data_7HDS
# 
_entry.id   7HDS 
# 
_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   7HDS         pdb_00007hds 10.2210/pdb7hds/pdb 
WWPDB D_1001407346 ?            ?                   
# 
_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                        7HDS 
_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)-3-cyclobutyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' 246.308   1   ?                      ? 
? ?                                                                                    
4 non-polymer syn 'CHLORIDE ION'                                                            35.453    1   ?                      ? 
? ?                                                                                    
5 water       nat water                                                                     18.015    415 ?                      ? 
? ?                                                                                    
# 
_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)-3-cyclobutyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' A1A81 
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 
A1A81 non-polymer         . '(2S)-3-cyclobutyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' ? 'C13 H18 N4 O'   246.308 
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 A1A81 1   202 201  A1A81 LA1 A . 
E 4 CL    1   203 1    CL    CL  A . 
F 5 HOH   1   301 196  HOH   HOH A . 
F 5 HOH   2   302 292  HOH   HOH A . 
F 5 HOH   3   303 153  HOH   HOH A . 
F 5 HOH   4   304 136  HOH   HOH A . 
F 5 HOH   5   305 86   HOH   HOH A . 
F 5 HOH   6   306 229  HOH   HOH A . 
F 5 HOH   7   307 1289 HOH   HOH A . 
F 5 HOH   8   308 625  HOH   HOH A . 
F 5 HOH   9   309 405  HOH   HOH A . 
F 5 HOH   10  310 493  HOH   HOH A . 
F 5 HOH   11  311 209  HOH   HOH A . 
F 5 HOH   12  312 1301 HOH   HOH A . 
F 5 HOH   13  313 148  HOH   HOH A . 
F 5 HOH   14  314 109  HOH   HOH A . 
F 5 HOH   15  315 1295 HOH   HOH A . 
F 5 HOH   16  316 1283 HOH   HOH A . 
F 5 HOH   17  317 124  HOH   HOH A . 
F 5 HOH   18  318 76   HOH   HOH A . 
F 5 HOH   19  319 192  HOH   HOH A . 
F 5 HOH   20  320 661  HOH   HOH A . 
F 5 HOH   21  321 151  HOH   HOH A . 
F 5 HOH   22  322 236  HOH   HOH A . 
F 5 HOH   23  323 1290 HOH   HOH A . 
F 5 HOH   24  324 409  HOH   HOH A . 
F 5 HOH   25  325 21   HOH   HOH A . 
F 5 HOH   26  326 469  HOH   HOH A . 
F 5 HOH   27  327 105  HOH   HOH A . 
F 5 HOH   28  328 247  HOH   HOH A . 
F 5 HOH   29  329 15   HOH   HOH A . 
F 5 HOH   30  330 225  HOH   HOH A . 
F 5 HOH   31  331 155  HOH   HOH A . 
F 5 HOH   32  332 57   HOH   HOH A . 
F 5 HOH   33  333 1300 HOH   HOH A . 
F 5 HOH   34  334 393  HOH   HOH A . 
F 5 HOH   35  335 18   HOH   HOH A . 
F 5 HOH   36  336 320  HOH   HOH A . 
F 5 HOH   37  337 140  HOH   HOH A . 
F 5 HOH   38  338 241  HOH   HOH A . 
F 5 HOH   39  339 164  HOH   HOH A . 
F 5 HOH   40  340 165  HOH   HOH A . 
F 5 HOH   41  341 630  HOH   HOH A . 
F 5 HOH   42  342 74   HOH   HOH A . 
F 5 HOH   43  343 17   HOH   HOH A . 
F 5 HOH   44  344 92   HOH   HOH A . 
F 5 HOH   45  345 1310 HOH   HOH A . 
F 5 HOH   46  346 7    HOH   HOH A . 
F 5 HOH   47  347 39   HOH   HOH A . 
F 5 HOH   48  348 354  HOH   HOH A . 
F 5 HOH   49  349 42   HOH   HOH A . 
F 5 HOH   50  350 337  HOH   HOH A . 
F 5 HOH   51  351 66   HOH   HOH A . 
F 5 HOH   52  352 93   HOH   HOH A . 
F 5 HOH   53  353 964  HOH   HOH A . 
F 5 HOH   54  354 33   HOH   HOH A . 
F 5 HOH   55  355 81   HOH   HOH A . 
F 5 HOH   56  356 169  HOH   HOH A . 
F 5 HOH   57  357 396  HOH   HOH A . 
F 5 HOH   58  358 19   HOH   HOH A . 
F 5 HOH   59  359 2    HOH   HOH A . 
F 5 HOH   60  360 162  HOH   HOH A . 
F 5 HOH   61  361 159  HOH   HOH A . 
F 5 HOH   62  362 102  HOH   HOH A . 
F 5 HOH   63  363 366  HOH   HOH A . 
F 5 HOH   64  364 139  HOH   HOH A . 
F 5 HOH   65  365 85   HOH   HOH A . 
F 5 HOH   66  366 45   HOH   HOH A . 
F 5 HOH   67  367 5    HOH   HOH A . 
F 5 HOH   68  368 26   HOH   HOH A . 
F 5 HOH   69  369 939  HOH   HOH A . 
F 5 HOH   70  370 138  HOH   HOH A . 
F 5 HOH   71  371 49   HOH   HOH A . 
F 5 HOH   72  372 27   HOH   HOH A . 
F 5 HOH   73  373 1275 HOH   HOH A . 
F 5 HOH   74  374 662  HOH   HOH A . 
F 5 HOH   75  375 56   HOH   HOH A . 
F 5 HOH   76  376 1    HOH   HOH A . 
F 5 HOH   77  377 62   HOH   HOH A . 
F 5 HOH   78  378 1308 HOH   HOH A . 
F 5 HOH   79  379 36   HOH   HOH A . 
F 5 HOH   80  380 46   HOH   HOH A . 
F 5 HOH   81  381 218  HOH   HOH A . 
F 5 HOH   82  382 4    HOH   HOH A . 
F 5 HOH   83  383 186  HOH   HOH A . 
F 5 HOH   84  384 140  HOH   HOH A . 
F 5 HOH   85  385 115  HOH   HOH A . 
F 5 HOH   86  386 134  HOH   HOH A . 
F 5 HOH   87  387 24   HOH   HOH A . 
F 5 HOH   88  388 35   HOH   HOH A . 
F 5 HOH   89  389 154  HOH   HOH A . 
F 5 HOH   90  390 333  HOH   HOH A . 
F 5 HOH   91  391 296  HOH   HOH A . 
F 5 HOH   92  392 461  HOH   HOH A . 
F 5 HOH   93  393 6    HOH   HOH A . 
F 5 HOH   94  394 34   HOH   HOH A . 
F 5 HOH   95  395 6    HOH   HOH A . 
F 5 HOH   96  396 4    HOH   HOH A . 
F 5 HOH   97  397 116  HOH   HOH A . 
F 5 HOH   98  398 195  HOH   HOH A . 
F 5 HOH   99  399 58   HOH   HOH A . 
F 5 HOH   100 400 12   HOH   HOH A . 
F 5 HOH   101 401 1315 HOH   HOH A . 
F 5 HOH   102 402 281  HOH   HOH A . 
F 5 HOH   103 403 121  HOH   HOH A . 
F 5 HOH   104 404 199  HOH   HOH A . 
F 5 HOH   105 405 83   HOH   HOH A . 
F 5 HOH   106 406 96   HOH   HOH A . 
F 5 HOH   107 407 67   HOH   HOH A . 
F 5 HOH   108 408 351  HOH   HOH A . 
F 5 HOH   109 409 278  HOH   HOH A . 
F 5 HOH   110 410 303  HOH   HOH A . 
F 5 HOH   111 411 125  HOH   HOH A . 
F 5 HOH   112 412 123  HOH   HOH A . 
F 5 HOH   113 413 1279 HOH   HOH A . 
F 5 HOH   114 414 1068 HOH   HOH A . 
F 5 HOH   115 415 25   HOH   HOH A . 
F 5 HOH   116 416 381  HOH   HOH A . 
F 5 HOH   117 417 3    HOH   HOH A . 
F 5 HOH   118 418 68   HOH   HOH A . 
F 5 HOH   119 419 1313 HOH   HOH A . 
F 5 HOH   120 420 51   HOH   HOH A . 
F 5 HOH   121 421 132  HOH   HOH A . 
F 5 HOH   122 422 122  HOH   HOH A . 
F 5 HOH   123 423 156  HOH   HOH A . 
F 5 HOH   124 424 53   HOH   HOH A . 
F 5 HOH   125 425 397  HOH   HOH A . 
F 5 HOH   126 426 8    HOH   HOH A . 
F 5 HOH   127 427 95   HOH   HOH A . 
F 5 HOH   128 428 70   HOH   HOH A . 
F 5 HOH   129 429 78   HOH   HOH A . 
F 5 HOH   130 430 582  HOH   HOH A . 
F 5 HOH   131 431 7    HOH   HOH A . 
F 5 HOH   132 432 1222 HOH   HOH A . 
F 5 HOH   133 433 1296 HOH   HOH A . 
F 5 HOH   134 434 71   HOH   HOH A . 
F 5 HOH   135 435 1238 HOH   HOH A . 
F 5 HOH   136 436 944  HOH   HOH A . 
F 5 HOH   137 437 5    HOH   HOH A . 
F 5 HOH   138 438 40   HOH   HOH A . 
F 5 HOH   139 439 80   HOH   HOH A . 
F 5 HOH   140 440 188  HOH   HOH A . 
F 5 HOH   141 441 1309 HOH   HOH A . 
F 5 HOH   142 442 212  HOH   HOH A . 
F 5 HOH   143 443 73   HOH   HOH A . 
F 5 HOH   144 444 1286 HOH   HOH A . 
F 5 HOH   145 445 94   HOH   HOH A . 
F 5 HOH   146 446 16   HOH   HOH A . 
F 5 HOH   147 447 952  HOH   HOH A . 
F 5 HOH   148 448 79   HOH   HOH A . 
F 5 HOH   149 449 104  HOH   HOH A . 
F 5 HOH   150 450 1094 HOH   HOH A . 
F 5 HOH   151 451 97   HOH   HOH A . 
F 5 HOH   152 452 1189 HOH   HOH A . 
F 5 HOH   153 453 576  HOH   HOH A . 
F 5 HOH   154 454 1134 HOH   HOH A . 
F 5 HOH   155 455 330  HOH   HOH A . 
F 5 HOH   156 456 509  HOH   HOH A . 
F 5 HOH   157 457 1119 HOH   HOH A . 
F 5 HOH   158 458 107  HOH   HOH A . 
F 5 HOH   159 459 726  HOH   HOH A . 
F 5 HOH   160 460 163  HOH   HOH A . 
F 5 HOH   161 461 408  HOH   HOH A . 
F 5 HOH   162 462 756  HOH   HOH A . 
F 5 HOH   163 463 126  HOH   HOH A . 
F 5 HOH   164 464 319  HOH   HOH A . 
F 5 HOH   165 465 361  HOH   HOH A . 
F 5 HOH   166 466 280  HOH   HOH A . 
F 5 HOH   167 467 556  HOH   HOH A . 
F 5 HOH   168 468 801  HOH   HOH A . 
F 5 HOH   169 469 1276 HOH   HOH A . 
F 5 HOH   170 470 1307 HOH   HOH A . 
F 5 HOH   171 471 342  HOH   HOH A . 
F 5 HOH   172 472 63   HOH   HOH A . 
F 5 HOH   173 473 250  HOH   HOH A . 
F 5 HOH   174 474 370  HOH   HOH A . 
F 5 HOH   175 475 224  HOH   HOH A . 
F 5 HOH   176 476 202  HOH   HOH A . 
F 5 HOH   177 477 695  HOH   HOH A . 
F 5 HOH   178 478 267  HOH   HOH A . 
F 5 HOH   179 479 1287 HOH   HOH A . 
F 5 HOH   180 480 135  HOH   HOH A . 
F 5 HOH   181 481 1306 HOH   HOH A . 
F 5 HOH   182 482 919  HOH   HOH A . 
F 5 HOH   183 483 674  HOH   HOH A . 
F 5 HOH   184 484 521  HOH   HOH A . 
F 5 HOH   185 485 318  HOH   HOH A . 
F 5 HOH   186 486 1299 HOH   HOH A . 
F 5 HOH   187 487 1314 HOH   HOH A . 
F 5 HOH   188 488 309  HOH   HOH A . 
F 5 HOH   189 489 331  HOH   HOH A . 
F 5 HOH   190 490 805  HOH   HOH A . 
F 5 HOH   191 491 315  HOH   HOH A . 
F 5 HOH   192 492 941  HOH   HOH A . 
F 5 HOH   193 493 1284 HOH   HOH A . 
F 5 HOH   194 494 711  HOH   HOH A . 
F 5 HOH   195 495 263  HOH   HOH A . 
F 5 HOH   196 496 208  HOH   HOH A . 
F 5 HOH   197 497 152  HOH   HOH A . 
F 5 HOH   198 498 3    HOH   HOH A . 
F 5 HOH   199 499 326  HOH   HOH A . 
F 5 HOH   200 500 1071 HOH   HOH A . 
F 5 HOH   201 501 180  HOH   HOH A . 
F 5 HOH   202 502 350  HOH   HOH A . 
F 5 HOH   203 503 363  HOH   HOH A . 
F 5 HOH   204 504 313  HOH   HOH A . 
F 5 HOH   205 505 356  HOH   HOH A . 
F 5 HOH   206 506 371  HOH   HOH A . 
F 5 HOH   207 507 185  HOH   HOH A . 
F 5 HOH   208 508 429  HOH   HOH A . 
F 5 HOH   209 509 70   HOH   HOH A . 
F 5 HOH   210 510 376  HOH   HOH A . 
F 5 HOH   211 511 772  HOH   HOH A . 
F 5 HOH   212 512 1074 HOH   HOH A . 
F 5 HOH   213 513 1292 HOH   HOH A . 
F 5 HOH   214 514 346  HOH   HOH A . 
F 5 HOH   215 515 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 549  HOH   HOH B . 
G 5 HOH   3   203 240  HOH   HOH B . 
G 5 HOH   4   204 758  HOH   HOH B . 
G 5 HOH   5   205 364  HOH   HOH B . 
G 5 HOH   6   206 358  HOH   HOH B . 
G 5 HOH   7   207 1249 HOH   HOH B . 
G 5 HOH   8   208 654  HOH   HOH B . 
G 5 HOH   9   209 232  HOH   HOH B . 
G 5 HOH   10  210 398  HOH   HOH B . 
G 5 HOH   11  211 900  HOH   HOH B . 
G 5 HOH   12  212 531  HOH   HOH B . 
G 5 HOH   13  213 452  HOH   HOH B . 
G 5 HOH   14  214 353  HOH   HOH B . 
G 5 HOH   15  215 205  HOH   HOH B . 
G 5 HOH   16  216 743  HOH   HOH B . 
G 5 HOH   17  217 120  HOH   HOH B . 
G 5 HOH   18  218 50   HOH   HOH B . 
G 5 HOH   19  219 1140 HOH   HOH B . 
G 5 HOH   20  220 264  HOH   HOH B . 
G 5 HOH   21  221 1278 HOH   HOH B . 
G 5 HOH   22  222 75   HOH   HOH B . 
G 5 HOH   23  223 343  HOH   HOH B . 
G 5 HOH   24  224 444  HOH   HOH B . 
G 5 HOH   25  225 332  HOH   HOH B . 
G 5 HOH   26  226 82   HOH   HOH B . 
G 5 HOH   27  227 723  HOH   HOH B . 
G 5 HOH   28  228 131  HOH   HOH B . 
G 5 HOH   29  229 69   HOH   HOH B . 
G 5 HOH   30  230 282  HOH   HOH B . 
G 5 HOH   31  231 300  HOH   HOH B . 
G 5 HOH   32  232 172  HOH   HOH B . 
G 5 HOH   33  233 54   HOH   HOH B . 
G 5 HOH   34  234 60   HOH   HOH B . 
G 5 HOH   35  235 1    HOH   HOH B . 
G 5 HOH   36  236 110  HOH   HOH B . 
G 5 HOH   37  237 127  HOH   HOH B . 
G 5 HOH   38  238 272  HOH   HOH B . 
G 5 HOH   39  239 128  HOH   HOH B . 
G 5 HOH   40  240 325  HOH   HOH B . 
G 5 HOH   41  241 1312 HOH   HOH B . 
G 5 HOH   42  242 14   HOH   HOH B . 
G 5 HOH   43  243 133  HOH   HOH B . 
G 5 HOH   44  244 30   HOH   HOH B . 
G 5 HOH   45  245 166  HOH   HOH B . 
G 5 HOH   46  246 276  HOH   HOH B . 
G 5 HOH   47  247 391  HOH   HOH B . 
G 5 HOH   48  248 181  HOH   HOH B . 
G 5 HOH   49  249 129  HOH   HOH B . 
G 5 HOH   50  250 144  HOH   HOH B . 
G 5 HOH   51  251 9    HOH   HOH B . 
G 5 HOH   52  252 231  HOH   HOH B . 
G 5 HOH   53  253 252  HOH   HOH B . 
G 5 HOH   54  254 143  HOH   HOH B . 
G 5 HOH   55  255 52   HOH   HOH B . 
G 5 HOH   56  256 31   HOH   HOH B . 
G 5 HOH   57  257 72   HOH   HOH B . 
G 5 HOH   58  258 41   HOH   HOH B . 
G 5 HOH   59  259 150  HOH   HOH B . 
G 5 HOH   60  260 147  HOH   HOH B . 
G 5 HOH   61  261 271  HOH   HOH B . 
G 5 HOH   62  262 47   HOH   HOH B . 
G 5 HOH   63  263 242  HOH   HOH B . 
G 5 HOH   64  264 302  HOH   HOH B . 
G 5 HOH   65  265 347  HOH   HOH B . 
G 5 HOH   66  266 10   HOH   HOH B . 
G 5 HOH   67  267 103  HOH   HOH B . 
G 5 HOH   68  268 61   HOH   HOH B . 
G 5 HOH   69  269 20   HOH   HOH B . 
G 5 HOH   70  270 221  HOH   HOH B . 
G 5 HOH   71  271 59   HOH   HOH B . 
G 5 HOH   72  272 117  HOH   HOH B . 
G 5 HOH   73  273 243  HOH   HOH B . 
G 5 HOH   74  274 287  HOH   HOH B . 
G 5 HOH   75  275 1277 HOH   HOH B . 
G 5 HOH   76  276 11   HOH   HOH B . 
G 5 HOH   77  277 77   HOH   HOH B . 
G 5 HOH   78  278 114  HOH   HOH B . 
G 5 HOH   79  279 84   HOH   HOH B . 
G 5 HOH   80  280 43   HOH   HOH B . 
G 5 HOH   81  281 216  HOH   HOH B . 
G 5 HOH   82  282 175  HOH   HOH B . 
G 5 HOH   83  283 1305 HOH   HOH B . 
G 5 HOH   84  284 22   HOH   HOH B . 
G 5 HOH   85  285 220  HOH   HOH B . 
G 5 HOH   86  286 1066 HOH   HOH B . 
G 5 HOH   87  287 106  HOH   HOH B . 
G 5 HOH   88  288 235  HOH   HOH B . 
G 5 HOH   89  289 99   HOH   HOH B . 
G 5 HOH   90  290 89   HOH   HOH B . 
G 5 HOH   91  291 88   HOH   HOH B . 
G 5 HOH   92  292 13   HOH   HOH B . 
G 5 HOH   93  293 311  HOH   HOH B . 
G 5 HOH   94  294 137  HOH   HOH B . 
G 5 HOH   95  295 112  HOH   HOH B . 
G 5 HOH   96  296 160  HOH   HOH B . 
G 5 HOH   97  297 416  HOH   HOH B . 
G 5 HOH   98  298 1106 HOH   HOH B . 
G 5 HOH   99  299 299  HOH   HOH B . 
G 5 HOH   100 300 316  HOH   HOH B . 
G 5 HOH   101 301 297  HOH   HOH B . 
G 5 HOH   102 302 387  HOH   HOH B . 
G 5 HOH   103 303 118  HOH   HOH B . 
G 5 HOH   104 304 1285 HOH   HOH B . 
G 5 HOH   105 305 101  HOH   HOH B . 
G 5 HOH   106 306 142  HOH   HOH B . 
G 5 HOH   107 307 635  HOH   HOH B . 
G 5 HOH   108 308 215  HOH   HOH B . 
G 5 HOH   109 309 38   HOH   HOH B . 
G 5 HOH   110 310 37   HOH   HOH B . 
G 5 HOH   111 311 32   HOH   HOH B . 
G 5 HOH   112 312 170  HOH   HOH B . 
G 5 HOH   113 313 23   HOH   HOH B . 
G 5 HOH   114 314 341  HOH   HOH B . 
G 5 HOH   115 315 48   HOH   HOH B . 
G 5 HOH   116 316 161  HOH   HOH B . 
G 5 HOH   117 317 1274 HOH   HOH B . 
G 5 HOH   118 318 207  HOH   HOH B . 
G 5 HOH   119 319 91   HOH   HOH B . 
G 5 HOH   120 320 28   HOH   HOH B . 
G 5 HOH   121 321 177  HOH   HOH B . 
G 5 HOH   122 322 197  HOH   HOH B . 
G 5 HOH   123 323 44   HOH   HOH B . 
G 5 HOH   124 324 704  HOH   HOH B . 
G 5 HOH   125 325 182  HOH   HOH B . 
G 5 HOH   126 326 29   HOH   HOH B . 
G 5 HOH   127 327 100  HOH   HOH B . 
G 5 HOH   128 328 1294 HOH   HOH B . 
G 5 HOH   129 329 141  HOH   HOH B . 
G 5 HOH   130 330 98   HOH   HOH B . 
G 5 HOH   131 331 55   HOH   HOH B . 
G 5 HOH   132 332 1291 HOH   HOH B . 
G 5 HOH   133 333 334  HOH   HOH B . 
G 5 HOH   134 334 717  HOH   HOH B . 
G 5 HOH   135 335 1126 HOH   HOH B . 
G 5 HOH   136 336 65   HOH   HOH B . 
G 5 HOH   137 337 1293 HOH   HOH B . 
G 5 HOH   138 338 234  HOH   HOH B . 
G 5 HOH   139 339 445  HOH   HOH B . 
G 5 HOH   140 340 619  HOH   HOH B . 
G 5 HOH   141 341 960  HOH   HOH B . 
G 5 HOH   142 342 178  HOH   HOH B . 
G 5 HOH   143 343 362  HOH   HOH B . 
G 5 HOH   144 344 339  HOH   HOH B . 
G 5 HOH   145 345 87   HOH   HOH B . 
G 5 HOH   146 346 90   HOH   HOH B . 
G 5 HOH   147 347 1304 HOH   HOH B . 
G 5 HOH   148 348 335  HOH   HOH B . 
G 5 HOH   149 349 463  HOH   HOH B . 
G 5 HOH   150 350 191  HOH   HOH B . 
G 5 HOH   151 351 623  HOH   HOH B . 
G 5 HOH   152 352 1046 HOH   HOH B . 
G 5 HOH   153 353 304  HOH   HOH B . 
G 5 HOH   154 354 1280 HOH   HOH B . 
G 5 HOH   155 355 541  HOH   HOH B . 
G 5 HOH   156 356 203  HOH   HOH B . 
G 5 HOH   157 357 290  HOH   HOH B . 
G 5 HOH   158 358 1077 HOH   HOH B . 
G 5 HOH   159 359 718  HOH   HOH B . 
G 5 HOH   160 360 389  HOH   HOH B . 
G 5 HOH   161 361 1072 HOH   HOH B . 
G 5 HOH   162 362 283  HOH   HOH B . 
G 5 HOH   163 363 479  HOH   HOH B . 
G 5 HOH   164 364 1316 HOH   HOH B . 
G 5 HOH   165 365 291  HOH   HOH B . 
G 5 HOH   166 366 898  HOH   HOH B . 
G 5 HOH   167 367 615  HOH   HOH B . 
G 5 HOH   168 368 340  HOH   HOH B . 
G 5 HOH   169 369 373  HOH   HOH B . 
G 5 HOH   170 370 667  HOH   HOH B . 
G 5 HOH   171 371 190  HOH   HOH B . 
G 5 HOH   172 372 310  HOH   HOH B . 
G 5 HOH   173 373 1303 HOH   HOH B . 
G 5 HOH   174 374 431  HOH   HOH B . 
G 5 HOH   175 375 149  HOH   HOH B . 
G 5 HOH   176 376 183  HOH   HOH B . 
G 5 HOH   177 377 1173 HOH   HOH B . 
G 5 HOH   178 378 1163 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 1311 HOH   HOH B . 
G 5 HOH   182 382 176  HOH   HOH B . 
G 5 HOH   183 383 981  HOH   HOH B . 
G 5 HOH   184 384 491  HOH   HOH B . 
G 5 HOH   185 385 424  HOH   HOH B . 
G 5 HOH   186 386 248  HOH   HOH B . 
G 5 HOH   187 387 265  HOH   HOH B . 
G 5 HOH   188 388 470  HOH   HOH B . 
G 5 HOH   189 389 1298 HOH   HOH B . 
G 5 HOH   190 390 184  HOH   HOH B . 
G 5 HOH   191 391 360  HOH   HOH B . 
G 5 HOH   192 392 410  HOH   HOH B . 
G 5 HOH   193 393 355  HOH   HOH B . 
G 5 HOH   194 394 274  HOH   HOH B . 
G 5 HOH   195 395 314  HOH   HOH B . 
G 5 HOH   196 396 566  HOH   HOH B . 
G 5 HOH   197 397 157  HOH   HOH B . 
G 5 HOH   198 398 321  HOH   HOH B . 
G 5 HOH   199 399 792  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           7HDS 
_cell.length_a           88.796 
_cell.length_b           88.796 
_cell.length_c           39.521 
_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                         7HDS 
_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          7HDS 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.7 
_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                     7HDS 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.400 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   156305 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.800 
_reflns.pdbx_Rmerge_I_obs            0.040 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.800 
_reflns.B_iso_Wilson_estimate        12.320 
_reflns.pdbx_redundancy              6.500 
_reflns.pdbx_Rrim_I_all              0.043 
_reflns.pdbx_Rpim_I_all              0.017 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1011018 
_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 1.020 1.040  ? 41659 7492 ? 1.214 ? ? ? 5.600 ? 1.100  ? ? ? ? ? ? 97.000 1.341 0.557 0.746 
1 2 5.590 44.400 ? 7163  1040 ? 0.025 ? ? ? 6.900 ? 61.200 ? ? ? ? ? ? 99.900 0.027 0.010 0.999 
# 
_refine.entry_id                                 7HDS 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             44.4000 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.7600 
_refine.ls_number_reflns_obs                     156216 
_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                          0.1483 
_refine.ls_R_factor_R_work                       0.1477 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1619 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7536 
_refine.ls_number_reflns_R_work                  148680 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.1776 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1200 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                68.250 
_refine.B_iso_min                                8.740 
_refine.pdbx_overall_phase_error                 18.5800 
_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                       1.0200 
_refine_hist.d_res_low                        44.4000 
_refine_hist.pdbx_number_atoms_ligand         44 
_refine_hist.number_atoms_solvent             415 
_refine_hist.number_atoms_total               3001 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           20.34 
_refine_hist.pdbx_B_iso_mean_solvent          30.28 
_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 
1.0200 1.0300  30 95.0000  4771 . 0.4521 0.4326 . 196 0.0000 4967 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 4932 . 0.3677 0.3797 . 278 0.0000 5210 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 4884 . 0.3012 0.2836 . 276 0.0000 5160 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 4906 . 0.2646 0.2650 . 277 0.0000 5183 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 4909 . 0.2364 0.2607 . 237 0.0000 5146 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 4983 . 0.2136 0.2366 . 242 0.0000 5225 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 100.0000 4875 . 0.1854 0.2027 . 265 0.0000 5140 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5016 . 0.1778 0.1847 . 218 0.0000 5234 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 4938 . 0.1637 0.1859 . 243 0.0000 5181 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 4966 . 0.1500 0.1752 . 255 0.0000 5221 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 4911 . 0.1424 0.1768 . 248 0.0000 5159 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 4899 . 0.1334 0.1649 . 270 0.0000 5169 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5013 . 0.1308 0.1617 . 219 0.0000 5232 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 4924 . 0.1324 0.1560 . 251 0.0000 5175 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 4957 . 0.1391 0.1549 . 249 0.0000 5206 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 4939 . 0.1376 0.1473 . 268 0.0000 5207 . 'X-RAY DIFFRACTION' 
1.3200 1.3500  30 100.0000 4946 . 0.1402 0.1654 . 249 0.0000 5195 . 'X-RAY DIFFRACTION' 
1.3500 1.3800  30 100.0000 4947 . 0.1356 0.1644 . 257 0.0000 5204 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 4970 . 0.1312 0.1748 . 236 0.0000 5206 . 'X-RAY DIFFRACTION' 
1.4300 1.4700  30 100.0000 4953 . 0.1273 0.1470 . 252 0.0000 5205 . 'X-RAY DIFFRACTION' 
1.4700 1.5200  30 100.0000 4997 . 0.1202 0.1286 . 237 0.0000 5234 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 4950 . 0.1208 0.1408 . 263 0.0000 5213 . 'X-RAY DIFFRACTION' 
1.5900 1.6600  30 100.0000 4955 . 0.1223 0.1334 . 262 0.0000 5217 . 'X-RAY DIFFRACTION' 
1.6600 1.7400  30 100.0000 5016 . 0.1312 0.1478 . 206 0.0000 5222 . 'X-RAY DIFFRACTION' 
1.7400 1.8500  30 100.0000 4944 . 0.1348 0.1480 . 292 0.0000 5236 . 'X-RAY DIFFRACTION' 
1.8500 2.0000  30 100.0000 4998 . 0.1359 0.1381 . 245 0.0000 5243 . 'X-RAY DIFFRACTION' 
2.0000 2.2000  30 100.0000 4944 . 0.1390 0.1411 . 288 0.0000 5232 . 'X-RAY DIFFRACTION' 
2.2000 2.5200  30 100.0000 5021 . 0.1400 0.1442 . 254 0.0000 5275 . 'X-RAY DIFFRACTION' 
2.5200 3.1700  30 100.0000 5039 . 0.1521 0.1634 . 251 0.0000 5290 . 'X-RAY DIFFRACTION' 
3.1700 44.4000 30 100.0000 5177 . 0.1506 0.1750 . 252 0.0000 5429 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDS 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003641' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDS 
_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 7HDS A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDS 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 7HDS SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDS MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDS SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDS MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F 
2 1 B,G       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HDS 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    212 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    322 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.15 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 56.25 -133.24 
2 1 SER A 128 ? B 66.75 -3.09   
3 1 HIS B 86  ? ? 57.37 -127.96 
# 
_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 513 ? 5.90 . 
2 1 O ? A HOH 514 ? 5.95 . 
3 1 O ? A HOH 515 ? 7.62 . 
4 1 O ? B HOH 400 ? 6.51 . 
# 
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 
A1A81 N2   N  Y N 1   
A1A81 C3   C  N N 2   
A1A81 C6   C  N N 3   
A1A81 C9   C  Y N 4   
A1A81 C12  C  Y N 5   
A1A81 C1   C  N N 6   
A1A81 C10  C  Y N 7   
A1A81 C11  C  Y N 8   
A1A81 C13  C  Y N 9   
A1A81 C2   C  N S 10  
A1A81 C4   C  N N 11  
A1A81 C5   C  N N 12  
A1A81 C7   C  N N 13  
A1A81 C8   C  Y N 14  
A1A81 N1   N  N N 15  
A1A81 N3   N  Y N 16  
A1A81 N4   N  Y N 17  
A1A81 O1   O  N N 18  
A1A81 H6   H  N N 19  
A1A81 H5   H  N N 20  
A1A81 H10  H  N N 21  
A1A81 H11  H  N N 22  
A1A81 H15  H  N N 23  
A1A81 H16  H  N N 24  
A1A81 H4   H  N N 25  
A1A81 H3   H  N N 26  
A1A81 H17  H  N N 27  
A1A81 H1   H  N N 28  
A1A81 H7   H  N N 29  
A1A81 H8   H  N N 30  
A1A81 H9   H  N N 31  
A1A81 H13  H  N N 32  
A1A81 H12  H  N N 33  
A1A81 H14  H  N N 34  
A1A81 H18  H  N N 35  
A1A81 H2   H  N N 36  
ALA   N    N  N N 37  
ALA   CA   C  N S 38  
ALA   C    C  N N 39  
ALA   O    O  N N 40  
ALA   CB   C  N N 41  
ALA   OXT  O  N N 42  
ALA   H    H  N N 43  
ALA   H2   H  N N 44  
ALA   HA   H  N N 45  
ALA   HB1  H  N N 46  
ALA   HB2  H  N N 47  
ALA   HB3  H  N N 48  
ALA   HXT  H  N N 49  
ARG   N    N  N N 50  
ARG   CA   C  N S 51  
ARG   C    C  N N 52  
ARG   O    O  N N 53  
ARG   CB   C  N N 54  
ARG   CG   C  N N 55  
ARG   CD   C  N N 56  
ARG   NE   N  N N 57  
ARG   CZ   C  N N 58  
ARG   NH1  N  N N 59  
ARG   NH2  N  N N 60  
ARG   OXT  O  N N 61  
ARG   H    H  N N 62  
ARG   H2   H  N N 63  
ARG   HA   H  N N 64  
ARG   HB2  H  N N 65  
ARG   HB3  H  N N 66  
ARG   HG2  H  N N 67  
ARG   HG3  H  N N 68  
ARG   HD2  H  N N 69  
ARG   HD3  H  N N 70  
ARG   HE   H  N N 71  
ARG   HH11 H  N N 72  
ARG   HH12 H  N N 73  
ARG   HH21 H  N N 74  
ARG   HH22 H  N N 75  
ARG   HXT  H  N N 76  
ASN   N    N  N N 77  
ASN   CA   C  N S 78  
ASN   C    C  N N 79  
ASN   O    O  N N 80  
ASN   CB   C  N N 81  
ASN   CG   C  N N 82  
ASN   OD1  O  N N 83  
ASN   ND2  N  N N 84  
ASN   OXT  O  N N 85  
ASN   H    H  N N 86  
ASN   H2   H  N N 87  
ASN   HA   H  N N 88  
ASN   HB2  H  N N 89  
ASN   HB3  H  N N 90  
ASN   HD21 H  N N 91  
ASN   HD22 H  N N 92  
ASN   HXT  H  N N 93  
ASP   N    N  N N 94  
ASP   CA   C  N S 95  
ASP   C    C  N N 96  
ASP   O    O  N N 97  
ASP   CB   C  N N 98  
ASP   CG   C  N N 99  
ASP   OD1  O  N N 100 
ASP   OD2  O  N N 101 
ASP   OXT  O  N N 102 
ASP   H    H  N N 103 
ASP   H2   H  N N 104 
ASP   HA   H  N N 105 
ASP   HB2  H  N N 106 
ASP   HB3  H  N N 107 
ASP   HD2  H  N N 108 
ASP   HXT  H  N N 109 
CL    CL   CL N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
GLN   N    N  N N 125 
GLN   CA   C  N S 126 
GLN   C    C  N N 127 
GLN   O    O  N N 128 
GLN   CB   C  N N 129 
GLN   CG   C  N N 130 
GLN   CD   C  N N 131 
GLN   OE1  O  N N 132 
GLN   NE2  N  N N 133 
GLN   OXT  O  N N 134 
GLN   H    H  N N 135 
GLN   H2   H  N N 136 
GLN   HA   H  N N 137 
GLN   HB2  H  N N 138 
GLN   HB3  H  N N 139 
GLN   HG2  H  N N 140 
GLN   HG3  H  N N 141 
GLN   HE21 H  N N 142 
GLN   HE22 H  N N 143 
GLN   HXT  H  N N 144 
GLU   N    N  N N 145 
GLU   CA   C  N S 146 
GLU   C    C  N N 147 
GLU   O    O  N N 148 
GLU   CB   C  N N 149 
GLU   CG   C  N N 150 
GLU   CD   C  N N 151 
GLU   OE1  O  N N 152 
GLU   OE2  O  N N 153 
GLU   OXT  O  N N 154 
GLU   H    H  N N 155 
GLU   H2   H  N N 156 
GLU   HA   H  N N 157 
GLU   HB2  H  N N 158 
GLU   HB3  H  N N 159 
GLU   HG2  H  N N 160 
GLU   HG3  H  N N 161 
GLU   HE2  H  N N 162 
GLU   HXT  H  N N 163 
GLY   N    N  N N 164 
GLY   CA   C  N N 165 
GLY   C    C  N N 166 
GLY   O    O  N N 167 
GLY   OXT  O  N N 168 
GLY   H    H  N N 169 
GLY   H2   H  N N 170 
GLY   HA2  H  N N 171 
GLY   HA3  H  N N 172 
GLY   HXT  H  N N 173 
HIS   N    N  N N 174 
HIS   CA   C  N S 175 
HIS   C    C  N N 176 
HIS   O    O  N N 177 
HIS   CB   C  N N 178 
HIS   CG   C  Y N 179 
HIS   ND1  N  Y N 180 
HIS   CD2  C  Y N 181 
HIS   CE1  C  Y N 182 
HIS   NE2  N  Y N 183 
HIS   OXT  O  N N 184 
HIS   H    H  N N 185 
HIS   H2   H  N N 186 
HIS   HA   H  N N 187 
HIS   HB2  H  N N 188 
HIS   HB3  H  N N 189 
HIS   HD1  H  N N 190 
HIS   HD2  H  N N 191 
HIS   HE1  H  N N 192 
HIS   HE2  H  N N 193 
HIS   HXT  H  N N 194 
HOH   O    O  N N 195 
HOH   H1   H  N N 196 
HOH   H2   H  N N 197 
ILE   N    N  N N 198 
ILE   CA   C  N S 199 
ILE   C    C  N N 200 
ILE   O    O  N N 201 
ILE   CB   C  N S 202 
ILE   CG1  C  N N 203 
ILE   CG2  C  N N 204 
ILE   CD1  C  N N 205 
ILE   OXT  O  N N 206 
ILE   H    H  N N 207 
ILE   H2   H  N N 208 
ILE   HA   H  N N 209 
ILE   HB   H  N N 210 
ILE   HG12 H  N N 211 
ILE   HG13 H  N N 212 
ILE   HG21 H  N N 213 
ILE   HG22 H  N N 214 
ILE   HG23 H  N N 215 
ILE   HD11 H  N N 216 
ILE   HD12 H  N N 217 
ILE   HD13 H  N N 218 
ILE   HXT  H  N N 219 
LEU   N    N  N N 220 
LEU   CA   C  N S 221 
LEU   C    C  N N 222 
LEU   O    O  N N 223 
LEU   CB   C  N N 224 
LEU   CG   C  N N 225 
LEU   CD1  C  N N 226 
LEU   CD2  C  N N 227 
LEU   OXT  O  N N 228 
LEU   H    H  N N 229 
LEU   H2   H  N N 230 
LEU   HA   H  N N 231 
LEU   HB2  H  N N 232 
LEU   HB3  H  N N 233 
LEU   HG   H  N N 234 
LEU   HD11 H  N N 235 
LEU   HD12 H  N N 236 
LEU   HD13 H  N N 237 
LEU   HD21 H  N N 238 
LEU   HD22 H  N N 239 
LEU   HD23 H  N N 240 
LEU   HXT  H  N N 241 
LYS   N    N  N N 242 
LYS   CA   C  N S 243 
LYS   C    C  N N 244 
LYS   O    O  N N 245 
LYS   CB   C  N N 246 
LYS   CG   C  N N 247 
LYS   CD   C  N N 248 
LYS   CE   C  N N 249 
LYS   NZ   N  N N 250 
LYS   OXT  O  N N 251 
LYS   H    H  N N 252 
LYS   H2   H  N N 253 
LYS   HA   H  N N 254 
LYS   HB2  H  N N 255 
LYS   HB3  H  N N 256 
LYS   HG2  H  N N 257 
LYS   HG3  H  N N 258 
LYS   HD2  H  N N 259 
LYS   HD3  H  N N 260 
LYS   HE2  H  N N 261 
LYS   HE3  H  N N 262 
LYS   HZ1  H  N N 263 
LYS   HZ2  H  N N 264 
LYS   HZ3  H  N N 265 
LYS   HXT  H  N N 266 
MET   N    N  N N 267 
MET   CA   C  N S 268 
MET   C    C  N N 269 
MET   O    O  N N 270 
MET   CB   C  N N 271 
MET   CG   C  N N 272 
MET   SD   S  N N 273 
MET   CE   C  N N 274 
MET   OXT  O  N N 275 
MET   H    H  N N 276 
MET   H2   H  N N 277 
