATOM   2976 H  HB3  A LEU   A 1 153 ? 14.794 -7.920  5.753   0.74 16.53 ?  153 LEU   A HB3  1 
ATOM   2977 H  HB3  B LEU   A 1 153 ? 14.774 -7.614  5.880   0.26 15.59 ?  153 LEU   A HB3  1 
ATOM   2978 H  HG   A LEU   A 1 153 ? 16.331 -10.160 6.502   0.74 17.03 ?  153 LEU   A HG   1 
ATOM   2979 H  HG   B LEU   A 1 153 ? 16.352 -9.864  6.476   0.26 14.81 ?  153 LEU   A HG   1 
ATOM   2980 H  HD11 A LEU   A 1 153 ? 15.793 -11.180 4.567   0.74 17.25 ?  153 LEU   A HD11 1 
ATOM   2981 H  HD11 B LEU   A 1 153 ? 15.714 -10.811 4.452   0.26 15.10 ?  153 LEU   A HD11 1 
ATOM   2982 H  HD12 A LEU   A 1 153 ? 14.412 -10.703 5.186   0.74 17.25 ?  153 LEU   A HD12 1 
ATOM   2983 H  HD12 B LEU   A 1 153 ? 14.451 -10.663 5.404   0.26 15.10 ?  153 LEU   A HD12 1 
ATOM   2984 H  HD13 A LEU   A 1 153 ? 15.079 -9.874  4.008   0.74 17.25 ?  153 LEU   A HD13 1 
ATOM   2985 H  HD13 B LEU   A 1 153 ? 14.680 -9.627  4.221   0.26 15.10 ?  153 LEU   A HD13 1 
ATOM   2986 H  HD21 A LEU   A 1 153 ? 17.740 -9.544  4.722   0.74 17.36 ?  153 LEU   A HD21 1 
ATOM   2987 H  HD21 B LEU   A 1 153 ? 17.555 -9.221  4.582   0.26 14.98 ?  153 LEU   A HD21 1 
ATOM   2988 H  HD22 A LEU   A 1 153 ? 16.860 -8.242  4.499   0.74 17.36 ?  153 LEU   A HD22 1 
ATOM   2989 H  HD22 B LEU   A 1 153 ? 16.580 -7.981  4.392   0.26 14.98 ?  153 LEU   A HD22 1 
ATOM   2990 H  HD23 A LEU   A 1 153 ? 17.698 -8.415  5.837   0.74 17.36 ?  153 LEU   A HD23 1 
ATOM   2991 H  HD23 B LEU   A 1 153 ? 17.539 -8.051  5.657   0.26 14.98 ?  153 LEU   A HD23 1 
ATOM   2992 N  N    A ALA   A 1 154 ? 15.002 -5.419  7.796   0.74 13.77 ?  154 ALA   A N    1 
ATOM   2993 N  N    B ALA   A 1 154 ? 14.997 -5.278  8.105   0.26 13.11 ?  154 ALA   A N    1 
ATOM   2994 C  CA   A ALA   A 1 154 ? 14.144 -4.264  8.021   0.74 14.06 ?  154 ALA   A CA   1 
ATOM   2995 C  CA   B ALA   A 1 154 ? 14.125 -4.153  8.411   0.26 13.47 ?  154 ALA   A CA   1 
ATOM   2996 C  C    A ALA   A 1 154 ? 13.646 -3.763  6.672   0.74 13.46 ?  154 ALA   A C    1 
ATOM   2997 C  C    B ALA   A 1 154 ? 13.655 -3.550  7.095   0.26 13.12 ?  154 ALA   A C    1 
ATOM   2998 O  O    A ALA   A 1 154 ? 14.449 -3.419  5.798   0.74 13.51 ?  154 ALA   A O    1 
ATOM   2999 O  O    B ALA   A 1 154 ? 14.473 -3.084  6.295   0.26 12.71 ?  154 ALA   A O    1 
ATOM   3000 C  CB   A ALA   A 1 154 ? 14.920 -3.161  8.739   0.74 14.17 ?  154 ALA   A CB   1 
ATOM   3001 C  CB   B ALA   A 1 154 ? 14.860 -3.106  9.245   0.26 13.71 ?  154 ALA   A CB   1 
ATOM   3002 H  H    A ALA   A 1 154 ? 15.786 -5.209  7.513   0.74 16.53 ?  154 ALA   A H    1 
ATOM   3003 H  H    B ALA   A 1 154 ? 15.773 -5.040  7.820   0.26 15.74 ?  154 ALA   A H    1 
ATOM   3004 H  HA   A ALA   A 1 154 ? 13.384 -4.513  8.568   0.74 16.88 ?  154 ALA   A HA   1 
ATOM   3005 H  HA   B ALA   A 1 154 ? 13.352 -4.459  8.908   0.26 16.17 ?  154 ALA   A HA   1 
ATOM   3006 H  HB1  A ALA   A 1 154 ? 14.336 -2.398  8.879   0.74 17.01 ?  154 ALA   A HB1  1 
ATOM   3007 H  HB1  B ALA   A 1 154 ? 14.256 -2.369  9.431   0.26 16.46 ?  154 ALA   A HB1  1 
ATOM   3008 H  HB2  A ALA   A 1 154 ? 15.238 -3.494  9.594   0.74 17.01 ?  154 ALA   A HB2  1 
ATOM   3009 H  HB2  B ALA   A 1 154 ? 15.152 -3.512  10.076  0.26 16.46 ?  154 ALA   A HB2  1 
ATOM   3010 H  HB3  A ALA   A 1 154 ? 15.679 -2.895  8.190   0.74 17.01 ?  154 ALA   A HB3  1 
ATOM   3011 H  HB3  B ALA   A 1 154 ? 15.628 -2.785  8.746   0.26 16.46 ?  154 ALA   A HB3  1 
ATOM   3012 N  N    A VAL   A 1 155 ? 12.327 -3.729  6.504   0.64 12.98 ?  155 VAL   A N    1 
ATOM   3013 N  N    B VAL   A 1 155 ? 12.344 -3.566  6.875   0.26 13.70 ?  155 VAL   A N    1 
ATOM   3014 C  CA   A VAL   A 1 155 ? 11.683 -3.300  5.267   0.64 14.90 ?  155 VAL   A CA   1 
ATOM   3015 C  CA   B VAL   A 1 155 ? 11.731 -3.037  5.662   0.26 14.87 ?  155 VAL   A CA   1 
ATOM   3016 C  CA   T VAL   A 1 155 ? 11.655 -3.322  5.384   0.10 16.16 ?  155 VAL   A CA   1 
ATOM   3017 C  C    A VAL   A 1 155 ? 10.938 -2.004  5.564   0.64 15.86 ?  155 VAL   A C    1 
ATOM   3018 C  C    B VAL   A 1 155 ? 10.933 -1.804  6.058   0.26 16.58 ?  155 VAL   A C    1 
ATOM   3019 C  C    T VAL   A 1 155 ? 11.049 -1.952  5.686   0.10 16.34 ?  155 VAL   A C    1 
ATOM   3020 O  O    A VAL   A 1 155 ? 9.955  -1.997  6.314   0.64 16.84 ?  155 VAL   A O    1 
ATOM   3021 O  O    B VAL   A 1 155 ? 9.981  -1.895  6.843   0.26 16.80 ?  155 VAL   A O    1 
ATOM   3022 O  O    T VAL   A 1 155 ? 10.206 -1.814  6.571   0.10 16.17 ?  155 VAL   A O    1 
ATOM   3023 C  CB   A VAL   A 1 155 ? 10.739 -4.376  4.713   0.64 15.57 ?  155 VAL   A CB   1 
ATOM   3024 C  CB   B VAL   A 1 155 ? 10.854 -4.089  4.965   0.26 14.61 ?  155 VAL   A CB   1 
ATOM   3025 C  CB   T VAL   A 1 155 ? 10.632 -4.294  4.762   0.10 16.00 ?  155 VAL   A CB   1 
ATOM   3026 C  CG1  A VAL   A 1 155 ? 10.034 -3.875  3.459   0.64 16.10 ?  155 VAL   A CG1  1 
ATOM   3027 C  CG1  B VAL   A 1 155 ? 10.146 -3.486  3.762   0.26 14.71 ?  155 VAL   A CG1  1 
ATOM   3028 C  CG1  T VAL   A 1 155 ? 9.972  -3.670  3.543   0.10 15.98 ?  155 VAL   A CG1  1 
ATOM   3029 C  CG2  A VAL   A 1 155 ? 11.524 -5.647  4.409   0.64 16.40 ?  155 VAL   A CG2  1 
ATOM   3030 C  CG2  B VAL   A 1 155 ? 11.710 -5.281  4.541   0.26 14.51 ?  155 VAL   A CG2  1 
ATOM   3031 C  CG2  T VAL   A 1 155 ? 11.309 -5.609  4.392   0.10 16.07 ?  155 VAL   A CG2  1 
ATOM   3032 H  H    A VAL   A 1 155 ? 11.771 -3.980  7.111   0.64 15.59 ?  155 VAL   A H    1 
ATOM   3033 H  H    B VAL   A 1 155 ? 11.771 -3.876  7.436   0.26 16.44 ?  155 VAL   A H    1 
ATOM   3034 H  HA   A VAL   A 1 155 ? 12.365 -3.120  4.600   0.64 17.89 ?  155 VAL   A HA   1 
ATOM   3035 H  HA   B VAL   A 1 155 ? 12.425 -2.768  5.040   0.26 17.86 ?  155 VAL   A HA   1 
ATOM   3036 H  HB   A VAL   A 1 155 ? 10.067 -4.589  5.381   0.64 18.69 ?  155 VAL   A HB   1 
ATOM   3037 H  HB   B VAL   A 1 155 ? 10.183 -4.410  5.588   0.26 17.54 ?  155 VAL   A HB   1 
ATOM   3038 H  HB   T VAL   A 1 155 ? 9.941  -4.487  5.415   0.10 19.20 ?  155 VAL   A HB   1 
ATOM   3039 H  HG11 A VAL   A 1 155 ? 9.581  -4.621  3.035   0.64 19.33 ?  155 VAL   A HG11 1 
ATOM   3040 H  HG11 B VAL   A 1 155 ? 9.767  -4.203  3.229   0.26 17.66 ?  155 VAL   A HG11 1 
ATOM   3041 H  HG11 T VAL   A 1 155 ? 9.496  -4.361  3.055   0.10 19.19 ?  155 VAL   A HG11 1 
ATOM   3042 H  HG12 A VAL   A 1 155 ? 9.389  -3.196  3.709   0.64 19.33 ?  155 VAL   A HG12 1 
ATOM   3043 H  HG12 B VAL   A 1 155 ? 9.442  -2.897  4.072   0.26 17.66 ?  155 VAL   A HG12 1 
ATOM   3044 H  HG12 T VAL   A 1 155 ? 9.351  -2.985  3.834   0.10 19.19 ?  155 VAL   A HG12 1 
ATOM   3045 H  HG13 A VAL   A 1 155 ? 10.694 -3.503  2.855   0.64 19.33 ?  155 VAL   A HG13 1 
ATOM   3046 H  HG13 B VAL   A 1 155 ? 10.791 -2.989  3.236   0.26 17.66 ?  155 VAL   A HG13 1 
ATOM   3047 H  HG13 T VAL   A 1 155 ? 10.658 -3.282  2.978   0.10 19.19 ?  155 VAL   A HG13 1 
ATOM   3048 H  HG21 A VAL   A 1 155 ? 10.931 -6.294  3.993   0.64 19.69 ?  155 VAL   A HG21 1 
ATOM   3049 H  HG21 B VAL   A 1 155 ? 11.151 -5.926  4.081   0.26 17.42 ?  155 VAL   A HG21 1 
ATOM   3050 H  HG21 T VAL   A 1 155 ? 10.650 -6.209  4.008   0.10 19.29 ?  155 VAL   A HG21 1 
ATOM   3051 H  HG22 A VAL   A 1 155 ? 12.253 -5.432  3.805   0.64 19.69 ?  155 VAL   A HG22 1 
ATOM   3052 H  HG22 B VAL   A 1 155 ? 12.413 -4.970  3.948   0.26 17.42 ?  155 VAL   A HG22 1 
ATOM   3053 H  HG22 T VAL   A 1 155 ? 12.010 -5.432  3.744   0.10 19.29 ?  155 VAL   A HG22 1 
ATOM   3054 H  HG23 A VAL   A 1 155 ? 11.878 -6.010  5.237   0.64 19.69 ?  155 VAL   A HG23 1 
ATOM   3055 H  HG23 B VAL   A 1 155 ? 12.103 -5.688  5.330   0.26 17.42 ?  155 VAL   A HG23 1 
ATOM   3056 H  HG23 T VAL   A 1 155 ? 11.691 -6.005  5.191   0.10 19.29 ?  155 VAL   A HG23 1 
ATOM   3057 N  N    A PHE   A 1 156 ? 11.405 -0.901  4.973   0.64 17.85 ?  156 PHE   A N    1 
ATOM   3058 N  N    B PHE   A 1 156 ? 11.333 -0.648  5.525   0.26 17.60 ?  156 PHE   A N    1 
ATOM   3059 N  N    T PHE   A 1 156 ? 11.498 -0.937  4.943   0.10 16.88 ?  156 PHE   A N    1 
ATOM   3060 C  CA   A PHE   A 1 156 ? 10.881 0.421   5.328   0.64 19.77 ?  156 PHE   A CA   1 
ATOM   3061 C  CA   B PHE   A 1 156 ? 10.764 0.617   5.981   0.26 19.16 ?  156 PHE   A CA   1 
ATOM   3062 C  CA   T PHE   A 1 156 ? 11.064 0.432   5.212   0.10 17.42 ?  156 PHE   A CA   1 
ATOM   3063 C  C    A PHE   A 1 156 ? 9.408  0.577   4.956   0.64 20.24 ?  156 PHE   A C    1 
ATOM   3064 C  C    B PHE   A 1 156 ? 9.286  0.742   5.624   0.26 19.22 ?  156 PHE   A C    1 
ATOM   3065 C  C    T PHE   A 1 156 ? 9.608  0.649   4.816   0.10 17.82 ?  156 PHE   A C    1 
ATOM   3066 O  O    A PHE   A 1 156 ? 8.622  1.135   5.731   0.64 21.39 ?  156 PHE   A O    1 
ATOM   3067 O  O    B PHE   A 1 156 ? 8.486  1.214   6.440   0.26 19.61 ?  156 PHE   A O    1 
ATOM   3068 O  O    T PHE   A 1 156 ? 8.852  1.301   5.546   0.10 18.13 ?  156 PHE   A O    1 
ATOM   3069 C  CB   A PHE   A 1 156 ? 11.726 1.505   4.659   0.64 20.82 ?  156 PHE   A CB   1 
ATOM   3070 C  CB   B PHE   A 1 156 ? 11.560 1.782   5.395   0.26 20.69 ?  156 PHE   A CB   1 
ATOM   3071 C  CB   T PHE   A 1 156 ? 11.972 1.412   4.468   0.10 17.45 ?  156 PHE   A CB   1 
ATOM   3072 C  CG   A PHE   A 1 156 ? 11.278 2.911   4.978   0.64 23.22 ?  156 PHE   A CG   1 
ATOM   3073 C  CG   B PHE   A 1 156 ? 10.995 3.131   5.734   0.26 22.12 ?  156 PHE   A CG   1 
ATOM   3074 C  CG   T PHE   A 1 156 ? 11.606 2.858   4.666   0.10 17.69 ?  156 PHE   A CG   1 
ATOM   3075 C  CD1  A PHE   A 1 156 ? 11.283 3.371   6.288   0.64 24.67 ?  156 PHE   A CD1  1 
ATOM   3076 C  CD1  B PHE   A 1 156 ? 10.974 3.573   7.045   0.26 22.58 ?  156 PHE   A CD1  1 
ATOM   3077 C  CD1  T PHE   A 1 156 ? 11.976 3.528   5.821   0.10 17.89 ?  156 PHE   A CD1  1 
ATOM   3078 C  CD2  A PHE   A 1 156 ? 10.860 3.773   3.974   0.64 24.52 ?  156 PHE   A CD2  1 
ATOM   3079 C  CD2  B PHE   A 1 156 ? 10.492 3.958   4.744   0.26 22.69 ?  156 PHE   A CD2  1 
ATOM   3080 C  CD2  T PHE   A 1 156 ? 10.909 3.551   3.689   0.10 17.90 ?  156 PHE   A CD2  1 
ATOM   3081 C  CE1  A PHE   A 1 156 ? 10.874 4.659   6.593   0.64 26.03 ?  156 PHE   A CE1  1 
ATOM   3082 C  CE1  B PHE   A 1 156 ? 10.458 4.814   7.366   0.26 23.09 ?  156 PHE   A CE1  1 
ATOM   3083 C  CE1  T PHE   A 1 156 ? 11.647 4.859   6.004   0.10 17.93 ?  156 PHE   A CE1  1 
ATOM   3084 C  CE2  A PHE   A 1 156 ? 10.452 5.067   4.272   0.64 25.79 ?  156 PHE   A CE2  1 
ATOM   3085 C  CE2  B PHE   A 1 156 ? 9.974  5.201   5.058   0.26 23.30 ?  156 PHE   A CE2  1 
ATOM   3086 C  CE2  T PHE   A 1 156 ? 10.577 4.883   3.866   0.10 17.99 ?  156 PHE   A CE2  1 
ATOM   3087 C  CZ   A PHE   A 1 156 ? 10.464 5.510   5.585   0.64 26.29 ?  156 PHE   A CZ   1 
ATOM   3088 C  CZ   B PHE   A 1 156 ? 9.958  5.628   6.372   0.26 23.46 ?  156 PHE   A CZ   1 
ATOM   3089 C  CZ   T PHE   A 1 156 ? 10.948 5.538   5.026   0.10 18.00 ?  156 PHE   A CZ   1 
ATOM   3090 H  H    A PHE   A 1 156 ? 12.021 -0.895  4.374   0.64 21.43 ?  156 PHE   A H    1 
ATOM   3091 H  H    B PHE   A 1 156 ? 11.933 -0.573  4.913   0.26 21.13 ?  156 PHE   A H    1 
ATOM   3092 H  H    T PHE   A 1 156 ? 12.053 -1.015  4.291   0.10 20.27 ?  156 PHE   A H    1 
ATOM   3093 H  HA   A PHE   A 1 156 ? 10.961 0.540   6.286   0.64 23.74 ?  156 PHE   A HA   1 
ATOM   3094 H  HA   B PHE   A 1 156 ? 10.842 0.663   6.946   0.26 23.00 ?  156 PHE   A HA   1 
ATOM   3095 H  HA   T PHE   A 1 156 ? 11.146 0.606   6.161   0.10 20.92 ?  156 PHE   A HA   1 
ATOM   3096 H  HB2  A PHE   A 1 156 ? 12.646 1.416   4.953   0.64 25.00 ?  156 PHE   A HB2  1 
ATOM   3097 H  HB2  B PHE   A 1 156 ? 12.469 1.745   5.737   0.26 24.83 ?  156 PHE   A HB2  1 
ATOM   3098 H  HB2  T PHE   A 1 156 ? 12.881 1.291   4.781   0.10 20.95 ?  156 PHE   A HB2  1 
ATOM   3099 H  HB3  A PHE   A 1 156 ? 11.678 1.393   3.696   0.64 25.00 ?  156 PHE   A HB3  1 
ATOM   3100 H  HB3  B PHE   A 1 156 ? 11.572 1.698   4.428   0.26 24.83 ?  156 PHE   A HB3  1 
ATOM   3101 H  HB3  T PHE   A 1 156 ? 11.923 1.222   3.518   0.10 20.95 ?  156 PHE   A HB3  1 
ATOM   3102 H  HD1  A PHE   A 1 156 ? 11.563 2.800   6.971   0.64 29.61 ?  156 PHE   A HD1  1 
ATOM   3103 H  HD1  B PHE   A 1 156 ? 11.311 3.025   7.718   0.26 27.11 ?  156 PHE   A HD1  1 
ATOM   3104 H  HD1  T PHE   A 1 156 ? 12.445 3.075   6.485   0.10 21.48 ?  156 PHE   A HD1  1 
ATOM   3105 H  HD2  A PHE   A 1 156 ? 10.850 3.482   3.092   0.64 29.44 ?  156 PHE   A HD2  1 
ATOM   3106 H  HD2  B PHE   A 1 156 ? 10.502 3.674   3.858   0.26 27.24 ?  156 PHE   A HD2  1 
ATOM   3107 H  HD2  T PHE   A 1 156 ? 10.656 3.116   2.907   0.10 21.48 ?  156 PHE   A HD2  1 
ATOM   3108 H  HE1  A PHE   A 1 156 ? 10.885 4.951   7.478   0.64 31.25 ?  156 PHE   A HE1  1 
ATOM   3109 H  HE1  B PHE   A 1 156 ? 10.449 5.099   8.251   0.26 27.72 ?  156 PHE   A HE1  1 
ATOM   3110 H  HE1  T PHE   A 1 156 ? 11.896 5.296   6.786   0.10 21.52 ?  156 PHE   A HE1  1 
ATOM   3111 H  HE2  A PHE   A 1 156 ? 10.171 5.637   3.594   0.64 30.96 ?  156 PHE   A HE2  1 
ATOM   3112 H  HE2  B PHE   A 1 156 ? 9.639  5.749   4.386   0.26 27.97 ?  156 PHE   A HE2  1 
ATOM   3113 H  HE2  T PHE   A 1 156 ? 10.106 5.338   3.205   0.10 21.59 ?  156 PHE   A HE2  1 
ATOM   3114 H  HZ   A PHE   A 1 156 ? 10.188 6.374   5.791   0.64 31.56 ?  156 PHE   A HZ   1 
ATOM   3115 H  HZ   B PHE   A 1 156 ? 9.612  6.463   6.585   0.26 28.16 ?  156 PHE   A HZ   1 
ATOM   3116 H  HZ   T PHE   A 1 156 ? 10.726 6.432   5.149   0.10 21.61 ?  156 PHE   A HZ   1 
ATOM   3117 N  N    A ASP   A 1 157 ? 9.011  0.074   3.793   0.64 19.97 ?  157 ASP   A N    1 
ATOM   3118 N  N    B ASP   A 1 157 ? 8.902  0.328   4.418   0.26 18.57 ?  157 ASP   A N    1 
ATOM   3119 N  N    T ASP   A 1 157 ? 9.197  0.113   3.671   0.10 18.02 ?  157 ASP   A N    1 
ATOM   3120 C  CA   A ASP   A 1 157 ? 7.690  0.337   3.232   0.64 20.20 ?  157 ASP   A CA   1 
ATOM   3121 C  CA   B ASP   A 1 157 ? 7.550  0.565   3.928   0.26 18.71 ?  157 ASP   A CA   1 
ATOM   3122 C  CA   T ASP   A 1 157 ? 7.877  0.376   3.114   0.10 18.40 ?  157 ASP   A CA   1 
ATOM   3123 C  C    A ASP   A 1 157 ? 6.687  -0.701  3.735   0.64 20.55 ?  157 ASP   A C    1 
ATOM   3124 C  C    B ASP   A 1 157 ? 6.594  -0.520  4.413   0.26 19.64 ?  157 ASP   A C    1 
ATOM   3125 C  C    T ASP   A 1 157 ? 6.877  -0.629  3.676   0.10 19.24 ?  157 ASP   A C    1 
ATOM   3126 O  O    A ASP   A 1 157 ? 6.842  -1.900  3.475   0.64 18.85 ?  157 ASP   A O    1 
ATOM   3127 O  O    B ASP   A 1 157 ? 6.890  -1.715  4.308   0.26 19.94 ?  157 ASP   A O    1 
ATOM   3128 O  O    T ASP   A 1 157 ? 7.061  -1.843  3.533   0.10 19.11 ?  157 ASP   A O    1 
ATOM   3129 C  CB   A ASP   A 1 157 ? 7.797  0.282   1.710   0.64 20.72 ?  157 ASP   A CB   1 
ATOM   3130 C  CB   B ASP   A 1 157 ? 7.555  0.609   2.402   0.26 18.14 ?  157 ASP   A CB   1 
ATOM   3131 C  CB   T ASP   A 1 157 ? 7.941  0.290   1.591   0.10 17.96 ?  157 ASP   A CB   1 
ATOM   3132 C  CG   A ASP   A 1 157 ? 6.582  0.851   1.017   0.64 22.47 ?  157 ASP   A CG   1 
ATOM   3133 C  CG   B ASP   A 1 157 ? 6.206  0.980   1.825   0.26 18.07 ?  157 ASP   A CG   1 
ATOM   3134 C  CG   T ASP   A 1 157 ? 6.725  0.887   0.919   0.10 17.48 ?  157 ASP   A CG   1 
ATOM   3135 O  OD1  A ASP   A 1 157 ? 6.441  2.092   0.986   0.64 25.00 ?  157 ASP   A OD1  1 
ATOM   3136 O  OD1  B ASP   A 1 157 ? 5.795  2.155   1.944   0.26 17.75 ?  157 ASP   A OD1  1 
ATOM   3137 O  OD1  T ASP   A 1 157 ? 5.597  0.434   1.208   0.10 17.65 ?  157 ASP   A OD1  1 
ATOM   3138 O  OD2  A ASP   A 1 157 ? 5.768  0.056   0.496   0.64 22.09 -1 157 ASP   A OD2  1 
ATOM   3139 O  OD2  B ASP   A 1 157 ? 5.550  0.086   1.252   0.26 18.27 -1 157 ASP   A OD2  1 
ATOM   3140 O  OD2  T ASP   A 1 157 ? 6.900  1.816   0.103   0.10 16.94 -1 157 ASP   A OD2  1 
ATOM   3141 H  H    A ASP   A 1 157 ? 9.495  -0.445  3.306   0.64 23.97 ?  157 ASP   A H    1 
ATOM   3142 H  H    B ASP   A 1 157 ? 9.411  -0.092  3.865   0.26 22.29 ?  157 ASP   A H    1 
ATOM   3143 H  H    T ASP   A 1 157 ? 9.674  -0.415  3.189   0.10 21.64 ?  157 ASP   A H    1 
ATOM   3144 H  HA   A ASP   A 1 157 ? 7.392  1.221   3.498   0.64 24.25 ?  157 ASP   A HA   1 
ATOM   3145 H  HA   B ASP   A 1 157 ? 7.239  1.420   4.261   0.26 22.46 ?  157 ASP   A HA   1 
ATOM   3146 H  HA   T ASP   A 1 157 ? 7.590  1.268   3.362   0.10 22.09 ?  157 ASP   A HA   1 
ATOM   3147 H  HB2  A ASP   A 1 157 ? 8.577  0.791   1.434   0.64 24.87 ?  157 ASP   A HB2  1 
ATOM   3148 H  HB2  B ASP   A 1 157 ? 8.215  1.255   2.107   0.26 21.78 ?  157 ASP   A HB2  1 
ATOM   3149 H  HB2  T ASP   A 1 157 ? 8.726  0.768   1.282   0.10 21.56 ?  157 ASP   A HB2  1 
ATOM   3150 H  HB3  A ASP   A 1 157 ? 7.896  -0.642  1.437   0.64 24.87 ?  157 ASP   A HB3  1 
ATOM   3151 H  HB3  B ASP   A 1 157 ? 7.771  -0.270  2.061   0.26 21.78 ?  157 ASP   A HB3  1 
ATOM   3152 H  HB3  T ASP   A 1 157 ? 7.998  -0.639  1.326   0.10 21.56 ?  157 ASP   A HB3  1 
ATOM   3153 N  N    A LYS   A 1 158 ? 5.644  -0.239  4.435   0.64 21.97 ?  158 LYS   A N    1 
ATOM   3154 N  N    B LYS   A 1 158 ? 5.434  -0.099  4.926   0.26 20.23 ?  158 LYS   A N    1 
ATOM   3155 N  N    T LYS   A 1 158 ? 5.816  -0.120  4.310   0.10 20.24 ?  158 LYS   A N    1 
ATOM   3156 C  CA   A LYS   A 1 158 ? 4.678  -1.169  5.020   0.64 23.21 ?  158 LYS   A CA   1 
ATOM   3157 C  CA   B LYS   A 1 158 ? 4.451  -1.058  5.421   0.26 20.79 ?  158 LYS   A CA   1 
ATOM   3158 C  CA   T LYS   A 1 158 ? 4.832  -1.001  4.932   0.10 21.33 ?  158 LYS   A CA   1 
ATOM   3159 C  C    A LYS   A 1 158 ? 3.940  -1.951  3.938   0.64 22.59 ?  158 LYS   A C    1 
ATOM   3160 C  C    B LYS   A 1 158 ? 3.791  -1.814  4.274   0.26 20.36 ?  158 LYS   A C    1 
ATOM   3161 C  C    T LYS   A 1 158 ? 4.069  -1.809  3.887   0.10 21.58 ?  158 LYS   A C    1 
ATOM   3162 O  O    A LYS   A 1 158 ? 3.750  -3.168  4.059   0.64 22.71 ?  158 LYS   A O    1 
ATOM   3163 O  O    B LYS   A 1 158 ? 3.608  -3.035  4.352   0.26 21.03 ?  158 LYS   A O    1 
ATOM   3164 O  O    T LYS   A 1 158 ? 3.872  -3.018  4.054   0.10 21.65 ?  158 LYS   A O    1 
ATOM   3165 C  CB   A LYS   A 1 158 ? 3.703  -0.419  5.938   0.64 25.36 ?  158 LYS   A CB   1 
ATOM   3166 C  CB   B LYS   A 1 158 ? 3.403  -0.342  6.277   0.26 21.90 ?  158 LYS   A CB   1 
ATOM   3167 C  CB   T LYS   A 1 158 ? 3.873  -0.184  5.802   0.10 22.17 ?  158 LYS   A CB   1 
ATOM   3168 C  CG   A LYS   A 1 158 ? 2.487  -1.227  6.409   0.64 27.24 ?  158 LYS   A CG   1 
ATOM   3169 C  CG   B LYS   A 1 158 ? 2.243  -1.222  6.736   0.26 23.04 ?  158 LYS   A CG   1 
ATOM   3170 C  CG   T LYS   A 1 158 ? 2.653  -0.956  6.297   0.10 22.88 ?  158 LYS   A CG   1 
ATOM   3171 C  CD   A LYS   A 1 158 ? 2.854  -2.491  7.198   0.64 28.70 ?  158 LYS   A CD   1 
ATOM   3172 C  CD   B LYS   A 1 158 ? 2.717  -2.409  7.564   0.26 23.96 ?  158 LYS   A CD   1 
ATOM   3173 C  CD   T LYS   A 1 158 ? 3.044  -2.147  7.160   0.10 23.57 ?  158 LYS   A CD   1 
ATOM   3174 C  CE   A LYS   A 1 158 ? 1.588  -3.196  7.711   0.64 29.68 ?  158 LYS   A CE   1 
ATOM   3175 C  CE   B LYS   A 1 158 ? 1.539  -3.149  8.178   0.26 24.37 ?  158 LYS   A CE   1 
ATOM   3176 C  CE   T LYS   A 1 158 ? 1.822  -2.960  7.560   0.10 24.13 ?  158 LYS   A CE   1 
ATOM   3177 N  NZ   A LYS   A 1 158 ? 1.838  -4.549  8.297   0.64 29.84 ?  158 LYS   A NZ   1 
ATOM   3178 N  NZ   B LYS   A 1 158 ? 1.949  -4.425  8.823   0.26 24.52 ?  158 LYS   A NZ   1 
ATOM   3179 N  NZ   T LYS   A 1 158 ? 2.180  -4.154  8.374   0.10 24.34 ?  158 LYS   A NZ   1 
ATOM   3180 H  H    A LYS   A 1 158 ? 5.481  0.591   4.585   0.64 26.37 ?  158 LYS   A H    1 
ATOM   3181 H  H    B LYS   A 1 158 ? 5.198  0.725   4.990   0.26 24.29 ?  158 LYS   A H    1 
ATOM   3182 H  H    T LYS   A 1 158 ? 5.647  0.719   4.391   0.10 24.29 ?  158 LYS   A H    1 
ATOM   3183 H  HA   A LYS   A 1 158 ? 5.156  -1.809  5.569   0.64 27.86 ?  158 LYS   A HA   1 
ATOM   3184 H  HA   B LYS   A 1 158 ? 4.903  -1.704  5.985   0.26 24.96 ?  158 LYS   A HA   1 
ATOM   3185 H  HA   T LYS   A 1 158 ? 5.293  -1.626  5.511   0.10 25.60 ?  158 LYS   A HA   1 
ATOM   3186 H  HB2  A LYS   A 1 158 ? 4.185  -0.132  6.733   0.64 30.43 ?  158 LYS   A HB2  1 
ATOM   3187 H  HB2  B LYS   A 1 158 ? 3.838  0.005   7.074   0.26 26.29 ?  158 LYS   A HB2  1 
ATOM   3188 H  HB2  T LYS   A 1 158 ? 4.355  0.131   6.586   0.10 26.61 ?  158 LYS   A HB2  1 
ATOM   3189 H  HB3  A LYS   A 1 158 ? 3.371  0.361   5.467   0.64 30.43 ?  158 LYS   A HB3  1 
ATOM   3190 H  HB3  B LYS   A 1 158 ? 3.030  0.391   5.765   0.26 26.29 ?  158 LYS   A HB3  1 
ATOM   3191 H  HB3  T LYS   A 1 158 ? 3.553  0.575   5.292   0.10 26.61 ?  158 LYS   A HB3  1 
ATOM   3192 H  HG2  A LYS   A 1 158 ? 1.947  -0.664  6.989   0.64 32.70 ?  158 LYS   A HG2  1 
ATOM   3193 H  HG2  B LYS   A 1 158 ? 1.643  -0.694  7.287   0.26 27.66 ?  158 LYS   A HG2  1 
ATOM   3194 H  HG2  T LYS   A 1 158 ? 2.106  -0.366  6.837   0.10 27.47 ?  158 LYS   A HG2  1 
ATOM   3195 H  HG3  A LYS   A 1 158 ? 1.962  -1.494  5.638   0.64 32.70 ?  158 LYS   A HG3  1 
ATOM   3196 H  HG3  B LYS   A 1 158 ? 1.765  -1.562  5.962   0.26 27.66 ?  158 LYS   A HG3  1 
ATOM   3197 H  HG3  T LYS   A 1 158 ? 2.138  -1.281  5.541   0.10 27.47 ?  158 LYS   A HG3  1 
ATOM   3198 H  HD2  A LYS   A 1 158 ? 3.335  -3.103  6.622   0.64 34.44 ?  158 LYS   A HD2  1 
ATOM   3199 H  HD2  B LYS   A 1 158 ? 3.202  -3.026  6.994   0.26 28.76 ?  158 LYS   A HD2  1 
ATOM   3200 H  HD2  T LYS   A 1 158 ? 3.643  -2.725  6.663   0.10 28.29 ?  158 LYS   A HD2  1 
ATOM   3201 H  HD3  A LYS   A 1 158 ? 3.399  -2.245  7.963   0.64 34.44 ?  158 LYS   A HD3  1 
ATOM   3202 H  HD3  B LYS   A 1 158 ? 3.287  -2.093  8.283   0.26 28.76 ?  158 LYS   A HD3  1 
ATOM   3203 H  HD3  T LYS   A 1 158 ? 3.476  -1.828  7.968   0.10 28.29 ?  158 LYS   A HD3  1 
ATOM   3204 H  HE2  A LYS   A 1 158 ? 1.182  -2.645  8.399   0.64 35.63 ?  158 LYS   A HE2  1 
ATOM   3205 H  HE2  B LYS   A 1 158 ? 1.135  -2.586  8.855   0.26 29.25 ?  158 LYS   A HE2  1 
ATOM   3206 H  HE2  T LYS   A 1 158 ? 1.226  -2.403  8.086   0.10 28.97 ?  158 LYS   A HE2  1 
ATOM   3207 H  HE3  A LYS   A 1 158 ? 0.970  -3.301  6.971   0.64 35.63 ?  158 LYS   A HE3  1 
ATOM   3208 H  HE3  B LYS   A 1 158 ? 0.890  -3.348  7.485   0.26 29.25 ?  158 LYS   A HE3  1 
ATOM   3209 H  HE3  T LYS   A 1 158 ? 1.369  -3.267  6.759   0.10 28.97 ?  158 LYS   A HE3  1 
ATOM   3210 H  HZ1  A LYS   A 1 158 ? 1.072  -4.907  8.575   0.64 35.82 ?  158 LYS   A HZ1  1 
ATOM   3211 H  HZ1  B LYS   A 1 158 ? 1.239  -4.832  9.171   0.26 29.43 ?  158 LYS   A HZ1  1 
ATOM   3212 H  HZ1  T LYS   A 1 158 ? 1.445  -4.606  8.591   0.10 29.22 ?  158 LYS   A HZ1  1 
ATOM   3213 H  HZ2  A LYS   A 1 158 ? 2.200  -5.084  7.684   0.64 35.82 ?  158 LYS   A HZ2  1 
ATOM   3214 H  HZ2  B LYS   A 1 158 ? 2.327  -4.962  8.222   0.26 29.43 ?  158 LYS   A HZ2  1 
ATOM   3215 H  HZ2  T LYS   A 1 158 ? 2.721  -4.687  7.910   0.10 29.22 ?  158 LYS   A HZ2  1 
ATOM   3216 H  HZ3  A LYS   A 1 158 ? 2.394  -4.484  8.989   0.64 35.82 ?  158 LYS   A HZ3  1 
ATOM   3217 H  HZ3  B LYS   A 1 158 ? 2.536  -4.260  9.472   0.26 29.43 ?  158 LYS   A HZ3  1 
ATOM   3218 H  HZ3  T LYS   A 1 158 ? 2.594  -3.900  9.120   0.10 29.22 ?  158 LYS   A HZ3  1 
ATOM   3219 N  N    A ASN   A 1 159 ? 3.529  -1.276  2.864   0.64 23.66 ?  159 ASN   A N    1 
ATOM   3220 N  N    B ASN   A 1 159 ? 3.422  -1.107  3.203   0.26 19.73 ?  159 ASN   A N    1 
ATOM   3221 N  N    T ASN   A 1 159 ? 3.631  -1.164  2.812   0.10 21.93 ?  159 ASN   A N    1 
ATOM   3222 C  CA   A ASN   A 1 159 ? 2.839  -1.973  1.784   0.64 23.47 ?  159 ASN   A CA   1 
ATOM   3223 C  CA   B ASN   A 1 159 ? 2.840  -1.781  2.047   0.26 18.81 ?  159 ASN   A CA   1 
ATOM   3224 C  CA   T ASN   A 1 159 ? 2.892  -1.853  1.759   0.10 22.08 ?  159 ASN   A CA   1 
ATOM   3225 C  C    A ASN   A 1 159 ? 3.717  -3.065  1.173   0.64 22.16 ?  159 ASN   A C    1 
ATOM   3226 C  C    B ASN   A 1 159 ? 3.773  -2.864  1.526   0.26 18.61 ?  159 ASN   A C    1 
ATOM   3227 C  C    T ASN   A 1 159 ? 3.738  -2.943  1.114   0.10 21.65 ?  159 ASN   A C    1 
ATOM   3228 O  O    A ASN   A 1 159 ? 3.251  -4.188  0.938   0.64 22.49 ?  159 ASN   A O    1 
ATOM   3229 O  O    B ASN   A 1 159 ? 3.332  -3.977  1.215   0.26 18.35 ?  159 ASN   A O    1 
ATOM   3230 O  O    T ASN   A 1 159 ? 3.223  -3.994  0.733   0.10 21.77 ?  159 ASN   A O    1 
ATOM   3231 C  CB   A ASN   A 1 159 ? 2.356  -0.959  0.742   0.64 26.26 ?  159 ASN   A CB   1 
ATOM   3232 C  CB   B ASN   A 1 159 ? 2.529  -0.763  0.946   0.26 18.73 ?  159 ASN   A CB   1 
ATOM   3233 C  CB   T ASN   A 1 159 ? 2.412  -0.860  0.698   0.10 22.76 ?  159 ASN   A CB   1 
ATOM   3234 C  CG   A ASN   A 1 159 ? 1.171  -0.142  1.234   0.64 29.08 ?  159 ASN   A CG   1 
ATOM   3235 C  CG   B ASN   A 1 159 ? 1.723  -1.361  -0.197  0.26 19.28 ?  159 ASN   A CG   1 
ATOM   3236 C  CG   T ASN   A 1 159 ? 1.237  -0.027  1.172   0.10 23.42 ?  159 ASN   A CG   1 
ATOM   3237 O  OD1  A ASN   A 1 159 ? 0.286  -0.671  1.904   0.64 30.13 ?  159 ASN   A OD1  1 
ATOM   3238 O  OD1  B ASN   A 1 159 ? 0.507  -1.164  -0.282  0.26 20.13 ?  159 ASN   A OD1  1 
ATOM   3239 O  OD1  T ASN   A 1 159 ? 0.403  -0.495  1.946   0.10 23.72 ?  159 ASN   A OD1  1 
ATOM   3240 N  ND2  A ASN   A 1 159 ? 1.151  1.149   0.910   0.64 30.46 ?  159 ASN   A ND2  1 
ATOM   3241 N  ND2  B ASN   A 1 159 ? 2.397  -2.084  -1.088  0.26 19.92 ?  159 ASN   A ND2  1 
ATOM   3242 N  ND2  T ASN   A 1 159 ? 1.163  1.213   0.706   0.10 23.71 ?  159 ASN   A ND2  1 
ATOM   3243 H  H    A ASN   A 1 159 ? 3.647  -0.431  2.739   0.64 28.41 ?  159 ASN   A H    1 
ATOM   3244 H  H    B ASN   A 1 159 ? 3.502  -0.257  3.122   0.26 23.69 ?  159 ASN   A H    1 
ATOM   3245 H  H    T ASN   A 1 159 ? 3.747  -0.325  2.669   0.10 26.33 ?  159 ASN   A H    1 
ATOM   3246 H  HA   A ASN   A 1 159 ? 2.056  -2.403  2.153   0.64 28.18 ?  159 ASN   A HA   1 
ATOM   3247 H  HA   B ASN   A 1 159 ? 2.008  -2.203  2.311   0.26 22.58 ?  159 ASN   A HA   1 
ATOM   3248 H  HA   T ASN   A 1 159 ? 2.112  -2.276  2.146   0.10 26.51 ?  159 ASN   A HA   1 
ATOM   3249 H  HB2  A ASN   A 1 159 ? 3.074  -0.341  0.536   0.64 31.52 ?  159 ASN   A HB2  1 
ATOM   3250 H  HB2  B ASN   A 1 159 ? 2.010  -0.037  1.324   0.26 22.48 ?  159 ASN   A HB2  1 
ATOM   3251 H  HB2  T ASN   A 1 159 ? 3.138  -0.257  0.477   0.10 27.32 ?  159 ASN   A HB2  1 
ATOM   3252 H  HB3  A ASN   A 1 159 ? 2.077  -1.429  -0.056  0.64 31.52 ?  159 ASN   A HB3  1 
ATOM   3253 H  HB3  B ASN   A 1 159 ? 3.359  -0.427  0.580   0.26 22.48 ?  159 ASN   A HB3  1 
ATOM   3254 H  HB3  T ASN   A 1 159 ? 2.135  -1.351  -0.092  0.10 27.32 ?  159 ASN   A HB3  1 
ATOM   3255 H  HD21 A ASN   A 1 159 ? 0.500  1.652   1.170   0.64 36.56 ?  159 ASN   A HD21 1 
ATOM   3256 H  HD21 B ASN   A 1 159 ? 1.986  -2.449  -1.752  0.26 23.91 ?  159 ASN   A HD21 1 
ATOM   3257 H  HD21 T ASN   A 1 159 ? 0.513  1.723   0.946   0.10 28.47 ?  159 ASN   A HD21 1 
ATOM   3258 H  HD22 A ASN   A 1 159 ? 1.789  1.483   0.442   0.64 36.56 ?  159 ASN   A HD22 1 
ATOM   3259 H  HD22 B ASN   A 1 159 ? 3.246  -2.197  -0.998  0.26 23.91 ?  159 ASN   A HD22 1 
ATOM   3260 H  HD22 T ASN   A 1 159 ? 1.764  1.506   0.167   0.10 28.47 ?  159 ASN   A HD22 1 
ATOM   3261 N  N    A LEU   A 1 160 ? 4.997  -2.770  0.942   0.64 20.14 ?  160 LEU   A N    1 
ATOM   3262 N  N    B LEU   A 1 160 ? 5.068  -2.563  1.436   0.26 18.06 ?  160 LEU   A N    1 
ATOM   3263 N  N    T LEU   A 1 160 ? 5.036  -2.691  0.993   0.10 21.17 ?  160 LEU   A N    1 
ATOM   3264 C  CA   A LEU   A 1 160 ? 5.891  -3.779  0.384   0.64 19.07 ?  160 LEU   A CA   1 
ATOM   3265 C  CA   B LEU   A 1 160 ? 6.014  -3.558  0.944   0.26 16.91 ?  160 LEU   A CA   1 
ATOM   3266 C  CA   T LEU   A 1 160 ? 5.949  -3.677  0.433   0.10 20.75 ?  160 LEU   A CA   1 
ATOM   3267 C  C    A LEU   A 1 160 ? 6.116  -4.925  1.364   0.64 17.66 ?  160 LEU   A C    1 
ATOM   3268 C  C    B LEU   A 1 160 ? 6.190  -4.695  1.943   0.26 16.23 ?  160 LEU   A C    1 
ATOM   3269 O  O    A LEU   A 1 160 ? 6.161  -6.093  0.963   0.64 17.33 ?  160 LEU   A O    1 
ATOM   3270 O  O    B LEU   A 1 160 ? 6.206  -5.868  1.555   0.26 15.75 ?  160 LEU   A O    1 
ATOM   3271 C  CB   A LEU   A 1 160 ? 7.220  -3.137  -0.001  0.64 18.56 ?  160 LEU   A CB   1 
ATOM   3272 C  CB   B LEU   A 1 160 ? 7.358  -2.903  0.627   0.26 16.13 ?  160 LEU   A CB   1 
ATOM   3273 C  CB   T LEU   A 1 160 ? 7.334  -3.069  0.218   0.10 20.36 ?  160 LEU   A CB   1 
ATOM   3274 C  CG   A LEU   A 1 160 ? 8.311  -4.130  -0.392  0.64 19.12 ?  160 LEU   A CG   1 
ATOM   3275 C  CG   B LEU   A 1 160 ? 8.420  -3.903  0.165   0.26 15.71 ?  160 LEU   A CG   1 
ATOM   3276 C  CG   T LEU   A 1 160 ? 8.405  -4.070  -0.209  0.10 20.16 ?  160 LEU   A CG   1 
ATOM   3277 C  CD1  A LEU   A 1 160 ? 7.875  -4.937  -1.591  0.64 19.91 ?  160 LEU   A CD1  1 
ATOM   3278 C  CD1  B LEU   A 1 160 ? 8.025  -4.546  -1.158  0.26 15.48 ?  160 LEU   A CD1  1 
ATOM   3279 C  CD1  T LEU   A 1 160 ? 7.915  -4.888  -1.389  0.10 20.10 ?  160 LEU   A CD1  1 
ATOM   3280 C  CD2  A LEU   A 1 160 ? 9.610  -3.402  -0.675  0.64 19.12 ?  160 LEU   A CD2  1 
ATOM   3281 C  CD2  B LEU   A 1 160 ? 9.773  -3.240  0.052   0.26 15.41 ?  160 LEU   A CD2  1 
ATOM   3282 C  CD2  T LEU   A 1 160 ? 9.703  -3.358  -0.548  0.10 20.07 ?  160 LEU   A CD2  1 
ATOM   3283 H  H    A LEU   A 1 160 ? 5.369  -2.012  1.112   0.64 24.17 ?  160 LEU   A H    1 
ATOM   3284 H  H    B LEU   A 1 160 ? 5.416  -1.806  1.652   0.26 21.67 ?  160 LEU   A H    1 
ATOM   3285 H  H    T LEU   A 1 160 ? 5.414  -1.954  1.228   0.10 25.41 ?  160 LEU   A H    1 
ATOM   3286 H  HA   A LEU   A 1 160 ? 5.491  -4.142  -0.417  0.64 22.90 ?  160 LEU   A HA   1 
ATOM   3287 H  HA   B LEU   A 1 160 ? 5.668  -3.933  0.123   0.26 20.30 ?  160 LEU   A HA   1 
ATOM   3288 H  HB2  A LEU   A 1 160 ? 7.076  -2.542  -0.758  0.64 22.28 ?  160 LEU   A HB2  1 
ATOM   3289 H  HB2  B LEU   A 1 160 ? 7.232  -2.250  -0.082  0.26 19.37 ?  160 LEU   A HB2  1 
ATOM   3290 H  HB2  T LEU   A 1 160 ? 7.273  -2.382  -0.468  0.10 24.44 ?  160 LEU   A HB2  1 
ATOM   3291 H  HB3  A LEU   A 1 160 ? 7.550  -2.628  0.755   0.64 22.28 ?  160 LEU   A HB3  1 
ATOM   3292 H  HB3  B LEU   A 1 160 ? 7.691  -2.461  1.424   0.26 19.37 ?  160 LEU   A HB3  1 
ATOM   3293 H  HB3  T LEU   A 1 160 ? 7.629  -2.676  1.053   0.10 24.44 ?  160 LEU   A HB3  1 
ATOM   3294 H  HG   A LEU   A 1 160 ? 8.474  -4.741  0.344   0.64 22.95 ?  160 LEU   A HG   1 
ATOM   3295 H  HG   B LEU   A 1 160 ? 8.501  -4.609  0.822   0.26 18.86 ?  160 LEU   A HG   1 
ATOM   3296 H  HG   T LEU   A 1 160 ? 8.580  -4.677  0.528   0.10 24.20 ?  160 LEU   A HG   1 
ATOM   3297 H  HD11 A LEU   A 1 160 ? 8.596  -5.529  -1.844  0.64 23.90 ?  160 LEU   A HD11 1 
ATOM   3298 H  HD11 B LEU   A 1 160 ? 8.769  -5.075  -1.484  0.26 18.59 ?  160 LEU   A HD11 1 
ATOM   3299 H  HD11 T LEU   A 1 160 ? 8.658  -5.396  -1.747  0.10 24.12 ?  160 LEU   A HD11 1 
ATOM   3300 H  HD12 A LEU   A 1 160 ? 7.089  -5.455  -1.355  0.64 23.90 ?  160 LEU   A HD12 1 
ATOM   3301 H  HD12 B LEU   A 1 160 ? 7.252  -5.116  -1.016  0.26 18.59 ?  160 LEU   A HD12 1 
ATOM   3302 H  HD12 T LEU   A 1 160 ? 7.217  -5.491  -1.089  0.10 24.12 ?  160 LEU   A HD12 1 
ATOM   3303 H  HD13 A LEU   A 1 160 ? 7.667  -4.330  -2.318  0.64 23.90 ?  160 LEU   A HD13 1 
ATOM   3304 H  HD13 B LEU   A 1 160 ? 7.809  -3.849  -1.797  0.26 18.59 ?  160 LEU   A HD13 1 
ATOM   3305 H  HD13 T LEU   A 1 160 ? 7.568  -4.286  -2.066  0.10 24.12 ?  160 LEU   A HD13 1 
ATOM   3306 H  HD21 A LEU   A 1 160 ? 10.291 -4.053  -0.915  0.64 22.95 ?  160 LEU   A HD21 1 
ATOM   3307 H  HD21 B LEU   A 1 160 ? 10.452 -3.926  -0.049  0.26 18.51 ?  160 LEU   A HD21 1 
ATOM   3308 H  HD21 T LEU   A 1 160 ? 10.364 -4.017  -0.811  0.10 24.10 ?  160 LEU   A HD21 1 
ATOM   3309 H  HD22 A LEU   A 1 160 ? 9.474  -2.782  -1.408  0.64 22.95 ?  160 LEU   A HD22 1 
ATOM   3310 H  HD22 B LEU   A 1 160 ? 9.770  -2.660  -0.724  0.26 18.51 ?  160 LEU   A HD22 1 
ATOM   3311 H  HD22 T LEU   A 1 160 ? 9.541  -2.741  -1.279  0.10 24.10 ?  160 LEU   A HD22 1 
ATOM   3312 H  HD23 A LEU   A 1 160 ? 9.885  -2.918  0.121   0.64 22.95 ?  160 LEU   A HD23 1 
ATOM   3313 H  HD23 B LEU   A 1 160 ? 9.941  -2.723  0.856   0.26 18.51 ?  160 LEU   A HD23 1 
ATOM   3314 H  HD23 T LEU   A 1 160 ? 10.010 -2.873  0.234   0.10 24.10 ?  160 LEU   A HD23 1 
ATOM   3315 N  N    A TYR   A 1 161 ? 6.281  -4.606  2.648   0.74 17.74 ?  161 TYR   A N    1 
ATOM   3316 N  N    B TYR   A 1 161 ? 6.327  -4.371  3.230   0.26 16.27 ?  161 TYR   A N    1 
ATOM   3317 C  CA   A TYR   A 1 161 ? 6.418  -5.640  3.667   0.74 16.92 ?  161 TYR   A CA   1 
ATOM   3318 C  CA   B TYR   A 1 161 ? 6.512  -5.412  4.238   0.26 15.79 ?  161 TYR   A CA   1 
ATOM   3319 C  C    A TYR   A 1 161 ? 5.274  -6.646  3.594   0.74 16.97 ?  161 TYR   A C    1 
ATOM   3320 C  C    B TYR   A 1 161 ? 5.372  -6.424  4.203   0.26 16.22 ?  161 TYR   A C    1 
ATOM   3321 O  O    A TYR   A 1 161 ? 5.495  -7.863  3.613   0.74 16.42 ?  161 TYR   A O    1 
ATOM   3322 O  O    B TYR   A 1 161 ? 5.604  -7.639  4.209   0.26 16.67 ?  161 TYR   A O    1 
ATOM   3323 C  CB   A TYR   A 1 161 ? 6.490  -4.997  5.053   0.74 16.97 ?  161 TYR   A CB   1 
ATOM   3324 C  CB   B TYR   A 1 161 ? 6.646  -4.787  5.628   0.26 15.75 ?  161 TYR   A CB   1 
ATOM   3325 C  CG   A TYR   A 1 161 ? 6.405  -6.002  6.174   0.74 16.46 ?  161 TYR   A CG   1 
ATOM   3326 C  CG   B TYR   A 1 161 ? 6.490  -5.780  6.759   0.26 15.54 ?  161 TYR   A CG   1 
ATOM   3327 C  CD1  A TYR   A 1 161 ? 7.534  -6.695  6.596   0.74 16.39 ?  161 TYR   A CD1  1 
ATOM   3328 C  CD1  B TYR   A 1 161 ? 7.571  -6.529  7.211   0.26 15.45 ?  161 TYR   A CD1  1 
ATOM   3329 C  CD2  A TYR   A 1 161 ? 5.191  -6.285  6.793   0.74 17.18 ?  161 TYR   A CD2  1 
ATOM   3330 C  CD2  B TYR   A 1 161 ? 5.260  -5.967  7.377   0.26 15.94 ?  161 TYR   A CD2  1 
ATOM   3331 C  CE1  A TYR   A 1 161 ? 7.459  -7.625  7.607   0.74 16.38 ?  161 TYR   A CE1  1 
ATOM   3332 C  CE1  B TYR   A 1 161 ? 7.427  -7.438  8.245   0.26 16.09 ?  161 TYR   A CE1  1 
ATOM   3333 C  CE2  A TYR   A 1 161 ? 5.107  -7.218  7.806   0.74 16.57 ?  161 TYR   A CE2  1 
ATOM   3334 C  CE2  B TYR   A 1 161 ? 5.107  -6.874  8.408   0.26 16.53 ?  161 TYR   A CE2  1 
ATOM   3335 C  CZ   A TYR   A 1 161 ? 6.245  -7.885  8.208   0.74 17.02 ?  161 TYR   A CZ   1 
ATOM   3336 C  CZ   B TYR   A 1 161 ? 6.191  -7.606  8.837   0.26 16.94 ?  161 TYR   A CZ   1 
ATOM   3337 O  OH   A TYR   A 1 161 ? 6.185  -8.820  9.214   0.74 18.14 ?  161 TYR   A OH   1 
ATOM   3338 O  OH   B TYR   A 1 161 ? 6.037  -8.506  9.868   0.26 18.04 ?  161 TYR   A OH   1 
ATOM   3339 H  H    A TYR   A 1 161 ? 6.308  -3.808  2.953   0.74 21.29 ?  161 TYR   A H    1 
ATOM   3340 H  H    B TYR   A 1 161 ? 6.315  -3.568  3.540   0.26 19.53 ?  161 TYR   A H    1 
ATOM   3341 H  HA   A TYR   A 1 161 ? 7.240  -6.128  3.522   0.74 20.31 ?  161 TYR   A HA   1 
ATOM   3342 H  HA   B TYR   A 1 161 ? 7.333  -5.887  4.050   0.26 18.96 ?  161 TYR   A HA   1 
ATOM   3343 H  HB2  A TYR   A 1 161 ? 7.336  -4.530  5.137   0.74 20.37 ?  161 TYR   A HB2  1 
ATOM   3344 H  HB2  B TYR   A 1 161 ? 7.526  -4.384  5.708   0.26 18.91 ?  161 TYR   A HB2  1 
ATOM   3345 H  HB3  A TYR   A 1 161 ? 5.755  -4.375  5.155   0.74 20.37 ?  161 TYR   A HB3  1 
ATOM   3346 H  HB3  B TYR   A 1 161 ? 5.964  -4.106  5.737   0.26 18.91 ?  161 TYR   A HB3  1 
ATOM   3347 H  HD1  A TYR   A 1 161 ? 8.352  -6.523  6.192   0.74 19.67 ?  161 TYR   A HD1  1 
ATOM   3348 H  HD1  B TYR   A 1 161 ? 8.404  -6.417  6.815   0.26 18.54 ?  161 TYR   A HD1  1 
ATOM   3349 H  HD2  A TYR   A 1 161 ? 4.422  -5.838  6.525   0.74 20.62 ?  161 TYR   A HD2  1 
ATOM   3350 H  HD2  B TYR   A 1 161 ? 4.524  -5.477  7.092   0.26 19.14 ?  161 TYR   A HD2  1 
ATOM   3351 H  HE1  A TYR   A 1 161 ? 8.224  -8.081  7.881   0.74 19.66 ?  161 TYR   A HE1  1 
ATOM   3352 H  HE1  B TYR   A 1 161 ? 8.160  -7.933  8.539   0.26 19.32 ?  161 TYR   A HE1  1 
ATOM   3353 H  HE2  A TYR   A 1 161 ? 4.286  -7.397  8.217   0.74 19.89 ?  161 TYR   A HE2  1 
ATOM   3354 H  HE2  B TYR   A 1 161 ? 4.277  -6.990  8.813   0.26 19.84 ?  161 TYR   A HE2  1 
ATOM   3355 H  HH   A TYR   A 1 161 ? 6.942  -9.153  9.356   0.74 21.78 ?  161 TYR   A HH   1 
ATOM   3356 H  HH   B TYR   A 1 161 ? 5.238  -8.507  10.132  0.26 21.65 ?  161 TYR   A HH   1 
ATOM   3357 N  N    A ASP   A 1 162 ? 4.041  -6.146  3.509   0.74 17.76 ?  162 ASP   A N    1 
ATOM   3358 N  N    B ASP   A 1 162 ? 4.128  -5.941  4.169   0.26 16.43 ?  162 ASP   A N    1 
ATOM   3359 C  CA   A ASP   A 1 162 ? 2.883  -7.035  3.458   0.74 18.39 ?  162 ASP   A CA   1 
ATOM   3360 C  CA   B ASP   A 1 162 ? 2.986  -6.851  4.146   0.26 16.72 ?  162 ASP   A CA   1 
ATOM   3361 C  C    A ASP   A 1 162 ? 2.918  -7.911  2.211   0.74 18.51 ?  162 ASP   A C    1 
ATOM   3362 C  C    B ASP   A 1 162 ? 2.996  -7.712  2.891   0.26 17.21 ?  162 ASP   A C    1 
ATOM   3363 O  O    A ASP   A 1 162 ? 2.556  -9.093  2.264   0.74 18.53 ?  162 ASP   A O    1 
ATOM   3364 O  O    B ASP   A 1 162 ? 2.660  -8.902  2.939   0.26 16.80 ?  162 ASP   A O    1 
ATOM   3365 C  CB   A ASP   A 1 162 ? 1.587  -6.217  3.507   0.74 19.36 ?  162 ASP   A CB   1 
ATOM   3366 C  CB   B ASP   A 1 162 ? 1.679  -6.063  4.236   0.26 16.50 ?  162 ASP   A CB   1 
ATOM   3367 C  CG   A ASP   A 1 162 ? 1.268  -5.682  4.890   0.74 21.08 ?  162 ASP   A CG   1 
ATOM   3368 C  CG   B ASP   A 1 162 ? 1.467  -5.428  5.595   0.26 17.25 ?  162 ASP   A CG   1 
ATOM   3369 O  OD1  A ASP   A 1 162 ? 1.897  -6.113  5.877   0.74 21.74 ?  162 ASP   A OD1  1 
ATOM   3370 O  OD1  B ASP   A 1 162 ? 2.231  -5.736  6.531   0.26 17.27 ?  162 ASP   A OD1  1 
ATOM   3371 O  OD2  A ASP   A 1 162 ? 0.363  -4.822  4.979   0.74 22.10 -1 162 ASP   A OD2  1 
ATOM   3372 O  OD2  B ASP   A 1 162 ? 0.533  -4.609  5.722   0.26 18.18 -1 162 ASP   A OD2  1 
ATOM   3373 H  H    A ASP   A 1 162 ? 3.846  -5.313  3.485   0.74 21.32 ?  162 ASP   A H    1 
ATOM   3374 H  H    B ASP   A 1 162 ? 3.921  -5.105  4.156   0.26 19.73 ?  162 ASP   A H    1 
ATOM   3375 H  HA   A ASP   A 1 162 ? 2.890  -7.626  4.225   0.74 22.08 ?  162 ASP   A HA   1 
ATOM   3376 H  HA   B ASP   A 1 162 ? 3.034  -7.443  4.914   0.26 20.07 ?  162 ASP   A HA   1 
ATOM   3377 H  HB2  A ASP   A 1 162 ? 1.664  -5.453  2.922   0.74 23.24 ?  162 ASP   A HB2  1 
ATOM   3378 H  HB2  B ASP   A 1 162 ? 1.693  -5.345  3.589   0.26 19.81 ?  162 ASP   A HB2  1 
ATOM   3379 H  HB3  A ASP   A 1 162 ? 0.840  -6.774  3.241   0.74 23.24 ?  162 ASP   A HB3  1 
ATOM   3380 H  HB3  B ASP   A 1 162 ? 0.934  -6.662  4.052   0.26 19.81 ?  162 ASP   A HB3  1 
ATOM   3381 N  N    A LYS   A 1 163 ? 3.352  -7.348  1.080   0.74 19.75 ?  163 LYS   A N    1 
ATOM   3382 N  N    B LYS   A 1 163 ? 3.375  -7.127  1.753   0.26 17.96 ?  163 LYS   A N    1 
ATOM   3383 C  CA   A LYS   A 1 163 ? 3.450  -8.127  -0.152  0.74 20.04 ?  163 LYS   A CA   1 
ATOM   3384 C  CA   B LYS   A 1 163 ? 3.448  -7.899  0.518   0.26 19.07 ?  163 LYS   A CA   1 
ATOM   3385 C  C    A LYS   A 1 163 ? 4.540  -9.192  -0.048  0.74 18.68 ?  163 LYS   A C    1 
ATOM   3386 C  C    B LYS   A 1 163 ? 4.559  -8.939  0.584   0.26 18.21 ?  163 LYS   A C    1 
ATOM   3387 O  O    A LYS   A 1 163 ? 4.369  -10.317 -0.532  0.74 19.78 ?  163 LYS   A O    1 
ATOM   3388 O  O    B LYS   A 1 163 ? 4.415  -10.044 0.050   0.26 18.29 ?  163 LYS   A O    1 
ATOM   3389 C  CB   A LYS   A 1 163 ? 3.721  -7.188  -1.328  0.74 24.00 ?  163 LYS   A CB   1 
ATOM   3390 C  CB   B LYS   A 1 163 ? 3.664  -6.960  -0.666  0.26 21.34 ?  163 LYS   A CB   1 
ATOM   3391 C  CG   A LYS   A 1 163 ? 3.774  -7.873  -2.680  0.74 28.21 ?  163 LYS   A CG   1 
ATOM   3392 C  CG   B LYS   A 1 163 ? 3.781  -7.669  -1.999  0.26 23.24 ?  163 LYS   A CG   1 
ATOM   3393 C  CD   A LYS   A 1 163 ? 4.207  -6.897  -3.758  0.74 31.98 ?  163 LYS   A CD   1 
ATOM   3394 C  CD   B LYS   A 1 163 ? 3.845  -6.668  -3.133  0.26 24.98 ?  163 LYS   A CD   1 
ATOM   3395 C  CE   A LYS   A 1 163 ? 4.070  -7.504  -5.143  0.74 34.42 ?  163 LYS   A CE   1 
ATOM   3396 C  CE   B LYS   A 1 163 ? 3.775  -7.354  -4.483  0.26 26.28 ?  163 LYS   A CE   1 
ATOM   3397 N  NZ   A LYS   A 1 163 ? 4.779  -6.696  -6.170  0.74 35.34 ?  163 LYS   A NZ   1 
ATOM   3398 N  NZ   B LYS   A 1 163 ? 3.710  -6.368  -5.596  0.26 26.91 ?  163 LYS   A NZ   1 
ATOM   3399 H  H    A LYS   A 1 163 ? 3.590  -6.523  1.002   0.74 23.71 ?  163 LYS   A H    1 
ATOM   3400 H  H    B LYS   A 1 163 ? 3.594  -6.298  1.675   0.26 21.56 ?  163 LYS   A H    1 
ATOM   3401 H  HA   A LYS   A 1 163 ? 2.600  -8.567  -0.316  0.74 24.05 ?  163 LYS   A HA   1 
ATOM   3402 H  HA   B LYS   A 1 163 ? 2.608  -8.362  0.384   0.26 22.89 ?  163 LYS   A HA   1 
ATOM   3403 H  HB2  A LYS   A 1 163 ? 3.013  -6.520  -1.369  0.74 28.81 ?  163 LYS   A HB2  1 
ATOM   3404 H  HB2  B LYS   A 1 163 ? 2.911  -6.350  -0.721  0.26 25.62 ?  163 LYS   A HB2  1 
ATOM   3405 H  HB3  A LYS   A 1 163 ? 4.572  -6.748  -1.189  0.74 28.81 ?  163 LYS   A HB3  1 
ATOM   3406 H  HB3  B LYS   A 1 163 ? 4.482  -6.460  -0.524  0.26 25.62 ?  163 LYS   A HB3  1 
ATOM   3407 H  HG2  A LYS   A 1 163 ? 4.416  -8.599  -2.652  0.74 33.86 ?  163 LYS   A HG2  1 
ATOM   3408 H  HG2  B LYS   A 1 163 ? 4.594  -8.199  -2.014  0.26 27.90 ?  163 LYS   A HG2  1 
ATOM   3409 H  HG3  A LYS   A 1 163 ? 2.892  -8.211  -2.907  0.74 33.86 ?  163 LYS   A HG3  1 
ATOM   3410 H  HG3  B LYS   A 1 163 ? 3.005  -8.236  -2.132  0.26 27.90 ?  163 LYS   A HG3  1 
ATOM   3411 H  HD2  A LYS   A 1 163 ? 3.646  -6.105  -3.716  0.74 38.39 ?  163 LYS   A HD2  1 
ATOM   3412 H  HD2  B LYS   A 1 163 ? 3.095  -6.057  -3.062  0.26 29.98 ?  163 LYS   A HD2  1 
ATOM   3413 H  HD3  A LYS   A 1 163 ? 5.136  -6.657  -3.619  0.74 38.39 ?  163 LYS   A HD3  1 
ATOM   3414 H  HD3  B LYS   A 1 163 ? 4.682  -6.180  -3.080  0.26 29.98 ?  163 LYS   A HD3  1 
ATOM   3415 H  HE2  A LYS   A 1 163 ? 4.438  -8.401  -5.139  0.74 41.31 ?  163 LYS   A HE2  1 
ATOM   3416 H  HE2  B LYS   A 1 163 ? 4.569  -7.899  -4.605  0.26 31.55 ?  163 LYS   A HE2  1 
ATOM   3417 H  HE3  A LYS   A 1 163 ? 3.131  -7.534  -5.381  0.74 41.31 ?  163 LYS   A HE3  1 
ATOM   3418 H  HE3  B LYS   A 1 163 ? 2.980  -7.908  -4.519  0.26 31.55 ?  163 LYS   A HE3  1 
ATOM   3419 H  HZ1  A LYS   A 1 163 ? 4.685  -7.073  -6.970  0.74 42.42 ?  163 LYS   A HZ1  1 
ATOM   3420 H  HZ1  B LYS   A 1 163 ? 3.670  -6.793  -6.376  0.26 32.30 ?  163 LYS   A HZ1  1 
ATOM   3421 H  HZ2  A LYS   A 1 163 ? 4.440  -5.873  -6.195  0.74 42.42 ?  163 LYS   A HZ2  1 
ATOM   3422 H  HZ2  B LYS   A 1 163 ? 2.986  -5.858  -5.506  0.26 32.30 ?  163 LYS   A HZ2  1 
ATOM   3423 H  HZ3  A LYS   A 1 163 ? 5.646  -6.646  -5.973  0.74 42.42 ?  163 LYS   A HZ3  1 
ATOM   3424 H  HZ3  B LYS   A 1 163 ? 4.433  -5.849  -5.584  0.26 32.30 ?  163 LYS   A HZ3  1 
ATOM   3425 N  N    A LEU   A 1 164 ? 5.673  -8.848  0.567   0.74 16.93 ?  164 LEU   A N    1 
ATOM   3426 N  N    B LEU   A 1 164 ? 5.673  -8.604  1.236   0.26 17.35 ?  164 LEU   A N    1 
ATOM   3427 C  CA   A LEU   A 1 164 ? 6.754  -9.812  0.745   0.74 16.44 ?  164 LEU   A CA   1 
ATOM   3428 C  CA   B LEU   A 1 164 ? 6.777  -9.551  1.348   0.26 16.74 ?  164 LEU   A CA   1 
ATOM   3429 C  C    A LEU   A 1 164 ? 6.313  -10.980 1.619   0.74 16.60 ?  164 LEU   A C    1 
ATOM   3430 C  C    B LEU   A 1 164 ? 6.377  -10.771 2.167   0.26 16.50 ?  164 LEU   A C    1 
ATOM   3431 O  O    A LEU   A 1 164 ? 6.605  -12.143 1.315   0.74 17.58 ?  164 LEU   A O    1 
ATOM   3432 O  O    B LEU   A 1 164 ? 6.708  -11.906 1.805   0.26 16.33 ?  164 LEU   A O    1 
ATOM   3433 C  CB   A LEU   A 1 164 ? 7.954  -9.102  1.373   0.74 16.24 ?  164 LEU   A CB   1 
ATOM   3434 C  CB   B LEU   A 1 164 ? 7.986  -8.859  1.974   0.26 16.27 ?  164 LEU   A CB   1 
ATOM   3435 C  CG   A LEU   A 1 164 ? 8.702  -8.080  0.507   0.74 16.33 ?  164 LEU   A CG   1 
ATOM   3436 C  CG   B LEU   A 1 164 ? 8.723  -7.860  1.083   0.26 16.48 ?  164 LEU   A CG   1 
ATOM   3437 C  CD1  A LEU   A 1 164 ? 9.628  -7.194  1.339   0.74 16.28 ?  164 LEU   A CD1  1 
ATOM   3438 C  CD1  B LEU   A 1 164 ? 9.772  -7.124  1.895   0.26 16.41 ?  164 LEU   A CD1  1 
ATOM   3439 C  CD2  A LEU   A 1 164 ? 9.492  -8.786  -0.576  0.74 17.17 ?  164 LEU   A CD2  1 
ATOM   3440 C  CD2  B LEU   A 1 164 ? 9.354  -8.562  -0.109  0.26 16.65 ?  164 LEU   A CD2  1 
ATOM   3441 H  H    A LEU   A 1 164 ? 5.837  -8.064  0.876   0.74 20.32 ?  164 LEU   A H    1 
ATOM   3442 H  H    B LEU   A 1 164 ? 5.811  -7.844  1.617   0.26 20.82 ?  164 LEU   A H    1 
ATOM   3443 H  HA   A LEU   A 1 164 ? 7.021  -10.160 -0.124  0.74 19.74 ?  164 LEU   A HA   1 
ATOM   3444 H  HA   B LEU   A 1 164 ? 7.026  -9.857  0.465   0.26 20.09 ?  164 LEU   A HA   1 
ATOM   3445 H  HB2  A LEU   A 1 164 ? 7.644  -8.636  2.162   0.74 19.49 ?  164 LEU   A HB2  1 
ATOM   3446 H  HB2  B LEU   A 1 164 ? 7.690  -8.378  2.762   0.26 19.53 ?  164 LEU   A HB2  1 
ATOM   3447 H  HB3  A LEU   A 1 164 ? 8.597  -9.779  1.631   0.74 19.49 ?  164 LEU   A HB3  1 
ATOM   3448 H  HB3  B LEU   A 1 164 ? 8.627  -9.539  2.233   0.26 19.53 ?  164 LEU   A HB3  1 
ATOM   3449 H  HG   A LEU   A 1 164 ? 8.053  -7.503  0.075   0.74 19.61 ?  164 LEU   A HG   1 
ATOM   3450 H  HG   B LEU   A 1 164 ? 8.090  -7.205  0.747   0.26 19.78 ?  164 LEU   A HG   1 
ATOM   3451 H  HD11 A LEU   A 1 164 ? 10.076 -6.565  0.751   0.74 19.54 ?  164 LEU   A HD11 1 
ATOM   3452 H  HD11 B LEU   A 1 164 ? 10.232 -6.494  1.320   0.26 19.70 ?  164 LEU   A HD11 1 
ATOM   3453 H  HD12 A LEU   A 1 164 ? 9.099  -6.712  1.996   0.74 19.54 ?  164 LEU   A HD12 1 
ATOM   3454 H  HD12 B LEU   A 1 164 ? 9.334  -6.651  2.621   0.26 19.70 ?  164 LEU   A HD12 1 
ATOM   3455 H  HD13 A LEU   A 1 164 ? 10.282 -7.753  1.787   0.74 19.54 ?  164 LEU   A HD13 1 
ATOM   3456 H  HD13 B LEU   A 1 164 ? 10.402 -7.769  2.253   0.26 19.70 ?  164 LEU   A HD13 1 
ATOM   3457 H  HD21 A LEU   A 1 164 ? 9.979  -8.124  -1.092  0.74 20.61 ?  164 LEU   A HD21 1 
ATOM   3458 H  HD21 B LEU   A 1 164 ? 9.946  -7.942  -0.564  0.26 19.99 ?  164 LEU   A HD21 1 
ATOM   3459 H  HD22 A LEU   A 1 164 ? 10.113 -9.404  -0.162  0.74 20.61 ?  164 LEU   A HD22 1 
ATOM   3460 H  HD22 B LEU   A 1 164 ? 9.857  -9.328  0.208   0.26 19.99 ?  164 LEU   A HD22 1 
ATOM   3461 H  HD23 A LEU   A 1 164 ? 8.878  -9.267  -1.151  0.74 20.61 ?  164 LEU   A HD23 1 
ATOM   3462 H  HD23 B LEU   A 1 164 ? 8.653  -8.853  -0.713  0.26 19.99 ?  164 LEU   A HD23 1 
ATOM   3463 N  N    A VAL   A 1 165 ? 5.633  -10.684 2.725   0.74 16.64 ?  165 VAL   A N    1 
ATOM   3464 N  N    B VAL   A 1 165 ? 5.673  -10.557 3.278   0.26 16.44 ?  165 VAL   A N    1 
ATOM   3465 C  CA   A VAL   A 1 165 ? 5.141  -11.735 3.612   0.74 16.32 ?  165 VAL   A CA   1 
ATOM   3466 C  CA   B VAL   A 1 165 ? 5.242  -11.679 4.105   0.26 16.54 ?  165 VAL   A CA   1 
ATOM   3467 C  C    A VAL   A 1 165 ? 4.111  -12.603 2.895   0.74 16.24 ?  165 VAL   A C    1 
ATOM   3468 C  C    B VAL   A 1 165 ? 4.172  -12.493 3.386   0.26 16.74 ?  165 VAL   A C    1 
ATOM   3469 O  O    A VAL   A 1 165 ? 4.221  -13.835 2.859   0.74 16.81 ?  165 VAL   A O    1 
ATOM   3470 O  O    B VAL   A 1 165 ? 4.237  -13.726 3.331   0.26 16.55 ?  165 VAL   A O    1 
ATOM   3471 C  CB   A VAL   A 1 165 ? 4.566  -11.115 4.901   0.74 17.10 ?  165 VAL   A CB   1 
ATOM   3472 C  CB   B VAL   A 1 165 ? 4.754  -11.182 5.478   0.26 16.07 ?  165 VAL   A CB   1 
ATOM   3473 C  CG1  A VAL   A 1 165 ? 3.810  -12.156 5.719   0.74 17.76 ?  165 VAL   A CG1  1 
ATOM   3474 C  CG1  B VAL   A 1 165 ? 4.141  -12.329 6.267   0.26 15.74 ?  165 VAL   A CG1  1 
ATOM   3475 C  CG2  A VAL   A 1 165 ? 5.674  -10.466 5.725   0.74 18.22 ?  165 VAL   A CG2  1 
ATOM   3476 C  CG2  B VAL   A 1 165 ? 5.901  -10.547 6.253   0.26 16.13 ?  165 VAL   A CG2  1 
ATOM   3477 H  H    A VAL   A 1 165 ? 5.453  -9.886  2.985   0.74 19.97 ?  165 VAL   A H    1 
ATOM   3478 H  H    B VAL   A 1 165 ? 5.437  -9.782  3.572   0.26 19.74 ?  165 VAL   A H    1 
ATOM   3479 H  HA   A VAL   A 1 165 ? 5.884  -12.304 3.865   0.74 19.59 ?  165 VAL   A HA   1 
ATOM   3480 H  HA   B VAL   A 1 165 ? 6.000  -12.261 4.259   0.26 19.86 ?  165 VAL   A HA   1 
ATOM   3481 H  HB   A VAL   A 1 165 ? 3.938  -10.419 4.656   0.74 20.53 ?  165 VAL   A HB   1 
ATOM   3482 H  HB   B VAL   A 1 165 ? 4.070  -10.507 5.349   0.26 19.30 ?  165 VAL   A HB   1 
ATOM   3483 H  HG11 A VAL   A 1 165 ? 3.696  -11.821 6.622   0.74 21.32 ?  165 VAL   A HG11 1 
ATOM   3484 H  HG11 B VAL   A 1 165 ? 4.002  -12.040 7.180   0.26 18.90 ?  165 VAL   A HG11 1 
ATOM   3485 H  HG12 A VAL   A 1 165 ? 2.943  -12.309 5.313   0.74 21.32 ?  165 VAL   A HG12 1 
ATOM   3486 H  HG12 B VAL   A 1 165 ? 3.291  -12.572 5.869   0.26 18.90 ?  165 VAL   A HG12 1 
ATOM   3487 H  HG13 A VAL   A 1 165 ? 4.322  -12.979 5.735   0.74 21.32 ?  165 VAL   A HG13 1 
ATOM   3488 H  HG13 B VAL   A 1 165 ? 4.748  -13.085 6.247   0.26 18.90 ?  165 VAL   A HG13 1 
ATOM   3489 H  HG21 A VAL   A 1 165 ? 5.288  -10.078 6.526   0.74 21.87 ?  165 VAL   A HG21 1 
ATOM   3490 H  HG21 B VAL   A 1 165 ? 5.576  -10.262 7.121   0.26 19.36 ?  165 VAL   A HG21 1 
ATOM   3491 H  HG22 A VAL   A 1 165 ? 6.328  -11.140 5.966   0.74 21.87 ?  165 VAL   A HG22 1 
ATOM   3492 H  HG22 B VAL   A 1 165 ? 6.608  -11.202 6.361   0.26 19.36 ?  165 VAL   A HG22 1 
ATOM   3493 H  HG23 A VAL   A 1 165 ? 6.098  -9.771  5.194   0.74 21.87 ?  165 VAL   A HG23 1 
ATOM   3494 H  HG23 B VAL   A 1 165 ? 6.231  -9.782  5.755   0.26 19.36 ?  165 VAL   A HG23 1 
ATOM   3495 N  N    A SER   A 1 166 ? 3.096  -11.967 2.306   0.74 17.02 ?  166 SER   A N    1 
ATOM   3496 N  N    B SER   A 1 166 ? 3.173  -11.815 2.820   0.26 17.20 ?  166 SER   A N    1 
ATOM   3497 C  CA   A SER   A 1 166 ? 1.991  -12.713 1.714   0.74 18.43 ?  166 SER   A CA   1 
ATOM   3498 C  CA   B SER   A 1 166 ? 2.013  -12.513 2.282   0.26 17.72 ?  166 SER   A CA   1 
ATOM   3499 C  C    A SER   A 1 166 ? 2.447  -13.572 0.544   0.74 19.34 ?  166 SER   A C    1 
ATOM   3500 C  C    B SER   A 1 166 ? 2.318  -13.311 1.022   0.26 18.65 ?  166 SER   A C    1 
ATOM   3501 O  O    A SER   A 1 166 ? 1.868  -14.640 0.300   0.74 21.62 ?  166 SER   A O    1 
ATOM   3502 O  O    B SER   A 1 166 ? 1.464  -14.089 0.589   0.26 19.18 ?  166 SER   A O    1 
ATOM   3503 C  CB   A SER   A 1 166 ? 0.895  -11.744 1.267   0.74 19.59 ?  166 SER   A CB   1 
ATOM   3504 C  CB   B SER   A 1 166 ? 0.905  -11.516 1.960   0.26 17.88 ?  166 SER   A CB   1 
ATOM   3505 O  OG   A SER   A 1 166 ? 0.236  -11.149 2.381   0.74 21.38 ?  166 SER   A OG   1 
ATOM   3506 O  OG   B SER   A 1 166 ? 1.233  -10.765 0.808   0.26 18.25 ?  166 SER   A OG   1 
ATOM   3507 H  H    A SER   A 1 166 ? 3.027  -11.117 2.240   0.74 20.43 ?  166 SER   A H    1 
ATOM   3508 H  H    B SER   A 1 166 ? 3.144  -10.956 2.739   0.26 20.65 ?  166 SER   A H    1 
ATOM   3509 H  HA   A SER   A 1 166 ? 1.611  -13.305 2.378   0.74 22.13 ?  166 SER   A HA   1 
ATOM   3510 H  HA   B SER   A 1 166 ? 1.676  -13.118 2.960   0.26 21.28 ?  166 SER   A HA   1 
ATOM   3511 H  HB2  A SER   A 1 166 ? 1.294  -11.045 0.724   0.74 23.52 ?  166 SER   A HB2  1 
ATOM   3512 H  HB2  B SER   A 1 166 ? 0.079  -12.002 1.791   0.26 21.46 ?  166 SER   A HB2  1 
ATOM   3513 H  HB3  A SER   A 1 166 ? 0.236  -12.229 0.745   0.74 23.52 ?  166 SER   A HB3  1 
ATOM   3514 H  HB3  B SER   A 1 166 ? 0.783  -10.917 2.715   0.26 21.46 ?  166 SER   A HB3  1 
ATOM   3515 H  HG   A SER   A 1 166 ? 0.803  -10.718 2.842   0.74 25.67 ?  166 SER   A HG   1 
ATOM   3516 H  HG   B SER   A 1 166 ? 1.949  -10.338 0.940   0.26 21.91 ?  166 SER   A HG   1 
ATOM   3517 N  N    A SER   A 1 167 ? 3.477  -13.139 -0.185  0.74 18.61 ?  167 SER   A N    1 
ATOM   3518 N  N    B SER   A 1 167 ? 3.486  -13.130 0.406   0.26 19.47 ?  167 SER   A N    1 
ATOM   3519 C  CA   A SER   A 1 167 ? 3.956  -13.867 -1.352  0.74 19.85 ?  167 SER   A CA   1 
ATOM   3520 C  CA   B SER   A 1 167 ? 3.806  -13.831 -0.833  0.26 20.61 ?  167 SER   A CA   1 
ATOM   3521 C  C    A SER   A 1 167 ? 5.097  -14.820 -1.029  0.74 20.55 ?  167 SER   A C    1 
ATOM   3522 C  C    B SER   A 1 167 ? 5.029  -14.732 -0.695  0.26 20.76 ?  167 SER   A C    1 
ATOM   3523 O  O    A SER   A 1 167 ? 5.577  -15.517 -1.932  0.74 22.17 ?  167 SER   A O    1 
ATOM   3524 O  O    B SER   A 1 167 ? 5.666  -15.058 -1.702  0.26 20.83 ?  167 SER   A O    1 
ATOM   3525 C  CB   A SER   A 1 167 ? 4.400  -12.889 -2.454  0.74 20.68 ?  167 SER   A CB   1 
ATOM   3526 C  CB   B SER   A 1 167 ? 4.008  -12.840 -1.982  0.26 22.01 ?  167 SER   A CB   1 
ATOM   3527 O  OG   A SER   A 1 167 ? 5.451  -12.048 -2.005  0.74 21.51 ?  167 SER   A OG   1 
ATOM   3528 O  OG   B SER   A 1 167 ? 5.140  -12.016 -1.756  0.26 22.94 ?  167 SER   A OG   1 
ATOM   3529 H  H    A SER   A 1 167 ? 3.916  -12.415 -0.023  0.74 22.35 ?  167 SER   A H    1 
ATOM   3530 H  H    B SER   A 1 167 ? 4.104  -12.599 0.684   0.26 23.37 ?  167 SER   A H    1 
ATOM   3531 H  HA   A SER   A 1 167 ? 3.229  -14.395 -1.709  0.74 23.83 ?  167 SER   A HA   1 
ATOM   3532 H  HA   B SER   A 1 167 ? 3.047  -14.388 -1.070  0.26 24.74 ?  167 SER   A HA   1 
ATOM   3533 H  HB2  A SER   A 1 167 ? 4.711  -13.398 -3.220  0.74 24.83 ?  167 SER   A HB2  1 
ATOM   3534 H  HB2  B SER   A 1 167 ? 4.140  -13.340 -2.803  0.26 26.42 ?  167 SER   A HB2  1 
ATOM   3535 H  HB3  A SER   A 1 167 ? 3.636  -12.344 -2.715  0.74 24.83 ?  167 SER   A HB3  1 
ATOM   3536 H  HB3  B SER   A 1 167 ? 3.218  -12.283 -2.057  0.26 26.42 ?  167 SER   A HB3  1 
ATOM   3537 H  HG   A SER   A 1 167 ? 5.183  -11.597 -1.344  0.74 25.82 ?  167 SER   A HG   1 
ATOM   3538 H  HG   B SER   A 1 167 ? 5.036  -11.575 -1.049  0.26 27.53 ?  167 SER   A HG   1 
ATOM   3539 N  N    A PHE   A 1 168 ? 5.553  -14.865 0.222   0.74 20.36 ?  168 PHE   A N    1 
ATOM   3540 N  N    B PHE   A 1 168 ? 5.377  -15.141 0.523   0.26 21.00 ?  168 PHE   A N    1 
ATOM   3541 C  CA   A PHE   A 1 168 ? 6.739  -15.651 0.544   0.74 20.80 ?  168 PHE   A CA   1 
ATOM   3542 C  CA   B PHE   A 1 168 ? 6.587  -15.922 0.743   0.26 21.54 ?  168 PHE   A CA   1 
ATOM   3543 C  C    A PHE   A 1 168 ? 6.433  -17.138 0.464   0.74 22.15 ?  168 PHE   A C    1 
ATOM   3544 C  C    B PHE   A 1 168 ? 6.309  -17.411 0.578   0.26 23.83 ?  168 PHE   A C    1 
ATOM   3545 O  O    A PHE   A 1 168 ? 5.462  -17.624 1.054   0.74 25.03 ?  168 PHE   A O    1 
ATOM   3546 O  O    B PHE   A 1 168 ? 5.346  -17.939 1.143   0.26 24.65 ?  168 PHE   A O    1 
ATOM   3547 C  CB   A PHE   A 1 168 ? 7.261  -15.321 1.940   0.74 19.78 ?  168 PHE   A CB   1 
ATOM   3548 C  CB   B PHE   A 1 168 ? 7.167  -15.649 2.130   0.26 20.10 ?  168 PHE   A CB   1 
ATOM   3549 C  CG   A PHE   A 1 168 ? 8.524  -16.063 2.285   0.74 18.91 ?  168 PHE   A CG   1 
ATOM   3550 C  CG   B PHE   A 1 168 ? 8.411  -16.435 2.423   0.26 19.13 ?  168 PHE   A CG   1 
ATOM   3551 C  CD1  A PHE   A 1 168 ? 9.733  -15.665 1.745   0.74 18.90 ?  168 PHE   A CD1  1 
ATOM   3552 C  CD1  B PHE   A 1 168 ? 9.563  -16.229 1.682   0.26 18.71 ?  168 PHE   A CD1  1 
ATOM   3553 C  CD2  A PHE   A 1 168 ? 8.505  -17.174 3.114   0.74 18.74 ?  168 PHE   A CD2  1 
ATOM   3554 C  CD2  B PHE   A 1 168 ? 8.430  -17.386 3.431   0.26 18.70 ?  168 PHE   A CD2  1 
ATOM   3555 C  CE1  A PHE   A 1 168 ? 10.896 -16.343 2.039   0.74 18.66 ?  168 PHE   A CE1  1 
ATOM   3556 C  CE1  B PHE   A 1 168 ? 10.712 -16.952 1.943   0.26 18.50 ?  168 PHE   A CE1  1 
ATOM   3557 C  CE2  A PHE   A 1 168 ? 9.676  -17.854 3.413   0.74 18.62 ?  168 PHE   A CE2  1 
ATOM   3558 C  CE2  B PHE   A 1 168 ? 9.577  -18.110 3.698   0.26 18.66 ?  168 PHE   A CE2  1 
ATOM   3559 C  CZ   A PHE   A 1 168 ? 10.868 -17.440 2.872   0.74 18.60 ?  168 PHE   A CZ   1 
ATOM   3560 C  CZ   B PHE   A 1 168 ? 10.718 -17.894 2.951   0.26 18.62 ?  168 PHE   A CZ   1 
ATOM   3561 H  H    A PHE   A 1 168 ? 5.210  -14.443 0.886   0.74 24.45 ?  168 PHE   A H    1 
ATOM   3562 H  H    B PHE   A 1 168 ? 4.937  -14.964 1.247   0.26 25.21 ?  168 PHE   A H    1 
ATOM   3563 H  HA   A PHE   A 1 168 ? 7.443  -15.445 -0.097  0.74 24.97 ?  168 PHE   A HA   1 
ATOM   3564 H  HA   B PHE   A 1 168 ? 7.249  -15.667 0.082   0.26 25.85 ?  168 PHE   A HA   1 
ATOM   3565 H  HB2  A PHE   A 1 168 ? 7.450  -14.370 1.993   0.74 23.74 ?  168 PHE   A HB2  1 
ATOM   3566 H  HB2  B PHE   A 1 168 ? 7.386  -14.707 2.194   0.26 24.12 ?  168 PHE   A HB2  1 
ATOM   3567 H  HB3  A PHE   A 1 168 ? 6.586  -15.561 2.592   0.74 23.74 ?  168 PHE   A HB3  1 
ATOM   3568 H  HB3  B PHE   A 1 168 ? 6.503  -15.880 2.797   0.26 24.12 ?  168 PHE   A HB3  1 
ATOM   3569 H  HD1  A PHE   A 1 168 ? 9.766  -14.924 1.182   0.74 22.69 ?  168 PHE   A HD1  1 
ATOM   3570 H  HD1  B PHE   A 1 168 ? 9.564  -15.597 1.000   0.26 22.46 ?  168 PHE   A HD1  1 
ATOM   3571 H  HD2  A PHE   A 1 168 ? 7.701  -17.459 3.481   0.74 22.50 ?  168 PHE   A HD2  1 
ATOM   3572 H  HD2  B PHE   A 1 168 ? 7.662  -17.534 3.936   0.26 22.45 ?  168 PHE   A HD2  1 
ATOM   3573 H  HE1  A PHE   A 1 168 ? 11.707 -16.060 1.675   0.74 22.39 ?  168 PHE   A HE1  1 
ATOM   3574 H  HE1  B PHE   A 1 168 ? 11.479 -16.805 1.438   0.26 22.21 ?  168 PHE   A HE1  1 
ATOM   3575 H  HE2  A PHE   A 1 168 ? 9.650  -18.597 3.975   0.74 22.35 ?  168 PHE   A HE2  1 
ATOM   3576 H  HE2  B PHE   A 1 168 ? 9.579  -18.745 4.377   0.26 22.40 ?  168 PHE   A HE2  1 
ATOM   3577 H  HZ   A PHE   A 1 168 ? 11.657 -17.896 3.071   0.74 22.33 ?  168 PHE   A HZ   1 
ATOM   3578 H  HZ   B PHE   A 1 168 ? 11.490 -18.381 3.128   0.26 22.36 ?  168 PHE   A HZ   1 
ATOM   3579 N  N    A LEU   A 1 169 ? 7.287  -17.866 -0.245  0.74 23.97 ?  169 LEU   A N    1 
ATOM   3580 N  N    B LEU   A 1 169 ? 7.168  -18.082 -0.184  0.26 26.03 ?  169 LEU   A N    1 
ATOM   3581 C  CA   A LEU   A 1 169 ? 7.104  -19.292 -0.398  0.74 27.77 ?  169 LEU   A CA   1 
ATOM   3582 C  CA   B LEU   A 1 169 ? 7.040  -19.511 -0.433  0.26 28.63 ?  169 LEU   A CA   1 
ATOM   3583 C  C    A LEU   A 1 169 ? 7.933  -20.020 0.651   0.74 27.36 ?  169 LEU   A C    1 
ATOM   3584 C  C    B LEU   A 1 169 ? 8.349  -20.211 -0.069  0.26 29.33 ?  169 LEU   A C    1 
ATOM   3585 O  O    A LEU   A 1 169 ? 7.389  -20.476 1.658   0.74 27.79 ?  169 LEU   A O    1 
ATOM   3586 O  O    B LEU   A 1 169 ? 8.379  -21.195 0.672   0.26 29.75 ?  169 LEU   A O    1 
ATOM   3587 C  CB   A LEU   A 1 169 ? 7.485  -19.731 -1.816  0.74 30.84 ?  169 LEU   A CB   1 
ATOM   3588 C  CB   B LEU   A 1 169 ? 6.723  -19.758 -1.909  0.26 30.07 ?  169 LEU   A CB   1 
ATOM   3589 C  CG   A LEU   A 1 169 ? 7.128  -21.169 -2.199  0.74 33.30 ?  169 LEU   A CG   1 
ATOM   3590 C  CG   B LEU   A 1 169 ? 6.704  -21.216 -2.381  0.26 31.25 ?  169 LEU   A CG   1 
ATOM   3591 C  CD1  A LEU   A 1 169 ? 5.694  -21.493 -1.806  0.74 34.74 ?  169 LEU   A CD1  1 
ATOM   3592 C  CD1  B LEU   A 1 169 ? 5.438  -21.924 -1.923  0.26 31.74 ?  169 LEU   A CD1  1 
ATOM   3593 C  CD2  A LEU   A 1 169 ? 7.331  -21.386 -3.692  0.74 33.84 ?  169 LEU   A CD2  1 
ATOM   3594 C  CD2  B LEU   A 1 169 ? 6.856  -21.290 -3.893  0.26 31.65 ?  169 LEU   A CD2  1 
ATOM   3595 O  OXT  A LEU   A 1 169 ? 9.153  -20.151 0.530   0.74 26.45 -1 169 LEU   A OXT  1 
ATOM   3596 O  OXT  B LEU   A 1 169 ? 9.421  -19.804 -0.518  0.26 29.58 -1 169 LEU   A OXT  1 
ATOM   3597 H  H    A LEU   A 1 169 ? 7.984  -17.554 -0.645  0.74 28.77 ?  169 LEU   A H    1 
ATOM   3598 H  H    B LEU   A 1 169 ? 7.847  -17.725 -0.573  0.26 31.25 ?  169 LEU   A H    1 
ATOM   3599 H  HA   A LEU   A 1 169 ? 6.172  -19.506 -0.247  0.74 33.33 ?  169 LEU   A HA   1 
ATOM   3600 H  HA   B LEU   A 1 169 ? 6.312  -19.871 0.102   0.26 34.36 ?  169 LEU   A HA   1 
ATOM   3601 H  HB2  A LEU   A 1 169 ? 7.034  -19.147 -2.447  0.74 37.02 ?  169 LEU   A HB2  1 
ATOM   3602 H  HB2  B LEU   A 1 169 ? 5.848  -19.386 -2.097  0.26 36.10 ?  169 LEU   A HB2  1 
ATOM   3603 H  HB3  A LEU   A 1 169 ? 8.444  -19.637 -1.919  0.74 37.02 ?  169 LEU   A HB3  1 
ATOM   3604 H  HB3  B LEU   A 1 169 ? 7.389  -19.295 -2.439  0.26 36.10 ?  169 LEU   A HB3  1 
ATOM   3605 H  HG   A LEU   A 1 169 ? 7.715  -21.780 -1.727  0.74 39.96 ?  169 LEU   A HG   1 
ATOM   3606 H  HG   B LEU   A 1 169 ? 7.457  -21.686 -1.994  0.26 37.51 ?  169 LEU   A HG   1 
ATOM   3607 H  HD11 A LEU   A 1 169 ? 5.416  -22.301 -2.263  0.74 41.70 ?  169 LEU   A HD11 1 
ATOM   3608 H  HD11 B LEU   A 1 169 ? 5.459  -22.841 -2.239  0.26 38.10 ?  169 LEU   A HD11 1 
ATOM   3609 H  HD12 A LEU   A 1 169 ? 5.652  -21.625 -0.845  0.74 41.70 ?  169 LEU   A HD12 1 
ATOM   3610 H  HD12 B LEU   A 1 169 ? 5.400  -21.908 -0.954  0.26 38.10 ?  169 LEU   A HD12 1 
ATOM   3611 H  HD13 A LEU   A 1 169 ? 5.122  -20.753 -2.064  0.74 41.70 ?  169 LEU   A HD13 1 
ATOM   3612 H  HD13 B LEU   A 1 169 ? 4.668  -21.464 -2.293  0.26 38.10 ?  169 LEU   A HD13 1 
ATOM   3613 H  HD21 A LEU   A 1 169 ? 7.108  -22.304 -3.912  0.74 40.62 ?  169 LEU   A HD21 1 
ATOM   3614 H  HD21 B LEU   A 1 169 ? 6.832  -22.220 -4.166  0.26 37.99 ?  169 LEU   A HD21 1 
ATOM   3615 H  HD22 A LEU   A 1 169 ? 6.750  -20.780 -4.180  0.74 40.62 ?  169 LEU   A HD22 1 
ATOM   3616 H  HD22 B LEU   A 1 169 ? 6.128  -20.803 -4.308  0.26 37.99 ?  169 LEU   A HD22 1 
ATOM   3617 H  HD23 A LEU   A 1 169 ? 8.257  -21.208 -3.915  0.74 40.62 ?  169 LEU   A HD23 1 
ATOM   3618 H  HD23 B LEU   A 1 169 ? 7.706  -20.894 -4.145  0.26 37.99 ?  169 LEU   A HD23 1 
ATOM   3619 N  N    . SER   B 1 1   ? 50.800 -9.243  -23.739 1.00 31.18 ?  1   SER   B N    1 
ATOM   3620 C  CA   . SER   B 1 1   ? 51.290 -10.281 -22.813 1.00 30.50 ?  1   SER   B CA   1 
ATOM   3621 C  C    . SER   B 1 1   ? 50.223 -11.338 -22.559 1.00 28.68 ?  1   SER   B C    1 
ATOM   3622 O  O    . SER   B 1 1   ? 49.035 -11.161 -22.882 1.00 27.93 ?  1   SER   B O    1 
ATOM   3623 C  CB   . SER   B 1 1   ? 51.739 -9.675  -21.488 1.00 30.95 ?  1   SER   B CB   1 
ATOM   3624 O  OG   . SER   B 1 1   ? 50.649 -9.574  -20.595 1.00 33.67 ?  1   SER   B OG   1 
ATOM   3625 H  H1   . SER   B 1 1   ? 50.609 -9.619  -24.520 1.00 37.43 ?  1   SER   B H1   1 
ATOM   3626 H  H2   . SER   B 1 1   ? 50.074 -8.869  -23.396 1.00 37.43 ?  1   SER   B H2   1 
ATOM   3627 H  H3   . SER   B 1 1   ? 51.435 -8.631  -23.845 1.00 37.43 ?  1   SER   B H3   1 
ATOM   3628 H  HA   . SER   B 1 1   ? 52.054 -10.711 -23.221 1.00 36.61 ?  1   SER   B HA   1 
ATOM   3629 H  HB2  . SER   B 1 1   ? 52.412 -10.250 -21.096 1.00 37.15 ?  1   SER   B HB2  1 
ATOM   3630 H  HB3  . SER   B 1 1   ? 52.106 -8.792  -21.650 1.00 37.15 ?  1   SER   B HB3  1 
ATOM   3631 H  HG   . SER   B 1 1   ? 50.925 -9.611  -19.802 1.00 40.42 ?  1   SER   B HG   1 
ATOM   3632 N  N    A MET   B 1 2   ? 50.671 -12.449 -21.990 0.74 28.42 ?  2   MET   B N    1 
ATOM   3633 N  N    B MET   B 1 2   ? 50.647 -12.432 -21.935 0.26 28.75 ?  2   MET   B N    1 
ATOM   3634 C  CA   A MET   B 1 2   ? 49.868 -13.658 -21.850 0.74 28.54 ?  2   MET   B CA   1 
ATOM   3635 C  CA   B MET   B 1 2   ? 49.828 -13.627 -21.768 0.26 28.67 ?  2   MET   B CA   1 
ATOM   3636 C  C    A MET   B 1 2   ? 49.629 -13.908 -20.369 0.74 26.54 ?  2   MET   B C    1 
ATOM   3637 C  C    B MET   B 1 2   ? 49.578 -13.850 -20.282 0.26 27.08 ?  2   MET   B C    1 
ATOM   3638 O  O    A MET   B 1 2   ? 50.549 -14.298 -19.644 0.74 27.22 ?  2   MET   B O    1 
ATOM   3639 O  O    B MET   B 1 2   ? 50.481 -14.275 -19.553 0.26 27.60 ?  2   MET   B O    1 
ATOM   3640 C  CB   A MET   B 1 2   ? 50.606 -14.830 -22.489 0.74 32.62 ?  2   MET   B CB   1 
ATOM   3641 C  CB   B MET   B 1 2   ? 50.555 -14.815 -22.384 0.26 30.64 ?  2   MET   B CB   1 
ATOM   3642 C  CG   A MET   B 1 2   ? 49.779 -16.091 -22.675 0.74 36.67 ?  2   MET   B CG   1 
ATOM   3643 C  CG   B MET   B 1 2   ? 49.670 -15.987 -22.772 0.26 32.36 ?  2   MET   B CG   1 
ATOM   3644 S  SD   A MET   B 1 2   ? 50.655 -17.292 -23.697 0.74 40.55 ?  2   MET   B SD   1 
ATOM   3645 S  SD   B MET   B 1 2   ? 50.549 -17.118 -23.861 0.26 33.88 ?  2   MET   B SD   1 
ATOM   3646 C  CE   A MET   B 1 2   ? 51.169 -16.236 -25.040 0.74 40.40 ?  2   MET   B CE   1 
ATOM   3647 C  CE   B MET   B 1 2   ? 51.388 -15.948 -24.917 0.26 33.97 ?  2   MET   B CE   1 
ATOM   3648 H  H    A MET   B 1 2   ? 51.465 -12.536 -21.669 0.74 34.11 ?  2   MET   B H    1 
ATOM   3649 H  H    B MET   B 1 2   ? 51.434 -12.511 -21.598 0.26 34.50 ?  2   MET   B H    1 
ATOM   3650 H  HA   A MET   B 1 2   ? 49.022 -13.552 -22.306 0.74 34.25 ?  2   MET   B HA   1 
ATOM   3651 H  HA   B MET   B 1 2   ? 48.988 -13.522 -22.239 0.26 34.42 ?  2   MET   B HA   1 
ATOM   3652 H  HB2  A MET   B 1 2   ? 50.913 -14.529 -23.352 0.74 39.15 ?  2   MET   B HB2  1 
ATOM   3653 H  HB2  B MET   B 1 2   ? 51.001 -14.464 -23.165 0.26 36.78 ?  2   MET   B HB2  1 
ATOM   3654 H  HB3  A MET   B 1 2   ? 51.365 -15.075 -21.940 0.74 39.15 ?  2   MET   B HB3  1 
ATOM   3655 H  HB3  B MET   B 1 2   ? 51.213 -15.159 -21.767 0.26 36.78 ?  2   MET   B HB3  1 
ATOM   3656 H  HG2  A MET   B 1 2   ? 49.605 -16.494 -21.806 0.74 44.01 ?  2   MET   B HG2  1 
ATOM   3657 H  HG2  B MET   B 1 2   ? 49.407 -16.471 -21.970 0.26 38.84 ?  2   MET   B HG2  1 
ATOM   3658 H  HG3  A MET   B 1 2   ? 48.944 -15.874 -23.116 0.74 44.01 ?  2   MET   B HG3  1 
ATOM   3659 H  HG3  B MET   B 1 2   ? 48.888 -15.671 -23.244 0.26 38.84 ?  2   MET   B HG3  1 
ATOM   3660 H  HE1  A MET   B 1 2   ? 51.336 -16.781 -25.813 0.74 48.49 ?  2   MET   B HE1  1 
ATOM   3661 H  HE1  B MET   B 1 2   ? 51.626 -16.398 -25.724 0.26 40.77 ?  2   MET   B HE1  1 
ATOM   3662 H  HE2  A MET   B 1 2   ? 50.456 -15.601 -25.221 0.74 48.49 ?  2   MET   B HE2  1 
ATOM   3663 H  HE2  B MET   B 1 2   ? 50.784 -15.209 -25.111 0.26 40.77 ?  2   MET   B HE2  1 
ATOM   3664 H  HE3  A MET   B 1 2   ? 51.976 -15.761 -24.779 0.74 48.49 ?  2   MET   B HE3  1 
ATOM   3665 H  HE3  B MET   B 1 2   ? 52.187 -15.618 -24.465 0.26 40.77 ?  2   MET   B HE3  1 
ATOM   3666 N  N    A VAL   B 1 3   ? 48.399 -13.667 -19.920 0.74 23.51 ?  3   VAL   B N    1 
ATOM   3667 N  N    B VAL   B 1 3   ? 48.360 -13.554 -19.836 0.26 24.90 ?  3   VAL   B N    1 
ATOM   3668 C  CA   A VAL   B 1 3   ? 47.987 -13.930 -18.549 0.74 22.10 ?  3   VAL   B CA   1 
ATOM   3669 C  CA   B VAL   B 1 3   ? 47.932 -13.829 -18.470 0.26 23.01 ?  3   VAL   B CA   1 
ATOM   3670 C  C    A VAL   B 1 3   ? 46.746 -14.819 -18.584 0.74 19.83 ?  3   VAL   B C    1 
ATOM   3671 C  C    B VAL   B 1 3   ? 46.675 -14.690 -18.510 0.26 20.72 ?  3   VAL   B C    1 
ATOM   3672 O  O    A VAL   B 1 3   ? 46.030 -14.897 -19.585 0.74 20.54 ?  3   VAL   B O    1 
ATOM   3673 O  O    B VAL   B 1 3   ? 45.869 -14.607 -19.442 0.26 20.91 ?  3   VAL   B O    1 
ATOM   3674 C  CB   A VAL   B 1 3   ? 47.718 -12.622 -17.761 0.74 24.36 ?  3   VAL   B CB   1 
ATOM   3675 C  CB   B VAL   B 1 3   ? 47.681 -12.539 -17.656 0.26 23.59 ?  3   VAL   B CB   1 
ATOM   3676 C  CG1  A VAL   B 1 3   ? 48.997 -11.782 -17.647 0.74 25.26 ?  3   VAL   B CG1  1 
ATOM   3677 C  CG1  B VAL   B 1 3   ? 48.959 -11.717 -17.536 0.26 23.86 ?  3   VAL   B CG1  1 
ATOM   3678 C  CG2  A VAL   B 1 3   ? 46.607 -11.817 -18.418 0.74 25.18 ?  3   VAL   B CG2  1 
ATOM   3679 C  CG2  B VAL   B 1 3   ? 46.563 -11.718 -18.281 0.26 23.78 ?  3   VAL   B CG2  1 
ATOM   3680 H  H    A VAL   B 1 3   ? 47.770 -13.344 -20.408 0.74 28.23 ?  3   VAL   B H    1 
ATOM   3681 H  H    B VAL   B 1 3   ? 47.760 -13.177 -20.321 0.26 29.88 ?  3   VAL   B H    1 
ATOM   3682 H  HA   A VAL   B 1 3   ? 48.692 -14.412 -18.088 0.74 26.53 ?  3   VAL   B HA   1 
ATOM   3683 H  HA   B VAL   B 1 3   ? 48.630 -14.331 -18.022 0.26 27.63 ?  3   VAL   B HA   1 
ATOM   3684 H  HB   A VAL   B 1 3   ? 47.434 -12.850 -16.861 0.74 29.24 ?  3   VAL   B HB   1 
ATOM   3685 H  HB   B VAL   B 1 3   ? 47.404 -12.788 -16.761 0.26 28.31 ?  3   VAL   B HB   1 
ATOM   3686 H  HG11 A VAL   B 1 3   ? 48.802 -10.978 -17.141 0.74 30.33 ?  3   VAL   B HG11 1 
ATOM   3687 H  HG11 B VAL   B 1 3   ? 48.775 -10.924 -17.007 0.26 28.64 ?  3   VAL   B HG11 1 
ATOM   3688 H  HG12 A VAL   B 1 3   ? 49.677 -12.304 -17.192 0.74 30.33 ?  3   VAL   B HG12 1 
ATOM   3689 H  HG12 B VAL   B 1 3   ? 49.639 -12.254 -17.100 0.26 28.64 ?  3   VAL   B HG12 1 
ATOM   3690 H  HG13 A VAL   B 1 3   ? 49.300 -11.549 -18.538 0.74 30.33 ?  3   VAL   B HG13 1 
ATOM   3691 H  HG13 B VAL   B 1 3   ? 49.256 -11.463 -18.423 0.26 28.64 ?  3   VAL   B HG13 1 
ATOM   3692 H  HG21 A VAL   B 1 3   ? 46.542 -10.956 -17.979 0.74 30.23 ?  3   VAL   B HG21 1 
ATOM   3693 H  HG21 B VAL   B 1 3   ? 46.516 -10.860 -17.833 0.26 28.55 ?  3   VAL   B HG21 1 
ATOM   3694 H  HG22 A VAL   B 1 3   ? 46.815 -11.699 -19.356 0.74 30.23 ?  3   VAL   B HG22 1 
ATOM   3695 H  HG22 B VAL   B 1 3   ? 46.752 -11.592 -19.223 0.26 28.55 ?  3   VAL   B HG22 1 
ATOM   3696 H  HG23 A VAL   B 1 3   ? 45.770 -12.301 -18.321 0.74 30.23 ?  3   VAL   B HG23 1 
ATOM   3697 H  HG23 B VAL   B 1 3   ? 45.724 -12.194 -18.173 0.26 28.55 ?  3   VAL   B HG23 1 
ATOM   3698 N  N    . ASN   B 1 4   ? 46.506 -15.513 -17.474 1.00 18.76 ?  4   ASN   B N    1 
ATOM   3699 C  CA   . ASN   B 1 4   ? 45.367 -16.428 -17.376 1.00 17.37 ?  4   ASN   B CA   1 
ATOM   3700 C  C    . ASN   B 1 4   ? 45.324 -17.386 -18.564 1.00 18.02 ?  4   ASN   B C    1 
ATOM   3701 O  O    . ASN   B 1 4   ? 44.267 -17.639 -19.136 1.00 18.68 ?  4   ASN   B O    1 
ATOM   3702 C  CB   . ASN   B 1 4   ? 44.050 -15.661 -17.227 1.00 16.78 ?  4   ASN   B CB   1 
ATOM   3703 C  CG   . ASN   B 1 4   ? 43.997 -14.857 -15.946 1.00 15.99 ?  4   ASN   B CG   1 
ATOM   3704 O  OD1  . ASN   B 1 4   ? 44.318 -15.359 -14.871 1.00 15.63 ?  4   ASN   B OD1  1 
ATOM   3705 N  ND2  . ASN   B 1 4   ? 43.627 -13.585 -16.058 1.00 16.97 ?  4   ASN   B ND2  1 
ATOM   3706 H  H    A ASN   B 1 4   ? 46.994 -15.477 -16.769 0.74 22.53 ?  4   ASN   B H    1 
ATOM   3707 H  H    B ASN   B 1 4   ? 47.041 -15.549 -16.805 0.26 22.53 ?  4   ASN   B H    1 
ATOM   3708 H  HA   . ASN   B 1 4   ? 45.482 -16.962 -16.579 1.00 20.85 ?  4   ASN   B HA   1 
ATOM   3709 H  HB2  . ASN   B 1 4   ? 43.948 -15.048 -17.974 1.00 20.14 ?  4   ASN   B HB2  1 
ATOM   3710 H  HB3  . ASN   B 1 4   ? 43.314 -16.295 -17.220 1.00 20.14 ?  4   ASN   B HB3  1 
ATOM   3711 H  HD21 . ASN   B 1 4   ? 43.578 -13.084 -15.357 1.00 20.37 ?  4   ASN   B HD21 1 
ATOM   3712 H  HD22 . ASN   B 1 4   ? 43.413 -13.257 -16.827 1.00 20.37 ?  4   ASN   B HD22 1 
ATOM   3713 N  N    . SER   B 1 5   ? 46.485 -17.936 -18.932 1.00 18.39 ?  5   SER   B N    1 
ATOM   3714 C  CA   . SER   B 1 5   ? 46.587 -18.851 -20.072 1.00 21.14 ?  5   SER   B CA   1 
ATOM   3715 C  C    . SER   B 1 5   ? 46.580 -20.280 -19.538 1.00 22.89 ?  5   SER   B C    1 
ATOM   3716 O  O    . SER   B 1 5   ? 47.603 -20.957 -19.478 1.00 25.85 ?  5   SER   B O    1 
ATOM   3717 C  CB   . SER   B 1 5   ? 47.834 -18.557 -20.902 1.00 23.58 ?  5   SER   B CB   1 
ATOM   3718 O  OG   . SER   B 1 5   ? 49.016 -18.777 -20.149 1.00 27.47 ?  5   SER   B OG   1 
ATOM   3719 H  H    . SER   B 1 5   ? 47.239 -17.792 -18.535 1.00 22.08 ?  5   SER   B H    1 
ATOM   3720 H  HA   . SER   B 1 5   ? 45.814 -18.742 -20.639 1.00 25.37 ?  5   SER   B HA   1 
ATOM   3721 H  HB2  . SER   B 1 5   ? 47.836 -19.134 -21.685 1.00 28.31 ?  5   SER   B HB2  1 
ATOM   3722 H  HB3  . SER   B 1 5   ? 47.801 -17.629 -21.180 1.00 28.31 ?  5   SER   B HB3  1 
ATOM   3723 H  HG   . SER   B 1 5   ? 49.073 -19.590 -19.941 1.00 32.97 ?  5   SER   B HG   1 
ATOM   3724 N  N    . PHE   B 1 6   ? 45.394 -20.732 -19.139 1.00 22.94 ?  6   PHE   B N    1 
ATOM   3725 C  CA   . PHE   B 1 6   ? 45.216 -22.079 -18.612 1.00 21.97 ?  6   PHE   B CA   1 
ATOM   3726 C  C    . PHE   B 1 6   ? 45.157 -23.071 -19.763 1.00 25.51 ?  6   PHE   B C    1 
ATOM   3727 O  O    . PHE   B 1 6   ? 44.477 -22.831 -20.764 1.00 28.09 ?  6   PHE   B O    1 
ATOM   3728 C  CB   . PHE   B 1 6   ? 43.923 -22.142 -17.796 1.00 20.09 ?  6   PHE   B CB   1 
ATOM   3729 C  CG   . PHE   B 1 6   ? 43.935 -21.270 -16.569 1.00 17.85 ?  6   PHE   B CG   1 
ATOM   3730 C  CD1  . PHE   B 1 6   ? 44.442 -21.747 -15.378 1.00 17.14 ?  6   PHE   B CD1  1 
ATOM   3731 C  CD2  . PHE   B 1 6   ? 43.448 -19.973 -16.613 1.00 17.58 ?  6   PHE   B CD2  1 
ATOM   3732 C  CE1  . PHE   B 1 6   ? 44.455 -20.952 -14.239 1.00 16.51 ?  6   PHE   B CE1  1 
ATOM   3733 C  CE2  . PHE   B 1 6   ? 43.465 -19.163 -15.485 1.00 18.28 ?  6   PHE   B CE2  1 
ATOM   3734 C  CZ   . PHE   B 1 6   ? 43.969 -19.647 -14.298 1.00 17.11 ?  6   PHE   B CZ   1 
ATOM   3735 H  H    . PHE   B 1 6   ? 44.670 -20.272 -19.165 1.00 27.53 ?  6   PHE   B H    1 
ATOM   3736 H  HA   . PHE   B 1 6   ? 45.959 -22.313 -18.037 1.00 26.37 ?  6   PHE   B HA   1 
ATOM   3737 H  HB2  . PHE   B 1 6   ? 43.184 -21.856 -18.357 1.00 24.11 ?  6   PHE   B HB2  1 
ATOM   3738 H  HB3  . PHE   B 1 6   ? 43.779 -23.057 -17.506 1.00 24.11 ?  6   PHE   B HB3  1 
ATOM   3739 H  HD1  . PHE   B 1 6   ? 44.774 -22.614 -15.334 1.00 20.57 ?  6   PHE   B HD1  1 
ATOM   3740 H  HD2  . PHE   B 1 6   ? 43.106 -19.640 -17.411 1.00 21.10 ?  6   PHE   B HD2  1 
ATOM   3741 H  HE1  . PHE   B 1 6   ? 44.806 -21.278 -13.440 1.00 19.82 ?  6   PHE   B HE1  1 
ATOM   3742 H  HE2  . PHE   B 1 6   ? 43.131 -18.293 -15.529 1.00 21.95 ?  6   PHE   B HE2  1 
ATOM   3743 H  HZ   . PHE   B 1 6   ? 43.980 -19.108 -13.538 1.00 20.54 ?  6   PHE   B HZ   1 
ATOM   3744 N  N    A SER   B 1 7   ? 45.869 -24.189 -19.618 0.74 24.94 ?  7   SER   B N    1 
ATOM   3745 N  N    B SER   B 1 7   ? 45.878 -24.184 -19.622 0.26 26.47 ?  7   SER   B N    1 
ATOM   3746 C  CA   A SER   B 1 7   ? 45.955 -25.187 -20.674 0.74 27.47 ?  7   SER   B CA   1 
ATOM   3747 C  CA   B SER   B 1 7   ? 45.986 -25.181 -20.677 0.26 27.91 ?  7   SER   B CA   1 
ATOM   3748 C  C    A SER   B 1 7   ? 45.928 -26.587 -20.078 0.74 26.69 ?  7   SER   B C    1 
ATOM   3749 C  C    B SER   B 1 7   ? 45.961 -26.575 -20.071 0.26 27.56 ?  7   SER   B C    1 
ATOM   3750 O  O    A SER   B 1 7   ? 46.526 -26.841 -19.028 0.74 27.80 ?  7   SER   B O    1 
ATOM   3751 O  O    B SER   B 1 7   ? 46.559 -26.816 -19.018 0.26 27.98 ?  7   SER   B O    1 
ATOM   3752 C  CB   A SER   B 1 7   ? 47.234 -25.005 -21.501 0.74 30.44 ?  7   SER   B CB   1 
ATOM   3753 C  CB   B SER   B 1 7   ? 47.286 -24.998 -21.473 0.26 29.50 ?  7   SER   B CB   1 
ATOM   3754 O  OG   A SER   B 1 7   ? 47.200 -25.801 -22.672 0.74 33.33 ?  7   SER   B OG   1 
ATOM   3755 O  OG   B SER   B 1 7   ? 47.398 -25.971 -22.497 0.26 30.75 ?  7   SER   B OG   1 
ATOM   3756 H  H    A SER   B 1 7   ? 46.313 -24.389 -18.906 0.74 29.94 ?  7   SER   B H    1 
ATOM   3757 H  H    B SER   B 1 7   ? 46.319 -24.384 -18.911 0.26 31.77 ?  7   SER   B H    1 
ATOM   3758 H  HA   A SER   B 1 7   ? 45.194 -25.097 -21.264 0.74 32.97 ?  7   SER   B HA   1 
ATOM   3759 H  HA   B SER   B 1 7   ? 45.237 -25.096 -21.285 0.26 33.50 ?  7   SER   B HA   1 
ATOM   3760 H  HB2  A SER   B 1 7   ? 47.312 -24.071 -21.758 0.74 36.54 ?  7   SER   B HB2  1 
ATOM   3761 H  HB2  B SER   B 1 7   ? 47.287 -24.113 -21.873 0.26 35.41 ?  7   SER   B HB2  1 
ATOM   3762 H  HB3  A SER   B 1 7   ? 47.999 -25.262 -20.962 0.74 36.54 ?  7   SER   B HB3  1 
ATOM   3763 H  HB3  B SER   B 1 7   ? 48.041 -25.089 -20.871 0.26 35.41 ?  7   SER   B HB3  1 
ATOM   3764 H  HG   A SER   B 1 7   ? 47.907 -25.693 -23.113 0.74 40.01 ?  7   SER   B HG   1 
ATOM   3765 H  HG   B SER   B 1 7   ? 48.111 -25.855 -22.927 0.26 36.91 ?  7   SER   B HG   1 
ATOM   3766 N  N    A GLY   B 1 8   ? 45.232 -27.495 -20.761 0.74 26.42 ?  8   GLY   B N    1 
ATOM   3767 N  N    B GLY   B 1 8   ? 45.266 -27.490 -20.744 0.26 27.00 ?  8   GLY   B N    1 
ATOM   3768 C  CA   A GLY   B 1 8   ? 45.214 -28.886 -20.364 0.74 26.37 ?  8   GLY   B CA   1 
ATOM   3769 C  CA   B GLY   B 1 8   ? 45.243 -28.876 -20.326 0.26 26.27 ?  8   GLY   B CA   1 
ATOM   3770 C  C    A GLY   B 1 8   ? 44.250 -29.226 -19.257 0.74 25.37 ?  8   GLY   B C    1 
ATOM   3771 C  C    B GLY   B 1 8   ? 44.288 -29.194 -19.202 0.26 25.18 ?  8   GLY   B C    1 
ATOM   3772 O  O    A GLY   B 1 8   ? 44.375 -30.299 -18.654 0.74 26.79 ?  8   GLY   B O    1 
ATOM   3773 O  O    B GLY   B 1 8   ? 44.464 -30.216 -18.530 0.26 25.60 ?  8   GLY   B O    1 
ATOM   3774 H  H    A GLY   B 1 8   ? 44.760 -27.320 -21.455 0.74 31.71 ?  8   GLY   B H    1 
ATOM   3775 H  H    B GLY   B 1 8   ? 44.798 -27.326 -21.446 0.26 32.41 ?  8   GLY   B H    1 
ATOM   3776 H  HA2  A GLY   B 1 8   ? 44.980 -29.428 -21.133 0.74 31.65 ?  8   GLY   B HA2  1 
ATOM   3777 H  HA2  B GLY   B 1 8   ? 45.003 -29.429 -21.087 0.26 31.53 ?  8   GLY   B HA2  1 
ATOM   3778 H  HA3  A GLY   B 1 8   ? 46.100 -29.143 -20.072 0.74 31.65 ?  8   GLY   B HA3  1 
ATOM   3779 H  HA3  B GLY   B 1 8   ? 46.130 -29.133 -20.036 0.26 31.53 ?  8   GLY   B HA3  1 
ATOM   3780 N  N    . TYR   B 1 9   ? 43.280 -28.358 -18.973 1.00 23.91 ?  9   TYR   B N    1 
ATOM   3781 C  CA   . TYR   B 1 9   ? 42.304 -28.612 -17.924 1.00 21.12 ?  9   TYR   B CA   1 
ATOM   3782 C  C    . TYR   B 1 9   ? 41.123 -29.405 -18.460 1.00 20.83 ?  9   TYR   B C    1 
ATOM   3783 O  O    . TYR   B 1 9   ? 40.729 -29.271 -19.622 1.00 23.38 ?  9   TYR   B O    1 
ATOM   3784 C  CB   . TYR   B 1 9   ? 41.795 -27.312 -17.307 1.00 20.40 ?  9   TYR   B CB   1 
ATOM   3785 C  CG   . TYR   B 1 9   ? 42.811 -26.687 -16.386 1.00 19.63 ?  9   TYR   B CG   1 
ATOM   3786 C  CD1  . TYR   B 1 9   ? 43.933 -26.046 -16.898 1.00 20.48 ?  9   TYR   B CD1  1 
ATOM   3787 C  CD2  . TYR   B 1 9   ? 42.674 -26.761 -15.007 1.00 19.43 ?  9   TYR   B CD2  1 
ATOM   3788 C  CE1  . TYR   B 1 9   ? 44.877 -25.487 -16.069 1.00 20.93 ?  9   TYR   B CE1  1 
ATOM   3789 C  CE2  . TYR   B 1 9   ? 43.620 -26.208 -14.165 1.00 19.81 ?  9   TYR   B CE2  1 
ATOM   3790 C  CZ   . TYR   B 1 9   ? 44.717 -25.567 -14.705 1.00 21.19 ?  9   TYR   B CZ   1 
ATOM   3791 O  OH   . TYR   B 1 9   ? 45.671 -25.014 -13.886 1.00 21.40 ?  9   TYR   B OH   1 
ATOM   3792 H  H    A TYR   B 1 9   ? 43.154 -27.617 -19.390 0.74 28.70 ?  9   TYR   B H    1 
ATOM   3793 H  H    B TYR   B 1 9   ? 43.131 -27.639 -19.421 0.26 28.70 ?  9   TYR   B H    1 
ATOM   3794 H  HA   . TYR   B 1 9   ? 42.718 -29.131 -17.222 1.00 25.35 ?  9   TYR   B HA   1 
ATOM   3795 H  HB2  . TYR   B 1 9   ? 41.587 -26.674 -18.010 1.00 24.48 ?  9   TYR   B HB2  1 
ATOM   3796 H  HB3  . TYR   B 1 9   ? 41.002 -27.507 -16.788 1.00 24.48 ?  9   TYR   B HB3  1 
ATOM   3797 H  HD1  . TYR   B 1 9   ? 44.043 -25.990 -17.820 1.00 24.58 ?  9   TYR   B HD1  1 
ATOM   3798 H  HD2  . TYR   B 1 9   ? 41.931 -27.191 -14.642 1.00 23.32 ?  9   TYR   B HD2  1 
ATOM   3799 H  HE1  . TYR   B 1 9   ? 45.618 -25.061 -16.427 1.00 25.12 ?  9   TYR   B HE1  1 
ATOM   3800 H  HE2  . TYR   B 1 9   ? 43.511 -26.258 -13.239 1.00 23.78 ?  9   TYR   B HE2  1 
ATOM   3801 H  HH   . TYR   B 1 9   ? 46.274 -24.661 -14.346 1.00 25.69 ?  9   TYR   B HH   1 
ATOM   3802 N  N    . LEU   B 1 10  ? 40.564 -30.241 -17.590 1.00 19.00 ?  10  LEU   B N    1 
ATOM   3803 C  CA   . LEU   B 1 10  ? 39.360 -31.004 -17.876 1.00 19.34 ?  10  LEU   B CA   1 
ATOM   3804 C  C    . LEU   B 1 10  ? 38.166 -30.239 -17.326 1.00 18.24 ?  10  LEU   B C    1 
ATOM   3805 O  O    . LEU   B 1 10  ? 38.177 -29.809 -16.168 1.00 18.43 ?  10  LEU   B O    1 
ATOM   3806 C  CB   . LEU   B 1 10  ? 39.438 -32.376 -17.211 1.00 20.49 ?  10  LEU   B CB   1 
ATOM   3807 C  CG   . LEU   B 1 10  ? 38.260 -33.293 -17.519 1.00 22.11 ?  10  LEU   B CG   1 
ATOM   3808 C  CD1  . LEU   B 1 10  ? 38.326 -33.755 -18.969 1.00 23.87 ?  10  LEU   B CD1  1 
ATOM   3809 C  CD2  . LEU   B 1 10  ? 38.245 -34.476 -16.573 1.00 23.92 ?  10  LEU   B CD2  1 
ATOM   3810 H  H    . LEU   B 1 10  ? 40.878 -30.385 -16.798 1.00 22.81 ?  10  LEU   B H    1 
ATOM   3811 H  HA   . LEU   B 1 10  ? 39.258 -31.119 -18.831 1.00 23.22 ?  10  LEU   B HA   1 
ATOM   3812 H  HB2  . LEU   B 1 10  ? 40.246 -32.824 -17.508 1.00 24.60 ?  10  LEU   B HB2  1 
ATOM   3813 H  HB3  . LEU   B 1 10  ? 39.471 -32.254 -16.246 1.00 24.60 ?  10  LEU   B HB3  1 
ATOM   3814 H  HG   . LEU   B 1 10  ? 37.431 -32.802 -17.398 1.00 26.55 ?  10  LEU   B HG   1 
ATOM   3815 H  HD11 . LEU   B 1 10  ? 37.627 -34.406 -19.122 1.00 28.65 ?  10  LEU   B HD11 1 
ATOM   3816 H  HD12 . LEU   B 1 10  ? 38.196 -32.986 -19.550 1.00 28.65 ?  10  LEU   B HD12 1 
ATOM   3817 H  HD13 . LEU   B 1 10  ? 39.195 -34.150 -19.132 1.00 28.65 ?  10  LEU   B HD13 1 
ATOM   3818 H  HD21 . LEU   B 1 10  ? 37.490 -35.042 -16.793 1.00 28.71 ?  10  LEU   B HD21 1 
ATOM   3819 H  HD22 . LEU   B 1 10  ? 39.072 -34.968 -16.674 1.00 28.71 ?  10  LEU   B HD22 1 
ATOM   3820 H  HD23 . LEU   B 1 10  ? 38.160 -34.148 -15.664 1.00 28.71 ?  10  LEU   B HD23 1 
ATOM   3821 N  N    . LYS   B 1 11  ? 37.149 -30.054 -18.158 1.00 19.54 ?  11  LYS   B N    1 
ATOM   3822 C  CA   . LYS   B 1 11  ? 35.961 -29.320 -17.747 1.00 20.85 ?  11  LYS   B CA   1 
ATOM   3823 C  C    . LYS   B 1 11  ? 35.048 -30.230 -16.930 1.00 20.10 ?  11  LYS   B C    1 
ATOM   3824 O  O    . LYS   B 1 11  ? 34.616 -31.289 -17.411 1.00 23.22 ?  11  LYS   B O    1 
ATOM   3825 C  CB   . LYS   B 1 11  ? 35.235 -28.807 -18.987 1.00 24.99 ?  11  LYS   B CB   1 
ATOM   3826 C  CG   . LYS   B 1 11  ? 34.019 -27.951 -18.701 1.00 28.61 ?  11  LYS   B CG   1 
ATOM   3827 C  CD   . LYS   B 1 11  ? 33.265 -27.659 -19.991 1.00 32.18 ?  11  LYS   B CD   1 
ATOM   3828 C  CE   . LYS   B 1 11  ? 32.241 -26.554 -19.808 1.00 34.73 ?  11  LYS   B CE   1 
ATOM   3829 N  NZ   . LYS   B 1 11  ? 32.892 -25.227 -19.644 1.00 36.38 ?  11  LYS   B NZ   1 
ATOM   3830 H  H    . LYS   B 1 11  ? 37.124 -30.343 -18.968 1.00 23.46 ?  11  LYS   B H    1 
ATOM   3831 H  HA   . LYS   B 1 11  ? 36.225 -28.559 -17.200 1.00 25.03 ?  11  LYS   B HA   1 
ATOM   3832 H  HB2  . LYS   B 1 11  ? 35.854 -28.273 -19.510 1.00 30.00 ?  11  LYS   B HB2  1 
ATOM   3833 H  HB3  . LYS   B 1 11  ? 34.943 -29.570 -19.508 1.00 30.00 ?  11  LYS   B HB3  1 
ATOM   3834 H  HG2  . LYS   B 1 11  ? 33.422 -28.422 -18.097 1.00 34.34 ?  11  LYS   B HG2  1 
ATOM   3835 H  HG3  . LYS   B 1 11  ? 34.300 -27.108 -18.309 1.00 34.34 ?  11  LYS   B HG3  1 
ATOM   3836 H  HD2  . LYS   B 1 11  ? 33.897 -27.378 -20.672 1.00 38.63 ?  11  LYS   B HD2  1 
ATOM   3837 H  HD3  . LYS   B 1 11  ? 32.801 -28.462 -20.277 1.00 38.63 ?  11  LYS   B HD3  1 
ATOM   3838 H  HE2  . LYS   B 1 11  ? 31.666 -26.518 -20.589 1.00 41.69 ?  11  LYS   B HE2  1 
ATOM   3839 H  HE3  . LYS   B 1 11  ? 31.714 -26.736 -19.014 1.00 41.69 ?  11  LYS   B HE3  1 
ATOM   3840 H  HZ1  . LYS   B 1 11  ? 32.273 -24.594 -19.552 1.00 43.67 ?  11  LYS   B HZ1  1 
ATOM   3841 H  HZ2  . LYS   B 1 11  ? 33.413 -25.230 -18.923 1.00 43.67 ?  11  LYS   B HZ2  1 
ATOM   3842 H  HZ3  . LYS   B 1 11  ? 33.389 -25.043 -20.360 1.00 43.67 ?  11  LYS   B HZ3  1 
ATOM   3843 N  N    . LEU   B 1 12  ? 34.731 -29.809 -15.703 1.00 18.84 ?  12  LEU   B N    1 
ATOM   3844 C  CA   . LEU   B 1 12  ? 33.764 -30.516 -14.863 1.00 18.88 ?  12  LEU   B CA   1 
ATOM   3845 C  C    . LEU   B 1 12  ? 32.366 -29.913 -14.942 1.00 19.10 ?  12  LEU   B C    1 
ATOM   3846 O  O    . LEU   B 1 12  ? 31.380 -30.641 -15.108 1.00 19.66 ?  12  LEU   B O    1 
ATOM   3847 C  CB   . LEU   B 1 12  ? 34.235 -30.556 -13.404 1.00 17.81 ?  12  LEU   B CB   1 
ATOM   3848 C  CG   . LEU   B 1 12  ? 35.573 -31.246 -13.124 1.00 18.19 ?  12  LEU   B CG   1 
ATOM   3849 C  CD1  . LEU   B 1 12  ? 35.882 -31.187 -11.644 1.00 17.96 ?  12  LEU   B CD1  1 
ATOM   3850 C  CD2  . LEU   B 1 12  ? 35.563 -32.693 -13.608 1.00 19.64 ?  12  LEU   B CD2  1 
ATOM   3851 H  H    . LEU   B 1 12  ? 35.063 -29.102 -15.333 1.00 22.62 ?  12  LEU   B H    1 
ATOM   3852 H  HA   . LEU   B 1 12  ? 33.697 -31.424 -15.174 1.00 22.66 ?  12  LEU   B HA   1 
ATOM   3853 H  HB2  . LEU   B 1 12  ? 34.313 -29.643 -13.083 1.00 21.38 ?  12  LEU   B HB2  1 
ATOM   3854 H  HB3  . LEU   B 1 12  ? 33.563 -31.020 -12.884 1.00 21.38 ?  12  LEU   B HB3  1 
ATOM   3855 H  HG   . LEU   B 1 12  ? 36.279 -30.771 -13.594 1.00 21.84 ?  12  LEU   B HG   1 
ATOM   3856 H  HD11 . LEU   B 1 12  ? 36.734 -31.626 -11.481 1.00 21.56 ?  12  LEU   B HD11 1 
ATOM   3857 H  HD12 . LEU   B 1 12  ? 35.932 -30.260 -11.364 1.00 21.56 ?  12  LEU   B HD12 1 
ATOM   3858 H  HD13 . LEU   B 1 12  ? 35.179 -31.644 -11.156 1.00 21.56 ?  12  LEU   B HD13 1 
ATOM   3859 H  HD21 . LEU   B 1 12  ? 36.382 -33.126 -13.323 1.00 23.57 ?  12  LEU   B HD21 1 
ATOM   3860 H  HD22 . LEU   B 1 12  ? 34.796 -33.145 -13.225 1.00 23.57 ?  12  LEU   B HD22 1 
ATOM   3861 H  HD23 . LEU   B 1 12  ? 35.503 -32.700 -14.576 1.00 23.57 ?  12  LEU   B HD23 1 
ATOM   3862 N  N    . THR   B 1 13  ? 32.259 -28.594 -14.808 1.00 19.46 ?  13  THR   B N    1 
ATOM   3863 C  CA   . THR   B 1 13  ? 31.022 -27.858 -15.012 1.00 19.03 ?  13  THR   B CA   1 
ATOM   3864 C  C    . THR   B 1 13  ? 31.339 -26.654 -15.890 1.00 21.06 ?  13  THR   B C    1 
ATOM   3865 O  O    . THR   B 1 13  ? 32.476 -26.460 -16.326 1.00 21.85 ?  13  THR   B O    1 
ATOM   3866 C  CB   . THR   B 1 13  ? 30.417 -27.380 -13.687 1.00 19.36 ?  13  THR   B CB   1 
ATOM   3867 O  OG1  . THR   B 1 13  ? 31.274 -26.381 -13.124 1.00 18.34 ?  13  THR   B OG1  1 
ATOM   3868 C  CG2  . THR   B 1 13  ? 30.283 -28.530 -12.701 1.00 19.22 ?  13  THR   B CG2  1 
ATOM   3869 H  H    . THR   B 1 13  ? 32.917 -28.079 -14.586 1.00 23.36 ?  13  THR   B H    1 
ATOM   3870 H  HA   . THR   B 1 13  ? 30.376 -28.421 -15.461 1.00 22.85 ?  13  THR   B HA   1 
ATOM   3871 H  HB   . THR   B 1 13  ? 29.533 -27.002 -13.845 1.00 23.24 ?  13  THR   B HB   1 
ATOM   3872 H  HG1  . THR   B 1 13  ? 30.974 -25.611 -13.296 1.00 22.02 ?  13  THR   B HG1  1 
ATOM   3873 H  HG21 . THR   B 1 13  ? 29.766 -28.249 -11.928 1.00 23.07 ?  13  THR   B HG21 1 
ATOM   3874 H  HG22 . THR   B 1 13  ? 29.830 -29.278 -13.122 1.00 23.07 ?  13  THR   B HG22 1 
ATOM   3875 H  HG23 . THR   B 1 13  ? 31.159 -28.819 -12.405 1.00 23.07 ?  13  THR   B HG23 1 
ATOM   3876 N  N    A ASP   B 1 14  ? 30.321 -25.830 -16.139 0.74 22.30 ?  14  ASP   B N    1 
ATOM   3877 N  N    B ASP   B 1 14  ? 30.324 -25.819 -16.128 0.26 21.97 ?  14  ASP   B N    1 
ATOM   3878 C  CA   A ASP   B 1 14  ? 30.520 -24.660 -16.987 0.74 24.04 ?  14  ASP   B CA   1 
ATOM   3879 C  CA   B ASP   B 1 14  ? 30.510 -24.655 -16.988 0.26 22.81 ?  14  ASP   B CA   1 
ATOM   3880 C  C    A ASP   B 1 14  ? 31.618 -23.747 -16.456 0.74 21.86 ?  14  ASP   B C    1 
ATOM   3881 C  C    B ASP   B 1 14  ? 31.524 -23.665 -16.430 0.26 21.02 ?  14  ASP   B C    1 
ATOM   3882 O  O    A ASP   B 1 14  ? 32.257 -23.035 -17.240 0.74 23.81 ?  14  ASP   B O    1 
ATOM   3883 O  O    B ASP   B 1 14  ? 31.989 -22.796 -17.175 0.26 21.54 ?  14  ASP   B O    1 
ATOM   3884 C  CB   A ASP   B 1 14  ? 29.211 -23.889 -17.146 0.74 27.80 ?  14  ASP   B CB   1 
ATOM   3885 C  CB   B ASP   B 1 14  ? 29.180 -23.939 -17.222 0.26 25.28 ?  14  ASP   B CB   1 
ATOM   3886 C  CG   A ASP   B 1 14  ? 28.258 -24.547 -18.122 0.74 32.21 ?  14  ASP   B CG   1 
ATOM   3887 C  CG   B ASP   B 1 14  ? 28.280 -24.682 -18.192 0.26 27.69 ?  14  ASP   B CG   1 
ATOM   3888 O  OD1  A ASP   B 1 14  ? 28.671 -25.484 -18.842 0.74 33.36 ?  14  ASP   B OD1  1 
ATOM   3889 O  OD1  B ASP   B 1 14  ? 28.808 -25.367 -19.094 0.26 28.51 ?  14  ASP   B OD1  1 
ATOM   3890 O  OD2  A ASP   B 1 14  ? 27.086 -24.128 -18.159 0.74 34.15 -1 14  ASP   B OD2  1 
ATOM   3891 O  OD2  B ASP   B 1 14  ? 27.043 -24.587 -18.051 0.26 28.54 -1 14  ASP   B OD2  1 
ATOM   3892 H  H    A ASP   B 1 14  ? 29.522 -25.922 -15.828 0.74 26.77 ?  14  ASP   B H    1 
ATOM   3893 H  H    B ASP   B 1 14  ? 29.530 -25.903 -15.805 0.26 26.37 ?  14  ASP   B H    1 
ATOM   3894 H  HA   A ASP   B 1 14  ? 30.795 -24.955 -17.864 0.74 28.86 ?  14  ASP   B HA   1 
ATOM   3895 H  HA   B ASP   B 1 14  ? 30.837 -24.957 -17.848 0.26 27.39 ?  14  ASP   B HA   1 
ATOM   3896 H  HB2  A ASP   B 1 14  ? 28.756 -23.846 -16.292 0.74 33.37 ?  14  ASP   B HB2  1 
ATOM   3897 H  HB2  B ASP   B 1 14  ? 28.706 -23.865 -16.380 0.26 30.35 ?  14  ASP   B HB2  1 
ATOM   3898 H  HB3  A ASP   B 1 14  ? 29.404 -22.992 -17.466 0.74 33.37 ?  14  ASP   B HB3  1 
ATOM   3899 H  HB3  B ASP   B 1 14  ? 29.360 -23.049 -17.577 0.26 30.35 ?  14  ASP   B HB3  1 
ATOM   3900 N  N    . ASN   B 1 15  ? 31.864 -23.755 -15.139 1.00 19.10 ?  15  ASN   B N    1 
ATOM   3901 C  CA   . ASN   B 1 15  ? 32.836 -22.838 -14.545 1.00 16.85 ?  15  ASN   B CA   1 
ATOM   3902 C  C    . ASN   B 1 15  ? 33.936 -23.490 -13.717 1.00 15.28 ?  15  ASN   B C    1 
ATOM   3903 O  O    . ASN   B 1 15  ? 34.762 -22.762 -13.165 1.00 16.02 ?  15  ASN   B O    1 
ATOM   3904 C  CB   . ASN   B 1 15  ? 32.136 -21.776 -13.679 1.00 16.86 ?  15  ASN   B CB   1 
ATOM   3905 C  CG   . ASN   B 1 15  ? 31.490 -22.370 -12.449 1.00 15.83 ?  15  ASN   B CG   1 
ATOM   3906 O  OD1  . ASN   B 1 15  ? 30.534 -23.160 -12.542 1.00 18.18 ?  15  ASN   B OD1  1 
ATOM   3907 N  ND2  . ASN   B 1 15  ? 32.004 -22.012 -11.287 1.00 15.34 ?  15  ASN   B ND2  1 
ATOM   3908 H  H    A ASN   B 1 15  ? 31.476 -24.278 -14.575 0.74 22.93 ?  15  ASN   B H    1 
ATOM   3909 H  H    B ASN   B 1 15  ? 31.523 -24.320 -14.585 0.26 22.93 ?  15  ASN   B H    1 
ATOM   3910 H  HA   . ASN   B 1 15  ? 33.278 -22.361 -15.257 1.00 20.23 ?  15  ASN   B HA   1 
ATOM   3911 H  HB2  . ASN   B 1 15  ? 32.800 -21.114 -13.394 1.00 20.24 ?  15  ASN   B HB2  1 
ATOM   3912 H  HB3  . ASN   B 1 15  ? 31.449 -21.333 -14.203 1.00 20.24 ?  15  ASN   B HB3  1 
ATOM   3913 H  HD21 . ASN   B 1 15  ? 31.669 -22.319 -10.556 1.00 18.42 ?  15  ASN   B HD21 1 
ATOM   3914 H  HD22 . ASN   B 1 15  ? 32.675 -21.467 -11.248 1.00 18.42 ?  15  ASN   B HD22 1 
ATOM   3915 N  N    . VAL   B 1 16  ? 33.963 -24.815 -13.588 1.00 15.06 ?  16  VAL   B N    1 
ATOM   3916 C  CA   . VAL   B 1 16  ? 34.959 -25.508 -12.772 1.00 14.53 ?  16  VAL   B CA   1 
ATOM   3917 C  C    . VAL   B 1 16  ? 35.751 -26.450 -13.665 1.00 14.97 ?  16  VAL   B C    1 
ATOM   3918 O  O    . VAL   B 1 16  ? 35.167 -27.315 -14.338 1.00 16.14 ?  16  VAL   B O    1 
ATOM   3919 C  CB   . VAL   B 1 16  ? 34.324 -26.276 -11.596 1.00 15.06 ?  16  VAL   B CB   1 
ATOM   3920 C  CG1  . VAL   B 1 16  ? 35.390 -26.990 -10.774 1.00 15.09 ?  16  VAL   B CG1  1 
ATOM   3921 C  CG2  . VAL   B 1 16  ? 33.501 -25.336 -10.716 1.00 15.85 ?  16  VAL   B CG2  1 
ATOM   3922 H  H    . VAL   B 1 16  ? 33.397 -25.347 -13.961 1.00 18.07 ?  16  VAL   B H    1 
ATOM   3923 H  HA   . VAL   B 1 16  ? 35.574 -24.854 -12.401 1.00 17.44 ?  16  VAL   B HA   1 
ATOM   3924 H  HB   . VAL   B 1 16  ? 33.726 -26.951 -11.955 1.00 18.08 ?  16  VAL   B HB   1 
ATOM   3925 H  HG11 . VAL   B 1 16  ? 34.988 -27.319 -9.953  1.00 18.11 ?  16  VAL   B HG11 1 
ATOM   3926 H  HG12 . VAL   B 1 16  ? 35.750 -27.730 -11.284 1.00 18.11 ?  16  VAL   B HG12 1 
ATOM   3927 H  HG13 . VAL   B 1 16  ? 36.099 -26.359 -10.559 1.00 18.11 ?  16  VAL   B HG13 1 
ATOM   3928 H  HG21 . VAL   B 1 16  ? 33.154 -25.839 -9.962  1.00 19.03 ?  16  VAL   B HG21 1 
ATOM   3929 H  HG22 . VAL   B 1 16  ? 34.067 -24.617 -10.408 1.00 19.03 ?  16  VAL   B HG22 1 
ATOM   3930 H  HG23 . VAL   B 1 16  ? 32.764 -24.981 -11.241 1.00 19.03 ?  16  VAL   B HG23 1 
ATOM   3931 N  N    . TYR   B 1 17  ? 37.077 -26.296 -13.630 1.00 15.15 ?  17  TYR   B N    1 
ATOM   3932 C  CA   . TYR   B 1 17  ? 38.019 -27.045 -14.447 1.00 15.59 ?  17  TYR   B CA   1 
ATOM   3933 C  C    . TYR   B 1 17  ? 39.072 -27.650 -13.528 1.00 14.73 ?  17  TYR   B C    1 
ATOM   3934 O  O    . TYR   B 1 17  ? 39.344 -27.120 -12.447 1.00 15.60 ?  17  TYR   B O    1 
ATOM   3935 C  CB   . TYR   B 1 17  ? 38.731 -26.122 -15.450 1.00 17.74 ?  17  TYR   B CB   1 
ATOM   3936 C  CG   . TYR   B 1 17  ? 37.806 -25.350 -16.355 1.00 20.97 ?  17  TYR   B CG   1 
ATOM   3937 C  CD1  . TYR   B 1 17  ? 37.213 -24.165 -15.935 1.00 22.19 ?  17  TYR   B CD1  1 
ATOM   3938 C  CD2  . TYR   B 1 17  ? 37.527 -25.802 -17.637 1.00 23.39 ?  17  TYR   B CD2  1 
ATOM   3939 C  CE1  . TYR   B 1 17  ? 36.361 -23.457 -16.766 1.00 24.00 ?  17  TYR   B CE1  1 
ATOM   3940 C  CE2  . TYR   B 1 17  ? 36.682 -25.100 -18.477 1.00 24.64 ?  17  TYR   B CE2  1 
ATOM   3941 C  CZ   . TYR   B 1 17  ? 36.100 -23.932 -18.036 1.00 25.15 ?  17  TYR   B CZ   1 
ATOM   3942 O  OH   . TYR   B 1 17  ? 35.261 -23.233 -18.874 1.00 26.57 ?  17  TYR   B OH   1 
ATOM   3943 H  H    . TYR   B 1 17  ? 37.478 -25.734 -13.103 1.00 18.19 ?  17  TYR   B H    1 
ATOM   3944 H  HA   . TYR   B 1 17  ? 37.556 -27.751 -14.928 1.00 18.72 ?  17  TYR   B HA   1 
ATOM   3945 H  HB2  . TYR   B 1 17  ? 39.274 -25.483 -14.962 1.00 21.29 ?  17  TYR   B HB2  1 
ATOM   3946 H  HB3  . TYR   B 1 17  ? 39.296 -26.666 -16.018 1.00 21.29 ?  17  TYR   B HB3  1 
ATOM   3947 H  HD1  . TYR   B 1 17  ? 37.385 -23.844 -15.081 1.00 26.64 ?  17  TYR   B HD1  1 
ATOM   3948 H  HD2  . TYR   B 1 17  ? 37.912 -26.591 -17.939 1.00 28.08 ?  17  TYR   B HD2  1 
ATOM   3949 H  HE1  . TYR   B 1 17  ? 35.967 -22.664 -16.473 1.00 28.81 ?  17  TYR   B HE1  1 
ATOM   3950 H  HE2  . TYR   B 1 17  ? 36.497 -25.417 -19.334 1.00 29.58 ?  17  TYR   B HE2  1 
ATOM   3951 H  HH   . TYR   B 1 17  ? 35.181 -23.630 -19.610 1.00 31.89 ?  17  TYR   B HH   1 
ATOM   3952 N  N    . ILE   B 1 18  ? 39.701 -28.749 -13.964 1.00 14.94 ?  18  ILE   B N    1 
ATOM   3953 C  CA   . ILE   B 1 18  ? 40.636 -29.462 -13.098 1.00 14.60 ?  18  ILE   B CA   1 
ATOM   3954 C  C    . ILE   B 1 18  ? 41.804 -30.020 -13.906 1.00 14.83 ?  18  ILE   B C    1 
ATOM   3955 O  O    . ILE   B 1 18  ? 41.650 -30.435 -15.058 1.00 16.12 ?  18  ILE   B O    1 
ATOM   3956 C  CB   . ILE   B 1 18  ? 39.884 -30.562 -12.300 1.00 14.98 ?  18  ILE   B CB   1 
ATOM   3957 C  CG1  . ILE   B 1 18  ? 40.739 -31.113 -11.155 1.00 15.56 ?  18  ILE   B CG1  1 
ATOM   3958 C  CG2  . ILE   B 1 18  ? 39.380 -31.683 -13.223 1.00 15.33 ?  18  ILE   B CG2  1 
ATOM   3959 C  CD1  . ILE   B 1 18  ? 39.933 -31.954 -10.150 1.00 16.79 ?  18  ILE   B CD1  1 
ATOM   3960 H  H    . ILE   B 1 18  ? 39.610 -29.095 -14.749 1.00 17.94 ?  18  ILE   B H    1 
ATOM   3961 H  HA   . ILE   B 1 18  ? 41.000 -28.836 -12.454 1.00 17.53 ?  18  ILE   B HA   1 
ATOM   3962 H  HB   . ILE   B 1 18  ? 39.105 -30.150 -11.896 1.00 17.98 ?  18  ILE   B HB   1 
ATOM   3963 H  HG12 . ILE   B 1 18  ? 41.435 -31.678 -11.523 1.00 18.68 ?  18  ILE   B HG12 1 
ATOM   3964 H  HG13 . ILE   B 1 18  ? 41.136 -30.372 -10.671 1.00 18.68 ?  18  ILE   B HG13 1 
ATOM   3965 H  HG21 . ILE   B 1 18  ? 38.797 -32.273 -12.717 1.00 18.40 ?  18  ILE   B HG21 1 
ATOM   3966 H  HG22 . ILE   B 1 18  ? 38.893 -31.289 -13.959 1.00 18.40 ?  18  ILE   B HG22 1 
ATOM   3967 H  HG23 . ILE   B 1 18  ? 40.142 -32.185 -13.558 1.00 18.40 ?  18  ILE   B HG23 1 
ATOM   3968 H  HD11 . ILE   B 1 18  ? 40.516 -32.223 -9.422  1.00 20.15 ?  18  ILE   B HD11 1 
ATOM   3969 H  HD12 . ILE   B 1 18  ? 39.201 -31.417 -9.805  1.00 20.15 ?  18  ILE   B HD12 1 
ATOM   3970 H  HD13 . ILE   B 1 18  ? 39.583 -32.738 -10.601 1.00 20.15 ?  18  ILE   B HD13 1 
ATOM   3971 N  N    . LYS   B 1 19  ? 42.983 -30.041 -13.280 1.00 15.79 ?  19  LYS   B N    1 
ATOM   3972 C  CA   . LYS   B 1 19  ? 44.193 -30.520 -13.929 1.00 16.07 ?  19  LYS   B CA   1 
ATOM   3973 C  C    . LYS   B 1 19  ? 45.076 -31.208 -12.898 1.00 16.09 ?  19  LYS   B C    1 
ATOM   3974 O  O    . LYS   B 1 19  ? 45.145 -30.788 -11.741 1.00 15.65 ?  19  LYS   B O    1 
ATOM   3975 C  CB   . LYS   B 1 19  ? 44.970 -29.356 -14.566 1.00 17.12 ?  19  LYS   B CB   1 
ATOM   3976 C  CG   . LYS   B 1 19  ? 46.180 -29.767 -15.387 1.00 19.11 ?  19  LYS   B CG   1 
ATOM   3977 C  CD   . LYS   B 1 19  ? 46.901 -28.530 -15.918 1.00 21.24 ?  19  LYS   B CD   1 
ATOM   3978 C  CE   . LYS   B 1 19  ? 48.055 -28.902 -16.827 1.00 23.52 ?  19  LYS   B CE   1 
ATOM   3979 N  NZ   . LYS   B 1 19  ? 48.833 -27.712 -17.275 1.00 25.62 ?  19  LYS   B NZ   1 
ATOM   3980 H  H    . LYS   B 1 19  ? 43.101 -29.775 -12.471 1.00 18.96 ?  19  LYS   B H    1 
ATOM   3981 H  HA   . LYS   B 1 19  ? 43.961 -31.161 -14.622 1.00 19.29 ?  19  LYS   B HA   1 
ATOM   3982 H  HB2  . LYS   B 1 19  ? 44.369 -28.872 -15.155 1.00 20.55 ?  19  LYS   B HB2  1 
ATOM   3983 H  HB3  . LYS   B 1 19  ? 45.277 -28.766 -13.859 1.00 20.55 ?  19  LYS   B HB3  1 
ATOM   3984 H  HG2  . LYS   B 1 19  ? 46.794 -30.270 -14.831 1.00 22.94 ?  19  LYS   B HG2  1 
ATOM   3985 H  HG3  . LYS   B 1 19  ? 45.889 -30.304 -16.143 1.00 22.94 ?  19  LYS   B HG3  1 
ATOM   3986 H  HD2  . LYS   B 1 19  ? 46.275 -27.987 -16.424 1.00 25.49 ?  19  LYS   B HD2  1 
ATOM   3987 H  HD3  . LYS   B 1 19  ? 47.253 -28.021 -15.169 1.00 25.49 ?  19  LYS   B HD3  1 
ATOM   3988 H  HE2  . LYS   B 1 19  ? 48.656 -29.496 -16.348 1.00 28.23 ?  19  LYS   B HE2  1 
ATOM   3989 H  HE3  . LYS   B 1 19  ? 47.705 -29.351 -17.614 1.00 28.23 ?  19  LYS   B HE3  1 
ATOM   3990 H  HZ1  . LYS   B 1 19  ? 49.451 -27.960 -17.866 1.00 30.75 ?  19  LYS   B HZ1  1 
ATOM   3991 H  HZ2  . LYS   B 1 19  ? 48.288 -27.122 -17.658 1.00 30.75 ?  19  LYS   B HZ2  1 
ATOM   3992 H  HZ3  . LYS   B 1 19  ? 49.232 -27.332 -16.579 1.00 30.75 ?  19  LYS   B HZ3  1 
ATOM   3993 N  N    . ASN   B 1 20  ? 45.775 -32.253 -13.333 1.00 17.57 ?  20  ASN   B N    1 
ATOM   3994 C  CA   . ASN   B 1 20  ? 46.796 -32.893 -12.506 1.00 18.37 ?  20  ASN   B CA   1 
ATOM   3995 C  C    . ASN   B 1 20  ? 48.070 -32.080 -12.684 1.00 19.02 ?  20  ASN   B C    1 
ATOM   3996 O  O    . ASN   B 1 20  ? 48.722 -32.155 -13.730 1.00 21.33 ?  20  ASN   B O    1 
ATOM   3997 C  CB   . ASN   B 1 20  ? 46.978 -34.339 -12.956 1.00 20.21 ?  20  ASN   B CB   1 
ATOM   3998 C  CG   . ASN   B 1 20  ? 48.133 -35.062 -12.256 1.00 20.94 ?  20  ASN   B CG   1 
ATOM   3999 O  OD1  . ASN   B 1 20  ? 48.772 -35.945 -12.846 1.00 23.73 ?  20  ASN   B OD1  1 
ATOM   4000 N  ND2  . ASN   B 1 20  ? 48.396 -34.708 -11.005 1.00 19.97 ?  20  ASN   B ND2  1 
ATOM   4001 H  H    . ASN   B 1 20  ? 45.678 -32.611 -14.109 1.00 21.10 ?  20  ASN   B H    1 
ATOM   4002 H  HA   . ASN   B 1 20  ? 46.516 -32.871 -11.576 1.00 22.05 ?  20  ASN   B HA   1 
ATOM   4003 H  HB2  . ASN   B 1 20  ? 46.161 -34.827 -12.765 1.00 24.26 ?  20  ASN   B HB2  1 
ATOM   4004 H  HB3  . ASN   B 1 20  ? 47.151 -34.344 -13.909 1.00 24.26 ?  20  ASN   B HB3  1 
ATOM   4005 H  HD21 . ASN   B 1 20  ? 49.040 -35.083 -10.582 1.00 23.97 ?  20  ASN   B HD21 1 
ATOM   4006 H  HD22 . ASN   B 1 20  ? 47.930 -34.093 -10.615 1.00 23.97 ?  20  ASN   B HD22 1 
ATOM   4007 N  N    . ALA   B 1 21  ? 48.422 -31.282 -11.673 1.00 18.50 ?  21  ALA   B N    1 
ATOM   4008 C  CA   . ALA   B 1 21  ? 49.523 -30.343 -11.824 1.00 19.42 ?  21  ALA   B CA   1 
ATOM   4009 C  C    . ALA   B 1 21  ? 49.990 -29.854 -10.462 1.00 18.31 ?  21  ALA   B C    1 
ATOM   4010 O  O    . ALA   B 1 21  ? 49.250 -29.885 -9.475  1.00 18.09 ?  21  ALA   B O    1 
ATOM   4011 C  CB   . ALA   B 1 21  ? 49.117 -29.155 -12.698 1.00 21.41 ?  21  ALA   B CB   1 
ATOM   4012 H  H    . ALA   B 1 21  ? 48.037 -31.259 -10.895 1.00 22.21 ?  21  ALA   B H    1 
ATOM   4013 H  HA   . ALA   B 1 21  ? 50.263 -30.797 -12.252 1.00 23.32 ?  21  ALA   B HA   1 
ATOM   4014 H  HB1  . ALA   B 1 21  ? 49.896 -28.602 -12.845 1.00 25.70 ?  21  ALA   B HB1  1 
ATOM   4015 H  HB2  . ALA   B 1 21  ? 48.783 -29.493 -13.543 1.00 25.70 ?  21  ALA   B HB2  1 
ATOM   4016 H  HB3  . ALA   B 1 21  ? 48.424 -28.652 -12.244 1.00 25.70 ?  21  ALA   B HB3  1 
ATOM   4017 N  N    . ASP   B 1 22  ? 51.244 -29.395 -10.447 1.00 17.19 ?  22  ASP   B N    1 
ATOM   4018 C  CA   . ASP   B 1 22  ? 51.860 -28.692 -9.325  1.00 16.87 ?  22  ASP   B CA   1 
ATOM   4019 C  C    . ASP   B 1 22  ? 51.445 -27.226 -9.408  1.00 14.71 ?  22  ASP   B C    1 
ATOM   4020 O  O    . ASP   B 1 22  ? 51.755 -26.554 -10.396 1.00 15.44 ?  22  ASP   B O    1 
ATOM   4021 C  CB   . ASP   B 1 22  ? 53.379 -28.860 -9.478  1.00 17.99 ?  22  ASP   B CB   1 
ATOM   4022 C  CG   . ASP   B 1 22  ? 54.198 -28.101 -8.444  1.00 19.84 ?  22  ASP   B CG   1 
ATOM   4023 O  OD1  . ASP   B 1 22  ? 53.839 -26.977 -8.053  1.00 20.37 ?  22  ASP   B OD1  1 
ATOM   4024 O  OD2  . ASP   B 1 22  ? 55.264 -28.623 -8.052  1.00 23.07 -1 22  ASP   B OD2  1 
ATOM   4025 H  H    . ASP   B 1 22  ? 51.785 -29.481 -11.117 1.00 20.63 ?  22  ASP   B H    1 
ATOM   4026 H  HA   . ASP   B 1 22  ? 51.571 -29.076 -8.480  1.00 20.26 ?  22  ASP   B HA   1 
ATOM   4027 H  HB2  . ASP   B 1 22  ? 53.605 -29.795 -9.401  1.00 21.59 ?  22  ASP   B HB2  1 
ATOM   4028 H  HB3  . ASP   B 1 22  ? 53.642 -28.523 -10.349 1.00 21.59 ?  22  ASP   B HB3  1 
ATOM   4029 N  N    . ILE   B 1 23  ? 50.730 -26.735 -8.386  1.00 15.09 ?  23  ILE   B N    1 
ATOM   4030 C  CA   . ILE   B 1 23  ? 50.135 -25.399 -8.462  1.00 14.85 ?  23  ILE   B CA   1 
ATOM   4031 C  C    . ILE   B 1 23  ? 51.189 -24.309 -8.608  1.00 14.00 ?  23  ILE   B C    1 
ATOM   4032 O  O    . ILE   B 1 23  ? 50.926 -23.264 -9.218  1.00 13.87 ?  23  ILE   B O    1 
ATOM   4033 C  CB   . ILE   B 1 23  ? 49.197 -25.152 -7.263  1.00 15.55 ?  23  ILE   B CB   1 
ATOM   4034 C  CG1  . ILE   B 1 23  ? 48.364 -23.888 -7.481  1.00 16.32 ?  23  ILE   B CG1  1 
ATOM   4035 C  CG2  . ILE   B 1 23  ? 49.967 -25.082 -5.962  1.00 16.76 ?  23  ILE   B CG2  1 
ATOM   4036 C  CD1  . ILE   B 1 23  ? 47.247 -23.703 -6.457  1.00 17.07 ?  23  ILE   B CD1  1 
ATOM   4037 H  H    . ILE   B 1 23  ? 50.578 -27.152 -7.648  1.00 18.12 ?  23  ILE   B H    1 
ATOM   4038 H  HA   . ILE   B 1 23  ? 49.585 -25.364 -9.258  1.00 17.83 ?  23  ILE   B HA   1 
ATOM   4039 H  HB   . ILE   B 1 23  ? 48.588 -25.901 -7.206  1.00 18.67 ?  23  ILE   B HB   1 
ATOM   4040 H  HG12 . ILE   B 1 23  ? 48.950 -23.113 -7.427  1.00 19.59 ?  23  ILE   B HG12 1 
ATOM   4041 H  HG13 . ILE   B 1 23  ? 47.960 -23.928 -8.364  1.00 19.59 ?  23  ILE   B HG13 1 
ATOM   4042 H  HG21 . ILE   B 1 23  ? 49.340 -25.087 -5.224  1.00 20.13 ?  23  ILE   B HG21 1 
ATOM   4043 H  HG22 . ILE   B 1 23  ? 50.556 -25.850 -5.903  1.00 20.13 ?  23  ILE   B HG22 1 
ATOM   4044 H  HG23 . ILE   B 1 23  ? 50.490 -24.264 -5.947  1.00 20.13 ?  23  ILE   B HG23 1 
ATOM   4045 H  HD11 . ILE   B 1 23  ? 46.718 -22.930 -6.705  1.00 20.49 ?  23  ILE   B HD11 1 
ATOM   4046 H  HD12 . ILE   B 1 23  ? 46.692 -24.499 -6.455  1.00 20.49 ?  23  ILE   B HD12 1 
ATOM   4047 H  HD13 . ILE   B 1 23  ? 47.641 -23.571 -5.582  1.00 20.49 ?  23  ILE   B HD13 1 
ATOM   4048 N  N    . VAL   B 1 24  ? 52.380 -24.513 -8.047  1.00 14.26 ?  24  VAL   B N    1 
ATOM   4049 C  CA   . VAL   B 1 24  ? 53.452 -23.530 -8.209  1.00 15.48 ?  24  VAL   B CA   1 
ATOM   4050 C  C    . VAL   B 1 24  ? 53.912 -23.485 -9.660  1.00 16.32 ?  24  VAL   B C    1 
ATOM   4051 O  O    . VAL   B 1 24  ? 54.062 -22.409 -10.254 1.00 16.26 ?  24  VAL   B O    1 
ATOM   4052 C  CB   . VAL   B 1 24  ? 54.625 -23.842 -7.259  1.00 15.73 ?  24  VAL   B CB   1 
ATOM   4053 C  CG1  . VAL   B 1 24  ? 55.830 -22.938 -7.574  1.00 17.77 ?  24  VAL   B CG1  1 
ATOM   4054 C  CG2  . VAL   B 1 24  ? 54.198 -23.659 -5.828  1.00 16.77 ?  24  VAL   B CG2  1 
ATOM   4055 H  H    . VAL   B 1 24  ? 52.592 -25.201 -7.577  1.00 17.13 ?  24  VAL   B H    1 
ATOM   4056 H  HA   . VAL   B 1 24  ? 53.110 -22.654 -7.978  1.00 18.58 ?  24  VAL   B HA   1 
ATOM   4057 H  HB   . VAL   B 1 24  ? 54.897 -24.768 -7.375  1.00 18.88 ?  24  VAL   B HB   1 
ATOM   4058 H  HG11 . VAL   B 1 24  ? 56.425 -22.931 -6.808  1.00 21.33 ?  24  VAL   B HG11 1 
ATOM   4059 H  HG12 . VAL   B 1 24  ? 56.293 -23.289 -8.349  1.00 21.33 ?  24  VAL   B HG12 1 
ATOM   4060 H  HG13 . VAL   B 1 24  ? 55.510 -22.039 -7.752  1.00 21.33 ?  24  VAL   B HG13 1 
ATOM   4061 H  HG21 . VAL   B 1 24  ? 54.905 -23.970 -5.244  1.00 20.13 ?  24  VAL   B HG21 1 
ATOM   4062 H  HG22 . VAL   B 1 24  ? 54.030 -22.716 -5.672  1.00 20.13 ?  24  VAL   B HG22 1 
ATOM   4063 H  HG23 . VAL   B 1 24  ? 53.388 -24.170 -5.669  1.00 20.13 ?  24  VAL   B HG23 1 
ATOM   4064 N  N    . GLU   B 1 25  ? 54.179 -24.657 -10.242 1.00 17.40 ?  25  GLU   B N    1 
ATOM   4065 C  CA   . GLU   B 1 25  ? 54.566 -24.694 -11.645 1.00 18.29 ?  25  GLU   B CA   1 
ATOM   4066 C  C    . GLU   B 1 25  ? 53.458 -24.145 -12.532 1.00 16.65 ?  25  GLU   B C    1 
ATOM   4067 O  O    . GLU   B 1 25  ? 53.729 -23.425 -13.502 1.00 17.76 ?  25  GLU   B O    1 
ATOM   4068 C  CB   . GLU   B 1 25  ? 54.971 -26.116 -12.037 1.00 22.23 ?  25  GLU   B CB   1 
ATOM   4069 C  CG   . GLU   B 1 25  ? 56.285 -26.549 -11.394 1.00 27.61 ?  25  GLU   B CG   1 
ATOM   4070 C  CD   . GLU   B 1 25  ? 57.384 -25.493 -11.497 1.00 33.28 ?  25  GLU   B CD   1 
ATOM   4071 O  OE1  . GLU   B 1 25  ? 57.762 -25.123 -12.630 1.00 35.14 ?  25  GLU   B OE1  1 
ATOM   4072 O  OE2  . GLU   B 1 25  ? 57.860 -25.012 -10.440 1.00 35.27 -1 25  GLU   B OE2  1 
ATOM   4073 H  H    . GLU   B 1 25  ? 54.144 -25.423 -9.853  1.00 20.89 ?  25  GLU   B H    1 
ATOM   4074 H  HA   . GLU   B 1 25  ? 55.327 -24.107 -11.768 1.00 21.96 ?  25  GLU   B HA   1 
ATOM   4075 H  HB2  . GLU   B 1 25  ? 54.278 -26.734 -11.747 1.00 26.69 ?  25  GLU   B HB2  1 
ATOM   4076 H  HB3  . GLU   B 1 25  ? 55.072 -26.163 -13.000 1.00 26.69 ?  25  GLU   B HB3  1 
ATOM   4077 H  HG2  . GLU   B 1 25  ? 56.141 -26.706 -10.454 1.00 33.14 ?  25  GLU   B HG2  1 
ATOM   4078 H  HG3  . GLU   B 1 25  ? 56.595 -27.358 -11.831 1.00 33.14 ?  25  GLU   B HG3  1 
ATOM   4079 N  N    . GLU   B 1 26  ? 52.203 -24.451 -12.197 1.00 15.65 ?  26  GLU   B N    1 
ATOM   4080 C  CA   . GLU   B 1 26  ? 51.082 -23.924 -12.967 1.00 16.18 ?  26  GLU   B CA   1 
ATOM   4081 C  C    . GLU   B 1 26  ? 51.031 -22.404 -12.891 1.00 15.53 ?  26  GLU   B C    1 
ATOM   4082 O  O    . GLU   B 1 26  ? 50.822 -21.731 -13.905 1.00 16.80 ?  26  GLU   B O    1 
ATOM   4083 C  CB   . GLU   B 1 26  ? 49.764 -24.515 -12.463 1.00 18.70 ?  26  GLU   B CB   1 
ATOM   4084 C  CG   . GLU   B 1 26  ? 49.362 -25.807 -13.124 1.00 22.48 ?  26  GLU   B CG   1 
ATOM   4085 C  CD   . GLU   B 1 26  ? 49.108 -25.656 -14.623 1.00 23.93 ?  26  GLU   B CD   1 
ATOM   4086 O  OE1  . GLU   B 1 26  ? 48.130 -24.986 -15.035 1.00 24.19 ?  26  GLU   B OE1  1 
ATOM   4087 O  OE2  . GLU   B 1 26  ? 49.882 -26.237 -15.386 1.00 26.65 -1 26  GLU   B OE2  1 
ATOM   4088 H  H    . GLU   B 1 26  ? 51.980 -24.961 -11.537 1.00 18.79 ?  26  GLU   B H    1 
ATOM   4089 H  HA   . GLU   B 1 26  ? 51.197 -24.175 -13.894 1.00 19.43 ?  26  GLU   B HA   1 
ATOM   4090 H  HB2  . GLU   B 1 26  ? 49.840 -24.683 -11.510 1.00 22.45 ?  26  GLU   B HB2  1 
ATOM   4091 H  HB3  . GLU   B 1 26  ? 49.055 -23.873 -12.624 1.00 22.45 ?  26  GLU   B HB3  1 
ATOM   4092 H  HG2  . GLU   B 1 26  ? 50.072 -26.455 -12.982 1.00 26.98 ?  26  GLU   B HG2  1 
ATOM   4093 H  HG3  . GLU   B 1 26  ? 48.539 -26.126 -12.726 1.00 26.98 ?  26  GLU   B HG3  1 
ATOM   4094 N  N    . ALA   B 1 27  ? 51.183 -21.844 -11.686 1.00 14.90 ?  27  ALA   B N    1 
ATOM   4095 C  CA   . ALA   B 1 27  ? 51.140 -20.392 -11.543 1.00 15.27 ?  27  ALA   B CA   1 
ATOM   4096 C  C    . ALA   B 1 27  ? 52.210 -19.725 -12.394 1.00 15.79 ?  27  ALA   B C    1 
ATOM   4097 O  O    . ALA   B 1 27  ? 51.949 -18.720 -13.064 1.00 16.61 ?  27  ALA   B O    1 
ATOM   4098 C  CB   . ALA   B 1 27  ? 51.283 -20.002 -10.073 1.00 15.55 ?  27  ALA   B CB   1 
ATOM   4099 H  H    . ALA   B 1 27  ? 51.296 -22.280 -10.950 1.00 17.89 ?  27  ALA   B H    1 
ATOM   4100 H  HA   . ALA   B 1 27  ? 50.279 -20.074 -11.849 1.00 18.34 ?  27  ALA   B HA   1 
ATOM   4101 H  HB1  . ALA   B 1 27  ? 51.246 -19.035 -10.000 1.00 18.67 ?  27  ALA   B HB1  1 
ATOM   4102 H  HB2  . ALA   B 1 27  ? 50.551 -20.397 -9.570  1.00 18.67 ?  27  ALA   B HB2  1 
ATOM   4103 H  HB3  . ALA   B 1 27  ? 52.129 -20.329 -9.738  1.00 18.67 ?  27  ALA   B HB3  1 
ATOM   4104 N  N    . LYS   B 1 28  ? 53.424 -20.279 -12.393 1.00 17.98 ?  28  LYS   B N    1 
ATOM   4105 C  CA   . LYS   B 1 28  ? 54.499 -19.660 -13.160 1.00 19.78 ?  28  LYS   B CA   1 
ATOM   4106 C  C    . LYS   B 1 28  ? 54.242 -19.736 -14.661 1.00 21.09 ?  28  LYS   B C    1 
ATOM   4107 O  O    . LYS   B 1 28  ? 54.672 -18.846 -15.406 1.00 23.19 ?  28  LYS   B O    1 
ATOM   4108 C  CB   . LYS   B 1 28  ? 55.854 -20.265 -12.774 1.00 23.21 ?  28  LYS   B CB   1 
ATOM   4109 C  CG   . LYS   B 1 28  ? 56.293 -19.889 -11.356 1.00 26.68 ?  28  LYS   B CG   1 
ATOM   4110 C  CD   . LYS   B 1 28  ? 57.723 -20.312 -11.029 1.00 31.28 ?  28  LYS   B CD   1 
ATOM   4111 C  CE   . LYS   B 1 28  ? 57.797 -21.762 -10.621 1.00 34.70 ?  28  LYS   B CE   1 
ATOM   4112 N  NZ   . LYS   B 1 28  ? 59.141 -22.103 -10.070 1.00 37.11 ?  28  LYS   B NZ   1 
ATOM   4113 H  H    . LYS   B 1 28  ? 53.647 -20.989 -11.963 1.00 21.59 ?  28  LYS   B H    1 
ATOM   4114 H  HA   . LYS   B 1 28  ? 54.534 -18.718 -12.931 1.00 23.75 ?  28  LYS   B HA   1 
ATOM   4115 H  HB2  . LYS   B 1 28  ? 55.796 -21.230 -12.821 1.00 27.86 ?  28  LYS   B HB2  1 
ATOM   4116 H  HB3  . LYS   B 1 28  ? 56.532 -19.942 -13.390 1.00 27.86 ?  28  LYS   B HB3  1 
ATOM   4117 H  HG2  . LYS   B 1 28  ? 56.235 -18.925 -11.259 1.00 32.03 ?  28  LYS   B HG2  1 
ATOM   4118 H  HG3  . LYS   B 1 28  ? 55.700 -20.321 -10.724 1.00 32.03 ?  28  LYS   B HG3  1 
ATOM   4119 H  HD2  . LYS   B 1 28  ? 58.279 -20.183 -11.814 1.00 37.55 ?  28  LYS   B HD2  1 
ATOM   4120 H  HD3  . LYS   B 1 28  ? 58.051 -19.768 -10.294 1.00 37.55 ?  28  LYS   B HD3  1 
ATOM   4121 H  HE2  . LYS   B 1 28  ? 57.133 -21.936 -9.935  1.00 41.65 ?  28  LYS   B HE2  1 
ATOM   4122 H  HE3  . LYS   B 1 28  ? 57.633 -22.322 -11.396 1.00 41.65 ?  28  LYS   B HE3  1 
ATOM   4123 H  HZ1  . LYS   B 1 28  ? 59.165 -22.961 -9.836  1.00 44.54 ?  28  LYS   B HZ1  1 
ATOM   4124 H  HZ2  . LYS   B 1 28  ? 59.768 -21.953 -10.684 1.00 44.54 ?  28  LYS   B HZ2  1 
ATOM   4125 H  HZ3  . LYS   B 1 28  ? 59.312 -21.603 -9.354  1.00 44.54 ?  28  LYS   B HZ3  1 
ATOM   4126 N  N    A LYS   B 1 29  ? 53.543 -20.771 -15.122 0.74 21.53 ?  29  LYS   B N    1 
ATOM   4127 N  N    B LYS   B 1 29  ? 53.532 -20.767 -15.121 0.26 22.20 ?  29  LYS   B N    1 
ATOM   4128 C  CA   A LYS   B 1 29  ? 53.252 -20.917 -16.544 0.74 23.75 ?  29  LYS   B CA   1 
ATOM   4129 C  CA   B LYS   B 1 29  ? 53.248 -20.919 -16.544 0.26 23.76 ?  29  LYS   B CA   1 
ATOM   4130 C  C    A LYS   B 1 29  ? 51.986 -20.178 -16.969 0.74 23.22 ?  29  LYS   B C    1 
ATOM   4131 C  C    B LYS   B 1 29  ? 51.977 -20.195 -16.977 0.26 22.99 ?  29  LYS   B C    1 
ATOM   4132 O  O    A LYS   B 1 29  ? 51.962 -19.572 -18.045 0.74 24.86 ?  29  LYS   B O    1 
ATOM   4133 O  O    B LYS   B 1 29  ? 51.941 -19.609 -18.065 0.26 23.58 ?  29  LYS   B O    1 
ATOM   4134 C  CB   A LYS   B 1 29  ? 53.126 -22.399 -16.902 0.74 27.85 ?  29  LYS   B CB   1 
ATOM   4135 C  CB   B LYS   B 1 29  ? 53.146 -22.403 -16.905 0.26 26.53 ?  29  LYS   B CB   1 
ATOM   4136 C  CG   A LYS   B 1 29  ? 52.943 -22.661 -18.384 0.74 31.77 ?  29  LYS   B CG   1 
ATOM   4137 C  CG   B LYS   B 1 29  ? 53.019 -22.669 -18.397 0.26 29.07 ?  29  LYS   B CG   1 
ATOM   4138 C  CD   A LYS   B 1 29  ? 53.158 -24.130 -18.719 0.74 34.88 ?  29  LYS   B CD   1 
ATOM   4139 C  CD   B LYS   B 1 29  ? 53.277 -24.132 -18.722 0.26 31.08 ?  29  LYS   B CD   1 
ATOM   4140 C  CE   A LYS   B 1 29  ? 52.046 -25.006 -18.165 0.74 36.86 ?  29  LYS   B CE   1 
ATOM   4141 C  CE   B LYS   B 1 29  ? 52.222 -25.042 -18.114 0.26 32.49 ?  29  LYS   B CE   1 
ATOM   4142 N  NZ   A LYS   B 1 29  ? 52.267 -26.445 -18.489 0.74 37.97 ?  29  LYS   B NZ   1 
ATOM   4143 N  NZ   B LYS   B 1 29  ? 52.477 -26.474 -18.434 0.26 33.29 ?  29  LYS   B NZ   1 
ATOM   4144 H  H    A LYS   B 1 29  ? 53.219 -21.403 -14.628 0.74 25.84 ?  29  LYS   B H    1 
ATOM   4145 H  H    B LYS   B 1 29  ? 53.208 -21.395 -14.625 0.26 26.64 ?  29  LYS   B H    1 
ATOM   4146 H  HA   A LYS   B 1 29  ? 53.993 -20.552 -17.048 0.74 28.51 ?  29  LYS   B HA   1 
ATOM   4147 H  HA   B LYS   B 1 29  ? 53.983 -20.545 -17.044 0.26 28.52 ?  29  LYS   B HA   1 
ATOM   4148 H  HB2  A LYS   B 1 29  ? 53.935 -22.856 -16.621 0.74 33.43 ?  29  LYS   B HB2  1 
ATOM   4149 H  HB2  B LYS   B 1 29  ? 53.946 -22.854 -16.593 0.26 31.84 ?  29  LYS   B HB2  1 
ATOM   4150 H  HB3  A LYS   B 1 29  ? 52.361 -22.770 -16.440 0.74 33.43 ?  29  LYS   B HB3  1 
ATOM   4151 H  HB3  B LYS   B 1 29  ? 52.366 -22.778 -16.470 0.26 31.84 ?  29  LYS   B HB3  1 
ATOM   4152 H  HG2  A LYS   B 1 29  ? 52.040 -22.418 -18.642 0.74 38.13 ?  29  LYS   B HG2  1 
ATOM   4153 H  HG2  B LYS   B 1 29  ? 52.120 -22.446 -18.688 0.26 34.89 ?  29  LYS   B HG2  1 
ATOM   4154 H  HG3  A LYS   B 1 29  ? 53.588 -22.136 -18.885 0.74 38.13 ?  29  LYS   B HG3  1 
ATOM   4155 H  HG3  B LYS   B 1 29  ? 53.670 -22.131 -18.876 0.26 34.89 ?  29  LYS   B HG3  1 
ATOM   4156 H  HD2  A LYS   B 1 29  ? 53.177 -24.239 -19.682 0.74 41.87 ?  29  LYS   B HD2  1 
ATOM   4157 H  HD2  B LYS   B 1 29  ? 53.263 -24.253 -19.684 0.26 37.30 ?  29  LYS   B HD2  1 
ATOM   4158 H  HD3  A LYS   B 1 29  ? 53.997 -24.427 -18.331 0.74 41.87 ?  29  LYS   B HD3  1 
ATOM   4159 H  HD3  B LYS   B 1 29  ? 54.141 -24.390 -18.365 0.26 37.30 ?  29  LYS   B HD3  1 
ATOM   4160 H  HE2  A LYS   B 1 29  ? 52.014 -24.915 -17.200 0.74 44.24 ?  29  LYS   B HE2  1 
ATOM   4161 H  HE2  B LYS   B 1 29  ? 52.228 -24.944 -17.149 0.26 38.99 ?  29  LYS   B HE2  1 
ATOM   4162 H  HE3  A LYS   B 1 29  ? 51.200 -24.734 -18.555 0.74 44.24 ?  29  LYS   B HE3  1 
ATOM   4163 H  HE3  B LYS   B 1 29  ? 51.351 -24.802 -18.469 0.26 38.99 ?  29  LYS   B HE3  1 
ATOM   4164 H  HZ1  A LYS   B 1 29  ? 51.604 -26.937 -18.156 0.74 45.57 ?  29  LYS   B HZ1  1 
ATOM   4165 H  HZ1  B LYS   B 1 29  ? 51.847 -26.985 -18.068 0.26 39.96 ?  29  LYS   B HZ1  1 
ATOM   4166 H  HZ2  A LYS   B 1 29  ? 52.295 -26.557 -19.371 0.74 45.57 ?  29  LYS   B HZ2  1 
ATOM   4167 H  HZ2  B LYS   B 1 29  ? 52.471 -26.594 -19.316 0.26 39.96 ?  29  LYS   B HZ2  1 
ATOM   4168 H  HZ3  A LYS   B 1 29  ? 53.037 -26.720 -18.138 0.74 45.57 ?  29  LYS   B HZ3  1 
ATOM   4169 H  HZ3  B LYS   B 1 29  ? 53.270 -26.720 -18.114 0.26 39.96 ?  29  LYS   B HZ3  1 
ATOM   4170 N  N    . VAL   B 1 30  ? 50.932 -20.229 -16.149 1.00 21.81 ?  30  VAL   B N    1 
ATOM   4171 C  CA   . VAL   B 1 30  ? 49.649 -19.621 -16.516 1.00 21.58 ?  30  VAL   B CA   1 
ATOM   4172 C  C    . VAL   B 1 30  ? 49.657 -18.106 -16.364 1.00 20.48 ?  30  VAL   B C    1 
ATOM   4173 O  O    . VAL   B 1 30  ? 48.925 -17.399 -17.071 1.00 21.32 ?  30  VAL   B O    1 
ATOM   4174 C  CB   . VAL   B 1 30  ? 48.550 -20.235 -15.630 1.00 22.59 ?  30  VAL   B CB   1 
ATOM   4175 C  CG1  . VAL   B 1 30  ? 47.276 -19.417 -15.702 1.00 22.92 ?  30  VAL   B CG1  1 
ATOM   4176 C  CG2  . VAL   B 1 30  ? 48.302 -21.691 -16.015 1.00 23.59 ?  30  VAL   B CG2  1 
ATOM   4177 H  H    A VAL   B 1 30  ? 50.927 -20.626 -15.382 0.74 26.18 ?  30  VAL   B H    1 
ATOM   4178 H  H    B VAL   B 1 30  ? 50.934 -20.606 -15.372 0.26 26.18 ?  30  VAL   B H    1 
ATOM   4179 H  HA   . VAL   B 1 30  ? 49.447 -19.847 -17.437 1.00 25.90 ?  30  VAL   B HA   1 
ATOM   4180 H  HB   . VAL   B 1 30  ? 48.851 -20.233 -14.708 1.00 27.11 ?  30  VAL   B HB   1 
ATOM   4181 H  HG11 . VAL   B 1 30  ? 46.532 -19.988 -15.451 1.00 27.51 ?  30  VAL   B HG11 1 
ATOM   4182 H  HG12 . VAL   B 1 30  ? 47.340 -18.675 -15.084 1.00 27.51 ?  30  VAL   B HG12 1 
ATOM   4183 H  HG13 . VAL   B 1 30  ? 47.151 -19.103 -16.605 1.00 27.51 ?  30  VAL   B HG13 1 
ATOM   4184 H  HG21 . VAL   B 1 30  ? 47.611 -22.058 -15.439 1.00 28.31 ?  30  VAL   B HG21 1 
ATOM   4185 H  HG22 . VAL   B 1 30  ? 48.009 -21.725 -16.941 1.00 28.31 ?  30  VAL   B HG22 1 
ATOM   4186 H  HG23 . VAL   B 1 30  ? 49.123 -22.192 -15.908 1.00 28.31 ?  30  VAL   B HG23 1 
ATOM   4187 N  N    . LYS   B 1 31  ? 50.418 -17.598 -15.410 1.00 19.97 ?  31  LYS   B N    1 
ATOM   4188 C  CA   . LYS   B 1 31  ? 50.449 -16.185 -15.067 1.00 20.66 ?  31  LYS   B CA   1 
ATOM   4189 C  C    . LYS   B 1 31  ? 49.054 -15.709 -14.671 1.00 18.09 ?  31  LYS   B C    1 
ATOM   4190 O  O    . LYS   B 1 31  ? 48.508 -14.797 -15.297 1.00 19.98 ?  31  LYS   B O    1 
ATOM   4191 C  CB   . LYS   B 1 31  ? 51.062 -15.383 -16.220 1.00 23.90 ?  31  LYS   B CB   1 
ATOM   4192 C  CG   . LYS   B 1 31  ? 52.480 -15.862 -16.578 1.00 27.27 ?  31  LYS   B CG   1 
ATOM   4193 C  CD   . LYS   B 1 31  ? 53.063 -15.100 -17.751 1.00 30.69 ?  31  LYS   B CD   1 
ATOM   4194 C  CE   . LYS   B 1 31  ? 54.540 -15.399 -17.918 1.00 33.37 ?  31  LYS   B CE   1 
ATOM   4195 N  NZ   . LYS   B 1 31  ? 55.307 -15.005 -16.701 1.00 34.48 ?  31  LYS   B NZ   1 
ATOM   4196 H  H    . LYS   B 1 31  ? 50.936 -18.079 -14.931 1.00 23.97 ?  31  LYS   B H    1 
ATOM   4197 H  HA   . LYS   B 1 31  ? 51.018 -16.082 -14.301 1.00 24.80 ?  31  LYS   B HA   1 
ATOM   4198 H  HB2  . LYS   B 1 31  ? 50.511 -15.472 -17.012 1.00 28.69 ?  31  LYS   B HB2  1 
ATOM   4199 H  HB3  . LYS   B 1 31  ? 51.123 -14.451 -15.958 1.00 28.69 ?  31  LYS   B HB3  1 
ATOM   4200 H  HG2  . LYS   B 1 31  ? 53.061 -15.733 -15.811 1.00 32.73 ?  31  LYS   B HG2  1 
ATOM   4201 H  HG3  . LYS   B 1 31  ? 52.452 -16.803 -16.817 1.00 32.73 ?  31  LYS   B HG3  1 
ATOM   4202 H  HD2  . LYS   B 1 31  ? 52.605 -15.365 -18.563 1.00 36.84 ?  31  LYS   B HD2  1 
ATOM   4203 H  HD3  . LYS   B 1 31  ? 52.960 -14.150 -17.598 1.00 36.84 ?  31  LYS   B HD3  1 
ATOM   4204 H  HE2  . LYS   B 1 31  ? 54.664 -16.352 -18.061 1.00 40.06 ?  31  LYS   B HE2  1 
ATOM   4205 H  HE3  . LYS   B 1 31  ? 54.888 -14.898 -18.673 1.00 40.06 ?  31  LYS   B HE3  1 
ATOM   4206 H  HZ1  . LYS   B 1 31  ? 56.181 -15.043 -16.865 1.00 41.39 ?  31  LYS   B HZ1  1 
ATOM   4207 H  HZ2  . LYS   B 1 31  ? 55.093 -14.174 -16.463 1.00 41.39 ?  31  LYS   B HZ2  1 
ATOM   4208 H  HZ3  . LYS   B 1 31  ? 55.116 -15.555 -16.027 1.00 41.39 ?  31  LYS   B HZ3  1 
ATOM   4209 N  N    . PRO   B 1 32  ? 48.443 -16.311 -13.646 1.00 15.36 ?  32  PRO   B N    1 
ATOM   4210 C  CA   . PRO   B 1 32  ? 47.064 -15.949 -13.297 1.00 15.18 ?  32  PRO   B CA   1 
ATOM   4211 C  C    . PRO   B 1 32  ? 46.977 -14.605 -12.598 1.00 14.73 ?  32  PRO   B C    1 
ATOM   4212 O  O    . PRO   B 1 32  ? 47.893 -14.179 -11.891 1.00 16.39 ?  32  PRO   B O    1 
ATOM   4213 C  CB   . PRO   B 1 32  ? 46.657 -17.061 -12.331 1.00 15.60 ?  32  PRO   B CB   1 
ATOM   4214 C  CG   . PRO   B 1 32  ? 47.951 -17.419 -11.648 1.00 16.12 ?  32  PRO   B CG   1 
ATOM   4215 C  CD   . PRO   B 1 32  ? 49.009 -17.298 -12.707 1.00 15.92 ?  32  PRO   B CD   1 
ATOM   4216 H  HA   . PRO   B 1 32  ? 46.488 -15.957 -14.082 1.00 18.23 ?  32  PRO   B HA   1 
ATOM   4217 H  HB2  . PRO   B 1 32  ? 46.007 -16.725 -11.692 1.00 18.72 ?  32  PRO   B HB2  1 
ATOM   4218 H  HB3  . PRO   B 1 32  ? 46.302 -17.817 -12.823 1.00 18.72 ?  32  PRO   B HB3  1 
ATOM   4219 H  HG2  . PRO   B 1 32  ? 48.121 -16.795 -10.922 1.00 19.35 ?  32  PRO   B HG2  1 
ATOM   4220 H  HG3  . PRO   B 1 32  ? 47.907 -18.327 -11.315 1.00 19.35 ?  32  PRO   B HG3  1 
ATOM   4221 H  HD2  . PRO   B 1 32  ? 49.831 -16.956 -12.322 1.00 19.11 ?  32  PRO   B HD2  1 
ATOM   4222 H  HD3  . PRO   B 1 32  ? 49.142 -18.146 -13.147 1.00 19.11 ?  32  PRO   B HD3  1 
ATOM   4223 N  N    . THR   B 1 33  ? 45.827 -13.953 -12.772 1.00 14.55 ?  33  THR   B N    1 
ATOM   4224 C  CA   . THR   B 1 33  ? 45.527 -12.772 -11.969 1.00 15.07 ?  33  THR   B CA   1 
ATOM   4225 C  C    . THR   B 1 33  ? 45.478 -13.120 -10.485 1.00 14.30 ?  33  THR   B C    1 
ATOM   4226 O  O    . THR   B 1 33  ? 45.942 -12.339 -9.643  1.00 15.26 ?  33  THR   B O    1 
ATOM   4227 C  CB   . THR   B 1 33  ? 44.202 -12.163 -12.425 1.00 15.73 ?  33  THR   B CB   1 
ATOM   4228 O  OG1  . THR   B 1 33  ? 44.259 -11.874 -13.826 1.00 15.32 ?  33  THR   B OG1  1 
ATOM   4229 C  CG2  . THR   B 1 33  ? 43.909 -10.869 -11.662 1.00 17.00 ?  33  THR   B CG2  1 
ATOM   4230 H  H    . THR   B 1 33  ? 45.214 -14.172 -13.337 1.00 17.47 ?  33  THR   B H    1 
ATOM   4231 H  HA   . THR   B 1 33  ? 46.220 -12.113 -12.102 1.00 18.10 ?  33  THR   B HA   1 
ATOM   4232 H  HB   . THR   B 1 33  ? 43.478 -12.792 -12.248 1.00 18.88 ?  33  THR   B HB   1 
ATOM   4233 H  HG1  . THR   B 1 33  ? 43.528 -11.533 -14.077 1.00 18.40 ?  33  THR   B HG1  1 
ATOM   4234 H  HG21 . THR   B 1 33  ? 43.155 -10.416 -12.061 1.00 20.41 ?  33  THR   B HG21 1 
ATOM   4235 H  HG22 . THR   B 1 33  ? 43.704 -11.070 -10.734 1.00 20.41 ?  33  THR   B HG22 1 
ATOM   4236 H  HG23 . THR   B 1 33  ? 44.685 -10.289 -11.696 1.00 20.41 ?  33  THR   B HG23 1 
ATOM   4237 N  N    . VAL   B 1 34  ? 44.938 -14.295 -10.146 1.00 13.21 ?  34  VAL   B N    1 
ATOM   4238 C  CA   . VAL   B 1 34  ? 44.739 -14.707 -8.759  1.00 13.09 ?  34  VAL   B CA   1 
ATOM   4239 C  C    . VAL   B 1 34  ? 45.170 -16.161 -8.597  1.00 11.72 ?  34  VAL   B C    1 
ATOM   4240 O  O    . VAL   B 1 34  ? 44.655 -17.055 -9.282  1.00 12.85 ?  34  VAL   B O    1 
ATOM   4241 C  CB   . VAL   B 1 34  ? 43.266 -14.557 -8.314  1.00 13.86 ?  34  VAL   B CB   1 
ATOM   4242 C  CG1  . VAL   B 1 34  ? 43.093 -15.004 -6.875  1.00 14.76 ?  34  VAL   B CG1  1 
ATOM   4243 C  CG2  . VAL   B 1 34  ? 42.767 -13.114 -8.502  1.00 14.63 ?  34  VAL   B CG2  1 
ATOM   4244 H  H    . VAL   B 1 34  ? 44.694 -14.894 -10.716 1.00 15.86 ?  34  VAL   B H    1 
ATOM   4245 H  HA   . VAL   B 1 34  ? 45.292 -14.159 -8.177  1.00 15.72 ?  34  VAL   B HA   1 
ATOM   4246 H  HB   . VAL   B 1 34  ? 42.719 -15.131 -8.871  1.00 16.64 ?  34  VAL   B HB   1 
ATOM   4247 H  HG11 . VAL   B 1 34  ? 42.231 -14.698 -6.549  1.00 17.72 ?  34  VAL   B HG11 1 
ATOM   4248 H  HG12 . VAL   B 1 34  ? 43.129 -15.975 -6.834  1.00 17.72 ?  34  VAL   B HG12 1 
ATOM   4249 H  HG13 . VAL   B 1 34  ? 43.802 -14.625 -6.333  1.00 17.72 ?  34  VAL   B HG13 1 
ATOM   4250 H  HG21 . VAL   B 1 34  ? 41.847 -13.058 -8.197  1.00 17.57 ?  34  VAL   B HG21 1 
ATOM   4251 H  HG22 . VAL   B 1 34  ? 43.325 -12.515 -7.986  1.00 17.57 ?  34  VAL   B HG22 1 
ATOM   4252 H  HG23 . VAL   B 1 34  ? 42.814 -12.883 -9.445  1.00 17.57 ?  34  VAL   B HG23 1 
ATOM   4253 N  N    . VAL   B 1 35  ? 46.066 -16.409 -7.651  1.00 11.91 ?  35  VAL   B N    1 
ATOM   4254 C  CA   . VAL   B 1 35  ? 46.312 -17.755 -7.140  1.00 11.45 ?  35  VAL   B CA   1 
ATOM   4255 C  C    . VAL   B 1 35  ? 45.774 -17.812 -5.717  1.00 11.19 ?  35  VAL   B C    1 
ATOM   4256 O  O    . VAL   B 1 35  ? 46.000 -16.888 -4.925  1.00 11.74 ?  35  VAL   B O    1 
ATOM   4257 C  CB   . VAL   B 1 35  ? 47.799 -18.157 -7.222  1.00 11.87 ?  35  VAL   B CB   1 
ATOM   4258 C  CG1  . VAL   B 1 35  ? 48.678 -17.317 -6.299  1.00 13.41 ?  35  VAL   B CG1  1 
ATOM   4259 C  CG2  . VAL   B 1 35  ? 47.943 -19.642 -6.902  1.00 13.21 ?  35  VAL   B CG2  1 
ATOM   4260 H  H    . VAL   B 1 35  ? 46.555 -15.803 -7.279  1.00 14.31 ?  35  VAL   B H    1 
ATOM   4261 H  HA   . VAL   B 1 35  ? 45.802 -18.385 -7.668  1.00 13.75 ?  35  VAL   B HA   1 
ATOM   4262 H  HB   . VAL   B 1 35  ? 48.108 -18.022 -8.133  1.00 14.25 ?  35  VAL   B HB   1 
ATOM   4263 H  HG11 . VAL   B 1 35  ? 49.609 -17.519 -6.479  1.00 16.10 ?  35  VAL   B HG11 1 
ATOM   4264 H  HG12 . VAL   B 1 35  ? 48.504 -16.378 -6.464  1.00 16.10 ?  35  VAL   B HG12 1 
ATOM   4265 H  HG13 . VAL   B 1 35  ? 48.467 -17.535 -5.376  1.00 16.10 ?  35  VAL   B HG13 1 
ATOM   4266 H  HG21 . VAL   B 1 35  ? 48.864 -19.907 -7.018  1.00 15.86 ?  35  VAL   B HG21 1 
ATOM   4267 H  HG22 . VAL   B 1 35  ? 47.664 -19.797 -5.983  1.00 15.86 ?  35  VAL   B HG22 1 
ATOM   4268 H  HG23 . VAL   B 1 35  ? 47.371 -20.153 -7.503  1.00 15.86 ?  35  VAL   B HG23 1 
ATOM   4269 N  N    . VAL   B 1 36  ? 45.053 -18.890 -5.396  1.00 11.18 ?  36  VAL   B N    1 
ATOM   4270 C  CA   . VAL   B 1 36  ? 44.506 -19.095 -4.065  1.00 10.74 ?  36  VAL   B CA   1 
ATOM   4271 C  C    . VAL   B 1 36  ? 45.504 -19.859 -3.209  1.00 10.60 ?  36  VAL   B C    1 
ATOM   4272 O  O    . VAL   B 1 36  ? 46.060 -20.886 -3.638  1.00 12.07 ?  36  VAL   B O    1 
ATOM   4273 C  CB   . VAL   B 1 36  ? 43.166 -19.844 -4.141  1.00 11.66 ?  36  VAL   B CB   1 
ATOM   4274 C  CG1  . VAL   B 1 36  ? 42.670 -20.208 -2.745  1.00 12.14 ?  36  VAL   B CG1  1 
ATOM   4275 C  CG2  . VAL   B 1 36  ? 42.145 -19.014 -4.896  1.00 12.30 ?  36  VAL   B CG2  1 
ATOM   4276 H  H    . VAL   B 1 36  ? 44.877 -19.529 -5.942  1.00 13.43 ?  36  VAL   B H    1 
ATOM   4277 H  HA   . VAL   B 1 36  ? 44.341 -18.232 -3.649  1.00 12.90 ?  36  VAL   B HA   1 
ATOM   4278 H  HB   . VAL   B 1 36  ? 43.298 -20.672 -4.633  1.00 14.00 ?  36  VAL   B HB   1 
ATOM   4279 H  HG11 . VAL   B 1 36  ? 41.726 -20.434 -2.795  1.00 14.58 ?  36  VAL   B HG11 1 
ATOM   4280 H  HG12 . VAL   B 1 36  ? 43.171 -20.969 -2.413  1.00 14.58 ?  36  VAL   B HG12 1 
ATOM   4281 H  HG13 . VAL   B 1 36  ? 42.793 -19.445 -2.158  1.00 14.58 ?  36  VAL   B HG13 1 
ATOM   4282 H  HG21 . VAL   B 1 36  ? 41.299 -19.488 -4.909  1.00 14.77 ?  36  VAL   B HG21 1 
ATOM   4283 H  HG22 . VAL   B 1 36  ? 42.040 -18.160 -4.448  1.00 14.77 ?  36  VAL   B HG22 1 
ATOM   4284 H  HG23 . VAL   B 1 36  ? 42.459 -18.875 -5.804  1.00 14.77 ?  36  VAL   B HG23 1 
ATOM   4285 N  N    . ASN   B 1 37  ? 45.730 -19.354 -1.997  1.00 11.14 ?  37  ASN   B N    1 
ATOM   4286 C  CA   . ASN   B 1 37  ? 46.494 -20.065 -0.986  1.00 10.84 ?  37  ASN   B CA   1 
ATOM   4287 C  C    . ASN   B 1 37  ? 45.555 -20.754 -0.000  1.00 12.07 ?  37  ASN   B C    1 
ATOM   4288 O  O    . ASN   B 1 37  ? 44.538 -20.188 0.407   1.00 12.03 ?  37  ASN   B O    1 
ATOM   4289 C  CB   . ASN   B 1 37  ? 47.441 -19.125 -0.238  1.00 11.34 ?  37  ASN   B CB   1 
ATOM   4290 C  CG   . ASN   B 1 37  ? 48.289 -19.845 0.783   1.00 11.89 ?  37  ASN   B CG   1 
ATOM   4291 O  OD1  . ASN   B 1 37  ? 48.643 -21.019 0.598   1.00 12.69 ?  37  ASN   B OD1  1 
ATOM   4292 N  ND2  . ASN   B 1 37  ? 48.622 -19.159 1.869   1.00 11.97 ?  37  ASN   B ND2  1 
ATOM   4293 H  H    . ASN   B 1 37  ? 45.447 -18.580 -1.731  1.00 13.38 ?  37  ASN   B H    1 
ATOM   4294 H  HA   . ASN   B 1 37  ? 47.025 -20.752 -1.416  1.00 13.02 ?  37  ASN   B HA   1 
ATOM   4295 H  HB2  . ASN   B 1 37  ? 48.046 -18.716 -0.879  1.00 13.61 ?  37  ASN   B HB2  1 
ATOM   4296 H  HB3  . ASN   B 1 37  ? 46.929 -18.448 0.220   1.00 13.61 ?  37  ASN   B HB3  1 
ATOM   4297 H  HD21 . ASN   B 1 37  ? 49.101 -19.527 2.486   1.00 14.37 ?  37  ASN   B HD21 1 
ATOM   4298 H  HD22 . ASN   B 1 37  ? 48.361 -18.348 1.971   1.00 14.37 ?  37  ASN   B HD22 1 
ATOM   4299 N  N    . ALA   B 1 38  ? 45.909 -21.986 0.374   1.00 11.86 ?  38  ALA   B N    1 
ATOM   4300 C  CA   . ALA   B 1 38  ? 45.241 -22.725 1.446   1.00 11.96 ?  38  ALA   B CA   1 
ATOM   4301 C  C    . ALA   B 1 38  ? 45.824 -22.238 2.773   1.00 12.19 ?  38  ALA   B C    1 
ATOM   4302 O  O    . ALA   B 1 38  ? 46.719 -22.859 3.364   1.00 12.86 ?  38  ALA   B O    1 
ATOM   4303 C  CB   . ALA   B 1 38  ? 45.442 -24.226 1.257   1.00 13.53 ?  38  ALA   B CB   1 
ATOM   4304 H  H    . ALA   B 1 38  ? 46.563 -22.421 0.016   1.00 14.24 ?  38  ALA   B H    1 
ATOM   4305 H  HA   . ALA   B 1 38  ? 44.292 -22.532 1.433   1.00 14.36 ?  38  ALA   B HA   1 
ATOM   4306 H  HB1  . ALA   B 1 38  ? 44.986 -24.698 1.978   1.00 16.24 ?  38  ALA   B HB1  1 
ATOM   4307 H  HB2  . ALA   B 1 38  ? 45.059 -24.491 0.405   1.00 16.24 ?  38  ALA   B HB2  1 
ATOM   4308 H  HB3  . ALA   B 1 38  ? 46.386 -24.428 1.277   1.00 16.24 ?  38  ALA   B HB3  1 
ATOM   4309 N  N    . ALA   B 1 39  ? 45.308 -21.091 3.236   1.00 11.88 ?  39  ALA   B N    1 
ATOM   4310 C  CA   . ALA   B 1 39  ? 45.858 -20.370 4.374   1.00 12.14 ?  39  ALA   B CA   1 
ATOM   4311 C  C    . ALA   B 1 39  ? 45.244 -20.827 5.697   1.00 12.33 ?  39  ALA   B C    1 
ATOM   4312 O  O    . ALA   B 1 39  ? 44.218 -21.512 5.741   1.00 13.24 ?  39  ALA   B O    1 
ATOM   4313 C  CB   . ALA   B 1 39  ? 45.632 -18.864 4.199   1.00 12.53 ?  39  ALA   B CB   1 
ATOM   4314 H  H    . ALA   B 1 39  ? 44.618 -20.710 2.897   1.00 14.27 ?  39  ALA   B H    1 
ATOM   4315 H  HA   . ALA   B 1 39  ? 46.811 -20.525 4.423   1.00 14.57 ?  39  ALA   B HA   1 
ATOM   4316 H  HB1  . ALA   B 1 39  ? 46.002 -18.394 4.965   1.00 15.04 ?  39  ALA   B HB1  1 
ATOM   4317 H  HB2  . ALA   B 1 39  ? 46.074 -18.571 3.388   1.00 15.04 ?  39  ALA   B HB2  1 
ATOM   4318 H  HB3  . ALA   B 1 39  ? 44.678 -18.689 4.137   1.00 15.04 ?  39  ALA   B HB3  1 
ATOM   4319 N  N    . ASN   B 1 40  ? 45.873 -20.395 6.790   1.00 12.77 ?  40  ASN   B N    1 
ATOM   4320 C  CA   . ASN   B 1 40  ? 45.306 -20.458 8.132   1.00 13.63 ?  40  ASN   B CA   1 
ATOM   4321 C  C    . ASN   B 1 40  ? 45.126 -19.034 8.661   1.00 13.42 ?  40  ASN   B C    1 
ATOM   4322 O  O    . ASN   B 1 40  ? 45.544 -18.058 8.032   1.00 13.30 ?  40  ASN   B O    1 
ATOM   4323 C  CB   . ASN   B 1 40  ? 46.160 -21.333 9.069   1.00 15.05 ?  40  ASN   B CB   1 
ATOM   4324 C  CG   . ASN   B 1 40  ? 47.612 -20.924 9.098   1.00 15.63 ?  40  ASN   B CG   1 
ATOM   4325 O  OD1  . ASN   B 1 40  ? 47.931 -19.744 9.147   1.00 17.82 ?  40  ASN   B OD1  1 
ATOM   4326 N  ND2  . ASN   B 1 40  ? 48.503 -21.897 9.063   1.00 16.16 ?  40  ASN   B ND2  1 
ATOM   4327 H  H    . ASN   B 1 40  ? 46.660 -20.049 6.777   1.00 15.33 ?  40  ASN   B H    1 
ATOM   4328 H  HA   . ASN   B 1 40  ? 44.422 -20.858 8.080   1.00 16.37 ?  40  ASN   B HA   1 
ATOM   4329 H  HB2  . ASN   B 1 40  ? 45.810 -21.265 9.972   1.00 18.07 ?  40  ASN   B HB2  1 
ATOM   4330 H  HB3  . ASN   B 1 40  ? 46.114 -22.254 8.766   1.00 18.07 ?  40  ASN   B HB3  1 
ATOM   4331 H  HD21 . ASN   B 1 40  ? 49.342 -21.712 9.077   1.00 19.41 ?  40  ASN   B HD21 1 
ATOM   4332 H  HD22 . ASN   B 1 40  ? 48.242 -22.715 9.025   1.00 19.41 ?  40  ASN   B HD22 1 
ATOM   4333 N  N    . VAL   B 1 41  ? 44.475 -18.908 9.820   1.00 14.20 ?  41  VAL   B N    1 
ATOM   4334 C  CA   . VAL   B 1 41  ? 44.021 -17.583 10.264  1.00 14.72 ?  41  VAL   B CA   1 
ATOM   4335 C  C    . VAL   B 1 41  ? 45.175 -16.636 10.565  1.00 14.83 ?  41  VAL   B C    1 
ATOM   4336 O  O    . VAL   B 1 41  ? 45.003 -15.413 10.486  1.00 15.07 ?  41  VAL   B O    1 
ATOM   4337 C  CB   . VAL   B 1 41  ? 43.045 -17.655 11.454  1.00 15.79 ?  41  VAL   B CB   1 
ATOM   4338 C  CG1  . VAL   B 1 41  ? 41.747 -18.349 11.050  1.00 16.60 ?  41  VAL   B CG1  1 
ATOM   4339 C  CG2  . VAL   B 1 41  ? 43.695 -18.343 12.646  1.00 16.94 ?  41  VAL   B CG2  1 
ATOM   4340 H  H    . VAL   B 1 41  ? 44.284 -19.553 10.347  1.00 17.05 ?  41  VAL   B H    1 
ATOM   4341 H  HA   . VAL   B 1 41  ? 43.527 -17.185 9.530   1.00 17.68 ?  41  VAL   B HA   1 
ATOM   4342 H  HB   . VAL   B 1 41  ? 42.819 -16.750 11.723  1.00 18.96 ?  41  VAL   B HB   1 
ATOM   4343 H  HG11 . VAL   B 1 41  ? 41.142 -18.354 11.808  1.00 19.93 ?  41  VAL   B HG11 1 
ATOM   4344 H  HG12 . VAL   B 1 41  ? 41.347 -17.866 10.309  1.00 19.93 ?  41  VAL   B HG12 1 
ATOM   4345 H  HG13 . VAL   B 1 41  ? 41.948 -19.259 10.780  1.00 19.93 ?  41  VAL   B HG13 1 
ATOM   4346 H  HG21 . VAL   B 1 41  ? 43.057 -18.377 13.374  1.00 20.33 ?  41  VAL   B HG21 1 
ATOM   4347 H  HG22 . VAL   B 1 41  ? 43.950 -19.244 12.388  1.00 20.33 ?  41  VAL   B HG22 1 
ATOM   4348 H  HG23 . VAL   B 1 41  ? 44.478 -17.840 12.912  1.00 20.33 ?  41  VAL   B HG23 1 
ATOM   4349 N  N    . TYR   B 1 42  ? 46.343 -17.153 10.944  1.00 14.75 ?  42  TYR   B N    1 
ATOM   4350 C  CA   . TYR   B 1 42  ? 47.496 -16.302 11.216  1.00 15.16 ?  42  TYR   B CA   1 
ATOM   4351 C  C    . TYR   B 1 42  ? 48.462 -16.220 10.035  1.00 14.50 ?  42  TYR   B C    1 
ATOM   4352 O  O    . TYR   B 1 42  ? 49.550 -15.645 10.172  1.00 16.02 ?  42  TYR   B O    1 
ATOM   4353 C  CB   . TYR   B 1 42  ? 48.196 -16.714 12.519  1.00 17.46 ?  42  TYR   B CB   1 
ATOM   4354 C  CG   . TYR   B 1 42  ? 47.594 -16.033 13.744  1.00 18.62 ?  42  TYR   B CG   1 
ATOM   4355 C  CD1  . TYR   B 1 42  ? 47.799 -14.672 13.972  1.00 17.84 ?  42  TYR   B CD1  1 
ATOM   4356 C  CD2  . TYR   B 1 42  ? 46.819 -16.735 14.655  1.00 21.03 ?  42  TYR   B CD2  1 
ATOM   4357 C  CE1  . TYR   B 1 42  ? 47.256 -14.039 15.070  1.00 18.91 ?  42  TYR   B CE1  1 
ATOM   4358 C  CE2  . TYR   B 1 42  ? 46.272 -16.107 15.761  1.00 21.01 ?  42  TYR   B CE2  1 
ATOM   4359 C  CZ   . TYR   B 1 42  ? 46.492 -14.757 15.963  1.00 20.73 ?  42  TYR   B CZ   1 
ATOM   4360 O  OH   . TYR   B 1 42  ? 45.951 -14.118 17.063  1.00 24.16 ?  42  TYR   B OH   1 
ATOM   4361 H  H    . TYR   B 1 42  ? 46.493 -17.998 11.047  1.00 17.71 ?  42  TYR   B H    1 
ATOM   4362 H  HA   . TYR   B 1 42  ? 47.165 -15.406 11.358  1.00 18.21 ?  42  TYR   B HA   1 
ATOM   4363 H  HB2  . TYR   B 1 42  ? 48.113 -17.673 12.638  1.00 20.96 ?  42  TYR   B HB2  1 
ATOM   4364 H  HB3  . TYR   B 1 42  ? 49.133 -16.466 12.465  1.00 20.96 ?  42  TYR   B HB3  1 
ATOM   4365 H  HD1  . TYR   B 1 42  ? 48.315 -14.183 13.364  1.00 21.42 ?  42  TYR   B HD1  1 
ATOM   4366 H  HD2  . TYR   B 1 42  ? 46.670 -17.645 14.517  1.00 25.24 ?  42  TYR   B HD2  1 
ATOM   4367 H  HE1  . TYR   B 1 42  ? 47.405 -13.130 15.203  1.00 22.70 ?  42  TYR   B HE1  1 
ATOM   4368 H  HE2  . TYR   B 1 42  ? 45.755 -16.591 16.363  1.00 25.22 ?  42  TYR   B HE2  1 
ATOM   4369 H  HH   . TYR   B 1 42  ? 46.167 -13.307 17.049  1.00 29.00 ?  42  TYR   B HH   1 
ATOM   4370 N  N    . LEU   B 1 43  ? 48.077 -16.752 8.876   1.00 13.52 ?  43  LEU   B N    1 
ATOM   4371 C  CA   . LEU   B 1 43  ? 48.886 -16.666 7.664   1.00 13.67 ?  43  LEU   B CA   1 
ATOM   4372 C  C    . LEU   B 1 43  ? 50.301 -17.171 7.919   1.00 13.97 ?  43  LEU   B C    1 
ATOM   4373 O  O    . LEU   B 1 43  ? 51.280 -16.578 7.469   1.00 14.46 ?  43  LEU   B O    1 
ATOM   4374 C  CB   . LEU   B 1 43  ? 48.895 -15.256 7.069   1.00 13.95 ?  43  LEU   B CB   1 
ATOM   4375 C  CG   . LEU   B 1 43  ? 47.540 -14.647 6.683   1.00 13.97 ?  43  LEU   B CG   1 
ATOM   4376 C  CD1  . LEU   B 1 43  ? 47.761 -13.234 6.127   1.00 15.40 ?  43  LEU   B CD1  1 
ATOM   4377 C  CD2  . LEU   B 1 43  ? 46.789 -15.518 5.690   1.00 13.77 ?  43  LEU   B CD2  1 
ATOM   4378 H  H    . LEU   B 1 43  ? 47.347 -17.200 8.769   1.00 16.24 ?  43  LEU   B H    1 
ATOM   4379 H  HA   . LEU   B 1 43  ? 48.493 -17.253 6.999   1.00 16.41 ?  43  LEU   B HA   1 
ATOM   4380 H  HB2  . LEU   B 1 43  ? 49.306 -14.658 7.716   1.00 16.75 ?  43  LEU   B HB2  1 
ATOM   4381 H  HB3  . LEU   B 1 43  ? 49.437 -15.274 6.265   1.00 16.75 ?  43  LEU   B HB3  1 
ATOM   4382 H  HG   . LEU   B 1 43  ? 46.997 -14.564 7.481   1.00 16.77 ?  43  LEU   B HG   1 
ATOM   4383 H  HD11 . LEU   B 1 43  ? 46.901 -12.850 5.887   1.00 18.49 ?  43  LEU   B HD11 1 
ATOM   4384 H  HD12 . LEU   B 1 43  ? 48.183 -12.684 6.811   1.00 18.49 ?  43  LEU   B HD12 1 
ATOM   4385 H  HD13 . LEU   B 1 43  ? 48.331 -13.282 5.346   1.00 18.49 ?  43  LEU   B HD13 1 
ATOM   4386 H  HD21 . LEU   B 1 43  ? 45.979 -15.058 5.411   1.00 16.54 ?  43  LEU   B HD21 1 
ATOM   4387 H  HD22 . LEU   B 1 43  ? 47.354 -15.684 4.919   1.00 16.54 ?  43  LEU   B HD22 1 
ATOM   4388 H  HD23 . LEU   B 1 43  ? 46.559 -16.359 6.117   1.00 16.54 ?  43  LEU   B HD23 1 
ATOM   4389 N  N    . LYS   B 1 44  ? 50.405 -18.295 8.632   1.00 14.09 ?  44  LYS   B N    1 
ATOM   4390 C  CA   . LYS   B 1 44  ? 51.675 -18.967 8.873   1.00 14.25 ?  44  LYS   B CA   1 
ATOM   4391 C  C    . LYS   B 1 44  ? 51.792 -20.080 7.845   1.00 14.01 ?  44  LYS   B C    1 
ATOM   4392 O  O    . LYS   B 1 44  ? 51.088 -21.092 7.932   1.00 14.87 ?  44  LYS   B O    1 
ATOM   4393 C  CB   . LYS   B 1 44  ? 51.737 -19.499 10.305  1.00 16.60 ?  44  LYS   B CB   1 
ATOM   4394 C  CG   . LYS   B 1 44  ? 51.917 -18.404 11.347  1.00 19.37 ?  44  LYS   B CG   1 
ATOM   4395 C  CD   . LYS   B 1 44  ? 53.135 -17.541 10.993  1.00 22.61 ?  44  LYS   B CD   1 
ATOM   4396 C  CE   . LYS   B 1 44  ? 53.554 -16.612 12.103  1.00 25.82 ?  44  LYS   B CE   1 
ATOM   4397 N  NZ   . LYS   B 1 44  ? 54.780 -15.845 11.754  1.00 26.95 ?  44  LYS   B NZ   1 
ATOM   4398 H  H    . LYS   B 1 44  ? 49.738 -18.690 9.003   1.00 16.92 ?  44  LYS   B H    1 
ATOM   4399 H  HA   . LYS   B 1 44  ? 52.410 -18.354 8.719   1.00 17.11 ?  44  LYS   B HA   1 
ATOM   4400 H  HB2  . LYS   B 1 44  ? 50.903 -19.961 10.504  1.00 19.93 ?  44  LYS   B HB2  1 
ATOM   4401 H  HB3  . LYS   B 1 44  ? 52.480 -20.113 10.387  1.00 19.93 ?  44  LYS   B HB3  1 
ATOM   4402 H  HG2  . LYS   B 1 44  ? 51.129 -17.840 11.367  1.00 23.25 ?  44  LYS   B HG2  1 
ATOM   4403 H  HG3  . LYS   B 1 44  ? 52.067 -18.809 12.219  1.00 23.25 ?  44  LYS   B HG3  1 
ATOM   4404 H  HD2  . LYS   B 1 44  ? 53.879 -18.131 10.774  1.00 27.14 ?  44  LYS   B HD2  1 
ATOM   4405 H  HD3  . LYS   B 1 44  ? 52.913 -16.993 10.223  1.00 27.14 ?  44  LYS   B HD3  1 
ATOM   4406 H  HE2  . LYS   B 1 44  ? 52.844 -15.978 12.253  1.00 30.99 ?  44  LYS   B HE2  1 
ATOM   4407 H  HE3  . LYS   B 1 44  ? 53.730 -17.131 12.902  1.00 30.99 ?  44  LYS   B HE3  1 
ATOM   4408 H  HZ1  . LYS   B 1 44  ? 55.001 -15.307 12.426  1.00 32.35 ?  44  LYS   B HZ1  1 
ATOM   4409 H  HZ2  . LYS   B 1 44  ? 55.456 -16.401 11.593  1.00 32.35 ?  44  LYS   B HZ2  1 
ATOM   4410 H  HZ3  . LYS   B 1 44  ? 54.633 -15.351 11.025  1.00 32.35 ?  44  LYS   B HZ3  1 
ATOM   4411 N  N    . HIS   B 1 45  ? 52.643 -19.861 6.844   1.00 13.51 ?  45  HIS   B N    1 
ATOM   4412 C  CA   . HIS   B 1 45  ? 52.671 -20.693 5.641   1.00 13.69 ?  45  HIS   B CA   1 
ATOM   4413 C  C    . HIS   B 1 45  ? 53.690 -21.821 5.800   1.00 16.36 ?  45  HIS   B C    1 
ATOM   4414 O  O    . HIS   B 1 45  ? 54.760 -21.831 5.202   1.00 18.44 ?  45  HIS   B O    1 
ATOM   4415 C  CB   . HIS   B 1 45  ? 52.977 -19.834 4.425   1.00 13.50 ?  45  HIS   B CB   1 
ATOM   4416 C  CG   . HIS   B 1 45  ? 52.104 -18.629 4.320   1.00 12.71 ?  45  HIS   B CG   1 
ATOM   4417 N  ND1  . HIS   B 1 45  ? 50.726 -18.713 4.294   1.00 13.87 ?  45  HIS   B ND1  1 
ATOM   4418 C  CD2  . HIS   B 1 45  ? 52.411 -17.314 4.253   1.00 14.19 ?  45  HIS   B CD2  1 
ATOM   4419 C  CE1  . HIS   B 1 45  ? 50.230 -17.494 4.195   1.00 13.35 ?  45  HIS   B CE1  1 
ATOM   4420 N  NE2  . HIS   B 1 45  ? 51.228 -16.629 4.176   1.00 14.00 ?  45  HIS   B NE2  1 
ATOM   4421 H  H    . HIS   B 1 45  ? 53.219 -19.219 6.837   1.00 16.22 ?  45  HIS   B H    1 
ATOM   4422 H  HA   . HIS   B 1 45  ? 51.793 -21.090 5.516   1.00 16.43 ?  45  HIS   B HA   1 
ATOM   4423 H  HB2  . HIS   B 1 45  ? 53.896 -19.534 4.473   1.00 16.21 ?  45  HIS   B HB2  1 
ATOM   4424 H  HB3  . HIS   B 1 45  ? 52.845 -20.368 3.624   1.00 16.21 ?  45  HIS   B HB3  1 
ATOM   4425 H  HD2  . HIS   B 1 45  ? 53.267 -16.943 4.259   1.00 17.04 ?  45  HIS   B HD2  1 
ATOM   4426 H  HE1  . HIS   B 1 45  ? 49.326 -17.278 4.154   1.00 16.02 ?  45  HIS   B HE1  1 
ATOM   4427 H  HE2  . HIS   B 1 45  ? 51.146 -15.772 4.123   1.00 16.81 ?  45  HIS   B HE2  1 
ATOM   4428 N  N    A GLY   B 1 46  ? 53.315 -22.803 6.614   0.74 17.19 ?  46  GLY   B N    1 
ATOM   4429 N  N    B GLY   B 1 46  ? 53.327 -22.788 6.634   0.26 17.46 ?  46  GLY   B N    1 
ATOM   4430 C  CA   A GLY   B 1 46  ? 54.240 -23.856 6.996   0.74 19.25 ?  46  GLY   B CA   1 
ATOM   4431 C  CA   B GLY   B 1 46  ? 54.247 -23.854 6.971   0.26 18.86 ?  46  GLY   B CA   1 
ATOM   4432 C  C    A GLY   B 1 46  ? 54.294 -25.074 6.094   0.74 21.83 ?  46  GLY   B C    1 
ATOM   4433 C  C    B GLY   B 1 46  ? 54.275 -24.998 5.979   0.26 20.28 ?  46  GLY   B C    1 
ATOM   4434 O  O    A GLY   B 1 46  ? 55.374 -25.483 5.659   0.74 25.28 ?  46  GLY   B O    1 
ATOM   4435 O  O    B GLY   B 1 46  ? 55.302 -25.258 5.346   0.26 20.99 ?  46  GLY   B O    1 
ATOM   4436 H  H    A GLY   B 1 46  ? 52.532 -22.871 6.968   0.74 20.63 ?  46  GLY   B H    1 
ATOM   4437 H  H    B GLY   B 1 46  ? 52.558 -22.844 7.016   0.26 20.96 ?  46  GLY   B H    1 
ATOM   4438 H  HA2  A GLY   B 1 46  ? 55.133 -23.483 7.045   0.74 23.11 ?  46  GLY   B HA2  1 
ATOM   4439 H  HA2  B GLY   B 1 46  ? 55.144 -23.489 7.032   0.26 22.64 ?  46  GLY   B HA2  1 
ATOM   4440 H  HA3  A GLY   B 1 46  ? 54.002 -24.173 7.880   0.74 23.11 ?  46  GLY   B HA3  1 
ATOM   4441 H  HA3  B GLY   B 1 46  ? 54.009 -24.212 7.839   0.26 22.64 ?  46  GLY   B HA3  1 
ATOM   4442 N  N    . GLY   B 1 47  ? 53.144 -25.685 5.819   1.00 20.95 ?  47  GLY   B N    1 
ATOM   4443 C  CA   . GLY   B 1 47  ? 53.095 -26.943 5.104   1.00 18.25 ?  47  GLY   B CA   1 
ATOM   4444 C  C    . GLY   B 1 47  ? 52.181 -26.901 3.894   1.00 15.73 ?  47  GLY   B C    1 
ATOM   4445 O  O    . GLY   B 1 47  ? 51.536 -25.888 3.605   1.00 15.44 ?  47  GLY   B O    1 
ATOM   4446 H  H    A GLY   B 1 47  ? 52.374 -25.394 6.061   0.74 25.15 ?  47  GLY   B H    1 
ATOM   4447 H  H    B GLY   B 1 47  ? 52.383 -25.433 6.125   0.26 25.15 ?  47  GLY   B H    1 
ATOM   4448 H  HA2  . GLY   B 1 47  ? 53.986 -27.186 4.799   1.00 21.91 ?  47  GLY   B HA2  1 
ATOM   4449 H  HA3  . GLY   B 1 47  ? 52.784 -27.641 5.704   1.00 21.91 ?  47  GLY   B HA3  1 
ATOM   4450 N  N    . GLY   B 1 48  ? 52.119 -28.039 3.204   1.00 15.04 ?  48  GLY   B N    1 
ATOM   4451 C  CA   . GLY   B 1 48  ? 51.191 -28.192 2.098   1.00 14.90 ?  48  GLY   B CA   1 
ATOM   4452 C  C    . GLY   B 1 48  ? 51.338 -27.088 1.073   1.00 13.94 ?  48  GLY   B C    1 
ATOM   4453 O  O    . GLY   B 1 48  ? 52.443 -26.647 0.752   1.00 14.08 ?  48  GLY   B O    1 
ATOM   4454 H  H    . GLY   B 1 48  ? 52.618 -28.724 3.346   1.00 18.06 ?  48  GLY   B H    1 
ATOM   4455 H  HA2  . GLY   B 1 48  ? 51.343 -29.048 1.660   1.00 17.89 ?  48  GLY   B HA2  1 
ATOM   4456 H  HA3  . GLY   B 1 48  ? 50.280 -28.181 2.435   1.00 17.89 ?  48  GLY   B HA3  1 
ATOM   4457 N  N    . VAL   B 1 49  ? 50.199 -26.637 0.547   1.00 13.71 ?  49  VAL   B N    1 
ATOM   4458 C  CA   . VAL   B 1 49  ? 50.184 -25.614 -0.496  1.00 13.51 ?  49  VAL   B CA   1 
ATOM   4459 C  C    . VAL   B 1 49  ? 50.838 -24.330 -0.007  1.00 12.66 ?  49  VAL   B C    1 
ATOM   4460 O  O    . VAL   B 1 49  ? 51.634 -23.710 -0.725  1.00 13.75 ?  49  VAL   B O    1 
ATOM   4461 C  CB   . VAL   B 1 49  ? 48.735 -25.356 -0.959  1.00 14.84 ?  49  VAL   B CB   1 
ATOM   4462 C  CG1  . VAL   B 1 49  ? 48.640 -24.088 -1.805  1.00 14.72 ?  49  VAL   B CG1  1 
ATOM   4463 C  CG2  . VAL   B 1 49  ? 48.202 -26.552 -1.724  1.00 17.36 ?  49  VAL   B CG2  1 
ATOM   4464 H  H    . VAL   B 1 49  ? 49.417 -26.915 0.777   1.00 16.47 ?  49  VAL   B H    1 
ATOM   4465 H  HA   . VAL   B 1 49  ? 50.687 -25.933 -1.259  1.00 16.22 ?  49  VAL   B HA   1 
ATOM   4466 H  HB   . VAL   B 1 49  ? 48.175 -25.235 -0.176  1.00 17.82 ?  49  VAL   B HB   1 
ATOM   4467 H  HG11 . VAL   B 1 49  ? 47.804 -24.102 -2.294  1.00 17.67 ?  49  VAL   B HG11 1 
ATOM   4468 H  HG12 . VAL   B 1 49  ? 48.666 -23.315 -1.218  1.00 17.67 ?  49  VAL   B HG12 1 
ATOM   4469 H  HG13 . VAL   B 1 49  ? 49.386 -24.066 -2.421  1.00 17.67 ?  49  VAL   B HG13 1 
ATOM   4470 H  HG21 . VAL   B 1 49  ? 47.290 -26.366 -1.995  1.00 20.84 ?  49  VAL   B HG21 1 
ATOM   4471 H  HG22 . VAL   B 1 49  ? 48.759 -26.692 -2.506  1.00 20.84 ?  49  VAL   B HG22 1 
ATOM   4472 H  HG23 . VAL   B 1 49  ? 48.230 -27.329 -1.150  1.00 20.84 ?  49  VAL   B HG23 1 
ATOM   4473 N  N    . ALA   B 1 50  ? 50.479 -23.885 1.202   1.00 12.58 ?  50  ALA   B N    1 
ATOM   4474 C  CA   . ALA   B 1 50  ? 51.002 -22.613 1.694   1.00 12.38 ?  50  ALA   B CA   1 
ATOM   4475 C  C    . ALA   B 1 50  ? 52.520 -22.648 1.802   1.00 12.70 ?  50  ALA   B C    1 
ATOM   4476 O  O    . ALA   B 1 50  ? 53.198 -21.689 1.425   1.00 13.09 ?  50  ALA   B O    1 
ATOM   4477 C  CB   . ALA   B 1 50  ? 50.366 -22.260 3.035   1.00 13.03 ?  50  ALA   B CB   1 
ATOM   4478 H  H    . ALA   B 1 50  ? 49.952 -24.291 1.747   1.00 15.11 ?  50  ALA   B H    1 
ATOM   4479 H  HA   . ALA   B 1 50  ? 50.772 -21.913 1.066   1.00 14.86 ?  50  ALA   B HA   1 
ATOM   4480 H  HB1  . ALA   B 1 50  ? 50.724 -21.410 3.344   1.00 15.65 ?  50  ALA   B HB1  1 
ATOM   4481 H  HB2  . ALA   B 1 50  ? 49.405 -22.190 2.922   1.00 15.65 ?  50  ALA   B HB2  1 
ATOM   4482 H  HB3  . ALA   B 1 50  ? 50.574 -22.956 3.679   1.00 15.65 ?  50  ALA   B HB3  1 
ATOM   4483 N  N    . GLY   B 1 51  ? 53.078 -23.738 2.318   1.00 13.62 ?  51  GLY   B N    1 
ATOM   4484 C  CA   . GLY   B 1 51  ? 54.527 -23.823 2.385   1.00 14.35 ?  51  GLY   B CA   1 
ATOM   4485 C  C    . GLY   B 1 51  ? 55.170 -23.783 1.012   1.00 13.67 ?  51  GLY   B C    1 
ATOM   4486 O  O    . GLY   B 1 51  ? 56.220 -23.161 0.820   1.00 14.95 ?  51  GLY   B O    1 
ATOM   4487 H  H    . GLY   B 1 51  ? 52.657 -24.422 2.627   1.00 16.36 ?  51  GLY   B H    1 
ATOM   4488 H  HA2  . GLY   B 1 51  ? 54.875 -23.080 2.908   1.00 17.23 ?  51  GLY   B HA2  1 
ATOM   4489 H  HA3  . GLY   B 1 51  ? 54.787 -24.650 2.825   1.00 17.23 ?  51  GLY   B HA3  1 
ATOM   4490 N  N    . ALA   B 1 52  ? 54.558 -24.461 0.038   1.00 13.68 ?  52  ALA   B N    1 
ATOM   4491 C  CA   . ALA   B 1 52  ? 55.119 -24.468 -1.308  1.00 14.05 ?  52  ALA   B CA   1 
ATOM   4492 C  C    . ALA   B 1 52  ? 55.042 -23.083 -1.951  1.00 13.40 ?  52  ALA   B C    1 
ATOM   4493 O  O    . ALA   B 1 52  ? 56.013 -22.624 -2.573  1.00 14.05 ?  52  ALA   B O    1 
ATOM   4494 C  CB   . ALA   B 1 52  ? 54.395 -25.491 -2.170  1.00 14.80 ?  52  ALA   B CB   1 
ATOM   4495 H  H    . ALA   B 1 52  ? 53.825 -24.905 0.132   1.00 16.43 ?  52  ALA   B H    1 
ATOM   4496 H  HA   . ALA   B 1 52  ? 56.050 -24.720 -1.254  1.00 16.87 ?  52  ALA   B HA   1 
ATOM   4497 H  HB1  . ALA   B 1 52  ? 54.782 -25.478 -3.059  1.00 17.77 ?  52  ALA   B HB1  1 
ATOM   4498 H  HB2  . ALA   B 1 52  ? 54.501 -26.366 -1.773  1.00 17.77 ?  52  ALA   B HB2  1 
ATOM   4499 H  HB3  . ALA   B 1 52  ? 53.454 -25.256 -2.215  1.00 17.77 ?  52  ALA   B HB3  1 
ATOM   4500 N  N    . LEU   B 1 53  ? 53.900 -22.398 -1.822  1.00 13.16 ?  53  LEU   B N    1 
ATOM   4501 C  CA   . LEU   B 1 53  ? 53.787 -21.061 -2.400  1.00 13.19 ?  53  LEU   B CA   1 
ATOM   4502 C  C    . LEU   B 1 53  ? 54.794 -20.114 -1.764  1.00 12.93 ?  53  LEU   B C    1 
ATOM   4503 O  O    . LEU   B 1 53  ? 55.476 -19.355 -2.461  1.00 13.66 ?  53  LEU   B O    1 
ATOM   4504 C  CB   . LEU   B 1 53  ? 52.362 -20.518 -2.240  1.00 13.87 ?  53  LEU   B CB   1 
ATOM   4505 C  CG   . LEU   B 1 53  ? 51.219 -21.251 -2.957  1.00 14.22 ?  53  LEU   B CG   1 
ATOM   4506 C  CD1  . LEU   B 1 53  ? 49.883 -20.601 -2.642  1.00 15.85 ?  53  LEU   B CD1  1 
ATOM   4507 C  CD2  . LEU   B 1 53  ? 51.473 -21.296 -4.457  1.00 16.36 ?  53  LEU   B CD2  1 
ATOM   4508 H  H    . LEU   B 1 53  ? 53.200 -22.676 -1.408  1.00 15.80 ?  53  LEU   B H    1 
ATOM   4509 H  HA   . LEU   B 1 53  ? 53.989 -21.114 -3.348  1.00 15.84 ?  53  LEU   B HA   1 
ATOM   4510 H  HB2  . LEU   B 1 53  ? 52.148 -20.525 -1.297  1.00 16.66 ?  53  LEU   B HB2  1 
ATOM   4511 H  HB3  . LEU   B 1 53  ? 52.353 -19.609 -2.565  1.00 16.66 ?  53  LEU   B HB3  1 
ATOM   4512 H  HG   . LEU   B 1 53  ? 51.181 -22.167 -2.634  1.00 17.07 ?  53  LEU   B HG   1 
ATOM   4513 H  HD11 . LEU   B 1 53  ? 49.179 -21.084 -3.104  1.00 19.03 ?  53  LEU   B HD11 1 
ATOM   4514 H  HD12 . LEU   B 1 53  ? 49.732 -20.634 -1.684  1.00 19.03 ?  53  LEU   B HD12 1 
ATOM   4515 H  HD13 . LEU   B 1 53  ? 49.903 -19.679 -2.943  1.00 19.03 ?  53  LEU   B HD13 1 
ATOM   4516 H  HD21 . LEU   B 1 53  ? 50.716 -21.717 -4.895  1.00 19.64 ?  53  LEU   B HD21 1 
ATOM   4517 H  HD22 . LEU   B 1 53  ? 51.584 -20.393 -4.786  1.00 19.64 ?  53  LEU   B HD22 1 
ATOM   4518 H  HD23 . LEU   B 1 53  ? 52.277 -21.813 -4.626  1.00 19.64 ?  53  LEU   B HD23 1 
ATOM   4519 N  N    . ASN   B 1 54  ? 54.892 -20.136 -0.434  1.00 12.81 ?  54  ASN   B N    1 
ATOM   4520 C  CA   . ASN   B 1 54  ? 55.809 -19.229 0.242   1.00 13.79 ?  54  ASN   B CA   1 
ATOM   4521 C  C    . ASN   B 1 54  ? 57.249 -19.514 -0.153  1.00 14.42 ?  54  ASN   B C    1 
ATOM   4522 O  O    . ASN   B 1 54  ? 58.022 -18.580 -0.398  1.00 14.97 ?  54  ASN   B O    1 
ATOM   4523 C  CB   . ASN   B 1 54  ? 55.645 -19.308 1.752   1.00 14.53 ?  54  ASN   B CB   1 
ATOM   4524 C  CG   . ASN   B 1 54  ? 56.621 -18.392 2.469   1.00 14.23 ?  54  ASN   B CG   1 
ATOM   4525 O  OD1  . ASN   B 1 54  ? 56.653 -17.178 2.223   1.00 14.85 ?  54  ASN   B OD1  1 
ATOM   4526 N  ND2  . ASN   B 1 54  ? 57.452 -18.965 3.330   1.00 16.07 ?  54  ASN   B ND2  1 
ATOM   4527 H  H    . ASN   B 1 54  ? 54.444 -20.654 0.089   1.00 15.38 ?  54  ASN   B H    1 
ATOM   4528 H  HA   . ASN   B 1 54  ? 55.603 -18.320 -0.030  1.00 16.56 ?  54  ASN   B HA   1 
ATOM   4529 H  HB2  . ASN   B 1 54  ? 54.744 -19.032 1.992   1.00 17.45 ?  54  ASN   B HB2  1 
ATOM   4530 H  HB3  . ASN   B 1 54  ? 55.809 -20.214 2.047   1.00 17.45 ?  54  ASN   B HB3  1 
ATOM   4531 H  HD21 . ASN   B 1 54  ? 58.031 -18.489 3.756   1.00 19.29 ?  54  ASN   B HD21 1 
ATOM   4532 H  HD22 . ASN   B 1 54  ? 57.411 -19.812 3.469   1.00 19.29 ?  54  ASN   B HD22 1 
ATOM   4533 N  N    . LYS   B 1 55  ? 57.630 -20.798 -0.221  1.00 14.94 ?  55  LYS   B N    1 
ATOM   4534 C  CA   . LYS   B 1 55  ? 58.986 -21.140 -0.639  1.00 15.95 ?  55  LYS   B CA   1 
ATOM   4535 C  C    . LYS   B 1 55  ? 59.285 -20.591 -2.029  1.00 15.20 ?  55  LYS   B C    1 
ATOM   4536 O  O    . LYS   B 1 55  ? 60.383 -20.075 -2.278  1.00 15.71 ?  55  LYS   B O    1 
ATOM   4537 C  CB   . LYS   B 1 55  ? 59.204 -22.654 -0.595  1.00 17.39 ?  55  LYS   B CB   1 
ATOM   4538 C  CG   . LYS   B 1 55  ? 60.626 -23.069 -0.950  1.00 21.99 ?  55  LYS   B CG   1 
ATOM   4539 C  CD   . LYS   B 1 55  ? 60.831 -24.570 -0.812  1.00 25.88 ?  55  LYS   B CD   1 
ATOM   4540 C  CE   . LYS   B 1 55  ? 60.804 -25.025 0.649   1.00 28.95 ?  55  LYS   B CE   1 
ATOM   4541 N  NZ   . LYS   B 1 55  ? 61.157 -26.459 0.790   1.00 31.04 ?  55  LYS   B NZ   1 
ATOM   4542 H  H    . LYS   B 1 55  ? 57.119 -21.475 -0.043  1.00 17.94 ?  55  LYS   B H    1 
ATOM   4543 H  HA   . LYS   B 1 55  ? 59.608 -20.739 -0.025  1.00 19.15 ?  55  LYS   B HA   1 
ATOM   4544 H  HB2  . LYS   B 1 55  ? 59.013 -22.971 0.302   1.00 20.88 ?  55  LYS   B HB2  1 
ATOM   4545 H  HB3  . LYS   B 1 55  ? 58.603 -23.084 -1.228  1.00 20.88 ?  55  LYS   B HB3  1 
ATOM   4546 H  HG2  . LYS   B 1 55  ? 60.810 -22.825 -1.870  1.00 26.39 ?  55  LYS   B HG2  1 
ATOM   4547 H  HG3  . LYS   B 1 55  ? 61.244 -22.621 -0.353  1.00 26.39 ?  55  LYS   B HG3  1 
ATOM   4548 H  HD2  . LYS   B 1 55  ? 60.122 -25.039 -1.283  1.00 31.07 ?  55  LYS   B HD2  1 
ATOM   4549 H  HD3  . LYS   B 1 55  ? 61.694 -24.813 -1.184  1.00 31.07 ?  55  LYS   B HD3  1 
ATOM   4550 H  HE2  . LYS   B 1 55  ? 61.446 -24.497 1.155   1.00 34.74 ?  55  LYS   B HE2  1 
ATOM   4551 H  HE3  . LYS   B 1 55  ? 59.911 -24.890 1.007   1.00 34.74 ?  55  LYS   B HE3  1 
ATOM   4552 H  HZ1  . LYS   B 1 55  ? 61.122 -26.696 1.648   1.00 37.26 ?  55  LYS   B HZ1  1 
ATOM   4553 H  HZ2  . LYS   B 1 55  ? 60.581 -26.958 0.330   1.00 37.26 ?  55  LYS   B HZ2  1 
ATOM   4554 H  HZ3  . LYS   B 1 55  ? 61.977 -26.602 0.482   1.00 37.26 ?  55  LYS   B HZ3  1 
ATOM   4555 N  N    . ALA   B 1 56  ? 58.310 -20.666 -2.944  1.00 14.64 ?  56  ALA   B N    1 
ATOM   4556 C  CA   . ALA   B 1 56  ? 58.536 -20.155 -4.291  1.00 15.64 ?  56  ALA   B CA   1 
ATOM   4557 C  C    . ALA   B 1 56  ? 58.807 -18.656 -4.283  1.00 14.86 ?  56  ALA   B C    1 
ATOM   4558 O  O    . ALA   B 1 56  ? 59.530 -18.158 -5.154  1.00 16.45 ?  56  ALA   B O    1 
ATOM   4559 C  CB   . ALA   B 1 56  ? 57.350 -20.496 -5.195  1.00 17.11 ?  56  ALA   B CB   1 
ATOM   4560 H  H    . ALA   B 1 56  ? 57.525 -20.988 -2.813  1.00 17.58 ?  56  ALA   B H    1 
ATOM   4561 H  HA   . ALA   B 1 56  ? 59.321 -20.586 -4.660  1.00 18.78 ?  56  ALA   B HA   1 
ATOM   4562 H  HB1  . ALA   B 1 56  ? 57.524 -20.155 -6.089  1.00 20.55 ?  56  ALA   B HB1  1 
ATOM   4563 H  HB2  . ALA   B 1 56  ? 57.248 -21.461 -5.227  1.00 20.55 ?  56  ALA   B HB2  1 
ATOM   4564 H  HB3  . ALA   B 1 56  ? 56.549 -20.089 -4.836  1.00 20.55 ?  56  ALA   B HB3  1 
ATOM   4565 N  N    . THR   B 1 57  ? 58.234 -17.920 -3.326  1.00 15.63 ?  57  THR   B N    1 
ATOM   4566 C  CA   . THR   B 1 57  ? 58.487 -16.486 -3.203  1.00 15.17 ?  57  THR   B CA   1 
ATOM   4567 C  C    . THR   B 1 57  ? 59.738 -16.167 -2.386  1.00 16.04 ?  57  THR   B C    1 
ATOM   4568 O  O    . THR   B 1 57  ? 59.978 -14.995 -2.067  1.00 16.43 ?  57  THR   B O    1 
ATOM   4569 C  CB   . THR   B 1 57  ? 57.293 -15.752 -2.569  1.00 14.17 ?  57  THR   B CB   1 
ATOM   4570 O  OG1  . THR   B 1 57  ? 57.265 -15.989 -1.154  1.00 14.54 ?  57  THR   B OG1  1 
ATOM   4571 C  CG2  . THR   B 1 57  ? 55.968 -16.152 -3.226  1.00 14.30 ?  57  THR   B CG2  1 
ATOM   4572 H  H    . THR   B 1 57  ? 57.676 -18.229 -2.746  1.00 18.77 ?  57  THR   B H    1 
ATOM   4573 H  HA   . THR   B 1 57  ? 58.612 -16.118 -4.092  1.00 18.21 ?  57  THR   B HA   1 
ATOM   4574 H  HB   . THR   B 1 57  ? 57.409 -14.797 -2.715  1.00 17.01 ?  57  THR   B HB   1 
ATOM   4575 H  HG1  . THR   B 1 57  ? 57.167 -16.813 -1.004  1.00 17.46 ?  57  THR   B HG1  1 
ATOM   4576 H  HG21 . THR   B 1 57  ? 55.246 -15.609 -2.878  1.00 17.17 ?  57  THR   B HG21 1 
ATOM   4577 H  HG22 . THR   B 1 57  ? 56.024 -16.024 -4.188  1.00 17.17 ?  57  THR   B HG22 1 
ATOM   4578 H  HG23 . THR   B 1 57  ? 55.778 -17.085 -3.046  1.00 17.17 ?  57  THR   B HG23 1 
ATOM   4579 N  N    . ASN   B 1 58  ? 60.542 -17.171 -2.038  1.00 16.46 ?  58  ASN   B N    1 
ATOM   4580 C  CA   . ASN   B 1 58  ? 61.735 -16.952 -1.220  1.00 20.40 ?  58  ASN   B CA   1 
ATOM   4581 C  C    . ASN   B 1 58  ? 61.381 -16.236 0.085   1.00 17.40 ?  58  ASN   B C    1 
ATOM   4582 O  O    . ASN   B 1 58  ? 62.095 -15.344 0.546   1.00 18.18 ?  58  ASN   B O    1 
ATOM   4583 C  CB   . ASN   B 1 58  ? 62.828 -16.206 -1.991  1.00 29.71 ?  58  ASN   B CB   1 
ATOM   4584 C  CG   . ASN   B 1 58  ? 64.196 -16.360 -1.352  1.00 40.72 ?  58  ASN   B CG   1 
ATOM   4585 O  OD1  . ASN   B 1 58  ? 64.493 -17.385 -0.737  1.00 42.72 ?  58  ASN   B OD1  1 
ATOM   4586 N  ND2  . ASN   B 1 58  ? 65.035 -15.339 -1.491  1.00 48.04 ?  58  ASN   B ND2  1 
ATOM   4587 H  H    . ASN   B 1 58  ? 60.420 -17.997 -2.266  1.00 19.76 ?  58  ASN   B H    1 
ATOM   4588 H  HA   . ASN   B 1 58  ? 62.099 -17.824 -0.990  1.00 24.49 ?  58  ASN   B HA   1 
ATOM   4589 H  HB2  . ASN   B 1 58  ? 62.880 -16.556 -2.897  1.00 35.66 ?  58  ASN   B HB2  1 
ATOM   4590 H  HB3  . ASN   B 1 58  ? 62.615 -15.262 -2.013  1.00 35.66 ?  58  ASN   B HB3  1 
ATOM   4591 H  HD21 . ASN   B 1 58  ? 65.823 -15.379 -1.146  1.00 57.66 ?  58  ASN   B HD21 1 
ATOM   4592 H  HD22 . ASN   B 1 58  ? 64.792 -14.638 -1.925  1.00 57.66 ?  58  ASN   B HD22 1 
ATOM   4593 N  N    . ASN   B 1 59  ? 60.258 -16.632 0.689   1.00 16.25 ?  59  ASN   B N    1 
ATOM   4594 C  CA   . ASN   B 1 59  ? 59.776 -16.158 1.988   1.00 16.08 ?  59  ASN   B CA   1 
ATOM   4595 C  C    . ASN   B 1 59  ? 59.189 -14.751 1.937   1.00 15.82 ?  59  ASN   B C    1 
ATOM   4596 O  O    . ASN   B 1 59  ? 58.766 -14.243 2.977   1.00 15.75 ?  59  ASN   B O    1 
ATOM   4597 C  CB   . ASN   B 1 59  ? 60.847 -16.218 3.093   1.00 17.29 ?  59  ASN   B CB   1 
ATOM   4598 C  CG   . ASN   B 1 59  ? 60.257 -16.407 4.474   1.00 19.36 ?  59  ASN   B CG   1 
ATOM   4599 O  OD1  . ASN   B 1 59  ? 59.439 -17.305 4.697   1.00 19.12 ?  59  ASN   B OD1  1 
ATOM   4600 N  ND2  . ASN   B 1 59  ? 60.686 -15.575 5.417   1.00 20.26 ?  59  ASN   B ND2  1 
ATOM   4601 H  H    . ASN   B 1 59  ? 59.724 -17.216 0.340   1.00 19.51 ?  59  ASN   B H    1 
ATOM   4602 H  HA   . ASN   B 1 59  ? 59.064 -16.756 2.269   1.00 19.30 ?  59  ASN   B HA   1 
ATOM   4603 H  HB2  . ASN   B 1 59  ? 61.444 -16.964 2.928   1.00 20.76 ?  59  ASN   B HB2  1 
ATOM   4604 H  HB3  . ASN   B 1 59  ? 61.345 -15.388 3.102   1.00 20.76 ?  59  ASN   B HB3  1 
ATOM   4605 H  HD21 . ASN   B 1 59  ? 60.383 -15.635 6.223   1.00 24.32 ?  59  ASN   B HD21 1 
ATOM   4606 H  HD22 . ASN   B 1 59  ? 61.256 -14.960 5.223   1.00 24.32 ?  59  ASN   B HD22 1 
ATOM   4607 N  N    . ALA   B 1 60  ? 59.134 -14.106 0.768   1.00 15.53 ?  60  ALA   B N    1 
ATOM   4608 C  CA   . ALA   B 1 60  ? 58.531 -12.775 0.705   1.00 15.13 ?  60  ALA   B CA   1 
ATOM   4609 C  C    . ALA   B 1 60  ? 57.056 -12.807 1.094   1.00 14.72 ?  60  ALA   B C    1 
ATOM   4610 O  O    . ALA   B 1 60  ? 56.559 -11.864 1.719   1.00 15.04 ?  60  ALA   B O    1 
ATOM   4611 C  CB   . ALA   B 1 60  ? 58.703 -12.173 -0.689  1.00 16.56 ?  60  ALA   B CB   1 
ATOM   4612 H  H    . ALA   B 1 60  ? 59.427 -14.410 0.018   1.00 18.65 ?  60  ALA   B H    1 
ATOM   4613 H  HA   . ALA   B 1 60  ? 58.986 -12.199 1.336   1.00 18.17 ?  60  ALA   B HA   1 
ATOM   4614 H  HB1  . ALA   B 1 60  ? 58.299 -11.293 -0.706  1.00 19.88 ?  60  ALA   B HB1  1 
ATOM   4615 H  HB2  . ALA   B 1 60  ? 59.652 -12.106 -0.887  1.00 19.88 ?  60  ALA   B HB2  1 
ATOM   4616 H  HB3  . ALA   B 1 60  ? 58.272 -12.750 -1.339  1.00 19.88 ?  60  ALA   B HB3  1 
ATOM   4617 N  N    . MET   B 1 61  ? 56.348 -13.883 0.749   1.00 14.02 ?  61  MET   B N    1 
ATOM   4618 C  CA   . MET   B 1 61  ? 54.947 -13.998 1.140   1.00 14.02 ?  61  MET   B CA   1 
ATOM   4619 C  C    . MET   B 1 61  ? 54.807 -14.007 2.660   1.00 13.81 ?  61  MET   B C    1 
ATOM   4620 O  O    . MET   B 1 61  ? 53.917 -13.347 3.216   1.00 13.88 ?  61  MET   B O    1 
ATOM   4621 C  CB   . MET   B 1 61  ? 54.364 -15.266 0.517   1.00 14.12 ?  61  MET   B CB   1 
ATOM   4622 C  CG   . MET   B 1 61  ? 52.907 -15.558 0.909   1.00 13.58 ?  61  MET   B CG   1 
ATOM   4623 S  SD   . MET   B 1 61  ? 52.287 -17.074 0.152   1.00 14.18 ?  61  MET   B SD   1 
ATOM   4624 C  CE   . MET   B 1 61  ? 51.991 -16.510 -1.512  1.00 15.09 ?  61  MET   B CE   1 
ATOM   4625 H  H    . MET   B 1 61  ? 56.650 -14.551 0.291   1.00 16.83 ?  61  MET   B H    1 
ATOM   4626 H  HA   . MET   B 1 61  ? 54.455 -13.244 0.780   1.00 16.83 ?  61  MET   B HA   1 
ATOM   4627 H  HB2  . MET   B 1 61  ? 54.401 -15.183 -0.451  1.00 16.95 ?  61  MET   B HB2  1 
ATOM   4628 H  HB3  . MET   B 1 61  ? 54.903 -16.025 0.797   1.00 16.95 ?  61  MET   B HB3  1 
ATOM   4629 H  HG2  . MET   B 1 61  ? 52.845 -15.658 1.871   1.00 16.30 ?  61  MET   B HG2  1 
ATOM   4630 H  HG3  . MET   B 1 61  ? 52.346 -14.818 0.617   1.00 16.30 ?  61  MET   B HG3  1 
ATOM   4631 H  HE1  . MET   B 1 61  ? 51.625 -17.245 -2.032  1.00 18.11 ?  61  MET   B HE1  1 
ATOM   4632 H  HE2  . MET   B 1 61  ? 51.356 -15.774 -1.497  1.00 18.11 ?  61  MET   B HE2  1 
ATOM   4633 H  HE3  . MET   B 1 61  ? 52.827 -16.214 -1.901  1.00 18.11 ?  61  MET   B HE3  1 
ATOM   4634 N  N    . GLN   B 1 62  ? 55.697 -14.715 3.355   1.00 13.17 ?  62  GLN   B N    1 
ATOM   4635 C  CA   . GLN   B 1 62  ? 55.597 -14.790 4.811   1.00 14.21 ?  62  GLN   B CA   1 
ATOM   4636 C  C    . GLN   B 1 62  ? 55.887 -13.441 5.458   1.00 14.31 ?  62  GLN   B C    1 
ATOM   4637 O  O    . GLN   B 1 62  ? 55.202 -13.041 6.409   1.00 15.06 ?  62  GLN   B O    1 
ATOM   4638 C  CB   . GLN   B 1 62  ? 56.543 -15.857 5.362   1.00 14.53 ?  62  GLN   B CB   1 
ATOM   4639 C  CG   . GLN   B 1 62  ? 56.327 -16.136 6.840   1.00 14.89 ?  62  GLN   B CG   1 
ATOM   4640 C  CD   . GLN   B 1 62  ? 54.953 -16.730 7.092   1.00 14.31 ?  62  GLN   B CD   1 
ATOM   4641 O  OE1  . GLN   B 1 62  ? 54.688 -17.873 6.738   1.00 14.60 ?  62  GLN   B OE1  1 
ATOM   4642 N  NE2  . GLN   B 1 62  ? 54.060 -15.937 7.670   1.00 14.26 ?  62  GLN   B NE2  1 
ATOM   4643 H  H    . GLN   B 1 62  ? 56.356 -15.157 3.013   1.00 15.82 ?  62  GLN   B H    1 
ATOM   4644 H  HA   . GLN   B 1 62  ? 54.691 -15.047 5.043   1.00 17.06 ?  62  GLN   B HA   1 
ATOM   4645 H  HB2  . GLN   B 1 62  ? 56.404 -16.687 4.878   1.00 17.44 ?  62  GLN   B HB2  1 
ATOM   4646 H  HB3  . GLN   B 1 62  ? 57.459 -15.557 5.245   1.00 17.44 ?  62  GLN   B HB3  1 
ATOM   4647 H  HG2  . GLN   B 1 62  ? 56.995 -16.771 7.145   1.00 17.87 ?  62  GLN   B HG2  1 
ATOM   4648 H  HG3  . GLN   B 1 62  ? 56.400 -15.308 7.340   1.00 17.87 ?  62  GLN   B HG3  1 
ATOM   4649 H  HE21 . GLN   B 1 62  ? 54.277 -15.136 7.894   1.00 17.12 ?  62  GLN   B HE21 1 
ATOM   4650 H  HE22 . GLN   B 1 62  ? 53.268 -16.229 7.829   1.00 17.12 ?  62  GLN   B HE22 1 
ATOM   4651 N  N    . VAL   B 1 63  ? 56.896 -12.717 4.961   1.00 15.01 ?  63  VAL   B N    1 
ATOM   4652 C  CA   . VAL   B 1 63  ? 57.197 -11.395 5.514   1.00 16.24 ?  63  VAL   B CA   1 
ATOM   4653 C  C    . VAL   B 1 63  ? 56.001 -10.465 5.332   1.00 15.23 ?  63  VAL   B C    1 
ATOM   4654 O  O    . VAL   B 1 63  ? 55.577 -9.771  6.268   1.00 15.77 ?  63  VAL   B O    1 
ATOM   4655 C  CB   . VAL   B 1 63  ? 58.490 -10.827 4.894   1.00 17.49 ?  63  VAL   B CB   1 
ATOM   4656 C  CG1  . VAL   B 1 63  ? 58.724 -9.375  5.346   1.00 17.97 ?  63  VAL   B CG1  1 
ATOM   4657 C  CG2  . VAL   B 1 63  ? 59.683 -11.692 5.281   1.00 18.23 ?  63  VAL   B CG2  1 
ATOM   4658 H  H    . VAL   B 1 63  ? 57.408 -12.970 4.315   1.00 18.02 ?  63  VAL   B H    1 
ATOM   4659 H  HA   . VAL   B 1 63  ? 57.352 -11.491 6.462   1.00 19.50 ?  63  VAL   B HA   1 
ATOM   4660 H  HB   . VAL   B 1 63  ? 58.419 -10.835 3.926   1.00 21.00 ?  63  VAL   B HB   1 
ATOM   4661 H  HG11 . VAL   B 1 63  ? 59.634 -9.114  5.122   1.00 21.57 ?  63  VAL   B HG11 1 
ATOM   4662 H  HG12 . VAL   B 1 63  ? 58.097 -8.792  4.893   1.00 21.57 ?  63  VAL   B HG12 1 
ATOM   4663 H  HG13 . VAL   B 1 63  ? 58.598 -9.317  6.308   1.00 21.57 ?  63  VAL   B HG13 1 
ATOM   4664 H  HG21 . VAL   B 1 63  ? 60.491 -11.309 4.899   1.00 21.89 ?  63  VAL   B HG21 1 
ATOM   4665 H  HG22 . VAL   B 1 63  ? 59.757 -11.711 6.250   1.00 21.89 ?  63  VAL   B HG22 1 
ATOM   4666 H  HG23 . VAL   B 1 63  ? 59.550 -12.589 4.942   1.00 21.89 ?  63  VAL   B HG23 1 
ATOM   4667 N  N    . GLU   B 1 64  ? 55.429 -10.449 4.127   1.00 15.34 ?  64  GLU   B N    1 
ATOM   4668 C  CA   . GLU   B 1 64  ? 54.256 -9.619  3.860   1.00 14.59 ?  64  GLU   B CA   1 
ATOM   4669 C  C    . GLU   B 1 64  ? 53.081 -10.025 4.746   1.00 14.30 ?  64  GLU   B C    1 
ATOM   4670 O  O    . GLU   B 1 64  ? 52.333 -9.170  5.250   1.00 14.91 ?  64  GLU   B O    1 
ATOM   4671 C  CB   . GLU   B 1 64  ? 53.887 -9.767  2.383   1.00 14.60 ?  64  GLU   B CB   1 
ATOM   4672 C  CG   . GLU   B 1 64  ? 52.632 -9.015  1.945   1.00 14.61 ?  64  GLU   B CG   1 
ATOM   4673 C  CD   . GLU   B 1 64  ? 52.093 -9.526  0.621   1.00 15.55 ?  64  GLU   B CD   1 
ATOM   4674 O  OE1  . GLU   B 1 64  ? 52.269 -10.739 0.317   1.00 16.58 ?  64  GLU   B OE1  1 
ATOM   4675 O  OE2  . GLU   B 1 64  ? 51.468 -8.726  -0.114  1.00 16.69 -1 64  GLU   B OE2  1 
ATOM   4676 H  H    . GLU   B 1 64  ? 55.707 -10.906 3.446   1.00 18.41 ?  64  GLU   B H    1 
ATOM   4677 H  HA   . GLU   B 1 64  ? 54.472 -8.690  4.035   1.00 17.51 ?  64  GLU   B HA   1 
ATOM   4678 H  HB2  . GLU   B 1 64  ? 54.626 -9.431  1.844   1.00 17.53 ?  64  GLU   B HB2  1 
ATOM   4679 H  HB3  . GLU   B 1 64  ? 53.750 -10.704 2.192   1.00 17.53 ?  64  GLU   B HB3  1 
ATOM   4680 H  HG2  . GLU   B 1 64  ? 51.936 -9.123  2.614   1.00 17.54 ?  64  GLU   B HG2  1 
ATOM   4681 H  HG3  . GLU   B 1 64  ? 52.846 -8.072  1.844   1.00 17.54 ?  64  GLU   B HG3  1 
ATOM   4682 N  N    . SER   B 1 65  ? 52.890 -11.330 4.924   1.00 13.85 ?  65  SER   B N    1 
ATOM   4683 C  CA   . SER   B 1 65  ? 51.780 -11.844 5.723   1.00 14.21 ?  65  SER   B CA   1 
ATOM   4684 C  C    . SER   B 1 65  ? 51.914 -11.455 7.193   1.00 14.50 ?  65  SER   B C    1 
ATOM   4685 O  O    . SER   B 1 65  ? 50.923 -11.069 7.828   1.00 14.66 ?  65  SER   B O    1 
ATOM   4686 C  CB   . SER   B 1 65  ? 51.696 -13.365 5.588   1.00 13.78 ?  65  SER   B CB   1 
ATOM   4687 O  OG   . SER   B 1 65  ? 51.341 -13.764 4.274   1.00 14.05 ?  65  SER   B OG   1 
ATOM   4688 H  H    . SER   B 1 65  ? 53.396 -11.951 4.594   1.00 16.63 ?  65  SER   B H    1 
ATOM   4689 H  HA   . SER   B 1 65  ? 50.951 -11.470 5.388   1.00 17.05 ?  65  SER   B HA   1 
ATOM   4690 H  HB2  . SER   B 1 65  ? 52.556 -13.751 5.805   1.00 16.55 ?  65  SER   B HB2  1 
ATOM   4691 H  HB3  . SER   B 1 65  ? 51.021 -13.697 6.205   1.00 16.55 ?  65  SER   B HB3  1 
ATOM   4692 H  HG   . SER   B 1 65  ? 51.911 -13.471 3.722   1.00 16.87 ?  65  SER   B HG   1 
ATOM   4693 N  N    . ASP   B 1 66  ? 53.124 -11.553 7.758   1.00 14.45 ?  66  ASP   B N    1 
ATOM   4694 C  CA   . ASP   B 1 66  ? 53.320 -11.156 9.152   1.00 14.61 ?  66  ASP   B CA   1 
ATOM   4695 C  C    . ASP   B 1 66  ? 52.997 -9.682  9.358   1.00 15.00 ?  66  ASP   B C    1 
ATOM   4696 O  O    . ASP   B 1 66  ? 52.416 -9.299  10.382  1.00 15.47 ?  66  ASP   B O    1 
ATOM   4697 C  CB   . ASP   B 1 66  ? 54.754 -11.460 9.597   1.00 16.60 ?  66  ASP   B CB   1 
ATOM   4698 C  CG   . ASP   B 1 66  ? 55.026 -12.950 9.750   1.00 18.16 ?  66  ASP   B CG   1 
ATOM   4699 O  OD1  . ASP   B 1 66  ? 54.075 -13.762 9.651   1.00 18.69 ?  66  ASP   B OD1  1 
ATOM   4700 O  OD2  . ASP   B 1 66  ? 56.203 -13.311 9.977   1.00 21.56 -1 66  ASP   B OD2  1 
ATOM   4701 H  H    . ASP   B 1 66  ? 53.826 -11.842 7.361   1.00 17.35 ?  66  ASP   B H    1 
ATOM   4702 H  HA   . ASP   B 1 66  ? 52.717 -11.667 9.713   1.00 17.54 ?  66  ASP   B HA   1 
ATOM   4703 H  HB2  . ASP   B 1 66  ? 55.369 -11.115 8.933   1.00 19.93 ?  66  ASP   B HB2  1 
ATOM   4704 H  HB3  . ASP   B 1 66  ? 54.914 -11.034 10.453  1.00 19.93 ?  66  ASP   B HB3  1 
ATOM   4705 N  N    . ASP   B 1 67  ? 53.370 -8.839  8.402   1.00 14.83 ?  67  ASP   B N    1 
ATOM   4706 C  CA   . ASP   B 1 67  ? 53.026 -7.425  8.505   1.00 15.29 ?  67  ASP   B CA   1 
ATOM   4707 C  C    . ASP   B 1 67  ? 51.515 -7.207  8.419   1.00 15.32 ?  67  ASP   B C    1 
ATOM   4708 O  O    . ASP   B 1 67  ? 50.956 -6.384  9.157   1.00 16.04 ?  67  ASP   B O    1 
ATOM   4709 C  CB   . ASP   B 1 67  ? 53.738 -6.654  7.406   1.00 16.60 ?  67  ASP   B CB   1 
ATOM   4710 C  CG   . ASP   B 1 67  ? 53.321 -5.213  7.370   1.00 18.05 ?  67  ASP   B CG   1 
ATOM   4711 O  OD1  . ASP   B 1 67  ? 53.809 -4.415  8.207   1.00 19.25 ?  67  ASP   B OD1  1 
ATOM   4712 O  OD2  . ASP   B 1 67  ? 52.475 -4.882  6.524   1.00 19.71 -1 67  ASP   B OD2  1 
ATOM   4713 H  H    . ASP   B 1 67  ? 53.822 -9.048  7.703   1.00 17.80 ?  67  ASP   B H    1 
ATOM   4714 H  HA   . ASP   B 1 67  ? 53.333 -7.079  9.361   1.00 18.36 ?  67  ASP   B HA   1 
ATOM   4715 H  HB2  . ASP   B 1 67  ? 54.696 -6.684  7.563   1.00 19.93 ?  67  ASP   B HB2  1 
ATOM   4716 H  HB3  . ASP   B 1 67  ? 53.531 -7.058  6.548   1.00 19.93 ?  67  ASP   B HB3  1 
ATOM   4717 N  N    . TYR   B 1 68  ? 50.838 -7.935  7.524   1.00 14.43 ?  68  TYR   B N    1 
ATOM   4718 C  CA   . TYR   B 1 68  ? 49.381 -7.855  7.450   1.00 15.67 ?  68  TYR   B CA   1 
ATOM   4719 C  C    . TYR   B 1 68  ? 48.744 -8.212  8.790   1.00 15.19 ?  68  TYR   B C    1 
ATOM   4720 O  O    . TYR   B 1 68  ? 47.811 -7.540  9.245   1.00 15.80 ?  68  TYR   B O    1 
ATOM   4721 C  CB   . TYR   B 1 68  ? 48.852 -8.778  6.346   1.00 16.65 ?  68  TYR   B CB   1 
ATOM   4722 C  CG   . TYR   B 1 68  ? 47.345 -8.932  6.398   1.00 17.25 ?  68  TYR   B CG   1 
ATOM   4723 C  CD1  . TYR   B 1 68  ? 46.752 -9.892  7.213   1.00 18.78 ?  68  TYR   B CD1  1 
ATOM   4724 C  CD2  . TYR   B 1 68  ? 46.515 -8.102  5.663   1.00 18.20 ?  68  TYR   B CD2  1 
ATOM   4725 C  CE1  . TYR   B 1 68  ? 45.386 -10.021 7.294   1.00 19.95 ?  68  TYR   B CE1  1 
ATOM   4726 C  CE2  . TYR   B 1 68  ? 45.131 -8.232  5.736   1.00 19.37 ?  68  TYR   B CE2  1 
ATOM   4727 C  CZ   . TYR   B 1 68  ? 44.584 -9.190  6.556   1.00 19.47 ?  68  TYR   B CZ   1 
ATOM   4728 O  OH   . TYR   B 1 68  ? 43.215 -9.324  6.651   1.00 21.00 ?  68  TYR   B OH   1 
ATOM   4729 H  H    . TYR   B 1 68  ? 51.197 -8.478  6.960   1.00 17.33 ?  68  TYR   B H    1 
ATOM   4730 H  HA   . TYR   B 1 68  ? 49.131 -6.943  7.230   1.00 18.82 ?  68  TYR   B HA   1 
ATOM   4731 H  HB2  . TYR   B 1 68  ? 49.088 -8.405  5.484   1.00 19.99 ?  68  TYR   B HB2  1 
ATOM   4732 H  HB3  . TYR   B 1 68  ? 49.253 -9.655  6.452   1.00 19.99 ?  68  TYR   B HB3  1 
ATOM   4733 H  HD1  . TYR   B 1 68  ? 47.295 -10.460 7.718   1.00 22.55 ?  68  TYR   B HD1  1 
ATOM   4734 H  HD2  . TYR   B 1 68  ? 46.890 -7.446  5.124   1.00 21.85 ?  68  TYR   B HD2  1 
ATOM   4735 H  HE1  . TYR   B 1 68  ? 45.007 -10.678 7.834   1.00 23.95 ?  68  TYR   B HE1  1 
ATOM   4736 H  HE2  . TYR   B 1 68  ? 44.576 -7.670  5.244   1.00 23.26 ?  68  TYR   B HE2  1 
ATOM   4737 H  HH   . TYR   B 1 68  ? 42.827 -8.770  6.142   1.00 25.21 ?  68  TYR   B HH   1 
ATOM   4738 N  N    . ILE   B 1 69  ? 49.232 -9.274  9.435   1.00 15.16 ?  69  ILE   B N    1 
ATOM   4739 C  CA   . ILE   B 1 69  ? 48.662 -9.712  10.708  1.00 15.89 ?  69  ILE   B CA   1 
ATOM   4740 C  C    . ILE   B 1 69  ? 48.916 -8.672  11.796  1.00 15.57 ?  69  ILE   B C    1 
ATOM   4741 O  O    . ILE   B 1 69  ? 48.042 -8.389  12.624  1.00 15.87 ?  69  ILE   B O    1 
ATOM   4742 C  CB   . ILE   B 1 69  ? 49.232 -11.096 11.087  1.00 16.98 ?  69  ILE   B CB   1 
ATOM   4743 C  CG1  . ILE   B 1 69  ? 48.693 -12.188 10.158  1.00 17.76 ?  69  ILE   B CG1  1 
ATOM   4744 C  CG2  . ILE   B 1 69  ? 48.935 -11.434 12.543  1.00 17.84 ?  69  ILE   B CG2  1 
ATOM   4745 C  CD1  . ILE   B 1 69  ? 47.206 -12.475 10.310  1.00 18.56 ?  69  ILE   B CD1  1 
ATOM   4746 H  H    . ILE   B 1 69  ? 49.884 -9.755  9.155   1.00 18.20 ?  69  ILE   B H    1 
ATOM   4747 H  HA   . ILE   B 1 69  ? 47.703 -9.802  10.608  1.00 19.07 ?  69  ILE   B HA   1 
ATOM   4748 H  HB   . ILE   B 1 69  ? 50.196 -11.063 10.979  1.00 20.38 ?  69  ILE   B HB   1 
ATOM   4749 H  HG12 . ILE   B 1 69  ? 48.847 -11.918 9.239   1.00 21.32 ?  69  ILE   B HG12 1 
ATOM   4750 H  HG13 . ILE   B 1 69  ? 49.171 -13.014 10.339  1.00 21.32 ?  69  ILE   B HG13 1 
ATOM   4751 H  HG21 . ILE   B 1 69  ? 49.078 -12.385 12.675  1.00 21.42 ?  69  ILE   B HG21 1 
ATOM   4752 H  HG22 . ILE   B 1 69  ? 49.533 -10.930 13.115  1.00 21.42 ?  69  ILE   B HG22 1 
ATOM   4753 H  HG23 . ILE   B 1 69  ? 48.013 -11.208 12.736  1.00 21.42 ?  69  ILE   B HG23 1 
ATOM   4754 H  HD11 . ILE   B 1 69  ? 46.957 -13.186 9.700   1.00 22.28 ?  69  ILE   B HD11 1 
ATOM   4755 H  HD12 . ILE   B 1 69  ? 47.022 -12.751 11.224  1.00 22.28 ?  69  ILE   B HD12 1 
ATOM   4756 H  HD13 . ILE   B 1 69  ? 46.700 -11.674 10.102  1.00 22.28 ?  69  ILE   B HD13 1 
ATOM   4757 N  N    . ALA   B 1 70  ? 50.112 -8.082  11.816  1.00 15.64 ?  70  ALA   B N    1 
ATOM   4758 C  CA   . ALA   B 1 70  ? 50.400 -7.050  12.809  1.00 14.85 ?  70  ALA   B CA   1 
ATOM   4759 C  C    . ALA   B 1 70  ? 49.405 -5.898  12.710  1.00 15.47 ?  70  ALA   B C    1 
ATOM   4760 O  O    . ALA   B 1 70  ? 48.958 -5.356  13.728  1.00 16.61 ?  70  ALA   B O    1 
ATOM   4761 C  CB   . ALA   B 1 70  ? 51.824 -6.531  12.632  1.00 15.90 ?  70  ALA   B CB   1 
ATOM   4762 H  H    . ALA   B 1 70  ? 50.756 -8.262  11.280  1.00 18.78 ?  70  ALA   B H    1 
ATOM   4763 H  HA   . ALA   B 1 70  ? 50.332 -7.433  13.698  1.00 17.83 ?  70  ALA   B HA   1 
ATOM   4764 H  HB1  . ALA   B 1 70  ? 52.013 -5.876  13.323  1.00 19.09 ?  70  ALA   B HB1  1 
ATOM   4765 H  HB2  . ALA   B 1 70  ? 52.446 -7.275  12.708  1.00 19.09 ?  70  ALA   B HB2  1 
ATOM   4766 H  HB3  . ALA   B 1 70  ? 51.908 -6.123  11.756  1.00 19.09 ?  70  ALA   B HB3  1 
ATOM   4767 N  N    . THR   B 1 71  ? 49.036 -5.518  11.487  1.00 16.05 ?  71  THR   B N    1 
ATOM   4768 C  CA   . THR   B 1 71  ? 48.134 -4.392  11.275  1.00 17.23 ?  71  THR   B CA   1 
ATOM   4769 C  C    . THR   B 1 71  ? 46.667 -4.769  11.483  1.00 17.58 ?  71  THR   B C    1 
ATOM   4770 O  O    . THR   B 1 71  ? 45.891 -3.967  12.019  1.00 19.44 ?  71  THR   B O    1 
ATOM   4771 C  CB   . THR   B 1 71  ? 48.359 -3.831  9.871   1.00 18.89 ?  71  THR   B CB   1 
ATOM   4772 O  OG1  . THR   B 1 71  ? 49.688 -3.303  9.782   1.00 21.25 ?  71  THR   B OG1  1 
ATOM   4773 C  CG2  . THR   B 1 71  ? 47.347 -2.741  9.549   1.00 19.86 ?  71  THR   B CG2  1 
ATOM   4774 H  H    . THR   B 1 71  ? 49.295 -5.903  10.764  1.00 19.27 ?  71  THR   B H    1 
ATOM   4775 H  HA   . THR   B 1 71  ? 48.352 -3.695  11.910  1.00 20.69 ?  71  THR   B HA   1 
ATOM   4776 H  HB   . THR   B 1 71  ? 48.260 -4.540  9.217   1.00 22.67 ?  71  THR   B HB   1 
ATOM   4777 H  HG1  . THR   B 1 71  ? 49.823 -2.978  9.015   1.00 25.51 ?  71  THR   B HG1  1 
ATOM   4778 H  HG21 . THR   B 1 71  ? 47.647 -2.224  8.784   1.00 23.84 ?  71  THR   B HG21 1 
ATOM   4779 H  HG22 . THR   B 1 71  ? 46.485 -3.134  9.343   1.00 23.84 ?  71  THR   B HG22 1 
ATOM   4780 H  HG23 . THR   B 1 71  ? 47.250 -2.143  10.308  1.00 23.84 ?  71  THR   B HG23 1 
ATOM   4781 N  N    . ASN   B 1 72  ? 46.267 -5.976  11.079  1.00 17.20 ?  72  ASN   B N    1 
ATOM   4782 C  CA   . ASN   B 1 72  ? 44.861 -6.323  10.952  1.00 17.52 ?  72  ASN   B CA   1 
ATOM   4783 C  C    . ASN   B 1 72  ? 44.381 -7.425  11.884  1.00 18.16 ?  72  ASN   B C    1 
ATOM   4784 O  O    . ASN   B 1 72  ? 43.163 -7.577  12.044  1.00 19.28 ?  72  ASN   B O    1 
ATOM   4785 C  CB   . ASN   B 1 72  ? 44.551 -6.741  9.508   1.00 18.71 ?  72  ASN   B CB   1 
ATOM   4786 C  CG   . ASN   B 1 72  ? 44.830 -5.643  8.523   1.00 19.71 ?  72  ASN   B CG   1 
ATOM   4787 O  OD1  . ASN   B 1 72  ? 45.843 -5.655  7.816   1.00 20.65 ?  72  ASN   B OD1  1 
ATOM   4788 N  ND2  . ASN   B 1 72  ? 43.944 -4.663  8.487   1.00 21.20 ?  72  ASN   B ND2  1 
ATOM   4789 H  H    . ASN   B 1 72  ? 46.802 -6.620  10.874  1.00 20.65 ?  72  ASN   B H    1 
ATOM   4790 H  HA   . ASN   B 1 72  ? 44.333 -5.534  11.144  1.00 21.03 ?  72  ASN   B HA   1 
ATOM   4791 H  HB2  . ASN   B 1 72  ? 45.107 -7.503  9.274   1.00 22.46 ?  72  ASN   B HB2  1 
ATOM   4792 H  HB3  . ASN   B 1 72  ? 43.616 -6.977  9.440   1.00 22.46 ?  72  ASN   B HB3  1 
ATOM   4793 H  HD21 . ASN   B 1 72  ? 44.050 -4.004  7.945   1.00 25.44 ?  72  ASN   B HD21 1 
ATOM   4794 H  HD22 . ASN   B 1 72  ? 43.250 -4.689  8.998   1.00 25.44 ?  72  ASN   B HD22 1 
ATOM   4795 N  N    . GLY   B 1 73  ? 45.279 -8.185  12.504  1.00 17.38 ?  73  GLY   B N    1 
ATOM   4796 C  CA   . GLY   B 1 73  ? 44.888 -9.337  13.281  1.00 16.47 ?  73  GLY   B CA   1 
ATOM   4797 C  C    . GLY   B 1 73  ? 44.547 -10.527 12.411  1.00 15.29 ?  73  GLY   B C    1 
ATOM   4798 O  O    . GLY   B 1 73  ? 44.554 -10.452 11.179  1.00 15.63 ?  73  GLY   B O    1 
ATOM   4799 H  H    . GLY   B 1 73  ? 46.129 -8.052  12.482  1.00 20.86 ?  73  GLY   B H    1 
ATOM   4800 H  HA2  . GLY   B 1 73  ? 45.610 -9.588  13.875  1.00 19.77 ?  73  GLY   B HA2  1 
ATOM   4801 H  HA3  . GLY   B 1 73  ? 44.109 -9.114  13.818  1.00 19.77 ?  73  GLY   B HA3  1 
ATOM   4802 N  N    . PRO   B 1 74  ? 44.224 -11.646 13.051  1.00 16.38 ?  74  PRO   B N    1 
ATOM   4803 C  CA   . PRO   B 1 74  ? 43.970 -12.883 12.309  1.00 15.67 ?  74  PRO   B CA   1 
ATOM   4804 C  C    . PRO   B 1 74  ? 42.672 -12.836 11.517  1.00 15.16 ?  74  PRO   B C    1 
ATOM   4805 O  O    . PRO   B 1 74  ? 41.733 -12.103 11.843  1.00 16.28 ?  74  PRO   B O    1 
ATOM   4806 C  CB   . PRO   B 1 74  ? 43.896 -13.938 13.419  1.00 16.65 ?  74  PRO   B CB   1 
ATOM   4807 C  CG   . PRO   B 1 74  ? 43.446 -13.181 14.623  1.00 18.22 ?  74  PRO   B CG   1 
ATOM   4808 C  CD   . PRO   B 1 74  ? 44.103 -11.838 14.507  1.00 17.58 ?  74  PRO   B CD   1 
ATOM   4809 H  HA   . PRO   B 1 74  ? 44.718 -13.081 11.716  1.00 18.81 ?  74  PRO   B HA   1 