MET   HA   H  N N 278 
MET   HB2  H  N N 279 
MET   HB3  H  N N 280 
MET   HG2  H  N N 281 
MET   HG3  H  N N 282 
MET   HE1  H  N N 283 
MET   HE2  H  N N 284 
MET   HE3  H  N N 285 
MET   HXT  H  N N 286 
PHE   N    N  N N 287 
PHE   CA   C  N S 288 
PHE   C    C  N N 289 
PHE   O    O  N N 290 
PHE   CB   C  N N 291 
PHE   CG   C  Y N 292 
PHE   CD1  C  Y N 293 
PHE   CD2  C  Y N 294 
PHE   CE1  C  Y N 295 
PHE   CE2  C  Y N 296 
PHE   CZ   C  Y N 297 
PHE   OXT  O  N N 298 
PHE   H    H  N N 299 
PHE   H2   H  N N 300 
PHE   HA   H  N N 301 
PHE   HB2  H  N N 302 
PHE   HB3  H  N N 303 
PHE   HD1  H  N N 304 
PHE   HD2  H  N N 305 
PHE   HE1  H  N N 306 
PHE   HE2  H  N N 307 
PHE   HZ   H  N N 308 
PHE   HXT  H  N N 309 
PRO   N    N  N N 310 
PRO   CA   C  N S 311 
PRO   C    C  N N 312 
PRO   O    O  N N 313 
PRO   CB   C  N N 314 
PRO   CG   C  N N 315 
PRO   CD   C  N N 316 
PRO   OXT  O  N N 317 
PRO   H    H  N N 318 
PRO   HA   H  N N 319 
PRO   HB2  H  N N 320 
PRO   HB3  H  N N 321 
PRO   HG2  H  N N 322 
PRO   HG3  H  N N 323 
PRO   HD2  H  N N 324 
PRO   HD3  H  N N 325 
PRO   HXT  H  N N 326 
SER   N    N  N N 327 
SER   CA   C  N S 328 
SER   C    C  N N 329 
SER   O    O  N N 330 
SER   CB   C  N N 331 
SER   OG   O  N N 332 
SER   OXT  O  N N 333 
SER   H    H  N N 334 
SER   H2   H  N N 335 
SER   HA   H  N N 336 
SER   HB2  H  N N 337 
SER   HB3  H  N N 338 
SER   HG   H  N N 339 
SER   HXT  H  N N 340 
TFA   C1   C  N N 341 
TFA   C2   C  N N 342 
TFA   O    O  N N 343 
TFA   F1   F  N N 344 
TFA   F2   F  N N 345 
TFA   F3   F  N N 346 
TFA   OXT  O  N N 347 
TFA   HXT  H  N N 348 
THR   N    N  N N 349 
THR   CA   C  N S 350 
THR   C    C  N N 351 
THR   O    O  N N 352 
THR   CB   C  N R 353 
THR   OG1  O  N N 354 
THR   CG2  C  N N 355 
THR   OXT  O  N N 356 
THR   H    H  N N 357 
THR   H2   H  N N 358 
THR   HA   H  N N 359 
THR   HB   H  N N 360 
THR   HG1  H  N N 361 
THR   HG21 H  N N 362 
THR   HG22 H  N N 363 
THR   HG23 H  N N 364 
THR   HXT  H  N N 365 
TYR   N    N  N N 366 
TYR   CA   C  N S 367 
TYR   C    C  N N 368 
TYR   O    O  N N 369 
TYR   CB   C  N N 370 
TYR   CG   C  Y N 371 
TYR   CD1  C  Y N 372 
TYR   CD2  C  Y N 373 
TYR   CE1  C  Y N 374 
TYR   CE2  C  Y N 375 
TYR   CZ   C  Y N 376 
TYR   OH   O  N N 377 
TYR   OXT  O  N N 378 
TYR   H    H  N N 379 
TYR   H2   H  N N 380 
TYR   HA   H  N N 381 
TYR   HB2  H  N N 382 
TYR   HB3  H  N N 383 
TYR   HD1  H  N N 384 
TYR   HD2  H  N N 385 
TYR   HE1  H  N N 386 
TYR   HE2  H  N N 387 
TYR   HH   H  N N 388 
TYR   HXT  H  N N 389 
VAL   N    N  N N 390 
VAL   CA   C  N S 391 
VAL   C    C  N N 392 
VAL   O    O  N N 393 
VAL   CB   C  N N 394 
VAL   CG1  C  N N 395 
VAL   CG2  C  N N 396 
VAL   OXT  O  N N 397 
VAL   H    H  N N 398 
VAL   H2   H  N N 399 
VAL   HA   H  N N 400 
VAL   HB   H  N N 401 
VAL   HG11 H  N N 402 
VAL   HG12 H  N N 403 
VAL   HG13 H  N N 404 
VAL   HG21 H  N N 405 
VAL   HG22 H  N N 406 
VAL   HG23 H  N N 407 
VAL   HXT  H  N N 408 
# 
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 
A1A81 C7  C6   sing N N 1   
A1A81 C7  C4   sing N N 2   
A1A81 C6  C5   sing N N 3   
A1A81 C3  C4   sing N N 4   
A1A81 C3  C2   sing N N 5   
A1A81 O1  C1   sing N N 6   
A1A81 C4  C5   sing N N 7   
A1A81 C1  C2   sing N N 8   
A1A81 C2  N1   sing N N 9   
A1A81 N1  C8   sing N N 10  
A1A81 C8  C11  doub Y N 11  
A1A81 C8  N2   sing Y N 12  
A1A81 C12 C11  sing Y N 13  
A1A81 C12 C13  doub Y N 14  
A1A81 C11 C10  sing Y N 15  
A1A81 N2  C9   doub Y N 16  
A1A81 C13 N4   sing Y N 17  
A1A81 C10 N4   sing Y N 18  
A1A81 C10 N3   doub Y N 19  
A1A81 C9  N3   sing Y N 20  
A1A81 C3  H6   sing N N 21  
A1A81 C3  H5   sing N N 22  
A1A81 C6  H10  sing N N 23  
A1A81 C6  H11  sing N N 24  
A1A81 C9  H15  sing N N 25  
A1A81 C12 H16  sing N N 26  
A1A81 C1  H4   sing N N 27  
A1A81 C1  H3   sing N N 28  
A1A81 C13 H17  sing N N 29  
A1A81 C2  H1   sing N N 30  
A1A81 C4  H7   sing N N 31  
A1A81 C5  H8   sing N N 32  
A1A81 C5  H9   sing N N 33  
A1A81 C7  H13  sing N N 34  
A1A81 C7  H12  sing N N 35  
A1A81 N1  H14  sing N N 36  
A1A81 N4  H18  sing N N 37  
A1A81 O1  H2   sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
HIS   N   CA   sing N N 167 
HIS   N   H    sing N N 168 
HIS   N   H2   sing N N 169 
HIS   CA  C    sing N N 170 
HIS   CA  CB   sing N N 171 
HIS   CA  HA   sing N N 172 
HIS   C   O    doub N N 173 
HIS   C   OXT  sing N N 174 
HIS   CB  CG   sing N N 175 
HIS   CB  HB2  sing N N 176 
HIS   CB  HB3  sing N N 177 
HIS   CG  ND1  sing Y N 178 
HIS   CG  CD2  doub Y N 179 
HIS   ND1 CE1  doub Y N 180 
HIS   ND1 HD1  sing N N 181 
HIS   CD2 NE2  sing Y N 182 
HIS   CD2 HD2  sing N N 183 
HIS   CE1 NE2  sing Y N 184 
HIS   CE1 HE1  sing N N 185 
HIS   NE2 HE2  sing N N 186 
HIS   OXT HXT  sing N N 187 
HOH   O   H1   sing N N 188 
HOH   O   H2   sing N N 189 
ILE   N   CA   sing N N 190 
ILE   N   H    sing N N 191 
ILE   N   H2   sing N N 192 
ILE   CA  C    sing N N 193 
ILE   CA  CB   sing N N 194 
ILE   CA  HA   sing N N 195 
ILE   C   O    doub N N 196 
ILE   C   OXT  sing N N 197 
ILE   CB  CG1  sing N N 198 
ILE   CB  CG2  sing N N 199 
ILE   CB  HB   sing N N 200 
ILE   CG1 CD1  sing N N 201 
ILE   CG1 HG12 sing N N 202 
ILE   CG1 HG13 sing N N 203 
ILE   CG2 HG21 sing N N 204 
ILE   CG2 HG22 sing N N 205 
ILE   CG2 HG23 sing N N 206 
ILE   CD1 HD11 sing N N 207 
ILE   CD1 HD12 sing N N 208 
ILE   CD1 HD13 sing N N 209 
ILE   OXT HXT  sing N N 210 
LEU   N   CA   sing N N 211 
LEU   N   H    sing N N 212 
LEU   N   H2   sing N N 213 
LEU   CA  C    sing N N 214 
LEU   CA  CB   sing N N 215 
LEU   CA  HA   sing N N 216 
LEU   C   O    doub N N 217 
LEU   C   OXT  sing N N 218 
LEU   CB  CG   sing N N 219 
LEU   CB  HB2  sing N N 220 
LEU   CB  HB3  sing N N 221 
LEU   CG  CD1  sing N N 222 
LEU   CG  CD2  sing N N 223 
LEU   CG  HG   sing N N 224 
LEU   CD1 HD11 sing N N 225 
LEU   CD1 HD12 sing N N 226 
LEU   CD1 HD13 sing N N 227 
LEU   CD2 HD21 sing N N 228 
LEU   CD2 HD22 sing N N 229 
LEU   CD2 HD23 sing N N 230 
LEU   OXT HXT  sing N N 231 
LYS   N   CA   sing N N 232 
LYS   N   H    sing N N 233 
LYS   N   H2   sing N N 234 
LYS   CA  C    sing N N 235 
LYS   CA  CB   sing N N 236 
LYS   CA  HA   sing N N 237 
LYS   C   O    doub N N 238 
LYS   C   OXT  sing N N 239 
LYS   CB  CG   sing N N 240 
LYS   CB  HB2  sing N N 241 
LYS   CB  HB3  sing N N 242 
LYS   CG  CD   sing N N 243 
LYS   CG  HG2  sing N N 244 
LYS   CG  HG3  sing N N 245 
LYS   CD  CE   sing N N 246 
LYS   CD  HD2  sing N N 247 
LYS   CD  HD3  sing N N 248 
LYS   CE  NZ   sing N N 249 
LYS   CE  HE2  sing N N 250 
LYS   CE  HE3  sing N N 251 
LYS   NZ  HZ1  sing N N 252 
LYS   NZ  HZ2  sing N N 253 
LYS   NZ  HZ3  sing N N 254 
LYS   OXT HXT  sing N N 255 
MET   N   CA   sing N N 256 
MET   N   H    sing N N 257 
MET   N   H2   sing N N 258 
MET   CA  C    sing N N 259 
MET   CA  CB   sing N N 260 
MET   CA  HA   sing N N 261 
MET   C   O    doub N N 262 
MET   C   OXT  sing N N 263 
MET   CB  CG   sing N N 264 
MET   CB  HB2  sing N N 265 
MET   CB  HB3  sing N N 266 
MET   CG  SD   sing N N 267 
MET   CG  HG2  sing N N 268 
MET   CG  HG3  sing N N 269 
MET   SD  CE   sing N N 270 
MET   CE  HE1  sing N N 271 
MET   CE  HE2  sing N N 272 
MET   CE  HE3  sing N N 273 
MET   OXT HXT  sing N N 274 
PHE   N   CA   sing N N 275 
PHE   N   H    sing N N 276 
PHE   N   H2   sing N N 277 
PHE   CA  C    sing N N 278 
PHE   CA  CB   sing N N 279 
PHE   CA  HA   sing N N 280 
PHE   C   O    doub N N 281 
PHE   C   OXT  sing N N 282 
PHE   CB  CG   sing N N 283 
PHE   CB  HB2  sing N N 284 
PHE   CB  HB3  sing N N 285 
PHE   CG  CD1  doub Y N 286 
PHE   CG  CD2  sing Y N 287 
PHE   CD1 CE1  sing Y N 288 
PHE   CD1 HD1  sing N N 289 
PHE   CD2 CE2  doub Y N 290 
PHE   CD2 HD2  sing N N 291 
PHE   CE1 CZ   doub Y N 292 
PHE   CE1 HE1  sing N N 293 
PHE   CE2 CZ   sing Y N 294 
PHE   CE2 HE2  sing N N 295 
PHE   CZ  HZ   sing N N 296 
PHE   OXT HXT  sing N N 297 
PRO   N   CA   sing N N 298 
PRO   N   CD   sing N N 299 
PRO   N   H    sing N N 300 
PRO   CA  C    sing N N 301 
PRO   CA  CB   sing N N 302 
PRO   CA  HA   sing N N 303 
PRO   C   O    doub N N 304 
PRO   C   OXT  sing N N 305 
PRO   CB  CG   sing N N 306 
PRO   CB  HB2  sing N N 307 
PRO   CB  HB3  sing N N 308 
PRO   CG  CD   sing N N 309 
PRO   CG  HG2  sing N N 310 
PRO   CG  HG3  sing N N 311 
PRO   CD  HD2  sing N N 312 
PRO   CD  HD3  sing N N 313 
PRO   OXT HXT  sing N N 314 
SER   N   CA   sing N N 315 
SER   N   H    sing N N 316 
SER   N   H2   sing N N 317 
SER   CA  C    sing N N 318 
SER   CA  CB   sing N N 319 
SER   CA  HA   sing N N 320 
SER   C   O    doub N N 321 
SER   C   OXT  sing N N 322 
SER   CB  OG   sing N N 323 
SER   CB  HB2  sing N N 324 
SER   CB  HB3  sing N N 325 
SER   OG  HG   sing N N 326 
SER   OXT HXT  sing N N 327 
TFA   C1  C2   sing N N 328 
TFA   C1  O    doub N N 329 
TFA   C1  OXT  sing N N 330 
TFA   C2  F1   sing N N 331 
TFA   C2  F2   sing N N 332 
TFA   C2  F3   sing N N 333 
TFA   OXT HXT  sing N N 334 
THR   N   CA   sing N N 335 
THR   N   H    sing N N 336 
THR   N   H2   sing N N 337 
THR   CA  C    sing N N 338 
THR   CA  CB   sing N N 339 
THR   CA  HA   sing N N 340 
THR   C   O    doub N N 341 
THR   C   OXT  sing N N 342 
THR   CB  OG1  sing N N 343 
THR   CB  CG2  sing N N 344 
THR   CB  HB   sing N N 345 
THR   OG1 HG1  sing N N 346 
THR   CG2 HG21 sing N N 347 
THR   CG2 HG22 sing N N 348 
THR   CG2 HG23 sing N N 349 
THR   OXT HXT  sing N N 350 
TYR   N   CA   sing N N 351 
TYR   N   H    sing N N 352 
TYR   N   H2   sing N N 353 
TYR   CA  C    sing N N 354 
TYR   CA  CB   sing N N 355 
TYR   CA  HA   sing N N 356 
TYR   C   O    doub N N 357 
TYR   C   OXT  sing N N 358 
TYR   CB  CG   sing N N 359 
TYR   CB  HB2  sing N N 360 
TYR   CB  HB3  sing N N 361 
TYR   CG  CD1  doub Y N 362 
TYR   CG  CD2  sing Y N 363 
TYR   CD1 CE1  sing Y N 364 
TYR   CD1 HD1  sing N N 365 
TYR   CD2 CE2  doub Y N 366 
TYR   CD2 HD2  sing N N 367 
TYR   CE1 CZ   doub Y N 368 
TYR   CE1 HE1  sing N N 369 
TYR   CE2 CZ   sing Y N 370 
TYR   CE2 HE2  sing N N 371 
TYR   CZ  OH   sing N N 372 
TYR   OH  HH   sing N N 373 
TYR   OXT HXT  sing N N 374 
VAL   N   CA   sing N N 375 
VAL   N   H    sing N N 376 
VAL   N   H2   sing N N 377 
VAL   CA  C    sing N N 378 
VAL   CA  CB   sing N N 379 
VAL   CA  HA   sing N N 380 
VAL   C   O    doub N N 381 
VAL   C   OXT  sing N N 382 
VAL   CB  CG1  sing N N 383 
VAL   CB  CG2  sing N N 384 
VAL   CB  HB   sing N N 385 
VAL   CG1 HG11 sing N N 386 
VAL   CG1 HG12 sing N N 387 
VAL   CG1 HG13 sing N N 388 
VAL   CG2 HG21 sing N N 389 
VAL   CG2 HG22 sing N N 390 
VAL   CG2 HG23 sing N N 391 
VAL   OXT HXT  sing N N 392 
# 
_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                    7HDS 
_atom_sites.fract_transf_matrix[1][1]   0.011262 
_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]   0.011262 
_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]   0.025303 
_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    . VAL   A 1 3   ? 19.553 -16.159 22.271  1.00 55.67 ?  3   VAL   A N    1 
ATOM   2    C  CA   . VAL   A 1 3   ? 18.610 -15.062 22.455  1.00 54.96 ?  3   VAL   A CA   1 
ATOM   3    C  C    . VAL   A 1 3   ? 19.273 -13.732 22.115  1.00 52.37 ?  3   VAL   A C    1 
ATOM   4    O  O    . VAL   A 1 3   ? 20.393 -13.461 22.550  1.00 53.08 ?  3   VAL   A O    1 
ATOM   5    C  CB   . VAL   A 1 3   ? 18.029 -15.056 23.886  1.00 56.24 ?  3   VAL   A CB   1 
ATOM   6    C  CG1  . VAL   A 1 3   ? 17.028 -13.920 24.053  1.00 56.78 ?  3   VAL   A CG1  1 
ATOM   7    C  CG2  . VAL   A 1 3   ? 17.377 -16.395 24.200  1.00 56.51 ?  3   VAL   A CG2  1 
ATOM   8    H  HA   . VAL   A 1 3   ? 17.869 -15.182 21.846  1.00 66.07 ?  3   VAL   A HA   1 
ATOM   9    H  HB   . VAL   A 1 3   ? 18.747 -14.917 24.523  1.00 67.60 ?  3   VAL   A HB   1 
ATOM   10   H  HG11 . VAL   A 1 3   ? 16.549 -14.042 24.888  1.00 68.25 ?  3   VAL   A HG11 1 
ATOM   11   H  HG12 . VAL   A 1 3   ? 17.505 -13.076 24.067  1.00 68.25 ?  3   VAL   A HG12 1 
ATOM   12   H  HG13 . VAL   A 1 3   ? 16.405 -13.937 23.310  1.00 68.25 ?  3   VAL   A HG13 1 
ATOM   13   H  HG21 . VAL   A 1 3   ? 16.949 -16.343 25.069  1.00 67.93 ?  3   VAL   A HG21 1 
ATOM   14   H  HG22 . VAL   A 1 3   ? 16.717 -16.591 23.517  1.00 67.93 ?  3   VAL   A HG22 1 
ATOM   15   H  HG23 . VAL   A 1 3   ? 18.059 -17.084 24.208  1.00 67.93 ?  3   VAL   A HG23 1 
ATOM   16   N  N    . ASN   A 1 4   ? 18.583 -12.910 21.326  1.00 48.39 ?  4   ASN   A N    1 
ATOM   17   C  CA   . ASN   A 1 4   ? 19.031 -11.558 21.011  1.00 43.90 ?  4   ASN   A CA   1 
ATOM   18   C  C    . ASN   A 1 4   ? 17.899 -10.575 21.302  1.00 39.50 ?  4   ASN   A C    1 
ATOM   19   O  O    . ASN   A 1 4   ? 16.807 -10.961 21.732  1.00 39.68 ?  4   ASN   A O    1 
ATOM   20   C  CB   . ASN   A 1 4   ? 19.570 -11.447 19.577  1.00 43.46 ?  4   ASN   A CB   1 
ATOM   21   C  CG   . ASN   A 1 4   ? 18.554 -11.851 18.534  1.00 42.89 ?  4   ASN   A CG   1 
ATOM   22   O  OD1  . ASN   A 1 4   ? 17.436 -11.337 18.507  1.00 42.50 ?  4   ASN   A OD1  1 
ATOM   23   N  ND2  . ASN   A 1 4   ? 18.940 -12.780 17.665  1.00 42.59 ?  4   ASN   A ND2  1 
ATOM   24   H  H    . ASN   A 1 4   ? 17.834 -13.121 20.956  1.00 58.19 ?  4   ASN   A H    1 
ATOM   25   H  HA   . ASN   A 1 4   ? 19.761 -11.338 21.602  1.00 52.80 ?  4   ASN   A HA   1 
ATOM   26   H  HB2  . ASN   A 1 4   ? 19.827 -10.526 19.407  1.00 52.27 ?  4   ASN   A HB2  1 
ATOM   27   H  HB3  . ASN   A 1 4   ? 20.341 -12.027 19.487  1.00 52.27 ?  4   ASN   A HB3  1 
ATOM   28   H  HD21 . ASN   A 1 4   ? 18.403 -13.045 17.049  1.00 51.22 ?  4   ASN   A HD21 1 
ATOM   29   H  HD22 . ASN   A 1 4   ? 19.731 -13.117 17.718  1.00 51.22 ?  4   ASN   A HD22 1 
ATOM   30   N  N    A SER   A 1 5   ? 18.171 -9.290  21.078  0.64 37.00 ?  5   SER   A N    1 
ATOM   31   N  N    B SER   A 1 5   ? 18.161 -9.294  21.042  0.36 37.37 ?  5   SER   A N    1 
ATOM   32   C  CA   A SER   A 1 5   ? 17.248 -8.223  21.440  0.64 34.42 ?  5   SER   A CA   1 
ATOM   33   C  CA   B SER   A 1 5   ? 17.282 -8.209  21.460  0.36 35.08 ?  5   SER   A CA   1 
ATOM   34   C  C    A SER   A 1 5   ? 16.390 -7.749  20.271  0.64 31.06 ?  5   SER   A C    1 
ATOM   35   C  C    B SER   A 1 5   ? 16.410 -7.662  20.334  0.36 32.04 ?  5   SER   A C    1 
ATOM   36   O  O    A SER   A 1 5   ? 15.716 -6.721  20.389  0.64 31.46 ?  5   SER   A O    1 
ATOM   37   O  O    B SER   A 1 5   ? 15.766 -6.625  20.519  0.36 32.33 ?  5   SER   A O    1 
ATOM   38   C  CB   A SER   A 1 5   ? 18.008 -7.045  22.057  0.64 35.00 ?  5   SER   A CB   1 
ATOM   39   C  CB   B SER   A 1 5   ? 18.101 -7.073  22.078  0.36 35.59 ?  5   SER   A CB   1 
ATOM   40   O  OG   A SER   A 1 5   ? 18.982 -6.540  21.161  0.64 35.48 ?  5   SER   A OG   1 
ATOM   41   O  OG   B SER   A 1 5   ? 18.970 -6.492  21.121  0.36 35.99 ?  5   SER   A OG   1 
ATOM   42   H  H    A SER   A 1 5   ? 18.896 -9.011  20.708  0.64 44.52 ?  5   SER   A H    1 
ATOM   43   H  H    B SER   A 1 5   ? 18.856 -9.027  20.611  0.36 44.96 ?  5   SER   A H    1 
ATOM   44   H  HA   A SER   A 1 5   ? 16.648 -8.559  22.121  0.64 41.42 ?  5   SER   A HA   1 
ATOM   45   H  HA   B SER   A 1 5   ? 16.692 -8.544  22.150  0.36 42.21 ?  5   SER   A HA   1 
ATOM   46   H  HB2  A SER   A 1 5   ? 17.379 -6.336  22.267  0.64 42.11 ?  5   SER   A HB2  1 
ATOM   47   H  HB2  B SER   A 1 5   ? 17.494 -6.392  22.410  0.36 42.83 ?  5   SER   A HB2  1 
ATOM   48   H  HB3  A SER   A 1 5   ? 18.448 -7.344  22.871  0.64 42.11 ?  5   SER   A HB3  1 
ATOM   49   H  HB3  B SER   A 1 5   ? 18.631 -7.427  22.809  0.36 42.83 ?  5   SER   A HB3  1 
ATOM   50   H  HG   A SER   A 1 5   ? 19.394 -5.898  21.518  0.64 42.70 ?  5   SER   A HG   1 
ATOM   51   H  HG   B SER   A 1 5   ? 19.410 -5.868  21.474  0.36 43.30 ?  5   SER   A HG   1 
ATOM   52   N  N    A PHE   A 1 6   ? 16.396 -8.468  19.152  0.64 27.17 ?  6   PHE   A N    1 
ATOM   53   N  N    B PHE   A 1 6   ? 16.373 -8.319  19.178  0.36 28.63 ?  6   PHE   A N    1 
ATOM   54   C  CA   A PHE   A 1 6   ? 15.503 -8.130  18.051  0.64 23.49 ?  6   PHE   A CA   1 
ATOM   55   C  CA   B PHE   A 1 6   ? 15.482 -7.879  18.112  0.36 25.28 ?  6   PHE   A CA   1 
ATOM   56   C  C    A PHE   A 1 6   ? 14.074 -8.521  18.406  0.64 22.56 ?  6   PHE   A C    1 
ATOM   57   C  C    B PHE   A 1 6   ? 14.036 -8.152  18.509  0.36 24.32 ?  6   PHE   A C    1 
ATOM   58   O  O    A PHE   A 1 6   ? 13.830 -9.624  18.903  0.64 23.93 ?  6   PHE   A O    1 
ATOM   59   O  O    B PHE   A 1 6   ? 13.688 -9.272  18.896  0.36 24.57 ?  6   PHE   A O    1 
ATOM   60   C  CB   A PHE   A 1 6   ? 15.942 -8.847  16.779  0.64 21.23 ?  6   PHE   A CB   1 
ATOM   61   C  CB   B PHE   A 1 6   ? 15.822 -8.600  16.809  0.36 23.21 ?  6   PHE   A CB   1 
ATOM   62   C  CG   A PHE   A 1 6   ? 17.202 -8.288  16.180  0.64 19.88 ?  6   PHE   A CG   1 
ATOM   63   C  CG   B PHE   A 1 6   ? 17.136 -8.177  16.206  0.36 21.61 ?  6   PHE   A CG   1 
ATOM   64   C  CD1  A PHE   A 1 6   ? 17.173 -7.113  15.448  0.64 19.36 ?  6   PHE   A CD1  1 
ATOM   65   C  CD1  B PHE   A 1 6   ? 17.254 -6.961  15.551  0.36 20.91 ?  6   PHE   A CD1  1 
ATOM   66   C  CD2  A PHE   A 1 6   ? 18.414 -8.934  16.354  0.64 20.34 ?  6   PHE   A CD2  1 
ATOM   67   C  CD2  B PHE   A 1 6   ? 18.250 -8.998  16.287  0.36 21.38 ?  6   PHE   A CD2  1 
ATOM   68   C  CE1  A PHE   A 1 6   ? 18.327 -6.593  14.896  0.64 19.41 ?  6   PHE   A CE1  1 
ATOM   69   C  CE1  B PHE   A 1 6   ? 18.458 -6.569  14.993  0.36 20.69 ?  6   PHE   A CE1  1 
ATOM   70   C  CE2  A PHE   A 1 6   ? 19.570 -8.421  15.804  0.64 20.43 ?  6   PHE   A CE2  1 
ATOM   71   C  CE2  B PHE   A 1 6   ? 19.456 -8.612  15.730  0.36 21.10 ?  6   PHE   A CE2  1 
ATOM   72   C  CZ   A PHE   A 1 6   ? 19.527 -7.247  15.075  0.64 19.78 ?  6   PHE   A CZ   1 
ATOM   73   C  CZ   B PHE   A 1 6   ? 19.560 -7.395  15.083  0.36 20.76 ?  6   PHE   A CZ   1 
ATOM   74   H  H    A PHE   A 1 6   ? 16.900 -9.150  19.010  0.64 32.72 ?  6   PHE   A H    1 
ATOM   75   H  H    B PHE   A 1 6   ? 16.844 -9.013  18.988  0.36 34.47 ?  6   PHE   A H    1 
ATOM   76   H  HA   A PHE   A 1 6   ? 15.526 -7.179  17.900  0.64 28.30 ?  6   PHE   A HA   1 
ATOM   77   H  HA   B PHE   A 1 6   ? 15.588 -6.927  17.976  0.36 30.46 ?  6   PHE   A HA   1 
ATOM   78   H  HB2  A PHE   A 1 6   ? 16.095 -9.785  16.986  0.64 25.59 ?  6   PHE   A HB2  1 
ATOM   79   H  HB2  B PHE   A 1 6   ? 15.868 -9.553  16.982  0.36 27.97 ?  6   PHE   A HB2  1 
ATOM   80   H  HB3  A PHE   A 1 6   ? 15.234 -8.771  16.121  0.64 25.59 ?  6   PHE   A HB3  1 
ATOM   81   H  HB3  B PHE   A 1 6   ? 15.126 -8.416  16.160  0.36 27.97 ?  6   PHE   A HB3  1 
ATOM   82   H  HD1  A PHE   A 1 6   ? 16.361 -6.671  15.328  0.64 23.35 ?  6   PHE   A HD1  1 
ATOM   83   H  HD1  B PHE   A 1 6   ? 16.515 -6.400  15.489  0.36 25.21 ?  6   PHE   A HD1  1 
ATOM   84   H  HD2  A PHE   A 1 6   ? 18.447 -9.726  16.847  0.64 24.53 ?  6   PHE   A HD2  1 
ATOM   85   H  HD2  B PHE   A 1 6   ? 18.187 -9.817  16.722  0.36 25.77 ?  6   PHE   A HD2  1 
ATOM   86   H  HE1  A PHE   A 1 6   ? 18.292 -5.803  14.406  0.64 23.41 ?  6   PHE   A HE1  1 
ATOM   87   H  HE1  B PHE   A 1 6   ? 18.525 -5.749  14.557  0.36 24.94 ?  6   PHE   A HE1  1 
ATOM   88   H  HE2  A PHE   A 1 6   ? 20.378 -8.862  15.927  0.64 24.63 ?  6   PHE   A HE2  1 
ATOM   89   H  HE2  B PHE   A 1 6   ? 20.199 -9.169  15.791  0.36 25.44 ?  6   PHE   A HE2  1 
ATOM   90   H  HZ   A PHE   A 1 6   ? 20.303 -6.898  14.705  0.64 23.86 ?  6   PHE   A HZ   1 
ATOM   91   H  HZ   B PHE   A 1 6   ? 20.371 -7.134  14.707  0.36 25.03 ?  6   PHE   A HZ   1 
ATOM   92   N  N    A SER   A 1 7   ? 13.127 -7.620  18.139  0.64 20.78 ?  7   SER   A N    1 
ATOM   93   N  N    B SER   A 1 7   ? 13.190 -7.127  18.413  0.36 23.34 ?  7   SER   A N    1 
ATOM   94   C  CA   A SER   A 1 7   ? 11.753 -7.764  18.607  0.64 20.37 ?  7   SER   A CA   1 
ATOM   95   C  CA   B SER   A 1 7   ? 11.837 -7.170  18.950  0.36 22.82 ?  7   SER   A CA   1 
ATOM   96   C  C    A SER   A 1 7   ? 10.762 -7.488  17.483  0.64 18.13 ?  7   SER   A C    1 
ATOM   97   C  C    B SER   A 1 7   ? 10.816 -6.970  17.837  0.36 21.57 ?  7   SER   A C    1 
ATOM   98   O  O    A SER   A 1 7   ? 10.972 -6.595  16.658  0.64 18.41 ?  7   SER   A O    1 
ATOM   99   O  O    B SER   A 1 7   ? 10.988 -6.110  16.969  0.36 21.76 ?  7   SER   A O    1 
ATOM   100  C  CB   A SER   A 1 7   ? 11.484 -6.795  19.766  0.64 22.49 ?  7   SER   A CB   1 
ATOM   101  C  CB   B SER   A 1 7   ? 11.652 -6.086  20.022  0.36 23.54 ?  7   SER   A CB   1 
ATOM   102  O  OG   A SER   A 1 7   ? 10.134 -6.858  20.186  0.64 24.17 ?  7   SER   A OG   1 
ATOM   103  O  OG   B SER   A 1 7   ? 10.492 -6.327  20.796  0.36 24.08 ?  7   SER   A OG   1 
ATOM   104  H  H    A SER   A 1 7   ? 13.262 -6.915  17.672  0.64 25.05 ?  7   SER   A H    1 
ATOM   105  H  H    B SER   A 1 7   ? 13.384 -6.380  18.029  0.36 28.12 ?  7   SER   A H    1 
ATOM   106  H  HA   A SER   A 1 7   ? 11.612 -8.669  18.926  0.64 24.56 ?  7   SER   A HA   1 
ATOM   107  H  HA   B SER   A 1 7   ? 11.677 -8.031  19.362  0.36 27.49 ?  7   SER   A HA   1 
ATOM   108  H  HB2  A SER   A 1 7   ? 12.058 -7.030  20.513  0.64 27.10 ?  7   SER   A HB2  1 
ATOM   109  H  HB2  B SER   A 1 7   ? 12.433 -6.080  20.603  0.36 28.36 ?  7   SER   A HB2  1 
ATOM   110  H  HB3  A SER   A 1 7   ? 11.685 -5.891  19.471  0.64 27.10 ?  7   SER   A HB3  1 
ATOM   111  H  HB3  B SER   A 1 7   ? 11.561 -5.223  19.589  0.36 28.36 ?  7   SER   A HB3  1 
ATOM   112  H  HG   A SER   A 1 7   ? 10.006 -6.318  20.816  0.64 29.11 ?  7   SER   A HG   1 
ATOM   113  H  HG   B SER   A 1 7   ? 10.413 -5.735  21.388  0.36 29.01 ?  7   SER   A HG   1 
ATOM   114  N  N    A GLY   A 1 8   ? 9.670  -8.256  17.462  0.64 16.68 ?  8   GLY   A N    1 
ATOM   115  N  N    B GLY   A 1 8   ? 9.757  -7.778  17.869  0.36 20.24 ?  8   GLY   A N    1 
ATOM   116  C  CA   A GLY   A 1 8   ? 8.586  -8.004  16.532  0.64 15.57 ?  8   GLY   A CA   1 
ATOM   117  C  CA   B GLY   A 1 8   ? 8.636  -7.608  16.966  0.36 18.94 ?  8   GLY   A CA   1 
ATOM   118  C  C    A GLY   A 1 8   ? 8.800  -8.510  15.125  0.64 14.96 ?  8   GLY   A C    1 
ATOM   119  C  C    B GLY   A 1 8   ? 8.825  -8.149  15.569  0.36 17.30 ?  8   GLY   A C    1 
ATOM   120  O  O    A GLY   A 1 8   ? 8.060  -8.104  14.219  0.64 15.73 ?  8   GLY   A O    1 
ATOM   121  O  O    B GLY   A 1 8   ? 8.054  -7.788  14.675  0.36 17.61 ?  8   GLY   A O    1 
ATOM   122  H  H    A GLY   A 1 8   ? 9.544  -8.932  17.978  0.64 20.13 ?  8   GLY   A H    1 
ATOM   123  H  H    B GLY   A 1 8   ? 9.670  -8.435  18.411  0.36 24.41 ?  8   GLY   A H    1 
ATOM   124  H  HA2  A GLY   A 1 8   ? 7.780  -8.412  16.880  0.64 18.80 ?  8   GLY   A HA2  1 
ATOM   125  H  HA2  B GLY   A 1 8   ? 7.859  -8.045  17.349  0.36 22.84 ?  8   GLY   A HA2  1 
ATOM   126  H  HA3  A GLY   A 1 8   ? 8.441  -7.047  16.480  0.64 18.80 ?  8   GLY   A HA3  1 
ATOM   127  H  HA3  B GLY   A 1 8   ? 8.435  -6.663  16.885  0.36 22.84 ?  8   GLY   A HA3  1 
ATOM   128  N  N    A TYR   A 1 9   ? 9.784  -9.381  14.908  0.64 13.91 ?  9   TYR   A N    1 
ATOM   129  N  N    B TYR   A 1 9   ? 9.824  -8.999  15.343  0.36 15.84 ?  9   TYR   A N    1 
ATOM   130  C  CA   A TYR   A 1 9   ? 10.061 -9.918  13.586  0.64 12.73 ?  9   TYR   A CA   1 
ATOM   131  C  CA   B TYR   A 1 9   ? 10.078 -9.529  14.009  0.36 14.51 ?  9   TYR   A CA   1 
ATOM   132  C  C    A TYR   A 1 9   ? 9.199  -11.140 13.306  0.64 11.62 ?  9   TYR   A C    1 
ATOM   133  C  C    B TYR   A 1 9   ? 9.248  -10.779 13.747  0.36 13.98 ?  9   TYR   A C    1 
ATOM   134  O  O    A TYR   A 1 9   ? 8.930  -11.953 14.195  0.64 13.22 ?  9   TYR   A O    1 
ATOM   135  O  O    B TYR   A 1 9   ? 9.027  -11.597 14.645  0.36 15.04 ?  9   TYR   A O    1 
ATOM   136  C  CB   A TYR   A 1 9   ? 11.536 -10.315 13.456  0.64 12.98 ?  9   TYR   A CB   1 
ATOM   137  C  CB   B TYR   A 1 9   ? 11.563 -9.853  13.827  0.36 14.24 ?  9   TYR   A CB   1 
ATOM   138  C  CG   A TYR   A 1 9   ? 12.465 -9.136  13.303  0.64 13.11 ?  9   TYR   A CG   1 
ATOM   139  C  CG   B TYR   A 1 9   ? 12.420 -8.634  13.585  0.36 13.72 ?  9   TYR   A CG   1 
ATOM   140  C  CD1  A TYR   A 1 9   ? 12.810 -8.356  14.398  0.64 13.31 ?  9   TYR   A CD1  1 
ATOM   141  C  CD1  B TYR   A 1 9   ? 12.680 -7.739  14.610  0.36 13.80 ?  9   TYR   A CD1  1 
ATOM   142  C  CD2  A TYR   A 1 9   ? 12.976 -8.796  12.061  0.64 13.54 ?  9   TYR   A CD2  1 
ATOM   143  C  CD2  B TYR   A 1 9   ? 12.957 -8.372  12.331  0.36 13.31 ?  9   TYR   A CD2  1 
ATOM   144  C  CE1  A TYR   A 1 9   ? 13.645 -7.269  14.262  0.64 14.22 ?  9   TYR   A CE1  1 
ATOM   145  C  CE1  B TYR   A 1 9   ? 13.450 -6.619  14.396  0.36 13.41 ?  9   TYR   A CE1  1 
ATOM   146  C  CE2  A TYR   A 1 9   ? 13.807 -7.717  11.912  0.64 13.79 ?  9   TYR   A CE2  1 
ATOM   147  C  CE2  B TYR   A 1 9   ? 13.733 -7.251  12.108  0.36 13.17 ?  9   TYR   A CE2  1 
ATOM   148  C  CZ   A TYR   A 1 9   ? 14.136 -6.954  13.013  0.64 14.31 ?  9   TYR   A CZ   1 
ATOM   149  C  CZ   B TYR   A 1 9   ? 13.976 -6.381  13.145  0.36 13.18 ?  9   TYR   A CZ   1 
ATOM   150  O  OH   A TYR   A 1 9   ? 14.968 -5.875  12.855  0.64 15.52 ?  9   TYR   A OH   1 
ATOM   151  O  OH   B TYR   A 1 9   ? 14.741 -5.262  12.929  0.36 13.30 ?  9   TYR   A OH   1 
ATOM   152  H  H    A TYR   A 1 9   ? 10.300 -9.689  15.523  0.64 16.80 ?  9   TYR   A H    1 
ATOM   153  H  H    B TYR   A 1 9   ? 10.375 -9.281  15.946  0.36 19.13 ?  9   TYR   A H    1 
ATOM   154  H  HA   A TYR   A 1 9   ? 9.865  -9.251  12.915  0.64 15.39 ?  9   TYR   A HA   1 
ATOM   155  H  HA   B TYR   A 1 9   ? 9.833  -8.859  13.353  0.36 17.53 ?  9   TYR   A HA   1 
ATOM   156  H  HB2  A TYR   A 1 9   ? 11.802 -10.811 14.248  0.64 15.70 ?  9   TYR   A HB2  1 
ATOM   157  H  HB2  B TYR   A 1 9   ? 11.891 -10.297 14.625  0.36 17.20 ?  9   TYR   A HB2  1 
ATOM   158  H  HB3  A TYR   A 1 9   ? 11.630 -10.877 12.671  0.64 15.70 ?  9   TYR   A HB3  1 
ATOM   159  H  HB3  B TYR   A 1 9   ? 11.659 -10.441 13.062  0.36 17.20 ?  9   TYR   A HB3  1 
ATOM   160  H  HD1  A TYR   A 1 9   ? 12.464 -8.575  15.239  0.64 16.09 ?  9   TYR   A HD1  1 
ATOM   161  H  HD1  B TYR   A 1 9   ? 12.325 -7.897  15.456  0.36 16.68 ?  9   TYR   A HD1  1 
ATOM   162  H  HD2  A TYR   A 1 9   ? 12.752 -9.315  11.319  0.64 16.37 ?  9   TYR   A HD2  1 
ATOM   163  H  HD2  B TYR   A 1 9   ? 12.790 -8.961  11.630  0.36 16.09 ?  9   TYR   A HD2  1 
ATOM   164  H  HE1  A TYR   A 1 9   ? 13.873 -6.761  15.004  0.64 17.18 ?  9   TYR   A HE1  1 
ATOM   165  H  HE1  B TYR   A 1 9   ? 13.619 -6.028  15.094  0.36 16.21 ?  9   TYR   A HE1  1 
ATOM   166  H  HE2  A TYR   A 1 9   ? 14.156 -7.509  11.075  0.64 16.66 ?  9   TYR   A HE2  1 
ATOM   167  H  HE2  B TYR   A 1 9   ? 14.089 -7.086  11.263  0.36 15.92 ?  9   TYR   A HE2  1 
ATOM   168  H  HH   A TYR   A 1 9   ? 15.113 -5.515  13.600  0.64 18.75 ?  9   TYR   A HH   1 
ATOM   169  H  HH   B TYR   A 1 9   ? 14.827 -4.828  13.644  0.36 16.08 ?  9   TYR   A HH   1 
ATOM   170  N  N    A LEU   A 1 10  ? 8.789  -11.271 12.052  0.64 11.54 ?  10  LEU   A N    1 
ATOM   171  N  N    B LEU   A 1 10  ? 8.775  -10.905 12.508  0.36 13.29 ?  10  LEU   A N    1 
ATOM   172  C  CA   A LEU   A 1 10  ? 8.193  -12.500 11.551  0.64 11.27 ?  10  LEU   A CA   1 
ATOM   173  C  CA   B LEU   A 1 10  ? 8.116  -12.112 12.030  0.36 13.53 ?  10  LEU   A CA   1 
ATOM   174  C  C    A LEU   A 1 10  ? 9.319  -13.438 11.120  0.64 11.28 ?  10  LEU   A C    1 
ATOM   175  C  C    B LEU   A 1 10  ? 9.179  -13.084 11.535  0.36 12.82 ?  10  LEU   A C    1 
ATOM   176  O  O    A LEU   A 1 10  ? 10.271 -13.008 10.457  0.64 11.41 ?  10  LEU   A O    1 
ATOM   177  O  O    B LEU   A 1 10  ? 10.103 -12.692 10.815  0.36 12.21 ?  10  LEU   A O    1 
ATOM   178  C  CB   A LEU   A 1 10  ? 7.306  -12.170 10.354  0.64 11.85 ?  10  LEU   A CB   1 
ATOM   179  C  CB   B LEU   A 1 10  ? 7.163  -11.757 10.889  0.36 14.31 ?  10  LEU   A CB   1 
ATOM   180  C  CG   A LEU   A 1 10  ? 6.587  -13.335 9.687   0.64 14.21 ?  10  LEU   A CG   1 
ATOM   181  C  CG   B LEU   A 1 10  ? 6.304  -12.876 10.313  0.36 15.61 ?  10  LEU   A CG   1 
ATOM   182  C  CD1  A LEU   A 1 10  ? 5.546  -13.914 10.623  0.64 15.23 ?  10  LEU   A CD1  1 
ATOM   183  C  CD1  B LEU   A 1 10  ? 5.401  -13.441 11.394  0.36 16.17 ?  10  LEU   A CD1  1 
ATOM   184  C  CD2  A LEU   A 1 10  ? 5.951  -12.885 8.383   0.64 15.20 ?  10  LEU   A CD2  1 
ATOM   185  C  CD2  B LEU   A 1 10  ? 5.481  -12.334 9.155   0.36 16.51 ?  10  LEU   A CD2  1 
ATOM   186  H  H    A LEU   A 1 10  ? 8.853  -10.658 11.452  0.64 13.96 ?  10  LEU   A H    1 
ATOM   187  H  H    B LEU   A 1 10  ? 8.818  -10.281 11.915  0.36 16.07 ?  10  LEU   A H    1 
ATOM   188  H  HA   A LEU   A 1 10  ? 7.666  -12.931 12.247  0.64 13.63 ?  10  LEU   A HA   1 
ATOM   189  H  HA   B LEU   A 1 10  ? 7.610  -12.524 12.750  0.36 16.35 ?  10  LEU   A HA   1 
ATOM   190  H  HB2  A LEU   A 1 10  ? 6.630  -11.550 10.645  0.64 14.33 ?  10  LEU   A HB2  1 
ATOM   191  H  HB2  B LEU   A 1 10  ? 6.550  -11.072 11.207  0.36 17.29 ?  10  LEU   A HB2  1 
ATOM   192  H  HB3  A LEU   A 1 10  ? 7.862  -11.760 9.678   0.64 14.33 ?  10  LEU   A HB3  1 
ATOM   193  H  HB3  B LEU   A 1 10  ? 7.686  -11.398 10.159  0.36 17.29 ?  10  LEU   A HB3  1 
ATOM   194  H  HG   A LEU   A 1 10  ? 7.226  -14.041 9.482   0.64 17.16 ?  10  LEU   A HG   1 
ATOM   195  H  HG   B LEU   A 1 10  ? 6.875  -13.587 9.980   0.36 18.84 ?  10  LEU   A HG   1 
ATOM   196  H  HD11 A LEU   A 1 10  ? 5.115  -14.672 10.195  0.64 18.39 ?  10  LEU   A HD11 1 
ATOM   197  H  HD11 B LEU   A 1 10  ? 4.808  -14.097 10.998  0.36 19.52 ?  10  LEU   A HD11 1 
ATOM   198  H  HD12 A LEU   A 1 10  ? 5.975  -14.200 11.444  0.64 18.39 ?  10  LEU   A HD12 1 
ATOM   199  H  HD12 B LEU   A 1 10  ? 5.946  -13.856 12.078  0.36 19.52 ?  10  LEU   A HD12 1 
ATOM   200  H  HD13 A LEU   A 1 10  ? 4.885  -13.230 10.820  0.64 18.39 ?  10  LEU   A HD13 1 
ATOM   201  H  HD13 B LEU   A 1 10  ? 4.882  -12.716 11.779  0.36 19.52 ?  10  LEU   A HD13 1 
ATOM   202  H  HD21 A LEU   A 1 10  ? 5.495  -13.641 7.977   0.64 18.36 ?  10  LEU   A HD21 1 
ATOM   203  H  HD21 B LEU   A 1 10  ? 4.938  -13.048 8.791   0.36 19.93 ?  10  LEU   A HD21 1 
ATOM   204  H  HD22 A LEU   A 1 10  ? 5.317  -12.179 8.573   0.64 18.36 ?  10  LEU   A HD22 1 
ATOM   205  H  HD22 B LEU   A 1 10  ? 4.912  -11.618 9.483   0.36 19.93 ?  10  LEU   A HD22 1 
ATOM   206  H  HD23 A LEU   A 1 10  ? 6.646  -12.562 7.791   0.64 18.36 ?  10  LEU   A HD23 1 
ATOM   207  H  HD23 B LEU   A 1 10  ? 6.081  -11.991 8.474   0.36 19.93 ?  10  LEU   A HD23 1 
ATOM   208  N  N    A LYS   A 1 11  ? 9.219  -14.710 11.511  0.64 11.84 ?  11  LYS   A N    1 
ATOM   209  N  N    B LYS   A 1 11  ? 9.052  -14.346 11.926  0.36 12.58 ?  11  LYS   A N    1 
ATOM   210  C  CA   A LYS   A 1 11  ? 10.221 -15.713 11.175  0.64 11.97 ?  11  LYS   A CA   1 
ATOM   211  C  CA   B LYS   A 1 11  ? 10.018 -15.365 11.542  0.36 12.09 ?  11  LYS   A CA   1 
ATOM   212  C  C    A LYS   A 1 11  ? 9.867  -16.313 9.822   0.64 12.00 ?  11  LYS   A C    1 
ATOM   213  C  C    B LYS   A 1 11  ? 9.659  -15.901 10.160  0.36 11.59 ?  11  LYS   A C    1 
ATOM   214  O  O    A LYS   A 1 11  ? 8.803  -16.920 9.671   0.64 13.76 ?  11  LYS   A O    1 
ATOM   215  O  O    B LYS   A 1 11  ? 8.538  -16.375 9.947   0.36 11.84 ?  11  LYS   A O    1 
ATOM   216  C  CB   A LYS   A 1 11  ? 10.275 -16.790 12.261  0.64 12.25 ?  11  LYS   A CB   1 
ATOM   217  C  CB   B LYS   A 1 11  ? 10.007 -16.487 12.576  0.36 12.03 ?  11  LYS   A CB   1 
ATOM   218  C  CG   A LYS   A 1 11  ? 11.311 -17.898 12.050  0.64 12.77 ?  11  LYS   A CG   1 
ATOM   219  C  CG   B LYS   A 1 11  ? 11.016 -17.589 12.336  0.36 12.03 ?  11  LYS   A CG   1 
ATOM   220  C  CD   A LYS   A 1 11  ? 11.447 -18.729 13.331  0.64 13.25 ?  11  LYS   A CD   1 
ATOM   221  C  CD   B LYS   A 1 11  ? 11.023 -18.557 13.506  0.36 12.23 ?  11  LYS   A CD   1 
ATOM   222  C  CE   A LYS   A 1 11  ? 12.430 -19.888 13.207  0.64 13.54 ?  11  LYS   A CE   1 
ATOM   223  C  CE   B LYS   A 1 11  ? 12.021 -19.683 13.297  0.36 11.96 ?  11  LYS   A CE   1 
ATOM   224  N  NZ   A LYS   A 1 11  ? 13.802 -19.429 12.883  0.64 13.58 ?  11  LYS   A NZ   1 
ATOM   225  N  NZ   B LYS   A 1 11  ? 13.421 -19.174 13.223  0.36 11.84 ?  11  LYS   A NZ   1 
ATOM   226  H  H    A LYS   A 1 11  ? 8.565  -15.021 11.976  0.64 14.32 ?  11  LYS   A H    1 
ATOM   227  H  H    B LYS   A 1 11  ? 8.408  -14.637 12.415  0.36 15.21 ?  11  LYS   A H    1 
ATOM   228  H  HA   A LYS   A 1 11  ? 11.094 -15.296 11.112  0.64 14.48 ?  11  LYS   A HA   1 
ATOM   229  H  HA   B LYS   A 1 11  ? 10.907 -14.972 11.507  0.36 14.63 ?  11  LYS   A HA   1 
ATOM   230  H  HB2  A LYS   A 1 11  ? 10.486 -16.363 13.108  0.64 14.82 ?  11  LYS   A HB2  1 
ATOM   231  H  HB2  B LYS   A 1 11  ? 10.196 -16.101 13.446  0.36 14.55 ?  11  LYS   A HB2  1 
ATOM   232  H  HB3  A LYS   A 1 11  ? 9.409  -17.216 12.321  0.64 14.82 ?  11  LYS   A HB3  1 
ATOM   233  H  HB3  B LYS   A 1 11  ? 9.128  -16.889 12.580  0.36 14.55 ?  11  LYS   A HB3  1 
ATOM   234  H  HG2  A LYS   A 1 11  ? 11.023 -18.488 11.333  0.64 15.44 ?  11  LYS   A HG2  1 
ATOM   235  H  HG2  B LYS   A 1 11  ? 10.778 -18.080 11.534  0.36 14.55 ?  11  LYS   A HG2  1 
ATOM   236  H  HG3  A LYS   A 1 11  ? 12.177 -17.511 11.844  0.64 15.44 ?  11  LYS   A HG3  1 
ATOM   237  H  HG3  B LYS   A 1 11  ? 11.904 -17.207 12.249  0.36 14.55 ?  11  LYS   A HG3  1 
ATOM   238  H  HD2  A LYS   A 1 11  ? 11.756 -18.157 14.049  0.64 16.01 ?  11  LYS   A HD2  1 
ATOM   239  H  HD2  B LYS   A 1 11  ? 11.267 -18.081 14.316  0.36 14.79 ?  11  LYS   A HD2  1 
ATOM   240  H  HD3  A LYS   A 1 11  ? 10.580 -19.104 13.558  0.64 16.01 ?  11  LYS   A HD3  1 
ATOM   241  H  HD3  B LYS   A 1 11  ? 10.138 -18.948 13.604  0.36 14.79 ?  11  LYS   A HD3  1 
ATOM   242  H  HE2  A LYS   A 1 11  ? 12.466 -20.370 14.053  0.64 16.37 ?  11  LYS   A HE2  1 
ATOM   243  H  HE2  B LYS   A 1 11  ? 11.962 -20.306 14.038  0.36 14.47 ?  11  LYS   A HE2  1 
ATOM   244  H  HE3  A LYS   A 1 11  ? 12.135 -20.484 12.502  0.64 16.37 ?  11  LYS   A HE3  1 
ATOM   245  H  HE3  B LYS   A 1 11  ? 11.819 -20.137 12.462  0.36 14.47 ?  11  LYS   A HE3  1 
ATOM   246  H  HZ1  A LYS   A 1 11  ? 14.350 -20.131 12.822  0.64 16.41 ?  11  LYS   A HZ1  1 
ATOM   247  H  HZ1  B LYS   A 1 11  ? 13.987 -19.852 13.124  0.36 14.32 ?  11  LYS   A HZ1  1 
ATOM   248  H  HZ2  A LYS   A 1 11  ? 13.800 -18.996 12.108  0.64 16.41 ?  11  LYS   A HZ2  1 
ATOM   249  H  HZ2  B LYS   A 1 11  ? 13.507 -18.621 12.530  0.36 14.32 ?  11  LYS   A HZ2  1 
ATOM   250  H  HZ3  A LYS   A 1 11  ? 14.100 -18.887 13.521  0.64 16.41 ?  11  LYS   A HZ3  1 
ATOM   251  H  HZ3  B LYS   A 1 11  ? 13.623 -18.734 13.970  0.36 14.32 ?  11  LYS   A HZ3  1 
ATOM   252  N  N    A LEU   A 1 12  ? 10.758 -16.158 8.841   0.64 11.20 ?  12  LEU   A N    1 
ATOM   253  N  N    B LEU   A 1 12  ? 10.592 -15.800 9.213   0.36 11.64 ?  12  LEU   A N    1 
ATOM   254  C  CA   A LEU   A 1 12  ? 10.504 -16.736 7.525   0.64 11.07 ?  12  LEU   A CA   1 
ATOM   255  C  CA   B LEU   A 1 12  ? 10.374 -16.315 7.865   0.36 11.97 ?  12  LEU   A CA   1 
ATOM   256  C  C    A LEU   A 1 12  ? 11.095 -18.132 7.370   0.64 11.44 ?  12  LEU   A C    1 
ATOM   257  C  C    B LEU   A 1 12  ? 10.937 -17.718 7.676   0.36 11.85 ?  12  LEU   A C    1 
ATOM   258  O  O    A LEU   A 1 12  ? 10.467 -19.002 6.756   0.64 12.01 ?  12  LEU   A O    1 
ATOM   259  O  O    B LEU   A 1 12  ? 10.271 -18.586 7.102   0.36 11.99 ?  12  LEU   A O    1 
ATOM   260  C  CB   A LEU   A 1 12  ? 11.049 -15.832 6.415   0.64 11.46 ?  12  LEU   A CB   1 
ATOM   261  C  CB   B LEU   A 1 12  ? 10.978 -15.365 6.821   0.36 12.84 ?  12  LEU   A CB   1 
ATOM   262  C  CG   A LEU   A 1 12  ? 10.390 -14.465 6.226   0.64 12.38 ?  12  LEU   A CG   1 
ATOM   263  C  CG   B LEU   A 1 12  ? 10.301 -14.001 6.687   0.36 13.77 ?  12  LEU   A CG   1 
ATOM   264  C  CD1  A LEU   A 1 12  ? 11.146 -13.677 5.173   0.64 12.88 ?  12  LEU   A CD1  1 
ATOM   265  C  CD1  B LEU   A 1 12  ? 10.868 -13.222 5.504   0.36 14.15 ?  12  LEU   A CD1  1 
ATOM   266  C  CD2  A LEU   A 1 12  ? 8.919  -14.620 5.837   0.64 13.13 ?  12  LEU   A CD2  1 
ATOM   267  C  CD2  B LEU   A 1 12  ? 8.797  -14.165 6.552   0.36 14.00 ?  12  LEU   A CD2  1 
ATOM   268  H  H    A LEU   A 1 12  ? 11.512 -15.732 8.912   0.64 13.56 ?  12  LEU   A H    1 
ATOM   269  H  H    B LEU   A 1 12  ? 11.361 -15.416 9.325   0.36 14.08 ?  12  LEU   A H    1 
ATOM   270  H  HA   A LEU   A 1 12  ? 9.551  -16.812 7.406   0.64 13.40 ?  12  LEU   A HA   1 
ATOM   271  H  HA   B LEU   A 1 12  ? 9.420  -16.362 7.709   0.36 14.48 ?  12  LEU   A HA   1 
ATOM   272  H  HB2  A LEU   A 1 12  ? 11.988 -15.673 6.587   0.64 13.86 ?  12  LEU   A HB2  1 
ATOM   273  H  HB2  B LEU   A 1 12  ? 11.907 -15.202 7.050   0.36 15.52 ?  12  LEU   A HB2  1 
ATOM   274  H  HB3  A LEU   A 1 12  ? 10.957 -16.310 5.574   0.64 13.86 ?  12  LEU   A HB3  1 
ATOM   275  H  HB3  B LEU   A 1 12  ? 10.930 -15.795 5.953   0.36 15.52 ?  12  LEU   A HB3  1 
ATOM   276  H  HG   A LEU   A 1 12  ? 10.429 -13.974 7.060   0.64 14.97 ?  12  LEU   A HG   1 
ATOM   277  H  HG   B LEU   A 1 12  ? 10.473 -13.483 7.490   0.36 16.64 ?  12  LEU   A HG   1 
ATOM   278  H  HD11 A LEU   A 1 12  ? 10.718 -12.818 5.051   0.64 15.58 ?  12  LEU   A HD11 1 
ATOM   279  H  HD11 B LEU   A 1 12  ? 10.425 -12.359 5.452   0.36 17.10 ?  12  LEU   A HD11 1 
ATOM   280  H  HD12 A LEU   A 1 12  ? 12.062 -13.553 5.472   0.64 15.58 ?  12  LEU   A HD12 1 
ATOM   281  H  HD12 B LEU   A 1 12  ? 11.820 -13.097 5.636   0.36 17.10 ?  12  LEU   A HD12 1 
ATOM   282  H  HD13 A LEU   A 1 12  ? 11.138 -14.175 4.339   0.64 15.58 ?  12  LEU   A HD13 1 
ATOM   283  H  HD13 B LEU   A 1 12  ? 10.708 -13.725 4.690   0.36 17.10 ?  12  LEU   A HD13 1 
ATOM   284  H  HD21 A LEU   A 1 12  ? 8.544  -13.747 5.648   0.64 15.88 ?  12  LEU   A HD21 1 
ATOM   285  H  HD21 B LEU   A 1 12  ? 8.417  -13.343 6.209   0.36 16.92 ?  12  LEU   A HD21 1 
ATOM   286  H  HD22 A LEU   A 1 12  ? 8.857  -15.182 5.046   0.64 15.88 ?  12  LEU   A HD22 1 
ATOM   287  H  HD22 B LEU   A 1 12  ? 8.614  -14.898 5.945   0.36 16.92 ?  12  LEU   A HD22 1 
ATOM   288  H  HD23 A LEU   A 1 12  ? 8.435  -15.035 6.570   0.64 15.88 ?  12  LEU   A HD23 1 
ATOM   289  H  HD23 B LEU   A 1 12  ? 8.423  -14.361 7.428   0.36 16.92 ?  12  LEU   A HD23 1 
ATOM   290  N  N    A THR   A 1 13  ? 12.299 -18.348 7.894   0.64 11.72 ?  13  THR   A N    1 
ATOM   291  N  N    B THR   A 1 13  ? 12.160 -17.950 8.138   0.36 12.00 ?  13  THR   A N    1 
ATOM   292  C  CA   A THR   A 1 13  ? 13.004 -19.623 7.806   0.64 12.36 ?  13  THR   A CA   1 
ATOM   293  C  CA   B THR   A 1 13  ? 12.805 -19.248 8.022   0.36 12.26 ?  13  THR   A CA   1 
ATOM   294  C  C    A THR   A 1 13  ? 13.782 -19.824 9.100   0.64 12.84 ?  13  THR   A C    1 
ATOM   295  C  C    B THR   A 1 13  ? 13.557 -19.526 9.315   0.36 12.79 ?  13  THR   A C    1 
ATOM   296  O  O    A THR   A 1 13  ? 13.679 -19.035 10.044  0.64 12.76 ?  13  THR   A O    1 
ATOM   297  O  O    B THR   A 1 13  ? 13.456 -18.785 10.299  0.36 12.90 ?  13  THR   A O    1 
ATOM   298  C  CB   A THR   A 1 13  ? 13.980 -19.675 6.621   0.64 13.39 ?  13  THR   A CB   1 
ATOM   299  C  CB   B THR   A 1 13  ? 13.771 -19.291 6.829   0.36 12.49 ?  13  THR   A CB   1 
ATOM   300  O  OG1  A THR   A 1 13  ? 15.057 -18.761 6.853   0.64 13.59 ?  13  THR   A OG1  1 
ATOM   301  O  OG1  B THR   A 1 13  ? 14.833 -18.360 7.053   0.36 12.43 ?  13  THR   A OG1  1 
ATOM   302  C  CG2  A THR   A 1 13  ? 13.303 -19.334 5.308   0.64 14.48 ?  13  THR   A CG2  1 
ATOM   303  C  CG2  B THR   A 1 13  ? 13.062 -18.970 5.514   0.36 12.96 ?  13  THR   A CG2  1 
ATOM   304  H  H    A THR   A 1 13  ? 12.751 -17.751 8.316   0.64 14.18 ?  13  THR   A H    1 
ATOM   305  H  H    B THR   A 1 13  ? 12.647 -17.349 8.518   0.36 14.51 ?  13  THR   A H    1 
ATOM   306  H  HA   A THR   A 1 13  ? 12.368 -20.351 7.709   0.64 14.94 ?  13  THR   A HA   1 
ATOM   307  H  HA   B THR   A 1 13  ? 12.135 -19.932 7.900   0.36 14.83 ?  13  THR   A HA   1 
ATOM   308  H  HB   A THR   A 1 13  ? 14.347 -20.571 6.543   0.64 16.18 ?  13  THR   A HB   1 
ATOM   309  H  HB   B THR   A 1 13  ? 14.152 -20.176 6.755   0.36 15.10 ?  13  THR   A HB   1 
ATOM   310  H  HG1  A THR   A 1 13  ? 15.595 -18.775 6.199   0.64 16.42 ?  13  THR   A HG1  1 
ATOM   311  H  HG1  B THR   A 1 13  ? 15.366 -18.359 6.397   0.36 15.04 ?  13  THR   A HG1  1 
ATOM   312  H  HG21 A THR   A 1 13  ? 13.901 -19.527 4.569   0.64 17.49 ?  13  THR   A HG21 1 
ATOM   313  H  HG21 B THR   A 1 13  ? 13.684 -19.057 4.771   0.36 15.67 ?  13  THR   A HG21 1 
ATOM   314  H  HG22 A THR   A 1 13  ? 12.498 -19.865 5.208   0.64 17.49 ?  13  THR   A HG22 1 
ATOM   315  H  HG22 B THR   A 1 13  ? 12.327 -19.591 5.377   0.36 15.67 ?  13  THR   A HG22 1 
ATOM   316  H  HG23 A THR   A 1 13  ? 13.069 -18.395 5.291   0.64 17.49 ?  13  THR   A HG23 1 
ATOM   317  H  HG23 B THR   A 1 13  ? 12.715 -18.068 5.529   0.36 15.67 ?  13  THR   A HG23 1 
ATOM   318  N  N    A ASP   A 1 14  ? 14.611 -20.871 9.124   0.64 13.68 ?  14  ASP   A N    1 
ATOM   319  N  N    B ASP   A 1 14  ? 14.328 -20.609 9.288   0.36 13.47 ?  14  ASP   A N    1 
ATOM   320  C  CA   A ASP   A 1 14  ? 15.430 -21.132 10.299  0.64 14.64 ?  14  ASP   A CA   1 
ATOM   321  C  CA   B ASP   A 1 14  ? 15.210 -20.942 10.395  0.36 14.45 ?  14  ASP   A CA   1 
ATOM   322  C  C    A ASP   A 1 14  ? 16.256 -19.921 10.722  0.64 14.23 ?  14  ASP   A C    1 
ATOM   323  C  C    B ASP   A 1 14  ? 16.085 -19.754 10.769  0.36 13.75 ?  14  ASP   A C    1 
ATOM   324  O  O    A ASP   A 1 14  ? 16.533 -19.750 11.915  0.64 15.17 ?  14  ASP   A O    1 
ATOM   325  O  O    B ASP   A 1 14  ? 16.228 -19.432 11.955  0.36 13.49 ?  14  ASP   A O    1 
ATOM   326  C  CB   A ASP   A 1 14  ? 16.366 -22.305 10.033  0.64 16.69 ?  14  ASP   A CB   1 
ATOM   327  C  CB   B ASP   A 1 14  ? 16.068 -22.140 9.988   0.36 16.43 ?  14  ASP   A CB   1 
ATOM   328  C  CG   A ASP   A 1 14  ? 17.240 -22.598 11.211  0.64 19.96 ?  14  ASP   A CG   1 
ATOM   329  C  CG   B ASP   A 1 14  ? 17.093 -22.525 11.045  0.36 18.74 ?  14  ASP   A CG   1 
ATOM   330  O  OD1  A ASP   A 1 14  ? 16.702 -23.107 12.217  0.64 20.78 ?  14  ASP   A OD1  1 
ATOM   331  O  OD1  B ASP   A 1 14  ? 16.815 -22.341 12.250  0.36 19.60 ?  14  ASP   A OD1  1 
ATOM   332  O  OD2  A ASP   A 1 14  ? 18.438 -22.276 11.140  0.64 21.68 -1 14  ASP   A OD2  1 
ATOM   333  O  OD2  B ASP   A 1 14  ? 18.179 -23.018 10.669  0.36 19.69 -1 14  ASP   A OD2  1 
ATOM   334  H  H    A ASP   A 1 14  ? 14.734 -21.434 8.476   0.64 16.54 ?  14  ASP   A H    1 
ATOM   335  H  H    B ASP   A 1 14  ? 14.365 -21.152 8.632   0.36 16.28 ?  14  ASP   A H    1 
ATOM   336  H  HA   A ASP   A 1 14  ? 14.861 -21.378 11.039  0.64 17.68 ?  14  ASP   A HA   1 
ATOM   337  H  HA   B ASP   A 1 14  ? 14.677 -21.184 11.167  0.36 17.45 ?  14  ASP   A HA   1 
ATOM   338  H  HB2  A ASP   A 1 14  ? 15.846 -23.112 9.863   0.64 20.15 ?  14  ASP   A HB2  1 
ATOM   339  H  HB2  B ASP   A 1 14  ? 15.480 -22.903 9.845   0.36 19.83 ?  14  ASP   A HB2  1 
ATOM   340  H  HB3  A ASP   A 1 14  ? 16.936 -22.116 9.273   0.64 20.15 ?  14  ASP   A HB3  1 
ATOM   341  H  HB3  B ASP   A 1 14  ? 16.530 -21.926 9.161   0.36 19.83 ?  14  ASP   A HB3  1 
ATOM   342  N  N    . ASN   A 1 15  ? 16.656 -19.068 9.772   1.00 13.78 ?  15  ASN   A N    1 
ATOM   343  C  CA   . ASN   A 1 15  ? 17.639 -18.021 10.033  1.00 14.30 ?  15  ASN   A CA   1 
ATOM   344  C  C    . ASN   A 1 15  ? 17.267 -16.630 9.530   1.00 14.28 ?  15  ASN   A C    1 
ATOM   345  O  O    . ASN   A 1 15  ? 18.056 -15.709 9.741   1.00 15.87 ?  15  ASN   A O    1 
ATOM   346  C  CB   . ASN   A 1 15  ? 19.009 -18.424 9.457   1.00 14.17 ?  15  ASN   A CB   1 
ATOM   347  C  CG   . ASN   A 1 15  ? 18.998 -18.520 7.945   1.00 14.64 ?  15  ASN   A CG   1 
ATOM   348  O  OD1  . ASN   A 1 15  ? 18.278 -19.342 7.370   1.00 15.51 ?  15  ASN   A OD1  1 
ATOM   349  N  ND2  . ASN   A 1 15  ? 19.794 -17.674 7.289   1.00 14.55 ?  15  ASN   A ND2  1 
ATOM   350  H  H    A ASN   A 1 15  ? 16.365 -19.078 8.968   0.64 16.66 ?  15  ASN   A H    1 
ATOM   351  H  H    B ASN   A 1 15  ? 16.498 -19.202 8.941   0.36 16.66 ?  15  ASN   A H    1 
ATOM   352  H  HA   . ASN   A 1 15  ? 17.756 -17.943 10.993  1.00 17.28 ?  15  ASN   A HA   1 
ATOM   353  H  HB2  . ASN   A 1 15  ? 19.671 -17.751 9.716   1.00 17.11 ?  15  ASN   A HB2  1 
ATOM   354  H  HB3  . ASN   A 1 15  ? 19.269 -19.286 9.817   1.00 17.11 ?  15  ASN   A HB3  1 
ATOM   355  H  HD21 . ASN   A 1 15  ? 19.820 -17.688 6.430   1.00 17.58 ?  15  ASN   A HD21 1 
ATOM   356  H  HD22 . ASN   A 1 15  ? 20.282 -17.107 7.721   1.00 17.58 ?  15  ASN   A HD22 1 
ATOM   357  N  N    A VAL   A 1 16  ? 16.180 -16.490 8.766   0.64 13.41 ?  16  VAL   A N    1 
ATOM   358  N  N    B VAL   A 1 16  ? 16.057 -16.393 9.024   0.36 13.07 ?  16  VAL   A N    1 
ATOM   359  C  CA   A VAL   A 1 16  ? 15.781 -15.236 8.135   0.64 13.00 ?  16  VAL   A CA   1 
ATOM   360  C  CA   B VAL   A 1 16  ? 15.692 -15.074 8.508   0.36 11.90 ?  16  VAL   A CA   1 
ATOM   361  C  C    A VAL   A 1 16  ? 14.496 -14.740 8.786   0.64 12.17 ?  16  VAL   A C    1 
ATOM   362  C  C    B VAL   A 1 16  ? 14.436 -14.553 9.204   0.36 11.65 ?  16  VAL   A C    1 
ATOM   363  O  O    A VAL   A 1 16  ? 13.481 -15.451 8.821   0.64 11.33 ?  16  VAL   A O    1 
ATOM   364  O  O    B VAL   A 1 16  ? 13.461 -15.291 9.390   0.36 11.41 ?  16  VAL   A O    1 
ATOM   365  C  CB   A VAL   A 1 16  ? 15.608 -15.385 6.611   0.64 13.47 ?  16  VAL   A CB   1 
ATOM   366  C  CB   B VAL   A 1 16  ? 15.538 -15.076 6.972   0.36 11.56 ?  16  VAL   A CB   1 
ATOM   367  C  CG1  A VAL   A 1 16  ? 15.151 -14.067 5.992   0.64 13.94 ?  16  VAL   A CG1  1 
ATOM   368  C  CG1  B VAL   A 1 16  ? 15.199 -13.675 6.460   0.36 11.44 ?  16  VAL   A CG1  1 
ATOM   369  C  CG2  A VAL   A 1 16  ? 16.900 -15.856 5.955   0.64 14.04 ?  16  VAL   A CG2  1 
ATOM   370  C  CG2  B VAL   A 1 16  ? 16.807 -15.599 6.313   0.36 12.19 ?  16  VAL   A CG2  1 
ATOM   371  H  H    A VAL   A 1 16  ? 15.656 -17.150 8.582   0.64 16.21 ?  16  VAL   A H    1 
ATOM   372  H  H    B VAL   A 1 16  ? 15.420 -16.971 8.992   0.36 15.80 ?  16  VAL   A H    1 
ATOM   373  H  HA   A VAL   A 1 16  ? 16.479 -14.582 8.288   0.64 15.71 ?  16  VAL   A HA   1 
ATOM   374  H  HA   B VAL   A 1 16  ? 16.398 -14.450 8.719   0.36 14.40 ?  16  VAL   A HA   1 
ATOM   375  H  HB   A VAL   A 1 16  ? 14.930 -16.057 6.433   0.64 16.28 ?  16  VAL   A HB   1 
ATOM   376  H  HB   B VAL   A 1 16  ? 14.812 -15.667 6.730   0.36 13.99 ?  16  VAL   A HB   1 
ATOM   377  H  HG11 A VAL   A 1 16  ? 15.219 -14.135 5.026   0.64 16.85 ?  16  VAL   A HG11 1 
ATOM   378  H  HG11 B VAL   A 1 16  ? 15.274 -13.668 5.492   0.36 13.84 ?  16  VAL   A HG11 1 
ATOM   379  H  HG12 A VAL   A 1 16  ? 14.231 -13.904 6.248   0.64 16.85 ?  16  VAL   A HG12 1 
ATOM   380  H  HG12 B VAL   A 1 16  ? 14.292 -13.452 6.720   0.36 13.84 ?  16  VAL   A HG12 1 
ATOM   381  H  HG13 A VAL   A 1 16  ? 15.722 -13.356 6.316   0.64 16.85 ?  16  VAL   A HG13 1 
ATOM   382  H  HG13 B VAL   A 1 16  ? 15.821 -13.037 6.843   0.36 13.84 ?  16  VAL   A HG13 1 
ATOM   383  H  HG21 A VAL   A 1 16  ? 16.797 -15.816 4.991   0.64 16.97 ?  16  VAL   A HG21 1 
ATOM   384  H  HG21 B VAL   A 1 16  ? 16.821 -15.324 5.384   0.36 14.74 ?  16  VAL   A HG21 1 
ATOM   385  H  HG22 A VAL   A 1 16  ? 17.625 -15.277 6.234   0.64 16.97 ?  16  VAL   A HG22 1 
ATOM   386  H  HG22 B VAL   A 1 16  ? 17.578 -15.242 6.778   0.36 14.74 ?  16  VAL   A HG22 1 
ATOM   387  H  HG23 A VAL   A 1 16  ? 17.083 -16.770 6.230   0.64 16.97 ?  16  VAL   A HG23 1 
ATOM   388  H  HG23 B VAL   A 1 16  ? 16.813 -16.569 6.371   0.36 14.74 ?  16  VAL   A HG23 1 
ATOM   389  N  N    A TYR   A 1 17  ? 14.543 -13.501 9.262   0.64 11.94 ?  17  TYR   A N    1 
ATOM   390  N  N    B TYR   A 1 17  ? 14.468 -13.262 9.571   0.36 11.67 ?  17  TYR   A N    1 
ATOM   391  C  CA   A TYR   A 1 17  ? 13.453 -12.812 9.931   0.64 11.81 ?  17  TYR   A CA   1 
ATOM   392  C  CA   B TYR   A 1 17  ? 13.399 -12.580 10.295  0.36 11.34 ?  17  TYR   A CA   1 
ATOM   393  C  C    A TYR   A 1 17  ? 13.179 -11.499 9.204   0.64 11.85 ?  17  TYR   A C    1 
ATOM   394  C  C    B TYR   A 1 17  ? 13.137 -11.227 9.643   0.36 10.67 ?  17  TYR   A C    1 
ATOM   395  O  O    A TYR   A 1 17  ? 14.073 -10.948 8.557   0.64 11.40 ?  17  TYR   A O    1 
ATOM   396  O  O    B TYR   A 1 17  ? 14.060 -10.615 9.105   0.36 10.39 ?  17  TYR   A O    1 
ATOM   397  C  CB   A TYR   A 1 17  ? 13.850 -12.524 11.381  0.64 12.47 ?  17  TYR   A CB   1 
ATOM   398  C  CB   B TYR   A 1 17  ? 13.803 -12.382 11.767  0.36 12.25 ?  17  TYR   A CB   1 
ATOM   399  C  CG   A TYR   A 1 17  ? 14.005 -13.767 12.229  0.64 14.24 ?  17  TYR   A CG   1 
ATOM   400  C  CG   B TYR   A 1 17  ? 14.092 -13.685 12.491  0.36 13.34 ?  17  TYR   A CG   1 
ATOM   401  C  CD1  A TYR   A 1 17  ? 15.164 -14.541 12.187  0.64 15.23 ?  17  TYR   A CD1  1 
ATOM   402  C  CD1  B TYR   A 1 17  ? 15.307 -14.348 12.334  0.36 14.07 ?  17  TYR   A CD1  1 
ATOM   403  C  CD2  A TYR   A 1 17  ? 12.977 -14.181 13.065  0.64 14.44 ?  17  TYR   A CD2  1 
ATOM   404  C  CD2  B TYR   A 1 17  ? 13.140 -14.259 13.322  0.36 13.74 ?  17  TYR   A CD2  1 
ATOM   405  C  CE1  A TYR   A 1 17  ? 15.291 -15.690 12.964  0.64 15.61 ?  17  TYR   A CE1  1 
ATOM   406  C  CE1  B TYR   A 1 17  ? 15.562 -15.547 12.989  0.36 14.56 ?  17  TYR   A CE1  1 
ATOM   407  C  CE2  A TYR   A 1 17  ? 13.090 -15.330 13.840  0.64 15.34 ?  17  TYR   A CE2  1 
ATOM   408  C  CE2  B TYR   A 1 17  ? 13.386 -15.457 13.981  0.36 14.37 ?  17  TYR   A CE2  1 
ATOM   409  C  CZ   A TYR   A 1 17  ? 14.250 -16.079 13.791  0.64 15.60 ?  17  TYR   A CZ   1 
ATOM   410  C  CZ   B TYR   A 1 17  ? 14.597 -16.098 13.813  0.36 14.48 ?  17  TYR   A CZ   1 
ATOM   411  O  OH   A TYR   A 1 17  ? 14.361 -17.217 14.563  0.64 16.00 ?  17  TYR   A OH   1 
ATOM   412  O  OH   B TYR   A 1 17  ? 14.838 -17.285 14.471  0.36 14.95 ?  17  TYR   A OH   1 
ATOM   413  H  H    A TYR   A 1 17  ? 15.250 -13.022 9.199   0.64 14.44 ?  17  TYR   A H    1 
ATOM   414  H  H    B TYR   A 1 17  ? 15.136 -12.729 9.404   0.36 14.12 ?  17  TYR   A H    1 
ATOM   415  H  HA   A TYR   A 1 17  ? 12.657 -13.373 9.920   0.64 14.29 ?  17  TYR   A HA   1 
ATOM   416  H  HA   B TYR   A 1 17  ? 12.585 -13.094 10.255  0.36 13.72 ?  17  TYR   A HA   1 
ATOM   417  H  HB2  A TYR   A 1 17  ? 14.698 -12.060 11.387  0.64 15.08 ?  17  TYR   A HB2  1 
ATOM   418  H  HB2  B TYR   A 1 17  ? 14.603 -11.833 11.802  0.36 14.81 ?  17  TYR   A HB2  1 
ATOM   419  H  HB3  A TYR   A 1 17  ? 13.166 -11.979 11.784  0.64 15.08 ?  17  TYR   A HB3  1 
ATOM   420  H  HB3  B TYR   A 1 17  ? 13.079 -11.931 12.234  0.36 14.81 ?  17  TYR   A HB3  1 
ATOM   421  H  HD1  A TYR   A 1 17  ? 15.869 -14.288 11.633  0.64 18.39 ?  17  TYR   A HD1  1 
ATOM   422  H  HD1  B TYR   A 1 17  ? 15.958 -13.984 11.777  0.36 16.99 ?  17  TYR   A HD1  1 
ATOM   423  H  HD2  A TYR   A 1 17  ? 12.192 -13.688 13.107  0.64 17.45 ?  17  TYR   A HD2  1 
ATOM   424  H  HD2  B TYR   A 1 17  ? 12.320 -13.831 13.437  0.36 16.60 ?  17  TYR   A HD2  1 
ATOM   425  H  HE1  A TYR   A 1 17  ? 16.074 -16.198 12.930  0.64 18.85 ?  17  TYR   A HE1  1 
ATOM   426  H  HE1  B TYR   A 1 17  ? 16.380 -15.978 12.877  0.36 17.58 ?  17  TYR   A HE1  1 
ATOM   427  H  HE2  A TYR   A 1 17  ? 12.390 -15.586 14.398  0.64 18.52 ?  17  TYR   A HE2  1 
ATOM   428  H  HE2  B TYR   A 1 17  ? 12.736 -15.821 14.537  0.36 17.35 ?  17  TYR   A HE2  1 
ATOM   429  H  HH   A TYR   A 1 17  ? 13.607 -17.426 14.867  0.64 19.32 ?  17  TYR   A HH   1 
ATOM   430  H  HH   B TYR   A 1 17  ? 15.587 -17.593 14.246  0.36 18.06 ?  17  TYR   A HH   1 
ATOM   431  N  N    A ILE   A 1 18  ? 11.950 -10.983 9.308   0.64 11.96 ?  18  ILE   A N    1 
ATOM   432  N  N    B ILE   A 1 18  ? 11.885 -10.744 9.694   0.36 10.36 ?  18  ILE   A N    1 
ATOM   433  C  CA   A ILE   A 1 18  ? 11.567 -9.796  8.545   0.64 11.65 ?  18  ILE   A CA   1 
ATOM   434  C  CA   B ILE   A 1 18  ? 11.502 -9.537  8.962   0.36 10.15 ?  18  ILE   A CA   1 
ATOM   435  C  C    A ILE   A 1 18  ? 10.591 -8.939  9.342   0.64 12.10 ?  18  ILE   A C    1 
ATOM   436  C  C    B ILE   A 1 18  ? 10.588 -8.648  9.801   0.36 10.17 ?  18  ILE   A C    1 
ATOM   437  O  O    A ILE   A 1 18  ? 9.772  -9.450  10.107  0.64 12.55 ?  18  ILE   A O    1 
ATOM   438  O  O    B ILE   A 1 18  ? 9.756  -9.130  10.576  0.36 10.87 ?  18  ILE   A O    1 
ATOM   439  C  CB   A ILE   A 1 18  ? 11.020 -10.198 7.158   0.64 11.30 ?  18  ILE   A CB   1 
ATOM   440  C  CB   B ILE   A 1 18  ? 10.867 -9.879  7.592   0.36 9.86  ?  18  ILE   A CB   1 
ATOM   441  C  CG1  A ILE   A 1 18  ? 10.980 -8.991  6.226   0.64 11.67 ?  18  ILE   A CG1  1 
ATOM   442  C  CG1  B ILE   A 1 18  ? 10.804 -8.639  6.694   0.36 10.79 ?  18  ILE   A CG1  1 
ATOM   443  C  CG2  A ILE   A 1 18  ? 9.666  -10.891 7.288   0.64 11.53 ?  18  ILE   A CG2  1 
ATOM   444  C  CG2  B ILE   A 1 18  ? 9.479  -10.485 7.771   0.36 10.66 ?  18  ILE   A CG2  1 
ATOM   445  C  CD1  A ILE   A 1 18  ? 10.736 -9.362  4.793   0.64 12.87 ?  18  ILE   A CD1  1 
ATOM   446  C  CD1  B ILE   A 1 18  ? 10.464 -8.952  5.253   0.36 11.99 ?  18  ILE   A CD1  1 
ATOM   447  H  H    A ILE   A 1 18  ? 11.333 -11.316 9.812   0.64 14.46 ?  18  ILE   A H    1 
ATOM   448  H  H    B ILE   A 1 18  ? 11.238 -11.098 10.142  0.36 12.55 ?  18  ILE   A H    1 
ATOM   449  H  HA   A ILE   A 1 18  ? 12.369 -9.274  8.399   0.64 14.09 ?  18  ILE   A HA   1 
ATOM   450  H  HA   B ILE   A 1 18  ? 12.302 -9.024  8.779   0.36 12.30 ?  18  ILE   A HA   1 
ATOM   451  H  HB   A ILE   A 1 18  ? 11.638 -10.845 6.775   0.64 13.67 ?  18  ILE   A HB   1 
ATOM   452  H  HB   B ILE   A 1 18  ? 11.429 -10.531 7.155   0.36 11.95 ?  18  ILE   A HB   1 
ATOM   453  H  HG12 A ILE   A 1 18  ? 10.271 -8.400  6.513   0.64 14.12 ?  18  ILE   A HG12 1 
ATOM   454  H  HG12 B ILE   A 1 18  ? 10.125 -8.032  7.030   0.36 13.06 ?  18  ILE   A HG12 1 
ATOM   455  H  HG13 A ILE   A 1 18  ? 11.835 -8.533  6.274   0.64 14.12 ?  18  ILE   A HG13 1 
ATOM   456  H  HG13 B ILE   A 1 18  ? 11.669 -8.195  6.700   0.36 13.06 ?  18  ILE   A HG13 1 
ATOM   457  H  HG21 A ILE   A 1 18  ? 9.425  -11.281 6.430   0.64 13.95 ?  18  ILE   A HG21 1 
ATOM   458  H  HG21 B ILE   A 1 18  ? 9.189  -10.864 6.925   0.36 12.91 ?  18  ILE   A HG21 1 
ATOM   459  H  HG22 A ILE   A 1 18  ? 9.726  -11.590 7.959   0.64 13.95 ?  18  ILE   A HG22 1 
ATOM   460  H  HG22 B ILE   A 1 18  ? 9.526  -11.178 8.445   0.36 12.91 ?  18  ILE   A HG22 1 
ATOM   461  H  HG23 A ILE   A 1 18  ? 8.998  -10.238 7.551   0.64 13.95 ?  18  ILE   A HG23 1 
ATOM   462  H  HG23 B ILE   A 1 18  ? 8.859  -9.792  8.050   0.36 12.91 ?  18  ILE   A HG23 1 
ATOM   463  H  HD11 A ILE   A 1 18  ? 10.773 -8.556  4.251   0.64 15.56 ?  18  ILE   A HD11 1 
ATOM   464  H  HD11 B ILE   A 1 18  ? 10.492 -8.132  4.732   0.36 14.51 ?  18  ILE   A HD11 1 
ATOM   465  H  HD12 A ILE   A 1 18  ? 11.414 -9.988  4.505   0.64 15.56 ?  18  ILE   A HD12 1 
ATOM   466  H  HD12 B ILE   A 1 18  ? 11.112 -9.584  4.905   0.36 14.51 ?  18  ILE   A HD12 1 
ATOM   467  H  HD13 A ILE   A 1 18  ? 9.856  -9.767  4.719   0.64 15.56 ?  18  ILE   A HD13 1 
ATOM   468  H  HD13 B ILE   A 1 18  ? 9.573  -9.335  5.213   0.36 14.51 ?  18  ILE   A HD13 1 
ATOM   469  N  N    A LYS   A 1 19  ? 10.669 -7.622  9.134   0.64 12.53 ?  19  LYS   A N    1 
ATOM   470  N  N    B LYS   A 1 19  ? 10.748 -7.331  9.626   0.36 10.37 ?  19  LYS   A N    1 
ATOM   471  C  CA   A LYS   A 1 19  ? 9.860  -6.666  9.882   0.64 12.92 ?  19  LYS   A CA   1 
ATOM   472  C  CA   B LYS   A 1 19  ? 9.963  -6.339  10.351  0.36 11.41 ?  19  LYS   A CA   1 
ATOM   473  C  C    A LYS   A 1 19  ? 9.688  -5.390  9.059   0.64 13.20 ?  19  LYS   A C    1 
ATOM   474  C  C    B LYS   A 1 19  ? 9.756  -5.119  9.464   0.36 12.22 ?  19  LYS   A C    1 
ATOM   475  O  O    A LYS   A 1 19  ? 10.574 -5.015  8.287   0.64 13.01 ?  19  LYS   A O    1 
ATOM   476  O  O    B LYS   A 1 19  ? 10.667 -4.716  8.740   0.36 12.21 ?  19  LYS   A O    1 
ATOM   477  C  CB   A LYS   A 1 19  ? 10.551 -6.350  11.217  0.64 14.47 ?  19  LYS   A CB   1 
ATOM   478  C  CB   B LYS   A 1 19  ? 10.693 -5.907  11.629  0.36 12.04 ?  19  LYS   A CB   1 
ATOM   479  C  CG   A LYS   A 1 19  ? 9.841  -5.364  12.134  0.64 15.98 ?  19  LYS   A CG   1 
ATOM   480  C  CG   B LYS   A 1 19  ? 9.894  -5.001  12.541  0.36 13.56 ?  19  LYS   A CG   1 
ATOM   481  C  CD   A LYS   A 1 19  ? 10.698 -5.121  13.376  0.64 17.19 ?  19  LYS   A CD   1 
ATOM   482  C  CD   B LYS   A 1 19  ? 10.710 -4.624  13.762  0.36 15.05 ?  19  LYS   A CD   1 
ATOM   483  C  CE   A LYS   A 1 19  ? 10.068 -4.156  14.365  0.64 18.01 ?  19  LYS   A CE   1 
ATOM   484  C  CE   B LYS   A 1 19  ? 9.927  -3.733  14.704  0.36 16.11 ?  19  LYS   A CE   1 
ATOM   485  N  NZ   A LYS   A 1 19  ? 10.970 -3.936  15.539  0.64 18.42 ?  19  LYS   A NZ   1 
ATOM   486  N  NZ   B LYS   A 1 19  ? 10.746 -3.359  15.884  0.36 16.72 ?  19  LYS   A NZ   1 
ATOM   487  H  H    A LYS   A 1 19  ? 11.200 -7.265  8.562   0.64 15.16 ?  19  LYS   A H    1 
ATOM   488  H  H    B LYS   A 1 19  ? 11.328 -6.974  9.085   0.36 12.56 ?  19  LYS   A H    1 
ATOM   489  H  HA   A LYS   A 1 19  ? 8.988  -7.059  10.060  0.64 15.61 ?  19  LYS   A HA   1 
ATOM   490  H  HA   B LYS   A 1 19  ? 9.103  -6.705  10.595  0.36 13.81 ?  19  LYS   A HA   1 
ATOM   491  H  HB2  A LYS   A 1 19  ? 10.648 -7.184  11.712  0.64 17.48 ?  19  LYS   A HB2  1 
ATOM   492  H  HB2  B LYS   A 1 19  ? 10.914 -6.697  12.145  0.36 14.57 ?  19  LYS   A HB2  1 
ATOM   493  H  HB3  A LYS   A 1 19  ? 11.427 -5.991  11.024  0.64 17.48 ?  19  LYS   A HB3  1 
ATOM   494  H  HB3  B LYS   A 1 19  ? 11.509 -5.435  11.390  0.36 14.57 ?  19  LYS   A HB3  1 
ATOM   495  H  HG2  A LYS   A 1 19  ? 9.717  -4.520  11.672  0.64 19.29 ?  19  LYS   A HG2  1 
ATOM   496  H  HG2  B LYS   A 1 19  ? 9.658  -4.188  12.070  0.36 16.39 ?  19  LYS   A HG2  1 
ATOM   497  H  HG3  A LYS   A 1 19  ? 8.986  -5.730  12.413  0.64 19.29 ?  19  LYS   A HG3  1 
ATOM   498  H  HG3  B LYS   A 1 19  ? 9.096  -5.466  12.840  0.36 16.39 ?  19  LYS   A HG3  1 
ATOM   499  H  HD2  A LYS   A 1 19  ? 10.837 -5.965  13.833  0.64 20.75 ?  19  LYS   A HD2  1 
ATOM   500  H  HD2  B LYS   A 1 19  ? 10.955 -5.431  14.243  0.36 18.17 ?  19  LYS   A HD2  1 
ATOM   501  H  HD3  A LYS   A 1 19  ? 11.551 -4.750  13.101  0.64 20.75 ?  19  LYS   A HD3  1 
ATOM   502  H  HD3  B LYS   A 1 19  ? 11.506 -4.147  13.480  0.36 18.17 ?  19  LYS   A HD3  1 
ATOM   503  H  HE2  A LYS   A 1 19  ? 9.918  -3.299  13.934  0.64 21.73 ?  19  LYS   A HE2  1 
ATOM   504  H  HE2  B LYS   A 1 19  ? 9.671  -2.923  14.238  0.36 19.44 ?  19  LYS   A HE2  1 
ATOM   505  H  HE3  A LYS   A 1 19  ? 9.230  -4.521  14.690  0.64 21.73 ?  19  LYS   A HE3  1 
ATOM   506  H  HE3  B LYS   A 1 19  ? 9.141  -4.209  15.013  0.36 19.44 ?  19  LYS   A HE3  1 
ATOM   507  H  HZ1  A LYS   A 1 19  ? 10.603 -3.352  16.101  0.64 22.22 ?  19  LYS   A HZ1  1 