ATOM   4810 H  HB2  . PRO   B 1 74  ? 43.251 -14.619 13.178  1.00 19.98 ?  74  PRO   B HB2  1 
ATOM   4811 H  HB3  . PRO   B 1 74  ? 44.773 -14.327 13.564  1.00 19.98 ?  74  PRO   B HB3  1 
ATOM   4812 H  HG2  . PRO   B 1 74  ? 42.480 -13.091 14.610  1.00 21.87 ?  74  PRO   B HG2  1 
ATOM   4813 H  HG3  . PRO   B 1 74  ? 43.739 -13.637 15.425  1.00 21.87 ?  74  PRO   B HG3  1 
ATOM   4814 H  HD2  . PRO   B 1 74  ? 43.538 -11.149 14.900  1.00 21.11 ?  74  PRO   B HD2  1 
ATOM   4815 H  HD3  . PRO   B 1 74  ? 44.981 -11.850 14.919  1.00 21.11 ?  74  PRO   B HD3  1 
ATOM   4816 N  N    . LEU   B 1 75  ? 42.637 -13.634 10.454  1.00 14.24 ?  75  LEU   B N    1 
ATOM   4817 C  CA   . LEU   B 1 75  ? 41.424 -13.865 9.689   1.00 14.49 ?  75  LEU   B CA   1 
ATOM   4818 C  C    . LEU   B 1 75  ? 40.459 -14.736 10.493  1.00 14.71 ?  75  LEU   B C    1 
ATOM   4819 O  O    . LEU   B 1 75  ? 40.796 -15.274 11.546  1.00 15.67 ?  75  LEU   B O    1 
ATOM   4820 C  CB   . LEU   B 1 75  ? 41.761 -14.568 8.375   1.00 14.59 ?  75  LEU   B CB   1 
ATOM   4821 C  CG   . LEU   B 1 75  ? 42.597 -13.809 7.341   1.00 15.63 ?  75  LEU   B CG   1 
ATOM   4822 C  CD1  . LEU   B 1 75  ? 42.759 -14.607 6.060   1.00 16.82 ?  75  LEU   B CD1  1 
ATOM   4823 C  CD2  . LEU   B 1 75  ? 42.018 -12.457 7.035   1.00 19.65 ?  75  LEU   B CD2  1 
ATOM   4824 H  H    . LEU   B 1 75  ? 43.321 -14.064 10.154  1.00 17.10 ?  75  LEU   B H    1 
ATOM   4825 H  HA   . LEU   B 1 75  ? 40.993 -13.018 9.496   1.00 17.40 ?  75  LEU   B HA   1 
ATOM   4826 H  HB2  . LEU   B 1 75  ? 42.249 -15.381 8.590   1.00 17.52 ?  75  LEU   B HB2  1 
ATOM   4827 H  HB3  . LEU   B 1 75  ? 40.927 -14.808 7.943   1.00 17.52 ?  75  LEU   B HB3  1 
ATOM   4828 H  HG   . LEU   B 1 75  ? 43.485 -13.670 7.707   1.00 18.76 ?  75  LEU   B HG   1 
ATOM   4829 H  HD11 . LEU   B 1 75  ? 43.302 -14.099 5.434   1.00 20.19 ?  75  LEU   B HD11 1 
ATOM   4830 H  HD12 . LEU   B 1 75  ? 43.196 -15.451 6.261   1.00 20.19 ?  75  LEU   B HD12 1 
ATOM   4831 H  HD13 . LEU   B 1 75  ? 41.884 -14.774 5.675   1.00 20.19 ?  75  LEU   B HD13 1 
ATOM   4832 H  HD21 . LEU   B 1 75  ? 42.515 -12.058 6.306   1.00 23.59 ?  75  LEU   B HD21 1 
ATOM   4833 H  HD22 . LEU   B 1 75  ? 41.087 -12.563 6.785   1.00 23.59 ?  75  LEU   B HD22 1 
ATOM   4834 H  HD23 . LEU   B 1 75  ? 42.086 -11.899 7.827   1.00 23.59 ?  75  LEU   B HD23 1 
ATOM   4835 N  N    . LYS   B 1 76  ? 39.233 -14.855 9.982   1.00 16.04 ?  76  LYS   B N    1 
ATOM   4836 C  CA   . LYS   B 1 76  ? 38.248 -15.813 10.472  1.00 17.95 ?  76  LYS   B CA   1 
ATOM   4837 C  C    . LYS   B 1 76  ? 38.323 -17.073 9.619   1.00 15.59 ?  76  LYS   B C    1 
ATOM   4838 O  O    . LYS   B 1 76  ? 38.596 -17.002 8.419   1.00 15.23 ?  76  LYS   B O    1 
ATOM   4839 C  CB   . LYS   B 1 76  ? 36.826 -15.249 10.323  1.00 21.02 ?  76  LYS   B CB   1 
ATOM   4840 C  CG   . LYS   B 1 76  ? 36.580 -13.838 10.875  1.00 23.19 ?  76  LYS   B CG   1 
ATOM   4841 C  CD   . LYS   B 1 76  ? 35.152 -13.349 10.561  1.00 25.06 ?  76  LYS   B CD   1 
ATOM   4842 C  CE   . LYS   B 1 76  ? 34.860 -11.994 11.193  1.00 27.46 ?  76  LYS   B CE   1 
ATOM   4843 N  NZ   . LYS   B 1 76  ? 33.563 -11.410 10.749  1.00 28.36 ?  76  LYS   B NZ   1 
ATOM   4844 H  H    . LYS   B 1 76  ? 38.943 -14.376 9.332   1.00 19.26 ?  76  LYS   B H    1 
ATOM   4845 H  HA   . LYS   B 1 76  ? 38.420 -16.041 11.402  1.00 21.55 ?  76  LYS   B HA   1 
ATOM   4846 H  HB2  . LYS   B 1 76  ? 36.611 -15.232 9.377   1.00 25.23 ?  76  LYS   B HB2  1 
ATOM   4847 H  HB3  . LYS   B 1 76  ? 36.217 -15.849 10.779  1.00 25.23 ?  76  LYS   B HB3  1 
ATOM   4848 H  HG2  . LYS   B 1 76  ? 36.695 -13.848 11.838  1.00 27.83 ?  76  LYS   B HG2  1 
ATOM   4849 H  HG3  . LYS   B 1 76  ? 37.210 -13.221 10.469  1.00 27.83 ?  76  LYS   B HG3  1 
ATOM   4850 H  HD2  . LYS   B 1 76  ? 35.049 -13.264 9.599   1.00 30.09 ?  76  LYS   B HD2  1 
ATOM   4851 H  HD3  . LYS   B 1 76  ? 34.512 -13.990 10.909  1.00 30.09 ?  76  LYS   B HD3  1 
ATOM   4852 H  HE2  . LYS   B 1 76  ? 34.829 -12.097 12.157  1.00 32.97 ?  76  LYS   B HE2  1 
ATOM   4853 H  HE3  . LYS   B 1 76  ? 35.567 -11.375 10.950  1.00 32.97 ?  76  LYS   B HE3  1 
ATOM   4854 H  HZ1  . LYS   B 1 76  ? 33.433 -10.619 11.142  1.00 34.04 ?  76  LYS   B HZ1  1 
ATOM   4855 H  HZ2  . LYS   B 1 76  ? 33.565 -11.293 9.866   1.00 34.04 ?  76  LYS   B HZ2  1 
ATOM   4856 H  HZ3  . LYS   B 1 76  ? 32.891 -11.951 10.967  1.00 34.04 ?  76  LYS   B HZ3  1 
ATOM   4857 N  N    . VAL   B 1 77  ? 38.072 -18.236 10.237  1.00 16.18 ?  77  VAL   B N    1 
ATOM   4858 C  CA   . VAL   B 1 77  ? 37.854 -19.442 9.442   1.00 16.30 ?  77  VAL   B CA   1 
ATOM   4859 C  C    . VAL   B 1 77  ? 36.666 -19.193 8.526   1.00 14.64 ?  77  VAL   B C    1 
ATOM   4860 O  O    . VAL   B 1 77  ? 35.599 -18.761 8.978   1.00 14.44 ?  77  VAL   B O    1 
ATOM   4861 C  CB   . VAL   B 1 77  ? 37.639 -20.669 10.340  1.00 18.05 ?  77  VAL   B CB   1 
ATOM   4862 C  CG1  . VAL   B 1 77  ? 37.324 -21.888 9.483   1.00 18.82 ?  77  VAL   B CG1  1 
ATOM   4863 C  CG2  . VAL   B 1 77  ? 38.866 -20.925 11.222  1.00 19.79 ?  77  VAL   B CG2  1 
ATOM   4864 H  H    . VAL   B 1 77  ? 38.037 -18.350 11.086  1.00 19.43 ?  77  VAL   B H    1 
ATOM   4865 H  HA   . VAL   B 1 77  ? 38.632 -19.608 8.887   1.00 19.56 ?  77  VAL   B HA   1 
ATOM   4866 H  HB   . VAL   B 1 77  ? 36.876 -20.508 10.919  1.00 21.66 ?  77  VAL   B HB   1 
ATOM   4867 H  HG11 . VAL   B 1 77  ? 37.376 -22.683 10.036  1.00 22.59 ?  77  VAL   B HG11 1 
ATOM   4868 H  HG12 . VAL   B 1 77  ? 36.425 -21.801 9.121   1.00 22.59 ?  77  VAL   B HG12 1 
ATOM   4869 H  HG13 . VAL   B 1 77  ? 37.967 -21.942 8.762   1.00 22.59 ?  77  VAL   B HG13 1 
ATOM   4870 H  HG21 . VAL   B 1 77  ? 38.709 -21.724 11.748  1.00 23.75 ?  77  VAL   B HG21 1 
ATOM   4871 H  HG22 . VAL   B 1 77  ? 39.638 -21.046 10.652  1.00 23.75 ?  77  VAL   B HG22 1 
ATOM   4872 H  HG23 . VAL   B 1 77  ? 38.994 -20.162 11.804  1.00 23.75 ?  77  VAL   B HG23 1 
ATOM   4873 N  N    . GLY   B 1 78  ? 36.854 -19.449 7.230   1.00 14.20 ?  78  GLY   B N    1 
ATOM   4874 C  CA   . GLY   B 1 78  ? 35.876 -19.132 6.219   1.00 13.60 ?  78  GLY   B CA   1 
ATOM   4875 C  C    . GLY   B 1 78  ? 36.119 -17.818 5.514   1.00 13.46 ?  78  GLY   B C    1 
ATOM   4876 O  O    . GLY   B 1 78  ? 35.424 -17.529 4.530   1.00 14.05 ?  78  GLY   B O    1 
ATOM   4877 H  H    . GLY   B 1 78  ? 37.562 -19.818 6.915   1.00 17.05 ?  78  GLY   B H    1 
ATOM   4878 H  HA2  . GLY   B 1 78  ? 35.871 -19.831 5.551   1.00 16.33 ?  78  GLY   B HA2  1 
ATOM   4879 H  HA3  . GLY   B 1 78  ? 34.996 -19.090 6.625   1.00 16.33 ?  78  GLY   B HA3  1 
ATOM   4880 N  N    . GLY   B 1 79  ? 37.074 -17.019 5.995   1.00 13.94 ?  79  GLY   B N    1 
ATOM   4881 C  CA   . GLY   B 1 79  ? 37.367 -15.720 5.427   1.00 13.77 ?  79  GLY   B CA   1 
ATOM   4882 C  C    . GLY   B 1 79  ? 38.602 -15.724 4.541   1.00 12.98 ?  79  GLY   B C    1 
ATOM   4883 O  O    . GLY   B 1 79  ? 39.224 -16.755 4.289   1.00 13.54 ?  79  GLY   B O    1 
ATOM   4884 H  H    . GLY   B 1 79  ? 37.575 -17.216 6.661   1.00 16.73 ?  79  GLY   B H    1 
ATOM   4885 H  HA2  . GLY   B 1 79  ? 36.611 -15.421 4.892   1.00 16.53 ?  79  GLY   B HA2  1 
ATOM   4886 H  HA3  . GLY   B 1 79  ? 37.507 -15.080 6.139   1.00 16.53 ?  79  GLY   B HA3  1 
ATOM   4887 N  N    . SER   B 1 80  ? 38.982 -14.527 4.083   1.00 13.34 ?  80  SER   B N    1 
ATOM   4888 C  CA   . SER   B 1 80  ? 40.092 -14.389 3.145   1.00 13.36 ?  80  SER   B CA   1 
ATOM   4889 C  C    . SER   B 1 80  ? 40.659 -12.979 3.204   1.00 13.20 ?  80  SER   B C    1 
ATOM   4890 O  O    . SER   B 1 80  ? 40.041 -12.055 3.742   1.00 14.65 ?  80  SER   B O    1 
ATOM   4891 C  CB   . SER   B 1 80  ? 39.650 -14.700 1.706   1.00 13.21 ?  80  SER   B CB   1 
ATOM   4892 O  OG   . SER   B 1 80  ? 38.795 -13.679 1.200   1.00 14.35 ?  80  SER   B OG   1 
ATOM   4893 H  H    . SER   B 1 80  ? 38.608 -13.785 4.298   1.00 16.01 ?  80  SER   B H    1 
ATOM   4894 H  HA   . SER   B 1 80  ? 40.788 -15.008 3.398   1.00 16.04 ?  80  SER   B HA   1 
ATOM   4895 H  HB2  . SER   B 1 80  ? 40.437 -14.756 1.139   1.00 15.86 ?  80  SER   B HB2  1 
ATOM   4896 H  HB3  . SER   B 1 80  ? 39.174 -15.544 1.695   1.00 15.86 ?  80  SER   B HB3  1 
ATOM   4897 H  HG   . SER   B 1 80  ? 38.106 -13.616 1.684   1.00 17.23 ?  80  SER   B HG   1 
ATOM   4898 N  N    . CYS   B 1 81  ? 41.843 -12.828 2.620   1.00 13.17 ?  81  CYS   B N    1 
ATOM   4899 C  CA   . CYS   B 1 81  ? 42.397 -11.520 2.308   1.00 12.93 ?  81  CYS   B CA   1 
ATOM   4900 C  C    . CYS   B 1 81  ? 43.168 -11.612 1.002   1.00 12.70 ?  81  CYS   B C    1 
ATOM   4901 O  O    . CYS   B 1 81  ? 43.686 -12.672 0.638   1.00 13.43 ?  81  CYS   B O    1 
ATOM   4902 C  CB   . CYS   B 1 81  ? 43.283 -10.985 3.437   1.00 14.35 ?  81  CYS   B CB   1 
ATOM   4903 S  SG   . CYS   B 1 81  ? 44.809 -11.917 3.695   1.00 14.36 ?  81  CYS   B SG   1 
ATOM   4904 H  H    . CYS   B 1 81  ? 42.351 -13.482 2.389   1.00 15.81 ?  81  CYS   B H    1 
ATOM   4905 H  HA   . CYS   B 1 81  ? 41.659 -10.893 2.181   1.00 15.52 ?  81  CYS   B HA   1 
ATOM   4906 H  HB2  . CYS   B 1 81  ? 43.527 -10.070 3.230   1.00 17.23 ?  81  CYS   B HB2  1 
ATOM   4907 H  HB3  . CYS   B 1 81  ? 42.776 -11.007 4.266   1.00 17.23 ?  81  CYS   B HB3  1 
ATOM   4908 H  HG   . CYS   B 1 81  ? 45.424 -11.418 4.599   1.00 17.24 ?  81  CYS   B HG   1 
ATOM   4909 N  N    . VAL   B 1 82  ? 43.280 -10.473 0.324   1.00 13.01 ?  82  VAL   B N    1 
ATOM   4910 C  CA   . VAL   B 1 82  ? 44.043 -10.349 -0.915  1.00 13.03 ?  82  VAL   B CA   1 
ATOM   4911 C  C    . VAL   B 1 82  ? 45.382 -9.704  -0.593  1.00 13.14 ?  82  VAL   B C    1 
ATOM   4912 O  O    . VAL   B 1 82  ? 45.428 -8.586  -0.062  1.00 14.18 ?  82  VAL   B O    1 
ATOM   4913 C  CB   . VAL   B 1 82  ? 43.296 -9.497  -1.949  1.00 13.70 ?  82  VAL   B CB   1 
ATOM   4914 C  CG1  . VAL   B 1 82  ? 44.138 -9.333  -3.216  1.00 15.24 ?  82  VAL   B CG1  1 
ATOM   4915 C  CG2  . VAL   B 1 82  ? 41.922 -10.082 -2.244  1.00 15.19 ?  82  VAL   B CG2  1 
ATOM   4916 H  H    . VAL   B 1 82  ? 42.896 -9.738  0.560   1.00 15.63 ?  82  VAL   B H    1 
ATOM   4917 H  HA   . VAL   B 1 82  ? 44.201 -11.229 -1.290  1.00 15.64 ?  82  VAL   B HA   1 
ATOM   4918 H  HB   . VAL   B 1 82  ? 43.167 -8.613  -1.580  1.00 16.45 ?  82  VAL   B HB   1 
ATOM   4919 H  HG11 . VAL   B 1 82  ? 43.576 -8.998  -3.930  1.00 18.29 ?  82  VAL   B HG11 1 
ATOM   4920 H  HG12 . VAL   B 1 82  ? 44.861 -8.704  -3.044  1.00 18.29 ?  82  VAL   B HG12 1 
ATOM   4921 H  HG13 . VAL   B 1 82  ? 44.509 -10.196 -3.467  1.00 18.29 ?  82  VAL   B HG13 1 
ATOM   4922 H  HG21 . VAL   B 1 82  ? 41.500 -9.558  -2.946  1.00 18.23 ?  82  VAL   B HG21 1 
ATOM   4923 H  HG22 . VAL   B 1 82  ? 42.023 -11.001 -2.536  1.00 18.23 ?  82  VAL   B HG22 1 
ATOM   4924 H  HG23 . VAL   B 1 82  ? 41.385 -10.046 -1.438  1.00 18.23 ?  82  VAL   B HG23 1 
ATOM   4925 N  N    . LEU   B 1 83  ? 46.469 -10.387 -0.954  1.00 12.78 ?  83  LEU   B N    1 
ATOM   4926 C  CA   . LEU   B 1 83  ? 47.822 -9.858  -0.830  1.00 12.52 ?  83  LEU   B CA   1 
ATOM   4927 C  C    . LEU   B 1 83  ? 48.531 -10.005 -2.178  1.00 12.27 ?  83  LEU   B C    1 
ATOM   4928 O  O    . LEU   B 1 83  ? 47.936 -10.425 -3.176  1.00 12.60 ?  83  LEU   B O    1 
ATOM   4929 C  CB   . LEU   B 1 83  ? 48.572 -10.524 0.332   1.00 13.54 ?  83  LEU   B CB   1 
ATOM   4930 C  CG   . LEU   B 1 83  ? 48.034 -10.177 1.727   1.00 14.67 ?  83  LEU   B CG   1 
ATOM   4931 C  CD1  . LEU   B 1 83  ? 48.659 -11.062 2.797   1.00 15.53 ?  83  LEU   B CD1  1 
ATOM   4932 C  CD2  . LEU   B 1 83  ? 48.246 -8.696  2.064   1.00 15.10 ?  83  LEU   B CD2  1 
ATOM   4933 H  H    . LEU   B 1 83  ? 46.444 -11.182 -1.289  1.00 15.34 ?  83  LEU   B H    1 
ATOM   4934 H  HA   . LEU   B 1 83  ? 47.766 -8.913  -0.636  1.00 15.04 ?  83  LEU   B HA   1 
ATOM   4935 H  HB2  . LEU   B 1 83  ? 48.517 -11.487 0.227   1.00 16.26 ?  83  LEU   B HB2  1 
ATOM   4936 H  HB3  . LEU   B 1 83  ? 49.501 -10.247 0.300   1.00 16.26 ?  83  LEU   B HB3  1 
ATOM   4937 H  HG   . LEU   B 1 83  ? 47.078 -10.343 1.734   1.00 17.61 ?  83  LEU   B HG   1 
ATOM   4938 H  HD11 . LEU   B 1 83  ? 48.291 -10.819 3.662   1.00 18.64 ?  83  LEU   B HD11 1 
ATOM   4939 H  HD12 . LEU   B 1 83  ? 48.446 -11.991 2.601   1.00 18.64 ?  83  LEU   B HD12 1 
ATOM   4940 H  HD13 . LEU   B 1 83  ? 49.617 -10.935 2.796   1.00 18.64 ?  83  LEU   B HD13 1 
ATOM   4941 H  HD21 . LEU   B 1 83  ? 48.010 -8.546  2.993   1.00 18.13 ?  83  LEU   B HD21 1 
ATOM   4942 H  HD22 . LEU   B 1 83  ? 49.178 -8.469  1.919   1.00 18.13 ?  83  LEU   B HD22 1 
ATOM   4943 H  HD23 . LEU   B 1 83  ? 47.681 -8.155  1.489   1.00 18.13 ?  83  LEU   B HD23 1 
ATOM   4944 N  N    . SER   B 1 84  ? 49.808 -9.623  -2.229  1.00 13.58 ?  84  SER   B N    1 
ATOM   4945 C  CA   . SER   B 1 84  ? 50.552 -9.746  -3.478  1.00 13.87 ?  84  SER   B CA   1 
ATOM   4946 C  C    . SER   B 1 84  ? 50.702 -11.208 -3.892  1.00 13.02 ?  84  SER   B C    1 
ATOM   4947 O  O    . SER   B 1 84  ? 50.813 -12.102 -3.060  1.00 13.39 ?  84  SER   B O    1 
ATOM   4948 C  CB   . SER   B 1 84  ? 51.944 -9.127  -3.343  1.00 15.55 ?  84  SER   B CB   1 
ATOM   4949 O  OG   . SER   B 1 84  ? 52.673 -9.352  -4.531  1.00 17.81 ?  84  SER   B OG   1 
ATOM   4950 H  H    . SER   B 1 84  ? 50.253 -9.283  -1.577  1.00 16.31 ?  84  SER   B H    1 
ATOM   4951 H  HA   . SER   B 1 84  ? 50.079 -9.284  -4.186  1.00 16.65 ?  84  SER   B HA   1 
ATOM   4952 H  HB2  . SER   B 1 84  ? 51.860 -8.171  -3.201  1.00 18.67 ?  84  SER   B HB2  1 
ATOM   4953 H  HB3  . SER   B 1 84  ? 52.414 -9.539  -2.604  1.00 18.67 ?  84  SER   B HB3  1 
ATOM   4954 H  HG   . SER   B 1 84  ? 53.446 -9.011  -4.476  1.00 21.38 ?  84  SER   B HG   1 
ATOM   4955 N  N    . GLY   B 1 85  ? 50.752 -11.437 -5.207  1.00 14.28 ?  85  GLY   B N    1 
ATOM   4956 C  CA   . GLY   B 1 85  ? 51.103 -12.720 -5.769  1.00 15.30 ?  85  GLY   B CA   1 
ATOM   4957 C  C    . GLY   B 1 85  ? 52.578 -12.903 -6.065  1.00 13.97 ?  85  GLY   B C    1 
ATOM   4958 O  O    . GLY   B 1 85  ? 52.967 -13.978 -6.517  1.00 14.39 ?  85  GLY   B O    1 
ATOM   4959 H  H    . GLY   B 1 85  ? 50.585 -10.847 -5.799  1.00 17.14 ?  85  GLY   B H    1 
ATOM   4960 H  HA2  . GLY   B 1 85  ? 50.837 -13.424 -5.153  1.00 18.37 ?  85  GLY   B HA2  1 
ATOM   4961 H  HA3  . GLY   B 1 85  ? 50.615 -12.853 -6.595  1.00 18.37 ?  85  GLY   B HA3  1 
ATOM   4962 N  N    . HIS   B 1 86  ? 53.419 -11.902 -5.824  1.00 14.15 ?  86  HIS   B N    1 
ATOM   4963 C  CA   . HIS   B 1 86  ? 54.891 -12.055 -5.897  1.00 14.49 ?  86  HIS   B CA   1 
ATOM   4964 C  C    . HIS   B 1 86  ? 55.270 -12.559 -7.288  1.00 14.85 ?  86  HIS   B C    1 
ATOM   4965 O  O    . HIS   B 1 86  ? 54.882 -11.939 -8.291  1.00 15.24 ?  86  HIS   B O    1 
ATOM   4966 C  CB   . HIS   B 1 86  ? 55.395 -12.896 -4.729  1.00 14.78 ?  86  HIS   B CB   1 
ATOM   4967 C  CG   . HIS   B 1 86  ? 55.078 -12.301 -3.398  1.00 14.13 ?  86  HIS   B CG   1 
ATOM   4968 N  ND1  . HIS   B 1 86  ? 55.896 -11.382 -2.777  1.00 16.04 ?  86  HIS   B ND1  1 
ATOM   4969 C  CD2  . HIS   B 1 86  ? 54.009 -12.469 -2.584  1.00 14.89 ?  86  HIS   B CD2  1 
ATOM   4970 C  CE1  . HIS   B 1 86  ? 55.338 -11.003 -1.642  1.00 15.70 ?  86  HIS   B CE1  1 
ATOM   4971 N  NE2  . HIS   B 1 86  ? 54.191 -11.647 -1.501  1.00 15.51 ?  86  HIS   B NE2  1 
ATOM   4972 H  H    . HIS   B 1 86  ? 53.166 -11.109 -5.625  1.00 16.98 ?  86  HIS   B H    1 
ATOM   4973 H  HA   . HIS   B 1 86  ? 55.286 -11.176 -5.802  1.00 17.39 ?  86  HIS   B HA   1 
ATOM   4974 H  HB2  . HIS   B 1 86  ? 54.989 -13.776 -4.773  1.00 17.74 ?  86  HIS   B HB2  1 
ATOM   4975 H  HB3  . HIS   B 1 86  ? 56.362 -12.979 -4.794  1.00 17.74 ?  86  HIS   B HB3  1 
ATOM   4976 H  HD2  . HIS   B 1 86  ? 53.276 -13.025 -2.742  1.00 17.88 ?  86  HIS   B HD2  1 
ATOM   4977 H  HE1  . HIS   B 1 86  ? 55.698 -10.403 -1.032  1.00 18.85 ?  86  HIS   B HE1  1 
ATOM   4978 H  HE2  . HIS   B 1 86  ? 53.653 -11.581 -0.832  1.00 18.62 ?  86  HIS   B HE2  1 
ATOM   4979 N  N    . ASN   B 1 87  ? 56.018 -13.651 -7.400  1.00 14.97 ?  87  ASN   B N    1 
ATOM   4980 C  CA   . ASN   B 1 87  ? 56.413 -14.217 -8.682  1.00 15.91 ?  87  ASN   B CA   1 
ATOM   4981 C  C    . ASN   B 1 87  ? 55.445 -15.269 -9.181  1.00 15.64 ?  87  ASN   B C    1 
ATOM   4982 O  O    . ASN   B 1 87  ? 55.781 -15.989 -10.126 1.00 17.16 ?  87  ASN   B O    1 
ATOM   4983 C  CB   . ASN   B 1 87  ? 57.809 -14.838 -8.572  1.00 17.18 ?  87  ASN   B CB   1 
ATOM   4984 C  CG   . ASN   B 1 87  ? 57.874 -15.958 -7.538  1.00 18.03 ?  87  ASN   B CG   1 
ATOM   4985 O  OD1  . ASN   B 1 87  ? 57.261 -15.877 -6.470  1.00 17.50 ?  87  ASN   B OD1  1 
ATOM   4986 N  ND2  . ASN   B 1 87  ? 58.620 -17.019 -7.861  1.00 20.88 ?  87  ASN   B ND2  1 
ATOM   4987 H  H    . ASN   B 1 87  ? 56.322 -14.092 -6.727  1.00 17.97 ?  87  ASN   B H    1 
ATOM   4988 H  HA   . ASN   B 1 87  ? 56.453 -13.510 -9.341  1.00 19.10 ?  87  ASN   B HA   1 
ATOM   4989 H  HB2  . ASN   B 1 87  ? 58.059 -15.208 -9.438  1.00 20.63 ?  87  ASN   B HB2  1 
ATOM   4990 H  HB3  . ASN   B 1 87  ? 58.443 -14.150 -8.315  1.00 20.63 ?  87  ASN   B HB3  1 
ATOM   4991 H  HD21 . ASN   B 1 87  ? 58.688 -17.675 -7.314  1.00 25.07 ?  87  ASN   B HD21 1 
ATOM   4992 H  HD22 . ASN   B 1 87  ? 59.028 -17.046 -8.621  1.00 25.07 ?  87  ASN   B HD22 1 
ATOM   4993 N  N    . LEU   B 1 88  ? 54.263 -15.373 -8.571  1.00 13.90 ?  88  LEU   B N    1 
ATOM   4994 C  CA   . LEU   B 1 88  ? 53.291 -16.409 -8.900  1.00 13.73 ?  88  LEU   B CA   1 
ATOM   4995 C  C    . LEU   B 1 88  ? 52.060 -15.893 -9.620  1.00 14.05 ?  88  LEU   B C    1 
ATOM   4996 O  O    . LEU   B 1 88  ? 51.458 -16.643 -10.399 1.00 15.39 ?  88  LEU   B O    1 
ATOM   4997 C  CB   . LEU   B 1 88  ? 52.820 -17.107 -7.620  1.00 14.76 ?  88  LEU   B CB   1 
ATOM   4998 C  CG   . LEU   B 1 88  ? 53.956 -17.716 -6.813  1.00 17.27 ?  88  LEU   B CG   1 
ATOM   4999 C  CD1  . LEU   B 1 88  ? 53.481 -18.102 -5.421  1.00 18.71 ?  88  LEU   B CD1  1 
ATOM   5000 C  CD2  . LEU   B 1 88  ? 54.507 -18.915 -7.557  1.00 21.22 ?  88  LEU   B CD2  1 
ATOM   5001 H  H    . LEU   B 1 88  ? 53.994 -14.845 -7.936  1.00 16.69 ?  88  LEU   B H    1 
ATOM   5002 H  HA   . LEU   B 1 88  ? 53.709 -17.069 -9.465  1.00 16.48 ?  88  LEU   B HA   1 
ATOM   5003 H  HB2  . LEU   B 1 88  ? 52.363 -16.468 -7.051  1.00 17.72 ?  88  LEU   B HB2  1 
ATOM   5004 H  HB3  . LEU   B 1 88  ? 52.208 -17.828 -7.856  1.00 17.72 ?  88  LEU   B HB3  1 
ATOM   5005 H  HG   . LEU   B 1 88  ? 54.668 -17.062 -6.722  1.00 20.74 ?  88  LEU   B HG   1 
ATOM   5006 H  HD11 . LEU   B 1 88  ? 54.168 -18.632 -4.991  1.00 22.46 ?  88  LEU   B HD11 1 
ATOM   5007 H  HD12 . LEU   B 1 88  ? 53.317 -17.293 -4.911  1.00 22.46 ?  88  LEU   B HD12 1 
ATOM   5008 H  HD13 . LEU   B 1 88  ? 52.665 -18.615 -5.503  1.00 22.46 ?  88  LEU   B HD13 1 
ATOM   5009 H  HD21 . LEU   B 1 88  ? 55.155 -19.361 -6.991  1.00 25.47 ?  88  LEU   B HD21 1 
ATOM   5010 H  HD22 . LEU   B 1 88  ? 53.777 -19.516 -7.766  1.00 25.47 ?  88  LEU   B HD22 1 
ATOM   5011 H  HD23 . LEU   B 1 88  ? 54.934 -18.612 -8.373  1.00 25.47 ?  88  LEU   B HD23 1 
ATOM   5012 N  N    . ALA   B 1 89  ? 51.654 -14.654 -9.357  1.00 13.77 ?  89  ALA   B N    1 
ATOM   5013 C  CA   . ALA   B 1 89  ? 50.363 -14.154 -9.804  1.00 12.90 ?  89  ALA   B CA   1 
ATOM   5014 C  C    . ALA   B 1 89  ? 50.328 -12.663 -9.522  1.00 13.59 ?  89  ALA   B C    1 
ATOM   5015 O  O    . ALA   B 1 89  ? 51.151 -12.132 -8.774  1.00 14.12 ?  89  ALA   B O    1 
ATOM   5016 C  CB   . ALA   B 1 89  ? 49.228 -14.839 -9.049  1.00 13.28 ?  89  ALA   B CB   1 
ATOM   5017 H  H    . ALA   B 1 89  ? 52.107 -14.071 -8.911  1.00 16.53 ?  89  ALA   B H    1 
ATOM   5018 H  HA   . ALA   B 1 89  ? 50.252 -14.303 -10.759 1.00 15.49 ?  89  ALA   B HA   1 
ATOM   5019 H  HB1  . ALA   B 1 89  ? 48.376 -14.502 -9.382  1.00 15.95 ?  89  ALA   B HB1  1 
ATOM   5020 H  HB2  . ALA   B 1 89  ? 49.280 -15.797 -9.202  1.00 15.95 ?  89  ALA   B HB2  1 
ATOM   5021 H  HB3  . ALA   B 1 89  ? 49.313 -14.647 -8.106  1.00 15.95 ?  89  ALA   B HB3  1 
ATOM   5022 N  N    . LYS   B 1 90  ? 49.333 -11.985 -10.088 1.00 14.04 ?  90  LYS   B N    1 
ATOM   5023 C  CA   . LYS   B 1 90  ? 49.128 -10.600 -9.682  1.00 14.47 ?  90  LYS   B CA   1 
ATOM   5024 C  C    . LYS   B 1 90  ? 48.804 -10.526 -8.193  1.00 14.63 ?  90  LYS   B C    1 
ATOM   5025 O  O    . LYS   B 1 90  ? 49.423 -9.754  -7.447  1.00 16.13 ?  90  LYS   B O    1 
ATOM   5026 C  CB   . LYS   B 1 90  ? 48.048 -9.944  -10.536 1.00 16.11 ?  90  LYS   B CB   1 
ATOM   5027 C  CG   . LYS   B 1 90  ? 47.751 -8.495  -10.164 1.00 17.70 ?  90  LYS   B CG   1 
ATOM   5028 C  CD   . LYS   B 1 90  ? 48.964 -7.597  -10.257 1.00 21.57 ?  90  LYS   B CD   1 
ATOM   5029 C  CE   . LYS   B 1 90  ? 48.539 -6.153  -10.045 1.00 23.93 ?  90  LYS   B CE   1 
ATOM   5030 N  NZ   . LYS   B 1 90  ? 49.712 -5.249  -9.906  1.00 22.55 ?  90  LYS   B NZ   1 
ATOM   5031 H  H    . LYS   B 1 90  ? 48.783 -12.293 -10.678 1.00 16.86 ?  90  LYS   B H    1 
ATOM   5032 H  HA   . LYS   B 1 90  ? 49.952 -10.117 -9.828  1.00 17.37 ?  90  LYS   B HA   1 
ATOM   5033 H  HB2  . LYS   B 1 90  ? 48.337 -9.953  -11.464 1.00 19.34 ?  90  LYS   B HB2  1 
ATOM   5034 H  HB3  . LYS   B 1 90  ? 47.225 -10.448 -10.448 1.00 19.34 ?  90  LYS   B HB3  1 
ATOM   5035 H  HG2  . LYS   B 1 90  ? 47.073 -8.148  -10.767 1.00 21.25 ?  90  LYS   B HG2  1 
ATOM   5036 H  HG3  . LYS   B 1 90  ? 47.419 -8.464  -9.250  1.00 21.25 ?  90  LYS   B HG3  1 
ATOM   5037 H  HD2  . LYS   B 1 90  ? 49.603 -7.837  -9.566  1.00 25.89 ?  90  LYS   B HD2  1 
ATOM   5038 H  HD3  . LYS   B 1 90  ? 49.365 -7.679  -11.136 1.00 25.89 ?  90  LYS   B HD3  1 
ATOM   5039 H  HE2  . LYS   B 1 90  ? 48.021 -5.851  -10.809 1.00 28.72 ?  90  LYS   B HE2  1 
ATOM   5040 H  HE3  . LYS   B 1 90  ? 48.012 -6.082  -9.234  1.00 28.72 ?  90  LYS   B HE3  1 
ATOM   5041 H  HZ1  . LYS   B 1 90  ? 49.445 -4.406  -9.784  1.00 27.07 ?  90  LYS   B HZ1  1 
ATOM   5042 H  HZ2  . LYS   B 1 90  ? 50.209 -5.494  -9.208  1.00 27.07 ?  90  LYS   B HZ2  1 
ATOM   5043 H  HZ3  . LYS   B 1 90  ? 50.217 -5.283  -10.641 1.00 27.07 ?  90  LYS   B HZ3  1 
ATOM   5044 N  N    . HIS   B 1 91  ? 47.854 -11.348 -7.740  1.00 12.61 ?  91  HIS   B N    1 
ATOM   5045 C  CA   . HIS   B 1 91  ? 47.402 -11.359 -6.361  1.00 12.64 ?  91  HIS   B CA   1 
ATOM   5046 C  C    . HIS   B 1 91  ? 47.406 -12.788 -5.852  1.00 12.22 ?  91  HIS   B C    1 
ATOM   5047 O  O    . HIS   B 1 91  ? 47.158 -13.734 -6.607  1.00 12.37 ?  91  HIS   B O    1 
ATOM   5048 C  CB   . HIS   B 1 91  ? 45.938 -10.894 -6.246  1.00 14.70 ?  91  HIS   B CB   1 
ATOM   5049 C  CG   . HIS   B 1 91  ? 45.699 -9.502  -6.718  1.00 18.46 ?  91  HIS   B CG   1 
ATOM   5050 N  ND1  . HIS   B 1 91  ? 46.266 -8.404  -6.111  1.00 21.25 ?  91  HIS   B ND1  1 
ATOM   5051 C  CD2  . HIS   B 1 91  ? 44.916 -9.024  -7.711  1.00 21.14 ?  91  HIS   B CD2  1 
ATOM   5052 C  CE1  . HIS   B 1 91  ? 45.863 -7.306  -6.730  1.00 22.72 ?  91  HIS   B CE1  1 
ATOM   5053 N  NE2  . HIS   B 1 91  ? 45.038 -7.657  -7.701  1.00 23.23 ?  91  HIS   B NE2  1 
ATOM   5054 H  H    . HIS   B 1 91  ? 47.444 -11.920 -8.231  1.00 15.14 ?  91  HIS   B H    1 
ATOM   5055 H  HA   . HIS   B 1 91  ? 47.966 -10.801 -5.800  1.00 15.17 ?  91  HIS   B HA   1 
ATOM   5056 H  HB2  . HIS   B 1 91  ? 45.379 -11.482 -6.773  1.00 17.64 ?  91  HIS   B HB2  1 
ATOM   5057 H  HB3  . HIS   B 1 91  ? 45.669 -10.938 -5.311  1.00 17.64 ?  91  HIS   B HB3  1 
ATOM   5058 H  HD1  . HIS   B 1 91  ? 46.807 -8.420  -5.441  1.00 25.51 ?  91  HIS   B HD1  1 
ATOM   5059 H  HD2  . HIS   B 1 91  ? 44.401 -9.525  -8.297  1.00 25.38 ?  91  HIS   B HD2  1 
ATOM   5060 H  HE1  . HIS   B 1 91  ? 46.110 -6.432  -6.514  1.00 27.27 ?  91  HIS   B HE1  1 
ATOM   5061 N  N    . CYS   B 1 92  ? 47.619 -12.933 -4.550  1.00 12.51 ?  92  CYS   B N    1 
ATOM   5062 C  CA   . CYS   B 1 92  ? 47.300 -14.169 -3.844  1.00 12.10 ?  92  CYS   B CA   1 
ATOM   5063 C  C    . CYS   B 1 92  ? 46.073 -13.929 -2.977  1.00 11.75 ?  92  CYS   B C    1 
ATOM   5064 O  O    . CYS   B 1 92  ? 46.077 -13.048 -2.114  1.00 12.71 ?  92  CYS   B O    1 
ATOM   5065 C  CB   . CYS   B 1 92  ? 48.456 -14.613 -2.961  1.00 12.53 ?  92  CYS   B CB   1 
ATOM   5066 S  SG   . CYS   B 1 92  ? 48.122 -16.165 -2.090  1.00 12.64 ?  92  CYS   B SG   1 
ATOM   5067 H  H    . CYS   B 1 92  ? 47.976 -12.326 -4.050  1.00 15.02 ?  92  CYS   B H    1 
ATOM   5068 H  HA   . CYS   B 1 92  ? 47.106 -14.867 -4.487  1.00 14.53 ?  92  CYS   B HA   1 
ATOM   5069 H  HB2  . CYS   B 1 92  ? 49.240 -14.733 -3.514  1.00 15.05 ?  92  CYS   B HB2  1 
ATOM   5070 H  HB3  . CYS   B 1 92  ? 48.618 -13.923 -2.298  1.00 15.05 ?  92  CYS   B HB3  1 
ATOM   5071 H  HG   . CYS   B 1 92  ? 49.094 -16.460 -1.447  1.00 15.18 ?  92  CYS   B HG   1 
ATOM   5072 N  N    . LEU   B 1 93  ? 45.050 -14.761 -3.170  1.00 11.86 ?  93  LEU   B N    1 
ATOM   5073 C  CA   . LEU   B 1 93  ? 43.872 -14.766 -2.311  1.00 12.20 ?  93  LEU   B CA   1 
ATOM   5074 C  C    . LEU   B 1 93  ? 44.091 -15.831 -1.240  1.00 11.43 ?  93  LEU   B C    1 
ATOM   5075 O  O    . LEU   B 1 93  ? 44.024 -17.033 -1.534  1.00 11.74 ?  93  LEU   B O    1 
ATOM   5076 C  CB   . LEU   B 1 93  ? 42.607 -15.070 -3.117  1.00 12.98 ?  93  LEU   B CB   1 
ATOM   5077 C  CG   . LEU   B 1 93  ? 41.289 -15.066 -2.322  1.00 13.62 ?  93  LEU   B CG   1 
ATOM   5078 C  CD1  . LEU   B 1 93  ? 40.923 -13.670 -1.842  1.00 13.39 ?  93  LEU   B CD1  1 
ATOM   5079 C  CD2  . LEU   B 1 93  ? 40.153 -15.676 -3.143  1.00 13.35 ?  93  LEU   B CD2  1 
ATOM   5080 H  H    . LEU   B 1 93  ? 45.020 -15.354 -3.799  1.00 14.24 ?  93  LEU   B H    1 
ATOM   5081 H  HA   . LEU   B 1 93  ? 43.775 -13.904 -1.883  1.00 14.65 ?  93  LEU   B HA   1 
ATOM   5082 H  HB2  . LEU   B 1 93  ? 42.527 -14.405 -3.816  1.00 15.58 ?  93  LEU   B HB2  1 
ATOM   5083 H  HB3  . LEU   B 1 93  ? 42.702 -15.949 -3.513  1.00 15.58 ?  93  LEU   B HB3  1 
ATOM   5084 H  HG   . LEU   B 1 93  ? 41.405 -15.618 -1.537  1.00 16.35 ?  93  LEU   B HG   1 
ATOM   5085 H  HD11 . LEU   B 1 93  ? 40.073 -13.709 -1.377  1.00 16.08 ?  93  LEU   B HD11 1 
ATOM   5086 H  HD12 . LEU   B 1 93  ? 41.615 -13.348 -1.243  1.00 16.08 ?  93  LEU   B HD12 1 
ATOM   5087 H  HD13 . LEU   B 1 93  ? 40.851 -13.079 -2.610  1.00 16.08 ?  93  LEU   B HD13 1 
ATOM   5088 H  HD21 . LEU   B 1 93  ? 39.334 -15.655 -2.620  1.00 16.02 ?  93  LEU   B HD21 1 
ATOM   5089 H  HD22 . LEU   B 1 93  ? 40.031 -15.159 -3.959  1.00 16.02 ?  93  LEU   B HD22 1 
ATOM   5090 H  HD23 . LEU   B 1 93  ? 40.375 -16.594 -3.369  1.00 16.02 ?  93  LEU   B HD23 1 
ATOM   5091 N  N    . HIS   B 1 94  ? 44.369 -15.397 -0.013  1.00 11.50 ?  94  HIS   B N    1 
ATOM   5092 C  CA   . HIS   B 1 94  ? 44.585 -16.295 1.117   1.00 11.20 ?  94  HIS   B CA   1 
ATOM   5093 C  C    . HIS   B 1 94  ? 43.217 -16.654 1.687   1.00 12.21 ?  94  HIS   B C    1 
ATOM   5094 O  O    . HIS   B 1 94  ? 42.540 -15.798 2.253   1.00 12.93 ?  94  HIS   B O    1 
ATOM   5095 C  CB   . HIS   B 1 94  ? 45.460 -15.614 2.169   1.00 11.91 ?  94  HIS   B CB   1 
ATOM   5096 C  CG   . HIS   B 1 94  ? 46.847 -15.308 1.694   1.00 11.96 ?  94  HIS   B CG   1 
ATOM   5097 N  ND1  . HIS   B 1 94  ? 47.880 -16.219 1.782   1.00 12.40 ?  94  HIS   B ND1  1 
ATOM   5098 C  CD2  . HIS   B 1 94  ? 47.352 -14.208 1.086   1.00 12.09 ?  94  HIS   B CD2  1 
ATOM   5099 C  CE1  . HIS   B 1 94  ? 48.972 -15.676 1.270   1.00 13.06 ?  94  HIS   B CE1  1 
ATOM   5100 N  NE2  . HIS   B 1 94  ? 48.681 -14.458 0.844   1.00 12.62 ?  94  HIS   B NE2  1 
ATOM   5101 H  H    . HIS   B 1 94  ? 44.439 -14.559 0.194   1.00 13.81 ?  94  HIS   B H    1 
ATOM   5102 H  HA   . HIS   B 1 94  ? 45.026 -17.103 0.812   1.00 13.45 ?  94  HIS   B HA   1 
ATOM   5103 H  HB2  . HIS   B 1 94  ? 45.047 -14.778 2.426   1.00 14.30 ?  94  HIS   B HB2  1 
ATOM   5104 H  HB3  . HIS   B 1 94  ? 45.536 -16.199 2.937   1.00 14.30 ?  94  HIS   B HB3  1 
ATOM   5105 H  HD2  . HIS   B 1 94  ? 46.893 -13.427 0.882   1.00 14.52 ?  94  HIS   B HD2  1 
ATOM   5106 H  HE1  . HIS   B 1 94  ? 49.804 -16.092 1.213   1.00 15.68 ?  94  HIS   B HE1  1 
ATOM   5107 H  HE2  . HIS   B 1 94  ? 49.231 -13.921 0.466   1.00 15.16 ?  94  HIS   B HE2  1 
ATOM   5108 N  N    . VAL   B 1 95  ? 42.788 -17.910 1.537   1.00 11.76 ?  95  VAL   B N    1 
ATOM   5109 C  CA   . VAL   B 1 95  ? 41.460 -18.361 1.965   1.00 12.14 ?  95  VAL   B CA   1 
ATOM   5110 C  C    . VAL   B 1 95  ? 41.623 -19.404 3.058   1.00 12.60 ?  95  VAL   B C    1 
ATOM   5111 O  O    . VAL   B 1 95  ? 42.416 -20.338 2.905   1.00 12.90 ?  95  VAL   B O    1 
ATOM   5112 C  CB   . VAL   B 1 95  ? 40.664 -18.962 0.794   1.00 12.16 ?  95  VAL   B CB   1 
ATOM   5113 C  CG1  . VAL   B 1 95  ? 39.272 -19.437 1.255   1.00 13.77 ?  95  VAL   B CG1  1 
ATOM   5114 C  CG2  . VAL   B 1 95  ? 40.538 -17.961 -0.336  1.00 12.49 ?  95  VAL   B CG2  1 
ATOM   5115 H  H    . VAL   B 1 95  ? 43.260 -18.535 1.182   1.00 14.12 ?  95  VAL   B H    1 
ATOM   5116 H  HA   . VAL   B 1 95  ? 40.957 -17.612 2.325   1.00 14.57 ?  95  VAL   B HA   1 
ATOM   5117 H  HB   . VAL   B 1 95  ? 41.145 -19.737 0.455   1.00 14.61 ?  95  VAL   B HB   1 
ATOM   5118 H  HG11 . VAL   B 1 95  ? 38.736 -19.644 0.469   1.00 16.53 ?  95  VAL   B HG11 1 
ATOM   5119 H  HG12 . VAL   B 1 95  ? 39.369 -20.233 1.801   1.00 16.53 ?  95  VAL   B HG12 1 
ATOM   5120 H  HG13 . VAL   B 1 95  ? 38.849 -18.731 1.763   1.00 16.53 ?  95  VAL   B HG13 1 
ATOM   5121 H  HG21 . VAL   B 1 95  ? 39.977 -18.343 -1.028  1.00 14.99 ?  95  VAL   B HG21 1 
ATOM   5122 H  HG22 . VAL   B 1 95  ? 40.140 -17.151 0.009   1.00 14.99 ?  95  VAL   B HG22 1 
ATOM   5123 H  HG23 . VAL   B 1 95  ? 41.422 -17.778 -0.689  1.00 14.99 ?  95  VAL   B HG23 1 
ATOM   5124 N  N    . VAL   B 1 96  ? 40.881 -19.243 4.152   1.00 12.63 ?  96  VAL   B N    1 
ATOM   5125 C  CA   . VAL   B 1 96  ? 40.963 -20.149 5.297   1.00 13.46 ?  96  VAL   B CA   1 
ATOM   5126 C  C    . VAL   B 1 96  ? 39.779 -21.114 5.249   1.00 13.40 ?  96  VAL   B C    1 
ATOM   5127 O  O    . VAL   B 1 96  ? 38.657 -20.753 5.620   1.00 13.95 ?  96  VAL   B O    1 
ATOM   5128 C  CB   . VAL   B 1 96  ? 41.022 -19.396 6.634   1.00 13.70 ?  96  VAL   B CB   1 
ATOM   5129 C  CG1  . VAL   B 1 96  ? 41.183 -20.382 7.787   1.00 14.71 ?  96  VAL   B CG1  1 
ATOM   5130 C  CG2  . VAL   B 1 96  ? 42.148 -18.359 6.653   1.00 13.97 ?  96  VAL   B CG2  1 
ATOM   5131 H  H    . VAL   B 1 96  ? 40.311 -18.603 4.260   1.00 15.16 ?  96  VAL   B H    1 
ATOM   5132 H  HA   . VAL   B 1 96  ? 41.780 -20.669 5.224   1.00 16.16 ?  96  VAL   B HA   1 
ATOM   5133 H  HB   . VAL   B 1 96  ? 40.186 -18.922 6.766   1.00 16.45 ?  96  VAL   B HB   1 
ATOM   5134 H  HG11 . VAL   B 1 96  ? 41.374 -19.890 8.604   1.00 17.67 ?  96  VAL   B HG11 1 
ATOM   5135 H  HG12 . VAL   B 1 96  ? 40.364 -20.888 7.894   1.00 17.67 ?  96  VAL   B HG12 1 
ATOM   5136 H  HG13 . VAL   B 1 96  ? 41.922 -20.983 7.591   1.00 17.67 ?  96  VAL   B HG13 1 
ATOM   5137 H  HG21 . VAL   B 1 96  ? 42.178 -17.932 7.528   1.00 16.77 ?  96  VAL   B HG21 1 
ATOM   5138 H  HG22 . VAL   B 1 96  ? 42.993 -18.797 6.473   1.00 16.77 ?  96  VAL   B HG22 1 
ATOM   5139 H  HG23 . VAL   B 1 96  ? 41.974 -17.685 5.972   1.00 16.77 ?  96  VAL   B HG23 1 
ATOM   5140 N  N    . GLY   B 1 97  ? 40.032 -22.347 4.819   1.00 13.34 ?  97  GLY   B N    1 
ATOM   5141 C  CA   . GLY   B 1 97  ? 39.062 -23.404 4.974   1.00 14.06 ?  97  GLY   B CA   1 
ATOM   5142 C  C    . GLY   B 1 97  ? 39.171 -24.001 6.361   1.00 15.35 ?  97  GLY   B C    1 
ATOM   5143 O  O    . GLY   B 1 97  ? 40.205 -23.874 7.026   1.00 15.22 ?  97  GLY   B O    1 
ATOM   5144 H  H    . GLY   B 1 97  ? 40.772 -22.594 4.443   1.00 16.01 ?  97  GLY   B H    1 
ATOM   5145 H  HA2  . GLY   B 1 97  ? 38.170 -23.044 4.844   1.00 16.88 ?  97  GLY   B HA2  1 
ATOM   5146 H  HA3  . GLY   B 1 97  ? 39.219 -24.096 4.308   1.00 16.88 ?  97  GLY   B HA3  1 
ATOM   5147 N  N    . PRO   B 1 98  ? 38.126 -24.690 6.818   1.00 15.18 ?  98  PRO   B N    1 
ATOM   5148 C  CA   . PRO   B 1 98  ? 38.216 -25.384 8.107   1.00 15.76 ?  98  PRO   B CA   1 
ATOM   5149 C  C    . PRO   B 1 98  ? 39.237 -26.510 8.060   1.00 15.52 ?  98  PRO   B C    1 
ATOM   5150 O  O    . PRO   B 1 98  ? 39.334 -27.252 7.081   1.00 16.13 ?  98  PRO   B O    1 
ATOM   5151 C  CB   . PRO   B 1 98  ? 36.796 -25.927 8.320   1.00 15.93 ?  98  PRO   B CB   1 
ATOM   5152 C  CG   . PRO   B 1 98  ? 36.219 -26.045 6.952   1.00 15.42 ?  98  PRO   B CG   1 
ATOM   5153 C  CD   . PRO   B 1 98  ? 36.810 -24.885 6.181   1.00 15.34 ?  98  PRO   B CD   1 
ATOM   5154 H  HA   . PRO   B 1 98  ? 38.445 -24.765 8.810   1.00 18.92 ?  98  PRO   B HA   1 
ATOM   5155 H  HB2  . PRO   B 1 98  ? 36.840 -26.796 8.750   1.00 19.13 ?  98  PRO   B HB2  1 
ATOM   5156 H  HB3  . PRO   B 1 98  ? 36.288 -25.302 8.853   1.00 19.13 ?  98  PRO   B HB3  1 
ATOM   5157 H  HG2  . PRO   B 1 98  ? 36.480 -26.896 6.557   1.00 18.51 ?  98  PRO   B HG2  1 
ATOM   5158 H  HG3  . PRO   B 1 98  ? 35.251 -25.976 6.999   1.00 18.51 ?  98  PRO   B HG3  1 
ATOM   5159 H  HD2  . PRO   B 1 98  ? 36.908 -25.123 5.242   1.00 18.42 ?  98  PRO   B HD2  1 
ATOM   5160 H  HD3  . PRO   B 1 98  ? 36.263 -24.095 6.291   1.00 18.42 ?  98  PRO   B HD3  1 
ATOM   5161 N  N    . ASN   B 1 99  ? 39.998 -26.634 9.142   1.00 15.94 ?  99  ASN   B N    1 
ATOM   5162 C  CA   . ASN   B 1 99  ? 40.973 -27.712 9.311   1.00 16.98 ?  99  ASN   B CA   1 
ATOM   5163 C  C    . ASN   B 1 99  ? 40.327 -28.796 10.175  1.00 19.34 ?  99  ASN   B C    1 
ATOM   5164 O  O    . ASN   B 1 99  ? 40.230 -28.656 11.396  1.00 20.45 ?  99  ASN   B O    1 
ATOM   5165 C  CB   . ASN   B 1 99  ? 42.244 -27.155 9.940   1.00 17.80 ?  99  ASN   B CB   1 
ATOM   5166 C  CG   . ASN   B 1 99  ? 43.381 -28.157 9.941   1.00 19.26 ?  99  ASN   B CG   1 
ATOM   5167 O  OD1  . ASN   B 1 99  ? 43.157 -29.353 10.091  1.00 20.37 ?  99  ASN   B OD1  1 
ATOM   5168 N  ND2  . ASN   B 1 99  ? 44.605 -27.672 9.760   1.00 19.65 ?  99  ASN   B ND2  1 
ATOM   5169 H  H    . ASN   B 1 99  ? 39.967 -26.095 9.809   1.00 19.14 ?  99  ASN   B H    1 
ATOM   5170 H  HA   . ASN   B 1 99  ? 41.195 -28.097 8.449   1.00 20.38 ?  99  ASN   B HA   1 
ATOM   5171 H  HB2  . ASN   B 1 99  ? 42.527 -26.376 9.442   1.00 21.37 ?  99  ASN   B HB2  1 
ATOM   5172 H  HB3  . ASN   B 1 99  ? 42.055 -26.910 10.863  1.00 21.37 ?  99  ASN   B HB3  1 
ATOM   5173 H  HD21 . ASN   B 1 99  ? 45.281 -28.200 9.754   1.00 23.59 ?  99  ASN   B HD21 1 
ATOM   5174 H  HD22 . ASN   B 1 99  ? 44.716 -26.825 9.657   1.00 23.59 ?  99  ASN   B HD22 1 
ATOM   5175 N  N    A VAL   B 1 100 ? 39.861 -29.871 9.530   0.74 20.94 ?  100 VAL   B N    1 
ATOM   5176 N  N    B VAL   B 1 100 ? 39.874 -29.873 9.526   0.26 21.30 ?  100 VAL   B N    1 
ATOM   5177 C  CA   A VAL   B 1 100 ? 39.240 -30.974 10.263  0.74 24.17 ?  100 VAL   B CA   1 
ATOM   5178 C  CA   B VAL   B 1 100 ? 39.249 -30.981 10.246  0.26 23.76 ?  100 VAL   B CA   1 
ATOM   5179 C  C    A VAL   B 1 100 ? 40.241 -31.640 11.200  0.74 24.80 ?  100 VAL   B C    1 
ATOM   5180 C  C    B VAL   B 1 100 ? 40.241 -31.638 11.194  0.26 24.58 ?  100 VAL   B C    1 
ATOM   5181 O  O    A VAL   B 1 100 ? 39.866 -32.138 12.268  0.74 25.86 ?  100 VAL   B O    1 
ATOM   5182 O  O    B VAL   B 1 100 ? 39.860 -32.119 12.269  0.26 25.21 ?  100 VAL   B O    1 
ATOM   5183 C  CB   A VAL   B 1 100 ? 38.600 -31.980 9.281   0.74 27.07 ?  100 VAL   B CB   1 
ATOM   5184 C  CB   B VAL   B 1 100 ? 38.645 -31.990 9.247   0.26 25.44 ?  100 VAL   B CB   1 
ATOM   5185 C  CG1  A VAL   B 1 100 ? 38.125 -33.229 10.012  0.74 28.46 ?  100 VAL   B CG1  1 
ATOM   5186 C  CG1  B VAL   B 1 100 ? 38.141 -33.233 9.969   0.26 26.20 ?  100 VAL   B CG1  1 
ATOM   5187 C  CG2  A VAL   B 1 100 ? 37.439 -31.332 8.537   0.74 27.79 ?  100 VAL   B CG2  1 
ATOM   5188 C  CG2  B VAL   B 1 100 ? 37.519 -31.341 8.458   0.26 25.88 ?  100 VAL   B CG2  1 
ATOM   5189 H  H    A VAL   B 1 100 ? 39.880 -29.975 8.676   0.74 25.14 ?  100 VAL   B H    1 
ATOM   5190 H  H    B VAL   B 1 100 ? 39.915 -29.983 8.675   0.26 25.57 ?  100 VAL   B H    1 
ATOM   5191 H  HA   A VAL   B 1 100 ? 38.523 -30.616 10.810  0.74 29.01 ?  100 VAL   B HA   1 
ATOM   5192 H  HA   B VAL   B 1 100 ? 38.520 -30.633 10.781  0.26 28.52 ?  100 VAL   B HA   1 
ATOM   5193 H  HB   A VAL   B 1 100 ? 39.263 -32.250 8.628   0.74 32.49 ?  100 VAL   B HB   1 
ATOM   5194 H  HB   B VAL   B 1 100 ? 39.331 -32.265 8.619   0.26 30.53 ?  100 VAL   B HB   1 
ATOM   5195 H  HG11 A VAL   B 1 100 ? 37.535 -33.731 9.425   0.74 34.16 ?  100 VAL   B HG11 1 
ATOM   5196 H  HG11 B VAL   B 1 100 ? 37.571 -33.737 9.366   0.26 31.45 ?  100 VAL   B HG11 1 
ATOM   5197 H  HG12 A VAL   B 1 100 ? 38.893 -33.772 10.248  0.74 34.16 ?  100 VAL   B HG12 1 
ATOM   5198 H  HG12 B VAL   B 1 100 ? 38.899 -33.777 10.234  0.26 31.45 ?  100 VAL   B HG12 1 
ATOM   5199 H  HG13 A VAL   B 1 100 ? 37.644 -32.965 10.811  0.74 34.16 ?  100 VAL   B HG13 1 
ATOM   5200 H  HG13 B VAL   B 1 100 ? 37.635 -32.962 10.750  0.26 31.45 ?  100 VAL   B HG13 1 
ATOM   5201 H  HG21 A VAL   B 1 100 ? 37.059 -31.979 7.920   0.74 33.36 ?  100 VAL   B HG21 1 
ATOM   5202 H  HG21 B VAL   B 1 100 ? 37.145 -31.994 7.847   0.26 31.07 ?  100 VAL   B HG21 1 
ATOM   5203 H  HG22 A VAL   B 1 100 ? 36.767 -31.055 9.180   0.74 33.36 ?  100 VAL   B HG22 1 
ATOM   5204 H  HG22 B VAL   B 1 100 ? 36.836 -31.037 9.077   0.26 31.07 ?  100 VAL   B HG22 1 
ATOM   5205 H  HG23 A VAL   B 1 100 ? 37.767 -30.563 8.048   0.74 33.36 ?  100 VAL   B HG23 1 
ATOM   5206 H  HG23 B VAL   B 1 100 ? 37.875 -30.588 7.962   0.26 31.07 ?  100 VAL   B HG23 1 
ATOM   5207 N  N    . ASN   B 1 101 ? 41.520 -31.681 10.818  1.00 24.86 ?  101 ASN   B N    1 
ATOM   5208 C  CA   . ASN   B 1 101 ? 42.548 -32.224 11.704  1.00 26.99 ?  101 ASN   B CA   1 
ATOM   5209 C  C    . ASN   B 1 101 ? 42.739 -31.384 12.961  1.00 28.21 ?  101 ASN   B C    1 
ATOM   5210 O  O    . ASN   B 1 101 ? 43.384 -31.850 13.906  1.00 30.46 ?  101 ASN   B O    1 
ATOM   5211 C  CB   . ASN   B 1 101 ? 43.877 -32.351 10.957  1.00 27.27 ?  101 ASN   B CB   1 
ATOM   5212 C  CG   . ASN   B 1 101 ? 43.880 -33.497 9.966   1.00 27.37 ?  101 ASN   B CG   1 
ATOM   5213 O  OD1  . ASN   B 1 101 ? 43.232 -34.514 10.186  1.00 28.70 ?  101 ASN   B OD1  1 
ATOM   5214 N  ND2  . ASN   B 1 101 ? 44.605 -33.331 8.867   1.00 26.94 ?  101 ASN   B ND2  1 
ATOM   5215 H  H    A ASN   B 1 101 ? 41.811 -31.417 10.053  0.74 29.84 ?  101 ASN   B H    1 
ATOM   5216 H  H    B ASN   B 1 101 ? 41.813 -31.412 10.056  0.26 29.84 ?  101 ASN   B H    1 
ATOM   5217 H  HA   . ASN   B 1 101 ? 42.280 -33.112 11.980  1.00 32.39 ?  101 ASN   B HA   1 
ATOM   5218 H  HB2  . ASN   B 1 101 ? 44.051 -31.534 10.467  1.00 32.74 ?  101 ASN   B HB2  1 
ATOM   5219 H  HB3  . ASN   B 1 101 ? 44.586 -32.509 11.600  1.00 32.74 ?  101 ASN   B HB3  1 
ATOM   5220 H  HD21 . ASN   B 1 101 ? 44.638 -33.956 8.276   1.00 32.34 ?  101 ASN   B HD21 1 
ATOM   5221 H  HD22 . ASN   B 1 101 ? 45.045 -32.602 8.746   1.00 32.34 ?  101 ASN   B HD22 1 
ATOM   5222 N  N    . LYS   B 1 102 ? 42.209 -30.162 12.987  1.00 29.94 ?  102 LYS   B N    1 
ATOM   5223 C  CA   . LYS   B 1 102 ? 42.179 -29.326 14.180  1.00 32.22 ?  102 LYS   B CA   1 
ATOM   5224 C  C    . LYS   B 1 102 ? 40.796 -29.277 14.815  1.00 31.22 ?  102 LYS   B C    1 
ATOM   5225 O  O    . LYS   B 1 102 ? 40.573 -28.477 15.729  1.00 32.32 ?  102 LYS   B O    1 
ATOM   5226 C  CB   . LYS   B 1 102 ? 42.605 -27.899 13.840  1.00 35.60 ?  102 LYS   B CB   1 
ATOM   5227 C  CG   . LYS   B 1 102 ? 44.060 -27.716 13.458  1.00 39.28 ?  102 LYS   B CG   1 
ATOM   5228 C  CD   . LYS   B 1 102 ? 44.288 -26.280 13.010  1.00 42.33 ?  102 LYS   B CD   1 
ATOM   5229 C  CE   . LYS   B 1 102 ? 45.752 -25.976 12.751  1.00 44.83 ?  102 LYS   B CE   1 
ATOM   5230 N  NZ   . LYS   B 1 102 ? 45.935 -24.572 12.275  1.00 46.47 ?  102 LYS   B NZ   1 
ATOM   5231 H  H    . LYS   B 1 102 ? 41.844 -29.788 12.306  1.00 35.93 ?  102 LYS   B H    1 
ATOM   5232 H  HA   . LYS   B 1 102 ? 42.805 -29.679 14.831  1.00 38.67 ?  102 LYS   B HA   1 
ATOM   5233 H  HB2  . LYS   B 1 102 ? 42.067 -27.589 13.095  1.00 42.73 ?  102 LYS   B HB2  1 
ATOM   5234 H  HB3  . LYS   B 1 102 ? 42.436 -27.338 14.614  1.00 42.73 ?  102 LYS   B HB3  1 
ATOM   5235 H  HG2  . LYS   B 1 102 ? 44.626 -27.894 14.226  1.00 47.14 ?  102 LYS   B HG2  1 
ATOM   5236 H  HG3  . LYS   B 1 102 ? 44.283 -28.309 12.724  1.00 47.14 ?  102 LYS   B HG3  1 
ATOM   5237 H  HD2  . LYS   B 1 102 ? 43.797 -26.124 12.187  1.00 50.81 ?  102 LYS   B HD2  1 
ATOM   5238 H  HD3  . LYS   B 1 102 ? 43.972 -25.679 13.703  1.00 50.81 ?  102 LYS   B HD3  1 
ATOM   5239 H  HE2  . LYS   B 1 102 ? 46.254 -26.088 13.574  1.00 53.81 ?  102 LYS   B HE2  1 
ATOM   5240 H  HE3  . LYS   B 1 102 ? 46.088 -26.577 12.067  1.00 53.81 ?  102 LYS   B HE3  1 
ATOM   5241 H  HZ1  . LYS   B 1 102 ? 46.797 -24.410 12.128  1.00 55.77 ?  102 LYS   B HZ1  1 
ATOM   5242 H  HZ2  . LYS   B 1 102 ? 45.483 -24.447 11.518  1.00 55.77 ?  102 LYS   B HZ2  1 
ATOM   5243 H  HZ3  . LYS   B 1 102 ? 45.633 -24.002 12.889  1.00 55.77 ?  102 LYS   B HZ3  1 
ATOM   5244 N  N    . GLY   B 1 103 ? 39.857 -30.088 14.336  1.00 29.76 ?  103 GLY   B N    1 
ATOM   5245 C  CA   . GLY   B 1 103 ? 38.526 -30.137 14.904  1.00 29.83 ?  103 GLY   B CA   1 
ATOM   5246 C  C    . GLY   B 1 103 ? 37.582 -29.055 14.437  1.00 29.04 ?  103 GLY   B C    1 
ATOM   5247 O  O    . GLY   B 1 103 ? 36.492 -28.922 15.006  1.00 30.03 ?  103 GLY   B O    1 
ATOM   5248 H  H    . GLY   B 1 103 ? 39.972 -30.624 13.678  1.00 35.72 ?  103 GLY   B H    1 
ATOM   5249 H  HA2  . GLY   B 1 103 ? 38.123 -30.989 14.685  1.00 35.81 ?  103 GLY   B HA2  1 
ATOM   5250 H  HA3  . GLY   B 1 103 ? 38.594 -30.078 15.872  1.00 35.81 ?  103 GLY   B HA3  1 
ATOM   5251 N  N    A GLU   B 1 104 ? 37.958 -28.281 13.423  0.74 26.98 ?  104 GLU   B N    1 
ATOM   5252 N  N    B GLU   B 1 104 ? 37.946 -28.288 13.415  0.26 28.75 ?  104 GLU   B N    1 
ATOM   5253 C  CA   A GLU   B 1 104 ? 37.125 -27.180 12.972  0.74 24.58 ?  104 GLU   B CA   1 
ATOM   5254 C  CA   B GLU   B 1 104 ? 37.100 -27.194 12.962  0.26 28.15 ?  104 GLU   B CA   1 
ATOM   5255 C  C    A GLU   B 1 104 ? 35.945 -27.700 12.152  0.74 25.89 ?  104 GLU   B C    1 
ATOM   5256 C  C    B GLU   B 1 104 ? 35.940 -27.722 12.123  0.26 28.26 ?  104 GLU   B C    1 
ATOM   5257 O  O    A GLU   B 1 104 ? 35.981 -28.793 11.577  0.74 27.53 ?  104 GLU   B O    1 
ATOM   5258 O  O    B GLU   B 1 104 ? 36.024 -28.785 11.501  0.26 28.72 ?  104 GLU   B O    1 
ATOM   5259 C  CB   A GLU   B 1 104 ? 37.964 -26.166 12.192  0.74 22.57 ?  104 GLU   B CB   1 
ATOM   5260 C  CB   B GLU   B 1 104 ? 37.929 -26.175 12.180  0.26 27.60 ?  104 GLU   B CB   1 
ATOM   5261 C  CG   A GLU   B 1 104 ? 39.056 -25.560 13.059  0.74 20.49 ?  104 GLU   B CG   1 
ATOM   5262 C  CG   B GLU   B 1 104 ? 39.009 -25.533 13.039  0.26 27.08 ?  104 GLU   B CG   1 
ATOM   5263 C  CD   A GLU   B 1 104 ? 40.022 -24.666 12.313  0.74 19.90 ?  104 GLU   B CD   1 
ATOM   5264 C  CD   B GLU   B 1 104 ? 39.975 -24.674 12.248  0.26 26.84 ?  104 GLU   B CD   1 
ATOM   5265 O  OE1  A GLU   B 1 104 ? 40.047 -24.668 11.061  0.74 18.45 ?  104 GLU   B OE1  1 
ATOM   5266 O  OE1  B GLU   B 1 104 ? 39.890 -24.656 11.002  0.26 26.53 ?  104 GLU   B OE1  1 
ATOM   5267 O  OE2  A GLU   B 1 104 ? 40.771 -23.953 13.010  0.74 21.29 -1 104 GLU   B OE2  1 
ATOM   5268 O  OE2  B GLU   B 1 104 ? 40.826 -24.015 12.881  0.26 27.29 -1 104 GLU   B OE2  1 
ATOM   5269 H  H    A GLU   B 1 104 ? 38.693 -28.372 12.984  0.74 32.39 ?  104 GLU   B H    1 
ATOM   5270 H  H    B GLU   B 1 104 ? 38.675 -28.380 12.970  0.26 34.51 ?  104 GLU   B H    1 
ATOM   5271 H  HA   A GLU   B 1 104 ? 36.768 -26.723 13.751  0.74 29.50 ?  104 GLU   B HA   1 
ATOM   5272 H  HA   B GLU   B 1 104 ? 36.728 -26.743 13.735  0.26 33.78 ?  104 GLU   B HA   1 
ATOM   5273 H  HB2  A GLU   B 1 104 ? 38.385 -26.607 11.440  0.74 27.10 ?  104 GLU   B HB2  1 
ATOM   5274 H  HB2  B GLU   B 1 104 ? 38.360 -26.619 11.434  0.26 33.12 ?  104 GLU   B HB2  1 
ATOM   5275 H  HB3  A GLU   B 1 104 ? 37.391 -25.446 11.883  0.74 27.10 ?  104 GLU   B HB3  1 
ATOM   5276 H  HB3  B GLU   B 1 104 ? 37.344 -25.471 11.856  0.26 33.12 ?  104 GLU   B HB3  1 
ATOM   5277 H  HG2  A GLU   B 1 104 ? 38.647 -25.024 13.758  0.74 24.60 ?  104 GLU   B HG2  1 
ATOM   5278 H  HG2  B GLU   B 1 104 ? 38.585 -24.971 13.708  0.26 32.50 ?  104 GLU   B HG2  1 
ATOM   5279 H  HG3  A GLU   B 1 104 ? 39.578 -26.272 13.461  0.74 24.60 ?  104 GLU   B HG3  1 
ATOM   5280 H  HG3  B GLU   B 1 104 ? 39.520 -26.233 13.477  0.26 32.50 ?  104 GLU   B HG3  1 
ATOM   5281 N  N    A ASP   B 1 105 ? 34.881 -26.901 12.124  0.74 26.19 ?  105 ASP   B N    1 
ATOM   5282 N  N    B ASP   B 1 105 ? 34.847 -26.961 12.119  0.26 28.05 ?  105 ASP   B N    1 
ATOM   5283 C  CA   A ASP   B 1 105 ? 33.597 -27.339 11.593  0.74 27.46 ?  105 ASP   B CA   1 
ATOM   5284 C  CA   B ASP   B 1 105 ? 33.589 -27.435 11.554  0.26 28.12 ?  105 ASP   B CA   1 
ATOM   5285 C  C    A ASP   B 1 105 ? 33.644 -27.374 10.070  0.74 26.21 ?  105 ASP   B C    1 
ATOM   5286 C  C    B ASP   B 1 105 ? 33.663 -27.449 10.031  0.26 27.61 ?  105 ASP   B C    1 
ATOM   5287 O  O    A ASP   B 1 105 ? 33.786 -26.333 9.421   0.74 25.41 ?  105 ASP   B O    1 
ATOM   5288 O  O    B ASP   B 1 105 ? 33.890 -26.411 9.400   0.26 27.28 ?  105 ASP   B O    1 
ATOM   5289 C  CB   A ASP   B 1 105 ? 32.493 -26.401 12.078  0.74 30.48 ?  105 ASP   B CB   1 
ATOM   5290 C  CB   B ASP   B 1 105 ? 32.445 -26.541 12.029  0.26 28.66 ?  105 ASP   B CB   1 
ATOM   5291 C  CG   A ASP   B 1 105 ? 31.116 -26.829 11.613  0.74 33.76 ?  105 ASP   B CG   1 
ATOM   5292 C  CG   B ASP   B 1 105 ? 31.080 -27.128 11.714  0.26 29.20 ?  105 ASP   B CG   1 
ATOM   5293 O  OD1  A ASP   B 1 105 ? 30.994 -27.920 11.018  0.74 33.94 ?  105 ASP   B OD1  1 
ATOM   5294 O  OD1  B ASP   B 1 105 ? 31.018 -28.120 10.956  0.26 29.51 ?  105 ASP   B OD1  1 
ATOM   5295 O  OD2  A ASP   B 1 105 ? 30.150 -26.067 11.841  0.74 36.55 -1 105 ASP   B OD2  1 
ATOM   5296 O  OD2  B ASP   B 1 105 ? 30.068 -26.609 12.235  0.26 29.05 -1 105 ASP   B OD2  1 
ATOM   5297 H  H    A ASP   B 1 105 ? 34.883 -26.086 12.403  0.74 31.43 ?  105 ASP   B H    1 
ATOM   5298 H  H    B ASP   B 1 105 ? 34.810 -26.163 12.433  0.26 33.67 ?  105 ASP   B H    1 
ATOM   5299 H  HA   A ASP   B 1 105 ? 33.404 -28.232 11.915  0.74 32.96 ?  105 ASP   B HA   1 
ATOM   5300 H  HA   B ASP   B 1 105 ? 33.414 -28.338 11.860  0.26 33.76 ?  105 ASP   B HA   1 
ATOM   5301 H  HB2  A ASP   B 1 105 ? 32.510 -26.372 13.051  0.74 36.59 ?  105 ASP   B HB2  1 
ATOM   5302 H  HB2  B ASP   B 1 105 ? 32.509 -26.429 12.992  0.26 34.40 ?  105 ASP   B HB2  1 
ATOM   5303 H  HB3  A ASP   B 1 105 ? 32.648 -25.514 11.720  0.74 36.59 ?  105 ASP   B HB3  1 
ATOM   5304 H  HB3  B ASP   B 1 105 ? 32.519 -25.674 11.594  0.26 34.40 ?  105 ASP   B HB3  1 
ATOM   5305 N  N    A ILE   B 1 106 ? 33.509 -28.576 9.504   0.74 25.78 ?  106 ILE   B N    1 
ATOM   5306 N  N    B ILE   B 1 106 ? 33.462 -28.631 9.443   0.26 27.29 ?  106 ILE   B N    1 
ATOM   5307 C  CA   A ILE   B 1 106 ? 33.503 -28.755 8.058   0.74 24.88 ?  106 ILE   B CA   1 
ATOM   5308 C  CA   B ILE   B 1 106 ? 33.475 -28.780 7.993   0.26 27.03 ?  106 ILE   B CA   1 
ATOM   5309 C  C    A ILE   B 1 106 ? 32.402 -27.936 7.389   0.74 22.73 ?  106 ILE   B C    1 
ATOM   5310 C  C    B ILE   B 1 106 ? 32.386 -27.946 7.329   0.26 26.43 ?  106 ILE   B C    1 
ATOM   5311 O  O    A ILE   B 1 106 ? 32.497 -27.629 6.194   0.74 21.28 ?  106 ILE   B O    1 
ATOM   5312 O  O    B ILE   B 1 106 ? 32.487 -27.632 6.138   0.26 26.27 ?  106 ILE   B O    1 
ATOM   5313 C  CB   A ILE   B 1 106 ? 33.397 -30.265 7.737   0.74 26.09 ?  106 ILE   B CB   1 
ATOM   5314 C  CB   B ILE   B 1 106 ? 33.366 -30.279 7.626   0.26 27.45 ?  106 ILE   B CB   1 
ATOM   5315 C  CG1  A ILE   B 1 106 ? 33.682 -30.535 6.260   0.74 26.70 ?  106 ILE   B CG1  1 
ATOM   5316 C  CG1  B ILE   B 1 106 ? 33.659 -30.504 6.140   0.26 27.67 ?  106 ILE   B CG1  1 
ATOM   5317 C  CG2  A ILE   B 1 106 ? 32.026 -30.806 8.134   0.74 27.69 ?  106 ILE   B CG2  1 
ATOM   5318 C  CG2  B ILE   B 1 106 ? 31.987 -30.821 7.983   0.26 27.87 ?  106 ILE   B CG2  1 
ATOM   5319 C  CD1  A ILE   B 1 106 ? 35.045 -30.054 5.816   0.74 27.04 ?  106 ILE   B CD1  1 
ATOM   5320 C  CD1  B ILE   B 1 106 ? 35.040 -30.055 5.720   0.26 27.82 ?  106 ILE   B CD1  1 
ATOM   5321 H  H    A ILE   B 1 106 ? 33.425 -29.306 9.946   0.74 30.94 ?  106 ILE   B H    1 
ATOM   5322 H  H    B ILE   B 1 106 ? 33.324 -29.363 9.868   0.26 32.76 ?  106 ILE   B H    1 
ATOM   5323 H  HA   A ILE   B 1 106 ? 34.349 -28.434 7.714   0.74 29.87 ?  106 ILE   B HA   1 
ATOM   5324 H  HA   B ILE   B 1 106 ? 34.324 -28.456 7.665   0.26 32.45 ?  106 ILE   B HA   1 
ATOM   5325 H  HB   A ILE   B 1 106 ? 34.066 -30.731 8.261   0.74 31.32 ?  106 ILE   B HB   1 
ATOM   5326 H  HB   B ILE   B 1 106 ? 34.026 -30.768 8.141   0.26 32.95 ?  106 ILE   B HB   1 
ATOM   5327 H  HG12 A ILE   B 1 106 ? 33.644 -31.493 6.102   0.74 32.05 ?  106 ILE   B HG12 1 
ATOM   5328 H  HG12 B ILE   B 1 106 ? 33.588 -31.454 5.947   0.26 33.21 ?  106 ILE   B HG12 1 
ATOM   5329 H  HG13 A ILE   B 1 106 ? 33.018 -30.085 5.719   0.74 32.05 ?  106 ILE   B HG13 1 
ATOM   5330 H  HG13 B ILE   B 1 106 ? 33.013 -30.014 5.611   0.26 33.21 ?  106 ILE   B HG13 1 
ATOM   5331 H  HG21 A ILE   B 1 106 ? 32.037 -31.773 8.062   0.74 33.23 ?  106 ILE   B HG21 1 
ATOM   5332 H  HG21 B ILE   B 1 106 ? 31.999 -31.788 7.904   0.26 33.45 ?  106 ILE   B HG21 1 
ATOM   5333 H  HG22 A ILE   B 1 106 ? 31.839 -30.545 9.049   0.74 33.23 ?  106 ILE   B HG22 1 
ATOM   5334 H  HG22 B ILE   B 1 106 ? 31.777 -30.567 8.895   0.26 33.45 ?  106 ILE   B HG22 1 
ATOM   5335 H  HG23 A ILE   B 1 106 ? 31.355 -30.438 7.540   0.74 33.23 ?  106 ILE   B HG23 1 
ATOM   5336 H  HG23 B ILE   B 1 106 ? 31.331 -30.447 7.375   0.26 33.45 ?  106 ILE   B HG23 1 
ATOM   5337 H  HD11 A ILE   B 1 106 ? 35.281 -30.491 4.984   0.74 32.46 ?  106 ILE   B HD11 1 
ATOM   5338 H  HD11 B ILE   B 1 106 ? 35.253 -30.452 4.862   0.26 33.40 ?  106 ILE   B HD11 1 
ATOM   5339 H  HD12 A ILE   B 1 106 ? 35.016 -29.092 5.686   0.74 32.46 ?  106 ILE   B HD12 1 
ATOM   5340 H  HD12 B ILE   B 1 106 ? 35.049 -29.087 5.648   0.26 33.40 ?  106 ILE   B HD12 1 
ATOM   5341 H  HD13 A ILE   B 1 106 ? 35.698 -30.274 6.500   0.74 32.46 ?  106 ILE   B HD13 1 
ATOM   5342 H  HD13 B ILE   B 1 106 ? 35.682 -30.344 6.387   0.26 33.40 ?  106 ILE   B HD13 1 
ATOM   5343 N  N    A GLN   B 1 107 ? 31.363 -27.556 8.136   0.74 24.40 ?  107 GLN   B N    1 
ATOM   5344 N  N    B GLN   B 1 107 ? 31.342 -27.573 8.075   0.26 26.43 ?  107 GLN   B N    1 
ATOM   5345 C  CA   A GLN   B 1 107 ? 30.282 -26.765 7.558   0.74 25.28 ?  107 GLN   B CA   1 
ATOM   5346 C  CA   B GLN   B 1 107 ? 30.268 -26.762 7.513   0.26 26.40 ?  107 GLN   B CA   1 
ATOM   5347 C  C    A GLN   B 1 107 ? 30.770 -25.417 7.041   0.74 23.69 ?  107 GLN   B C    1 
ATOM   5348 C  C    B GLN   B 1 107 ? 30.757 -25.395 7.043   0.26 24.03 ?  107 GLN   B C    1 
ATOM   5349 O  O    A GLN   B 1 107 ? 30.135 -24.841 6.154   0.74 24.74 ?  107 GLN   B O    1 
ATOM   5350 O  O    B GLN   B 1 107 ? 30.100 -24.774 6.201   0.26 24.50 ?  107 GLN   B O    1 
ATOM   5351 C  CB   A GLN   B 1 107 ? 29.177 -26.570 8.599   0.74 29.58 ?  107 GLN   B CB   1 
ATOM   5352 C  CB   B GLN   B 1 107 ? 29.150 -26.604 8.549   0.26 28.98 ?  107 GLN   B CB   1 
ATOM   5353 C  CG   A GLN   B 1 107 ? 27.851 -26.073 8.038   0.74 33.96 ?  107 GLN   B CG   1 
ATOM   5354 C  CG   B GLN   B 1 107 ? 27.823 -26.112 7.984   0.26 31.44 ?  107 GLN   B CG   1 
ATOM   5355 C  CD   A GLN   B 1 107 ? 27.784 -24.560 7.927   0.74 36.89 ?  107 GLN   B CD   1 
ATOM   5356 C  CD   B GLN   B 1 107 ? 27.703 -24.599 7.986   0.26 33.28 ?  107 GLN   B CD   1 
ATOM   5357 O  OE1  A GLN   B 1 107 ? 28.631 -23.846 8.470   0.74 38.31 ?  107 GLN   B OE1  1 
ATOM   5358 O  OE1  B GLN   B 1 107 ? 28.548 -23.896 8.544   0.26 34.08 ?  107 GLN   B OE1  1 
ATOM   5359 N  NE2  A GLN   B 1 107 ? 26.770 -24.063 7.224   0.74 38.02 ?  107 GLN   B NE2  1 
ATOM   5360 N  NE2  B GLN   B 1 107 ? 26.646 -24.090 7.363   0.26 33.90 ?  107 GLN   B NE2  1 
ATOM   5361 H  H    A GLN   B 1 107 ? 31.272 -27.726 8.970   0.74 29.29 ?  107 GLN   B H    1 
ATOM   5362 H  H    B GLN   B 1 107 ? 31.231 -27.784 8.900   0.26 31.73 ?  107 GLN   B H    1 
ATOM   5363 H  HA   A GLN   B 1 107 ? 29.902 -27.257 6.812   0.74 30.34 ?  107 GLN   B HA   1 
ATOM   5364 H  HA   B GLN   B 1 107 ? 29.893 -27.227 6.747   0.26 31.69 ?  107 GLN   B HA   1 
ATOM   5365 H  HB2  A GLN   B 1 107 ? 29.010 -27.418 9.032   0.74 35.51 ?  107 GLN   B HB2  1 
ATOM   5366 H  HB2  B GLN   B 1 107 ? 28.986 -27.465 8.962   0.26 34.78 ?  107 GLN   B HB2  1 
ATOM   5367 H  HB3  A GLN   B 1 107 ? 29.481 -25.923 9.256   0.74 35.51 ?  107 GLN   B HB3  1 
ATOM   5368 H  HB3  B GLN   B 1 107 ? 29.438 -25.971 9.225   0.26 34.78 ?  107 GLN   B HB3  1 
ATOM   5369 H  HG2  A GLN   B 1 107 ? 27.722 -26.441 7.150   0.74 40.76 ?  107 GLN   B HG2  1 
ATOM   5370 H  HG2  B GLN   B 1 107 ? 27.735 -26.416 7.068   0.26 37.74 ?  107 GLN   B HG2  1 
ATOM   5371 H  HG3  A GLN   B 1 107 ? 27.130 -26.367 8.623   0.74 40.76 ?  107 GLN   B HG3  1 
ATOM   5372 H  HG3  B GLN   B 1 107 ? 27.097 -26.473 8.522   0.26 37.74 ?  107 GLN   B HG3  1 
ATOM   5373 H  HE21 A GLN   B 1 107 ? 26.199 -24.592 6.857   0.74 45.64 ?  107 GLN   B HE21 1 
ATOM   5374 H  HE21 B GLN   B 1 107 ? 26.077 -24.612 6.983   0.26 40.69 ?  107 GLN   B HE21 1 
ATOM   5375 H  HE22 A GLN   B 1 107 ? 26.684 -23.212 7.136   0.74 45.64 ?  107 GLN   B HE22 1 
ATOM   5376 H  HE22 B GLN   B 1 107 ? 26.531 -23.238 7.339   0.26 40.69 ?  107 GLN   B HE22 1 
ATOM   5377 N  N    . LEU   B 1 108 ? 31.891 -24.913 7.561   1.00 21.26 ?  108 LEU   B N    1 
ATOM   5378 C  CA   . LEU   B 1 108 ? 32.443 -23.621 7.143   1.00 19.42 ?  108 LEU   B CA   1 
ATOM   5379 C  C    . LEU   B 1 108 ? 33.094 -23.653 5.768   1.00 17.11 ?  108 LEU   B C    1 
ATOM   5380 O  O    . LEU   B 1 108 ? 33.517 -22.596 5.272   1.00 16.52 ?  108 LEU   B O    1 
ATOM   5381 C  CB   . LEU   B 1 108 ? 33.444 -23.124 8.184   1.00 19.60 ?  108 LEU   B CB   1 
ATOM   5382 C  CG   . LEU   B 1 108 ? 32.816 -22.692 9.510   1.00 21.43 ?  108 LEU   B CG   1 
ATOM   5383 C  CD1  . LEU   B 1 108 ? 33.854 -22.587 10.614  1.00 21.71 ?  108 LEU   B CD1  1 
ATOM   5384 C  CD2  . LEU   B 1 108 ? 32.116 -21.361 9.327   1.00 23.22 ?  108 LEU   B CD2  1 
ATOM   5385 H  H    A LEU   B 1 108 ? 32.341 -25.302 8.177   0.74 25.53 ?  108 LEU   B H    1 
ATOM   5386 H  H    B LEU   B 1 108 ? 32.350 -25.315 8.162   0.26 25.53 ?  108 LEU   B H    1 
ATOM   5387 H  HA   . LEU   B 1 108 ? 31.718 -22.982 7.104   1.00 23.31 ?  108 LEU   B HA   1 
ATOM   5388 H  HB2  . LEU   B 1 108 ? 34.072 -23.834 8.379   1.00 23.53 ?  108 LEU   B HB2  1 
ATOM   5389 H  HB3  . LEU   B 1 108 ? 33.911 -22.358 7.823   1.00 23.53 ?  108 LEU   B HB3  1 
ATOM   5390 H  HG   . LEU   B 1 108 ? 32.151 -23.348 9.783   1.00 25.73 ?  108 LEU   B HG   1 
ATOM   5391 H  HD11 . LEU   B 1 108 ? 33.409 -22.357 11.447  1.00 26.06 ?  108 LEU   B HD11 1 
ATOM   5392 H  HD12 . LEU   B 1 108 ? 34.304 -23.441 10.707  1.00 26.06 ?  108 LEU   B HD12 1 
ATOM   5393 H  HD13 . LEU   B 1 108 ? 34.493 -21.897 10.381  1.00 26.06 ?  108 LEU   B HD13 1 
ATOM   5394 H  HD21 . LEU   B 1 108 ? 31.802 -21.047 10.188  1.00 27.87 ?  108 LEU   B HD21 1 
ATOM   5395 H  HD22 . LEU   B 1 108 ? 32.745 -20.726 8.951   1.00 27.87 ?  108 LEU   B HD22 1 
ATOM   5396 H  HD23 . LEU   B 1 108 ? 31.365 -21.479 8.724   1.00 27.87 ?  108 LEU   B HD23 1 
ATOM   5397 N  N    . LEU   B 1 109 ? 33.169 -24.824 5.137   1.00 16.23 ?  109 LEU   B N    1 
ATOM   5398 C  CA   . LEU   B 1 109 ? 33.806 -24.925 3.830   1.00 15.08 ?  109 LEU   B CA   1 
ATOM   5399 C  C    . LEU   B 1 109 ? 33.038 -24.146 2.767   1.00 13.92 ?  109 LEU   B C    1 
ATOM   5400 O  O    . LEU   B 1 109 ? 33.648 -23.554 1.869   1.00 14.19 ?  109 LEU   B O    1 
ATOM   5401 C  CB   . LEU   B 1 109 ? 33.953 -26.405 3.455   1.00 15.50 ?  109 LEU   B CB   1 
ATOM   5402 C  CG   . LEU   B 1 109 ? 34.712 -26.757 2.179   1.00 14.98 ?  109 LEU   B CG   1 
ATOM   5403 C  CD1  . LEU   B 1 109 ? 36.092 -26.081 2.148   1.00 15.16 ?  109 LEU   B CD1  1 
ATOM   5404 C  CD2  . LEU   B 1 109 ? 34.866 -28.262 2.054   1.00 15.52 ?  109 LEU   B CD2  1 
ATOM   5405 H  H    . LEU   B 1 109 ? 32.870 -25.567 5.441   1.00 19.49 ?  109 LEU   B H    1 
ATOM   5406 H  HA   . LEU   B 1 109 ? 34.695 -24.545 3.880   1.00 18.11 ?  109 LEU   B HA   1 
ATOM   5407 H  HB2  . LEU   B 1 109 ? 34.412 -26.853 4.181   1.00 18.60 ?  109 LEU   B HB2  1 
ATOM   5408 H  HB3  . LEU   B 1 109 ? 33.064 -26.782 3.362   1.00 18.60 ?  109 LEU   B HB3  1 
ATOM   5409 H  HG   . LEU   B 1 109 ? 34.207 -26.452 1.407   1.00 17.98 ?  109 LEU   B HG   1 
ATOM   5410 H  HD11 . LEU   B 1 109 ? 36.596 -26.420 1.391   1.00 18.21 ?  109 LEU   B HD11 1 
ATOM   5411 H  HD12 . LEU   B 1 109 ? 35.969 -25.124 2.060   1.00 18.21 ?  109 LEU   B HD12 1 
ATOM   5412 H  HD13 . LEU   B 1 109 ? 36.560 -26.284 2.973   1.00 18.21 ?  109 LEU   B HD13 1 
ATOM   5413 H  HD21 . LEU   B 1 109 ? 35.429 -28.467 1.287   1.00 18.63 ?  109 LEU   B HD21 1 
ATOM   5414 H  HD22 . LEU   B 1 109 ? 35.276 -28.610 2.861   1.00 18.63 ?  109 LEU   B HD22 1 
ATOM   5415 H  HD23 . LEU   B 1 109 ? 33.990 -28.667 1.931   1.00 18.63 ?  109 LEU   B HD23 1 
ATOM   5416 N  N    . LYS   B 1 110 ? 31.706 -24.096 2.861   1.00 13.52 ?  110 LYS   B N    1 
ATOM   5417 C  CA   . LYS   B 1 110 ? 30.949 -23.336 1.869   1.00 13.52 ?  110 LYS   B CA   1 
ATOM   5418 C  C    . LYS   B 1 110 ? 31.287 -21.848 1.949   1.00 13.05 ?  110 LYS   B C    1 
ATOM   5419 O  O    . LYS   B 1 110 ? 31.529 -21.203 0.926   1.00 13.46 ?  110 LYS   B O    1 
ATOM   5420 C  CB   . LYS   B 1 110 ? 29.445 -23.584 2.022   1.00 14.54 ?  110 LYS   B CB   1 
ATOM   5421 C  CG   . LYS   B 1 110 ? 28.625 -22.955 0.904   1.00 15.06 ?  110 LYS   B CG   1 
ATOM   5422 C  CD   . LYS   B 1 110 ? 27.178 -23.433 0.907   1.00 15.27 ?  110 LYS   B CD   1 
ATOM   5423 C  CE   . LYS   B 1 110 ? 26.410 -22.893 -0.296  1.00 16.28 ?  110 LYS   B CE   1 
ATOM   5424 N  NZ   . LYS   B 1 110 ? 26.747 -23.583 -1.568  1.00 16.02 ?  110 LYS   B NZ   1 
ATOM   5425 H  H    . LYS   B 1 110 ? 31.234 -24.486 3.465   1.00 16.23 ?  110 LYS   B H    1 
ATOM   5426 H  HA   . LYS   B 1 110 ? 31.206 -23.646 0.983   1.00 16.23 ?  110 LYS   B HA   1 
ATOM   5427 H  HB2  . LYS   B 1 110 ? 29.281 -24.545 2.005   1.00 17.46 ?  110 LYS   B HB2  1 
ATOM   5428 H  HB3  . LYS   B 1 110 ? 29.146 -23.213 2.862   1.00 17.46 ?  110 LYS   B HB3  1 
ATOM   5429 H  HG2  . LYS   B 1 110 ? 28.622 -21.990 1.017   1.00 18.08 ?  110 LYS   B HG2  1 
ATOM   5430 H  HG3  . LYS   B 1 110 ? 29.017 -23.186 0.046   1.00 18.08 ?  110 LYS   B HG3  1 
ATOM   5431 H  HD2  . LYS   B 1 110 ? 27.159 -24.405 0.869   1.00 18.33 ?  110 LYS   B HD2  1 
ATOM   5432 H  HD3  . LYS   B 1 110 ? 26.735 -23.123 1.714   1.00 18.33 ?  110 LYS   B HD3  1 
ATOM   5433 H  HE2  . LYS   B 1 110 ? 25.460 -23.007 -0.141  1.00 19.54 ?  110 LYS   B HE2  1 
ATOM   5434 H  HE3  . LYS   B 1 110 ? 26.619 -21.954 -0.403  1.00 19.54 ?  110 LYS   B HE3  1 
ATOM   5435 H  HZ1  . LYS   B 1 110 ? 26.279 -23.233 -2.235  1.00 19.23 ?  110 LYS   B HZ1  1 
ATOM   5436 H  HZ2  . LYS   B 1 110 ? 27.617 -23.489 -1.740  1.00 19.23 ?  110 LYS   B HZ2  1 
ATOM   5437 H  HZ3  . LYS   B 1 110 ? 26.559 -24.450 -1.501  1.00 19.23 ?  110 LYS   B HZ3  1 
ATOM   5438 N  N    . SER   B 1 111 ? 31.321 -21.295 3.167   1.00 14.37 ?  111 SER   B N    1 
ATOM   5439 C  CA   . SER   B 1 111 ? 31.714 -19.897 3.346   1.00 14.00 ?  111 SER   B CA   1 
ATOM   5440 C  C    . SER   B 1 111 ? 33.096 -19.640 2.761   1.00 13.97 ?  111 SER   B C    1 
ATOM   5441 O  O    . SER   B 1 111 ? 33.319 -18.620 2.100   1.00 13.97 ?  111 SER   B O    1 
ATOM   5442 C  CB   . SER   B 1 111 ? 31.702 -19.540 4.831   1.00 14.93 ?  111 SER   B CB   1 
ATOM   5443 O  OG   . SER   B 1 111 ? 30.391 -19.549 5.351   1.00 17.57 ?  111 SER   B OG   1 
ATOM   5444 H  H    . SER   B 1 111 ? 31.127 -21.709 3.896   1.00 17.25 ?  111 SER   B H    1 
ATOM   5445 H  HA   . SER   B 1 111 ? 31.079 -19.324 2.891   1.00 16.80 ?  111 SER   B HA   1 
ATOM   5446 H  HB2  . SER   B 1 111 ? 32.237 -20.188 5.316   1.00 17.93 ?  111 SER   B HB2  1 
ATOM   5447 H  HB3  . SER   B 1 111 ? 32.075 -18.653 4.946   1.00 17.93 ?  111 SER   B HB3  1 
ATOM   5448 H  HG   . SER   B 1 111 ? 30.086 -20.332 5.368   1.00 21.09 ?  111 SER   B HG   1 
ATOM   5449 N  N    . ALA   B 1 112 ? 34.036 -20.555 2.992   1.00 14.00 ?  112 ALA   B N    1 
ATOM   5450 C  CA   . ALA   B 1 112 ? 35.379 -20.398 2.440   1.00 13.29 ?  112 ALA   B CA   1 
ATOM   5451 C  C    . ALA   B 1 112 ? 35.335 -20.289 0.917   1.00 12.78 ?  112 ALA   B C    1 
ATOM   5452 O  O    . ALA   B 1 112 ? 35.961 -19.396 0.328   1.00 13.09 ?  112 ALA   B O    1 
ATOM   5453 C  CB   . ALA   B 1 112 ? 36.267 -21.566 2.888   1.00 14.42 ?  112 ALA   B CB   1 
ATOM   5454 H  H    . ALA   B 1 112 ? 33.924 -21.263 3.469   1.00 16.81 ?  112 ALA   B H    1 
ATOM   5455 H  HA   . ALA   B 1 112 ? 35.767 -19.581 2.786   1.00 15.96 ?  112 ALA   B HA   1 
ATOM   5456 H  HB1  . ALA   B 1 112 ? 37.157 -21.443 2.523   1.00 17.31 ?  112 ALA   B HB1  1 
ATOM   5457 H  HB2  . ALA   B 1 112 ? 36.309 -21.575 3.860   1.00 17.31 ?  112 ALA   B HB2  1 
ATOM   5458 H  HB3  . ALA   B 1 112 ? 35.887 -22.396 2.568   1.00 17.31 ?  112 ALA   B HB3  1 
ATOM   5459 N  N    . TYR   B 1 113 ? 34.605 -21.201 0.257   1.00 12.62 ?  113 TYR   B N    1 
ATOM   5460 C  CA   . TYR   B 1 113 ? 34.521 -21.153 -1.201  1.00 12.46 ?  113 TYR   B CA   1 
ATOM   5461 C  C    . TYR   B 1 113 ? 33.815 -19.892 -1.712  1.00 12.40 ?  113 TYR   B C    1 
ATOM   5462 O  O    . TYR   B 1 113 ? 34.090 -19.447 -2.831  1.00 12.62 ?  113 TYR   B O    1 
ATOM   5463 C  CB   . TYR   B 1 113 ? 33.851 -22.412 -1.755  1.00 13.25 ?  113 TYR   B CB   1 
ATOM   5464 C  CG   . TYR   B 1 113 ? 34.817 -23.558 -2.016  1.00 13.87 ?  113 TYR   B CG   1 
ATOM   5465 C  CD1  . TYR   B 1 113 ? 35.806 -23.452 -2.988  1.00 14.22 ?  113 TYR   B CD1  1 
ATOM   5466 C  CD2  . TYR   B 1 113 ? 34.708 -24.751 -1.317  1.00 14.09 ?  113 TYR   B CD2  1 
ATOM   5467 C  CE1  . TYR   B 1 113 ? 36.691 -24.484 -3.236  1.00 14.31 ?  113 TYR   B CE1  1 
ATOM   5468 C  CE2  . TYR   B 1 113 ? 35.592 -25.794 -1.557  1.00 14.67 ?  113 TYR   B CE2  1 
ATOM   5469 C  CZ   . TYR   B 1 113 ? 36.573 -25.663 -2.523  1.00 14.45 ?  113 TYR   B CZ   1 
ATOM   5470 O  OH   . TYR   B 1 113 ? 37.456 -26.687 -2.794  1.00 14.45 ?  113 TYR   B OH   1 
ATOM   5471 H  H    . TYR   B 1 113 ? 34.154 -21.837 0.629   1.00 15.16 ?  113 TYR   B H    1 
ATOM   5472 H  HA   . TYR   B 1 113 ? 35.422 -21.134 -1.543  1.00 14.95 ?  113 TYR   B HA   1 
ATOM   5473 H  HB2  . TYR   B 1 113 ? 33.186 -22.723 -1.117  1.00 15.90 ?  113 TYR   B HB2  1 
ATOM   5474 H  HB3  . TYR   B 1 113 ? 33.414 -22.186 -2.593  1.00 15.90 ?  113 TYR   B HB3  1 
ATOM   5475 H  HD1  . TYR   B 1 113 ? 35.891 -22.657 -3.473  1.00 17.07 ?  113 TYR   B HD1  1 
ATOM   5476 H  HD2  . TYR   B 1 113 ? 34.044 -24.839 -0.671  1.00 16.92 ?  113 TYR   B HD2  1 
ATOM   5477 H  HE1  . TYR   B 1 113 ? 37.349 -24.394 -3.892  1.00 17.18 ?  113 TYR   B HE1  1 
ATOM   5478 H  HE2  . TYR   B 1 113 ? 35.505 -26.591 -1.085  1.00 17.61 ?  113 TYR   B HE2  1 
ATOM   5479 H  HH   . TYR   B 1 113 ? 37.266 -27.358 -2.329  1.00 17.35 ?  113 TYR   B HH   1 
ATOM   5480 N  N    . GLU   B 1 114 ? 32.901 -19.310 -0.928  1.00 12.65 ?  114 GLU   B N    1 
ATOM   5481 C  CA   . GLU   B 1 114 ? 32.210 -18.106 -1.388  1.00 12.27 ?  114 GLU   B CA   1 
ATOM   5482 C  C    . GLU   B 1 114 ? 33.195 -16.978 -1.679  1.00 12.54 ?  114 GLU   B C    1 
ATOM   5483 O  O    . GLU   B 1 114 ? 32.926 -16.129 -2.525  1.00 13.01 ?  114 GLU   B O    1 
ATOM   5484 C  CB   . GLU   B 1 114 ? 31.156 -17.672 -0.370  1.00 13.22 ?  114 GLU   B CB   1 
ATOM   5485 C  CG   . GLU   B 1 114 ? 29.914 -18.597 -0.423  1.00 13.39 ?  114 GLU   B CG   1 
ATOM   5486 C  CD   . GLU   B 1 114 ? 28.900 -18.395 0.686   1.00 13.56 ?  114 GLU   B CD   1 
ATOM   5487 O  OE1  . GLU   B 1 114 ? 29.207 -17.760 1.716   1.00 13.56 ?  114 GLU   B OE1  1 
ATOM   5488 O  OE2  . GLU   B 1 114 ? 27.770 -18.931 0.528   1.00 14.04 -1 114 GLU   B OE2  1 
ATOM   5489 H  H    . GLU   B 1 114 ? 32.653 -19.598 -0.155  1.00 15.19 ?  114 GLU   B H    1 
ATOM   5490 H  HA   . GLU   B 1 114 ? 31.749 -18.306 -2.218  1.00 14.74 ?  114 GLU   B HA   1 
ATOM   5491 H  HB2  . GLU   B 1 114 ? 31.535 -17.714 0.521   1.00 15.87 ?  114 GLU   B HB2  1 
ATOM   5492 H  HB3  . GLU   B 1 114 ? 30.869 -16.768 -0.572  1.00 15.87 ?  114 GLU   B HB3  1 
ATOM   5493 H  HG2  . GLU   B 1 114 ? 29.451 -18.452 -1.257  1.00 16.08 ?  114 GLU   B HG2  1 
ATOM   5494 H  HG3  . GLU   B 1 114 ? 30.216 -19.521 -0.373  1.00 16.08 ?  114 GLU   B HG3  1 
ATOM   5495 N  N    . ASN   B 1 115 ? 34.356 -16.976 -1.025  1.00 12.45 ?  115 ASN   B N    1 
ATOM   5496 C  CA   . ASN   B 1 115 ? 35.352 -15.949 -1.321  1.00 12.43 ?  115 ASN   B CA   1 
ATOM   5497 C  C    . ASN   B 1 115 ? 35.769 -15.966 -2.788  1.00 12.24 ?  115 ASN   B C    1 
ATOM   5498 O  O    . ASN   B 1 115 ? 36.150 -14.929 -3.340  1.00 12.54 ?  115 ASN   B O    1 
ATOM   5499 C  CB   . ASN   B 1 115 ? 36.591 -16.145 -0.440  1.00 13.20 ?  115 ASN   B CB   1 
ATOM   5500 C  CG   . ASN   B 1 115 ? 36.329 -15.868 1.022   1.00 13.40 ?  115 ASN   B CG   1 
ATOM   5501 O  OD1  . ASN   B 1 115 ? 36.314 -14.714 1.449   1.00 15.38 ?  115 ASN   B OD1  1 
ATOM   5502 N  ND2  . ASN   B 1 115 ? 36.163 -16.924 1.809   1.00 13.20 ?  115 ASN   B ND2  1 
ATOM   5503 H  H    . ASN   B 1 115 ? 34.584 -17.534 -0.406  1.00 14.94 ?  115 ASN   B H    1 
ATOM   5504 H  HA   . ASN   B 1 115 ? 34.984 -15.076 -1.122  1.00 14.93 ?  115 ASN   B HA   1 
ATOM   5505 H  HB2  . ASN   B 1 115 ? 36.898 -17.063 -0.520  1.00 15.85 ?  115 ASN   B HB2  1 
ATOM   5506 H  HB3  . ASN   B 1 115 ? 37.290 -15.539 -0.733  1.00 15.85 ?  115 ASN   B HB3  1 
ATOM   5507 H  HD21 . ASN   B 1 115 ? 36.020 -16.814 2.650   1.00 15.85 ?  115 ASN   B HD21 1 
ATOM   5508 H  HD22 . ASN   B 1 115 ? 36.190 -17.716 1.477   1.00 15.85 ?  115 ASN   B HD22 1 
ATOM   5509 N  N    . PHE   B 1 116 ? 35.751 -17.140 -3.425  1.00 12.15 ?  116 PHE   B N    1 
ATOM   5510 C  CA   . PHE   B 1 116 ? 36.168 -17.236 -4.819  1.00 12.38 ?  116 PHE   B CA   1 
ATOM   5511 C  C    . PHE   B 1 116 ? 35.271 -16.410 -5.730  1.00 11.49 ?  116 PHE   B C    1 
ATOM   5512 O  O    . PHE   B 1 116 ? 35.709 -15.977 -6.801  1.00 12.61 ?  116 PHE   B O    1 
ATOM   5513 C  CB   . PHE   B 1 116 ? 36.121 -18.688 -5.328  1.00 11.74 ?  116 PHE   B CB   1 
ATOM   5514 C  CG   . PHE   B 1 116 ? 37.202 -19.632 -4.793  1.00 12.23 ?  116 PHE   B CG   1 
ATOM   5515 C  CD1  . PHE   B 1 116 ? 37.844 -19.447 -3.581  1.00 12.54 ?  116 PHE   B CD1  1 
ATOM   5516 C  CD2  . PHE   B 1 116 ? 37.522 -20.770 -5.537  1.00 12.73 ?  116 PHE   B CD2  1 
ATOM   5517 C  CE1  . PHE   B 1 116 ? 38.795 -20.374 -3.131  1.00 13.20 ?  116 PHE   B CE1  1 
ATOM   5518 C  CE2  . PHE   B 1 116 ? 38.465 -21.701 -5.086  1.00 12.68 ?  116 PHE   B CE2  1 
ATOM   5519 C  CZ   . PHE   B 1 116 ? 39.095 -21.499 -3.891  1.00 12.66 ?  116 PHE   B CZ   1 
ATOM   5520 H  H    . PHE   B 1 116 ? 35.499 -17.886 -3.076  1.00 14.59 ?  116 PHE   B H    1 
ATOM   5521 H  HA   . PHE   B 1 116 ? 37.076 -16.914 -4.912  1.00 14.86 ?  116 PHE   B HA   1 
ATOM   5522 H  HB2  . PHE   B 1 116 ? 35.254 -19.067 -5.085  1.00 14.10 ?  116 PHE   B HB2  1 
ATOM   5523 H  HB3  . PHE   B 1 116 ? 36.196 -18.678 -6.295  1.00 14.10 ?  116 PHE   B HB3  1 
ATOM   5524 H  HD1  . PHE   B 1 116 ? 37.640 -18.707 -3.058  1.00 15.05 ?  116 PHE   B HD1  1 
ATOM   5525 H  HD2  . PHE   B 1 116 ? 37.087 -20.922 -6.347  1.00 15.29 ?  116 PHE   B HD2  1 
ATOM   5526 H  HE1  . PHE   B 1 116 ? 39.230 -20.238 -2.320  1.00 15.85 ?  116 PHE   B HE1  1 
ATOM   5527 H  HE2  . PHE   B 1 116 ? 38.671 -22.444 -5.607  1.00 15.23 ?  116 PHE   B HE2  1 
ATOM   5528 H  HZ   . PHE   B 1 116 ? 39.739 -22.101 -3.597  1.00 15.20 ?  116 PHE   B HZ   1 
ATOM   5529 N  N    . ASN   B 1 117 ? 34.003 -16.198 -5.344  1.00 11.97 ?  117 ASN   B N    1 
ATOM   5530 C  CA   . ASN   B 1 117 ? 33.066 -15.494 -6.211  1.00 12.08 ?  117 ASN   B CA   1 
ATOM   5531 C  C    . ASN   B 1 117 ? 33.383 -14.017 -6.371  1.00 12.16 ?  117 ASN   B C    1 
ATOM   5532 O  O    . ASN   B 1 117 ? 32.785 -13.366 -7.235  1.00 13.66 ?  117 ASN   B O    1 
ATOM   5533 C  CB   . ASN   B 1 117 ? 31.635 -15.706 -5.716  1.00 13.07 ?  117 ASN   B CB   1 
ATOM   5534 C  CG   . ASN   B 1 117 ? 31.167 -17.122 -5.960  1.00 12.77 ?  117 ASN   B CG   1 
ATOM   5535 O  OD1  . ASN   B 1 117 ? 31.524 -17.716 -6.987  1.00 13.88 ?  117 ASN   B OD1  1 
ATOM   5536 N  ND2  . ASN   B 1 117 ? 30.433 -17.696 -5.012  1.00 13.50 ?  117 ASN   B ND2  1 
ATOM   5537 H  H    . ASN   B 1 117 ? 33.675 -16.445 -4.582  1.00 14.38 ?  117 ASN   B H    1 
ATOM   5538 H  HA   . ASN   B 1 117 ? 33.122 -15.895 -7.087  1.00 14.50 ?  117 ASN   B HA   1 
ATOM   5539 H  HB2  . ASN   B 1 117 ? 31.595 -15.535 -4.757  1.00 15.70 ?  117 ASN   B HB2  1 
ATOM   5540 H  HB3  . ASN   B 1 117 ? 31.040 -15.102 -6.185  1.00 15.70 ?  117 ASN   B HB3  1 
ATOM   5541 H  HD21 . ASN   B 1 117 ? 30.151 -18.505 -5.113  1.00 16.21 ?  117 ASN   B HD21 1 
ATOM   5542 H  HD22 . ASN   B 1 117 ? 30.214 -17.256 -4.304  1.00 16.21 ?  117 ASN   B HD22 1 
ATOM   5543 N  N    . GLN   B 1 118 ? 34.301 -13.481 -5.577  1.00 12.55 ?  118 GLN   B N    1 
ATOM   5544 C  CA   . GLN   B 1 118 ? 34.725 -12.091 -5.719  1.00 12.97 ?  118 GLN   B CA   1 
ATOM   5545 C  C    . GLN   B 1 118 ? 35.797 -11.900 -6.791  1.00 13.97 ?  118 GLN   B C    1 
ATOM   5546 O  O    . GLN   B 1 118 ? 36.291 -10.782 -6.965  1.00 14.77 ?  118 GLN   B O    1 
ATOM   5547 C  CB   . GLN   B 1 118 ? 35.208 -11.562 -4.364  1.00 13.82 ?  118 GLN   B CB   1 
ATOM   5548 C  CG   . GLN   B 1 118 ? 34.127 -11.600 -3.294  1.00 14.38 ?  118 GLN   B CG   1 
ATOM   5549 C  CD   . GLN   B 1 118 ? 32.964 -10.697 -3.627  1.00 13.88 ?  118 GLN   B CD   1 
ATOM   5550 O  OE1  . GLN   B 1 118 ? 33.157 -9.550  -4.053  1.00 14.89 ?  118 GLN   B OE1  1 
ATOM   5551 N  NE2  . GLN   B 1 118 ? 31.751 -11.195 -3.438  1.00 14.76 ?  118 GLN   B NE2  1 
ATOM   5552 H  H    . GLN   B 1 118 ? 34.713 -13.903 -4.946  1.00 15.07 ?  118 GLN   B H    1 
ATOM   5553 H  HA   . GLN   B 1 118 ? 33.959 -11.562 -5.988  1.00 15.57 ?  118 GLN   B HA   1 
ATOM   5554 H  HB2  . GLN   B 1 118 ? 35.955 -12.099 -4.061  1.00 16.60 ?  118 GLN   B HB2  1 
ATOM   5555 H  HB3  . GLN   B 1 118 ? 35.488 -10.636 -4.466  1.00 16.60 ?  118 GLN   B HB3  1 
ATOM   5556 H  HG2  . GLN   B 1 118 ? 33.801 -12.515 -3.216  1.00 17.27 ?  118 GLN   B HG2  1 
ATOM   5557 H  HG3  . GLN   B 1 118 ? 34.509 -11.313 -2.452  1.00 17.27 ?  118 GLN   B HG3  1 
ATOM   5558 H  HE21 . GLN   B 1 118 ? 31.657 -11.997 -3.139  1.00 17.72 ?  118 GLN   B HE21 1 
ATOM   5559 H  HE22 . GLN   B 1 118 ? 31.066 -10.719 -3.624  1.00 17.72 ?  118 GLN   B HE22 1 
ATOM   5560 N  N    . HIS   B 1 119 ? 36.162 -12.956 -7.519  1.00 12.88 ?  119 HIS   B N    1 
ATOM   5561 C  CA   . HIS   B 1 119 ? 37.197 -12.911 -8.544  1.00 13.05 ?  119 HIS   B CA   1 
ATOM   5562 C  C    . HIS   B 1 119 ? 36.714 -13.656 -9.778  1.00 12.83 ?  119 HIS   B C    1 
ATOM   5563 O  O    . HIS   B 1 119 ? 36.232 -14.787 -9.674  1.00 13.93 ?  119 HIS   B O    1 
ATOM   5564 C  CB   . HIS   B 1 119 ? 38.482 -13.539 -7.994  1.00 13.51 ?  119 HIS   B CB   1 
ATOM   5565 C  CG   . HIS   B 1 119 ? 38.968 -12.847 -6.765  1.00 14.33 ?  119 HIS   B CG   1 
ATOM   5566 N  ND1  . HIS   B 1 119 ? 39.755 -11.715 -6.814  1.00 17.08 ?  119 HIS   B ND1  1 
ATOM   5567 C  CD2  . HIS   B 1 119 ? 38.683 -13.054 -5.458  1.00 16.17 ?  119 HIS   B CD2  1 
ATOM   5568 C  CE1  . HIS   B 1 119 ? 39.971 -11.285 -5.585  1.00 18.51 ?  119 HIS   B CE1  1 
ATOM   5569 N  NE2  . HIS   B 1 119 ? 39.325 -12.073 -4.745  1.00 18.54 ?  119 HIS   B NE2  1 
ATOM   5570 H  H    . HIS   B 1 119 ? 35.804 -13.738 -7.440  1.00 15.46 ?  119 HIS   B H    1 
ATOM   5571 H  HA   . HIS   B 1 119 ? 37.376 -11.987 -8.786  1.00 15.67 ?  119 HIS   B HA   1 
ATOM   5572 H  HB2  . HIS   B 1 119 ? 38.314 -14.466 -7.776  1.00 16.22 ?  119 HIS   B HB2  1 
ATOM   5573 H  HB3  . HIS   B 1 119 ? 39.177 -13.477 -8.673  1.00 16.22 ?  119 HIS   B HB3  1 
ATOM   5574 H  HD2  . HIS   B 1 119 ? 38.154 -13.737 -5.113  1.00 19.41 ?  119 HIS   B HD2  1 
ATOM   5575 H  HE1  . HIS   B 1 119 ? 40.497 -10.555 -5.345  1.00 22.23 ?  119 HIS   B HE1  1 
ATOM   5576 H  HE2  . HIS   B 1 119 ? 39.329 -12.002 -3.887  1.00 22.26 ?  119 HIS   B HE2  1 
ATOM   5577 N  N    . GLU   B 1 120 ? 36.870 -13.041 -10.952 1.00 13.66 ?  120 GLU   B N    1 
ATOM   5578 C  CA   . GLU   B 1 120 ? 36.284 -13.623 -12.153 1.00 14.74 ?  120 GLU   B CA   1 
ATOM   5579 C  C    . GLU   B 1 120 ? 36.968 -14.920 -12.568 1.00 14.04 ?  120 GLU   B C    1 
ATOM   5580 O  O    . GLU   B 1 120 ? 36.308 -15.788 -13.146 1.00 13.88 ?  120 GLU   B O    1 
ATOM   5581 C  CB   . GLU   B 1 120 ? 36.285 -12.618 -13.302 1.00 19.76 ?  120 GLU   B CB   1 
ATOM   5582 C  CG   . GLU   B 1 120 ? 35.321 -11.469 -13.071 1.00 25.90 ?  120 GLU   B CG   1 
ATOM   5583 C  CD   . GLU   B 1 120 ? 35.161 -10.565 -14.277 1.00 32.26 ?  120 GLU   B CD   1 
ATOM   5584 O  OE1  . GLU   B 1 120 ? 36.158 -10.354 -15.004 1.00 35.11 ?  120 GLU   B OE1  1 
ATOM   5585 O  OE2  . GLU   B 1 120 ? 34.038 -10.066 -14.492 1.00 35.98 -1 120 GLU   B OE2  1 
ATOM   5586 H  H    . GLU   B 1 120 ? 37.306 -12.303 -11.079 1.00 16.40 ?  120 GLU   B H    1 
ATOM   5587 H  HA   . GLU   B 1 120 ? 35.365 -13.842 -11.959 1.00 17.70 ?  120 GLU   B HA   1 
ATOM   5588 H  HB2  . GLU   B 1 120 ? 37.174 -12.248 -13.405 1.00 23.72 ?  120 GLU   B HB2  1 
ATOM   5589 H  HB3  . GLU   B 1 120 ? 36.017 -13.073 -14.118 1.00 23.72 ?  120 GLU   B HB3  1 
ATOM   5590 H  HG2  . GLU   B 1 120 ? 34.447 -11.830 -12.850 1.00 31.09 ?  120 GLU   B HG2  1 
ATOM   5591 H  HG3  . GLU   B 1 120 ? 35.649 -10.927 -12.337 1.00 31.09 ?  120 GLU   B HG3  1 
ATOM   5592 N  N    . VAL   B 1 121 ? 38.267 -15.070 -12.296 1.00 13.25 ?  121 VAL   B N    1 
ATOM   5593 C  CA   . VAL   B 1 121 ? 39.017 -16.277 -12.651 1.00 13.13 ?  121 VAL   B CA   1 
ATOM   5594 C  C    . VAL   B 1 121 ? 40.130 -16.481 -11.633 1.00 13.02 ?  121 VAL   B C    1 
ATOM   5595 O  O    . VAL   B 1 121 ? 40.802 -15.522 -11.236 1.00 13.42 ?  121 VAL   B O    1 
ATOM   5596 C  CB   . VAL   B 1 121 ? 39.538 -16.228 -14.107 1.00 15.10 ?  121 VAL   B CB   1 
ATOM   5597 C  CG1  . VAL   B 1 121 ? 40.410 -14.994 -14.352 1.00 17.36 ?  121 VAL   B CG1  1 
ATOM   5598 C  CG2  . VAL   B 1 121 ? 40.284 -17.509 -14.471 1.00 16.85 ?  121 VAL   B CG2  1 
ATOM   5599 H  H    . VAL   B 1 121 ? 38.751 -14.469 -11.911 1.00 15.91 ?  121 VAL   B H    1 
ATOM   5600 H  HA   . VAL   B 1 121 ? 38.415 -17.030 -12.591 1.00 15.77 ?  121 VAL   B HA   1 
ATOM   5601 H  HB   . VAL   B 1 121 ? 38.775 -16.160 -14.705 1.00 18.13 ?  121 VAL   B HB   1 
ATOM   5602 H  HG11 . VAL   B 1 121 ? 40.716 -15.002 -15.274 1.00 20.84 ?  121 VAL   B HG11 1 
ATOM   5603 H  HG12 . VAL   B 1 121 ? 39.883 -14.197 -14.188 1.00 20.84 ?  121 VAL   B HG12 1 
ATOM   5604 H  HG13 . VAL   B 1 121 ? 41.170 -15.020 -13.752 1.00 20.84 ?  121 VAL   B HG13 1 
ATOM   5605 H  HG21 . VAL   B 1 121 ? 40.491 -17.492 -15.421 1.00 20.23 ?  121 VAL   B HG21 1 
ATOM   5606 H  HG22 . VAL   B 1 121 ? 41.105 -17.552 -13.957 1.00 20.23 ?  121 VAL   B HG22 1 
ATOM   5607 H  HG23 . VAL   B 1 121 ? 39.721 -18.268 -14.269 1.00 20.23 ?  121 VAL   B HG23 1 
ATOM   5608 N  N    . LEU   B 1 122 ? 40.312 -17.734 -11.199 1.00 12.65 ?  122 LEU   B N    1 
ATOM   5609 C  CA   . LEU   B 1 122 ? 41.299 -18.088 -10.180 1.00 11.99 ?  122 LEU   B CA   1 
ATOM   5610 C  C    . LEU   B 1 122 ? 41.958 -19.421 -10.500 1.00 12.04 ?  122 LEU   B C    1 
ATOM   5611 O  O    . LEU   B 1 122 ? 41.300 -20.340 -10.997 1.00 13.44 ?  122 LEU   B O    1 
ATOM   5612 C  CB   . LEU   B 1 122 ? 40.666 -18.311 -8.794  1.00 14.37 ?  122 LEU   B CB   1 
ATOM   5613 C  CG   . LEU   B 1 122 ? 39.626 -17.293 -8.314  1.00 14.61 ?  122 LEU   B CG   1 
ATOM   5614 C  CD1  . LEU   B 1 122 ? 38.208 -17.680 -8.762  1.00 15.77 ?  122 LEU   B CD1  1 
ATOM   5615 C  CD2  . LEU   B 1 122 ? 39.691 -17.150 -6.807  1.00 14.11 ?  122 LEU   B CD2  1 
ATOM   5616 H  H    . LEU   B 1 122 ? 39.862 -18.414 -11.485 1.00 15.19 ?  122 LEU   B H    1 
ATOM   5617 H  HA   . LEU   B 1 122 ? 41.977 -17.396 -10.111 1.00 14.39 ?  122 LEU   B HA   1 
ATOM   5618 H  HB2  . LEU   B 1 122 ? 40.224 -19.175 -8.803  1.00 17.25 ?  122 LEU   B HB2  1 
ATOM   5619 H  HB3  . LEU   B 1 122 ? 41.373 -18.320 -8.136  1.00 17.25 ?  122 LEU   B HB3  1 
ATOM   5620 H  HG   . LEU   B 1 122 ? 39.833 -16.428 -8.702  1.00 17.53 ?  122 LEU   B HG   1 
ATOM   5621 H  HD11 . LEU   B 1 122 ? 37.580 -17.024 -8.416  1.00 18.93 ?  122 LEU   B HD11 1 
ATOM   5622 H  HD12 . LEU   B 1 122 ? 38.174 -17.687 -9.731  1.00 18.93 ?  122 LEU   B HD12 1 
ATOM   5623 H  HD13 . LEU   B 1 122 ? 37.995 -18.557 -8.414  1.00 18.93 ?  122 LEU   B HD13 1 
ATOM   5624 H  HD21 . LEU   B 1 122 ? 39.009 -16.524 -6.518  1.00 16.94 ?  122 LEU   B HD21 1 
ATOM   5625 H  HD22 . LEU   B 1 122 ? 39.545 -18.015 -6.399  1.00 16.94 ?  122 LEU   B HD22 1 
ATOM   5626 H  HD23 . LEU   B 1 122 ? 40.571 -16.812 -6.561  1.00 16.94 ?  122 LEU   B HD23 1 
ATOM   5627 N  N    . LEU   B 1 123 ? 43.249 -19.524 -10.158 1.00 11.99 ?  123 LEU   B N    1 
ATOM   5628 C  CA   . LEU   B 1 123 ? 43.964 -20.794 -10.028 1.00 12.41 ?  123 LEU   B CA   1 
ATOM   5629 C  C    . LEU   B 1 123 ? 43.933 -21.182 -8.552  1.00 11.88 ?  123 LEU   B C    1 
ATOM   5630 O  O    . LEU   B 1 123 ? 44.291 -20.352 -7.699  1.00 12.13 ?  123 LEU   B O    1 
ATOM   5631 C  CB   . LEU   B 1 123 ? 45.418 -20.608 -10.483 1.00 12.85 ?  123 LEU   B CB   1 
ATOM   5632 C  CG   . LEU   B 1 123 ? 46.350 -21.797 -10.238 1.00 13.07 ?  123 LEU   B CG   1 
ATOM   5633 C  CD1  . LEU   B 1 123 ? 45.919 -23.031 -11.023 1.00 14.12 ?  123 LEU   B CD1  1 
ATOM   5634 C  CD2  . LEU   B 1 123 ? 47.782 -21.395 -10.577 1.00 14.09 ?  123 LEU   B CD2  1 
ATOM   5635 H  H    . LEU   B 1 123 ? 43.753 -18.843 -9.986  1.00 14.40 ?  123 LEU   B H    1 
ATOM   5636 H  HA   . LEU   B 1 123 ? 43.539 -21.484 -10.563 1.00 14.90 ?  123 LEU   B HA   1 
ATOM   5637 H  HB2  . LEU   B 1 123 ? 45.421 -20.436 -11.439 1.00 15.42 ?  123 LEU   B HB2  1 
ATOM   5638 H  HB3  . LEU   B 1 123 ? 45.791 -19.848 -10.016 1.00 15.42 ?  123 LEU   B HB3  1 
ATOM   5639 H  HG   . LEU   B 1 123 ? 46.329 -22.027 -9.294  1.00 15.70 ?  123 LEU   B HG   1 
ATOM   5640 H  HD11 . LEU   B 1 123 ? 46.552 -23.746 -10.861 1.00 16.95 ?  123 LEU   B HD11 1 
ATOM   5641 H  HD12 . LEU   B 1 123 ? 45.033 -23.300 -10.726 1.00 16.95 ?  123 LEU   B HD12 1 
ATOM   5642 H  HD13 . LEU   B 1 123 ? 45.898 -22.812 -11.967 1.00 16.95 ?  123 LEU   B HD13 1 
ATOM   5643 H  HD21 . LEU   B 1 123 ? 48.369 -22.151 -10.420 1.00 16.91 ?  123 LEU   B HD21 1 
ATOM   5644 H  HD22 . LEU   B 1 123 ? 47.822 -21.133 -11.510 1.00 16.91 ?  123 LEU   B HD22 1 
ATOM   5645 H  HD23 . LEU   B 1 123 ? 48.043 -20.651 -10.012 1.00 16.91 ?  123 LEU   B HD23 1 
ATOM   5646 N  N    . ALA   B 1 124 ? 43.504 -22.417 -8.241  1.00 11.93 ?  124 ALA   B N    1 
ATOM   5647 C  CA   . ALA   B 1 124 ? 43.228 -22.740 -6.846  1.00 11.84 ?  124 ALA   B CA   1 
ATOM   5648 C  C    . ALA   B 1 124 ? 43.496 -24.202 -6.508  1.00 11.52 ?  124 ALA   B C    1 
ATOM   5649 O  O    . ALA   B 1 124 ? 43.360 -25.079 -7.371  1.00 12.11 ?  124 ALA   B O    1 
ATOM   5650 C  CB   . ALA   B 1 124 ? 41.768 -22.412 -6.498  1.00 12.56 ?  124 ALA   B CB   1 
ATOM   5651 H  H    . ALA   B 1 124 ? 43.371 -23.063 -8.805  1.00 14.32 ?  124 ALA   B H    1 
ATOM   5652 H  HA   . ALA   B 1 124 ? 43.795 -22.190 -6.297  1.00 14.22 ?  124 ALA   B HA   1 
ATOM   5653 H  HB1  . ALA   B 1 124 ? 41.604 -22.631 -5.570  1.00 15.08 ?  124 ALA   B HB1  1 
ATOM   5654 H  HB2  . ALA   B 1 124 ? 41.615 -21.463 -6.647  1.00 15.08 ?  124 ALA   B HB2  1 
ATOM   5655 H  HB3  . ALA   B 1 124 ? 41.178 -22.930 -7.071  1.00 15.08 ?  124 ALA   B HB3  1 
ATOM   5656 N  N    . PRO   B 1 125 ? 43.812 -24.491 -5.250  1.00 11.84 ?  125 PRO   B N    1 
ATOM   5657 C  CA   . PRO   B 1 125 ? 43.751 -25.859 -4.733  1.00 13.12 ?  125 PRO   B CA   1 
ATOM   5658 C  C    . PRO   B 1 125 ? 42.350 -26.135 -4.188  1.00 13.03 ?  125 PRO   B C    1 
ATOM   5659 O  O    . PRO   B 1 125 ? 41.546 -25.228 -3.980  1.00 13.57 ?  125 PRO   B O    1 
ATOM   5660 C  CB   . PRO   B 1 125 ? 44.743 -25.799 -3.567  1.00 14.16 ?  125 PRO   B CB   1 
ATOM   5661 C  CG   . PRO   B 1 125 ? 44.507 -24.400 -3.001  1.00 13.96 ?  125 PRO   B CG   1 
ATOM   5662 C  CD   . PRO   B 1 125 ? 44.149 -23.526 -4.191  1.00 12.18 ?  125 PRO   B CD   1 
ATOM   5663 H  HA   . PRO   B 1 125 ? 44.022 -26.526 -5.387  1.00 15.76 ?  125 PRO   B HA   1 
ATOM   5664 H  HB2  . PRO   B 1 125 ? 44.534 -26.478 -2.907  1.00 17.00 ?  125 PRO   B HB2  1 
ATOM   5665 H  HB3  . PRO   B 1 125 ? 45.655 -25.892 -3.889  1.00 17.00 ?  125 PRO   B HB3  1 
ATOM   5666 H  HG2  . PRO   B 1 125 ? 43.771 -24.419 -2.366  1.00 16.76 ?  125 PRO   B HG2  1 
ATOM   5667 H  HG3  . PRO   B 1 125 ? 45.315 -24.073 -2.570  1.00 16.76 ?  125 PRO   B HG3  1 
ATOM   5668 H  HD2  . PRO   B 1 125 ? 43.381 -22.965 -3.998  1.00 14.62 ?  125 PRO   B HD2  1 
ATOM   5669 H  HD3  . PRO   B 1 125 ? 44.915 -22.983 -4.463  1.00 14.62 ?  125 PRO   B HD3  1 
ATOM   5670 N  N    . LEU   B 1 126 ? 42.076 -27.414 -3.921  1.00 13.73 ?  126 LEU   B N    1 
ATOM   5671 C  CA   . LEU   B 1 126 ? 40.851 -27.792 -3.212  1.00 13.69 ?  126 LEU   B CA   1 
ATOM   5672 C  C    . LEU   B 1 126 ? 40.951 -27.388 -1.745  1.00 13.53 ?  126 LEU   B C    1 
ATOM   5673 O  O    . LEU   B 1 126 ? 41.837 -27.853 -1.018  1.00 15.69 ?  126 LEU   B O    1 
ATOM   5674 C  CB   . LEU   B 1 126 ? 40.598 -29.296 -3.332  1.00 15.15 ?  126 LEU   B CB   1 
ATOM   5675 C  CG   . LEU   B 1 126 ? 40.067 -29.786 -4.683  1.00 16.01 ?  126 LEU   B CG   1 
ATOM   5676 C  CD1  . LEU   B 1 126 ? 40.118 -31.303 -4.759  1.00 18.12 ?  126 LEU   B CD1  1 
ATOM   5677 C  CD2  . LEU   B 1 126 ? 38.649 -29.291 -4.952  1.00 17.06 ?  126 LEU   B CD2  1 
ATOM   5678 H  H    . LEU   B 1 126 ? 42.583 -28.080 -4.131  1.00 16.48 ?  126 LEU   B H    1 
ATOM   5679 H  HA   . LEU   B 1 126 ? 40.100 -27.320 -3.605  1.00 16.43 ?  126 LEU   B HA   1 
ATOM   5680 H  HB2  . LEU   B 1 126 ? 41.428 -29.760 -3.164  1.00 18.19 ?  126 LEU   B HB2  1 
ATOM   5681 H  HB3  . LEU   B 1 126 ? 39.943 -29.546 -2.658  1.00 18.19 ?  126 LEU   B HB3  1 
ATOM   5682 H  HG   . LEU   B 1 126 ? 40.636 -29.425 -5.384  1.00 19.22 ?  126 LEU   B HG   1 
ATOM   5683 H  HD11 . LEU   B 1 126 ? 39.775 -31.585 -5.621  1.00 21.75 ?  126 LEU   B HD11 1 
ATOM   5684 H  HD12 . LEU   B 1 126 ? 41.034 -31.590 -4.652  1.00 21.75 ?  126 LEU   B HD12 1 
ATOM   5685 H  HD13 . LEU   B 1 126 ? 39.567 -31.669 -4.048  1.00 21.75 ?  126 LEU   B HD13 1 
ATOM   5686 H  HD21 . LEU   B 1 126 ? 38.326 -29.689 -5.777  1.00 20.48 ?  126 LEU   B HD21 1 
ATOM   5687 H  HD22 . LEU   B 1 126 ? 38.076 -29.550 -4.215  1.00 20.48 ?  126 LEU   B HD22 1 
ATOM   5688 H  HD23 . LEU   B 1 126 ? 38.654 -28.321 -5.039  1.00 20.48 ?  126 LEU   B HD23 1 
ATOM   5689 N  N    . LEU   B 1 127 ? 40.013 -26.562 -1.288  1.00 13.97 ?  127 LEU   B N    1 
ATOM   5690 C  CA   . LEU   B 1 127 ? 40.080 -26.060 0.074   1.00 13.95 ?  127 LEU   B CA   1 
ATOM   5691 C  C    . LEU   B 1 127 ? 39.814 -27.175 1.079   1.00 14.12 ?  127 LEU   B C    1 
ATOM   5692 O  O    . LEU   B 1 127 ? 38.995 -28.074 0.856   1.00 14.11 ?  127 LEU   B O    1 
ATOM   5693 C  CB   . LEU   B 1 127 ? 39.068 -24.931 0.281   1.00 15.16 ?  127 LEU   B CB   1 
ATOM   5694 C  CG   . LEU   B 1 127 ? 39.252 -23.663 -0.553  1.00 14.61 ?  127 LEU   B CG   1 
ATOM   5695 C  CD1  . LEU   B 1 127 ? 38.123 -22.704 -0.240  1.00 15.41 ?  127 LEU   B CD1  1 
ATOM   5696 C  CD2  . LEU   B 1 127 ? 40.606 -23.021 -0.297  1.00 15.32 ?  127 LEU   B CD2  1 
ATOM   5697 H  H    . LEU   B 1 127 ? 39.341 -26.274 -1.742  1.00 16.77 ?  127 LEU   B H    1 
ATOM   5698 H  HA   . LEU   B 1 127 ? 40.974 -25.702 0.238   1.00 16.75 ?  127 LEU   B HA   1 
ATOM   5699 H  HB2  . LEU   B 1 127 ? 38.187 -25.277 0.084   1.00 18.20 ?  127 LEU   B HB2  1 
ATOM   5700 H  HB3  . LEU   B 1 127 ? 39.104 -24.662 1.215   1.00 18.20 ?  127 LEU   B HB3  1 
ATOM   5701 H  HG   . LEU   B 1 127 ? 39.193 -23.885 -1.493  1.00 17.54 ?  127 LEU   B HG   1 
ATOM   5702 H  HD11 . LEU   B 1 127 ? 38.239 -21.894 -0.763  1.00 18.51 ?  127 LEU   B HD11 1 
ATOM   5703 H  HD12 . LEU   B 1 127 ? 37.278 -23.124 -0.464  1.00 18.51 ?  127 LEU   B HD12 1 
ATOM   5704 H  HD13 . LEU   B 1 127 ? 38.144 -22.489 0.707   1.00 18.51 ?  127 LEU   B HD13 1 
ATOM   5705 H  HD21 . LEU   B 1 127 ? 40.647 -22.167 -0.760  1.00 18.39 ?  127 LEU   B HD21 1 
ATOM   5706 H  HD22 . LEU   B 1 127 ? 40.716 -22.881 0.657   1.00 18.39 ?  127 LEU   B HD22 1 
ATOM   5707 H  HD23 . LEU   B 1 127 ? 41.300 -23.609 -0.629  1.00 18.39 ?  127 LEU   B HD23 1 
ATOM   5708 N  N    . SER   B 1 128 ? 40.504 -27.091 2.208   1.00 14.30 ?  128 SER   B N    1 
ATOM   5709 C  CA   . SER   B 1 128 ? 40.390 -28.011 3.330   1.00 14.74 ?  128 SER   B CA   1 
ATOM   5710 C  C    . SER   B 1 128 ? 40.893 -29.417 3.008   1.00 15.23 ?  128 SER   B C    1 
ATOM   5711 O  O    . SER   B 1 128 ? 40.781 -30.299 3.853   1.00 16.68 ?  128 SER   B O    1 
ATOM   5712 C  CB   . SER   B 1 128 ? 38.980 -28.034 3.947   1.00 15.49 ?  128 SER   B CB   1 
ATOM   5713 O  OG   . SER   B 1 128 ? 38.651 -26.758 4.508   1.00 15.79 ?  128 SER   B OG   1 
ATOM   5714 H  H    . SER   B 1 128 ? 41.076 -26.467 2.355   1.00 17.16 ?  128 SER   B H    1 
ATOM   5715 H  HA   . SER   B 1 128 ? 40.970 -27.674 4.022   1.00 17.70 ?  128 SER   B HA   1 
ATOM   5716 H  HB2  . SER   B 1 128 ? 38.331 -28.256 3.261   1.00 18.60 ?  128 SER   B HB2  1 
ATOM   5717 H  HB3  . SER   B 1 128 ? 38.954 -28.707 4.652   1.00 18.60 ?  128 SER   B HB3  1 
ATOM   5718 H  HG   . SER   B 1 128 ? 39.216 -26.563 5.103   1.00 18.96 ?  128 SER   B HG   1 
ATOM   5719 N  N    . ALA   B 1 129 ? 41.485 -29.637 1.833   1.00 16.59 ?  129 ALA   B N    1 
ATOM   5720 C  CA   . ALA   B 1 129 ? 42.029 -30.941 1.478   1.00 17.53 ?  129 ALA   B CA   1 
ATOM   5721 C  C    . ALA   B 1 129 ? 43.420 -31.124 2.070   1.00 16.43 ?  129 ALA   B C    1 
ATOM   5722 O  O    . ALA   B 1 129 ? 43.971 -30.233 2.730   1.00 16.19 ?  129 ALA   B O    1 
ATOM   5723 C  CB   . ALA   B 1 129 ? 42.071 -31.106 -0.038  1.00 19.95 ?  129 ALA   B CB   1 
ATOM   5724 H  H    . ALA   B 1 129 ? 41.593 -29.039 1.223   1.00 19.92 ?  129 ALA   B H    1 
ATOM   5725 H  HA   . ALA   B 1 129 ? 41.462 -31.632 1.844   1.00 21.04 ?  129 ALA   B HA   1 
ATOM   5726 H  HB1  . ALA   B 1 129 ? 42.425 -31.985 -0.249  1.00 23.95 ?  129 ALA   B HB1  1 
ATOM   5727 H  HB2  . ALA   B 1 129 ? 41.172 -31.018 -0.385  1.00 23.95 ?  129 ALA   B HB2  1 
ATOM   5728 H  HB3  . ALA   B 1 129 ? 42.644 -30.420 -0.415  1.00 23.95 ?  129 ALA   B HB3  1 
ATOM   5729 N  N    . GLY   B 1 130 ? 43.987 -32.310 1.832   1.00 16.86 ?  130 GLY   B N    1 
ATOM   5730 C  CA   . GLY   B 1 130 ? 45.373 -32.560 2.191   1.00 17.52 ?  130 GLY   B CA   1 
ATOM   5731 C  C    . GLY   B 1 130 ? 45.583 -32.468 3.686   1.00 17.94 ?  130 GLY   B C    1 
ATOM   5732 O  O    . GLY   B 1 130 ? 44.880 -33.110 4.479   1.00 18.39 ?  130 GLY   B O    1 
ATOM   5733 H  H    . GLY   B 1 130 ? 43.591 -32.975 1.464   1.00 20.24 ?  130 GLY   B H    1 
ATOM   5734 H  HA2  . GLY   B 1 130 ? 45.632 -33.448 1.895   1.00 21.03 ?  130 GLY   B HA2  1 
ATOM   5735 H  HA3  . GLY   B 1 130 ? 45.948 -31.911 1.757   1.00 21.03 ?  130 GLY   B HA3  1 
ATOM   5736 N  N    . ILE   B 1 131 ? 46.554 -31.641 4.084   1.00 18.04 ?  131 ILE   B N    1 
ATOM   5737 C  CA   . ILE   B 1 131 ? 46.901 -31.509 5.492   1.00 18.93 ?  131 ILE   B CA   1 
ATOM   5738 C  C    . ILE   B 1 131 ? 45.781 -30.906 6.321   1.00 17.68 ?  131 ILE   B C    1 
ATOM   5739 O  O    . ILE   B 1 131 ? 45.863 -30.944 7.552   1.00 19.45 ?  131 ILE   B O    1 
ATOM   5740 C  CB   . ILE   B 1 131 ? 48.216 -30.723 5.698   1.00 20.51 ?  131 ILE   B CB   1 
ATOM   5741 C  CG1  . ILE   B 1 131 ? 48.045 -29.243 5.331   1.00 21.34 ?  131 ILE   B CG1  1 
ATOM   5742 C  CG2  . ILE   B 1 131 ? 49.349 -31.338 4.880   1.00 21.98 ?  131 ILE   B CG2  1 
ATOM   5743 C  CD1  . ILE   B 1 131 ? 49.264 -28.383 5.647   1.00 22.57 ?  131 ILE   B CD1  1 
ATOM   5744 H  H    . ILE   B 1 131 ? 47.030 -31.155 3.557   1.00 21.66 ?  131 ILE   B H    1 
ATOM   5745 H  HA   . ILE   B 1 131 ? 47.050 -32.399 5.846   1.00 22.72 ?  131 ILE   B HA   1 
ATOM   5746 H  HB   . ILE   B 1 131 ? 48.455 -30.777 6.637   1.00 24.62 ?  131 ILE   B HB   1 
ATOM   5747 H  HG12 . ILE   B 1 131 ? 47.871 -29.179 4.380   1.00 25.62 ?  131 ILE   B HG12 1 
ATOM   5748 H  HG13 . ILE   B 1 131 ? 47.295 -28.875 5.826   1.00 25.62 ?  131 ILE   B HG13 1 
ATOM   5749 H  HG21 . ILE   B 1 131 ? 50.187 -30.938 5.154   1.00 26.38 ?  131 ILE   B HG21 1 
ATOM   5750 H  HG22 . ILE   B 1 131 ? 49.366 -32.293 5.038   1.00 26.38 ?  131 ILE   B HG22 1 
ATOM   5751 H  HG23 . ILE   B 1 131 ? 49.186 -31.160 3.940   1.00 26.38 ?  131 ILE   B HG23 1 
ATOM   5752 H  HD11 . ILE   B 1 131 ? 49.037 -27.452 5.495   1.00 27.09 ?  131 ILE   B HD11 1 
ATOM   5753 H  HD12 . ILE   B 1 131 ? 49.511 -28.516 6.575   1.00 27.09 ?  131 ILE   B HD12 1 
ATOM   5754 H  HD13 . ILE   B 1 131 ? 49.994 -28.646 5.068   1.00 27.09 ?  131 ILE   B HD13 1 
ATOM   5755 N  N    . PHE   B 1 132 ? 44.749 -30.335 5.685   1.00 16.50 ?  132 PHE   B N    1 
ATOM   5756 C  CA   . PHE   B 1 132 ? 43.587 -29.822 6.409   1.00 16.79 ?  132 PHE   B CA   1 
ATOM   5757 C  C    . PHE   B 1 132 ? 42.559 -30.907 6.740   1.00 18.00 ?  132 PHE   B C    1 
ATOM   5758 O  O    . PHE   B 1 132 ? 41.655 -30.650 7.542   1.00 20.31 ?  132 PHE   B O    1 
ATOM   5759 C  CB   . PHE   B 1 132 ? 42.908 -28.683 5.631   1.00 15.94 ?  132 PHE   B CB   1 
ATOM   5760 C  CG   . PHE   B 1 132 ? 43.595 -27.344 5.759   1.00 16.39 ?  132 PHE   B CG   1 
ATOM   5761 C  CD1  . PHE   B 1 132 ? 44.884 -27.147 5.283   1.00 17.42 ?  132 PHE   B CD1  1 
ATOM   5762 C  CD2  . PHE   B 1 132 ? 42.921 -26.262 6.309   1.00 15.46 ?  132 PHE   B CD2  1 
ATOM   5763 C  CE1  . PHE   B 1 132 ? 45.502 -25.900 5.390   1.00 17.98 ?  132 PHE   B CE1  1 
ATOM   5764 C  CE2  . PHE   B 1 132 ? 43.522 -25.012 6.405   1.00 16.44 ?  132 PHE   B CE2  1 
ATOM   5765 C  CZ   . PHE   B 1 132 ? 44.815 -24.835 5.951   1.00 18.17 ?  132 PHE   B CZ   1 
ATOM   5766 H  H    . PHE   B 1 132 ? 44.704 -30.231 4.830   1.00 19.80 ?  132 PHE   B H    1 
ATOM   5767 H  HA   . PHE   B 1 132 ? 43.895 -29.449 7.247   1.00 20.16 ?  132 PHE   B HA   1 
ATOM   5768 H  HB2  . PHE   B 1 132 ? 42.899 -28.911 4.691   1.00 19.14 ?  132 PHE   B HB2  1 
ATOM   5769 H  HB3  . PHE   B 1 132 ? 42.000 -28.579 5.956   1.00 19.14 ?  132 PHE   B HB3  1 
ATOM   5770 H  HD1  . PHE   B 1 132 ? 45.349 -27.858 4.908   1.00 20.92 ?  132 PHE   B HD1  1 
ATOM   5771 H  HD2  . PHE   B 1 132 ? 42.052 -26.371 6.621   1.00 18.57 ?  132 PHE   B HD2  1 
ATOM   5772 H  HE1  . PHE   B 1 132 ? 46.372 -25.782 5.078   1.00 21.59 ?  132 PHE   B HE1  1 
ATOM   5773 H  HE2  . PHE   B 1 132 ? 43.063 -24.298 6.793   1.00 19.74 ?  132 PHE   B HE2  1 
ATOM   5774 H  HZ   . PHE   B 1 132 ? 45.224 -23.998 6.025   1.00 21.81 ?  132 PHE   B HZ   1 
ATOM   5775 N  N    . GLY   B 1 133 ? 42.655 -32.102 6.143   1.00 17.26 ?  133 GLY   B N    1 
ATOM   5776 C  CA   . GLY   B 1 133 ? 41.945 -33.268 6.639   1.00 18.20 ?  133 GLY   B CA   1 
ATOM   5777 C  C    . GLY   B 1 133 ? 40.552 -33.532 6.103   1.00 18.15 ?  133 GLY   B C    1 
ATOM   5778 O  O    . GLY   B 1 133 ? 39.971 -34.563 6.462   1.00 21.09 ?  133 GLY   B O    1 
ATOM   5779 H  H    . GLY   B 1 133 ? 43.138 -32.256 5.446   1.00 20.72 ?  133 GLY   B H    1 
ATOM   5780 H  HA2  . GLY   B 1 133 ? 42.480 -34.051 6.452   1.00 21.85 ?  133 GLY   B HA2  1 
ATOM   5781 H  HA3  . GLY   B 1 133 ? 41.872 -33.186 7.604   1.00 21.85 ?  133 GLY   B HA3  1 
ATOM   5782 N  N    . ALA   B 1 134 ? 39.984 -32.660 5.277   1.00 17.49 ?  134 ALA   B N    1 
ATOM   5783 C  CA   . ALA   B 1 134 ? 38.663 -32.938 4.734   1.00 18.06 ?  134 ALA   B CA   1 
ATOM   5784 C  C    . ALA   B 1 134 ? 38.751 -33.934 3.580   1.00 17.98 ?  134 ALA   B C    1 
ATOM   5785 O  O    . ALA   B 1 134 ? 39.810 -34.148 2.983   1.00 19.09 ?  134 ALA   B O    1 
ATOM   5786 C  CB   . ALA   B 1 134 ? 37.998 -31.648 4.257   1.00 18.63 ?  134 ALA   B CB   1 
ATOM   5787 H  H    . ALA   B 1 134 ? 40.330 -31.911 5.032   1.00 21.00 ?  134 ALA   B H    1 
ATOM   5788 H  HA   . ALA   B 1 134 ? 38.107 -33.323 5.430   1.00 21.68 ?  134 ALA   B HA   1 
ATOM   5789 H  HB1  . ALA   B 1 134 ? 37.114 -31.857 3.916   1.00 22.37 ?  134 ALA   B HB1  1 
ATOM   5790 H  HB2  . ALA   B 1 134 ? 37.929 -31.033 5.003   1.00 22.37 ?  134 ALA   B HB2  1 
ATOM   5791 H  HB3  . ALA   B 1 134 ? 38.539 -31.256 3.553   1.00 22.37 ?  134 ALA   B HB3  1 
ATOM   5792 N  N    . ASP   B 1 135 ? 37.617 -34.562 3.285   1.00 18.17 ?  135 ASP   B N    1 
ATOM   5793 C  CA   . ASP   B 1 135 ? 37.525 -35.455 2.138   1.00 19.22 ?  135 ASP   B CA   1 
ATOM   5794 C  C    . ASP   B 1 135 ? 37.621 -34.618 0.868   1.00 17.78 ?  135 ASP   B C    1 
ATOM   5795 O  O    . ASP   B 1 135 ? 36.763 -33.752 0.644   1.00 17.49 ?  135 ASP   B O    1 
ATOM   5796 C  CB   . ASP   B 1 135 ? 36.185 -36.194 2.198   1.00 21.51 ?  135 ASP   B CB   1 
ATOM   5797 C  CG   . ASP   B 1 135 ? 35.989 -37.179 1.054   1.00 23.57 ?  135 ASP   B CG   1 
ATOM   5798 O  OD1  . ASP   B 1 135 ? 36.850 -37.254 0.149   1.00 23.09 ?  135 ASP   B OD1  1 
ATOM   5799 O  OD2  . ASP   B 1 135 ? 34.963 -37.902 1.077   1.00 26.88 -1 135 ASP   B OD2  1 
ATOM   5800 H  H    . ASP   B 1 135 ? 36.887 -34.490 3.735   1.00 21.81 ?  135 ASP   B H    1 
ATOM   5801 H  HA   . ASP   B 1 135 ? 38.246 -36.109 2.171   1.00 23.07 ?  135 ASP   B HA   1 
ATOM   5802 H  HB2  . ASP   B 1 135 ? 36.139 -36.694 3.028   1.00 25.83 ?  135 ASP   B HB2  1 
ATOM   5803 H  HB3  . ASP   B 1 135 ? 35.470 -35.542 2.163   1.00 25.83 ?  135 ASP   B HB3  1 
ATOM   5804 N  N    . PRO   B 1 136 ? 38.630 -34.822 0.020   1.00 18.15 ?  136 PRO   B N    1 
ATOM   5805 C  CA   . PRO   B 1 136 ? 38.722 -34.000 -1.197  1.00 17.58 ?  136 PRO   B CA   1 
ATOM   5806 C  C    . PRO   B 1 136 ? 37.532 -34.160 -2.123  1.00 16.57 ?  136 PRO   B C    1 
ATOM   5807 O  O    . PRO   B 1 136 ? 37.209 -33.226 -2.864  1.00 15.96 ?  136 PRO   B O    1 
ATOM   5808 C  CB   . PRO   B 1 136 ? 40.035 -34.467 -1.844  1.00 18.43 ?  136 PRO   B CB   1 
ATOM   5809 C  CG   . PRO   B 1 136 ? 40.231 -35.866 -1.320  1.00 20.42 ?  136 PRO   B CG   1 
ATOM   5810 C  CD   . PRO   B 1 136 ? 39.712 -35.819 0.094   1.00 18.87 ?  136 PRO   B CD   1 
ATOM   5811 H  HA   . PRO   B 1 136 ? 38.805 -33.066 -0.960  1.00 21.10 ?  136 PRO   B HA   1 
ATOM   5812 H  HB2  . PRO   B 1 136 ? 39.943 -34.469 -2.812  1.00 22.13 ?  136 PRO   B HB2  1 
ATOM   5813 H  HB3  . PRO   B 1 136 ? 40.760 -33.887 -1.569  1.00 22.13 ?  136 PRO   B HB3  1 
ATOM   5814 H  HG2  . PRO   B 1 136 ? 39.717 -36.498 -1.851  1.00 24.51 ?  136 PRO   B HG2  1 
ATOM   5815 H  HG3  . PRO   B 1 136 ? 41.174 -36.097 -1.332  1.00 24.51 ?  136 PRO   B HG3  1 
ATOM   5816 H  HD2  . PRO   B 1 136 ? 39.359 -36.686 0.357   1.00 22.65 ?  136 PRO   B HD2  1 
ATOM   5817 H  HD3  . PRO   B 1 136 ? 40.408 -35.521 0.705   1.00 22.65 ?  136 PRO   B HD3  1 
ATOM   5818 N  N    . ILE   B 1 137 ? 36.873 -35.323 -2.119  1.00 16.58 ?  137 ILE   B N    1 
ATOM   5819 C  CA   . ILE   B 1 137 ? 35.664 -35.485 -2.925  1.00 17.06 ?  137 ILE   B CA   1 
ATOM   5820 C  C    . ILE   B 1 137 ? 34.578 -34.531 -2.446  1.00 16.51 ?  137 ILE   B C    1 
ATOM   5821 O  O    . ILE   B 1 137 ? 33.856 -33.921 -3.250  1.00 16.30 ?  137 ILE   B O    1 
ATOM   5822 C  CB   . ILE   B 1 137 ? 35.199 -36.956 -2.890  1.00 19.58 ?  137 ILE   B CB   1 
ATOM   5823 C  CG1  . ILE   B 1 137 ? 36.197 -37.850 -3.631  1.00 22.22 ?  137 ILE   B CG1  1 
ATOM   5824 C  CG2  . ILE   B 1 137 ? 33.809 -37.112 -3.490  1.00 20.49 ?  137 ILE   B CG2  1 
ATOM   5825 C  CD1  . ILE   B 1 137 ? 35.895 -39.334 -3.519  1.00 24.99 ?  137 ILE   B CD1  1 
ATOM   5826 H  H    . ILE   B 1 137 ? 37.096 -36.023 -1.666  1.00 19.91 ?  137 ILE   B H    1 
ATOM   5827 H  HA   . ILE   B 1 137 ? 35.869 -35.264 -3.847  1.00 20.48 ?  137 ILE   B HA   1 
ATOM   5828 H  HB   . ILE   B 1 137 ? 35.162 -37.245 -1.968  1.00 23.51 ?  137 ILE   B HB   1 
ATOM   5829 H  HG12 . ILE   B 1 137 ? 36.188 -37.618 -4.574  1.00 26.67 ?  137 ILE   B HG12 1 
ATOM   5830 H  HG13 . ILE   B 1 137 ? 37.082 -37.701 -3.264  1.00 26.67 ?  137 ILE   B HG13 1 
ATOM   5831 H  HG21 . ILE   B 1 137 ? 33.584 -38.054 -3.547  1.00 24.59 ?  137 ILE   B HG21 1 
ATOM   5832 H  HG22 . ILE   B 1 137 ? 33.165 -36.665 -2.922  1.00 24.59 ?  137 ILE   B HG22 1 
ATOM   5833 H  HG23 . ILE   B 1 137 ? 33.803 -36.719 -4.376  1.00 24.59 ?  137 ILE   B HG23 1 
ATOM   5834 H  HD11 . ILE   B 1 137 ? 36.636 -39.828 -3.896  1.00 30.00 ?  137 ILE   B HD11 1 
ATOM   5835 H  HD12 . ILE   B 1 137 ? 35.781 -39.567 -2.582  1.00 30.00 ?  137 ILE   B HD12 1 
ATOM   5836 H  HD13 . ILE   B 1 137 ? 35.083 -39.538 -4.011  1.00 30.00 ?  137 ILE   B HD13 1 
ATOM   5837 N  N    . HIS   B 1 138 ? 34.453 -34.376 -1.130  1.00 17.10 ?  138 HIS   B N    1 
ATOM   5838 C  CA   . HIS   B 1 138 ? 33.501 -33.415 -0.593  1.00 16.92 ?  138 HIS   B CA   1 
ATOM   5839 C  C    . HIS   B 1 138 ? 33.911 -31.987 -0.924  1.00 16.13 ?  138 HIS   B C    1 
ATOM   5840 O  O    . HIS   B 1 138 ? 33.056 -31.146 -1.232  1.00 16.47 ?  138 HIS   B O    1 
ATOM   5841 C  CB   . HIS   B 1 138 ? 33.383 -33.581 0.915   1.00 18.37 ?  138 HIS   B CB   1 
ATOM   5842 C  CG   . HIS   B 1 138 ? 32.425 -32.616 1.535   1.00 19.07 ?  138 HIS   B CG   1 
ATOM   5843 N  ND1  . HIS   B 1 138 ? 31.088 -32.588 1.202   1.00 20.61 ?  138 HIS   B ND1  1 
ATOM   5844 C  CD2  . HIS   B 1 138 ? 32.613 -31.615 2.427   1.00 19.46 ?  138 HIS   B CD2  1 
ATOM   5845 C  CE1  . HIS   B 1 138 ? 30.488 -31.626 1.879   1.00 20.42 ?  138 HIS   B CE1  1 
ATOM   5846 N  NE2  . HIS   B 1 138 ? 31.389 -31.024 2.636   1.00 19.57 ?  138 HIS   B NE2  1 
ATOM   5847 H  H    . HIS   B 1 138 ? 34.906 -34.803 -0.542  1.00 20.53 ?  138 HIS   B H    1 
ATOM   5848 H  HA   . HIS   B 1 138 ? 32.631 -33.578 -0.985  1.00 20.32 ?  138 HIS   B HA   1 
ATOM   5849 H  HB2  . HIS   B 1 138 ? 33.070 -34.476 1.110   1.00 22.06 ?  138 HIS   B HB2  1 
ATOM   5850 H  HB3  . HIS   B 1 138 ? 34.254 -33.436 1.318   1.00 22.06 ?  138 HIS   B HB3  1 
ATOM   5851 H  HD1  . HIS   B 1 138 ? 30.707 -33.119 0.639   1.00 24.74 ?  138 HIS   B HD1  1 
ATOM   5852 H  HD2  . HIS   B 1 138 ? 33.407 -31.381 2.842   1.00 23.37 ?  138 HIS   B HD2  1 
ATOM   5853 H  HE1  . HIS   B 1 138 ? 29.580 -31.418 1.830   1.00 24.52 ?  138 HIS   B HE1  1 
ATOM   5854 N  N    . SER   B 1 139 ? 35.209 -31.679 -0.847  1.00 15.44 ?  139 SER   B N    1 
ATOM   5855 C  CA   . SER   B 1 139 ? 35.645 -30.326 -1.167  1.00 14.91 ?  139 SER   B CA   1 
ATOM   5856 C  C    . SER   B 1 139 ? 35.300 -29.969 -2.602  1.00 14.70 ?  139 SER   B C    1 
ATOM   5857 O  O    . SER   B 1 139 ? 34.848 -28.854 -2.877  1.00 15.28 ?  139 SER   B O    1 
ATOM   5858 C  CB   . SER   B 1 139 ? 37.145 -30.186 -0.921  1.00 15.18 ?  139 SER   B CB   1 
ATOM   5859 O  OG   . SER   B 1 139 ? 37.553 -28.846 -1.159  1.00 15.43 ?  139 SER   B OG   1 
ATOM   5860 H  H    . SER   B 1 139 ? 35.833 -32.218 -0.616  1.00 18.54 ?  139 SER   B H    1 
ATOM   5861 H  HA   . SER   B 1 139 ? 35.190 -29.699 -0.594  1.00 17.90 ?  139 SER   B HA   1 
ATOM   5862 H  HB2  . SER   B 1 139 ? 37.341 -30.420 -0.000  1.00 18.23 ?  139 SER   B HB2  1 
ATOM   5863 H  HB3  . SER   B 1 139 ? 37.629 -30.776 -1.524  1.00 18.23 ?  139 SER   B HB3  1 
ATOM   5864 H  HG   . SER   B 1 139 ? 37.170 -28.325 -0.622  1.00 18.52 ?  139 SER   B HG   1 
ATOM   5865 N  N    . LEU   B 1 140 ? 35.516 -30.900 -3.535  1.00 14.29 ?  140 LEU   B N    1 
ATOM   5866 C  CA   . LEU   B 1 140 ? 35.145 -30.659 -4.923  1.00 14.53 ?  140 LEU   B CA   1 
ATOM   5867 C  C    . LEU   B 1 140 ? 33.642 -30.429 -5.049  1.00 14.34 ?  140 LEU   B C    1 
ATOM   5868 O  O    . LEU   B 1 140 ? 33.201 -29.544 -5.789  1.00 15.06 ?  140 LEU   B O    1 
ATOM   5869 C  CB   . LEU   B 1 140 ? 35.616 -31.821 -5.806  1.00 15.23 ?  140 LEU   B CB   1 
ATOM   5870 C  CG   . LEU   B 1 140 ? 35.257 -31.686 -7.281  1.00 15.67 ?  140 LEU   B CG   1 
ATOM   5871 C  CD1  . LEU   B 1 140 ? 35.855 -30.430 -7.865  1.00 17.14 ?  140 LEU   B CD1  1 
ATOM   5872 C  CD2  . LEU   B 1 140 ? 35.752 -32.916 -8.026  1.00 16.56 ?  140 LEU   B CD2  1 
ATOM   5873 H  H    . LEU   B 1 140 ? 35.876 -31.669 -3.395  1.00 17.16 ?  140 LEU   B H    1 
ATOM   5874 H  HA   . LEU   B 1 140 ? 35.593 -29.858 -5.235  1.00 17.45 ?  140 LEU   B HA   1 
ATOM   5875 H  HB2  . LEU   B 1 140 ? 36.586 -31.888 -5.751  1.00 18.28 ?  140 LEU   B HB2  1 
ATOM   5876 H  HB3  . LEU   B 1 140 ? 35.220 -32.648 -5.482  1.00 18.28 ?  140 LEU   B HB3  1 
ATOM   5877 H  HG   . LEU   B 1 140 ? 34.290 -31.643 -7.376  1.00 18.82 ?  140 LEU   B HG   1 
ATOM   5878 H  HD11 . LEU   B 1 140 ? 35.760 -30.453 -8.827  1.00 20.58 ?  140 LEU   B HD11 1 
ATOM   5879 H  HD12 . LEU   B 1 140 ? 35.394 -29.661 -7.500  1.00 20.58 ?  140 LEU   B HD12 1 
ATOM   5880 H  HD13 . LEU   B 1 140 ? 36.798 -30.396 -7.626  1.00 20.58 ?  140 LEU   B HD13 1 
ATOM   5881 H  HD21 . LEU   B 1 140 ? 35.515 -32.832 -8.965  1.00 19.88 ?  140 LEU   B HD21 1 
ATOM   5882 H  HD22 . LEU   B 1 140 ? 36.712 -32.978 -7.930  1.00 19.88 ?  140 LEU   B HD22 1 
ATOM   5883 H  HD23 . LEU   B 1 140 ? 35.328 -33.706 -7.651  1.00 19.88 ?  140 LEU   B HD23 1 
ATOM   5884 N  N    . ARG   B 1 141 ? 32.848 -31.221 -4.328  1.00 14.36 ?  141 ARG   B N    1 
ATOM   5885 C  CA   . ARG   B 1 141 ? 31.396 -31.053 -4.319  1.00 15.76 ?  141 ARG   B CA   1 
ATOM   5886 C  C    . ARG   B 1 141 ? 31.004 -29.644 -3.892  1.00 14.85 ?  141 ARG   B C    1 
ATOM   5887 O  O    . ARG   B 1 141 ? 30.206 -28.967 -4.564  1.00 15.47 ?  141 ARG   B O    1 
ATOM   5888 C  CB   . ARG   B 1 141 ? 30.814 -32.083 -3.347  1.00 17.66 ?  141 ARG   B CB   1 
ATOM   5889 C  CG   . ARG   B 1 141 ? 29.344 -31.954 -3.021  1.00 20.81 ?  141 ARG   B CG   1 
ATOM   5890 C  CD   . ARG   B 1 141 ? 28.544 -32.616 -4.073  1.00 22.35 ?  141 ARG   B CD   1 
ATOM   5891 N  NE   . ARG   B 1 141 ? 28.282 -31.725 -5.193  1.00 23.13 ?  141 ARG   B NE   1 
ATOM   5892 C  CZ   . ARG   B 1 141 ? 28.317 -32.088 -6.467  1.00 23.47 ?  141 ARG   B CZ   1 
ATOM   5893 N  NH1  . ARG   B 1 141 ? 28.792 -33.268 -6.841  1.00 23.27 ?  141 ARG   B NH1  1 
ATOM   5894 N  NH2  . ARG   B 1 141 ? 27.860 -31.249 -7.390  1.00 24.08 ?  141 ARG   B NH2  1 
ATOM   5895 H  H    . ARG   B 1 141 ? 33.131 -31.865 -3.832  1.00 17.25 ?  141 ARG   B H    1 
ATOM   5896 H  HA   . ARG   B 1 141 ? 31.041 -31.224 -5.204  1.00 18.93 ?  141 ARG   B HA   1 
ATOM   5897 H  HB2  . ARG   B 1 141 ? 30.957 -32.972 -3.719  1.00 21.20 ?  141 ARG   B HB2  1 
ATOM   5898 H  HB3  . ARG   B 1 141 ? 31.294 -32.020 -2.509  1.00 21.20 ?  141 ARG   B HB3  1 
ATOM   5899 H  HG2  . ARG   B 1 141 ? 29.166 -32.387 -2.173  1.00 24.98 ?  141 ARG   B HG2  1 
ATOM   5900 H  HG3  . ARG   B 1 141 ? 29.088 -31.016 -2.977  1.00 24.98 ?  141 ARG   B HG3  1 
ATOM   5901 H  HD2  . ARG   B 1 141 ? 29.021 -33.400 -4.391  1.00 26.83 ?  141 ARG   B HD2  1 
ATOM   5902 H  HD3  . ARG   B 1 141 ? 27.697 -32.885 -3.693  1.00 26.83 ?  141 ARG   B HD3  1 
ATOM   5903 H  HE   . ARG   B 1 141 ? 28.063 -30.914 -5.013  1.00 27.76 ?  141 ARG   B HE   1 
ATOM   5904 H  HH11 . ARG   B 1 141 ? 29.075 -33.833 -6.256  1.00 27.94 ?  141 ARG   B HH11 1 
ATOM   5905 H  HH12 . ARG   B 1 141 ? 28.807 -33.479 -7.673  1.00 27.94 ?  141 ARG   B HH12 1 
ATOM   5906 H  HH21 . ARG   B 1 141 ? 27.557 -30.478 -7.159  1.00 28.91 ?  141 ARG   B HH21 1 
ATOM   5907 H  HH22 . ARG   B 1 141 ? 27.895 -31.464 -8.222  1.00 28.91 ?  141 ARG   B HH22 1 
ATOM   5908 N  N    . VAL   B 1 142 ? 31.547 -29.191 -2.762  1.00 15.00 ?  142 VAL   B N    1 
ATOM   5909 C  CA   . VAL   B 1 142 ? 31.216 -27.855 -2.277  1.00 14.47 ?  142 VAL   B CA   1 
ATOM   5910 C  C    . VAL   B 1 142 ? 31.698 -26.801 -3.267  1.00 14.37 ?  142 VAL   B C    1 
ATOM   5911 O  O    . VAL   B 1 142 ? 30.997 -25.818 -3.531  1.00 14.52 ?  142 VAL   B O    1 
ATOM   5912 C  CB   . VAL   B 1 142 ? 31.765 -27.631 -0.855  1.00 15.39 ?  142 VAL   B CB   1 
ATOM   5913 C  CG1  . VAL   B 1 142 ? 31.456 -26.210 -0.382  1.00 15.39 ?  142 VAL   B CG1  1 
ATOM   5914 C  CG2  . VAL   B 1 142 ? 31.201 -28.655 0.119   1.00 16.38 ?  142 VAL   B CG2  1 
ATOM   5915 H  H    . VAL   B 1 142 ? 32.095 -29.633 -2.266  1.00 18.01 ?  142 VAL   B H    1 
ATOM   5916 H  HA   . VAL   B 1 142 ? 30.256 -27.780 -2.224  1.00 17.37 ?  142 VAL   B HA   1 
ATOM   5917 H  HB   . VAL   B 1 142 ? 32.731 -27.738 -0.870  1.00 18.47 ?  142 VAL   B HB   1 
ATOM   5918 H  HG11 . VAL   B 1 142 ? 31.652 -26.145 0.565   1.00 18.48 ?  142 VAL   B HG11 1 
ATOM   5919 H  HG12 . VAL   B 1 142 ? 32.010 -25.583 -0.876  1.00 18.48 ?  142 VAL   B HG12 1 
ATOM   5920 H  HG13 . VAL   B 1 142 ? 30.520 -26.022 -0.541  1.00 18.48 ?  142 VAL   B HG13 1 
ATOM   5921 H  HG21 . VAL   B 1 142 ? 31.539 -28.466 1.008   1.00 19.66 ?  142 VAL   B HG21 1 
ATOM   5922 H  HG22 . VAL   B 1 142 ? 30.235 -28.600 0.111   1.00 19.66 ?  142 VAL   B HG22 1 
ATOM   5923 H  HG23 . VAL   B 1 142 ? 31.484 -29.544 -0.156  1.00 19.66 ?  142 VAL   B HG23 1 
ATOM   5924 N  N    . CYS   B 1 143 ? 32.882 -27.002 -3.847  1.00 13.85 ?  143 CYS   B N    1 
ATOM   5925 C  CA   . CYS   B 1 143 ? 33.382 -26.067 -4.854  1.00 13.50 ?  143 CYS   B CA   1 
ATOM   5926 C  C    . CYS   B 1 143 ? 32.388 -25.914 -6.003  1.00 13.59 ?  143 CYS   B C    1 
ATOM   5927 O  O    . CYS   B 1 143 ? 31.970 -24.802 -6.346  1.00 14.57 ?  143 CYS   B O    1 
ATOM   5928 C  CB   . CYS   B 1 143 ? 34.748 -26.526 -5.366  1.00 14.09 ?  143 CYS   B CB   1 
ATOM   5929 S  SG   . CYS   B 1 143 ? 35.471 -25.438 -6.604  1.00 14.93 ?  143 CYS   B SG   1 
ATOM   5930 H  H    . CYS   B 1 143 ? 33.414 -27.662 -3.678  1.00 16.63 ?  143 CYS   B H    1 
ATOM   5931 H  HA   . CYS   B 1 143 ? 33.500 -25.199 -4.444  1.00 16.21 ?  143 CYS   B HA   1 
ATOM   5932 H  HB2  . CYS   B 1 143 ? 35.369 -26.585 -4.621  1.00 16.92 ?  143 CYS   B HB2  1 
ATOM   5933 H  HB3  . CYS   B 1 143 ? 34.653 -27.405 -5.766  1.00 16.92 ?  143 CYS   B HB3  1 
ATOM   5934 H  HG   . CYS   B 1 143 ? 36.559 -25.862 -6.910  1.00 17.93 ?  143 CYS   B HG   1 
ATOM   5935 N  N    . VAL   B 1 144 ? 31.958 -27.027 -6.589  1.00 14.78 ?  144 VAL   B N    1 
ATOM   5936 C  CA   . VAL   B 1 144 ? 31.069 -26.951 -7.743  1.00 15.53 ?  144 VAL   B CA   1 
ATOM   5937 C  C    . VAL   B 1 144 ? 29.719 -26.341 -7.375  1.00 15.43 ?  144 VAL   B C    1 
ATOM   5938 O  O    . VAL   B 1 144 ? 29.080 -25.675 -8.202  1.00 16.36 ?  144 VAL   B O    1 
ATOM   5939 C  CB   . VAL   B 1 144 ? 30.913 -28.364 -8.332  1.00 19.34 ?  144 VAL   B CB   1 
ATOM   5940 C  CG1  . VAL   B 1 144 ? 29.648 -28.489 -9.181  1.00 22.76 ?  144 VAL   B CG1  1 
ATOM   5941 C  CG2  . VAL   B 1 144 ? 32.167 -28.769 -9.111  1.00 18.96 ?  144 VAL   B CG2  1 
ATOM   5942 H  H    . VAL   B 1 144 ? 32.169 -27.828 -6.347  1.00 17.75 ?  144 VAL   B H    1 
ATOM   5943 H  HA   . VAL   B 1 144 ? 31.475 -26.392 -8.421  1.00 18.64 ?  144 VAL   B HA   1 
ATOM   5944 H  HB   . VAL   B 1 144 ? 30.829 -28.994 -7.597  1.00 23.22 ?  144 VAL   B HB   1 
ATOM   5945 H  HG11 . VAL   B 1 144 ? 29.734 -29.274 -9.750  1.00 27.32 ?  144 VAL   B HG11 1 
ATOM   5946 H  HG12 . VAL   B 1 144 ? 28.886 -28.593 -8.594  1.00 27.32 ?  144 VAL   B HG12 1 
ATOM   5947 H  HG13 . VAL   B 1 144 ? 29.557 -27.697 -9.726  1.00 27.32 ?  144 VAL   B HG13 1 
ATOM   5948 H  HG21 . VAL   B 1 144 ? 32.047 -29.664 -9.465  1.00 22.76 ?  144 VAL   B HG21 1 
ATOM   5949 H  HG22 . VAL   B 1 144 ? 32.298 -28.141 -9.841  1.00 22.76 ?  144 VAL   B HG22 1 
ATOM   5950 H  HG23 . VAL   B 1 144 ? 32.931 -28.746 -8.516  1.00 22.76 ?  144 VAL   B HG23 1 
ATOM   5951 N  N    . ASP   B 1 145 ? 29.249 -26.572 -6.154  1.00 15.58 ?  145 ASP   B N    1 
ATOM   5952 C  CA   . ASP   B 1 145 ? 27.936 -26.119 -5.723  1.00 15.97 ?  145 ASP   B CA   1 
ATOM   5953 C  C    . ASP   B 1 145 ? 27.957 -24.706 -5.160  1.00 15.98 ?  145 ASP   B C    1 
ATOM   5954 O  O    . ASP   B 1 145 ? 26.898 -24.182 -4.805  1.00 17.73 ?  145 ASP   B O    1 
ATOM   5955 C  CB   . ASP   B 1 145 ? 27.385 -27.051 -4.637  1.00 18.32 ?  145 ASP   B CB   1 
ATOM   5956 C  CG   . ASP   B 1 145 ? 26.993 -28.424 -5.157  1.00 19.15 ?  145 ASP   B CG   1 
ATOM   5957 O  OD1  . ASP   B 1 145 ? 26.863 -28.623 -6.383  1.00 19.50 ?  145 ASP   B OD1  1 
ATOM   5958 O  OD2  . ASP   B 1 145 ? 26.783 -29.306 -4.305  1.00 21.78 -1 145 ASP   B OD2  1 
ATOM   5959 H  H    . ASP   B 1 145 ? 29.687 -26.987 -5.543  1.00 18.71 ?  145 ASP   B H    1 
ATOM   5960 H  HA   . ASP   B 1 145 ? 27.329 -26.125 -6.480  1.00 19.17 ?  145 ASP   B HA   1 
ATOM   5961 H  HB2  . ASP   B 1 145 ? 28.062 -27.179 -3.961  1.00 22.00 ?  145 ASP   B HB2  1 
ATOM   5962 H  HB3  . ASP   B 1 145 ? 26.596 -26.638 -4.244  1.00 22.00 ?  145 ASP   B HB3  1 
ATOM   5963 N  N    . THR   B 1 146 ? 29.132 -24.072 -5.050  1.00 14.54 ?  146 THR   B N    1 
ATOM   5964 C  CA   . THR   B 1 146 ? 29.285 -22.754 -4.435  1.00 14.56 ?  146 THR   B CA   1 
ATOM   5965 C  C    . THR   B 1 146 ? 29.924 -21.735 -5.353  1.00 13.73 ?  146 THR   B C    1 
ATOM   5966 O  O    . THR   B 1 146 ? 29.458 -20.587 -5.411  1.00 14.30 ?  146 THR   B O    1 
ATOM   5967 C  CB   . THR   B 1 146 ? 30.104 -22.872 -3.137  1.00 14.48 ?  146 THR   B CB   1 
ATOM   5968 O  OG1  . THR   B 1 146 ? 29.525 -23.866 -2.277  1.00 14.79 ?  146 THR   B OG1  1 
ATOM   5969 C  CG2  . THR   B 1 146 ? 30.211 -21.520 -2.421  1.00 15.02 ?  146 THR   B CG2  1 
ATOM   5970 H  H    . THR   B 1 146 ? 29.879 -24.395 -5.335  1.00 17.46 ?  146 THR   B H    1 
ATOM   5971 H  HA   . THR   B 1 146 ? 28.413 -22.418 -4.197  1.00 17.48 ?  146 THR   B HA   1 
ATOM   5972 H  HB   . THR   B 1 146 ? 31.006 -23.145 -3.367  1.00 17.38 ?  146 THR   B HB   1 
ATOM   5973 H  HG1  . THR   B 1 146 ? 29.554 -24.624 -2.662  1.00 17.75 ?  146 THR   B HG1  1 
ATOM   5974 H  HG21 . THR   B 1 146 ? 30.564 -21.647 -1.527  1.00 18.04 ?  146 THR   B HG21 1 
ATOM   5975 H  HG22 . THR   B 1 146 ? 30.809 -20.929 -2.911  1.00 18.04 ?  146 THR   B HG22 1 
ATOM   5976 H  HG23 . THR   B 1 146 ? 29.339 -21.105 -2.360  1.00 18.04 ?  146 THR   B HG23 1 
ATOM   5977 N  N    . VAL   B 1 147 ? 30.977 -22.117 -6.058  1.00 13.36 ?  147 VAL   B N    1 
ATOM   5978 C  CA   . VAL   B 1 147 ? 31.702 -21.169 -6.889  1.00 12.99 ?  147 VAL   B CA   1 
ATOM   5979 C  C    . VAL   B 1 147 ? 30.979 -21.025 -8.215  1.00 13.66 ?  147 VAL   B C    1 
ATOM   5980 O  O    . VAL   B 1 147 ? 30.611 -22.020 -8.852  1.00 15.09 ?  147 VAL   B O    1 
ATOM   5981 C  CB   . VAL   B 1 147 ? 33.155 -21.618 -7.091  1.00 13.14 ?  147 VAL   B CB   1 
ATOM   5982 C  CG1  . VAL   B 1 147 ? 33.915 -20.610 -7.937  1.00 13.39 ?  147 VAL   B CG1  1 
ATOM   5983 C  CG2  . VAL   B 1 147 ? 33.844 -21.806 -5.755  1.00 13.00 ?  147 VAL   B CG2  1 
ATOM   5984 H  H    . VAL   B 1 147 ? 31.287 -22.920 -6.081  1.00 16.04 ?  147 VAL   B H    1 
ATOM   5985 H  HA   . VAL   B 1 147 ? 31.713 -20.301 -6.454  1.00 15.59 ?  147 VAL   B HA   1 
ATOM   5986 H  HB   . VAL   B 1 147 ? 33.164 -22.470 -7.561  1.00 15.77 ?  147 VAL   B HB   1 
ATOM   5987 H  HG11 . VAL   B 1 147 ? 34.860 -20.824 -7.916  1.00 16.07 ?  147 VAL   B HG11 1 
ATOM   5988 H  HG12 . VAL   B 1 147 ? 33.589 -20.643 -8.851  1.00 16.07 ?  147 VAL   B HG12 1 
ATOM   5989 H  HG13 . VAL   B 1 147 ? 33.772 -19.720 -7.570  1.00 16.07 ?  147 VAL   B HG13 1 
ATOM   5990 H  HG21 . VAL   B 1 147 ? 34.780 -22.014 -5.909  1.00 15.61 ?  147 VAL   B HG21 1 
ATOM   5991 H  HG22 . VAL   B 1 147 ? 33.769 -20.983 -5.246  1.00 15.61 ?  147 VAL   B HG22 1 
ATOM   5992 H  HG23 . VAL   B 1 147 ? 33.417 -22.532 -5.277  1.00 15.61 ?  147 VAL   B HG23 1 
ATOM   5993 N  N    . ARG   B 1 148 ? 30.754 -19.773 -8.620  1.00 13.50 ?  148 ARG   B N    1 
ATOM   5994 C  CA   . ARG   B 1 148 ? 30.126 -19.451 -9.892  1.00 14.05 ?  148 ARG   B CA   1 
ATOM   5995 C  C    . ARG   B 1 148 ? 31.080 -18.794 -10.877 1.00 13.63 ?  148 ARG   B C    1 
ATOM   5996 O  O    . ARG   B 1 148 ? 30.790 -18.784 -12.075 1.00 14.93 ?  148 ARG   B O    1 
ATOM   5997 C  CB   . ARG   B 1 148 ? 28.893 -18.558 -9.672  1.00 14.33 ?  148 ARG   B CB   1 
ATOM   5998 C  CG   . ARG   B 1 148 ? 27.804 -19.270 -8.869  1.00 14.96 ?  148 ARG   B CG   1 
ATOM   5999 C  CD   . ARG   B 1 148 ? 26.592 -18.387 -8.571  1.00 15.73 ?  148 ARG   B CD   1 
ATOM   6000 N  NE   . ARG   B 1 148 ? 26.978 -17.185 -7.843  1.00 16.05 ?  148 ARG   B NE   1 
ATOM   6001 C  CZ   . ARG   B 1 148 ? 27.287 -17.151 -6.552  1.00 15.27 ?  148 ARG   B CZ   1 
ATOM   6002 N  NH1  . ARG   B 1 148 ? 27.207 -18.232 -5.791  1.00 14.53 ?  148 ARG   B NH1  1 
ATOM   6003 N  NH2  . ARG   B 1 148 ? 27.696 -16.006 -6.014  1.00 15.18 ?  148 ARG   B NH2  1 
ATOM   6004 H  H    . ARG   B 1 148 ? 30.971 -19.074 -8.161  1.00 16.21 ?  148 ARG   B H    1 
ATOM   6005 H  HA   . ARG   B 1 148 ? 29.816 -20.269 -10.296 1.00 16.87 ?  148 ARG   B HA   1 
ATOM   6006 H  HB2  . ARG   B 1 148 ? 29.154 -17.759 -9.186  1.00 17.20 ?  148 ARG   B HB2  1 
ATOM   6007 H  HB3  . ARG   B 1 148 ? 28.516 -18.314 -10.534 1.00 17.20 ?  148 ARG   B HB3  1 
ATOM   6008 H  HG2  . ARG   B 1 148 ? 27.502 -20.040 -9.369  1.00 17.96 ?  148 ARG   B HG2  1 
ATOM   6009 H  HG3  . ARG   B 1 148 ? 28.184 -19.554 -8.020  1.00 17.96 ?  148 ARG   B HG3  1 
ATOM   6010 H  HD2  . ARG   B 1 148 ? 26.182 -18.119 -9.405  1.00 18.89 ?  148 ARG   B HD2  1 
ATOM   6011 H  HD3  . ARG   B 1 148 ? 25.963 -18.887 -8.029  1.00 18.89 ?  148 ARG   B HD3  1 
ATOM   6012 H  HE   . ARG   B 1 148 ? 27.009 -16.446 -8.277  1.00 19.27 ?  148 ARG   B HE   1 
ATOM   6013 H  HH11 . ARG   B 1 148 ? 26.950 -18.983 -6.123  1.00 17.44 ?  148 ARG   B HH11 1 
ATOM   6014 H  HH12 . ARG   B 1 148 ? 27.414 -18.188 -4.953  1.00 17.44 ?  148 ARG   B HH12 1 
ATOM   6015 H  HH21 . ARG   B 1 148 ? 27.748 -15.298 -6.498  1.00 18.23 ?  148 ARG   B HH21 1 
ATOM   6016 H  HH22 . ARG   B 1 148 ? 27.894 -15.968 -5.177  1.00 18.23 ?  148 ARG   B HH22 1 
ATOM   6017 N  N    . THR   B 1 149 ? 32.180 -18.219 -10.398 1.00 13.93 ?  149 THR   B N    1 
ATOM   6018 C  CA   . THR   B 1 149 ? 33.220 -17.668 -11.252 1.00 13.92 ?  149 THR   B CA   1 
ATOM   6019 C  C    . THR   B 1 149 ? 34.115 -18.807 -11.745 1.00 13.83 ?  149 THR   B C    1 
ATOM   6020 O  O    . THR   B 1 149 ? 33.906 -19.981 -11.416 1.00 14.37 ?  149 THR   B O    1 
ATOM   6021 C  CB   . THR   B 1 149 ? 33.999 -16.615 -10.475 1.00 14.00 ?  149 THR   B CB   1 
ATOM   6022 O  OG1  . THR   B 1 149 ? 34.477 -17.201 -9.256  1.00 14.07 ?  149 THR   B OG1  1 
ATOM   6023 C  CG2  . THR   B 1 149 ? 33.111 -15.419 -10.172 1.00 15.20 ?  149 THR   B CG2  1 
ATOM   6024 H  H    . THR   B 1 149 ? 32.342 -18.127 -9.561  1.00 16.72 ?  149 THR   B H    1 
ATOM   6025 H  HA   . THR   B 1 149 ? 32.813 -17.241 -12.023 1.00 16.71 ?  149 THR   B HA   1 
ATOM   6026 H  HB   . THR   B 1 149 ? 34.750 -16.312 -11.008 1.00 16.80 ?  149 THR   B HB   1 
ATOM   6027 H  HG1  . THR   B 1 149 ? 34.908 -16.627 -8.815  1.00 16.89 ?  149 THR   B HG1  1 
ATOM   6028 H  HG21 . THR   B 1 149 ? 33.617 -14.741 -9.705  1.00 18.24 ?  149 THR   B HG21 1 
ATOM   6029 H  HG22 . THR   B 1 149 ? 32.766 -15.045 -11.000 1.00 18.24 ?  149 THR   B HG22 1 
ATOM   6030 H  HG23 . THR   B 1 149 ? 32.362 -15.695 -9.619  1.00 18.24 ?  149 THR   B HG23 1 
ATOM   6031 N  N    . ASN   B 1 150 ? 35.092 -18.482 -12.583 1.00 13.93 ?  150 ASN   B N    1 
ATOM   6032 C  CA   . ASN   B 1 150 ? 35.858 -19.509 -13.285 1.00 13.74 ?  150 ASN   B CA   1 
ATOM   6033 C  C    . ASN   B 1 150 ? 37.026 -19.963 -12.419 1.00 13.45 ?  150 ASN   B C    1 
ATOM   6034 O  O    . ASN   B 1 150 ? 37.954 -19.190 -12.160 1.00 14.32 ?  150 ASN   B O    1 
ATOM   6035 C  CB   . ASN   B 1 150 ? 36.329 -18.978 -14.631 1.00 15.82 ?  150 ASN   B CB   1 
ATOM   6036 C  CG   . ASN   B 1 150 ? 35.184 -18.751 -15.577 1.00 18.71 ?  150 ASN   B CG   1 
ATOM   6037 O  OD1  . ASN   B 1 150 ? 34.306 -19.599 -15.699 1.00 20.29 ?  150 ASN   B OD1  1 
ATOM   6038 N  ND2  . ASN   B 1 150 ? 35.157 -17.598 -16.221 1.00 20.99 ?  150 ASN   B ND2  1 
ATOM   6039 H  H    . ASN   B 1 150 ? 35.341 -17.676 -12.766 1.00 16.73 ?  150 ASN   B H    1 
ATOM   6040 H  HA   . ASN   B 1 150 ? 35.282 -20.276 -13.452 1.00 16.50 ?  150 ASN   B HA   1 
ATOM   6041 H  HB2  . ASN   B 1 150 ? 36.779 -18.128 -14.496 1.00 18.99 ?  150 ASN   B HB2  1 
ATOM   6042 H  HB3  . ASN   B 1 150 ? 36.937 -19.616 -15.033 1.00 18.99 ?  150 ASN   B HB3  1 
ATOM   6043 H  HD21 . ASN   B 1 150 ? 34.519 -17.429 -16.773 1.00 25.19 ?  150 ASN   B HD21 1 
ATOM   6044 H  HD22 . ASN   B 1 150 ? 35.783 -17.021 -16.099 1.00 25.19 ?  150 ASN   B HD22 1 
ATOM   6045 N  N    . VAL   B 1 151 ? 36.985 -21.213 -11.969 1.00 13.32 ?  151 VAL   B N    1 
ATOM   6046 C  CA   . VAL   B 1 151 ? 38.006 -21.749 -11.083 1.00 13.55 ?  151 VAL   B CA   1 
ATOM   6047 C  C    . VAL   B 1 151 ? 38.722 -22.911 -11.762 1.00 13.28 ?  151 VAL   B C    1 
ATOM   6048 O  O    . VAL   B 1 151 ? 38.084 -23.855 -12.264 1.00 14.27 ?  151 VAL   B O    1 
ATOM   6049 C  CB   . VAL   B 1 151 ? 37.444 -22.101 -9.690  1.00 14.90 ?  151 VAL   B CB   1 
ATOM   6050 C  CG1  . VAL   B 1 151 ? 36.263 -23.067 -9.774  1.00 16.31 ?  151 VAL   B CG1  1 
ATOM   6051 C  CG2  . VAL   B 1 151 ? 38.548 -22.632 -8.790  1.00 15.09 ?  151 VAL   B CG2  1 
ATOM   6052 H  H    . VAL   B 1 151 ? 36.357 -21.780 -12.168 1.00 16.00 ?  151 VAL   B H    1 
ATOM   6053 H  HA   . VAL   B 1 151 ? 38.665 -21.054 -10.948 1.00 16.27 ?  151 VAL   B HA   1 
ATOM   6054 H  HB   . VAL   B 1 151 ? 37.120 -21.281 -9.283  1.00 17.89 ?  151 VAL   B HB   1 
ATOM   6055 H  HG11 . VAL   B 1 151 ? 35.961 -23.277 -8.874  1.00 19.58 ?  151 VAL   B HG11 1 
ATOM   6056 H  HG12 . VAL   B 1 151 ? 35.541 -22.644 -10.269 1.00 19.58 ?  151 VAL   B HG12 1 
ATOM   6057 H  HG13 . VAL   B 1 151 ? 36.543 -23.877 -10.225 1.00 19.58 ?  151 VAL   B HG13 1 
ATOM   6058 H  HG21 . VAL   B 1 151 ? 38.208 -22.704 -7.883  1.00 18.12 ?  151 VAL   B HG21 1 
ATOM   6059 H  HG22 . VAL   B 1 151 ? 38.825 -23.507 -9.106  1.00 18.12 ?  151 VAL   B HG22 1 
ATOM   6060 H  HG23 . VAL   B 1 151 ? 39.301 -22.020 -8.810  1.00 18.12 ?  151 VAL   B HG23 1 
ATOM   6061 N  N    . TYR   B 1 152 ? 40.052 -22.818 -11.774 1.00 13.07 ?  152 TYR   B N    1 
ATOM   6062 C  CA   . TYR   B 1 152 ? 40.956 -23.801 -12.352 1.00 12.76 ?  152 TYR   B CA   1 
ATOM   6063 C  C    . TYR   B 1 152 ? 41.675 -24.493 -11.196 1.00 12.19 ?  152 TYR   B C    1 
ATOM   6064 O  O    . TYR   B 1 152 ? 42.524 -23.886 -10.536 1.00 13.14 ?  152 TYR   B O    1 
ATOM   6065 C  CB   . TYR   B 1 152 ? 41.928 -23.100 -13.304 1.00 13.76 ?  152 TYR   B CB   1 
ATOM   6066 C  CG   . TYR   B 1 152 ? 41.242 -22.644 -14.569 1.00 14.83 ?  152 TYR   B CG   1 
ATOM   6067 C  CD1  . TYR   B 1 152 ? 40.552 -21.433 -14.625 1.00 14.73 ?  152 TYR   B CD1  1 
ATOM   6068 C  CD2  . TYR   B 1 152 ? 41.267 -23.438 -15.707 1.00 15.40 ?  152 TYR   B CD2  1 
ATOM   6069 C  CE1  . TYR   B 1 152 ? 39.906 -21.031 -15.780 1.00 15.87 ?  152 TYR   B CE1  1 
ATOM   6070 C  CE2  . TYR   B 1 152 ? 40.622 -23.046 -16.867 1.00 16.27 ?  152 TYR   B CE2  1 
ATOM   6071 C  CZ   . TYR   B 1 152 ? 39.945 -21.843 -16.899 1.00 15.80 ?  152 TYR   B CZ   1 
ATOM   6072 O  OH   . TYR   B 1 152 ? 39.322 -21.488 -18.065 1.00 19.12 ?  152 TYR   B OH   1 
ATOM   6073 H  H    . TYR   B 1 152 ? 40.476 -22.154 -11.418 1.00 15.70 ?  152 TYR   B H    1 
ATOM   6074 H  HA   . TYR   B 1 152 ? 40.446 -24.459 -12.853 1.00 15.32 ?  152 TYR   B HA   1 
ATOM   6075 H  HB2  . TYR   B 1 152 ? 42.301 -22.320 -12.860 1.00 16.52 ?  152 TYR   B HB2  1 
ATOM   6076 H  HB3  . TYR   B 1 152 ? 42.639 -23.714 -13.546 1.00 16.52 ?  152 TYR   B HB3  1 
ATOM   6077 H  HD1  . TYR   B 1 152 ? 40.517 -20.890 -13.869 1.00 17.68 ?  152 TYR   B HD1  1 
ATOM   6078 H  HD2  . TYR   B 1 152 ? 41.724 -24.251 -15.687 1.00 18.49 ?  152 TYR   B HD2  1 
ATOM   6079 H  HE1  . TYR   B 1 152 ? 39.444 -20.222 -15.809 1.00 19.06 ?  152 TYR   B HE1  1 
ATOM   6080 H  HE2  . TYR   B 1 152 ? 40.653 -23.584 -17.624 1.00 19.53 ?  152 TYR   B HE2  1 
ATOM   6081 H  HH   . TYR   B 1 152 ? 38.944 -20.737 -17.972 1.00 22.95 ?  152 TYR   B HH   1 
ATOM   6082 N  N    . LEU   B 1 153 ? 41.300 -25.749 -10.931 1.00 12.76 ?  153 LEU   B N    1 
ATOM   6083 C  CA   . LEU   B 1 153 ? 41.820 -26.497 -9.795  1.00 12.86 ?  153 LEU   B CA   1 
ATOM   6084 C  C    . LEU   B 1 153 ? 43.060 -27.300 -10.183 1.00 13.49 ?  153 LEU   B C    1 
ATOM   6085 O  O    . LEU   B 1 153 ? 43.050 -28.035 -11.176 1.00 14.24 ?  153 LEU   B O    1 
ATOM   6086 C  CB   . LEU   B 1 153 ? 40.737 -27.459 -9.288  1.00 13.42 ?  153 LEU   B CB   1 
ATOM   6087 C  CG   . LEU   B 1 153 ? 39.478 -26.802 -8.706  1.00 14.14 ?  153 LEU   B CG   1 
ATOM   6088 C  CD1  . LEU   B 1 153 ? 38.372 -27.830 -8.557  1.00 15.63 ?  153 LEU   B CD1  1 
ATOM   6089 C  CD2  . LEU   B 1 153 ? 39.784 -26.161 -7.363  1.00 14.51 ?  153 LEU   B CD2  1 
ATOM   6090 H  H    . LEU   B 1 153 ? 40.723 -26.189 -11.404 1.00 15.32 ?  153 LEU   B H    1 
ATOM   6091 H  HA   . LEU   B 1 153 ? 42.043 -25.884 -9.083  1.00 15.44 ?  153 LEU   B HA   1 
ATOM   6092 H  HB2  . LEU   B 1 153 ? 40.447 -28.020 -10.025 1.00 16.11 ?  153 LEU   B HB2  1 
ATOM   6093 H  HB3  . LEU   B 1 153 ? 41.117 -28.014 -8.590  1.00 16.11 ?  153 LEU   B HB3  1 
ATOM   6094 H  HG   . LEU   B 1 153 ? 39.171 -26.104 -9.307  1.00 16.98 ?  153 LEU   B HG   1 
ATOM   6095 H  HD11 . LEU   B 1 153 ? 37.571 -27.390 -8.227  1.00 18.76 ?  153 LEU   B HD11 1 
ATOM   6096 H  HD12 . LEU   B 1 153 ? 38.194 -28.227 -9.424  1.00 18.76 ?  153 LEU   B HD12 1 
ATOM   6097 H  HD13 . LEU   B 1 153 ? 38.656 -28.512 -7.931  1.00 18.76 ?  153 LEU   B HD13 1 
ATOM   6098 H  HD21 . LEU   B 1 153 ? 38.970 -25.788 -6.992  1.00 17.42 ?  153 LEU   B HD21 1 
ATOM   6099 H  HD22 . LEU   B 1 153 ? 40.140 -26.838 -6.763  1.00 17.42 ?  153 LEU   B HD22 1 
ATOM   6100 H  HD23 . LEU   B 1 153 ? 40.443 -25.457 -7.487  1.00 17.42 ?  153 LEU   B HD23 1 
ATOM   6101 N  N    . ALA   B 1 154 ? 44.107 -27.195 -9.367  1.00 13.37 ?  154 ALA   B N    1 
ATOM   6102 C  CA   . ALA   B 1 154 ? 45.336 -27.963 -9.550  1.00 14.49 ?  154 ALA   B CA   1 
ATOM   6103 C  C    . ALA   B 1 154 ? 45.420 -29.034 -8.466  1.00 14.78 ?  154 ALA   B C    1 
ATOM   6104 O  O    . ALA   B 1 154 ? 45.344 -28.726 -7.270  1.00 16.35 ?  154 ALA   B O    1 
ATOM   6105 C  CB   . ALA   B 1 154 ? 46.550 -27.043 -9.510  1.00 15.22 ?  154 ALA   B CB   1 
ATOM   6106 H  H    . ALA   B 1 154 ? 44.117 -26.675 -8.682  1.00 16.06 ?  154 ALA   B H    1 
ATOM   6107 H  HA   . ALA   B 1 154 ? 45.309 -28.402 -10.410 1.00 17.40 ?  154 ALA   B HA   1 
ATOM   6108 H  HB1  . ALA   B 1 154 ? 47.349 -27.573 -9.631  1.00 18.28 ?  154 ALA   B HB1  1 
ATOM   6109 H  HB2  . ALA   B 1 154 ? 46.473 -26.388 -10.223 1.00 18.28 ?  154 ALA   B HB2  1 
ATOM   6110 H  HB3  . ALA   B 1 154 ? 46.577 -26.589 -8.651  1.00 18.28 ?  154 ALA   B HB3  1 
ATOM   6111 N  N    . VAL   B 1 155 ? 45.543 -30.287 -8.892  1.00 13.99 ?  155 VAL   B N    1 
ATOM   6112 C  CA   . VAL   B 1 155 ? 45.648 -31.434 -7.998  1.00 13.72 ?  155 VAL   B CA   1 
ATOM   6113 C  C    . VAL   B 1 155 ? 46.993 -32.097 -8.272  1.00 13.70 ?  155 VAL   B C    1 
ATOM   6114 O  O    . VAL   B 1 155 ? 47.225 -32.615 -9.372  1.00 15.74 ?  155 VAL   B O    1 
ATOM   6115 C  CB   . VAL   B 1 155 ? 44.486 -32.426 -8.195  1.00 15.65 ?  155 VAL   B CB   1 
ATOM   6116 C  CG1  . VAL   B 1 155 ? 44.677 -33.630 -7.289  1.00 17.08 ?  155 VAL   B CG1  1 
ATOM   6117 C  CG2  . VAL   B 1 155 ? 43.141 -31.739 -7.927  1.00 16.30 ?  155 VAL   B CG2  1 
ATOM   6118 H  H    . VAL   B 1 155 ? 45.577 -30.505 -9.725  1.00 16.79 ?  155 VAL   B H    1 
ATOM   6119 H  HA   . VAL   B 1 155 ? 45.635 -31.129 -7.078  1.00 16.48 ?  155 VAL   B HA   1 
ATOM   6120 H  HB   . VAL   B 1 155 ? 44.482 -32.733 -9.114  1.00 18.78 ?  155 VAL   B HB   1 
ATOM   6121 H  HG11 . VAL   B 1 155 ? 43.850 -34.139 -7.256  1.00 20.51 ?  155 VAL   B HG11 1 
ATOM   6122 H  HG12 . VAL   B 1 155 ? 45.389 -34.187 -7.643  1.00 20.51 ?  155 VAL   B HG12 1 
ATOM   6123 H  HG13 . VAL   B 1 155 ? 44.908 -33.325 -6.397  1.00 20.51 ?  155 VAL   B HG13 1 
ATOM   6124 H  HG21 . VAL   B 1 155 ? 42.429 -32.389 -8.022  1.00 19.57 ?  155 VAL   B HG21 1 
ATOM   6125 H  HG22 . VAL   B 1 155 ? 43.144 -31.384 -7.022  1.00 19.57 ?  155 VAL   B HG22 1 
ATOM   6126 H  HG23 . VAL   B 1 155 ? 43.020 -31.018 -8.563  1.00 19.57 ?  155 VAL   B HG23 1 
ATOM   6127 N  N    . PHE   B 1 156 ? 47.860 -32.128 -7.258  1.00 14.52 ?  156 PHE   B N    1 
ATOM   6128 C  CA   . PHE   B 1 156 ? 49.237 -32.587 -7.455  1.00 15.88 ?  156 PHE   B CA   1 
ATOM   6129 C  C    . PHE   B 1 156 ? 49.325 -34.087 -7.752  1.00 16.25 ?  156 PHE   B C    1 
ATOM   6130 O  O    . PHE   B 1 156 ? 50.044 -34.506 -8.669  1.00 18.63 ?  156 PHE   B O    1 
ATOM   6131 C  CB   . PHE   B 1 156 ? 50.054 -32.235 -6.217  1.00 16.27 ?  156 PHE   B CB   1 
ATOM   6132 C  CG   . PHE   B 1 156 ? 51.479 -32.697 -6.281  1.00 16.88 ?  156 PHE   B CG   1 
ATOM   6133 C  CD1  . PHE   B 1 156 ? 52.348 -32.143 -7.202  1.00 18.75 ?  156 PHE   B CD1  1 
ATOM   6134 C  CD2  . PHE   B 1 156 ? 51.960 -33.670 -5.414  1.00 18.13 ?  156 PHE   B CD2  1 
ATOM   6135 C  CE1  . PHE   B 1 156 ? 53.674 -32.556 -7.268  1.00 19.72 ?  156 PHE   B CE1  1 
ATOM   6136 C  CE2  . PHE   B 1 156 ? 53.290 -34.090 -5.476  1.00 18.87 ?  156 PHE   B CE2  1 
ATOM   6137 C  CZ   . PHE   B 1 156 ? 54.138 -33.530 -6.407  1.00 19.94 ?  156 PHE   B CZ   1 
ATOM   6138 H  H    . PHE   B 1 156 ? 47.671 -31.892 -6.450  1.00 17.43 ?  156 PHE   B H    1 
ATOM   6139 H  HA   . PHE   B 1 156 ? 49.614 -32.112 -8.207  1.00 19.06 ?  156 PHE   B HA   1 
ATOM   6140 H  HB2  . PHE   B 1 156 ? 50.054 -31.270 -6.111  1.00 19.53 ?  156 PHE   B HB2  1 
ATOM   6141 H  HB3  . PHE   B 1 156 ? 49.643 -32.649 -5.441  1.00 19.53 ?  156 PHE   B HB3  1 
ATOM   6142 H  HD1  . PHE   B 1 156 ? 52.043 -31.485 -7.789  1.00 22.51 ?  156 PHE   B HD1  1 
ATOM   6143 H  HD2  . PHE   B 1 156 ? 51.381 -34.046 -4.791  1.00 21.77 ?  156 PHE   B HD2  1 
ATOM   6144 H  HE1  . PHE   B 1 156 ? 54.247 -32.177 -7.895  1.00 23.67 ?  156 PHE   B HE1  1 
ATOM   6145 H  HE2  . PHE   B 1 156 ? 53.597 -34.744 -4.894  1.00 22.65 ?  156 PHE   B HE2  1 
ATOM   6146 H  HZ   . PHE   B 1 156 ? 55.024 -33.804 -6.450  1.00 23.93 ?  156 PHE   B HZ   1 
ATOM   6147 N  N    . ASP   B 1 157 ? 48.667 -34.912 -6.949  1.00 16.63 ?  157 ASP   B N    1 
ATOM   6148 C  CA   . ASP   B 1 157 ? 48.804 -36.364 -7.049  1.00 18.13 ?  157 ASP   B CA   1 
ATOM   6149 C  C    . ASP   B 1 157 ? 47.892 -36.920 -8.141  1.00 17.81 ?  157 ASP   B C    1 
ATOM   6150 O  O    . ASP   B 1 157 ? 46.665 -36.818 -8.035  1.00 17.24 ?  157 ASP   B O    1 
ATOM   6151 C  CB   . ASP   B 1 157 ? 48.431 -36.984 -5.708  1.00 19.40 ?  157 ASP   B CB   1 
ATOM   6152 C  CG   . ASP   B 1 157 ? 48.571 -38.488 -5.694  1.00 22.04 ?  157 ASP   B CG   1 
ATOM   6153 O  OD1  . ASP   B 1 157 ? 48.921 -39.083 -6.738  1.00 23.24 ?  157 ASP   B OD1  1 
ATOM   6154 O  OD2  . ASP   B 1 157 ? 48.347 -39.065 -4.614  1.00 24.65 -1 157 ASP   B OD2  1 
ATOM   6155 H  H    . ASP   B 1 157 ? 48.131 -34.656 -6.327  1.00 19.96 ?  157 ASP   B H    1 
ATOM   6156 H  HA   . ASP   B 1 157 ? 49.723 -36.599 -7.258  1.00 21.76 ?  157 ASP   B HA   1 
ATOM   6157 H  HB2  . ASP   B 1 157 ? 49.006 -36.615 -5.023  1.00 23.28 ?  157 ASP   B HB2  1 
ATOM   6158 H  HB3  . ASP   B 1 157 ? 47.504 -36.770 -5.513  1.00 23.28 ?  157 ASP   B HB3  1 
ATOM   6159 N  N    . LYS   B 1 158 ? 48.488 -37.531 -9.173  1.00 19.42 ?  158 LYS   B N    1 
ATOM   6160 C  CA   . LYS   B 1 158 ? 47.713 -38.154 -10.252 1.00 20.43 ?  158 LYS   B CA   1 
ATOM   6161 C  C    . LYS   B 1 158 ? 46.655 -39.121 -9.724  1.00 20.63 ?  158 LYS   B C    1 
ATOM   6162 O  O    . LYS   B 1 158 ? 45.551 -39.207 -10.276 1.00 21.32 ?  158 LYS   B O    1 
ATOM   6163 C  CB   . LYS   B 1 158 ? 48.658 -38.872 -11.223 1.00 22.55 ?  158 LYS   B CB   1 
ATOM   6164 C  CG   . LYS   B 1 158 ? 47.969 -39.774 -12.243 1.00 24.48 ?  158 LYS   B CG   1 
ATOM   6165 C  CD   . LYS   B 1 158 ? 47.139 -38.991 -13.242 1.00 27.15 ?  158 LYS   B CD   1 
ATOM   6166 C  CE   . LYS   B 1 158 ? 46.544 -39.915 -14.296 1.00 29.39 ?  158 LYS   B CE   1 
ATOM   6167 N  NZ   . LYS   B 1 158 ? 45.450 -39.259 -15.069 1.00 29.59 ?  158 LYS   B NZ   1 
ATOM   6168 H  H    . LYS   B 1 158 ? 49.345 -37.601 -9.271  1.00 23.32 ?  158 LYS   B H    1 
ATOM   6169 H  HA   . LYS   B 1 158 ? 47.261 -37.456 -10.752 1.00 24.52 ?  158 LYS   B HA   1 
ATOM   6170 H  HB2  . LYS   B 1 158 ? 49.161 -38.205 -11.725 1.00 27.07 ?  158 LYS   B HB2  1 
ATOM   6171 H  HB3  . LYS   B 1 158 ? 49.273 -39.422 -10.716 1.00 27.07 ?  158 LYS   B HB3  1 
ATOM   6172 H  HG2  . LYS   B 1 158 ? 48.649 -40.257 -12.742 1.00 29.38 ?  158 LYS   B HG2  1 
ATOM   6173 H  HG3  . LYS   B 1 158 ? 47.390 -40.411 -11.793 1.00 29.38 ?  158 LYS   B HG3  1 
ATOM   6174 H  HD2  . LYS   B 1 158 ? 46.414 -38.545 -12.779 1.00 32.59 ?  158 LYS   B HD2  1 
ATOM   6175 H  HD3  . LYS   B 1 158 ? 47.705 -38.342 -13.689 1.00 32.59 ?  158 LYS   B HD3  1 
ATOM   6176 H  HE2  . LYS   B 1 158 ? 47.239 -40.176 -14.919 1.00 35.28 ?  158 LYS   B HE2  1 
ATOM   6177 H  HE3  . LYS   B 1 158 ? 46.177 -40.701 -13.860 1.00 35.28 ?  158 LYS   B HE3  1 
ATOM   6178 H  HZ1  . LYS   B 1 158 ? 45.122 -39.823 -15.674 1.00 35.52 ?  158 LYS   B HZ1  1 
ATOM   6179 H  HZ2  . LYS   B 1 158 ? 44.794 -39.012 -14.520 1.00 35.52 ?  158 LYS   B HZ2  1 
ATOM   6180 H  HZ3  . LYS   B 1 158 ? 45.763 -38.537 -15.486 1.00 35.52 ?  158 LYS   B HZ3  1 
ATOM   6181 N  N    A ASN   B 1 159 ? 46.977 -39.876 -8.673  0.74 19.81 ?  159 ASN   B N    1 
ATOM   6182 N  N    B ASN   B 1 159 ? 46.974 -39.866 -8.666  0.26 19.98 ?  159 ASN   B N    1 
ATOM   6183 C  CA   A ASN   B 1 159 ? 46.019 -40.856 -8.167  0.74 21.30 ?  159 ASN   B CA   1 
ATOM   6184 C  CA   B ASN   B 1 159 ? 46.024 -40.855 -8.165  0.26 20.13 ?  159 ASN   B CA   1 
ATOM   6185 C  C    A ASN   B 1 159 ? 44.816 -40.177 -7.509  0.74 20.01 ?  159 ASN   B C    1 
ATOM   6186 C  C    B ASN   B 1 159 ? 44.830 -40.200 -7.474  0.26 19.69 ?  159 ASN   B C    1 
ATOM   6187 O  O    A ASN   B 1 159 ? 43.680 -40.662 -7.629  0.74 20.43 ?  159 ASN   B O    1 
ATOM   6188 O  O    B ASN   B 1 159 ? 43.714 -40.729 -7.540  0.26 19.81 ?  159 ASN   B O    1 
ATOM   6189 C  CB   A ASN   B 1 159 ? 46.724 -41.833 -7.224  0.74 23.39 ?  159 ASN   B CB   1 
ATOM   6190 C  CB   B ASN   B 1 159 ? 46.737 -41.848 -7.246  0.26 20.59 ?  159 ASN   B CB   1 
ATOM   6191 C  CG   A ASN   B 1 159 ? 47.748 -42.696 -7.941  0.74 25.47 ?  159 ASN   B CG   1 
ATOM   6192 C  CG   B ASN   B 1 159 ? 47.773 -42.679 -7.981  0.26 21.24 ?  159 ASN   B CG   1 
ATOM   6193 O  OD1  A ASN   B 1 159 ? 47.486 -43.223 -9.029  0.74 26.37 ?  159 ASN   B OD1  1 
ATOM   6194 O  OD1  B ASN   B 1 159 ? 47.552 -43.107 -9.116  0.26 21.68 ?  159 ASN   B OD1  1 
ATOM   6195 N  ND2  A ASN   B 1 159 ? 48.920 -42.850 -7.335  0.74 26.23 ?  159 ASN   B ND2  1 
ATOM   6196 N  ND2  B ASN   B 1 159 ? 48.911 -42.912 -7.337  0.26 21.54 ?  159 ASN   B ND2  1 
ATOM   6197 H  H    A ASN   B 1 159 ? 47.726 -39.837 -8.251  0.74 23.78 ?  159 ASN   B H    1 
ATOM   6198 H  H    B ASN   B 1 159 ? 47.716 -39.818 -8.237  0.26 23.99 ?  159 ASN   B H    1 
ATOM   6199 H  HA   A ASN   B 1 159 ? 45.691 -41.367 -8.923  0.74 25.57 ?  159 ASN   B HA   1 
ATOM   6200 H  HA   B ASN   B 1 159 ? 45.682 -41.357 -8.922  0.26 24.17 ?  159 ASN   B HA   1 
ATOM   6201 H  HB2  A ASN   B 1 159 ? 47.183 -41.333 -6.533  0.74 28.08 ?  159 ASN   B HB2  1 
ATOM   6202 H  HB2  B ASN   B 1 159 ? 47.189 -41.361 -6.542  0.26 24.72 ?  159 ASN   B HB2  1 
ATOM   6203 H  HB3  A ASN   B 1 159 ? 46.062 -42.420 -6.832  0.74 28.08 ?  159 ASN   B HB3  1 
ATOM   6204 H  HB3  B ASN   B 1 159 ? 46.080 -42.453 -6.868  0.26 24.72 ?  159 ASN   B HB3  1 
ATOM   6205 H  HD21 A ASN   B 1 159 ? 49.536 -43.328 -7.702  0.74 31.48 ?  159 ASN   B HD21 1 
ATOM   6206 H  HD21 B ASN   B 1 159 ? 49.530 -43.379 -7.711  0.26 25.85 ?  159 ASN   B HD21 1 
ATOM   6207 H  HD22 A ASN   B 1 159 ? 49.064 -42.478 -6.573  0.74 31.48 ?  159 ASN   B HD22 1 
ATOM   6208 H  HD22 B ASN   B 1 159 ? 49.028 -42.599 -6.545  0.26 25.85 ?  159 ASN   B HD22 1 
ATOM   6209 N  N    . LEU   B 1 160 ? 45.036 -39.057 -6.812  1.00 19.50 ?  160 LEU   B N    1 
ATOM   6210 C  CA   . LEU   B 1 160 ? 43.903 -38.324 -6.263  1.00 18.30 ?  160 LEU   B CA   1 
ATOM   6211 C  C    . LEU   B 1 160 ? 43.111 -37.665 -7.381  1.00 16.69 ?  160 LEU   B C    1 
ATOM   6212 O  O    . LEU   B 1 160 ? 41.875 -37.666 -7.364  1.00 16.54 ?  160 LEU   B O    1 
ATOM   6213 C  CB   . LEU   B 1 160 ? 44.369 -37.287 -5.241  1.00 17.91 ?  160 LEU   B CB   1 
ATOM   6214 C  CG   . LEU   B 1 160 ? 43.239 -36.393 -4.703  1.00 17.16 ?  160 LEU   B CG   1 
ATOM   6215 C  CD1  . LEU   B 1 160 ? 42.122 -37.234 -4.077  1.00 19.31 ?  160 LEU   B CD1  1 
ATOM   6216 C  CD2  . LEU   B 1 160 ? 43.786 -35.380 -3.703  1.00 17.37 ?  160 LEU   B CD2  1 
ATOM   6217 H  H    A LEU   B 1 160 ? 45.810 -38.717 -6.647  0.74 23.41 ?  160 LEU   B H    1 
ATOM   6218 H  H    B LEU   B 1 160 ? 45.806 -38.698 -6.675  0.26 23.41 ?  160 LEU   B H    1 
ATOM   6219 H  HA   . LEU   B 1 160 ? 43.318 -38.950 -5.811  1.00 21.97 ?  160 LEU   B HA   1 
ATOM   6220 H  HB2  . LEU   B 1 160 ? 44.774 -37.753 -4.487  1.00 21.50 ?  160 LEU   B HB2  1 
ATOM   6221 H  HB3  . LEU   B 1 160 ? 45.036 -36.714 -5.659  1.00 21.50 ?  160 LEU   B HB3  1 
ATOM   6222 H  HG   . LEU   B 1 160 ? 42.861 -35.901 -5.443  1.00 20.60 ?  160 LEU   B HG   1 
ATOM   6223 H  HD11 . LEU   B 1 160 ? 41.494 -36.641 -3.644  1.00 23.18 ?  160 LEU   B HD11 1 
ATOM   6224 H  HD12 . LEU   B 1 160 ? 41.673 -37.740 -4.775  1.00 23.18 ?  160 LEU   B HD12 1 
ATOM   6225 H  HD13 . LEU   B 1 160 ? 42.508 -37.843 -3.426  1.00 23.18 ?  160 LEU   B HD13 1 
ATOM   6226 H  HD21 . LEU   B 1 160 ? 43.058 -34.813 -3.405  1.00 20.85 ?  160 LEU   B HD21 1 
ATOM   6227 H  HD22 . LEU   B 1 160 ? 44.169 -35.853 -2.947  1.00 20.85 ?  160 LEU   B HD22 1 
ATOM   6228 H  HD23 . LEU   B 1 160 ? 44.468 -34.843 -4.137  1.00 20.85 ?  160 LEU   B HD23 1 
ATOM   6229 N  N    . TYR   B 1 161 ? 43.805 -37.089 -8.361  1.00 17.18 ?  161 TYR   B N    1 
ATOM   6230 C  CA   . TYR   B 1 161 ? 43.134 -36.510 -9.519  1.00 17.25 ?  161 TYR   B CA   1 
ATOM   6231 C  C    . TYR   B 1 161 ? 42.194 -37.523 -10.155 1.00 17.17 ?  161 TYR   B C    1 
ATOM   6232 O  O    . TYR   B 1 161 ? 41.029 -37.214 -10.431 1.00 17.13 ?  161 TYR   B O    1 
ATOM   6233 C  CB   . TYR   B 1 161 ? 44.181 -36.019 -10.531 1.00 18.03 ?  161 TYR   B CB   1 
ATOM   6234 C  CG   . TYR   B 1 161 ? 43.605 -35.558 -11.845 1.00 18.70 ?  161 TYR   B CG   1 
ATOM   6235 C  CD1  . TYR   B 1 161 ? 43.193 -34.243 -12.010 1.00 19.05 ?  161 TYR   B CD1  1 
ATOM   6236 C  CD2  . TYR   B 1 161 ? 43.442 -36.434 -12.913 1.00 18.78 ?  161 TYR   B CD2  1 
ATOM   6237 C  CE1  . TYR   B 1 161 ? 42.660 -33.805 -13.200 1.00 20.21 ?  161 TYR   B CE1  1 
ATOM   6238 C  CE2  . TYR   B 1 161 ? 42.905 -36.008 -14.108 1.00 19.77 ?  161 TYR   B CE2  1 
ATOM   6239 C  CZ   . TYR   B 1 161 ? 42.511 -34.693 -14.243 1.00 19.92 ?  161 TYR   B CZ   1 
ATOM   6240 O  OH   . TYR   B 1 161 ? 41.973 -34.259 -15.427 1.00 22.08 ?  161 TYR   B OH   1 
ATOM   6241 H  H    . TYR   B 1 161 ? 44.662 -37.020 -8.379  1.00 20.62 ?  161 TYR   B H    1 
ATOM   6242 H  HA   . TYR   B 1 161 ? 42.605 -35.746 -9.235  1.00 20.71 ?  161 TYR   B HA   1 
ATOM   6243 H  HB2  . TYR   B 1 161 ? 44.659 -35.271 -10.145 1.00 21.64 ?  161 TYR   B HB2  1 
ATOM   6244 H  HB3  . TYR   B 1 161 ? 44.793 -36.744 -10.719 1.00 21.64 ?  161 TYR   B HB3  1 
ATOM   6245 H  HD1  . TYR   B 1 161 ? 43.289 -33.636 -11.310 1.00 22.87 ?  161 TYR   B HD1  1 
ATOM   6246 H  HD2  . TYR   B 1 161 ? 43.703 -37.322 -12.826 1.00 22.55 ?  161 TYR   B HD2  1 
ATOM   6247 H  HE1  . TYR   B 1 161 ? 42.392 -32.917 -13.297 1.00 24.26 ?  161 TYR   B HE1  1 
ATOM   6248 H  HE2  . TYR   B 1 161 ? 42.803 -36.603 -14.819 1.00 23.74 ?  161 TYR   B HE2  1 
ATOM   6249 H  HH   . TYR   B 1 161 ? 41.941 -34.896 -15.979 1.00 26.50 ?  161 TYR   B HH   1 
ATOM   6250 N  N    . ASP   B 1 162 ? 42.689 -38.746 -10.383 1.00 17.67 ?  162 ASP   B N    1 
ATOM   6251 C  CA   . ASP   B 1 162 ? 41.869 -39.780 -11.004 1.00 18.35 ?  162 ASP   B CA   1 
ATOM   6252 C  C    . ASP   B 1 162 ? 40.659 -40.120 -10.144 1.00 18.22 ?  162 ASP   B C    1 
ATOM   6253 O  O    . ASP   B 1 162 ? 39.558 -40.330 -10.669 1.00 18.60 ?  162 ASP   B O    1 
ATOM   6254 C  CB   . ASP   B 1 162 ? 42.708 -41.037 -11.253 1.00 19.93 ?  162 ASP   B CB   1 
ATOM   6255 C  CG   . ASP   B 1 162 ? 43.706 -40.871 -12.390 1.00 22.20 ?  162 ASP   B CG   1 
ATOM   6256 O  OD1  . ASP   B 1 162 ? 43.563 -39.938 -13.203 1.00 21.85 ?  162 ASP   B OD1  1 
ATOM   6257 O  OD2  . ASP   B 1 162 ? 44.622 -41.709 -12.493 1.00 23.87 -1 162 ASP   B OD2  1 
ATOM   6258 H  H    . ASP   B 1 162 ? 43.495 -38.990 -10.201 1.00 21.22 ?  162 ASP   B H    1 
ATOM   6259 H  HA   . ASP   B 1 162 ? 41.548 -39.462 -11.860 1.00 22.02 ?  162 ASP   B HA   1 
ATOM   6260 H  HB2  . ASP   B 1 162 ? 43.212 -41.251 -10.453 1.00 23.93 ?  162 ASP   B HB2  1 
ATOM   6261 H  HB3  . ASP   B 1 162 ? 42.118 -41.774 -11.481 1.00 23.93 ?  162 ASP   B HB3  1 
ATOM   6262 N  N    A LYS   B 1 163 ? 40.844 -40.194 -8.823  0.74 17.10 ?  163 LYS   B N    1 
ATOM   6263 N  N    B LYS   B 1 163 ? 40.840 -40.180 -8.822  0.26 18.55 ?  163 LYS   B N    1 
ATOM   6264 C  CA   A LYS   B 1 163 ? 39.720 -40.486 -7.942  0.74 18.16 ?  163 LYS   B CA   1 
ATOM   6265 C  CA   B LYS   B 1 163 ? 39.715 -40.488 -7.945  0.26 19.41 ?  163 LYS   B CA   1 
ATOM   6266 C  C    A LYS   B 1 163 ? 38.672 -39.380 -8.003  0.74 17.37 ?  163 LYS   B C    1 
ATOM   6267 C  C    B LYS   B 1 163 ? 38.672 -39.377 -7.974  0.26 17.91 ?  163 LYS   B C    1 
ATOM   6268 O  O    A LYS   B 1 163 ? 37.461 -39.655 -8.002  0.74 17.78 ?  163 LYS   B O    1 
ATOM   6269 O  O    B LYS   B 1 163 ? 37.464 -39.645 -7.921  0.26 17.98 ?  163 LYS   B O    1 
ATOM   6270 C  CB   A LYS   B 1 163 ? 40.200 -40.682 -6.507  0.74 21.12 ?  163 LYS   B CB   1 
ATOM   6271 C  CB   B LYS   B 1 163 ? 40.205 -40.725 -6.517  0.26 22.04 ?  163 LYS   B CB   1 
ATOM   6272 C  CG   A LYS   B 1 163 ? 39.119 -41.237 -5.603  0.74 25.56 ?  163 LYS   B CG   1 
ATOM   6273 C  CG   B LYS   B 1 163 ? 39.132 -41.286 -5.604  0.26 25.23 ?  163 LYS   B CG   1 
ATOM   6274 C  CD   A LYS   B 1 163 ? 39.516 -41.248 -4.139  0.74 30.01 ?  163 LYS   B CD   1 
ATOM   6275 C  CD   B LYS   B 1 163 ? 39.593 -41.381 -4.161  0.26 28.36 ?  163 LYS   B CD   1 
ATOM   6276 C  CE   A LYS   B 1 163 ? 38.445 -41.947 -3.308  0.74 32.84 ?  163 LYS   B CE   1 
ATOM   6277 C  CE   B LYS   B 1 163 ? 38.547 -42.088 -3.312  0.26 30.29 ?  163 LYS   B CE   1 
ATOM   6278 N  NZ   A LYS   B 1 163 ? 38.494 -41.566 -1.869  0.74 34.57 ?  163 LYS   B NZ   1 
ATOM   6279 N  NZ   B LYS   B 1 163 ? 38.647 -41.733 -1.871  0.26 31.19 ?  163 LYS   B NZ   1 
ATOM   6280 H  H    A LYS   B 1 163 ? 41.601 -40.078 -8.424  0.74 20.53 ?  163 LYS   B H    1 
ATOM   6281 H  H    B LYS   B 1 163 ? 41.591 -40.049 -8.419  0.26 22.27 ?  163 LYS   B H    1 
ATOM   6282 H  HA   A LYS   B 1 163 ? 39.305 -41.311 -8.233  0.74 21.80 ?  163 LYS   B HA   1 
ATOM   6283 H  HA   B LYS   B 1 163 ? 39.292 -41.302 -8.254  0.26 23.30 ?  163 LYS   B HA   1 
ATOM   6284 H  HB2  A LYS   B 1 163 ? 40.944 -41.310 -6.503  0.74 25.35 ?  163 LYS   B HB2  1 
ATOM   6285 H  HB2  B LYS   B 1 163 ? 40.940 -41.360 -6.537  0.26 26.46 ?  163 LYS   B HB2  1 
ATOM   6286 H  HB3  A LYS   B 1 163 ? 40.486 -39.830 -6.145  0.74 25.35 ?  163 LYS   B HB3  1 
ATOM   6287 H  HB3  B LYS   B 1 163 ? 40.507 -39.883 -6.142  0.26 26.46 ?  163 LYS   B HB3  1 
ATOM   6288 H  HG2  A LYS   B 1 163 ? 38.320 -40.694 -5.690  0.74 30.68 ?  163 LYS   B HG2  1 
ATOM   6289 H  HG2  B LYS   B 1 163 ? 38.354 -40.707 -5.632  0.26 30.29 ?  163 LYS   B HG2  1 
ATOM   6290 H  HG3  A LYS   B 1 163 ? 38.924 -42.152 -5.867  0.74 30.68 ?  163 LYS   B HG3  1 
ATOM   6291 H  HG3  B LYS   B 1 163 ? 38.893 -42.177 -5.903  0.26 30.29 ?  163 LYS   B HG3  1 
ATOM   6292 H  HD2  A LYS   B 1 163 ? 40.350 -41.732 -4.033  0.74 36.02 ?  163 LYS   B HD2  1 
ATOM   6293 H  HD2  B LYS   B 1 163 ? 40.419 -41.890 -4.119  0.26 34.04 ?  163 LYS   B HD2  1 
ATOM   6294 H  HD3  A LYS   B 1 163 ? 39.608 -40.337 -3.821  0.74 36.02 ?  163 LYS   B HD3  1 
ATOM   6295 H  HD3  B LYS   B 1 163 ? 39.727 -40.489 -3.804  0.26 34.04 ?  163 LYS   B HD3  1 
ATOM   6296 H  HE2  A LYS   B 1 163 ? 37.568 -41.719 -3.656  0.74 39.41 ?  163 LYS   B HE2  1 
ATOM   6297 H  HE2  B LYS   B 1 163 ? 37.663 -41.838 -3.625  0.26 36.36 ?  163 LYS   B HE2  1 
ATOM   6298 H  HE3  A LYS   B 1 163 ? 38.579 -42.905 -3.366  0.74 39.41 ?  163 LYS   B HE3  1 
ATOM   6299 H  HE3  B LYS   B 1 163 ? 38.668 -43.047 -3.395  0.26 36.36 ?  163 LYS   B HE3  1 
ATOM   6300 H  HZ1  A LYS   B 1 163 ? 37.854 -41.992 -1.420  0.74 41.50 ?  163 LYS   B HZ1  1 
ATOM   6301 H  HZ1  B LYS   B 1 163 ? 38.020 -42.163 -1.408  0.26 37.44 ?  163 LYS   B HZ1  1 
ATOM   6302 H  HZ2  A LYS   B 1 163 ? 39.284 -41.785 -1.524  0.74 41.50 ?  163 LYS   B HZ2  1 
ATOM   6303 H  HZ2  B LYS   B 1 163 ? 39.447 -41.960 -1.557  0.26 37.44 ?  163 LYS   B HZ2  1 
ATOM   6304 H  HZ3  A LYS   B 1 163 ? 38.372 -40.689 -1.782  0.74 41.50 ?  163 LYS   B HZ3  1 
ATOM   6305 H  HZ3  B LYS   B 1 163 ? 38.533 -40.856 -1.766  0.26 37.44 ?  163 LYS   B HZ3  1 
ATOM   6306 N  N    . LEU   B 1 164 ? 39.122 -38.124 -8.057  1.00 16.44 ?  164 LEU   B N    1 
ATOM   6307 C  CA   . LEU   B 1 164 ? 38.200 -36.994 -8.099  1.00 16.01 ?  164 LEU   B CA   1 
ATOM   6308 C  C    . LEU   B 1 164 ? 37.428 -36.972 -9.408  1.00 15.65 ?  164 LEU   B C    1 
ATOM   6309 O  O    . LEU   B 1 164 ? 36.210 -36.750 -9.418  1.00 16.59 ?  164 LEU   B O    1 
ATOM   6310 C  CB   . LEU   B 1 164 ? 38.983 -35.688 -7.928  1.00 15.50 ?  164 LEU   B CB   1 
ATOM   6311 C  CG   . LEU   B 1 164 ? 39.530 -35.400 -6.533  1.00 16.37 ?  164 LEU   B CG   1 
ATOM   6312 C  CD1  . LEU   B 1 164 ? 40.629 -34.346 -6.593  1.00 15.86 ?  164 LEU   B CD1  1 
ATOM   6313 C  CD2  . LEU   B 1 164 ? 38.436 -34.964 -5.586  1.00 17.82 ?  164 LEU   B CD2  1 
ATOM   6314 H  H    A LEU   B 1 164 ? 39.956 -37.902 -8.075  0.74 19.74 ?  164 LEU   B H    1 
ATOM   6315 H  H    B LEU   B 1 164 ? 39.956 -37.904 -8.098  0.26 19.74 ?  164 LEU   B H    1 
ATOM   6316 H  HA   . LEU   B 1 164 ? 37.566 -37.072 -7.377  1.00 19.22 ?  164 LEU   B HA   1 
ATOM   6317 H  HB2  . LEU   B 1 164 ? 39.739 -35.702 -8.534  1.00 18.61 ?  164 LEU   B HB2  1 
ATOM   6318 H  HB3  . LEU   B 1 164 ? 38.397 -34.951 -8.164  1.00 18.61 ?  164 LEU   B HB3  1 
ATOM   6319 H  HG   . LEU   B 1 164 ? 39.919 -36.211 -6.179  1.00 19.65 ?  164 LEU   B HG   1 
ATOM   6320 H  HD11 . LEU   B 1 164 ? 40.955 -34.174 -5.694  1.00 19.04 ?  164 LEU   B HD11 1 
ATOM   6321 H  HD12 . LEU   B 1 164 ? 41.357 -34.676 -7.147  1.00 19.04 ?  164 LEU   B HD12 1 
ATOM   6322 H  HD13 . LEU   B 1 164 ? 40.271 -33.529 -6.975  1.00 19.04 ?  164 LEU   B HD13 1 
ATOM   6323 H  HD21 . LEU   B 1 164 ? 38.829 -34.769 -4.718  1.00 21.39 ?  164 LEU   B HD21 1 
ATOM   6324 H  HD22 . LEU   B 1 164 ? 38.008 -34.166 -5.937  1.00 21.39 ?  164 LEU   B HD22 1 
ATOM   6325 H  HD23 . LEU   B 1 164 ? 37.787 -35.678 -5.500  1.00 21.39 ?  164 LEU   B HD23 1 
ATOM   6326 N  N    . VAL   B 1 165 ? 38.126 -37.159 -10.530 1.00 16.91 ?  165 VAL   B N    1 
ATOM   6327 C  CA   . VAL   B 1 165 ? 37.467 -37.082 -11.830 1.00 18.38 ?  165 VAL   B CA   1 
ATOM   6328 C  C    . VAL   B 1 165 ? 36.532 -38.266 -12.016 1.00 19.97 ?  165 VAL   B C    1 
ATOM   6329 O  O    . VAL   B 1 165 ? 35.371 -38.108 -12.411 1.00 21.31 ?  165 VAL   B O    1 
ATOM   6330 C  CB   . VAL   B 1 165 ? 38.500 -36.983 -12.969 1.00 19.25 ?  165 VAL   B CB   1 
ATOM   6331 C  CG1  . VAL   B 1 165 ? 37.808 -37.060 -14.316 1.00 21.30 ?  165 VAL   B CG1  1 
ATOM   6332 C  CG2  . VAL   B 1 165 ? 39.307 -35.694 -12.850 1.00 19.14 ?  165 VAL   B CG2  1 
ATOM   6333 H  H    . VAL   B 1 165 ? 38.971 -37.330 -10.568 1.00 20.30 ?  165 VAL   B H    1 
ATOM   6334 H  HA   . VAL   B 1 165 ? 36.928 -36.281 -11.861 1.00 22.07 ?  165 VAL   B HA   1 
ATOM   6335 H  HB   . VAL   B 1 165 ? 39.122 -37.725 -12.906 1.00 23.11 ?  165 VAL   B HB   1 
ATOM   6336 H  HG11 . VAL   B 1 165 ? 38.415 -36.748 -15.003 1.00 25.57 ?  165 VAL   B HG11 1 
ATOM   6337 H  HG12 . VAL   B 1 165 ? 37.565 -37.985 -14.491 1.00 25.57 ?  165 VAL   B HG12 1 
ATOM   6338 H  HG13 . VAL   B 1 165 ? 37.014 -36.507 -14.296 1.00 25.57 ?  165 VAL   B HG13 1 
ATOM   6339 H  HG21 . VAL   B 1 165 ? 39.933 -35.639 -13.591 1.00 22.98 ?  165 VAL   B HG21 1 
ATOM   6340 H  HG22 . VAL   B 1 165 ? 38.701 -34.936 -12.878 1.00 22.98 ?  165 VAL   B HG22 1 
ATOM   6341 H  HG23 . VAL   B 1 165 ? 39.792 -35.697 -12.010 1.00 22.98 ?  165 VAL   B HG23 1 
ATOM   6342 N  N    . SER   B 1 166 ? 37.034 -39.472 -11.728 1.00 20.50 ?  166 SER   B N    1 
ATOM   6343 C  CA   . SER   B 1 166 ? 36.266 -40.679 -12.010 1.00 22.13 ?  166 SER   B CA   1 
ATOM   6344 C  C    . SER   B 1 166 ? 35.008 -40.753 -11.158 1.00 22.24 ?  166 SER   B C    1 
ATOM   6345 O  O    . SER   B 1 166 ? 34.021 -41.362 -11.579 1.00 24.19 ?  166 SER   B O    1 
ATOM   6346 C  CB   . SER   B 1 166 ? 37.135 -41.935 -11.842 1.00 23.13 ?  166 SER   B CB   1 
ATOM   6347 O  OG   . SER   B 1 166 ? 37.526 -42.146 -10.495 1.00 23.05 ?  166 SER   B OG   1 
ATOM   6348 H  H    . SER   B 1 166 ? 37.816 -39.612 -11.386 1.00 24.60 ?  166 SER   B H    1 
ATOM   6349 H  HA   . SER   B 1 166 ? 35.992 -40.655 -12.938 1.00 26.56 ?  166 SER   B HA   1 
ATOM   6350 H  HB2  . SER   B 1 166 ? 36.633 -42.706 -12.146 1.00 27.76 ?  166 SER   B HB2  1 
ATOM   6351 H  HB3  . SER   B 1 166 ? 37.939 -41.839 -12.384 1.00 27.76 ?  166 SER   B HB3  1 
ATOM   6352 H  HG   . SER   B 1 166 ? 37.971 -41.493 -10.219 1.00 27.67 ?  166 SER   B HG   1 
ATOM   6353 N  N    . SER   B 1 167 ? 35.016 -40.158 -9.967  1.00 20.84 ?  167 SER   B N    1 
ATOM   6354 C  CA   . SER   B 1 167 ? 33.863 -40.204 -9.076  1.00 20.87 ?  167 SER   B CA   1 
ATOM   6355 C  C    . SER   B 1 167 ? 32.952 -38.980 -9.182  1.00 20.50 ?  167 SER   B C    1 
ATOM   6356 O  O    . SER   B 1 167 ? 31.875 -38.967 -8.570  1.00 20.64 ?  167 SER   B O    1 
ATOM   6357 C  CB   . SER   B 1 167 ? 34.316 -40.394 -7.621  1.00 20.41 ?  167 SER   B CB   1 
ATOM   6358 O  OG   . SER   B 1 167 ? 34.978 -39.231 -7.137  1.00 20.06 ?  167 SER   B OG   1 
ATOM   6359 H  H    . SER   B 1 167 ? 35.690 -39.730 -9.651  1.00 25.02 ?  167 SER   B H    1 
ATOM   6360 H  HA   . SER   B 1 167 ? 33.334 -40.981 -9.315  1.00 25.05 ?  167 SER   B HA   1 
ATOM   6361 H  HB2  . SER   B 1 167 ? 33.534 -40.569 -7.074  1.00 24.50 ?  167 SER   B HB2  1 
ATOM   6362 H  HB3  . SER   B 1 167 ? 34.922 -41.157 -7.577  1.00 24.50 ?  167 SER   B HB3  1 
ATOM   6363 H  HG   . SER   B 1 167 ? 35.663 -39.088 -7.603  1.00 24.08 ?  167 SER   B HG   1 
ATOM   6364 N  N    . PHE   B 1 168 ? 33.335 -37.962 -9.955  1.00 20.11 ?  168 PHE   B N    1 
ATOM   6365 C  CA   . PHE   B 1 168 ? 32.515 -36.754 -10.027 1.00 19.55 ?  168 PHE   B CA   1 
ATOM   6366 C  C    . PHE   B 1 168 ? 31.189 -37.031 -10.729 1.00 17.52 ?  168 PHE   B C    1 
ATOM   6367 O  O    . PHE   B 1 168 ? 30.154 -36.431 -10.388 1.00 17.54 ?  168 PHE   B O    1 
ATOM   6368 C  CB   . PHE   B 1 168 ? 33.266 -35.631 -10.740 1.00 20.63 ?  168 PHE   B CB   1 
ATOM   6369 C  CG   . PHE   B 1 168 ? 32.462 -34.375 -10.864 1.00 19.92 ?  168 PHE   B CG   1 
ATOM   6370 C  CD1  . PHE   B 1 168 ? 32.157 -33.631 -9.734  1.00 21.81 ?  168 PHE   B CD1  1 
ATOM   6371 C  CD2  . PHE   B 1 168 ? 31.985 -33.951 -12.090 1.00 19.67 ?  168 PHE   B CD2  1 
ATOM   6372 C  CE1  . PHE   B 1 168 ? 31.402 -32.485 -9.821  1.00 22.44 ?  168 PHE   B CE1  1 
ATOM   6373 C  CE2  . PHE   B 1 168 ? 31.239 -32.774 -12.195 1.00 21.29 ?  168 PHE   B CE2  1 
ATOM   6374 C  CZ   . PHE   B 1 168 ? 30.940 -32.047 -11.057 1.00 22.07 ?  168 PHE   B CZ   1 
ATOM   6375 H  H    . PHE   B 1 168 ? 34.048 -37.945 -10.443 1.00 24.14 ?  168 PHE   B H    1 
ATOM   6376 H  HA   . PHE   B 1 168 ? 32.315 -36.459 -9.130  1.00 23.47 ?  168 PHE   B HA   1 
ATOM   6377 H  HB2  . PHE   B 1 168 ? 34.071 -35.423 -10.237 1.00 24.76 ?  168 PHE   B HB2  1 
ATOM   6378 H  HB3  . PHE   B 1 168 ? 33.503 -35.922 -11.634 1.00 24.76 ?  168 PHE   B HB3  1 
ATOM   6379 H  HD1  . PHE   B 1 168 ? 32.463 -33.920 -8.903  1.00 26.18 ?  168 PHE   B HD1  1 
ATOM   6380 H  HD2  . PHE   B 1 168 ? 32.191 -34.436 -12.856 1.00 23.61 ?  168 PHE   B HD2  1 
ATOM   6381 H  HE1  . PHE   B 1 168 ? 31.207 -31.995 -9.053  1.00 26.93 ?  168 PHE   B HE1  1 
ATOM   6382 H  HE2  . PHE   B 1 168 ? 30.926 -32.497 -13.025 1.00 25.55 ?  168 PHE   B HE2  1 
ATOM   6383 H  HZ   . PHE   B 1 168 ? 30.431 -31.271 -11.120 1.00 26.50 ?  168 PHE   B HZ   1 
ATOM   6384 N  N    . LEU   B 1 169 ? 31.214 -37.893 -11.740 1.00 18.11 ?  169 LEU   B N    1 
ATOM   6385 C  CA   . LEU   B 1 169 ? 30.030 -38.204 -12.529 1.00 21.07 ?  169 LEU   B CA   1 
ATOM   6386 C  C    . LEU   B 1 169 ? 30.033 -39.649 -13.020 1.00 24.43 ?  169 LEU   B C    1 
ATOM   6387 O  O    . LEU   B 1 169 ? 29.146 -40.074 -13.760 1.00 26.69 ?  169 LEU   B O    1 
ATOM   6388 C  CB   . LEU   B 1 169 ? 29.939 -37.267 -13.733 1.00 23.00 ?  169 LEU   B CB   1 
ATOM   6389 C  CG   . LEU   B 1 169 ? 28.677 -36.407 -13.825 1.00 27.15 ?  169 LEU   B CG   1 
ATOM   6390 C  CD1  . LEU   B 1 169 ? 28.631 -35.712 -15.169 1.00 28.16 ?  169 LEU   B CD1  1 
ATOM   6391 C  CD2  . LEU   B 1 169 ? 27.419 -37.231 -13.600 1.00 27.58 ?  169 LEU   B CD2  1 
ATOM   6392 O  OXT  . LEU   B 1 169 ? 30.921 -40.426 -12.701 1.00 25.09 -1 169 LEU   B OXT  1 
ATOM   6393 H  H    . LEU   B 1 169 ? 31.922 -38.308 -12.007 1.00 21.74 ?  169 LEU   B H    1 
ATOM   6394 H  HA   . LEU   B 1 169 ? 29.249 -38.069 -11.978 1.00 25.29 ?  169 LEU   B HA   1 
ATOM   6395 H  HB2  . LEU   B 1 169 ? 30.697 -36.659 -13.713 1.00 27.61 ?  169 LEU   B HB2  1 
ATOM   6396 H  HB3  . LEU   B 1 169 ? 29.978 -37.797 -14.545 1.00 27.61 ?  169 LEU   B HB3  1 
ATOM   6397 H  HG   . LEU   B 1 169 ? 28.711 -35.721 -13.138 1.00 32.59 ?  169 LEU   B HG   1 
ATOM   6398 H  HD11 . LEU   B 1 169 ? 27.839 -35.152 -15.206 1.00 33.80 ?  169 LEU   B HD11 1 
ATOM   6399 H  HD12 . LEU   B 1 169 ? 29.427 -35.169 -15.269 1.00 33.80 ?  169 LEU   B HD12 1 
ATOM   6400 H  HD13 . LEU   B 1 169 ? 28.595 -36.384 -15.867 1.00 33.80 ?  169 LEU   B HD13 1 
ATOM   6401 H  HD21 . LEU   B 1 169 ? 26.664 -36.777 -14.002 1.00 33.10 ?  169 LEU   B HD21 1 
ATOM   6402 H  HD22 . LEU   B 1 169 ? 27.538 -38.103 -14.012 1.00 33.10 ?  169 LEU   B HD22 1 
ATOM   6403 H  HD23 . LEU   B 1 169 ? 27.277 -37.334 -12.647 1.00 33.10 ?  169 LEU   B HD23 1 
HETATM 6404 C  C1   T TFA   C 2 .   ? 12.195 -1.318  1.470   0.10 10.74 ?  201 TFA   A C1   1 
HETATM 6405 C  C2   T TFA   C 2 .   ? 12.863 -1.744  0.137   0.10 12.60 ?  201 TFA   A C2   1 
HETATM 6406 O  O    T TFA   C 2 .   ? 12.895 -1.576  2.456   0.10 8.81  ?  201 TFA   A O    1 
HETATM 6407 F  F1   T TFA   C 2 .   ? 12.981 -3.083  0.084   0.10 13.46 ?  201 TFA   A F1   1 
HETATM 6408 F  F2   T TFA   C 2 .   ? 12.151 -1.366  -0.939  0.10 13.20 ?  201 TFA   A F2   1 
HETATM 6409 F  F3   T TFA   C 2 .   ? 14.092 -1.238  -0.030  0.10 13.13 ?  201 TFA   A F3   1 
HETATM 6410 O  OXT  T TFA   C 2 .   ? 11.083 -0.789  1.377   0.10 11.48 ?  201 TFA   A OXT  1 
HETATM 6411 N  N2   B A1A86 D 3 .   ? 15.003 -0.163  3.864   0.26 16.27 ?  202 A1A86 A N2   1 
HETATM 6412 C  C3   B A1A86 D 3 .   ? 12.034 -0.847  1.741   0.26 17.93 ?  202 A1A86 A C3   1 
HETATM 6413 C  C6   B A1A86 D 3 .   ? 14.951 -0.421  0.879   0.26 16.45 ?  202 A1A86 A C6   1 
HETATM 6414 C  C9   B A1A86 D 3 .   ? 14.975 -0.068  5.247   0.26 15.92 ?  202 A1A86 A C9   1 
HETATM 6415 C  C12  B A1A86 D 3 .   ? 15.816 3.594   3.480   0.26 14.58 ?  202 A1A86 A C12  1 
HETATM 6416 C  C1   B A1A86 D 3 .   ? 12.218 1.564   1.102   0.26 17.94 ?  202 A1A86 A C1   1 
HETATM 6417 C  C10  B A1A86 D 3 .   ? 15.446 2.140   5.208   0.26 14.84 ?  202 A1A86 A C10  1 
HETATM 6418 C  C11  B A1A86 D 3 .   ? 15.504 2.196   3.766   0.26 15.15 ?  202 A1A86 A C11  1 
HETATM 6419 C  C13  B A1A86 D 3 .   ? 15.918 4.274   4.687   0.26 14.02 ?  202 A1A86 A C13  1 
HETATM 6420 C  C2   B A1A86 D 3 .   ? 12.299 0.108   0.565   0.26 17.88 ?  202 A1A86 A C2   1 
HETATM 6421 C  C4   B A1A86 D 3 .   ? 11.230 -0.053  -0.538  0.26 18.42 ?  202 A1A86 A C4   1 
HETATM 6422 C  C5   B A1A86 D 3 .   ? 13.699 -0.217  -0.072  0.26 17.18 ?  202 A1A86 A C5   1 
HETATM 6423 C  C7   B A1A86 D 3 .   ? 16.204 -0.837  0.024   0.26 17.45 ?  202 A1A86 A C7   1 
HETATM 6424 C  C8   B A1A86 D 3 .   ? 15.262 0.944   3.086   0.26 15.98 ?  202 A1A86 A C8   1 
HETATM 6425 N  N1   B A1A86 D 3 .   ? 15.283 0.800   1.676   0.26 15.93 ?  202 A1A86 A N1   1 
HETATM 6426 N  N3   B A1A86 D 3 .   ? 15.181 1.036   5.974   0.26 15.37 ?  202 A1A86 A N3   1 
HETATM 6427 N  N4   B A1A86 D 3 .   ? 15.697 3.373   5.676   0.26 14.17 ?  202 A1A86 A N4   1 
HETATM 6428 O  O1   B A1A86 D 3 .   ? 17.181 -1.463  0.818   0.26 17.58 ?  202 A1A86 A O1   1 
HETATM 6429 H  H7   B A1A86 D 3 .   ? 12.045 -1.909  1.448   0.26 21.53 ?  202 A1A86 A H7   1 
HETATM 6430 H  H6   B A1A86 D 3 .   ? 11.062 -0.685  2.227   0.26 21.53 ?  202 A1A86 A H6   1 
HETATM 6431 H  H5   B A1A86 D 3 .   ? 12.773 -0.767  2.560   0.26 21.53 ?  202 A1A86 A H5   1 
HETATM 6432 H  H1   B A1A86 D 3 .   ? 14.687 -1.297  1.554   0.26 19.75 ?  202 A1A86 A H1   1 
HETATM 6433 H  H17  B A1A86 D 3 .   ? 14.751 -0.982  5.841   0.26 19.11 ?  202 A1A86 A H17  1 
HETATM 6434 H  H18  B A1A86 D 3 .   ? 15.950 4.082   2.531   0.26 17.51 ?  202 A1A86 A H18  1 
HETATM 6435 H  H2   B A1A86 D 3 .   ? 12.511 2.314   0.363   0.26 21.54 ?  202 A1A86 A H2   1 
HETATM 6436 H  H4   B A1A86 D 3 .   ? 12.854 1.756   1.982   0.26 21.54 ?  202 A1A86 A H4   1 
HETATM 6437 H  H3   B A1A86 D 3 .   ? 11.200 1.868   1.423   0.26 21.54 ?  202 A1A86 A H3   1 
HETATM 6438 H  H19  B A1A86 D 3 .   ? 16.123 5.295   4.986   0.26 16.83 ?  202 A1A86 A H19  1 
HETATM 6439 H  H9   B A1A86 D 3 .   ? 11.382 0.623   -1.400  0.26 22.11 ?  202 A1A86 A H9   1 
HETATM 6440 H  H8   B A1A86 D 3 .   ? 10.197 0.145   -0.200  0.26 22.11 ?  202 A1A86 A H8   1 
HETATM 6441 H  H10  B A1A86 D 3 .   ? 11.203 -1.059  -0.970  0.26 22.11 ?  202 A1A86 A H10  1 
HETATM 6442 H  H12  B A1A86 D 3 .   ? 13.924 0.581   -0.799  0.26 20.63 ?  202 A1A86 A H12  1 
HETATM 6443 H  H11  B A1A86 D 3 .   ? 13.592 -1.113  -0.719  0.26 20.63 ?  202 A1A86 A H11  1 
HETATM 6444 H  H13  B A1A86 D 3 .   ? 15.856 -1.529  -0.773  0.26 20.95 ?  202 A1A86 A H13  1 
HETATM 6445 H  H14  B A1A86 D 3 .   ? 16.624 0.035   -0.515  0.26 20.95 ?  202 A1A86 A H14  1 
HETATM 6446 H  H16  B A1A86 D 3 .   ? 15.554 1.605   1.109   0.26 19.13 ?  202 A1A86 A H16  1 
HETATM 6447 H  H20  B A1A86 D 3 .   ? 15.702 3.604   6.697   0.26 17.01 ?  202 A1A86 A H20  1 
HETATM 6448 H  H15  B A1A86 D 3 .   ? 17.851 -1.863  0.250   0.26 21.10 ?  202 A1A86 A H15  1 
HETATM 6449 CL CL   B CL    E 4 .   ? 16.035 2.752   -0.918  0.26 18.99 ?  203 CL    A CL   1 
HETATM 6450 O  O    . HOH   F 5 .   ? 14.801 -4.694  20.567  1.00 46.39 ?  301 HOH   A O    1 
HETATM 6451 O  O    . HOH   F 5 .   ? 12.123 0.303   14.807  1.00 35.96 ?  302 HOH   A O    1 
HETATM 6452 O  O    . HOH   F 5 .   ? 34.435 -1.874  12.514  1.00 39.51 ?  303 HOH   A O    1 
HETATM 6453 O  O    A HOH   F 5 .   ? 4.755  3.901   0.628   0.74 24.03 ?  304 HOH   A O    1 
HETATM 6454 O  O    . HOH   F 5 .   ? 28.962 0.461   -9.742  1.00 23.38 ?  305 HOH   A O    1 
HETATM 6455 O  O    . HOH   F 5 .   ? 14.481 -24.697 11.642  1.00 32.64 ?  306 HOH   A O    1 
HETATM 6456 O  O    . HOH   F 5 .   ? 17.123 -18.038 15.092  1.00 26.00 ?  307 HOH   A O    1 
HETATM 6457 O  O    . HOH   F 5 .   ? 15.219 -12.264 18.765  1.00 35.56 ?  308 HOH   A O    1 
HETATM 6458 O  O    . HOH   F 5 .   ? 42.551 10.561  5.232   1.00 21.51 ?  309 HOH   A O    1 
HETATM 6459 O  O    . HOH   F 5 .   ? 14.729 -13.981 16.734  1.00 25.38 ?  310 HOH   A O    1 
HETATM 6460 O  O    . HOH   F 5 .   ? 22.807 12.525  1.651   1.00 16.80 ?  311 HOH   A O    1 
HETATM 6461 O  O    . HOH   F 5 .   ? 18.754 -2.415  -16.400 1.00 45.21 ?  312 HOH   A O    1 
HETATM 6462 O  O    . HOH   F 5 .   ? 7.955  -12.676 -0.856  1.00 22.40 ?  313 HOH   A O    1 
HETATM 6463 O  O    . HOH   F 5 .   ? 31.054 6.173   -12.300 1.00 30.38 ?  314 HOH   A O    1 
HETATM 6464 O  O    . HOH   F 5 .   ? 8.067  -21.529 3.957   1.00 50.57 ?  315 HOH   A O    1 
HETATM 6465 O  O    . HOH   F 5 .   ? 18.926 -21.979 6.887   1.00 35.00 ?  316 HOH   A O    1 
HETATM 6466 O  O    . HOH   F 5 .   ? 28.306 -6.392  19.672  1.00 42.99 ?  317 HOH   A O    1 
HETATM 6467 O  O    A HOH   F 5 .   ? 17.556 -1.733  0.450   0.74 20.03 ?  318 HOH   A O    1 
HETATM 6468 O  O    . HOH   F 5 .   ? -0.435 -3.078  3.138   1.00 39.10 ?  319 HOH   A O    1 
HETATM 6469 O  O    . HOH   F 5 .   ? 3.525  -9.378  9.852   1.00 36.21 ?  320 HOH   A O    1 
HETATM 6470 O  O    . HOH   F 5 .   ? 0.648  -4.519  0.327   1.00 34.12 ?  321 HOH   A O    1 
HETATM 6471 O  O    . HOH   F 5 .   ? 9.203  -10.192 19.340  1.00 43.25 ?  322 HOH   A O    1 
HETATM 6472 O  O    . HOH   F 5 .   ? 10.412 -22.163 -1.254  1.00 44.67 ?  323 HOH   A O    1 
HETATM 6473 O  O    . HOH   F 5 .   ? 34.080 -1.029  -8.937  1.00 27.43 ?  324 HOH   A O    1 
HETATM 6474 O  O    . HOH   F 5 .   ? 30.304 -13.356 -8.592  1.00 21.83 ?  325 HOH   A O    1 
HETATM 6475 O  O    . HOH   F 5 .   ? 14.223 -4.512  -11.871 1.00 32.18 ?  326 HOH   A O    1 
HETATM 6476 O  O    . HOH   F 5 .   ? 18.617 9.441   9.024   1.00 23.49 ?  327 HOH   A O    1 
HETATM 6477 O  O    . HOH   F 5 .   ? 37.611 2.777   10.174  1.00 29.96 ?  328 HOH   A O    1 
HETATM 6478 O  O    . HOH   F 5 .   ? 42.665 4.361   5.390   1.00 31.91 ?  329 HOH   A O    1 
HETATM 6479 O  O    . HOH   F 5 .   ? 31.077 -18.159 7.781   1.00 21.90 ?  330 HOH   A O    1 
HETATM 6480 O  O    B HOH   F 5 .   ? 4.832  4.302   0.653   0.26 35.29 ?  331 HOH   A O    1 
HETATM 6481 O  O    . HOH   F 5 .   ? 19.937 -12.566 -8.874  1.00 27.65 ?  332 HOH   A O    1 
HETATM 6482 O  O    . HOH   F 5 .   ? 36.283 -5.055  -0.552  1.00 30.25 ?  333 HOH   A O    1 
HETATM 6483 O  O    . HOH   F 5 .   ? 26.538 -19.395 -1.832  1.00 15.08 ?  334 HOH   A O    1 
HETATM 6484 O  O    . HOH   F 5 .   ? 26.907 11.412  1.669   1.00 18.24 ?  335 HOH   A O    1 
HETATM 6485 O  O    . HOH   F 5 .   ? 38.329 10.129  7.219   1.00 32.85 ?  336 HOH   A O    1 
HETATM 6486 O  O    . HOH   F 5 .   ? 28.456 -0.201  -13.387 1.00 33.23 ?  337 HOH   A O    1 
HETATM 6487 O  O    B HOH   F 5 .   ? 22.690 5.433   -1.989  0.26 19.45 ?  338 HOH   A O    1 
HETATM 6488 O  O    . HOH   F 5 .   ? 27.312 13.848  2.917   1.00 32.66 ?  339 HOH   A O    1 
HETATM 6489 O  O    . HOH   F 5 .   ? 39.832 -0.979  -5.193  1.00 22.53 ?  340 HOH   A O    1 
HETATM 6490 O  O    . HOH   F 5 .   ? 22.356 5.392   18.990  1.00 44.59 ?  341 HOH   A O    1 
HETATM 6491 O  O    . HOH   F 5 .   ? 38.657 4.982   6.981   1.00 17.49 ?  342 HOH   A O    1 
HETATM 6492 O  O    A HOH   F 5 .   ? 14.695 -3.675  3.102   0.74 16.64 ?  343 HOH   A O    1 
HETATM 6493 O  O    . HOH   F 5 .   ? 44.381 7.043   6.474   1.00 27.92 ?  344 HOH   A O    1 
HETATM 6494 O  O    . HOH   F 5 .   ? 14.578 -0.488  -12.120 1.00 26.70 ?  345 HOH   A O    1 
HETATM 6495 O  O    . HOH   F 5 .   ? 24.087 -2.097  -2.073  1.00 12.14 ?  346 HOH   A O    1 
HETATM 6496 O  O    . HOH   F 5 .   ? 37.498 11.893  4.979   1.00 33.16 ?  347 HOH   A O    1 
HETATM 6497 O  O    . HOH   F 5 .   ? 20.654 -19.721 -5.089  1.00 27.90 ?  348 HOH   A O    1 
HETATM 6498 O  O    . HOH   F 5 .   ? 15.139 3.958   17.770  1.00 43.62 ?  349 HOH   A O    1 
HETATM 6499 O  O    . HOH   F 5 .   ? 18.681 -19.446 13.555  1.00 34.84 ?  350 HOH   A O    1 
HETATM 6500 O  O    . HOH   F 5 .   ? 8.820  -12.167 17.137  1.00 44.83 ?  351 HOH   A O    1 
HETATM 6501 O  O    . HOH   F 5 .   ? 31.099 -13.950 -2.493  1.00 15.54 ?  352 HOH   A O    1 
HETATM 6502 O  O    . HOH   F 5 .   ? 31.813 8.196   14.866  1.00 24.20 ?  353 HOH   A O    1 
HETATM 6503 O  O    . HOH   F 5 .   ? 35.831 -12.734 6.819   1.00 17.32 ?  354 HOH   A O    1 
HETATM 6504 O  O    . HOH   F 5 .   ? 21.322 -2.357  -2.201  1.00 17.41 ?  355 HOH   A O    1 
HETATM 6505 O  O    . HOH   F 5 .   ? 37.358 -2.846  9.642   1.00 40.22 ?  356 HOH   A O    1 
HETATM 6506 O  O    . HOH   F 5 .   ? 16.506 -22.074 0.941   1.00 29.35 ?  357 HOH   A O    1 
HETATM 6507 O  O    . HOH   F 5 .   ? 17.157 -17.789 -5.027  1.00 28.67 ?  358 HOH   A O    1 
HETATM 6508 O  O    . HOH   F 5 .   ? 13.574 -15.238 -7.476  1.00 27.86 ?  359 HOH   A O    1 
HETATM 6509 O  O    . HOH   F 5 .   ? 21.900 -21.945 8.384   1.00 30.09 ?  360 HOH   A O    1 
HETATM 6510 O  O    . HOH   F 5 .   ? 13.295 -1.434  -6.611  1.00 17.88 ?  361 HOH   A O    1 
HETATM 6511 O  O    . HOH   F 5 .   ? 22.288 -19.342 11.404  1.00 33.20 ?  362 HOH   A O    1 
HETATM 6512 O  O    . HOH   F 5 .   ? 27.968 0.835   -7.141  1.00 15.96 ?  363 HOH   A O    1 
HETATM 6513 O  O    . HOH   F 5 .   ? 43.473 7.825   2.693   1.00 26.68 ?  364 HOH   A O    1 
HETATM 6514 O  O    . HOH   F 5 .   ? 15.541 11.910  7.951   1.00 35.28 ?  365 HOH   A O    1 
HETATM 6515 O  O    . HOH   F 5 .   ? 13.963 -5.001  17.496  1.00 26.74 ?  366 HOH   A O    1 
HETATM 6516 O  O    . HOH   F 5 .   ? 11.786 -10.830 -10.142 1.00 43.99 ?  367 HOH   A O    1 
HETATM 6517 O  O    . HOH   F 5 .   ? 9.870  -21.417 5.775   1.00 19.99 ?  368 HOH   A O    1 
HETATM 6518 O  O    . HOH   F 5 .   ? 27.535 -10.664 14.055  1.00 18.50 ?  369 HOH   A O    1 
HETATM 6519 O  O    . HOH   F 5 .   ? 30.881 3.076   8.274   1.00 13.66 ?  370 HOH   A O    1 
HETATM 6520 O  O    . HOH   F 5 .   ? -0.616 -8.512  2.166   1.00 42.05 ?  371 HOH   A O    1 
HETATM 6521 O  O    . HOH   F 5 .   ? 22.657 -11.979 21.847  1.00 44.72 ?  372 HOH   A O    1 
HETATM 6522 O  O    . HOH   F 5 .   ? 44.015 8.477   -3.101  1.00 29.34 ?  373 HOH   A O    1 
HETATM 6523 O  O    . HOH   F 5 .   ? 14.330 -21.202 -4.274  1.00 31.24 ?  374 HOH   A O    1 
HETATM 6524 O  O    . HOH   F 5 .   ? 28.568 -10.682 -14.015 1.00 46.96 ?  375 HOH   A O    1 
HETATM 6525 O  O    A HOH   F 5 .   ? 14.335 0.548   6.809   0.74 21.26 ?  376 HOH   A O    1 
HETATM 6526 O  O    . HOH   F 5 .   ? 21.305 10.282  15.051  1.00 35.25 ?  377 HOH   A O    1 
HETATM 6527 O  O    . HOH   F 5 .   ? 7.686  -6.454  -6.650  1.00 38.79 ?  378 HOH   A O    1 
HETATM 6528 O  O    . HOH   F 5 .   ? 33.695 -7.145  4.317   1.00 19.07 ?  379 HOH   A O    1 
HETATM 6529 O  O    . HOH   F 5 .   ? 23.535 11.375  4.095   1.00 13.95 ?  380 HOH   A O    1 
HETATM 6530 O  O    . HOH   F 5 .   ? 24.466 3.573   -1.799  1.00 17.43 ?  381 HOH   A O    1 
HETATM 6531 O  O    . HOH   F 5 .   ? 24.651 2.012   -7.070  1.00 21.48 ?  382 HOH   A O    1 
HETATM 6532 O  O    . HOH   F 5 .   ? 31.813 -7.288  -9.872  1.00 23.33 ?  383 HOH   A O    1 
HETATM 6533 O  O    . HOH   F 5 .   ? 32.000 -9.304  -6.660  1.00 24.19 ?  384 HOH   A O    1 
HETATM 6534 O  O    . HOH   F 5 .   ? 17.016 -19.282 4.899   1.00 16.55 ?  385 HOH   A O    1 
HETATM 6535 O  O    T HOH   F 5 .   ? 15.468 -0.442  2.395   0.10 7.67  ?  386 HOH   A O    1 
HETATM 6536 O  O    . HOH   F 5 .   ? 37.599 -2.028  5.793   1.00 26.79 ?  387 HOH   A O    1 
HETATM 6537 O  O    . HOH   F 5 .   ? 33.555 -17.062 8.039   1.00 20.68 ?  388 HOH   A O    1 
HETATM 6538 O  O    A HOH   F 5 .   ? 7.006  -8.190  11.848  0.74 19.60 ?  389 HOH   A O    1 
HETATM 6539 O  O    . HOH   F 5 .   ? 6.746  -3.365  12.937  1.00 33.31 ?  390 HOH   A O    1 
HETATM 6540 O  O    . HOH   F 5 .   ? 20.154 4.535   -7.574  1.00 21.45 ?  391 HOH   A O    1 
HETATM 6541 O  O    . HOH   F 5 .   ? 5.270  2.716   5.086   1.00 34.07 ?  392 HOH   A O    1 
HETATM 6542 O  O    . HOH   F 5 .   ? 21.436 3.112   -0.304  1.00 14.69 ?  393 HOH   A O    1 
HETATM 6543 O  O    . HOH   F 5 .   ? 25.780 -0.811  -7.341  1.00 16.13 ?  394 HOH   A O    1 
HETATM 6544 O  O    . HOH   F 5 .   ? 24.288 -7.807  14.470  1.00 18.39 ?  395 HOH   A O    1 
HETATM 6545 O  O    . HOH   F 5 .   ? 32.881 -9.256  6.015   1.00 21.14 ?  396 HOH   A O    1 
HETATM 6546 O  O    . HOH   F 5 .   ? 15.249 -21.592 14.270  1.00 19.40 ?  397 HOH   A O    1 
HETATM 6547 O  O    . HOH   F 5 .   ? 24.747 -17.602 12.717  1.00 26.68 ?  398 HOH   A O    1 
HETATM 6548 O  O    . HOH   F 5 .   ? 27.419 -6.060  -14.010 1.00 38.39 ?  399 HOH   A O    1 
HETATM 6549 O  O    . HOH   F 5 .   ? 11.094 1.686   12.708  1.00 26.22 ?  400 HOH   A O    1 
HETATM 6550 O  O    A HOH   F 5 .   ? 11.128 -0.399  1.942   0.64 25.90 ?  401 HOH   A O    1 
HETATM 6551 O  O    . HOH   F 5 .   ? 23.993 -15.682 -9.151  1.00 35.75 ?  402 HOH   A O    1 
HETATM 6552 O  O    . HOH   F 5 .   ? 20.570 -20.064 2.769   1.00 19.00 ?  403 HOH   A O    1 
HETATM 6553 O  O    . HOH   F 5 .   ? 30.757 1.843   16.682  1.00 23.68 ?  404 HOH   A O    1 
HETATM 6554 O  O    B HOH   F 5 .   ? 19.147 -0.711  -1.822  0.26 21.23 ?  405 HOH   A O    1 
HETATM 6555 O  O    . HOH   F 5 .   ? 30.113 -10.155 13.031  1.00 22.80 ?  406 HOH   A O    1 
HETATM 6556 O  O    B HOH   F 5 .   ? 14.858 -2.982  3.357   0.26 18.72 ?  407 HOH   A O    1 
HETATM 6557 O  O    . HOH   F 5 .   ? 27.370 2.339   18.746  1.00 30.11 ?  408 HOH   A O    1 
HETATM 6558 O  O    A HOH   F 5 .   ? 15.860 -0.969  5.278   0.74 23.12 ?  409 HOH   A O    1 
HETATM 6559 O  O    . HOH   F 5 .   ? 15.930 2.078   24.810  1.00 49.14 ?  410 HOH   A O    1 
HETATM 6560 O  O    . HOH   F 5 .   ? 41.600 1.611   4.939   1.00 36.43 ?  411 HOH   A O    1 
HETATM 6561 O  O    . HOH   F 5 .   ? 27.010 4.171   -0.662  1.00 13.93 ?  412 HOH   A O    1 
HETATM 6562 O  O    A HOH   F 5 .   ? 19.020 -0.686  -1.617  0.74 13.08 ?  413 HOH   A O    1 
HETATM 6563 O  O    . HOH   F 5 .   ? 14.111 -23.129 7.461   1.00 20.27 ?  414 HOH   A O    1 
HETATM 6564 O  O    . HOH   F 5 .   ? 40.980 -8.295  -6.716  1.00 38.81 ?  415 HOH   A O    1 
HETATM 6565 O  O    . HOH   F 5 .   ? 23.976 -20.318 -1.369  1.00 17.55 ?  416 HOH   A O    1 
HETATM 6566 O  O    . HOH   F 5 .   ? 38.214 -1.337  -1.972  1.00 21.32 ?  417 HOH   A O    1 
HETATM 6567 O  O    A HOH   F 5 .   ? 6.525  -5.633  11.180  0.74 19.38 ?  418 HOH   A O    1 
HETATM 6568 O  O    . HOH   F 5 .   ? 32.579 -10.621 3.194   1.00 33.23 ?  419 HOH   A O    1 
HETATM 6569 O  O    . HOH   F 5 .   ? 15.182 -8.071  -9.619  1.00 24.74 ?  420 HOH   A O    1 
HETATM 6570 O  O    . HOH   F 5 .   ? 32.664 -4.220  -9.926  1.00 28.79 ?  421 HOH   A O    1 
HETATM 6571 O  O    . HOH   F 5 .   ? 16.208 16.651  8.715   1.00 33.36 ?  422 HOH   A O    1 
HETATM 6572 O  O    . HOH   F 5 .   ? 35.083 -5.217  -3.081  1.00 19.57 ?  423 HOH   A O    1 
HETATM 6573 O  O    . HOH   F 5 .   ? 30.427 -12.961 13.479  1.00 21.19 ?  424 HOH   A O    1 
HETATM 6574 O  O    . HOH   F 5 .   ? 36.772 -5.042  5.342   1.00 26.35 ?  425 HOH   A O    1 
HETATM 6575 O  O    . HOH   F 5 .   ? 21.790 -13.821 -8.198  1.00 37.16 ?  426 HOH   A O    1 
HETATM 6576 O  O    . HOH   F 5 .   ? 45.003 -0.739  2.986   1.00 41.71 ?  427 HOH   A O    1 
HETATM 6577 O  O    . HOH   F 5 .   ? 22.741 8.070   18.436  1.00 45.08 ?  428 HOH   A O    1 
HETATM 6578 O  O    . HOH   F 5 .   ? 24.118 3.965   -4.885  1.00 25.49 ?  429 HOH   A O    1 
HETATM 6579 O  O    . HOH   F 5 .   ? 10.394 -13.769 -1.699  1.00 18.76 ?  430 HOH   A O    1 
HETATM 6580 O  O    T HOH   F 5 .   ? 11.983 -2.162  -3.648  0.10 6.99  ?  431 HOH   A O    1 
HETATM 6581 O  O    . HOH   F 5 .   ? 16.042 6.899   2.983   1.00 19.78 ?  432 HOH   A O    1 
HETATM 6582 O  O    . HOH   F 5 .   ? 16.166 -14.159 20.276  1.00 42.96 ?  433 HOH   A O    1 
HETATM 6583 O  O    . HOH   F 5 .   ? 11.717 -10.770 17.012  1.00 25.18 ?  434 HOH   A O    1 
HETATM 6584 O  O    . HOH   F 5 .   ? 9.486  -16.363 -1.989  1.00 45.32 ?  435 HOH   A O    1 
HETATM 6585 O  O    . HOH   F 5 .   ? 20.631 -17.825 24.784  1.00 50.62 ?  436 HOH   A O    1 
HETATM 6586 O  O    . HOH   F 5 .   ? 27.191 -3.239  19.373  1.00 38.49 ?  437 HOH   A O    1 
HETATM 6587 O  O    B HOH   F 5 .   ? 23.285 7.867   -3.119  0.26 16.96 ?  438 HOH   A O    1 
HETATM 6588 O  O    . HOH   F 5 .   ? 31.409 -12.767 0.008   1.00 21.24 ?  439 HOH   A O    1 
HETATM 6589 O  O    . HOH   F 5 .   ? 23.601 -8.086  17.130  1.00 22.91 ?  440 HOH   A O    1 
HETATM 6590 O  O    . HOH   F 5 .   ? 23.339 -20.983 1.333   1.00 20.04 ?  441 HOH   A O    1 
HETATM 6591 O  O    A HOH   F 5 .   ? 16.320 2.931   -1.428  0.74 16.25 ?  442 HOH   A O    1 
HETATM 6592 O  O    B HOH   F 5 .   ? 19.215 1.968   -0.973  0.26 22.84 ?  443 HOH   A O    1 
HETATM 6593 O  O    . HOH   F 5 .   ? 34.465 -8.111  -0.549  1.00 30.39 ?  444 HOH   A O    1 
HETATM 6594 O  O    . HOH   F 5 .   ? 21.336 -9.311  21.384  1.00 46.71 ?  445 HOH   A O    1 
HETATM 6595 O  O    . HOH   F 5 .   ? 19.541 -11.019 24.143  1.00 66.27 ?  446 HOH   A O    1 
HETATM 6596 O  O    . HOH   F 5 .   ? 18.492 -16.051 16.397  1.00 37.79 ?  447 HOH   A O    1 
HETATM 6597 O  O    . HOH   F 5 .   ? 18.548 4.908   -15.128 1.00 50.61 ?  448 HOH   A O    1 
HETATM 6598 O  O    . HOH   F 5 .   ? 21.583 -14.722 18.051  1.00 52.13 ?  449 HOH   A O    1 
HETATM 6599 O  O    A HOH   F 5 .   ? 14.088 -0.360  3.470   0.64 30.37 ?  450 HOH   A O    1 
HETATM 6600 O  O    . HOH   F 5 .   ? 30.662 14.811  2.817   1.00 21.24 ?  451 HOH   A O    1 
HETATM 6601 O  O    . HOH   F 5 .   ? 37.776 -8.826  -3.460  1.00 25.83 ?  452 HOH   A O    1 
HETATM 6602 O  O    A HOH   F 5 .   ? 18.924 2.015   -0.739  0.74 14.14 ?  453 HOH   A O    1 
HETATM 6603 O  O    A HOH   F 5 .   ? -1.370 -4.966  7.646   0.74 37.94 ?  454 HOH   A O    1 
HETATM 6604 O  O    A HOH   F 5 .   ? 23.263 7.496   -3.218  0.74 32.98 ?  455 HOH   A O    1 
HETATM 6605 O  O    . HOH   F 5 .   ? 29.874 -16.111 10.638  1.00 33.87 ?  456 HOH   A O    1 
HETATM 6606 O  O    . HOH   F 5 .   ? 27.875 7.070   -6.360  1.00 36.77 ?  457 HOH   A O    1 
HETATM 6607 O  O    B HOH   F 5 .   ? 5.345  -1.316  -2.477  0.26 25.48 ?  458 HOH   A O    1 
HETATM 6608 O  O    . HOH   F 5 .   ? 25.451 8.259   -4.811  1.00 25.67 ?  459 HOH   A O    1 
HETATM 6609 O  O    . HOH   F 5 .   ? 29.912 -1.959  -12.713 1.00 44.64 ?  460 HOH   A O    1 
HETATM 6610 O  O    . HOH   F 5 .   ? 32.532 -16.038 10.777  1.00 38.08 ?  461 HOH   A O    1 
HETATM 6611 O  O    . HOH   F 5 .   ? 19.928 -17.325 -5.096  1.00 26.21 ?  462 HOH   A O    1 
HETATM 6612 O  O    . HOH   F 5 .   ? 24.921 5.634   20.785  1.00 52.57 ?  463 HOH   A O    1 
HETATM 6613 O  O    . HOH   F 5 .   ? 24.635 14.603  7.895   1.00 36.81 ?  464 HOH   A O    1 
HETATM 6614 O  O    . HOH   F 5 .   ? 23.196 -22.415 -3.389  1.00 37.42 ?  465 HOH   A O    1 
HETATM 6615 O  O    . HOH   F 5 .   ? 26.987 11.666  -1.373  1.00 32.67 ?  466 HOH   A O    1 
HETATM 6616 O  O    B HOH   F 5 .   ? 7.923  -0.199  -1.571  0.26 23.87 ?  467 HOH   A O    1 
HETATM 6617 O  O    . HOH   F 5 .   ? 15.735 -21.518 3.713   1.00 23.68 ?  468 HOH   A O    1 
HETATM 6618 O  O    . HOH   F 5 .   ? 12.334 1.616   17.365  1.00 44.15 ?  469 HOH   A O    1 
HETATM 6619 O  O    . HOH   F 5 .   ? 18.798 10.856  11.354  1.00 35.46 ?  470 HOH   A O    1 
HETATM 6620 O  O    . HOH   F 5 .   ? 23.556 13.706  5.548   1.00 20.70 ?  471 HOH   A O    1 
HETATM 6621 O  O    A HOH   F 5 .   ? 22.028 5.254   -5.820  0.74 32.15 ?  472 HOH   A O    1 
HETATM 6622 O  O    . HOH   F 5 .   ? 25.824 10.838  -3.761  1.00 28.21 ?  473 HOH   A O    1 
HETATM 6623 O  O    . HOH   F 5 .   ? 12.022 -13.442 16.378  1.00 44.71 ?  474 HOH   A O    1 
HETATM 6624 O  O    . HOH   F 5 .   ? 27.623 -11.540 16.522  1.00 37.12 ?  475 HOH   A O    1 
HETATM 6625 O  O    . HOH   F 5 .   ? 39.668 -6.935  -3.393  1.00 42.62 ?  476 HOH   A O    1 
HETATM 6626 O  O    . HOH   F 5 .   ? 28.944 8.963   17.503  1.00 39.99 ?  477 HOH   A O    1 
HETATM 6627 O  O    . HOH   F 5 .   ? 23.172 11.870  -4.059  1.00 21.18 ?  478 HOH   A O    1 
HETATM 6628 O  O    . HOH   F 5 .   ? 10.958 -15.118 -6.080  1.00 37.71 ?  479 HOH   A O    1 
HETATM 6629 O  O    . HOH   F 5 .   ? 17.456 -18.781 19.833  1.00 49.26 ?  480 HOH   A O    1 
HETATM 6630 O  O    . HOH   F 5 .   ? 18.155 -16.231 -8.812  1.00 41.27 ?  481 HOH   A O    1 
HETATM 6631 O  O    . HOH   F 5 .   ? 35.313 7.411   12.255  1.00 44.24 ?  482 HOH   A O    1 
HETATM 6632 O  O    . HOH   F 5 .   ? 15.689 -17.135 -7.014  1.00 33.64 ?  483 HOH   A O    1 
HETATM 6633 O  O    . HOH   F 5 .   ? 41.038 -4.004  -0.358  1.00 40.32 ?  484 HOH   A O    1 
HETATM 6634 O  O    . HOH   F 5 .   ? 30.928 0.738   19.175  1.00 40.73 ?  485 HOH   A O    1 
HETATM 6635 O  O    B HOH   F 5 .   ? 22.234 5.375   -6.101  0.26 30.42 ?  486 HOH   A O    1 
HETATM 6636 O  O    . HOH   F 5 .   ? 14.020 -10.294 -10.831 1.00 35.45 ?  487 HOH   A O    1 
HETATM 6637 O  O    . HOH   F 5 .   ? 16.824 -20.563 16.225  1.00 30.59 ?  488 HOH   A O    1 
HETATM 6638 O  O    . HOH   F 5 .   ? 23.326 -12.964 19.380  1.00 45.67 ?  489 HOH   A O    1 
HETATM 6639 O  O    . HOH   F 5 .   ? 20.534 -16.022 -7.391  1.00 30.79 ?  490 HOH   A O    1 
HETATM 6640 O  O    . HOH   F 5 .   ? 28.717 -7.962  -15.322 1.00 45.74 ?  491 HOH   A O    1 
HETATM 6641 O  O    . HOH   F 5 .   ? 28.693 -4.668  -12.289 1.00 35.66 ?  492 HOH   A O    1 
HETATM 6642 O  O    . HOH   F 5 .   ? 44.616 10.482  -1.557  1.00 30.66 ?  493 HOH   A O    1 