ATOM   508  H  HZ1  B LYS   A 1 19  ? 10.273 -2.838  16.427  0.36 20.18 ?  19  LYS   A HZ1  1 
ATOM   509  H  HZ2  A LYS   A 1 19  ? 11.103 -4.705  15.967  0.64 22.22 ?  19  LYS   A HZ2  1 
ATOM   510  H  HZ2  B LYS   A 1 19  ? 10.993 -4.091  16.326  0.36 20.18 ?  19  LYS   A HZ2  1 
ATOM   511  H  HZ3  A LYS   A 1 19  ? 11.754 -3.619  15.264  0.64 22.22 ?  19  LYS   A HZ3  1 
ATOM   512  H  HZ3  B LYS   A 1 19  ? 11.474 -2.921  15.621  0.36 20.18 ?  19  LYS   A HZ3  1 
ATOM   513  N  N    A ASN   A 1 20  ? 8.536  -4.732  9.225   0.64 14.11 ?  20  ASN   A N    1 
ATOM   514  N  N    B ASN   A 1 20  ? 8.560  -4.533  9.521   0.36 13.50 ?  20  ASN   A N    1 
ATOM   515  C  CA   A ASN   A 1 20  ? 8.325  -3.395  8.668   0.64 15.48 ?  20  ASN   A CA   1 
ATOM   516  C  CA   B ASN   A 1 20  ? 8.302  -3.255  8.854   0.36 14.89 ?  20  ASN   A CA   1 
ATOM   517  C  C    A ASN   A 1 20  ? 8.955  -2.393  9.631   0.64 16.26 ?  20  ASN   A C    1 
ATOM   518  C  C    B ASN   A 1 20  ? 8.868  -2.136  9.715   0.36 15.46 ?  20  ASN   A C    1 
ATOM   519  O  O    A ASN   A 1 20  ? 8.453  -2.188  10.741  0.64 17.06 ?  20  ASN   A O    1 
ATOM   520  O  O    B ASN   A 1 20  ? 8.226  -1.682  10.666  0.36 16.12 ?  20  ASN   A O    1 
ATOM   521  C  CB   A ASN   A 1 20  ? 6.830  -3.140  8.460   0.64 16.65 ?  20  ASN   A CB   1 
ATOM   522  C  CB   B ASN   A 1 20  ? 6.810  -3.049  8.623   0.36 16.18 ?  20  ASN   A CB   1 
ATOM   523  C  CG   A ASN   A 1 20  ? 6.510  -1.714  7.996   0.64 17.66 ?  20  ASN   A CG   1 
ATOM   524  C  CG   B ASN   A 1 20  ? 6.468  -1.607  8.282   0.36 17.49 ?  20  ASN   A CG   1 
ATOM   525  O  OD1  A ASN   A 1 20  ? 5.443  -1.177  8.311   0.64 19.40 ?  20  ASN   A OD1  1 
ATOM   526  O  OD1  B ASN   A 1 20  ? 5.641  -0.981  8.945   0.36 19.26 ?  20  ASN   A OD1  1 
ATOM   527  N  ND2  A ASN   A 1 20  ? 7.423  -1.105  7.241   0.64 18.09 ?  20  ASN   A ND2  1 
ATOM   528  N  ND2  B ASN   A 1 20  ? 7.121  -1.068  7.256   0.36 17.35 ?  20  ASN   A ND2  1 
ATOM   529  H  H    A ASN   A 1 20  ? 7.861  -5.051  9.659   0.64 17.05 ?  20  ASN   A H    1 
ATOM   530  H  H    B ASN   A 1 20  ? 7.881  -4.868  9.926   0.36 16.32 ?  20  ASN   A H    1 
ATOM   531  H  HA   A ASN   A 1 20  ? 8.775  -3.342  7.813   0.64 18.69 ?  20  ASN   A HA   1 
ATOM   532  H  HA   B ASN   A 1 20  ? 8.756  -3.243  7.998   0.36 17.98 ?  20  ASN   A HA   1 
ATOM   533  H  HB2  A ASN   A 1 20  ? 6.501  -3.751  7.784   0.64 20.10 ?  20  ASN   A HB2  1 
ATOM   534  H  HB2  B ASN   A 1 20  ? 6.525  -3.610  7.886   0.36 19.53 ?  20  ASN   A HB2  1 
ATOM   535  H  HB3  A ASN   A 1 20  ? 6.371  -3.301  9.299   0.64 20.10 ?  20  ASN   A HB3  1 
ATOM   536  H  HB3  B ASN   A 1 20  ? 6.329  -3.292  9.429   0.36 19.53 ?  20  ASN   A HB3  1 
ATOM   537  H  HD21 A ASN   A 1 20  ? 7.285  -0.305  6.971   0.64 21.82 ?  20  ASN   A HD21 1 
ATOM   538  H  HD21 B ASN   A 1 20  ? 6.962  -0.257  7.024   0.36 20.93 ?  20  ASN   A HD21 1 
ATOM   539  H  HD22 A ASN   A 1 20  ? 8.153  -1.513  7.026   0.64 21.82 ?  20  ASN   A HD22 1 
ATOM   540  H  HD22 B ASN   A 1 20  ? 7.702  -1.535  6.823   0.36 20.93 ?  20  ASN   A HD22 1 
ATOM   541  N  N    A ALA   A 1 21  ? 10.078 -1.798  9.235   0.64 16.16 ?  21  ALA   A N    1 
ATOM   542  N  N    B ALA   A 1 21  ? 10.068 -1.676  9.372   0.36 15.79 ?  21  ALA   A N    1 
ATOM   543  C  CA   A ALA   A 1 21  ? 10.781 -0.917  10.156  0.64 15.98 ?  21  ALA   A CA   1 
ATOM   544  C  CA   B ALA   A 1 21  ? 10.710 -0.619  10.136  0.36 16.09 ?  21  ALA   A CA   1 
ATOM   545  C  C    A ALA   A 1 21  ? 11.726 -0.001  9.397   0.64 15.74 ?  21  ALA   A C    1 
ATOM   546  C  C    B ALA   A 1 21  ? 11.813 0.008   9.300   0.36 15.48 ?  21  ALA   A C    1 
ATOM   547  O  O    A ALA   A 1 21  ? 12.183 -0.327  8.297   0.64 16.09 ?  21  ALA   A O    1 
ATOM   548  O  O    B ALA   A 1 21  ? 12.338 -0.604  8.366   0.36 15.71 ?  21  ALA   A O    1 
ATOM   549  C  CB   A ALA   A 1 21  ? 11.561 -1.715  11.203  0.64 16.14 ?  21  ALA   A CB   1 
ATOM   550  C  CB   B ALA   A 1 21  ? 11.292 -1.148  11.451  0.36 16.85 ?  21  ALA   A CB   1 
ATOM   551  H  H    A ALA   A 1 21  ? 10.441 -1.891  8.463   0.64 19.50 ?  21  ALA   A H    1 
ATOM   552  H  H    B ALA   A 1 21  ? 10.524 -1.958  8.700   0.36 19.07 ?  21  ALA   A H    1 
ATOM   553  H  HA   A ALA   A 1 21  ? 10.128 -0.367  10.620  0.64 19.29 ?  21  ALA   A HA   1 
ATOM   554  H  HA   B ALA   A 1 21  ? 10.053 0.064   10.347  0.36 19.43 ?  21  ALA   A HA   1 
ATOM   555  H  HB1  A ALA   A 1 21  ? 11.990 -1.095  11.809  0.64 19.48 ?  21  ALA   A HB1  1 
ATOM   556  H  HB1  B ALA   A 1 21  ? 11.709 -0.411  11.927  0.36 20.33 ?  21  ALA   A HB1  1 
ATOM   557  H  HB2  A ALA   A 1 21  ? 10.940 -2.281  11.693  0.64 19.48 ?  21  ALA   A HB2  1 
ATOM   558  H  HB2  B ALA   A 1 21  ? 10.577 -1.524  11.986  0.36 20.33 ?  21  ALA   A HB2  1 
ATOM   559  H  HB3  A ALA   A 1 21  ? 12.222 -2.260  10.754  0.64 19.48 ?  21  ALA   A HB3  1 
ATOM   560  H  HB3  B ALA   A 1 21  ? 11.954 -1.828  11.252  0.36 20.33 ?  21  ALA   A HB3  1 
ATOM   561  N  N    A ASP   A 1 22  ? 11.990 1.156   10.005  0.64 15.66 ?  22  ASP   A N    1 
ATOM   562  N  N    B ASP   A 1 22  ? 12.137 1.250   9.647   0.36 15.23 ?  22  ASP   A N    1 
ATOM   563  C  CA   A ASP   A 1 22  ? 13.029 2.072   9.552   0.64 15.61 ?  22  ASP   A CA   1 
ATOM   564  C  CA   B ASP   A 1 22  ? 13.327 1.908   9.127   0.36 15.25 ?  22  ASP   A CA   1 
ATOM   565  C  C    A ASP   A 1 22  ? 14.358 1.601   10.130  0.64 14.25 ?  22  ASP   A C    1 
ATOM   566  C  C    B ASP   A 1 22  ? 14.556 1.275   9.773   0.36 14.06 ?  22  ASP   A C    1 
ATOM   567  O  O    A ASP   A 1 22  ? 14.543 1.605   11.352  0.64 14.79 ?  22  ASP   A O    1 
ATOM   568  O  O    B ASP   A 1 22  ? 14.639 1.175   11.001  0.36 14.26 ?  22  ASP   A O    1 
ATOM   569  C  CB   A ASP   A 1 22  ? 12.695 3.481   10.040  0.64 17.43 ?  22  ASP   A CB   1 
ATOM   570  C  CB   B ASP   A 1 22  ? 13.249 3.397   9.479   0.36 16.83 ?  22  ASP   A CB   1 
ATOM   571  C  CG   A ASP   A 1 22  ? 13.719 4.524   9.605   0.64 19.65 ?  22  ASP   A CG   1 
ATOM   572  C  CG   B ASP   A 1 22  ? 14.351 4.226   8.854   0.36 17.84 ?  22  ASP   A CG   1 
ATOM   573  O  OD1  A ASP   A 1 22  ? 14.847 4.170   9.206   0.64 20.20 ?  22  ASP   A OD1  1 
ATOM   574  O  OD1  B ASP   A 1 22  ? 15.294 3.649   8.279   0.36 17.73 ?  22  ASP   A OD1  1 
ATOM   575  O  OD2  A ASP   A 1 22  ? 13.389 5.723   9.678   0.64 21.29 -1 22  ASP   A OD2  1 
ATOM   576  O  OD2  B ASP   A 1 22  ? 14.266 5.472   8.948   0.36 18.62 -1 22  ASP   A OD2  1 
ATOM   577  H  H    A ASP   A 1 22  ? 11.556 1.441   10.696  0.64 18.91 ?  22  ASP   A H    1 
ATOM   578  H  H    B ASP   A 1 22  ? 11.671 1.739   10.183  0.36 18.39 ?  22  ASP   A H    1 
ATOM   579  H  HA   A ASP   A 1 22  ? 13.077 2.074   8.584   0.64 18.85 ?  22  ASP   A HA   1 
ATOM   580  H  HA   B ASP   A 1 22  ? 13.373 1.801   8.160   0.36 18.42 ?  22  ASP   A HA   1 
ATOM   581  H  HB2  A ASP   A 1 22  ? 11.826 3.745   9.685   0.64 21.04 ?  22  ASP   A HB2  1 
ATOM   582  H  HB2  B ASP   A 1 22  ? 12.407 3.752   9.166   0.36 20.31 ?  22  ASP   A HB2  1 
ATOM   583  H  HB3  A ASP   A 1 22  ? 12.660 3.482   11.011  0.64 21.04 ?  22  ASP   A HB3  1 
ATOM   584  H  HB3  B ASP   A 1 22  ? 13.323 3.494   10.438  0.36 20.31 ?  22  ASP   A HB3  1 
ATOM   585  N  N    A ILE   A 1 23  ? 15.276 1.183   9.254   0.64 13.77 ?  23  ILE   A N    1 
ATOM   586  N  N    B ILE   A 1 23  ? 15.505 0.829   8.945   0.36 13.51 ?  23  ILE   A N    1 
ATOM   587  C  CA   A ILE   A 1 23  ? 16.527 0.574   9.702   0.64 13.29 ?  23  ILE   A CA   1 
ATOM   588  C  CA   B ILE   A 1 23  ? 16.713 0.189   9.465   0.36 12.76 ?  23  ILE   A CA   1 
ATOM   589  C  C    A ILE   A 1 23  ? 17.326 1.527   10.579  0.64 13.58 ?  23  ILE   A C    1 
ATOM   590  C  C    B ILE   A 1 23  ? 17.467 1.134   10.389  0.36 13.22 ?  23  ILE   A C    1 
ATOM   591  O  O    A ILE   A 1 23  ? 18.037 1.091   11.494  0.64 14.31 ?  23  ILE   A O    1 
ATOM   592  O  O    B ILE   A 1 23  ? 18.134 0.693   11.334  0.36 13.13 ?  23  ILE   A O    1 
ATOM   593  C  CB   A ILE   A 1 23  ? 17.332 0.050   8.492   0.64 13.42 ?  23  ILE   A CB   1 
ATOM   594  C  CB   B ILE   A 1 23  ? 17.605 -0.342  8.319   0.36 12.26 ?  23  ILE   A CB   1 
ATOM   595  C  CG1  A ILE   A 1 23  ? 18.466 -0.865  8.955   0.64 13.49 ?  23  ILE   A CG1  1 
ATOM   596  C  CG1  B ILE   A 1 23  ? 18.684 -1.284  8.872   0.36 12.18 ?  23  ILE   A CG1  1 
ATOM   597  C  CG2  A ILE   A 1 23  ? 17.851 1.204   7.639   0.64 13.82 ?  23  ILE   A CG2  1 
ATOM   598  C  CG2  B ILE   A 1 23  ? 18.241 0.808   7.538   0.36 12.33 ?  23  ILE   A CG2  1 
ATOM   599  C  CD1  A ILE   A 1 23  ? 19.151 -1.584  7.817   0.64 13.65 ?  23  ILE   A CD1  1 
ATOM   600  C  CD1  B ILE   A 1 23  ? 19.560 -1.934  7.806   0.36 12.13 ?  23  ILE   A CD1  1 
ATOM   601  H  H    A ILE   A 1 23  ? 15.190 1.248   8.404   0.64 16.64 ?  23  ILE   A H    1 
ATOM   602  H  H    B ILE   A 1 23  ? 15.478 0.885   8.096   0.36 16.33 ?  23  ILE   A H    1 
ATOM   603  H  HA   A ILE   A 1 23  ? 16.303 -0.190  10.250  0.64 16.07 ?  23  ILE   A HA   1 
ATOM   604  H  HA   B ILE   A 1 23  ? 16.443 -0.578  9.992   0.36 15.43 ?  23  ILE   A HA   1 
ATOM   605  H  HB   A ILE   A 1 23  ? 16.729 -0.476  7.945   0.64 16.22 ?  23  ILE   A HB   1 
ATOM   606  H  HB   B ILE   A 1 23  ? 17.050 -0.851  7.709   0.36 14.83 ?  23  ILE   A HB   1 
ATOM   607  H  HG12 A ILE   A 1 23  ? 19.132 -0.332  9.415   0.64 16.30 ?  23  ILE   A HG12 1 
ATOM   608  H  HG12 B ILE   A 1 23  ? 19.266 -0.783  9.463   0.36 14.73 ?  23  ILE   A HG12 1 
ATOM   609  H  HG13 A ILE   A 1 23  ? 18.104 -1.535  9.557   0.64 16.30 ?  23  ILE   A HG13 1 
ATOM   610  H  HG13 B ILE   A 1 23  ? 18.250 -1.997  9.369   0.36 14.73 ?  23  ILE   A HG13 1 
ATOM   611  H  HG21 A ILE   A 1 23  ? 18.198 0.849   6.806   0.64 16.70 ?  23  ILE   A HG21 1 
ATOM   612  H  HG21 B ILE   A 1 23  ? 18.630 0.456   6.719   0.36 14.91 ?  23  ILE   A HG21 1 
ATOM   613  H  HG22 A ILE   A 1 23  ? 17.118 1.815   7.455   0.64 16.70 ?  23  ILE   A HG22 1 
ATOM   614  H  HG22 B ILE   A 1 23  ? 17.555 1.457   7.324   0.36 14.91 ?  23  ILE   A HG22 1 
ATOM   615  H  HG23 A ILE   A 1 23  ? 18.552 1.667   8.121   0.64 16.70 ?  23  ILE   A HG23 1 
ATOM   616  H  HG23 B ILE   A 1 23  ? 18.931 1.218   8.080   0.36 14.91 ?  23  ILE   A HG23 1 
ATOM   617  H  HD11 A ILE   A 1 23  ? 19.796 -2.208  8.182   0.64 16.49 ?  23  ILE   A HD11 1 
ATOM   618  H  HD11 B ILE   A 1 23  ? 20.144 -2.585  8.231   0.36 14.67 ?  23  ILE   A HD11 1 
ATOM   619  H  HD12 A ILE   A 1 23  ? 18.482 -2.063  7.301   0.64 16.49 ?  23  ILE   A HD12 1 
ATOM   620  H  HD12 B ILE   A 1 23  ? 18.992 -2.379  7.158   0.36 14.67 ?  23  ILE   A HD12 1 
ATOM   621  H  HD13 A ILE   A 1 23  ? 19.597 -0.933  7.255   0.64 16.49 ?  23  ILE   A HD13 1 
ATOM   622  H  HD13 B ILE   A 1 23  ? 20.090 -1.251  7.371   0.36 14.67 ?  23  ILE   A HD13 1 
ATOM   623  N  N    A VAL   A 1 24  ? 17.212 2.835   10.340  0.64 14.10 ?  24  VAL   A N    1 
ATOM   624  N  N    B VAL   A 1 24  ? 17.369 2.442   10.140  0.36 14.24 ?  24  VAL   A N    1 
ATOM   625  C  CA   A VAL   A 1 24  ? 17.895 3.806   11.193  0.64 15.46 ?  24  VAL   A CA   1 
ATOM   626  C  CA   B VAL   A 1 24  ? 18.015 3.424   11.005  0.36 15.75 ?  24  VAL   A CA   1 
ATOM   627  C  C    A VAL   A 1 24  ? 17.368 3.721   12.618  0.64 16.20 ?  24  VAL   A C    1 
ATOM   628  C  C    B VAL   A 1 24  ? 17.392 3.398   12.395  0.36 16.67 ?  24  VAL   A C    1 
ATOM   629  O  O    A VAL   A 1 24  ? 18.139 3.636   13.584  0.64 17.01 ?  24  VAL   A O    1 
ATOM   630  O  O    B VAL   A 1 24  ? 18.097 3.434   13.411  0.36 17.40 ?  24  VAL   A O    1 
ATOM   631  C  CB   A VAL   A 1 24  ? 17.747 5.226   10.618  0.64 16.19 ?  24  VAL   A CB   1 
ATOM   632  C  CB   B VAL   A 1 24  ? 17.938 4.820   10.359  0.36 16.71 ?  24  VAL   A CB   1 
ATOM   633  C  CG1  A VAL   A 1 24  ? 18.234 6.266   11.623  0.64 16.60 ?  24  VAL   A CG1  1 
ATOM   634  C  CG1  B VAL   A 1 24  ? 18.563 5.867   11.265  0.36 17.50 ?  24  VAL   A CG1  1 
ATOM   635  C  CG2  A VAL   A 1 24  ? 18.507 5.345   9.309   0.64 16.88 ?  24  VAL   A CG2  1 
ATOM   636  C  CG2  B VAL   A 1 24  ? 18.618 4.805   8.996   0.36 16.67 ?  24  VAL   A CG2  1 
ATOM   637  H  H    A VAL   A 1 24  ? 16.750 3.183   9.700   0.64 17.04 ?  24  VAL   A H    1 
ATOM   638  H  H    B VAL   A 1 24  ? 16.935 2.780   9.481   0.36 17.21 ?  24  VAL   A H    1 
ATOM   639  H  HA   A VAL   A 1 24  ? 18.838 3.595   11.215  0.64 18.67 ?  24  VAL   A HA   1 
ATOM   640  H  HA   B VAL   A 1 24  ? 18.951 3.194   11.097  0.36 19.02 ?  24  VAL   A HA   1 
ATOM   641  H  HB   A VAL   A 1 24  ? 16.811 5.403   10.433  0.64 19.55 ?  24  VAL   A HB   1 
ATOM   642  H  HB   B VAL   A 1 24  ? 17.008 5.057   10.222  0.36 20.16 ?  24  VAL   A HB   1 
ATOM   643  H  HG11 A VAL   A 1 24  ? 18.406 7.098   11.156  0.64 20.04 ?  24  VAL   A HG11 1 
ATOM   644  H  HG11 B VAL   A 1 24  ? 18.680 6.687   10.762  0.36 21.11 ?  24  VAL   A HG11 1 
ATOM   645  H  HG12 A VAL   A 1 24  ? 17.551 6.399   12.296  0.64 20.04 ?  24  VAL   A HG12 1 
ATOM   646  H  HG12 B VAL   A 1 24  ? 17.972 6.024   12.018  0.36 21.11 ?  24  VAL   A HG12 1 
ATOM   647  H  HG13 A VAL   A 1 24  ? 19.052 5.945   12.035  0.64 20.04 ?  24  VAL   A HG13 1 
ATOM   648  H  HG13 B VAL   A 1 24  ? 19.421 5.542   11.575  0.36 21.11 ?  24  VAL   A HG13 1 
ATOM   649  H  HG21 A VAL   A 1 24  ? 18.278 6.186   8.882   0.64 20.37 ?  24  VAL   A HG21 1 
ATOM   650  H  HG21 B VAL   A 1 24  ? 18.621 5.705   8.633   0.36 20.13 ?  24  VAL   A HG21 1 
ATOM   651  H  HG22 A VAL   A 1 24  ? 19.460 5.321   9.492   0.64 20.37 ?  24  VAL   A HG22 1 
ATOM   652  H  HG22 B VAL   A 1 24  ? 19.529 4.490   9.102   0.36 20.13 ?  24  VAL   A HG22 1 
ATOM   653  H  HG23 A VAL   A 1 24  ? 18.263 4.606   8.729   0.64 20.37 ?  24  VAL   A HG23 1 
ATOM   654  H  HG23 B VAL   A 1 24  ? 18.131 4.212   8.403   0.36 20.13 ?  24  VAL   A HG23 1 
ATOM   655  N  N    A GLU   A 1 25  ? 16.041 3.753   12.770  0.64 16.62 ?  25  GLU   A N    1 
ATOM   656  N  N    B GLU   A 1 25  ? 16.060 3.326   12.461  0.36 17.14 ?  25  GLU   A N    1 
ATOM   657  C  CA   A GLU   A 1 25  ? 15.449 3.690   14.102  0.64 17.80 ?  25  GLU   A CA   1 
ATOM   658  C  CA   B GLU   A 1 25  ? 15.384 3.259   13.753  0.36 17.98 ?  25  GLU   A CA   1 
ATOM   659  C  C    A GLU   A 1 25  ? 15.685 2.331   14.748  0.64 16.94 ?  25  GLU   A C    1 
ATOM   660  C  C    B GLU   A 1 25  ? 15.663 1.934   14.457  0.36 17.79 ?  25  GLU   A C    1 
ATOM   661  O  O    A GLU   A 1 25  ? 15.912 2.246   15.961  0.64 17.84 ?  25  GLU   A O    1 
ATOM   662  O  O    B GLU   A 1 25  ? 15.882 1.907   15.673  0.36 18.11 ?  25  GLU   A O    1 
ATOM   663  C  CB   A GLU   A 1 25  ? 13.958 4.033   14.031  0.64 20.25 ?  25  GLU   A CB   1 
ATOM   664  C  CB   B GLU   A 1 25  ? 13.883 3.499   13.573  0.36 19.21 ?  25  GLU   A CB   1 
ATOM   665  C  CG   A GLU   A 1 25  ? 13.696 5.498   13.695  0.64 23.23 ?  25  GLU   A CG   1 
ATOM   666  C  CG   B GLU   A 1 25  ? 13.548 4.891   13.050  0.36 21.10 ?  25  GLU   A CG   1 
ATOM   667  C  CD   A GLU   A 1 25  ? 14.525 6.459   14.537  0.64 25.64 ?  25  GLU   A CD   1 
ATOM   668  C  CD   B GLU   A 1 25  ? 14.040 5.988   13.974  0.36 22.80 ?  25  GLU   A CD   1 
ATOM   669  O  OE1  A GLU   A 1 25  ? 14.589 6.276   15.772  0.64 26.36 ?  25  GLU   A OE1  1 
ATOM   670  O  OE1  B GLU   A 1 25  ? 13.988 5.791   15.207  0.36 23.45 ?  25  GLU   A OE1  1 
ATOM   671  O  OE2  A GLU   A 1 25  ? 15.136 7.381   13.958  0.64 26.85 -1 25  GLU   A OE2  1 
ATOM   672  O  OE2  B GLU   A 1 25  ? 14.488 7.039   13.467  0.36 23.61 -1 25  GLU   A OE2  1 
ATOM   673  H  H    A GLU   A 1 25  ? 15.470 3.827   12.125  0.64 20.05 ?  25  GLU   A H    1 
ATOM   674  H  H    B GLU   A 1 25  ? 15.536 3.319   11.779  0.36 20.69 ?  25  GLU   A H    1 
ATOM   675  H  HA   A GLU   A 1 25  ? 15.880 4.348   14.665  0.64 21.48 ?  25  GLU   A HA   1 
ATOM   676  H  HA   B GLU   A 1 25  ? 15.728 3.964   14.317  0.36 21.69 ?  25  GLU   A HA   1 
ATOM   677  H  HB2  A GLU   A 1 25  ? 13.535 3.494   13.338  0.64 24.41 ?  25  GLU   A HB2  1 
ATOM   678  H  HB2  B GLU   A 1 25  ? 13.532 2.857   12.937  0.36 23.16 ?  25  GLU   A HB2  1 
ATOM   679  H  HB3  A GLU   A 1 25  ? 13.541 3.848   14.887  0.64 24.41 ?  25  GLU   A HB3  1 
ATOM   680  H  HB3  B GLU   A 1 25  ? 13.442 3.393   14.429  0.36 23.16 ?  25  GLU   A HB3  1 
ATOM   681  H  HG2  A GLU   A 1 25  ? 13.926 5.652   12.767  0.64 27.99 ?  25  GLU   A HG2  1 
ATOM   682  H  HG2  B GLU   A 1 25  ? 13.971 5.019   12.186  0.36 25.43 ?  25  GLU   A HG2  1 
ATOM   683  H  HG3  A GLU   A 1 25  ? 12.755 5.692   13.843  0.64 27.99 ?  25  GLU   A HG3  1 
ATOM   684  H  HG3  B GLU   A 1 25  ? 12.586 4.980   12.967  0.36 25.43 ?  25  GLU   A HG3  1 
ATOM   685  N  N    A GLU   A 1 26  ? 15.655 1.259   13.952  0.64 16.62 ?  26  GLU   A N    1 
ATOM   686  N  N    B GLU   A 1 26  ? 15.673 0.825   13.712  0.36 17.49 ?  26  GLU   A N    1 
ATOM   687  C  CA   A GLU   A 1 26  ? 15.939 -0.069  14.488  0.64 16.68 ?  26  GLU   A CA   1 
ATOM   688  C  CA   B GLU   A 1 26  ? 16.063 -0.449  14.307  0.36 17.62 ?  26  GLU   A CA   1 
ATOM   689  C  C    A GLU   A 1 26  ? 17.358 -0.150  15.038  0.64 15.95 ?  26  GLU   A C    1 
ATOM   690  C  C    B GLU   A 1 26  ? 17.493 -0.407  14.826  0.36 17.20 ?  26  GLU   A C    1 
ATOM   691  O  O    A GLU   A 1 26  ? 17.577 -0.622  16.158  0.64 15.97 ?  26  GLU   A O    1 
ATOM   692  O  O    B GLU   A 1 26  ? 17.807 -1.042  15.839  0.36 16.94 ?  26  GLU   A O    1 
ATOM   693  C  CB   A GLU   A 1 26  ? 15.742 -1.125  13.400  0.64 18.01 ?  26  GLU   A CB   1 
ATOM   694  C  CB   B GLU   A 1 26  ? 15.907 -1.578  13.286  0.36 18.40 ?  26  GLU   A CB   1 
ATOM   695  C  CG   A GLU   A 1 26  ? 14.327 -1.639  13.246  0.64 21.00 ?  26  GLU   A CG   1 
ATOM   696  C  CG   B GLU   A 1 26  ? 14.472 -1.973  13.021  0.36 19.02 ?  26  GLU   A CG   1 
ATOM   697  C  CD   A GLU   A 1 26  ? 13.897 -2.538  14.397  0.64 22.78 ?  26  GLU   A CD   1 
ATOM   698  C  CD   B GLU   A 1 26  ? 13.763 -2.452  14.261  0.36 19.05 ?  26  GLU   A CD   1 
ATOM   699  O  OE1  A GLU   A 1 26  ? 14.331 -3.714  14.468  0.64 23.03 ?  26  GLU   A OE1  1 
ATOM   700  O  OE1  B GLU   A 1 26  ? 14.338 -3.284  14.993  0.36 19.34 ?  26  GLU   A OE1  1 
ATOM   701  O  OE2  A GLU   A 1 26  ? 13.126 -2.054  15.240  0.64 23.64 -1 26  GLU   A OE2  1 
ATOM   702  O  OE2  B GLU   A 1 26  ? 12.640 -1.972  14.505  0.36 18.07 -1 26  GLU   A OE2  1 
ATOM   703  H  H    A GLU   A 1 26  ? 15.476 1.284   13.109  0.64 20.05 ?  26  GLU   A H    1 
ATOM   704  H  H    B GLU   A 1 26  ? 15.462 0.784   12.879  0.36 21.10 ?  26  GLU   A H    1 
ATOM   705  H  HA   A GLU   A 1 26  ? 15.316 -0.251  15.206  0.64 20.13 ?  26  GLU   A HA   1 
ATOM   706  H  HA   B GLU   A 1 26  ? 15.482 -0.639  15.059  0.36 21.26 ?  26  GLU   A HA   1 
ATOM   707  H  HB2  A GLU   A 1 26  ? 16.010 -0.743  12.549  0.64 21.73 ?  26  GLU   A HB2  1 
ATOM   708  H  HB2  B GLU   A 1 26  ? 16.292 -1.292  12.442  0.36 22.20 ?  26  GLU   A HB2  1 
ATOM   709  H  HB3  A GLU   A 1 26  ? 16.308 -1.881  13.610  0.64 21.73 ?  26  GLU   A HB3  1 
ATOM   710  H  HB3  B GLU   A 1 26  ? 16.378 -2.363  13.610  0.36 22.20 ?  26  GLU   A HB3  1 
ATOM   711  H  HG2  A GLU   A 1 26  ? 13.723 -0.877  13.199  0.64 25.31 ?  26  GLU   A HG2  1 
ATOM   712  H  HG2  B GLU   A 1 26  ? 13.980 -1.204  12.702  0.36 22.94 ?  26  GLU   A HG2  1 
ATOM   713  H  HG3  A GLU   A 1 26  ? 14.266 -2.156  12.430  0.64 25.31 ?  26  GLU   A HG3  1 
ATOM   714  H  HG3  B GLU   A 1 26  ? 14.449 -2.685  12.366  0.36 22.94 ?  26  GLU   A HG3  1 
ATOM   715  N  N    A ALA   A 1 27  ? 18.344 0.285   14.249  0.64 15.37 ?  27  ALA   A N    1 
ATOM   716  N  N    B ALA   A 1 27  ? 18.373 0.332   14.153  0.36 17.06 ?  27  ALA   A N    1 
ATOM   717  C  CA   A ALA   A 1 27  ? 19.731 0.215   14.698  0.64 15.70 ?  27  ALA   A CA   1 
ATOM   718  C  CA   B ALA   A 1 27  ? 19.759 0.409   14.601  0.36 17.34 ?  27  ALA   A CA   1 
ATOM   719  C  C    A ALA   A 1 27  ? 19.942 1.032   15.966  0.64 17.28 ?  27  ALA   A C    1 
ATOM   720  C  C    B ALA   A 1 27  ? 19.867 1.183   15.909  0.36 18.81 ?  27  ALA   A C    1 
ATOM   721  O  O    A ALA   A 1 27  ? 20.626 0.588   16.895  0.64 17.58 ?  27  ALA   A O    1 
ATOM   722  O  O    B ALA   A 1 27  ? 20.513 0.729   16.861  0.36 18.69 ?  27  ALA   A O    1 
ATOM   723  C  CB   A ALA   A 1 27  ? 20.672 0.683   13.584  0.64 15.22 ?  27  ALA   A CB   1 
ATOM   724  C  CB   B ALA   A 1 27  ? 20.625 1.052   13.517  0.36 16.68 ?  27  ALA   A CB   1 
ATOM   725  H  H    A ALA   A 1 27  ? 18.234 0.610   13.463  0.64 18.56 ?  27  ALA   A H    1 
ATOM   726  H  H    B ALA   A 1 27  ? 18.191 0.791   13.449  0.36 20.59 ?  27  ALA   A H    1 
ATOM   727  H  HA   A ALA   A 1 27  ? 19.945 -0.711  14.899  0.64 18.95 ?  27  ALA   A HA   1 
ATOM   728  H  HA   B ALA   A 1 27  ? 20.087 -0.490  14.753  0.36 20.92 ?  27  ALA   A HA   1 
ATOM   729  H  HB1  A ALA   A 1 27  ? 21.587 0.624   13.901  0.64 18.38 ?  27  ALA   A HB1  1 
ATOM   730  H  HB1  B ALA   A 1 27  ? 21.545 1.062   13.820  0.36 20.13 ?  27  ALA   A HB1  1 
ATOM   731  H  HB2  A ALA   A 1 27  ? 20.554 0.107   12.810  0.64 18.38 ?  27  ALA   A HB2  1 
ATOM   732  H  HB2  B ALA   A 1 27  ? 20.549 0.531   12.702  0.36 20.13 ?  27  ALA   A HB2  1 
ATOM   733  H  HB3  A ALA   A 1 27  ? 20.457 1.597   13.353  0.64 18.38 ?  27  ALA   A HB3  1 
ATOM   734  H  HB3  B ALA   A 1 27  ? 20.315 1.958   13.361  0.36 20.13 ?  27  ALA   A HB3  1 
ATOM   735  N  N    A LYS   A 1 28  ? 19.349 2.225   16.034  0.64 19.56 ?  28  LYS   A N    1 
ATOM   736  N  N    B LYS   A 1 28  ? 19.225 2.351   15.982  0.36 20.78 ?  28  LYS   A N    1 
ATOM   737  C  CA   A LYS   A 1 28  ? 19.500 3.050   17.228  0.64 22.43 ?  28  LYS   A CA   1 
ATOM   738  C  CA   B LYS   A 1 28  ? 19.342 3.182   17.176  0.36 23.05 ?  28  LYS   A CA   1 
ATOM   739  C  C    A LYS   A 1 28  ? 18.938 2.358   18.462  0.64 23.35 ?  28  LYS   A C    1 
ATOM   740  C  C    B LYS   A 1 28  ? 18.768 2.496   18.409  0.36 24.05 ?  28  LYS   A C    1 
ATOM   741  O  O    A LYS   A 1 28  ? 19.467 2.534   19.565  0.64 24.34 ?  28  LYS   A O    1 
ATOM   742  O  O    B LYS   A 1 28  ? 19.233 2.746   19.527  0.36 24.38 ?  28  LYS   A O    1 
ATOM   743  C  CB   A LYS   A 1 28  ? 18.854 4.421   17.013  0.64 24.87 ?  28  LYS   A CB   1 
ATOM   744  C  CB   B LYS   A 1 28  ? 18.664 4.533   16.948  0.36 24.57 ?  28  LYS   A CB   1 
ATOM   745  C  CG   A LYS   A 1 28  ? 19.674 5.338   16.117  0.64 27.24 ?  28  LYS   A CG   1 
ATOM   746  C  CG   B LYS   A 1 28  ? 19.455 5.456   16.039  0.36 26.29 ?  28  LYS   A CG   1 
ATOM   747  C  CD   A LYS   A 1 28  ? 19.213 6.784   16.192  0.64 29.62 ?  28  LYS   A CD   1 
ATOM   748  C  CD   B LYS   A 1 28  ? 18.982 6.897   16.135  0.36 28.00 ?  28  LYS   A CD   1 
ATOM   749  C  CE   A LYS   A 1 28  ? 17.925 7.000   15.425  0.64 31.48 ?  28  LYS   A CE   1 
ATOM   750  C  CE   B LYS   A 1 28  ? 17.695 7.120   15.364  0.36 29.45 ?  28  LYS   A CE   1 
ATOM   751  N  NZ   A LYS   A 1 28  ? 17.564 8.444   15.361  0.64 32.48 ?  28  LYS   A NZ   1 
ATOM   752  N  NZ   B LYS   A 1 28  ? 17.377 8.571   15.245  0.36 30.16 ?  28  LYS   A NZ   1 
ATOM   753  H  H    A LYS   A 1 28  ? 18.864 2.566   15.418  0.64 23.59 ?  28  LYS   A H    1 
ATOM   754  H  H    B LYS   A 1 28  ? 18.730 2.679   15.362  0.36 25.05 ?  28  LYS   A H    1 
ATOM   755  H  HA   A LYS   A 1 28  ? 20.443 3.192   17.392  0.64 27.04 ?  28  LYS   A HA   1 
ATOM   756  H  HA   B LYS   A 1 28  ? 20.281 3.348   17.342  0.36 27.78 ?  28  LYS   A HA   1 
ATOM   757  H  HB2  A LYS   A 1 28  ? 17.988 4.301   16.598  0.64 29.96 ?  28  LYS   A HB2  1 
ATOM   758  H  HB2  B LYS   A 1 28  ? 17.797 4.385   16.541  0.36 29.60 ?  28  LYS   A HB2  1 
ATOM   759  H  HB3  A LYS   A 1 28  ? 18.754 4.861   17.871  0.64 29.96 ?  28  LYS   A HB3  1 
ATOM   760  H  HB3  B LYS   A 1 28  ? 18.557 4.975   17.804  0.36 29.60 ?  28  LYS   A HB3  1 
ATOM   761  H  HG2  A LYS   A 1 28  ? 20.603 5.305   16.392  0.64 32.80 ?  28  LYS   A HG2  1 
ATOM   762  H  HG2  B LYS   A 1 28  ? 20.391 5.427   16.293  0.36 31.66 ?  28  LYS   A HG2  1 
ATOM   763  H  HG3  A LYS   A 1 28  ? 19.588 5.043   15.197  0.64 32.80 ?  28  LYS   A HG3  1 
ATOM   764  H  HG3  B LYS   A 1 28  ? 19.350 5.163   15.120  0.36 31.66 ?  28  LYS   A HG3  1 
ATOM   765  H  HD2  A LYS   A 1 28  ? 19.058 7.024   17.119  0.64 35.67 ?  28  LYS   A HD2  1 
ATOM   766  H  HD2  B LYS   A 1 28  ? 18.820 7.119   17.066  0.36 33.72 ?  28  LYS   A HD2  1 
ATOM   767  H  HD3  A LYS   A 1 28  ? 19.895 7.358   15.807  0.64 35.67 ?  28  LYS   A HD3  1 
ATOM   768  H  HD3  B LYS   A 1 28  ? 19.662 7.480   15.766  0.36 33.72 ?  28  LYS   A HD3  1 
ATOM   769  H  HE2  A LYS   A 1 28  ? 18.034 6.673   14.518  0.64 37.90 ?  28  LYS   A HE2  1 
ATOM   770  H  HE2  B LYS   A 1 28  ? 17.789 6.754   14.470  0.36 35.46 ?  28  LYS   A HE2  1 
ATOM   771  H  HE3  A LYS   A 1 28  ? 17.205 6.526   15.869  0.64 37.90 ?  28  LYS   A HE3  1 
ATOM   772  H  HE3  B LYS   A 1 28  ? 16.963 6.685   15.829  0.36 35.46 ?  28  LYS   A HE3  1 
ATOM   773  H  HZ1  A LYS   A 1 28  ? 16.806 8.548   14.907  0.64 39.09 ?  28  LYS   A HZ1  1 
ATOM   774  H  HZ1  B LYS   A 1 28  ? 16.621 8.681   14.790  0.36 36.31 ?  28  LYS   A HZ1  1 
ATOM   775  H  HZ2  A LYS   A 1 28  ? 17.455 8.767   16.183  0.64 39.09 ?  28  LYS   A HZ2  1 
ATOM   776  H  HZ2  B LYS   A 1 28  ? 17.283 8.929   16.054  0.36 36.31 ?  28  LYS   A HZ2  1 
ATOM   777  H  HZ3  A LYS   A 1 28  ? 18.210 8.901   14.954  0.64 39.09 ?  28  LYS   A HZ3  1 
ATOM   778  H  HZ3  B LYS   A 1 28  ? 18.036 8.992   14.818  0.36 36.31 ?  28  LYS   A HZ3  1 
ATOM   779  N  N    A LYS   A 1 29  ? 17.887 1.552   18.298  0.64 23.79 ?  29  LYS   A N    1 
ATOM   780  N  N    B LYS   A 1 29  ? 17.762 1.639   18.233  0.36 24.98 ?  29  LYS   A N    1 
ATOM   781  C  CA   A LYS   A 1 29  ? 17.290 0.852   19.432  0.64 25.61 ?  29  LYS   A CA   1 
ATOM   782  C  CA   B LYS   A 1 29  ? 17.156 0.957   19.372  0.36 26.33 ?  29  LYS   A CA   1 
ATOM   783  C  C    A LYS   A 1 29  ? 18.105 -0.380  19.812  0.64 25.02 ?  29  LYS   A C    1 
ATOM   784  C  C    B LYS   A 1 29  ? 17.943 -0.286  19.770  0.36 25.86 ?  29  LYS   A C    1 
ATOM   785  O  O    A LYS   A 1 29  ? 18.442 -0.574  20.986  0.64 25.86 ?  29  LYS   A O    1 
ATOM   786  O  O    B LYS   A 1 29  ? 18.174 -0.520  20.962  0.36 26.07 ?  29  LYS   A O    1 
ATOM   787  C  CB   A LYS   A 1 29  ? 15.851 0.452   19.092  0.64 28.29 ?  29  LYS   A CB   1 
ATOM   788  C  CB   B LYS   A 1 29  ? 15.714 0.572   19.040  0.36 28.35 ?  29  LYS   A CB   1 
ATOM   789  C  CG   A LYS   A 1 29  ? 15.111 -0.258  20.218  0.64 31.07 ?  29  LYS   A CG   1 
ATOM   790  C  CG   B LYS   A 1 29  ? 14.943 -0.051  20.196  0.36 30.16 ?  29  LYS   A CG   1 
ATOM   791  C  CD   A LYS   A 1 29  ? 14.766 0.701   21.344  0.64 33.37 ?  29  LYS   A CD   1 
ATOM   792  C  CD   B LYS   A 1 29  ? 14.623 0.976   21.270  0.36 31.68 ?  29  LYS   A CD   1 
ATOM   793  C  CE   A LYS   A 1 29  ? 13.881 0.035   22.386  0.64 35.01 ?  29  LYS   A CE   1 
ATOM   794  C  CE   B LYS   A 1 29  ? 13.724 0.388   22.345  0.36 32.81 ?  29  LYS   A CE   1 
ATOM   795  N  NZ   A LYS   A 1 29  ? 13.443 0.995   23.436  0.64 35.93 ?  29  LYS   A NZ   1 
ATOM   796  N  NZ   B LYS   A 1 29  ? 13.375 1.394   23.385  0.36 33.46 ?  29  LYS   A NZ   1 
ATOM   797  H  H    A LYS   A 1 29  ? 17.507 1.390   17.544  0.64 28.66 ?  29  LYS   A H    1 
ATOM   798  H  H    B LYS   A 1 29  ? 17.411 1.444   17.475  0.36 30.09 ?  29  LYS   A H    1 
ATOM   799  H  HA   A LYS   A 1 29  ? 17.263 1.445   20.197  0.64 30.85 ?  29  LYS   A HA   1 
ATOM   800  H  HA   B LYS   A 1 29  ? 17.143 1.558   20.132  0.36 31.71 ?  29  LYS   A HA   1 
ATOM   801  H  HB2  A LYS   A 1 29  ? 15.348 1.252   18.872  0.64 34.07 ?  29  LYS   A HB2  1 
ATOM   802  H  HB2  B LYS   A 1 29  ? 15.237 1.370   18.767  0.36 34.13 ?  29  LYS   A HB2  1 
ATOM   803  H  HB3  A LYS   A 1 29  ? 15.865 -0.146  18.329  0.64 34.07 ?  29  LYS   A HB3  1 
ATOM   804  H  HB3  B LYS   A 1 29  ? 15.722 -0.071  18.314  0.36 34.13 ?  29  LYS   A HB3  1 
ATOM   805  H  HG2  A LYS   A 1 29  ? 14.284 -0.627  19.872  0.64 37.40 ?  29  LYS   A HG2  1 
ATOM   806  H  HG2  B LYS   A 1 29  ? 14.106 -0.411  19.863  0.36 36.31 ?  29  LYS   A HG2  1 
ATOM   807  H  HG3  A LYS   A 1 29  ? 15.665 -0.968  20.580  0.64 37.40 ?  29  LYS   A HG3  1 
ATOM   808  H  HG3  B LYS   A 1 29  ? 15.472 -0.758  20.600  0.36 36.31 ?  29  LYS   A HG3  1 
ATOM   809  H  HD2  A LYS   A 1 29  ? 15.582 0.992   21.779  0.64 40.16 ?  29  LYS   A HD2  1 
ATOM   810  H  HD2  B LYS   A 1 29  ? 15.447 1.270   21.689  0.36 38.13 ?  29  LYS   A HD2  1 
ATOM   811  H  HD3  A LYS   A 1 29  ? 14.288 1.463   20.981  0.64 40.16 ?  29  LYS   A HD3  1 
ATOM   812  H  HD3  B LYS   A 1 29  ? 14.163 1.729   20.867  0.36 38.13 ?  29  LYS   A HD3  1 
ATOM   813  H  HE2  A LYS   A 1 29  ? 13.090 -0.322  21.952  0.64 42.13 ?  29  LYS   A HE2  1 
ATOM   814  H  HE2  B LYS   A 1 29  ? 12.901 0.075   21.937  0.36 39.49 ?  29  LYS   A HE2  1 
ATOM   815  H  HE3  A LYS   A 1 29  ? 14.377 -0.680  22.816  0.64 42.13 ?  29  LYS   A HE3  1 
ATOM   816  H  HE3  B LYS   A 1 29  ? 14.184 -0.349  22.778  0.36 39.49 ?  29  LYS   A HE3  1 
ATOM   817  H  HZ1  A LYS   A 1 29  ? 12.928 0.580   24.032  0.64 43.23 ?  29  LYS   A HZ1  1 
ATOM   818  H  HZ1  B LYS   A 1 29  ? 12.849 1.025   24.001  0.36 40.27 ?  29  LYS   A HZ1  1 