HETATM 6643 O  O    . HOH   F 5 .   ? 41.789 9.339   -4.085  1.00 35.05 ?  494 HOH   A O    1 
HETATM 6644 O  O    . HOH   F 5 .   ? 31.589 -0.598  -10.567 1.00 30.48 ?  495 HOH   A O    1 
HETATM 6645 O  O    . HOH   F 5 .   ? 18.470 -23.214 1.897   1.00 41.94 ?  496 HOH   A O    1 
HETATM 6646 O  O    . HOH   F 5 .   ? 39.232 2.391   7.536   1.00 35.79 ?  497 HOH   A O    1 
HETATM 6647 O  O    . HOH   F 5 .   ? 40.558 -0.275  -7.840  1.00 38.15 ?  498 HOH   A O    1 
HETATM 6648 O  O    . HOH   F 5 .   ? 20.044 -22.361 4.116   1.00 28.60 ?  499 HOH   A O    1 
HETATM 6649 O  O    . HOH   F 5 .   ? 16.058 -6.798  -11.800 1.00 43.91 ?  500 HOH   A O    1 
HETATM 6650 O  O    . HOH   F 5 .   ? 30.700 5.904   -14.680 1.00 38.67 ?  501 HOH   A O    1 
HETATM 6651 O  O    . HOH   F 5 .   ? 14.073 -25.395 8.895   1.00 32.17 ?  502 HOH   A O    1 
HETATM 6652 O  O    . HOH   F 5 .   ? 16.192 -23.383 5.744   1.00 29.24 ?  503 HOH   A O    1 
HETATM 6653 O  O    . HOH   F 5 .   ? 30.780 -5.859  -11.866 1.00 47.76 ?  504 HOH   A O    1 
HETATM 6654 O  O    . HOH   F 5 .   ? 37.476 -6.707  7.509   1.00 28.05 ?  505 HOH   A O    1 
HETATM 6655 O  O    . HOH   F 5 .   ? 23.161 -23.853 1.656   1.00 32.53 ?  506 HOH   A O    1 
HETATM 6656 O  O    . HOH   F 5 .   ? 39.606 0.016   6.631   1.00 31.55 ?  507 HOH   A O    1 
HETATM 6657 O  O    . HOH   F 5 .   ? 29.005 14.407  0.904   1.00 46.04 ?  508 HOH   A O    1 
HETATM 6658 O  O    B HOH   F 5 .   ? 5.819  6.876   1.119   0.26 32.76 ?  509 HOH   A O    1 
HETATM 6659 O  O    . HOH   F 5 .   ? 38.096 13.955  6.760   1.00 41.30 ?  510 HOH   A O    1 
HETATM 6660 O  O    . HOH   F 5 .   ? 8.121  -3.096  -5.699  1.00 40.22 ?  511 HOH   A O    1 
HETATM 6661 O  O    B HOH   F 5 .   ? 14.963 8.396   4.777   0.26 28.66 ?  512 HOH   A O    1 
HETATM 6662 O  O    B HOH   F 5 .   ? 10.014 1.319   -4.654  0.26 19.43 ?  513 HOH   A O    1 
HETATM 6663 O  O    . HOH   F 5 .   ? 36.491 -6.563  10.113  1.00 43.33 ?  514 HOH   A O    1 
HETATM 6664 O  O    . HOH   F 5 .   ? 22.046 -24.116 4.471   1.00 28.70 ?  515 HOH   A O    1 
HETATM 6665 O  O    A HOH   F 5 .   ? 14.912 8.628   4.907   0.74 42.87 ?  516 HOH   A O    1 
HETATM 6666 O  O    . HOH   F 5 .   ? 17.388 -6.613  -14.154 1.00 38.83 ?  517 HOH   A O    1 
HETATM 6667 O  O    B HOH   F 5 .   ? 9.091  2.286   -2.488  0.26 21.39 ?  518 HOH   A O    1 
HETATM 6668 O  O    . HOH   F 5 .   ? 24.124 9.036   -7.247  1.00 35.89 ?  519 HOH   A O    1 
HETATM 6669 O  O    . HOH   F 5 .   ? 16.495 -21.158 18.769  1.00 34.24 ?  520 HOH   A O    1 
HETATM 6670 O  O    . HOH   F 5 .   ? 16.007 -12.250 27.526  1.00 44.27 ?  521 HOH   A O    1 
HETATM 6671 O  O    . HOH   F 5 .   ? 14.677 -22.836 19.891  1.00 36.67 ?  522 HOH   A O    1 
HETATM 6672 O  O    . HOH   G 5 .   ? 29.876 -22.463 5.477   1.00 23.74 ?  201 HOH   B O    1 
HETATM 6673 O  O    . HOH   G 5 .   ? 49.437 -22.660 -19.751 1.00 49.46 ?  202 HOH   B O    1 
HETATM 6674 O  O    . HOH   G 5 .   ? 48.243 -6.925  15.614  1.00 34.53 ?  203 HOH   B O    1 
HETATM 6675 O  O    . HOH   G 5 .   ? 37.976 -39.543 -0.231  1.00 42.71 ?  204 HOH   B O    1 
HETATM 6676 O  O    . HOH   G 5 .   ? 59.345 -18.778 6.815   1.00 40.54 ?  205 HOH   B O    1 
HETATM 6677 O  O    . HOH   G 5 .   ? 47.493 -7.488  -4.006  1.00 40.80 ?  206 HOH   B O    1 
HETATM 6678 O  O    . HOH   G 5 .   ? 54.576 -9.398  -8.779  1.00 22.41 ?  207 HOH   B O    1 
HETATM 6679 O  O    . HOH   G 5 .   ? 56.434 -19.733 7.308   1.00 36.02 ?  208 HOH   B O    1 
HETATM 6680 O  O    . HOH   G 5 .   ? 41.450 -7.750  5.516   1.00 39.83 ?  209 HOH   B O    1 
HETATM 6681 O  O    . HOH   G 5 .   ? 41.971 -35.951 -17.443 1.00 28.71 ?  210 HOH   B O    1 
HETATM 6682 O  O    . HOH   G 5 .   ? 57.835 -24.559 5.043   1.00 37.86 ?  211 HOH   B O    1 
HETATM 6683 O  O    . HOH   G 5 .   ? 57.268 -26.951 -7.621  1.00 42.97 ?  212 HOH   B O    1 
HETATM 6684 O  O    . HOH   G 5 .   ? 29.940 -26.350 3.988   1.00 29.32 ?  213 HOH   B O    1 
HETATM 6685 O  O    . HOH   G 5 .   ? 50.402 -3.273  7.229   1.00 37.57 ?  214 HOH   B O    1 
HETATM 6686 O  O    . HOH   G 5 .   ? 55.502 -16.553 -14.357 1.00 37.73 ?  215 HOH   B O    1 
HETATM 6687 O  O    . HOH   G 5 .   ? 56.784 -30.794 -7.785  1.00 34.08 ?  216 HOH   B O    1 
HETATM 6688 O  O    . HOH   G 5 .   ? 30.296 -41.082 -8.166  1.00 17.70 ?  217 HOH   B O    1 
HETATM 6689 O  O    . HOH   G 5 .   ? 50.847 -6.137  0.188   1.00 29.68 ?  218 HOH   B O    1 
HETATM 6690 O  O    . HOH   G 5 .   ? 29.854 -34.318 -0.440  1.00 35.65 ?  219 HOH   B O    1 
HETATM 6691 O  O    . HOH   G 5 .   ? 27.861 -41.949 -15.193 1.00 35.52 ?  220 HOH   B O    1 
HETATM 6692 O  O    . HOH   G 5 .   ? 37.196 -19.833 -18.109 1.00 39.28 ?  221 HOH   B O    1 
HETATM 6693 O  O    . HOH   G 5 .   ? 48.721 -36.495 -15.487 1.00 42.60 ?  222 HOH   B O    1 
HETATM 6694 O  O    . HOH   G 5 .   ? 27.824 -29.266 -1.814  1.00 37.27 ?  223 HOH   B O    1 
HETATM 6695 O  O    . HOH   G 5 .   ? 58.369 -12.896 8.418   1.00 37.75 ?  224 HOH   B O    1 
HETATM 6696 O  O    . HOH   G 5 .   ? 45.223 -35.004 6.838   1.00 43.00 ?  225 HOH   B O    1 
HETATM 6697 O  O    . HOH   G 5 .   ? 44.532 -7.299  2.140   1.00 34.15 ?  226 HOH   B O    1 
HETATM 6698 O  O    . HOH   G 5 .   ? 57.471 -16.258 -12.222 1.00 21.95 ?  227 HOH   B O    1 
HETATM 6699 O  O    . HOH   G 5 .   ? 41.592 -39.221 -14.936 1.00 22.88 ?  228 HOH   B O    1 
HETATM 6700 O  O    . HOH   G 5 .   ? 36.039 -43.378 -8.576  1.00 33.56 ?  229 HOH   B O    1 
HETATM 6701 O  O    . HOH   G 5 .   ? 34.656 -36.469 -7.194  1.00 18.93 ?  230 HOH   B O    1 
HETATM 6702 O  O    . HOH   G 5 .   ? 53.058 -13.501 -20.362 1.00 38.43 ?  231 HOH   B O    1 
HETATM 6703 O  O    . HOH   G 5 .   ? 40.697 -16.082 14.151  1.00 28.06 ?  232 HOH   B O    1 
HETATM 6704 O  O    . HOH   G 5 .   ? 30.890 -28.864 4.229   1.00 26.68 ?  233 HOH   B O    1 
HETATM 6705 O  O    . HOH   G 5 .   ? 46.407 -1.609  13.296  1.00 29.59 ?  234 HOH   B O    1 
HETATM 6706 O  O    . HOH   G 5 .   ? 50.809 -12.995 -0.476  1.00 13.41 ?  235 HOH   B O    1 
HETATM 6707 O  O    . HOH   G 5 .   ? 43.200 -43.314 -8.268  1.00 30.36 ?  236 HOH   B O    1 
HETATM 6708 O  O    . HOH   G 5 .   ? 42.634 -25.419 2.602   1.00 16.36 ?  237 HOH   B O    1 
HETATM 6709 O  O    . HOH   G 5 .   ? 28.471 -19.746 -13.176 1.00 26.59 ?  238 HOH   B O    1 
HETATM 6710 O  O    . HOH   G 5 .   ? 41.449 -9.674  13.085  1.00 25.05 ?  239 HOH   B O    1 
HETATM 6711 O  O    . HOH   G 5 .   ? 35.195 -8.014  -3.027  1.00 20.18 ?  240 HOH   B O    1 
HETATM 6712 O  O    . HOH   G 5 .   ? 45.116 -43.593 -10.546 1.00 29.70 ?  241 HOH   B O    1 
HETATM 6713 O  O    . HOH   G 5 .   ? 48.256 -24.549 -17.758 1.00 29.82 ?  242 HOH   B O    1 
HETATM 6714 O  O    . HOH   G 5 .   ? 44.583 -27.800 -0.728  1.00 24.67 ?  243 HOH   B O    1 
HETATM 6715 O  O    . HOH   G 5 .   ? 39.342 -10.910 6.157   1.00 27.10 ?  244 HOH   B O    1 
HETATM 6716 O  O    . HOH   G 5 .   ? 34.291 -18.595 11.406  1.00 24.87 ?  245 HOH   B O    1 
HETATM 6717 O  O    . HOH   G 5 .   ? 51.792 -6.543  4.424   1.00 22.79 ?  246 HOH   B O    1 
HETATM 6718 O  O    . HOH   G 5 .   ? 57.706 -24.416 -3.830  1.00 23.39 ?  247 HOH   B O    1 
HETATM 6719 O  O    . HOH   G 5 .   ? 32.884 -43.875 -11.344 1.00 22.29 ?  248 HOH   B O    1 
HETATM 6720 O  O    . HOH   G 5 .   ? 51.669 -13.961 11.009  1.00 30.46 ?  249 HOH   B O    1 
HETATM 6721 O  O    . HOH   G 5 .   ? 40.405 -12.796 -11.546 1.00 16.67 ?  250 HOH   B O    1 
HETATM 6722 O  O    . HOH   G 5 .   ? 51.061 -40.032 -8.225  1.00 33.76 ?  251 HOH   B O    1 
HETATM 6723 O  O    . HOH   G 5 .   ? 30.896 -15.769 2.658   1.00 14.88 ?  252 HOH   B O    1 
HETATM 6724 O  O    . HOH   G 5 .   ? 25.455 -26.030 -1.327  1.00 32.89 ?  253 HOH   B O    1 
HETATM 6725 O  O    . HOH   G 5 .   ? 42.716 -22.934 3.852   1.00 13.19 ?  254 HOH   B O    1 
HETATM 6726 O  O    . HOH   G 5 .   ? 43.294 -32.446 -17.076 1.00 23.84 ?  255 HOH   B O    1 
HETATM 6727 O  O    . HOH   G 5 .   ? 29.811 -25.275 -10.868 1.00 17.57 ?  256 HOH   B O    1 
HETATM 6728 O  O    . HOH   G 5 .   ? 43.412 -15.846 -12.178 1.00 15.78 ?  257 HOH   B O    1 
HETATM 6729 O  O    . HOH   G 5 .   ? 48.045 -22.824 5.827   1.00 18.90 ?  258 HOH   B O    1 
HETATM 6730 O  O    . HOH   G 5 .   ? 39.559 -11.136 0.317   1.00 18.91 ?  259 HOH   B O    1 
HETATM 6731 O  O    . HOH   G 5 .   ? 41.941 -23.582 9.306   1.00 19.43 ?  260 HOH   B O    1 
HETATM 6732 O  O    . HOH   G 5 .   ? 27.200 -31.911 -10.032 1.00 23.33 ?  261 HOH   B O    1 
HETATM 6733 O  O    . HOH   G 5 .   ? 30.670 -42.333 -10.661 1.00 29.09 ?  262 HOH   B O    1 
HETATM 6734 O  O    . HOH   G 5 .   ? 49.442 -28.768 -6.910  1.00 16.63 ?  263 HOH   B O    1 
HETATM 6735 O  O    . HOH   G 5 .   ? 28.343 -34.474 -9.482  1.00 22.47 ?  264 HOH   B O    1 
HETATM 6736 O  O    . HOH   G 5 .   ? 34.525 -12.850 2.589   1.00 24.84 ?  265 HOH   B O    1 
HETATM 6737 O  O    . HOH   G 5 .   ? 49.778 -0.532  10.320  1.00 32.48 ?  266 HOH   B O    1 
HETATM 6738 O  O    . HOH   G 5 .   ? 58.275 -10.622 -4.098  1.00 22.28 ?  267 HOH   B O    1 
HETATM 6739 O  O    . HOH   G 5 .   ? 42.463 -34.781 3.727   1.00 27.60 ?  268 HOH   B O    1 
HETATM 6740 O  O    . HOH   G 5 .   ? 38.465 -11.162 -2.210  1.00 20.49 ?  269 HOH   B O    1 
HETATM 6741 O  O    . HOH   G 5 .   ? 38.954 -12.055 12.365  1.00 34.00 ?  270 HOH   B O    1 
HETATM 6742 O  O    . HOH   G 5 .   ? 46.722 -31.308 -4.796  1.00 21.56 ?  271 HOH   B O    1 
HETATM 6743 O  O    . HOH   G 5 .   ? 34.932 -24.687 13.897  1.00 28.27 ?  272 HOH   B O    1 
HETATM 6744 O  O    . HOH   G 5 .   ? 57.591 -9.236  1.441   1.00 21.64 ?  273 HOH   B O    1 
HETATM 6745 O  O    . HOH   G 5 .   ? 31.873 -17.989 -14.578 1.00 32.08 ?  274 HOH   B O    1 
HETATM 6746 O  O    . HOH   G 5 .   ? 42.404 -9.936  9.395   1.00 22.99 ?  275 HOH   B O    1 
HETATM 6747 O  O    . HOH   G 5 .   ? 57.041 -8.658  8.436   1.00 22.13 ?  276 HOH   B O    1 
HETATM 6748 O  O    . HOH   G 5 .   ? 37.466 -35.714 7.161   1.00 37.47 ?  277 HOH   B O    1 
HETATM 6749 O  O    . HOH   G 5 .   ? 56.306 -23.525 -14.714 1.00 27.58 ?  278 HOH   B O    1 
HETATM 6750 O  O    . HOH   G 5 .   ? 27.662 -26.822 -15.726 1.00 33.91 ?  279 HOH   B O    1 
HETATM 6751 O  O    . HOH   G 5 .   ? 28.543 -30.955 -14.829 1.00 33.23 ?  280 HOH   B O    1 
HETATM 6752 O  O    . HOH   G 5 .   ? 28.012 -22.938 -8.050  1.00 18.39 ?  281 HOH   B O    1 
HETATM 6753 O  O    . HOH   G 5 .   ? 52.660 -10.466 12.995  1.00 25.36 ?  282 HOH   B O    1 
HETATM 6754 O  O    . HOH   G 5 .   ? 57.239 -12.101 12.368  1.00 39.19 ?  283 HOH   B O    1 
HETATM 6755 O  O    . HOH   G 5 .   ? 35.053 -33.478 -19.223 1.00 31.25 ?  284 HOH   B O    1 
HETATM 6756 O  O    . HOH   G 5 .   ? 46.951 -29.657 9.883   1.00 32.59 ?  285 HOH   B O    1 
HETATM 6757 O  O    . HOH   G 5 .   ? 48.805 -20.094 5.932   1.00 15.13 ?  286 HOH   B O    1 
HETATM 6758 O  O    . HOH   G 5 .   ? 48.520 -25.091 3.098   1.00 14.74 ?  287 HOH   B O    1 
HETATM 6759 O  O    . HOH   G 5 .   ? 42.951 -20.387 -20.826 1.00 37.17 ?  288 HOH   B O    1 
HETATM 6760 O  O    . HOH   G 5 .   ? 50.085 -24.678 5.787   1.00 38.04 ?  289 HOH   B O    1 
HETATM 6761 O  O    . HOH   G 5 .   ? 41.178 -24.449 15.826  1.00 48.02 ?  290 HOH   B O    1 
HETATM 6762 O  O    . HOH   G 5 .   ? 41.197 -5.521  11.543  1.00 44.12 ?  291 HOH   B O    1 
HETATM 6763 O  O    . HOH   G 5 .   ? 47.183 -34.048 -4.626  1.00 18.70 ?  292 HOH   B O    1 
HETATM 6764 O  O    . HOH   G 5 .   ? 36.844 -12.803 -1.507  1.00 29.75 ?  293 HOH   B O    1 
HETATM 6765 O  O    . HOH   G 5 .   ? 59.895 -15.412 8.195   1.00 33.94 ?  294 HOH   B O    1 
HETATM 6766 O  O    . HOH   G 5 .   ? 45.510 -33.510 -15.930 1.00 25.69 ?  295 HOH   B O    1 
HETATM 6767 O  O    . HOH   G 5 .   ? 42.347 -9.997  -14.932 1.00 36.13 ?  296 HOH   B O    1 
HETATM 6768 O  O    . HOH   G 5 .   ? 51.360 -37.678 -9.562  1.00 28.31 ?  297 HOH   B O    1 
HETATM 6769 O  O    . HOH   G 5 .   ? 33.557 -15.387 -13.985 1.00 23.59 ?  298 HOH   B O    1 
HETATM 6770 O  O    . HOH   G 5 .   ? 44.126 -29.360 -4.708  1.00 26.11 ?  299 HOH   B O    1 
HETATM 6771 O  O    . HOH   G 5 .   ? 62.900 -20.158 -0.812  1.00 42.82 ?  300 HOH   B O    1 
HETATM 6772 O  O    . HOH   G 5 .   ? 46.038 -40.546 -3.630  1.00 30.88 ?  301 HOH   B O    1 
HETATM 6773 O  O    . HOH   G 5 .   ? 26.005 -21.534 -3.505  1.00 17.44 ?  302 HOH   B O    1 
HETATM 6774 O  O    . HOH   G 5 .   ? 57.777 -22.162 3.076   1.00 30.43 ?  303 HOH   B O    1 
HETATM 6775 O  O    . HOH   G 5 .   ? 44.734 -27.516 1.972   1.00 17.15 ?  304 HOH   B O    1 
HETATM 6776 O  O    . HOH   G 5 .   ? 42.754 -12.322 -18.551 1.00 31.00 ?  305 HOH   B O    1 
HETATM 6777 O  O    . HOH   G 5 .   ? 37.597 -18.295 13.126  1.00 28.68 ?  306 HOH   B O    1 
HETATM 6778 O  O    . HOH   G 5 .   ? 51.484 -32.940 -10.688 1.00 36.75 ?  307 HOH   B O    1 
HETATM 6779 O  O    . HOH   G 5 .   ? 40.302 -10.857 -9.566  1.00 17.96 ?  308 HOH   B O    1 
HETATM 6780 O  O    . HOH   G 5 .   ? 32.896 -34.657 -5.931  1.00 18.46 ?  309 HOH   B O    1 
HETATM 6781 O  O    . HOH   G 5 .   ? 52.706 -29.309 -13.006 1.00 25.28 ?  310 HOH   B O    1 
HETATM 6782 O  O    . HOH   G 5 .   ? 35.105 -33.578 4.476   1.00 31.02 ?  311 HOH   B O    1 
HETATM 6783 O  O    . HOH   G 5 .   ? 53.178 -16.053 -12.752 1.00 31.26 ?  312 HOH   B O    1 
HETATM 6784 O  O    . HOH   G 5 .   ? 48.228 -32.678 -16.597 1.00 45.85 ?  313 HOH   B O    1 
HETATM 6785 O  O    . HOH   G 5 .   ? 52.748 -35.702 -8.599  1.00 31.84 ?  314 HOH   B O    1 
HETATM 6786 O  O    . HOH   G 5 .   ? 43.578 -15.415 18.263  1.00 32.92 ?  315 HOH   B O    1 
HETATM 6787 O  O    . HOH   G 5 .   ? 62.764 -13.570 4.764   1.00 30.90 ?  316 HOH   B O    1 
HETATM 6788 O  O    . HOH   G 5 .   ? 37.887 -10.265 -10.764 1.00 19.03 ?  317 HOH   B O    1 
HETATM 6789 O  O    . HOH   G 5 .   ? 60.059 -17.183 -10.460 1.00 35.12 ?  318 HOH   B O    1 
HETATM 6790 O  O    . HOH   G 5 .   ? 44.653 -24.679 9.587   1.00 21.11 ?  319 HOH   B O    1 
HETATM 6791 O  O    . HOH   G 5 .   ? 53.559 -30.275 4.552   1.00 20.54 ?  320 HOH   B O    1 
HETATM 6792 O  O    . HOH   G 5 .   ? 26.372 -21.057 -6.260  1.00 17.77 ?  321 HOH   B O    1 
HETATM 6793 O  O    . HOH   G 5 .   ? 51.815 -5.923  -7.896  1.00 48.68 ?  322 HOH   B O    1 
HETATM 6794 O  O    . HOH   G 5 .   ? 38.444 -9.433  -13.314 1.00 27.11 ?  323 HOH   B O    1 
HETATM 6795 O  O    . HOH   G 5 .   ? 37.233 -30.666 -21.084 1.00 33.35 ?  324 HOH   B O    1 
HETATM 6796 O  O    . HOH   G 5 .   ? 43.244 -21.507 10.670  1.00 17.30 ?  325 HOH   B O    1 
HETATM 6797 O  O    . HOH   G 5 .   ? 27.873 -14.803 -9.430  1.00 36.76 ?  326 HOH   B O    1 
HETATM 6798 O  O    . HOH   G 5 .   ? 41.698 -8.121  1.315   1.00 27.39 ?  327 HOH   B O    1 
HETATM 6799 O  O    . HOH   G 5 .   ? 36.774 -12.481 4.299   1.00 20.06 ?  328 HOH   B O    1 
HETATM 6800 O  O    . HOH   G 5 .   ? 39.500 -23.526 -20.302 1.00 36.72 ?  329 HOH   B O    1 
HETATM 6801 O  O    . HOH   G 5 .   ? 38.408 -12.766 7.931   1.00 20.42 ?  330 HOH   B O    1 
HETATM 6802 O  O    . HOH   G 5 .   ? 47.265 -24.533 8.181   1.00 27.84 ?  331 HOH   B O    1 
HETATM 6803 O  O    . HOH   G 5 .   ? 44.237 -1.774  7.543   1.00 46.26 ?  332 HOH   B O    1 
HETATM 6804 O  O    . HOH   G 5 .   ? 53.716 -12.604 -22.298 1.00 36.18 ?  333 HOH   B O    1 
HETATM 6805 O  O    . HOH   G 5 .   ? 33.587 -31.245 11.051  1.00 37.37 ?  334 HOH   B O    1 
HETATM 6806 O  O    . HOH   G 5 .   ? 48.719 -11.957 -13.866 1.00 28.66 ?  335 HOH   B O    1 
HETATM 6807 O  O    . HOH   G 5 .   ? 43.233 -34.711 0.040   1.00 22.12 ?  336 HOH   B O    1 
HETATM 6808 O  O    . HOH   G 5 .   ? 43.018 -43.569 -14.390 1.00 45.16 ?  337 HOH   B O    1 
HETATM 6809 O  O    . HOH   G 5 .   ? 47.584 -27.489 1.985   1.00 16.69 ?  338 HOH   B O    1 
HETATM 6810 O  O    . HOH   G 5 .   ? 46.942 -19.901 12.262  1.00 32.13 ?  339 HOH   B O    1 
HETATM 6811 O  O    . HOH   G 5 .   ? 45.882 -36.354 -16.138 1.00 34.79 ?  340 HOH   B O    1 
HETATM 6812 O  O    . HOH   G 5 .   ? 37.106 -15.136 -16.510 1.00 39.17 ?  341 HOH   B O    1 
HETATM 6813 O  O    . HOH   G 5 .   ? 37.205 -45.347 -9.893  1.00 38.80 ?  342 HOH   B O    1 
HETATM 6814 O  O    . HOH   G 5 .   ? 28.944 -43.024 -12.349 1.00 36.51 ?  343 HOH   B O    1 
HETATM 6815 O  O    . HOH   G 5 .   ? 33.035 -14.734 1.012   1.00 20.43 ?  344 HOH   B O    1 
HETATM 6816 O  O    . HOH   G 5 .   ? 39.895 -44.350 -11.237 1.00 39.81 ?  345 HOH   B O    1 
HETATM 6817 O  O    . HOH   G 5 .   ? 38.491 -12.344 -16.327 1.00 39.11 ?  346 HOH   B O    1 
HETATM 6818 O  O    . HOH   G 5 .   ? 38.650 -22.287 15.053  1.00 41.52 ?  347 HOH   B O    1 
HETATM 6819 O  O    . HOH   G 5 .   ? 27.806 -26.678 -0.659  1.00 33.03 ?  348 HOH   B O    1 
HETATM 6820 O  O    . HOH   G 5 .   ? 55.663 -8.269  10.859  1.00 24.96 ?  349 HOH   B O    1 
HETATM 6821 O  O    . HOH   G 5 .   ? 62.629 -20.240 -4.842  1.00 46.14 ?  350 HOH   B O    1 
HETATM 6822 O  O    . HOH   G 5 .   ? 33.819 -9.325  -8.821  1.00 33.60 ?  351 HOH   B O    1 
HETATM 6823 O  O    . HOH   G 5 .   ? 40.514 -43.595 -9.109  1.00 30.59 ?  352 HOH   B O    1 
HETATM 6824 O  O    . HOH   G 5 .   ? 44.244 -37.447 -17.743 1.00 35.89 ?  353 HOH   B O    1 
HETATM 6825 O  O    . HOH   G 5 .   ? 23.258 -23.748 6.794   1.00 33.94 ?  354 HOH   B O    1 
HETATM 6826 O  O    . HOH   G 5 .   ? 56.698 -7.328  3.176   1.00 28.91 ?  355 HOH   B O    1 
HETATM 6827 O  O    . HOH   G 5 .   ? 36.171 -8.522  -9.754  1.00 36.57 ?  356 HOH   B O    1 
HETATM 6828 O  O    . HOH   G 5 .   ? 43.267 -12.703 -21.187 1.00 41.66 ?  357 HOH   B O    1 
HETATM 6829 O  O    . HOH   G 5 .   ? 61.617 -19.946 1.621   1.00 36.22 ?  358 HOH   B O    1 
HETATM 6830 O  O    . HOH   G 5 .   ? 34.798 -10.339 7.401   1.00 27.47 ?  359 HOH   B O    1 
HETATM 6831 O  O    . HOH   G 5 .   ? 34.259 -7.750  11.391  1.00 42.74 ?  360 HOH   B O    1 
HETATM 6832 O  O    . HOH   G 5 .   ? 40.276 -8.859  9.935   1.00 39.74 ?  361 HOH   B O    1 
HETATM 6833 O  O    . HOH   G 5 .   ? 27.218 -26.034 -11.510 1.00 35.56 ?  362 HOH   B O    1 
HETATM 6834 O  O    . HOH   G 5 .   ? 57.099 -21.612 -16.436 1.00 43.50 ?  363 HOH   B O    1 
HETATM 6835 O  O    . HOH   G 5 .   ? 32.513 -23.712 14.095  1.00 41.20 ?  364 HOH   B O    1 
HETATM 6836 O  O    . HOH   G 5 .   ? 48.429 -26.614 8.843   1.00 42.27 ?  365 HOH   B O    1 
HETATM 6837 O  O    . HOH   G 5 .   ? 54.351 -5.803  2.992   1.00 39.47 ?  366 HOH   B O    1 
HETATM 6838 O  O    . HOH   G 5 .   ? 36.227 -8.789  8.988   1.00 38.44 ?  367 HOH   B O    1 
HETATM 6839 O  O    . HOH   G 5 .   ? 41.857 -10.068 -17.421 1.00 57.81 ?  368 HOH   B O    1 
HETATM 6840 O  O    . HOH   G 5 .   ? 40.105 -11.374 -13.953 1.00 32.06 ?  369 HOH   B O    1 
HETATM 6841 O  O    . HOH   G 5 .   ? 59.126 -10.404 9.195   1.00 38.60 ?  370 HOH   B O    1 
HETATM 6842 O  O    . HOH   G 5 .   ? 39.908 -6.994  7.863   1.00 42.13 ?  371 HOH   B O    1 
HETATM 6843 O  O    . HOH   G 5 .   ? 38.138 -10.615 10.107  1.00 30.89 ?  372 HOH   B O    1 
HETATM 6844 O  O    . HOH   G 5 .   ? 56.140 -7.741  -0.578  1.00 36.33 ?  373 HOH   B O    1 
HETATM 6845 O  O    . HOH   G 5 .   ? 52.098 -12.941 13.395  1.00 34.32 ?  374 HOH   B O    1 
HETATM 6846 O  O    . HOH   G 5 .   ? 63.219 -12.444 6.936   1.00 41.08 ?  375 HOH   B O    1 
HETATM 6847 O  O    . HOH   G 5 .   ? 41.875 -6.749  -4.863  1.00 50.42 ?  376 HOH   B O    1 
HETATM 6848 O  O    . HOH   G 5 .   ? 44.116 -5.611  -3.558  1.00 43.09 ?  377 HOH   B O    1 
HETATM 6849 O  O    . HOH   G 5 .   ? 36.552 -22.841 13.284  1.00 26.39 ?  378 HOH   B O    1 
HETATM 6850 O  O    . HOH   G 5 .   ? 42.713 -17.097 -23.262 1.00 46.31 ?  379 HOH   B O    1 
HETATM 6851 O  O    . HOH   G 5 .   ? 40.176 -7.627  3.271   1.00 34.07 ?  380 HOH   B O    1 
HETATM 6852 O  O    . HOH   G 5 .   ? 52.927 -29.929 7.208   1.00 26.48 ?  381 HOH   B O    1 
HETATM 6853 O  O    . HOH   G 5 .   ? 60.613 -22.267 2.773   1.00 44.18 ?  382 HOH   B O    1 
HETATM 6854 O  O    . HOH   G 5 .   ? 39.817 -14.072 15.748  1.00 49.84 ?  383 HOH   B O    1 
HETATM 6855 O  O    . HOH   G 5 .   ? 35.446 -33.768 7.258   1.00 42.58 ?  384 HOH   B O    1 
HETATM 6856 O  O    . HOH   G 5 .   ? 23.967 -20.890 -7.698  1.00 29.43 ?  385 HOH   B O    1 
HETATM 6857 O  O    . HOH   G 5 .   ? 25.885 -18.945 -11.956 1.00 38.84 ?  386 HOH   B O    1 
HETATM 6858 O  O    . HOH   G 5 .   ? 46.891 -5.404  2.949   1.00 43.70 ?  387 HOH   B O    1 
HETATM 6859 O  O    . HOH   G 5 .   ? 40.998 -9.837  15.820  1.00 47.99 ?  388 HOH   B O    1 
HETATM 6860 O  O    . HOH   G 5 .   ? 35.432 -20.378 13.381  1.00 30.40 ?  389 HOH   B O    1 
HETATM 6861 O  O    . HOH   G 5 .   ? 40.812 -6.608  -0.872  1.00 27.11 ?  390 HOH   B O    1 
HETATM 6862 O  O    . HOH   G 5 .   ? 44.204 -31.831 -3.863  1.00 34.89 ?  391 HOH   B O    1 
HETATM 6863 O  O    . HOH   G 5 .   ? 26.721 -28.062 -13.628 1.00 37.75 ?  392 HOH   B O    1 
HETATM 6864 O  O    . HOH   G 5 .   ? 27.909 -27.155 2.123   1.00 34.69 ?  393 HOH   B O    1 
HETATM 6865 O  O    . HOH   G 5 .   ? 50.698 -30.821 8.663   1.00 29.59 ?  394 HOH   B O    1 
HETATM 6866 O  O    . HOH   G 5 .   ? 24.661 -20.761 -10.461 1.00 36.86 ?  395 HOH   B O    1 
HETATM 6867 O  O    . HOH   G 5 .   ? 34.461 -33.548 9.605   1.00 35.59 ?  396 HOH   B O    1 
HETATM 6868 O  O    . HOH   G 5 .   ? 26.856 -30.712 -12.667 1.00 31.43 ?  397 HOH   B O    1 
HETATM 6869 O  O    . HOH   G 5 .   ? 45.871 -20.303 15.176  1.00 54.95 ?  398 HOH   B O    1 
HETATM 6870 O  O    . HOH   G 5 .   ? 57.658 -6.400  -2.343  1.00 35.99 ?  399 HOH   B O    1 
HETATM 6871 O  O    . HOH   G 5 .   ? 40.980 -11.802 -22.373 1.00 45.82 ?  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   ? 0.6257 0.6315 0.6890 -0.0020 -0.0228 0.0937  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.6246 0.6311 0.6630 -0.0107 -0.0171 0.0649  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.6228 0.6282 0.6796 -0.0042 -0.0214 0.0926  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.6215 0.6286 0.6571 -0.0120 -0.0172 0.0667  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.6068 0.6169 0.6465 -0.0137 -0.0249 0.0967  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.6072 0.6182 0.6353 -0.0180 -0.0214 0.0795  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.6074 0.6172 0.6511 -0.0094 -0.0261 0.1026  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.6096 0.6201 0.6415 -0.0156 -0.0214 0.0794  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.6336 0.6341 0.6950 0.0010  -0.0164 0.0905  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.6301 0.6342 0.6671 -0.0082 -0.0137 0.0583  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.6371 0.6359 0.6980 0.0026  -0.0142 0.0905  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.6331 0.6362 0.6708 -0.0071 -0.0123 0.0555  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.6372 0.6355 0.7015 0.0036  -0.0144 0.0920  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.6329 0.6358 0.6716 -0.0065 -0.0126 0.0563  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.5874 0.6043 0.5940 -0.0267 -0.0258 0.0939  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.5481 0.5742 0.4934 -0.0498 -0.0263 0.1014  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.5090 0.5501 0.4290 -0.0633 -0.0141 0.0785  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.5059 0.5468 0.3968 -0.0693 -0.0191 0.0896  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.5452 0.5694 0.4537 -0.0586 -0.0363 0.1273  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.5434 0.5630 0.4134 -0.0661 -0.0499 0.1548  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.5464 0.5568 0.3883 -0.0708 -0.0547 0.1680  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.5390 0.5602 0.4069 -0.0679 -0.0570 0.1681  4   ASN   A ND2 
46   N  N   . SER   A 5   ? 0.4705 0.5239 0.3854 -0.0738 -0.0005 0.0478  5   SER   A N   
47   C  CA  . SER   A 5   ? 0.4321 0.5031 0.3569 -0.0817 0.0153  0.0139  5   SER   A CA  
48   C  C   . SER   A 5   ? 0.3900 0.4683 0.3104 -0.0797 0.0265  -0.0131 5   SER   A C   
49   O  O   . SER   A 5   ? 0.3982 0.4797 0.3125 -0.0657 0.0353  -0.0326 5   SER   A O   
50   C  CB  . SER   A 5   ? 0.4414 0.5171 0.3767 -0.0889 0.0152  0.0061  5   SER   A CB  
51   O  OG  . SER   A 5   ? 0.4476 0.5247 0.3860 -0.0946 0.0186  0.0027  5   SER   A OG  
57   N  N   . PHE   A 6   ? 0.3337 0.4201 0.2617 -0.0905 0.0344  -0.0113 6   PHE   A N   
58   C  CA  . PHE   A 6   ? 0.2810 0.3706 0.2149 -0.0929 0.0365  0.0144  6   PHE   A CA  
59   C  C   . PHE   A 6   ? 0.2682 0.3782 0.2567 -0.1040 0.0556  0.0187  6   PHE   A C   
60   O  O   . PHE   A 6   ? 0.2659 0.3917 0.2944 -0.1108 0.0309  0.0288  6   PHE   A O   
61   C  CB  . PHE   A 6   ? 0.2726 0.3277 0.1805 -0.0659 0.0378  0.0264  6   PHE   A CB  
62   C  CG  . PHE   A 6   ? 0.2624 0.2943 0.1799 -0.0598 0.0237  0.0252  6   PHE   A CG  
63   C  CD1 . PHE   A 6   ? 0.2557 0.2808 0.1979 -0.0401 0.0236  0.0370  6   PHE   A CD1 
64   C  CD2 . PHE   A 6   ? 0.2669 0.2898 0.2125 -0.0489 0.0213  0.0291  6   PHE   A CD2 
65   C  CE1 . PHE   A 6   ? 0.2510 0.2784 0.2265 -0.0378 0.0264  0.0437  6   PHE   A CE1 
66   C  CE2 . PHE   A 6   ? 0.2621 0.2830 0.2473 -0.0475 0.0236  0.0363  6   PHE   A CE2 
67   C  CZ  . PHE   A 6   ? 0.2557 0.2844 0.2336 -0.0409 0.0243  0.0412  6   PHE   A CZ  
77   N  N   . SER   A 7   ? 0.2561 0.3650 0.2570 -0.1020 0.0757  0.0040  7   SER   A N   
78   C  CA  . SER   A 7   ? 0.2784 0.3719 0.2765 -0.0816 0.0743  -0.0113 7   SER   A CA  
79   C  C   . SER   A 7   ? 0.2630 0.3273 0.2590 -0.0829 0.0814  -0.0046 7   SER   A C   
80   O  O   . SER   A 7   ? 0.2749 0.3229 0.2584 -0.0834 0.0795  -0.0116 7   SER   A O   
81   C  CB  . SER   A 7   ? 0.3111 0.4206 0.3170 -0.0641 0.0783  -0.0122 7   SER   A CB  
82   O  OG  . SER   A 7   ? 0.3402 0.4529 0.3646 -0.0508 0.0670  -0.0259 7   SER   A OG  
88   N  N   . GLY   A 8   ? 0.2471 0.3022 0.2568 -0.0668 0.0767  -0.0172 8   GLY   A N   
89   C  CA  . GLY   A 8   ? 0.2422 0.2747 0.2770 -0.0401 0.0774  -0.0120 8   GLY   A CA  
90   C  C   . GLY   A 8   ? 0.2175 0.2413 0.2550 -0.0304 0.0594  -0.0086 8   GLY   A C   
91   O  O   . GLY   A 8   ? 0.2070 0.2399 0.2781 -0.0090 0.0371  -0.0293 8   GLY   A O   
95   N  N   A TYR   A 9   ? 0.1994 0.2234 0.2432 -0.0259 0.0549  0.0187  9   TYR   A N   
96   N  N   B TYR   A 9   ? 0.2140 0.2331 0.2375 -0.0267 0.0503  0.0019  9   TYR   A N   
97   C  CA  A TYR   A 9   ? 0.1957 0.2065 0.2300 -0.0135 0.0511  0.0380  9   TYR   A CA  
98   C  CA  B TYR   A 9   ? 0.2136 0.2245 0.2187 -0.0216 0.0431  0.0081  9   TYR   A CA  
99   C  C   A TYR   A 9   ? 0.1896 0.1945 0.2297 -0.0097 0.0378  0.0617  9   TYR   A C   
100  C  C   B TYR   A 9   ? 0.2132 0.2181 0.2093 -0.0175 0.0369  0.0137  9   TYR   A C   
101  O  O   A TYR   A 9   ? 0.2101 0.2199 0.2543 -0.0114 0.0382  0.0654  9   TYR   A O   
102  O  O   B TYR   A 9   ? 0.2183 0.2266 0.2114 -0.0199 0.0377  0.0091  9   TYR   A O   
103  C  CB  A TYR   A 9   ? 0.1850 0.2307 0.2338 -0.0014 0.0498  0.0254  9   TYR   A CB  
104  C  CB  B TYR   A 9   ? 0.2099 0.2315 0.2158 -0.0183 0.0392  0.0061  9   TYR   A CB  
105  C  CG  A TYR   A 9   ? 0.1777 0.2438 0.2282 0.0001  0.0555  0.0098  9   TYR   A CG  
106  C  CG  B TYR   A 9   ? 0.2072 0.2352 0.2124 -0.0188 0.0372  0.0004  9   TYR   A CG  
107  C  CD1 A TYR   A 9   ? 0.1839 0.2544 0.2421 -0.0140 0.0616  -0.0015 9   TYR   A CD1 
108  C  CD1 B TYR   A 9   ? 0.2115 0.2393 0.2193 -0.0255 0.0379  -0.0021 9   TYR   A CD1 
109  C  CD2 A TYR   A 9   ? 0.1724 0.2388 0.2187 -0.0048 0.0428  0.0249  9   TYR   A CD2 
110  C  CD2 B TYR   A 9   ? 0.2047 0.2324 0.2053 -0.0180 0.0338  0.0047  9   TYR   A CD2 
111  C  CE1 A TYR   A 9   ? 0.1914 0.2532 0.2465 -0.0171 0.0580  -0.0161 9   TYR   A CE1 
112  C  CE1 B TYR   A 9   ? 0.2140 0.2381 0.2219 -0.0270 0.0378  -0.0073 9   TYR   A CE1 
113  C  CE2 A TYR   A 9   ? 0.1677 0.2450 0.2200 -0.0028 0.0542  -0.0013 9   TYR   A CE2 
114  C  CE2 B TYR   A 9   ? 0.2050 0.2342 0.2099 -0.0179 0.0391  -0.0008 9   TYR   A CE2 
115  C  CZ  A TYR   A 9   ? 0.1752 0.2541 0.2380 -0.0195 0.0627  -0.0128 9   TYR   A CZ  
116  C  CZ  B TYR   A 9   ? 0.2098 0.2379 0.2207 -0.0282 0.0415  -0.0043 9   TYR   A CZ  
117  O  OH  A TYR   A 9   ? 0.1842 0.2712 0.2710 -0.0334 0.0575  -0.0137 9   TYR   A OH  
118  O  OH  B TYR   A 9   ? 0.2201 0.2448 0.2374 -0.0368 0.0432  -0.0034 9   TYR   A OH  
137  N  N   A LEU   A 10  ? 0.1729 0.1734 0.2318 -0.0190 0.0288  0.0542  10  LEU   A N   
138  N  N   B LEU   A 10  ? 0.2109 0.2059 0.2007 -0.0176 0.0310  0.0200  10  LEU   A N   
139  C  CA  A LEU   A 10  ? 0.1562 0.1756 0.2354 -0.0257 0.0277  0.0446  10  LEU   A CA  
140  C  CA  B LEU   A 10  ? 0.2090 0.1945 0.1975 -0.0142 0.0283  0.0297  10  LEU   A CA  
141  C  C   A LEU   A 10  ? 0.1566 0.1775 0.2151 -0.0268 0.0315  0.0400  10  LEU   A C   
142  C  C   B LEU   A 10  ? 0.2083 0.1873 0.2153 -0.0177 0.0216  0.0364  10  LEU   A C   
143  O  O   A LEU   A 10  ? 0.1502 0.1633 0.1872 -0.0280 0.0233  0.0424  10  LEU   A O   
144  O  O   B LEU   A 10  ? 0.1981 0.1876 0.2391 -0.0230 0.0097  0.0328  10  LEU   A O   
145  C  CB  A LEU   A 10  ? 0.1592 0.1780 0.2719 -0.0199 0.0010  0.0516  10  LEU   A CB  
146  C  CB  B LEU   A 10  ? 0.2109 0.1890 0.1962 -0.0155 0.0251  0.0394  10  LEU   A CB  
147  C  CG  A LEU   A 10  ? 0.1865 0.1850 0.3153 -0.0101 -0.0464 0.0600  10  LEU   A CG  
148  C  CG  B LEU   A 10  ? 0.2211 0.1909 0.1968 -0.0150 0.0054  0.0410  10  LEU   A CG  
149  C  CD1 A LEU   A 10  ? 0.2199 0.1952 0.3582 -0.0380 -0.0365 0.0555  10  LEU   A CD1 
150  C  CD1 B LEU   A 10  ? 0.2166 0.1996 0.1975 -0.0195 -0.0016 0.0433  10  LEU   A CD1 
151  C  CD2 A LEU   A 10  ? 0.2229 0.2170 0.3280 -0.0144 -0.0443 0.0579  10  LEU   A CD2 
152  C  CD2 B LEU   A 10  ? 0.2226 0.1923 0.1985 -0.0098 -0.0088 0.0373  10  LEU   A CD2 
175  N  N   A LYS   A 11  ? 0.1680 0.1902 0.2202 -0.0173 0.0445  0.0412  11  LYS   A N   
176  N  N   B LYS   A 11  ? 0.2122 0.1868 0.2090 -0.0174 0.0127  0.0425  11  LYS   A N   
177  C  CA  A LYS   A 11  ? 0.1541 0.1864 0.2165 -0.0210 0.0216  0.0516  11  LYS   A CA  
178  C  CA  B LYS   A 11  ? 0.2047 0.1752 0.2030 -0.0225 0.0140  0.0430  11  LYS   A CA  
179  C  C   A LYS   A 11  ? 0.1687 0.1891 0.2129 -0.0167 0.0096  0.0392  11  LYS   A C   
180  C  C   B LYS   A 11  ? 0.1917 0.1615 0.1968 -0.0224 0.0201  0.0242  11  LYS   A C   
181  O  O   A LYS   A 11  ? 0.1829 0.2078 0.2625 -0.0509 0.0167  0.0344  11  LYS   A O   
182  O  O   B LYS   A 11  ? 0.1821 0.1604 0.2126 -0.0224 0.0164  0.0145  11  LYS   A O   
183  C  CB  A LYS   A 11  ? 0.1658 0.1709 0.2089 -0.0208 0.0126  0.0116  11  LYS   A CB  
184  C  CB  B LYS   A 11  ? 0.2137 0.1771 0.1935 -0.0197 0.0091  0.0405  11  LYS   A CB  
185  C  CG  A LYS   A 11  ? 0.1717 0.1637 0.2003 -0.0211 0.0100  0.0151  11  LYS   A CG  
186  C  CG  B LYS   A 11  ? 0.2176 0.1847 0.1835 -0.0171 0.0040  0.0438  11  LYS   A CG  
187  C  CD  A LYS   A 11  ? 0.1867 0.1748 0.1967 -0.0204 0.0020  0.0209  11  LYS   A CD  
188  C  CD  B LYS   A 11  ? 0.2190 0.1860 0.1814 -0.0090 0.0058  0.0488  11  LYS   A CD  
189  C  CE  A LYS   A 11  ? 0.1951 0.1742 0.2023 -0.0151 0.0081  0.0176  11  LYS   A CE  
190  C  CE  B LYS   A 11  ? 0.2166 0.1908 0.1808 -0.0075 0.0149  0.0478  11  LYS   A CE  
191  N  NZ  A LYS   A 11  ? 0.2014 0.1643 0.2163 0.0030  -0.0007 0.0294  11  LYS   A NZ  
192  N  NZ  B LYS   A 11  ? 0.2147 0.1887 0.1749 0.0003  0.0251  0.0536  11  LYS   A NZ  
219  N  N   A LEU   A 12  ? 0.1534 0.1954 0.1966 -0.0060 -0.0004 0.0390  12  LEU   A N   
220  N  N   B LEU   A 12  ? 0.1755 0.1591 0.2006 -0.0194 0.0203  0.0204  12  LEU   A N   
221  C  CA  A LEU   A 12  ? 0.1434 0.1922 0.1962 -0.0061 -0.0018 0.0589  12  LEU   A CA  
222  C  CA  B LEU   A 12  ? 0.1760 0.1644 0.1878 -0.0139 0.0265  0.0337  12  LEU   A CA  
223  C  C   A LEU   A 12  ? 0.1601 0.1712 0.1995 -0.0186 0.0026  0.0619  12  LEU   A C   
224  C  C   B LEU   A 12  ? 0.1755 0.1598 0.1892 -0.0216 0.0297  0.0314  12  LEU   A C   
225  O  O   A LEU   A 12  ? 0.1482 0.1832 0.2232 -0.0178 0.0079  0.0386  12  LEU   A O   
226  O  O   B LEU   A 12  ? 0.1788 0.1625 0.1973 -0.0163 0.0179  0.0286  12  LEU   A O   
227  C  CB  A LEU   A 12  ? 0.1591 0.1939 0.2224 0.0063  -0.0003 0.0691  12  LEU   A CB  
228  C  CB  B LEU   A 12  ? 0.1823 0.1678 0.1920 -0.0063 0.0256  0.0350  12  LEU   A CB  
229  C  CG  A LEU   A 12  ? 0.1690 0.1942 0.2482 0.0147  0.0145  0.0598  12  LEU   A CG  
230  C  CG  B LEU   A 12  ? 0.1772 0.1617 0.2015 -0.0017 0.0419  0.0247  12  LEU   A CG  
231  C  CD1 A LEU   A 12  ? 0.2007 0.1912 0.2512 0.0223  0.0216  0.0649  12  LEU   A CD1 
232  C  CD1 B LEU   A 12  ? 0.1818 0.1640 0.1972 0.0081  0.0493  0.0153  12  LEU   A CD1 
233  C  CD2 A LEU   A 12  ? 0.1668 0.2148 0.2788 0.0134  -0.0093 0.0501  12  LEU   A CD2 
234  C  CD2 B LEU   A 12  ? 0.1751 0.1624 0.2184 -0.0064 0.0400  0.0209  12  LEU   A CD2 
257  N  N   A THR   A 13  ? 0.1717 0.1815 0.1951 -0.0082 -0.0069 0.0390  13  THR   A N   
258  N  N   B THR   A 13  ? 0.1733 0.1621 0.2071 -0.0190 0.0192  0.0242  13  THR   A N   
259  C  CA  A THR   A 13  ? 0.1520 0.1834 0.1888 -0.0099 0.0112  0.0296  13  THR   A CA  
260  C  CA  B THR   A 13  ? 0.1724 0.1702 0.2195 -0.0260 0.0180  0.0307  13  THR   A CA  
261  C  C   A THR   A 13  ? 0.1607 0.1810 0.1960 -0.0091 0.0151  0.0278  13  THR   A C   
262  C  C   B THR   A 13  ? 0.1681 0.1743 0.2330 -0.0387 0.0121  0.0331  13  THR   A C   
263  O  O   A THR   A 13  ? 0.1594 0.1771 0.1889 -0.0133 0.0090  0.0280  13  THR   A O   
264  O  O   B THR   A 13  ? 0.1703 0.1760 0.2492 -0.0466 -0.0009 0.0509  13  THR   A O   
265  C  CB  A THR   A 13  ? 0.1564 0.1995 0.2111 -0.0090 0.0011  0.0319  13  THR   A CB  
266  C  CB  B THR   A 13  ? 0.1637 0.1718 0.2212 -0.0233 0.0048  0.0326  13  THR   A CB  
267  O  OG1 A THR   A 13  ? 0.1542 0.1767 0.2164 -0.0000 0.0008  0.0404  13  THR   A OG1 
268  O  OG1 B THR   A 13  ? 0.1545 0.1704 0.2339 -0.0274 0.0134  0.0295  13  THR   A OG1 
269  C  CG2 A THR   A 13  ? 0.1551 0.2158 0.2416 -0.0142 0.0038  0.0151  13  THR   A CG2 
270  C  CG2 B THR   A 13  ? 0.1718 0.1728 0.2259 -0.0104 0.0009  0.0334  13  THR   A CG2 
285  N  N   A ASP   A 14  ? 0.1732 0.1716 0.1979 -0.0115 0.0069  0.0447  14  ASP   A N   
286  N  N   B ASP   A 14  ? 0.1756 0.1810 0.2314 -0.0363 -0.0019 0.0243  14  ASP   A N   
287  C  CA  A ASP   A 14  ? 0.1720 0.1871 0.2164 -0.0144 -0.0083 0.0603  14  ASP   A CA  
288  C  CA  B ASP   A 14  ? 0.1749 0.1870 0.2219 -0.0414 -0.0018 0.0350  14  ASP   A CA  
289  C  C   A ASP   A 14  ? 0.1812 0.1783 0.1977 -0.0136 -0.0255 0.0526  14  ASP   A C   
290  C  C   B ASP   A 14  ? 0.1808 0.1744 0.2007 -0.0333 -0.0078 0.0429  14  ASP   A C   
291  O  O   A ASP   A 14  ? 0.2052 0.1864 0.2149 -0.0341 -0.0180 0.0482  14  ASP   A O   
292  O  O   B ASP   A 14  ? 0.1826 0.1839 0.2042 -0.0252 -0.0140 0.0312  14  ASP   A O   
293  C  CB  A ASP   A 14  ? 0.1874 0.2286 0.2863 -0.0177 -0.0124 0.0597  14  ASP   A CB  
294  C  CB  B ASP   A 14  ? 0.1725 0.2141 0.2513 -0.0450 0.0081  0.0351  14  ASP   A CB  
295  C  CG  A ASP   A 14  ? 0.2186 0.2774 0.3833 -0.0155 -0.0228 0.0456  14  ASP   A CG  
296  C  CG  B ASP   A 14  ? 0.1673 0.2376 0.2854 -0.0458 0.0174  0.0320  14  ASP   A CG  
297  O  OD1 A ASP   A 14  ? 0.2242 0.2985 0.4160 0.0054  -0.0436 0.0424  14  ASP   A OD1 
298  O  OD1 B ASP   A 14  ? 0.1704 0.2413 0.2910 -0.0446 0.0195  0.0404  14  ASP   A OD1 
299  O  OD2 A ASP   A 14  ? 0.2366 0.3073 0.4197 -0.0243 -0.0283 0.0272  14  ASP   A OD2 
300  O  OD2 B ASP   A 14  ? 0.1661 0.2587 0.3067 -0.0451 0.0151  0.0234  14  ASP   A OD2 
309  N  N   A ASN   A 15  ? 0.1634 0.1683 0.1983 -0.0191 -0.0002 0.0520  15  ASN   A N   
310  N  N   B ASN   A 15  ? 0.1861 0.1541 0.1884 -0.0433 0.0059  0.0650  15  ASN   A N   
311  C  CA  A ASN   A 15  ? 0.1786 0.1710 0.2208 -0.0085 -0.0030 0.0230  15  ASN   A CA  
312  C  CA  B ASN   A 15  ? 0.1891 0.1504 0.1937 -0.0432 0.0013  0.0443  15  ASN   A CA  
313  C  C   A ASN   A 15  ? 0.1748 0.1722 0.2231 -0.0060 -0.0069 0.0261  15  ASN   A C   
314  C  C   B ASN   A 15  ? 0.1790 0.1524 0.1976 -0.0345 0.0119  0.0532  15  ASN   A C   
315  O  O   A ASN   A 15  ? 0.1700 0.1765 0.2294 -0.0142 -0.0186 0.0350  15  ASN   A O   
316  O  O   B ASN   A 15  ? 0.1811 0.1555 0.2110 -0.0283 0.0269  0.0619  15  ASN   A O   
317  C  CB  A ASN   A 15  ? 0.1737 0.1755 0.2158 0.0070  0.0120  0.0384  15  ASN   A CB  
318  C  CB  B ASN   A 15  ? 0.1979 0.1476 0.1859 -0.0561 -0.0023 0.0321  15  ASN   A CB  
319  C  CG  A ASN   A 15  ? 0.1767 0.1721 0.2387 0.0064  0.0242  0.0278  15  ASN   A CG  
320  C  CG  B ASN   A 15  ? 0.2001 0.1458 0.1857 -0.0605 0.0037  0.0192  15  ASN   A CG  
321  O  OD1 A ASN   A 15  ? 0.1861 0.1898 0.2813 -0.0114 0.0392  0.0229  15  ASN   A OD1 
322  O  OD1 B ASN   A 15  ? 0.2003 0.1521 0.2025 -0.0716 0.0086  0.0063  15  ASN   A OD1 
323  N  ND2 A ASN   A 15  ? 0.1765 0.1879 0.2183 0.0057  0.0237  0.0179  15  ASN   A ND2 
324  N  ND2 B ASN   A 15  ? 0.1989 0.1527 0.1681 -0.0581 0.0025  0.0240  15  ASN   A ND2 
337  N  N   A VAL   A 16  ? 0.1637 0.1776 0.2089 -0.0002 -0.0028 0.0281  16  VAL   A N   
338  N  N   B VAL   A 16  ? 0.1651 0.1611 0.1881 -0.0309 0.0193  0.0453  16  VAL   A N   
339  C  CA  A VAL   A 16  ? 0.1685 0.1753 0.2129 0.0046  0.0008  0.0422  16  VAL   A CA  
340  C  CA  B VAL   A 16  ? 0.1616 0.1661 0.1882 -0.0265 0.0256  0.0492  16  VAL   A CA  
341  C  C   A VAL   A 16  ? 0.1630 0.1462 0.1931 -0.0165 0.0043  0.0378  16  VAL   A C   
342  C  C   B VAL   A 16  ? 0.1623 0.1677 0.1829 -0.0182 0.0222  0.0522  16  VAL   A C   
343  O  O   A VAL   A 16  ? 0.1636 0.1517 0.2083 -0.0077 0.0190  0.0142  16  VAL   A O   
344  O  O   B VAL   A 16  ? 0.1521 0.1761 0.1864 -0.0094 0.0146  0.0533  16  VAL   A O   
345  C  CB  A VAL   A 16  ? 0.1667 0.1822 0.2233 0.0110  0.0182  0.0587  16  VAL   A CB  
346  C  CB  B VAL   A 16  ? 0.1571 0.1733 0.1966 -0.0302 0.0255  0.0545  16  VAL   A CB  
347  C  CG1 A VAL   A 16  ? 0.1574 0.1920 0.2436 0.0170  0.0317  0.0675  16  VAL   A CG1 
348  C  CG1 B VAL   A 16  ? 0.1625 0.1786 0.2031 -0.0232 0.0238  0.0543  16  VAL   A CG1 
349  C  CG2 A VAL   A 16  ? 0.1637 0.1924 0.2314 0.0100  0.0197  0.0424  16  VAL   A CG2 
350  C  CG2 B VAL   A 16  ? 0.1586 0.1773 0.2102 -0.0348 0.0255  0.0490  16  VAL   A CG2 
369  N  N   A TYR   A 17  ? 0.1609 0.1496 0.1855 -0.0153 0.0329  0.0287  17  TYR   A N   
370  N  N   B TYR   A 17  ? 0.1746 0.1711 0.1800 -0.0215 0.0249  0.0521  17  TYR   A N   
371  C  CA  A TYR   A 17  ? 0.1593 0.1572 0.1815 -0.0140 0.0339  0.0323  17  TYR   A CA  
372  C  CA  B TYR   A 17  ? 0.1802 0.1843 0.1771 -0.0148 0.0163  0.0381  17  TYR   A CA  
373  C  C   A TYR   A 17  ? 0.1850 0.1440 0.2144 -0.0160 0.0383  0.0168  17  TYR   A C   
374  C  C   B TYR   A 17  ? 0.1789 0.1813 0.1824 -0.0106 0.0192  0.0340  17  TYR   A C   
375  O  O   A TYR   A 17  ? 0.1709 0.1539 0.2345 -0.0119 0.0303  0.0464  17  TYR   A O   
376  O  O   B TYR   A 17  ? 0.1612 0.1776 0.2050 -0.0165 0.0139  0.0410  17  TYR   A O   
377  C  CB  A TYR   A 17  ? 0.1702 0.1748 0.1948 -0.0241 0.0170  0.0376  17  TYR   A CB  
378  C  CB  B TYR   A 17  ? 0.1878 0.1886 0.1840 -0.0126 0.0029  0.0338  17  TYR   A CB  
379  C  CG  A TYR   A 17  ? 0.2021 0.1886 0.1961 -0.0348 0.0151  0.0378  17  TYR   A CG  
380  C  CG  B TYR   A 17  ? 0.1965 0.1976 0.1898 -0.0032 -0.0004 0.0263  17  TYR   A CG  
381  C  CD1 A TYR   A 17  ? 0.2148 0.1987 0.2069 -0.0265 -0.0035 0.0430  17  TYR   A CD1 
382  C  CD1 B TYR   A 17  ? 0.1998 0.1996 0.2020 0.0070  -0.0045 0.0281  17  TYR   A CD1 
383  C  CD2 A TYR   A 17  ? 0.2289 0.1881 0.1866 -0.0501 0.0099  0.0456  17  TYR   A CD2 
384  C  CD2 B TYR   A 17  ? 0.2052 0.2057 0.1899 -0.0047 -0.0040 0.0225  17  TYR   A CD2 
385  C  CE1 A TYR   A 17  ? 0.2424 0.1944 0.2180 -0.0240 -0.0181 0.0374  17  TYR   A CE1 
386  C  CE1 B TYR   A 17  ? 0.2078 0.2052 0.2125 0.0131  -0.0035 0.0313  17  TYR   A CE1 
387  C  CE2 A TYR   A 17  ? 0.2438 0.1873 0.2086 -0.0545 -0.0020 0.0425  17  TYR   A CE2 
388  C  CE2 B TYR   A 17  ? 0.2087 0.2110 0.2024 0.0004  -0.0033 0.0233  17  TYR   A CE2 
389  C  CZ  A TYR   A 17  ? 0.2595 0.1897 0.2006 -0.0400 -0.0264 0.0476  17  TYR   A CZ  
390  C  CZ  B TYR   A 17  ? 0.2131 0.2132 0.2088 0.0102  -0.0078 0.0312  17  TYR   A CZ  
391  O  OH  A TYR   A 17  ? 0.2787 0.1922 0.2123 -0.0489 -0.0291 0.0312  17  TYR   A OH  
392  O  OH  B TYR   A 17  ? 0.2205 0.2220 0.2190 0.0145  -0.0055 0.0305  17  TYR   A OH  
411  N  N   A ILE   A 18  ? 0.1725 0.1567 0.2118 -0.0309 0.0476  0.0262  18  ILE   A N   
412  N  N   B ILE   A 18  ? 0.1718 0.1711 0.1555 -0.0098 0.0186  0.0358  18  ILE   A N   
413  C  CA  A ILE   A 18  ? 0.1678 0.1751 0.2078 -0.0169 0.0466  0.0216  18  ILE   A CA  
414  C  CA  B ILE   A 18  ? 0.1690 0.1584 0.1341 -0.0025 0.0130  0.0294  18  ILE   A CA  
415  C  C   A ILE   A 18  ? 0.1747 0.1792 0.1856 -0.0310 0.0353  0.0275  18  ILE   A C   
416  C  C   B ILE   A 18  ? 0.1773 0.1719 0.1033 -0.0010 -0.0014 0.0154  18  ILE   A C   
417  O  O   A ILE   A 18  ? 0.1783 0.1723 0.2145 -0.0174 0.0518  0.0339  18  ILE   A O   
418  O  O   B ILE   A 18  ? 0.1739 0.1780 0.1063 -0.0020 -0.0038 0.0081  18  ILE   A O   
419  C  CB  A ILE   A 18  ? 0.1677 0.1712 0.1945 0.0014  0.0275  0.0352  18  ILE   A CB  
420  C  CB  B ILE   A 18  ? 0.1728 0.1450 0.1295 -0.0014 0.0236  0.0395  18  ILE   A CB  
421  C  CG1 A ILE   A 18  ? 0.1769 0.1754 0.1888 0.0259  0.0242  0.0374  18  ILE   A CG1 
422  C  CG1 B ILE   A 18  ? 0.1826 0.1367 0.1529 -0.0040 0.0334  0.0532  18  ILE   A CG1 
423  C  CG2 A ILE   A 18  ? 0.1702 0.1755 0.2134 0.0019  0.0287  0.0159  18  ILE   A CG2 
424  C  CG2 B ILE   A 18  ? 0.1746 0.1574 0.1197 -0.0073 0.0207  0.0398  18  ILE   A CG2 
425  C  CD1 A ILE   A 18  ? 0.1972 0.1906 0.2032 0.0338  0.0267  0.0355  18  ILE   A CD1 
426  C  CD1 B ILE   A 18  ? 0.1873 0.1401 0.1818 -0.0021 0.0446  0.0259  18  ILE   A CD1 
449  N  N   A LYS   A 19  ? 0.1696 0.1882 0.1929 -0.0362 0.0521  0.0209  19  LYS   A N   
450  N  N   B LYS   A 19  ? 0.1836 0.1774 0.1106 0.0108  0.0054  -0.0145 19  LYS   A N   
451  C  CA  A LYS   A 19  ? 0.1735 0.1975 0.1882 -0.0342 0.0515  0.0231  19  LYS   A CA  
452  C  CA  B LYS   A 19  ? 0.1848 0.1879 0.1284 0.0194  0.0091  -0.0334 19  LYS   A CA  
453  C  C   A LYS   A 19  ? 0.1741 0.1856 0.2071 -0.0256 0.0498  0.0188  19  LYS   A C   
454  C  C   B LYS   A 19  ? 0.1888 0.1933 0.1513 0.0320  0.0061  -0.0359 19  LYS   A C   
455  O  O   A LYS   A 19  ? 0.1603 0.1964 0.1971 -0.0151 0.0252  0.0198  19  LYS   A O   
456  O  O   B LYS   A 19  ? 0.1884 0.1877 0.1435 0.0354  0.0080  -0.0472 19  LYS   A O   
457  C  CB  A LYS   A 19  ? 0.1884 0.2232 0.2121 -0.0261 0.0431  0.0149  19  LYS   A CB  
458  C  CB  B LYS   A 19  ? 0.1848 0.1939 0.1346 0.0128  0.0047  -0.0462 19  LYS   A CB  
459  C  CG  A LYS   A 19  ? 0.2133 0.2462 0.2253 -0.0433 0.0334  -0.0080 19  LYS   A CG  
460  C  CG  B LYS   A 19  ? 0.1933 0.2075 0.1392 0.0088  0.0095  -0.0376 19  LYS   A CG  
461  C  CD  A LYS   A 19  ? 0.2513 0.2715 0.2481 -0.0455 0.0327  -0.0028 19  LYS   A CD  
462  C  CD  B LYS   A 19  ? 0.2039 0.2167 0.1374 0.0028  0.0120  -0.0323 19  LYS   A CD  
463  C  CE  A LYS   A 19  ? 0.2761 0.2852 0.2526 -0.0616 0.0252  -0.0145 19  LYS   A CE  
464  C  CE  B LYS   A 19  ? 0.2103 0.2283 0.1548 -0.0036 0.0068  -0.0322 19  LYS   A CE  
465  N  NZ  A LYS   A 19  ? 0.2935 0.2931 0.2356 -0.0745 0.0298  -0.0234 19  LYS   A NZ  
466  N  NZ  B LYS   A 19  ? 0.2196 0.2326 0.1682 -0.0143 0.0109  -0.0320 19  LYS   A NZ  
493  N  N   A ASN   A 20  ? 0.1852 0.1938 0.2411 -0.0274 0.0522  0.0379  20  ASN   A N   
494  N  N   B ASN   A 20  ? 0.1998 0.2049 0.1762 0.0341  0.0173  -0.0388 20  ASN   A N   
495  C  CA  A ASN   A 20  ? 0.1987 0.2057 0.2803 0.0033  0.0815  0.0369  20  ASN   A CA  
496  C  CA  B ASN   A 20  ? 0.2153 0.2127 0.2034 0.0328  0.0143  -0.0423 20  ASN   A CA  
497  C  C   A ASN   A 20  ? 0.2044 0.2009 0.2906 -0.0069 0.1049  0.0098  20  ASN   A C   
498  C  C   B ASN   A 20  ? 0.2179 0.2105 0.2100 0.0221  0.0101  -0.0430 20  ASN   A C   
499  O  O   A ASN   A 20  ? 0.2327 0.2208 0.3171 -0.0390 0.1029  -0.0059 20  ASN   A O   
500  O  O   B ASN   A 20  ? 0.2297 0.2225 0.2120 0.0130  -0.0050 -0.0579 20  ASN   A O   
501  C  CB  A ASN   A 20  ? 0.2065 0.2126 0.2862 0.0213  0.0884  0.0719  20  ASN   A CB  
502  C  CB  B ASN   A 20  ? 0.2264 0.2144 0.2161 0.0411  0.0187  -0.0426 20  ASN   A CB  
503  C  CG  A ASN   A 20  ? 0.2149 0.2270 0.3268 0.0473  0.0836  0.0695  20  ASN   A CG  
504  C  CG  B ASN   A 20  ? 0.2374 0.2224 0.2293 0.0492  0.0270  -0.0389 20  ASN   A CG  
505  O  OD1 A ASN   A 20  ? 0.2457 0.2450 0.3591 0.0565  0.0826  0.0565  20  ASN   A OD1 
506  O  OD1 B ASN   A 20  ? 0.2520 0.2348 0.2373 0.0477  0.0300  -0.0459 20  ASN   A OD1 
507  N  ND2 A ASN   A 20  ? 0.2195 0.2141 0.3353 0.0569  0.0686  0.0844  20  ASN   A ND2 
508  N  ND2 B ASN   A 20  ? 0.2411 0.2191 0.2306 0.0558  0.0319  -0.0334 20  ASN   A ND2 
521  N  N   A ALA   A 21  ? 0.2181 0.2020 0.3077 0.0006  0.0936  -0.0067 21  ALA   A N   
522  N  N   B ALA   A 21  ? 0.2209 0.1996 0.2261 0.0112  0.0140  -0.0273 21  ALA   A N   
523  C  CA  A ALA   A 21  ? 0.2246 0.2058 0.3012 -0.0062 0.0781  0.0043  21  ALA   A CA  
524  C  CA  B ALA   A 21  ? 0.2177 0.1895 0.2327 -0.0033 0.0320  -0.0119 21  ALA   A CA  
525  C  C   A ALA   A 21  ? 0.2216 0.1972 0.2977 0.0034  0.0609  0.0218  21  ALA   A C   
526  C  C   B ALA   A 21  ? 0.2094 0.1837 0.2326 -0.0130 0.0564  -0.0063 21  ALA   A C   
527  O  O   A ALA   A 21  ? 0.2209 0.2060 0.2891 0.0199  0.0534  0.0511  21  ALA   A O   
528  O  O   B ALA   A 21  ? 0.2111 0.1863 0.2379 -0.0081 0.0705  -0.0059 21  ALA   A O   
529  C  CB  A ALA   A 21  ? 0.2477 0.2186 0.3296 -0.0212 0.0506  0.0066  21  ALA   A CB  
530  C  CB  B ALA   A 21  ? 0.2231 0.1809 0.2560 -0.0028 0.0237  -0.0065 21  ALA   A CB  
541  N  N   A ASP   A 22  ? 0.2366 0.1842 0.3114 -0.0015 0.0522  0.0265  22  ASP   A N   
542  N  N   B ASP   A 22  ? 0.2044 0.1783 0.2421 -0.0301 0.0649  0.0045  22  ASP   A N   
543  C  CA  A ASP   A 22  ? 0.2357 0.1937 0.2916 0.0072  0.0380  0.0389  22  ASP   A CA  
544  C  CA  B ASP   A 22  ? 0.1980 0.1836 0.2443 -0.0386 0.0616  0.0185  22  ASP   A CA  
545  C  C   A ASP   A 22  ? 0.2160 0.2040 0.2461 0.0067  0.0356  0.0204  22  ASP   A C   
546  C  C   B ASP   A 22  ? 0.1829 0.1779 0.2165 -0.0506 0.0671  0.0093  22  ASP   A C   
547  O  O   A ASP   A 22  ? 0.2303 0.2081 0.2581 0.0096  0.0469  0.0154  22  ASP   A O   
548  O  O   B ASP   A 22  ? 0.1769 0.1762 0.2213 -0.0580 0.0758  -0.0019 22  ASP   A O   
549  C  CB  A ASP   A 22  ? 0.2502 0.1966 0.3305 0.0003  0.0397  0.0378  22  ASP   A CB  
550  C  CB  B ASP   A 22  ? 0.2011 0.1981 0.2648 -0.0323 0.0584  0.0189  22  ASP   A CB  
551  C  CG  A ASP   A 22  ? 0.2700 0.1991 0.3844 -0.0025 0.0163  0.0269  22  ASP   A CG  
552  C  CG  B ASP   A 22  ? 0.1922 0.2067 0.2775 -0.0279 0.0637  0.0192  22  ASP   A CG  
553  O  OD1 A ASP   A 22  ? 0.2784 0.2051 0.4084 -0.0170 -0.0055 0.0477  22  ASP   A OD1 
554  O  OD1 B ASP   A 22  ? 0.1861 0.2044 0.2677 -0.0289 0.0783  0.0146  22  ASP   A OD1 
555  O  OD2 A ASP   A 22  ? 0.2895 0.2157 0.4355 0.0060  0.0243  0.0059  22  ASP   A OD2 
556  O  OD2 B ASP   A 22  ? 0.1888 0.2208 0.2866 -0.0258 0.0645  0.0119  22  ASP   A OD2 
565  N  N   A ILE   A 23  ? 0.2073 0.2236 0.2318 -0.0095 0.0383  0.0087  23  ILE   A N   
566  N  N   B ILE   A 23  ? 0.1806 0.1764 0.2111 -0.0474 0.0588  0.0093  23  ILE   A N   
567  C  CA  A ILE   A 23  ? 0.2028 0.2185 0.2033 -0.0078 0.0383  0.0128  23  ILE   A CA  
568  C  CA  B ILE   A 23  ? 0.1812 0.1834 0.2018 -0.0446 0.0374  0.0117  23  ILE   A CA  
569  C  C   A ILE   A 23  ? 0.2027 0.2336 0.1780 -0.0043 0.0593  0.0226  23  ILE   A C   
570  C  C   B ILE   A 23  ? 0.1991 0.1836 0.2002 -0.0482 0.0383  0.0048  23  ILE   A C   
571  O  O   A ILE   A 23  ? 0.2158 0.2452 0.1743 -0.0006 0.0447  0.0100  23  ILE   A O   
572  O  O   B ILE   A 23  ? 0.2044 0.1888 0.2041 -0.0461 0.0268  -0.0107 23  ILE   A O   
573  C  CB  A ILE   A 23  ? 0.2168 0.2010 0.1607 0.0019  0.0292  0.0080  23  ILE   A CB  
574  C  CB  B ILE   A 23  ? 0.1768 0.1854 0.1905 -0.0274 0.0127  0.0200  23  ILE   A CB  
575  C  CG1 A ILE   A 23  ? 0.2162 0.2029 0.1593 0.0053  0.0211  -0.0031 23  ILE   A CG1 
576  C  CG1 B ILE   A 23  ? 0.1697 0.1817 0.1799 -0.0297 -0.0002 0.0161  23  ILE   A CG1 
577  C  CG2 A ILE   A 23  ? 0.2309 0.2051 0.1590 -0.0013 0.0306  0.0179  23  ILE   A CG2 
578  C  CG2 B ILE   A 23  ? 0.1732 0.1868 0.1944 -0.0143 0.0051  0.0209  23  ILE   A CG2 
579  C  CD1 A ILE   A 23  ? 0.2246 0.1979 0.1627 0.0100  -0.0001 -0.0037 23  ILE   A CD1 
580  C  CD1 B ILE   A 23  ? 0.1608 0.1821 0.1750 -0.0285 -0.0148 0.0146  23  ILE   A CD1 
603  N  N   A VAL   A 24  ? 0.2079 0.2451 0.1954 -0.0191 0.0533  0.0075  24  VAL   A N   
604  N  N   B VAL   A 24  ? 0.2117 0.1889 0.2153 -0.0576 0.0325  -0.0023 24  VAL   A N   
605  C  CA  A VAL   A 24  ? 0.2249 0.2519 0.2276 -0.0235 0.0441  -0.0136 24  VAL   A CA  
606  C  CA  B VAL   A 24  ? 0.2292 0.2027 0.2316 -0.0538 0.0299  -0.0010 24  VAL   A CA  
607  C  C   A VAL   A 24  ? 0.2308 0.2641 0.2445 -0.0351 0.0483  -0.0242 24  VAL   A C   
608  C  C   B VAL   A 24  ? 0.2374 0.2181 0.2403 -0.0517 0.0353  -0.0033 24  VAL   A C   
609  O  O   A VAL   A 24  ? 0.2323 0.2607 0.2409 -0.0366 0.0600  -0.0219 24  VAL   A O   
610  O  O   B VAL   A 24  ? 0.2390 0.2215 0.2478 -0.0483 0.0415  0.0026  24  VAL   A O   
611  C  CB  A VAL   A 24  ? 0.2380 0.2633 0.2456 -0.0336 0.0473  -0.0127 24  VAL   A CB  
612  C  CB  B VAL   A 24  ? 0.2391 0.2122 0.2418 -0.0541 0.0225  0.0072  24  VAL   A CB  
613  C  CG1 A VAL   A 24  ? 0.2531 0.2847 0.2569 -0.0253 0.0592  -0.0325 24  VAL   A CG1 
614  C  CG1 B VAL   A 24  ? 0.2485 0.2223 0.2470 -0.0471 0.0180  0.0021  24  VAL   A CG1 
615  C  CG2 A VAL   A 24  ? 0.2546 0.2733 0.2583 -0.0255 0.0648  -0.0031 24  VAL   A CG2 
616  C  CG2 B VAL   A 24  ? 0.2456 0.2092 0.2360 -0.0563 0.0218  0.0109  24  VAL   A CG2 
635  N  N   A GLU   A 25  ? 0.2417 0.2808 0.2430 -0.0363 0.0780  -0.0249 25  GLU   A N   
636  N  N   B GLU   A 25  ? 0.2436 0.2281 0.2410 -0.0523 0.0432  -0.0118 25  GLU   A N   
637  C  CA  A GLU   A 25  ? 0.2645 0.3038 0.2530 -0.0274 0.0813  -0.0358 25  GLU   A CA  
638  C  CA  B GLU   A 25  ? 0.2558 0.2413 0.2589 -0.0503 0.0385  -0.0101 25  GLU   A CA  
639  C  C   A GLU   A 25  ? 0.2576 0.3027 0.2234 -0.0335 0.0967  -0.0273 25  GLU   A C   
640  C  C   B GLU   A 25  ? 0.2598 0.2392 0.2609 -0.0508 0.0429  -0.0123 25  GLU   A C   
641  O  O   A GLU   A 25  ? 0.2637 0.3164 0.2378 -0.0484 0.0996  -0.0242 25  GLU   A O   
642  O  O   B GLU   A 25  ? 0.2678 0.2416 0.2751 -0.0542 0.0427  -0.0151 25  GLU   A O   
643  C  CB  A GLU   A 25  ? 0.2927 0.3280 0.3092 -0.0195 0.0786  -0.0298 25  GLU   A CB  
644  C  CB  B GLU   A 25  ? 0.2646 0.2505 0.2843 -0.0515 0.0364  -0.0090 25  GLU   A CB  
645  C  CG  A GLU   A 25  ? 0.3239 0.3549 0.3763 -0.0221 0.0646  -0.0273 25  GLU   A CG  
646  C  CG  B GLU   A 25  ? 0.2777 0.2626 0.3190 -0.0541 0.0315  -0.0071 25  GLU   A CG  
647  C  CD  A GLU   A 25  ? 0.3443 0.3780 0.4353 -0.0218 0.0529  -0.0189 25  GLU   A CD  
648  C  CD  B GLU   A 25  ? 0.2827 0.2710 0.3503 -0.0571 0.0220  -0.0081 25  GLU   A CD  
649  O  OE1 A GLU   A 25  ? 0.3569 0.3894 0.4528 -0.0175 0.0360  -0.0278 25  GLU   A OE1 
650  O  OE1 B GLU   A 25  ? 0.2859 0.2696 0.3703 -0.0585 0.0181  -0.0095 25  GLU   A OE1 
651  O  OE2 A GLU   A 25  ? 0.3461 0.3864 0.4757 -0.0239 0.0522  -0.0225 25  GLU   A OE2 
652  O  OE2 B GLU   A 25  ? 0.2858 0.2784 0.3615 -0.0567 0.0225  -0.0032 25  GLU   A OE2 
665  N  N   A GLU   A 26  ? 0.2433 0.2885 0.2309 -0.0388 0.1004  -0.0282 26  GLU   A N   
666  N  N   B GLU   A 26  ? 0.2569 0.2304 0.2544 -0.0501 0.0558  -0.0139 26  GLU   A N   
667  C  CA  A GLU   A 26  ? 0.2579 0.2895 0.2220 -0.0450 0.0848  -0.0108 26  GLU   A CA  
668  C  CA  B GLU   A 26  ? 0.2589 0.2239 0.2457 -0.0439 0.0654  -0.0093 26  GLU   A CA  
669  C  C   A GLU   A 26  ? 0.2647 0.2669 0.1967 -0.0427 0.0667  -0.0104 26  GLU   A C   
670  C  C   B GLU   A 26  ? 0.2596 0.2294 0.2193 -0.0453 0.0630  -0.0075 26  GLU   A C   
671  O  O   A GLU   A 26  ? 0.2733 0.2624 0.1996 -0.0702 0.0522  -0.0119 26  GLU   A O   
672  O  O   B GLU   A 26  ? 0.2666 0.2263 0.2217 -0.0500 0.0666  -0.0091 26  GLU   A O   
673  C  CB  A GLU   A 26  ? 0.2704 0.3115 0.2498 -0.0472 0.0693  -0.0148 26  GLU   A CB  
674  C  CB  B GLU   A 26  ? 0.2600 0.2114 0.2628 -0.0417 0.0644  -0.0170 26  GLU   A CB  
675  C  CG  A GLU   A 26  ? 0.2871 0.3395 0.3161 -0.0596 0.0710  -0.0156 26  GLU   A CG  
676  C  CG  B GLU   A 26  ? 0.2555 0.1882 0.2671 -0.0474 0.0867  -0.0250 26  GLU   A CG  
677  C  CD  A GLU   A 26  ? 0.2867 0.3597 0.3608 -0.0782 0.0903  -0.0106 26  GLU   A CD  
678  C  CD  B GLU   A 26  ? 0.2425 0.1613 0.2574 -0.0671 0.1179  -0.0381 26  GLU   A CD  
679  O  OE1 A GLU   A 26  ? 0.2904 0.3797 0.3401 -0.0801 0.1111  -0.0266 26  GLU   A OE1 
680  O  OE1 B GLU   A 26  ? 0.2344 0.1490 0.2669 -0.0666 0.1363  -0.0716 26  GLU   A OE1 
681  O  OE2 A GLU   A 26  ? 0.2982 0.3703 0.4121 -0.0835 0.0711  -0.0082 26  GLU   A OE2 
682  O  OE2 B GLU   A 26  ? 0.2410 0.1569 0.2292 -0.0564 0.1341  -0.0360 26  GLU   A OE2 
695  N  N   . ALA   A 27  ? 0.2484 0.2359 0.2009 -0.0543 0.0614  -0.0036 27  ALA   A N   
696  C  CA  . ALA   A 27  ? 0.2545 0.2565 0.1774 -0.0437 0.0501  -0.0049 27  ALA   A CA  
697  C  C   . ALA   A 27  ? 0.2840 0.2758 0.1854 -0.0620 0.0643  -0.0153 27  ALA   A C   
698  O  O   . ALA   A 27  ? 0.2754 0.2567 0.2193 -0.0735 0.0453  -0.0189 27  ALA   A O   
699  C  CB  . ALA   A 27  ? 0.2365 0.2502 0.1826 -0.0457 0.0524  -0.0002 27  ALA   A CB  
706  N  N   A LYS   A 28  ? 0.3141 0.2923 0.1852 -0.0575 0.0672  -0.0472 28  LYS   A N   
707  N  N   B LYS   A 28  ? 0.3116 0.3030 0.2148 -0.0591 0.0668  -0.0208 28  LYS   A N   
708  C  CA  A LYS   A 28  ? 0.3526 0.3224 0.2413 -0.0472 0.0598  -0.0663 28  LYS   A CA  
709  C  CA  B LYS   A 28  ? 0.3423 0.3331 0.2584 -0.0536 0.0650  -0.0270 28  LYS   A CA  
710  C  C   A LYS   A 28  ? 0.3669 0.3538 0.2378 -0.0514 0.0772  -0.0559 28  LYS   A C   
711  C  C   B LYS   A 28  ? 0.3580 0.3549 0.2467 -0.0570 0.0814  -0.0297 28  LYS   A C   
712  O  O   A LYS   A 28  ? 0.3811 0.3736 0.2904 -0.0474 0.0586  -0.0494 28  LYS   A O   
713  O  O   B LYS   A 28  ? 0.3651 0.3634 0.2759 -0.0547 0.0712  -0.0267 28  LYS   A O   
714  C  CB  A LYS   A 28  ? 0.3720 0.3296 0.2890 -0.0305 0.0514  -0.0772 28  LYS   A CB  
715  C  CB  B LYS   A 28  ? 0.3564 0.3430 0.3054 -0.0444 0.0524  -0.0264 28  LYS   A CB  
716  C  CG  A LYS   A 28  ? 0.3918 0.3384 0.3526 -0.0135 0.0480  -0.0757 28  LYS   A CG  
717  C  CG  B LYS   A 28  ? 0.3700 0.3523 0.3525 -0.0355 0.0423  -0.0241 28  LYS   A CG  
718  C  CD  A LYS   A 28  ? 0.4107 0.3551 0.4299 -0.0027 0.0353  -0.0757 28  LYS   A CD  
719  C  CD  B LYS   A 28  ? 0.3823 0.3638 0.3978 -0.0291 0.0309  -0.0233 28  LYS   A CD  
720  C  CE  A LYS   A 28  ? 0.4222 0.3636 0.4825 0.0048  0.0268  -0.0733 28  LYS   A CE  
721  C  CE  B LYS   A 28  ? 0.3898 0.3707 0.4307 -0.0257 0.0233  -0.0220 28  LYS   A CE  
722  N  NZ  A LYS   A 28  ? 0.4317 0.3669 0.5128 0.0088  0.0254  -0.0742 28  LYS   A NZ  
723  N  NZ  B LYS   A 28  ? 0.3941 0.3740 0.4482 -0.0235 0.0206  -0.0232 28  LYS   A NZ  
750  N  N   . LYS   A 29  ? 0.3635 0.3667 0.2172 -0.0646 0.1071  -0.0266 29  LYS   A N   
751  C  CA  . LYS   A 29  ? 0.3892 0.4063 0.2328 -0.0708 0.1202  -0.0132 29  LYS   A CA  
752  C  C   . LYS   A 29  ? 0.3992 0.4125 0.2020 -0.0808 0.1025  -0.0014 29  LYS   A C   
753  O  O   . LYS   A 29  ? 0.4211 0.4296 0.2341 -0.0720 0.0939  -0.0050 29  LYS   A O   
754  C  CB  . LYS   A 29  ? 0.4067 0.4380 0.3139 -0.0656 0.1341  -0.0045 29  LYS   A CB  
755  C  CG  . LYS   A 29  ? 0.4280 0.4629 0.3999 -0.0630 0.1386  0.0013  29  LYS   A CG  
756  C  CD  . LYS   A 29  ? 0.4433 0.4837 0.4777 -0.0582 0.1417  0.0004  29  LYS   A CD  
757  C  CE  . LYS   A 29  ? 0.4572 0.4975 0.5285 -0.0552 0.1418  0.0018  29  LYS   A CE  
758  N  NZ  . LYS   A 29  ? 0.4644 0.5054 0.5618 -0.0510 0.1378  0.0086  29  LYS   A NZ  
773  N  N   . VAL   A 30  ? 0.3839 0.3942 0.1946 -0.0950 0.1041  0.0040  30  VAL   A N   
774  C  CA  . VAL   A 30  ? 0.3766 0.3760 0.1870 -0.1096 0.0795  0.0304  30  VAL   A CA  
775  C  C   . VAL   A 30  ? 0.3807 0.3610 0.1590 -0.1109 0.0673  0.0283  30  VAL   A C   
776  O  O   . VAL   A 30  ? 0.3879 0.3650 0.1661 -0.1072 0.0587  0.0257  30  VAL   A O   
777  C  CB  . VAL   A 30  ? 0.3700 0.3686 0.2378 -0.1293 0.0437  0.0416  30  VAL   A CB  
778  C  CG1 . VAL   A 30  ? 0.3703 0.3701 0.2502 -0.1301 0.0299  0.0469  30  VAL   A CG1 
779  C  CG2 . VAL   A 30  ? 0.3707 0.3651 0.2773 -0.1292 0.0442  0.0566  30  VAL   A CG2 
789  N  N   . LYS   A 31  ? 0.3688 0.3342 0.1323 -0.1154 0.0428  0.0157  31  LYS   A N   
790  C  CA  . LYS   A 31  ? 0.3929 0.3423 0.1436 -0.1021 0.0114  0.0085  31  LYS   A CA  
791  C  C   . LYS   A 31  ? 0.3534 0.3108 0.1097 -0.0747 -0.0060 0.0365  31  LYS   A C   
792  O  O   . LYS   A 31  ? 0.3649 0.3257 0.1339 -0.0611 -0.0290 0.0525  31  LYS   A O   
793  C  CB  . LYS   A 31  ? 0.4462 0.3873 0.2518 -0.1040 -0.0127 -0.0086 31  LYS   A CB  
794  C  CG  . LYS   A 31  ? 0.4950 0.4380 0.4114 -0.0987 -0.0338 -0.0190 31  LYS   A CG  
795  C  CD  . LYS   A 31  ? 0.5349 0.4786 0.5308 -0.0940 -0.0499 -0.0295 31  LYS   A CD  
796  C  CE  . LYS   A 31  ? 0.5719 0.5014 0.5980 -0.0871 -0.0618 -0.0398 31  LYS   A CE  
797  N  NZ  . LYS   A 31  ? 0.5895 0.5119 0.6310 -0.0863 -0.0711 -0.0491 31  LYS   A NZ  
811  N  N   . PRO   A 32  ? 0.3020 0.2716 0.1076 -0.0760 -0.0028 0.0253  32  PRO   A N   
812  C  CA  . PRO   A 32  ? 0.2948 0.2485 0.1520 -0.0693 -0.0032 0.0347  32  PRO   A CA  
813  C  C   . PRO   A 32  ? 0.2876 0.2506 0.1469 -0.0609 -0.0154 0.0466  32  PRO   A C   
814  O  O   . PRO   A 32  ? 0.2893 0.2512 0.1617 -0.0712 -0.0330 0.0492  32  PRO   A O   
815  C  CB  . PRO   A 32  ? 0.2848 0.2416 0.1819 -0.0708 -0.0033 0.0357  32  PRO   A CB  
816  C  CG  . PRO   A 32  ? 0.2730 0.2505 0.1458 -0.0656 -0.0222 0.0121  32  PRO   A CG  
817  C  CD  . PRO   A 32  ? 0.2751 0.2637 0.1096 -0.0615 -0.0142 0.0182  32  PRO   A CD  
825  N  N   . THR   A 33  ? 0.2966 0.2471 0.1452 -0.0502 -0.0042 0.0464  33  THR   A N   
826  C  CA  . THR   A 33  ? 0.2883 0.2492 0.1589 -0.0330 -0.0219 0.0421  33  THR   A CA  
827  C  C   . THR   A 33  ? 0.2524 0.2259 0.1493 -0.0314 -0.0280 0.0259  33  THR   A C   
828  O  O   . THR   A 33  ? 0.2373 0.2396 0.1733 -0.0321 -0.0436 0.0470  33  THR   A O   
829  C  CB  . THR   A 33  ? 0.3161 0.2682 0.1712 -0.0292 -0.0248 0.0691  33  THR   A CB  
830  O  OG1 . THR   A 33  ? 0.3473 0.2906 0.2148 -0.0062 -0.0239 0.0872  33  THR   A OG1 
831  C  CG2 . THR   A 33  ? 0.3264 0.2901 0.2219 -0.0252 -0.0357 0.0517  33  THR   A CG2 
839  N  N   . VAL   A 34  ? 0.2331 0.2036 0.1260 -0.0217 -0.0150 0.0222  34  VAL   A N   
840  C  CA  . VAL   A 34  ? 0.2170 0.1972 0.1146 -0.0254 -0.0248 0.0225  34  VAL   A CA  
841  C  C   . VAL   A 34  ? 0.2074 0.1812 0.1203 -0.0282 -0.0168 0.0130  34  VAL   A C   
842  O  O   . VAL   A 34  ? 0.2102 0.1883 0.1435 -0.0344 -0.0082 0.0161  34  VAL   A O   
843  C  CB  . VAL   A 34  ? 0.2128 0.1973 0.1498 -0.0401 -0.0117 0.0150  34  VAL   A CB  
844  C  CG1 . VAL   A 34  ? 0.2077 0.2017 0.1582 -0.0234 0.0132  0.0132  34  VAL   A CG1 
845  C  CG2 . VAL   A 34  ? 0.2251 0.2020 0.1930 -0.0308 -0.0326 0.0123  34  VAL   A CG2 
855  N  N   . VAL   A 35  ? 0.1898 0.1702 0.1283 -0.0291 -0.0162 0.0145  35  VAL   A N   
856  C  CA  . VAL   A 35  ? 0.1643 0.1796 0.1147 -0.0257 0.0008  0.0113  35  VAL   A CA  
857  C  C   . VAL   A 35  ? 0.1526 0.1819 0.1158 -0.0062 -0.0082 0.0156  35  VAL   A C   
858  O  O   . VAL   A 35  ? 0.1524 0.1889 0.1403 -0.0168 0.0090  0.0139  35  VAL   A O   
859  C  CB  . VAL   A 35  ? 0.1912 0.1713 0.1366 -0.0173 0.0053  -0.0005 35  VAL   A CB  
860  C  CG1 . VAL   A 35  ? 0.2130 0.1823 0.1381 -0.0093 0.0015  -0.0096 35  VAL   A CG1 
861  C  CG2 . VAL   A 35  ? 0.1980 0.1576 0.1740 -0.0054 0.0188  -0.0058 35  VAL   A CG2 
871  N  N   . VAL   A 36  ? 0.1471 0.1653 0.1160 -0.0173 0.0088  0.0330  36  VAL   A N   
872  C  CA  . VAL   A 36  ? 0.1449 0.1507 0.1125 -0.0204 0.0106  0.0236  36  VAL   A CA  
873  C  C   . VAL   A 36  ? 0.1472 0.1561 0.1200 -0.0154 0.0245  0.0289  36  VAL   A C   
874  O  O   . VAL   A 36  ? 0.1466 0.1597 0.1407 -0.0073 0.0223  0.0150  36  VAL   A O   
875  C  CB  . VAL   A 36  ? 0.1529 0.1465 0.1206 -0.0122 -0.0038 0.0135  36  VAL   A CB  
876  C  CG1 . VAL   A 36  ? 0.1498 0.1617 0.1326 -0.0136 -0.0013 0.0098  36  VAL   A CG1 
877  C  CG2 . VAL   A 36  ? 0.1716 0.1578 0.1540 -0.0195 -0.0016 0.0387  36  VAL   A CG2 
887  N  N   . ASN   A 37  ? 0.1476 0.1497 0.1011 -0.0091 0.0080  0.0179  37  ASN   A N   
888  C  CA  . ASN   A 37  ? 0.1448 0.1509 0.1029 0.0001  0.0073  0.0254  37  ASN   A CA  
889  C  C   . ASN   A 37  ? 0.1485 0.1492 0.1217 -0.0038 0.0091  0.0279  37  ASN   A C   
890  O  O   . ASN   A 37  ? 0.1618 0.1587 0.1155 0.0079  0.0139  0.0050  37  ASN   A O   
891  C  CB  . ASN   A 37  ? 0.1679 0.1487 0.1261 0.0006  0.0053  0.0246  37  ASN   A CB  
892  C  CG  . ASN   A 37  ? 0.1607 0.1501 0.1311 0.0048  0.0093  0.0034  37  ASN   A CG  
893  O  OD1 . ASN   A 37  ? 0.1433 0.1467 0.1636 0.0069  0.0040  0.0108  37  ASN   A OD1 
894  N  ND2 . ASN   A 37  ? 0.1548 0.1433 0.1379 0.0022  0.0054  0.0182  37  ASN   A ND2 
901  N  N   . ALA   A 38  ? 0.1426 0.1580 0.1271 0.0091  0.0057  0.0132  38  ALA   A N   
902  C  CA  . ALA   A 38  ? 0.1716 0.1468 0.1093 0.0143  0.0054  0.0151  38  ALA   A CA  
903  C  C   . ALA   A 38  ? 0.1806 0.1450 0.1290 0.0122  -0.0096 0.0032  38  ALA   A C   
904  O  O   . ALA   A 38  ? 0.1747 0.1411 0.1353 0.0056  -0.0118 0.0119  38  ALA   A O   
905  C  CB  . ALA   A 38  ? 0.1712 0.1886 0.1447 0.0039  -0.0034 0.0090  38  ALA   A CB  
911  N  N   A ALA   A 39  ? 0.1632 0.1388 0.1426 0.0171  0.0047  0.0050  39  ALA   A N   
912  N  N   B ALA   A 39  ? 0.1760 0.1415 0.1345 0.0037  -0.0184 -0.0007 39  ALA   A N   
913  C  CA  A ALA   A 39  ? 0.1676 0.1423 0.1290 0.0125  0.0159  0.0271  39  ALA   A CA  
914  C  CA  B ALA   A 39  ? 0.1813 0.1441 0.1342 -0.0082 -0.0265 0.0082  39  ALA   A CA  
915  C  C   A ALA   A 39  ? 0.1451 0.1371 0.1424 0.0119  0.0029  0.0123  39  ALA   A C   
916  C  C   B ALA   A 39  ? 0.1723 0.1349 0.1372 -0.0185 -0.0165 0.0120  39  ALA   A C   
917  O  O   A ALA   A 39  ? 0.1540 0.1441 0.1504 0.0092  0.0007  0.0090  39  ALA   A O   
918  O  O   B ALA   A 39  ? 0.1730 0.1269 0.1286 -0.0277 -0.0168 0.0298  39  ALA   A O   
919  C  CB  A ALA   A 39  ? 0.1834 0.1508 0.1428 0.0091  0.0061  0.0056  39  ALA   A CB  
920  C  CB  B ALA   A 39  ? 0.1891 0.1557 0.1372 -0.0061 -0.0471 -0.0017 39  ALA   A CB  
931  N  N   A ASN   A 40  ? 0.1615 0.1578 0.1294 -0.0070 0.0135  0.0138  40  ASN   A N   
932  N  N   B ASN   A 40  ? 0.1780 0.1422 0.1426 -0.0207 -0.0014 0.0061  40  ASN   A N   
933  C  CA  A ASN   A 40  ? 0.1530 0.1745 0.1172 0.0020  0.0146  0.0099  40  ASN   A CA  
934  C  CA  B ASN   A 40  ? 0.1796 0.1507 0.1493 -0.0160 0.0062  0.0088  40  ASN   A CA  
935  C  C   A ASN   A 40  ? 0.1532 0.1514 0.1091 -0.0029 0.0287  0.0100  40  ASN   A C   
936  C  C   B ASN   A 40  ? 0.1761 0.1464 0.1542 -0.0092 -0.0016 0.0186  40  ASN   A C   
937  O  O   A ASN   A 40  ? 0.1562 0.1499 0.1158 -0.0067 0.0234  0.0076  40  ASN   A O   
938  O  O   B ASN   A 40  ? 0.1735 0.1446 0.1714 -0.0049 -0.0179 0.0241  40  ASN   A O   
939  C  CB  A ASN   A 40  ? 0.1572 0.1818 0.1452 0.0005  -0.0040 0.0061  40  ASN   A CB  
940  C  CB  B ASN   A 40  ? 0.1847 0.1475 0.1604 -0.0175 0.0190  -0.0086 40  ASN   A CB  
941  C  CG  A ASN   A 40  ? 0.1750 0.1834 0.1796 0.0099  -0.0180 0.0175  40  ASN   A CG  
942  C  CG  B ASN   A 40  ? 0.1958 0.1437 0.1898 -0.0202 0.0321  -0.0154 40  ASN   A CG  
943  O  OD1 A ASN   A 40  ? 0.1926 0.1835 0.2296 0.0123  -0.0336 0.0194  40  ASN   A OD1 
944  O  OD1 B ASN   A 40  ? 0.2041 0.1436 0.1916 -0.0201 0.0461  -0.0192 40  ASN   A OD1 
945  N  ND2 A ASN   A 40  ? 0.1672 0.1928 0.1669 0.0078  -0.0142 0.0069  40  ASN   A ND2 
946  N  ND2 B ASN   A 40  ? 0.1958 0.1455 0.1976 -0.0256 0.0302  -0.0153 40  ASN   A ND2 
959  N  N   A VAL   A 41  ? 0.1677 0.1407 0.1217 -0.0063 0.0266  0.0079  41  VAL   A N   
960  N  N   B VAL   A 41  ? 0.1814 0.1448 0.1506 -0.0069 0.0022  0.0237  41  VAL   A N   
961  C  CA  A VAL   A 41  ? 0.1706 0.1474 0.1199 0.0034  0.0284  0.0272  41  VAL   A CA  
962  C  CA  B VAL   A 41  ? 0.1824 0.1456 0.1485 -0.0104 0.0197  0.0388  41  VAL   A CA  
963  C  C   A VAL   A 41  ? 0.1819 0.1599 0.1421 0.0110  0.0232  0.0182  41  VAL   A C   
964  C  C   B VAL   A 41  ? 0.1827 0.1482 0.1541 -0.0169 0.0193  0.0409  41  VAL   A C   
965  O  O   A VAL   A 41  ? 0.1888 0.1552 0.1691 0.0179  0.0231  -0.0085 41  VAL   A O   
966  O  O   B VAL   A 41  ? 0.1838 0.1426 0.1593 -0.0275 0.0124  0.0422  41  VAL   A O   
967  C  CB  A VAL   A 41  ? 0.1804 0.1607 0.1202 -0.0095 0.0220  0.0055  41  VAL   A CB  
968  C  CB  B VAL   A 41  ? 0.1849 0.1558 0.1557 -0.0076 0.0313  0.0398  41  VAL   A CB  
969  C  CG1 A VAL   A 41  ? 0.1980 0.1783 0.1485 -0.0001 0.0260  -0.0149 41  VAL   A CG1 
970  C  CG1 B VAL   A 41  ? 0.1924 0.1682 0.1613 -0.0120 0.0481  0.0289  41  VAL   A CG1 
971  C  CG2 A VAL   A 41  ? 0.1892 0.1694 0.1291 -0.0132 0.0327  0.0094  41  VAL   A CG2 
972  C  CG2 B VAL   A 41  ? 0.1880 0.1618 0.1555 -0.0080 0.0209  0.0439  41  VAL   A CG2 
991  N  N   A TYR   A 42  ? 0.1708 0.1485 0.1471 0.0025  0.0308  0.0278  42  TYR   A N   
992  N  N   B TYR   A 42  ? 0.1735 0.1492 0.1610 -0.0107 0.0141  0.0413  42  TYR   A N   
993  C  CA  A TYR   A 42  ? 0.1718 0.1412 0.1449 -0.0118 0.0356  0.0278  42  TYR   A CA  
994  C  CA  B TYR   A 42  ? 0.1734 0.1596 0.1616 -0.0128 0.0058  0.0368  42  TYR   A CA  
995  C  C   A TYR   A 42  ? 0.1619 0.1328 0.1559 -0.0058 0.0306  0.0223  42  TYR   A C   
996  C  C   B TYR   A 42  ? 0.1644 0.1610 0.1549 -0.0110 -0.0103 0.0293  42  TYR   A C   
997  O  O   A TYR   A 42  ? 0.1491 0.1573 0.1771 -0.0084 0.0262  0.0089  42  TYR   A O   
998  O  O   B TYR   A 42  ? 0.1514 0.1709 0.1589 -0.0214 -0.0242 0.0213  42  TYR   A O   
999  C  CB  A TYR   A 42  ? 0.2051 0.1576 0.1384 -0.0044 0.0533  0.0330  42  TYR   A CB  
1000 C  CB  B TYR   A 42  ? 0.1888 0.1733 0.1705 -0.0049 0.0125  0.0291  42  TYR   A CB  
1001 C  CG  A TYR   A 42  ? 0.2371 0.1708 0.1497 0.0009  0.0452  0.0411  42  TYR   A CG  
1002 C  CG  B TYR   A 42  ? 0.2032 0.1876 0.1744 0.0028  0.0209  0.0244  42  TYR   A CG  
1003 C  CD1 A TYR   A 42  ? 0.2475 0.1692 0.1681 -0.0093 0.0440  0.0182  42  TYR   A CD1 
1004 C  CD1 B TYR   A 42  ? 0.2069 0.1886 0.1706 0.0024  0.0235  0.0162  42  TYR   A CD1 
1005 C  CD2 A TYR   A 42  ? 0.2486 0.1922 0.1887 0.0004  0.0317  0.0384  42  TYR   A CD2 
1006 C  CD2 B TYR   A 42  ? 0.2096 0.2003 0.1848 0.0058  0.0213  0.0183  42  TYR   A CD2 
1007 C  CE1 A TYR   A 42  ? 0.2530 0.1868 0.1820 -0.0236 0.0558  0.0224  42  TYR   A CE1 
1008 C  CE1 B TYR   A 42  ? 0.2100 0.1989 0.1791 -0.0017 0.0348  0.0110  42  TYR   A CE1 
1009 C  CE2 A TYR   A 42  ? 0.2579 0.1983 0.1968 -0.0166 0.0411  0.0495  42  TYR   A CE2 
1010 C  CE2 B TYR   A 42  ? 0.2154 0.2073 0.1860 0.0012  0.0280  0.0189  42  TYR   A CE2 
1011 C  CZ  A TYR   A 42  ? 0.2723 0.2107 0.1765 -0.0190 0.0492  0.0301  42  TYR   A CZ  
1012 C  CZ  B TYR   A 42  ? 0.2194 0.2124 0.1812 -0.0018 0.0370  0.0092  42  TYR   A CZ  
1013 O  OH  A TYR   A 42  ? 0.2869 0.2203 0.1986 -0.0278 0.0367  0.0018  42  TYR   A OH  
1014 O  OH  B TYR   A 42  ? 0.2233 0.2214 0.1944 -0.0073 0.0406  -0.0029 42  TYR   A OH  
1033 N  N   A LEU   A 43  ? 0.1599 0.1284 0.1531 -0.0074 0.0337  0.0185  43  LEU   A N   
1034 N  N   B LEU   A 43  ? 0.1653 0.1653 0.1483 -0.0055 -0.0140 0.0209  43  LEU   A N   
1035 C  CA  A LEU   A 43  ? 0.1572 0.1289 0.1431 -0.0136 0.0296  0.0237  43  LEU   A CA  
1036 C  CA  B LEU   A 43  ? 0.1708 0.1653 0.1360 -0.0035 -0.0173 0.0122  43  LEU   A CA  
1037 C  C   A LEU   A 43  ? 0.1425 0.1350 0.1497 0.0043  0.0113  0.0129  43  LEU   A C   
1038 C  C   B LEU   A 43  ? 0.1745 0.1679 0.1566 0.0037  -0.0141 0.0001  43  LEU   A C   
1039 O  O   A LEU   A 43  ? 0.1528 0.1634 0.1713 0.0067  -0.0001 0.0019  43  LEU   A O   
1040 O  O   B LEU   A 43  ? 0.1786 0.1756 0.1652 0.0053  -0.0175 -0.0094 43  LEU   A O   
1041 C  CB  A LEU   A 43  ? 0.1714 0.1395 0.1699 -0.0083 0.0391  0.0261  43  LEU   A CB  
1042 C  CB  B LEU   A 43  ? 0.1771 0.1646 0.1309 -0.0040 -0.0175 0.0166  43  LEU   A CB  
1043 C  CG  A LEU   A 43  ? 0.1796 0.1391 0.1744 0.0010  0.0258  0.0239  43  LEU   A CG  
1044 C  CG  B LEU   A 43  ? 0.1829 0.1607 0.1382 -0.0073 -0.0177 0.0148  43  LEU   A CG  
1045 C  CD1 A LEU   A 43  ? 0.1868 0.1581 0.1906 0.0113  0.0081  0.0371  43  LEU   A CD1 
1046 C  CD1 B LEU   A 43  ? 0.1866 0.1659 0.1560 -0.0043 -0.0181 0.0207  43  LEU   A CD1 
1047 C  CD2 A LEU   A 43  ? 0.1846 0.1319 0.1867 0.0059  0.0193  0.0304  43  LEU   A CD2 
1048 C  CD2 B LEU   A 43  ? 0.1855 0.1565 0.1326 -0.0098 -0.0230 0.0167  43  LEU   A CD2 
1071 N  N   A LYS   A 44  ? 0.1434 0.1484 0.1448 -0.0100 0.0131  0.0121  44  LYS   A N   
1072 N  N   B LYS   A 44  ? 0.1820 0.1684 0.1701 0.0039  -0.0062 0.0023  44  LYS   A N   
1073 C  CA  A LYS   A 44  ? 0.1783 0.1379 0.1421 0.0025  0.0222  0.0281  44  LYS   A CA  
1074 C  CA  B LYS   A 44  ? 0.1953 0.1636 0.1806 0.0059  0.0048  0.0075  44  LYS   A CA  
1075 C  C   A LYS   A 44  ? 0.1680 0.1417 0.1409 0.0075  0.0080  0.0152  44  LYS   A C   
1076 C  C   B LYS   A 44  ? 0.1759 0.1506 0.1615 0.0054  0.0050  0.0113  44  LYS   A C   
1077 O  O   A LYS   A 44  ? 0.1883 0.1553 0.1652 0.0027  -0.0025 0.0021  44  LYS   A O   
1078 O  O   B LYS   A 44  ? 0.1856 0.1518 0.1649 0.0050  0.0062  0.0023  44  LYS   A O   
1079 C  CB  A LYS   A 44  ? 0.2056 0.1523 0.2105 0.0004  0.0297  0.0362  44  LYS   A CB  
1080 C  CB  B LYS   A 44  ? 0.2236 0.1801 0.2297 0.0062  0.0136  0.0067  44  LYS   A CB  
1081 C  CG  A LYS   A 44  ? 0.2327 0.1882 0.2938 -0.0134 0.0569  0.0223  44  LYS   A CG  
1082 C  CG  B LYS   A 44  ? 0.2501 0.1935 0.2834 0.0079  0.0263  0.0020  44  LYS   A CG  
1083 C  CD  A LYS   A 44  ? 0.2693 0.2336 0.3852 -0.0114 0.0433  0.0211  44  LYS   A CD  
1084 C  CD  B LYS   A 44  ? 0.2778 0.2104 0.3350 0.0105  0.0268  0.0023  44  LYS   A CD  
1085 C  CE  A LYS   A 44  ? 0.2852 0.2672 0.4355 -0.0123 0.0385  0.0193  44  LYS   A CE  
1086 C  CE  B LYS   A 44  ? 0.2891 0.2132 0.3659 0.0112  0.0311  0.0022  44  LYS   A CE  
1087 N  NZ  A LYS   A 44  ? 0.2954 0.2838 0.4480 -0.0234 0.0340  0.0184  44  LYS   A NZ  
1088 N  NZ  B LYS   A 44  ? 0.2975 0.2147 0.3810 0.0082  0.0325  0.0126  44  LYS   A NZ  
1115 N  N   . HIS   A 45  ? 0.1535 0.1401 0.1524 0.0016  -0.0025 0.0253  45  HIS   A N   
1116 C  CA  . HIS   A 45  ? 0.1567 0.1598 0.1531 -0.0055 0.0033  0.0146  45  HIS   A CA  
1117 C  C   . HIS   A 45  ? 0.1550 0.1697 0.1586 0.0023  -0.0008 0.0131  45  HIS   A C   
1118 O  O   . HIS   A 45  ? 0.1853 0.1672 0.1954 0.0217  -0.0130 -0.0104 45  HIS   A O   
1119 C  CB  . HIS   A 45  ? 0.1677 0.1649 0.1400 -0.0025 0.0033  0.0065  45  HIS   A CB  
1120 C  CG  . HIS   A 45  ? 0.1639 0.1554 0.1279 -0.0117 -0.0042 0.0096  45  HIS   A CG  
1121 N  ND1 . HIS   A 45  ? 0.1466 0.1568 0.1493 -0.0128 0.0033  0.0086  45  HIS   A ND1 
1122 C  CD2 . HIS   A 45  ? 0.1638 0.1527 0.1412 -0.0085 -0.0099 0.0329  45  HIS   A CD2 
1123 C  CE1 . HIS   A 45  ? 0.1378 0.1418 0.1466 -0.0031 -0.0063 -0.0002 45  HIS   A CE1 
1124 N  NE2 . HIS   A 45  ? 0.1563 0.1578 0.1343 0.0010  0.0070  0.0321  45  HIS   A NE2 
1133 N  N   A GLY   A 46  ? 0.1646 0.1710 0.1895 0.0148  -0.0072 0.0208  46  GLY   A N   
1134 N  N   B GLY   A 46  ? 0.1624 0.1751 0.1648 0.0058  -0.0012 0.0131  46  GLY   A N   
1135 C  CA  A GLY   A 46  ? 0.1621 0.1823 0.1908 0.0204  -0.0108 0.0268  46  GLY   A CA  
1136 C  CA  B GLY   A 46  ? 0.1586 0.1728 0.1678 0.0025  -0.0066 0.0142  46  GLY   A CA  
1137 C  C   A GLY   A 46  ? 0.1496 0.1906 0.2046 0.0240  -0.0232 0.0385  46  GLY   A C   
1138 C  C   B GLY   A 46  ? 0.1552 0.1668 0.1656 0.0052  -0.0203 0.0201  46  GLY   A C   
1139 O  O   A GLY   A 46  ? 0.1500 0.1898 0.2222 0.0184  -0.0141 0.0311  46  GLY   A O   
1140 O  O   B GLY   A 46  ? 0.1584 0.1684 0.1843 -0.0045 -0.0211 0.0334  46  GLY   A O   
1147 N  N   A GLY   A 47  ? 0.1675 0.1802 0.1926 0.0101  -0.0184 0.0296  47  GLY   A N   
1148 N  N   B GLY   A 47  ? 0.1590 0.1569 0.1627 0.0184  -0.0318 0.0085  47  GLY   A N   
1149 C  CA  A GLY   A 47  ? 0.1779 0.1877 0.1867 0.0056  -0.0517 0.0190  47  GLY   A CA  
1150 C  CA  B GLY   A 47  ? 0.1692 0.1612 0.1638 0.0223  -0.0474 -0.0010 47  GLY   A CA  
1151 C  C   A GLY   A 47  ? 0.1561 0.1652 0.1882 0.0030  -0.0533 0.0012  47  GLY   A C   
1152 C  C   B GLY   A 47  ? 0.1698 0.1615 0.1652 0.0215  -0.0269 -0.0178 47  GLY   A C   
1153 O  O   A GLY   A 47  ? 0.1526 0.1606 0.1977 0.0112  -0.0405 0.0274  47  GLY   A O   
1154 O  O   B GLY   A 47  ? 0.1722 0.1571 0.1754 0.0273  -0.0218 -0.0371 47  GLY   A O   
1161 N  N   A GLY   A 48  ? 0.1525 0.1697 0.2088 0.0078  -0.0617 0.0126  48  GLY   A N   
1162 N  N   B GLY   A 48  ? 0.1727 0.1606 0.1616 0.0116  -0.0186 -0.0159 48  GLY   A N   
1163 C  CA  A GLY   A 48  ? 0.1352 0.1632 0.2169 -0.0066 -0.0319 -0.0105 48  GLY   A CA  
1164 C  CA  B GLY   A 48  ? 0.1836 0.1569 0.1669 0.0010  -0.0093 -0.0072 48  GLY   A CA  
1165 C  C   A GLY   A 48  ? 0.1524 0.1585 0.1607 -0.0028 -0.0189 -0.0131 48  GLY   A C   
1166 C  C   B GLY   A 48  ? 0.1870 0.1541 0.1559 -0.0007 -0.0087 -0.0031 48  GLY   A C   
1167 O  O   A GLY   A 48  ? 0.1729 0.1658 0.1910 0.0019  -0.0278 -0.0346 48  GLY   A O   
1168 O  O   B GLY   A 48  ? 0.1969 0.1524 0.1725 -0.0024 -0.0213 -0.0112 48  GLY   A O   
1175 N  N   A VAL   A 49  ? 0.1370 0.1414 0.1345 -0.0079 0.0036  -0.0088 49  VAL   A N   
1176 N  N   B VAL   A 49  ? 0.1724 0.1507 0.1523 -0.0065 0.0005  0.0042  49  VAL   A N   
1177 C  CA  A VAL   A 49  ? 0.1662 0.1434 0.1209 -0.0163 0.0228  0.0005  49  VAL   A CA  
1178 C  CA  B VAL   A 49  ? 0.1541 0.1565 0.1469 -0.0112 0.0078  -0.0023 49  VAL   A CA  
1179 C  C   A VAL   A 49  ? 0.1725 0.1448 0.0959 -0.0027 0.0234  -0.0060 49  VAL   A C   
1180 C  C   B VAL   A 49  ? 0.1380 0.1533 0.1499 -0.0162 -0.0006 -0.0033 49  VAL   A C   
1181 O  O   A VAL   A 49  ? 0.1750 0.1439 0.1016 0.0052  0.0250  -0.0034 49  VAL   A O   
1182 O  O   B VAL   A 49  ? 0.1152 0.1568 0.1684 -0.0182 0.0006  -0.0105 49  VAL   A O   
1183 C  CB  A VAL   A 49  ? 0.1867 0.1548 0.1293 -0.0243 0.0295  -0.0003 49  VAL   A CB  
1184 C  CB  B VAL   A 49  ? 0.1529 0.1583 0.1323 -0.0178 0.0327  -0.0018 49  VAL   A CB  
1185 C  CG1 A VAL   A 49  ? 0.2147 0.1645 0.1398 -0.0131 0.0249  0.0110  49  VAL   A CG1 
1186 C  CG1 B VAL   A 49  ? 0.1561 0.1545 0.1063 -0.0230 0.0432  -0.0073 49  VAL   A CG1 
1187 C  CG2 A VAL   A 49  ? 0.2103 0.1752 0.1931 -0.0507 0.0344  0.0018  49  VAL   A CG2 
1188 C  CG2 B VAL   A 49  ? 0.1555 0.1659 0.1433 -0.0106 0.0590  0.0003  49  VAL   A CG2 
1207 N  N   A ALA   A 50  ? 0.1550 0.1470 0.1102 -0.0073 -0.0142 0.0061  50  ALA   A N   
1208 N  N   B ALA   A 50  ? 0.1460 0.1507 0.1335 -0.0147 -0.0150 -0.0046 50  ALA   A N   
1209 C  CA  A ALA   A 50  ? 0.1553 0.1414 0.1266 -0.0189 -0.0188 0.0132  50  ALA   A CA  
1210 C  CA  B ALA   A 50  ? 0.1475 0.1393 0.1216 -0.0179 -0.0136 -0.0151 50  ALA   A CA  
1211 C  C   A ALA   A 50  ? 0.1584 0.1454 0.1198 -0.0181 -0.0074 0.0177  50  ALA   A C   
1212 C  C   B ALA   A 50  ? 0.1493 0.1408 0.1064 -0.0045 -0.0124 -0.0159 50  ALA   A C   
1213 O  O   A ALA   A 50  ? 0.1508 0.1532 0.1458 -0.0011 0.0055  0.0182  50  ALA   A O   
1214 O  O   B ALA   A 50  ? 0.1516 0.1452 0.1147 0.0089  -0.0159 -0.0241 50  ALA   A O   
1215 C  CB  A ALA   A 50  ? 0.1459 0.1474 0.1149 -0.0075 0.0034  0.0078  50  ALA   A CB  
1216 C  CB  B ALA   A 50  ? 0.1520 0.1434 0.1143 -0.0168 0.0005  -0.0081 50  ALA   A CB  
1227 N  N   A GLY   A 51  ? 0.1532 0.1593 0.1277 -0.0103 0.0018  0.0092  51  GLY   A N   
1228 N  N   B GLY   A 51  ? 0.1484 0.1503 0.1167 0.0076  -0.0104 -0.0031 51  GLY   A N   
1229 C  CA  A GLY   A 51  ? 0.1676 0.1497 0.1416 -0.0094 -0.0023 -0.0068 51  GLY   A CA  
1230 C  CA  B GLY   A 51  ? 0.1485 0.1452 0.1422 0.0087  -0.0122 0.0189  51  GLY   A CA  
1231 C  C   A GLY   A 51  ? 0.1506 0.1332 0.1500 0.0035  -0.0036 -0.0296 51  GLY   A C   
1232 C  C   B GLY   A 51  ? 0.1395 0.1445 0.1651 0.0136  -0.0147 0.0242  51  GLY   A C   
1233 O  O   A GLY   A 51  ? 0.1596 0.1461 0.1616 -0.0002 -0.0059 -0.0172 51  GLY   A O   
1234 O  O   B GLY   A 51  ? 0.1362 0.1541 0.1753 0.0100  -0.0305 0.0282  51  GLY   A O   
1241 N  N   A ALA   A 52  ? 0.1582 0.1418 0.1249 -0.0036 0.0031  -0.0109 52  ALA   A N   
1242 N  N   B ALA   A 52  ? 0.1340 0.1544 0.1630 0.0091  -0.0179 0.0287  52  ALA   A N   
1243 C  CA  A ALA   A 52  ? 0.1503 0.1522 0.1403 -0.0114 -0.0005 -0.0132 52  ALA   A CA  
1244 C  CA  B ALA   A 52  ? 0.1400 0.1540 0.1709 0.0045  -0.0138 0.0285  52  ALA   A CA  
1245 C  C   A ALA   A 52  ? 0.1437 0.1472 0.1235 -0.0042 0.0068  -0.0145 52  ALA   A C   
1246 C  C   B ALA   A 52  ? 0.1486 0.1555 0.1762 0.0076  -0.0108 0.0120  52  ALA   A C   
1247 O  O   A ALA   A 52  ? 0.1454 0.1663 0.1570 0.0091  0.0130  -0.0285 52  ALA   A O   
1248 O  O   B ALA   A 52  ? 0.1561 0.1573 0.1910 0.0212  -0.0212 0.0125  52  ALA   A O   
1249 C  CB  A ALA   A 52  ? 0.1704 0.1749 0.1678 -0.0055 -0.0114 -0.0050 52  ALA   A CB  
1250 C  CB  B ALA   A 52  ? 0.1455 0.1649 0.1709 -0.0009 -0.0259 0.0354  52  ALA   A CB  
1261 N  N   A LEU   A 53  ? 0.1595 0.1389 0.1126 -0.0089 -0.0069 -0.0057 53  LEU   A N   
1262 N  N   B LEU   A 53  ? 0.1581 0.1568 0.1701 0.0016  -0.0163 -0.0002 53  LEU   A N   
1263 C  CA  A LEU   A 53  ? 0.1598 0.1636 0.1109 0.0059  -0.0096 -0.0115 53  LEU   A CA  
1264 C  CA  B LEU   A 53  ? 0.1580 0.1621 0.1726 -0.0057 -0.0095 -0.0045 53  LEU   A CA  
1265 C  C   A LEU   A 53  ? 0.1589 0.1635 0.0906 0.0072  0.0054  -0.0029 53  LEU   A C   
1266 C  C   B LEU   A 53  ? 0.1581 0.1638 0.1634 0.0083  -0.0196 -0.0233 53  LEU   A C   
1267 O  O   A LEU   A 53  ? 0.1627 0.1797 0.1292 -0.0208 0.0286  0.0013  53  LEU   A O   
1268 O  O   B LEU   A 53  ? 0.1673 0.1648 0.1644 0.0161  -0.0343 -0.0341 53  LEU   A O   
1269 C  CB  A LEU   A 53  ? 0.1539 0.1683 0.1166 0.0113  -0.0106 -0.0185 53  LEU   A CB  
1270 C  CB  B LEU   A 53  ? 0.1563 0.1657 0.1811 -0.0202 0.0087  0.0155  53  LEU   A CB  
1271 C  CG  A LEU   A 53  ? 0.1688 0.1700 0.1236 -0.0032 -0.0083 -0.0100 53  LEU   A CG  
1272 C  CG  B LEU   A 53  ? 0.1551 0.1658 0.1777 -0.0342 0.0192  0.0249  53  LEU   A CG  
1273 C  CD1 A LEU   A 53  ? 0.1831 0.1857 0.1284 0.0079  -0.0113 -0.0091 53  LEU   A CD1 
1274 C  CD1 B LEU   A 53  ? 0.1496 0.1670 0.1702 -0.0283 0.0101  0.0291  53  LEU   A CD1 
1275 C  CD2 A LEU   A 53  ? 0.2059 0.1538 0.1587 -0.0031 0.0128  -0.0021 53  LEU   A CD2 
1276 C  CD2 B LEU   A 53  ? 0.1670 0.1757 0.1796 -0.0333 0.0163  0.0215  53  LEU   A CD2 
1299 N  N   A ASN   A 54  ? 0.1408 0.1572 0.1149 -0.0066 -0.0100 0.0065  54  ASN   A N   
1300 N  N   B ASN   A 54  ? 0.1544 0.1610 0.1621 0.0039  -0.0202 -0.0193 54  ASN   A N   
1301 C  CA  A ASN   A 54  ? 0.1399 0.1648 0.1244 -0.0053 -0.0136 -0.0194 54  ASN   A CA  
1302 C  CA  B ASN   A 54  ? 0.1532 0.1633 0.1577 0.0012  -0.0103 -0.0225 54  ASN   A CA  
1303 C  C   A ASN   A 54  ? 0.1453 0.1655 0.1223 -0.0044 -0.0081 -0.0218 54  ASN   A C   
1304 C  C   B ASN   A 54  ? 0.1499 0.1639 0.1479 0.0014  -0.0131 -0.0224 54  ASN   A C   
1305 O  O   A ASN   A 54  ? 0.1436 0.1669 0.1349 -0.0090 -0.0033 -0.0119 54  ASN   A O   
1306 O  O   B ASN   A 54  ? 0.1504 0.1667 0.1504 0.0003  -0.0171 -0.0215 54  ASN   A O   
1307 C  CB  A ASN   A 54  ? 0.1496 0.1534 0.1321 0.0072  -0.0259 -0.0074 54  ASN   A CB  
1308 C  CB  B ASN   A 54  ? 0.1575 0.1603 0.1544 -0.0000 0.0070  -0.0111 54  ASN   A CB  
1309 C  CG  A ASN   A 54  ? 0.1570 0.1666 0.1392 -0.0003 -0.0244 -0.0039 54  ASN   A CG  
1310 C  CG  B ASN   A 54  ? 0.1609 0.1626 0.1441 -0.0082 0.0271  0.0010  54  ASN   A CG  
1311 O  OD1 A ASN   A 54  ? 0.1588 0.1615 0.1563 0.0036  -0.0235 -0.0052 54  ASN   A OD1 
1312 O  OD1 B ASN   A 54  ? 0.1619 0.1600 0.1438 -0.0142 0.0435  0.0001  54  ASN   A OD1 
1313 N  ND2 A ASN   A 54  ? 0.1617 0.1796 0.1573 -0.0096 -0.0274 0.0071  54  ASN   A ND2 
1314 N  ND2 B ASN   A 54  ? 0.1612 0.1676 0.1448 -0.0116 0.0331  0.0254  54  ASN   A ND2 
1327 N  N   . LYS   A 55  ? 0.1445 0.1606 0.1478 0.0024  -0.0088 -0.0199 55  LYS   A N   
1328 C  CA  . LYS   A 55  ? 0.1576 0.1727 0.1525 0.0140  -0.0132 -0.0196 55  LYS   A CA  
1329 C  C   . LYS   A 55  ? 0.1522 0.1696 0.1443 -0.0039 -0.0050 -0.0105 55  LYS   A C   
1330 O  O   . LYS   A 55  ? 0.1696 0.1695 0.1779 0.0010  -0.0090 -0.0241 55  LYS   A O   
1331 C  CB  . LYS   A 55  ? 0.1506 0.1808 0.1845 0.0240  0.0040  -0.0242 55  LYS   A CB  
1332 C  CG  . LYS   A 55  ? 0.1673 0.2088 0.2005 0.0318  -0.0121 -0.0354 55  LYS   A CG  
1333 C  CD  . LYS   A 55  ? 0.1792 0.2324 0.2197 0.0453  -0.0036 -0.0360 55  LYS   A CD  
1334 C  CE  . LYS   A 55  ? 0.2003 0.2729 0.2283 0.0515  -0.0213 -0.0390 55  LYS   A CE  
1335 N  NZ  . LYS   A 55  ? 0.2185 0.3032 0.2352 0.0603  -0.0242 -0.0154 55  LYS   A NZ  
1350 N  N   . ALA   A 56  ? 0.1716 0.1754 0.1541 -0.0064 0.0103  -0.0297 56  ALA   A N   
1351 C  CA  . ALA   A 56  ? 0.1901 0.2007 0.1525 0.0008  0.0076  -0.0310 56  ALA   A CA  
1352 C  C   . ALA   A 56  ? 0.1942 0.2156 0.1344 0.0074  0.0124  -0.0352 56  ALA   A C   
1353 O  O   . ALA   A 56  ? 0.1837 0.2495 0.1513 0.0169  0.0171  -0.0289 56  ALA   A O   
1354 C  CB  . ALA   A 56  ? 0.1860 0.2214 0.1660 -0.0109 0.0124  -0.0170 56  ALA   A CB  
1360 N  N   . THR   A 57  ? 0.1765 0.1908 0.1281 0.0087  0.0170  -0.0190 57  THR   A N   
1361 C  CA  . THR   A 57  ? 0.1617 0.1992 0.1398 -0.0043 -0.0087 -0.0108 57  THR   A CA  
1362 C  C   . THR   A 57  ? 0.1480 0.2134 0.1533 -0.0021 -0.0052 -0.0177 57  THR   A C   
1363 O  O   . THR   A 57  ? 0.1554 0.2145 0.1619 -0.0018 -0.0216 -0.0308 57  THR   A O   
1364 C  CB  . THR   A 57  ? 0.1573 0.1965 0.1240 -0.0110 0.0026  -0.0078 57  THR   A CB  
1365 O  OG1 . THR   A 57  ? 0.1641 0.1830 0.1452 -0.0003 0.0008  -0.0056 57  THR   A OG1 
1366 C  CG2 . THR   A 57  ? 0.1668 0.2030 0.1348 -0.0159 -0.0093 -0.0024 57  THR   A CG2 
1374 N  N   . ASN   A 58  ? 0.1565 0.2042 0.1669 -0.0102 0.0135  -0.0406 58  ASN   A N   
1375 C  CA  . ASN   A 58  ? 0.1999 0.1970 0.1762 -0.0079 0.0133  -0.0494 58  ASN   A CA  
1376 C  C   . ASN   A 58  ? 0.1893 0.1795 0.1676 -0.0028 -0.0109 -0.0301 58  ASN   A C   
1377 O  O   . ASN   A 58  ? 0.1716 0.1863 0.1920 -0.0113 -0.0149 -0.0480 58  ASN   A O   
1378 C  CB  . ASN   A 58  ? 0.2582 0.2082 0.2103 -0.0139 0.0572  -0.0579 58  ASN   A CB  
1379 C  CG  . ASN   A 58  ? 0.3183 0.2497 0.2973 -0.0179 0.0612  -0.0342 58  ASN   A CG  
1380 O  OD1 . ASN   A 58  ? 0.3410 0.2334 0.3722 0.0229  0.0948  -0.0314 58  ASN   A OD1 
1381 N  ND2 . ASN   A 58  ? 0.3441 0.2667 0.3190 -0.0328 0.0525  -0.0238 58  ASN   A ND2 
1388 N  N   . ASN   A 59  ? 0.1671 0.1646 0.1504 -0.0100 -0.0066 -0.0221 59  ASN   A N   
1389 C  CA  . ASN   A 59  ? 0.1610 0.1640 0.1569 -0.0080 -0.0019 -0.0145 59  ASN   A CA  
1390 C  C   . ASN   A 59  ? 0.1644 0.1571 0.1526 -0.0066 0.0050  -0.0037 59  ASN   A C   
1391 O  O   . ASN   A 59  ? 0.1590 0.1713 0.1494 -0.0087 -0.0070 -0.0014 59  ASN   A O   
1392 C  CB  . ASN   A 59  ? 0.1585 0.1555 0.1636 -0.0077 -0.0111 -0.0214 59  ASN   A CB  
1393 C  CG  . ASN   A 59  ? 0.1626 0.1574 0.1825 -0.0054 -0.0263 -0.0083 59  ASN   A CG  
1394 O  OD1 . ASN   A 59  ? 0.1740 0.1596 0.1667 -0.0103 -0.0173 -0.0001 59  ASN   A OD1 
1395 N  ND2 . ASN   A 59  ? 0.1740 0.1630 0.2070 -0.0047 -0.0271 0.0072  59  ASN   A ND2 
1402 N  N   . ALA   A 60  ? 0.1607 0.1602 0.1607 -0.0026 -0.0006 0.0056  60  ALA   A N   
1403 C  CA  . ALA   A 60  ? 0.1606 0.1562 0.1456 -0.0019 -0.0047 -0.0063 60  ALA   A CA  
1404 C  C   . ALA   A 60  ? 0.1763 0.1507 0.1669 -0.0042 -0.0065 0.0021  60  ALA   A C   
1405 O  O   . ALA   A 60  ? 0.1574 0.1587 0.1817 0.0010  -0.0122 -0.0035 60  ALA   A O   
1406 C  CB  . ALA   A 60  ? 0.1639 0.1722 0.1521 -0.0012 0.0058  -0.0307 60  ALA   A CB  
1412 N  N   . MET   A 61  ? 0.1760 0.1268 0.1757 -0.0143 -0.0052 -0.0132 61  MET   A N   
1413 C  CA  . MET   A 61  ? 0.1581 0.1453 0.1628 -0.0104 -0.0026 -0.0001 61  MET   A CA  
1414 C  C   . MET   A 61  ? 0.1412 0.1506 0.1587 -0.0092 -0.0008 0.0046  61  MET   A C   
1415 O  O   . MET   A 61  ? 0.1440 0.1482 0.1668 -0.0057 -0.0011 0.0008  61  MET   A O   
1416 C  CB  . MET   A 61  ? 0.1509 0.1425 0.1524 -0.0144 -0.0047 -0.0180 61  MET   A CB  
1417 C  CG  . MET   A 61  ? 0.1299 0.1605 0.1575 -0.0128 -0.0077 -0.0040 61  MET   A CG  
1418 S  SD  . MET   A 61  ? 0.1640 0.1605 0.1883 -0.0100 0.0041  -0.0156 61  MET   A SD  
1419 C  CE  . MET   A 61  ? 0.1912 0.1713 0.2112 0.0002  0.0232  -0.0396 61  MET   A CE  
1429 N  N   . GLN   A 62  ? 0.1564 0.1431 0.1525 -0.0039 0.0062  0.0097  62  GLN   A N   
1430 C  CA  . GLN   A 62  ? 0.1367 0.1476 0.1628 0.0018  0.0028  0.0060  62  GLN   A CA  
1431 C  C   . GLN   A 62  ? 0.1315 0.1384 0.1670 0.0047  0.0112  -0.0031 62  GLN   A C   
1432 O  O   . GLN   A 62  ? 0.1443 0.1597 0.1646 0.0025  0.0169  -0.0012 62  GLN   A O   
1433 C  CB  . GLN   A 62  ? 0.1692 0.1509 0.1727 0.0059  -0.0127 0.0237  62  GLN   A CB  
1434 C  CG  . GLN   A 62  ? 0.1626 0.1454 0.1685 -0.0076 -0.0039 0.0266  62  GLN   A CG  
1435 C  CD  . GLN   A 62  ? 0.1781 0.1448 0.1458 0.0013  0.0034  0.0062  62  GLN   A CD  
1436 O  OE1 . GLN   A 62  ? 0.1794 0.1614 0.1536 -0.0070 -0.0012 0.0072  62  GLN   A OE1 
1437 N  NE2 . GLN   A 62  ? 0.1688 0.1545 0.1617 0.0004  -0.0022 -0.0050 62  GLN   A NE2 
1446 N  N   . VAL   A 63  ? 0.1438 0.1491 0.1815 -0.0104 0.0149  -0.0155 63  VAL   A N   
1447 C  CA  . VAL   A 63  ? 0.1454 0.1680 0.1930 -0.0126 0.0058  -0.0233 63  VAL   A CA  
1448 C  C   . VAL   A 63  ? 0.1333 0.1635 0.1748 -0.0136 0.0038  -0.0259 63  VAL   A C   
1449 O  O   . VAL   A 63  ? 0.1470 0.1636 0.1946 -0.0190 0.0037  -0.0091 63  VAL   A O   
1450 C  CB  . VAL   A 63  ? 0.1581 0.1778 0.2356 -0.0065 0.0053  -0.0328 63  VAL   A CB  
1451 C  CG1 . VAL   A 63  ? 0.1681 0.1998 0.2608 -0.0032 -0.0007 -0.0595 63  VAL   A CG1 
1452 C  CG2 . VAL   A 63  ? 0.1722 0.1807 0.2471 -0.0164 0.0103  -0.0356 63  VAL   A CG2 
1462 N  N   . GLU   A 64  ? 0.1406 0.1540 0.1828 -0.0054 -0.0069 -0.0135 64  GLU   A N   
1463 C  CA  . GLU   A 64  ? 0.1462 0.1526 0.1727 -0.0065 -0.0201 -0.0055 64  GLU   A CA  
1464 C  C   . GLU   A 64  ? 0.1522 0.1338 0.1729 0.0053  -0.0063 0.0065  64  GLU   A C   
1465 O  O   . GLU   A 64  ? 0.1439 0.1511 0.1888 -0.0012 0.0004  -0.0035 64  GLU   A O   
1466 C  CB  . GLU   A 64  ? 0.1530 0.1671 0.1806 -0.0057 -0.0040 0.0017  64  GLU   A CB  
1467 C  CG  . GLU   A 64  ? 0.1652 0.1767 0.1837 -0.0081 0.0048  0.0108  64  GLU   A CG  
1468 C  CD  . GLU   A 64  ? 0.1876 0.1884 0.1821 -0.0059 0.0023  0.0065  64  GLU   A CD  
1469 O  OE1 . GLU   A 64  ? 0.1931 0.1974 0.2082 -0.0120 0.0133  -0.0061 64  GLU   A OE1 
1470 O  OE2 . GLU   A 64  ? 0.2109 0.1854 0.1875 -0.0321 0.0001  0.0056  64  GLU   A OE2 
1477 N  N   . SER   A 65  ? 0.1552 0.1545 0.1570 0.0020  -0.0137 0.0011  65  SER   A N   
1478 C  CA  . SER   A 65  ? 0.1623 0.1494 0.1452 0.0051  -0.0039 0.0015  65  SER   A CA  
1479 C  C   . SER   A 65  ? 0.1665 0.1477 0.1510 -0.0116 -0.0024 0.0083  65  SER   A C   
1480 O  O   . SER   A 65  ? 0.1624 0.1535 0.1888 -0.0023 0.0154  -0.0105 65  SER   A O   
1481 C  CB  . SER   A 65  ? 0.1583 0.1417 0.1555 -0.0057 -0.0045 0.0146  65  SER   A CB  
1482 O  OG  . SER   A 65  ? 0.1585 0.1503 0.1608 -0.0056 -0.0066 0.0132  65  SER   A OG  
1488 N  N   . ASP   A 66  ? 0.1550 0.1401 0.1623 0.0055  0.0215  0.0080  66  ASP   A N   
1489 C  CA  . ASP   A 66  ? 0.1594 0.1511 0.1750 -0.0056 0.0171  0.0083  66  ASP   A CA  
1490 C  C   . ASP   A 66  ? 0.1488 0.1487 0.1856 -0.0030 0.0272  0.0200  66  ASP   A C   
1491 O  O   . ASP   A 66  ? 0.1562 0.1749 0.2188 0.0044  0.0365  0.0204  66  ASP   A O   
1492 C  CB  . ASP   A 66  ? 0.1856 0.1686 0.2110 -0.0051 0.0268  0.0280  66  ASP   A CB  
1493 C  CG  . ASP   A 66  ? 0.2047 0.1825 0.2656 -0.0081 0.0228  0.0297  66  ASP   A CG  
1494 O  OD1 . ASP   A 66  ? 0.1837 0.2009 0.2629 -0.0011 0.0053  0.0575  66  ASP   A OD1 
1495 O  OD2 . ASP   A 66  ? 0.2175 0.2130 0.3538 0.0121  -0.0069 0.0052  66  ASP   A OD2 
1500 N  N   . ASP   A 67  ? 0.1480 0.1641 0.2025 0.0091  0.0036  0.0133  67  ASP   A N   
1501 C  CA  . ASP   A 67  ? 0.1724 0.1792 0.2085 0.0054  0.0107  0.0329  67  ASP   A CA  
1502 C  C   . ASP   A 67  ? 0.1729 0.1547 0.2042 -0.0010 0.0212  0.0249  67  ASP   A C   
1503 O  O   . ASP   A 67  ? 0.1684 0.1699 0.2249 0.0034  0.0350  0.0312  67  ASP   A O   
1504 C  CB  . ASP   A 67  ? 0.1663 0.1895 0.2295 -0.0129 -0.0127 0.0315  67  ASP   A CB  
1505 C  CG  . ASP   A 67  ? 0.1807 0.1952 0.2614 -0.0135 -0.0330 0.0315  67  ASP   A CG  
1506 O  OD1 . ASP   A 67  ? 0.1818 0.2072 0.3691 -0.0114 -0.0438 0.0434  67  ASP   A OD1 
1507 O  OD2 . ASP   A 67  ? 0.1738 0.2035 0.2330 -0.0002 -0.0156 0.0224  67  ASP   A OD2 
1512 N  N   . TYR   A 68  ? 0.1706 0.1482 0.2157 0.0046  0.0205  0.0291  68  TYR   A N   
1513 C  CA  . TYR   A 68  ? 0.1707 0.1542 0.2000 -0.0022 0.0195  0.0110  68  TYR   A CA  
1514 C  C   . TYR   A 68  ? 0.1393 0.1621 0.1962 0.0014  0.0229  0.0106  68  TYR   A C   
1515 O  O   . TYR   A 68  ? 0.1603 0.1653 0.2086 0.0125  0.0308  0.0250  68  TYR   A O   
1516 C  CB  . TYR   A 68  ? 0.1610 0.1613 0.2172 -0.0135 0.0372  0.0101  68  TYR   A CB  
1517 C  CG  . TYR   A 68  ? 0.1649 0.1911 0.2257 -0.0085 0.0481  0.0286  68  TYR   A CG  
1518 C  CD1 . TYR   A 68  ? 0.1787 0.2092 0.2502 -0.0199 0.0393  -0.0098 68  TYR   A CD1 
1519 C  CD2 . TYR   A 68  ? 0.1910 0.2012 0.2808 -0.0101 0.0599  0.0118  68  TYR   A CD2 
1520 C  CE1 . TYR   A 68  ? 0.1840 0.2222 0.3135 -0.0280 0.0420  -0.0231 68  TYR   A CE1 
1521 C  CE2 . TYR   A 68  ? 0.1915 0.1959 0.3159 -0.0163 0.0712  -0.0210 68  TYR   A CE2 
1522 C  CZ  . TYR   A 68  ? 0.2089 0.2027 0.3266 -0.0243 0.0525  -0.0444 68  TYR   A CZ  
1523 O  OH  . TYR   A 68  ? 0.2503 0.2161 0.3718 -0.0287 0.0486  -0.0826 68  TYR   A OH  
1533 N  N   . ILE   A 69  ? 0.1462 0.1414 0.2031 0.0007  0.0193  0.0185  69  ILE   A N   
1534 C  CA  . ILE   A 69  ? 0.1632 0.1564 0.1962 -0.0058 0.0236  -0.0066 69  ILE   A CA  
1535 C  C   . ILE   A 69  ? 0.1553 0.1513 0.1916 -0.0045 0.0417  0.0155  69  ILE   A C   
1536 O  O   . ILE   A 69  ? 0.1531 0.1776 0.1715 0.0007  0.0180  0.0243  69  ILE   A O   
1537 C  CB  . ILE   A 69  ? 0.1817 0.1823 0.1837 0.0013  0.0109  -0.0111 69  ILE   A CB  
1538 C  CG1 . ILE   A 69  ? 0.2000 0.1856 0.1820 0.0017  0.0229  -0.0260 69  ILE   A CG1 
1539 C  CG2 . ILE   A 69  ? 0.2015 0.2086 0.1942 0.0183  0.0078  -0.0114 69  ILE   A CG2 
1540 C  CD1 . ILE   A 69  ? 0.2088 0.1875 0.2028 -0.0052 0.0123  -0.0208 69  ILE   A CD1 
1552 N  N   . ALA   A 70  ? 0.1565 0.1646 0.1942 -0.0039 0.0288  0.0190  70  ALA   A N   
1553 C  CA  . ALA   A 70  ? 0.1663 0.1847 0.2079 -0.0136 0.0493  0.0116  70  ALA   A CA  
1554 C  C   . ALA   A 70  ? 0.1697 0.2061 0.2121 -0.0055 0.0511  0.0108  70  ALA   A C   
1555 O  O   . ALA   A 70  ? 0.1867 0.2353 0.2379 0.0178  0.0598  0.0447  70  ALA   A O   
1556 C  CB  . ALA   A 70  ? 0.1693 0.1792 0.2420 -0.0154 0.0371  0.0049  70  ALA   A CB  
1562 N  N   . THR   A 71  ? 0.1699 0.1860 0.2102 -0.0046 0.0319  0.0172  71  THR   A N   
1563 C  CA  . THR   A 71  ? 0.1890 0.2143 0.2366 0.0169  0.0282  0.0159  71  THR   A CA  
1564 C  C   . THR   A 71  ? 0.1679 0.2120 0.2413 0.0165  0.0488  0.0153  71  THR   A C   
1565 O  O   . THR   A 71  ? 0.1751 0.2382 0.2871 -0.0028 0.0477  -0.0202 71  THR   A O   
1566 C  CB  . THR   A 71  ? 0.2201 0.2316 0.2538 0.0244  -0.0127 0.0313  71  THR   A CB  
1567 O  OG1 . THR   A 71  ? 0.2493 0.2574 0.2606 0.0146  -0.0437 0.0240  71  THR   A OG1 
1568 C  CG2 . THR   A 71  ? 0.2289 0.2530 0.2841 0.0436  -0.0232 0.0486  71  THR   A CG2 
1576 N  N   . ASN   A 72  ? 0.1681 0.1886 0.2310 0.0035  0.0325  0.0215  72  ASN   A N   
1577 C  CA  . ASN   A 72  ? 0.1732 0.1923 0.2308 0.0001  0.0572  0.0242  72  ASN   A CA  
1578 C  C   . ASN   A 72  ? 0.1842 0.2088 0.2168 -0.0070 0.0668  -0.0040 72  ASN   A C   
1579 O  O   . ASN   A 72  ? 0.2004 0.1984 0.2366 0.0075  0.0461  0.0011  72  ASN   A O   
1580 C  CB  . ASN   A 72  ? 0.2041 0.1810 0.2158 0.0141  0.0525  0.0127  72  ASN   A CB  
1581 C  CG  . ASN   A 72  ? 0.2243 0.2062 0.2159 0.0084  0.0452  0.0264  72  ASN   A CG  
1582 O  OD1 . ASN   A 72  ? 0.2516 0.2611 0.2354 0.0095  0.0599  0.0286  72  ASN   A OD1 
1583 N  ND2 . ASN   A 72  ? 0.2334 0.2177 0.2312 0.0447  0.0296  0.0241  72  ASN   A ND2 
1590 N  N   . GLY   A 73  ? 0.1925 0.2001 0.1999 -0.0072 0.0535  0.0017  73  GLY   A N   
1591 C  CA  . GLY   A 73  ? 0.1948 0.1950 0.1956 -0.0166 0.0508  0.0002  73  GLY   A CA  
1592 C  C   . GLY   A 73  ? 0.1911 0.1643 0.1719 -0.0108 0.0570  0.0171  73  GLY   A C   
1593 O  O   . GLY   A 73  ? 0.1797 0.1713 0.1987 0.0191  0.0341  0.0225  73  GLY   A O   
1597 N  N   . PRO   A 74  ? 0.1992 0.1778 0.1722 -0.0139 0.0602  -0.0015 74  PRO   A N   
1598 C  CA  . PRO   A 74  ? 0.1904 0.1730 0.1812 -0.0034 0.0466  0.0040  74  PRO   A CA  
1599 C  C   . PRO   A 74  ? 0.1786 0.1613 0.1909 0.0013  0.0285  0.0198  74  PRO   A C   
1600 O  O   . PRO   A 74  ? 0.1814 0.1736 0.2204 -0.0038 0.0309  0.0004  74  PRO   A O   
1601 C  CB  . PRO   A 74  ? 0.2172 0.1947 0.2038 -0.0027 0.0422  0.0318  74  PRO   A CB  
1602 C  CG  . PRO   A 74  ? 0.2482 0.2461 0.2574 -0.0231 0.0335  0.0120  74  PRO   A CG  
1603 C  CD  . PRO   A 74  ? 0.2242 0.2092 0.1881 -0.0133 0.0399  -0.0042 74  PRO   A CD  
1611 N  N   . LEU   A 75  ? 0.1802 0.1657 0.1602 0.0033  0.0215  -0.0002 75  LEU   A N   
1612 C  CA  . LEU   A 75  ? 0.1925 0.1590 0.1332 -0.0001 0.0203  0.0039  75  LEU   A CA  
1613 C  C   . LEU   A 75  ? 0.2152 0.1493 0.1483 0.0136  0.0316  0.0191  75  LEU   A C   
1614 O  O   . LEU   A 75  ? 0.2450 0.1573 0.1575 0.0069  0.0134  0.0196  75  LEU   A O   
1615 C  CB  . LEU   A 75  ? 0.2055 0.1636 0.1234 -0.0030 0.0178  0.0161  75  LEU   A CB  
1616 C  CG  . LEU   A 75  ? 0.2082 0.1962 0.1504 -0.0324 0.0224  0.0106  75  LEU   A CG  
1617 C  CD1 . LEU   A 75  ? 0.2138 0.2393 0.1755 -0.0329 0.0216  -0.0089 75  LEU   A CD1 
1618 C  CD2 . LEU   A 75  ? 0.2457 0.2310 0.2329 -0.0070 0.0174  0.0202  75  LEU   A CD2 
1630 N  N   . LYS   A 76  ? 0.2172 0.1318 0.1527 -0.0020 0.0239  0.0011  76  LYS   A N   
1631 C  CA  . LYS   A 76  ? 0.1923 0.1622 0.1665 -0.0051 0.0263  -0.0096 76  LYS   A CA  
1632 C  C   . LYS   A 76  ? 0.1797 0.1725 0.1560 -0.0028 0.0244  0.0079  76  LYS   A C   
1633 O  O   . LYS   A 76  ? 0.1861 0.1612 0.1574 0.0008  0.0206  0.0144  76  LYS   A O   
1634 C  CB  . LYS   A 76  ? 0.1907 0.1933 0.2325 0.0133  0.0342  -0.0506 76  LYS   A CB  
1635 C  CG  . LYS   A 76  ? 0.2019 0.1962 0.2905 0.0167  0.0302  -0.0330 76  LYS   A CG  
1636 C  CD  . LYS   A 76  ? 0.2134 0.1976 0.3241 0.0238  0.0115  -0.0310 76  LYS   A CD  
1637 C  CE  . LYS   A 76  ? 0.2351 0.2220 0.3807 0.0027  0.0184  -0.0574 76  LYS   A CE  
1638 N  NZ  . LYS   A 76  ? 0.2222 0.2154 0.4271 -0.0169 0.0135  -0.0799 76  LYS   A NZ  
1652 N  N   . VAL   A 77  ? 0.1981 0.1800 0.1438 0.0006  0.0265  0.0190  77  VAL   A N   
1653 C  CA  . VAL   A 77  ? 0.1877 0.1787 0.1340 0.0078  0.0248  0.0151  77  VAL   A CA  
1654 C  C   . VAL   A 77  ? 0.1857 0.1721 0.1219 0.0078  0.0287  -0.0041 77  VAL   A C   
1655 O  O   . VAL   A 77  ? 0.2010 0.1858 0.1314 0.0115  0.0339  -0.0114 77  VAL   A O   
1656 C  CB  . VAL   A 77  ? 0.2104 0.1927 0.1477 0.0049  0.0138  0.0265  77  VAL   A CB  
1657 C  CG1 . VAL   A 77  ? 0.2173 0.2037 0.1612 0.0030  -0.0032 0.0082  77  VAL   A CG1 
1658 C  CG2 . VAL   A 77  ? 0.2301 0.1942 0.1773 0.0021  0.0014  0.0411  77  VAL   A CG2 
1668 N  N   . GLY   A 78  ? 0.1907 0.1642 0.1229 0.0126  0.0249  0.0080  78  GLY   A N   
1669 C  CA  . GLY   A 78  ? 0.1840 0.1767 0.1396 -0.0019 0.0253  0.0190  78  GLY   A CA  
1670 C  C   . GLY   A 78  ? 0.1739 0.1528 0.1505 0.0091  0.0159  0.0167  78  GLY   A C   
1671 O  O   . GLY   A 78  ? 0.1758 0.1619 0.1666 0.0075  0.0121  0.0236  78  GLY   A O   
1675 N  N   . GLY   A 79  ? 0.1776 0.1575 0.1530 -0.0001 0.0145  0.0023  79  GLY   A N   
1676 C  CA  . GLY   A 79  ? 0.1743 0.1629 0.1640 -0.0063 0.0198  -0.0035 79  GLY   A CA  
1677 C  C   . GLY   A 79  ? 0.1651 0.1521 0.1534 -0.0013 0.0179  0.0050  79  GLY   A C   
1678 O  O   . GLY   A 79  ? 0.1560 0.1528 0.1624 0.0219  0.0121  0.0049  79  GLY   A O   
1682 N  N   . SER   A 80  ? 0.1526 0.1540 0.1649 -0.0055 0.0128  0.0037  80  SER   A N   
1683 C  CA  . SER   A 80  ? 0.1508 0.1501 0.1414 -0.0007 -0.0043 -0.0054 80  SER   A CA  
1684 C  C   . SER   A 80  ? 0.1662 0.1539 0.1443 0.0048  0.0180  0.0108  80  SER   A C   
1685 O  O   . SER   A 80  ? 0.1565 0.1726 0.1858 0.0145  0.0106  -0.0022 80  SER   A O   
1686 C  CB  . SER   A 80  ? 0.1588 0.1414 0.1776 0.0020  0.0129  0.0025  80  SER   A CB  
1687 O  OG  . SER   A 80  ? 0.1815 0.1602 0.2271 -0.0013 -0.0011 0.0276  80  SER   A OG  
1693 N  N   . CYS   A 81  ? 0.1685 0.1548 0.1339 -0.0009 0.0016  0.0120  81  CYS   A N   
1694 C  CA  . CYS   A 81  ? 0.1594 0.1706 0.1446 -0.0097 -0.0027 0.0210  81  CYS   A CA  
1695 C  C   . CYS   A 81  ? 0.1327 0.1717 0.1555 -0.0165 -0.0149 0.0197  81  CYS   A C   
1696 O  O   . CYS   A 81  ? 0.1447 0.1831 0.1663 0.0016  -0.0005 0.0344  81  CYS   A O   
1697 C  CB  . CYS   A 81  ? 0.1575 0.1482 0.1828 -0.0037 0.0074  0.0275  81  CYS   A CB  
1698 S  SG  . CYS   A 81  ? 0.1687 0.1635 0.1732 -0.0163 0.0027  0.0099  81  CYS   A SG  
1704 N  N   . VAL   A 82  ? 0.1374 0.1724 0.1492 -0.0110 -0.0253 0.0110  82  VAL   A N   
1705 C  CA  . VAL   A 82  ? 0.1546 0.1904 0.1297 -0.0013 -0.0083 0.0186  82  VAL   A CA  
1706 C  C   . VAL   A 82  ? 0.1525 0.1956 0.1581 -0.0069 0.0097  0.0099  82  VAL   A C   
1707 O  O   . VAL   A 82  ? 0.1545 0.1937 0.1805 0.0043  0.0026  -0.0115 82  VAL   A O   
1708 C  CB  . VAL   A 82  ? 0.1980 0.1960 0.1426 -0.0067 0.0086  0.0225  82  VAL   A CB  
1709 C  CG1 . VAL   A 82  ? 0.2209 0.2057 0.1646 -0.0140 0.0088  0.0322  82  VAL   A CG1 
1710 C  CG2 . VAL   A 82  ? 0.2044 0.1943 0.1798 -0.0049 0.0043  0.0097  82  VAL   A CG2 
1720 N  N   . LEU   A 83  ? 0.1459 0.1857 0.1529 -0.0204 0.0000  0.0091  83  LEU   A N   
1721 C  CA  . LEU   A 83  ? 0.1531 0.1892 0.1264 -0.0175 -0.0046 0.0076  83  LEU   A CA  
1722 C  C   . LEU   A 83  ? 0.1582 0.1776 0.1407 -0.0204 -0.0098 0.0028  83  LEU   A C   
1723 O  O   . LEU   A 83  ? 0.1633 0.1793 0.1577 -0.0153 -0.0040 0.0181  83  LEU   A O   
1724 C  CB  . LEU   A 83  ? 0.1852 0.1989 0.1190 -0.0217 -0.0103 0.0221  83  LEU   A CB  
1725 C  CG  . LEU   A 83  ? 0.1870 0.1991 0.1256 -0.0115 -0.0096 0.0111  83  LEU   A CG  
1726 C  CD1 . LEU   A 83  ? 0.2201 0.1982 0.1328 -0.0323 -0.0006 0.0231  83  LEU   A CD1 
1727 C  CD2 . LEU   A 83  ? 0.1787 0.2155 0.1720 -0.0035 0.0220  0.0166  83  LEU   A CD2 
1739 N  N   . SER   A 84  ? 0.1756 0.1843 0.1419 -0.0261 -0.0084 0.0019  84  SER   A N   
1740 C  CA  . SER   A 84  ? 0.1800 0.1918 0.1184 -0.0150 -0.0166 -0.0005 84  SER   A CA  
1741 C  C   . SER   A 84  ? 0.1850 0.1871 0.1208 -0.0175 -0.0001 0.0101  84  SER   A C   
1742 O  O   . SER   A 84  ? 0.1866 0.1835 0.1390 -0.0170 -0.0034 0.0092  84  SER   A O   
1743 C  CB  . SER   A 84  ? 0.1923 0.2068 0.1485 -0.0191 -0.0070 -0.0078 84  SER   A CB  
1744 O  OG  . SER   A 84  ? 0.1985 0.2196 0.1566 -0.0121 -0.0231 -0.0182 84  SER   A OG  
1750 N  N   . GLY   A 85  ? 0.2012 0.1923 0.1232 -0.0142 0.0132  -0.0016 85  GLY   A N   
1751 C  CA  . GLY   A 85  ? 0.2079 0.1995 0.1467 -0.0198 0.0148  -0.0146 85  GLY   A CA  
1752 C  C   . GLY   A 85  ? 0.2046 0.1997 0.1302 -0.0140 -0.0055 -0.0020 85  GLY   A C   
1753 O  O   . GLY   A 85  ? 0.1974 0.2222 0.1488 -0.0274 0.0243  -0.0152 85  GLY   A O   
1757 N  N   . HIS   A 86  ? 0.1896 0.1916 0.1284 -0.0174 -0.0112 -0.0010 86  HIS   A N   
1758 C  CA  . HIS   A 86  ? 0.2155 0.2135 0.1370 -0.0257 -0.0067 -0.0010 86  HIS   A CA  
1759 C  C   . HIS   A 86  ? 0.2450 0.2327 0.1312 -0.0321 0.0078  -0.0009 86  HIS   A C   
1760 O  O   . HIS   A 86  ? 0.2650 0.2458 0.1438 -0.0238 0.0227  -0.0068 86  HIS   A O   
1761 C  CB  . HIS   A 86  ? 0.2183 0.2097 0.1279 -0.0098 0.0063  -0.0022 86  HIS   A CB  
1762 C  CG  . HIS   A 86  ? 0.2065 0.1966 0.1342 -0.0091 0.0096  0.0039  86  HIS   A CG  
1763 N  ND1 . HIS   A 86  ? 0.2072 0.2016 0.1834 -0.0237 -0.0078 0.0050  86  HIS   A ND1 
1764 C  CD2 . HIS   A 86  ? 0.2159 0.1948 0.1320 -0.0030 0.0096  0.0101  86  HIS   A CD2 
1765 C  CE1 . HIS   A 86  ? 0.2124 0.2089 0.1777 -0.0138 0.0186  0.0109  86  HIS   A CE1 
1766 N  NE2 . HIS   A 86  ? 0.2142 0.1992 0.1716 -0.0008 0.0145  0.0319  86  HIS   A NE2 
1774 N  N   . ASN   A 87  ? 0.2573 0.2374 0.1474 -0.0269 0.0296  -0.0198 87  ASN   A N   
1775 C  CA  . ASN   A 87  ? 0.2764 0.2422 0.1512 -0.0125 0.0593  -0.0222 87  ASN   A CA  
1776 C  C   . ASN   A 87  ? 0.2771 0.2600 0.1810 -0.0178 0.0773  -0.0170 87  ASN   A C   
1777 O  O   . ASN   A 87  ? 0.3081 0.2855 0.2498 -0.0341 0.1189  -0.0203 87  ASN   A O   
1778 C  CB  . ASN   A 87  ? 0.2962 0.2450 0.1798 0.0007  0.0425  -0.0219 87  ASN   A CB  
1779 C  CG  . ASN   A 87  ? 0.3062 0.2611 0.1622 0.0158  0.0665  -0.0152 87  ASN   A CG  
1780 O  OD1 . ASN   A 87  ? 0.3316 0.2658 0.1752 0.0320  0.0548  0.0063  87  ASN   A OD1 
1781 N  ND2 . ASN   A 87  ? 0.3126 0.2924 0.1704 0.0171  0.0555  -0.0063 87  ASN   A ND2 
1788 N  N   . LEU   A 88  ? 0.2485 0.2362 0.1835 -0.0265 0.0363  -0.0015 88  LEU   A N   
1789 C  CA  . LEU   A 88  ? 0.2498 0.2368 0.1925 -0.0327 0.0241  0.0225  88  LEU   A CA  
1790 C  C   . LEU   A 88  ? 0.2444 0.2330 0.1823 -0.0245 0.0285  0.0334  88  LEU   A C   
1791 O  O   . LEU   A 88  ? 0.2538 0.2454 0.2154 -0.0216 0.0354  0.0494  88  LEU   A O   
1792 C  CB  . LEU   A 88  ? 0.2442 0.2544 0.2048 -0.0365 -0.0090 0.0471  88  LEU   A CB  
1793 C  CG  . LEU   A 88  ? 0.2572 0.2632 0.2521 -0.0381 -0.0120 0.0374  88  LEU   A CG  
1794 C  CD1 . LEU   A 88  ? 0.2733 0.2737 0.2422 -0.0407 -0.0142 0.0066  88  LEU   A CD1 
1795 C  CD2 . LEU   A 88  ? 0.2626 0.2620 0.3138 -0.0271 -0.0178 0.0263  88  LEU   A CD2 
1807 N  N   . ALA   A 89  ? 0.2289 0.2209 0.1452 -0.0291 0.0202  0.0110  89  ALA   A N   
1808 C  CA  . ALA   A 89  ? 0.2341 0.2303 0.1331 -0.0233 0.0048  0.0165  89  ALA   A CA  
1809 C  C   . ALA   A 89  ? 0.2297 0.2300 0.1557 -0.0085 -0.0149 0.0171  89  ALA   A C   
1810 O  O   . ALA   A 89  ? 0.2328 0.2333 0.1935 -0.0277 -0.0215 -0.0044 89  ALA   A O   
1811 C  CB  . ALA   A 89  ? 0.2238 0.2385 0.1406 -0.0209 0.0005  0.0140  89  ALA   A CB  
1817 N  N   . LYS   A 90  ? 0.2366 0.2465 0.1471 -0.0284 -0.0234 0.0231  90  LYS   A N   
1818 C  CA  . LYS   A 90  ? 0.2456 0.2591 0.1613 -0.0142 -0.0380 0.0250  90  LYS   A CA  
1819 C  C   . LYS   A 90  ? 0.2262 0.2464 0.1437 -0.0226 -0.0282 0.0183  90  LYS   A C   
1820 O  O   . LYS   A 90  ? 0.2326 0.2818 0.1803 -0.0347 -0.0370 0.0087  90  LYS   A O   
1821 C  CB  . LYS   A 90  ? 0.2750 0.2938 0.1967 -0.0239 -0.0413 0.0480  90  LYS   A CB  
1822 C  CG  . LYS   A 90  ? 0.3182 0.3332 0.2938 -0.0255 -0.0351 0.0538  90  LYS   A CG  
1823 C  CD  . LYS   A 90  ? 0.3593 0.3745 0.3999 -0.0253 -0.0295 0.0618  90  LYS   A CD  
1824 C  CE  . LYS   A 90  ? 0.3851 0.4032 0.4778 -0.0199 -0.0236 0.0575  90  LYS   A CE  
1825 N  NZ  . LYS   A 90  ? 0.4010 0.4211 0.5307 -0.0199 -0.0134 0.0460  90  LYS   A NZ  
1839 N  N   . HIS   A 91  ? 0.2087 0.2190 0.1169 -0.0097 -0.0292 0.0208  91  HIS   A N   
1840 C  CA  . HIS   A 91  ? 0.2033 0.1995 0.1192 -0.0163 -0.0348 0.0260  91  HIS   A CA  
1841 C  C   . HIS   A 91  ? 0.1855 0.1813 0.1036 -0.0143 -0.0172 0.0210  91  HIS   A C   
1842 O  O   . HIS   A 91  ? 0.1806 0.2055 0.1379 -0.0202 -0.0061 0.0201  91  HIS   A O   
1843 C  CB  . HIS   A 91  ? 0.2176 0.2269 0.1831 0.0078  -0.0406 0.0228  91  HIS   A CB  
1844 C  CG  . HIS   A 91  ? 0.2793 0.2742 0.2798 0.0094  -0.0756 0.0048  91  HIS   A CG  
1845 N  ND1 . HIS   A 91  ? 0.2962 0.3012 0.3337 0.0154  -0.0973 -0.0171 91  HIS   A ND1 
1846 C  CD2 . HIS   A 91  ? 0.3030 0.2981 0.3170 0.0144  -0.0962 0.0133  91  HIS   A CD2 
1847 C  CE1 . HIS   A 91  ? 0.2963 0.3072 0.3471 0.0134  -0.1020 0.0040  91  HIS   A CE1 
1848 N  NE2 . HIS   A 91  ? 0.3113 0.3129 0.3448 0.0164  -0.1077 -0.0006 91  HIS   A NE2 
1856 N  N   . CYS   A 92  ? 0.1648 0.1820 0.1149 -0.0117 -0.0184 0.0180  92  CYS   A N   
1857 C  CA  . CYS   A 92  ? 0.1562 0.1750 0.1205 -0.0217 0.0047  0.0236  92  CYS   A CA  
1858 C  C   . CYS   A 92  ? 0.1539 0.1729 0.1312 -0.0185 0.0174  0.0103  92  CYS   A C   
1859 O  O   . CYS   A 92  ? 0.1673 0.1818 0.1431 -0.0111 0.0048  0.0166  92  CYS   A O   
1860 C  CB  . CYS   A 92  ? 0.1694 0.1795 0.1559 -0.0084 0.0071  0.0254  92  CYS   A CB  
1861 S  SG  . CYS   A 92  ? 0.1648 0.1632 0.1383 -0.0149 -0.0008 0.0082  92  CYS   A SG  
1867 N  N   . LEU   A 93  ? 0.1612 0.1467 0.1326 -0.0132 0.0110  0.0075  93  LEU   A N   
1868 C  CA  . LEU   A 93  ? 0.1334 0.1440 0.1255 -0.0170 -0.0058 0.0012  93  LEU   A CA  
1869 C  C   . LEU   A 93  ? 0.1619 0.1341 0.1135 -0.0012 -0.0109 0.0097  93  LEU   A C   
1870 O  O   . LEU   A 93  ? 0.1500 0.1499 0.1247 0.0053  -0.0154 0.0086  93  LEU   A O   
1871 C  CB  . LEU   A 93  ? 0.1538 0.1550 0.1251 0.0011  -0.0038 0.0107  93  LEU   A CB  
1872 C  CG  . LEU   A 93  ? 0.1711 0.1534 0.1365 -0.0136 0.0035  0.0184  93  LEU   A CG  
1873 C  CD1 . LEU   A 93  ? 0.1604 0.1517 0.1676 -0.0019 0.0053  0.0070  93  LEU   A CD1 
1874 C  CD2 . LEU   A 93  ? 0.1726 0.1623 0.1584 -0.0035 -0.0107 0.0115  93  LEU   A CD2 
1886 N  N   . HIS   A 94  ? 0.1548 0.1263 0.1332 -0.0021 0.0135  0.0217  94  HIS   A N   
1887 C  CA  . HIS   A 94  ? 0.1573 0.1383 0.1319 -0.0087 0.0019  0.0253  94  HIS   A CA  
1888 C  C   . HIS   A 94  ? 0.1494 0.1313 0.1363 -0.0077 0.0030  0.0047  94  HIS   A C   
1889 O  O   . HIS   A 94  ? 0.1400 0.1532 0.1736 0.0074  0.0101  -0.0044 94  HIS   A O   
1890 C  CB  . HIS   A 94  ? 0.1580 0.1501 0.1311 -0.0009 -0.0171 0.0283  94  HIS   A CB  
1891 C  CG  . HIS   A 94  ? 0.1461 0.1589 0.1228 -0.0035 -0.0093 0.0109  94  HIS   A CG  
1892 N  ND1 . HIS   A 94  ? 0.1572 0.1429 0.1379 -0.0039 0.0034  0.0097  94  HIS   A ND1 
1893 C  CD2 . HIS   A 94  ? 0.1532 0.1714 0.1347 -0.0114 -0.0029 0.0104  94  HIS   A CD2 
1894 C  CE1 . HIS   A 94  ? 0.1653 0.1199 0.1409 -0.0065 -0.0265 0.0061  94  HIS   A CE1 
1895 N  NE2 . HIS   A 94  ? 0.1661 0.1507 0.1408 -0.0056 0.0004  -0.0071 94  HIS   A NE2 
1903 N  N   . VAL   A 95  ? 0.1465 0.1412 0.1339 -0.0044 -0.0039 0.0001  95  VAL   A N   
1904 C  CA  . VAL   A 95  ? 0.1725 0.1393 0.1142 -0.0108 0.0060  0.0249  95  VAL   A CA  
1905 C  C   . VAL   A 95  ? 0.1405 0.1417 0.1144 -0.0300 0.0051  0.0160  95  VAL   A C   
1906 O  O   . VAL   A 95  ? 0.1473 0.1762 0.1234 0.0090  0.0077  0.0053  95  VAL   A O   
1907 C  CB  . VAL   A 95  ? 0.1653 0.1443 0.1369 -0.0183 -0.0005 0.0082  95  VAL   A CB  
1908 C  CG1 . VAL   A 95  ? 0.1744 0.1393 0.1718 -0.0198 -0.0012 0.0068  95  VAL   A CG1 
1909 C  CG2 . VAL   A 95  ? 0.1595 0.1457 0.1391 -0.0210 0.0030  0.0227  95  VAL   A CG2 
1919 N  N   . VAL   A 96  ? 0.1606 0.1383 0.1061 -0.0105 0.0159  0.0174  96  VAL   A N   
1920 C  CA  . VAL   A 96  ? 0.1771 0.1435 0.1119 -0.0068 0.0231  0.0183  96  VAL   A CA  
1921 C  C   . VAL   A 96  ? 0.1642 0.1556 0.1178 0.0059  0.0247  -0.0019 96  VAL   A C   
1922 O  O   . VAL   A 96  ? 0.1772 0.1703 0.1315 -0.0064 0.0265  -0.0114 96  VAL   A O   
1923 C  CB  . VAL   A 96  ? 0.1779 0.1501 0.1243 -0.0073 0.0211  0.0106  96  VAL   A CB  
1924 C  CG1 . VAL   A 96  ? 0.1786 0.1514 0.1172 -0.0066 0.0190  -0.0019 96  VAL   A CG1 
1925 C  CG2 . VAL   A 96  ? 0.1665 0.1598 0.1466 -0.0109 0.0049  0.0113  96  VAL   A CG2 
1935 N  N   . GLY   A 97  ? 0.1626 0.1539 0.1305 0.0021  0.0142  0.0117  97  GLY   A N   
1936 C  CA  . GLY   A 97  ? 0.1825 0.1547 0.1281 0.0014  0.0066  0.0096  97  GLY   A CA  
1937 C  C   . GLY   A 97  ? 0.1687 0.1712 0.1235 0.0017  0.0032  0.0142  97  GLY   A C   
1938 O  O   . GLY   A 97  ? 0.1850 0.1668 0.1441 -0.0069 -0.0008 0.0186  97  GLY   A O   
1942 N  N   . PRO   A 98  ? 0.1790 0.1846 0.1119 0.0030  -0.0064 0.0140  98  PRO   A N   
1943 C  CA  . PRO   A 98  ? 0.1831 0.2089 0.1363 -0.0059 0.0058  -0.0013 98  PRO   A CA  
1944 C  C   . PRO   A 98  ? 0.1968 0.2231 0.1242 -0.0118 0.0049  0.0298  98  PRO   A C   
1945 O  O   . PRO   A 98  ? 0.1864 0.2028 0.1557 -0.0054 0.0046  0.0222  98  PRO   A O   
1946 C  CB  . PRO   A 98  ? 0.1889 0.2145 0.1398 -0.0005 0.0047  -0.0148 98  PRO   A CB  
1947 C  CG  . PRO   A 98  ? 0.1965 0.2036 0.1422 -0.0041 0.0075  -0.0156 98  PRO   A CG  
1948 C  CD  . PRO   A 98  ? 0.1822 0.1895 0.1170 0.0087  -0.0056 -0.0071 98  PRO   A CD  
1956 N  N   A ASN   A 99  ? 0.2049 0.2472 0.1246 -0.0096 0.0066  0.0557  99  ASN   A N   
1957 N  N   B ASN   A 99  ? 0.2131 0.2265 0.1523 -0.0134 -0.0147 0.0520  99  ASN   A N   
1958 C  CA  A ASN   A 99  ? 0.2217 0.2682 0.1302 -0.0117 -0.0017 0.0732  99  ASN   A CA  
1959 C  CA  B ASN   A 99  ? 0.2332 0.2280 0.1825 -0.0173 -0.0333 0.0695  99  ASN   A CA  
1960 C  C   A ASN   A 99  ? 0.2420 0.3047 0.1120 -0.0217 -0.0046 0.0780  99  ASN   A C   
1961 C  C   B ASN   A 99  ? 0.2445 0.2426 0.1956 -0.0126 -0.0382 0.0533  99  ASN   A C   
1962 O  O   A ASN   A 99  ? 0.2541 0.3219 0.1285 -0.0285 -0.0024 0.0724  99  ASN   A O   
1963 O  O   B ASN   A 99  ? 0.2411 0.2281 0.1907 -0.0113 -0.0455 0.0506  99  ASN   A O   
1964 C  CB  A ASN   A 99  ? 0.2198 0.2668 0.1584 -0.0027 -0.0170 0.0787  99  ASN   A CB  
1965 C  CB  B ASN   A 99  ? 0.2429 0.2198 0.1967 -0.0248 -0.0482 0.1039  99  ASN   A CB  
1966 C  CG  A ASN   A 99  ? 0.2215 0.2804 0.1743 0.0044  -0.0228 0.0437  99  ASN   A CG  
1967 C  CG  B ASN   A 99  ? 0.2534 0.2207 0.2162 -0.0311 -0.0578 0.1150  99  ASN   A CG  
1968 O  OD1 A ASN   A 99  ? 0.2408 0.2859 0.1969 0.0193  -0.0382 0.0490  99  ASN   A OD1 
1969 O  OD1 B ASN   A 99  ? 0.2598 0.2285 0.1995 -0.0382 -0.0580 0.1177  99  ASN   A OD1 
1970 N  ND2 A ASN   A 99  ? 0.2211 0.2775 0.1889 0.0107  -0.0045 0.0454  99  ASN   A ND2 
1971 N  ND2 B ASN   A 99  ? 0.2554 0.2165 0.2351 -0.0256 -0.0582 0.1130  99  ASN   A ND2 
1984 N  N   A VAL   A 100 ? 0.2535 0.3251 0.1153 -0.0421 -0.0277 0.0707  100 VAL   A N   
1985 N  N   B VAL   A 100 ? 0.2571 0.2667 0.2128 -0.0187 -0.0356 0.0410  100 VAL   A N   
1986 C  CA  A VAL   A 100 ? 0.2847 0.3528 0.1590 -0.0432 -0.0253 0.0598  100 VAL   A CA  
1987 C  CA  B VAL   A 100 ? 0.2750 0.2916 0.2373 -0.0211 -0.0197 0.0347  100 VAL   A CA  
1988 C  C   A VAL   A 100 ? 0.2984 0.3682 0.1439 -0.0503 -0.0431 0.0923  100 VAL   A C   
1989 C  C   B VAL   A 100 ? 0.2940 0.3160 0.2502 -0.0218 -0.0152 0.0471  100 VAL   A C   
1990 O  O   A VAL   A 100 ? 0.3134 0.3814 0.1715 -0.0552 -0.0180 0.1094  100 VAL   A O   
1991 O  O   B VAL   A 100 ? 0.2950 0.3293 0.2518 -0.0222 -0.0078 0.0490  100 VAL   A O   
1992 C  CB  A VAL   A 100 ? 0.3070 0.3603 0.2147 -0.0496 -0.0295 0.0395  100 VAL   A CB  
1993 C  CB  B VAL   A 100 ? 0.2789 0.2944 0.2552 -0.0263 -0.0134 0.0254  100 VAL   A CB  
1994 C  CG1 A VAL   A 100 ? 0.3120 0.3626 0.2422 -0.0574 -0.0258 0.0505  100 VAL   A CG1 
1995 C  CG1 B VAL   A 100 ? 0.2806 0.2968 0.2597 -0.0298 -0.0090 0.0271  100 VAL   A CG1 
1996 C  CG2 A VAL   A 100 ? 0.3168 0.3680 0.2149 -0.0535 -0.0181 0.0239  100 VAL   A CG2 
1997 C  CG2 B VAL   A 100 ? 0.2855 0.2973 0.2694 -0.0276 -0.0078 0.0168  100 VAL   A CG2 
2016 N  N   A ASN   A 101 ? 0.3055 0.3689 0.1847 -0.0520 -0.0563 0.1262  101 ASN   A N   
2017 N  N   B ASN   A 101 ? 0.3109 0.3233 0.2804 -0.0226 -0.0195 0.0554  101 ASN   A N   
2018 C  CA  A ASN   A 101 ? 0.3259 0.3793 0.2353 -0.0668 -0.0488 0.1534  101 ASN   A CA  
2019 C  CA  B ASN   A 101 ? 0.3271 0.3289 0.3020 -0.0226 -0.0260 0.0564  101 ASN   A CA  
2020 C  C   A ASN   A 101 ? 0.3496 0.4100 0.2649 -0.0785 -0.0113 0.1785  101 ASN   A C   
2021 C  C   B ASN   A 101 ? 0.3448 0.3440 0.3383 -0.0203 -0.0143 0.0572  101 ASN   A C   
2022 O  O   A ASN   A 101 ? 0.3692 0.4222 0.3351 -0.0731 -0.0096 0.1632  101 ASN   A O   
2023 O  O   B ASN   A 101 ? 0.3512 0.3473 0.3616 -0.0223 -0.0156 0.0494  101 ASN   A O   
2024 C  CB  A ASN   A 101 ? 0.3267 0.3564 0.2409 -0.0568 -0.0735 0.1403  101 ASN   A CB  
2025 C  CB  B ASN   A 101 ? 0.3236 0.3170 0.2897 -0.0240 -0.0367 0.0465  101 ASN   A CB  
2026 C  CG  A ASN   A 101 ? 0.3262 0.3404 0.2256 -0.0504 -0.0860 0.1064  101 ASN   A CG  
2027 C  CG  B ASN   A 101 ? 0.3202 0.3019 0.2744 -0.0273 -0.0401 0.0294  101 ASN   A CG  
2028 O  OD1 A ASN   A 101 ? 0.3256 0.3459 0.2459 -0.0442 -0.0795 0.0531  101 ASN   A OD1 
2029 O  OD1 B ASN   A 101 ? 0.3151 0.2969 0.2688 -0.0275 -0.0421 0.0128  101 ASN   A OD1 
2030 N  ND2 A ASN   A 101 ? 0.3307 0.3273 0.2297 -0.0541 -0.0931 0.1079  101 ASN   A ND2 
2031 N  ND2 B ASN   A 101 ? 0.3223 0.2937 0.2747 -0.0309 -0.0436 0.0231  101 ASN   A ND2 
2044 N  N   A LYS   A 102 ? 0.3433 0.4412 0.2837 -0.0958 0.0095  0.1733  102 LYS   A N   
2045 N  N   B LYS   A 102 ? 0.3525 0.3546 0.3487 -0.0198 -0.0035 0.0570  102 LYS   A N   
2046 C  CA  A LYS   A 102 ? 0.3539 0.4738 0.2792 -0.0963 0.0057  0.1558  102 LYS   A CA  
2047 C  CA  B LYS   A 102 ? 0.3625 0.3646 0.3453 -0.0201 0.0076  0.0549  102 LYS   A CA  
2048 C  C   A LYS   A 102 ? 0.3684 0.5022 0.2569 -0.0791 0.0049  0.1410  102 LYS   A C   
2049 C  C   B LYS   A 102 ? 0.3632 0.3681 0.3219 -0.0221 0.0028  0.0664  102 LYS   A C   
2050 O  O   A LYS   A 102 ? 0.3735 0.5231 0.2648 -0.0746 0.0041  0.1276  102 LYS   A O   
2051 O  O   B LYS   A 102 ? 0.3654 0.3725 0.3240 -0.0230 0.0029  0.0672  102 LYS   A O   
2052 C  CB  A LYS   A 102 ? 0.3508 0.4785 0.3152 -0.1081 -0.0122 0.1344  102 LYS   A CB  
2053 C  CB  B LYS   A 102 ? 0.3706 0.3705 0.3677 -0.0217 0.0137  0.0380  102 LYS   A CB  
2054 C  CG  A LYS   A 102 ? 0.3474 0.4806 0.3432 -0.1189 -0.0359 0.1086  102 LYS   A CG  
2055 C  CG  B LYS   A 102 ? 0.3782 0.3744 0.3867 -0.0233 0.0187  0.0243  102 LYS   A CG  
2056 C  CD  A LYS   A 102 ? 0.3505 0.4834 0.3742 -0.1272 -0.0513 0.0794  102 LYS   A CD  
2057 C  CD  B LYS   A 102 ? 0.3853 0.3796 0.4105 -0.0240 0.0237  0.0101  102 LYS   A CD  
2058 C  CE  A LYS   A 102 ? 0.3605 0.4866 0.3987 -0.1260 -0.0576 0.0658  102 LYS   A CE  
2059 C  CE  B LYS   A 102 ? 0.3902 0.3844 0.4283 -0.0235 0.0245  0.0024  102 LYS   A CE  
2060 N  NZ  A LYS   A 102 ? 0.3623 0.4855 0.4147 -0.1354 -0.0547 0.0511  102 LYS   A NZ  
2061 N  NZ  B LYS   A 102 ? 0.3933 0.3871 0.4363 -0.0227 0.0257  0.0004  102 LYS   A NZ  
2088 N  N   A GLY   A 103 ? 0.3684 0.5139 0.2476 -0.0620 -0.0175 0.1072  103 GLY   A N   
2089 N  N   B GLY   A 103 ? 0.3595 0.3705 0.3060 -0.0195 -0.0058 0.0658  103 GLY   A N   
2090 C  CA  A GLY   A 103 ? 0.3718 0.5184 0.2303 -0.0463 -0.0106 0.0772  103 GLY   A CA  
2091 C  CA  B GLY   A 103 ? 0.3551 0.3694 0.2847 -0.0202 -0.0061 0.0705  103 GLY   A CA  
2092 C  C   A GLY   A 103 ? 0.3704 0.5188 0.2249 -0.0357 0.0104  0.0529  103 GLY   A C   
2093 C  C   B GLY   A 103 ? 0.3477 0.3673 0.2553 -0.0234 -0.0004 0.0721  103 GLY   A C   
2094 O  O   A GLY   A 103 ? 0.3868 0.5294 0.2466 -0.0338 0.0182  0.0367  103 GLY   A O   
2095 O  O   B GLY   A 103 ? 0.3480 0.3652 0.2338 -0.0267 -0.0041 0.0823  103 GLY   A O   
2102 N  N   A GLU   A 104 ? 0.3495 0.5057 0.1652 -0.0328 0.0155  0.0414  104 GLU   A N   
2103 N  N   B GLU   A 104 ? 0.3407 0.3684 0.2520 -0.0218 -0.0011 0.0600  104 GLU   A N   
2104 C  CA  A GLU   A 104 ? 0.3219 0.4849 0.1312 -0.0430 0.0200  0.0361  104 GLU   A CA  
2105 C  CA  B GLU   A 104 ? 0.3330 0.3670 0.2517 -0.0241 -0.0054 0.0443  104 GLU   A CA  
2106 C  C   A GLU   A 104 ? 0.3241 0.4889 0.1358 -0.0462 0.0193  0.0160  104 GLU   A C   
2107 C  C   B GLU   A 104 ? 0.3384 0.3729 0.2690 -0.0230 -0.0045 0.0323  104 GLU   A C   
2108 O  O   A GLU   A 104 ? 0.3200 0.4847 0.1859 -0.0493 0.0020  0.0049  104 GLU   A O   
2109 O  O   B GLU   A 104 ? 0.3351 0.3674 0.2685 -0.0218 -0.0056 0.0356  104 GLU   A O   
2110 C  CB  A GLU   A 104 ? 0.2911 0.4451 0.1337 -0.0431 0.0351  0.0514  104 GLU   A CB  
2111 C  CB  B GLU   A 104 ? 0.3213 0.3606 0.2461 -0.0256 -0.0071 0.0393  104 GLU   A CB  
2112 C  CG  A GLU   A 104 ? 0.2711 0.4410 0.1557 -0.0443 0.0300  0.0669  104 GLU   A CG  
2113 C  CG  B GLU   A 104 ? 0.3123 0.3545 0.2556 -0.0265 -0.0116 0.0342  104 GLU   A CG  
2114 C  CD  A GLU   A 104 ? 0.2507 0.4177 0.1471 -0.0411 0.0204  0.0868  104 GLU   A CD  
2115 C  CD  B GLU   A 104 ? 0.3041 0.3481 0.2583 -0.0287 -0.0170 0.0316  104 GLU   A CD  
2116 O  OE1 A GLU   A 104 ? 0.2390 0.3969 0.1327 -0.0318 0.0034  0.0849  104 GLU   A OE1 
2117 O  OE1 B GLU   A 104 ? 0.3002 0.3434 0.2531 -0.0285 -0.0225 0.0299  104 GLU   A OE1 
2118 O  OE2 A GLU   A 104 ? 0.2694 0.4158 0.1778 -0.0446 0.0240  0.0999  104 GLU   A OE2 
2119 O  OE2 B GLU   A 104 ? 0.3056 0.3458 0.2760 -0.0299 -0.0157 0.0292  104 GLU   A OE2 
2132 N  N   A ASP   A 105 ? 0.3295 0.4895 0.1508 -0.0487 0.0427  -0.0122 105 ASP   A N   
2133 N  N   B ASP   A 105 ? 0.3487 0.3835 0.2899 -0.0267 -0.0001 0.0152  105 ASP   A N   
2134 C  CA  A ASP   A 105 ? 0.3345 0.4889 0.1958 -0.0453 0.0491  -0.0405 105 ASP   A CA  
2135 C  CA  B ASP   A 105 ? 0.3574 0.3917 0.3113 -0.0269 0.0044  -0.0039 105 ASP   A CA  
2136 C  C   A ASP   A 105 ? 0.2981 0.4656 0.1596 -0.0542 0.0377  -0.0561 105 ASP   A C   
2137 C  C   B ASP   A 105 ? 0.3477 0.3897 0.3006 -0.0303 0.0029  -0.0146 105 ASP   A C   
2138 O  O   A ASP   A 105 ? 0.2740 0.4310 0.1316 -0.0456 0.0286  -0.0675 105 ASP   A O   
2139 O  O   B ASP   A 105 ? 0.3449 0.3912 0.2908 -0.0291 0.0005  -0.0183 105 ASP   A O   
2140 C  CB  A ASP   A 105 ? 0.3715 0.5097 0.2816 -0.0358 0.0725  -0.0569 105 ASP   A CB  
2141 C  CB  B ASP   A 105 ? 0.3742 0.3979 0.3420 -0.0248 0.0126  -0.0136 105 ASP   A CB  
2142 C  CG  A ASP   A 105 ? 0.4004 0.5248 0.3600 -0.0272 0.0817  -0.0732 105 ASP   A CG  
2143 C  CG  B ASP   A 105 ? 0.3877 0.4034 0.3673 -0.0200 0.0176  -0.0219 105 ASP   A CG  
2144 O  OD1 A ASP   A 105 ? 0.4043 0.5307 0.3575 -0.0335 0.0771  -0.0920 105 ASP   A OD1 
2145 O  OD1 B ASP   A 105 ? 0.3945 0.4035 0.3670 -0.0205 0.0201  -0.0278 105 ASP   A OD1 
2146 O  OD2 A ASP   A 105 ? 0.4219 0.5320 0.4199 -0.0241 0.0944  -0.0624 105 ASP   A OD2 
2147 O  OD2 B ASP   A 105 ? 0.3955 0.4075 0.3926 -0.0205 0.0164  -0.0203 105 ASP   A OD2 
2156 N  N   A ILE   A 106 ? 0.2890 0.4521 0.1839 -0.0625 0.0058  -0.0463 106 ILE   A N   
2157 N  N   B ILE   A 106 ? 0.3416 0.3841 0.3020 -0.0344 -0.0004 -0.0192 106 ILE   A N   
2158 C  CA  A ILE   A 106 ? 0.2624 0.4291 0.2161 -0.0769 -0.0128 -0.0741 106 ILE   A CA  
2159 C  CA  B ILE   A 106 ? 0.3308 0.3730 0.3030 -0.0385 0.0003  -0.0306 106 ILE   A CA  
2160 C  C   A ILE   A 106 ? 0.2490 0.3937 0.2335 -0.0932 -0.0069 -0.0995 106 ILE   A C   
2161 C  C   B ILE   A 106 ? 0.3214 0.3534 0.3039 -0.0441 0.0073  -0.0435 106 ILE   A C   
2162 O  O   A ILE   A 106 ? 0.2182 0.3719 0.2572 -0.0983 0.0147  -0.1021 106 ILE   A O   
2163 O  O   B ILE   A 106 ? 0.3169 0.3477 0.3015 -0.0435 0.0089  -0.0499 106 ILE   A O   
2164 C  CB  A ILE   A 106 ? 0.2695 0.4457 0.2820 -0.0677 -0.0368 -0.0478 106 ILE   A CB  
2165 C  CB  B ILE   A 106 ? 0.3330 0.3808 0.3166 -0.0352 -0.0059 -0.0241 106 ILE   A CB  
2166 C  CG1 A ILE   A 106 ? 0.2728 0.4462 0.3238 -0.0605 -0.0437 -0.0225 106 ILE   A CG1 
2167 C  CG1 B ILE   A 106 ? 0.3340 0.3818 0.3257 -0.0322 -0.0106 -0.0159 106 ILE   A CG1 
2168 C  CG2 A ILE   A 106 ? 0.2801 0.4513 0.3031 -0.0601 -0.0453 -0.0508 106 ILE   A CG2 
2169 C  CG2 B ILE   A 106 ? 0.3356 0.3837 0.3243 -0.0340 -0.0082 -0.0241 106 ILE   A CG2 
2170 C  CD1 A ILE   A 106 ? 0.2750 0.4419 0.3446 -0.0524 -0.0350 -0.0137 106 ILE   A CD1 
2171 C  CD1 B ILE   A 106 ? 0.3345 0.3807 0.3295 -0.0287 -0.0107 -0.0120 106 ILE   A CD1 
2194 N  N   A GLN   A 107 ? 0.2757 0.3736 0.2513 -0.0844 0.0069  -0.1294 107 GLN   A N   
2195 N  N   B GLN   A 107 ? 0.3178 0.3371 0.3171 -0.0467 0.0171  -0.0519 107 GLN   A N   
2196 C  CA  A GLN   A 107 ? 0.3082 0.3543 0.3456 -0.0624 0.0466  -0.1274 107 GLN   A CA  
2197 C  CA  B GLN   A 107 ? 0.3137 0.3201 0.3410 -0.0452 0.0343  -0.0611 107 GLN   A CA  
2198 C  C   A GLN   A 107 ? 0.2812 0.3022 0.3426 -0.0560 0.0672  -0.0875 107 GLN   A C   
2199 C  C   B GLN   A 107 ? 0.2832 0.2880 0.3159 -0.0483 0.0538  -0.0614 107 GLN   A C   
2200 O  O   A GLN   A 107 ? 0.2918 0.3034 0.4208 -0.0568 0.0728  -0.0731 107 GLN   A O   
2201 O  O   B GLN   A 107 ? 0.2881 0.2900 0.3497 -0.0485 0.0551  -0.0526 107 GLN   A O   
2202 C  CB  A GLN   A 107 ? 0.3530 0.3873 0.4333 -0.0704 0.0315  -0.1379 107 GLN   A CB  
2203 C  CB  B GLN   A 107 ? 0.3343 0.3351 0.3904 -0.0479 0.0217  -0.0551 107 GLN   A CB  
2204 C  CG  A GLN   A 107 ? 0.3998 0.4328 0.5469 -0.0705 0.0196  -0.1226 107 GLN   A CG  
2205 C  CG  B GLN   A 107 ? 0.3540 0.3529 0.4475 -0.0500 0.0123  -0.0423 107 GLN   A CG  
2206 C  CD  A GLN   A 107 ? 0.4338 0.4607 0.6366 -0.0745 0.0175  -0.1021 107 GLN   A CD  
2207 C  CD  B GLN   A 107 ? 0.3734 0.3678 0.4938 -0.0491 0.0083  -0.0281 107 GLN   A CD  
2208 O  OE1 A GLN   A 107 ? 0.4474 0.4809 0.6796 -0.0741 0.0171  -0.0960 107 GLN   A OE1 
2209 O  OE1 B GLN   A 107 ? 0.3800 0.3741 0.5090 -0.0506 0.0100  -0.0207 107 GLN   A OE1 
2210 N  NE2 A GLN   A 107 ? 0.4435 0.4696 0.6635 -0.0813 0.0156  -0.0997 107 GLN   A NE2 
2211 N  NE2 B GLN   A 107 ? 0.3771 0.3729 0.5096 -0.0496 0.0035  -0.0235 107 GLN   A NE2 
2228 N  N   . LEU   A 108 ? 0.2454 0.2506 0.2607 -0.0536 0.0659  -0.0742 108 LEU   A N   
2229 C  CA  . LEU   A 108 ? 0.2166 0.2155 0.2247 -0.0214 0.0417  -0.0286 108 LEU   A CA  
2230 C  C   . LEU   A 108 ? 0.1827 0.1902 0.2067 -0.0093 0.0295  0.0075  108 LEU   A C   
2231 O  O   . LEU   A 108 ? 0.1875 0.1801 0.2396 -0.0031 0.0368  0.0032  108 LEU   A O   
2232 C  CB  . LEU   A 108 ? 0.2145 0.2250 0.1840 -0.0212 0.0451  -0.0226 108 LEU   A CB  
2233 C  CG  . LEU   A 108 ? 0.2362 0.2423 0.2286 -0.0253 0.0461  -0.0098 108 LEU   A CG  
2234 C  CD1 . LEU   A 108 ? 0.2643 0.2459 0.2434 -0.0370 0.0573  -0.0102 108 LEU   A CD1 
2235 C  CD2 . LEU   A 108 ? 0.2405 0.2632 0.2916 -0.0091 0.0388  0.0028  108 LEU   A CD2 
2248 N  N   . LEU   A 109 ? 0.1699 0.1803 0.1909 -0.0017 0.0228  0.0119  109 LEU   A N   
2249 C  CA  . LEU   A 109 ? 0.1741 0.1858 0.1659 -0.0040 -0.0026 0.0199  109 LEU   A CA  
2250 C  C   . LEU   A 109 ? 0.1717 0.1823 0.1483 -0.0138 0.0069  -0.0046 109 LEU   A C   
2251 O  O   . LEU   A 109 ? 0.1603 0.1591 0.1844 -0.0091 -0.0080 -0.0005 109 LEU   A O   
2252 C  CB  . LEU   A 109 ? 0.1723 0.1865 0.1907 0.0091  -0.0109 0.0213  109 LEU   A CB  
2253 C  CG  . LEU   A 109 ? 0.1708 0.1927 0.1995 0.0035  0.0065  0.0230  109 LEU   A CG  
2254 C  CD1 . LEU   A 109 ? 0.1634 0.1903 0.2119 -0.0085 0.0127  -0.0053 109 LEU   A CD1 
2255 C  CD2 . LEU   A 109 ? 0.1676 0.2031 0.2299 0.0179  -0.0040 0.0230  109 LEU   A CD2 
2267 N  N   . LYS   A 110 ? 0.1747 0.1846 0.1414 -0.0070 -0.0127 0.0107  110 LYS   A N   
2268 C  CA  . LYS   A 110 ? 0.1787 0.1921 0.1487 -0.0098 -0.0154 0.0052  110 LYS   A CA  
2269 C  C   . LYS   A 110 ? 0.1832 0.1730 0.1270 -0.0104 0.0026  -0.0040 110 LYS   A C   
2270 O  O   . LYS   A 110 ? 0.1573 0.1436 0.1611 -0.0145 0.0037  -0.0038 110 LYS   A O   
2271 C  CB  . LYS   A 110 ? 0.1757 0.1962 0.1829 -0.0178 -0.0254 0.0030  110 LYS   A CB  
2272 C  CG  . LYS   A 110 ? 0.1812 0.1906 0.1839 -0.0141 -0.0123 0.0003  110 LYS   A CG  
2273 C  CD  . LYS   A 110 ? 0.1861 0.1879 0.2079 -0.0224 -0.0067 -0.0047 110 LYS   A CD  
2274 C  CE  . LYS   A 110 ? 0.2012 0.1977 0.2216 -0.0315 0.0140  0.0055  110 LYS   A CE  
2275 N  NZ  . LYS   A 110 ? 0.2013 0.1918 0.2364 -0.0440 0.0175  -0.0037 110 LYS   A NZ  
2289 N  N   . SER   A 111 ? 0.1950 0.1528 0.1444 -0.0019 -0.0133 0.0118  111 SER   A N   
2290 C  CA  . SER   A 111 ? 0.1840 0.1655 0.1438 0.0022  -0.0083 0.0079  111 SER   A CA  
2291 C  C   . SER   A 111 ? 0.1570 0.1647 0.1491 -0.0023 0.0006  0.0120  111 SER   A C   
2292 O  O   . SER   A 111 ? 0.1607 0.1474 0.1810 -0.0030 0.0100  0.0170  111 SER   A O   
2293 C  CB  . SER   A 111 ? 0.2005 0.1814 0.1671 0.0051  0.0209  -0.0095 111 SER   A CB  
2294 O  OG  . SER   A 111 ? 0.2332 0.1947 0.1923 0.0014  0.0279  -0.0143 111 SER   A OG  
2300 N  N   . ALA   A 112 ? 0.1518 0.1664 0.1710 0.0055  0.0054  -0.0063 112 ALA   A N   
2301 C  CA  . ALA   A 112 ? 0.1445 0.1591 0.1543 -0.0017 0.0080  0.0142  112 ALA   A CA  
2302 C  C   . ALA   A 112 ? 0.1285 0.1442 0.1704 0.0091  0.0044  -0.0012 112 ALA   A C   
2303 O  O   . ALA   A 112 ? 0.1467 0.1484 0.1647 -0.0084 0.0133  0.0012  112 ALA   A O   
2304 C  CB  . ALA   A 112 ? 0.1673 0.1571 0.1681 -0.0115 0.0058  0.0110  112 ALA   A CB  
2310 N  N   . TYR   A 113 ? 0.1229 0.1491 0.1937 -0.0030 0.0003  0.0143  113 TYR   A N   
2311 C  CA  . TYR   A 113 ? 0.1282 0.1384 0.1732 -0.0057 -0.0032 0.0128  113 TYR   A CA  
2312 C  C   . TYR   A 113 ? 0.1318 0.1493 0.1662 -0.0176 0.0035  0.0081  113 TYR   A C   
2313 O  O   . TYR   A 113 ? 0.1457 0.1511 0.1794 -0.0012 0.0064  0.0052  113 TYR   A O   
2314 C  CB  . TYR   A 113 ? 0.1427 0.1660 0.1798 -0.0003 -0.0122 0.0068  113 TYR   A CB  
2315 C  CG  . TYR   A 113 ? 0.1373 0.1566 0.1598 -0.0211 -0.0024 0.0161  113 TYR   A CG  
2316 C  CD1 . TYR   A 113 ? 0.1387 0.1850 0.1628 -0.0104 -0.0047 0.0166  113 TYR   A CD1 
2317 C  CD2 . TYR   A 113 ? 0.1450 0.1539 0.1866 -0.0141 -0.0014 0.0108  113 TYR   A CD2 
2318 C  CE1 . TYR   A 113 ? 0.1431 0.1996 0.1461 -0.0121 0.0042  0.0145  113 TYR   A CE1 
2319 C  CE2 . TYR   A 113 ? 0.1510 0.1638 0.1703 -0.0113 -0.0143 0.0219  113 TYR   A CE2 
2320 C  CZ  . TYR   A 113 ? 0.1474 0.1806 0.1514 0.0004  0.0114  0.0226  113 TYR   A CZ  
2321 O  OH  . TYR   A 113 ? 0.1488 0.1884 0.1826 0.0088  0.0065  0.0223  113 TYR   A OH  
2331 N  N   . GLU   A 114 ? 0.1227 0.1394 0.1818 -0.0057 0.0095  0.0123  114 GLU   A N   
2332 C  CA  . GLU   A 114 ? 0.1487 0.1192 0.1685 0.0039  0.0187  0.0139  114 GLU   A CA  
2333 C  C   . GLU   A 114 ? 0.1535 0.1352 0.1493 -0.0021 0.0085  -0.0048 114 GLU   A C   
2334 O  O   . GLU   A 114 ? 0.1533 0.1668 0.1462 0.0010  -0.0004 0.0089  114 GLU   A O   
2335 C  CB  . GLU   A 114 ? 0.1444 0.1281 0.1678 -0.0051 0.0066  0.0028  114 GLU   A CB  
2336 C  CG  . GLU   A 114 ? 0.1508 0.1261 0.1887 -0.0030 0.0216  0.0002  114 GLU   A CG  
2337 C  CD  . GLU   A 114 ? 0.1667 0.1253 0.1948 -0.0104 0.0017  -0.0057 114 GLU   A CD  
2338 O  OE1 . GLU   A 114 ? 0.1735 0.1419 0.1980 -0.0089 0.0154  -0.0136 114 GLU   A OE1 
2339 O  OE2 . GLU   A 114 ? 0.1819 0.1458 0.2126 -0.0071 0.0226  -0.0141 114 GLU   A OE2 
2346 N  N   . ASN   A 115 ? 0.1403 0.1342 0.1601 -0.0037 0.0112  -0.0042 115 ASN   A N   
2347 C  CA  . ASN   A 115 ? 0.1452 0.1588 0.1578 -0.0120 0.0032  -0.0103 115 ASN   A CA  
2348 C  C   . ASN   A 115 ? 0.1420 0.1714 0.1281 -0.0083 0.0030  0.0100  115 ASN   A C   
2349 O  O   . ASN   A 115 ? 0.1427 0.1631 0.1683 -0.0110 0.0120  0.0142  115 ASN   A O   
2350 C  CB  . ASN   A 115 ? 0.1568 0.1500 0.1576 -0.0156 0.0113  0.0086  115 ASN   A CB  
2351 C  CG  . ASN   A 115 ? 0.1515 0.1810 0.1718 -0.0161 0.0134  -0.0065 115 ASN   A CG  
2352 O  OD1 . ASN   A 115 ? 0.1558 0.2709 0.1860 -0.0145 0.0202  0.0271  115 ASN   A OD1 
2353 N  ND2 . ASN   A 115 ? 0.1336 0.1670 0.1772 -0.0164 0.0196  0.0072  115 ASN   A ND2 
2360 N  N   . PHE   A 116 ? 0.1285 0.1733 0.1529 -0.0013 0.0148  0.0086  116 PHE   A N   
2361 C  CA  . PHE   A 116 ? 0.1310 0.1929 0.1252 0.0000  0.0115  0.0236  116 PHE   A CA  
2362 C  C   . PHE   A 116 ? 0.1528 0.1955 0.1318 0.0033  0.0190  0.0135  116 PHE   A C   
2363 O  O   . PHE   A 116 ? 0.1551 0.1629 0.1607 0.0053  0.0112  0.0247  116 PHE   A O   
2364 C  CB  . PHE   A 116 ? 0.1207 0.1873 0.1580 -0.0037 0.0192  0.0258  116 PHE   A CB  
2365 C  CG  . PHE   A 116 ? 0.1250 0.1601 0.1489 0.0050  0.0132  0.0262  116 PHE   A CG  
2366 C  CD1 . PHE   A 116 ? 0.1290 0.1652 0.1520 0.0031  0.0143  0.0216  116 PHE   A CD1 
2367 C  CD2 . PHE   A 116 ? 0.1391 0.1701 0.1568 0.0029  0.0107  0.0099  116 PHE   A CD2 
2368 C  CE1 . PHE   A 116 ? 0.1502 0.1525 0.1566 -0.0134 0.0097  0.0152  116 PHE   A CE1 
2369 C  CE2 . PHE   A 116 ? 0.1284 0.1634 0.1884 0.0020  -0.0057 0.0164  116 PHE   A CE2 
2370 C  CZ  . PHE   A 116 ? 0.1513 0.1496 0.1697 0.0006  0.0136  0.0261  116 PHE   A CZ  
2380 N  N   . ASN   A 117 ? 0.1454 0.1858 0.1441 -0.0059 0.0200  0.0327  117 ASN   A N   
2381 C  CA  . ASN   A 117 ? 0.1816 0.1808 0.1552 0.0058  0.0078  0.0364  117 ASN   A CA  
2382 C  C   . ASN   A 117 ? 0.1774 0.1598 0.1785 0.0118  0.0125  0.0236  117 ASN   A C   
2383 O  O   . ASN   A 117 ? 0.1677 0.1654 0.2158 -0.0086 -0.0037 0.0393  117 ASN   A O   
2384 C  CB  . ASN   A 117 ? 0.1842 0.1752 0.1588 -0.0005 -0.0008 0.0167  117 ASN   A CB  
2385 C  CG  . ASN   A 117 ? 0.1706 0.1729 0.1845 0.0004  -0.0101 -0.0033 117 ASN   A CG  
2386 O  OD1 . ASN   A 117 ? 0.1817 0.1802 0.1780 -0.0002 0.0154  0.0164  117 ASN   A OD1 
2387 N  ND2 . ASN   A 117 ? 0.1585 0.1397 0.2102 -0.0005 -0.0031 0.0122  117 ASN   A ND2 
2394 N  N   . GLN   A 118 ? 0.1658 0.1571 0.1827 -0.0012 0.0040  0.0241  118 GLN   A N   
2395 C  CA  . GLN   A 118 ? 0.1776 0.1722 0.1746 -0.0075 -0.0086 0.0386  118 GLN   A CA  
2396 C  C   . GLN   A 118 ? 0.1678 0.1739 0.1535 0.0018  0.0060  0.0381  118 GLN   A C   
2397 O  O   . GLN   A 118 ? 0.1706 0.2119 0.2110 0.0089  -0.0174 0.0139  118 GLN   A O   
2398 C  CB  . GLN   A 118 ? 0.1799 0.1713 0.1856 -0.0051 0.0154  0.0370  118 GLN   A CB  
2399 C  CG  . GLN   A 118 ? 0.1545 0.1828 0.1916 -0.0015 0.0041  0.0348  118 GLN   A CG  
2400 C  CD  . GLN   A 118 ? 0.1493 0.1849 0.2128 -0.0053 -0.0099 0.0310  118 GLN   A CD  
2401 O  OE1 . GLN   A 118 ? 0.1438 0.1939 0.2324 0.0082  -0.0045 0.0105  118 GLN   A OE1 
2402 N  NE2 . GLN   A 118 ? 0.1740 0.1759 0.2190 -0.0010 0.0072  0.0321  118 GLN   A NE2 
2411 N  N   . HIS   A 119 ? 0.1693 0.1742 0.1516 0.0074  0.0191  0.0283  119 HIS   A N   
2412 C  CA  . HIS   A 119 ? 0.1847 0.1836 0.1733 0.0031  0.0134  0.0429  119 HIS   A CA  
2413 C  C   . HIS   A 119 ? 0.2082 0.1923 0.1668 -0.0078 0.0178  0.0481  119 HIS   A C   
2414 O  O   . HIS   A 119 ? 0.2131 0.2100 0.1684 -0.0288 0.0028  0.0397  119 HIS   A O   
2415 C  CB  . HIS   A 119 ? 0.1881 0.1814 0.1769 0.0008  0.0174  0.0345  119 HIS   A CB  
2416 C  CG  . HIS   A 119 ? 0.1821 0.1830 0.2362 -0.0024 0.0161  0.0417  119 HIS   A CG  
2417 N  ND1 . HIS   A 119 ? 0.2081 0.2033 0.3058 -0.0048 0.0166  0.0390  119 HIS   A ND1 
2418 C  CD2 . HIS   A 119 ? 0.1682 0.1925 0.2651 0.0073  0.0310  0.0566  119 HIS   A CD2 
2419 C  CE1 . HIS   A 119 ? 0.1925 0.2090 0.3221 -0.0056 0.0274  0.0643  119 HIS   A CE1 
2420 N  NE2 . HIS   A 119 ? 0.1901 0.1979 0.3201 -0.0022 0.0482  0.0685  119 HIS   A NE2 
2428 N  N   . GLU   A 120 ? 0.2025 0.2096 0.1840 -0.0076 0.0038  0.0648  120 GLU   A N   
2429 C  CA  . GLU   A 120 ? 0.2417 0.2355 0.1825 -0.0027 0.0051  0.0881  120 GLU   A CA  
2430 C  C   . GLU   A 120 ? 0.2128 0.2154 0.1726 -0.0095 0.0137  0.0817  120 GLU   A C   
2431 O  O   . GLU   A 120 ? 0.2091 0.2055 0.1849 -0.0048 0.0100  0.0672  120 GLU   A O   
2432 C  CB  . GLU   A 120 ? 0.3186 0.3210 0.2543 0.0158  0.0146  0.1349  120 GLU   A CB  
2433 C  CG  . GLU   A 120 ? 0.4211 0.4202 0.3913 0.0309  0.0106  0.1317  120 GLU   A CG  
2434 C  CD  . GLU   A 120 ? 0.5206 0.5187 0.5508 0.0414  0.0156  0.1189  120 GLU   A CD  
2435 O  OE1 . GLU   A 120 ? 0.5516 0.5345 0.5737 0.0440  0.0121  0.1142  120 GLU   A OE1 
2436 O  OE2 . GLU   A 120 ? 0.6151 0.6151 0.6271 0.0449  0.0199  0.1152  120 GLU   A OE2 
2443 N  N   . VAL   A 121 ? 0.2064 0.2231 0.1544 -0.0081 0.0170  0.0547  121 VAL   A N   
2444 C  CA  . VAL   A 121 ? 0.2084 0.2231 0.1517 -0.0097 0.0206  0.0515  121 VAL   A CA  
2445 C  C   . VAL   A 121 ? 0.1932 0.2024 0.1366 -0.0239 0.0117  0.0387  121 VAL   A C   
2446 O  O   . VAL   A 121 ? 0.1922 0.2071 0.1599 -0.0245 0.0031  0.0355  121 VAL   A O   
2447 C  CB  . VAL   A 121 ? 0.2487 0.2620 0.1915 0.0125  0.0385  0.0601  121 VAL   A CB  
2448 C  CG1 . VAL   A 121 ? 0.2529 0.2772 0.1884 0.0233  0.0476  0.0592  121 VAL   A CG1 
2449 C  CG2 . VAL   A 121 ? 0.2687 0.2798 0.2544 -0.0011 0.0331  0.0365  121 VAL   A CG2 
2459 N  N   . LEU   A 122 ? 0.1804 0.1821 0.1567 -0.0271 0.0029  0.0390  122 LEU   A N   
2460 C  CA  . LEU   A 122 ? 0.2010 0.1718 0.1573 -0.0233 0.0272  0.0354  122 LEU   A CA  
2461 C  C   . LEU   A 122 ? 0.1976 0.1573 0.1421 -0.0330 0.0226  0.0262  122 LEU   A C   
2462 O  O   . LEU   A 122 ? 0.1998 0.1727 0.1800 -0.0440 0.0094  0.0309  122 LEU   A O   
2463 C  CB  . LEU   A 122 ? 0.2040 0.1742 0.1903 -0.0120 0.0237  0.0542  122 LEU   A CB  
2464 C  CG  . LEU   A 122 ? 0.1918 0.1842 0.1854 -0.0170 0.0319  0.0080  122 LEU   A CG  
2465 C  CD1 . LEU   A 122 ? 0.2232 0.2057 0.1687 -0.0309 0.0246  0.0194  122 LEU   A CD1 
2466 C  CD2 . LEU   A 122 ? 0.1944 0.1662 0.1803 -0.0118 0.0411  0.0097  122 LEU   A CD2 
2478 N  N   . LEU   A 123 ? 0.1823 0.1629 0.1457 -0.0271 0.0024  0.0335  123 LEU   A N   
2479 C  CA  . LEU   A 123 ? 0.1748 0.1747 0.1457 -0.0196 0.0129  0.0211  123 LEU   A CA  
2480 C  C   . LEU   A 123 ? 0.1674 0.1647 0.1391 0.0003  0.0148  0.0337  123 LEU   A C   
2481 O  O   . LEU   A 123 ? 0.1687 0.1700 0.1510 -0.0154 0.0040  0.0300  123 LEU   A O   
2482 C  CB  . LEU   A 123 ? 0.1832 0.1845 0.1453 -0.0287 0.0283  0.0243  123 LEU   A CB  
2483 C  CG  . LEU   A 123 ? 0.1925 0.1911 0.1495 -0.0205 0.0128  0.0101  123 LEU   A CG  
2484 C  CD1 . LEU   A 123 ? 0.1932 0.1978 0.1776 -0.0147 0.0076  0.0048  123 LEU   A CD1 
2485 C  CD2 . LEU   A 123 ? 0.2166 0.2042 0.1626 -0.0111 0.0143  0.0081  123 LEU   A CD2 
2497 N  N   . ALA   A 124 ? 0.1571 0.1602 0.1426 -0.0150 0.0057  0.0274  124 ALA   A N   
2498 C  CA  . ALA   A 124 ? 0.1583 0.1656 0.1388 -0.0041 -0.0079 0.0262  124 ALA   A CA  
2499 C  C   . ALA   A 124 ? 0.1704 0.1609 0.1422 -0.0046 0.0150  0.0201  124 ALA   A C   
2500 O  O   . ALA   A 124 ? 0.1670 0.1730 0.1585 -0.0072 0.0155  0.0239  124 ALA   A O   
2501 C  CB  . ALA   A 124 ? 0.1544 0.1690 0.1626 0.0115  0.0013  0.0298  124 ALA   A CB  
2507 N  N   . PRO   A 125 ? 0.1556 0.1591 0.1499 -0.0014 -0.0019 0.0229  125 PRO   A N   
2508 C  CA  . PRO   A 125 ? 0.1666 0.1708 0.1510 -0.0025 -0.0062 0.0336  125 PRO   A CA  
2509 C  C   . PRO   A 125 ? 0.1622 0.1813 0.1591 -0.0066 0.0066  0.0189  125 PRO   A C   
2510 O  O   . PRO   A 125 ? 0.1542 0.1656 0.1671 -0.0136 0.0036  0.0171  125 PRO   A O   
2511 C  CB  . PRO   A 125 ? 0.1629 0.1664 0.1501 -0.0085 0.0064  0.0366  125 PRO   A CB  
2512 C  CG  . PRO   A 125 ? 0.1687 0.1685 0.1480 -0.0066 0.0136  0.0334  125 PRO   A CG  
2513 C  CD  . PRO   A 125 ? 0.1674 0.1510 0.1591 -0.0226 0.0183  0.0259  125 PRO   A CD  
2521 N  N   . LEU   A 126 ? 0.1640 0.1918 0.1556 0.0033  0.0073  0.0121  126 LEU   A N   
2522 C  CA  . LEU   A 126 ? 0.1550 0.1821 0.1535 -0.0041 0.0089  0.0216  126 LEU   A CA  
2523 C  C   . LEU   A 126 ? 0.1532 0.1823 0.1361 -0.0097 0.0154  0.0243  126 LEU   A C   
2524 O  O   . LEU   A 126 ? 0.1828 0.1671 0.1819 -0.0021 0.0317  0.0233  126 LEU   A O   
2525 C  CB  . LEU   A 126 ? 0.1712 0.2067 0.1681 -0.0228 0.0137  0.0219  126 LEU   A CB  
2526 C  CG  . LEU   A 126 ? 0.1828 0.2286 0.1884 -0.0174 0.0104  0.0115  126 LEU   A CG  
2527 C  CD1 . LEU   A 126 ? 0.1864 0.2475 0.2360 -0.0110 0.0036  0.0037  126 LEU   A CD1 
2528 C  CD2 . LEU   A 126 ? 0.1954 0.2293 0.2098 -0.0326 -0.0073 0.0393  126 LEU   A CD2 
2540 N  N   . LEU   A 127 ? 0.1580 0.1825 0.1491 -0.0021 0.0066  0.0250  127 LEU   A N   
2541 C  CA  . LEU   A 127 ? 0.1578 0.1818 0.1396 0.0001  -0.0053 0.0240  127 LEU   A CA  
2542 C  C   . LEU   A 127 ? 0.1430 0.1508 0.1388 0.0017  0.0000  0.0097  127 LEU   A C   
2543 O  O   . LEU   A 127 ? 0.1638 0.1483 0.1632 -0.0107 -0.0037 0.0180  127 LEU   A O   
2544 C  CB  . LEU   A 127 ? 0.1568 0.2201 0.1560 0.0029  0.0072  0.0306  127 LEU   A CB  
2545 C  CG  . LEU   A 127 ? 0.1502 0.2412 0.1688 0.0148  -0.0131 0.0392  127 LEU   A CG  
2546 C  CD1 . LEU   A 127 ? 0.1540 0.2250 0.1962 0.0236  0.0018  0.0451  127 LEU   A CD1 
2547 C  CD2 . LEU   A 127 ? 0.1761 0.2637 0.1853 -0.0024 -0.0150 0.0350  127 LEU   A CD2 
2559 N  N   . SER   A 128 ? 0.1513 0.1571 0.1384 -0.0064 -0.0006 0.0109  128 SER   A N   
2560 C  CA  . SER   A 128 ? 0.1656 0.1563 0.1298 -0.0078 -0.0076 0.0119  128 SER   A CA  
2561 C  C   . SER   A 128 ? 0.1697 0.1672 0.1407 -0.0063 -0.0109 0.0053  128 SER   A C   
2562 O  O   . SER   A 128 ? 0.1762 0.1740 0.1738 -0.0048 -0.0250 0.0009  128 SER   A O   
2563 C  CB  . SER   A 128 ? 0.1555 0.1813 0.1252 -0.0043 -0.0070 0.0168  128 SER   A CB  
2564 O  OG  . SER   A 128 ? 0.1652 0.1863 0.1436 -0.0152 0.0017  0.0155  128 SER   A OG  
2570 N  N   . ALA   A 129 ? 0.1569 0.1834 0.1773 0.0020  -0.0066 0.0227  129 ALA   A N   
2571 C  CA  . ALA   A 129 ? 0.1598 0.1793 0.1932 -0.0033 0.0035  0.0330  129 ALA   A CA  
2572 C  C   . ALA   A 129 ? 0.1800 0.1746 0.1776 -0.0055 0.0041  0.0203  129 ALA   A C   
2573 O  O   . ALA   A 129 ? 0.1822 0.1721 0.1719 -0.0002 0.0049  0.0217  129 ALA   A O   
2574 C  CB  . ALA   A 129 ? 0.1572 0.1936 0.2648 0.0102  0.0053  0.0425  129 ALA   A CB  
2580 N  N   . GLY   A 130 ? 0.1824 0.1701 0.2011 -0.0088 -0.0181 0.0082  130 GLY   A N   
2581 C  CA  . GLY   A 130 ? 0.1943 0.1683 0.2038 0.0014  -0.0159 0.0134  130 GLY   A CA  
2582 C  C   . GLY   A 130 ? 0.1934 0.1615 0.1941 0.0064  -0.0109 0.0039  130 GLY   A C   
2583 O  O   . GLY   A 130 ? 0.1948 0.1679 0.1939 0.0112  -0.0288 -0.0024 130 GLY   A O   
2587 N  N   . ILE   A 131 ? 0.2011 0.1494 0.1897 0.0009  -0.0154 0.0158  131 ILE   A N   
2588 C  CA  . ILE   A 131 ? 0.2081 0.1733 0.1577 -0.0134 -0.0363 0.0018  131 ILE   A CA  
2589 C  C   . ILE   A 131 ? 0.2150 0.1649 0.1434 -0.0086 -0.0277 0.0236  131 ILE   A C   
2590 O  O   . ILE   A 131 ? 0.2146 0.1690 0.1692 0.0062  -0.0270 0.0296  131 ILE   A O   
2591 C  CB  . ILE   A 131 ? 0.2300 0.1907 0.1914 -0.0148 -0.0385 -0.0139 131 ILE   A CB  
2592 C  CG1 . ILE   A 131 ? 0.2379 0.2222 0.2169 -0.0209 -0.0440 -0.0216 131 ILE   A CG1 
2593 C  CG2 . ILE   A 131 ? 0.2450 0.1671 0.2023 -0.0124 -0.0128 -0.0192 131 ILE   A CG2 
2594 C  CD1 . ILE   A 131 ? 0.2489 0.2432 0.2592 -0.0297 -0.0482 -0.0180 131 ILE   A CD1 
2606 N  N   . PHE   A 132 ? 0.2018 0.1635 0.1561 -0.0045 -0.0147 0.0274  132 PHE   A N   
2607 C  CA  . PHE   A 132 ? 0.1898 0.1757 0.1455 -0.0018 -0.0179 0.0073  132 PHE   A CA  
2608 C  C   . PHE   A 132 ? 0.1978 0.1891 0.1417 0.0079  -0.0240 0.0149  132 PHE   A C   
2609 O  O   . PHE   A 132 ? 0.2014 0.2162 0.1668 -0.0041 -0.0152 -0.0053 132 PHE   A O   
2610 C  CB  . PHE   A 132 ? 0.1977 0.1711 0.1267 -0.0041 -0.0335 0.0233  132 PHE   A CB  
2611 C  CG  . PHE   A 132 ? 0.2072 0.1728 0.1160 0.0030  -0.0255 0.0186  132 PHE   A CG  
2612 C  CD1 . PHE   A 132 ? 0.2094 0.1824 0.1389 0.0107  -0.0213 -0.0020 132 PHE   A CD1 
2613 C  CD2 . PHE   A 132 ? 0.2020 0.1767 0.1545 0.0036  -0.0196 0.0022  132 PHE   A CD2 
2614 C  CE1 . PHE   A 132 ? 0.2135 0.1890 0.1627 0.0195  -0.0384 -0.0040 132 PHE   A CE1 
2615 C  CE2 . PHE   A 132 ? 0.2012 0.1944 0.1568 0.0126  -0.0230 -0.0035 132 PHE   A CE2 
2616 C  CZ  . PHE   A 132 ? 0.1966 0.1848 0.1698 0.0080  -0.0377 0.0008  132 PHE   A CZ  
2626 N  N   . GLY   A 133 ? 0.2047 0.2021 0.1408 0.0065  -0.0395 0.0222  133 GLY   A N   
2627 C  CA  . GLY   A 133 ? 0.2064 0.2129 0.1632 -0.0044 -0.0440 0.0086  133 GLY   A CA  
2628 C  C   . GLY   A 133 ? 0.2167 0.2159 0.1511 -0.0014 -0.0508 -0.0020 133 GLY   A C   
2629 O  O   . GLY   A 133 ? 0.2580 0.2200 0.1723 0.0009  -0.0505 -0.0210 133 GLY   A O   
2633 N  N   . ALA   A 134 ? 0.2085 0.2048 0.1581 -0.0164 -0.0245 -0.0030 134 ALA   A N   
2634 C  CA  . ALA   A 134 ? 0.1886 0.2001 0.1788 -0.0060 -0.0346 -0.0082 134 ALA   A CA  
2635 C  C   . ALA   A 134 ? 0.1984 0.2008 0.1816 -0.0066 -0.0342 -0.0080 134 ALA   A C   
2636 O  O   . ALA   A 134 ? 0.2218 0.2164 0.2217 0.0025  -0.0124 -0.0039 134 ALA   A O   
2637 C  CB  . ALA   A 134 ? 0.1898 0.1961 0.2274 -0.0062 -0.0386 -0.0005 134 ALA   A CB  
2643 N  N   . ASP   A 135 ? 0.2229 0.2091 0.2043 -0.0125 -0.0403 0.0015  135 ASP   A N   
2644 C  CA  . ASP   A 135 ? 0.2171 0.2267 0.2462 -0.0280 -0.0522 0.0223  135 ASP   A CA  
2645 C  C   . ASP   A 135 ? 0.1897 0.2175 0.2431 -0.0231 -0.0421 0.0308  135 ASP   A C   
2646 O  O   . ASP   A 135 ? 0.1917 0.2039 0.2512 -0.0262 -0.0294 0.0485  135 ASP   A O   
2647 C  CB  . ASP   A 135 ? 0.2465 0.2747 0.2975 -0.0681 -0.0740 0.0167  135 ASP   A CB  
2648 C  CG  . ASP   A 135 ? 0.2763 0.3285 0.3609 -0.0878 -0.0774 0.0200  135 ASP   A CG  
2649 O  OD1 . ASP   A 135 ? 0.2632 0.3490 0.3479 -0.0850 -0.0855 0.0636  135 ASP   A OD1 
2650 O  OD2 . ASP   A 135 ? 0.3128 0.3639 0.4570 -0.0895 -0.0322 0.0113  135 ASP   A OD2 
2655 N  N   . PRO   A 136 ? 0.1792 0.2061 0.2450 -0.0041 -0.0369 0.0515  136 PRO   A N   
2656 C  CA  . PRO   A 136 ? 0.1818 0.2039 0.2543 -0.0175 -0.0120 0.0307  136 PRO   A CA  
2657 C  C   . PRO   A 136 ? 0.1638 0.2062 0.2298 -0.0006 -0.0190 0.0278  136 PRO   A C   
2658 O  O   . PRO   A 136 ? 0.1648 0.1905 0.2156 0.0036  -0.0083 0.0254  136 PRO   A O   
2659 C  CB  . PRO   A 136 ? 0.1896 0.2070 0.2997 -0.0064 -0.0144 0.0344  136 PRO   A CB  
2660 C  CG  . PRO   A 136 ? 0.2084 0.2348 0.3252 0.0135  -0.0076 0.0288  136 PRO   A CG  
2661 C  CD  . PRO   A 136 ? 0.1926 0.2295 0.3019 0.0166  -0.0044 0.0478  136 PRO   A CD  
2669 N  N   . ILE   A 137 ? 0.1598 0.2085 0.2397 -0.0030 -0.0370 0.0291  137 ILE   A N   
2670 C  CA  . ILE   A 137 ? 0.1651 0.2256 0.2386 -0.0108 -0.0317 0.0407  137 ILE   A CA  
2671 C  C   . ILE   A 137 ? 0.1659 0.2341 0.2172 -0.0123 -0.0229 0.0380  137 ILE   A C   
2672 O  O   . ILE   A 137 ? 0.1845 0.2156 0.2203 -0.0221 -0.0074 0.0366  137 ILE   A O   
2673 C  CB  . ILE   A 137 ? 0.1843 0.2306 0.2974 -0.0184 -0.0468 0.0407  137 ILE   A CB  
2674 C  CG1 . ILE   A 137 ? 0.1873 0.2637 0.3747 -0.0058 -0.0773 0.0454  137 ILE   A CG1 
2675 C  CG2 . ILE   A 137 ? 0.1964 0.2324 0.3116 -0.0229 -0.0595 0.0347  137 ILE   A CG2 
2676 C  CD1 . ILE   A 137 ? 0.2188 0.2803 0.4228 0.0053  -0.0578 0.0442  137 ILE   A CD1 
2688 N  N   . HIS   A 138 ? 0.1687 0.2346 0.2067 -0.0033 0.0005  0.0284  138 HIS   A N   
2689 C  CA  . HIS   A 138 ? 0.1771 0.2466 0.1891 -0.0081 0.0001  0.0087  138 HIS   A CA  
2690 C  C   . HIS   A 138 ? 0.1684 0.2303 0.1874 -0.0055 -0.0170 0.0110  138 HIS   A C   
2691 O  O   . HIS   A 138 ? 0.1600 0.2285 0.1930 -0.0150 -0.0059 0.0178  138 HIS   A O   
2692 C  CB  . HIS   A 138 ? 0.2009 0.2452 0.1879 0.0023  -0.0154 -0.0061 138 HIS   A CB  
2693 C  CG  . HIS   A 138 ? 0.2182 0.2562 0.1939 -0.0055 -0.0147 -0.0228 138 HIS   A CG  
2694 N  ND1 . HIS   A 138 ? 0.2254 0.2630 0.2220 -0.0091 -0.0125 -0.0329 138 HIS   A ND1 
2695 C  CD2 . HIS   A 138 ? 0.2129 0.2574 0.2086 -0.0088 -0.0206 0.0037  138 HIS   A CD2 
2696 C  CE1 . HIS   A 138 ? 0.2331 0.2753 0.2267 0.0004  -0.0232 -0.0172 138 HIS   A CE1 
2697 N  NE2 . HIS   A 138 ? 0.2168 0.2731 0.1982 -0.0057 -0.0145 -0.0074 138 HIS   A NE2 
2705 N  N   . SER   A 139 ? 0.1709 0.2011 0.1846 -0.0020 -0.0103 0.0374  139 SER   A N   
2706 C  CA  . SER   A 139 ? 0.1680 0.1909 0.1726 -0.0097 0.0031  0.0353  139 SER   A CA  
2707 C  C   . SER   A 139 ? 0.1643 0.1778 0.1815 -0.0110 0.0070  0.0219  139 SER   A C   
2708 O  O   . SER   A 139 ? 0.1615 0.1838 0.1947 -0.0202 -0.0065 0.0324  139 SER   A O   
2709 C  CB  . SER   A 139 ? 0.1797 0.1902 0.1845 -0.0123 -0.0139 0.0350  139 SER   A CB  
2710 O  OG  . SER   A 139 ? 0.1808 0.1877 0.1862 -0.0226 -0.0221 0.0366  139 SER   A OG  
2716 N  N   . LEU   A 140 ? 0.1591 0.1847 0.1904 0.0012  0.0112  0.0390  140 LEU   A N   
2717 C  CA  . LEU   A 140 ? 0.1613 0.1741 0.1886 -0.0017 0.0120  0.0248  140 LEU   A CA  
2718 C  C   . LEU   A 140 ? 0.1546 0.1845 0.1846 -0.0075 0.0109  0.0368  140 LEU   A C   
2719 O  O   . LEU   A 140 ? 0.1447 0.1909 0.2181 -0.0053 0.0138  0.0414  140 LEU   A O   
2720 C  CB  . LEU   A 140 ? 0.1464 0.1874 0.2120 -0.0003 0.0186  0.0137  140 LEU   A CB  
2721 C  CG  . LEU   A 140 ? 0.1433 0.1967 0.2122 -0.0104 0.0158  0.0285  140 LEU   A CG  
2722 C  CD1 . LEU   A 140 ? 0.1530 0.1901 0.2189 -0.0002 0.0059  0.0180  140 LEU   A CD1 
2723 C  CD2 . LEU   A 140 ? 0.1595 0.2222 0.2249 -0.0069 0.0144  0.0404  140 LEU   A CD2 
2735 N  N   . ARG   A 141 ? 0.1705 0.1947 0.1939 -0.0114 0.0050  0.0244  141 ARG   A N   
2736 C  CA  . ARG   A 141 ? 0.1802 0.2086 0.1943 -0.0185 -0.0104 0.0175  141 ARG   A CA  
2737 C  C   . ARG   A 141 ? 0.1827 0.1774 0.1903 -0.0094 -0.0101 0.0204  141 ARG   A C   
2738 O  O   . ARG   A 141 ? 0.1650 0.1836 0.2110 -0.0226 0.0144  0.0143  141 ARG   A O   
2739 C  CB  . ARG   A 141 ? 0.1800 0.2343 0.2383 -0.0305 -0.0215 -0.0141 141 ARG   A CB  
2740 C  CG  . ARG   A 141 ? 0.2122 0.2671 0.3061 -0.0364 -0.0180 -0.0211 141 ARG   A CG  
2741 C  CD  . ARG   A 141 ? 0.2502 0.2841 0.3638 -0.0403 -0.0151 -0.0238 141 ARG   A CD  
2742 N  NE  . ARG   A 141 ? 0.2426 0.3096 0.3764 -0.0304 -0.0278 -0.0152 141 ARG   A NE  
2743 C  CZ  . ARG   A 141 ? 0.2291 0.3310 0.3860 -0.0313 -0.0247 -0.0220 141 ARG   A CZ  
2744 N  NH1 . ARG   A 141 ? 0.2014 0.3290 0.3853 -0.0335 -0.0193 -0.0419 141 ARG   A NH1 
2745 N  NH2 . ARG   A 141 ? 0.2556 0.3467 0.4088 -0.0259 -0.0304 -0.0121 141 ARG   A NH2 
2759 N  N   . VAL   A 142 ? 0.1692 0.1708 0.1747 -0.0071 -0.0110 0.0147  142 VAL   A N   
2760 C  CA  . VAL   A 142 ? 0.1698 0.1791 0.1777 -0.0060 0.0105  0.0062  142 VAL   A CA  
2761 C  C   . VAL   A 142 ? 0.1466 0.1712 0.1724 -0.0266 0.0019  -0.0023 142 VAL   A C   
2762 O  O   . VAL   A 142 ? 0.1699 0.1742 0.1969 -0.0027 0.0122  0.0067  142 VAL   A O   
2763 C  CB  . VAL   A 142 ? 0.1795 0.1967 0.1587 -0.0059 0.0097  0.0124  142 VAL   A CB  
2764 C  CG1 . VAL   A 142 ? 0.1783 0.1904 0.1854 -0.0076 0.0189  0.0069  142 VAL   A CG1 
2765 C  CG2 . VAL   A 142 ? 0.1847 0.2122 0.1876 -0.0002 0.0212  0.0258  142 VAL   A CG2 
2775 N  N   . CYS   A 143 ? 0.1591 0.1726 0.1652 -0.0194 -0.0064 0.0070  143 CYS   A N   
2776 C  CA  . CYS   A 143 ? 0.1566 0.1892 0.1609 -0.0187 0.0135  0.0067  143 CYS   A CA  
2777 C  C   . CYS   A 143 ? 0.1570 0.1797 0.1755 -0.0243 -0.0039 0.0262  143 CYS   A C   
2778 O  O   . CYS   A 143 ? 0.1625 0.1512 0.1857 -0.0108 0.0058  0.0241  143 CYS   A O   
2779 C  CB  . CYS   A 143 ? 0.1417 0.1997 0.1913 -0.0024 0.0231  0.0066  143 CYS   A CB  
2780 S  SG  . CYS   A 143 ? 0.1767 0.1891 0.1756 0.0050  0.0154  0.0091  143 CYS   A SG  
2786 N  N   . VAL   A 144 ? 0.1430 0.1840 0.2024 -0.0102 0.0098  0.0363  144 VAL   A N   
2787 C  CA  . VAL   A 144 ? 0.1441 0.2007 0.2475 -0.0112 0.0232  0.0298  144 VAL   A CA  
2788 C  C   . VAL   A 144 ? 0.1579 0.1956 0.2274 -0.0163 -0.0090 0.0309  144 VAL   A C   
2789 O  O   . VAL   A 144 ? 0.1796 0.1869 0.2390 -0.0187 0.0046  0.0329  144 VAL   A O   
2790 C  CB  . VAL   A 144 ? 0.1669 0.2237 0.3216 0.0024  0.0492  0.0256  144 VAL   A CB  
2791 C  CG1 . VAL   A 144 ? 0.1979 0.2514 0.3626 -0.0076 0.0394  0.0217  144 VAL   A CG1 
2792 C  CG2 . VAL   A 144 ? 0.1603 0.2236 0.3325 0.0082  0.0682  0.0346  144 VAL   A CG2 
2802 N  N   . ASP   A 145 ? 0.1637 0.1846 0.2318 -0.0117 0.0096  0.0221  145 ASP   A N   
2803 C  CA  . ASP   A 145 ? 0.1642 0.1988 0.2444 -0.0119 -0.0054 -0.0048 145 ASP   A CA  
2804 C  C   . ASP   A 145 ? 0.1549 0.1827 0.2342 -0.0142 0.0181  -0.0093 145 ASP   A C   
2805 O  O   . ASP   A 145 ? 0.1856 0.1727 0.2999 -0.0182 -0.0071 -0.0401 145 ASP   A O   
2806 C  CB  . ASP   A 145 ? 0.1909 0.2133 0.2605 -0.0309 -0.0158 -0.0053 145 ASP   A CB  
2807 C  CG  . ASP   A 145 ? 0.2150 0.2359 0.2764 -0.0489 -0.0311 -0.0019 145 ASP   A CG  
2808 O  OD1 . ASP   A 145 ? 0.2109 0.2454 0.2972 -0.0431 -0.0170 0.0183  145 ASP   A OD1 
2809 O  OD2 . ASP   A 145 ? 0.2345 0.2651 0.2991 -0.0735 -0.0485 -0.0053 145 ASP   A OD2 
2814 N  N   . THR   A 146 ? 0.1532 0.1741 0.1854 -0.0176 0.0183  0.0019  146 THR   A N   
2815 C  CA  . THR   A 146 ? 0.1359 0.1793 0.1746 -0.0212 -0.0031 0.0094  146 THR   A CA  
2816 C  C   . THR   A 146 ? 0.1356 0.1691 0.1795 -0.0027 0.0097  0.0044  146 THR   A C   
2817 O  O   . THR   A 146 ? 0.1557 0.1677 0.2086 0.0084  -0.0110 -0.0016 146 THR   A O   
2818 C  CB  . THR   A 146 ? 0.1432 0.1788 0.1705 -0.0024 0.0065  0.0097  146 THR   A CB  
2819 O  OG1 . THR   A 146 ? 0.1441 0.1903 0.1964 0.0062  -0.0052 0.0012  146 THR   A OG1 
2820 C  CG2 . THR   A 146 ? 0.1396 0.1771 0.2039 0.0002  0.0144  0.0133  146 THR   A CG2 
2828 N  N   . VAL   A 147 ? 0.1501 0.1725 0.1706 0.0054  0.0171  0.0051  147 VAL   A N   
2829 C  CA  . VAL   A 147 ? 0.1379 0.1772 0.1758 -0.0063 0.0304  0.0052  147 VAL   A CA  
2830 C  C   . VAL   A 147 ? 0.1640 0.1713 0.1886 -0.0215 0.0145  0.0210  147 VAL   A C   
2831 O  O   . VAL   A 147 ? 0.1660 0.1689 0.1933 -0.0145 0.0081  0.0182  147 VAL   A O   
2832 C  CB  . VAL   A 147 ? 0.1567 0.1796 0.1864 -0.0063 0.0305  0.0051  147 VAL   A CB  
2833 C  CG1 . VAL   A 147 ? 0.2006 0.1806 0.2008 -0.0019 0.0324  0.0298  147 VAL   A CG1 
2834 C  CG2 . VAL   A 147 ? 0.1608 0.1752 0.1909 -0.0177 0.0093  0.0104  147 VAL   A CG2 
2844 N  N   . ARG   A 148 ? 0.1723 0.1692 0.2024 -0.0187 0.0109  0.0437  148 ARG   A N   
2845 C  CA  . ARG   A 148 ? 0.1505 0.1718 0.2106 -0.0110 0.0094  0.0388  148 ARG   A CA  
2846 C  C   . ARG   A 148 ? 0.1688 0.1588 0.2159 -0.0140 0.0162  0.0566  148 ARG   A C   
2847 O  O   . ARG   A 148 ? 0.2080 0.1622 0.2419 -0.0226 0.0087  0.0621  148 ARG   A O   
2848 C  CB  . ARG   A 148 ? 0.1567 0.1602 0.2240 -0.0105 0.0240  0.0356  148 ARG   A CB  
2849 C  CG  . ARG   A 148 ? 0.1865 0.1773 0.2525 -0.0109 0.0246  0.0176  148 ARG   A CG  
2850 C  CD  . ARG   A 148 ? 0.1947 0.1806 0.2672 -0.0068 0.0422  0.0190  148 ARG   A CD  
2851 N  NE  . ARG   A 148 ? 0.1884 0.1716 0.2739 -0.0049 0.0479  0.0304  148 ARG   A NE  
2852 C  CZ  . ARG   A 148 ? 0.1802 0.1731 0.2612 -0.0023 0.0504  0.0397  148 ARG   A CZ  
2853 N  NH1 . ARG   A 148 ? 0.1825 0.1707 0.2891 -0.0225 0.0273  0.0179  148 ARG   A NH1 
2854 N  NH2 . ARG   A 148 ? 0.1798 0.1832 0.2605 0.0127  0.0518  0.0396  148 ARG   A NH2 
2868 N  N   . THR   A 149 ? 0.1716 0.1778 0.1940 -0.0197 -0.0121 0.0405  149 THR   A N   
2869 C  CA  . THR   A 149 ? 0.1864 0.1633 0.1953 -0.0228 0.0017  0.0427  149 THR   A CA  
2870 C  C   . THR   A 149 ? 0.1895 0.1769 0.1867 -0.0187 0.0107  0.0612  149 THR   A C   
2871 O  O   . THR   A 149 ? 0.1682 0.1926 0.1969 -0.0150 0.0062  0.0416  149 THR   A O   
2872 C  CB  . THR   A 149 ? 0.1893 0.1821 0.2121 -0.0137 0.0172  0.0319  149 THR   A CB  
2873 O  OG1 . THR   A 149 ? 0.1984 0.1726 0.2077 -0.0316 0.0103  0.0370  149 THR   A OG1 
2874 C  CG2 . THR   A 149 ? 0.1893 0.2159 0.2167 -0.0076 -0.0085 0.0184  149 THR   A CG2 
2882 N  N   . ASN   A 150 ? 0.1760 0.1629 0.2042 -0.0046 0.0102  0.0561  150 ASN   A N   
2883 C  CA  . ASN   A 150 ? 0.1996 0.1747 0.1911 -0.0078 0.0103  0.0453  150 ASN   A CA  
2884 C  C   . ASN   A 150 ? 0.1759 0.1756 0.2019 -0.0199 0.0105  0.0288  150 ASN   A C   
2885 O  O   . ASN   A 150 ? 0.1816 0.1676 0.2397 -0.0100 -0.0115 0.0276  150 ASN   A O   
2886 C  CB  . ASN   A 150 ? 0.2506 0.2136 0.2111 -0.0133 0.0224  0.0538  150 ASN   A CB  
2887 C  CG  . ASN   A 150 ? 0.2974 0.2551 0.2879 -0.0205 -0.0046 0.0736  150 ASN   A CG  
2888 O  OD1 . ASN   A 150 ? 0.3111 0.2701 0.3225 -0.0391 0.0071  0.0938  150 ASN   A OD1 
2889 N  ND2 . ASN   A 150 ? 0.3403 0.2821 0.3350 -0.0148 -0.0214 0.0738  150 ASN   A ND2 
2896 N  N   . VAL   A 151 ? 0.1720 0.1732 0.1977 -0.0249 0.0042  0.0445  151 VAL   A N   
2897 C  CA  . VAL   A 151 ? 0.1839 0.1661 0.1804 -0.0245 0.0275  0.0444  151 VAL   A CA  
2898 C  C   . VAL   A 151 ? 0.1902 0.1503 0.1764 -0.0361 0.0318  0.0373  151 VAL   A C   
2899 O  O   . VAL   A 151 ? 0.1985 0.1668 0.2144 -0.0230 0.0260  0.0251  151 VAL   A O   
2900 C  CB  . VAL   A 151 ? 0.2208 0.1989 0.1869 -0.0141 0.0169  0.0465  151 VAL   A CB  
2901 C  CG1 . VAL   A 151 ? 0.2234 0.2163 0.2090 -0.0104 -0.0007 0.0418  151 VAL   A CG1 
2902 C  CG2 . VAL   A 151 ? 0.2357 0.1970 0.1696 -0.0162 0.0283  0.0432  151 VAL   A CG2 
2912 N  N   A TYR   A 152 ? 0.1884 0.1578 0.1702 -0.0231 0.0271  0.0327  152 TYR   A N   
2913 N  N   B TYR   A 152 ? 0.1945 0.1616 0.1754 -0.0277 0.0138  0.0361  152 TYR   A N   
2914 C  CA  A TYR   A 152 ? 0.1864 0.1681 0.1544 -0.0260 0.0271  0.0190  152 TYR   A CA  
2915 C  CA  B TYR   A 152 ? 0.1982 0.1745 0.1673 -0.0240 -0.0023 0.0306  152 TYR   A CA  
2916 C  C   A TYR   A 152 ? 0.1823 0.1709 0.1623 -0.0226 0.0387  0.0278  152 TYR   A C   
2917 C  C   B TYR   A 152 ? 0.1937 0.1712 0.1470 -0.0190 -0.0198 0.0438  152 TYR   A C   
2918 O  O   A TYR   A 152 ? 0.1706 0.1574 0.1794 -0.0143 0.0470  0.0227  152 TYR   A O   
2919 O  O   B TYR   A 152 ? 0.1900 0.1653 0.1585 -0.0219 -0.0284 0.0461  152 TYR   A O   
2920 C  CB  A TYR   A 152 ? 0.2120 0.1703 0.1603 -0.0153 0.0325  0.0264  152 TYR   A CB  
2921 C  CB  B TYR   A 152 ? 0.2122 0.1877 0.1851 -0.0219 0.0066  0.0230  152 TYR   A CB  
2922 C  CG  A TYR   A 152 ? 0.2259 0.1911 0.1680 -0.0192 0.0358  0.0430  152 TYR   A CG  
2923 C  CG  B TYR   A 152 ? 0.2206 0.2027 0.1968 -0.0212 0.0135  0.0231  152 TYR   A CG  
2924 C  CD1 A TYR   A 152 ? 0.2317 0.2119 0.1966 -0.0087 0.0280  0.0564  152 TYR   A CD1 
2925 C  CD1 B TYR   A 152 ? 0.2223 0.2123 0.2106 -0.0187 0.0156  0.0273  152 TYR   A CD1 
2926 C  CD2 A TYR   A 152 ? 0.2291 0.2137 0.1526 -0.0336 0.0403  0.0391  152 TYR   A CD2 
2927 C  CD2 B TYR   A 152 ? 0.2233 0.2126 0.1970 -0.0261 0.0177  0.0221  152 TYR   A CD2 
2928 C  CE1 A TYR   A 152 ? 0.2499 0.2266 0.2018 -0.0050 0.0156  0.0593  152 TYR   A CE1 
2929 C  CE1 B TYR   A 152 ? 0.2312 0.2195 0.2207 -0.0159 0.0107  0.0260  152 TYR   A CE1 
2930 C  CE2 A TYR   A 152 ? 0.2489 0.2265 0.1680 -0.0290 0.0374  0.0431  152 TYR   A CE2 
2931 C  CE2 B TYR   A 152 ? 0.2309 0.2182 0.2064 -0.0264 0.0190  0.0229  152 TYR   A CE2 
2932 C  CZ  A TYR   A 152 ? 0.2654 0.2292 0.1713 -0.0207 0.0229  0.0700  152 TYR   A CZ  
2933 C  CZ  B TYR   A 152 ? 0.2383 0.2220 0.2183 -0.0229 0.0127  0.0291  152 TYR   A CZ  
2934 O  OH  A TYR   A 152 ? 0.2932 0.2554 0.2134 -0.0098 0.0200  0.0817  152 TYR   A OH  
2935 O  OH  B TYR   A 152 ? 0.2507 0.2355 0.2455 -0.0183 0.0130  0.0331  152 TYR   A OH  
2954 N  N   A LEU   A 153 ? 0.1712 0.1779 0.1770 -0.0197 0.0500  0.0308  153 LEU   A N   
2955 N  N   B LEU   A 153 ? 0.1889 0.1739 0.1326 -0.0047 -0.0263 0.0468  153 LEU   A N   
2956 C  CA  A LEU   A 153 ? 0.1472 0.1801 0.1849 -0.0139 0.0481  0.0262  153 LEU   A CA  
2957 C  CA  B LEU   A 153 ? 0.1808 0.1772 0.1255 0.0127  -0.0281 0.0451  153 LEU   A CA  
2958 C  C   A LEU   A 153 ? 0.1482 0.1852 0.1986 -0.0191 0.0547  0.0174  153 LEU   A C   
2959 C  C   B LEU   A 153 ? 0.1826 0.1911 0.1185 0.0125  -0.0112 0.0444  153 LEU   A C   
2960 O  O   A LEU   A 153 ? 0.1655 0.1866 0.2269 -0.0083 0.0625  0.0178  153 LEU   A O   
2961 O  O   B LEU   A 153 ? 0.1935 0.1961 0.1199 0.0078  0.0039  0.0407  153 LEU   A O   
2962 C  CB  A LEU   A 153 ? 0.1406 0.1676 0.2149 -0.0153 0.0510  0.0234  153 LEU   A CB  
2963 C  CB  B LEU   A 153 ? 0.1771 0.1739 0.1425 0.0285  -0.0276 0.0310  153 LEU   A CB  
2964 C  CG  A LEU   A 153 ? 0.1554 0.1725 0.2110 -0.0125 0.0506  0.0173  153 LEU   A CG  
2965 C  CG  B LEU   A 153 ? 0.1769 0.1630 0.1288 0.0446  -0.0135 0.0328  153 LEU   A CG  
2966 C  CD1 A LEU   A 153 ? 0.1567 0.1682 0.2211 -0.0135 0.0243  0.0172  153 LEU   A CD1 
2967 C  CD1 B LEU   A 153 ? 0.1838 0.1599 0.1341 0.0475  -0.0145 0.0216  153 LEU   A CD1 
2968 C  CD2 A LEU   A 153 ? 0.1692 0.1714 0.2089 -0.0108 0.0552  0.0142  153 LEU   A CD2 
2969 C  CD2 B LEU   A 153 ? 0.1773 0.1600 0.1368 0.0456  -0.0001 0.0292  153 LEU   A CD2 
2992 N  N   A ALA   A 154 ? 0.1571 0.1727 0.1935 -0.0136 0.0453  0.0191  154 ALA   A N   
2993 N  N   B ALA   A 154 ? 0.1827 0.1908 0.1245 0.0125  -0.0083 0.0373  154 ALA   A N   
2994 C  CA  A ALA   A 154 ? 0.1638 0.1670 0.2035 -0.0082 0.0378  0.0110  154 ALA   A CA  
2995 C  CA  B ALA   A 154 ? 0.1862 0.1905 0.1349 0.0101  -0.0109 0.0249  154 ALA   A CA  
2996 C  C   A ALA   A 154 ? 0.1703 0.1485 0.1925 -0.0041 0.0536  0.0190  154 ALA   A C   
2997 C  C   B ALA   A 154 ? 0.1917 0.1849 0.1220 0.0128  -0.0135 0.0131  154 ALA   A C   
2998 O  O   A ALA   A 154 ? 0.1665 0.1680 0.1787 -0.0049 0.0309  0.0125  154 ALA   A O   
2999 O  O   B ALA   A 154 ? 0.1928 0.1806 0.1097 0.0141  -0.0040 0.0072  154 ALA   A O   
3000 C  CB  A ALA   A 154 ? 0.1865 0.1541 0.1975 0.0062  0.0282  0.0022  154 ALA   A CB  
3001 C  CB  B ALA   A 154 ? 0.1874 0.1904 0.1431 0.0067  -0.0077 0.0193  154 ALA   A CB  
3012 N  N   A VAL   A 155 ? 0.1638 0.1403 0.1892 0.0036  0.0580  0.0410  155 VAL   A N   
3013 N  N   B VAL   A 155 ? 0.1926 0.1882 0.1396 0.0181  -0.0288 0.0150  155 VAL   A N   
3014 C  CA  A VAL   A 155 ? 0.1785 0.1546 0.2330 0.0085  0.0474  0.0490  155 VAL   A CA  
3015 C  CA  B VAL   A 155 ? 0.1987 0.1996 0.1669 0.0194  -0.0463 0.0161  155 VAL   A CA  
3016 C  CA  T VAL   A 155 ? 0.2110 0.2080 0.1950 -0.0047 -0.0001 0.0243  155 VAL   A CA  
3017 C  C   A VAL   A 155 ? 0.1843 0.1782 0.2403 0.0263  0.0549  0.0716  155 VAL   A C   
3018 C  C   B VAL   A 155 ? 0.2089 0.2134 0.2077 0.0357  -0.0534 0.0201  155 VAL   A C   
3019 C  C   T VAL   A 155 ? 0.2119 0.2107 0.1983 -0.0023 0.0068  0.0263  155 VAL   A C   
3020 O  O   A VAL   A 155 ? 0.1875 0.1956 0.2568 0.0357  0.0712  0.0613  155 VAL   A O   
3021 O  O   B VAL   A 155 ? 0.2044 0.2163 0.2174 0.0415  -0.0717 0.0195  155 VAL   A O   
3022 O  O   T VAL   A 155 ? 0.2111 0.2097 0.1937 -0.0018 0.0071  0.0259  155 VAL   A O   
3023 C  CB  A VAL   A 155 ? 0.1728 0.1717 0.2469 -0.0003 0.0155  0.0313  155 VAL   A CB  
3024 C  CB  B VAL   A 155 ? 0.1891 0.1950 0.1708 0.0087  -0.0507 0.0124  155 VAL   A CB  
3025 C  CB  T VAL   A 155 ? 0.2088 0.2078 0.1911 -0.0050 -0.0085 0.0238  155 VAL   A CB  
3026 C  CG1 A VAL   A 155 ? 0.1902 0.1635 0.2582 0.0034  0.0001  0.0239  155 VAL   A CG1 
3027 C  CG1 B VAL   A 155 ? 0.1910 0.1987 0.1693 -0.0019 -0.0525 0.0159  155 VAL   A CG1 
3028 C  CG1 T VAL   A 155 ? 0.2097 0.2077 0.1899 -0.0048 -0.0125 0.0253  155 VAL   A CG1 
3029 C  CG2 A VAL   A 155 ? 0.1828 0.1754 0.2649 0.0066  -0.0004 0.0160  155 VAL   A CG2 
3030 C  CG2 B VAL   A 155 ? 0.1869 0.1879 0.1767 0.0075  -0.0515 0.0173  155 VAL   A CG2 
3031 C  CG2 T VAL   A 155 ? 0.2106 0.2080 0.1919 -0.0044 -0.0104 0.0209  155 VAL   A CG2 
3057 N  N   A PHE   A 156 ? 0.2097 0.1882 0.2804 0.0313  0.0514  0.0935  156 PHE   A N   
3058 N  N   B PHE   A 156 ? 0.2250 0.2184 0.2252 0.0414  -0.0439 0.0111  156 PHE   A N   
3059 N  N   T PHE   A 156 ? 0.2155 0.2139 0.2121 -0.0021 0.0133  0.0279  156 PHE   A N   
3060 C  CA  A PHE   A 156 ? 0.2353 0.2053 0.3106 0.0395  0.0566  0.0909  156 PHE   A CA  
3061 C  CA  B PHE   A 156 ? 0.2427 0.2275 0.2578 0.0455  -0.0251 0.0054  156 PHE   A CA  
3062 C  CA  T PHE   A 156 ? 0.2198 0.2183 0.2239 -0.0022 0.0229  0.0251  156 PHE   A CA  
3063 C  C   A PHE   A 156 ? 0.2365 0.2147 0.3177 0.0510  0.0669  0.0969  156 PHE   A C   
3064 C  C   B PHE   A 156 ? 0.2457 0.2261 0.2587 0.0493  -0.0140 0.0102  156 PHE   A C   
3065 C  C   T PHE   A 156 ? 0.2251 0.2244 0.2275 -0.0007 0.0273  0.0259  156 PHE   A C   
3066 O  O   A PHE   A 156 ? 0.2430 0.2334 0.3364 0.0489  0.0808  0.0970  156 PHE   A O   
3067 O  O   B PHE   A 156 ? 0.2479 0.2316 0.2657 0.0451  -0.0100 0.0057  156 PHE   A O   
3068 O  O   T PHE   A 156 ? 0.2313 0.2276 0.2299 -0.0005 0.0325  0.0252  156 PHE   A O   
3069 C  CB  A PHE   A 156 ? 0.2701 0.1969 0.3243 0.0480  0.0450  0.0914  156 PHE   A CB  
3070 C  CB  B PHE   A 156 ? 0.2618 0.2375 0.2866 0.0440  -0.0147 0.0015  156 PHE   A CB  
3071 C  CB  T PHE   A 156 ? 0.2183 0.2147 0.2303 -0.0002 0.0257  0.0223  156 PHE   A CB  
3072 C  CG  A PHE   A 156 ? 0.3124 0.2166 0.3531 0.0624  0.0263  0.0744  156 PHE   A CG  
3073 C  CG  B PHE   A 156 ? 0.2761 0.2463 0.3181 0.0472  -0.0075 -0.0132 156 PHE   A CG  
3074 C  CG  T PHE   A 156 ? 0.2199 0.2154 0.2369 0.0039  0.0274  0.0181  156 PHE   A CG  
3075 C  CD1 A PHE   A 156 ? 0.3325 0.2305 0.3743 0.0741  0.0240  0.0598  156 PHE   A CD1 
3076 C  CD1 B PHE   A 156 ? 0.2836 0.2481 0.3264 0.0531  0.0015  -0.0188 156 PHE   A CD1 
3077 C  CD1 T PHE   A 156 ? 0.2206 0.2179 0.2413 0.0060  0.0262  0.0173  156 PHE   A CD1 
3078 C  CD2 A PHE   A 156 ? 0.3323 0.2269 0.3726 0.0665  0.0246  0.0609  156 PHE   A CD2 
3079 C  CD2 B PHE   A 156 ? 0.2816 0.2506 0.3299 0.0487  -0.0038 -0.0227 156 PHE   A CD2 
3080 C  CD2 T PHE   A 156 ? 0.2212 0.2153 0.2434 0.0047  0.0280  0.0123  156 PHE   A CD2 
3081 C  CE1 A PHE   A 156 ? 0.3481 0.2426 0.3984 0.0745  0.0294  0.0448  156 PHE   A CE1 
3082 C  CE1 B PHE   A 156 ? 0.2877 0.2528 0.3370 0.0546  0.0085  -0.0247 156 PHE   A CE1 
3083 C  CE1 T PHE   A 156 ? 0.2199 0.2185 0.2428 0.0055  0.0282  0.0134  156 PHE   A CE1 
3084 C  CE2 A PHE   A 156 ? 0.3473 0.2426 0.3902 0.0688  0.0275  0.0427  156 PHE   A CE2 
3085 C  CE2 B PHE   A 156 ? 0.2901 0.2552 0.3400 0.0492  0.0031  -0.0311 156 PHE   A CE2 
3086 C  CE2 T PHE   A 156 ? 0.2210 0.2161 0.2462 0.0046  0.0269  0.0108  156 PHE   A CE2 
3087 C  CZ  A PHE   A 156 ? 0.3523 0.2476 0.3989 0.0750  0.0313  0.0289  156 PHE   A CZ  
3088 C  CZ  B PHE   A 156 ? 0.2924 0.2570 0.3421 0.0542  0.0073  -0.0293 156 PHE   A CZ  
3089 C  CZ  T PHE   A 156 ? 0.2206 0.2170 0.2465 0.0039  0.0286  0.0122  156 PHE   A CZ  
3117 N  N   A ASP   A 157 ? 0.2376 0.2200 0.3012 0.0383  0.0445  0.1063  157 ASP   A N   
3118 N  N   B ASP   A 157 ? 0.2444 0.2176 0.2437 0.0506  -0.0042 0.0184  157 ASP   A N   
3119 N  N   T ASP   A 157 ? 0.2264 0.2291 0.2293 -0.0027 0.0209  0.0267  157 ASP   A N   
3120 C  CA  A ASP   A 157 ? 0.2400 0.2279 0.2994 0.0325  0.0444  0.1024  157 ASP   A CA  
3121 C  CA  B ASP   A 157 ? 0.2436 0.2206 0.2466 0.0440  0.0109  0.0353  157 ASP   A CA  
3122 C  CA  T ASP   A 157 ? 0.2293 0.2344 0.2354 -0.0023 0.0182  0.0260  157 ASP   A CA  
3123 C  C   A ASP   A 157 ? 0.2252 0.2493 0.3064 0.0410  0.0600  0.0967  157 ASP   A C   
3124 C  C   B ASP   A 157 ? 0.2388 0.2390 0.2685 0.0389  0.0143  0.0314  157 ASP   A C   
3125 C  C   T ASP   A 157 ? 0.2405 0.2477 0.2430 0.0035  0.0131  0.0239  157 ASP   A C   
3126 O  O   A ASP   A 157 ? 0.2061 0.2397 0.2705 0.0547  0.0570  0.0981  157 ASP   A O   
3127 O  O   B ASP   A 157 ? 0.2397 0.2478 0.2702 0.0364  0.0159  0.0305  157 ASP   A O   
3128 O  O   T ASP   A 157 ? 0.2409 0.2474 0.2376 0.0054  0.0086  0.0206  157 ASP   A O   
3129 C  CB  A ASP   A 157 ? 0.2512 0.2352 0.3008 0.0263  0.0457  0.1142  157 ASP   A CB  
3130 C  CB  B ASP   A 157 ? 0.2416 0.2091 0.2387 0.0436  0.0155  0.0503  157 ASP   A CB  
3131 C  CB  T ASP   A 157 ? 0.2204 0.2296 0.2325 -0.0062 0.0233  0.0293  157 ASP   A CB  
3132 C  CG  A ASP   A 157 ? 0.2721 0.2501 0.3314 0.0310  0.0143  0.1096  157 ASP   A CG  
3133 C  CG  B ASP   A 157 ? 0.2432 0.2060 0.2374 0.0434  0.0255  0.0696  157 ASP   A CG  
3134 C  CG  T ASP   A 157 ? 0.2121 0.2250 0.2270 -0.0074 0.0241  0.0306  157 ASP   A CG  
3135 O  OD1 A ASP   A 157 ? 0.3042 0.2732 0.3724 0.0199  -0.0120 0.0871  157 ASP   A OD1 
3136 O  OD1 B ASP   A 157 ? 0.2441 0.2011 0.2294 0.0454  0.0382  0.0969  157 ASP   A OD1 
3137 O  OD1 T ASP   A 157 ? 0.2104 0.2248 0.2353 -0.0126 0.0210  0.0240  157 ASP   A OD1 
3138 O  OD2 A ASP   A 157 ? 0.2554 0.2463 0.3377 0.0316  0.0182  0.1074  157 ASP   A OD2 
3139 O  OD2 B ASP   A 157 ? 0.2430 0.2053 0.2458 0.0318  0.0317  0.0709  157 ASP   A OD2 
3140 O  OD2 T ASP   A 157 ? 0.2051 0.2212 0.2172 -0.0065 0.0322  0.0362  157 ASP   A OD2 
3153 N  N   A LYS   A 158 ? 0.2244 0.2639 0.3465 0.0470  0.0737  0.0865  158 LYS   A N   
3154 N  N   B LYS   A 158 ? 0.2338 0.2415 0.2936 0.0343  0.0158  0.0343  158 LYS   A N   
3155 N  N   T LYS   A 158 ? 0.2506 0.2589 0.2595 0.0081  0.0134  0.0220  158 LYS   A N   
3156 C  CA  A LYS   A 158 ? 0.2224 0.2881 0.3715 0.0554  0.0931  0.0877  158 LYS   A CA  
3157 C  CA  B LYS   A 158 ? 0.2320 0.2502 0.3078 0.0283  0.0236  0.0398  158 LYS   A CA  
3158 C  CA  T LYS   A 158 ? 0.2596 0.2711 0.2795 0.0124  0.0142  0.0204  158 LYS   A CA  
3159 C  C   A LYS   A 158 ? 0.1977 0.2951 0.3655 0.0551  0.0796  0.1126  158 LYS   A C   
3160 C  C   B LYS   A 158 ? 0.2150 0.2547 0.3039 0.0238  0.0070  0.0458  158 LYS   A C   
3161 C  C   T LYS   A 158 ? 0.2614 0.2760 0.2824 0.0145  0.0133  0.0239  158 LYS   A C   
3162 O  O   A LYS   A 158 ? 0.1928 0.2949 0.3751 0.0429  0.0718  0.1253  158 LYS   A O   
3163 O  O   B LYS   A 158 ? 0.2200 0.2587 0.3202 0.0162  0.0092  0.0526  158 LYS   A O   
3164 O  O   T LYS   A 158 ? 0.2607 0.2786 0.2834 0.0151  0.0151  0.0245  158 LYS   A O   
3165 C  CB  A LYS   A 158 ? 0.2529 0.3023 0.4082 0.0526  0.1131  0.0752  158 LYS   A CB  
3166 C  CB  B LYS   A 158 ? 0.2490 0.2578 0.3254 0.0225  0.0469  0.0440  158 LYS   A CB  
3167 C  CB  T LYS   A 158 ? 0.2675 0.2777 0.2970 0.0130  0.0160  0.0158  158 LYS   A CB  
3168 C  CG  A LYS   A 158 ? 0.2775 0.3156 0.4420 0.0587  0.1209  0.0716  158 LYS   A CG  
3169 C  CG  B LYS   A 158 ? 0.2651 0.2670 0.3435 0.0216  0.0581  0.0472  158 LYS   A CG  
3170 C  CG  T LYS   A 158 ? 0.2732 0.2834 0.3128 0.0128  0.0167  0.0143  158 LYS   A CG  
3171 C  CD  A LYS   A 158 ? 0.2925 0.3306 0.4672 0.0667  0.1352  0.0747  158 LYS   A CD  
3172 C  CD  B LYS   A 158 ? 0.2754 0.2776 0.3573 0.0242  0.0737  0.0504  158 LYS   A CD  
3173 C  CD  T LYS   A 158 ? 0.2787 0.2884 0.3283 0.0130  0.0174  0.0163  158 LYS   A CD  
3174 C  CE  A LYS   A 158 ? 0.3095 0.3361 0.4822 0.0627  0.1435  0.0926  158 LYS   A CE  
3175 C  CE  B LYS   A 158 ? 0.2821 0.2821 0.3616 0.0229  0.0887  0.0615  158 LYS   A CE  
3176 C  CE  T LYS   A 158 ? 0.2851 0.2917 0.3402 0.0123  0.0164  0.0187  158 LYS   A CE  
3177 N  NZ  A LYS   A 158 ? 0.3152 0.3403 0.4785 0.0526  0.1440  0.1142  158 LYS   A NZ  
3178 N  NZ  B LYS   A 158 ? 0.2856 0.2849 0.3610 0.0208  0.0946  0.0706  158 LYS   A NZ  
3179 N  NZ  T LYS   A 158 ? 0.2881 0.2937 0.3432 0.0126  0.0131  0.0212  158 LYS   A NZ  
3219 N  N   A ASN   A 159 ? 0.1969 0.3138 0.3884 0.0656  0.0571  0.1027  159 ASN   A N   
3220 N  N   B ASN   A 159 ? 0.1944 0.2569 0.2984 0.0255  -0.0114 0.0397  159 ASN   A N   
3221 N  N   T ASN   A 159 ? 0.2647 0.2797 0.2890 0.0146  0.0103  0.0240  159 ASN   A N   
3222 C  CA  A ASN   A 159 ? 0.1968 0.3162 0.3789 0.0628  0.0347  0.1221  159 ASN   A CA  
3223 C  CA  B ASN   A 159 ? 0.1787 0.2541 0.2819 0.0183  -0.0312 0.0355  159 ASN   A CA  
3224 C  CA  T ASN   A 159 ? 0.2667 0.2808 0.2915 0.0126  0.0081  0.0273  159 ASN   A CA  
3225 C  C   A ASN   A 159 ? 0.1826 0.3123 0.3469 0.0395  0.0370  0.1113  159 ASN   A C   
3226 C  C   B ASN   A 159 ? 0.1834 0.2544 0.2695 0.0151  -0.0170 0.0248  159 ASN   A C   
3227 C  C   T ASN   A 159 ? 0.2644 0.2808 0.2774 0.0099  0.0082  0.0251  159 ASN   A C   
3228 O  O   A ASN   A 159 ? 0.1739 0.3288 0.3519 0.0399  0.0079  0.1065  159 ASN   A O   
3229 O  O   B ASN   A 159 ? 0.1774 0.2568 0.2629 0.0192  -0.0334 0.0133  159 ASN   A O   
3230 O  O   T ASN   A 159 ? 0.2640 0.2845 0.2789 0.0096  0.0052  0.0234  159 ASN   A O   
3231 C  CB  A ASN   A 159 ? 0.2390 0.3364 0.4224 0.0634  0.0173  0.1251  159 ASN   A CB  
3232 C  CB  B ASN   A 159 ? 0.1703 0.2576 0.2836 0.0105  -0.0587 0.0348  159 ASN   A CB  
3233 C  CB  T ASN   A 159 ? 0.2728 0.2835 0.3084 0.0115  0.0061  0.0299  159 ASN   A CB  
3234 C  CG  A ASN   A 159 ? 0.2772 0.3586 0.4690 0.0484  0.0153  0.1121  159 ASN   A CG  
3235 C  CG  B ASN   A 159 ? 0.1612 0.2701 0.3014 0.0009  -0.0677 0.0314  159 ASN   A CG  
3236 C  CG  T ASN   A 159 ? 0.2779 0.2863 0.3257 0.0098  0.0062  0.0310  159 ASN   A CG  
3237 O  OD1 A ASN   A 159 ? 0.2848 0.3732 0.4868 0.0434  0.0333  0.1033  159 ASN   A OD1 
3238 O  OD1 B ASN   A 159 ? 0.1533 0.2812 0.3305 0.0036  -0.0620 0.0169  159 ASN   A OD1 
3239 O  OD1 T ASN   A 159 ? 0.2786 0.2892 0.3333 0.0101  0.0128  0.0322  159 ASN   A OD1 
3240 N  ND2 A ASN   A 159 ? 0.2970 0.3690 0.4913 0.0367  0.0068  0.0990  159 ASN   A ND2 
3241 N  ND2 B ASN   A 159 ? 0.1765 0.2757 0.3046 -0.0019 -0.0712 0.0421  159 ASN   A ND2 
3242 N  ND2 T ASN   A 159 ? 0.2812 0.2879 0.3320 0.0077  0.0021  0.0293  159 ASN   A ND2 
3261 N  N   A LEU   A 160 ? 0.1650 0.2902 0.3100 0.0193  0.0165  0.1081  160 LEU   A N   
3262 N  N   B LEU   A 160 ? 0.1853 0.2451 0.2556 0.0103  -0.0057 0.0185  160 LEU   A N   
3263 N  N   T LEU   A 160 ? 0.2608 0.2768 0.2667 0.0078  0.0065  0.0244  160 LEU   A N   
3264 C  CA  A LEU   A 160 ? 0.1785 0.2734 0.2728 0.0058  0.0027  0.1075  160 LEU   A CA  
3265 C  CA  B LEU   A 160 ? 0.1886 0.2338 0.2201 0.0079  -0.0069 0.0166  160 LEU   A CA  
3266 C  CA  T LEU   A 160 ? 0.2602 0.2733 0.2550 0.0057  0.0059  0.0236  160 LEU   A CA  
3267 C  C   A LEU   A 160 ? 0.1743 0.2636 0.2333 -0.0050 0.0121  0.0964  160 LEU   A C   
3268 C  C   B LEU   A 160 ? 0.1825 0.2380 0.1961 0.0132  -0.0074 0.0093  160 LEU   A C   
3269 O  O   A LEU   A 160 ? 0.1543 0.2647 0.2395 -0.0168 0.0013  0.0893  160 LEU   A O   
3270 O  O   B LEU   A 160 ? 0.1638 0.2394 0.1951 0.0100  -0.0213 0.0134  160 LEU   A O   
3271 C  CB  A LEU   A 160 ? 0.1793 0.2711 0.2548 -0.0033 -0.0023 0.1129  160 LEU   A CB  
3272 C  CB  B LEU   A 160 ? 0.1894 0.2196 0.2038 -0.0027 0.0069  0.0275  160 LEU   A CB  
3273 C  CB  T LEU   A 160 ? 0.2587 0.2709 0.2440 0.0039  0.0077  0.0232  160 LEU   A CB  
3274 C  CG  A LEU   A 160 ? 0.1807 0.2817 0.2640 -0.0145 -0.0177 0.0921  160 LEU   A CG  
3275 C  CG  B LEU   A 160 ? 0.1872 0.2115 0.1982 -0.0216 0.0229  0.0204  160 LEU   A CG  
3276 C  CG  T LEU   A 160 ? 0.2580 0.2695 0.2386 0.0018  0.0072  0.0183  160 LEU   A CG  
3277 C  CD1 A LEU   A 160 ? 0.1858 0.2900 0.2807 -0.0114 -0.0181 0.0753  160 LEU   A CD1 
3278 C  CD1 B LEU   A 160 ? 0.1846 0.2054 0.1982 -0.0313 0.0220  0.0139  160 LEU   A CD1 
3279 C  CD1 T LEU   A 160 ? 0.2577 0.2688 0.2371 0.0022  0.0074  0.0167  160 LEU   A CD1 
3280 C  CD2 A LEU   A 160 ? 0.1817 0.2818 0.2630 -0.0211 -0.0003 0.0780  160 LEU   A CD2 
3281 C  CD2 B LEU   A 160 ? 0.1834 0.2161 0.1861 -0.0306 0.0368  0.0190  160 LEU   A CD2 
3282 C  CD2 T LEU   A 160 ? 0.2581 0.2689 0.2358 0.0004  0.0098  0.0145  160 LEU   A CD2 
3315 N  N   A TYR   A 161 ? 0.1937 0.2495 0.2307 -0.0029 0.0224  0.0857  161 TYR   A N   
3316 N  N   B TYR   A 161 ? 0.1967 0.2349 0.1866 0.0203  -0.0037 -0.0071 161 TYR   A N   
3317 C  CA  A TYR   A 161 ? 0.1994 0.2236 0.2198 -0.0059 0.0341  0.0891  161 TYR   A CA  
3318 C  CA  B TYR   A 161 ? 0.2033 0.2284 0.1682 0.0232  0.0131  -0.0218 161 TYR   A CA  
3319 C  C   A TYR   A 161 ? 0.1965 0.2282 0.2200 -0.0105 0.0283  0.0785  161 TYR   A C   
3320 C  C   B TYR   A 161 ? 0.2070 0.2464 0.1629 0.0248  0.0265  -0.0194 161 TYR   A C   
3321 O  O   A TYR   A 161 ? 0.1838 0.2373 0.2028 -0.0228 0.0221  0.0691  161 TYR   A O   
3322 O  O   B TYR   A 161 ? 0.2024 0.2558 0.1751 0.0136  0.0356  -0.0116 161 TYR   A O   
3323 C  CB  A TYR   A 161 ? 0.2063 0.2155 0.2228 -0.0049 0.0398  0.0654  161 TYR   A CB  
3324 C  CB  B TYR   A 161 ? 0.2097 0.2166 0.1722 0.0131  0.0142  -0.0298 161 TYR   A CB  
3325 C  CG  A TYR   A 161 ? 0.1988 0.2143 0.2123 0.0002  0.0407  0.0394  161 TYR   A CG  
3326 C  CG  B TYR   A 161 ? 0.2140 0.2044 0.1721 0.0036  0.0164  -0.0250 161 TYR   A CG  
3327 C  CD1 A TYR   A 161 ? 0.1923 0.2077 0.2226 0.0040  0.0363  0.0307  161 TYR   A CD1 
3328 C  CD1 B TYR   A 161 ? 0.2169 0.2001 0.1699 -0.0001 0.0175  -0.0167 161 TYR   A CD1 
3329 C  CD2 A TYR   A 161 ? 0.2042 0.2299 0.2186 0.0030  0.0468  0.0271  161 TYR   A CD2 
3330 C  CD2 B TYR   A 161 ? 0.2208 0.2057 0.1792 0.0033  0.0204  -0.0119 161 TYR   A CD2 
3331 C  CE1 A TYR   A 161 ? 0.1999 0.2084 0.2140 -0.0028 0.0363  0.0318  161 TYR   A CE1 
3332 C  CE1 B TYR   A 161 ? 0.2246 0.2004 0.1865 -0.0056 0.0263  -0.0072 161 TYR   A CE1 
3333 C  CE2 A TYR   A 161 ? 0.2067 0.2153 0.2075 -0.0022 0.0348  0.0336  161 TYR   A CE2 
3334 C  CE2 B TYR   A 161 ? 0.2266 0.2040 0.1974 0.0002  0.0226  0.0025  161 TYR   A CE2 
3335 C  CZ  A TYR   A 161 ? 0.2133 0.2113 0.2221 -0.0028 0.0205  0.0359  161 TYR   A CZ  
3336 C  CZ  B TYR   A 161 ? 0.2320 0.2059 0.2058 0.0005  0.0262  0.0046  161 TYR   A CZ  
3337 O  OH  A TYR   A 161 ? 0.2345 0.2163 0.2386 -0.0080 0.0153  0.0559  161 TYR   A OH  
3338 O  OH  B TYR   A 161 ? 0.2466 0.2105 0.2282 0.0054  0.0250  0.0158  161 TYR   A OH  
3357 N  N   A ASP   A 162 ? 0.1927 0.2355 0.2465 0.0044  0.0329  0.0839  162 ASP   A N   
3358 N  N   B ASP   A 162 ? 0.2051 0.2521 0.1672 0.0330  0.0280  -0.0242 162 ASP   A N   
3359 C  CA  A ASP   A 162 ? 0.1830 0.2574 0.2584 -0.0045 0.0340  0.0740  162 ASP   A CA  
3360 C  CA  B ASP   A 162 ? 0.2021 0.2560 0.1772 0.0368  0.0255  -0.0211 162 ASP   A CA  
3361 C  C   A ASP   A 162 ? 0.1741 0.2833 0.2459 -0.0111 0.0088  0.0699  162 ASP   A C   
3362 C  C   B ASP   A 162 ? 0.1928 0.2677 0.1932 0.0338  0.0195  -0.0245 162 ASP   A C   
3363 O  O   A ASP   A 162 ? 0.1708 0.2842 0.2490 -0.0185 0.0130  0.0510  162 ASP   A O   
3364 O  O   B ASP   A 162 ? 0.1820 0.2697 0.1865 0.0327  0.0233  -0.0336 162 ASP   A O   
3365 C  CB  A ASP   A 162 ? 0.1817 0.2711 0.2829 0.0005  0.0544  0.0627  162 ASP   A CB  
3366 C  CB  B ASP   A 162 ? 0.2000 0.2556 0.1713 0.0469  0.0254  -0.0222 162 ASP   A CB  
3367 C  CG  A ASP   A 162 ? 0.2051 0.2882 0.3076 0.0030  0.0307  0.0318  162 ASP   A CG  
3368 C  CG  B ASP   A 162 ? 0.2033 0.2620 0.1900 0.0506  0.0248  -0.0202 162 ASP   A CG  
3369 O  OD1 A ASP   A 162 ? 0.2068 0.2946 0.3246 -0.0185 0.0368  0.0141  162 ASP   A OD1 
3370 O  OD1 B ASP   A 162 ? 0.2062 0.2674 0.1824 0.0430  0.0176  -0.0308 162 ASP   A OD1 
3371 O  OD2 A ASP   A 162 ? 0.2252 0.3012 0.3132 0.0143  0.0349  0.0066  162 ASP   A OD2 
3372 O  OD2 B ASP   A 162 ? 0.2072 0.2675 0.2161 0.0519  0.0339  -0.0171 162 ASP   A OD2 
3381 N  N   A LYS   A 163 ? 0.1749 0.3063 0.2691 -0.0121 -0.0075 0.0767  163 LYS   A N   
3382 N  N   B LYS   A 163 ? 0.1995 0.2753 0.2075 0.0321  0.0056  -0.0240 163 LYS   A N   
3383 C  CA  A LYS   A 163 ? 0.1825 0.3233 0.2555 -0.0088 -0.0147 0.0720  163 LYS   A CA  
3384 C  CA  B LYS   A 163 ? 0.2108 0.2832 0.2306 0.0263  0.0018  -0.0196 163 LYS   A CA  
3385 C  C   A LYS   A 163 ? 0.1755 0.3073 0.2268 -0.0144 -0.0088 0.0620  163 LYS   A C   
3386 C  C   B LYS   A 163 ? 0.2049 0.2769 0.2102 0.0160  0.0081  -0.0151 163 LYS   A C   