ATOM   819  H  HZ2  A LYS   A 1 29  ? 14.153 1.334   23.853  0.64 43.23 ?  29  LYS   A HZ2  1 
ATOM   820  H  HZ2  B LYS   A 1 29  ? 14.115 1.694   23.778  0.36 40.27 ?  29  LYS   A HZ2  1 
ATOM   821  H  HZ3  A LYS   A 1 29  ? 12.980 1.659   23.066  0.64 43.23 ?  29  LYS   A HZ3  1 
ATOM   822  H  HZ3  B LYS   A 1 29  ? 12.947 2.080   23.013  0.36 40.27 ?  29  LYS   A HZ3  1 
ATOM   823  N  N    A VAL   A 1 30  ? 18.413 -1.231  18.833  0.64 23.86 ?  30  VAL   A N    1 
ATOM   824  N  N    B VAL   A 1 30  ? 18.351 -1.095  18.797  0.36 25.22 ?  30  VAL   A N    1 
ATOM   825  C  CA   A VAL   A 1 30  ? 19.076 -2.498  19.120  0.64 22.97 ?  30  VAL   A CA   1 
ATOM   826  C  CA   B VAL   A 1 30  ? 18.976 -2.380  19.098  0.36 24.57 ?  30  VAL   A CA   1 
ATOM   827  C  C    A VAL   A 1 30  ? 20.573 -2.316  19.347  0.64 21.83 ?  30  VAL   A C    1 
ATOM   828  C  C    B VAL   A 1 30  ? 20.473 -2.237  19.342  0.36 23.94 ?  30  VAL   A C    1 
ATOM   829  O  O    A VAL   A 1 30  ? 21.172 -3.039  20.151  0.64 22.39 ?  30  VAL   A O    1 
ATOM   830  O  O    B VAL   A 1 30  ? 21.038 -2.937  20.186  0.36 23.96 ?  30  VAL   A O    1 
ATOM   831  C  CB   A VAL   A 1 30  ? 18.794 -3.502  17.988  0.64 23.51 ?  30  VAL   A CB   1 
ATOM   832  C  CB   B VAL   A 1 30  ? 18.676 -3.384  17.967  0.36 24.76 ?  30  VAL   A CB   1 
ATOM   833  C  CG1  A VAL   A 1 30  ? 19.573 -4.796  18.203  0.64 24.16 ?  30  VAL   A CG1  1 
ATOM   834  C  CG1  B VAL   A 1 30  ? 19.399 -4.701  18.213  0.36 25.04 ?  30  VAL   A CG1  1 
ATOM   835  C  CG2  A VAL   A 1 30  ? 17.302 -3.784  17.887  0.64 23.63 ?  30  VAL   A CG2  1 
ATOM   836  C  CG2  B VAL   A 1 30  ? 17.177 -3.610  17.839  0.36 24.73 ?  30  VAL   A CG2  1 
ATOM   837  H  H    A VAL   A 1 30  ? 18.234 -1.105  18.001  0.64 28.75 ?  30  VAL   A H    1 
ATOM   838  H  H    B VAL   A 1 30  ? 18.273 -0.927  17.953  0.36 30.38 ?  30  VAL   A H    1 
ATOM   839  H  HA   A VAL   A 1 30  ? 18.698 -2.865  19.932  0.64 27.68 ?  30  VAL   A HA   1 
ATOM   840  H  HA   B VAL   A 1 30  ? 18.572 -2.730  19.906  0.36 29.59 ?  30  VAL   A HA   1 
ATOM   841  H  HB   A VAL   A 1 30  ? 19.084 -3.121  17.145  0.64 28.33 ?  30  VAL   A HB   1 
ATOM   842  H  HB   B VAL   A 1 30  ? 18.998 -3.022  17.127  0.36 29.82 ?  30  VAL   A HB   1 
ATOM   843  H  HG11 A VAL   A 1 30  ? 19.215 -5.480  17.613  0.64 29.11 ?  30  VAL   A HG11 1 
ATOM   844  H  HG11 B VAL   A 1 30  ? 19.029 -5.377  17.625  0.36 30.16 ?  30  VAL   A HG11 1 
ATOM   845  H  HG12 A VAL   A 1 30  ? 20.508 -4.643  18.001  0.64 29.11 ?  30  VAL   A HG12 1 
ATOM   846  H  HG12 B VAL   A 1 30  ? 20.344 -4.585  18.028  0.36 30.16 ?  30  VAL   A HG12 1 
ATOM   847  H  HG13 A VAL   A 1 30  ? 19.472 -5.075  19.127  0.64 29.11 ?  30  VAL   A HG13 1 
ATOM   848  H  HG13 B VAL   A 1 30  ? 19.270 -4.963  19.138  0.36 30.16 ?  30  VAL   A HG13 1 
ATOM   849  H  HG21 A VAL   A 1 30  ? 17.154 -4.455  17.202  0.64 28.47 ?  30  VAL   A HG21 1 
ATOM   850  H  HG21 B VAL   A 1 30  ? 17.015 -4.281  17.156  0.36 29.79 ?  30  VAL   A HG21 1 
ATOM   851  H  HG22 A VAL   A 1 30  ? 16.985 -4.111  18.743  0.64 28.47 ?  30  VAL   A HG22 1 
ATOM   852  H  HG22 B VAL   A 1 30  ? 16.830 -3.917  18.692  0.36 29.79 ?  30  VAL   A HG22 1 
ATOM   853  H  HG23 A VAL   A 1 30  ? 16.842 -2.964  17.653  0.64 28.47 ?  30  VAL   A HG23 1 
ATOM   854  H  HG23 B VAL   A 1 30  ? 16.752 -2.775  17.590  0.36 29.79 ?  30  VAL   A HG23 1 
ATOM   855  N  N    A LYS   A 1 31  ? 21.197 -1.363  18.660  0.64 20.91 ?  31  LYS   A N    1 
ATOM   856  N  N    B LYS   A 1 31  ? 21.130 -1.333  18.623  0.36 23.45 ?  31  LYS   A N    1 
ATOM   857  C  CA   A LYS   A 1 31  ? 22.649 -1.245  18.605  0.64 21.84 ?  31  LYS   A CA   1 
ATOM   858  C  CA   B LYS   A 1 31  ? 22.585 -1.247  18.590  0.36 23.49 ?  31  LYS   A CA   1 
ATOM   859  C  C    A LYS   A 1 31  ? 23.267 -2.602  18.256  0.64 19.97 ?  31  LYS   A C    1 
ATOM   860  C  C    B LYS   A 1 31  ? 23.191 -2.620  18.284  0.36 20.96 ?  31  LYS   A C    1 
ATOM   861  O  O    A LYS   A 1 31  ? 24.063 -3.147  19.027  0.64 20.78 ?  31  LYS   A O    1 
ATOM   862  O  O    B LYS   A 1 31  ? 23.902 -3.194  19.115  0.36 21.39 ?  31  LYS   A O    1 
ATOM   863  C  CB   A LYS   A 1 31  ? 23.227 -0.701  19.904  0.64 25.84 ?  31  LYS   A CB   1 
ATOM   864  C  CB   B LYS   A 1 31  ? 23.152 -0.673  19.881  0.36 26.52 ?  31  LYS   A CB   1 
ATOM   865  C  CG   A LYS   A 1 31  ? 22.553 0.565   20.405  0.64 30.24 ?  31  LYS   A CG   1 
ATOM   866  C  CG   B LYS   A 1 31  ? 22.475 0.609   20.336  0.36 29.59 ?  31  LYS   A CG   1 
ATOM   867  C  CD   A LYS   A 1 31  ? 23.571 1.624   20.800  0.64 33.63 ?  31  LYS   A CD   1 
ATOM   868  C  CD   B LYS   A 1 31  ? 23.480 1.594   20.911  0.36 32.00 ?  31  LYS   A CD   1 
ATOM   869  C  CE   A LYS   A 1 31  ? 22.955 2.669   21.718  0.64 36.05 ?  31  LYS   A CE   1 
ATOM   870  C  CE   B LYS   A 1 31  ? 22.798 2.653   21.763  0.36 33.80 ?  31  LYS   A CE   1 
ATOM   871  N  NZ   A LYS   A 1 31  ? 21.743 3.304   21.131  0.64 37.16 ?  31  LYS   A NZ   1 
ATOM   872  N  NZ   B LYS   A 1 31  ? 21.660 3.317   21.069  0.36 34.63 ?  31  LYS   A NZ   1 
ATOM   873  H  H    A LYS   A 1 31  ? 20.787 -0.758  18.203  0.64 25.21 ?  31  LYS   A H    1 
ATOM   874  H  H    B LYS   A 1 31  ? 20.741 -0.745  18.134  0.36 28.25 ?  31  LYS   A H    1 
ATOM   875  H  HA   A LYS   A 1 31  ? 22.880 -0.624  17.899  0.64 26.32 ?  31  LYS   A HA   1 
ATOM   876  H  HA   B LYS   A 1 31  ? 22.831 -0.645  17.876  0.36 28.30 ?  31  LYS   A HA   1 
ATOM   877  H  HB2  A LYS   A 1 31  ? 23.138 -1.376  20.591  0.64 31.13 ?  31  LYS   A HB2  1 
ATOM   878  H  HB2  B LYS   A 1 31  ? 23.046 -1.328  20.582  0.36 31.94 ?  31  LYS   A HB2  1 
ATOM   879  H  HB3  A LYS   A 1 31  ? 24.166 -0.498  19.762  0.64 31.13 ?  31  LYS   A HB3  1 
ATOM   880  H  HB3  B LYS   A 1 31  ? 24.096 -0.480  19.749  0.36 31.94 ?  31  LYS   A HB3  1 
ATOM   881  H  HG2  A LYS   A 1 31  ? 21.992 0.930   19.704  0.64 36.40 ?  31  LYS   A HG2  1 
ATOM   882  H  HG2  B LYS   A 1 31  ? 22.038 1.028   19.578  0.36 35.63 ?  31  LYS   A HG2  1 
ATOM   883  H  HG3  A LYS   A 1 31  ? 22.018 0.353   21.187  0.64 36.40 ?  31  LYS   A HG3  1 
ATOM   884  H  HG3  B LYS   A 1 31  ? 21.825 0.401   21.025  0.36 35.63 ?  31  LYS   A HG3  1 
ATOM   885  H  HD2  A LYS   A 1 31  ? 24.309 1.203   21.270  0.64 40.47 ?  31  LYS   A HD2  1 
ATOM   886  H  HD2  B LYS   A 1 31  ? 24.114 1.116   21.468  0.36 38.51 ?  31  LYS   A HD2  1 
ATOM   887  H  HD3  A LYS   A 1 31  ? 23.895 2.072   20.001  0.64 40.47 ?  31  LYS   A HD3  1 
ATOM   888  H  HD3  B LYS   A 1 31  ? 23.943 2.040   20.183  0.36 38.51 ?  31  LYS   A HD3  1 
ATOM   889  H  HE2  A LYS   A 1 31  ? 22.698 2.245   22.552  0.64 43.37 ?  31  LYS   A HE2  1 
ATOM   890  H  HE2  B LYS   A 1 31  ? 22.458 2.235   22.568  0.36 40.67 ?  31  LYS   A HE2  1 
ATOM   891  H  HE3  A LYS   A 1 31  ? 23.607 3.367   21.888  0.64 43.37 ?  31  LYS   A HE3  1 
ATOM   892  H  HE3  B LYS   A 1 31  ? 23.446 3.337   21.994  0.36 40.67 ?  31  LYS   A HE3  1 
ATOM   893  H  HZ1  A LYS   A 1 31  ? 21.425 3.923   21.686  0.64 44.70 ?  31  LYS   A HZ1  1 
ATOM   894  H  HZ1  B LYS   A 1 31  ? 21.314 3.951   21.590  0.36 41.67 ?  31  LYS   A HZ1  1 
ATOM   895  H  HZ2  A LYS   A 1 31  ? 21.947 3.689   20.355  0.64 44.70 ?  31  LYS   A HZ2  1 
ATOM   896  H  HZ2  B LYS   A 1 31  ? 21.940 3.688   20.310  0.36 41.67 ?  31  LYS   A HZ2  1 
ATOM   897  H  HZ3  A LYS   A 1 31  ? 21.114 2.690   20.992  0.64 44.70 ?  31  LYS   A HZ3  1 
ATOM   898  H  HZ3  B LYS   A 1 31  ? 21.026 2.720   20.882  0.36 41.67 ?  31  LYS   A HZ3  1 
ATOM   899  N  N    . PRO   A 1 32  ? 22.924 -3.166  17.101  1.00 18.43 ?  32  PRO   A N    1 
ATOM   900  C  CA   . PRO   A 1 32  ? 23.396 -4.512  16.778  1.00 17.92 ?  32  PRO   A CA   1 
ATOM   901  C  C    . PRO   A 1 32  ? 24.896 -4.526  16.568  1.00 17.88 ?  32  PRO   A C    1 
ATOM   902  O  O    . PRO   A 1 32  ? 25.538 -3.494  16.360  1.00 17.86 ?  32  PRO   A O    1 
ATOM   903  C  CB   . PRO   A 1 32  ? 22.672 -4.823  15.466  1.00 17.76 ?  32  PRO   A CB   1 
ATOM   904  C  CG   . PRO   A 1 32  ? 22.517 -3.477  14.825  1.00 16.86 ?  32  PRO   A CG   1 
ATOM   905  C  CD   . PRO   A 1 32  ? 22.223 -2.545  15.967  1.00 16.97 ?  32  PRO   A CD   1 
ATOM   906  H  HA   . PRO   A 1 32  ? 23.145 -5.148  17.465  1.00 21.62 ?  32  PRO   A HA   1 
ATOM   907  H  HB2  . PRO   A 1 32  ? 23.218 -5.415  14.920  1.00 21.43 ?  32  PRO   A HB2  1 
ATOM   908  H  HB3  . PRO   A 1 32  ? 21.809 -5.228  15.654  1.00 21.43 ?  32  PRO   A HB3  1 
ATOM   909  H  HG2  . PRO   A 1 32  ? 23.340 -3.241  14.376  1.00 20.35 ?  32  PRO   A HG2  1 
ATOM   910  H  HG3  . PRO   A 1 32  ? 21.776 -3.510  14.197  1.00 20.35 ?  32  PRO   A HG3  1 
ATOM   911  H  HD2  . PRO   A 1 32  ? 22.591 -1.669  15.770  1.00 20.49 ?  32  PRO   A HD2  1 
ATOM   912  H  HD3  . PRO   A 1 32  ? 21.271 -2.508  16.128  1.00 20.49 ?  32  PRO   A HD3  1 
ATOM   913  N  N    . THR   A 1 33  ? 25.450 -5.736  16.597  1.00 17.63 ?  33  THR   A N    1 
ATOM   914  C  CA   . THR   A 1 33  ? 26.864 -5.897  16.287  1.00 17.61 ?  33  THR   A CA   1 
ATOM   915  C  C    . THR   A 1 33  ? 27.168 -5.439  14.868  1.00 16.03 ?  33  THR   A C    1 
ATOM   916  O  O    . THR   A 1 33  ? 28.202 -4.799  14.621  1.00 16.26 ?  33  THR   A O    1 
ATOM   917  C  CB   . THR   A 1 33  ? 27.270 -7.355  16.485  1.00 19.36 ?  33  THR   A CB   1 
ATOM   918  O  OG1  . THR   A 1 33  ? 26.958 -7.747  17.824  1.00 21.27 ?  33  THR   A OG1  1 
ATOM   919  C  CG2  . THR   A 1 33  ? 28.761 -7.540  16.237  1.00 20.30 ?  33  THR   A CG2  1 
ATOM   920  H  H    . THR   A 1 33  ? 25.036 -6.465  16.781  1.00 21.27 ?  33  THR   A H    1 
ATOM   921  H  HA   . THR   A 1 33  ? 27.388 -5.357  16.897  1.00 21.24 ?  33  THR   A HA   1 
ATOM   922  H  HB   . THR   A 1 33  ? 26.783 -7.921  15.862  1.00 23.34 ?  33  THR   A HB   1 
ATOM   923  H  HG1  . THR   A 1 33  ? 27.391 -7.276  18.372  1.00 25.64 ?  33  THR   A HG1  1 
ATOM   924  H  HG21 . THR   A 1 33  ? 29.038 -8.426  16.522  1.00 24.47 ?  33  THR   A HG21 1 
ATOM   925  H  HG22 . THR   A 1 33  ? 28.958 -7.440  15.293  1.00 24.47 ?  33  THR   A HG22 1 
ATOM   926  H  HG23 . THR   A 1 33  ? 29.263 -6.879  16.737  1.00 24.47 ?  33  THR   A HG23 1 
ATOM   927  N  N    . VAL   A 1 34  ? 26.275 -5.743  13.924  1.00 14.46 ?  34  VAL   A N    1 
ATOM   928  C  CA   . VAL   A 1 34  ? 26.472 -5.423  12.515  1.00 13.40 ?  34  VAL   A CA   1 
ATOM   929  C  C    . VAL   A 1 34  ? 25.173 -4.866  11.944  1.00 12.46 ?  34  VAL   A C    1 
ATOM   930  O  O    . VAL   A 1 34  ? 24.134 -5.537  11.988  1.00 13.35 ?  34  VAL   A O    1 
ATOM   931  C  CB   . VAL   A 1 34  ? 26.910 -6.642  11.682  1.00 14.07 ?  34  VAL   A CB   1 
ATOM   932  C  CG1  . VAL   A 1 34  ? 27.092 -6.241  10.226  1.00 14.35 ?  34  VAL   A CG1  1 
ATOM   933  C  CG2  . VAL   A 1 34  ? 28.179 -7.264  12.252  1.00 15.18 ?  34  VAL   A CG2  1 
ATOM   934  H  H    . VAL   A 1 34  ? 25.533 -6.150  14.082  1.00 17.47 ?  34  VAL   A H    1 
ATOM   935  H  HA   . VAL   A 1 34  ? 27.157 -4.738  12.432  1.00 16.20 ?  34  VAL   A HA   1 
ATOM   936  H  HB   . VAL   A 1 34  ? 26.207 -7.310  11.723  1.00 17.00 ?  34  VAL   A HB   1 
ATOM   937  H  HG11 . VAL   A 1 34  ? 27.588 -6.939  9.771   1.00 17.34 ?  34  VAL   A HG11 1 
ATOM   938  H  HG12 . VAL   A 1 34  ? 26.220 -6.135  9.814   1.00 17.34 ?  34  VAL   A HG12 1 
ATOM   939  H  HG13 . VAL   A 1 34  ? 27.584 -5.407  10.188  1.00 17.34 ?  34  VAL   A HG13 1 
ATOM   940  H  HG21 . VAL   A 1 34  ? 28.448 -8.002  11.684  1.00 18.33 ?  34  VAL   A HG21 1 
ATOM   941  H  HG22 . VAL   A 1 34  ? 28.875 -6.591  12.277  1.00 18.33 ?  34  VAL   A HG22 1 
ATOM   942  H  HG23 . VAL   A 1 34  ? 27.997 -7.586  13.150  1.00 18.33 ?  34  VAL   A HG23 1 
ATOM   943  N  N    . VAL   A 1 35  ? 25.236 -3.651  11.396  1.00 11.79 ?  35  VAL   A N    1 
ATOM   944  C  CA   . VAL   A 1 35  ? 24.208 -3.135  10.501  1.00 11.29 ?  35  VAL   A CA   1 
ATOM   945  C  C    . VAL   A 1 35  ? 24.764 -3.144  9.084   1.00 10.88 ?  35  VAL   A C    1 
ATOM   946  O  O    . VAL   A 1 35  ? 25.915 -2.749  8.858   1.00 11.32 ?  35  VAL   A O    1 
ATOM   947  C  CB   . VAL   A 1 35  ? 23.678 -1.739  10.904  1.00 12.19 ?  35  VAL   A CB   1 
ATOM   948  C  CG1  . VAL   A 1 35  ? 24.751 -0.648  10.793  1.00 12.87 ?  35  VAL   A CG1  1 
ATOM   949  C  CG2  . VAL   A 1 35  ? 22.457 -1.382  10.059  1.00 12.84 ?  35  VAL   A CG2  1 
ATOM   950  H  H    . VAL   A 1 35  ? 25.876 -3.091  11.529  1.00 14.27 ?  35  VAL   A H    1 
ATOM   951  H  HA   . VAL   A 1 35  ? 23.451 -3.746  10.518  1.00 13.67 ?  35  VAL   A HA   1 
ATOM   952  H  HB   . VAL   A 1 35  ? 23.383 -1.774  11.825  1.00 14.74 ?  35  VAL   A HB   1 
ATOM   953  H  HG11 . VAL   A 1 35  ? 24.394 0.180   11.148  1.00 15.56 ?  35  VAL   A HG11 1 
ATOM   954  H  HG12 . VAL   A 1 35  ? 25.525 -0.924  11.306  1.00 15.56 ?  35  VAL   A HG12 1 
ATOM   955  H  HG13 . VAL   A 1 35  ? 24.992 -0.535  9.861   1.00 15.56 ?  35  VAL   A HG13 1 
ATOM   956  H  HG21 . VAL   A 1 35  ? 22.091 -0.541  10.369  1.00 15.53 ?  35  VAL   A HG21 1 
ATOM   957  H  HG22 . VAL   A 1 35  ? 22.729 -1.300  9.128   1.00 15.53 ?  35  VAL   A HG22 1 
ATOM   958  H  HG23 . VAL   A 1 35  ? 21.794 -2.085  10.144  1.00 15.53 ?  35  VAL   A HG23 1 
ATOM   959  N  N    . VAL   A 1 36  ? 23.951 -3.603  8.131   1.00 10.11 ?  36  VAL   A N    1 
ATOM   960  C  CA   . VAL   A 1 36  ? 24.332 -3.620  6.726   1.00 9.90  ?  36  VAL   A CA   1 
ATOM   961  C  C    . VAL   A 1 36  ? 23.877 -2.328  6.059   1.00 10.27 ?  36  VAL   A C    1 
ATOM   962  O  O    . VAL   A 1 36  ? 22.712 -1.922  6.190   1.00 10.81 ?  36  VAL   A O    1 
ATOM   963  C  CB   . VAL   A 1 36  ? 23.723 -4.832  6.007   1.00 9.95  ?  36  VAL   A CB   1 
ATOM   964  C  CG1  . VAL   A 1 36  ? 23.992 -4.761  4.524   1.00 10.85 ?  36  VAL   A CG1  1 
ATOM   965  C  CG2  . VAL   A 1 36  ? 24.268 -6.125  6.592   1.00 11.06 ?  36  VAL   A CG2  1 
ATOM   966  H  H    . VAL   A 1 36  ? 23.158 -3.910  8.278   1.00 12.25 ?  36  VAL   A H    1 
ATOM   967  H  HA   . VAL   A 1 36  ? 25.301 -3.683  6.656   1.00 12.00 ?  36  VAL   A HA   1 
ATOM   968  H  HB   . VAL   A 1 36  ? 22.762 -4.822  6.139   1.00 12.05 ?  36  VAL   A HB   1 
ATOM   969  H  HG11 . VAL   A 1 36  ? 23.853 -5.639  4.135   1.00 13.14 ?  36  VAL   A HG11 1 
ATOM   970  H  HG12 . VAL   A 1 36  ? 23.383 -4.123  4.116   1.00 13.14 ?  36  VAL   A HG12 1 
ATOM   971  H  HG13 . VAL   A 1 36  ? 24.910 -4.480  4.380   1.00 13.14 ?  36  VAL   A HG13 1 
ATOM   972  H  HG21 . VAL   A 1 36  ? 23.875 -6.879  6.117   1.00 13.38 ?  36  VAL   A HG21 1 
ATOM   973  H  HG22 . VAL   A 1 36  ? 25.232 -6.141  6.492   1.00 13.38 ?  36  VAL   A HG22 1 
ATOM   974  H  HG23 . VAL   A 1 36  ? 24.032 -6.177  7.533   1.00 13.38 ?  36  VAL   A HG23 1 
ATOM   975  N  N    . ASN   A 1 37  ? 24.797 -1.698  5.328   1.00 9.30  ?  37  ASN   A N    1 
ATOM   976  C  CA   . ASN   A 1 37  ? 24.476 -0.579  4.455   1.00 9.24  ?  37  ASN   A CA   1 
ATOM   977  C  C    . ASN   A 1 37  ? 24.347 -1.048  3.016   1.00 9.46  ?  37  ASN   A C    1 
ATOM   978  O  O    . ASN   A 1 37  ? 25.132 -1.882  2.548   1.00 9.90  ?  37  ASN   A O    1 
ATOM   979  C  CB   . ASN   A 1 37  ? 25.551 0.498   4.535   1.00 9.72  ?  37  ASN   A CB   1 
ATOM   980  C  CG   . ASN   A 1 37  ? 25.229 1.696   3.677   1.00 9.93  ?  37  ASN   A CG   1 
ATOM   981  O  OD1  . ASN   A 1 37  ? 24.059 2.036   3.479   1.00 10.37 ?  37  ASN   A OD1  1 
ATOM   982  N  ND2  . ASN   A 1 37  ? 26.269 2.345   3.162   1.00 10.42 ?  37  ASN   A ND2  1 
ATOM   983  H  H    . ASN   A 1 37  ? 25.636 -1.892  5.331   1.00 11.27 ?  37  ASN   A H    1 
ATOM   984  H  HA   . ASN   A 1 37  ? 23.635 -0.182  4.729   1.00 11.20 ?  37  ASN   A HA   1 
ATOM   985  H  HB2  . ASN   A 1 37  ? 25.636 0.797   5.454   1.00 11.78 ?  37  ASN   A HB2  1 
ATOM   986  H  HB3  . ASN   A 1 37  ? 26.398 0.124   4.231   1.00 11.78 ?  37  ASN   A HB3  1 
ATOM   987  H  HD21 . ASN   A 1 37  ? 26.138 3.034   2.664   1.00 12.62 ?  37  ASN   A HD21 1 
ATOM   988  H  HD22 . ASN   A 1 37  ? 27.067 2.082   3.320   1.00 12.62 ?  37  ASN   A HD22 1 
ATOM   989  N  N    A ALA   A 1 38  ? 23.327 -0.515  2.336   0.64 9.69  ?  38  ALA   A N    1 
ATOM   990  N  N    B ALA   A 1 38  ? 23.333 -0.535  2.316   0.36 9.94  ?  38  ALA   A N    1 
ATOM   991  C  CA   A ALA   A 1 38  ? 23.138 -0.638  0.891   0.64 9.78  ?  38  ALA   A CA   1 
ATOM   992  C  CA   B ALA   A 1 38  ? 23.170 -0.797  0.884   0.36 10.51 ?  38  ALA   A CA   1 
ATOM   993  C  C    A ALA   A 1 38  ? 24.066 0.358   0.195   0.64 9.60  ?  38  ALA   A C    1 
ATOM   994  C  C    B ALA   A 1 38  ? 23.989 0.237   0.115   0.36 10.43 ?  38  ALA   A C    1 
ATOM   995  O  O    A ALA   A 1 38  ? 23.668 1.460   -0.198  0.64 9.35  ?  38  ALA   A O    1 
ATOM   996  O  O    B ALA   A 1 38  ? 23.482 1.246   -0.386  0.36 10.09 ?  38  ALA   A O    1 
ATOM   997  C  CB   A ALA   A 1 38  ? 21.680 -0.374  0.533   0.64 10.52 ?  38  ALA   A CB   1 
ATOM   998  C  CB   B ALA   A 1 38  ? 21.697 -0.778  0.495   0.36 11.00 ?  38  ALA   A CB   1 
ATOM   999  H  H    A ALA   A 1 38  ? 22.710 -0.046  2.711   0.64 11.74 ?  38  ALA   A H    1 
ATOM   1000 H  H    B ALA   A 1 38  ? 22.723 -0.025  2.648   0.36 12.05 ?  38  ALA   A H    1 
ATOM   1001 H  HA   A ALA   A 1 38  ? 23.371 -1.532  0.603   0.64 11.86 ?  38  ALA   A HA   1 
ATOM   1002 H  HA   B ALA   A 1 38  ? 23.524 -1.678  0.680   0.36 12.73 ?  38  ALA   A HA   1 
ATOM   1003 H  HB1  A ALA   A 1 38  ? 21.565 -0.459  -0.427  0.64 12.74 ?  38  ALA   A HB1  1 
ATOM   1004 H  HB1  B ALA   A 1 38  ? 21.624 -0.914  -0.463  0.36 13.31 ?  38  ALA   A HB1  1 
ATOM   1005 H  HB2  A ALA   A 1 38  ? 21.117 -1.020  0.991   0.64 12.74 ?  38  ALA   A HB2  1 
ATOM   1006 H  HB2  B ALA   A 1 38  ? 21.233 -1.489  0.966   0.36 13.31 ?  38  ALA   A HB2  1 
ATOM   1007 H  HB3  A ALA   A 1 38  ? 21.440 0.526   0.814   0.64 12.74 ?  38  ALA   A HB3  1 
ATOM   1008 H  HB3  B ALA   A 1 38  ? 21.318 0.081   0.734   0.36 13.31 ?  38  ALA   A HB3  1 
ATOM   1009 N  N    A ALA   A 1 39  ? 25.327 -0.041  0.044   0.64 9.73  ?  39  ALA   A N    1 
ATOM   1010 N  N    B ALA   A 1 39  ? 25.287 -0.034  0.018   0.36 10.80 ?  39  ALA   A N    1 
ATOM   1011 C  CA   A ALA   A 1 39  ? 26.378 0.829   -0.457  0.64 9.78  ?  39  ALA   A CA   1 
ATOM   1012 C  CA   B ALA   A 1 39  ? 26.252 0.937   -0.464  0.36 11.08 ?  39  ALA   A CA   1 
ATOM   1013 C  C    A ALA   A 1 39  ? 26.467 0.794   -1.981  0.64 10.08 ?  39  ALA   A C    1 
ATOM   1014 C  C    B ALA   A 1 39  ? 26.496 0.788   -1.962  0.36 10.42 ?  39  ALA   A C    1 
ATOM   1015 O  O    A ALA   A 1 39  ? 25.939 -0.103  -2.646  0.64 10.58 ?  39  ALA   A O    1 
ATOM   1016 O  O    B ALA   A 1 39  ? 26.118 -0.203  -2.592  0.36 10.05 ?  39  ALA   A O    1 
ATOM   1017 C  CB   A ALA   A 1 39  ? 27.721 0.406   0.152   0.64 10.01 ?  39  ALA   A CB   1 
ATOM   1018 C  CB   B ALA   A 1 39  ? 27.568 0.776   0.297   0.36 12.31 ?  39  ALA   A CB   1 
ATOM   1019 H  H    A ALA   A 1 39  ? 25.596 -0.836  0.238   0.64 11.79 ?  39  ALA   A H    1 
ATOM   1020 H  H    B ALA   A 1 39  ? 25.633 -0.795  0.228   0.36 13.07 ?  39  ALA   A H    1 
ATOM   1021 H  HA   A ALA   A 1 39  ? 26.194 1.741   -0.179  0.64 11.85 ?  39  ALA   A HA   1 
ATOM   1022 H  HA   B ALA   A 1 39  ? 25.912 1.827   -0.298  0.36 13.42 ?  39  ALA   A HA   1 
ATOM   1023 H  HB1  A ALA   A 1 39  ? 28.416 0.996   -0.184  0.64 12.13 ?  39  ALA   A HB1  1 
ATOM   1024 H  HB1  B ALA   A 1 39  ? 28.201 1.432   -0.031  0.36 14.89 ?  39  ALA   A HB1  1 
ATOM   1025 H  HB2  A ALA   A 1 39  ? 27.669 0.486   1.122   0.64 12.13 ?  39  ALA   A HB2  1 
ATOM   1026 H  HB2  B ALA   A 1 39  ? 27.403 0.917   1.242   0.36 14.89 ?  39  ALA   A HB2  1 
ATOM   1027 H  HB3  A ALA   A 1 39  ? 27.910 -0.507  -0.095  0.64 12.13 ?  39  ALA   A HB3  1 
ATOM   1028 H  HB3  B ALA   A 1 39  ? 27.911 -0.119  0.151   0.36 14.89 ?  39  ALA   A HB3  1 
ATOM   1029 N  N    . ASN   A 1 40  ? 27.157 1.796   -2.528  1.00 10.38 ?  40  ASN   A N    1 
ATOM   1030 C  CA   . ASN   A 1 40  ? 27.685 1.748   -3.886  1.00 10.64 ?  40  ASN   A CA   1 
ATOM   1031 C  C    . ASN   A 1 40  ? 29.210 1.631   -3.825  1.00 10.06 ?  40  ASN   A C    1 
ATOM   1032 O  O    . ASN   A 1 40  ? 29.813 1.730   -2.752  1.00 10.29 ?  40  ASN   A O    1 
ATOM   1033 C  CB   . ASN   A 1 40  ? 27.224 2.940   -4.739  1.00 11.70 ?  40  ASN   A CB   1 
ATOM   1034 C  CG   . ASN   A 1 40  ? 27.593 4.279   -4.138  1.00 12.56 ?  40  ASN   A CG   1 
ATOM   1035 O  OD1  . ASN   A 1 40  ? 28.768 4.545   -3.857  1.00 12.83 ?  40  ASN   A OD1  1 
ATOM   1036 N  ND2  . ASN   A 1 40  ? 26.592 5.145   -3.962  1.00 13.77 ?  40  ASN   A ND2  1 
ATOM   1037 H  H    A ASN   A 1 40  ? 27.345 2.527   -2.120  0.64 12.57 ?  40  ASN   A H    1 
ATOM   1038 H  H    B ASN   A 1 40  ? 27.332 2.534   -2.127  0.36 12.57 ?  40  ASN   A H    1 
ATOM   1039 H  HA   . ASN   A 1 40  ? 27.355 0.944   -4.319  1.00 12.88 ?  40  ASN   A HA   1 
ATOM   1040 H  HB2  . ASN   A 1 40  ? 27.637 2.880   -5.617  1.00 14.15 ?  40  ASN   A HB2  1 
ATOM   1041 H  HB3  . ASN   A 1 40  ? 26.259 2.908   -4.830  1.00 14.15 ?  40  ASN   A HB3  1 
ATOM   1042 H  HD21 . ASN   A 1 40  ? 26.754 5.925   -3.632  1.00 16.64 ?  40  ASN   A HD21 1 
ATOM   1043 H  HD22 . ASN   A 1 40  ? 25.791 4.927   -4.175  1.00 16.64 ?  40  ASN   A HD22 1 
ATOM   1044 N  N    . VAL   A 1 41  ? 29.829 1.387   -4.984  1.00 10.63 ?  41  VAL   A N    1 
ATOM   1045 C  CA   . VAL   A 1 41  ? 31.259 1.074   -5.009  1.00 11.46 ?  41  VAL   A CA   1 
ATOM   1046 C  C    . VAL   A 1 41  ? 32.124 2.222   -4.528  1.00 11.39 ?  41  VAL   A C    1 
ATOM   1047 O  O    . VAL   A 1 41  ? 33.270 1.996   -4.114  1.00 11.98 ?  41  VAL   A O    1 
ATOM   1048 C  CB   . VAL   A 1 41  ? 31.744 0.595   -6.397  1.00 12.21 ?  41  VAL   A CB   1 
ATOM   1049 C  CG1  . VAL   A 1 41  ? 31.063 -0.706  -6.787  1.00 13.16 ?  41  VAL   A CG1  1 
ATOM   1050 C  CG2  . VAL   A 1 41  ? 31.563 1.660   -7.469  1.00 13.12 ?  41  VAL   A CG2  1 
ATOM   1051 H  H    . VAL   A 1 41  ? 29.448 1.389   -5.757  1.00 12.87 ?  41  VAL   A H    1 
ATOM   1052 H  HA   . VAL   A 1 41  ? 31.409 0.335   -4.398  1.00 13.87 ?  41  VAL   A HA   1 
ATOM   1053 H  HB   . VAL   A 1 41  ? 32.695 0.399   -6.340  1.00 14.77 ?  41  VAL   A HB   1 
ATOM   1054 H  HG11 . VAL   A 1 41  ? 31.397 -0.999  -7.650  1.00 15.91 ?  41  VAL   A HG11 1 
ATOM   1055 H  HG12 . VAL   A 1 41  ? 31.252 -1.382  -6.115  1.00 15.91 ?  41  VAL   A HG12 1 
ATOM   1056 H  HG13 . VAL   A 1 41  ? 30.104 -0.557  -6.840  1.00 15.91 ?  41  VAL   A HG13 1 
ATOM   1057 H  HG21 . VAL   A 1 41  ? 31.810 1.285   -8.333  1.00 15.86 ?  41  VAL   A HG21 1 
ATOM   1058 H  HG22 . VAL   A 1 41  ? 30.639 1.940   -7.483  1.00 15.86 ?  41  VAL   A HG22 1 
ATOM   1059 H  HG23 . VAL   A 1 41  ? 32.140 2.411   -7.263  1.00 15.86 ?  41  VAL   A HG23 1 
ATOM   1060 N  N    . TYR   A 1 42  ? 31.618 3.456   -4.594  1.00 11.25 ?  42  TYR   A N    1 
ATOM   1061 C  CA   . TYR   A 1 42  ? 32.356 4.640   -4.176  1.00 11.33 ?  42  TYR   A CA   1 
ATOM   1062 C  C    . TYR   A 1 42  ? 32.101 5.013   -2.724  1.00 11.03 ?  42  TYR   A C    1 
ATOM   1063 O  O    . TYR   A 1 42  ? 32.666 6.007   -2.243  1.00 11.59 ?  42  TYR   A O    1 
ATOM   1064 C  CB   . TYR   A 1 42  ? 32.009 5.825   -5.096  1.00 11.53 ?  42  TYR   A CB   1 
ATOM   1065 C  CG   . TYR   A 1 42  ? 32.192 5.510   -6.566  1.00 12.54 ?  42  TYR   A CG   1 
ATOM   1066 C  CD1  . TYR   A 1 42  ? 33.454 5.310   -7.101  1.00 13.28 ?  42  TYR   A CD1  1 
ATOM   1067 C  CD2  . TYR   A 1 42  ? 31.101 5.394   -7.416  1.00 14.16 ?  42  TYR   A CD2  1 
ATOM   1068 C  CE1  . TYR   A 1 42  ? 33.622 5.000   -8.439  1.00 14.21 ?  42  TYR   A CE1  1 
ATOM   1069 C  CE2  . TYR   A 1 42  ? 31.264 5.099   -8.757  1.00 15.11 ?  42  TYR   A CE2  1 
ATOM   1070 C  CZ   . TYR   A 1 42  ? 32.529 4.900   -9.262  1.00 15.13 ?  42  TYR   A CZ   1 
ATOM   1071 O  OH   . TYR   A 1 42  ? 32.702 4.594   -10.591 1.00 16.91 ?  42  TYR   A OH   1 
ATOM   1072 H  H    . TYR   A 1 42  ? 30.827 3.629   -4.891  1.00 13.62 ?  42  TYR   A H    1 
ATOM   1073 H  HA   . TYR   A 1 42  ? 33.301 4.469   -4.278  1.00 13.71 ?  42  TYR   A HA   1 
ATOM   1074 H  HB2  . TYR   A 1 42  ? 31.075 6.071   -4.956  1.00 13.95 ?  42  TYR   A HB2  1 
ATOM   1075 H  HB3  . TYR   A 1 42  ? 32.579 6.576   -4.877  1.00 13.95 ?  42  TYR   A HB3  1 
ATOM   1076 H  HD1  . TYR   A 1 42  ? 34.197 5.369   -6.546  1.00 16.05 ?  42  TYR   A HD1  1 
ATOM   1077 H  HD2  . TYR   A 1 42  ? 30.244 5.529   -7.080  1.00 17.10 ?  42  TYR   A HD2  1 
ATOM   1078 H  HE1  . TYR   A 1 42  ? 34.478 4.867   -8.782  1.00 17.17 ?  42  TYR   A HE1  1 
ATOM   1079 H  HE2  . TYR   A 1 42  ? 30.522 5.028   -9.316  1.00 18.25 ?  42  TYR   A HE2  1 
ATOM   1080 H  HH   . TYR   A 1 42  ? 33.523 4.494   -10.761 1.00 20.41 ?  42  TYR   A HH   1 
ATOM   1081 N  N    . LEU   A 1 43  ? 31.244 4.256   -2.034  1.00 10.73 ?  43  LEU   A N    1 
ATOM   1082 C  CA   . LEU   A 1 43  ? 30.798 4.596   -0.688  1.00 10.55 ?  43  LEU   A CA   1 
ATOM   1083 C  C    . LEU   A 1 43  ? 30.318 6.043   -0.600  1.00 10.62 ?  43  LEU   A C    1 
ATOM   1084 O  O    . LEU   A 1 43  ? 30.582 6.750   0.375   1.00 11.67 ?  43  LEU   A O    1 
ATOM   1085 C  CB   . LEU   A 1 43  ? 31.842 4.289   0.384   1.00 10.96 ?  43  LEU   A CB   1 
ATOM   1086 C  CG   . LEU   A 1 43  ? 32.341 2.839   0.475   1.00 11.08 ?  43  LEU   A CG   1 
ATOM   1087 C  CD1  . LEU   A 1 43  ? 33.375 2.725   1.583   1.00 11.91 ?  43  LEU   A CD1  1 
ATOM   1088 C  CD2  . LEU   A 1 43  ? 31.197 1.858   0.704   1.00 11.71 ?  43  LEU   A CD2  1 
ATOM   1089 H  H    . LEU   A 1 43  ? 30.910 3.513   -2.327  1.00 12.99 ?  43  LEU   A H    1 
ATOM   1090 H  HA   . LEU   A 1 43  ? 30.028 4.039   -0.486  1.00 12.77 ?  43  LEU   A HA   1 
ATOM   1091 H  HB2  . LEU   A 1 43  ? 32.615 4.852   0.227   1.00 13.27 ?  43  LEU   A HB2  1 
ATOM   1092 H  HB3  . LEU   A 1 43  ? 31.458 4.511   1.251   1.00 13.27 ?  43  LEU   A HB3  1 
ATOM   1093 H  HG   . LEU   A 1 43  ? 32.779 2.604   -0.357  1.00 13.42 ?  43  LEU   A HG   1 
ATOM   1094 H  HD11 . LEU   A 1 43  ? 33.686 1.804   1.632   1.00 14.41 ?  43  LEU   A HD11 1 
ATOM   1095 H  HD12 . LEU   A 1 43  ? 34.119 3.313   1.389   1.00 14.41 ?  43  LEU   A HD12 1 
ATOM   1096 H  HD13 . LEU   A 1 43  ? 32.965 2.976   2.427   1.00 14.41 ?  43  LEU   A HD13 1 
ATOM   1097 H  HD21 . LEU   A 1 43  ? 31.570 0.975   0.850   1.00 14.17 ?  43  LEU   A HD21 1 
ATOM   1098 H  HD22 . LEU   A 1 43  ? 30.696 2.142   1.480   1.00 14.17 ?  43  LEU   A HD22 1 
ATOM   1099 H  HD23 . LEU   A 1 43  ? 30.632 1.857   -0.081  1.00 14.17 ?  43  LEU   A HD23 1 
ATOM   1100 N  N    A LYS   A 1 44  ? 29.593 6.483   -1.628  0.64 10.61 ?  44  LYS   A N    1 
ATOM   1101 N  N    B LYS   A 1 44  ? 29.598 6.483   -1.633  0.36 10.99 ?  44  LYS   A N    1 
ATOM   1102 C  CA   A LYS   A 1 44  ? 28.949 7.796   -1.626  0.64 11.03 ?  44  LYS   A CA   1 
ATOM   1103 C  CA   B LYS   A 1 44  ? 28.940 7.788   -1.638  0.36 11.69 ?  44  LYS   A CA   1 
ATOM   1104 C  C    A LYS   A 1 44  ? 27.518 7.620   -1.136  0.64 10.53 ?  44  LYS   A C    1 
ATOM   1105 C  C    B LYS   A 1 44  ? 27.521 7.586   -1.125  0.36 10.87 ?  44  LYS   A C    1 
ATOM   1106 O  O    A LYS   A 1 44  ? 26.650 7.128   -1.863  0.64 11.46 ?  44  LYS   A O    1 
ATOM   1107 O  O    B LYS   A 1 44  ? 26.661 7.048   -1.827  0.36 11.26 ?  44  LYS   A O    1 
ATOM   1108 C  CB   A LYS   A 1 44  ? 29.005 8.421   -3.013  0.64 13.33 ?  44  LYS   A CB   1 
ATOM   1109 C  CB   B LYS   A 1 44  ? 28.952 8.388   -3.039  0.36 13.95 ?  44  LYS   A CB   1 
ATOM   1110 C  CG   A LYS   A 1 44  ? 30.394 8.869   -3.433  0.64 17.07 ?  44  LYS   A CG   1 
ATOM   1111 C  CG   B LYS   A 1 44  ? 30.308 8.912   -3.483  0.36 16.82 ?  44  LYS   A CG   1 
ATOM   1112 C  CD   A LYS   A 1 44  ? 31.058 9.773   -2.398  0.64 21.91 ?  44  LYS   A CD   1 
ATOM   1113 C  CD   B LYS   A 1 44  ? 30.894 9.888   -2.472  0.36 20.05 ?  44  LYS   A CD   1 
ATOM   1114 C  CE   A LYS   A 1 44  ? 32.389 10.299  -2.896  0.64 24.79 ?  44  LYS   A CE   1 
ATOM   1115 C  CE   B LYS   A 1 44  ? 32.221 10.436  -2.946  0.36 22.09 ?  44  LYS   A CE   1 
ATOM   1116 N  NZ   A LYS   A 1 44  ? 33.184 10.912  -1.801  0.64 26.17 ?  44  LYS   A NZ   1 
ATOM   1117 N  NZ   B LYS   A 1 44  ? 33.068 10.896  -1.814  0.36 23.31 ?  44  LYS   A NZ   1 
ATOM   1118 H  H    A LYS   A 1 44  ? 29.455 6.027   -2.347  0.64 12.85 ?  44  LYS   A H    1 
ATOM   1119 H  H    B LYS   A 1 44  ? 29.470 6.030   -2.355  0.36 13.31 ?  44  LYS   A H    1 
ATOM   1120 H  HA   A LYS   A 1 44  ? 29.398 8.370   -0.992  0.64 13.36 ?  44  LYS   A HA   1 
ATOM   1121 H  HA   B LYS   A 1 44  ? 29.391 8.382   -1.021  0.36 14.15 ?  44  LYS   A HA   1 
ATOM   1122 H  HB2  A LYS   A 1 44  ? 28.694 7.772   -3.662  0.64 16.11 ?  44  LYS   A HB2  1 
ATOM   1123 H  HB2  B LYS   A 1 44  ? 28.681 7.706   -3.674  0.36 16.85 ?  44  LYS   A HB2  1 
ATOM   1124 H  HB3  A LYS   A 1 44  ? 28.427 9.200   -3.024  0.64 16.11 ?  44  LYS   A HB3  1 
ATOM   1125 H  HB3  B LYS   A 1 44  ? 28.329 9.130   -3.068  0.36 16.85 ?  44  LYS   A HB3  1 
ATOM   1126 H  HG2  A LYS   A 1 44  ? 30.957 8.088   -3.555  0.64 20.60 ?  44  LYS   A HG2  1 
ATOM   1127 H  HG2  B LYS   A 1 44  ? 30.923 8.168   -3.582  0.36 20.30 ?  44  LYS   A HG2  1 
ATOM   1128 H  HG3  A LYS   A 1 44  ? 30.330 9.365   -4.265  0.64 20.60 ?  44  LYS   A HG3  1 
ATOM   1129 H  HG3  B LYS   A 1 44  ? 30.210 9.378   -4.331  0.36 20.30 ?  44  LYS   A HG3  1 
ATOM   1130 H  HD2  A LYS   A 1 44  ? 30.473 10.524  -2.210  0.64 26.40 ?  44  LYS   A HD2  1 