3387 O  O   A LYS   A 163 ? 0.1814 0.3278 0.2424 -0.0228 -0.0003 0.0455  163 LYS   A O   
3388 O  O   B LYS   A 163 ? 0.2023 0.2845 0.2082 0.0119  0.0185  -0.0170 163 LYS   A O   
3389 C  CB  A LYS   A 163 ? 0.2354 0.3626 0.3138 0.0130  -0.0267 0.0658  163 LYS   A CB  
3390 C  CB  B LYS   A 163 ? 0.2347 0.2990 0.2772 0.0338  -0.0104 -0.0189 163 LYS   A CB  
3391 C  CG  A LYS   A 163 ? 0.2902 0.3951 0.3866 0.0139  -0.0219 0.0639  163 LYS   A CG  
3392 C  CG  B LYS   A 163 ? 0.2546 0.3098 0.3187 0.0363  -0.0108 -0.0165 163 LYS   A CG  
3393 C  CD  A LYS   A 163 ? 0.3342 0.4242 0.4568 0.0148  -0.0206 0.0579  163 LYS   A CD  
3394 C  CD  B LYS   A 163 ? 0.2737 0.3201 0.3553 0.0376  -0.0065 -0.0146 163 LYS   A CD  
3395 C  CE  A LYS   A 163 ? 0.3574 0.4407 0.5095 0.0126  -0.0193 0.0560  163 LYS   A CE  
3396 C  CE  B LYS   A 163 ? 0.2862 0.3298 0.3825 0.0372  -0.0063 -0.0135 163 LYS   A CE  
3397 N  NZ  A LYS   A 163 ? 0.3590 0.4463 0.5375 0.0102  -0.0235 0.0548  163 LYS   A NZ  
3398 N  NZ  B LYS   A 163 ? 0.2926 0.3355 0.3943 0.0383  -0.0054 -0.0102 163 LYS   A NZ  
3425 N  N   A LEU   A 164 ? 0.1675 0.2813 0.1943 -0.0291 -0.0154 0.0550  164 LEU   A N   
3426 N  N   B LEU   A 164 ? 0.1978 0.2605 0.2007 0.0087  0.0085  -0.0151 164 LEU   A N   
3427 C  CA  A LEU   A 164 ? 0.1817 0.2502 0.1929 -0.0306 0.0096  0.0498  164 LEU   A CA  
3428 C  CA  B LEU   A 164 ? 0.1968 0.2450 0.1941 0.0002  0.0075  -0.0171 164 LEU   A CA  
3429 C  C   A LEU   A 164 ? 0.1822 0.2479 0.2005 -0.0281 0.0161  0.0636  164 LEU   A C   
3430 C  C   B LEU   A 164 ? 0.1902 0.2407 0.1961 -0.0085 0.0097  -0.0042 164 LEU   A C   
3431 O  O   A LEU   A 164 ? 0.1925 0.2601 0.2154 -0.0406 0.0273  0.0329  164 LEU   A O   
3432 O  O   B LEU   A 164 ? 0.1902 0.2424 0.1879 -0.0193 0.0286  -0.0087 164 LEU   A O   
3433 C  CB  A LEU   A 164 ? 0.1727 0.2385 0.2057 -0.0345 0.0087  0.0528  164 LEU   A CB  
3434 C  CB  B LEU   A 164 ? 0.1951 0.2340 0.1891 0.0028  0.0186  -0.0294 164 LEU   A CB  
3435 C  CG  A LEU   A 164 ? 0.1697 0.2296 0.2212 -0.0143 0.0158  0.0383  164 LEU   A CG  
3436 C  CG  B LEU   A 164 ? 0.2020 0.2261 0.1981 0.0018  0.0116  -0.0346 164 LEU   A CG  
3437 C  CD1 A LEU   A 164 ? 0.1593 0.2287 0.2305 -0.0010 -0.0063 0.0475  164 LEU   A CD1 
3438 C  CD1 B LEU   A 164 ? 0.1990 0.2270 0.1975 0.0043  0.0109  -0.0422 164 LEU   A CD1 
3439 C  CD2 A LEU   A 164 ? 0.1869 0.2293 0.2362 -0.0134 0.0324  0.0256  164 LEU   A CD2 
3440 C  CD2 B LEU   A 164 ? 0.2081 0.2203 0.2044 -0.0057 0.0155  -0.0302 164 LEU   A CD2 
3463 N  N   A VAL   A 165 ? 0.1775 0.2463 0.2084 -0.0261 0.0193  0.0747  165 VAL   A N   
3464 N  N   B VAL   A 165 ? 0.1851 0.2354 0.2041 -0.0089 0.0008  0.0067  165 VAL   A N   
3465 C  CA  A VAL   A 165 ? 0.1770 0.2480 0.1951 -0.0253 -0.0031 0.0771  165 VAL   A CA  
3466 C  CA  B VAL   A 165 ? 0.1842 0.2260 0.2183 -0.0114 0.0004  0.0040  165 VAL   A CA  
3467 C  C   A VAL   A 165 ? 0.1769 0.2629 0.1773 -0.0237 -0.0007 0.0743  165 VAL   A C   
3468 C  C   B VAL   A 165 ? 0.1812 0.2345 0.2204 -0.0078 0.0002  -0.0072 165 VAL   A C   
3469 O  O   A VAL   A 165 ? 0.1801 0.2734 0.1852 -0.0303 0.0106  0.0692  165 VAL   A O   
3470 O  O   B VAL   A 165 ? 0.1848 0.2388 0.2052 -0.0071 -0.0126 -0.0184 165 VAL   A O   
3471 C  CB  A VAL   A 165 ? 0.1854 0.2445 0.2199 -0.0219 -0.0057 0.0688  165 VAL   A CB  
3472 C  CB  B VAL   A 165 ? 0.1834 0.2120 0.2153 -0.0076 -0.0040 0.0231  165 VAL   A CB  
3473 C  CG1 A VAL   A 165 ? 0.1912 0.2460 0.2377 -0.0238 -0.0041 0.0659  165 VAL   A CG1 
3474 C  CG1 B VAL   A 165 ? 0.1852 0.2055 0.2074 -0.0148 -0.0128 0.0279  165 VAL   A CG1 
3475 C  CG2 A VAL   A 165 ? 0.1993 0.2523 0.2407 -0.0099 -0.0063 0.0673  165 VAL   A CG2 
3476 C  CG2 B VAL   A 165 ? 0.1816 0.2086 0.2226 0.0006  0.0010  0.0254  165 VAL   A CG2 
3495 N  N   A SER   A 166 ? 0.1743 0.2739 0.1985 -0.0195 -0.0040 0.0563  166 SER   A N   
3496 N  N   B SER   A 166 ? 0.1716 0.2435 0.2385 -0.0004 0.0118  0.0014  166 SER   A N   
3497 C  CA  A SER   A 166 ? 0.1816 0.2892 0.2295 -0.0137 0.0103  0.0451  166 SER   A CA  
3498 C  CA  B SER   A 166 ? 0.1645 0.2558 0.2531 0.0016  0.0179  0.0103  166 SER   A CA  
3499 C  C   A SER   A 166 ? 0.1745 0.3115 0.2489 -0.0090 0.0244  0.0228  166 SER   A C   
3500 C  C   B SER   A 166 ? 0.1756 0.2718 0.2610 0.0047  0.0142  0.0019  166 SER   A C   
3501 O  O   A SER   A 166 ? 0.1879 0.3266 0.3069 -0.0211 0.0328  -0.0171 166 SER   A O   
3502 O  O   B SER   A 166 ? 0.1752 0.2778 0.2757 0.0118  0.0248  -0.0080 166 SER   A O   
3503 C  CB  A SER   A 166 ? 0.1922 0.2921 0.2600 -0.0032 0.0153  0.0396  166 SER   A CB  
3504 C  CB  B SER   A 166 ? 0.1432 0.2582 0.2779 0.0013  0.0188  0.0256  166 SER   A CB  
3505 O  OG  A SER   A 166 ? 0.2123 0.2938 0.3064 -0.0085 0.0020  0.0484  166 SER   A OG  
3506 O  OG  B SER   A 166 ? 0.1212 0.2611 0.3111 -0.0010 0.0160  0.0455  166 SER   A OG  
3517 N  N   A SER   A 167 ? 0.1736 0.3295 0.2041 0.0051  0.0134  0.0405  167 SER   A N   
3518 N  N   B SER   A 167 ? 0.1934 0.2851 0.2612 0.0022  0.0077  0.0124  167 SER   A N   
3519 C  CA  A SER   A 167 ? 0.1957 0.3433 0.2152 0.0086  -0.0002 0.0309  167 SER   A CA  
3520 C  CA  B SER   A 167 ? 0.2113 0.2971 0.2747 -0.0006 0.0028  0.0137  167 SER   A CA  
3521 C  C   A SER   A 167 ? 0.1929 0.3472 0.2409 0.0093  0.0222  0.0263  167 SER   A C   
3522 C  C   B SER   A 167 ? 0.2215 0.2985 0.2688 -0.0025 0.0064  0.0211  167 SER   A C   
3523 O  O   A SER   A 167 ? 0.2174 0.3492 0.2757 -0.0003 0.0038  0.0197  167 SER   A O   
3524 O  O   B SER   A 167 ? 0.2304 0.2954 0.2657 -0.0002 -0.0032 0.0288  167 SER   A O   
3525 C  CB  A SER   A 167 ? 0.2099 0.3621 0.2138 0.0050  0.0099  0.0355  167 SER   A CB  
3526 C  CB  B SER   A 167 ? 0.2229 0.3114 0.3018 -0.0033 0.0015  0.0116  167 SER   A CB  
3527 O  OG  A SER   A 167 ? 0.2145 0.3745 0.2281 0.0115  0.0301  0.0496  167 SER   A OG  
3528 O  OG  B SER   A 167 ? 0.2300 0.3204 0.3211 -0.0008 -0.0064 0.0164  167 SER   A OG  
3539 N  N   A PHE   A 168 ? 0.1911 0.3471 0.2356 0.0212  0.0209  0.0417  168 PHE   A N   
3540 N  N   B PHE   A 168 ? 0.2322 0.3015 0.2640 -0.0047 0.0092  0.0200  168 PHE   A N   
3541 C  CA  A PHE   A 168 ? 0.1904 0.3385 0.2615 0.0202  0.0225  0.0292  168 PHE   A CA  
3542 C  CA  B PHE   A 168 ? 0.2482 0.3021 0.2679 -0.0085 0.0104  0.0127  168 PHE   A CA  
3543 C  C   A PHE   A 168 ? 0.1930 0.3557 0.2931 0.0033  0.0737  0.0203  168 PHE   A C   
3544 C  C   B PHE   A 168 ? 0.2718 0.3207 0.3129 -0.0071 0.0172  0.0053  168 PHE   A C   
3545 O  O   A PHE   A 168 ? 0.2194 0.3656 0.3661 -0.0101 0.0666  0.0309  168 PHE   A O   
3546 O  O   B PHE   A 168 ? 0.2779 0.3241 0.3346 -0.0132 0.0258  0.0062  168 PHE   A O   
3547 C  CB  A PHE   A 168 ? 0.1913 0.3072 0.2529 0.0072  -0.0068 0.0310  168 PHE   A CB  
3548 C  CB  B PHE   A 168 ? 0.2429 0.2851 0.2355 -0.0185 0.0048  0.0090  168 PHE   A CB  
3549 C  CG  A PHE   A 168 ? 0.1926 0.2841 0.2418 -0.0029 -0.0205 0.0432  168 PHE   A CG  
3550 C  CG  B PHE   A 168 ? 0.2379 0.2682 0.2206 -0.0251 -0.0053 0.0017  168 PHE   A CG  
3551 C  CD1 A PHE   A 168 ? 0.1963 0.2781 0.2438 -0.0174 -0.0177 0.0538  168 PHE   A CD1 
3552 C  CD1 B PHE   A 168 ? 0.2366 0.2605 0.2138 -0.0262 -0.0091 -0.0012 168 PHE   A CD1 
3553 C  CD2 A PHE   A 168 ? 0.1894 0.2798 0.2428 0.0003  -0.0016 0.0451  168 PHE   A CD2 
3554 C  CD2 B PHE   A 168 ? 0.2360 0.2614 0.2132 -0.0257 -0.0122 -0.0056 168 PHE   A CD2 
3555 C  CE1 A PHE   A 168 ? 0.1934 0.2730 0.2425 -0.0125 -0.0147 0.0670  168 PHE   A CE1 
3556 C  CE1 B PHE   A 168 ? 0.2308 0.2581 0.2141 -0.0311 -0.0129 -0.0061 168 PHE   A CE1 
3557 C  CE2 A PHE   A 168 ? 0.1843 0.2702 0.2529 -0.0100 0.0264  0.0598  168 PHE   A CE2 
3558 C  CE2 B PHE   A 168 ? 0.2358 0.2583 0.2149 -0.0286 -0.0143 -0.0061 168 PHE   A CE2 
3559 C  CZ  A PHE   A 168 ? 0.1878 0.2711 0.2477 -0.0127 0.0115  0.0669  168 PHE   A CZ  
3560 C  CZ  B PHE   A 168 ? 0.2327 0.2568 0.2181 -0.0307 -0.0123 -0.0028 168 PHE   A CZ  
3579 N  N   A LEU   A 169 ? 0.2218 0.3668 0.3220 -0.0048 0.0912  -0.0153 169 LEU   A N   
3580 N  N   B LEU   A 169 ? 0.2979 0.3379 0.3532 -0.0017 0.0097  -0.0075 169 LEU   A N   
3581 C  CA  A LEU   A 169 ? 0.2723 0.3853 0.3976 0.0017  0.0660  -0.0173 169 LEU   A CA  
3582 C  CA  B LEU   A 169 ? 0.3274 0.3577 0.4028 0.0103  -0.0010 -0.0144 169 LEU   A CA  
3583 C  C   A LEU   A 169 ? 0.2687 0.3725 0.3982 0.0032  0.0845  0.0014  169 LEU   A C   
3584 C  C   B LEU   A 169 ? 0.3375 0.3595 0.4175 0.0160  -0.0037 -0.0120 169 LEU   A C   
3585 O  O   A LEU   A 169 ? 0.2749 0.3685 0.4124 0.0078  0.0754  0.0078  169 LEU   A O   
3586 O  O   B LEU   A 169 ? 0.3408 0.3610 0.4285 0.0173  -0.0034 -0.0127 169 LEU   A O   
3587 C  CB  A LEU   A 169 ? 0.3195 0.4079 0.4445 0.0002  0.0389  -0.0367 169 LEU   A CB  
3588 C  CB  B LEU   A 169 ? 0.3416 0.3706 0.4305 0.0132  -0.0072 -0.0222 169 LEU   A CB  
3589 C  CG  A LEU   A 169 ? 0.3533 0.4260 0.4859 -0.0034 0.0117  -0.0575 169 LEU   A CG  
3590 C  CG  B LEU   A 169 ? 0.3527 0.3805 0.4542 0.0141  -0.0079 -0.0269 169 LEU   A CG  
3591 C  CD1 A LEU   A 169 ? 0.3756 0.4315 0.5131 -0.0011 0.0035  -0.0591 169 LEU   A CD1 
3592 C  CD1 B LEU   A 169 ? 0.3563 0.3818 0.4680 0.0161  -0.0092 -0.0258 169 LEU   A CD1 
3593 C  CD2 A LEU   A 169 ? 0.3619 0.4328 0.4911 -0.0049 0.0090  -0.0654 169 LEU   A CD2 
3594 C  CD2 B LEU   A 169 ? 0.3564 0.3851 0.4609 0.0128  -0.0085 -0.0287 169 LEU   A CD2 
3595 O  OXT A LEU   A 169 ? 0.2447 0.3709 0.3896 -0.0070 0.1139  0.0086  169 LEU   A OXT 
3596 O  OXT B LEU   A 169 ? 0.3420 0.3599 0.4220 0.0192  -0.0028 -0.0120 169 LEU   A OXT 
3619 N  N   . SER   B 1   ? 0.3913 0.3683 0.4252 -0.0990 -0.0852 0.0566  1   SER   B N   
3620 C  CA  . SER   B 1   ? 0.3806 0.3726 0.4056 -0.1035 -0.0892 0.0500  1   SER   B CA  
3621 C  C   . SER   B 1   ? 0.3463 0.3716 0.3717 -0.0930 -0.0927 0.0724  1   SER   B C   
3622 O  O   . SER   B 1   ? 0.3604 0.3677 0.3331 -0.0755 -0.0994 0.0695  1   SER   B O   
3623 C  CB  . SER   B 1   ? 0.3951 0.3663 0.4147 -0.1100 -0.0848 0.0158  1   SER   B CB  
3624 O  OG  . SER   B 1   ? 0.4173 0.3839 0.4783 -0.1091 -0.0740 0.0026  1   SER   B OG  
3632 N  N   A MET   B 2   ? 0.3267 0.3754 0.3778 -0.0983 -0.0860 0.1139  2   MET   B N   
3633 N  N   B MET   B 2   ? 0.3428 0.3706 0.3789 -0.0818 -0.0761 0.0770  2   MET   B N   
3634 C  CA  A MET   B 2   ? 0.3124 0.3824 0.3896 -0.0851 -0.0847 0.1319  2   MET   B CA  
3635 C  CA  B MET   B 2   ? 0.3390 0.3697 0.3808 -0.0656 -0.0627 0.0751  2   MET   B CA  
3636 C  C   A MET   B 2   ? 0.2833 0.3649 0.3603 -0.0659 -0.0858 0.1610  2   MET   B C   
3637 C  C   B MET   B 2   ? 0.3219 0.3534 0.3537 -0.0544 -0.0501 0.0764  2   MET   B C   
3638 O  O   A MET   B 2   ? 0.2790 0.3873 0.3679 -0.0518 -0.1051 0.1610  2   MET   B O   
3639 O  O   B MET   B 2   ? 0.3244 0.3628 0.3616 -0.0503 -0.0462 0.0742  2   MET   B O   
3640 C  CB  A MET   B 2   ? 0.3442 0.4187 0.4765 -0.0655 -0.0744 0.1019  2   MET   B CB  
3641 C  CB  B MET   B 2   ? 0.3550 0.3876 0.4216 -0.0540 -0.0626 0.0700  2   MET   B CB  
3642 C  CG  A MET   B 2   ? 0.3717 0.4521 0.5694 -0.0473 -0.0575 0.0862  2   MET   B CG  
3643 C  CG  B MET   B 2   ? 0.3678 0.4024 0.4592 -0.0434 -0.0615 0.0725  2   MET   B CG  
3644 S  SD  A MET   B 2   ? 0.3992 0.4855 0.6560 -0.0324 -0.0402 0.0703  2   MET   B SD  
3645 S  SD  B MET   B 2   ? 0.3783 0.4162 0.4929 -0.0345 -0.0633 0.0752  2   MET   B SD  
3646 C  CE  A MET   B 2   ? 0.3981 0.4912 0.6457 -0.0328 -0.0272 0.0703  2   MET   B CE  
3647 C  CE  B MET   B 2   ? 0.3784 0.4179 0.4944 -0.0365 -0.0577 0.0695  2   MET   B CE  
3666 N  N   A VAL   B 3   ? 0.2518 0.3157 0.3259 -0.0840 -0.0730 0.1763  3   VAL   B N   
3667 N  N   B VAL   B 3   ? 0.2997 0.3242 0.3220 -0.0539 -0.0452 0.0773  3   VAL   B N   
3668 C  CA  A VAL   B 3   ? 0.2457 0.2711 0.3229 -0.0775 -0.0771 0.1501  3   VAL   B CA  
3669 C  CA  B VAL   B 3   ? 0.2818 0.2941 0.2985 -0.0504 -0.0442 0.0741  3   VAL   B CA  
3670 C  C   A VAL   B 3   ? 0.2256 0.2576 0.2704 -0.0647 -0.0740 0.1205  3   VAL   B C   
3671 C  C   B VAL   B 3   ? 0.2572 0.2680 0.2619 -0.0485 -0.0458 0.0773  3   VAL   B C   
3672 O  O   A VAL   B 3   ? 0.2224 0.2763 0.2819 -0.0650 -0.0797 0.1230  3   VAL   B O   
3673 O  O   B VAL   B 3   ? 0.2586 0.2777 0.2580 -0.0436 -0.0440 0.0778  3   VAL   B O   
3674 C  CB  A VAL   B 3   ? 0.2678 0.2664 0.3913 -0.0855 -0.0755 0.1209  3   VAL   B CB  
3675 C  CB  B VAL   B 3   ? 0.2901 0.2925 0.3135 -0.0510 -0.0404 0.0665  3   VAL   B CB  
3676 C  CG1 A VAL   B 3   ? 0.2827 0.2634 0.4138 -0.0822 -0.0821 0.1133  3   VAL   B CG1 
3677 C  CG1 B VAL   B 3   ? 0.2949 0.2912 0.3204 -0.0504 -0.0398 0.0642  3   VAL   B CG1 
3678 C  CG2 A VAL   B 3   ? 0.2720 0.2704 0.4144 -0.0917 -0.0577 0.1308  3   VAL   B CG2 
3679 C  CG2 B VAL   B 3   ? 0.2928 0.2941 0.3167 -0.0514 -0.0374 0.0687  3   VAL   B CG2 
3698 N  N   . ASN   B 4   ? 0.2374 0.2326 0.2429 -0.0517 -0.0508 0.0826  4   ASN   B N   
3699 C  CA  . ASN   B 4   ? 0.2417 0.2095 0.2088 -0.0450 -0.0346 0.0417  4   ASN   B CA  
3700 C  C   . ASN   B 4   ? 0.2506 0.2310 0.2032 -0.0399 -0.0279 0.0217  4   ASN   B C   
3701 O  O   . ASN   B 4   ? 0.2480 0.2332 0.2284 -0.0396 -0.0204 -0.0022 4   ASN   B O   
3702 C  CB  . ASN   B 4   ? 0.2418 0.2007 0.1950 -0.0387 -0.0391 0.0409  4   ASN   B CB  
3703 C  CG  . ASN   B 4   ? 0.2325 0.1900 0.1849 -0.0459 -0.0466 0.0298  4   ASN   B CG  
3704 O  OD1 . ASN   B 4   ? 0.2235 0.1744 0.1962 -0.0440 -0.0509 0.0335  4   ASN   B OD1 
3705 N  ND2 . ASN   B 4   ? 0.2456 0.1909 0.2082 -0.0295 -0.0405 0.0220  4   ASN   B ND2 
3713 N  N   . SER   B 5   ? 0.2541 0.2518 0.1930 -0.0541 -0.0047 0.0336  5   SER   B N   
3714 C  CA  . SER   B 5   ? 0.2780 0.2967 0.2285 -0.0428 0.0098  0.0343  5   SER   B CA  
3715 C  C   . SER   B 5   ? 0.2945 0.3016 0.2737 -0.0580 0.0350  0.0309  5   SER   B C   
3716 O  O   . SER   B 5   ? 0.3103 0.3015 0.3704 -0.0510 0.0608  0.0238  5   SER   B O   
3717 C  CB  . SER   B 5   ? 0.2971 0.3246 0.2744 -0.0308 0.0094  0.0416  5   SER   B CB  
3718 O  OG  . SER   B 5   ? 0.3388 0.3579 0.3470 -0.0158 0.0125  0.0424  5   SER   B OG  
3724 N  N   . PHE   B 6   ? 0.3109 0.3206 0.2400 -0.0541 0.0499  0.0376  6   PHE   B N   
3725 C  CA  . PHE   B 6   ? 0.3178 0.3157 0.2011 -0.0751 0.0489  0.0133  6   PHE   B CA  
3726 C  C   . PHE   B 6   ? 0.3718 0.3470 0.2503 -0.0824 0.0656  -0.0202 6   PHE   B C   
3727 O  O   . PHE   B 6   ? 0.3917 0.3942 0.2812 -0.0730 0.0334  -0.0477 6   PHE   B O   
3728 C  CB  . PHE   B 6   ? 0.2834 0.2874 0.1924 -0.0689 0.0335  0.0065  6   PHE   B CB  
3729 C  CG  . PHE   B 6   ? 0.2396 0.2572 0.1813 -0.0652 0.0270  0.0051  6   PHE   B CG  
3730 C  CD1 . PHE   B 6   ? 0.2337 0.2401 0.1773 -0.0643 -0.0017 0.0076  6   PHE   B CD1 
3731 C  CD2 . PHE   B 6   ? 0.2202 0.2583 0.1894 -0.0412 0.0135  0.0379  6   PHE   B CD2 
3732 C  CE1 . PHE   B 6   ? 0.2294 0.2168 0.1810 -0.0415 0.0001  -0.0064 6   PHE   B CE1 
3733 C  CE2 . PHE   B 6   ? 0.2253 0.2503 0.2190 -0.0355 0.0152  0.0341  6   PHE   B CE2 
3734 C  CZ  . PHE   B 6   ? 0.2227 0.2227 0.2048 -0.0365 0.0071  0.0070  6   PHE   B CZ  
3744 N  N   A SER   B 7   ? 0.3994 0.3161 0.2322 -0.1082 0.0958  -0.0501 7   SER   B N   
3745 N  N   B SER   B 7   ? 0.3842 0.3397 0.2819 -0.0865 0.0684  -0.0253 7   SER   B N   
3746 C  CA  A SER   B 7   ? 0.4303 0.3263 0.2871 -0.1058 0.1119  -0.0673 7   SER   B CA  
3747 C  CA  B SER   B 7   ? 0.3965 0.3412 0.3227 -0.0826 0.0691  -0.0263 7   SER   B CA  
3748 C  C   A SER   B 7   ? 0.4229 0.3104 0.2809 -0.1172 0.1240  -0.0706 7   SER   B C   
3749 C  C   B SER   B 7   ? 0.3945 0.3284 0.3242 -0.0852 0.0731  -0.0297 7   SER   B C   
3750 O  O   A SER   B 7   ? 0.4269 0.3104 0.3188 -0.1236 0.1350  -0.0471 7   SER   B O   
3751 O  O   B SER   B 7   ? 0.3963 0.3299 0.3368 -0.0847 0.0742  -0.0215 7   SER   B O   
3752 C  CB  A SER   B 7   ? 0.4560 0.3452 0.3555 -0.0985 0.1218  -0.0747 7   SER   B CB  
3753 C  CB  B SER   B 7   ? 0.4069 0.3510 0.3632 -0.0776 0.0696  -0.0259 7   SER   B CB  
3754 O  OG  A SER   B 7   ? 0.4726 0.3649 0.4290 -0.1007 0.1184  -0.0556 7   SER   B OG  
3755 O  OG  B SER   B 7   ? 0.4134 0.3596 0.3953 -0.0756 0.0694  -0.0220 7   SER   B OG  
3766 N  N   A GLY   B 8   ? 0.4159 0.3030 0.2849 -0.0995 0.1323  -0.0785 8   GLY   B N   
3767 N  N   B GLY   B 8   ? 0.3908 0.3152 0.3198 -0.0819 0.0802  -0.0376 8   GLY   B N   
3768 C  CA  A GLY   B 8   ? 0.4038 0.2960 0.3022 -0.0866 0.1363  -0.0854 8   GLY   B CA  
3769 C  CA  B GLY   B 8   ? 0.3851 0.3018 0.3111 -0.0795 0.0882  -0.0482 8   GLY   B CA  
3770 C  C   A GLY   B 8   ? 0.3873 0.2794 0.2972 -0.0837 0.1306  -0.0677 8   GLY   B C   
3771 C  C   B GLY   B 8   ? 0.3781 0.2848 0.2938 -0.0790 0.0948  -0.0536 8   GLY   B C   
3772 O  O   A GLY   B 8   ? 0.3952 0.2865 0.3362 -0.0765 0.1332  -0.0714 8   GLY   B O   
3773 O  O   B GLY   B 8   ? 0.3808 0.2891 0.3027 -0.0765 0.0916  -0.0540 8   GLY   B O   
3780 N  N   . TYR   B 9   ? 0.3710 0.2679 0.2697 -0.0754 0.1013  -0.0677 9   TYR   B N   
3781 C  CA  . TYR   B 9   ? 0.3436 0.2316 0.2272 -0.0563 0.0711  -0.0554 9   TYR   B CA  
3782 C  C   . TYR   B 9   ? 0.3425 0.2258 0.2233 -0.0537 0.0275  -0.0465 9   TYR   B C   
3783 O  O   . TYR   B 9   ? 0.3661 0.2551 0.2671 -0.0546 0.0266  -0.0270 9   TYR   B O   
3784 C  CB  . TYR   B 9   ? 0.3320 0.2020 0.2409 -0.0427 0.0714  -0.0469 9   TYR   B CB  
3785 C  CG  . TYR   B 9   ? 0.3206 0.1840 0.2411 -0.0526 0.0723  -0.0580 9   TYR   B CG  
3786 C  CD1 . TYR   B 9   ? 0.3222 0.1883 0.2677 -0.0781 0.0721  -0.0479 9   TYR   B CD1 
3787 C  CD2 . TYR   B 9   ? 0.3189 0.1840 0.2354 -0.0405 0.0666  -0.0528 9   TYR   B CD2 
3788 C  CE1 . TYR   B 9   ? 0.3215 0.1986 0.2752 -0.0858 0.0900  -0.0608 9   TYR   B CE1 
3789 C  CE2 . TYR   B 9   ? 0.3256 0.1698 0.2571 -0.0499 0.0730  -0.0448 9   TYR   B CE2 
3790 C  CZ  . TYR   B 9   ? 0.3219 0.1984 0.2847 -0.0685 0.0807  -0.0713 9   TYR   B CZ  
3791 O  OH  . TYR   B 9   ? 0.3081 0.2006 0.3046 -0.0784 0.0779  -0.0836 9   TYR   B OH  
3802 N  N   . LEU   B 10  ? 0.3217 0.2037 0.1966 -0.0510 0.0183  -0.0352 10  LEU   B N   
3803 C  CA  . LEU   B 10  ? 0.3220 0.2018 0.2109 -0.0646 -0.0023 -0.0317 10  LEU   B CA  
3804 C  C   . LEU   B 10  ? 0.2959 0.2041 0.1931 -0.0650 -0.0152 -0.0242 10  LEU   B C   
3805 O  O   . LEU   B 10  ? 0.2843 0.2220 0.1938 -0.0484 -0.0108 -0.0183 10  LEU   B O   
3806 C  CB  . LEU   B 10  ? 0.3424 0.2067 0.2294 -0.0688 -0.0243 -0.0120 10  LEU   B CB  
3807 C  CG  . LEU   B 10  ? 0.3641 0.2104 0.2658 -0.0635 -0.0602 -0.0180 10  LEU   B CG  
3808 C  CD1 . LEU   B 10  ? 0.3746 0.2207 0.3114 -0.0658 -0.0580 -0.0251 10  LEU   B CD1 
3809 C  CD2 . LEU   B 10  ? 0.3786 0.2140 0.3161 -0.0683 -0.0514 -0.0072 10  LEU   B CD2 
3821 N  N   . LYS   B 11  ? 0.3072 0.2358 0.1996 -0.0516 -0.0273 -0.0251 11  LYS   B N   
3822 C  CA  . LYS   B 11  ? 0.3124 0.2648 0.2151 -0.0450 -0.0468 -0.0267 11  LYS   B CA  
3823 C  C   . LYS   B 11  ? 0.2929 0.2420 0.2288 -0.0655 -0.0453 -0.0430 11  LYS   B C   
3824 O  O   . LYS   B 11  ? 0.3125 0.2757 0.2941 -0.0678 -0.0392 -0.0810 11  LYS   B O   
3825 C  CB  . LYS   B 11  ? 0.3461 0.3255 0.2781 -0.0057 -0.0486 -0.0172 11  LYS   B CB  
3826 C  CG  . LYS   B 11  ? 0.3790 0.3623 0.3455 0.0163  -0.0527 -0.0065 11  LYS   B CG  
3827 C  CD  . LYS   B 11  ? 0.4079 0.3904 0.4245 0.0238  -0.0534 -0.0132 11  LYS   B CD  
3828 C  CE  . LYS   B 11  ? 0.4313 0.4061 0.4822 0.0234  -0.0476 -0.0181 11  LYS   B CE  
3829 N  NZ  . LYS   B 11  ? 0.4470 0.4182 0.5172 0.0231  -0.0419 -0.0172 11  LYS   B NZ  
3843 N  N   . LEU   B 12  ? 0.2664 0.2177 0.2318 -0.0588 -0.0451 -0.0377 12  LEU   B N   
3844 C  CA  . LEU   B 12  ? 0.2554 0.1967 0.2651 -0.0562 -0.0427 -0.0227 12  LEU   B CA  
3845 C  C   . LEU   B 12  ? 0.2487 0.2045 0.2725 -0.0604 -0.0605 -0.0274 12  LEU   B C   
3846 O  O   . LEU   B 12  ? 0.2580 0.1883 0.3007 -0.0629 -0.0641 -0.0145 12  LEU   B O   
3847 C  CB  . LEU   B 12  ? 0.2496 0.1684 0.2586 -0.0496 -0.0248 -0.0259 12  LEU   B CB  
3848 C  CG  . LEU   B 12  ? 0.2453 0.1884 0.2575 -0.0487 -0.0056 -0.0267 12  LEU   B CG  
3849 C  CD1 . LEU   B 12  ? 0.2506 0.2017 0.2301 -0.0327 -0.0033 -0.0108 12  LEU   B CD1 
3850 C  CD2 . LEU   B 12  ? 0.2599 0.1991 0.2870 -0.0520 0.0104  -0.0429 12  LEU   B CD2 
3862 N  N   . THR   B 13  ? 0.2465 0.2138 0.2791 -0.0508 -0.0470 -0.0497 13  THR   B N   
3863 C  CA  . THR   B 13  ? 0.2486 0.2071 0.2676 -0.0687 -0.0776 -0.0454 13  THR   B CA  
3864 C  C   . THR   B 13  ? 0.2855 0.2230 0.2917 -0.0722 -0.0787 -0.0235 13  THR   B C   
3865 O  O   . THR   B 13  ? 0.3082 0.2243 0.2978 -0.0740 -0.0328 -0.0198 13  THR   B O   
3866 C  CB  . THR   B 13  ? 0.2405 0.2124 0.2825 -0.0583 -0.0669 -0.0135 13  THR   B CB  
3867 O  OG1 . THR   B 13  ? 0.2233 0.1952 0.2784 -0.0587 -0.0519 -0.0144 13  THR   B OG1 
3868 C  CG2 . THR   B 13  ? 0.2376 0.2101 0.2824 -0.0504 -0.0449 -0.0026 13  THR   B CG2 
3876 N  N   A ASP   B 14  ? 0.2991 0.2478 0.3005 -0.0730 -0.1131 -0.0104 14  ASP   B N   
3877 N  N   B ASP   B 14  ? 0.2923 0.2378 0.3046 -0.0692 -0.0840 -0.0126 14  ASP   B N   
3878 C  CA  A ASP   B 14  ? 0.3105 0.2661 0.3367 -0.0750 -0.1089 0.0128  14  ASP   B CA  
3879 C  CA  B ASP   B 14  ? 0.2951 0.2480 0.3238 -0.0667 -0.0803 0.0013  14  ASP   B CA  
3880 C  C   A ASP   B 14  ? 0.2951 0.2424 0.2931 -0.0854 -0.0996 0.0049  14  ASP   B C   
3881 C  C   B ASP   B 14  ? 0.2772 0.2323 0.2892 -0.0700 -0.0891 -0.0002 14  ASP   B C   
3882 O  O   A ASP   B 14  ? 0.3336 0.2643 0.3066 -0.0815 -0.0792 0.0164  14  ASP   B O   
3883 O  O   B ASP   B 14  ? 0.2900 0.2368 0.2915 -0.0656 -0.0839 0.0010  14  ASP   B O   
3884 C  CB  A ASP   B 14  ? 0.3355 0.3077 0.4130 -0.0651 -0.1245 0.0195  14  ASP   B CB  
3885 C  CB  B ASP   B 14  ? 0.3137 0.2711 0.3758 -0.0590 -0.0737 0.0074  14  ASP   B CB  
3886 C  CG  A ASP   B 14  ? 0.3690 0.3521 0.5027 -0.0497 -0.1259 0.0062  14  ASP   B CG  
3887 C  CG  B ASP   B 14  ? 0.3330 0.2936 0.4256 -0.0471 -0.0673 0.0056  14  ASP   B CG  
3888 O  OD1 A ASP   B 14  ? 0.3871 0.3647 0.5159 -0.0559 -0.1292 -0.0158 14  ASP   B OD1 
3889 O  OD1 B ASP   B 14  ? 0.3413 0.3055 0.4364 -0.0456 -0.0676 -0.0046 14  ASP   B OD1 
3890 O  OD2 A ASP   B 14  ? 0.3726 0.3704 0.5545 -0.0401 -0.1287 0.0195  14  ASP   B OD2 
3891 O  OD2 B ASP   B 14  ? 0.3387 0.2958 0.4500 -0.0439 -0.0652 0.0182  14  ASP   B OD2 
3900 N  N   . ASN   B 15  ? 0.2510 0.2146 0.2602 -0.0669 -0.0959 0.0017  15  ASN   B N   
3901 C  CA  . ASN   B 15  ? 0.2085 0.1946 0.2371 -0.0469 -0.0748 -0.0076 15  ASN   B CA  
3902 C  C   . ASN   B 15  ? 0.1945 0.1757 0.2101 -0.0307 -0.0485 -0.0020 15  ASN   B C   
3903 O  O   . ASN   B 15  ? 0.1862 0.1740 0.2484 -0.0296 -0.0527 -0.0059 15  ASN   B O   
3904 C  CB  . ASN   B 15  ? 0.1996 0.1935 0.2475 -0.0144 -0.0570 0.0039  15  ASN   B CB  
3905 C  CG  . ASN   B 15  ? 0.1771 0.1870 0.2373 -0.0227 -0.0260 0.0075  15  ASN   B CG  
3906 O  OD1 . ASN   B 15  ? 0.2033 0.2111 0.2764 -0.0392 -0.0207 0.0076  15  ASN   B OD1 
3907 N  ND2 . ASN   B 15  ? 0.1762 0.1623 0.2444 -0.0164 0.0117  -0.0062 15  ASN   B ND2 
3915 N  N   . VAL   B 16  ? 0.1952 0.1708 0.2060 -0.0359 -0.0512 -0.0093 16  VAL   B N   
3916 C  CA  . VAL   B 16  ? 0.1945 0.1672 0.1904 -0.0252 -0.0355 -0.0121 16  VAL   B CA  
3917 C  C   . VAL   B 16  ? 0.1933 0.1784 0.1971 -0.0341 -0.0391 -0.0049 16  VAL   B C   
3918 O  O   . VAL   B 16  ? 0.1928 0.1917 0.2289 -0.0295 -0.0352 -0.0232 16  VAL   B O   
3919 C  CB  . VAL   B 16  ? 0.1893 0.1771 0.2056 -0.0151 -0.0297 -0.0206 16  VAL   B CB  
3920 C  CG1 . VAL   B 16  ? 0.1987 0.1657 0.2089 -0.0116 -0.0166 -0.0132 16  VAL   B CG1 
3921 C  CG2 . VAL   B 16  ? 0.1940 0.1757 0.2328 -0.0178 -0.0159 -0.0250 16  VAL   B CG2 
3931 N  N   . TYR   B 17  ? 0.1989 0.1969 0.1798 -0.0383 -0.0258 -0.0191 17  TYR   B N   
3932 C  CA  . TYR   B 17  ? 0.2123 0.1981 0.1821 -0.0402 -0.0106 -0.0118 17  TYR   B CA  
3933 C  C   . TYR   B 17  ? 0.2071 0.1686 0.1838 -0.0414 -0.0208 -0.0160 17  TYR   B C   
3934 O  O   . TYR   B 17  ? 0.2115 0.1773 0.2040 -0.0367 -0.0223 -0.0359 17  TYR   B O   
3935 C  CB  . TYR   B 17  ? 0.2346 0.2467 0.1926 -0.0264 -0.0077 0.0357  17  TYR   B CB  
3936 C  CG  . TYR   B 17  ? 0.2772 0.2890 0.2306 -0.0184 -0.0280 0.0391  17  TYR   B CG  
3937 C  CD1 . TYR   B 17  ? 0.2918 0.3008 0.2505 -0.0122 -0.0502 0.0473  17  TYR   B CD1 
3938 C  CD2 . TYR   B 17  ? 0.3127 0.3242 0.2518 -0.0072 -0.0408 0.0434  17  TYR   B CD2 
3939 C  CE1 . TYR   B 17  ? 0.3164 0.3330 0.2627 -0.0019 -0.0714 0.0326  17  TYR   B CE1 
3940 C  CE2 . TYR   B 17  ? 0.3301 0.3451 0.2611 0.0079  -0.0646 0.0497  17  TYR   B CE2 
3941 C  CZ  . TYR   B 17  ? 0.3393 0.3496 0.2666 0.0109  -0.0766 0.0371  17  TYR   B CZ  
3942 O  OH  . TYR   B 17  ? 0.3488 0.3595 0.3012 0.0196  -0.0855 0.0399  17  TYR   B OH  
3952 N  N   . ILE   B 18  ? 0.2136 0.1739 0.1801 -0.0298 -0.0142 -0.0205 18  ILE   B N   
3953 C  CA  . ILE   B 18  ? 0.2113 0.1645 0.1789 -0.0372 -0.0239 -0.0142 18  ILE   B CA  
3954 C  C   . ILE   B 18  ? 0.2247 0.1679 0.1708 -0.0305 -0.0051 -0.0234 18  ILE   B C   
3955 O  O   . ILE   B 18  ? 0.2458 0.1776 0.1890 -0.0317 0.0146  -0.0292 18  ILE   B O   
3956 C  CB  . ILE   B 18  ? 0.2172 0.1536 0.1983 -0.0403 -0.0125 -0.0228 18  ILE   B CB  
3957 C  CG1 . ILE   B 18  ? 0.2245 0.1618 0.2048 -0.0375 -0.0138 0.0043  18  ILE   B CG1 
3958 C  CG2 . ILE   B 18  ? 0.2245 0.1627 0.1952 -0.0338 -0.0151 -0.0069 18  ILE   B CG2 
3959 C  CD1 . ILE   B 18  ? 0.2318 0.1951 0.2109 -0.0325 -0.0292 0.0290  18  ILE   B CD1 
3971 N  N   . LYS   B 19  ? 0.2197 0.1684 0.2119 -0.0136 0.0253  -0.0348 19  LYS   B N   
3972 C  CA  . LYS   B 19  ? 0.2312 0.1685 0.2108 -0.0272 0.0308  -0.0352 19  LYS   B CA  
3973 C  C   . LYS   B 19  ? 0.2206 0.1626 0.2283 -0.0185 0.0307  -0.0484 19  LYS   B C   
3974 O  O   . LYS   B 19  ? 0.2080 0.1751 0.2115 -0.0063 0.0112  -0.0358 19  LYS   B O   
3975 C  CB  . LYS   B 19  ? 0.2413 0.1922 0.2170 -0.0405 0.0325  -0.0183 19  LYS   B CB  
3976 C  CG  . LYS   B 19  ? 0.2618 0.2199 0.2445 -0.0373 0.0395  -0.0284 19  LYS   B CG  
3977 C  CD  . LYS   B 19  ? 0.2942 0.2579 0.2548 -0.0410 0.0518  -0.0204 19  LYS   B CD  
3978 C  CE  . LYS   B 19  ? 0.3250 0.2894 0.2793 -0.0465 0.0458  -0.0248 19  LYS   B CE  
3979 N  NZ  . LYS   B 19  ? 0.3557 0.3185 0.2991 -0.0473 0.0502  -0.0239 19  LYS   B NZ  
3993 N  N   . ASN   B 20  ? 0.2347 0.1748 0.2583 -0.0234 0.0363  -0.0582 20  ASN   B N   
3994 C  CA  . ASN   B 20  ? 0.2250 0.1911 0.2818 -0.0151 0.0556  -0.0764 20  ASN   B CA  
3995 C  C   . ASN   B 20  ? 0.2121 0.2221 0.2886 -0.0188 0.0655  -0.0852 20  ASN   B C   
3996 O  O   . ASN   B 20  ? 0.2325 0.2630 0.3150 -0.0374 0.0776  -0.0878 20  ASN   B O   
3997 C  CB  . ASN   B 20  ? 0.2551 0.2008 0.3119 -0.0016 0.0281  -0.0713 20  ASN   B CB  
3998 C  CG  . ASN   B 20  ? 0.2770 0.2074 0.3114 0.0285  0.0437  -0.0841 20  ASN   B CG  
3999 O  OD1 . ASN   B 20  ? 0.3136 0.2459 0.3421 0.0487  0.0263  -0.0969 20  ASN   B OD1 
4000 N  ND2 . ASN   B 20  ? 0.2607 0.2072 0.2907 0.0297  0.0337  -0.0738 20  ASN   B ND2 
4007 N  N   . ALA   B 21  ? 0.2171 0.1896 0.2962 -0.0290 0.0527  -0.0655 21  ALA   B N   
4008 C  CA  . ALA   B 21  ? 0.2266 0.1974 0.3140 -0.0243 0.0465  -0.0525 21  ALA   B CA  
4009 C  C   . ALA   B 21  ? 0.2263 0.1984 0.2711 -0.0296 0.0513  -0.0384 21  ALA   B C   
4010 O  O   . ALA   B 21  ? 0.2356 0.2025 0.2492 -0.0470 0.0509  -0.0401 21  ALA   B O   
4011 C  CB  . ALA   B 21  ? 0.2504 0.2297 0.3335 -0.0377 0.0296  -0.0247 21  ALA   B CB  
4017 N  N   . ASP   B 22  ? 0.2077 0.1798 0.2655 -0.0274 0.0394  -0.0391 22  ASP   B N   
4018 C  CA  . ASP   B 22  ? 0.2105 0.1724 0.2582 -0.0110 0.0231  -0.0163 22  ASP   B CA  
4019 C  C   . ASP   B 22  ? 0.2024 0.1501 0.2064 -0.0111 0.0065  -0.0045 22  ASP   B C   
4020 O  O   . ASP   B 22  ? 0.2064 0.1611 0.2193 -0.0037 -0.0014 -0.0008 22  ASP   B O   
4021 C  CB  . ASP   B 22  ? 0.2134 0.1817 0.2883 -0.0026 0.0314  -0.0136 22  ASP   B CB  
4022 C  CG  . ASP   B 22  ? 0.2142 0.1986 0.3412 0.0086  -0.0074 -0.0133 22  ASP   B CG  
4023 O  OD1 . ASP   B 22  ? 0.2332 0.1880 0.3529 0.0107  -0.0312 -0.0104 22  ASP   B OD1 
4024 O  OD2 . ASP   B 22  ? 0.2279 0.2304 0.4184 0.0132  -0.0367 -0.0308 22  ASP   B OD2 
4029 N  N   . ILE   B 23  ? 0.2081 0.1618 0.2034 -0.0173 -0.0063 0.0196  23  ILE   B N   
4030 C  CA  . ILE   B 23  ? 0.1978 0.1758 0.1906 -0.0106 -0.0019 0.0082  23  ILE   B CA  
4031 C  C   . ILE   B 23  ? 0.1954 0.1703 0.1665 0.0034  -0.0135 0.0168  23  ILE   B C   
4032 O  O   . ILE   B 23  ? 0.1849 0.1684 0.1737 0.0014  -0.0031 0.0174  23  ILE   B O   
4033 C  CB  . ILE   B 23  ? 0.1866 0.1923 0.2119 -0.0079 0.0023  0.0138  23  ILE   B CB  
4034 C  CG1 . ILE   B 23  ? 0.1891 0.2053 0.2257 -0.0027 0.0169  0.0272  23  ILE   B CG1 
4035 C  CG2 . ILE   B 23  ? 0.2053 0.2038 0.2279 -0.0147 0.0041  0.0044  23  ILE   B CG2 
4036 C  CD1 . ILE   B 23  ? 0.2070 0.2071 0.2343 0.0032  0.0095  0.0219  23  ILE   B CD1 
4048 N  N   . VAL   B 24  ? 0.1983 0.1627 0.1809 -0.0038 -0.0194 0.0015  24  VAL   B N   
4049 C  CA  . VAL   B 24  ? 0.1852 0.1821 0.2209 -0.0056 -0.0197 -0.0025 24  VAL   B CA  
4050 C  C   . VAL   B 24  ? 0.1795 0.1991 0.2414 -0.0115 -0.0035 0.0033  24  VAL   B C   
4051 O  O   . VAL   B 24  ? 0.1720 0.2047 0.2411 -0.0142 -0.0011 0.0101  24  VAL   B O   
4052 C  CB  . VAL   B 24  ? 0.1908 0.1846 0.2222 -0.0045 -0.0229 0.0063  24  VAL   B CB  
4053 C  CG1 . VAL   B 24  ? 0.1984 0.1985 0.2783 -0.0039 -0.0368 0.0056  24  VAL   B CG1 
4054 C  CG2 . VAL   B 24  ? 0.1936 0.2184 0.2252 0.0063  -0.0113 -0.0141 24  VAL   B CG2 
4064 N  N   . GLU   B 25  ? 0.2016 0.2093 0.2503 -0.0156 0.0160  -0.0044 25  GLU   B N   
4065 C  CA  . GLU   B 25  ? 0.2133 0.2207 0.2610 -0.0006 0.0212  -0.0036 25  GLU   B CA  
4066 C  C   . GLU   B 25  ? 0.2137 0.1910 0.2279 -0.0076 0.0185  0.0074  25  GLU   B C   
4067 O  O   . GLU   B 25  ? 0.2074 0.2020 0.2655 -0.0087 0.0135  0.0178  25  GLU   B O   
4068 C  CB  . GLU   B 25  ? 0.2545 0.2695 0.3208 0.0190  0.0254  -0.0040 25  GLU   B CB  
4069 C  CG  . GLU   B 25  ? 0.3004 0.3275 0.4213 0.0256  0.0195  -0.0105 25  GLU   B CG  
4070 C  CD  . GLU   B 25  ? 0.3630 0.3950 0.5066 0.0186  0.0159  -0.0145 25  GLU   B CD  
4071 O  OE1 . GLU   B 25  ? 0.3684 0.4231 0.5438 0.0250  0.0236  -0.0130 25  GLU   B OE1 
4072 O  OE2 . GLU   B 25  ? 0.3744 0.4217 0.5439 0.0193  0.0064  -0.0278 25  GLU   B OE2 
4079 N  N   . GLU   B 26  ? 0.2086 0.1820 0.2041 -0.0320 0.0143  -0.0018 26  GLU   B N   
4080 C  CA  . GLU   B 26  ? 0.2202 0.1904 0.2042 -0.0366 -0.0043 -0.0018 26  GLU   B CA  
4081 C  C   . GLU   B 26  ? 0.2081 0.1930 0.1888 -0.0247 0.0055  0.0138  26  GLU   B C   
4082 O  O   . GLU   B 26  ? 0.2135 0.2252 0.1998 -0.0180 -0.0041 0.0337  26  GLU   B O   
4083 C  CB  . GLU   B 26  ? 0.2548 0.2222 0.2337 -0.0551 0.0300  -0.0025 26  GLU   B CB  
4084 C  CG  . GLU   B 26  ? 0.2994 0.2693 0.2852 -0.0604 0.0302  -0.0373 26  GLU   B CG  
4085 C  CD  . GLU   B 26  ? 0.3185 0.2936 0.2973 -0.0855 0.0368  -0.0600 26  GLU   B CD  
4086 O  OE1 . GLU   B 26  ? 0.3383 0.2765 0.3041 -0.0920 0.0786  -0.0432 26  GLU   B OE1 
4087 O  OE2 . GLU   B 26  ? 0.3173 0.3526 0.3425 -0.0787 0.0313  -0.0417 26  GLU   B OE2 
4094 N  N   . ALA   B 27  ? 0.1831 0.1862 0.1967 -0.0332 0.0150  0.0125  27  ALA   B N   
4095 C  CA  . ALA   B 27  ? 0.2028 0.1707 0.2068 -0.0169 -0.0008 0.0225  27  ALA   B CA  
4096 C  C   . ALA   B 27  ? 0.2045 0.1753 0.2203 -0.0035 0.0189  0.0405  27  ALA   B C   
4097 O  O   . ALA   B 27  ? 0.1921 0.1939 0.2451 -0.0059 0.0139  0.0526  27  ALA   B O   
4098 C  CB  . ALA   B 27  ? 0.2112 0.1464 0.2335 -0.0174 -0.0089 0.0247  27  ALA   B CB  
4104 N  N   . LYS   B 28  ? 0.2036 0.1955 0.2843 -0.0127 0.0283  0.0572  28  LYS   B N   
4105 C  CA  . LYS   B 28  ? 0.2167 0.2296 0.3054 0.0053  0.0756  0.0810  28  LYS   B CA  
4106 C  C   . LYS   B 28  ? 0.2457 0.2649 0.2908 0.0126  0.0874  0.0747  28  LYS   B C   
4107 O  O   . LYS   B 28  ? 0.2691 0.2870 0.3250 0.0032  0.0853  0.0743  28  LYS   B O   
4108 C  CB  . LYS   B 28  ? 0.2483 0.2652 0.3682 0.0270  0.0788  0.0952  28  LYS   B CB  
4109 C  CG  . LYS   B 28  ? 0.2780 0.3249 0.4110 0.0498  0.0674  0.1006  28  LYS   B CG  
4110 C  CD  . LYS   B 28  ? 0.3224 0.3902 0.4760 0.0588  0.0766  0.0896  28  LYS   B CD  
4111 C  CE  . LYS   B 28  ? 0.3576 0.4384 0.5223 0.0703  0.0749  0.0923  28  LYS   B CE  
4112 N  NZ  . LYS   B 28  ? 0.3898 0.4698 0.5503 0.0870  0.0718  0.1017  28  LYS   B NZ  
4126 N  N   A LYS   B 29  ? 0.2555 0.2818 0.2807 0.0344  0.0843  0.0555  29  LYS   B N   
4127 N  N   B LYS   B 29  ? 0.2615 0.2839 0.2979 0.0212  0.0703  0.0647  29  LYS   B N   
4128 C  CA  A LYS   B 29  ? 0.2944 0.3097 0.2984 0.0346  0.0742  0.0612  29  LYS   B CA  
4129 C  CA  B LYS   B 29  ? 0.2836 0.3058 0.3135 0.0235  0.0566  0.0620  29  LYS   B CA  
4130 C  C   A LYS   B 29  ? 0.2961 0.3166 0.2696 0.0400  0.0514  0.0798  29  LYS   B C   
4131 C  C   B LYS   B 29  ? 0.2830 0.3075 0.2830 0.0303  0.0476  0.0718  29  LYS   B C   
4132 O  O   A LYS   B 29  ? 0.3162 0.3402 0.2883 0.0473  0.0548  0.0901  29  LYS   B O   
4133 O  O   B LYS   B 29  ? 0.2908 0.3161 0.2890 0.0340  0.0493  0.0776  29  LYS   B O   
4134 C  CB  A LYS   B 29  ? 0.3439 0.3413 0.3730 0.0318  0.0520  0.0417  29  LYS   B CB  
4135 C  CB  B LYS   B 29  ? 0.3103 0.3289 0.3687 0.0207  0.0406  0.0470  29  LYS   B CB  
4136 C  CG  A LYS   B 29  ? 0.3864 0.3693 0.4514 0.0244  0.0388  0.0360  29  LYS   B CG  
4137 C  CG  B LYS   B 29  ? 0.3316 0.3490 0.4238 0.0162  0.0302  0.0385  29  LYS   B CG  
4138 C  CD  A LYS   B 29  ? 0.4240 0.3854 0.5161 0.0134  0.0436  0.0240  29  LYS   B CD  
4139 C  CD  B LYS   B 29  ? 0.3484 0.3625 0.4698 0.0107  0.0283  0.0286  29  LYS   B CD  
4140 C  CE  A LYS   B 29  ? 0.4455 0.3948 0.5603 0.0063  0.0506  0.0161  29  LYS   B CE  
4141 C  CE  B LYS   B 29  ? 0.3607 0.3711 0.5025 0.0071  0.0290  0.0213  29  LYS   B CE  
4142 N  NZ  A LYS   B 29  ? 0.4541 0.4032 0.5852 0.0041  0.0495  0.0108  29  LYS   B NZ  
4143 N  NZ  B LYS   B 29  ? 0.3672 0.3773 0.5204 0.0061  0.0264  0.0176  29  LYS   B NZ  
4170 N  N   . VAL   B 30  ? 0.2707 0.2999 0.2581 0.0303  0.0409  0.0724  30  VAL   B N   
4171 C  CA  . VAL   B 30  ? 0.2589 0.2752 0.2856 0.0195  0.0130  0.0872  30  VAL   B CA  
4172 C  C   . VAL   B 30  ? 0.2311 0.2779 0.2690 0.0094  0.0206  0.1025  30  VAL   B C   
4173 O  O   . VAL   B 30  ? 0.2231 0.3013 0.2858 0.0089  0.0181  0.1149  30  VAL   B O   
4174 C  CB  . VAL   B 30  ? 0.2625 0.2637 0.3319 -0.0017 -0.0141 0.0777  30  VAL   B CB  
4175 C  CG1 . VAL   B 30  ? 0.2682 0.2722 0.3305 -0.0078 -0.0117 0.0556  30  VAL   B CG1 
4176 C  CG2 . VAL   B 30  ? 0.2772 0.2627 0.3564 -0.0055 -0.0269 0.0644  30  VAL   B CG2 
4187 N  N   . LYS   B 31  ? 0.2098 0.2403 0.3085 -0.0102 0.0267  0.0984  31  LYS   B N   
4188 C  CA  . LYS   B 31  ? 0.2049 0.2361 0.3440 -0.0223 0.0075  0.1084  31  LYS   B CA  
4189 C  C   . LYS   B 31  ? 0.1988 0.1962 0.2925 -0.0226 -0.0282 0.1056  31  LYS   B C   
4190 O  O   . LYS   B 31  ? 0.2056 0.2308 0.3226 -0.0256 0.0022  0.1168  31  LYS   B O   
4191 C  CB  . LYS   B 31  ? 0.2180 0.2889 0.4011 -0.0069 0.0253  0.1084  31  LYS   B CB  
4192 C  CG  . LYS   B 31  ? 0.2531 0.3437 0.4393 -0.0007 0.0449  0.0947  31  LYS   B CG  
4193 C  CD  . LYS   B 31  ? 0.2885 0.3976 0.4802 0.0056  0.0412  0.0681  31  LYS   B CD  
4194 C  CE  . LYS   B 31  ? 0.3132 0.4331 0.5217 0.0106  0.0273  0.0481  31  LYS   B CE  
4195 N  NZ  . LYS   B 31  ? 0.3250 0.4493 0.5359 0.0196  0.0100  0.0286  31  LYS   B NZ  
4209 N  N   . PRO   B 32  ? 0.1937 0.1720 0.2177 -0.0246 -0.0496 0.0589  32  PRO   B N   
4210 C  CA  . PRO   B 32  ? 0.2036 0.1769 0.1964 -0.0380 -0.0453 0.0307  32  PRO   B CA  
4211 C  C   . PRO   B 32  ? 0.2116 0.1622 0.1860 -0.0434 -0.0681 0.0440  32  PRO   B C   
4212 O  O   . PRO   B 32  ? 0.2224 0.1746 0.2257 -0.0415 -0.0725 0.0343  32  PRO   B O   
4213 C  CB  . PRO   B 32  ? 0.2150 0.1684 0.2092 -0.0498 -0.0346 0.0169  32  PRO   B CB  
4214 C  CG  . PRO   B 32  ? 0.2372 0.1606 0.2146 -0.0435 -0.0520 0.0141  32  PRO   B CG  
4215 C  CD  . PRO   B 32  ? 0.2204 0.1612 0.2231 -0.0360 -0.0664 0.0169  32  PRO   B CD  
4223 N  N   . THR   B 33  ? 0.2188 0.1572 0.1768 -0.0335 -0.0558 0.0285  33  THR   B N   
4224 C  CA  . THR   B 33  ? 0.2277 0.1515 0.1935 -0.0387 -0.0440 0.0306  33  THR   B CA  
4225 C  C   . THR   B 33  ? 0.2196 0.1486 0.1753 -0.0322 -0.0420 0.0174  33  THR   B C   
4226 O  O   . THR   B 33  ? 0.2397 0.1487 0.1914 -0.0382 -0.0552 0.0168  33  THR   B O   
4227 C  CB  . THR   B 33  ? 0.2388 0.1642 0.1945 -0.0232 -0.0555 0.0234  33  THR   B CB  
4228 O  OG1 . THR   B 33  ? 0.2162 0.1822 0.1839 -0.0074 -0.0414 0.0379  33  THR   B OG1 
4229 C  CG2 . THR   B 33  ? 0.2582 0.1823 0.2056 -0.0288 -0.0539 0.0349  33  THR   B CG2 
4237 N  N   . VAL   B 34  ? 0.1998 0.1497 0.1523 -0.0327 -0.0238 0.0121  34  VAL   B N   
4238 C  CA  . VAL   B 34  ? 0.1972 0.1500 0.1503 -0.0220 -0.0262 0.0148  34  VAL   B CA  
4239 C  C   . VAL   B 34  ? 0.1676 0.1420 0.1358 -0.0239 -0.0080 0.0107  34  VAL   B C   
4240 O  O   . VAL   B 34  ? 0.1796 0.1646 0.1441 -0.0206 -0.0307 0.0031  34  VAL   B O   
4241 C  CB  . VAL   B 34  ? 0.2030 0.1584 0.1653 0.0002  -0.0128 -0.0074 34  VAL   B CB  
4242 C  CG1 . VAL   B 34  ? 0.1899 0.1774 0.1934 0.0010  -0.0050 -0.0245 34  VAL   B CG1 
4243 C  CG2 . VAL   B 34  ? 0.1937 0.1671 0.1951 -0.0018 -0.0128 -0.0094 34  VAL   B CG2 
4253 N  N   . VAL   B 35  ? 0.1792 0.1397 0.1338 -0.0279 -0.0172 0.0025  35  VAL   B N   
4254 C  CA  . VAL   B 35  ? 0.1690 0.1430 0.1231 -0.0168 -0.0092 0.0027  35  VAL   B CA  
4255 C  C   . VAL   B 35  ? 0.1494 0.1358 0.1400 -0.0186 -0.0058 -0.0069 35  VAL   B C   
4256 O  O   . VAL   B 35  ? 0.1740 0.1366 0.1356 -0.0207 -0.0004 -0.0011 35  VAL   B O   
4257 C  CB  . VAL   B 35  ? 0.1702 0.1424 0.1383 -0.0197 -0.0033 -0.0045 35  VAL   B CB  
4258 C  CG1 . VAL   B 35  ? 0.1767 0.1772 0.1556 -0.0195 -0.0014 0.0081  35  VAL   B CG1 
4259 C  CG2 . VAL   B 35  ? 0.1732 0.1516 0.1769 -0.0114 0.0047  -0.0077 35  VAL   B CG2 
4269 N  N   . VAL   B 36  ? 0.1519 0.1488 0.1242 -0.0126 -0.0215 0.0025  36  VAL   B N   
4270 C  CA  . VAL   B 36  ? 0.1576 0.1292 0.1212 -0.0081 -0.0283 0.0050  36  VAL   B CA  
4271 C  C   . VAL   B 36  ? 0.1542 0.1443 0.1042 -0.0118 -0.0151 -0.0061 36  VAL   B C   
4272 O  O   . VAL   B 36  ? 0.1691 0.1577 0.1318 -0.0162 0.0005  -0.0145 36  VAL   B O   
4273 C  CB  . VAL   B 36  ? 0.1580 0.1438 0.1411 -0.0238 -0.0183 0.0084  36  VAL   B CB  
4274 C  CG1 . VAL   B 36  ? 0.1502 0.1489 0.1622 -0.0223 -0.0160 -0.0014 36  VAL   B CG1 
4275 C  CG2 . VAL   B 36  ? 0.1655 0.1571 0.1448 -0.0213 -0.0155 0.0130  36  VAL   B CG2 
4285 N  N   . ASN   B 37  ? 0.1530 0.1478 0.1224 0.0031  -0.0043 0.0029  37  ASN   B N   
4286 C  CA  . ASN   B 37  ? 0.1430 0.1387 0.1303 0.0012  -0.0210 0.0012  37  ASN   B CA  
4287 C  C   . ASN   B 37  ? 0.1656 0.1492 0.1439 0.0013  -0.0081 0.0201  37  ASN   B C   
4288 O  O   . ASN   B 37  ? 0.1681 0.1527 0.1363 -0.0032 0.0011  0.0130  37  ASN   B O   
4289 C  CB  . ASN   B 37  ? 0.1486 0.1522 0.1300 -0.0036 -0.0216 -0.0033 37  ASN   B CB  
4290 C  CG  . ASN   B 37  ? 0.1637 0.1553 0.1327 -0.0039 -0.0232 -0.0145 37  ASN   B CG  
4291 O  OD1 . ASN   B 37  ? 0.1653 0.1587 0.1583 0.0028  -0.0068 -0.0098 37  ASN   B OD1 
4292 N  ND2 . ASN   B 37  ? 0.1759 0.1385 0.1404 0.0009  -0.0089 0.0078  37  ASN   B ND2 
4299 N  N   . ALA   B 38  ? 0.1660 0.1495 0.1351 0.0071  0.0031  0.0203  38  ALA   B N   
4300 C  CA  . ALA   B 38  ? 0.1627 0.1539 0.1379 0.0076  -0.0022 0.0071  38  ALA   B CA  
4301 C  C   . ALA   B 38  ? 0.1614 0.1492 0.1524 -0.0041 -0.0037 0.0075  38  ALA   B C   
4302 O  O   . ALA   B 38  ? 0.1803 0.1555 0.1528 0.0027  -0.0054 0.0084  38  ALA   B O   
4303 C  CB  . ALA   B 38  ? 0.2028 0.1562 0.1551 -0.0088 0.0178  0.0057  38  ALA   B CB  
4309 N  N   . ALA   B 39  ? 0.1652 0.1533 0.1329 -0.0013 -0.0046 -0.0075 39  ALA   B N   
4310 C  CA  . ALA   B 39  ? 0.1750 0.1536 0.1327 0.0064  -0.0026 0.0048  39  ALA   B CA  
4311 C  C   . ALA   B 39  ? 0.1781 0.1686 0.1218 0.0039  -0.0115 -0.0001 39  ALA   B C   
4312 O  O   . ALA   B 39  ? 0.1887 0.1708 0.1434 0.0113  -0.0113 0.0051  39  ALA   B O   
4313 C  CB  . ALA   B 39  ? 0.1822 0.1476 0.1463 -0.0035 0.0024  0.0068  39  ALA   B CB  
4319 N  N   . ASN   B 40  ? 0.1649 0.2001 0.1200 -0.0052 -0.0090 -0.0103 40  ASN   B N   
4320 C  CA  . ASN   B 40  ? 0.1824 0.2094 0.1261 -0.0036 -0.0203 -0.0076 40  ASN   B CA  
4321 C  C   . ASN   B 40  ? 0.1871 0.2033 0.1195 -0.0005 -0.0108 -0.0042 40  ASN   B C   
4322 O  O   . ASN   B 40  ? 0.1917 0.1831 0.1304 0.0045  -0.0066 0.0042  40  ASN   B O   
4323 C  CB  . ASN   B 40  ? 0.1881 0.2149 0.1689 0.0084  -0.0150 0.0133  40  ASN   B CB  
4324 C  CG  . ASN   B 40  ? 0.1952 0.2110 0.1877 -0.0014 -0.0392 0.0259  40  ASN   B CG  
4325 O  OD1 . ASN   B 40  ? 0.2059 0.1905 0.2806 -0.0044 -0.0403 0.0347  40  ASN   B OD1 
4326 N  ND2 . ASN   B 40  ? 0.2114 0.2083 0.1944 0.0043  -0.0224 0.0269  40  ASN   B ND2 
4333 N  N   . VAL   B 41  ? 0.1974 0.2048 0.1375 0.0125  -0.0021 -0.0056 41  VAL   B N   
4334 C  CA  . VAL   B 41  ? 0.2077 0.2090 0.1427 0.0082  -0.0065 -0.0188 41  VAL   B CA  
4335 C  C   . VAL   B 41  ? 0.2123 0.2111 0.1402 0.0213  -0.0166 -0.0140 41  VAL   B C   
4336 O  O   . VAL   B 41  ? 0.2119 0.2108 0.1498 0.0122  -0.0184 -0.0174 41  VAL   B O   
4337 C  CB  . VAL   B 41  ? 0.2188 0.2293 0.1519 0.0002  0.0079  -0.0269 41  VAL   B CB  
4338 C  CG1 . VAL   B 41  ? 0.2202 0.2352 0.1753 -0.0105 0.0177  -0.0240 41  VAL   B CG1 
4339 C  CG2 . VAL   B 41  ? 0.2240 0.2500 0.1695 -0.0073 0.0100  -0.0235 41  VAL   B CG2 
4349 N  N   . TYR   B 42  ? 0.2120 0.2079 0.1406 0.0152  -0.0217 0.0045  42  TYR   B N   
4350 C  CA  . TYR   B 42  ? 0.2117 0.2107 0.1537 0.0125  -0.0419 -0.0202 42  TYR   B CA  
4351 C  C   . TYR   B 42  ? 0.1970 0.1945 0.1596 0.0138  -0.0280 -0.0169 42  TYR   B C   
4352 O  O   . TYR   B 42  ? 0.1973 0.2049 0.2064 0.0183  -0.0272 -0.0268 42  TYR   B O   
4353 C  CB  . TYR   B 42  ? 0.2349 0.2412 0.1872 0.0054  -0.0436 -0.0091 42  TYR   B CB  
4354 C  CG  . TYR   B 42  ? 0.2523 0.2685 0.1868 0.0056  -0.0366 0.0101  42  TYR   B CG  
4355 C  CD1 . TYR   B 42  ? 0.2481 0.2682 0.1617 0.0099  -0.0248 -0.0089 42  TYR   B CD1 
4356 C  CD2 . TYR   B 42  ? 0.2733 0.2925 0.2332 0.0101  -0.0246 0.0250  42  TYR   B CD2 
4357 C  CE1 . TYR   B 42  ? 0.2669 0.2901 0.1614 0.0169  -0.0113 -0.0021 42  TYR   B CE1 
4358 C  CE2 . TYR   B 42  ? 0.2800 0.3050 0.2134 0.0094  0.0001  0.0316  42  TYR   B CE2 
4359 C  CZ  . TYR   B 42  ? 0.2897 0.3105 0.1874 0.0321  0.0142  0.0079  42  TYR   B CZ  
4360 O  OH  . TYR   B 42  ? 0.3366 0.3395 0.2419 0.0444  0.0274  0.0245  42  TYR   B OH  
4370 N  N   . LEU   B 43  ? 0.1839 0.1831 0.1468 0.0028  -0.0080 -0.0079 43  LEU   B N   
4371 C  CA  . LEU   B 43  ? 0.1990 0.1796 0.1409 -0.0082 -0.0158 0.0081  43  LEU   B CA  
4372 C  C   . LEU   B 43  ? 0.2095 0.1717 0.1498 -0.0029 -0.0102 -0.0071 43  LEU   B C   
4373 O  O   . LEU   B 43  ? 0.2009 0.1699 0.1785 0.0003  -0.0110 -0.0005 43  LEU   B O   
4374 C  CB  . LEU   B 43  ? 0.1990 0.1766 0.1544 -0.0066 -0.0345 -0.0063 43  LEU   B CB  
4375 C  CG  . LEU   B 43  ? 0.1948 0.1689 0.1670 -0.0021 -0.0331 -0.0046 43  LEU   B CG  
4376 C  CD1 . LEU   B 43  ? 0.2022 0.1714 0.2116 -0.0015 -0.0362 -0.0119 43  LEU   B CD1 
4377 C  CD2 . LEU   B 43  ? 0.1789 0.1649 0.1794 -0.0069 -0.0331 -0.0070 43  LEU   B CD2 
4389 N  N   . LYS   B 44  ? 0.2009 0.1735 0.1611 0.0024  -0.0021 -0.0121 44  LYS   B N   
4390 C  CA  . LYS   B 44  ? 0.2075 0.1827 0.1514 0.0059  -0.0135 0.0004  44  LYS   B CA  
4391 C  C   . LYS   B 44  ? 0.1917 0.1801 0.1603 0.0006  -0.0197 0.0107  44  LYS   B C   
4392 O  O   . LYS   B 44  ? 0.2012 0.1666 0.1973 0.0045  -0.0043 0.0001  44  LYS   B O   
4393 C  CB  . LYS   B 44  ? 0.2370 0.2127 0.1811 0.0116  -0.0347 -0.0090 44  LYS   B CB  
4394 C  CG  . LYS   B 44  ? 0.2818 0.2463 0.2079 0.0077  -0.0618 0.0048  44  LYS   B CG  
4395 C  CD  . LYS   B 44  ? 0.3168 0.2715 0.2708 -0.0132 -0.0798 -0.0048 44  LYS   B CD  
4396 C  CE  . LYS   B 44  ? 0.3532 0.2986 0.3292 -0.0217 -0.0695 0.0155  44  LYS   B CE  
4397 N  NZ  . LYS   B 44  ? 0.3618 0.3055 0.3568 -0.0203 -0.0737 0.0306  44  LYS   B NZ  
4411 N  N   . HIS   B 45  ? 0.1803 0.1901 0.1430 -0.0015 -0.0222 0.0232  45  HIS   B N   
4412 C  CA  . HIS   B 45  ? 0.1813 0.1851 0.1535 0.0093  -0.0043 0.0019  45  HIS   B CA  
4413 C  C   . HIS   B 45  ? 0.2002 0.2094 0.2121 0.0162  -0.0299 -0.0027 45  HIS   B C   
4414 O  O   . HIS   B 45  ? 0.2069 0.2274 0.2666 0.0423  -0.0095 0.0025  45  HIS   B O   
4415 C  CB  . HIS   B 45  ? 0.1692 0.1852 0.1586 0.0033  -0.0094 0.0041  45  HIS   B CB  
4416 C  CG  . HIS   B 45  ? 0.1703 0.1759 0.1366 0.0039  -0.0138 0.0063  45  HIS   B CG  
4417 N  ND1 . HIS   B 45  ? 0.1898 0.1793 0.1578 0.0096  -0.0193 -0.0148 45  HIS   B ND1 
4418 C  CD2 . HIS   B 45  ? 0.1885 0.1831 0.1675 -0.0145 -0.0203 0.0082  45  HIS   B CD2 
4419 C  CE1 . HIS   B 45  ? 0.2072 0.1592 0.1408 0.0014  -0.0387 -0.0198 45  HIS   B CE1 
4420 N  NE2 . HIS   B 45  ? 0.2067 0.1674 0.1578 -0.0055 -0.0288 -0.0107 45  HIS   B NE2 
4428 N  N   A GLY   B 46  ? 0.2111 0.2098 0.2322 0.0227  -0.0634 0.0043  46  GLY   B N   
4429 N  N   B GLY   B 46  ? 0.2139 0.2176 0.2319 0.0194  -0.0426 0.0066  46  GLY   B N   
4430 C  CA  A GLY   B 46  ? 0.2334 0.2176 0.2805 0.0198  -0.0774 0.0085  46  GLY   B CA  
4431 C  CA  B GLY   B 46  ? 0.2313 0.2268 0.2584 0.0177  -0.0497 0.0137  46  GLY   B CA  
4432 C  C   A GLY   B 46  ? 0.2501 0.2383 0.3409 0.0218  -0.0608 0.0056  46  GLY   B C   
4433 C  C   B GLY   B 46  ? 0.2442 0.2384 0.2879 0.0179  -0.0459 0.0174  46  GLY   B C   
4434 O  O   A GLY   B 46  ? 0.2607 0.2510 0.4487 0.0349  -0.0229 -0.0251 46  GLY   B O   
4435 O  O   B GLY   B 46  ? 0.2462 0.2460 0.3053 0.0285  -0.0336 0.0206  46  GLY   B O   
4442 N  N   . GLY   B 47  ? 0.2519 0.2414 0.3028 0.0000  -0.0449 0.0098  47  GLY   B N   
4443 C  CA  . GLY   B 47  ? 0.2381 0.2080 0.2475 0.0062  -0.0211 0.0094  47  GLY   B CA  
4444 C  C   . GLY   B 47  ? 0.1910 0.2034 0.2034 -0.0005 0.0057  0.0075  47  GLY   B C   
4445 O  O   . GLY   B 47  ? 0.2050 0.1801 0.2016 0.0006  -0.0129 0.0124  47  GLY   B O   
4450 N  N   . GLY   B 48  ? 0.1779 0.1997 0.1939 0.0006  -0.0115 0.0282  48  GLY   B N   
4451 C  CA  . GLY   B 48  ? 0.1872 0.1731 0.2060 -0.0053 -0.0038 0.0129  48  GLY   B CA  
4452 C  C   . GLY   B 48  ? 0.1861 0.1589 0.1845 0.0001  0.0109  0.0039  48  GLY   B C   
4453 O  O   . GLY   B 48  ? 0.1700 0.1683 0.1966 0.0100  0.0000  0.0133  48  GLY   B O   
4457 N  N   . VAL   B 49  ? 0.1847 0.1706 0.1658 0.0129  0.0062  0.0069  49  VAL   B N   
4458 C  CA  . VAL   B 49  ? 0.1814 0.1831 0.1489 0.0027  -0.0018 -0.0035 49  VAL   B CA  
4459 C  C   . VAL   B 49  ? 0.1694 0.1652 0.1462 0.0107  -0.0011 0.0081  49  VAL   B C   
4460 O  O   . VAL   B 49  ? 0.1793 0.1745 0.1687 0.0091  0.0023  0.0079  49  VAL   B O   
4461 C  CB  . VAL   B 49  ? 0.1850 0.1898 0.1892 -0.0039 -0.0252 -0.0085 49  VAL   B CB  
4462 C  CG1 . VAL   B 49  ? 0.1831 0.2008 0.1752 -0.0009 -0.0236 -0.0030 49  VAL   B CG1 
4463 C  CG2 . VAL   B 49  ? 0.1982 0.2155 0.2458 -0.0148 -0.0431 -0.0169 49  VAL   B CG2 
4473 N  N   . ALA   B 50  ? 0.1681 0.1573 0.1527 0.0042  -0.0013 0.0079  50  ALA   B N   
4474 C  CA  . ALA   B 50  ? 0.1592 0.1608 0.1503 0.0086  -0.0095 0.0071  50  ALA   B CA  
4475 C  C   . ALA   B 50  ? 0.1509 0.1721 0.1597 0.0101  -0.0099 0.0160  50  ALA   B C   
4476 O  O   . ALA   B 50  ? 0.1661 0.1769 0.1545 0.0055  0.0012  0.0104  50  ALA   B O   
4477 C  CB  . ALA   B 50  ? 0.1889 0.1524 0.1539 -0.0041 -0.0049 -0.0009 50  ALA   B CB  
4483 N  N   . GLY   B 51  ? 0.1631 0.1842 0.1703 0.0157  -0.0116 0.0075  51  GLY   B N   
4484 C  CA  . GLY   B 51  ? 0.1684 0.1873 0.1895 0.0183  -0.0231 0.0097  51  GLY   B CA  
4485 C  C   . GLY   B 51  ? 0.1623 0.1665 0.1906 0.0093  -0.0108 0.0011  51  GLY   B C   
4486 O  O   . GLY   B 51  ? 0.1633 0.1946 0.2101 0.0124  -0.0115 -0.0036 51  GLY   B O   
4490 N  N   . ALA   B 52  ? 0.1698 0.1652 0.1848 0.0138  -0.0011 0.0095  52  ALA   B N   
4491 C  CA  . ALA   B 52  ? 0.1659 0.1775 0.1905 0.0167  0.0164  -0.0022 52  ALA   B CA  
4492 C  C   . ALA   B 52  ? 0.1689 0.1762 0.1641 0.0098  0.0089  -0.0113 52  ALA   B C   
4493 O  O   . ALA   B 52  ? 0.1751 0.1733 0.1855 0.0079  0.0043  -0.0039 52  ALA   B O   
4494 C  CB  . ALA   B 52  ? 0.2001 0.1730 0.1892 -0.0011 0.0149  -0.0003 52  ALA   B CB  
4500 N  N   . LEU   B 53  ? 0.1738 0.1731 0.1533 0.0142  0.0079  0.0079  53  LEU   B N   
4501 C  CA  . LEU   B 53  ? 0.1671 0.1794 0.1548 0.0115  0.0003  0.0113  53  LEU   B CA  
4502 C  C   . LEU   B 53  ? 0.1655 0.1609 0.1648 0.0148  -0.0020 0.0164  53  LEU   B C   
4503 O  O   . LEU   B 53  ? 0.1686 0.1659 0.1844 -0.0022 -0.0003 0.0191  53  LEU   B O   
4504 C  CB  . LEU   B 53  ? 0.1654 0.1814 0.1803 0.0125  -0.0058 0.0024  53  LEU   B CB  
4505 C  CG  . LEU   B 53  ? 0.1819 0.1847 0.1738 0.0056  -0.0080 0.0254  53  LEU   B CG  
4506 C  CD1 . LEU   B 53  ? 0.1748 0.2221 0.2053 0.0269  -0.0065 0.0072  53  LEU   B CD1 
4507 C  CD2 . LEU   B 53  ? 0.2041 0.2128 0.2045 -0.0088 -0.0254 -0.0169 53  LEU   B CD2 
4519 N  N   . ASN   B 54  ? 0.1734 0.1523 0.1611 0.0098  0.0041  0.0108  54  ASN   B N   
4520 C  CA  . ASN   B 54  ? 0.1799 0.1706 0.1734 0.0159  -0.0073 -0.0063 54  ASN   B CA  
4521 C  C   . ASN   B 54  ? 0.1765 0.1801 0.1912 0.0163  -0.0074 0.0091  54  ASN   B C   
4522 O  O   . ASN   B 54  ? 0.1860 0.1855 0.1974 0.0002  0.0042  0.0006  54  ASN   B O   
4523 C  CB  . ASN   B 54  ? 0.1765 0.1828 0.1929 0.0153  -0.0063 -0.0062 54  ASN   B CB  
4524 C  CG  . ASN   B 54  ? 0.1814 0.1860 0.1732 0.0020  -0.0130 -0.0159 54  ASN   B CG  
4525 O  OD1 . ASN   B 54  ? 0.1735 0.1938 0.1969 0.0002  -0.0100 -0.0195 54  ASN   B OD1 
4526 N  ND2 . ASN   B 54  ? 0.1898 0.2010 0.2199 -0.0016 -0.0480 0.0004  54  ASN   B ND2 
4533 N  N   . LYS   B 55  ? 0.1644 0.1944 0.2091 0.0192  0.0112  0.0089  55  LYS   B N   
4534 C  CA  . LYS   B 55  ? 0.1764 0.2026 0.2272 0.0243  0.0053  0.0045  55  LYS   B CA  
4535 C  C   . LYS   B 55  ? 0.1521 0.2141 0.2115 0.0205  0.0201  0.0046  55  LYS   B C   
4536 O  O   . LYS   B 55  ? 0.1578 0.2215 0.2178 0.0134  0.0123  -0.0068 55  LYS   B O   
4537 C  CB  . LYS   B 55  ? 0.1984 0.1972 0.2652 0.0318  0.0198  0.0123  55  LYS   B CB  
4538 C  CG  . LYS   B 55  ? 0.2461 0.2320 0.3574 0.0363  0.0394  0.0242  55  LYS   B CG  
4539 C  CD  . LYS   B 55  ? 0.2917 0.2621 0.4297 0.0476  0.0639  0.0348  55  LYS   B CD  
4540 C  CE  . LYS   B 55  ? 0.3183 0.2860 0.4956 0.0528  0.0916  0.0445  55  LYS   B CE  
4541 N  NZ  . LYS   B 55  ? 0.3319 0.3089 0.5387 0.0516  0.0786  0.0471  55  LYS   B NZ  
4555 N  N   . ALA   B 56  ? 0.1548 0.2143 0.1873 0.0123  -0.0048 -0.0069 56  ALA   B N   
4556 C  CA  . ALA   B 56  ? 0.1723 0.2196 0.2024 0.0081  -0.0024 -0.0060 56  ALA   B CA  
4557 C  C   . ALA   B 56  ? 0.1744 0.2109 0.1794 -0.0003 0.0083  0.0068  56  ALA   B C   
4558 O  O   . ALA   B 56  ? 0.2003 0.2221 0.2026 0.0040  0.0345  0.0026  56  ALA   B O   
4559 C  CB  . ALA   B 56  ? 0.1851 0.2407 0.2244 -0.0092 -0.0037 -0.0007 56  ALA   B CB  
4565 N  N   . THR   B 57  ? 0.1849 0.2167 0.1923 -0.0030 0.0288  0.0040  57  THR   B N   
4566 C  CA  . THR   B 57  ? 0.1857 0.2055 0.1851 0.0012  0.0223  0.0063  57  THR   B CA  
4567 C  C   . THR   B 57  ? 0.1828 0.2214 0.2052 -0.0094 0.0127  0.0023  57  THR   B C   
4568 O  O   . THR   B 57  ? 0.1832 0.2235 0.2176 -0.0208 0.0062  -0.0005 57  THR   B O   
4569 C  CB  . THR   B 57  ? 0.1934 0.1865 0.1583 0.0033  0.0059  0.0181  57  THR   B CB  
4570 O  OG1 . THR   B 57  ? 0.1855 0.1802 0.1867 -0.0029 -0.0020 0.0071  57  THR   B OG1 
4571 C  CG2 . THR   B 57  ? 0.1978 0.1776 0.1680 0.0044  0.0050  0.0151  57  THR   B CG2 
4579 N  N   . ASN   B 58  ? 0.1761 0.2383 0.2110 -0.0096 -0.0018 -0.0164 58  ASN   B N   
4580 C  CA  . ASN   B 58  ? 0.2347 0.2806 0.2598 -0.0136 0.0239  -0.0028 58  ASN   B CA  
4581 C  C   . ASN   B 58  ? 0.1974 0.2397 0.2240 -0.0084 0.0089  -0.0159 58  ASN   B C   
4582 O  O   . ASN   B 58  ? 0.1924 0.2482 0.2503 -0.0124 -0.0062 -0.0199 58  ASN   B O   
4583 C  CB  . ASN   B 58  ? 0.3509 0.3812 0.3968 -0.0148 0.0658  0.0028  58  ASN   B CB  
4584 C  CG  . ASN   B 58  ? 0.4770 0.4902 0.5800 -0.0196 0.0842  0.0246  58  ASN   B CG  
4585 O  OD1 . ASN   B 58  ? 0.4820 0.5019 0.6394 -0.0204 0.0880  0.0330  58  ASN   B OD1 
4586 N  ND2 . ASN   B 58  ? 0.5885 0.5885 0.6485 -0.0229 0.0893  0.0279  58  ASN   B ND2 
4593 N  N   . ASN   B 59  ? 0.1900 0.2270 0.2004 -0.0112 0.0018  0.0023  59  ASN   B N   
4594 C  CA  . ASN   B 59  ? 0.1780 0.2301 0.2027 -0.0089 -0.0205 0.0095  59  ASN   B CA  
4595 C  C   . ASN   B 59  ? 0.1810 0.2215 0.1985 -0.0077 -0.0189 -0.0075 59  ASN   B C   
4596 O  O   . ASN   B 59  ? 0.1740 0.2136 0.2109 -0.0064 -0.0034 0.0034  59  ASN   B O   
4597 C  CB  . ASN   B 59  ? 0.1775 0.2455 0.2340 -0.0051 -0.0208 0.0213  59  ASN   B CB  
4598 C  CG  . ASN   B 59  ? 0.2057 0.2616 0.2682 0.0034  -0.0414 0.0201  59  ASN   B CG  
4599 O  OD1 . ASN   B 59  ? 0.2103 0.2608 0.2554 0.0033  -0.0346 0.0389  59  ASN   B OD1 
4600 N  ND2 . ASN   B 59  ? 0.1997 0.2676 0.3026 -0.0155 -0.0470 0.0059  59  ASN   B ND2 
4607 N  N   . ALA   B 60  ? 0.1788 0.2089 0.2024 0.0014  0.0008  -0.0006 60  ALA   B N   
4608 C  CA  . ALA   B 60  ? 0.1904 0.2027 0.1818 -0.0124 0.0027  0.0007  60  ALA   B CA  
4609 C  C   . ALA   B 60  ? 0.1855 0.1983 0.1757 -0.0045 0.0051  -0.0047 60  ALA   B C   
4610 O  O   . ALA   B 60  ? 0.1754 0.1966 0.1995 -0.0201 0.0071  -0.0093 60  ALA   B O   
4611 C  CB  . ALA   B 60  ? 0.2006 0.1994 0.2291 -0.0239 0.0016  0.0094  60  ALA   B CB  
4617 N  N   . MET   B 61  ? 0.1821 0.1766 0.1740 0.0041  0.0063  0.0143  61  MET   B N   
4618 C  CA  . MET   B 61  ? 0.1802 0.1699 0.1824 0.0020  -0.0061 -0.0029 61  MET   B CA  
4619 C  C   . MET   B 61  ? 0.1778 0.1595 0.1874 -0.0115 -0.0122 0.0119  61  MET   B C   
4620 O  O   . MET   B 61  ? 0.1833 0.1587 0.1853 0.0066  -0.0076 -0.0131 61  MET   B O   
4621 C  CB  . MET   B 61  ? 0.1784 0.1734 0.1846 -0.0033 -0.0130 0.0045  61  MET   B CB  
4622 C  CG  . MET   B 61  ? 0.1715 0.1769 0.1673 -0.0036 0.0135  0.0009  61  MET   B CG  
4623 S  SD  . MET   B 61  ? 0.1737 0.1731 0.1919 -0.0043 -0.0036 -0.0092 61  MET   B SD  
4624 C  CE  . MET   B 61  ? 0.1877 0.1859 0.1996 -0.0029 0.0004  -0.0301 61  MET   B CE  
4634 N  N   . GLN   B 62  ? 0.1706 0.1645 0.1654 -0.0095 -0.0174 -0.0019 62  GLN   B N   
4635 C  CA  . GLN   B 62  ? 0.1733 0.1849 0.1815 -0.0070 -0.0205 -0.0074 62  GLN   B CA  
4636 C  C   . GLN   B 62  ? 0.1814 0.1852 0.1770 -0.0008 -0.0327 -0.0059 62  GLN   B C   
4637 O  O   . GLN   B 62  ? 0.1972 0.1779 0.1972 -0.0009 -0.0169 -0.0269 62  GLN   B O   
4638 C  CB  . GLN   B 62  ? 0.1692 0.1966 0.1861 -0.0064 -0.0208 0.0161  62  GLN   B CB  
4639 C  CG  . GLN   B 62  ? 0.1688 0.2065 0.1902 -0.0046 -0.0222 -0.0130 62  GLN   B CG  
4640 C  CD  . GLN   B 62  ? 0.1663 0.1926 0.1851 -0.0026 -0.0177 0.0014  62  GLN   B CD  
4641 O  OE1 . GLN   B 62  ? 0.1750 0.1868 0.1928 0.0028  -0.0222 -0.0000 62  GLN   B OE1 
4642 N  NE2 . GLN   B 62  ? 0.1742 0.1762 0.1915 -0.0007 -0.0220 0.0066  62  GLN   B NE2 
4651 N  N   . VAL   B 63  ? 0.1874 0.1852 0.1978 -0.0185 -0.0278 -0.0075 63  VAL   B N   
4652 C  CA  . VAL   B 63  ? 0.1995 0.1883 0.2294 -0.0261 -0.0248 0.0056  63  VAL   B CA  
4653 C  C   . VAL   B 63  ? 0.1932 0.1803 0.2054 -0.0287 -0.0384 -0.0088 63  VAL   B C   
4654 O  O   . VAL   B 63  ? 0.2177 0.1720 0.2095 -0.0159 -0.0497 -0.0008 63  VAL   B O   
4655 C  CB  . VAL   B 63  ? 0.2018 0.1973 0.2655 -0.0232 -0.0116 0.0065  63  VAL   B CB  
4656 C  CG1 . VAL   B 63  ? 0.1966 0.2042 0.2820 -0.0312 -0.0099 0.0198  63  VAL   B CG1 
4657 C  CG2 . VAL   B 63  ? 0.1874 0.2142 0.2911 -0.0236 -0.0175 -0.0125 63  VAL   B CG2 
4667 N  N   . GLU   B 64  ? 0.1916 0.1843 0.2067 -0.0206 -0.0428 -0.0063 64  GLU   B N   
4668 C  CA  . GLU   B 64  ? 0.1838 0.1758 0.1946 -0.0091 -0.0440 0.0070  64  GLU   B CA  
4669 C  C   . GLU   B 64  ? 0.1774 0.1859 0.1799 -0.0081 -0.0389 0.0072  64  GLU   B C   
4670 O  O   . GLU   B 64  ? 0.1873 0.1930 0.1862 -0.0108 -0.0367 -0.0077 64  GLU   B O   
4671 C  CB  . GLU   B 64  ? 0.1890 0.1816 0.1842 -0.0161 -0.0265 0.0060  64  GLU   B CB  
4672 C  CG  . GLU   B 64  ? 0.1925 0.1765 0.1859 -0.0219 -0.0437 -0.0055 64  GLU   B CG  
4673 C  CD  . GLU   B 64  ? 0.2011 0.1949 0.1950 -0.0356 -0.0446 -0.0128 64  GLU   B CD  
4674 O  OE1 . GLU   B 64  ? 0.2160 0.2019 0.2123 -0.0481 -0.0282 -0.0402 64  GLU   B OE1 
4675 O  OE2 . GLU   B 64  ? 0.2120 0.1999 0.2223 -0.0379 -0.0516 -0.0091 64  GLU   B OE2 
4682 N  N   . SER   B 65  ? 0.1889 0.1677 0.1697 -0.0151 -0.0267 0.0017  65  SER   B N   
4683 C  CA  . SER   B 65  ? 0.1958 0.1635 0.1804 -0.0027 -0.0315 -0.0104 65  SER   B CA  
4684 C  C   . SER   B 65  ? 0.2093 0.1640 0.1775 0.0092  -0.0444 -0.0225 65  SER   B C   
4685 O  O   . SER   B 65  ? 0.1976 0.1741 0.1853 -0.0019 -0.0294 -0.0210 65  SER   B O   
4686 C  CB  . SER   B 65  ? 0.1917 0.1681 0.1639 -0.0070 -0.0149 -0.0076 65  SER   B CB  
4687 O  OG  . SER   B 65  ? 0.1921 0.1733 0.1685 -0.0034 -0.0186 -0.0169 65  SER   B OG  
4693 N  N   . ASP   B 66  ? 0.2147 0.1659 0.1684 0.0013  -0.0473 -0.0172 66  ASP   B N   
4694 C  CA  . ASP   B 66  ? 0.2160 0.1793 0.1596 0.0065  -0.0408 -0.0084 66  ASP   B CA  
4695 C  C   . ASP   B 66  ? 0.2112 0.1890 0.1699 -0.0108 -0.0253 -0.0232 66  ASP   B C   
4696 O  O   . ASP   B 66  ? 0.1981 0.1992 0.1907 0.0020  -0.0277 -0.0207 66  ASP   B O   
4697 C  CB  . ASP   B 66  ? 0.2225 0.1990 0.2092 0.0171  -0.0521 -0.0127 66  ASP   B CB  
4698 C  CG  . ASP   B 66  ? 0.2406 0.2199 0.2296 0.0166  -0.0612 -0.0098 66  ASP   B CG  
4699 O  OD1 . ASP   B 66  ? 0.2570 0.2265 0.2265 -0.0024 -0.0511 -0.0050 66  ASP   B OD1 
4700 O  OD2 . ASP   B 66  ? 0.2674 0.2470 0.3046 0.0433  -0.0564 -0.0063 66  ASP   B OD2 
4705 N  N   . ASP   B 67  ? 0.2108 0.1822 0.1704 -0.0154 -0.0325 -0.0110 67  ASP   B N   
4706 C  CA  . ASP   B 67  ? 0.2248 0.1767 0.1795 -0.0145 -0.0370 -0.0105 67  ASP   B CA  
4707 C  C   . ASP   B 67  ? 0.2150 0.1685 0.1987 0.0023  -0.0409 -0.0229 67  ASP   B C   
4708 O  O   . ASP   B 67  ? 0.2134 0.1766 0.2196 -0.0053 -0.0220 -0.0289 67  ASP   B O   
4709 C  CB  . ASP   B 67  ? 0.2435 0.1654 0.2219 -0.0168 -0.0352 0.0034  67  ASP   B CB  
4710 C  CG  . ASP   B 67  ? 0.2804 0.1822 0.2231 -0.0190 -0.0638 -0.0134 67  ASP   B CG  
4711 O  OD1 . ASP   B 67  ? 0.3054 0.1897 0.2362 -0.0168 -0.0505 -0.0151 67  ASP   B OD1 
4712 O  OD2 . ASP   B 67  ? 0.2924 0.2103 0.2462 0.0073  -0.0716 -0.0125 67  ASP   B OD2 
4717 N  N   . TYR   B 68  ? 0.1969 0.1726 0.1789 0.0034  -0.0357 -0.0337 68  TYR   B N   
4718 C  CA  . TYR   B 68  ? 0.2012 0.1936 0.2007 0.0073  -0.0487 -0.0264 68  TYR   B CA  
4719 C  C   . TYR   B 68  ? 0.1844 0.1969 0.1957 -0.0045 -0.0250 -0.0254 68  TYR   B C   
4720 O  O   . TYR   B 68  ? 0.1973 0.2003 0.2028 -0.0015 -0.0284 -0.0564 68  TYR   B O   
4721 C  CB  . TYR   B 68  ? 0.2026 0.2308 0.1992 0.0177  -0.0705 -0.0411 68  TYR   B CB  
4722 C  CG  . TYR   B 68  ? 0.2119 0.2374 0.2059 0.0242  -0.0574 -0.0670 68  TYR   B CG  
4723 C  CD1 . TYR   B 68  ? 0.2163 0.2426 0.2548 -0.0018 -0.0429 -0.0789 68  TYR   B CD1 
4724 C  CD2 . TYR   B 68  ? 0.2048 0.2622 0.2246 0.0226  -0.0657 -0.0664 68  TYR   B CD2 
4725 C  CE1 . TYR   B 68  ? 0.2207 0.2644 0.2729 -0.0019 -0.0473 -0.0818 68  TYR   B CE1 
4726 C  CE2 . TYR   B 68  ? 0.2000 0.2666 0.2694 0.0134  -0.0561 -0.0823 68  TYR   B CE2 
4727 C  CZ  . TYR   B 68  ? 0.1997 0.2655 0.2746 -0.0017 -0.0507 -0.0882 68  TYR   B CZ  
4728 O  OH  . TYR   B 68  ? 0.2067 0.2815 0.3098 -0.0116 -0.0307 -0.0729 68  TYR   B OH  
4738 N  N   . ILE   B 69  ? 0.1945 0.1932 0.1885 0.0004  -0.0252 -0.0240 69  ILE   B N   
4739 C  CA  . ILE   B 69  ? 0.1977 0.2043 0.2016 -0.0048 -0.0185 -0.0295 69  ILE   B CA  
4740 C  C   . ILE   B 69  ? 0.1892 0.2035 0.1989 -0.0028 -0.0401 -0.0207 69  ILE   B C   
4741 O  O   . ILE   B 69  ? 0.1877 0.2139 0.2015 0.0006  -0.0260 -0.0213 69  ILE   B O   
4742 C  CB  . ILE   B 69  ? 0.2097 0.2012 0.2341 -0.0085 0.0019  -0.0295 69  ILE   B CB  
4743 C  CG1 . ILE   B 69  ? 0.2142 0.2156 0.2450 -0.0292 0.0175  -0.0467 69  ILE   B CG1 
4744 C  CG2 . ILE   B 69  ? 0.2300 0.1964 0.2516 -0.0112 0.0057  -0.0271 69  ILE   B CG2 
4745 C  CD1 . ILE   B 69  ? 0.2125 0.2205 0.2723 -0.0355 0.0300  -0.0485 69  ILE   B CD1 
4757 N  N   . ALA   B 70  ? 0.1954 0.1896 0.2092 0.0080  -0.0345 -0.0285 70  ALA   B N   
4758 C  CA  . ALA   B 70  ? 0.2007 0.1902 0.1734 0.0000  -0.0448 -0.0380 70  ALA   B CA  
4759 C  C   . ALA   B 70  ? 0.2061 0.1937 0.1880 -0.0079 -0.0418 -0.0421 70  ALA   B C   
4760 O  O   . ALA   B 70  ? 0.2340 0.1847 0.2123 0.0124  -0.0410 -0.0408 70  ALA   B O   
4761 C  CB  . ALA   B 70  ? 0.2117 0.2122 0.1802 0.0012  -0.0449 -0.0315 70  ALA   B CB  
4767 N  N   . THR   B 71  ? 0.2111 0.2048 0.1940 -0.0009 -0.0577 -0.0360 71  THR   B N   
4768 C  CA  . THR   B 71  ? 0.2294 0.2090 0.2164 0.0127  -0.0703 -0.0366 71  THR   B CA  
4769 C  C   . THR   B 71  ? 0.2137 0.2096 0.2444 0.0329  -0.0649 -0.0606 71  THR   B C   
4770 O  O   . THR   B 71  ? 0.2261 0.2127 0.2999 0.0281  -0.0613 -0.0747 71  THR   B O   
4771 C  CB  . THR   B 71  ? 0.2539 0.2141 0.2497 0.0049  -0.0775 -0.0159 71  THR   B CB  
4772 O  OG1 . THR   B 71  ? 0.2758 0.2357 0.2959 -0.0178 -0.0787 0.0140  71  THR   B OG1 
4773 C  CG2 . THR   B 71  ? 0.2707 0.2057 0.2781 0.0005  -0.0637 -0.0063 71  THR   B CG2 
4781 N  N   . ASN   B 72  ? 0.2077 0.2098 0.2361 0.0234  -0.0656 -0.0702 72  ASN   B N   
4782 C  CA  . ASN   B 72  ? 0.2124 0.2143 0.2390 0.0218  -0.0570 -0.0729 72  ASN   B CA  
4783 C  C   . ASN   B 72  ? 0.2194 0.2223 0.2483 0.0081  -0.0230 -0.0652 72  ASN   B C   
4784 O  O   . ASN   B 72  ? 0.2243 0.2375 0.2708 0.0044  0.0012  -0.0763 72  ASN   B O   
4785 C  CB  . ASN   B 72  ? 0.2108 0.2436 0.2566 0.0171  -0.0664 -0.0660 72  ASN   B CB  
4786 C  CG  . ASN   B 72  ? 0.2285 0.2582 0.2623 0.0363  -0.0625 -0.0368 72  ASN   B CG  
4787 O  OD1 . ASN   B 72  ? 0.2692 0.2698 0.2456 0.0219  -0.0433 -0.0419 72  ASN   B OD1 
4788 N  ND2 . ASN   B 72  ? 0.2377 0.2617 0.3059 0.0487  -0.0471 -0.0013 72  ASN   B ND2 
4795 N  N   . GLY   B 73  ? 0.2102 0.2144 0.2355 0.0076  -0.0267 -0.0642 73  GLY   B N   
4796 C  CA  . GLY   B 73  ? 0.1924 0.2243 0.2091 0.0032  -0.0211 -0.0590 73  GLY   B CA  
4797 C  C   . GLY   B 73  ? 0.1958 0.2305 0.1549 -0.0014 -0.0167 -0.0618 73  GLY   B C   
4798 O  O   . GLY   B 73  ? 0.1914 0.2238 0.1785 0.0084  -0.0205 -0.0453 73  GLY   B O   
4802 N  N   . PRO   B 74  ? 0.2216 0.2485 0.1522 -0.0029 -0.0276 -0.0376 74  PRO   B N   
4803 C  CA  . PRO   B 74  ? 0.2104 0.2442 0.1407 0.0044  -0.0362 -0.0172 74  PRO   B CA  
4804 C  C   . PRO   B 74  ? 0.1928 0.2304 0.1528 0.0014  -0.0197 -0.0137 74  PRO   B C   
4805 O  O   . PRO   B 74  ? 0.1909 0.2210 0.2068 -0.0001 -0.0131 -0.0363 74  PRO   B O   
4806 C  CB  . PRO   B 74  ? 0.2300 0.2564 0.1461 0.0046  -0.0275 -0.0287 74  PRO   B CB  
4807 C  CG  . PRO   B 74  ? 0.2503 0.2654 0.1766 0.0026  -0.0330 -0.0213 74  PRO   B CG  
4808 C  CD  . PRO   B 74  ? 0.2445 0.2545 0.1690 0.0017  -0.0235 -0.0347 74  PRO   B CD  
4816 N  N   . LEU   B 75  ? 0.1947 0.2139 0.1324 0.0117  -0.0312 -0.0185 75  LEU   B N   
4817 C  CA  . LEU   B 75  ? 0.2071 0.2187 0.1248 0.0042  -0.0194 -0.0054 75  LEU   B CA  
4818 C  C   . LEU   B 75  ? 0.2118 0.2223 0.1249 0.0045  -0.0084 -0.0044 75  LEU   B C   
4819 O  O   . LEU   B 75  ? 0.2078 0.2297 0.1580 -0.0011 -0.0006 -0.0050 75  LEU   B O   
4820 C  CB  . LEU   B 75  ? 0.2044 0.2265 0.1237 -0.0015 -0.0152 0.0001  75  LEU   B CB  
4821 C  CG  . LEU   B 75  ? 0.2240 0.2276 0.1421 -0.0277 0.0035  -0.0031 75  LEU   B CG  
4822 C  CD1 . LEU   B 75  ? 0.2570 0.2316 0.1506 -0.0443 0.0182  -0.0073 75  LEU   B CD1 
4823 C  CD2 . LEU   B 75  ? 0.2568 0.2516 0.2383 -0.0146 -0.0017 -0.0015 75  LEU   B CD2 
4835 N  N   . LYS   B 76  ? 0.2098 0.2355 0.1643 0.0063  -0.0030 -0.0027 76  LYS   B N   
4836 C  CA  . LYS   B 76  ? 0.2216 0.2484 0.2119 -0.0008 0.0275  -0.0020 76  LYS   B CA  
4837 C  C   . LYS   B 76  ? 0.2011 0.2345 0.1567 -0.0034 0.0092  0.0053  76  LYS   B C   
4838 O  O   . LYS   B 76  ? 0.1891 0.2260 0.1636 -0.0084 0.0084  0.0095  76  LYS   B O   
4839 C  CB  . LYS   B 76  ? 0.2363 0.2642 0.2982 0.0020  0.0476  -0.0407 76  LYS   B CB  
4840 C  CG  . LYS   B 76  ? 0.2444 0.2960 0.3406 0.0187  0.0220  -0.0418 76  LYS   B CG  
4841 C  CD  . LYS   B 76  ? 0.2515 0.3103 0.3905 0.0301  0.0249  -0.0536 76  LYS   B CD  
4842 C  CE  . LYS   B 76  ? 0.2623 0.3368 0.4443 0.0339  0.0127  -0.0568 76  LYS   B CE  
4843 N  NZ  . LYS   B 76  ? 0.2564 0.3472 0.4739 0.0275  -0.0107 -0.0834 76  LYS   B NZ  
4857 N  N   . VAL   B 77  ? 0.2015 0.2486 0.1646 0.0068  0.0035  0.0170  77  VAL   B N   
4858 C  CA  . VAL   B 77  ? 0.1989 0.2451 0.1751 0.0089  0.0054  0.0311  77  VAL   B CA  
4859 C  C   . VAL   B 77  ? 0.1904 0.2020 0.1640 0.0185  0.0184  0.0253  77  VAL   B C   
4860 O  O   . VAL   B 77  ? 0.1854 0.1918 0.1716 0.0243  0.0251  0.0286  77  VAL   B O   
4861 C  CB  . VAL   B 77  ? 0.2160 0.2704 0.1993 0.0043  0.0067  0.0376  77  VAL   B CB  
4862 C  CG1 . VAL   B 77  ? 0.2232 0.2558 0.2361 -0.0064 0.0171  0.0606  77  VAL   B CG1 
4863 C  CG2 . VAL   B 77  ? 0.2356 0.2879 0.2284 -0.0023 -0.0064 0.0451  77  VAL   B CG2 
4873 N  N   . GLY   B 78  ? 0.1924 0.1884 0.1587 0.0236  0.0105  0.0126  78  GLY   B N   
4874 C  CA  . GLY   B 78  ? 0.1935 0.1805 0.1427 0.0128  0.0092  0.0108  78  GLY   B CA  
4875 C  C   . GLY   B 78  ? 0.1799 0.1884 0.1431 0.0156  0.0084  0.0142  78  GLY   B C   
4876 O  O   . GLY   B 78  ? 0.1801 0.1872 0.1666 0.0085  0.0066  0.0231  78  GLY   B O   
4880 N  N   . GLY   B 79  ? 0.1814 0.1930 0.1550 0.0078  0.0063  0.0081  79  GLY   B N   
4881 C  CA  . GLY   B 79  ? 0.1841 0.1832 0.1560 0.0220  0.0100  0.0096  79  GLY   B CA  
4882 C  C   . GLY   B 79  ? 0.1645 0.1818 0.1469 0.0199  0.0096  -0.0165 79  GLY   B C   
4883 O  O   . GLY   B 79  ? 0.1776 0.1778 0.1592 0.0138  0.0169  0.0125  79  GLY   B O   
4887 N  N   . SER   B 80  ? 0.1713 0.1822 0.1532 0.0094  0.0113  -0.0070 80  SER   B N   
4888 C  CA  . SER   B 80  ? 0.1608 0.1822 0.1646 0.0104  0.0002  -0.0041 80  SER   B CA  
4889 C  C   . SER   B 80  ? 0.1435 0.1859 0.1722 0.0132  -0.0093 -0.0143 80  SER   B C   
4890 O  O   . SER   B 80  ? 0.1664 0.1786 0.2116 0.0184  0.0007  -0.0116 80  SER   B O   
4891 C  CB  . SER   B 80  ? 0.1486 0.1705 0.1828 0.0030  -0.0107 -0.0034 80  SER   B CB  
4892 O  OG  . SER   B 80  ? 0.1683 0.1839 0.1929 0.0044  -0.0213 -0.0033 80  SER   B OG  
4898 N  N   . CYS   B 81  ? 0.1447 0.1745 0.1811 0.0083  -0.0115 -0.0167 81  CYS   B N   
4899 C  CA  . CYS   B 81  ? 0.1546 0.1692 0.1675 0.0057  -0.0233 -0.0138 81  CYS   B CA  
4900 C  C   . CYS   B 81  ? 0.1694 0.1714 0.1416 -0.0020 -0.0105 -0.0138 81  CYS   B C   
4901 O  O   . CYS   B 81  ? 0.1852 0.1606 0.1645 0.0044  -0.0020 -0.0243 81  CYS   B O   
4902 C  CB  . CYS   B 81  ? 0.1927 0.1724 0.1802 0.0006  -0.0193 -0.0021 81  CYS   B CB  
4903 S  SG  . CYS   B 81  ? 0.1780 0.1922 0.1755 -0.0044 -0.0282 -0.0130 81  CYS   B SG  
4909 N  N   . VAL   B 82  ? 0.1656 0.1681 0.1607 -0.0055 -0.0255 0.0074  82  VAL   B N   
4910 C  CA  . VAL   B 82  ? 0.1755 0.1662 0.1531 -0.0129 -0.0195 -0.0050 82  VAL   B CA  
4911 C  C   . VAL   B 82  ? 0.1826 0.1445 0.1723 -0.0119 -0.0194 -0.0049 82  VAL   B C   
4912 O  O   . VAL   B 82  ? 0.1846 0.1535 0.2007 -0.0137 -0.0076 -0.0158 82  VAL   B O   
4913 C  CB  . VAL   B 82  ? 0.1858 0.1710 0.1639 0.0034  -0.0183 0.0081  82  VAL   B CB  
4914 C  CG1 . VAL   B 82  ? 0.2142 0.1816 0.1831 -0.0030 -0.0280 0.0105  82  VAL   B CG1 
4915 C  CG2 . VAL   B 82  ? 0.1967 0.1861 0.1942 -0.0065 -0.0368 0.0121  82  VAL   B CG2 
4925 N  N   . LEU   B 83  ? 0.1659 0.1475 0.1722 -0.0242 -0.0201 -0.0039 83  LEU   B N   
4926 C  CA  . LEU   B 83  ? 0.1745 0.1585 0.1428 -0.0222 -0.0240 -0.0022 83  LEU   B CA  
4927 C  C   . LEU   B 83  ? 0.1634 0.1635 0.1392 -0.0199 -0.0212 0.0053  83  LEU   B C   
4928 O  O   . LEU   B 83  ? 0.1795 0.1636 0.1358 -0.0136 -0.0151 0.0051  83  LEU   B O   
4929 C  CB  . LEU   B 83  ? 0.1909 0.1694 0.1543 -0.0297 -0.0309 -0.0221 83  LEU   B CB  
4930 C  CG  . LEU   B 83  ? 0.2087 0.1836 0.1650 -0.0221 -0.0312 -0.0126 83  LEU   B CG  
4931 C  CD1 . LEU   B 83  ? 0.2207 0.1787 0.1905 -0.0084 -0.0315 -0.0119 83  LEU   B CD1 
4932 C  CD2 . LEU   B 83  ? 0.2117 0.1832 0.1789 -0.0112 -0.0192 -0.0233 83  LEU   B CD2 
4944 N  N   . SER   B 84  ? 0.1730 0.1705 0.1726 -0.0194 -0.0170 -0.0021 84  SER   B N   
4945 C  CA  . SER   B 84  ? 0.1794 0.1830 0.1645 -0.0269 -0.0077 0.0240  84  SER   B CA  
4946 C  C   . SER   B 84  ? 0.1822 0.1911 0.1213 -0.0166 -0.0190 0.0252  84  SER   B C   
4947 O  O   . SER   B 84  ? 0.1947 0.1761 0.1380 -0.0179 -0.0139 0.0001  84  SER   B O   
4948 C  CB  . SER   B 84  ? 0.1903 0.1843 0.2163 -0.0355 0.0130  0.0080  84  SER   B CB  
4949 O  OG  . SER   B 84  ? 0.1972 0.2036 0.2758 -0.0448 0.0194  0.0188  84  SER   B OG  
4955 N  N   . GLY   B 85  ? 0.1926 0.2094 0.1404 -0.0171 -0.0189 0.0213  85  GLY   B N   
4956 C  CA  . GLY   B 85  ? 0.1984 0.2178 0.1650 -0.0279 0.0015  -0.0074 85  GLY   B CA  
4957 C  C   . GLY   B 85  ? 0.1940 0.1850 0.1519 -0.0328 -0.0073 0.0063  85  GLY   B C   
4958 O  O   . GLY   B 85  ? 0.1957 0.1915 0.1595 -0.0548 0.0063  -0.0155 85  GLY   B O   
4962 N  N   . HIS   B 86  ? 0.2013 0.1750 0.1611 -0.0341 -0.0242 0.0168  86  HIS   B N   
4963 C  CA  . HIS   B 86  ? 0.1954 0.1838 0.1713 -0.0333 -0.0353 0.0214  86  HIS   B CA  
4964 C  C   . HIS   B 86  ? 0.1849 0.2023 0.1770 -0.0408 -0.0036 0.0376  86  HIS   B C   
4965 O  O   . HIS   B 86  ? 0.1994 0.2136 0.1658 -0.0308 0.0090  0.0342  86  HIS   B O   
4966 C  CB  . HIS   B 86  ? 0.1929 0.1796 0.1891 -0.0261 -0.0306 0.0104  86  HIS   B CB  
4967 C  CG  . HIS   B 86  ? 0.1902 0.1781 0.1688 -0.0175 -0.0348 0.0096  86  HIS   B CG  
4968 N  ND1 . HIS   B 86  ? 0.2007 0.2117 0.1970 -0.0340 -0.0376 -0.0039 86  HIS   B ND1 
4969 C  CD2 . HIS   B 86  ? 0.1855 0.1895 0.1907 -0.0127 -0.0306 0.0208  86  HIS   B CD2 
4970 C  CE1 . HIS   B 86  ? 0.2043 0.2099 0.1823 -0.0148 -0.0155 -0.0180 86  HIS   B CE1 
4971 N  NE2 . HIS   B 86  ? 0.1941 0.2035 0.1915 -0.0031 -0.0182 0.0047  86  HIS   B NE2 
4979 N  N   . ASN   B 87  ? 0.1718 0.2107 0.1863 -0.0269 -0.0036 0.0304  87  ASN   B N   
4980 C  CA  . ASN   B 87  ? 0.1998 0.2210 0.1837 -0.0238 0.0184  0.0192  87  ASN   B CA  
4981 C  C   . ASN   B 87  ? 0.2243 0.1994 0.1706 -0.0320 0.0348  0.0039  87  ASN   B C   
4982 O  O   . ASN   B 87  ? 0.2421 0.2109 0.1989 -0.0278 0.0586  0.0081  87  ASN   B O   
4983 C  CB  . ASN   B 87  ? 0.1998 0.2430 0.2101 -0.0200 0.0184  0.0170  87  ASN   B CB  
4984 C  CG  . ASN   B 87  ? 0.1979 0.2712 0.2160 0.0194  0.0343  0.0326  87  ASN   B CG  
4985 O  OD1 . ASN   B 87  ? 0.2003 0.2577 0.2069 0.0171  0.0451  0.0520  87  ASN   B OD1 
4986 N  ND2 . ASN   B 87  ? 0.2272 0.2963 0.2699 0.0254  0.0394  0.0120  87  ASN   B ND2 
4993 N  N   . LEU   B 88  ? 0.2024 0.1793 0.1465 -0.0334 0.0128  0.0000  88  LEU   B N   
4994 C  CA  . LEU   B 88  ? 0.2032 0.1691 0.1493 -0.0318 -0.0017 -0.0026 88  LEU   B CA  
4995 C  C   . LEU   B 88  ? 0.2098 0.1726 0.1514 -0.0310 -0.0155 -0.0046 88  LEU   B C   
4996 O  O   . LEU   B 88  ? 0.2115 0.1847 0.1883 -0.0149 -0.0296 -0.0057 88  LEU   B O   
4997 C  CB  . LEU   B 88  ? 0.2096 0.1782 0.1728 -0.0311 -0.0147 0.0137  88  LEU   B CB  
4998 C  CG  . LEU   B 88  ? 0.2400 0.2226 0.1937 -0.0253 -0.0296 0.0389  88  LEU   B CG  
4999 C  CD1 . LEU   B 88  ? 0.2545 0.2597 0.1966 -0.0431 -0.0273 0.0518  88  LEU   B CD1 
5000 C  CD2 . LEU   B 88  ? 0.2831 0.2524 0.2708 0.0188  -0.0640 0.0272  88  LEU   B CD2 
5012 N  N   . ALA   B 89  ? 0.2061 0.1722 0.1449 -0.0382 0.0038  -0.0040 89  ALA   B N   
5013 C  CA  . ALA   B 89  ? 0.2038 0.1616 0.1249 -0.0404 0.0041  0.0093  89  ALA   B CA  
5014 C  C   . ALA   B 89  ? 0.1990 0.1675 0.1498 -0.0465 0.0041  0.0062  89  ALA   B C   
5015 O  O   . ALA   B 89  ? 0.1676 0.1807 0.1882 -0.0365 0.0025  -0.0268 89  ALA   B O   
5016 C  CB  . ALA   B 89  ? 0.1989 0.1674 0.1383 -0.0457 -0.0076 0.0155  89  ALA   B CB  
5022 N  N   . LYS   B 90  ? 0.2208 0.1586 0.1542 -0.0494 -0.0088 0.0078  90  LYS   B N   
5023 C  CA  . LYS   B 90  ? 0.2392 0.1562 0.1544 -0.0560 -0.0073 0.0130  90  LYS   B CA  
5024 C  C   . LYS   B 90  ? 0.2310 0.1396 0.1854 -0.0398 -0.0037 -0.0117 90  LYS   B C   
5025 O  O   . LYS   B 90  ? 0.2438 0.1654 0.2037 -0.0565 0.0070  0.0025  90  LYS   B O   
5026 C  CB  . LYS   B 90  ? 0.2603 0.1750 0.1770 -0.0451 0.0163  0.0110  90  LYS   B CB  
5027 C  CG  . LYS   B 90  ? 0.2726 0.2035 0.1965 -0.0441 0.0398  -0.0018 90  LYS   B CG  
5028 C  CD  . LYS   B 90  ? 0.3152 0.2381 0.2661 -0.0319 0.0575  -0.0173 90  LYS   B CD  
5029 C  CE  . LYS   B 90  ? 0.3268 0.2579 0.3244 -0.0309 0.0621  -0.0296 90  LYS   B CE  
5030 N  NZ  . LYS   B 90  ? 0.3211 0.2471 0.2886 -0.0498 0.0855  -0.0250 90  LYS   B NZ  
5044 N  N   . HIS   B 91  ? 0.1953 0.1459 0.1378 -0.0248 -0.0126 0.0189  91  HIS   B N   
5045 C  CA  . HIS   B 91  ? 0.1882 0.1421 0.1498 -0.0271 -0.0185 0.0004  91  HIS   B CA  
5046 C  C   . HIS   B 91  ? 0.1798 0.1530 0.1314 -0.0373 -0.0097 -0.0045 91  HIS   B C   
5047 O  O   . HIS   B 91  ? 0.1752 0.1617 0.1333 -0.0255 -0.0217 0.0038  91  HIS   B O   
5048 C  CB  . HIS   B 91  ? 0.2136 0.1467 0.1981 -0.0133 -0.0096 0.0145  91  HIS   B CB  
5049 C  CG  . HIS   B 91  ? 0.2525 0.1755 0.2736 -0.0050 0.0268  0.0054  91  HIS   B CG  
5050 N  ND1 . HIS   B 91  ? 0.2824 0.1802 0.3448 -0.0134 0.0471  0.0027  91  HIS   B ND1 
5051 C  CD2 . HIS   B 91  ? 0.2673 0.1970 0.3389 0.0018  0.0197  0.0497  91  HIS   B CD2 
5052 C  CE1 . HIS   B 91  ? 0.2896 0.1944 0.3791 0.0113  0.0490  0.0076  91  HIS   B CE1 
5053 N  NE2 . HIS   B 91  ? 0.2833 0.2128 0.3866 0.0196  0.0551  0.0508  91  HIS   B NE2 
5061 N  N   . CYS   B 92  ? 0.1797 0.1540 0.1416 -0.0284 -0.0204 0.0003  92  CYS   B N   
5062 C  CA  . CYS   B 92  ? 0.1928 0.1439 0.1231 -0.0184 -0.0066 -0.0083 92  CYS   B CA  
5063 C  C   . CYS   B 92  ? 0.1932 0.1307 0.1226 -0.0120 -0.0081 -0.0169 92  CYS   B C   
5064 O  O   . CYS   B 92  ? 0.1792 0.1552 0.1485 -0.0185 -0.0045 0.0023  92  CYS   B O   
5065 C  CB  . CYS   B 92  ? 0.1736 0.1579 0.1447 -0.0112 -0.0180 -0.0176 92  CYS   B CB  
5066 S  SG  . CYS   B 92  ? 0.1661 0.1614 0.1529 -0.0079 -0.0121 0.0056  92  CYS   B SG  
5072 N  N   . LEU   B 93  ? 0.1877 0.1335 0.1293 -0.0056 -0.0003 -0.0122 93  LEU   B N   
5073 C  CA  . LEU   B 93  ? 0.1867 0.1559 0.1209 0.0109  -0.0165 -0.0006 93  LEU   B CA  
5074 C  C   . LEU   B 93  ? 0.1710 0.1569 0.1064 0.0006  -0.0020 -0.0084 93  LEU   B C   
5075 O  O   . LEU   B 93  ? 0.1586 0.1559 0.1317 -0.0082 -0.0067 -0.0127 93  LEU   B O   
5076 C  CB  . LEU   B 93  ? 0.1904 0.1660 0.1366 0.0121  -0.0163 0.0059  93  LEU   B CB  
5077 C  CG  . LEU   B 93  ? 0.1895 0.1740 0.1540 -0.0089 -0.0027 0.0140  93  LEU   B CG  
5078 C  CD1 . LEU   B 93  ? 0.1776 0.1758 0.1554 0.0127  -0.0038 -0.0027 93  LEU   B CD1 
5079 C  CD2 . LEU   B 93  ? 0.1825 0.1550 0.1696 -0.0034 -0.0278 -0.0149 93  LEU   B CD2 
5091 N  N   . HIS   B 94  ? 0.1726 0.1395 0.1250 -0.0095 -0.0034 -0.0134 94  HIS   B N   
5092 C  CA  . HIS   B 94  ? 0.1649 0.1536 0.1071 0.0000  -0.0011 0.0025  94  HIS   B CA  
5093 C  C   . HIS   B 94  ? 0.1515 0.1709 0.1416 0.0012  -0.0047 -0.0078 94  HIS   B C   
5094 O  O   . HIS   B 94  ? 0.1489 0.1616 0.1807 -0.0031 0.0149  -0.0047 94  HIS   B O   
5095 C  CB  . HIS   B 94  ? 0.1628 0.1557 0.1340 0.0089  -0.0003 -0.0041 94  HIS   B CB  
5096 C  CG  . HIS   B 94  ? 0.1514 0.1562 0.1470 -0.0105 -0.0211 0.0035  94  HIS   B CG  
5097 N  ND1 . HIS   B 94  ? 0.1586 0.1625 0.1501 -0.0012 -0.0147 -0.0043 94  HIS   B ND1 
5098 C  CD2 . HIS   B 94  ? 0.1609 0.1491 0.1493 0.0033  -0.0180 0.0036  94  HIS   B CD2 
5099 C  CE1 . HIS   B 94  ? 0.1709 0.1641 0.1611 -0.0025 -0.0133 0.0013  94  HIS   B CE1 
5100 N  NE2 . HIS   B 94  ? 0.1560 0.1728 0.1509 -0.0071 -0.0209 -0.0011 94  HIS   B NE2 
5108 N  N   . VAL   B 95  ? 0.1373 0.1596 0.1500 0.0015  0.0035  -0.0164 95  VAL   B N   
5109 C  CA  . VAL   B 95  ? 0.1519 0.1620 0.1474 0.0008  0.0029  0.0064  95  VAL   B CA  
5110 C  C   . VAL   B 95  ? 0.1496 0.1703 0.1590 -0.0004 0.0141  0.0102  95  VAL   B C   
5111 O  O   . VAL   B 95  ? 0.1584 0.1711 0.1608 0.0055  0.0084  0.0176  95  VAL   B O   
5112 C  CB  . VAL   B 95  ? 0.1668 0.1590 0.1364 0.0016  0.0018  0.0032  95  VAL   B CB  
5113 C  CG1 . VAL   B 95  ? 0.1861 0.1811 0.1560 -0.0019 0.0038  0.0114  95  VAL   B CG1 
5114 C  CG2 . VAL   B 95  ? 0.1741 0.1644 0.1359 0.0160  -0.0066 -0.0082 95  VAL   B CG2 
5124 N  N   . VAL   B 96  ? 0.1682 0.1558 0.1558 0.0075  0.0140  0.0169  96  VAL   B N   
5125 C  CA  . VAL   B 96  ? 0.2003 0.1612 0.1497 0.0007  0.0114  0.0197  96  VAL   B CA  
5126 C  C   . VAL   B 96  ? 0.2007 0.1467 0.1617 0.0034  0.0111  0.0169  96  VAL   B C   
5127 O  O   . VAL   B 96  ? 0.2060 0.1523 0.1719 0.0103  0.0231  -0.0020 96  VAL   B O   
5128 C  CB  . VAL   B 96  ? 0.1941 0.1781 0.1482 0.0094  0.0035  0.0083  96  VAL   B CB  
5129 C  CG1 . VAL   B 96  ? 0.1992 0.1985 0.1614 0.0262  0.0134  -0.0011 96  VAL   B CG1 
5130 C  CG2 . VAL   B 96  ? 0.1970 0.1655 0.1682 0.0021  0.0049  -0.0031 96  VAL   B CG2 
5140 N  N   . GLY   B 97  ? 0.1970 0.1544 0.1554 0.0007  0.0117  0.0234  97  GLY   B N   
5141 C  CA  . GLY   B 97  ? 0.2071 0.1605 0.1667 0.0026  0.0200  0.0213  97  GLY   B CA  
5142 C  C   . GLY   B 97  ? 0.2268 0.1873 0.1692 0.0100  -0.0034 0.0116  97  GLY   B C   
5143 O  O   . GLY   B 97  ? 0.2191 0.1938 0.1655 0.0061  -0.0013 0.0096  97  GLY   B O   
5147 N  N   . PRO   B 98  ? 0.2342 0.1753 0.1673 0.0036  0.0177  0.0213  98  PRO   B N   
5148 C  CA  . PRO   B 98  ? 0.2297 0.1835 0.1854 0.0039  0.0211  0.0133  98  PRO   B CA  
5149 C  C   . PRO   B 98  ? 0.2455 0.1895 0.1549 0.0239  0.0244  0.0250  98  PRO   B C   
5150 O  O   . PRO   B 98  ? 0.2469 0.1882 0.1776 0.0239  0.0255  0.0340  98  PRO   B O   
5151 C  CB  . PRO   B 98  ? 0.2186 0.1994 0.1875 0.0071  0.0434  0.0176  98  PRO   B CB  
5152 C  CG  . PRO   B 98  ? 0.2120 0.1880 0.1859 0.0035  0.0365  0.0350  98  PRO   B CG  
5153 C  CD  . PRO   B 98  ? 0.2129 0.1808 0.1891 0.0091  0.0348  0.0283  98  PRO   B CD  
5161 N  N   . ASN   B 99  ? 0.2335 0.2077 0.1645 0.0355  0.0220  0.0089  99  ASN   B N   
5162 C  CA  . ASN   B 99  ? 0.2594 0.2140 0.1716 0.0358  0.0196  0.0370  99  ASN   B CA  
5163 C  C   . ASN   B 99  ? 0.2951 0.2553 0.1844 0.0307  0.0304  0.0649  99  ASN   B C   
5164 O  O   . ASN   B 99  ? 0.3162 0.2659 0.1951 0.0415  0.0178  0.0533  99  ASN   B O   
5165 C  CB  . ASN   B 99  ? 0.2629 0.2226 0.1907 0.0459  0.0038  0.0237  99  ASN   B CB  
5166 C  CG  . ASN   B 99  ? 0.2753 0.2393 0.2173 0.0360  -0.0062 0.0355  99  ASN   B CG  
5167 O  OD1 . ASN   B 99  ? 0.2865 0.2464 0.2410 0.0344  -0.0073 0.0599  99  ASN   B OD1 
5168 N  ND2 . ASN   B 99  ? 0.2727 0.2438 0.2301 0.0446  -0.0197 0.0311  99  ASN   B ND2 
5175 N  N   A VAL   B 100 ? 0.3133 0.2603 0.2219 0.0218  0.0294  0.0851  100 VAL   B N   
5176 N  N   B VAL   B 100 ? 0.3170 0.2665 0.2258 0.0272  0.0246  0.0763  100 VAL   B N   
5177 C  CA  A VAL   B 100 ? 0.3481 0.2860 0.2842 0.0103  0.0328  0.0944  100 VAL   B CA  
5178 C  CA  B VAL   B 100 ? 0.3439 0.2841 0.2747 0.0217  0.0227  0.0817  100 VAL   B CA  
5179 C  C   A VAL   B 100 ? 0.3742 0.2945 0.2736 0.0202  0.0456  0.1222  100 VAL   B C   
5180 C  C   B VAL   B 100 ? 0.3658 0.2919 0.2764 0.0266  0.0321  0.1033  100 VAL   B C   
5181 O  O   A VAL   B 100 ? 0.3896 0.3126 0.2803 0.0158  0.0590  0.1193  100 VAL   B O   
5182 O  O   B VAL   B 100 ? 0.3715 0.3002 0.2860 0.0230  0.0354  0.0994  100 VAL   B O   
5183 C  CB  A VAL   B 100 ? 0.3581 0.3057 0.3647 -0.0177 0.0334  0.1022  100 VAL   B CB  
5184 C  CB  B VAL   B 100 ? 0.3502 0.2949 0.3214 0.0098  0.0166  0.0752  100 VAL   B CB  
5185 C  CG1 A VAL   B 100 ? 0.3664 0.3149 0.4000 -0.0241 0.0403  0.1016  100 VAL   B CG1 
5186 C  CG1 B VAL   B 100 ? 0.3550 0.3002 0.3404 0.0071  0.0184  0.0728  100 VAL   B CG1 
5187 C  CG2 A VAL   B 100 ? 0.3586 0.3132 0.3841 -0.0270 0.0396  0.1151  100 VAL   B CG2 
5188 C  CG2 B VAL   B 100 ? 0.3507 0.2986 0.3341 0.0056  0.0163  0.0761  100 VAL   B CG2 
5207 N  N   . ASN   B 101 ? 0.3786 0.2919 0.2738 0.0353  0.0374  0.1206  101 ASN   B N   
5208 C  CA  . ASN   B 101 ? 0.4146 0.3063 0.3045 0.0555  0.0267  0.1265  101 ASN   B CA  
5209 C  C   . ASN   B 101 ? 0.4540 0.3335 0.2844 0.0697  0.0115  0.1456  101 ASN   B C   
5210 O  O   . ASN   B 101 ? 0.4646 0.3518 0.3408 0.0801  0.0171  0.1040  101 ASN   B O   
5211 C  CB  . ASN   B 101 ? 0.4083 0.3001 0.3279 0.0497  0.0445  0.1138  101 ASN   B CB  
5212 C  CG  . ASN   B 101 ? 0.4009 0.2981 0.3410 0.0537  0.0488  0.1109  101 ASN   B CG  
5213 O  OD1 . ASN   B 101 ? 0.4110 0.2994 0.3801 0.0476  0.0671  0.1079  101 ASN   B OD1 
5214 N  ND2 . ASN   B 101 ? 0.3884 0.2993 0.3361 0.0573  0.0370  0.1001  101 ASN   B ND2 
5222 N  N   . LYS   B 102 ? 0.4826 0.3547 0.3001 0.0627  0.0148  0.1343  102 LYS   B N   
5223 C  CA  . LYS   B 102 ? 0.5115 0.3933 0.3194 0.0464  0.0185  0.1070  102 LYS   B CA  
5224 C  C   . LYS   B 102 ? 0.5062 0.3927 0.2873 0.0505  0.0373  0.0975  102 LYS   B C   
5225 O  O   . LYS   B 102 ? 0.5210 0.4017 0.3055 0.0543  0.0177  0.0727  102 LYS   B O   
5226 C  CB  . LYS   B 102 ? 0.5383 0.4333 0.3812 0.0294  0.0254  0.0721  102 LYS   B CB  
5227 C  CG  . LYS   B 102 ? 0.5589 0.4697 0.4638 0.0188  0.0305  0.0341  102 LYS   B CG  
5228 C  CD  . LYS   B 102 ? 0.5768 0.4948 0.5369 0.0116  0.0393  0.0091  102 LYS   B CD  
5229 C  CE  . LYS   B 102 ? 0.5907 0.5162 0.5966 0.0038  0.0476  -0.0083 102 LYS   B CE  
5230 N  NZ  . LYS   B 102 ? 0.5988 0.5314 0.6353 -0.0004 0.0505  -0.0175 102 LYS   B NZ  
5244 N  N   . GLY   B 103 ? 0.4821 0.3821 0.2666 0.0469  0.0669  0.1003  103 GLY   B N   
5245 C  CA  . GLY   B 103 ? 0.4621 0.3767 0.2948 0.0449  0.0842  0.0720  103 GLY   B CA  
5246 C  C   . GLY   B 103 ? 0.4392 0.3660 0.2981 0.0302  0.0888  0.0577  103 GLY   B C   
5247 O  O   . GLY   B 103 ? 0.4491 0.3816 0.3104 0.0233  0.0892  0.0595  103 GLY   B O   
5251 N  N   A GLU   B 104 ? 0.4123 0.3382 0.2747 0.0192  0.0996  0.0449  104 GLU   B N   
5252 N  N   B GLU   B 104 ? 0.4231 0.3589 0.3104 0.0198  0.0720  0.0472  104 GLU   B N   
5253 C  CA  A GLU   B 104 ? 0.3803 0.3149 0.2386 0.0181  0.1027  0.0263  104 GLU   B CA  
5254 C  CA  B GLU   B 104 ? 0.4060 0.3535 0.3100 0.0137  0.0528  0.0331  104 GLU   B CA  
5255 C  C   A GLU   B 104 ? 0.3887 0.3211 0.2737 0.0087  0.1247  0.0150  104 GLU   B C   
5256 C  C   B GLU   B 104 ? 0.3981 0.3514 0.3244 0.0049  0.0549  0.0260  104 GLU   B C   
5257 O  O   A GLU   B 104 ? 0.3927 0.3235 0.3297 0.0032  0.1170  0.0023  104 GLU   B O   
5258 O  O   B GLU   B 104 ? 0.3978 0.3523 0.3413 0.0030  0.0538  0.0220  104 GLU   B O   
5259 C  CB  A GLU   B 104 ? 0.3538 0.2888 0.2151 0.0239  0.0589  0.0096  104 GLU   B CB  
5260 C  CB  B GLU   B 104 ? 0.3994 0.3497 0.2994 0.0158  0.0309  0.0238  104 GLU   B CB  
5261 C  CG  A GLU   B 104 ? 0.3342 0.2706 0.1738 0.0289  0.0122  -0.0163 104 GLU   B CG  
5262 C  CG  B GLU   B 104 ? 0.3943 0.3468 0.2877 0.0176  0.0120  0.0118  104 GLU   B CG  
5263 C  CD  A GLU   B 104 ? 0.3241 0.2638 0.1682 0.0240  -0.0047 -0.0123 104 GLU   B CD  
5264 C  CD  B GLU   B 104 ? 0.3911 0.3451 0.2836 0.0169  0.0002  0.0053  104 GLU   B CD  
5265 O  OE1 A GLU   B 104 ? 0.2970 0.2465 0.1574 0.0202  0.0059  -0.0051 104 GLU   B OE1 
5266 O  OE1 B GLU   B 104 ? 0.3877 0.3421 0.2781 0.0164  -0.0011 0.0043  104 GLU   B OE1 
5267 O  OE2 A GLU   B 104 ? 0.3361 0.2764 0.1964 0.0227  -0.0405 -0.0249 104 GLU   B OE2 
5268 O  OE2 B GLU   B 104 ? 0.3921 0.3479 0.2970 0.0172  -0.0094 -0.0008 104 GLU   B OE2 
5281 N  N   A ASP   B 105 ? 0.3869 0.3340 0.2741 -0.0015 0.1487  0.0251  105 ASP   B N   
5282 N  N   B ASP   B 105 ? 0.3892 0.3505 0.3260 -0.0032 0.0582  0.0255  105 ASP   B N   
5283 C  CA  A ASP   B 105 ? 0.3978 0.3515 0.2939 -0.0117 0.1761  0.0292  105 ASP   B CA  
5284 C  CA  B ASP   B 105 ? 0.3851 0.3514 0.3320 -0.0106 0.0640  0.0224  105 ASP   B CA  
5285 C  C   A ASP   B 105 ? 0.3854 0.3283 0.2821 -0.0226 0.1690  0.0287  105 ASP   B C   
5286 C  C   B ASP   B 105 ? 0.3782 0.3465 0.3243 -0.0118 0.0578  0.0135  105 ASP   B C   
5287 O  O   A ASP   B 105 ? 0.3736 0.3169 0.2751 -0.0183 0.1668  0.0428  105 ASP   B O   
5288 O  O   B ASP   B 105 ? 0.3756 0.3434 0.3176 -0.0105 0.0572  0.0154  105 ASP   B O   
5289 C  CB  A ASP   B 105 ? 0.4158 0.3869 0.3554 -0.0019 0.1966  0.0053  105 ASP   B CB  
5290 C  CB  B ASP   B 105 ? 0.3842 0.3556 0.3490 -0.0146 0.0761  0.0231  105 ASP   B CB  
5291 C  CG  A ASP   B 105 ? 0.4338 0.4177 0.4311 0.0034  0.2087  -0.0103 105 ASP   B CG  
5292 C  CG  B ASP   B 105 ? 0.3852 0.3571 0.3670 -0.0200 0.0865  0.0289  105 ASP   B CG  
5293 O  OD1 A ASP   B 105 ? 0.4350 0.4219 0.4329 -0.0042 0.2296  0.0012  105 ASP   B OD1 
5294 O  OD1 B ASP   B 105 ? 0.3858 0.3600 0.3755 -0.0245 0.0874  0.0292  105 ASP   B OD1 
5295 O  OD2 A ASP   B 105 ? 0.4434 0.4358 0.5096 0.0105  0.1815  -0.0257 105 ASP   B OD2 
5296 O  OD2 B ASP   B 105 ? 0.3806 0.3547 0.3685 -0.0250 0.0971  0.0399  105 ASP   B OD2 
5305 N  N   A ILE   B 106 ? 0.3721 0.3125 0.2947 -0.0269 0.1528  0.0184  106 ILE   B N   
5306 N  N   B ILE   B 106 ? 0.3716 0.3430 0.3223 -0.0101 0.0489  0.0062  106 ILE   B N   
5307 C  CA  A ILE   B 106 ? 0.3502 0.2939 0.3014 -0.0393 0.1583  0.0153  106 ILE   B CA  
5308 C  CA  B ILE   B 106 ? 0.3626 0.3393 0.3253 -0.0087 0.0471  0.0010  106 ILE   B CA  
5309 C  C   A ILE   B 106 ? 0.3059 0.2860 0.2717 -0.0413 0.1541  -0.0173 106 ILE   B C   
5310 C  C   B ILE   B 106 ? 0.3461 0.3358 0.3223 -0.0049 0.0452  -0.0071 106 ILE   B C   
5311 O  O   A ILE   B 106 ? 0.2843 0.2625 0.2619 -0.0540 0.1319  -0.0404 106 ILE   B O   
5312 O  O   B ILE   B 106 ? 0.3450 0.3323 0.3209 -0.0053 0.0387  -0.0075 106 ILE   B O   
5313 C  CB  A ILE   B 106 ? 0.3757 0.2916 0.3239 -0.0438 0.1616  0.0381  106 ILE   B CB  
5314 C  CB  B ILE   B 106 ? 0.3713 0.3416 0.3303 -0.0108 0.0480  0.0033  106 ILE   B CB  
5315 C  CG1 A ILE   B 106 ? 0.3863 0.2978 0.3304 -0.0250 0.1515  0.0268  106 ILE   B CG1 
5316 C  CG1 B ILE   B 106 ? 0.3743 0.3432 0.3338 -0.0078 0.0459  0.0046  106 ILE   B CG1 
5317 C  CG2 A ILE   B 106 ? 0.3876 0.2967 0.3678 -0.0437 0.1592  0.0417  106 ILE   B CG2 
5318 C  CG2 B ILE   B 106 ? 0.3748 0.3439 0.3402 -0.0110 0.0491  0.0024  106 ILE   B CG2 
5319 C  CD1 A ILE   B 106 ? 0.3933 0.3043 0.3299 -0.0136 0.1411  0.0319  106 ILE   B CD1 
5320 C  CD1 B ILE   B 106 ? 0.3764 0.3446 0.3361 -0.0051 0.0444  0.0078  106 ILE   B CD1 
5343 N  N   A GLN   B 107 ? 0.2985 0.3126 0.3161 -0.0357 0.1393  -0.0139 107 GLN   B N   
5344 N  N   B GLN   B 107 ? 0.3323 0.3378 0.3343 -0.0037 0.0476  -0.0117 107 GLN   B N   
5345 C  CA  A GLN   B 107 ? 0.2898 0.3285 0.3421 -0.0280 0.1309  -0.0099 107 GLN   B CA  
5346 C  CA  B GLN   B 107 ? 0.3197 0.3366 0.3468 -0.0010 0.0533  -0.0119 107 GLN   B CA  
5347 C  C   A GLN   B 107 ? 0.2712 0.3092 0.3196 -0.0059 0.0826  -0.0155 107 GLN   B C   
5348 C  C   B GLN   B 107 ? 0.2894 0.3155 0.3081 0.0061  0.0584  -0.0123 107 GLN   B C   