ATOM   1131 H  HD2  B LYS   A 1 44  ? 30.273 10.623  -2.341  0.36 24.17 ?  44  LYS   A HD2  1 
ATOM   1132 H  HD3  A LYS   A 1 44  ? 31.224 9.264   -1.588  0.64 26.40 ?  44  LYS   A HD3  1 
ATOM   1133 H  HD3  B LYS   A 1 44  ? 31.053 9.427   -1.632  0.36 24.17 ?  44  LYS   A HD3  1 
ATOM   1134 H  HE2  A LYS   A 1 44  ? 32.901 9.564   -3.268  0.64 29.86 ?  44  LYS   A HE2  1 
ATOM   1135 H  HE2  B LYS   A 1 44  ? 32.700 9.737   -3.419  0.36 26.62 ?  44  LYS   A HE2  1 
ATOM   1136 H  HE3  A LYS   A 1 44  ? 32.230 10.973  -3.573  0.64 29.86 ?  44  LYS   A HE3  1 
ATOM   1137 H  HE3  B LYS   A 1 44  ? 32.060 11.188  -3.532  0.36 26.62 ?  44  LYS   A HE3  1 
ATOM   1138 H  HZ1  A LYS   A 1 44  ? 33.957 11.213  -2.120  0.64 31.51 ?  44  LYS   A HZ1  1 
ATOM   1139 H  HZ1  B LYS   A 1 44  ? 33.840 11.213  -2.123  0.36 28.09 ?  44  LYS   A HZ1  1 
ATOM   1140 H  HZ2  A LYS   A 1 44  ? 32.733 11.594  -1.445  0.64 31.51 ?  44  LYS   A HZ2  1 
ATOM   1141 H  HZ2  B LYS   A 1 44  ? 32.650 11.541  -1.365  0.36 28.09 ?  44  LYS   A HZ2  1 
ATOM   1142 H  HZ3  A LYS   A 1 44  ? 33.344 10.310  -1.167  0.64 31.51 ?  44  LYS   A HZ3  1 
ATOM   1143 H  HZ3  B LYS   A 1 44  ? 33.234 10.219  -1.261  0.36 28.09 ?  44  LYS   A HZ3  1 
ATOM   1144 N  N    . HIS   A 1 45  ? 27.281 7.997   0.117   1.00 10.30 ?  45  HIS   A N    1 
ATOM   1145 C  CA   . HIS   A 1 45  ? 26.041 7.660   0.812   1.00 10.20 ?  45  HIS   A CA   1 
ATOM   1146 C  C    . HIS   A 1 45  ? 25.026 8.790   0.643   1.00 11.12 ?  45  HIS   A C    1 
ATOM   1147 O  O    . HIS   A 1 45  ? 24.750 9.564   1.558   1.00 12.91 ?  45  HIS   A O    1 
ATOM   1148 C  CB   . HIS   A 1 45  ? 26.333 7.409   2.279   1.00 10.48 ?  45  HIS   A CB   1 
ATOM   1149 C  CG   . HIS   A 1 45  ? 27.449 6.443   2.514   1.00 10.03 ?  45  HIS   A CG   1 
ATOM   1150 N  ND1  . HIS   A 1 45  ? 27.442 5.154   2.019   1.00 10.67 ?  45  HIS   A ND1  1 
ATOM   1151 C  CD2  . HIS   A 1 45  ? 28.612 6.594   3.194   1.00 10.05 ?  45  HIS   A CD2  1 
ATOM   1152 C  CE1  . HIS   A 1 45  ? 28.561 4.556   2.394   1.00 10.21 ?  45  HIS   A CE1  1 
ATOM   1153 N  NE2  . HIS   A 1 45  ? 29.289 5.406   3.103   1.00 10.36 ?  45  HIS   A NE2  1 
ATOM   1154 H  H    A HIS   A 1 45  ? 27.826 8.465   0.589   0.64 12.48 ?  45  HIS   A H    1 
ATOM   1155 H  H    B HIS   A 1 45  ? 27.826 8.467   0.587   0.36 12.48 ?  45  HIS   A H    1 
ATOM   1156 H  HA   . HIS   A 1 45  ? 25.660 6.851   0.428   1.00 12.35 ?  45  HIS   A HA   1 
ATOM   1157 H  HB2  . HIS   A 1 45  ? 26.560 8.250   2.701   1.00 12.69 ?  45  HIS   A HB2  1 
ATOM   1158 H  HB3  . HIS   A 1 45  ? 25.528 7.044   2.698   1.00 12.69 ?  45  HIS   A HB3  1 
ATOM   1159 H  HD2  . HIS   A 1 45  ? 28.902 7.366   3.632   1.00 12.17 ?  45  HIS   A HD2  1 
ATOM   1160 H  HE1  . HIS   A 1 45  ? 28.793 3.677   2.205   1.00 12.37 ?  45  HIS   A HE1  1 
ATOM   1161 H  HE2  . HIS   A 1 45  ? 30.055 5.241   3.454   1.00 12.55 ?  45  HIS   A HE2  1 
ATOM   1162 N  N    A GLY   A 1 46  ? 24.409 8.832   -0.534  0.64 12.31 ?  46  GLY   A N    1 
ATOM   1163 N  N    B GLY   A 1 46  ? 24.486 8.894   -0.568  0.36 11.81 ?  46  GLY   A N    1 
ATOM   1164 C  CA   A GLY   A 1 46  ? 23.559 9.958   -0.876  0.64 12.94 ?  46  GLY   A CA   1 
ATOM   1165 C  CA   B GLY   A 1 46  ? 23.701 10.063  -0.926  0.36 12.20 ?  46  GLY   A CA   1 
ATOM   1166 C  C    A GLY   A 1 46  ? 22.078 9.787   -0.606  0.64 13.02 ?  46  GLY   A C    1 
ATOM   1167 C  C    B GLY   A 1 46  ? 22.225 9.983   -0.590  0.36 12.16 ?  46  GLY   A C    1 
ATOM   1168 O  O    A GLY   A 1 46  ? 21.405 10.744  -0.199  0.64 14.27 ?  46  GLY   A O    1 
ATOM   1169 O  O    B GLY   A 1 46  ? 21.592 11.008  -0.310  0.36 12.79 ?  46  GLY   A O    1 
ATOM   1170 H  H    A GLY   A 1 46  ? 24.462 8.228   -1.140  0.64 14.89 ?  46  GLY   A H    1 
ATOM   1171 H  H    B GLY   A 1 46  ? 24.552 8.308   -1.190  0.36 14.29 ?  46  GLY   A H    1 
ATOM   1172 H  HA2  A GLY   A 1 46  ? 23.848 10.735  -0.375  0.64 15.64 ?  46  GLY   A HA2  1 
ATOM   1173 H  HA2  B GLY   A 1 46  ? 24.072 10.842  -0.474  0.36 14.75 ?  46  GLY   A HA2  1 
ATOM   1174 H  HA3  A GLY   A 1 46  ? 23.667 10.154  -1.818  0.64 15.64 ?  46  GLY   A HA3  1 
ATOM   1175 H  HA3  B GLY   A 1 46  ? 23.772 10.211  -1.880  0.36 14.75 ?  46  GLY   A HA3  1 
ATOM   1176 N  N    A GLY   A 1 47  ? 21.551 8.586   -0.834  0.64 12.69 ?  47  GLY   A N    1 
ATOM   1177 N  N    B GLY   A 1 47  ? 21.660 8.782   -0.638  0.36 11.94 ?  47  GLY   A N    1 
ATOM   1178 C  CA   A GLY   A 1 47  ? 20.120 8.377   -0.788  0.64 12.49 ?  47  GLY   A CA   1 
ATOM   1179 C  CA   B GLY   A 1 47  ? 20.247 8.599   -0.393  0.36 12.20 ?  47  GLY   A CA   1 
ATOM   1180 C  C    A GLY   A 1 47  ? 19.793 6.957   -0.388  0.64 12.19 ?  47  GLY   A C    1 
ATOM   1181 C  C    B GLY   A 1 47  ? 19.934 7.151   -0.078  0.36 12.07 ?  47  GLY   A C    1 
ATOM   1182 O  O    A GLY   A 1 47  ? 20.683 6.133   -0.171  0.64 12.20 ?  47  GLY   A O    1 
ATOM   1183 O  O    B GLY   A 1 47  ? 20.832 6.322   0.084   0.36 12.07 ?  47  GLY   A O    1 
ATOM   1184 H  H    A GLY   A 1 47  ? 22.004 7.867   -1.002  0.64 15.35 ?  47  GLY   A H    1 
ATOM   1185 H  H    B GLY   A 1 47  ? 22.082 8.058   -0.819  0.36 14.45 ?  47  GLY   A H    1 
ATOM   1186 H  HA2  A GLY   A 1 47  ? 19.715 8.982   -0.149  0.64 15.10 ?  47  GLY   A HA2  1 
ATOM   1187 H  HA2  B GLY   A 1 47  ? 19.965 9.149   0.358   0.36 14.76 ?  47  GLY   A HA2  1 
ATOM   1188 H  HA3  A GLY   A 1 47  ? 19.733 8.535   -1.661  0.64 15.10 ?  47  GLY   A HA3  1 
ATOM   1189 H  HA3  B GLY   A 1 47  ? 19.742 8.872   -1.178  0.36 14.76 ?  47  GLY   A HA3  1 
ATOM   1190 N  N    A GLY   A 1 48  ? 18.496 6.668   -0.312  0.64 12.16 ?  48  GLY   A N    1 
ATOM   1191 N  N    B GLY   A 1 48  ? 18.639 6.854   0.020   0.36 12.53 ?  48  GLY   A N    1 
ATOM   1192 C  CA   A GLY   A 1 48  ? 18.070 5.364   0.137   0.64 12.43 ?  48  GLY   A CA   1 
ATOM   1193 C  CA   B GLY   A 1 48  ? 18.224 5.497   0.319   0.36 12.66 ?  48  GLY   A CA   1 
ATOM   1194 C  C    A GLY   A 1 48  ? 18.581 5.090   1.536   0.64 11.77 ?  48  GLY   A C    1 
ATOM   1195 C  C    B GLY   A 1 48  ? 18.688 5.061   1.697   0.36 12.20 ?  48  GLY   A C    1 
ATOM   1196 O  O    A GLY   A 1 48  ? 18.783 6.005   2.347   0.64 12.11 ?  48  GLY   A O    1 
ATOM   1197 O  O    B GLY   A 1 48  ? 18.771 5.855   2.643   0.36 12.47 ?  48  GLY   A O    1 
ATOM   1198 H  H    A GLY   A 1 48  ? 17.848 7.207   -0.498  0.64 14.71 ?  48  GLY   A H    1 
ATOM   1199 H  H    B GLY   A 1 48  ? 17.992 7.414   -0.069  0.36 15.15 ?  48  GLY   A H    1 
ATOM   1200 H  HA2  A GLY   A 1 48  ? 17.102 5.302   0.143   0.64 15.03 ?  48  GLY   A HA2  1 
ATOM   1201 H  HA2  B GLY   A 1 48  ? 17.257 5.431   0.275   0.36 15.31 ?  48  GLY   A HA2  1 
ATOM   1202 H  HA3  A GLY   A 1 48  ? 18.424 4.679   -0.451  0.64 15.03 ?  48  GLY   A HA3  1 
ATOM   1203 H  HA3  B GLY   A 1 48  ? 18.605 4.887   -0.334  0.36 15.31 ?  48  GLY   A HA3  1 
ATOM   1204 N  N    A VAL   A 1 49  ? 18.801 3.807   1.822   0.64 11.29 ?  49  VAL   A N    1 
ATOM   1205 N  N    B VAL   A 1 49  ? 18.994 3.767   1.813   0.36 11.68 ?  49  VAL   A N    1 
ATOM   1206 C  CA   A VAL   A 1 49  ? 19.315 3.402   3.126   0.64 11.52 ?  49  VAL   A CA   1 
ATOM   1207 C  CA   B VAL   A 1 49  ? 19.538 3.234   3.059   0.36 10.73 ?  49  VAL   A CA   1 
ATOM   1208 C  C    A VAL   A 1 49  ? 20.632 4.107   3.435   0.64 10.32 ?  49  VAL   A C    1 
ATOM   1209 C  C    B VAL   A 1 49  ? 20.809 3.978   3.446   0.36 9.70  ?  49  VAL   A C    1 
ATOM   1210 O  O    A VAL   A 1 49  ? 20.843 4.582   4.554   0.64 10.67 ?  49  VAL   A O    1 
ATOM   1211 O  O    B VAL   A 1 49  ? 21.004 4.340   4.610   0.36 9.62  ?  49  VAL   A O    1 
ATOM   1212 C  CB   A VAL   A 1 49  ? 19.451 1.868   3.184   0.64 12.30 ?  49  VAL   A CB   1 
ATOM   1213 C  CB   B VAL   A 1 49  ? 19.795 1.722   2.929   0.36 10.41 ?  49  VAL   A CB   1 
ATOM   1214 C  CG1  A VAL   A 1 49  ? 20.252 1.432   4.405   0.64 12.44 ?  49  VAL   A CG1  1 
ATOM   1215 C  CG1  B VAL   A 1 49  ? 20.650 1.229   4.094   0.36 9.83  ?  49  VAL   A CG1  1 
ATOM   1216 C  CG2  A VAL   A 1 49  ? 18.070 1.214   3.188   0.64 13.63 ?  49  VAL   A CG2  1 
ATOM   1217 C  CG2  B VAL   A 1 49  ? 18.480 0.954   2.856   0.36 10.84 ?  49  VAL   A CG2  1 
ATOM   1218 H  H    A VAL   A 1 49  ? 18.666 3.150   1.283   0.64 13.66 ?  49  VAL   A H    1 
ATOM   1219 H  H    B VAL   A 1 49  ? 18.906 3.185   1.188   0.36 14.13 ?  49  VAL   A H    1 
ATOM   1220 H  HA   A VAL   A 1 49  ? 18.685 3.661   3.811   0.64 13.95 ?  49  VAL   A HA   1 
ATOM   1221 H  HA   B VAL   A 1 49  ? 18.891 3.365   3.771   0.36 12.99 ?  49  VAL   A HA   1 
ATOM   1222 H  HB   A VAL   A 1 49  ? 19.925 1.558   2.396   0.64 14.88 ?  49  VAL   A HB   1 
ATOM   1223 H  HB   B VAL   A 1 49  ? 20.285 1.556   2.111   0.36 12.61 ?  49  VAL   A HB   1 
ATOM   1224 H  HG11 A VAL   A 1 49  ? 20.093 0.490   4.564   0.64 15.04 ?  49  VAL   A HG11 1 
ATOM   1225 H  HG11 B VAL   A 1 49  ? 20.552 0.268   4.172   0.36 11.92 ?  49  VAL   A HG11 1 
ATOM   1226 H  HG12 A VAL   A 1 49  ? 21.193 1.587   4.238   0.64 15.04 ?  49  VAL   A HG12 1 
ATOM   1227 H  HG12 B VAL   A 1 49  ? 21.581 1.451   3.924   0.36 11.92 ?  49  VAL   A HG12 1 
ATOM   1228 H  HG13 A VAL   A 1 49  ? 19.958 1.951   5.171   0.64 15.04 ?  49  VAL   A HG13 1 
ATOM   1229 H  HG13 B VAL   A 1 49  ? 20.351 1.658   4.912   0.36 11.92 ?  49  VAL   A HG13 1 
ATOM   1230 H  HG21 A VAL   A 1 49  ? 18.175 0.251   3.223   0.64 16.47 ?  49  VAL   A HG21 1 
ATOM   1231 H  HG21 B VAL   A 1 49  ? 18.671 0.014   2.717   0.36 13.13 ?  49  VAL   A HG21 1 
ATOM   1232 H  HG22 A VAL   A 1 49  ? 17.580 1.522   3.967   0.64 16.47 ?  49  VAL   A HG22 1 
ATOM   1233 H  HG22 B VAL   A 1 49  ? 17.998 1.075   3.690   0.36 13.13 ?  49  VAL   A HG22 1 
ATOM   1234 H  HG23 A VAL   A 1 49  ? 17.601 1.469   2.379   0.64 16.47 ?  49  VAL   A HG23 1 
ATOM   1235 H  HG23 B VAL   A 1 49  ? 17.956 1.300   2.118   0.36 13.13 ?  49  VAL   A HG23 1 
ATOM   1236 N  N    A ALA   A 1 50  ? 21.543 4.159   2.457   0.64 9.87  ?  50  ALA   A N    1 
ATOM   1237 N  N    B ALA   A 1 50  ? 21.711 4.174   2.481   0.36 9.25  ?  50  ALA   A N    1 
ATOM   1238 C  CA   A ALA   A 1 50  ? 22.871 4.717   2.704   0.64 9.69  ?  50  ALA   A CA   1 
ATOM   1239 C  CA   B ALA   A 1 50  ? 23.005 4.774   2.788   0.36 9.15  ?  50  ALA   A CA   1 
ATOM   1240 C  C    A ALA   A 1 50  ? 22.791 6.173   3.132   0.64 10.09 ?  50  ALA   A C    1 
ATOM   1241 C  C    B ALA   A 1 50  ? 22.851 6.228   3.212   0.36 9.01  ?  50  ALA   A C    1 
ATOM   1242 O  O    A ALA   A 1 50  ? 23.457 6.589   4.087   0.64 10.45 ?  50  ALA   A O    1 
ATOM   1243 O  O    B ALA   A 1 50  ? 23.436 6.659   4.214   0.36 8.74  ?  50  ALA   A O    1 
ATOM   1244 C  CB   A ALA   A 1 50  ? 23.730 4.592   1.448   0.64 9.79  ?  50  ALA   A CB   1 
ATOM   1245 C  CB   B ALA   A 1 50  ? 23.932 4.656   1.578   0.36 9.60  ?  50  ALA   A CB   1 
ATOM   1246 H  H    A ALA   A 1 50  ? 21.419 3.883   1.651   0.64 11.96 ?  50  ALA   A H    1 
ATOM   1247 H  H    B ALA   A 1 50  ? 21.593 3.967   1.653   0.36 11.21 ?  50  ALA   A H    1 
ATOM   1248 H  HA   A ALA   A 1 50  ? 23.300 4.222   3.418   0.64 11.74 ?  50  ALA   A HA   1 
ATOM   1249 H  HA   B ALA   A 1 50  ? 23.408 4.293   3.522   0.36 11.10 ?  50  ALA   A HA   1 
ATOM   1250 H  HB1  A ALA   A 1 50  ? 24.608 4.971   1.628   0.64 11.87 ?  50  ALA   A HB1  1 
ATOM   1251 H  HB1  B ALA   A 1 50  ? 24.790 5.052   1.798   0.36 11.63 ?  50  ALA   A HB1  1 
ATOM   1252 H  HB2  A ALA   A 1 50  ? 23.815 3.659   1.213   0.64 11.87 ?  50  ALA   A HB2  1 
ATOM   1253 H  HB2  B ALA   A 1 50  ? 24.049 3.718   1.357   0.36 11.63 ?  50  ALA   A HB2  1 
ATOM   1254 H  HB3  A ALA   A 1 50  ? 23.305 5.083   0.725   0.64 11.87 ?  50  ALA   A HB3  1 
ATOM   1255 H  HB3  B ALA   A 1 50  ? 23.536 5.125   0.825   0.36 11.63 ?  50  ALA   A HB3  1 
ATOM   1256 N  N    A GLY   A 1 51  ? 22.003 6.974   2.418   0.64 10.34 ?  51  GLY   A N    1 
ATOM   1257 N  N    B GLY   A 1 51  ? 22.065 6.999   2.462   0.36 9.70  ?  51  GLY   A N    1 
ATOM   1258 C  CA   A GLY   A 1 51  ? 21.852 8.363   2.808   0.64 10.57 ?  51  GLY   A CA   1 
ATOM   1259 C  CA   B GLY   A 1 51  ? 21.861 8.388   2.829   0.36 10.23 ?  51  GLY   A CA   1 
ATOM   1260 C  C    A GLY   A 1 51  ? 21.264 8.501   4.198   0.64 10.60 ?  51  GLY   A C    1 
ATOM   1261 C  C    B GLY   A 1 51  ? 21.233 8.532   4.199   0.36 10.56 ?  51  GLY   A C    1 
ATOM   1262 O  O    A GLY   A 1 51  ? 21.672 9.373   4.970   0.64 11.47 ?  51  GLY   A O    1 
ATOM   1263 O  O    B GLY   A 1 51  ? 21.583 9.437   4.961   0.36 11.02 ?  51  GLY   A O    1 
ATOM   1264 H  H    A GLY   A 1 51  ? 21.565 6.741   1.713   0.64 12.53 ?  51  GLY   A H    1 
ATOM   1265 H  H    B GLY   A 1 51  ? 21.647 6.744   1.752   0.36 11.75 ?  51  GLY   A H    1 
ATOM   1266 H  HA2  A GLY   A 1 51  ? 22.715 8.801   2.791   0.64 12.80 ?  51  GLY   A HA2  1 
ATOM   1267 H  HA2  B GLY   A 1 51  ? 22.712 8.850   2.828   0.36 12.39 ?  51  GLY   A HA2  1 
ATOM   1268 H  HA3  A GLY   A 1 51  ? 21.264 8.813   2.178   0.64 12.80 ?  51  GLY   A HA3  1 
ATOM   1269 H  HA3  B GLY   A 1 51  ? 21.277 8.812   2.181   0.36 12.39 ?  51  GLY   A HA3  1 
ATOM   1270 N  N    . ALA   A 1 52  ? 20.289 7.645   4.530   1.00 10.70 ?  52  ALA   A N    1 
ATOM   1271 C  CA   . ALA   A 1 52  ? 19.643 7.704   5.838   1.00 11.40 ?  52  ALA   A CA   1 
ATOM   1272 C  C    . ALA   A 1 52  ? 20.599 7.296   6.961   1.00 10.77 ?  52  ALA   A C    1 
ATOM   1273 O  O    . ALA   A 1 52  ? 20.678 7.967   7.996   1.00 11.89 ?  52  ALA   A O    1 
ATOM   1274 C  CB   . ALA   A 1 52  ? 18.383 6.837   5.834   1.00 12.97 ?  52  ALA   A CB   1 
ATOM   1275 H  H    A ALA   A 1 52  ? 19.999 7.013   4.019   0.64 12.96 ?  52  ALA   A H    1 
ATOM   1276 H  H    B ALA   A 1 52  ? 20.019 7.001   4.023   0.36 12.96 ?  52  ALA   A H    1 
ATOM   1277 H  HA   . ALA   A 1 52  ? 19.370 8.614   6.003   1.00 13.80 ?  52  ALA   A HA   1 
ATOM   1278 H  HB1  . ALA   A 1 52  ? 17.955 6.900   6.704   1.00 15.68 ?  52  ALA   A HB1  1 
ATOM   1279 H  HB2  . ALA   A 1 52  ? 17.779 7.163   5.148   1.00 15.68 ?  52  ALA   A HB2  1 
ATOM   1280 H  HB3  . ALA   A 1 52  ? 18.627 5.918   5.651   1.00 15.68 ?  52  ALA   A HB3  1 
ATOM   1281 N  N    A LEU   A 1 53  ? 21.333 6.195   6.784   0.64 10.68 ?  53  LEU   A N    1 
ATOM   1282 N  N    B LEU   A 1 53  ? 21.322 6.186   6.780   0.36 10.44 ?  53  LEU   A N    1 
ATOM   1283 C  CA   A LEU   A 1 53  ? 22.298 5.799   7.807   0.64 10.76 ?  53  LEU   A CA   1 
ATOM   1284 C  CA   B LEU   A 1 53  ? 22.306 5.776   7.780   0.36 10.31 ?  53  LEU   A CA   1 
ATOM   1285 C  C    A LEU   A 1 53  ? 23.352 6.882   7.998   0.64 10.14 ?  53  LEU   A C    1 
ATOM   1286 C  C    B LEU   A 1 53  ? 23.342 6.872   7.991   0.36 10.10 ?  53  LEU   A C    1 
ATOM   1287 O  O    A LEU   A 1 53  ? 23.686 7.249   9.129   0.64 11.29 ?  53  LEU   A O    1 
ATOM   1288 O  O    B LEU   A 1 53  ? 23.650 7.243   9.128   0.36 10.88 ?  53  LEU   A O    1 
ATOM   1289 C  CB   A LEU   A 1 53  ? 22.959 4.466   7.438   0.64 11.56 ?  53  LEU   A CB   1 
ATOM   1290 C  CB   B LEU   A 1 53  ? 22.996 4.473   7.353   0.36 10.26 ?  53  LEU   A CB   1 
ATOM   1291 C  CG   A LEU   A 1 53  ? 22.033 3.243   7.441   0.64 12.34 ?  53  LEU   A CG   1 
ATOM   1292 C  CG   B LEU   A 1 53  ? 22.274 3.129   7.514   0.36 10.11 ?  53  LEU   A CG   1 
ATOM   1293 C  CD1  A LEU   A 1 53  ? 22.751 2.026   6.889   0.64 12.42 ?  53  LEU   A CD1  1 
ATOM   1294 C  CD1  B LEU   A 1 53  ? 23.098 2.026   6.865   0.36 10.60 ?  53  LEU   A CD1  1 
ATOM   1295 C  CD2  A LEU   A 1 53  ? 21.507 2.958   8.839   0.64 12.91 ?  53  LEU   A CD2  1 
ATOM   1296 C  CD2  B LEU   A 1 53  ? 22.016 2.797   8.976   0.36 9.73  ?  53  LEU   A CD2  1 
ATOM   1297 H  H    A LEU   A 1 53  ? 21.284 5.666   6.103   0.64 12.93 ?  53  LEU   A H    1 
ATOM   1298 H  H    B LEU   A 1 53  ? 21.263 5.662   6.098   0.36 12.65 ?  53  LEU   A H    1 
ATOM   1299 H  HA   A LEU   A 1 53  ? 21.835 5.678   8.649   0.64 13.03 ?  53  LEU   A HA   1 
ATOM   1300 H  HA   B LEU   A 1 53  ? 21.857 5.615   8.625   0.36 12.49 ?  53  LEU   A HA   1 
ATOM   1301 H  HB2  A LEU   A 1 53  ? 23.334 4.541   6.546   0.64 13.99 ?  53  LEU   A HB2  1 
ATOM   1302 H  HB2  B LEU   A 1 53  ? 23.211 4.550   6.411   0.36 12.43 ?  53  LEU   A HB2  1 
ATOM   1303 H  HB3  A LEU   A 1 53  ? 23.672 4.287   8.072   0.64 13.99 ?  53  LEU   A HB3  1 
ATOM   1304 H  HB3  B LEU   A 1 53  ? 23.819 4.397   7.857   0.36 12.43 ?  53  LEU   A HB3  1 
ATOM   1305 H  HG   A LEU   A 1 53  ? 21.273 3.425   6.865   0.64 14.93 ?  53  LEU   A HG   1 
ATOM   1306 H  HG   B LEU   A 1 53  ? 21.418 3.165   7.058   0.36 12.25 ?  53  LEU   A HG   1 
ATOM   1307 H  HD11 A LEU   A 1 53  ? 22.144 1.271   6.901   0.64 15.02 ?  53  LEU   A HD11 1 
ATOM   1308 H  HD11 B LEU   A 1 53  ? 22.636 1.179   6.975   0.36 12.84 ?  53  LEU   A HD11 1 
ATOM   1309 H  HD12 A LEU   A 1 53  ? 23.034 2.213   5.981   0.64 15.02 ?  53  LEU   A HD12 1 
ATOM   1310 H  HD12 B LEU   A 1 53  ? 23.202 2.224   5.922   0.36 12.84 ?  53  LEU   A HD12 1 
ATOM   1311 H  HD13 A LEU   A 1 53  ? 23.524 1.841   7.445   0.64 15.02 ?  53  LEU   A HD13 1 
ATOM   1312 H  HD13 B LEU   A 1 53  ? 23.966 1.987   7.294   0.36 12.84 ?  53  LEU   A HD13 1 
ATOM   1313 H  HD21 A LEU   A 1 53  ? 20.998 2.135   8.823   0.64 15.61 ?  53  LEU   A HD21 1 
ATOM   1314 H  HD21 B LEU   A 1 53  ? 21.499 1.978   9.031   0.36 11.79 ?  53  LEU   A HD21 1 
ATOM   1315 H  HD22 A LEU   A 1 53  ? 22.257 2.875   9.446   0.64 15.61 ?  53  LEU   A HD22 1 
ATOM   1316 H  HD22 B LEU   A 1 53  ? 22.866 2.683   9.429   0.36 11.79 ?  53  LEU   A HD22 1 
ATOM   1317 H  HD23 A LEU   A 1 53  ? 20.936 3.693   9.118   0.64 15.61 ?  53  LEU   A HD23 1 
ATOM   1318 H  HD23 B LEU   A 1 53  ? 21.521 3.527   9.382   0.36 11.79 ?  53  LEU   A HD23 1 
ATOM   1319 N  N    . ASN   A 1 54  ? 23.886 7.408   6.898   1.00 10.02 ?  54  ASN   A N    1 
ATOM   1320 C  CA   . ASN   A 1 54  ? 24.929 8.413   7.025   1.00 10.30 ?  54  ASN   A CA   1 
ATOM   1321 C  C    . ASN   A 1 54  ? 24.413 9.660   7.743   1.00 10.45 ?  54  ASN   A C    1 
ATOM   1322 O  O    . ASN   A 1 54  ? 25.104 10.218  8.606   1.00 10.94 ?  54  ASN   A O    1 
ATOM   1323 C  CB   . ASN   A 1 54  ? 25.489 8.775   5.659   1.00 10.49 ?  54  ASN   A CB   1 
ATOM   1324 C  CG   . ASN   A 1 54  ? 26.510 9.872   5.762   1.00 10.57 ?  54  ASN   A CG   1 
ATOM   1325 O  OD1  . ASN   A 1 54  ? 27.521 9.729   6.461   1.00 10.51 ?  54  ASN   A OD1  1 
ATOM   1326 N  ND2  . ASN   A 1 54  ? 26.251 10.987  5.103   1.00 11.31 ?  54  ASN   A ND2  1 
ATOM   1327 H  H    A ASN   A 1 54  ? 23.667 7.200   6.094   0.64 12.14 ?  54  ASN   A H    1 
ATOM   1328 H  H    B ASN   A 1 54  ? 23.663 7.210   6.093   0.36 12.14 ?  54  ASN   A H    1 
ATOM   1329 H  HA   . ASN   A 1 54  ? 25.649 8.046   7.556   1.00 12.47 ?  54  ASN   A HA   1 
ATOM   1330 H  HB2  . ASN   A 1 54  ? 25.921 7.988   5.278   1.00 12.71 ?  54  ASN   A HB2  1 
ATOM   1331 H  HB3  . ASN   A 1 54  ? 24.770 9.071   5.084   1.00 12.71 ?  54  ASN   A HB3  1 
ATOM   1332 H  HD21 . ASN   A 1 54  ? 26.798 11.646  5.139   1.00 13.68 ?  54  ASN   A HD21 1 
ATOM   1333 H  HD22 . ASN   A 1 54  ? 25.528 11.054  4.636   1.00 13.68 ?  54  ASN   A HD22 1 
ATOM   1334 N  N    . LYS   A 1 55  ? 23.200 10.111  7.402   1.00 10.65 ?  55  LYS   A N    1 
ATOM   1335 C  CA   . LYS   A 1 55  ? 22.619 11.271  8.069   1.00 11.71 ?  55  LYS   A CA   1 
ATOM   1336 C  C    . LYS   A 1 55  ? 22.531 11.040  9.572   1.00 11.72 ?  55  LYS   A C    1 
ATOM   1337 O  O    . LYS   A 1 55  ? 22.809 11.945  10.368  1.00 12.40 ?  55  LYS   A O    1 
ATOM   1338 C  CB   . LYS   A 1 55  ? 21.244 11.563  7.461   1.00 12.55 ?  55  LYS   A CB   1 
ATOM   1339 C  CG   . LYS   A 1 55  ? 20.495 12.728  8.078   1.00 14.02 ?  55  LYS   A CG   1 
ATOM   1340 C  CD   . LYS   A 1 55  ? 19.167 12.948  7.352   1.00 15.76 ?  55  LYS   A CD   1 
ATOM   1341 C  CE   . LYS   A 1 55  ? 18.308 14.013  8.021   1.00 17.52 ?  55  LYS   A CE   1 
ATOM   1342 N  NZ   . LYS   A 1 55  ? 16.970 14.141  7.366   1.00 18.54 ?  55  LYS   A NZ   1 
ATOM   1343 H  H    . LYS   A 1 55  ? 22.694 9.757   6.796   1.00 12.89 ?  55  LYS   A H    1 
ATOM   1344 H  HA   . LYS   A 1 55  ? 23.183 12.041  7.913   1.00 14.17 ?  55  LYS   A HA   1 
ATOM   1345 H  HB2  . LYS   A 1 55  ? 21.357 11.763  6.519   1.00 15.18 ?  55  LYS   A HB2  1 
ATOM   1346 H  HB3  . LYS   A 1 55  ? 20.685 10.777  7.561   1.00 15.18 ?  55  LYS   A HB3  1 
ATOM   1347 H  HG2  . LYS   A 1 55  ? 20.299 12.536  9.009   1.00 16.94 ?  55  LYS   A HG2  1 
ATOM   1348 H  HG3  . LYS   A 1 55  ? 21.022 13.535  8.000   1.00 16.94 ?  55  LYS   A HG3  1 
ATOM   1349 H  HD2  . LYS   A 1 55  ? 19.349 13.233  6.441   1.00 19.03 ?  55  LYS   A HD2  1 
ATOM   1350 H  HD3  . LYS   A 1 55  ? 18.668 12.115  7.344   1.00 19.03 ?  55  LYS   A HD3  1 
ATOM   1351 H  HE2  . LYS   A 1 55  ? 18.168 13.771  8.950   1.00 21.14 ?  55  LYS   A HE2  1 
ATOM   1352 H  HE3  . LYS   A 1 55  ? 18.759 14.869  7.962   1.00 21.14 ?  55  LYS   A HE3  1 
ATOM   1353 H  HZ1  . LYS   A 1 55  ? 16.419 14.611  7.885   1.00 22.37 ?  55  LYS   A HZ1  1 
ATOM   1354 H  HZ2  . LYS   A 1 55  ? 17.050 14.560  6.583   1.00 22.37 ?  55  LYS   A HZ2  1 
ATOM   1355 H  HZ3  . LYS   A 1 55  ? 16.616 13.336  7.227   1.00 22.37 ?  55  LYS   A HZ3  1 
ATOM   1356 N  N    . ALA   A 1 56  ? 22.144 9.828   9.980   1.00 11.87 ?  56  ALA   A N    1 
ATOM   1357 C  CA   . ALA   A 1 56  ? 22.020 9.506   11.395  1.00 12.58 ?  56  ALA   A CA   1 
ATOM   1358 C  C    . ALA   A 1 56  ? 23.358 9.534   12.123  1.00 12.59 ?  56  ALA   A C    1 
ATOM   1359 O  O    . ALA   A 1 56  ? 23.374 9.719   13.341  1.00 13.72 ?  56  ALA   A O    1 
ATOM   1360 C  CB   . ALA   A 1 56  ? 21.327 8.151   11.579  1.00 13.44 ?  56  ALA   A CB   1 
ATOM   1361 H  H    . ALA   A 1 56  ? 21.954 9.177   9.450   1.00 14.36 ?  56  ALA   A H    1 
ATOM   1362 H  HA   . ALA   A 1 56  ? 21.456 10.167  11.811  1.00 15.21 ?  56  ALA   A HA   1 
ATOM   1363 H  HB1  . ALA   A 1 56  ? 21.254 7.956   12.529  1.00 16.24 ?  56  ALA   A HB1  1 
ATOM   1364 H  HB2  . ALA   A 1 56  ? 20.441 8.192   11.185  1.00 16.24 ?  56  ALA   A HB2  1 
ATOM   1365 H  HB3  . ALA   A 1 56  ? 21.850 7.459   11.143  1.00 16.24 ?  56  ALA   A HB3  1 
ATOM   1366 N  N    . THR   A 1 57  ? 24.471 9.343   11.408  1.00 11.71 ?  57  THR   A N    1 
ATOM   1367 C  CA   . THR   A 1 57  ? 25.811 9.476   11.986  1.00 11.68 ?  57  THR   A CA   1 
ATOM   1368 C  C    . THR   A 1 57  ? 26.366 10.895  11.899  1.00 12.07 ?  57  THR   A C    1 
ATOM   1369 O  O    . THR   A 1 57  ? 27.555 11.103  12.186  1.00 12.50 ?  57  THR   A O    1 
ATOM   1370 C  CB   . THR   A 1 57  ? 26.828 8.524   11.324  1.00 11.55 ?  57  THR   A CB   1 
ATOM   1371 O  OG1  . THR   A 1 57  ? 27.206 9.013   10.023  1.00 11.36 ?  57  THR   A OG1  1 
ATOM   1372 C  CG2  . THR   A 1 57  ? 26.294 7.107   11.224  1.00 11.56 ?  57  THR   A CG2  1 
ATOM   1373 H  H    . THR   A 1 57  ? 24.478 9.107   10.580  1.00 14.17 ?  57  THR   A H    1 
ATOM   1374 H  HA   . THR   A 1 57  ? 25.763 9.225   12.927  1.00 14.13 ?  57  THR   A HA   1 
ATOM   1375 H  HB   . THR   A 1 57  ? 27.624 8.487   11.883  1.00 13.97 ?  57  THR   A HB   1 
ATOM   1376 H  HG1  . THR   A 1 57  ? 26.524 9.070   9.536   1.00 13.74 ?  57  THR   A HG1  1 
ATOM   1377 H  HG21 . THR   A 1 57  ? 26.982 6.507   10.891  1.00 13.99 ?  57  THR   A HG21 1 
ATOM   1378 H  HG22 . THR   A 1 57  ? 26.005 6.791   12.098  1.00 13.99 ?  57  THR   A HG22 1 
ATOM   1379 H  HG23 . THR   A 1 57  ? 25.536 7.074   10.619  1.00 13.99 ?  57  THR   A HG23 1 
ATOM   1380 N  N    . ASN   A 1 58  ? 25.550 11.869  11.496  1.00 12.65 ?  58  ASN   A N    1 
ATOM   1381 C  CA   . ASN   A 1 58  ? 26.020 13.248  11.399  1.00 13.59 ?  58  ASN   A CA   1 
ATOM   1382 C  C    . ASN   A 1 58  ? 27.171 13.368  10.392  1.00 12.46 ?  58  ASN   A C    1 
ATOM   1383 O  O    . ASN   A 1 58  ? 28.067 14.201  10.545  1.00 12.97 ?  58  ASN   A O    1 
ATOM   1384 C  CB   . ASN   A 1 58  ? 26.400 13.774  12.797  1.00 16.02 ?  58  ASN   A CB   1 
ATOM   1385 C  CG   . ASN   A 1 58  ? 26.835 15.223  12.801  1.00 19.65 ?  58  ASN   A CG   1 
ATOM   1386 O  OD1  . ASN   A 1 58  ? 26.214 16.060  12.158  1.00 21.45 ?  58  ASN   A OD1  1 
ATOM   1387 N  ND2  . ASN   A 1 58  ? 27.905 15.530  13.543  1.00 20.81 ?  58  ASN   A ND2  1 
ATOM   1388 H  H    . ASN   A 1 58  ? 24.727 11.749  11.266  1.00 15.30 ?  58  ASN   A H    1 
ATOM   1389 H  HA   . ASN   A 1 58  ? 25.289 13.789  11.075  1.00 16.42 ?  58  ASN   A HA   1 
ATOM   1390 H  HB2  . ASN   A 1 58  ? 25.626 13.692  13.386  1.00 19.34 ?  58  ASN   A HB2  1 
ATOM   1391 H  HB3  . ASN   A 1 58  ? 27.132 13.250  13.153  1.00 19.34 ?  58  ASN   A HB3  1 
ATOM   1392 H  HD21 . ASN   A 1 58  ? 28.186 16.344  13.581  1.00 25.08 ?  58  ASN   A HD21 1 
ATOM   1393 H  HD22 . ASN   A 1 58  ? 28.310 14.915  13.982  1.00 25.08 ?  58  ASN   A HD22 1 
ATOM   1394 N  N    . ASN   A 1 59  ? 27.151 12.544  9.342   1.00 11.50 ?  59  ASN   A N    1 
ATOM   1395 C  CA   . ASN   A 1 59  ? 28.132 12.517  8.246   1.00 11.11 ?  59  ASN   A CA   1 
ATOM   1396 C  C    . ASN   A 1 59  ? 29.449 11.840  8.636   1.00 11.06 ?  59  ASN   A C    1 
ATOM   1397 O  O    . ASN   A 1 59  ? 30.371 11.792  7.812   1.00 11.04 ?  59  ASN   A O    1 
ATOM   1398 C  CB   . ASN   A 1 59  ? 28.421 13.904  7.637   1.00 11.42 ?  59  ASN   A CB   1 
ATOM   1399 C  CG   . ASN   A 1 59  ? 28.784 13.834  6.169   1.00 11.71 ?  59  ASN   A CG   1 
ATOM   1400 O  OD1  . ASN   A 1 59  ? 28.074 13.215  5.372   1.00 11.88 ?  59  ASN   A OD1  1 
ATOM   1401 N  ND2  . ASN   A 1 59  ? 29.883 14.492  5.794   1.00 12.51 ?  59  ASN   A ND2  1 
ATOM   1402 H  H    . ASN   A 1 59  ? 26.538 11.949  9.234   1.00 13.91 ?  59  ASN   A H    1 
ATOM   1403 H  HA   . ASN   A 1 59  ? 27.752 11.984  7.535   1.00 13.45 ?  59  ASN   A HA   1 
ATOM   1404 H  HB2  . ASN   A 1 59  ? 27.634 14.463  7.720   1.00 13.82 ?  59  ASN   A HB2  1 
ATOM   1405 H  HB3  . ASN   A 1 59  ? 29.168 14.311  8.106   1.00 13.82 ?  59  ASN   A HB3  1 
ATOM   1406 H  HD21 . ASN   A 1 59  ? 30.134 14.485  4.968   1.00 15.13 ?  59  ASN   A HD21 1 
ATOM   1407 H  HD22 . ASN   A 1 59  ? 30.358 14.914  6.377   1.00 15.13 ?  59  ASN   A HD22 1 
ATOM   1408 N  N    . ALA   A 1 60  ? 29.568 11.296  9.846   1.00 10.93 ?  60  ALA   A N    1 
ATOM   1409 C  CA   . ALA   A 1 60  ? 30.802 10.608  10.209  1.00 11.26 ?  60  ALA   A CA   1 
ATOM   1410 C  C    . ALA   A 1 60  ? 31.027 9.372   9.345   1.00 11.12 ?  60  ALA   A C    1 
ATOM   1411 O  O    . ALA   A 1 60  ? 32.172 9.043   9.017   1.00 11.50 ?  60  ALA   A O    1 
ATOM   1412 C  CB   . ALA   A 1 60  ? 30.795 10.252  11.692  1.00 12.01 ?  60  ALA   A CB   1 
ATOM   1413 H  H    . ALA   A 1 60  ? 28.963 11.301  10.459  1.00 13.23 ?  60  ALA   A H    1 
ATOM   1414 H  HA   . ALA   A 1 60  ? 31.548 11.214  10.056  1.00 13.63 ?  60  ALA   A HA   1 
ATOM   1415 H  HB1  . ALA   A 1 60  ? 31.625 9.802   11.913  1.00 14.53 ?  60  ALA   A HB1  1 
ATOM   1416 H  HB2  . ALA   A 1 60  ? 30.716 11.071  12.212  1.00 14.53 ?  60  ALA   A HB2  1 
ATOM   1417 H  HB3  . ALA   A 1 60  ? 30.042 9.672   11.874  1.00 14.53 ?  60  ALA   A HB3  1 
ATOM   1418 N  N    . MET   A 1 61  ? 29.955 8.681   8.961   1.00 10.45 ?  61  MET   A N    1 
ATOM   1419 C  CA   . MET   A 1 61  ? 30.094 7.544   8.058   1.00 10.45 ?  61  MET   A CA   1 
ATOM   1420 C  C    . MET   A 1 61  ? 30.729 7.965   6.735   1.00 10.56 ?  61  MET   A C    1 
ATOM   1421 O  O    . MET   A 1 61  ? 31.626 7.279   6.223   1.00 11.03 ?  61  MET   A O    1 
ATOM   1422 C  CB   . MET   A 1 61  ? 28.732 6.885   7.842   1.00 10.28 ?  61  MET   A CB   1 
ATOM   1423 C  CG   . MET   A 1 61  ? 28.743 5.715   6.873   1.00 10.87 ?  61  MET   A CG   1 
ATOM   1424 S  SD   . MET   A 1 61  ? 27.118 4.959   6.662   1.00 12.05 ?  61  MET   A SD   1 
ATOM   1425 C  CE   . MET   A 1 61  ? 26.987 4.068   8.219   1.00 13.47 ?  61  MET   A CE   1 
ATOM   1426 H  H    . MET   A 1 61  ? 29.146 8.854   9.196   1.00 12.66 ?  61  MET   A H    1 
ATOM   1427 H  HA   . MET   A 1 61  ? 30.671 6.889   8.477   1.00 12.65 ?  61  MET   A HA   1 
ATOM   1428 H  HB2  . MET   A 1 61  ? 28.406 6.561   8.694   1.00 12.46 ?  61  MET   A HB2  1 
ATOM   1429 H  HB3  . MET   A 1 61  ? 28.118 7.550   7.489   1.00 12.46 ?  61  MET   A HB3  1 
ATOM   1430 H  HG2  . MET   A 1 61  ? 29.028 6.013   6.000   1.00 13.16 ?  61  MET   A HG2  1 
ATOM   1431 H  HG3  . MET   A 1 61  ? 29.338 5.027   7.206   1.00 13.16 ?  61  MET   A HG3  1 
ATOM   1432 H  HE1  . MET   A 1 61  ? 26.146 3.584   8.240   1.00 16.28 ?  61  MET   A HE1  1 
ATOM   1433 H  HE2  . MET   A 1 61  ? 27.728 3.442   8.287   1.00 16.28 ?  61  MET   A HE2  1 
ATOM   1434 H  HE3  . MET   A 1 61  ? 27.023 4.699   8.956   1.00 16.28 ?  61  MET   A HE3  1 
ATOM   1435 N  N    . GLN   A 1 62  ? 30.288 9.094   6.171   1.00 10.52 ?  62  GLN   A N    1 
ATOM   1436 C  CA   . GLN   A 1 62  ? 30.858 9.558   4.908   1.00 10.70 ?  62  GLN   A CA   1 
ATOM   1437 C  C    . GLN   A 1 62  ? 32.329 9.932   5.060   1.00 10.61 ?  62  GLN   A C    1 
ATOM   1438 O  O    . GLN   A 1 62  ? 33.140 9.618   4.184   1.00 10.81 ?  62  GLN   A O    1 
ATOM   1439 C  CB   . GLN   A 1 62  ? 30.062 10.748  4.370   1.00 10.54 ?  62  GLN   A CB   1 
ATOM   1440 C  CG   . GLN   A 1 62  ? 30.436 11.108  2.941   1.00 10.71 ?  62  GLN   A CG   1 
ATOM   1441 C  CD   . GLN   A 1 62  ? 30.112 9.977   1.992   1.00 10.75 ?  62  GLN   A CD   1 
ATOM   1442 O  OE1  . GLN   A 1 62  ? 28.932 9.669   1.778   1.00 11.29 ?  62  GLN   A OE1  1 
ATOM   1443 N  NE2  . GLN   A 1 62  ? 31.136 9.306   1.472   1.00 11.41 ?  62  GLN   A NE2  1 
ATOM   1444 H  H    . GLN   A 1 62  ? 29.663 9.588   6.487   1.00 12.74 ?  62  GLN   A H    1 
ATOM   1445 H  HA   . GLN   A 1 62  ? 30.805 8.835   4.260   1.00 12.95 ?  62  GLN   A HA   1 
ATOM   1446 H  HB2  . GLN   A 1 62  ? 29.118 10.533  4.393   1.00 12.77 ?  62  GLN   A HB2  1 
ATOM   1447 H  HB3  . GLN   A 1 62  ? 30.241 11.521  4.930   1.00 12.77 ?  62  GLN   A HB3  1 
ATOM   1448 H  HG2  . GLN   A 1 62  ? 29.923 11.885  2.665   1.00 12.97 ?  62  GLN   A HG2  1 
ATOM   1449 H  HG3  . GLN   A 1 62  ? 31.383 11.291  2.887   1.00 12.97 ?  62  GLN   A HG3  1 
ATOM   1450 H  HE21 . GLN   A 1 62  ? 31.940 9.546   1.658   1.00 13.81 ?  62  GLN   A HE21 1 
ATOM   1451 H  HE22 . GLN   A 1 62  ? 30.994 8.653   0.933   1.00 13.81 ?  62  GLN   A HE22 1 
ATOM   1452 N  N    . VAL   A 1 63  ? 32.687 10.619  6.151   1.00 11.04 ?  63  VAL   A N    1 
ATOM   1453 C  CA   . VAL   A 1 63  ? 34.080 11.010  6.371   1.00 12.07 ?  63  VAL   A CA   1 
ATOM   1454 C  C    . VAL   A 1 63  ? 34.973 9.773   6.434   1.00 11.26 ?  63  VAL   A C    1 
ATOM   1455 O  O    . VAL   A 1 63  ? 36.030 9.706   5.788   1.00 11.78 ?  63  VAL   A O    1 
ATOM   1456 C  CB   . VAL   A 1 63  ? 34.191 11.878  7.639   1.00 13.48 ?  63  VAL   A CB   1 
ATOM   1457 C  CG1  . VAL   A 1 63  ? 35.640 12.120  8.000   1.00 15.04 ?  63  VAL   A CG1  1 
ATOM   1458 C  CG2  . VAL   A 1 63  ? 33.469 13.211  7.440   1.00 13.56 ?  63  VAL   A CG2  1 
ATOM   1459 H  H    . VAL   A 1 63  ? 32.145 10.868  6.776   1.00 13.36 ?  63  VAL   A H    1 
ATOM   1460 H  HA   . VAL   A 1 63  ? 34.372 11.548  5.621   1.00 14.60 ?  63  VAL   A HA   1 
ATOM   1461 H  HB   . VAL   A 1 63  ? 33.774 11.412  8.383   1.00 16.29 ?  63  VAL   A HB   1 
ATOM   1462 H  HG11 . VAL   A 1 63  ? 35.687 12.854  8.633   1.00 18.16 ?  63  VAL   A HG11 1 
ATOM   1463 H  HG12 . VAL   A 1 63  ? 36.011 11.318  8.397   1.00 18.16 ?  63  VAL   A HG12 1 
ATOM   1464 H  HG13 . VAL   A 1 63  ? 36.129 12.350  7.193   1.00 18.16 ?  63  VAL   A HG13 1 
ATOM   1465 H  HG21 . VAL   A 1 63  ? 33.557 13.740  8.249   1.00 16.39 ?  63  VAL   A HG21 1 
ATOM   1466 H  HG22 . VAL   A 1 63  ? 33.875 13.678  6.693   1.00 16.39 ?  63  VAL   A HG22 1 
ATOM   1467 H  HG23 . VAL   A 1 63  ? 32.534 13.037  7.257   1.00 16.39 ?  63  VAL   A HG23 1 
ATOM   1468 N  N    . GLU   A 1 64  ? 34.551 8.765   7.202   1.00 11.26 ?  64  GLU   A N    1 
ATOM   1469 C  CA   . GLU   A 1 64  ? 35.311 7.524   7.300   1.00 11.17 ?  64  GLU   A CA   1 
ATOM   1470 C  C    . GLU   A 1 64  ? 35.399 6.833   5.946   1.00 10.99 ?  64  GLU   A C    1 
ATOM   1471 O  O    . GLU   A 1 64  ? 36.452 6.293   5.569   1.00 11.50 ?  64  GLU   A O    1 
ATOM   1472 C  CB   . GLU   A 1 64  ? 34.616 6.617   8.317   1.00 11.54 ?  64  GLU   A CB   1 
ATOM   1473 C  CG   . GLU   A 1 64  ? 35.262 5.274   8.476   1.00 12.34 ?  64  GLU   A CG   1 
ATOM   1474 C  CD   . GLU   A 1 64  ? 34.380 4.281   9.202   1.00 13.14 ?  64  GLU   A CD   1 
ATOM   1475 O  OE1  . GLU   A 1 64  ? 33.142 4.370   9.063   1.00 13.66 ?  64  GLU   A OE1  1 
ATOM   1476 O  OE2  . GLU   A 1 64  ? 34.925 3.389   9.893   1.00 13.56 -1 64  GLU   A OE2  1 
ATOM   1477 H  H    . GLU   A 1 64  ? 33.825 8.777   7.664   1.00 13.62 ?  64  GLU   A H    1 
ATOM   1478 H  HA   . GLU   A 1 64  ? 36.209 7.722   7.617   1.00 13.52 ?  64  GLU   A HA   1 
ATOM   1479 H  HB2  . GLU   A 1 64  ? 34.628 7.058   9.186   1.00 13.97 ?  64  GLU   A HB2  1 
ATOM   1480 H  HB3  . GLU   A 1 64  ? 33.698 6.485   8.034   1.00 13.97 ?  64  GLU   A HB3  1 
ATOM   1481 H  HG2  . GLU   A 1 64  ? 35.463 4.905   7.598   1.00 14.92 ?  64  GLU   A HG2  1 
ATOM   1482 H  HG3  . GLU   A 1 64  ? 36.079 5.377   8.982   1.00 14.92 ?  64  GLU   A HG3  1 
ATOM   1483 N  N    . SER   A 1 65  ? 34.287 6.832   5.206   1.00 10.52 ?  65  SER   A N    1 
ATOM   1484 C  CA   . SER   A 1 65  ? 34.236 6.176   3.904   1.00 10.76 ?  65  SER   A CA   1 
ATOM   1485 C  C    . SER   A 1 65  ? 35.165 6.841   2.896   1.00 10.80 ?  65  SER   A C    1 
ATOM   1486 O  O    . SER   A 1 65  ? 35.798 6.159   2.084   1.00 11.49 ?  65  SER   A O    1 
ATOM   1487 C  CB   . SER   A 1 65  ? 32.801 6.189   3.373   1.00 10.89 ?  65  SER   A CB   1 
ATOM   1488 O  OG   . SER   A 1 65  ? 31.944 5.370   4.164   1.00 11.16 ?  65  SER   A OG   1 
ATOM   1489 H  H    . SER   A 1 65  ? 33.551 7.215   5.437   1.00 12.74 ?  65  SER   A H    1 
ATOM   1490 H  HA   . SER   A 1 65  ? 34.513 5.256   4.004   1.00 13.03 ?  65  SER   A HA   1 
ATOM   1491 H  HB2  . SER   A 1 65  ? 32.462 7.095   3.388   1.00 13.18 ?  65  SER   A HB2  1 
ATOM   1492 H  HB3  . SER   A 1 65  ? 32.800 5.849   2.464   1.00 13.18 ?  65  SER   A HB3  1 
ATOM   1493 H  HG   . SER   A 1 65  ? 31.938 5.647   4.962   1.00 13.51 ?  65  SER   A HG   1 
ATOM   1494 N  N    . ASP   A 1 66  ? 35.242 8.174   2.914   1.00 10.73 ?  66  ASP   A N    1 
ATOM   1495 C  CA   . ASP   A 1 66  ? 36.106 8.870   1.966   1.00 11.90 ?  66  ASP   A CA   1 
ATOM   1496 C  C    . ASP   A 1 66  ? 37.566 8.511   2.207   1.00 11.80 ?  66  ASP   A C    1 
ATOM   1497 O  O    . ASP   A 1 66  ? 38.337 8.334   1.256   1.00 12.65 ?  66  ASP   A O    1 
ATOM   1498 C  CB   . ASP   A 1 66  ? 35.887 10.377  2.068   1.00 13.37 ?  66  ASP   A CB   1 
ATOM   1499 C  CG   . ASP   A 1 66  ? 34.550 10.839  1.459   1.00 15.08 ?  66  ASP   A CG   1 
ATOM   1500 O  OD1  . ASP   A 1 66  ? 33.830 10.045  0.813   1.00 15.00 ?  66  ASP   A OD1  1 
ATOM   1501 O  OD2  . ASP   A 1 66  ? 34.255 12.042  1.604   1.00 17.73 -1 66  ASP   A OD2  1 
ATOM   1502 H  H    . ASP   A 1 66  ? 34.805 8.689   3.450   1.00 12.99 ?  66  ASP   A H    1 
ATOM   1503 H  HA   . ASP   A 1 66  ? 35.871 8.592   1.067   1.00 14.40 ?  66  ASP   A HA   1 
ATOM   1504 H  HB2  . ASP   A 1 66  ? 35.890 10.636  3.002   1.00 16.16 ?  66  ASP   A HB2  1 
ATOM   1505 H  HB3  . ASP   A 1 66  ? 36.606 10.831  1.597   1.00 16.16 ?  66  ASP   A HB3  1 
ATOM   1506 N  N    . ASP   A 1 67  ? 37.961 8.378   3.474   1.00 12.15 ?  67  ASP   A N    1 
ATOM   1507 C  CA   . ASP   A 1 67  ? 39.315 7.929   3.779   1.00 12.68 ?  67  ASP   A CA   1 
ATOM   1508 C  C    . ASP   A 1 67  ? 39.538 6.494   3.315   1.00 12.61 ?  67  ASP   A C    1 
ATOM   1509 O  O    . ASP   A 1 67  ? 40.596 6.171   2.762   1.00 13.31 ?  67  ASP   A O    1 
ATOM   1510 C  CB   . ASP   A 1 67  ? 39.584 8.074   5.274   1.00 13.94 ?  67  ASP   A CB   1 
ATOM   1511 C  CG   . ASP   A 1 67  ? 40.875 7.411   5.699   1.00 15.33 ?  67  ASP   A CG   1 
ATOM   1512 O  OD1  . ASP   A 1 67  ? 41.949 8.041   5.569   1.00 17.69 ?  67  ASP   A OD1  1 
ATOM   1513 O  OD2  . ASP   A 1 67  ? 40.819 6.247   6.160   1.00 15.38 -1 67  ASP   A OD2  1 
ATOM   1514 H  H    . ASP   A 1 67  ? 37.474 8.539   4.160   1.00 14.70 ?  67  ASP   A H    1 
ATOM   1515 H  HA   . ASP   A 1 67  ? 39.947 8.492   3.303   1.00 15.33 ?  67  ASP   A HA   1 
ATOM   1516 H  HB2  . ASP   A 1 67  ? 39.647 9.011   5.489   1.00 16.84 ?  67  ASP   A HB2  1 
ATOM   1517 H  HB3  . ASP   A 1 67  ? 38.861 7.657   5.763   1.00 16.84 ?  67  ASP   A HB3  1 
ATOM   1518 N  N    . TYR   A 1 68  ? 38.545 5.620   3.508   1.00 12.47 ?  68  TYR   A N    1 
ATOM   1519 C  CA   . TYR   A 1 68  ? 38.660 4.240   3.035   1.00 12.58 ?  68  TYR   A CA   1 
ATOM   1520 C  C    . TYR   A 1 68  ? 38.903 4.192   1.528   1.00 12.28 ?  68  TYR   A C    1 
ATOM   1521 O  O    . TYR   A 1 68  ? 39.787 3.464   1.054   1.00 12.61 ?  68  TYR   A O    1 
ATOM   1522 C  CB   . TYR   A 1 68  ? 37.407 3.422   3.411   1.00 12.70 ?  68  TYR   A CB   1 
ATOM   1523 C  CG   . TYR   A 1 68  ? 37.434 2.034   2.782   1.00 14.06 ?  68  TYR   A CG   1 
ATOM   1524 C  CD1  . TYR   A 1 68  ? 36.969 1.838   1.484   1.00 15.31 ?  68  TYR   A CD1  1 
ATOM   1525 C  CD2  . TYR   A 1 68  ? 37.971 0.946   3.454   1.00 15.54 ?  68  TYR   A CD2  1 
ATOM   1526 C  CE1  . TYR   A 1 68  ? 37.034 0.618   0.872   1.00 16.87 ?  68  TYR   A CE1  1 
ATOM   1527 C  CE2  . TYR   A 1 68  ? 38.033 -0.312  2.841   1.00 16.52 ?  68  TYR   A CE2  1 
ATOM   1528 C  CZ   . TYR   A 1 68  ? 37.571 -0.451  1.550   1.00 17.13 ?  68  TYR   A CZ   1 
ATOM   1529 O  OH   . TYR   A 1 68  ? 37.647 -1.667  0.927   1.00 18.22 ?  68  TYR   A OH   1 
ATOM   1530 H  H    . TYR   A 1 68  ? 37.802 5.798   3.908   1.00 15.08 ?  68  TYR   A H    1 
ATOM   1531 H  HA   . TYR   A 1 68  ? 39.418 3.824   3.469   1.00 15.21 ?  68  TYR   A HA   1 
ATOM   1532 H  HB2  . TYR   A 1 68  ? 37.370 3.317   4.375   1.00 15.36 ?  68  TYR   A HB2  1 
ATOM   1533 H  HB3  . TYR   A 1 68  ? 36.613 3.885   3.094   1.00 15.36 ?  68  TYR   A HB3  1 
ATOM   1534 H  HD1  . TYR   A 1 68  ? 36.618 2.568   1.017   1.00 18.48 ?  68  TYR   A HD1  1 
ATOM   1535 H  HD2  . TYR   A 1 68  ? 38.305 1.059   4.313   1.00 18.77 ?  68  TYR   A HD2  1 
ATOM   1536 H  HE1  . TYR   A 1 68  ? 36.708 0.516   0.008   1.00 20.36 ?  68  TYR   A HE1  1 
ATOM   1537 H  HE2  . TYR   A 1 68  ? 38.397 -1.038  3.285   1.00 19.94 ?  68  TYR   A HE2  1 
ATOM   1538 H  HH   . TYR   A 1 68  ? 37.973 -2.234  1.454   1.00 21.98 ?  68  TYR   A HH   1 
ATOM   1539 N  N    . ILE   A 1 69  ? 38.115 4.953   0.754   1.00 11.78 ?  69  ILE   A N    1 
ATOM   1540 C  CA   . ILE   A 1 69  ? 38.254 4.939   -0.701  1.00 11.84 ?  69  ILE   A CA   1 
ATOM   1541 C  C    . ILE   A 1 69  ? 39.593 5.540   -1.128  1.00 11.71 ?  69  ILE   A C    1 
ATOM   1542 O  O    . ILE   A 1 69  ? 40.240 5.058   -2.066  1.00 12.38 ?  69  ILE   A O    1 
ATOM   1543 C  CB   . ILE   A 1 69  ? 37.058 5.648   -1.371  1.00 12.94 ?  69  ILE   A CB   1 
ATOM   1544 C  CG1  . ILE   A 1 69  ? 35.743 4.912   -1.092  1.00 13.16 ?  69  ILE   A CG1  1 
ATOM   1545 C  CG2  . ILE   A 1 69  ? 37.308 5.841   -2.876  1.00 14.52 ?  69  ILE   A CG2  1 
ATOM   1546 C  CD1  . ILE   A 1 69  ? 35.578 3.622   -1.862  1.00 14.01 ?  69  ILE   A CD1  1 
ATOM   1547 H  H    . ILE   A 1 69  ? 37.510 5.488   1.050   1.00 14.26 ?  69  ILE   A H    1 
ATOM   1548 H  HA   . ILE   A 1 69  ? 38.248 4.018   -0.996  1.00 14.32 ?  69  ILE   A HA   1 
ATOM   1549 H  HB   . ILE   A 1 69  ? 36.983 6.528   -0.979  1.00 15.64 ?  69  ILE   A HB   1 
ATOM   1550 H  HG12 . ILE   A 1 69  ? 35.705 4.698   -0.144  1.00 15.91 ?  69  ILE   A HG12 1 
ATOM   1551 H  HG13 . ILE   A 1 69  ? 35.005 5.494   -1.323  1.00 15.91 ?  69  ILE   A HG13 1 
ATOM   1552 H  HG21 . ILE   A 1 69  ? 36.465 6.049   -3.313  1.00 17.53 ?  69  ILE   A HG21 1 
ATOM   1553 H  HG22 . ILE   A 1 69  ? 37.928 6.582   -3.003  1.00 17.53 ?  69  ILE   A HG22 1 
ATOM   1554 H  HG23 . ILE   A 1 69  ? 37.681 5.030   -3.248  1.00 17.53 ?  69  ILE   A HG23 1 
ATOM   1555 H  HD11 . ILE   A 1 69  ? 34.775 3.176   -1.552  1.00 16.93 ?  69  ILE   A HD11 1 
ATOM   1556 H  HD12 . ILE   A 1 69  ? 35.498 3.828   -2.806  1.00 16.93 ?  69  ILE   A HD12 1 
ATOM   1557 H  HD13 . ILE   A 1 69  ? 36.351 3.059   -1.707  1.00 16.93 ?  69  ILE   A HD13 1 
ATOM   1558 N  N    . ALA   A 1 70  ? 40.013 6.622   -0.473  1.00 12.53 ?  70  ALA   A N    1 
ATOM   1559 C  CA   . ALA   A 1 70  ? 41.293 7.229   -0.823  1.00 13.43 ?  70  ALA   A CA   1 
ATOM   1560 C  C    . ALA   A 1 70  ? 42.441 6.247   -0.651  1.00 13.63 ?  70  ALA   A C    1 
ATOM   1561 O  O    . ALA   A 1 70  ? 43.412 6.291   -1.410  1.00 15.92 ?  70  ALA   A O    1 
ATOM   1562 C  CB   . ALA   A 1 70  ? 41.533 8.485   0.016   1.00 13.99 ?  70  ALA   A CB   1 
ATOM   1563 H  H    . ALA   A 1 70  ? 39.583 7.017   0.154   1.00 15.15 ?  70  ALA   A H    1 
ATOM   1564 H  HA   . ALA   A 1 70  ? 41.271 7.502   -1.756  1.00 16.23 ?  70  ALA   A HA   1 
ATOM   1565 H  HB1  . ALA   A 1 70  ? 42.394 8.871   -0.231  1.00 16.90 ?  70  ALA   A HB1  1 
ATOM   1566 H  HB2  . ALA   A 1 70  ? 40.827 9.125   -0.153  1.00 16.90 ?  70  ALA   A HB2  1 
ATOM   1567 H  HB3  . ALA   A 1 70  ? 41.545 8.241   0.955   1.00 16.90 ?  70  ALA   A HB3  1 
ATOM   1568 N  N    . THR   A 1 71  ? 42.338 5.349   0.327   1.00 13.20 ?  71  THR   A N    1 
ATOM   1569 C  CA   . THR   A 1 71  ? 43.389 4.369   0.583   1.00 14.60 ?  71  THR   A CA   1 
ATOM   1570 C  C    . THR   A 1 71  ? 43.268 3.144   -0.311  1.00 14.60 ?  71  THR   A C    1 
ATOM   1571 O  O    . THR   A 1 71  ? 44.283 2.625   -0.798  1.00 16.66 ?  71  THR   A O    1 
ATOM   1572 C  CB   . THR   A 1 71  ? 43.304 3.919   2.036   1.00 16.67 ?  71  THR   A CB   1 
ATOM   1573 O  OG1  . THR   A 1 71  ? 43.544 5.044   2.888   1.00 18.38 ?  71  THR   A OG1  1 
ATOM   1574 C  CG2  . THR   A 1 71  ? 44.309 2.818   2.326   1.00 18.22 ?  71  THR   A CG2  1 
ATOM   1575 H  H    . THR   A 1 71  ? 41.666 5.287   0.857   1.00 15.96 ?  71  THR   A H    1 
ATOM   1576 H  HA   . THR   A 1 71  ? 44.258 4.774   0.432   1.00 17.64 ?  71  THR   A HA   1 
ATOM   1577 H  HB   . THR   A 1 71  ? 42.414 3.558   2.200   1.00 20.12 ?  71  THR   A HB   1 
ATOM   1578 H  HG1  . THR   A 1 71  ? 42.947 5.622   2.758   1.00 22.17 ?  71  THR   A HG1  1 
ATOM   1579 H  HG21 . THR   A 1 71  ? 44.444 2.737   3.283   1.00 21.97 ?  71  THR   A HG21 1 
ATOM   1580 H  HG22 . THR   A 1 71  ? 43.994 1.966   1.982   1.00 21.97 ?  71  THR   A HG22 1 
ATOM   1581 H  HG23 . THR   A 1 71  ? 45.162 3.028   1.908   1.00 21.97 ?  71  THR   A HG23 1 
ATOM   1582 N  N    . ASN   A 1 72  ? 42.043 2.642   -0.504  1.00 13.62 ?  72  ASN   A N    1 
ATOM   1583 C  CA   . ASN   A 1 72  ? 41.825 1.318   -1.068  1.00 13.88 ?  72  ASN   A CA   1 
ATOM   1584 C  C    . ASN   A 1 72  ? 41.206 1.304   -2.454  1.00 14.09 ?  72  ASN   A C    1 
ATOM   1585 O  O    . ASN   A 1 72  ? 41.216 0.248   -3.099  1.00 15.18 ?  72  ASN   A O    1 
ATOM   1586 C  CB   . ASN   A 1 72  ? 40.937 0.493   -0.130  1.00 14.65 ?  72  ASN   A CB   1 
ATOM   1587 C  CG   . ASN   A 1 72  ? 41.550 0.336   1.234   1.00 15.75 ?  72  ASN   A CG   1 
ATOM   1588 O  OD1  . ASN   A 1 72  ? 41.100 0.935   2.207   1.00 17.64 ?  72  ASN   A OD1  1 
ATOM   1589 N  ND2  . ASN   A 1 72  ? 42.605 -0.446  1.310   1.00 16.10 ?  72  ASN   A ND2  1 
ATOM   1590 H  H    . ASN   A 1 72  ? 41.311 3.065   -0.316  1.00 16.46 ?  72  ASN   A H    1 
ATOM   1591 H  HA   . ASN   A 1 72  ? 42.681 0.873   -1.135  1.00 16.77 ?  72  ASN   A HA   1 
ATOM   1592 H  HB2  . ASN   A 1 72  ? 40.081 0.931   -0.034  1.00 17.70 ?  72  ASN   A HB2  1 
ATOM   1593 H  HB3  . ASN   A 1 72  ? 40.820 -0.394  -0.511  1.00 17.70 ?  72  ASN   A HB3  1 
ATOM   1594 H  HD21 . ASN   A 1 72  ? 43.000 -0.558  2.067   1.00 19.44 ?  72  ASN   A HD21 1 
ATOM   1595 H  HD22 . ASN   A 1 72  ? 42.906 -0.836  0.607   1.00 19.44 ?  72  ASN   A HD22 1 
ATOM   1596 N  N    . GLY   A 1 73  ? 40.649 2.415   -2.917  1.00 13.71 ?  73  GLY   A N    1 
ATOM   1597 C  CA   . GLY   A 1 73  ? 39.917 2.422   -4.158  1.00 13.36 ?  73  GLY   A CA   1 
ATOM   1598 C  C    . GLY   A 1 73  ? 38.523 1.848   -3.995  1.00 12.91 ?  73  GLY   A C    1 
ATOM   1599 O  O    . GLY   A 1 73  ? 38.128 1.393   -2.913  1.00 13.41 ?  73  GLY   A O    1 
ATOM   1600 H  H    . GLY   A 1 73  ? 40.681 3.187   -2.527  1.00 16.57 ?  73  GLY   A H    1 
ATOM   1601 H  HA2  . GLY   A 1 73  ? 39.844 3.338   -4.486  1.00 16.15 ?  73  GLY   A HA2  1 
ATOM   1602 H  HA3  . GLY   A 1 73  ? 40.395 1.900   -4.823  1.00 16.15 ?  73  GLY   A HA3  1 
ATOM   1603 N  N    . PRO   A 1 74  ? 37.754 1.862   -5.083  1.00 13.36 ?  74  PRO   A N    1 
ATOM   1604 C  CA   . PRO   A 1 74  ? 36.355 1.436   -5.008  1.00 13.38 ?  74  PRO   A CA   1 
ATOM   1605 C  C    . PRO   A 1 74  ? 36.203 -0.046  -4.689  1.00 12.33 ?  74  PRO   A C    1 
ATOM   1606 O  O    . PRO   A 1 74  ? 37.070 -0.877  -4.979  1.00 13.34 ?  74  PRO   A O    1 
ATOM   1607 C  CB   . PRO   A 1 74  ? 35.812 1.738   -6.411  1.00 15.00 ?  74  PRO   A CB   1 
ATOM   1608 C  CG   . PRO   A 1 74  ? 36.783 2.692   -7.023  1.00 17.74 ?  74  PRO   A CG   1 
ATOM   1609 C  CD   . PRO   A 1 74  ? 38.111 2.357   -6.423  1.00 15.32 ?  74  PRO   A CD   1 
ATOM   1610 H  HA   . PRO   A 1 74  ? 35.873 1.963   -4.352  1.00 16.17 ?  74  PRO   A HA   1 
ATOM   1611 H  HB2  . PRO   A 1 74  ? 35.764 0.916   -6.925  1.00 18.12 ?  74  PRO   A HB2  1 
ATOM   1612 H  HB3  . PRO   A 1 74  ? 34.932 2.144   -6.338  1.00 18.12 ?  74  PRO   A HB3  1 
ATOM   1613 H  HG2  . PRO   A 1 74  ? 36.804 2.568   -7.985  1.00 21.40 ?  74  PRO   A HG2  1 
ATOM   1614 H  HG3  . PRO   A 1 74  ? 36.533 3.602   -6.801  1.00 21.40 ?  74  PRO   A HG3  1 
ATOM   1615 H  HD2  . PRO   A 1 74  ? 38.554 1.661   -6.941  1.00 18.50 ?  74  PRO   A HD2  1 
ATOM   1616 H  HD3  . PRO   A 1 74  ? 38.664 3.155   -6.366  1.00 18.50 ?  74  PRO   A HD3  1 
ATOM   1617 N  N    . LEU   A 1 75  ? 35.054 -0.369  -4.099  1.00 11.99 ?  75  LEU   A N    1 
ATOM   1618 C  CA   . LEU   A 1 75  ? 34.646 -1.757  -3.954  1.00 11.67 ?  75  LEU   A CA   1 
ATOM   1619 C  C    . LEU   A 1 75  ? 34.261 -2.333  -5.316  1.00 12.32 ?  75  LEU   A C    1 
ATOM   1620 O  O    . LEU   A 1 75  ? 34.142 -1.619  -6.318  1.00 13.43 ?  75  LEU   A O    1 
ATOM   1621 C  CB   . LEU   A 1 75  ? 33.459 -1.875  -2.996  1.00 11.88 ?  75  LEU   A CB   1 
ATOM   1622 C  CG   . LEU   A 1 75  ? 33.660 -1.462  -1.540  1.00 13.58 ?  75  LEU   A CG   1 
ATOM   1623 C  CD1  . LEU   A 1 75  ? 32.372 -1.665  -0.749  1.00 15.38 ?  75  LEU   A CD1  1 
ATOM   1624 C  CD2  . LEU   A 1 75  ? 34.801 -2.173  -0.875  1.00 16.70 ?  75  LEU   A CD2  1 
ATOM   1625 H  H    . LEU   A 1 75  ? 34.501 0.200   -3.774  1.00 14.50 ?  75  LEU   A H    1 
ATOM   1626 H  HA   . LEU   A 1 75  ? 35.385 -2.273  -3.600  1.00 14.12 ?  75  LEU   A HA   1 
ATOM   1627 H  HB2  . LEU   A 1 75  ? 32.739 -1.333  -3.346  1.00 14.37 ?  75  LEU   A HB2  1 
ATOM   1628 H  HB3  . LEU   A 1 75  ? 33.180 -2.805  -2.987  1.00 14.37 ?  75  LEU   A HB3  1 
ATOM   1629 H  HG   . LEU   A 1 75  ? 33.866 -0.513  -1.518  1.00 16.41 ?  75  LEU   A HG   1 
ATOM   1630 H  HD11 . LEU   A 1 75  ? 32.519 -1.393  0.171   1.00 18.57 ?  75  LEU   A HD11 1 
ATOM   1631 H  HD12 . LEU   A 1 75  ? 31.672 -1.121  -1.146  1.00 18.57 ?  75  LEU   A HD12 1 
ATOM   1632 H  HD13 . LEU   A 1 75  ? 32.125 -2.600  -0.784  1.00 18.57 ?  75  LEU   A HD13 1 
ATOM   1633 H  HD21 . LEU   A 1 75  ? 34.853 -1.897  0.054   1.00 20.15 ?  75  LEU   A HD21 1 
ATOM   1634 H  HD22 . LEU   A 1 75  ? 34.655 -3.129  -0.929  1.00 20.15 ?  75  LEU   A HD22 1 
ATOM   1635 H  HD23 . LEU   A 1 75  ? 35.630 -1.942  -1.331  1.00 20.15 ?  75  LEU   A HD23 1 
ATOM   1636 N  N    . LYS   A 1 76  ? 34.069 -3.652  -5.334  1.00 12.63 ?  76  LYS   A N    1 
ATOM   1637 C  CA   . LYS   A 1 76  ? 33.469 -4.368  -6.455  1.00 13.10 ?  76  LYS   A CA   1 
ATOM   1638 C  C    . LYS   A 1 76  ? 31.956 -4.450  -6.260  1.00 11.56 ?  76  LYS   A C    1 
ATOM   1639 O  O    . LYS   A 1 76  ? 31.471 -4.563  -5.135  1.00 11.77 ?  76  LYS   A O    1 
ATOM   1640 C  CB   . LYS   A 1 76  ? 34.013 -5.806  -6.516  1.00 14.70 ?  76  LYS   A CB   1 
ATOM   1641 C  CG   . LYS   A 1 76  ? 35.521 -5.920  -6.721  1.00 16.11 ?  76  LYS   A CG   1 
ATOM   1642 C  CD   . LYS   A 1 76  ? 36.030 -7.327  -6.511  1.00 17.40 ?  76  LYS   A CD   1 
ATOM   1643 C  CE   . LYS   A 1 76  ? 37.532 -7.390  -6.689  1.00 19.82 ?  76  LYS   A CE   1 
ATOM   1644 N  NZ   . LYS   A 1 76  ? 38.059 -8.750  -6.484  1.00 20.51 ?  76  LYS   A NZ   1 
ATOM   1645 H  H    . LYS   A 1 76  ? 34.291 -4.175  -4.683  1.00 15.27 ?  76  LYS   A H    1 
ATOM   1646 H  HA   . LYS   A 1 76  ? 33.667 -3.911  -7.287  1.00 15.84 ?  76  LYS   A HA   1 
ATOM   1647 H  HB2  . LYS   A 1 76  ? 33.797 -6.251  -5.683  1.00 17.76 ?  76  LYS   A HB2  1 
ATOM   1648 H  HB3  . LYS   A 1 76  ? 33.582 -6.263  -7.253  1.00 17.76 ?  76  LYS   A HB3  1 
ATOM   1649 H  HG2  . LYS   A 1 76  ? 35.739 -5.652  -7.629  1.00 19.45 ?  76  LYS   A HG2  1 
ATOM   1650 H  HG3  . LYS   A 1 76  ? 35.974 -5.337  -6.089  1.00 19.45 ?  76  LYS   A HG3  1 
ATOM   1651 H  HD2  . LYS   A 1 76  ? 35.814 -7.616  -5.610  1.00 21.00 ?  76  LYS   A HD2  1 
ATOM   1652 H  HD3  . LYS   A 1 76  ? 35.619 -7.919  -7.162  1.00 21.00 ?  76  LYS   A HD3  1 
ATOM   1653 H  HE2  . LYS   A 1 76  ? 37.757 -7.111  -7.589  1.00 23.90 ?  76  LYS   A HE2  1 
ATOM   1654 H  HE3  . LYS   A 1 76  ? 37.953 -6.805  -6.040  1.00 23.90 ?  76  LYS   A HE3  1 
ATOM   1655 H  HZ1  . LYS   A 1 76  ? 38.941 -8.763  -6.595  1.00 24.73 ?  76  LYS   A HZ1  1 
ATOM   1656 H  HZ2  . LYS   A 1 76  ? 37.868 -9.038  -5.662  1.00 24.73 ?  76  LYS   A HZ2  1 
ATOM   1657 H  HZ3  . LYS   A 1 76  ? 37.690 -9.316  -7.073  1.00 24.73 ?  76  LYS   A HZ3  1 
ATOM   1658 N  N    . VAL   A 1 77  ? 31.206 -4.412  -7.366  1.00 11.96 ?  77  VAL   A N    1 
ATOM   1659 C  CA   . VAL   A 1 77  ? 29.799 -4.800  -7.283  1.00 11.88 ?  77  VAL   A CA   1 
ATOM   1660 C  C    . VAL   A 1 77  ? 29.736 -6.253  -6.842  1.00 12.02 ?  77  VAL   A C    1 
ATOM   1661 O  O    . VAL   A 1 77  ? 30.390 -7.126  -7.426  1.00 12.20 ?  77  VAL   A O    1 
ATOM   1662 C  CB   . VAL   A 1 77  ? 29.076 -4.576  -8.620  1.00 12.97 ?  77  VAL   A CB   1 
ATOM   1663 C  CG1  . VAL   A 1 77  ? 27.610 -5.002  -8.514  1.00 13.89 ?  77  VAL   A CG1  1 
ATOM   1664 C  CG2  . VAL   A 1 77  ? 29.172 -3.122  -9.045  1.00 14.45 ?  77  VAL   A CG2  1 
ATOM   1665 H  H    . VAL   A 1 77  ? 31.484 -4.167  -8.144  1.00 14.47 ?  77  VAL   A H    1 
ATOM   1666 H  HA   . VAL   A 1 77  ? 29.363 -4.255  -6.608  1.00 14.38 ?  77  VAL   A HA   1 
ATOM   1667 H  HB   . VAL   A 1 77  ? 29.502 -5.114  -9.304  1.00 15.68 ?  77  VAL   A HB   1 
ATOM   1668 H  HG11 . VAL   A 1 77  ? 27.140 -4.701  -9.306  1.00 16.79 ?  77  VAL   A HG11 1 
ATOM   1669 H  HG12 . VAL   A 1 77  ? 27.566 -5.966  -8.446  1.00 16.79 ?  77  VAL   A HG12 1 
ATOM   1670 H  HG13 . VAL   A 1 77  ? 27.221 -4.593  -7.724  1.00 16.79 ?  77  VAL   A HG13 1 
ATOM   1671 H  HG21 . VAL   A 1 77  ? 28.659 -2.996  -9.856  1.00 17.46 ?  77  VAL   A HG21 1 
ATOM   1672 H  HG22 . VAL   A 1 77  ? 28.815 -2.562  -8.336  1.00 17.46 ?  77  VAL   A HG22 1 
ATOM   1673 H  HG23 . VAL   A 1 77  ? 30.103 -2.897  -9.203  1.00 17.46 ?  77  VAL   A HG23 1 
ATOM   1674 N  N    . GLY   A 1 78  ? 28.954 -6.519  -5.797  1.00 11.47 ?  78  GLY   A N    1 
ATOM   1675 C  CA   . GLY   A 1 78  ? 28.931 -7.809  -5.144  1.00 11.72 ?  78  GLY   A CA   1 
ATOM   1676 C  C    . GLY   A 1 78  ? 29.842 -7.904  -3.939  1.00 11.20 ?  78  GLY   A C    1 
ATOM   1677 O  O    . GLY   A 1 78  ? 29.782 -8.908  -3.212  1.00 12.05 ?  78  GLY   A O    1 
ATOM   1678 H  H    . GLY   A 1 78  ? 28.407 -5.943  -5.452  1.00 13.88 ?  78  GLY   A H    1 
ATOM   1679 H  HA2  . GLY   A 1 78  ? 28.027 -8.001  -4.858  1.00 14.18 ?  78  GLY   A HA2  1 
ATOM   1680 H  HA3  . GLY   A 1 78  ? 29.199 -8.488  -5.783  1.00 14.18 ?  78  GLY   A HA3  1 
ATOM   1681 N  N    . GLY   A 1 79  ? 30.700 -6.904  -3.716  1.00 11.00 ?  79  GLY   A N    1 
ATOM   1682 C  CA   . GLY   A 1 79  ? 31.656 -6.925  -2.633  1.00 11.37 ?  79  GLY   A CA   1 
ATOM   1683 C  C    . GLY   A 1 79  ? 31.211 -6.120  -1.423  1.00 11.04 ?  79  GLY   A C    1 
ATOM   1684 O  O    . GLY   A 1 79  ? 30.090 -5.610  -1.346  1.00 11.50 ?  79  GLY   A O    1 
ATOM   1685 H  H    . GLY   A 1 79  ? 30.743 -6.189  -4.197  1.00 13.31 ?  79  GLY   A H    1 
ATOM   1686 H  HA2  . GLY   A 1 79  ? 31.802 -7.849  -2.357  1.00 13.75 ?  79  GLY   A HA2  1 
ATOM   1687 H  HA3  . GLY   A 1 79  ? 32.502 -6.570  -2.946  1.00 13.75 ?  79  GLY   A HA3  1 
ATOM   1688 N  N    . SER   A 1 80  ? 32.116 -6.027  -0.450  1.00 11.67 ?  80  SER   A N    1 
ATOM   1689 C  CA   . SER   A 1 80  ? 31.796 -5.398  0.822   1.00 11.34 ?  80  SER   A CA   1 
ATOM   1690 C  C    . SER   A 1 80  ? 33.067 -4.950  1.526   1.00 11.05 ?  80  SER   A C    1 
ATOM   1691 O  O    . SER   A 1 80  ? 34.179 -5.382  1.199   1.00 12.50 ?  80  SER   A O    1 
ATOM   1692 C  CB   . SER   A 1 80  ? 31.029 -6.358  1.742   1.00 12.42 ?  80  SER   A CB   1 
ATOM   1693 O  OG   . SER   A 1 80  ? 31.862 -7.404  2.226   1.00 13.97 ?  80  SER   A OG   1 
ATOM   1694 H  H    . SER   A 1 80  ? 32.926 -6.312  -0.509  1.00 14.12 ?  80  SER   A H    1 
ATOM   1695 H  HA   . SER   A 1 80  ? 31.245 -4.613  0.643   1.00 13.72 ?  80  SER   A HA   1 
ATOM   1696 H  HB2  . SER   A 1 80  ? 30.684 -5.849  2.492   1.00 15.02 ?  80  SER   A HB2  1 
ATOM   1697 H  HB3  . SER   A 1 80  ? 30.295 -6.743  1.240   1.00 15.02 ?  80  SER   A HB3  1 
ATOM   1698 H  HG   . SER   A 1 80  ? 32.169 -7.839  1.579   1.00 16.88 ?  80  SER   A HG   1 
ATOM   1699 N  N    . CYS   A 1 81  ? 32.875 -4.101  2.532   1.00 11.12 ?  81  CYS   A N    1 
ATOM   1700 C  CA   . CYS   A 1 81  ? 33.923 -3.815  3.497   1.00 11.26 ?  81  CYS   A CA   1 
ATOM   1701 C  C    . CYS   A 1 81  ? 33.278 -3.578  4.855   1.00 11.00 ?  81  CYS   A C    1 
ATOM   1702 O  O    . CYS   A 1 81  ? 32.113 -3.174  4.943   1.00 12.17 ?  81  CYS   A O    1 
ATOM   1703 C  CB   . CYS   A 1 81  ? 34.797 -2.622  3.081   1.00 12.04 ?  81  CYS   A CB   1 
ATOM   1704 S  SG   . CYS   A 1 81  ? 33.909 -1.049  3.089   1.00 11.79 ?  81  CYS   A SG   1 
ATOM   1705 H  H    . CYS   A 1 81  ? 32.137 -3.683  2.684   1.00 13.45 ?  81  CYS   A H    1 
ATOM   1706 H  HA   . CYS   A 1 81  ? 34.501 -4.589  3.575   1.00 13.63 ?  81  CYS   A HA   1 
ATOM   1707 H  HB2  . CYS   A 1 81  ? 35.546 -2.551  3.697   1.00 14.56 ?  81  CYS   A HB2  1 
ATOM   1708 H  HB3  . CYS   A 1 81  ? 35.128 -2.776  2.181   1.00 14.56 ?  81  CYS   A HB3  1 
ATOM   1709 H  HG   . CYS   A 1 81  ? 34.668 -0.177  2.755   1.00 14.26 ?  81  CYS   A HG   1 
ATOM   1710 N  N    . VAL   A 1 82  ? 34.048 -3.834  5.913   1.00 11.42 ?  82  VAL   A N    1 
ATOM   1711 C  CA   . VAL   A 1 82  ? 33.621 -3.594  7.286   1.00 11.88 ?  82  VAL   A CA   1 
ATOM   1712 C  C    . VAL   A 1 82  ? 34.218 -2.277  7.757   1.00 11.98 ?  82  VAL   A C    1 
ATOM   1713 O  O    . VAL   A 1 82  ? 35.441 -2.100  7.735   1.00 12.75 ?  82  VAL   A O    1 
ATOM   1714 C  CB   . VAL   A 1 82  ? 34.048 -4.736  8.219   1.00 13.27 ?  82  VAL   A CB   1 
ATOM   1715 C  CG1  . VAL   A 1 82  ? 33.602 -4.440  9.641   1.00 15.10 ?  82  VAL   A CG1  1 
ATOM   1716 C  CG2  . VAL   A 1 82  ? 33.485 -6.061  7.741   1.00 14.21 ?  82  VAL   A CG2  1 
ATOM   1717 H  H    . VAL   A 1 82  ? 34.847 -4.165  5.859   1.00 13.82 ?  82  VAL   A H    1 
ATOM   1718 H  HA   . VAL   A 1 82  ? 32.654 -3.517  7.310   1.00 14.37 ?  82  VAL   A HA   1 
ATOM   1719 H  HB   . VAL   A 1 82  ? 35.015 -4.794  8.217   1.00 16.05 ?  82  VAL   A HB   1 
ATOM   1720 H  HG11 . VAL   A 1 82  ? 33.690 -5.248  10.168  1.00 18.23 ?  82  VAL   A HG11 1 
ATOM   1721 H  HG12 . VAL   A 1 82  ? 34.161 -3.740  10.015  1.00 18.23 ?  82  VAL   A HG12 1 
ATOM   1722 H  HG13 . VAL   A 1 82  ? 32.675 -4.153  9.629   1.00 18.23 ?  82  VAL   A HG13 1 
ATOM   1723 H  HG21 . VAL   A 1 82  ? 33.730 -6.752  8.374   1.00 17.17 ?  82  VAL   A HG21 1 
ATOM   1724 H  HG22 . VAL   A 1 82  ? 32.518 -5.992  7.684   1.00 17.17 ?  82  VAL   A HG22 1 
ATOM   1725 H  HG23 . VAL   A 1 82  ? 33.854 -6.264  6.868   1.00 17.17 ?  82  VAL   A HG23 1 
ATOM   1726 N  N    . LEU   A 1 83  ? 33.361 -1.351  8.174   1.00 11.40 ?  83  LEU   A N    1 
ATOM   1727 C  CA   . LEU   A 1 83  ? 33.783 -0.086  8.753   1.00 11.39 ?  83  LEU   A CA   1 
ATOM   1728 C  C    . LEU   A 1 83  ? 33.062 0.097   10.085  1.00 11.60 ?  83  LEU   A C    1 
ATOM   1729 O  O    . LEU   A 1 83  ? 32.340 -0.793  10.552  1.00 12.20 ?  83  LEU   A O    1 
ATOM   1730 C  CB   . LEU   A 1 83  ? 33.535 1.071   7.774   1.00 12.08 ?  83  LEU   A CB   1 
ATOM   1731 C  CG   . LEU   A 1 83  ? 34.437 1.065   6.538   1.00 12.69 ?  83  LEU   A CG   1 
ATOM   1732 C  CD1  . LEU   A 1 83  ? 34.006 2.113   5.532   1.00 13.40 ?  83  LEU   A CD1  1 
ATOM   1733 C  CD2  . LEU   A 1 83  ? 35.910 1.285   6.926   1.00 13.52 ?  83  LEU   A CD2  1 
ATOM   1734 H  H    . LEU   A 1 83  ? 32.505 -1.438  8.134   1.00 13.79 ?  83  LEU   A H    1 
ATOM   1735 H  HA   . LEU   A 1 83  ? 34.733 -0.117  8.931   1.00 13.79 ?  83  LEU   A HA   1 
ATOM   1736 H  HB2  . LEU   A 1 83  ? 32.617 1.028   7.457   1.00 14.61 ?  83  LEU   A HB2  1 
ATOM   1737 H  HB3  . LEU   A 1 83  ? 33.678 1.913   8.233   1.00 14.61 ?  83  LEU   A HB3  1 
ATOM   1738 H  HG   . LEU   A 1 83  ? 34.377 0.202   6.107   1.00 15.34 ?  83  LEU   A HG   1 
ATOM   1739 H  HD11 . LEU   A 1 83  ? 34.601 2.077   4.762   1.00 16.20 ?  83  LEU   A HD11 1 
ATOM   1740 H  HD12 . LEU   A 1 83  ? 33.098 1.926   5.255   1.00 16.20 ?  83  LEU   A HD12 1 
ATOM   1741 H  HD13 . LEU   A 1 83  ? 34.057 2.989   5.944   1.00 16.20 ?  83  LEU   A HD13 1 
ATOM   1742 H  HD21 . LEU   A 1 83  ? 36.435 1.440   6.121   1.00 16.33 ?  83  LEU   A HD21 1 
ATOM   1743 H  HD22 . LEU   A 1 83  ? 35.975 2.059   7.511   1.00 16.33 ?  83  LEU   A HD22 1 
ATOM   1744 H  HD23 . LEU   A 1 83  ? 36.242 0.498   7.385   1.00 16.33 ?  83  LEU   A HD23 1 
ATOM   1745 N  N    . SER   A 1 84  ? 33.281 1.247   10.717  1.00 12.10 ?  84  SER   A N    1 
ATOM   1746 C  CA   . SER   A 1 84  ? 32.634 1.507   11.995  1.00 12.34 ?  84  SER   A CA   1 
ATOM   1747 C  C    . SER   A 1 84  ? 31.116 1.597   11.846  1.00 12.14 ?  84  SER   A C    1 
ATOM   1748 O  O    . SER   A 1 84  ? 30.593 2.060   10.831  1.00 12.19 ?  84  SER   A O    1 
ATOM   1749 C  CB   . SER   A 1 84  ? 33.138 2.826   12.569  1.00 13.10 ?  84  SER   A CB   1 
ATOM   1750 O  OG   . SER   A 1 84  ? 32.498 3.106   13.797  1.00 14.16 ?  84  SER   A OG   1 
ATOM   1751 H  H    . SER   A 1 84  ? 33.790 1.885   10.429  1.00 14.64 ?  84  SER   A H    1 
ATOM   1752 H  HA   . SER   A 1 84  ? 32.854 0.797   12.613  1.00 14.92 ?  84  SER   A HA   1 
ATOM   1753 H  HB2  . SER   A 1 84  ? 34.097 2.768   12.713  1.00 15.84 ?  84  SER   A HB2  1 