5349 O  O   A GLN   B 107 ? 0.2542 0.3158 0.3701 0.0030  0.0546  -0.0326 107 GLN   B O   
5350 O  O   B GLN   B 107 ? 0.2860 0.3190 0.3259 0.0072  0.0493  -0.0197 107 GLN   B O   
5351 C  CB  A GLN   B 107 ? 0.3275 0.3724 0.4241 -0.0302 0.1228  -0.0119 107 GLN   B CB  
5352 C  CB  B GLN   B 107 ? 0.3421 0.3579 0.4011 -0.0030 0.0482  -0.0125 107 GLN   B CB  
5353 C  CG  A GLN   B 107 ? 0.3665 0.4161 0.5076 -0.0229 0.0954  -0.0118 107 GLN   B CG  
5354 C  CG  B GLN   B 107 ? 0.3623 0.3779 0.4545 -0.0019 0.0387  -0.0105 107 GLN   B CG  
5355 C  CD  A GLN   B 107 ? 0.3905 0.4401 0.5710 -0.0220 0.0719  -0.0107 107 GLN   B CD  
5356 C  CD  B GLN   B 107 ? 0.3768 0.3916 0.4961 -0.0025 0.0298  -0.0084 107 GLN   B CD  
5357 O  OE1 A GLN   B 107 ? 0.4038 0.4540 0.5979 -0.0147 0.0719  -0.0145 107 GLN   B OE1 
5358 O  OE1 B GLN   B 107 ? 0.3834 0.3993 0.5121 -0.0008 0.0302  -0.0085 107 GLN   B OE1 
5359 N  NE2 A GLN   B 107 ? 0.4017 0.4483 0.5948 -0.0208 0.0559  -0.0027 107 GLN   B NE2 
5360 N  NE2 B GLN   B 107 ? 0.3822 0.3937 0.5121 -0.0016 0.0254  -0.0049 107 GLN   B NE2 
5377 N  N   . LEU   B 108 ? 0.2572 0.2916 0.2591 0.0146  0.0769  -0.0039 108 LEU   B N   
5378 C  CA  . LEU   B 108 ? 0.2524 0.2618 0.2236 0.0301  0.0483  0.0169  108 LEU   B CA  
5379 C  C   . LEU   B 108 ? 0.2097 0.2255 0.2147 0.0160  0.0191  0.0440  108 LEU   B C   
5380 O  O   . LEU   B 108 ? 0.1986 0.2126 0.2163 0.0200  0.0267  0.0465  108 LEU   B O   
5381 C  CB  . LEU   B 108 ? 0.2674 0.2628 0.2145 0.0203  0.0642  0.0329  108 LEU   B CB  
5382 C  CG  . LEU   B 108 ? 0.2938 0.2938 0.2267 0.0244  0.0550  -0.0001 108 LEU   B CG  
5383 C  CD1 . LEU   B 108 ? 0.3105 0.3065 0.2079 0.0201  0.0548  0.0003  108 LEU   B CD1 
5384 C  CD2 . LEU   B 108 ? 0.3133 0.3110 0.2581 0.0324  0.0336  -0.0163 108 LEU   B CD2 
5397 N  N   . LEU   B 109 ? 0.1989 0.2151 0.2028 0.0130  0.0351  0.0209  109 LEU   B N   
5398 C  CA  . LEU   B 109 ? 0.1726 0.1910 0.2095 -0.0071 0.0306  0.0301  109 LEU   B CA  
5399 C  C   . LEU   B 109 ? 0.1659 0.1631 0.2000 -0.0004 0.0393  0.0234  109 LEU   B C   
5400 O  O   . LEU   B 109 ? 0.1573 0.1746 0.2071 0.0088  0.0263  0.0302  109 LEU   B O   
5401 C  CB  . LEU   B 109 ? 0.1916 0.1689 0.2283 0.0000  0.0164  0.0282  109 LEU   B CB  
5402 C  CG  . LEU   B 109 ? 0.1949 0.1535 0.2207 0.0008  0.0175  0.0174  109 LEU   B CG  
5403 C  CD1 . LEU   B 109 ? 0.1901 0.1719 0.2142 0.0028  0.0262  0.0168  109 LEU   B CD1 
5404 C  CD2 . LEU   B 109 ? 0.2251 0.1250 0.2394 -0.0048 0.0185  0.0263  109 LEU   B CD2 
5416 N  N   . LYS   B 110 ? 0.1631 0.1604 0.1901 -0.0070 0.0266  0.0303  110 LYS   B N   
5417 C  CA  . LYS   B 110 ? 0.1456 0.1576 0.2105 0.0075  0.0092  0.0145  110 LYS   B CA  
5418 C  C   . LYS   B 110 ? 0.1479 0.1506 0.1972 0.0030  0.0214  0.0095  110 LYS   B C   
5419 O  O   . LYS   B 110 ? 0.1593 0.1561 0.1961 -0.0006 0.0133  0.0056  110 LYS   B O   
5420 C  CB  . LYS   B 110 ? 0.1518 0.1660 0.2347 0.0095  0.0188  0.0116  110 LYS   B CB  
5421 C  CG  . LYS   B 110 ? 0.1580 0.1719 0.2424 -0.0014 0.0011  0.0118  110 LYS   B CG  
5422 C  CD  . LYS   B 110 ? 0.1669 0.1578 0.2553 -0.0091 0.0022  0.0206  110 LYS   B CD  
5423 C  CE  . LYS   B 110 ? 0.1703 0.1679 0.2803 -0.0065 0.0151  0.0004  110 LYS   B CE  
5424 N  NZ  . LYS   B 110 ? 0.1747 0.1752 0.2588 -0.0072 0.0072  -0.0001 110 LYS   B NZ  
5438 N  N   . SER   B 111 ? 0.1708 0.1587 0.2164 0.0012  0.0305  0.0252  111 SER   B N   
5439 C  CA  . SER   B 111 ? 0.1740 0.1686 0.1893 0.0045  0.0168  0.0229  111 SER   B CA  
5440 C  C   . SER   B 111 ? 0.1561 0.1689 0.2056 -0.0100 0.0100  0.0175  111 SER   B C   
5441 O  O   . SER   B 111 ? 0.1604 0.1596 0.2110 0.0018  0.0080  0.0061  111 SER   B O   
5442 C  CB  . SER   B 111 ? 0.1836 0.1786 0.2050 0.0015  0.0429  0.0328  111 SER   B CB  
5443 O  OG  . SER   B 111 ? 0.2143 0.2145 0.2386 0.0120  0.0511  0.0318  111 SER   B OG  
5449 N  N   . ALA   B 112 ? 0.1462 0.1782 0.2074 0.0099  0.0179  0.0146  112 ALA   B N   
5450 C  CA  . ALA   B 112 ? 0.1496 0.1688 0.1865 0.0070  0.0041  0.0010  112 ALA   B CA  
5451 C  C   . ALA   B 112 ? 0.1476 0.1493 0.1887 0.0048  0.0024  -0.0071 112 ALA   B C   
5452 O  O   . ALA   B 112 ? 0.1345 0.1616 0.2013 -0.0044 0.0042  -0.0058 112 ALA   B O   
5453 C  CB  . ALA   B 112 ? 0.1575 0.1725 0.2179 0.0152  0.0074  0.0126  112 ALA   B CB  
5459 N  N   . TYR   B 113 ? 0.1429 0.1433 0.1935 0.0025  0.0048  0.0057  113 TYR   B N   
5460 C  CA  . TYR   B 113 ? 0.1386 0.1593 0.1753 -0.0056 -0.0001 0.0086  113 TYR   B CA  
5461 C  C   . TYR   B 113 ? 0.1488 0.1591 0.1631 -0.0020 0.0086  0.0046  113 TYR   B C   
5462 O  O   . TYR   B 113 ? 0.1587 0.1513 0.1696 0.0006  0.0002  -0.0009 113 TYR   B O   
5463 C  CB  . TYR   B 113 ? 0.1530 0.1604 0.1898 0.0039  0.0240  0.0197  113 TYR   B CB  
5464 C  CG  . TYR   B 113 ? 0.1608 0.1755 0.1908 -0.0086 0.0064  0.0144  113 TYR   B CG  
5465 C  CD1 . TYR   B 113 ? 0.1559 0.1813 0.2029 -0.0036 0.0177  0.0002  113 TYR   B CD1 
5466 C  CD2 . TYR   B 113 ? 0.1533 0.1880 0.1942 -0.0044 0.0108  0.0163  113 TYR   B CD2 
5467 C  CE1 . TYR   B 113 ? 0.1532 0.1880 0.2026 -0.0080 0.0265  -0.0057 113 TYR   B CE1 
5468 C  CE2 . TYR   B 113 ? 0.1626 0.1816 0.2131 0.0025  0.0017  0.0001  113 TYR   B CE2 
5469 C  CZ  . TYR   B 113 ? 0.1494 0.1833 0.2163 0.0050  0.0086  0.0008  113 TYR   B CZ  
5470 O  OH  . TYR   B 113 ? 0.1572 0.1658 0.2261 0.0074  0.0130  -0.0030 113 TYR   B OH  
5480 N  N   . GLU   B 114 ? 0.1583 0.1278 0.1946 -0.0019 0.0173  0.0117  114 GLU   B N   
5481 C  CA  . GLU   B 114 ? 0.1661 0.1193 0.1810 0.0015  0.0059  0.0042  114 GLU   B CA  
5482 C  C   . GLU   B 114 ? 0.1765 0.1465 0.1536 0.0195  0.0044  0.0062  114 GLU   B C   
5483 O  O   . GLU   B 114 ? 0.1643 0.1505 0.1797 0.0098  -0.0019 0.0179  114 GLU   B O   
5484 C  CB  . GLU   B 114 ? 0.1527 0.1340 0.2155 -0.0018 0.0051  0.0046  114 GLU   B CB  
5485 C  CG  . GLU   B 114 ? 0.1634 0.1313 0.2140 -0.0086 0.0041  0.0012  114 GLU   B CG  
5486 C  CD  . GLU   B 114 ? 0.1668 0.1433 0.2049 -0.0072 0.0097  -0.0176 114 GLU   B CD  
5487 O  OE1 . GLU   B 114 ? 0.1497 0.1616 0.2041 -0.0051 0.0237  0.0118  114 GLU   B OE1 
5488 O  OE2 . GLU   B 114 ? 0.1634 0.1675 0.2027 -0.0271 -0.0020 0.0074  114 GLU   B OE2 
5495 N  N   . ASN   B 115 ? 0.1667 0.1467 0.1595 0.0014  0.0005  -0.0022 115 ASN   B N   
5496 C  CA  . ASN   B 115 ? 0.1612 0.1463 0.1649 -0.0037 0.0070  -0.0082 115 ASN   B CA  
5497 C  C   . ASN   B 115 ? 0.1389 0.1560 0.1701 -0.0151 -0.0016 -0.0126 115 ASN   B C   
5498 O  O   . ASN   B 115 ? 0.1562 0.1501 0.1702 -0.0132 -0.0051 0.0061  115 ASN   B O   
5499 C  CB  . ASN   B 115 ? 0.1728 0.1569 0.1720 0.0026  -0.0018 0.0066  115 ASN   B CB  
5500 C  CG  . ASN   B 115 ? 0.1661 0.1714 0.1718 0.0018  -0.0052 -0.0008 115 ASN   B CG  
5501 O  OD1 . ASN   B 115 ? 0.2184 0.1877 0.1780 0.0007  0.0206  -0.0097 115 ASN   B OD1 
5502 N  ND2 . ASN   B 115 ? 0.1466 0.1700 0.1850 -0.0082 0.0028  0.0118  115 ASN   B ND2 
5509 N  N   . PHE   B 116 ? 0.1446 0.1572 0.1600 -0.0026 0.0005  -0.0176 116 PHE   B N   
5510 C  CA  . PHE   B 116 ? 0.1374 0.1671 0.1658 -0.0079 -0.0168 -0.0026 116 PHE   B CA  
5511 C  C   . PHE   B 116 ? 0.1383 0.1397 0.1585 -0.0001 -0.0064 -0.0044 116 PHE   B C   
5512 O  O   . PHE   B 116 ? 0.1526 0.1629 0.1638 0.0001  -0.0047 -0.0031 116 PHE   B O   
5513 C  CB  . PHE   B 116 ? 0.1388 0.1598 0.1474 -0.0134 -0.0147 0.0043  116 PHE   B CB  
5514 C  CG  . PHE   B 116 ? 0.1472 0.1837 0.1336 -0.0014 -0.0018 0.0035  116 PHE   B CG  
5515 C  CD1 . PHE   B 116 ? 0.1459 0.1717 0.1587 0.0036  0.0047  0.0036  116 PHE   B CD1 
5516 C  CD2 . PHE   B 116 ? 0.1494 0.1883 0.1461 0.0020  -0.0073 -0.0148 116 PHE   B CD2 
5517 C  CE1 . PHE   B 116 ? 0.1491 0.1709 0.1817 -0.0029 -0.0192 -0.0057 116 PHE   B CE1 
5518 C  CE2 . PHE   B 116 ? 0.1402 0.1699 0.1717 -0.0129 -0.0085 0.0125  116 PHE   B CE2 
5519 C  CZ  . PHE   B 116 ? 0.1377 0.1747 0.1687 -0.0000 -0.0069 0.0062  116 PHE   B CZ  
5529 N  N   . ASN   B 117 ? 0.1474 0.1491 0.1585 -0.0031 -0.0078 0.0097  117 ASN   B N   
5530 C  CA  . ASN   B 117 ? 0.1507 0.1413 0.1669 -0.0033 -0.0080 -0.0089 117 ASN   B CA  
5531 C  C   . ASN   B 117 ? 0.1599 0.1350 0.1670 -0.0084 -0.0028 -0.0041 117 ASN   B C   
5532 O  O   . ASN   B 117 ? 0.1699 0.1455 0.2036 -0.0060 -0.0322 0.0030  117 ASN   B O   
5533 C  CB  . ASN   B 117 ? 0.1614 0.1495 0.1858 0.0053  -0.0030 0.0003  117 ASN   B CB  
5534 C  CG  . ASN   B 117 ? 0.1430 0.1361 0.2062 0.0002  -0.0159 0.0035  117 ASN   B CG  
5535 O  OD1 . ASN   B 117 ? 0.1723 0.1389 0.2163 -0.0100 -0.0032 -0.0110 117 ASN   B OD1 
5536 N  ND2 . ASN   B 117 ? 0.1668 0.1463 0.2000 -0.0049 -0.0064 -0.0018 117 ASN   B ND2 
5543 N  N   . GLN   B 118 ? 0.1699 0.1409 0.1660 -0.0008 -0.0189 -0.0088 118 GLN   B N   
5544 C  CA  . GLN   B 118 ? 0.1664 0.1532 0.1732 0.0089  -0.0112 -0.0058 118 GLN   B CA  
5545 C  C   . GLN   B 118 ? 0.1679 0.1661 0.1966 -0.0034 -0.0108 -0.0107 118 GLN   B C   
5546 O  O   . GLN   B 118 ? 0.1747 0.1581 0.2282 -0.0133 -0.0015 0.0013  118 GLN   B O   
5547 C  CB  . GLN   B 118 ? 0.1686 0.1498 0.2067 0.0034  -0.0127 -0.0101 118 GLN   B CB  
5548 C  CG  . GLN   B 118 ? 0.1823 0.1647 0.1995 0.0062  -0.0076 -0.0178 118 GLN   B CG  
5549 C  CD  . GLN   B 118 ? 0.1836 0.1539 0.1901 -0.0000 -0.0078 -0.0056 118 GLN   B CD  
5550 O  OE1 . GLN   B 118 ? 0.1840 0.1529 0.2290 -0.0014 0.0076  0.0106  118 GLN   B OE1 
5551 N  NE2 . GLN   B 118 ? 0.1912 0.1615 0.2082 0.0004  -0.0173 0.0053  118 GLN   B NE2 
5560 N  N   . HIS   B 119 ? 0.1707 0.1528 0.1657 -0.0079 -0.0090 -0.0020 119 HIS   B N   
5561 C  CA  . HIS   B 119 ? 0.1875 0.1590 0.1492 -0.0005 -0.0138 -0.0004 119 HIS   B CA  
5562 C  C   . HIS   B 119 ? 0.1708 0.1463 0.1703 0.0056  -0.0321 0.0019  119 HIS   B C   
5563 O  O   . HIS   B 119 ? 0.1885 0.1535 0.1873 -0.0259 -0.0135 0.0028  119 HIS   B O   
5564 C  CB  . HIS   B 119 ? 0.1963 0.1611 0.1560 -0.0040 -0.0216 -0.0079 119 HIS   B CB  
5565 C  CG  . HIS   B 119 ? 0.1951 0.1750 0.1743 0.0124  -0.0498 -0.0198 119 HIS   B CG  
5566 N  ND1 . HIS   B 119 ? 0.2217 0.1911 0.2362 0.0038  -0.0583 -0.0428 119 HIS   B ND1 
5567 C  CD2 . HIS   B 119 ? 0.2163 0.1950 0.2029 0.0479  -0.0610 -0.0306 119 HIS   B CD2 
5568 C  CE1 . HIS   B 119 ? 0.2429 0.2101 0.2505 0.0193  -0.0717 -0.0568 119 HIS   B CE1 
5569 N  NE2 . HIS   B 119 ? 0.2460 0.2249 0.2336 0.0360  -0.0615 -0.0497 119 HIS   B NE2 
5577 N  N   . GLU   B 120 ? 0.1981 0.1488 0.1720 -0.0062 -0.0294 0.0093  120 GLU   B N   
5578 C  CA  . GLU   B 120 ? 0.2249 0.1778 0.1575 -0.0059 -0.0445 0.0172  120 GLU   B CA  
5579 C  C   . GLU   B 120 ? 0.2088 0.1610 0.1636 -0.0065 -0.0193 0.0110  120 GLU   B C   
5580 O  O   . GLU   B 120 ? 0.2010 0.1654 0.1610 -0.0128 -0.0223 0.0124  120 GLU   B O   
5581 C  CB  . GLU   B 120 ? 0.3002 0.2208 0.2296 0.0223  -0.0720 0.0287  120 GLU   B CB  
5582 C  CG  . GLU   B 120 ? 0.3638 0.2827 0.3376 0.0303  -0.0931 0.0490  120 GLU   B CG  
5583 C  CD  . GLU   B 120 ? 0.4117 0.3556 0.4584 0.0201  -0.1004 0.0600  120 GLU   B CD  
5584 O  OE1 . GLU   B 120 ? 0.4396 0.3845 0.5099 0.0033  -0.0912 0.0758  120 GLU   B OE1 
5585 O  OE2 . GLU   B 120 ? 0.4397 0.3909 0.5363 0.0161  -0.1023 0.0495  120 GLU   B OE2 
5592 N  N   . VAL   B 121 ? 0.1906 0.1616 0.1512 -0.0132 -0.0104 0.0115  121 VAL   B N   
5593 C  CA  . VAL   B 121 ? 0.1760 0.1789 0.1440 -0.0127 -0.0184 -0.0003 121 VAL   B CA  
5594 C  C   . VAL   B 121 ? 0.1798 0.1622 0.1526 -0.0289 -0.0072 0.0192  121 VAL   B C   
5595 O  O   . VAL   B 121 ? 0.1820 0.1536 0.1743 -0.0326 -0.0244 0.0086  121 VAL   B O   
5596 C  CB  . VAL   B 121 ? 0.1960 0.2072 0.1707 0.0067  -0.0263 0.0263  121 VAL   B CB  
5597 C  CG1 . VAL   B 121 ? 0.2112 0.2217 0.2266 0.0057  0.0024  0.0173  121 VAL   B CG1 
5598 C  CG2 . VAL   B 121 ? 0.2236 0.2395 0.1773 0.0128  -0.0100 0.0139  121 VAL   B CG2 
5608 N  N   . LEU   B 122 ? 0.1755 0.1569 0.1482 -0.0186 -0.0158 0.0193  122 LEU   B N   
5609 C  CA  . LEU   B 122 ? 0.1467 0.1748 0.1339 -0.0158 -0.0214 0.0134  122 LEU   B CA  
5610 C  C   . LEU   B 122 ? 0.1653 0.1528 0.1392 -0.0149 -0.0166 0.0145  122 LEU   B C   
5611 O  O   . LEU   B 122 ? 0.1740 0.1527 0.1838 -0.0229 -0.0184 -0.0122 122 LEU   B O   
5612 C  CB  . LEU   B 122 ? 0.1757 0.1947 0.1756 0.0073  -0.0501 0.0040  122 LEU   B CB  
5613 C  CG  . LEU   B 122 ? 0.1758 0.1966 0.1826 -0.0075 -0.0247 -0.0064 122 LEU   B CG  
5614 C  CD1 . LEU   B 122 ? 0.1877 0.2206 0.1910 -0.0166 -0.0256 0.0153  122 LEU   B CD1 
5615 C  CD2 . LEU   B 122 ? 0.1974 0.1863 0.1525 -0.0051 -0.0164 -0.0105 122 LEU   B CD2 
5627 N  N   . LEU   B 123 ? 0.1643 0.1425 0.1489 -0.0070 -0.0110 0.0193  123 LEU   B N   
5628 C  CA  . LEU   B 123 ? 0.1676 0.1570 0.1470 -0.0188 -0.0218 0.0094  123 LEU   B CA  
5629 C  C   . LEU   B 123 ? 0.1618 0.1318 0.1579 -0.0170 -0.0197 -0.0014 123 LEU   B C   
5630 O  O   . LEU   B 123 ? 0.1761 0.1338 0.1511 -0.0202 -0.0069 -0.0104 123 LEU   B O   
5631 C  CB  . LEU   B 123 ? 0.1655 0.1636 0.1590 -0.0198 -0.0162 0.0050  123 LEU   B CB  
5632 C  CG  . LEU   B 123 ? 0.1598 0.1568 0.1801 -0.0151 -0.0043 0.0123  123 LEU   B CG  
5633 C  CD1 . LEU   B 123 ? 0.1733 0.1661 0.1970 -0.0261 -0.0001 -0.0052 123 LEU   B CD1 
5634 C  CD2 . LEU   B 123 ? 0.1696 0.1678 0.1977 -0.0155 -0.0066 0.0222  123 LEU   B CD2 
5646 N  N   . ALA   B 124 ? 0.1698 0.1390 0.1444 -0.0157 -0.0047 -0.0041 124 ALA   B N   
5647 C  CA  . ALA   B 124 ? 0.1611 0.1362 0.1527 -0.0148 -0.0117 -0.0009 124 ALA   B CA  
5648 C  C   . ALA   B 124 ? 0.1572 0.1340 0.1464 -0.0257 -0.0080 -0.0044 124 ALA   B C   
5649 O  O   . ALA   B 124 ? 0.1562 0.1385 0.1656 -0.0111 -0.0084 -0.0078 124 ALA   B O   
5650 C  CB  . ALA   B 124 ? 0.1669 0.1490 0.1613 -0.0021 0.0134  -0.0006 124 ALA   B CB  
5656 N  N   . PRO   B 125 ? 0.1667 0.1375 0.1459 -0.0179 -0.0189 0.0221  125 PRO   B N   
5657 C  CA  . PRO   B 125 ? 0.1831 0.1629 0.1527 -0.0211 -0.0228 0.0289  125 PRO   B CA  
5658 C  C   . PRO   B 125 ? 0.1581 0.1687 0.1684 -0.0229 -0.0114 0.0136  125 PRO   B C   
5659 O  O   . PRO   B 125 ? 0.1473 0.1688 0.1994 -0.0101 -0.0117 0.0108  125 PRO   B O   
5660 C  CB  . PRO   B 125 ? 0.1809 0.1807 0.1764 -0.0220 -0.0286 0.0229  125 PRO   B CB  
5661 C  CG  . PRO   B 125 ? 0.1902 0.1784 0.1618 -0.0376 -0.0150 0.0167  125 PRO   B CG  
5662 C  CD  . PRO   B 125 ? 0.1761 0.1562 0.1303 -0.0350 -0.0118 0.0052  125 PRO   B CD  
5670 N  N   . LEU   B 126 ? 0.1680 0.1653 0.1883 -0.0317 0.0068  0.0111  126 LEU   B N   
5671 C  CA  . LEU   B 126 ? 0.1819 0.1618 0.1763 -0.0184 0.0211  0.0201  126 LEU   B CA  
5672 C  C   . LEU   B 126 ? 0.1685 0.1582 0.1873 0.0035  0.0139  0.0172  126 LEU   B C   
5673 O  O   . LEU   B 126 ? 0.1914 0.1893 0.2153 0.0252  -0.0068 -0.0056 126 LEU   B O   
5674 C  CB  . LEU   B 126 ? 0.2023 0.1529 0.2204 -0.0168 0.0267  0.0157  126 LEU   B CB  
5675 C  CG  . LEU   B 126 ? 0.2294 0.1460 0.2330 -0.0186 0.0188  -0.0300 126 LEU   B CG  
5676 C  CD1 . LEU   B 126 ? 0.2362 0.1593 0.2928 -0.0235 0.0123  -0.0467 126 LEU   B CD1 
5677 C  CD2 . LEU   B 126 ? 0.2274 0.1738 0.2471 -0.0275 0.0051  -0.0297 126 LEU   B CD2 
5689 N  N   . LEU   B 127 ? 0.1733 0.1556 0.2020 0.0048  0.0269  0.0047  127 LEU   B N   
5690 C  CA  . LEU   B 127 ? 0.1678 0.1631 0.1991 -0.0046 0.0232  0.0236  127 LEU   B CA  
5691 C  C   . LEU   B 127 ? 0.1612 0.1550 0.2203 -0.0053 0.0207  0.0229  127 LEU   B C   
5692 O  O   . LEU   B 127 ? 0.1775 0.1431 0.2156 -0.0055 0.0079  0.0089  127 LEU   B O   
5693 C  CB  . LEU   B 127 ? 0.1778 0.1785 0.2196 -0.0002 0.0121  0.0127  127 LEU   B CB  
5694 C  CG  . LEU   B 127 ? 0.1827 0.1706 0.2017 -0.0107 0.0227  0.0186  127 LEU   B CG  
5695 C  CD1 . LEU   B 127 ? 0.1839 0.1782 0.2236 -0.0051 0.0257  -0.0011 127 LEU   B CD1 
5696 C  CD2 . LEU   B 127 ? 0.1910 0.1775 0.2137 -0.0117 0.0124  0.0328  127 LEU   B CD2 
5708 N  N   . SER   B 128 ? 0.1706 0.1741 0.1985 0.0114  0.0084  0.0208  128 SER   B N   
5709 C  CA  . SER   B 128 ? 0.1896 0.1886 0.1819 0.0224  -0.0041 0.0182  128 SER   B CA  
5710 C  C   . SER   B 128 ? 0.1993 0.1730 0.2065 0.0166  -0.0099 0.0266  128 SER   B C   
5711 O  O   . SER   B 128 ? 0.2109 0.1634 0.2594 0.0063  -0.0152 0.0397  128 SER   B O   
5712 C  CB  . SER   B 128 ? 0.2002 0.2008 0.1874 0.0157  0.0033  0.0239  128 SER   B CB  
5713 O  OG  . SER   B 128 ? 0.2063 0.2017 0.1919 0.0056  0.0138  0.0284  128 SER   B OG  
5719 N  N   . ALA   B 129 ? 0.2061 0.1798 0.2447 0.0405  -0.0114 -0.0051 129 ALA   B N   
5720 C  CA  . ALA   B 129 ? 0.2215 0.1879 0.2565 0.0359  -0.0127 -0.0190 129 ALA   B CA  
5721 C  C   . ALA   B 129 ? 0.2076 0.1774 0.2394 0.0347  -0.0005 -0.0147 129 ALA   B C   
5722 O  O   . ALA   B 129 ? 0.1996 0.1803 0.2351 0.0257  -0.0027 0.0118  129 ALA   B O   
5723 C  CB  . ALA   B 129 ? 0.2447 0.2156 0.2979 0.0369  -0.0002 -0.0340 129 ALA   B CB  
5729 N  N   . GLY   B 130 ? 0.2133 0.1836 0.2436 0.0410  -0.0022 -0.0093 130 GLY   B N   
5730 C  CA  . GLY   B 130 ? 0.2078 0.1907 0.2671 0.0323  0.0288  -0.0090 130 GLY   B CA  
5731 C  C   . GLY   B 130 ? 0.2172 0.1954 0.2692 0.0242  0.0168  0.0012  130 GLY   B C   
5732 O  O   . GLY   B 130 ? 0.2209 0.2029 0.2748 0.0251  0.0164  0.0048  130 GLY   B O   
5736 N  N   . ILE   B 131 ? 0.2143 0.1944 0.2769 0.0425  0.0157  -0.0076 131 ILE   B N   
5737 C  CA  . ILE   B 131 ? 0.2328 0.2167 0.2697 0.0393  0.0044  0.0132  131 ILE   B CA  
5738 C  C   . ILE   B 131 ? 0.2383 0.2062 0.2274 0.0215  0.0068  0.0217  131 ILE   B C   
5739 O  O   . ILE   B 131 ? 0.2633 0.2312 0.2444 0.0319  -0.0130 0.0378  131 ILE   B O   
5740 C  CB  . ILE   B 131 ? 0.2339 0.2389 0.3065 0.0399  -0.0009 0.0293  131 ILE   B CB  
5741 C  CG1 . ILE   B 131 ? 0.2436 0.2594 0.3079 0.0084  0.0093  0.0289  131 ILE   B CG1 
5742 C  CG2 . ILE   B 131 ? 0.2287 0.2620 0.3442 0.0479  -0.0081 0.0267  131 ILE   B CG2 
5743 C  CD1 . ILE   B 131 ? 0.2669 0.2743 0.3164 -0.0083 0.0174  0.0380  131 ILE   B CD1 
5755 N  N   . PHE   B 132 ? 0.2238 0.1838 0.2192 0.0185  0.0211  0.0220  132 PHE   B N   
5756 C  CA  . PHE   B 132 ? 0.2212 0.1952 0.2215 0.0082  0.0327  0.0212  132 PHE   B CA  
5757 C  C   . PHE   B 132 ? 0.2491 0.2030 0.2319 0.0096  0.0346  0.0182  132 PHE   B C   
5758 O  O   . PHE   B 132 ? 0.2671 0.2248 0.2799 -0.0030 0.0516  0.0307  132 PHE   B O   
5759 C  CB  . PHE   B 132 ? 0.1962 0.2029 0.2066 0.0078  0.0305  0.0186  132 PHE   B CB  
5760 C  CG  . PHE   B 132 ? 0.2011 0.2145 0.2071 0.0107  0.0296  0.0051  132 PHE   B CG  
5761 C  CD1 . PHE   B 132 ? 0.2164 0.2009 0.2447 0.0006  0.0274  0.0045  132 PHE   B CD1 
5762 C  CD2 . PHE   B 132 ? 0.1985 0.2116 0.1775 0.0237  0.0201  0.0188  132 PHE   B CD2 
5763 C  CE1 . PHE   B 132 ? 0.2180 0.2084 0.2569 -0.0031 0.0223  0.0096  132 PHE   B CE1 
5764 C  CE2 . PHE   B 132 ? 0.2182 0.2145 0.1920 0.0301  0.0056  0.0135  132 PHE   B CE2 
5765 C  CZ  . PHE   B 132 ? 0.2272 0.2205 0.2426 0.0179  0.0007  0.0115  132 PHE   B CZ  
5775 N  N   . GLY   B 133 ? 0.2401 0.1879 0.2278 0.0023  0.0021  0.0395  133 GLY   B N   
5776 C  CA  . GLY   B 133 ? 0.2554 0.2003 0.2359 -0.0164 -0.0158 0.0529  133 GLY   B CA  
5777 C  C   . GLY   B 133 ? 0.2633 0.2087 0.2176 -0.0279 0.0030  0.0521  133 GLY   B C   
5778 O  O   . GLY   B 133 ? 0.2901 0.2176 0.2938 -0.0373 0.0130  0.0574  133 GLY   B O   
5782 N  N   . ALA   B 134 ? 0.2454 0.2152 0.2039 -0.0277 -0.0020 0.0189  134 ALA   B N   
5783 C  CA  . ALA   B 134 ? 0.2483 0.2119 0.2260 -0.0231 0.0195  0.0154  134 ALA   B CA  
5784 C  C   . ALA   B 134 ? 0.2541 0.2014 0.2278 -0.0110 0.0138  0.0346  134 ALA   B C   
5785 O  O   . ALA   B 134 ? 0.2640 0.2209 0.2403 0.0044  0.0117  0.0218  134 ALA   B O   
5786 C  CB  . ALA   B 134 ? 0.2391 0.2102 0.2586 -0.0091 0.0281  0.0050  134 ALA   B CB  
5792 N  N   . ASP   B 135 ? 0.2646 0.1883 0.2374 -0.0167 0.0072  0.0314  135 ASP   B N   
5793 C  CA  . ASP   B 135 ? 0.2781 0.1744 0.2777 -0.0155 0.0005  0.0334  135 ASP   B CA  
5794 C  C   . ASP   B 135 ? 0.2440 0.1749 0.2566 -0.0087 0.0073  0.0220  135 ASP   B C   
5795 O  O   . ASP   B 135 ? 0.2324 0.1786 0.2536 -0.0017 0.0092  0.0100  135 ASP   B O   
5796 C  CB  . ASP   B 135 ? 0.3182 0.1877 0.3115 -0.0462 0.0097  0.0365  135 ASP   B CB  
5797 C  CG  . ASP   B 135 ? 0.3484 0.1909 0.3562 -0.0661 0.0143  0.0307  135 ASP   B CG  
5798 O  OD1 . ASP   B 135 ? 0.3594 0.1740 0.3439 -0.0404 -0.0035 0.0364  135 ASP   B OD1 
5799 O  OD2 . ASP   B 135 ? 0.3714 0.2277 0.4222 -0.0786 0.0151  0.0114  135 ASP   B OD2 
5804 N  N   . PRO   B 136 ? 0.2410 0.1905 0.2582 0.0118  -0.0151 0.0281  136 PRO   B N   
5805 C  CA  . PRO   B 136 ? 0.2208 0.1827 0.2644 0.0014  -0.0030 0.0098  136 PRO   B CA  
5806 C  C   . PRO   B 136 ? 0.2025 0.1659 0.2611 0.0103  0.0010  0.0098  136 PRO   B C   
5807 O  O   . PRO   B 136 ? 0.1892 0.1613 0.2558 0.0075  0.0024  0.0216  136 PRO   B O   
5808 C  CB  . PRO   B 136 ? 0.2288 0.1974 0.2742 0.0243  -0.0277 0.0078  136 PRO   B CB  
5809 C  CG  . PRO   B 136 ? 0.2544 0.2164 0.3051 0.0162  -0.0178 0.0034  136 PRO   B CG  
5810 C  CD  . PRO   B 136 ? 0.2529 0.1957 0.2684 0.0265  -0.0063 0.0176  136 PRO   B CD  
5818 N  N   . ILE   B 137 ? 0.1924 0.1636 0.2741 0.0139  0.0009  -0.0074 137 ILE   B N   
5819 C  CA  . ILE   B 137 ? 0.2098 0.1689 0.2695 -0.0112 -0.0035 -0.0016 137 ILE   B CA  
5820 C  C   . ILE   B 137 ? 0.1921 0.1780 0.2571 -0.0175 0.0072  0.0132  137 ILE   B C   
5821 O  O   . ILE   B 137 ? 0.1989 0.1702 0.2502 -0.0214 -0.0029 0.0098  137 ILE   B O   
5822 C  CB  . ILE   B 137 ? 0.2475 0.1838 0.3127 -0.0145 -0.0074 -0.0029 137 ILE   B CB  
5823 C  CG1 . ILE   B 137 ? 0.2801 0.1915 0.3725 -0.0159 -0.0151 -0.0131 137 ILE   B CG1 
5824 C  CG2 . ILE   B 137 ? 0.2607 0.1816 0.3361 -0.0345 -0.0054 0.0035  137 ILE   B CG2 
5825 C  CD1 . ILE   B 137 ? 0.3075 0.2245 0.4175 -0.0027 -0.0228 -0.0026 137 ILE   B CD1 
5837 N  N   . HIS   B 138 ? 0.2034 0.1729 0.2735 -0.0191 0.0223  0.0148  138 HIS   B N   
5838 C  CA  . HIS   B 138 ? 0.2069 0.1878 0.2483 -0.0155 0.0269  0.0192  138 HIS   B CA  
5839 C  C   . HIS   B 138 ? 0.1931 0.1920 0.2276 -0.0137 0.0138  0.0291  138 HIS   B C   
5840 O  O   . HIS   B 138 ? 0.1827 0.1852 0.2581 -0.0075 0.0202  0.0290  138 HIS   B O   
5841 C  CB  . HIS   B 138 ? 0.2318 0.1997 0.2666 -0.0197 0.0354  -0.0026 138 HIS   B CB  
5842 C  CG  . HIS   B 138 ? 0.2413 0.2085 0.2749 -0.0081 0.0558  0.0231  138 HIS   B CG  
5843 N  ND1 . HIS   B 138 ? 0.2451 0.2290 0.3089 -0.0033 0.0640  0.0093  138 HIS   B ND1 
5844 C  CD2 . HIS   B 138 ? 0.2604 0.2172 0.2619 -0.0177 0.0722  0.0223  138 HIS   B CD2 
5845 C  CE1 . HIS   B 138 ? 0.2583 0.2192 0.2985 -0.0029 0.0677  0.0328  138 HIS   B CE1 
5846 N  NE2 . HIS   B 138 ? 0.2666 0.2135 0.2635 -0.0017 0.0752  0.0331  138 HIS   B NE2 
5854 N  N   . SER   B 139 ? 0.1982 0.1729 0.2156 -0.0113 0.0112  0.0176  139 SER   B N   
5855 C  CA  . SER   B 139 ? 0.1926 0.1665 0.2074 -0.0167 0.0172  0.0071  139 SER   B CA  
5856 C  C   . SER   B 139 ? 0.1870 0.1610 0.2106 -0.0044 0.0123  0.0180  139 SER   B C   
5857 O  O   . SER   B 139 ? 0.1831 0.1554 0.2420 0.0043  -0.0002 0.0248  139 SER   B O   
5858 C  CB  . SER   B 139 ? 0.2043 0.1616 0.2110 0.0003  0.0051  0.0051  139 SER   B CB  
5859 O  OG  . SER   B 139 ? 0.2110 0.1440 0.2312 -0.0003 -0.0018 0.0190  139 SER   B OG  
5865 N  N   . LEU   B 140 ? 0.1858 0.1435 0.2138 -0.0011 0.0133  -0.0057 140 LEU   B N   
5866 C  CA  . LEU   B 140 ? 0.1810 0.1512 0.2200 0.0085  0.0166  -0.0010 140 LEU   B CA  
5867 C  C   . LEU   B 140 ? 0.1748 0.1545 0.2154 0.0055  0.0070  -0.0038 140 LEU   B C   
5868 O  O   . LEU   B 140 ? 0.1724 0.1787 0.2211 -0.0009 0.0121  0.0114  140 LEU   B O   
5869 C  CB  . LEU   B 140 ? 0.1777 0.1677 0.2332 -0.0155 0.0259  -0.0110 140 LEU   B CB  
5870 C  CG  . LEU   B 140 ? 0.1985 0.1678 0.2292 -0.0224 0.0180  0.0000  140 LEU   B CG  
5871 C  CD1 . LEU   B 140 ? 0.2155 0.1822 0.2537 -0.0412 0.0083  0.0271  140 LEU   B CD1 
5872 C  CD2 . LEU   B 140 ? 0.2185 0.1894 0.2213 -0.0131 -0.0014 -0.0073 140 LEU   B CD2 
5884 N  N   . ARG   B 141 ? 0.1880 0.1315 0.2263 -0.0001 0.0072  0.0157  141 ARG   B N   
5885 C  CA  . ARG   B 141 ? 0.1892 0.1415 0.2683 -0.0097 0.0209  0.0051  141 ARG   B CA  
5886 C  C   . ARG   B 141 ? 0.1620 0.1486 0.2535 -0.0055 0.0137  0.0035  141 ARG   B C   
5887 O  O   . ARG   B 141 ? 0.1704 0.1448 0.2727 -0.0237 -0.0118 -0.0062 141 ARG   B O   
5888 C  CB  . ARG   B 141 ? 0.1984 0.1552 0.3173 -0.0058 0.0418  0.0032  141 ARG   B CB  
5889 C  CG  . ARG   B 141 ? 0.2421 0.1895 0.3590 -0.0059 0.0375  -0.0010 141 ARG   B CG  
5890 C  CD  . ARG   B 141 ? 0.2820 0.1983 0.3690 -0.0140 0.0223  -0.0193 141 ARG   B CD  
5891 N  NE  . ARG   B 141 ? 0.3030 0.2005 0.3752 -0.0453 0.0373  -0.0129 141 ARG   B NE  
5892 C  CZ  . ARG   B 141 ? 0.3330 0.1935 0.3651 -0.0467 0.0482  -0.0191 141 ARG   B CZ  
5893 N  NH1 . ARG   B 141 ? 0.3496 0.1781 0.3566 -0.0429 0.0427  -0.0122 141 ARG   B NH1 
5894 N  NH2 . ARG   B 141 ? 0.3476 0.1891 0.3784 -0.0349 0.0277  -0.0355 141 ARG   B NH2 
5908 N  N   . VAL   B 142 ? 0.1732 0.1531 0.2437 -0.0128 0.0124  -0.0054 142 VAL   B N   
5909 C  CA  . VAL   B 142 ? 0.1627 0.1435 0.2436 -0.0063 0.0348  -0.0035 142 VAL   B CA  
5910 C  C   . VAL   B 142 ? 0.1626 0.1424 0.2411 -0.0058 0.0178  -0.0007 142 VAL   B C   
5911 O  O   . VAL   B 142 ? 0.1576 0.1400 0.2541 0.0062  0.0117  -0.0000 142 VAL   B O   
5912 C  CB  . VAL   B 142 ? 0.1784 0.1536 0.2526 -0.0057 0.0292  0.0023  142 VAL   B CB  
5913 C  CG1 . VAL   B 142 ? 0.1802 0.1527 0.2518 0.0037  0.0098  0.0016  142 VAL   B CG1 
5914 C  CG2 . VAL   B 142 ? 0.2007 0.1649 0.2566 -0.0073 0.0238  0.0098  142 VAL   B CG2 
5924 N  N   . CYS   B 143 ? 0.1623 0.1467 0.2174 -0.0074 0.0083  0.0085  143 CYS   B N   
5925 C  CA  . CYS   B 143 ? 0.1527 0.1438 0.2163 -0.0135 0.0027  0.0071  143 CYS   B CA  
5926 C  C   . CYS   B 143 ? 0.1357 0.1695 0.2114 -0.0221 -0.0021 0.0234  143 CYS   B C   
5927 O  O   . CYS   B 143 ? 0.1739 0.1756 0.2040 -0.0145 -0.0062 0.0124  143 CYS   B O   
5928 C  CB  . CYS   B 143 ? 0.1570 0.1655 0.2130 -0.0100 0.0100  -0.0001 143 CYS   B CB  
5929 S  SG  . CYS   B 143 ? 0.1672 0.1706 0.2295 -0.0050 0.0098  0.0037  143 CYS   B SG  
5935 N  N   . VAL   B 144 ? 0.1686 0.1712 0.2219 -0.0114 -0.0022 -0.0110 144 VAL   B N   
5936 C  CA  . VAL   B 144 ? 0.1734 0.1663 0.2504 -0.0122 -0.0043 -0.0067 144 VAL   B CA  
5937 C  C   . VAL   B 144 ? 0.1679 0.1580 0.2602 -0.0144 -0.0115 0.0093  144 VAL   B C   
5938 O  O   . VAL   B 144 ? 0.1702 0.1813 0.2700 0.0020  -0.0196 0.0105  144 VAL   B O   
5939 C  CB  . VAL   B 144 ? 0.2023 0.1927 0.3397 -0.0062 -0.0183 -0.0290 144 VAL   B CB  
5940 C  CG1 . VAL   B 144 ? 0.2249 0.2488 0.3909 -0.0070 -0.0183 -0.0276 144 VAL   B CG1 
5941 C  CG2 . VAL   B 144 ? 0.2106 0.1769 0.3329 0.0015  -0.0299 -0.0544 144 VAL   B CG2 
5951 N  N   . ASP   B 145 ? 0.1607 0.1460 0.2854 -0.0113 0.0052  -0.0187 145 ASP   B N   
5952 C  CA  . ASP   B 145 ? 0.1746 0.1238 0.3083 -0.0153 0.0149  -0.0010 145 ASP   B CA  
5953 C  C   . ASP   B 145 ? 0.1825 0.1364 0.2884 -0.0152 0.0271  -0.0080 145 ASP   B C   
5954 O  O   . ASP   B 145 ? 0.1807 0.1682 0.3249 -0.0111 0.0186  -0.0169 145 ASP   B O   
5955 C  CB  . ASP   B 145 ? 0.1882 0.1581 0.3498 -0.0203 0.0244  -0.0084 145 ASP   B CB  
5956 C  CG  . ASP   B 145 ? 0.2027 0.1580 0.3670 -0.0076 0.0399  -0.0020 145 ASP   B CG  
5957 O  OD1 . ASP   B 145 ? 0.2011 0.1642 0.3755 -0.0208 -0.0036 -0.0138 145 ASP   B OD1 
5958 O  OD2 . ASP   B 145 ? 0.2313 0.1684 0.4277 -0.0325 0.0427  -0.0013 145 ASP   B OD2 
5963 N  N   . THR   B 146 ? 0.1736 0.1405 0.2385 -0.0255 0.0117  0.0062  146 THR   B N   
5964 C  CA  . THR   B 146 ? 0.1666 0.1468 0.2399 -0.0148 0.0088  0.0083  146 THR   B CA  
5965 C  C   . THR   B 146 ? 0.1581 0.1445 0.2190 0.0014  -0.0078 0.0011  146 THR   B C   
5966 O  O   . THR   B 146 ? 0.1580 0.1568 0.2285 0.0040  -0.0142 0.0020  146 THR   B O   
5967 C  CB  . THR   B 146 ? 0.1654 0.1553 0.2294 0.0007  0.0255  0.0006  146 THR   B CB  
5968 O  OG1 . THR   B 146 ? 0.1789 0.1516 0.2313 -0.0073 0.0083  0.0185  146 THR   B OG1 
5969 C  CG2 . THR   B 146 ? 0.1773 0.1589 0.2346 0.0009  0.0242  -0.0078 146 THR   B CG2 
5977 N  N   . VAL   B 147 ? 0.1612 0.1446 0.2016 0.0014  0.0141  0.0076  147 VAL   B N   
5978 C  CA  . VAL   B 147 ? 0.1567 0.1359 0.2009 -0.0124 -0.0026 0.0059  147 VAL   B CA  
5979 C  C   . VAL   B 147 ? 0.1505 0.1487 0.2197 -0.0292 -0.0138 -0.0031 147 VAL   B C   
5980 O  O   . VAL   B 147 ? 0.1679 0.1717 0.2338 -0.0279 -0.0233 0.0066  147 VAL   B O   
5981 C  CB  . VAL   B 147 ? 0.1640 0.1472 0.1879 -0.0043 -0.0035 0.0008  147 VAL   B CB  
5982 C  CG1 . VAL   B 147 ? 0.1682 0.1668 0.1737 -0.0170 -0.0158 0.0072  147 VAL   B CG1 
5983 C  CG2 . VAL   B 147 ? 0.1692 0.1609 0.1638 -0.0082 -0.0009 0.0021  147 VAL   B CG2 
5993 N  N   . ARG   B 148 ? 0.1596 0.1426 0.2109 -0.0153 -0.0152 -0.0125 148 ARG   B N   
5994 C  CA  . ARG   B 148 ? 0.1742 0.1603 0.1993 -0.0116 -0.0247 -0.0217 148 ARG   B CA  
5995 C  C   . ARG   B 148 ? 0.1801 0.1646 0.1730 -0.0049 -0.0268 -0.0087 148 ARG   B C   
5996 O  O   . ARG   B 148 ? 0.1870 0.1905 0.1896 -0.0187 -0.0249 0.0065  148 ARG   B O   
5997 C  CB  . ARG   B 148 ? 0.1596 0.1751 0.2098 0.0022  -0.0338 -0.0104 148 ARG   B CB  
5998 C  CG  . ARG   B 148 ? 0.1688 0.1896 0.2100 -0.0046 -0.0277 -0.0290 148 ARG   B CG  
5999 C  CD  . ARG   B 148 ? 0.1683 0.2019 0.2277 0.0037  -0.0220 -0.0377 148 ARG   B CD  
6000 N  NE  . ARG   B 148 ? 0.1790 0.2031 0.2276 0.0164  -0.0375 -0.0412 148 ARG   B NE  
6001 C  CZ  . ARG   B 148 ? 0.1713 0.1953 0.2135 0.0104  -0.0288 -0.0290 148 ARG   B CZ  
6002 N  NH1 . ARG   B 148 ? 0.1472 0.1792 0.2256 -0.0049 -0.0146 -0.0138 148 ARG   B NH1 
6003 N  NH2 . ARG   B 148 ? 0.1962 0.1789 0.2017 0.0145  -0.0239 -0.0157 148 ARG   B NH2 
6017 N  N   . THR   B 149 ? 0.1867 0.1680 0.1745 -0.0019 -0.0261 -0.0062 149 THR   B N   
6018 C  CA  . THR   B 149 ? 0.1855 0.1698 0.1736 -0.0147 -0.0212 0.0011  149 THR   B CA  
6019 C  C   . THR   B 149 ? 0.1854 0.1797 0.1603 -0.0223 -0.0067 -0.0005 149 THR   B C   
6020 O  O   . THR   B 149 ? 0.1860 0.1758 0.1841 -0.0266 -0.0187 -0.0037 149 THR   B O   
6021 C  CB  . THR   B 149 ? 0.1824 0.1564 0.1930 -0.0144 -0.0218 -0.0049 149 THR   B CB  
6022 O  OG1 . THR   B 149 ? 0.1873 0.1694 0.1780 -0.0245 -0.0228 0.0006  149 THR   B OG1 
6023 C  CG2 . THR   B 149 ? 0.1853 0.1588 0.2333 -0.0135 -0.0069 0.0101  149 THR   B CG2 
6031 N  N   . ASN   B 150 ? 0.1926 0.1661 0.1708 -0.0132 -0.0245 -0.0028 150 ASN   B N   
6032 C  CA  . ASN   B 150 ? 0.1872 0.1653 0.1696 -0.0221 -0.0301 -0.0099 150 ASN   B CA  
6033 C  C   . ASN   B 150 ? 0.1872 0.1542 0.1696 -0.0225 -0.0225 -0.0016 150 ASN   B C   
6034 O  O   . ASN   B 150 ? 0.1916 0.1585 0.1938 -0.0293 -0.0450 -0.0055 150 ASN   B O   
6035 C  CB  . ASN   B 150 ? 0.2087 0.2056 0.1866 -0.0212 -0.0404 0.0115  150 ASN   B CB  
6036 C  CG  . ASN   B 150 ? 0.2422 0.2461 0.2226 -0.0200 -0.0416 0.0260  150 ASN   B CG  
6037 O  OD1 . ASN   B 150 ? 0.2594 0.2623 0.2494 -0.0342 -0.0539 0.0215  150 ASN   B OD1 
6038 N  ND2 . ASN   B 150 ? 0.2489 0.2723 0.2762 -0.0123 -0.0429 0.0708  150 ASN   B ND2 
6045 N  N   . VAL   B 151 ? 0.1713 0.1658 0.1691 -0.0296 -0.0203 -0.0048 151 VAL   B N   
6046 C  CA  . VAL   B 151 ? 0.1704 0.1840 0.1606 -0.0173 -0.0228 -0.0096 151 VAL   B CA  
6047 C  C   . VAL   B 151 ? 0.1705 0.1812 0.1527 -0.0185 -0.0247 -0.0139 151 VAL   B C   
6048 O  O   . VAL   B 151 ? 0.1843 0.1676 0.1903 -0.0136 -0.0131 -0.0111 151 VAL   B O   
6049 C  CB  . VAL   B 151 ? 0.1910 0.1915 0.1839 -0.0162 -0.0217 0.0030  151 VAL   B CB  
6050 C  CG1 . VAL   B 151 ? 0.2050 0.1998 0.2150 -0.0288 -0.0191 -0.0109 151 VAL   B CG1 
6051 C  CG2 . VAL   B 151 ? 0.2017 0.2062 0.1656 0.0011  -0.0138 0.0119  151 VAL   B CG2 
6061 N  N   . TYR   B 152 ? 0.1627 0.1771 0.1569 -0.0198 -0.0016 -0.0070 152 TYR   B N   
6062 C  CA  . TYR   B 152 ? 0.1664 0.1670 0.1514 -0.0279 -0.0083 -0.0058 152 TYR   B CA  
6063 C  C   . TYR   B 152 ? 0.1838 0.1450 0.1343 -0.0161 -0.0097 0.0006  152 TYR   B C   
6064 O  O   . TYR   B 152 ? 0.1872 0.1493 0.1627 -0.0182 -0.0097 0.0014  152 TYR   B O   
6065 C  CB  . TYR   B 152 ? 0.1689 0.1805 0.1735 -0.0247 -0.0084 0.0239  152 TYR   B CB  
6066 C  CG  . TYR   B 152 ? 0.1865 0.1865 0.1903 -0.0366 -0.0168 0.0124  152 TYR   B CG  
6067 C  CD1 . TYR   B 152 ? 0.1895 0.2007 0.1693 -0.0231 -0.0220 0.0094  152 TYR   B CD1 
6068 C  CD2 . TYR   B 152 ? 0.2044 0.1944 0.1865 -0.0288 -0.0184 -0.0034 152 TYR   B CD2 
6069 C  CE1 . TYR   B 152 ? 0.2206 0.2056 0.1769 -0.0196 -0.0335 0.0244  152 TYR   B CE1 
6070 C  CE2 . TYR   B 152 ? 0.2255 0.2087 0.1840 -0.0221 -0.0310 -0.0019 152 TYR   B CE2 
6071 C  CZ  . TYR   B 152 ? 0.2262 0.2202 0.1539 -0.0266 -0.0496 0.0283  152 TYR   B CZ  
6072 O  OH  . TYR   B 152 ? 0.2516 0.2694 0.2053 -0.0211 -0.0404 0.0271  152 TYR   B OH  
6082 N  N   . LEU   B 153 ? 0.1860 0.1439 0.1549 -0.0223 -0.0180 0.0019  153 LEU   B N   
6083 C  CA  . LEU   B 153 ? 0.1884 0.1272 0.1729 -0.0271 -0.0091 0.0008  153 LEU   B CA  
6084 C  C   . LEU   B 153 ? 0.1922 0.1386 0.1816 -0.0191 -0.0029 -0.0113 153 LEU   B C   
6085 O  O   . LEU   B 153 ? 0.1837 0.1529 0.2044 -0.0135 -0.0089 -0.0285 153 LEU   B O   
6086 C  CB  . LEU   B 153 ? 0.1935 0.1297 0.1866 -0.0270 -0.0043 0.0053  153 LEU   B CB  
6087 C  CG  . LEU   B 153 ? 0.1890 0.1424 0.2059 -0.0258 0.0047  -0.0020 153 LEU   B CG  
6088 C  CD1 . LEU   B 153 ? 0.2078 0.1658 0.2202 -0.0273 0.0113  -0.0045 153 LEU   B CD1 
6089 C  CD2 . LEU   B 153 ? 0.1924 0.1642 0.1946 -0.0246 0.0178  0.0052  153 LEU   B CD2 
6101 N  N   . ALA   B 154 ? 0.1867 0.1450 0.1764 -0.0074 -0.0170 -0.0013 154 ALA   B N   
6102 C  CA  . ALA   B 154 ? 0.2078 0.1550 0.1879 -0.0065 -0.0048 -0.0124 154 ALA   B CA  
6103 C  C   . ALA   B 154 ? 0.2252 0.1723 0.1642 -0.0051 -0.0128 -0.0285 154 ALA   B C   
6104 O  O   . ALA   B 154 ? 0.2564 0.1733 0.1916 -0.0049 -0.0132 -0.0168 154 ALA   B O   
6105 C  CB  . ALA   B 154 ? 0.2004 0.1626 0.2155 -0.0136 -0.0054 -0.0149 154 ALA   B CB  
6111 N  N   . VAL   B 155 ? 0.1879 0.1617 0.1818 -0.0175 -0.0000 -0.0171 155 VAL   B N   
6112 C  CA  . VAL   B 155 ? 0.1724 0.1522 0.1968 -0.0128 -0.0115 -0.0086 155 VAL   B CA  
6113 C  C   . VAL   B 155 ? 0.1622 0.1626 0.1956 0.0017  -0.0075 -0.0161 155 VAL   B C   
6114 O  O   . VAL   B 155 ? 0.1966 0.1811 0.2203 0.0085  -0.0143 -0.0342 155 VAL   B O   
6115 C  CB  . VAL   B 155 ? 0.1882 0.1629 0.2434 -0.0062 -0.0156 0.0004  155 VAL   B CB  
6116 C  CG1 . VAL   B 155 ? 0.1975 0.1735 0.2781 -0.0266 -0.0133 0.0114  155 VAL   B CG1 
6117 C  CG2 . VAL   B 155 ? 0.1792 0.1621 0.2782 0.0023  -0.0070 0.0191  155 VAL   B CG2 
6127 N  N   . PHE   B 156 ? 0.1620 0.1708 0.2187 -0.0080 -0.0055 -0.0197 156 PHE   B N   
6128 C  CA  . PHE   B 156 ? 0.1614 0.1804 0.2615 0.0071  -0.0088 -0.0128 156 PHE   B CA  
6129 C  C   . PHE   B 156 ? 0.1666 0.1819 0.2687 0.0047  -0.0215 -0.0297 156 PHE   B C   
6130 O  O   . PHE   B 156 ? 0.2072 0.1948 0.3059 0.0213  -0.0035 -0.0442 156 PHE   B O   
6131 C  CB  . PHE   B 156 ? 0.1739 0.1765 0.2677 0.0056  -0.0219 -0.0183 156 PHE   B CB  
6132 C  CG  . PHE   B 156 ? 0.1744 0.1843 0.2826 0.0113  -0.0221 0.0031  156 PHE   B CG  
6133 C  CD1 . PHE   B 156 ? 0.1818 0.1974 0.3332 0.0173  0.0025  0.0366  156 PHE   B CD1 
6134 C  CD2 . PHE   B 156 ? 0.1878 0.2025 0.2987 0.0160  -0.0419 0.0097  156 PHE   B CD2 
6135 C  CE1 . PHE   B 156 ? 0.1889 0.2156 0.3445 0.0136  -0.0040 0.0452  156 PHE   B CE1 
6136 C  CE2 . PHE   B 156 ? 0.1933 0.2076 0.3160 0.0246  -0.0276 0.0174  156 PHE   B CE2 
6137 C  CZ  . PHE   B 156 ? 0.1900 0.2182 0.3493 0.0187  -0.0253 0.0293  156 PHE   B CZ  
6147 N  N   . ASP   B 157 ? 0.1832 0.1533 0.2952 0.0151  -0.0335 -0.0121 157 ASP   B N   
6148 C  CA  . ASP   B 157 ? 0.2014 0.1638 0.3236 0.0009  -0.0328 -0.0144 157 ASP   B CA  
6149 C  C   . ASP   B 157 ? 0.1971 0.1596 0.3200 0.0049  -0.0222 -0.0469 157 ASP   B C   
6150 O  O   . ASP   B 157 ? 0.1718 0.1647 0.3184 0.0046  -0.0127 -0.0301 157 ASP   B O   
6151 C  CB  . ASP   B 157 ? 0.2161 0.1687 0.3521 0.0047  -0.0549 0.0041  157 ASP   B CB  
6152 C  CG  . ASP   B 157 ? 0.2678 0.1849 0.3847 -0.0057 -0.0458 0.0064  157 ASP   B CG  
6153 O  OD1 . ASP   B 157 ? 0.2758 0.1962 0.4111 0.0066  -0.0505 0.0061  157 ASP   B OD1 
6154 O  OD2 . ASP   B 157 ? 0.3069 0.2026 0.4269 -0.0170 -0.0257 -0.0010 157 ASP   B OD2 
6159 N  N   . LYS   B 158 ? 0.1985 0.1919 0.3476 0.0062  -0.0082 -0.0634 158 LYS   B N   
6160 C  CA  . LYS   B 158 ? 0.2112 0.2024 0.3625 0.0036  0.0041  -0.0843 158 LYS   B CA  
6161 C  C   . LYS   B 158 ? 0.2117 0.1962 0.3761 0.0117  -0.0064 -0.0653 158 LYS   B C   
6162 O  O   . LYS   B 158 ? 0.2185 0.1954 0.3963 0.0192  -0.0123 -0.0789 158 LYS   B O   
6163 C  CB  . LYS   B 158 ? 0.2298 0.2536 0.3735 0.0014  0.0082  -0.1071 158 LYS   B CB  
6164 C  CG  . LYS   B 158 ? 0.2594 0.2897 0.3810 0.0124  0.0138  -0.1138 158 LYS   B CG  
6165 C  CD  . LYS   B 158 ? 0.2930 0.3386 0.4001 0.0076  0.0193  -0.0986 158 LYS   B CD  
6166 C  CE  . LYS   B 158 ? 0.3227 0.3735 0.4205 0.0130  0.0219  -0.0853 158 LYS   B CE  
6167 N  NZ  . LYS   B 158 ? 0.3245 0.3855 0.4143 0.0091  0.0249  -0.0787 158 LYS   B NZ  
6181 N  N   A ASN   B 159 ? 0.1931 0.1662 0.3934 0.0084  -0.0048 -0.0415 159 ASN   B N   
6182 N  N   B ASN   B 159 ? 0.2041 0.1895 0.3657 0.0099  -0.0106 -0.0513 159 ASN   B N   
6183 C  CA  A ASN   B 159 ? 0.2078 0.1799 0.4216 0.0223  -0.0157 -0.0276 159 ASN   B CA  
6184 C  CA  B ASN   B 159 ? 0.2052 0.1962 0.3635 0.0138  -0.0175 -0.0383 159 ASN   B CA  
6185 C  C   A ASN   B 159 ? 0.1909 0.1626 0.4067 0.0057  -0.0456 -0.0334 159 ASN   B C   
6186 C  C   B ASN   B 159 ? 0.1942 0.1836 0.3703 0.0066  -0.0348 -0.0385 159 ASN   B C   
6187 O  O   A ASN   B 159 ? 0.1993 0.1508 0.4263 -0.0068 -0.0649 -0.0225 159 ASN   B O   
6188 O  O   B ASN   B 159 ? 0.1976 0.1838 0.3713 0.0016  -0.0440 -0.0354 159 ASN   B O   
6189 C  CB  A ASN   B 159 ? 0.2283 0.2045 0.4559 0.0358  -0.0206 -0.0272 159 ASN   B CB  
6190 C  CB  B ASN   B 159 ? 0.2136 0.2119 0.3570 0.0189  -0.0188 -0.0307 159 ASN   B CB  
6191 C  CG  A ASN   B 159 ? 0.2535 0.2314 0.4828 0.0384  -0.0402 -0.0339 159 ASN   B CG  
6192 C  CG  B ASN   B 159 ? 0.2217 0.2289 0.3562 0.0194  -0.0270 -0.0283 159 ASN   B CG  
6193 O  OD1 A ASN   B 159 ? 0.2742 0.2364 0.4911 0.0534  -0.0467 -0.0433 159 ASN   B OD1 
6194 O  OD1 B ASN   B 159 ? 0.2296 0.2366 0.3576 0.0233  -0.0286 -0.0291 159 ASN   B OD1 
6195 N  ND2 A ASN   B 159 ? 0.2446 0.2489 0.5030 0.0277  -0.0466 -0.0365 159 ASN   B ND2 
6196 N  ND2 B ASN   B 159 ? 0.2177 0.2369 0.3638 0.0162  -0.0293 -0.0307 159 ASN   B ND2 
6209 N  N   . LEU   B 160 ? 0.1871 0.1742 0.3798 0.0073  -0.0410 -0.0407 160 LEU   B N   
6210 C  CA  . LEU   B 160 ? 0.1832 0.1770 0.3354 0.0007  -0.0377 -0.0305 160 LEU   B CA  
6211 C  C   . LEU   B 160 ? 0.1745 0.1605 0.2990 0.0072  -0.0257 -0.0313 160 LEU   B C   
6212 O  O   . LEU   B 160 ? 0.1648 0.1702 0.2935 0.0043  -0.0386 -0.0166 160 LEU   B O   
6213 C  CB  . LEU   B 160 ? 0.1797 0.1738 0.3271 0.0144  -0.0381 -0.0149 160 LEU   B CB  
6214 C  CG  . LEU   B 160 ? 0.1767 0.1781 0.2972 0.0021  -0.0384 -0.0094 160 LEU   B CG  
6215 C  CD1 . LEU   B 160 ? 0.2157 0.2038 0.3140 -0.0096 -0.0109 -0.0106 160 LEU   B CD1 
6216 C  CD2 . LEU   B 160 ? 0.1814 0.1857 0.2928 0.0209  -0.0358 -0.0198 160 LEU   B CD2 
6229 N  N   . TYR   B 161 ? 0.1775 0.1640 0.3112 -0.0121 -0.0104 -0.0355 161 TYR   B N   
6230 C  CA  . TYR   B 161 ? 0.1863 0.1623 0.3067 -0.0118 0.0180  -0.0531 161 TYR   B CA  
6231 C  C   . TYR   B 161 ? 0.2022 0.1623 0.2881 -0.0023 0.0143  -0.0447 161 TYR   B C   
6232 O  O   . TYR   B 161 ? 0.2138 0.1636 0.2735 -0.0106 0.0035  -0.0289 161 TYR   B O   
6233 C  CB  . TYR   B 161 ? 0.2089 0.1684 0.3078 -0.0112 0.0361  -0.0441 161 TYR   B CB  
6234 C  CG  . TYR   B 161 ? 0.2332 0.1728 0.3047 -0.0265 0.0263  -0.0462 161 TYR   B CG  
6235 C  CD1 . TYR   B 161 ? 0.2404 0.1703 0.3131 -0.0299 0.0195  -0.0418 161 TYR   B CD1 
6236 C  CD2 . TYR   B 161 ? 0.2428 0.1727 0.2983 -0.0164 0.0276  -0.0415 161 TYR   B CD2 
6237 C  CE1 . TYR   B 161 ? 0.2517 0.1964 0.3199 -0.0389 0.0198  -0.0526 161 TYR   B CE1 
6238 C  CE2 . TYR   B 161 ? 0.2599 0.1883 0.3032 -0.0283 0.0395  -0.0512 161 TYR   B CE2 
6239 C  CZ  . TYR   B 161 ? 0.2584 0.1922 0.3062 -0.0353 0.0233  -0.0439 161 TYR   B CZ  
6240 O  OH  . TYR   B 161 ? 0.2787 0.2316 0.3285 -0.0417 0.0223  -0.0438 161 TYR   B OH  
6250 N  N   . ASP   B 162 ? 0.2093 0.1659 0.2962 -0.0098 0.0047  -0.0608 162 ASP   B N   
6251 C  CA  . ASP   B 162 ? 0.2117 0.1793 0.3061 -0.0090 0.0051  -0.0655 162 ASP   B CA  
6252 C  C   . ASP   B 162 ? 0.2067 0.1775 0.3080 -0.0158 -0.0057 -0.0414 162 ASP   B C   
6253 O  O   . ASP   B 162 ? 0.2192 0.1596 0.3278 -0.0340 -0.0211 -0.0301 162 ASP   B O   
6254 C  CB  . ASP   B 162 ? 0.2223 0.2050 0.3300 0.0038  0.0078  -0.0844 162 ASP   B CB  
6255 C  CG  . ASP   B 162 ? 0.2303 0.2383 0.3750 0.0102  0.0125  -0.0808 162 ASP   B CG  
6256 O  OD1 . ASP   B 162 ? 0.2259 0.2484 0.3561 0.0038  0.0101  -0.0832 162 ASP   B OD1 
6257 O  OD2 . ASP   B 162 ? 0.2428 0.2541 0.4101 0.0208  0.0254  -0.0830 162 ASP   B OD2 
6262 N  N   A LYS   B 163 ? 0.1834 0.1675 0.2987 -0.0126 -0.0377 -0.0157 163 LYS   B N   
6263 N  N   B LYS   B 163 ? 0.2033 0.1911 0.3103 -0.0139 -0.0159 -0.0267 163 LYS   B N   
6264 C  CA  A LYS   B 163 ? 0.1924 0.1864 0.3113 -0.0225 -0.0135 0.0113  163 LYS   B CA  
6265 C  CA  B LYS   B 163 ? 0.2063 0.2114 0.3197 -0.0159 -0.0077 -0.0108 163 LYS   B CA  
6266 C  C   A LYS   B 163 ? 0.1676 0.1928 0.2994 -0.0250 -0.0094 0.0032  163 LYS   B C   
6267 C  C   B LYS   B 163 ? 0.1770 0.2017 0.3017 -0.0171 -0.0063 -0.0069 163 LYS   B C   
6268 O  O   A LYS   B 163 ? 0.1712 0.1957 0.3088 -0.0160 -0.0111 0.0116  163 LYS   B O   
6269 O  O   B LYS   B 163 ? 0.1767 0.2023 0.3039 -0.0124 -0.0070 -0.0059 163 LYS   B O   
6270 C  CB  A LYS   B 163 ? 0.2378 0.2185 0.3463 -0.0160 -0.0091 0.0169  163 LYS   B CB  
6271 C  CB  B LYS   B 163 ? 0.2409 0.2427 0.3538 -0.0133 -0.0059 -0.0084 163 LYS   B CB  
6272 C  CG  A LYS   B 163 ? 0.3031 0.2728 0.3953 -0.0061 0.0035  0.0228  163 LYS   B CG  
6273 C  CG  B LYS   B 163 ? 0.2819 0.2836 0.3933 -0.0077 -0.0011 -0.0048 163 LYS   B CG  
6274 C  CD  A LYS   B 163 ? 0.3585 0.3230 0.4588 -0.0115 0.0023  0.0103  163 LYS   B CD  
6275 C  CD  B LYS   B 163 ? 0.3190 0.3230 0.4355 -0.0081 -0.0012 -0.0066 163 LYS   B CD  
6276 C  CE  A LYS   B 163 ? 0.3985 0.3526 0.4965 -0.0183 0.0064  0.0055  163 LYS   B CE  
6277 C  CE  B LYS   B 163 ? 0.3433 0.3414 0.4662 -0.0113 0.0001  -0.0063 163 LYS   B CE  
6278 N  NZ  A LYS   B 163 ? 0.4240 0.3678 0.5218 -0.0219 0.0057  0.0001  163 LYS   B NZ  
6279 N  NZ  B LYS   B 163 ? 0.3547 0.3455 0.4850 -0.0131 0.0003  -0.0067 163 LYS   B NZ  
6306 N  N   . LEU   B 164 ? 0.1526 0.1886 0.2834 -0.0180 -0.0088 0.0013  164 LEU   B N   
6307 C  CA  . LEU   B 164 ? 0.1567 0.1907 0.2609 -0.0108 -0.0171 -0.0004 164 LEU   B CA  
6308 C  C   . LEU   B 164 ? 0.1557 0.1839 0.2551 -0.0157 -0.0158 0.0096  164 LEU   B C   
6309 O  O   . LEU   B 164 ? 0.1591 0.1949 0.2764 -0.0099 -0.0279 -0.0144 164 LEU   B O   
6310 C  CB  . LEU   B 164 ? 0.1531 0.1816 0.2543 -0.0117 -0.0032 -0.0042 164 LEU   B CB  
6311 C  CG  . LEU   B 164 ? 0.1756 0.1699 0.2764 -0.0065 0.0005  0.0080  164 LEU   B CG  
6312 C  CD1 . LEU   B 164 ? 0.1883 0.1602 0.2543 -0.0217 -0.0214 -0.0006 164 LEU   B CD1 
6313 C  CD2 . LEU   B 164 ? 0.1918 0.1829 0.3022 -0.0038 0.0159  -0.0089 164 LEU   B CD2 
6326 N  N   . VAL   B 165 ? 0.1862 0.1780 0.2781 -0.0266 -0.0286 -0.0033 165 VAL   B N   
6327 C  CA  . VAL   B 165 ? 0.2273 0.1987 0.2724 -0.0408 -0.0472 -0.0053 165 VAL   B CA  
6328 C  C   . VAL   B 165 ? 0.2698 0.2071 0.2819 -0.0401 -0.0882 0.0051  165 VAL   B C   
6329 O  O   . VAL   B 165 ? 0.3031 0.2114 0.2952 -0.0459 -0.0887 0.0108  165 VAL   B O   
6330 C  CB  . VAL   B 165 ? 0.2519 0.2118 0.2676 -0.0220 -0.0221 -0.0323 165 VAL   B CB  
6331 C  CG1 . VAL   B 165 ? 0.2831 0.2179 0.3085 -0.0257 -0.0095 -0.0233 165 VAL   B CG1 
6332 C  CG2 . VAL   B 165 ? 0.2420 0.2118 0.2735 -0.0206 -0.0190 -0.0283 165 VAL   B CG2 
6342 N  N   . SER   B 166 ? 0.2734 0.1916 0.3137 -0.0406 -0.0909 -0.0150 166 SER   B N   
6343 C  CA  . SER   B 166 ? 0.2724 0.2030 0.3653 -0.0496 -0.0760 -0.0363 166 SER   B CA  
6344 C  C   . SER   B 166 ? 0.2586 0.1967 0.3895 -0.0523 -0.0547 -0.0049 166 SER   B C   
6345 O  O   . SER   B 166 ? 0.2734 0.2186 0.4273 -0.0594 -0.0773 -0.0271 166 SER   B O   
6346 C  CB  . SER   B 166 ? 0.2734 0.2103 0.3949 -0.0390 -0.0658 -0.0398 166 SER   B CB  
6347 O  OG  . SER   B 166 ? 0.2456 0.2054 0.4248 -0.0297 -0.0713 -0.0242 166 SER   B OG  
6353 N  N   . SER   B 167 ? 0.2345 0.1902 0.3671 -0.0512 -0.0700 0.0497  167 SER   B N   
6354 C  CA  . SER   B 167 ? 0.2228 0.2141 0.3561 -0.0319 -0.0579 0.0304  167 SER   B CA  
6355 C  C   . SER   B 167 ? 0.2058 0.2185 0.3546 -0.0522 -0.0467 0.0409  167 SER   B C   
6356 O  O   . SER   B 167 ? 0.2252 0.2238 0.3353 -0.0566 -0.0493 0.0375  167 SER   B O   
6357 C  CB  . SER   B 167 ? 0.1984 0.2250 0.3520 -0.0411 -0.0298 0.0115  167 SER   B CB  
6358 O  OG  . SER   B 167 ? 0.2022 0.2219 0.3379 -0.0328 -0.0135 0.0193  167 SER   B OG  
6364 N  N   . PHE   B 168 ? 0.2036 0.2172 0.3431 -0.0531 -0.0343 0.0575  168 PHE   B N   
6365 C  CA  . PHE   B 168 ? 0.2286 0.1998 0.3144 -0.0524 -0.0351 0.0431  168 PHE   B CA  
6366 C  C   . PHE   B 168 ? 0.2094 0.1895 0.2666 -0.0144 -0.0104 0.0176  168 PHE   B C   
6367 O  O   . PHE   B 168 ? 0.2209 0.1696 0.2759 -0.0154 -0.0198 0.0050  168 PHE   B O   
6368 C  CB  . PHE   B 168 ? 0.2581 0.2023 0.3233 -0.0624 -0.0456 0.0622  168 PHE   B CB  
6369 C  CG  . PHE   B 168 ? 0.2803 0.1793 0.2973 -0.0617 -0.0488 0.0416  168 PHE   B CG  
6370 C  CD1 . PHE   B 168 ? 0.3130 0.1977 0.3181 -0.0468 -0.0754 0.0344  168 PHE   B CD1 
6371 C  CD2 . PHE   B 168 ? 0.2708 0.1776 0.2990 -0.0517 -0.0516 0.0451  168 PHE   B CD2 
6372 C  CE1 . PHE   B 168 ? 0.3313 0.2012 0.3200 -0.0317 -0.0690 0.0384  168 PHE   B CE1 
6373 C  CE2 . PHE   B 168 ? 0.2960 0.1875 0.3252 -0.0452 -0.0563 0.0320  168 PHE   B CE2 
6374 C  CZ  . PHE   B 168 ? 0.3176 0.1922 0.3290 -0.0297 -0.0769 0.0478  168 PHE   B CZ  
6384 N  N   . LEU   B 169 ? 0.2233 0.2068 0.2581 0.0066  -0.0049 0.0017  169 LEU   B N   
6385 C  CA  . LEU   B 169 ? 0.2583 0.2436 0.2987 0.0038  -0.0098 -0.0346 169 LEU   B CA  
6386 C  C   . LEU   B 169 ? 0.2883 0.2688 0.3712 0.0165  -0.0074 -0.0613 169 LEU   B C   
6387 O  O   . LEU   B 169 ? 0.3028 0.2816 0.4298 0.0191  -0.0053 -0.0903 169 LEU   B O   
6388 C  CB  . LEU   B 169 ? 0.2881 0.2836 0.3022 -0.0119 -0.0197 0.0026  169 LEU   B CB  
6389 C  CG  . LEU   B 169 ? 0.3330 0.3222 0.3765 -0.0015 -0.0049 0.0110  169 LEU   B CG  
6390 C  CD1 . LEU   B 169 ? 0.3465 0.3440 0.3793 -0.0038 -0.0134 0.0243  169 LEU   B CD1 
6391 C  CD2 . LEU   B 169 ? 0.3286 0.3272 0.3921 0.0136  0.0118  -0.0039 169 LEU   B CD2 
6392 O  OXT . LEU   B 169 ? 0.2997 0.2770 0.3767 0.0460  0.0085  -0.0625 169 LEU   B OXT 
6404 C  C1  T TFA   C .   ? 0.1342 0.1226 0.1513 -0.0062 0.0027  0.0277  201 TFA   A C1  
6405 C  C2  T TFA   C .   ? 0.1515 0.1469 0.1803 -0.0090 -0.0070 0.0166  201 TFA   A C2  
6406 O  O   T TFA   C .   ? 0.1197 0.0882 0.1268 0.0140  0.0079  0.0568  201 TFA   A O   
6407 F  F1  T TFA   C .   ? 0.1623 0.1563 0.1927 -0.0078 -0.0195 0.0185  201 TFA   A F1  
6408 F  F2  T TFA   C .   ? 0.1540 0.1528 0.1945 -0.0153 -0.0067 0.0292  201 TFA   A F2  
6409 F  F3  T TFA   C .   ? 0.1584 0.1550 0.1854 -0.0087 0.0112  0.0107  201 TFA   A F3  
6410 O  OXT T TFA   C .   ? 0.1389 0.1291 0.1681 -0.0042 0.0012  0.0245  201 TFA   A OXT 
6411 N  N2  B A1A86 D .   ? 0.1784 0.1982 0.2417 -0.0197 -0.0066 0.0100  202 A1A86 A N2  
6412 C  C3  B A1A86 D .   ? 0.1817 0.2319 0.2678 -0.0155 -0.0039 0.0050  202 A1A86 A C3  
6413 C  C6  B A1A86 D .   ? 0.1781 0.2012 0.2457 -0.0041 -0.0128 0.0001  202 A1A86 A C6  
6414 C  C9  B A1A86 D .   ? 0.1763 0.1951 0.2335 -0.0151 -0.0099 0.0313  202 A1A86 A C9  
6415 C  C12 B A1A86 D .   ? 0.1281 0.1932 0.2328 -0.0055 0.0108  0.0351  202 A1A86 A C12 
6416 C  C1  B A1A86 D .   ? 0.1848 0.2261 0.2708 -0.0167 0.0067  -0.0153 202 A1A86 A C1  
6417 C  C10 B A1A86 D .   ? 0.1453 0.1907 0.2280 -0.0076 -0.0100 0.0370  202 A1A86 A C10 
6418 C  C11 B A1A86 D .   ? 0.1444 0.1961 0.2351 -0.0121 0.0060  0.0315  202 A1A86 A C11 
6419 C  C13 B A1A86 D .   ? 0.1164 0.1891 0.2271 -0.0036 -0.0023 0.0458  202 A1A86 A C13 
6420 C  C2  B A1A86 D .   ? 0.1873 0.2259 0.2661 -0.0121 -0.0142 -0.0041 202 A1A86 A C2  
6421 C  C4  B A1A86 D .   ? 0.1913 0.2332 0.2752 -0.0095 -0.0222 0.0014  202 A1A86 A C4  
6422 C  C5  B A1A86 D .   ? 0.1837 0.2139 0.2554 -0.0071 -0.0264 -0.0065 202 A1A86 A C5  
6423 C  C7  B A1A86 D .   ? 0.1922 0.2084 0.2625 0.0084  -0.0044 -0.0106 202 A1A86 A C7  
6424 C  C8  B A1A86 D .   ? 0.1666 0.2007 0.2398 -0.0159 -0.0068 0.0189  202 A1A86 A C8  
6425 N  N1  B A1A86 D .   ? 0.1725 0.1990 0.2338 -0.0149 -0.0126 0.0144  202 A1A86 A N1  
6426 N  N3  B A1A86 D .   ? 0.1663 0.1948 0.2230 -0.0144 -0.0121 0.0408  202 A1A86 A N3  
6427 N  N4  B A1A86 D .   ? 0.1289 0.1861 0.2234 0.0044  -0.0150 0.0488  202 A1A86 A N4  
6428 O  O1  B A1A86 D .   ? 0.1866 0.2135 0.2677 0.0111  0.0132  -0.0144 202 A1A86 A O1  
6449 CL CL  B CL    E .   ? 0.2314 0.1704 0.3197 -0.0584 0.0730  -0.0431 203 CL    A CL  
6450 O  O   . HOH   F .   ? 0.4299 0.7826 0.5501 -0.1365 0.0419  0.1153  301 HOH   A O   
6451 O  O   . HOH   F .   ? 0.4719 0.3642 0.5301 0.0355  0.1501  -0.0142 302 HOH   A O   
6452 O  O   . HOH   F .   ? 0.5951 0.5073 0.3988 0.1922  -0.1390 0.0584  303 HOH   A O   
6453 O  O   A HOH   F .   ? 0.2765 0.2500 0.3866 -0.0290 -0.0596 0.0824  304 HOH   A O   
6454 O  O   . HOH   F .   ? 0.3219 0.3884 0.1779 -0.0117 0.0639  0.0474  305 HOH   A O   
6455 O  O   . HOH   F .   ? 0.3636 0.3760 0.5004 0.0510  0.0389  -0.1220 306 HOH   A O   
6456 O  O   . HOH   F .   ? 0.2677 0.2657 0.4546 -0.0355 -0.0927 0.0970  307 HOH   A O   
6457 O  O   . HOH   F .   ? 0.5495 0.3172 0.4843 -0.0815 0.0869  0.0931  308 HOH   A O   
6458 O  O   . HOH   F .   ? 0.2283 0.2304 0.3586 -0.0252 -0.0196 -0.0201 309 HOH   A O   
6459 O  O   . HOH   F .   ? 0.3684 0.2767 0.3192 -0.0918 0.0618  0.0407  310 HOH   A O   
6460 O  O   . HOH   F .   ? 0.1987 0.2027 0.2370 0.0060  -0.0084 0.0328  311 HOH   A O   
6461 O  O   . HOH   F .   ? 0.6639 0.5521 0.5018 -0.0988 0.0733  0.1790  312 HOH   A O   
6462 O  O   . HOH   F .   ? 0.1894 0.3847 0.2772 -0.0010 0.0382  0.0519  313 HOH   A O   
6463 O  O   . HOH   F .   ? 0.4808 0.3541 0.3194 -0.0909 0.0506  0.0417  314 HOH   A O   
6464 O  O   . HOH   F .   ? 0.8990 0.4114 0.6108 -0.0211 -0.1431 0.0405  315 HOH   A O   
6465 O  O   . HOH   F .   ? 0.5419 0.2840 0.5040 0.0737  0.0272  -0.0190 316 HOH   A O   
6466 O  O   . HOH   F .   ? 0.7004 0.5915 0.3415 0.0186  -0.0301 0.1001  317 HOH   A O   
6467 O  O   A HOH   F .   ? 0.3042 0.2197 0.2369 -0.0072 0.0685  -0.0400 318 HOH   A O   
6468 O  O   . HOH   F .   ? 0.2950 0.5570 0.6336 0.1219  0.0453  0.1010  319 HOH   A O   
6469 O  O   . HOH   F .   ? 0.3192 0.4571 0.5996 0.0040  0.1162  0.2576  320 HOH   A O   
6470 O  O   . HOH   F .   ? 0.3127 0.4922 0.4915 -0.0482 -0.0841 0.0901  321 HOH   A O   
6471 O  O   . HOH   F .   ? 0.6401 0.5037 0.4996 -0.0507 0.1672  0.2063  322 HOH   A O   
6472 O  O   . HOH   F .   ? 0.5647 0.5778 0.5548 -0.0894 0.0788  -0.0078 323 HOH   A O   
6473 O  O   . HOH   F .   ? 0.3688 0.4018 0.2716 0.0030  0.0299  0.0542  324 HOH   A O   
6474 O  O   . HOH   F .   ? 0.1918 0.3038 0.3337 0.0304  -0.0135 -0.0196 325 HOH   A O   
6475 O  O   . HOH   F .   ? 0.4920 0.3638 0.3671 -0.0265 -0.1053 -0.0087 326 HOH   A O   
6476 O  O   . HOH   F .   ? 0.2181 0.2808 0.3936 0.0267  0.1043  -0.0670 327 HOH   A O   
6477 O  O   . HOH   F .   ? 0.2475 0.4471 0.4439 -0.0072 -0.0753 0.1601  328 HOH   A O   
6478 O  O   . HOH   F .   ? 0.3435 0.4344 0.4345 0.1550  0.0961  0.0601  329 HOH   A O   
6479 O  O   . HOH   F .   ? 0.2503 0.2484 0.3334 0.0299  0.0235  0.0274  330 HOH   A O   
6480 O  O   B HOH   F .   ? 0.4373 0.5043 0.3994 0.0871  0.0079  0.0089  331 HOH   A O   
6481 O  O   . HOH   F .   ? 0.2199 0.3785 0.4520 -0.0390 0.0420  -0.1129 332 HOH   A O   
6482 O  O   . HOH   F .   ? 0.3706 0.3304 0.4482 -0.0591 0.1460  -0.0096 333 HOH   A O   
6483 O  O   . HOH   F .   ? 0.1822 0.1624 0.2285 -0.0165 -0.0020 -0.0037 334 HOH   A O   
6484 O  O   . HOH   F .   ? 0.2412 0.2118 0.2399 0.0291  -0.0226 0.0087  335 HOH   A O   
6485 O  O   . HOH   F .   ? 0.3948 0.4586 0.3949 -0.0104 -0.0784 -0.0893 336 HOH   A O   
6486 O  O   . HOH   F .   ? 0.4925 0.5333 0.2367 -0.1621 0.0579  0.0719  337 HOH   A O   
6487 O  O   B HOH   F .   ? 0.1986 0.2888 0.2516 0.1121  0.0963  0.1444  338 HOH   A O   
6488 O  O   . HOH   F .   ? 0.4423 0.2626 0.5361 0.0369  -0.1143 0.0366  339 HOH   A O   
6489 O  O   . HOH   F .   ? 0.2282 0.2238 0.4039 0.0303  0.0975  -0.0019 340 HOH   A O   
6490 O  O   . HOH   F .   ? 0.6578 0.4820 0.5546 0.0437  0.2739  -0.1451 341 HOH   A O   
6491 O  O   . HOH   F .   ? 0.1827 0.2524 0.2295 0.0042  -0.0057 0.0612  342 HOH   A O   
6492 O  O   A HOH   F .   ? 0.1582 0.2539 0.2202 0.0476  0.0436  0.0692  343 HOH   A O   
6493 O  O   . HOH   F .   ? 0.2451 0.3980 0.4177 0.0950  -0.0578 -0.0095 344 HOH   A O   
6494 O  O   . HOH   F .   ? 0.3533 0.3534 0.3079 -0.0174 -0.1140 0.0437  345 HOH   A O   
6495 O  O   . HOH   F .   ? 0.1663 0.1435 0.1513 -0.0113 0.0180  0.0045  346 HOH   A O   
6496 O  O   . HOH   F .   ? 0.5029 0.2531 0.5039 -0.1341 0.1567  -0.0083 347 HOH   A O   
6497 O  O   . HOH   F .   ? 0.3172 0.3750 0.3678 -0.0487 -0.0446 -0.0127 348 HOH   A O   
6498 O  O   . HOH   F .   ? 0.5439 0.5347 0.5788 0.1927  0.1723  -0.0852 349 HOH   A O   
6499 O  O   . HOH   F .   ? 0.4883 0.4112 0.4242 -0.1786 -0.1458 0.1795  350 HOH   A O   
6500 O  O   . HOH   F .   ? 0.6381 0.5113 0.5539 -0.1359 0.0859  0.1464  351 HOH   A O   
6501 O  O   . HOH   F .   ? 0.1898 0.1621 0.2387 -0.0237 0.0204  -0.0161 352 HOH   A O   
6502 O  O   . HOH   F .   ? 0.2812 0.3616 0.2768 -0.0501 -0.0489 -0.0747 353 HOH   A O   
6503 O  O   . HOH   F .   ? 0.1820 0.2090 0.2670 0.0091  -0.0173 0.0081  354 HOH   A O   
6504 O  O   . HOH   F .   ? 0.1726 0.2002 0.2887 0.0078  -0.0402 -0.0454 355 HOH   A O   
6505 O  O   . HOH   F .   ? 0.3685 0.6861 0.4737 -0.0303 -0.1615 0.1464  356 HOH   A O   
6506 O  O   . HOH   F .   ? 0.3219 0.2613 0.5321 -0.0612 -0.0417 0.0204  357 HOH   A O   
6507 O  O   . HOH   F .   ? 0.2761 0.4705 0.3426 -0.0432 0.0453  0.0573  358 HOH   A O   
6508 O  O   . HOH   F .   ? 0.3204 0.3144 0.4238 -0.0723 -0.0118 -0.0336 359 HOH   A O   
6509 O  O   . HOH   F .   ? 0.4247 0.2783 0.4402 -0.1319 0.1138  0.0042  360 HOH   A O   
6510 O  O   . HOH   F .   ? 0.2388 0.1830 0.2575 0.0040  -0.0601 -0.0093 361 HOH   A O   
6511 O  O   . HOH   F .   ? 0.5187 0.4285 0.3143 0.0729  0.0561  0.1024  362 HOH   A O   
6512 O  O   . HOH   F .   ? 0.2634 0.1946 0.1483 -0.0087 0.0254  0.0140  363 HOH   A O   
6513 O  O   . HOH   F .   ? 0.2557 0.3932 0.3647 0.0035  0.0163  0.0438  364 HOH   A O   
6514 O  O   . HOH   F .   ? 0.3141 0.5201 0.5063 0.0887  0.0538  0.1076  365 HOH   A O   
6515 O  O   . HOH   F .   ? 0.3166 0.3205 0.3790 -0.0924 0.1109  -0.0247 366 HOH   A O   
6516 O  O   . HOH   F .   ? 0.5447 0.6733 0.4534 -0.0592 -0.0841 -0.0844 367 HOH   A O   
6517 O  O   . HOH   F .   ? 0.2541 0.2163 0.2892 -0.0311 0.0331  -0.0052 368 HOH   A O   
6518 O  O   . HOH   F .   ? 0.2365 0.2380 0.2284 -0.0194 -0.0348 0.0224  369 HOH   A O   
6519 O  O   . HOH   F .   ? 0.1779 0.1881 0.1528 -0.0094 -0.0086 -0.0022 370 HOH   A O   
6520 O  O   . HOH   F .   ? 0.5882 0.3816 0.6278 0.1210  -0.0836 0.0131  371 HOH   A O   
6521 O  O   . HOH   F .   ? 0.5615 0.5632 0.5745 -0.1211 -0.0019 0.0824  372 HOH   A O   
6522 O  O   . HOH   F .   ? 0.3335 0.4568 0.3244 0.0348  0.1002  0.1678  373 HOH   A O   
6523 O  O   . HOH   F .   ? 0.2906 0.3454 0.5509 -0.0551 -0.0789 -0.0944 374 HOH   A O   
6524 O  O   . HOH   F .   ? 0.6392 0.6750 0.4702 0.2256  -0.0428 -0.0578 375 HOH   A O   
6525 O  O   A HOH   F .   ? 0.2601 0.2923 0.2552 0.0529  0.0464  0.0385  376 HOH   A O   
6526 O  O   . HOH   F .   ? 0.3156 0.6414 0.3825 0.0914  0.0720  -0.1057 377 HOH   A O   
6527 O  O   . HOH   F .   ? 0.2733 0.6438 0.5568 -0.0178 -0.0365 0.1323  378 HOH   A O   
6528 O  O   . HOH   F .   ? 0.2584 0.2070 0.2593 -0.0522 -0.0240 0.0262  379 HOH   A O   
6529 O  O   . HOH   F .   ? 0.1701 0.1661 0.1939 0.0068  -0.0140 0.0023  380 HOH   A O   
6530 O  O   . HOH   F .   ? 0.2472 0.2164 0.1988 0.0018  0.0216  0.0246  381 HOH   A O   
6531 O  O   . HOH   F .   ? 0.2387 0.2293 0.3483 0.0044  -0.0498 0.0149  382 HOH   A O   
6532 O  O   . HOH   F .   ? 0.3348 0.3401 0.2115 0.0654  0.0752  0.0128  383 HOH   A O   
6533 O  O   . HOH   F .   ? 0.4298 0.2611 0.2283 0.1481  0.0397  0.0218  384 HOH   A O   
6534 O  O   . HOH   F .   ? 0.1917 0.1956 0.2417 -0.0217 0.0261  0.0316  385 HOH   A O   
6535 O  O   T HOH   F .   ? 0.0850 0.0680 0.1383 -0.0214 0.0136  0.0370  386 HOH   A O   
6536 O  O   . HOH   F .   ? 0.2927 0.3170 0.4082 -0.0123 0.1291  -0.0357 387 HOH   A O   
6537 O  O   . HOH   F .   ? 0.2106 0.2860 0.2893 0.0288  0.0277  0.0975  388 HOH   A O   
6538 O  O   A HOH   F .   ? 0.2493 0.2265 0.2691 -0.0290 0.0432  0.0701  389 HOH   A O   
6539 O  O   . HOH   F .   ? 0.3460 0.3909 0.5285 -0.0538 0.1619  -0.0283 390 HOH   A O   
6540 O  O   . HOH   F .   ? 0.2592 0.2524 0.3034 0.0027  -0.0149 0.0681  391 HOH   A O   
6541 O  O   . HOH   F .   ? 0.3822 0.3603 0.5520 0.0936  0.0875  0.0470  392 HOH   A O   
6542 O  O   . HOH   F .   ? 0.1905 0.1700 0.1976 0.0128  -0.0360 -0.0224 393 HOH   A O   
6543 O  O   . HOH   F .   ? 0.2052 0.2251 0.1826 -0.0012 0.0103  0.0496  394 HOH   A O   
6544 O  O   . HOH   F .   ? 0.2919 0.2122 0.1945 -0.0540 0.0201  0.0183  395 HOH   A O   
6545 O  O   . HOH   F .   ? 0.2069 0.2209 0.3752 0.0385  0.1013  0.0828  396 HOH   A O   
6546 O  O   . HOH   F .   ? 0.2271 0.2324 0.2776 -0.0205 -0.0247 0.0733  397 HOH   A O   
6547 O  O   . HOH   F .   ? 0.3431 0.3165 0.3539 0.0051  -0.0195 0.0910  398 HOH   A O   
6548 O  O   . HOH   F .   ? 0.4053 0.6501 0.4032 -0.0572 0.0526  0.1258  399 HOH   A O   
6549 O  O   . HOH   F .   ? 0.2808 0.3124 0.4031 -0.0191 0.0784  -0.0385 400 HOH   A O   
6550 O  O   A HOH   F .   ? 0.3350 0.2508 0.3983 0.0608  0.0387  0.1227  401 HOH   A O   
6551 O  O   . HOH   F .   ? 0.5583 0.3490 0.4510 0.0749  0.0238  -0.0599 402 HOH   A O   
6552 O  O   . HOH   F .   ? 0.2455 0.1883 0.2884 0.0119  -0.0160 0.0153  403 HOH   A O   
6553 O  O   . HOH   F .   ? 0.3440 0.3324 0.2235 -0.0751 -0.1011 0.0443  404 HOH   A O   
6554 O  O   B HOH   F .   ? 0.3120 0.2423 0.2522 -0.0029 -0.0299 -0.0064 405 HOH   A O   
6555 O  O   . HOH   F .   ? 0.2243 0.2803 0.3619 -0.0106 0.0027  0.0036  406 HOH   A O   
6556 O  O   B HOH   F .   ? 0.2594 0.1877 0.2643 0.0817  0.0114  0.0147  407 HOH   A O   
6557 O  O   . HOH   F .   ? 0.5348 0.3901 0.2190 -0.0344 0.0775  0.0431  408 HOH   A O   
6558 O  O   A HOH   F .   ? 0.2828 0.1899 0.4058 -0.0096 0.0528  0.0045  409 HOH   A O   
6559 O  O   . HOH   F .   ? 0.6118 0.7018 0.5535 0.0863  0.0169  0.0521  410 HOH   A O   
6560 O  O   . HOH   F .   ? 0.4389 0.5895 0.3558 -0.0695 -0.0332 0.0991  411 HOH   A O   
6561 O  O   . HOH   F .   ? 0.1950 0.1577 0.1765 -0.0233 0.0125  -0.0022 412 HOH   A O   
6562 O  O   A HOH   F .   ? 0.1577 0.1742 0.1652 0.0070  -0.0261 0.0013  413 HOH   A O   
6563 O  O   . HOH   F .   ? 0.2508 0.2162 0.3031 -0.0080 0.0069  0.0297  414 HOH   A O   
6564 O  O   . HOH   F .   ? 0.2347 0.4767 0.7630 -0.0066 0.1320  -0.0325 415 HOH   A O   
6565 O  O   . HOH   F .   ? 0.1842 0.1972 0.2856 -0.0000 -0.0002 0.0297  416 HOH   A O   
6566 O  O   . HOH   F .   ? 0.2882 0.2114 0.3105 -0.0695 -0.0037 0.0472  417 HOH   A O   
6567 O  O   A HOH   F .   ? 0.1819 0.2373 0.3170 -0.0168 0.0704  0.0477  418 HOH   A O   
6568 O  O   . HOH   F .   ? 0.4366 0.2337 0.5924 -0.0805 -0.2618 0.1027  419 HOH   A O   
6569 O  O   . HOH   F .   ? 0.2710 0.3194 0.3495 0.0166  -0.0555 -0.0258 420 HOH   A O   
6570 O  O   . HOH   F .   ? 0.2939 0.6201 0.1800 -0.0416 0.0384  0.0328  421 HOH   A O   
6571 O  O   . HOH   F .   ? 0.3915 0.4719 0.4042 0.1005  -0.0835 -0.1353 422 HOH   A O   
6572 O  O   . HOH   F .   ? 0.3549 0.1594 0.2291 -0.0069 -0.0491 0.0256  423 HOH   A O   
6573 O  O   . HOH   F .   ? 0.2492 0.2716 0.2843 -0.0051 -0.0734 0.0352  424 HOH   A O   
6574 O  O   . HOH   F .   ? 0.2632 0.4592 0.2787 0.1722  -0.0233 0.0286  425 HOH   A O   
6575 O  O   . HOH   F .   ? 0.3417 0.5949 0.4754 0.1331  0.0287  0.0513  426 HOH   A O   
6576 O  O   . HOH   F .   ? 0.6629 0.4374 0.4844 0.1996  -0.0446 0.1573  427 HOH   A O   
6577 O  O   . HOH   F .   ? 0.5869 0.6997 0.4260 0.1051  0.2246  -0.0408 428 HOH   A O   
6578 O  O   . HOH   F .   ? 0.2621 0.3129 0.3936 0.0064  -0.0047 -0.0590 429 HOH   A O   
6579 O  O   . HOH   F .   ? 0.1992 0.2223 0.2911 -0.0208 -0.0014 0.0313  430 HOH   A O   
6580 O  O   T HOH   F .   ? 0.0873 0.0605 0.1176 -0.0270 -0.0167 0.0354  431 HOH   A O   
6581 O  O   . HOH   F .   ? 0.2167 0.2148 0.3202 0.0125  -0.0524 0.0358  432 HOH   A O   
6582 O  O   . HOH   F .   ? 0.5900 0.4695 0.5729 -0.1988 -0.0499 -0.1180 433 HOH   A O   
6583 O  O   . HOH   F .   ? 0.3415 0.3402 0.2749 -0.0280 -0.0262 0.0271  434 HOH   A O   
6584 O  O   . HOH   F .   ? 0.5516 0.5373 0.6330 0.1002  0.0306  -0.0991 435 HOH   A O   
6585 O  O   . HOH   F .   ? 0.6706 0.6485 0.6040 0.0728  -0.1108 0.0616  436 HOH   A O   
6586 O  O   . HOH   F .   ? 0.5599 0.5366 0.3659 -0.0130 -0.1666 0.0447  437 HOH   A O   
6587 O  O   B HOH   F .   ? 0.2527 0.1567 0.2351 0.0589  -0.0382 0.0511  438 HOH   A O   
6588 O  O   . HOH   F .   ? 0.2628 0.2738 0.2704 -0.0013 -0.0118 -0.0451 439 HOH   A O   
6589 O  O   . HOH   F .   ? 0.3855 0.2938 0.1912 -0.0535 0.0117  0.0099  440 HOH   A O   
6590 O  O   . HOH   F .   ? 0.2751 0.2151 0.2713 -0.0141 0.0133  0.0119  441 HOH   A O   
6591 O  O   A HOH   F .   ? 0.1679 0.2128 0.2369 0.0304  -0.0464 -0.0443 442 HOH   A O   
6592 O  O   B HOH   F .   ? 0.2579 0.3404 0.2693 0.0574  -0.0622 0.0288  443 HOH   A O   
6593 O  O   . HOH   F .   ? 0.4226 0.4029 0.3293 0.2427  -0.0601 -0.0660 444 HOH   A O   
6594 O  O   . HOH   F .   ? 0.4880 0.6719 0.6147 -0.1979 -0.0040 -0.1235 445 HOH   A O   
6595 O  O   . HOH   F .   ? 0.9227 0.9307 0.6644 -0.0855 0.0469  -0.0280 446 HOH   A O   
6596 O  O   . HOH   F .   ? 0.4190 0.4846 0.5323 -0.1617 -0.0729 -0.1120 447 HOH   A O   
6597 O  O   . HOH   F .   ? 0.7860 0.7208 0.4162 0.2286  -0.1222 0.1559  448 HOH   A O   
6598 O  O   . HOH   F .   ? 0.5827 0.6005 0.7974 0.0393  -0.1581 0.1902  449 HOH   A O   
6599 O  O   A HOH   F .   ? 0.4887 0.2244 0.4408 -0.0769 0.0359  0.0837  450 HOH   A O   
6600 O  O   . HOH   F .   ? 0.2902 0.2279 0.2889 0.0093  0.0522  0.0265  451 HOH   A O   
6601 O  O   . HOH   F .   ? 0.2257 0.2146 0.5411 -0.0212 -0.0950 0.0858  452 HOH   A O   
6602 O  O   A HOH   F .   ? 0.2145 0.1652 0.1575 -0.0094 -0.0260 -0.0201 453 HOH   A O   
6603 O  O   A HOH   F .   ? 0.4804 0.4204 0.5408 0.0077  0.0615  0.2183  454 HOH   A O   
6604 O  O   A HOH   F .   ? 0.3480 0.3605 0.5444 -0.0053 0.1773  -0.1075 455 HOH   A O   
6605 O  O   . HOH   F .   ? 0.4967 0.3537 0.4366 0.0928  0.0115  0.0721  456 HOH   A O   
6606 O  O   . HOH   F .   ? 0.4627 0.4705 0.4641 0.0978  -0.0230 0.1023  457 HOH   A O   
6607 O  O   B HOH   F .   ? 0.3303 0.2565 0.3815 -0.0231 -0.0833 0.0303  458 HOH   A O   
6608 O  O   . HOH   F .   ? 0.3267 0.2827 0.3658 0.0622  -0.0228 0.0223  459 HOH   A O   
6609 O  O   . HOH   F .   ? 0.6171 0.5461 0.5330 -0.0173 0.0551  0.0821  460 HOH   A O   
6610 O  O   . HOH   F .   ? 0.5761 0.3791 0.4916 0.0196  0.0666  0.0769  461 HOH   A O   
6611 O  O   . HOH   F .   ? 0.3215 0.3144 0.3599 -0.0706 0.0418  -0.0997 462 HOH   A O   
6612 O  O   . HOH   F .   ? 0.6990 0.8092 0.4893 0.0177  -0.0428 -0.0475 463 HOH   A O   
6613 O  O   . HOH   F .   ? 0.3741 0.5236 0.5009 0.0614  -0.0701 0.0601  464 HOH   A O   
6614 O  O   . HOH   F .   ? 0.3025 0.5249 0.5943 -0.0752 0.0564  -0.2319 465 HOH   A O   
6615 O  O   . HOH   F .   ? 0.3653 0.3766 0.4996 -0.0354 -0.0314 -0.0268 466 HOH   A O   
6616 O  O   B HOH   F .   ? 0.3911 0.2191 0.2969 0.0717  -0.1039 -0.0205 467 HOH   A O   
6617 O  O   . HOH   F .   ? 0.2634 0.2503 0.3862 -0.0551 0.0420  -0.0398 468 HOH   A O   
6618 O  O   . HOH   F .   ? 0.5585 0.5700 0.5491 0.0046  0.0864  0.0296  469 HOH   A O   
6619 O  O   . HOH   F .   ? 0.3125 0.4501 0.5845 0.1055  -0.0309 -0.2053 470 HOH   A O   
6620 O  O   . HOH   F .   ? 0.2916 0.2320 0.2629 0.0585  -0.0635 -0.0309 471 HOH   A O   
6621 O  O   A HOH   F .   ? 0.2755 0.3235 0.6226 0.0451  -0.1366 -0.0284 472 HOH   A O   
6622 O  O   . HOH   F .   ? 0.2782 0.3223 0.4712 -0.0019 0.0510  -0.0193 473 HOH   A O   
6623 O  O   . HOH   F .   ? 0.6285 0.4574 0.6129 0.0751  0.1986  0.1438  474 HOH   A O   
6624 O  O   . HOH   F .   ? 0.4428 0.5837 0.3838 -0.0569 -0.0431 0.2118  475 HOH   A O   
6625 O  O   . HOH   F .   ? 0.5638 0.3532 0.7022 -0.0799 -0.0893 0.1962  476 HOH   A O   
6626 O  O   . HOH   F .   ? 0.4834 0.5247 0.5113 -0.2154 -0.0301 -0.0296 477 HOH   A O   
6627 O  O   . HOH   F .   ? 0.2520 0.2569 0.2959 0.0200  -0.0089 -0.0132 478 HOH   A O   
6628 O  O   . HOH   F .   ? 0.3904 0.6242 0.4181 0.0376  0.0047  -0.0504 479 HOH   A O   
6629 O  O   . HOH   F .   ? 0.6828 0.4836 0.7054 -0.1474 0.0480  -0.0666 480 HOH   A O   
6630 O  O   . HOH   F .   ? 0.5137 0.5787 0.4757 0.1115  -0.1331 -0.0937 481 HOH   A O   
6631 O  O   . HOH   F .   ? 0.5322 0.5202 0.6285 -0.2332 -0.0992 0.0206  482 HOH   A O   
6632 O  O   . HOH   F .   ? 0.4266 0.5424 0.3093 -0.0517 -0.0038 -0.0180 483 HOH   A O   
6633 O  O   . HOH   F .   ? 0.6615 0.4168 0.4537 0.0287  0.0556  -0.1279 484 HOH   A O   
6634 O  O   . HOH   F .   ? 0.7905 0.4118 0.3454 -0.0317 -0.1245 0.0307  485 HOH   A O   
6635 O  O   B HOH   F .   ? 0.3488 0.3723 0.4349 0.0841  -0.0074 -0.0262 486 HOH   A O   
6636 O  O   . HOH   F .   ? 0.5354 0.4206 0.3907 -0.0660 -0.0250 -0.0088 487 HOH   A O   
6637 O  O   . HOH   F .   ? 0.4817 0.2527 0.4278 -0.0451 -0.1344 0.0388  488 HOH   A O   
6638 O  O   . HOH   F .   ? 0.5992 0.6672 0.4690 -0.0793 0.1100  0.1002  489 HOH   A O   
6639 O  O   . HOH   F .   ? 0.3399 0.5164 0.3137 -0.0168 -0.0205 -0.0697 490 HOH   A O   
6640 O  O   . HOH   F .   ? 0.5367 0.5778 0.6233 0.0525  0.1049  -0.1185 491 HOH   A O   
6641 O  O   . HOH   F .   ? 0.5389 0.4093 0.4068 -0.0603 0.1083  -0.0159 492 HOH   A O   
6642 O  O   . HOH   F .   ? 0.2801 0.4312 0.4535 0.0066  0.0895  0.0609  493 HOH   A O   
6643 O  O   . HOH   F .   ? 0.3367 0.5770 0.4181 0.1417  0.1438  0.2558  494 HOH   A O   
6644 O  O   . HOH   F .   ? 0.4282 0.4167 0.3130 -0.0831 0.1321  -0.0725 495 HOH   A O   
6645 O  O   . HOH   F .   ? 0.5930 0.4567 0.5437 -0.0313 -0.1092 0.0311  496 HOH   A O   
6646 O  O   . HOH   F .   ? 0.3070 0.2830 0.7698 -0.0452 -0.1702 0.0596  497 HOH   A O   
6647 O  O   . HOH   F .   ? 0.5159 0.4307 0.5031 -0.0652 0.2578  0.0177  498 HOH   A O   
6648 O  O   . HOH   F .   ? 0.3117 0.2502 0.5248 0.0133  -0.0207 0.1108  499 HOH   A O   
6649 O  O   . HOH   F .   ? 0.5634 0.6053 0.4998 -0.0524 -0.1084 -0.0361 500 HOH   A O   
6650 O  O   . HOH   F .   ? 0.6321 0.2969 0.5403 -0.0826 0.0807  0.0833  501 HOH   A O   
6651 O  O   . HOH   F .   ? 0.4549 0.3158 0.4518 -0.0992 0.0441  0.0657  502 HOH   A O   
6652 O  O   . HOH   F .   ? 0.2716 0.3356 0.5039 0.0124  0.0956  -0.0289 503 HOH   A O   
6653 O  O   . HOH   F .   ? 0.4277 0.8243 0.5628 -0.0979 0.0025  0.2432  504 HOH   A O   
6654 O  O   . HOH   F .   ? 0.3381 0.3074 0.4202 0.0569  -0.1049 0.0426  505 HOH   A O   
6655 O  O   . HOH   F .   ? 0.5222 0.2822 0.4316 -0.1257 0.0191  0.0593  506 HOH   A O   
6656 O  O   . HOH   F .   ? 0.3351 0.3919 0.4719 0.0770  -0.0196 -0.0161 507 HOH   A O   
6657 O  O   . HOH   F .   ? 0.5441 0.6862 0.5191 0.0344  -0.0692 0.1031  508 HOH   A O   
6658 O  O   B HOH   F .   ? 0.4051 0.4690 0.3706 0.1089  -0.0078 0.0455  509 HOH   A O   
6659 O  O   . HOH   F .   ? 0.6663 0.3945 0.5083 0.0535  -0.0398 0.1390  510 HOH   A O   
6660 O  O   . HOH   F .   ? 0.5098 0.5783 0.4402 0.0176  -0.1351 0.0213  511 HOH   A O   
6661 O  O   B HOH   F .   ? 0.3238 0.4102 0.3550 0.1233  0.0141  -0.0016 512 HOH   A O   
6662 O  O   B HOH   F .   ? 0.3281 0.1515 0.2588 0.0120  -0.0325 0.0156  513 HOH   A O   
6663 O  O   . HOH   F .   ? 0.5119 0.6740 0.4606 0.2680  -0.0214 0.0824  514 HOH   A O   
6664 O  O   . HOH   F .   ? 0.2752 0.2598 0.5553 0.0143  0.0555  0.0869  515 HOH   A O   
6665 O  O   A HOH   F .   ? 0.4166 0.8383 0.3739 0.0681  0.1536  0.0401  516 HOH   A O   
6666 O  O   . HOH   F .   ? 0.4474 0.5872 0.4406 0.0712  -0.0567 -0.1516 517 HOH   A O   
6667 O  O   B HOH   F .   ? 0.2619 0.2821 0.2687 0.0842  0.0370  0.0368  518 HOH   A O   
6668 O  O   . HOH   F .   ? 0.2986 0.6913 0.3738 0.0214  0.0291  -0.0085 519 HOH   A O   
6669 O  O   . HOH   F .   ? 0.4010 0.5032 0.3969 0.0825  -0.0620 0.0877  520 HOH   A O   
6670 O  O   . HOH   F .   ? 0.4492 0.7030 0.5299 -0.0967 -0.0382 -0.0136 521 HOH   A O   
6671 O  O   . HOH   F .   ? 0.3638 0.4480 0.5816 0.0019  -0.0404 0.2250  522 HOH   A O   
6672 O  O   . HOH   G .   ? 0.2804 0.3027 0.3188 0.0188  0.0814  0.0334  201 HOH   B O   
6673 O  O   . HOH   G .   ? 0.6868 0.5869 0.6056 0.1923  0.0580  0.0542  202 HOH   B O   
6674 O  O   . HOH   G .   ? 0.4690 0.5775 0.2655 0.0277  -0.0178 -0.1346 203 HOH   B O   
6675 O  O   . HOH   G .   ? 0.6975 0.3851 0.5402 0.0796  0.1704  0.0384  204 HOH   B O   
6676 O  O   . HOH   G .   ? 0.3747 0.7291 0.4366 0.0913  0.0358  0.2730  205 HOH   B O   
6677 O  O   . HOH   G .   ? 0.4295 0.4379 0.6829 -0.0070 -0.1256 0.2889  206 HOH   B O   
6678 O  O   . HOH   G .   ? 0.1975 0.3036 0.3506 -0.0128 0.0008  -0.0392 207 HOH   B O   
6679 O  O   . HOH   G .   ? 0.3117 0.3286 0.7283 0.0750  -0.1267 0.0656  208 HOH   B O   
6680 O  O   . HOH   G .   ? 0.4188 0.6600 0.4347 0.2776  -0.0908 -0.0055 209 HOH   B O   
6681 O  O   . HOH   G .   ? 0.4194 0.3223 0.3490 -0.0829 0.0815  -0.0981 210 HOH   B O   
6682 O  O   . HOH   G .   ? 0.4249 0.5497 0.4638 0.2287  0.0457  -0.0236 211 HOH   B O   
6683 O  O   . HOH   G .   ? 0.5061 0.3977 0.7287 -0.0959 -0.1726 -0.0304 212 HOH   B O   
6684 O  O   . HOH   G .   ? 0.3306 0.2400 0.5436 -0.0066 0.2027  0.0520  213 HOH   B O   
6685 O  O   . HOH   G .   ? 0.4842 0.5428 0.4005 0.2713  -0.0296 0.0301  214 HOH   B O   
6686 O  O   . HOH   G .   ? 0.6350 0.3445 0.4540 -0.1715 0.0099  -0.0183 215 HOH   B O   
6687 O  O   . HOH   G .   ? 0.3726 0.3907 0.5318 0.0012  -0.0978 -0.0374 216 HOH   B O   
6688 O  O   . HOH   G .   ? 0.1946 0.2027 0.2753 -0.0191 -0.0000 0.0059  217 HOH   B O   
6689 O  O   . HOH   G .   ? 0.5616 0.2080 0.3581 0.0059  -0.0959 0.0251  218 HOH   B O   
6690 O  O   . HOH   G .   ? 0.4478 0.4273 0.4793 -0.1707 0.0590  0.0473  219 HOH   B O   
6691 O  O   . HOH   G .   ? 0.2572 0.5397 0.5525 -0.0136 0.1168  -0.2168 220 HOH   B O   
6692 O  O   . HOH   G .   ? 0.4898 0.6542 0.3483 0.2752  0.0289  0.0221  221 HOH   B O   
6693 O  O   . HOH   G .   ? 0.6682 0.4425 0.5077 0.1654  0.0355  -0.1192 222 HOH   B O   
6694 O  O   . HOH   G .   ? 0.3862 0.3126 0.7173 -0.0068 0.0047  -0.0460 223 HOH   B O   
6695 O  O   . HOH   G .   ? 0.5430 0.4757 0.4156 -0.0446 -0.0967 0.0926  224 HOH   B O   
6696 O  O   . HOH   G .   ? 0.5741 0.6957 0.3641 0.0932  -0.0258 0.0555  225 HOH   B O   
6697 O  O   . HOH   G .   ? 0.4098 0.4673 0.4205 0.0182  0.0589  -0.1725 226 HOH   B O   
6698 O  O   . HOH   G .   ? 0.2985 0.2161 0.3195 -0.0407 0.1379  0.0036  227 HOH   B O   
6699 O  O   . HOH   G .   ? 0.2428 0.2479 0.3785 -0.0240 0.0008  -0.0522 228 HOH   B O   
6700 O  O   . HOH   G .   ? 0.3833 0.3190 0.5728 -0.0200 0.0539  -0.0016 229 HOH   B O   
6701 O  O   . HOH   G .   ? 0.1989 0.2401 0.2804 -0.0017 0.0023  -0.0158 230 HOH   B O   
6702 O  O   . HOH   G .   ? 0.4064 0.4885 0.5654 -0.1011 0.0095  -0.2042 231 HOH   B O   
6703 O  O   . HOH   G .   ? 0.4158 0.3974 0.2529 0.0618  0.0707  0.0492  232 HOH   B O   
6704 O  O   . HOH   G .   ? 0.3107 0.2816 0.4214 0.0053  0.1205  0.0246  233 HOH   B O   
6705 O  O   . HOH   G .   ? 0.4231 0.2637 0.4376 0.0603  -0.0930 -0.1116 234 HOH   B O   
6706 O  O   . HOH   G .   ? 0.1750 0.1617 0.1729 -0.0075 -0.0054 0.0029  235 HOH   B O   
6707 O  O   . HOH   G .   ? 0.3271 0.1918 0.6347 -0.0130 -0.0963 -0.0483 236 HOH   B O   
6708 O  O   . HOH   G .   ? 0.1719 0.1893 0.2605 -0.0038 0.0015  -0.0305 237 HOH   B O   
6709 O  O   . HOH   G .   ? 0.2648 0.4103 0.3353 -0.0062 -0.0760 -0.0598 238 HOH   B O   
6710 O  O   . HOH   G .   ? 0.3238 0.2751 0.3528 0.0507  0.0172  -0.0880 239 HOH   B O   
6711 O  O   . HOH   G .   ? 0.2512 0.1542 0.3612 -0.0060 -0.0601 -0.0174 240 HOH   B O   
6712 O  O   . HOH   G .   ? 0.3643 0.2695 0.4946 0.0704  -0.0579 -0.0413 241 HOH   B O   
6713 O  O   . HOH   G .   ? 0.4786 0.3097 0.3448 -0.0801 0.0420  -0.0480 242 HOH   B O   
6714 O  O   . HOH   G .   ? 0.2656 0.4241 0.2478 -0.0474 -0.0175 0.0712  243 HOH   B O   
6715 O  O   . HOH   G .   ? 0.3302 0.3399 0.3597 -0.0729 0.0601  -0.0356 244 HOH   B O   
6716 O  O   . HOH   G .   ? 0.3344 0.3665 0.2440 0.0486  0.0986  0.0275  245 HOH   B O   
6717 O  O   . HOH   G .   ? 0.4178 0.2185 0.2298 -0.0261 -0.0855 -0.0044 246 HOH   B O   
6718 O  O   . HOH   G .   ? 0.3075 0.2766 0.3045 0.1036  0.0657  0.0121  247 HOH   B O   
6719 O  O   . HOH   G .   ? 0.2593 0.2643 0.3234 -0.0525 0.0107  -0.0427 248 HOH   B O   
6720 O  O   . HOH   G .   ? 0.2987 0.4646 0.3939 -0.1033 -0.0191 -0.0784 249 HOH   B O   
6721 O  O   . HOH   G .   ? 0.2428 0.1716 0.2188 -0.0312 -0.0386 0.0294  250 HOH   B O   
6722 O  O   . HOH   G .   ? 0.2937 0.4306 0.5585 0.1364  -0.0987 -0.1382 251 HOH   B O   
6723 O  O   . HOH   G .   ? 0.1773 0.1932 0.1949 -0.0135 0.0058  0.0124  252 HOH   B O   
6724 O  O   . HOH   G .   ? 0.5213 0.2933 0.4352 -0.1644 -0.0063 0.0198  253 HOH   B O   
6725 O  O   . HOH   G .   ? 0.1700 0.1639 0.1674 -0.0070 -0.0001 0.0058  254 HOH   B O   
6726 O  O   . HOH   G .   ? 0.3299 0.2605 0.3153 -0.0477 0.0183  -0.0557 255 HOH   B O   
6727 O  O   . HOH   G .   ? 0.1936 0.1845 0.2895 -0.0186 -0.0222 -0.0020 256 HOH   B O   
6728 O  O   . HOH   G .   ? 0.2159 0.2112 0.1726 -0.0405 -0.0527 0.0086  257 HOH   B O   
6729 O  O   . HOH   G .   ? 0.2500 0.2534 0.2146 0.0006  -0.0144 0.0005  258 HOH   B O   
6730 O  O   . HOH   G .   ? 0.2695 0.2310 0.2180 -0.0469 -0.0514 0.0288  259 HOH   B O   
6731 O  O   . HOH   G .   ? 0.2895 0.2528 0.1960 0.0196  -0.0205 0.0059  260 HOH   B O   
6732 O  O   . HOH   G .   ? 0.2564 0.2479 0.3823 -0.0212 -0.0441 -0.0281 261 HOH   B O   
6733 O  O   . HOH   G .   ? 0.4508 0.3466 0.3078 0.0713  -0.0576 -0.0991 262 HOH   B O   
6734 O  O   . HOH   G .   ? 0.2285 0.1808 0.2226 -0.0351 -0.0248 0.0183  263 HOH   B O   
6735 O  O   . HOH   G .   ? 0.2328 0.1637 0.4573 -0.0255 -0.0438 0.0197  264 HOH   B O   
6736 O  O   . HOH   G .   ? 0.2715 0.3231 0.3492 -0.0431 0.0575  -0.0787 265 HOH   B O   
6737 O  O   . HOH   G .   ? 0.4128 0.3266 0.4945 -0.0504 -0.0784 -0.0515 266 HOH   B O   
6738 O  O   . HOH   G .   ? 0.2414 0.3424 0.2627 -0.0468 0.0237  0.0573  267 HOH   B O   
6739 O  O   . HOH   G .   ? 0.3032 0.2652 0.4802 0.0394  0.0410  0.0539  268 HOH   B O   
6740 O  O   . HOH   G .   ? 0.2642 0.2506 0.2639 0.0841  -0.0753 -0.0615 269 HOH   B O   
6741 O  O   . HOH   G .   ? 0.3010 0.4423 0.5483 -0.0021 0.0623  -0.1076 270 HOH   B O   
6742 O  O   . HOH   G .   ? 0.2660 0.3083 0.2447 0.0750  -0.0088 -0.0085 271 HOH   B O   
6743 O  O   . HOH   G .   ? 0.4690 0.2985 0.3065 0.0445  0.0845  -0.0161 272 HOH   B O   
6744 O  O   . HOH   G .   ? 0.2953 0.2063 0.3204 -0.0628 0.0070  -0.0135 273 HOH   B O   
6745 O  O   . HOH   G .   ? 0.3033 0.5058 0.4097 -0.0675 -0.1229 0.1053  274 HOH   B O   
6746 O  O   . HOH   G .   ? 0.3215 0.2666 0.2853 -0.0507 -0.1023 0.0100  275 HOH   B O   
6747 O  O   . HOH   G .   ? 0.2630 0.3023 0.2755 -0.0562 -0.0853 -0.0386 276 HOH   B O   
6748 O  O   . HOH   G .   ? 0.5307 0.3636 0.5295 -0.1211 -0.0016 0.1483  277 HOH   B O   
6749 O  O   . HOH   G .   ? 0.2382 0.3689 0.4410 0.0204  0.0898  0.0142  278 HOH   B O   
6750 O  O   . HOH   G .   ? 0.2973 0.5060 0.4849 -0.0832 -0.1243 0.1032  279 HOH   B O   
6751 O  O   . HOH   G .   ? 0.2586 0.4853 0.5188 -0.0786 0.0042  -0.1398 280 HOH   B O   
6752 O  O   . HOH   G .   ? 0.1955 0.1894 0.3139 -0.0083 0.0137  -0.0075 281 HOH   B O   
6753 O  O   . HOH   G .   ? 0.3753 0.3548 0.2333 0.0707  -0.0564 0.0005  282 HOH   B O   
6754 O  O   . HOH   G .   ? 0.4205 0.5120 0.5565 -0.0227 -0.1204 -0.0102 283 HOH   B O   
6755 O  O   . HOH   G .   ? 0.3048 0.3243 0.5583 -0.0297 -0.0097 -0.0669 284 HOH   B O   
6756 O  O   . HOH   G .   ? 0.3639 0.3626 0.5119 0.0894  -0.0943 -0.0931 285 HOH   B O   
6757 O  O   . HOH   G .   ? 0.1810 0.2236 0.1702 -0.0138 -0.0281 -0.0029 286 HOH   B O   
6758 O  O   . HOH   G .   ? 0.1815 0.1854 0.1931 -0.0002 0.0048  0.0059  287 HOH   B O   
6759 O  O   . HOH   G .   ? 0.4031 0.7061 0.3032 -0.0727 -0.0904 0.1477  288 HOH   B O   
6760 O  O   . HOH   G .   ? 0.6321 0.4832 0.3300 0.3137  0.1246  0.1044  289 HOH   B O   
6761 O  O   . HOH   G .   ? 0.6752 0.6145 0.5347 -0.1407 0.0233  0.1384  290 HOH   B O   
6762 O  O   . HOH   G .   ? 0.2464 0.6935 0.7365 0.1064  -0.0506 -0.1522 291 HOH   B O   
6763 O  O   . HOH   G .   ? 0.1959 0.2316 0.2831 0.0131  0.0035  0.0082  292 HOH   B O   
6764 O  O   . HOH   G .   ? 0.3960 0.2561 0.4782 -0.0825 -0.2426 0.0805  293 HOH   B O   
6765 O  O   . HOH   G .   ? 0.2960 0.7128 0.2809 0.0639  -0.0288 -0.0296 294 HOH   B O   
6766 O  O   . HOH   G .   ? 0.3407 0.3222 0.3132 -0.0212 0.0098  -0.1546 295 HOH   B O   
6767 O  O   . HOH   G .   ? 0.3269 0.7149 0.3309 0.1544  -0.0082 0.0545  296 HOH   B O   
6768 O  O   . HOH   G .   ? 0.1959 0.3475 0.5323 0.0468  -0.0074 -0.1269 297 HOH   B O   
6769 O  O   . HOH   G .   ? 0.3218 0.2891 0.2855 0.0302  -0.0985 0.0161  298 HOH   B O   
6770 O  O   . HOH   G .   ? 0.3933 0.2166 0.3821 0.0842  0.1345  0.0422  299 HOH   B O   
6771 O  O   . HOH   G .   ? 0.4320 0.5081 0.6870 0.0195  -0.0484 0.0701  300 HOH   B O   
6772 O  O   . HOH   G .   ? 0.3418 0.3080 0.5233 0.0146  -0.0416 0.1316  301 HOH   B O   
6773 O  O   . HOH   G .   ? 0.1737 0.1945 0.2944 0.0057  0.0140  -0.0143 302 HOH   B O   
6774 O  O   . HOH   G .   ? 0.2649 0.4088 0.4825 -0.0361 -0.1218 0.1151  303 HOH   B O   
6775 O  O   . HOH   G .   ? 0.2021 0.1907 0.2588 0.0203  0.0119  0.0147  304 HOH   B O   
6776 O  O   . HOH   G .   ? 0.4777 0.4389 0.2612 0.1887  -0.0872 0.0094  305 HOH   B O   
6777 O  O   . HOH   G .   ? 0.4561 0.4293 0.2042 -0.0331 0.0456  0.0362  306 HOH   B O   
6778 O  O   . HOH   G .   ? 0.3489 0.3741 0.6733 0.0138  -0.0522 0.1892  307 HOH   B O   
6779 O  O   . HOH   G .   ? 0.2247 0.1894 0.2682 -0.0241 -0.0153 -0.0099 308 HOH   B O   
6780 O  O   . HOH   G .   ? 0.2095 0.1995 0.2922 -0.0327 -0.0292 0.0044  309 HOH   B O   
6781 O  O   . HOH   G .   ? 0.2937 0.2852 0.3816 -0.0363 0.1086  -0.0693 310 HOH   B O   
6782 O  O   . HOH   G .   ? 0.3483 0.3782 0.4523 -0.1110 0.1484  -0.1007 311 HOH   B O   
6783 O  O   . HOH   G .   ? 0.6000 0.3224 0.2655 -0.1756 0.0832  -0.0019 312 HOH   B O   
6784 O  O   . HOH   G .   ? 0.7451 0.4571 0.5398 0.1854  0.1003  -0.0457 313 HOH   B O   
6785 O  O   . HOH   G .   ? 0.2818 0.3314 0.5966 0.0757  -0.0512 -0.1094 314 HOH   B O   
6786 O  O   . HOH   G .   ? 0.5347 0.4271 0.2891 0.1456  -0.0821 -0.0392 315 HOH   B O   
6787 O  O   . HOH   G .   ? 0.2629 0.3712 0.5401 -0.0086 -0.0468 -0.0106 316 HOH   B O   
6788 O  O   . HOH   G .   ? 0.2753 0.1742 0.2736 -0.0100 -0.0066 0.0414  317 HOH   B O   
6789 O  O   . HOH   G .   ? 0.4188 0.3575 0.5583 0.0909  0.2089  0.1920  318 HOH   B O   
6790 O  O   . HOH   G .   ? 0.3109 0.2252 0.2660 0.0081  -0.0231 0.0148  319 HOH   B O   
6791 O  O   . HOH   G .   ? 0.2086 0.2120 0.3599 0.0367  -0.1020 -0.0022 320 HOH   B O   
6792 O  O   . HOH   G .   ? 0.2004 0.1936 0.2811 -0.0166 -0.0035 -0.0100 321 HOH   B O   
6793 O  O   . HOH   G .   ? 0.6773 0.6376 0.5346 0.3057  0.0041  0.0135  322 HOH   B O   
6794 O  O   . HOH   G .   ? 0.4641 0.2574 0.3084 0.0176  0.0333  0.0919  323 HOH   B O   
6795 O  O   . HOH   G .   ? 0.5231 0.4998 0.2440 0.0495  -0.0599 -0.0721 324 HOH   B O   
6796 O  O   . HOH   G .   ? 0.2316 0.2078 0.2180 -0.0039 0.0137  0.0209  325 HOH   B O   
6797 O  O   . HOH   G .   ? 0.8224 0.2522 0.3221 -0.0120 -0.0287 0.0242  326 HOH   B O   
6798 O  O   . HOH   G .   ? 0.4684 0.3085 0.2639 0.1980  0.1051  0.0623  327 HOH   B O   
6799 O  O   . HOH   G .   ? 0.2190 0.2269 0.3163 0.0423  0.0472  0.0279  328 HOH   B O   
6800 O  O   . HOH   G .   ? 0.5136 0.5435 0.3382 0.0133  -0.0783 0.0146  329 HOH   B O   
6801 O  O   . HOH   G .   ? 0.2210 0.3098 0.2452 -0.0123 -0.0286 0.0560  330 HOH   B O   
6802 O  O   . HOH   G .   ? 0.3036 0.2388 0.5154 -0.0293 -0.0130 0.0318  331 HOH   B O   
6803 O  O   . HOH   G .   ? 0.5984 0.5036 0.6555 0.0747  -0.1278 0.1838  332 HOH   B O   
6804 O  O   . HOH   G .   ? 0.2502 0.5869 0.5375 -0.0679 -0.0006 -0.0311 333 HOH   B O   
6805 O  O   . HOH   G .   ? 0.6668 0.3916 0.3613 -0.0512 0.1166  0.1159  334 HOH   B O   
6806 O  O   . HOH   G .   ? 0.2285 0.2730 0.5876 -0.0572 -0.0093 0.1470  335 HOH   B O   
6807 O  O   . HOH   G .   ? 0.2171 0.3274 0.2960 0.0520  -0.0137 -0.0450 336 HOH   B O   
6808 O  O   . HOH   G .   ? 0.6389 0.4400 0.6371 -0.0589 -0.0309 -0.1506 337 HOH   B O   
6809 O  O   . HOH   G .   ? 0.2024 0.1755 0.2562 0.0064  -0.0344 -0.0011 338 HOH   B O   
6810 O  O   . HOH   G .   ? 0.5083 0.3393 0.3732 0.0528  -0.1233 -0.0499 339 HOH   B O   
6811 O  O   . HOH   G .   ? 0.4843 0.3875 0.4501 0.0773  0.0181  -0.1463 340 HOH   B O   
6812 O  O   . HOH   G .   ? 0.4606 0.6784 0.3491 0.0517  -0.0095 0.1255  341 HOH   B O   
6813 O  O   . HOH   G .   ? 0.4212 0.6070 0.4461 -0.1254 -0.1224 -0.0691 342 HOH   B O   
6814 O  O   . HOH   G .   ? 0.2110 0.5719 0.6045 -0.0056 0.0739  0.0256  343 HOH   B O   
6815 O  O   . HOH   G .   ? 0.2421 0.2291 0.3053 -0.0004 0.0521  -0.0228 344 HOH   B O   
6816 O  O   . HOH   G .   ? 0.4482 0.5513 0.5131 0.0796  -0.0555 0.0416  345 HOH   B O   
6817 O  O   . HOH   G .   ? 0.6269 0.6049 0.2543 -0.0215 -0.0108 0.1063  346 HOH   B O   
6818 O  O   . HOH   G .   ? 0.5621 0.5399 0.4754 -0.0836 0.0311  0.1196  347 HOH   B O   
6819 O  O   . HOH   G .   ? 0.2294 0.4200 0.6056 0.0019  0.0449  0.0139  348 HOH   B O   
6820 O  O   . HOH   G .   ? 0.3764 0.2088 0.3634 -0.0486 0.0032  -0.0597 349 HOH   B O   
6821 O  O   . HOH   G .   ? 0.4839 0.6138 0.6553 -0.0337 0.0365  -0.1122 350 HOH   B O   
6822 O  O   . HOH   G .   ? 0.2340 0.6686 0.3741 0.1434  -0.0439 -0.1355 351 HOH   B O   
6823 O  O   . HOH   G .   ? 0.3128 0.2786 0.5710 -0.0379 -0.1047 -0.0712 352 HOH   B O   
6824 O  O   . HOH   G .   ? 0.4311 0.4075 0.5250 -0.1871 0.0160  -0.0008 353 HOH   B O   
6825 O  O   . HOH   G .   ? 0.4494 0.2858 0.5545 -0.0739 0.0997  0.0516  354 HOH   B O   
6826 O  O   . HOH   G .   ? 0.3497 0.2801 0.4685 -0.0524 -0.0175 -0.0678 355 HOH   B O   
6827 O  O   . HOH   G .   ? 0.5691 0.3873 0.4332 0.0572  0.1464  -0.0511 356 HOH   B O   
6828 O  O   . HOH   G .   ? 0.4779 0.5356 0.5693 -0.0150 -0.0330 0.0487  357 HOH   B O   
6829 O  O   . HOH   G .   ? 0.4460 0.3999 0.5305 0.0126  -0.1950 -0.0224 358 HOH   B O   
6830 O  O   . HOH   G .   ? 0.3427 0.2425 0.4585 0.0640  -0.1393 -0.0670 359 HOH   B O   
6831 O  O   . HOH   G .   ? 0.4731 0.5340 0.6168 0.1789  -0.1194 0.1964  360 HOH   B O   
6832 O  O   . HOH   G .   ? 0.3863 0.7481 0.3757 0.2109  0.0009  0.0592  361 HOH   B O   
6833 O  O   . HOH   G .   ? 0.2909 0.3819 0.6781 -0.0613 -0.0576 -0.0924 362 HOH   B O   
6834 O  O   . HOH   G .   ? 0.5511 0.4322 0.6696 0.0656  0.1172  0.1343  363 HOH   B O   
6835 O  O   . HOH   G .   ? 0.6091 0.4568 0.4996 0.0350  0.1043  0.0172  364 HOH   B O   
6836 O  O   . HOH   G .   ? 0.5604 0.5510 0.4945 -0.0394 -0.1046 -0.1245 365 HOH   B O   
6837 O  O   . HOH   G .   ? 0.5435 0.3350 0.6213 -0.1353 -0.1124 0.0370  366 HOH   B O   
6838 O  O   . HOH   G .   ? 0.5211 0.3788 0.5606 0.1258  -0.1786 -0.0110 367 HOH   B O   
6839 O  O   . HOH   G .   ? 0.7979 0.8422 0.5565 0.2702  -0.1564 0.1016  368 HOH   B O   
6840 O  O   . HOH   G .   ? 0.6442 0.2632 0.3107 0.0437  0.0471  0.0929  369 HOH   B O   
6841 O  O   . HOH   G .   ? 0.5168 0.5685 0.3812 0.0597  -0.1625 0.0454  370 HOH   B O   
6842 O  O   . HOH   G .   ? 0.4720 0.5429 0.5859 0.2035  0.0403  0.0609  371 HOH   B O   
6843 O  O   . HOH   G .   ? 0.2622 0.4431 0.4684 0.0021  -0.0581 -0.0150 372 HOH   B O   
6844 O  O   . HOH   G .   ? 0.6450 0.4021 0.3332 -0.1269 -0.0998 -0.0434 373 HOH   B O   
6845 O  O   . HOH   G .   ? 0.4076 0.4211 0.4753 0.0506  -0.1049 -0.0352 374 HOH   B O   
6846 O  O   . HOH   G .   ? 0.5027 0.4905 0.5679 -0.0875 -0.0668 0.0336  375 HOH   B O   
6847 O  O   . HOH   G .   ? 0.5367 0.7580 0.6212 0.1620  0.0694  0.2972  376 HOH   B O   
6848 O  O   . HOH   G .   ? 0.6672 0.3696 0.6003 -0.1024 -0.0441 0.0357  377 HOH   B O   
6849 O  O   . HOH   G .   ? 0.3592 0.3759 0.2676 0.0824  0.0382  0.0147  378 HOH   B O   
6850 O  O   . HOH   G .   ? 0.5489 0.7473 0.4632 -0.1633 0.0484  -0.1717 379 HOH   B O   
6851 O  O   . HOH   G .   ? 0.3275 0.4189 0.5480 0.0842  -0.0434 -0.0344 380 HOH   B O   
6852 O  O   . HOH   G .   ? 0.3298 0.2993 0.3770 -0.0054 0.0323  0.0248  381 HOH   B O   
6853 O  O   . HOH   G .   ? 0.3505 0.7722 0.5559 0.0844  0.1545  0.1356  382 HOH   B O   
6854 O  O   . HOH   G .   ? 0.5241 0.7499 0.6196 0.0442  0.2519  0.1474  383 HOH   B O   
6855 O  O   . HOH   G .   ? 0.6052 0.4470 0.5655 -0.0292 0.0480  -0.0130 384 HOH   B O   
6856 O  O   . HOH   G .   ? 0.2793 0.4754 0.3635 -0.0643 -0.0979 -0.0179 385 HOH   B O   
6857 O  O   . HOH   G .   ? 0.4966 0.4909 0.4884 0.0053  -0.0583 -0.0883 386 HOH   B O   
6858 O  O   . HOH   G .   ? 0.7492 0.4055 0.5058 0.0754  0.0743  -0.0616 387 HOH   B O   
6859 O  O   . HOH   G .   ? 0.7655 0.6479 0.4101 0.2543  0.0757  0.0971  388 HOH   B O   
6860 O  O   . HOH   G .   ? 0.4215 0.3866 0.3469 0.0121  0.0180  -0.0172 389 HOH   B O   
6861 O  O   . HOH   G .   ? 0.4340 0.2524 0.3436 0.0581  -0.0513 0.0176  390 HOH   B O   
6862 O  O   . HOH   G .   ? 0.5151 0.4555 0.3549 0.0044  0.0045  0.0568  391 HOH   B O   
6863 O  O   . HOH   G .   ? 0.2854 0.4749 0.6739 -0.1050 -0.0195 0.0358  392 HOH   B O   
6864 O  O   . HOH   G .   ? 0.5034 0.2577 0.5569 -0.0539 0.0805  0.0782  393 HOH   B O   
6865 O  O   . HOH   G .   ? 0.3698 0.3836 0.3710 0.0501  0.0323  -0.0392 394 HOH   B O   
6866 O  O   . HOH   G .   ? 0.4397 0.6315 0.3291 0.1412  -0.0374 -0.0434 395 HOH   B O   
6867 O  O   . HOH   G .   ? 0.4594 0.4300 0.4629 -0.0077 0.1020  0.1051  396 HOH   B O   
6868 O  O   . HOH   G .   ? 0.2911 0.3318 0.5714 -0.0637 -0.1019 -0.0301 397 HOH   B O   
6869 O  O   . HOH   G .   ? 0.5944 0.7338 0.7598 0.1673  -0.1179 0.1767  398 HOH   B O   
6870 O  O   . HOH   G .   ? 0.5713 0.4579 0.3383 -0.2425 -0.0506 0.1328  399 HOH   B O   
6871 O  O   . HOH   G .   ? 0.6833 0.6419 0.4158 0.1754  0.0056  0.0131  400 HOH   B O   
# 