ATOM   1754 H  HB3  . SER   A 1 84  ? 32.943 3.542   11.942  1.00 15.84 ?  84  SER   A HB3  1 
ATOM   1755 H  HG   . SER   A 1 84  ? 32.784 3.834   14.111  1.00 17.10 ?  84  SER   A HG   1 
ATOM   1756 N  N    . GLY   A 1 85  ? 30.406 1.174   12.892  1.00 13.00 ?  85  GLY   A N    1 
ATOM   1757 C  CA   . GLY   A 1 85  ? 28.983 1.414   12.983  1.00 13.55 ?  85  GLY   A CA   1 
ATOM   1758 C  C    . GLY   A 1 85  ? 28.619 2.735   13.626  1.00 13.23 ?  85  GLY   A C    1 
ATOM   1759 O  O    . GLY   A 1 85  ? 27.426 3.046   13.738  1.00 13.97 ?  85  GLY   A O    1 
ATOM   1760 H  H    . GLY   A 1 85  ? 30.738 0.740   13.560  1.00 15.71 ?  85  GLY   A H    1 
ATOM   1761 H  HA2  . GLY   A 1 85  ? 28.606 1.394   12.091  1.00 16.38 ?  85  GLY   A HA2  1 
ATOM   1762 H  HA3  . GLY   A 1 85  ? 28.578 0.701   13.498  1.00 16.38 ?  85  GLY   A HA3  1 
ATOM   1763 N  N    . HIS   A 1 86  ? 29.610 3.504   14.072  1.00 12.93 ?  86  HIS   A N    1 
ATOM   1764 C  CA   . HIS   A 1 86  ? 29.389 4.844   14.629  1.00 13.40 ?  86  HIS   A CA   1 
ATOM   1765 C  C    . HIS   A 1 86  ? 28.403 4.730   15.785  1.00 14.24 ?  86  HIS   A C    1 
ATOM   1766 O  O    . HIS   A 1 86  ? 28.579 3.850   16.644  1.00 15.36 ?  86  HIS   A O    1 
ATOM   1767 C  CB   . HIS   A 1 86  ? 29.016 5.818   13.518  1.00 13.61 ?  86  HIS   A CB   1 
ATOM   1768 C  CG   . HIS   A 1 86  ? 30.076 5.917   12.479  1.00 13.44 ?  86  HIS   A CG   1 
ATOM   1769 N  ND1  . HIS   A 1 86  ? 31.168 6.750   12.610  1.00 14.67 ?  86  HIS   A ND1  1 
ATOM   1770 C  CD2  . HIS   A 1 86  ? 30.252 5.238   11.324  1.00 12.84 ?  86  HIS   A CD2  1 
ATOM   1771 C  CE1  . HIS   A 1 86  ? 31.957 6.593   11.563  1.00 14.06 ?  86  HIS   A CE1  1 
ATOM   1772 N  NE2  . HIS   A 1 86  ? 31.434 5.670   10.777  1.00 13.42 ?  86  HIS   A NE2  1 
ATOM   1773 H  H    . HIS   A 1 86  ? 30.433 3.269   14.075  1.00 15.63 ?  86  HIS   A H    1 
ATOM   1774 H  HA   . HIS   A 1 86  ? 30.224 5.157   15.001  1.00 16.20 ?  86  HIS   A HA   1 
ATOM   1775 H  HB2  . HIS   A 1 86  ? 28.197 5.523   13.087  1.00 16.45 ?  86  HIS   A HB2  1 
ATOM   1776 H  HB3  . HIS   A 1 86  ? 28.887 6.706   13.894  1.00 16.45 ?  86  HIS   A HB3  1 
ATOM   1777 H  HD2  . HIS   A 1 86  ? 29.686 4.580   10.971  1.00 15.52 ?  86  HIS   A HD2  1 
ATOM   1778 H  HE1  . HIS   A 1 86  ? 32.751 7.047   11.395  1.00 16.99 ?  86  HIS   A HE1  1 
ATOM   1779 H  HE2  . HIS   A 1 86  ? 31.765 5.397   10.020  1.00 16.22 ?  86  HIS   A HE2  1 
ATOM   1780 N  N    . ASN   A 1 87  ? 27.390 5.583   15.854  1.00 15.16 ?  87  ASN   A N    1 
ATOM   1781 C  CA   . ASN   A 1 87  ? 26.412 5.572   16.925  1.00 16.19 ?  87  ASN   A CA   1 
ATOM   1782 C  C    . ASN   A 1 87  ? 25.278 4.586   16.689  1.00 17.32 ?  87  ASN   A C    1 
ATOM   1783 O  O    . ASN   A 1 87  ? 24.361 4.522   17.510  1.00 19.64 ?  87  ASN   A O    1 
ATOM   1784 C  CB   . ASN   A 1 87  ? 25.821 6.981   17.081  1.00 17.12 ?  87  ASN   A CB   1 
ATOM   1785 C  CG   . ASN   A 1 87  ? 25.321 7.556   15.762  1.00 17.82 ?  87  ASN   A CG   1 
ATOM   1786 O  OD1  . ASN   A 1 87  ? 25.967 7.427   14.724  1.00 18.44 ?  87  ASN   A OD1  1 
ATOM   1787 N  ND2  . ASN   A 1 87  ? 24.165 8.190   15.800  1.00 18.76 ?  87  ASN   A ND2  1 
ATOM   1788 H  H    . ASN   A 1 87  ? 27.239 6.191   15.268  1.00 18.31 ?  87  ASN   A H    1 
ATOM   1789 H  HA   . ASN   A 1 87  ? 26.838 5.327   17.763  1.00 19.55 ?  87  ASN   A HA   1 
ATOM   1790 H  HB2  . ASN   A 1 87  ? 25.070 6.944   17.703  1.00 20.66 ?  87  ASN   A HB2  1 
ATOM   1791 H  HB3  . ASN   A 1 87  ? 26.505 7.570   17.430  1.00 20.66 ?  87  ASN   A HB3  1 
ATOM   1792 H  HD21 . ASN   A 1 87  ? 23.842 8.523   15.078  1.00 22.63 ?  87  ASN   A HD21 1 
ATOM   1793 H  HD22 . ASN   A 1 87  ? 23.738 8.268   16.542  1.00 22.63 ?  87  ASN   A HD22 1 
ATOM   1794 N  N    A LEU   A 1 88  ? 25.320 3.819   15.602  0.64 15.98 ?  88  LEU   A N    1 
ATOM   1795 N  N    B LEU   A 1 88  ? 25.321 3.807   15.610  0.36 16.46 ?  88  LEU   A N    1 
ATOM   1796 C  CA   A LEU   A 1 88  ? 24.212 2.956   15.206  0.64 15.84 ?  88  LEU   A CA   1 
ATOM   1797 C  CA   B LEU   A 1 88  ? 24.203 2.956   15.220  0.36 16.31 ?  88  LEU   A CA   1 
ATOM   1798 C  C    A LEU   A 1 88  ? 24.431 1.484   15.524  0.64 15.49 ?  88  LEU   A C    1 
ATOM   1799 C  C    B LEU   A 1 88  ? 24.428 1.473   15.473  0.36 15.64 ?  88  LEU   A C    1 
ATOM   1800 O  O    A LEU   A 1 88  ? 23.455 0.761   15.755  0.64 16.52 ?  88  LEU   A O    1 
ATOM   1801 O  O    B LEU   A 1 88  ? 23.453 0.731   15.604  0.36 16.13 ?  88  LEU   A O    1 
ATOM   1802 C  CB   A LEU   A 1 88  ? 23.972 3.085   13.699  0.64 16.27 ?  88  LEU   A CB   1 
ATOM   1803 C  CB   B LEU   A 1 88  ? 23.898 3.143   13.729  0.36 16.83 ?  88  LEU   A CB   1 
ATOM   1804 C  CG   A LEU   A 1 88  ? 23.685 4.487   13.162  0.64 17.63 ?  88  LEU   A CG   1 
ATOM   1805 C  CG   B LEU   A 1 88  ? 23.627 4.582   13.284  0.36 17.60 ?  88  LEU   A CG   1 
ATOM   1806 C  CD1  A LEU   A 1 88  ? 23.548 4.444   11.649  0.64 17.80 ?  88  LEU   A CD1  1 
ATOM   1807 C  CD1  B LEU   A 1 88  ? 23.461 4.664   11.773  0.36 17.64 ?  88  LEU   A CD1  1 
ATOM   1808 C  CD2  A LEU   A 1 88  ? 22.431 5.070   13.799  0.64 19.21 ?  88  LEU   A CD2  1 
ATOM   1809 C  CD2  B LEU   A 1 88  ? 22.400 5.140   13.988  0.36 18.35 ?  88  LEU   A CD2  1 
ATOM   1810 H  H    A LEU   A 1 88  ? 25.996 3.780   15.074  0.64 19.30 ?  88  LEU   A H    1 
ATOM   1811 H  H    B LEU   A 1 88  ? 26.000 3.752   15.088  0.36 19.87 ?  88  LEU   A H    1 
ATOM   1812 H  HA   A LEU   A 1 88  ? 23.406 3.243   15.661  0.64 19.12 ?  88  LEU   A HA   1 
ATOM   1813 H  HA   B LEU   A 1 88  ? 23.415 3.226   15.718  0.36 19.68 ?  88  LEU   A HA   1 
ATOM   1814 H  HB2  A LEU   A 1 88  ? 24.756 2.762   13.235  0.64 19.64 ?  88  LEU   A HB2  1 
ATOM   1815 H  HB2  B LEU   A 1 88  ? 24.655 2.817   13.220  0.36 20.31 ?  88  LEU   A HB2  1 
ATOM   1816 H  HB3  A LEU   A 1 88  ? 23.209 2.534   13.465  0.64 19.64 ?  88  LEU   A HB3  1 
ATOM   1817 H  HB3  B LEU   A 1 88  ? 23.111 2.619   13.511  0.36 20.31 ?  88  LEU   A HB3  1 
ATOM   1818 H  HG   A LEU   A 1 88  ? 24.429 5.070   13.376  0.64 21.28 ?  88  LEU   A HG   1 
ATOM   1819 H  HG   B LEU   A 1 88  ? 24.386 5.133   13.527  0.36 21.24 ?  88  LEU   A HG   1 
ATOM   1820 H  HD11 A LEU   A 1 88  ? 23.397 5.344   11.318  0.64 21.47 ?  88  LEU   A HD11 1 
ATOM   1821 H  HD11 B LEU   A 1 88  ? 23.294 5.587   11.523  0.36 21.29 ?  88  LEU   A HD11 1 
ATOM   1822 H  HD12 A LEU   A 1 88  ? 24.364 4.084   11.268  0.64 21.47 ?  88  LEU   A HD12 1 
ATOM   1823 H  HD12 B LEU   A 1 88  ? 24.274 4.348   11.348  0.36 21.29 ?  88  LEU   A HD12 1 
ATOM   1824 H  HD13 A LEU   A 1 88  ? 22.795 3.876   11.417  0.64 21.47 ?  88  LEU   A HD13 1 
ATOM   1825 H  HD13 B LEU   A 1 88  ? 22.711 4.109   11.506  0.36 21.29 ?  88  LEU   A HD13 1 
ATOM   1826 H  HD21 A LEU   A 1 88  ? 22.229 5.920   13.378  0.64 23.17 ?  88  LEU   A HD21 1 
ATOM   1827 H  HD21 B LEU   A 1 88  ? 22.193 6.009   13.612  0.36 22.13 ?  88  LEU   A HD21 1 
ATOM   1828 H  HD22 A LEU   A 1 88  ? 21.696 4.452   13.667  0.64 23.17 ?  88  LEU   A HD22 1 
ATOM   1829 H  HD22 B LEU   A 1 88  ? 21.657 4.533   13.851  0.36 22.13 ?  88  LEU   A HD22 1 
ATOM   1830 H  HD23 A LEU   A 1 88  ? 22.592 5.199   14.746  0.64 23.17 ?  88  LEU   A HD23 1 
ATOM   1831 H  HD23 B LEU   A 1 88  ? 22.592 5.223   14.933  0.36 22.13 ?  88  LEU   A HD23 1 
ATOM   1832 N  N    . ALA   A 1 89  ? 25.679 1.026   15.521  1.00 14.96 ?  89  ALA   A N    1 
ATOM   1833 C  CA   . ALA   A 1 89  ? 26.009 -0.386  15.657  1.00 14.57 ?  89  ALA   A CA   1 
ATOM   1834 C  C    . ALA   A 1 89  ? 27.493 -0.460  15.975  1.00 15.43 ?  89  ALA   A C    1 
ATOM   1835 O  O    . ALA   A 1 89  ? 28.215 0.530   15.852  1.00 16.23 ?  89  ALA   A O    1 
ATOM   1836 C  CB   . ALA   A 1 89  ? 25.739 -1.122  14.347  1.00 14.16 ?  89  ALA   A CB   1 
ATOM   1837 H  H    A ALA   A 1 89  ? 26.370 1.531   15.436  0.64 18.06 ?  89  ALA   A H    1 
ATOM   1838 H  H    B ALA   A 1 89  ? 26.370 1.535   15.455  0.36 18.06 ?  89  ALA   A H    1 
ATOM   1839 H  HA   . ALA   A 1 89  ? 25.494 -0.786  16.376  1.00 17.60 ?  89  ALA   A HA   1 
ATOM   1840 H  HB1  . ALA   A 1 89  ? 25.984 -2.057  14.456  1.00 17.11 ?  89  ALA   A HB1  1 
ATOM   1841 H  HB2  . ALA   A 1 89  ? 24.795 -1.055  14.131  1.00 17.11 ?  89  ALA   A HB2  1 
ATOM   1842 H  HB3  . ALA   A 1 89  ? 26.270 -0.723  13.643  1.00 17.11 ?  89  ALA   A HB3  1 
ATOM   1843 N  N    . LYS   A 1 90  ? 27.960 -1.643  16.368  1.00 16.28 ?  90  LYS   A N    1 
ATOM   1844 C  CA   . LYS   A 1 90  ? 29.403 -1.807  16.520  1.00 16.76 ?  90  LYS   A CA   1 
ATOM   1845 C  C    . LYS   A 1 90  ? 30.108 -1.620  15.180  1.00 15.29 ?  90  LYS   A C    1 
ATOM   1846 O  O    . LYS   A 1 90  ? 31.042 -0.811  15.057  1.00 16.58 ?  90  LYS   A O    1 
ATOM   1847 C  CB   . LYS   A 1 90  ? 29.730 -3.172  17.130  1.00 19.45 ?  90  LYS   A CB   1 
ATOM   1848 C  CG   . LYS   A 1 90  ? 31.210 -3.336  17.461  1.00 24.60 ?  90  LYS   A CG   1 
ATOM   1849 C  CD   . LYS   A 1 90  ? 31.450 -4.540  18.360  1.00 29.65 ?  90  LYS   A CD   1 
ATOM   1850 C  CE   . LYS   A 1 90  ? 32.864 -4.547  18.928  1.00 33.15 ?  90  LYS   A CE   1 
ATOM   1851 N  NZ   . LYS   A 1 90  ? 33.895 -4.894  17.911  1.00 35.81 ?  90  LYS   A NZ   1 
ATOM   1852 H  H    . LYS   A 1 90  ? 27.481 -2.331  16.551  1.00 19.65 ?  90  LYS   A H    1 
ATOM   1853 H  HA   . LYS   A 1 90  ? 29.732 -1.127  17.125  1.00 20.22 ?  90  LYS   A HA   1 
ATOM   1854 H  HB2  . LYS   A 1 90  ? 29.223 -3.280  17.952  1.00 23.46 ?  90  LYS   A HB2  1 
ATOM   1855 H  HB3  . LYS   A 1 90  ? 29.484 -3.868  16.499  1.00 23.46 ?  90  LYS   A HB3  1 
ATOM   1856 H  HG2  . LYS   A 1 90  ? 31.710 -3.465  16.640  1.00 29.64 ?  90  LYS   A HG2  1 
ATOM   1857 H  HG3  . LYS   A 1 90  ? 31.523 -2.543  17.924  1.00 29.64 ?  90  LYS   A HG3  1 
ATOM   1858 H  HD2  . LYS   A 1 90  ? 30.825 -4.515  19.103  1.00 35.69 ?  90  LYS   A HD2  1 
ATOM   1859 H  HD3  . LYS   A 1 90  ? 31.325 -5.354  17.847  1.00 35.69 ?  90  LYS   A HD3  1 
ATOM   1860 H  HE2  . LYS   A 1 90  ? 33.070 -3.664  19.273  1.00 39.89 ?  90  LYS   A HE2  1 
ATOM   1861 H  HE3  . LYS   A 1 90  ? 32.915 -5.202  19.642  1.00 39.89 ?  90  LYS   A HE3  1 
ATOM   1862 H  HZ1  . LYS   A 1 90  ? 33.736 -5.706  17.581  1.00 43.09 ?  90  LYS   A HZ1  1 
ATOM   1863 H  HZ2  . LYS   A 1 90  ? 33.879 -4.304  17.246  1.00 43.09 ?  90  LYS   A HZ2  1 
ATOM   1864 H  HZ3  . LYS   A 1 90  ? 34.704 -4.888  18.284  1.00 43.09 ?  90  LYS   A HZ3  1 
ATOM   1865 N  N    . HIS   A 1 91  ? 29.645 -2.336  14.156  1.00 13.31 ?  91  HIS   A N    1 
ATOM   1866 C  CA   . HIS   A 1 91  ? 30.225 -2.321  12.829  1.00 12.98 ?  91  HIS   A CA   1 
ATOM   1867 C  C    . HIS   A 1 91  ? 29.144 -2.043  11.800  1.00 11.96 ?  91  HIS   A C    1 
ATOM   1868 O  O    . HIS   A 1 91  ? 27.978 -2.395  11.991  1.00 12.70 ?  91  HIS   A O    1 
ATOM   1869 C  CB   . HIS   A 1 91  ? 30.820 -3.684  12.468  1.00 15.31 ?  91  HIS   A CB   1 
ATOM   1870 C  CG   . HIS   A 1 91  ? 31.812 -4.199  13.459  1.00 19.93 ?  91  HIS   A CG   1 
ATOM   1871 N  ND1  . HIS   A 1 91  ? 33.097 -3.708  13.549  1.00 21.96 ?  91  HIS   A ND1  1 
ATOM   1872 C  CD2  . HIS   A 1 91  ? 31.718 -5.175  14.392  1.00 21.59 ?  91  HIS   A CD2  1 
ATOM   1873 C  CE1  . HIS   A 1 91  ? 33.749 -4.355  14.499  1.00 23.08 ?  91  HIS   A CE1  1 
ATOM   1874 N  NE2  . HIS   A 1 91  ? 32.935 -5.252  15.026  1.00 23.03 ?  91  HIS   A NE2  1 
ATOM   1875 H  H    . HIS   A 1 91  ? 28.963 -2.873  14.219  1.00 16.09 ?  91  HIS   A H    1 
ATOM   1876 H  HA   . HIS   A 1 91  ? 30.914 -1.643  12.771  1.00 15.69 ?  91  HIS   A HA   1 
ATOM   1877 H  HB2  . HIS   A 1 91  ? 30.102 -4.334  12.410  1.00 18.49 ?  91  HIS   A HB2  1 
ATOM   1878 H  HB3  . HIS   A 1 91  ? 31.268 -3.613  11.611  1.00 18.49 ?  91  HIS   A HB3  1 
ATOM   1879 H  HD1  . HIS   A 1 91  ? 33.425 -3.076  13.061  1.00 26.47 ?  91  HIS   A HD1  1 
ATOM   1880 H  HD2  . HIS   A 1 91  ? 30.975 -5.696  14.574  1.00 26.02 ?  91  HIS   A HD2  1 
ATOM   1881 H  HE1  . HIS   A 1 91  ? 34.635 -4.199  14.751  1.00 27.81 ?  91  HIS   A HE1  1 
ATOM   1882 N  N    . CYS   A 1 92  ? 29.556 -1.449  10.685  1.00 11.48 ?  92  CYS   A N    1 
ATOM   1883 C  CA   . CYS   A 1 92  ? 28.728 -1.369  9.490   1.00 11.18 ?  92  CYS   A CA   1 
ATOM   1884 C  C    . CYS   A 1 92  ? 29.377 -2.192  8.384   1.00 11.05 ?  92  CYS   A C    1 
ATOM   1885 O  O    . CYS   A 1 92  ? 30.540 -1.943  8.022   1.00 11.63 ?  92  CYS   A O    1 
ATOM   1886 C  CB   . CYS   A 1 92  ? 28.520 0.073   9.027   1.00 11.51 ?  92  CYS   A CB   1 
ATOM   1887 S  SG   . CYS   A 1 92  ? 27.505 0.181   7.512   1.00 11.16 ?  92  CYS   A SG   1 
ATOM   1888 H  H    . CYS   A 1 92  ? 30.331 -1.080  10.594  1.00 13.89 ?  92  CYS   A H    1 
ATOM   1889 H  HA   . CYS   A 1 92  ? 27.858 -1.748  9.682   1.00 13.53 ?  92  CYS   A HA   1 
ATOM   1890 H  HB2  . CYS   A 1 92  ? 28.069 0.574   9.727   1.00 13.92 ?  92  CYS   A HB2  1 
ATOM   1891 H  HB3  . CYS   A 1 92  ? 29.382 0.476   8.835   1.00 13.92 ?  92  CYS   A HB3  1 
ATOM   1892 H  HG   . CYS   A 1 92  ? 27.370 1.332   7.218   1.00 13.51 ?  92  CYS   A HG   1 
ATOM   1893 N  N    . LEU   A 1 93  ? 28.637 -3.178  7.875   1.00 10.81 ?  93  LEU   A N    1 
ATOM   1894 C  CA   . LEU   A 1 93  ? 29.043 -3.937  6.698   1.00 10.36 ?  93  LEU   A CA   1 
ATOM   1895 C  C    . LEU   A 1 93  ? 28.455 -3.248  5.471   1.00 10.02 ?  93  LEU   A C    1 
ATOM   1896 O  O    . LEU   A 1 93  ? 27.243 -3.299  5.245   1.00 10.19 ?  93  LEU   A O    1 
ATOM   1897 C  CB   . LEU   A 1 93  ? 28.556 -5.382  6.804   1.00 11.16 ?  93  LEU   A CB   1 
ATOM   1898 C  CG   . LEU   A 1 93  ? 28.947 -6.289  5.635   1.00 11.58 ?  93  LEU   A CG   1 
ATOM   1899 C  CD1  . LEU   A 1 93  ? 30.455 -6.554  5.630   1.00 12.17 ?  93  LEU   A CD1  1 
ATOM   1900 C  CD2  . LEU   A 1 93  ? 28.173 -7.612  5.673   1.00 12.28 ?  93  LEU   A CD2  1 
ATOM   1901 H  H    . LEU   A 1 93  ? 27.878 -3.423  8.206   1.00 13.09 ?  93  LEU   A H    1 
ATOM   1902 H  HA   . LEU   A 1 93  ? 30.005 -3.929  6.630   1.00 12.55 ?  93  LEU   A HA   1 
ATOM   1903 H  HB2  . LEU   A 1 93  ? 28.927 -5.767  7.614   1.00 13.50 ?  93  LEU   A HB2  1 
ATOM   1904 H  HB3  . LEU   A 1 93  ? 27.591 -5.379  6.859   1.00 13.50 ?  93  LEU   A HB3  1 
ATOM   1905 H  HG   . LEU   A 1 93  ? 28.733 -5.848  4.806   1.00 14.01 ?  93  LEU   A HG   1 
ATOM   1906 H  HD11 . LEU   A 1 93  ? 30.671 -7.168  4.911   1.00 14.71 ?  93  LEU   A HD11 1 
ATOM   1907 H  HD12 . LEU   A 1 93  ? 30.927 -5.717  5.504   1.00 14.71 ?  93  LEU   A HD12 1 
ATOM   1908 H  HD13 . LEU   A 1 93  ? 30.714 -6.950  6.484   1.00 14.71 ?  93  LEU   A HD13 1 
ATOM   1909 H  HD21 . LEU   A 1 93  ? 28.451 -8.160  4.921   1.00 14.85 ?  93  LEU   A HD21 1 
ATOM   1910 H  HD22 . LEU   A 1 93  ? 28.366 -8.069  6.505   1.00 14.85 ?  93  LEU   A HD22 1 
ATOM   1911 H  HD23 . LEU   A 1 93  ? 27.226 -7.418  5.610   1.00 14.85 ?  93  LEU   A HD23 1 
ATOM   1912 N  N    . HIS   A 1 94  ? 29.307 -2.560  4.709   1.00 9.80  ?  94  HIS   A N    1 
ATOM   1913 C  CA   . HIS   A 1 94  ? 28.885 -1.883  3.484   1.00 9.71  ?  94  HIS   A CA   1 
ATOM   1914 C  C    . HIS   A 1 94  ? 28.898 -2.915  2.370   1.00 9.90  ?  94  HIS   A C    1 
ATOM   1915 O  O    . HIS   A 1 94  ? 29.962 -3.434  2.030   1.00 11.35 ?  94  HIS   A O    1 
ATOM   1916 C  CB   . HIS   A 1 94  ? 29.847 -0.739  3.159   1.00 10.13 ?  94  HIS   A CB   1 
ATOM   1917 C  CG   . HIS   A 1 94  ? 29.831 0.355   4.173   1.00 9.68  ?  94  HIS   A CG   1 
ATOM   1918 N  ND1  . HIS   A 1 94  ? 28.961 1.425   4.114   1.00 10.05 ?  94  HIS   A ND1  1 
ATOM   1919 C  CD2  . HIS   A 1 94  ? 30.567 0.522   5.294   1.00 10.48 ?  94  HIS   A CD2  1 
ATOM   1920 C  CE1  . HIS   A 1 94  ? 29.173 2.201   5.160   1.00 10.15 ?  94  HIS   A CE1  1 
ATOM   1921 N  NE2  . HIS   A 1 94  ? 30.146 1.681   5.887   1.00 10.59 ?  94  HIS   A NE2  1 
ATOM   1922 H  H    . HIS   A 1 94  ? 30.145 -2.465  4.881   1.00 11.88 ?  94  HIS   A H    1 
ATOM   1923 H  HA   . HIS   A 1 94  ? 27.982 -1.531  3.585   1.00 11.77 ?  94  HIS   A HA   1 
ATOM   1924 H  HB2  . HIS   A 1 94  ? 30.741 -1.089  3.111   1.00 12.27 ?  94  HIS   A HB2  1 
ATOM   1925 H  HB3  . HIS   A 1 94  ? 29.588 -0.351  2.305   1.00 12.27 ?  94  HIS   A HB3  1 
ATOM   1926 H  HD2  . HIS   A 1 94  ? 31.239 -0.034  5.604   1.00 12.69 ?  94  HIS   A HD2  1 
ATOM   1927 H  HE1  . HIS   A 1 94  ? 28.708 2.990   5.344   1.00 12.29 ?  94  HIS   A HE1  1 
ATOM   1928 H  HE2  . HIS   A 1 94  ? 30.454 2.024   6.611   1.00 12.83 ?  94  HIS   A HE2  1 
ATOM   1929 N  N    . VAL   A 1 95  ? 27.729 -3.241  1.822   1.00 9.19  ?  95  VAL   A N    1 
ATOM   1930 C  CA   . VAL   A 1 95  ? 27.585 -4.279  0.804   1.00 9.86  ?  95  VAL   A CA   1 
ATOM   1931 C  C    . VAL   A 1 95  ? 27.037 -3.641  -0.461  1.00 9.56  ?  95  VAL   A C    1 
ATOM   1932 O  O    . VAL   A 1 95  ? 26.034 -2.920  -0.407  1.00 10.12 ?  95  VAL   A O    1 
ATOM   1933 C  CB   . VAL   A 1 95  ? 26.653 -5.422  1.254   1.00 10.30 ?  95  VAL   A CB   1 
ATOM   1934 C  CG1  . VAL   A 1 95  ? 26.553 -6.465  0.152   1.00 11.03 ?  95  VAL   A CG1  1 
ATOM   1935 C  CG2  . VAL   A 1 95  ? 27.149 -6.035  2.548   1.00 11.00 ?  95  VAL   A CG2  1 
ATOM   1936 H  H    . VAL   A 1 95  ? 26.980 -2.871  2.034   1.00 11.14 ?  95  VAL   A H    1 
ATOM   1937 H  HA   . VAL   A 1 95  ? 28.454 -4.653  0.597   1.00 11.95 ?  95  VAL   A HA   1 
ATOM   1938 H  HB   . VAL   A 1 95  ? 25.769 -5.069  1.408   1.00 12.48 ?  95  VAL   A HB   1 
ATOM   1939 H  HG11 . VAL   A 1 95  ? 26.162 -7.278  0.518   1.00 13.35 ?  95  VAL   A HG11 1 
ATOM   1940 H  HG12 . VAL   A 1 95  ? 25.992 -6.129  -0.564  1.00 13.35 ?  95  VAL   A HG12 1 
ATOM   1941 H  HG13 . VAL   A 1 95  ? 27.443 -6.661  -0.189  1.00 13.35 ?  95  VAL   A HG13 1 
ATOM   1942 H  HG21 . VAL   A 1 95  ? 26.583 -6.793  2.772   1.00 13.32 ?  95  VAL   A HG21 1 
ATOM   1943 H  HG22 . VAL   A 1 95  ? 28.064 -6.331  2.430   1.00 13.32 ?  95  VAL   A HG22 1 
ATOM   1944 H  HG23 . VAL   A 1 95  ? 27.101 -5.369  3.249   1.00 13.32 ?  95  VAL   A HG23 1 
ATOM   1945 N  N    . VAL   A 1 96  ? 27.665 -3.930  -1.598  1.00 9.49  ?  96  VAL   A N    1 
ATOM   1946 C  CA   . VAL   A 1 96  ? 27.265 -3.380  -2.887  1.00 10.08 ?  96  VAL   A CA   1 
ATOM   1947 C  C    . VAL   A 1 96  ? 26.455 -4.430  -3.643  1.00 10.38 ?  96  VAL   A C    1 
ATOM   1948 O  O    . VAL   A 1 96  ? 27.011 -5.381  -4.202  1.00 11.58 ?  96  VAL   A O    1 
ATOM   1949 C  CB   . VAL   A 1 96  ? 28.463 -2.906  -3.710  1.00 10.64 ?  96  VAL   A CB   1 
ATOM   1950 C  CG1  . VAL   A 1 96  ? 27.964 -2.270  -4.984  1.00 10.72 ?  96  VAL   A CG1  1 
ATOM   1951 C  CG2  . VAL   A 1 96  ? 29.327 -1.934  -2.914  1.00 11.31 ?  96  VAL   A CG2  1 
ATOM   1952 H  H    . VAL   A 1 96  ? 28.350 -4.458  -1.645  1.00 11.50 ?  96  VAL   A H    1 
ATOM   1953 H  HA   . VAL   A 1 96  ? 26.693 -2.612  -2.728  1.00 12.21 ?  96  VAL   A HA   1 
ATOM   1954 H  HB   . VAL   A 1 96  ? 29.009 -3.666  -3.945  1.00 12.88 ?  96  VAL   A HB   1 
ATOM   1955 H  HG11 . VAL   A 1 96  ? 28.703 -1.796  -5.405  1.00 12.98 ?  96  VAL   A HG11 1 
ATOM   1956 H  HG12 . VAL   A 1 96  ? 27.634 -2.956  -5.575  1.00 12.98 ?  96  VAL   A HG12 1 
ATOM   1957 H  HG13 . VAL   A 1 96  ? 27.257 -1.640  -4.768  1.00 12.98 ?  96  VAL   A HG13 1 
ATOM   1958 H  HG21 . VAL   A 1 96  ? 30.037 -1.598  -3.480  1.00 13.69 ?  96  VAL   A HG21 1 
ATOM   1959 H  HG22 . VAL   A 1 96  ? 28.775 -1.194  -2.604  1.00 13.69 ?  96  VAL   A HG22 1 
ATOM   1960 H  HG23 . VAL   A 1 96  ? 29.707 -2.398  -2.148  1.00 13.69 ?  96  VAL   A HG23 1 
ATOM   1961 N  N    . GLY   A 1 97  ? 25.138 -4.259  -3.682  1.00 10.43 ?  97  GLY   A N    1 
ATOM   1962 C  CA   . GLY   A 1 97  ? 24.320 -5.021  -4.588  1.00 11.17 ?  97  GLY   A CA   1 
ATOM   1963 C  C    . GLY   A 1 97  ? 24.322 -4.370  -5.958  1.00 11.27 ?  97  GLY   A C    1 
ATOM   1964 O  O    . GLY   A 1 97  ? 24.605 -3.176  -6.098  1.00 12.31 ?  97  GLY   A O    1 
ATOM   1965 H  H    . GLY   A 1 97  ? 24.702 -3.694  -3.189  1.00 12.64 ?  97  GLY   A H    1 
ATOM   1966 H  HA2  . GLY   A 1 97  ? 24.677 -5.920  -4.656  1.00 13.52 ?  97  GLY   A HA2  1 
ATOM   1967 H  HA3  . GLY   A 1 97  ? 23.413 -5.066  -4.248  1.00 13.52 ?  97  GLY   A HA3  1 
ATOM   1968 N  N    . PRO   A 1 98  ? 24.005 -5.132  -6.998  1.00 11.02 ?  98  PRO   A N    1 
ATOM   1969 C  CA   . PRO   A 1 98  ? 23.905 -4.532  -8.332  1.00 12.76 ?  98  PRO   A CA   1 
ATOM   1970 C  C    . PRO   A 1 98  ? 22.787 -3.499  -8.404  1.00 13.01 ?  98  PRO   A C    1 
ATOM   1971 O  O    . PRO   A 1 98  ? 21.709 -3.670  -7.829  1.00 12.80 ?  98  PRO   A O    1 
ATOM   1972 C  CB   . PRO   A 1 98  ? 23.620 -5.735  -9.239  1.00 13.05 ?  98  PRO   A CB   1 
ATOM   1973 C  CG   . PRO   A 1 98  ? 22.971 -6.738  -8.335  1.00 13.16 ?  98  PRO   A CG   1 
ATOM   1974 C  CD   . PRO   A 1 98  ? 23.696 -6.574  -7.015  1.00 11.77 ?  98  PRO   A CD   1 
ATOM   1975 H  HA   . PRO   A 1 98  ? 24.749 -4.124  -8.578  1.00 15.42 ?  98  PRO   A HA   1 
ATOM   1976 H  HB2  . PRO   A 1 98  ? 23.016 -5.466  -9.947  1.00 15.77 ?  98  PRO   A HB2  1 
ATOM   1977 H  HB3  . PRO   A 1 98  ? 24.450 -6.077  -9.596  1.00 15.77 ?  98  PRO   A HB3  1 
ATOM   1978 H  HG2  . PRO   A 1 98  ? 22.028 -6.530  -8.236  1.00 15.91 ?  98  PRO   A HG2  1 
ATOM   1979 H  HG3  . PRO   A 1 98  ? 23.097 -7.628  -8.690  1.00 15.91 ?  98  PRO   A HG3  1 
ATOM   1980 H  HD2  . PRO   A 1 98  ? 23.113 -6.812  -6.274  1.00 14.24 ?  98  PRO   A HD2  1 
ATOM   1981 H  HD3  . PRO   A 1 98  ? 24.513 -7.098  -7.006  1.00 14.24 ?  98  PRO   A HD3  1 
ATOM   1982 N  N    A ASN   A 1 99  ? 23.068 -2.375  -9.072  0.64 13.63 ?  99  ASN   A N    1 
ATOM   1983 N  N    B ASN   A 1 99  ? 23.058 -2.448  -9.162  0.36 14.23 ?  99  ASN   A N    1 
ATOM   1984 C  CA   A ASN   A 1 99  ? 22.092 -1.292  -9.253  0.64 14.40 ?  99  ASN   A CA   1 
ATOM   1985 C  CA   B ASN   A 1 99  ? 22.060 -1.454  -9.518  0.36 15.36 ?  99  ASN   A CA   1 
ATOM   1986 C  C    A ASN   A 1 99  ? 21.534 -1.400  -10.668 0.64 15.13 ?  99  ASN   A C    1 
ATOM   1987 C  C    B ASN   A 1 99  ? 21.473 -1.844  -10.870 0.36 16.12 ?  99  ASN   A C    1 
ATOM   1988 O  O    A ASN   A 1 99  ? 22.201 -1.043  -11.644 0.64 15.77 ?  99  ASN   A O    1 
ATOM   1989 O  O    B ASN   A 1 99  ? 22.176 -1.843  -11.887 0.36 15.68 ?  99  ASN   A O    1 
ATOM   1990 C  CB   A ASN   A 1 99  ? 22.715 0.081   -9.005  0.64 14.09 ?  99  ASN   A CB   1 
ATOM   1991 C  CB   B ASN   A 1 99  ? 22.721 -0.085  -9.590  0.36 16.05 ?  99  ASN   A CB   1 
ATOM   1992 C  CG   A ASN   A 1 99  ? 21.677 1.218   -8.990  0.64 13.60 ?  99  ASN   A CG   1 
ATOM   1993 C  CG   B ASN   A 1 99  ? 21.724 1.026   -9.783  0.36 16.66 ?  99  ASN   A CG   1 
ATOM   1994 O  OD1  A ASN   A 1 99  ? 20.685 1.180   -9.720  0.64 14.00 ?  99  ASN   A OD1  1 
ATOM   1995 O  OD1  B ASN   A 1 99  ? 20.814 0.921   -10.600 0.36 16.94 ?  99  ASN   A OD1  1 
ATOM   1996 N  ND2  A ASN   A 1 99  ? 21.925 2.244   -8.171  0.64 13.92 ?  99  ASN   A ND2  1 
ATOM   1997 N  ND2  B ASN   A 1 99  ? 21.885 2.100   -9.023  0.36 16.94 ?  99  ASN   A ND2  1 
ATOM   1998 H  H    A ASN   A 1 99  ? 23.835 -2.207  -9.425  0.64 16.47 ?  99  ASN   A H    1 
ATOM   1999 H  H    B ASN   A 1 99  ? 23.840 -2.282  -9.479  0.36 17.20 ?  99  ASN   A H    1 
ATOM   2000 H  HA   A ASN   A 1 99  ? 21.364 -1.407  -8.618  0.64 17.40 ?  99  ASN   A HA   1 
ATOM   2001 H  HA   B ASN   A 1 99  ? 21.354 -1.441  -8.848  0.36 18.55 ?  99  ASN   A HA   1 
ATOM   2002 H  HB2  A ASN   A 1 99  ? 23.169 0.081   -8.151  0.64 17.03 ?  99  ASN   A HB2  1 
ATOM   2003 H  HB2  B ASN   A 1 99  ? 23.203 0.076   -8.765  0.36 19.38 ?  99  ASN   A HB2  1 
ATOM   2004 H  HB3  A ASN   A 1 99  ? 23.350 0.271   -9.717  0.64 17.03 ?  99  ASN   A HB3  1 
ATOM   2005 H  HB3  B ASN   A 1 99  ? 23.336 -0.078  -10.341 0.36 19.38 ?  99  ASN   A HB3  1 
ATOM   2006 H  HD21 A ASN   A 1 99  ? 21.374 2.905   -8.126  0.64 16.82 ?  99  ASN   A HD21 1 
ATOM   2007 H  HD21 B ASN   A 1 99  ? 21.342 2.759   -9.093  0.36 20.45 ?  99  ASN   A HD21 1 
ATOM   2008 H  HD22 A ASN   A 1 99  ? 22.630 2.240   -7.681  0.64 16.82 ?  99  ASN   A HD22 1 
ATOM   2009 H  HD22 B ASN   A 1 99  ? 22.531 2.130   -8.457  0.36 20.45 ?  99  ASN   A HD22 1 
ATOM   2010 N  N    A VAL   A 1 100 ? 20.295 -1.894  -10.769 0.64 16.19 ?  100 VAL   A N    1 
ATOM   2011 N  N    B VAL   A 1 100 ? 20.184 -2.190  -10.870 0.36 17.53 ?  100 VAL   A N    1 
ATOM   2012 C  CA   A VAL   A 1 100 ? 19.670 -2.103  -12.073 0.64 17.71 ?  100 VAL   A CA   1 
ATOM   2013 C  CA   B VAL   A 1 100 ? 19.492 -2.562  -12.101 0.36 19.33 ?  100 VAL   A CA   1 
ATOM   2014 C  C    A VAL   A 1 100 ? 19.502 -0.786  -12.819 0.64 17.42 ?  100 VAL   A C    1 
ATOM   2015 C  C    B VAL   A 1 100 ? 19.600 -1.454  -13.135 0.36 20.00 ?  100 VAL   A C    1 
ATOM   2016 O  O    A VAL   A 1 100 ? 19.547 -0.755  -14.054 0.64 18.36 ?  100 VAL   A O    1 
ATOM   2017 O  O    B VAL   A 1 100 ? 19.783 -1.713  -14.332 0.36 20.09 ?  100 VAL   A O    1 
ATOM   2018 C  CB   A VAL   A 1 100 ? 18.343 -2.874  -11.915 0.64 19.71 ?  100 VAL   A CB   1 
ATOM   2019 C  CB   B VAL   A 1 100 ? 18.021 -2.892  -11.789 0.36 20.30 ?  100 VAL   A CB   1 
ATOM   2020 C  CG1  A VAL   A 1 100 ? 17.684 -3.116  -13.269 0.64 20.64 ?  100 VAL   A CG1  1 
ATOM   2021 C  CG1  B VAL   A 1 100 ? 17.144 -2.682  -13.019 0.36 20.52 ?  100 VAL   A CG1  1 
ATOM   2022 C  CG2  A VAL   A 1 100 ? 18.591 -4.197  -11.204 0.64 19.88 ?  100 VAL   A CG2  1 
ATOM   2023 C  CG2  B VAL   A 1 100 ? 17.899 -4.304  -11.274 0.36 20.61 ?  100 VAL   A CG2  1 
ATOM   2024 H  H    A VAL   A 1 100 ? 19.799 -2.123  -10.098 0.64 19.54 ?  100 VAL   A H    1 
ATOM   2025 H  H    B VAL   A 1 100 ? 19.693 -2.221  -10.167 0.36 21.16 ?  100 VAL   A H    1 
ATOM   2026 H  HA   A VAL   A 1 100 ? 20.258 -2.656  -12.603 0.64 21.37 ?  100 VAL   A HA   1 
ATOM   2027 H  HA   B VAL   A 1 100 ? 19.906 -3.354  -12.472 0.36 23.31 ?  100 VAL   A HA   1 
ATOM   2028 H  HB   A VAL   A 1 100 ? 17.730 -2.355  -11.373 0.64 23.77 ?  100 VAL   A HB   1 
ATOM   2029 H  HB   B VAL   A 1 100 ? 17.713 -2.292  -11.095 0.36 24.48 ?  100 VAL   A HB   1 
ATOM   2030 H  HG11 A VAL   A 1 100 ? 16.939 -3.728  -13.155 0.64 24.89 ?  100 VAL   A HG11 1 
ATOM   2031 H  HG11 B VAL   A 1 100 ? 16.294 -3.123  -12.871 0.36 24.74 ?  100 VAL   A HG11 1 
ATOM   2032 H  HG12 A VAL   A 1 100 ? 17.365 -2.271  -13.622 0.64 24.89 ?  100 VAL   A HG12 1 
ATOM   2033 H  HG12 B VAL   A 1 100 ? 16.996 -1.730  -13.154 0.36 24.74 ?  100 VAL   A HG12 1 
ATOM   2034 H  HG13 A VAL   A 1 100 ? 18.338 -3.503  -13.874 0.64 24.89 ?  100 VAL   A HG13 1 
ATOM   2035 H  HG13 B VAL   A 1 100 ? 17.583 -3.065  -13.793 0.36 24.74 ?  100 VAL   A HG13 1 
ATOM   2036 H  HG21 A VAL   A 1 100 ? 17.774 -4.720  -11.213 0.64 23.97 ?  100 VAL   A HG21 1 
ATOM   2037 H  HG21 B VAL   A 1 100 ? 16.967 -4.491  -11.090 0.36 24.85 ?  100 VAL   A HG21 1 
ATOM   2038 H  HG22 A VAL   A 1 100 ? 19.295 -4.677  -11.668 0.64 23.97 ?  100 VAL   A HG22 1 
ATOM   2039 H  HG22 B VAL   A 1 100 ? 18.234 -4.913  -11.950 0.36 24.85 ?  100 VAL   A HG22 1 
ATOM   2040 H  HG23 A VAL   A 1 100 ? 18.860 -4.020  -10.289 0.64 23.97 ?  100 VAL   A HG23 1 
ATOM   2041 H  HG23 B VAL   A 1 100 ? 18.423 -4.388  -10.462 0.36 24.85 ?  100 VAL   A HG23 1 
ATOM   2042 N  N    A ASN   A 1 101 ? 19.311 0.318   -12.100 0.64 17.98 ?  101 ASN   A N    1 
ATOM   2043 N  N    B ASN   A 1 101 ? 19.453 -0.204  -12.696 0.36 20.68 ?  101 ASN   A N    1 
ATOM   2044 C  CA   A ASN   A 1 101 ? 19.222 1.605   -12.780 0.64 18.98 ?  101 ASN   A CA   1 
ATOM   2045 C  CA   B ASN   A 1 101 ? 19.415 0.921   -13.620 0.36 21.26 ?  101 ASN   A CA   1 
ATOM   2046 C  C    A ASN   A 1 101 ? 20.564 2.067   -13.347 0.64 21.03 ?  101 ASN   A C    1 
ATOM   2047 C  C    B ASN   A 1 101 ? 20.762 1.174   -14.279 0.36 22.07 ?  101 ASN   A C    1 
ATOM   2048 O  O    A ASN   A 1 101 ? 20.607 3.117   -14.001 0.64 22.61 ?  101 ASN   A O    1 
ATOM   2049 O  O    B ASN   A 1 101 ? 20.808 1.820   -15.331 0.36 21.91 ?  101 ASN   A O    1 
ATOM   2050 C  CB   A ASN   A 1 101 ? 18.588 2.640   -11.850 0.64 18.62 ?  101 ASN   A CB   1 
ATOM   2051 C  CB   B ASN   A 1 101 ? 18.935 2.168   -12.877 0.36 21.28 ?  101 ASN   A CB   1 
ATOM   2052 C  CG   A ASN   A 1 101 ? 17.197 2.215   -11.379 0.64 18.29 ?  101 ASN   A CG   1 
ATOM   2053 C  CG   B ASN   A 1 101 ? 17.716 1.894   -12.013 0.36 21.55 ?  101 ASN   A CG   1 
ATOM   2054 O  OD1  A ASN   A 1 101 ? 16.397 1.695   -12.159 0.64 18.36 ?  101 ASN   A OD1  1 
ATOM   2055 O  OD1  B ASN   A 1 101 ? 16.792 1.191   -12.425 0.36 21.98 ?  101 ASN   A OD1  1 
ATOM   2056 N  ND2  A ASN   A 1 101 ? 16.916 2.411   -10.100 0.64 18.11 ?  101 ASN   A ND2  1 
ATOM   2057 N  ND2  B ASN   A 1 101 ? 17.717 2.433   -10.801 0.36 21.71 ?  101 ASN   A ND2  1 
ATOM   2058 H  H    A ASN   A 1 101 ? 19.223 0.351   -11.247 0.64 21.69 ?  101 ASN   A H    1 
ATOM   2059 H  H    B ASN   A 1 101 ? 19.369 0.018   -11.870 0.36 24.94 ?  101 ASN   A H    1 
ATOM   2060 H  HA   A ASN   A 1 101 ? 18.626 1.503   -13.535 0.64 22.90 ?  101 ASN   A HA   1 
ATOM   2061 H  HA   B ASN   A 1 101 ? 18.777 0.735   -14.324 0.36 25.63 ?  101 ASN   A HA   1 
ATOM   2062 H  HB2  A ASN   A 1 101 ? 19.151 2.757   -11.071 0.64 22.46 ?  101 ASN   A HB2  1 
ATOM   2063 H  HB2  B ASN   A 1 101 ? 19.645 2.491   -12.301 0.36 25.65 ?  101 ASN   A HB2  1 
ATOM   2064 H  HB3  A ASN   A 1 101 ? 18.505 3.485   -12.329 0.64 22.46 ?  101 ASN   A HB3  1 
ATOM   2065 H  HB3  B ASN   A 1 101 ? 18.695 2.853   -13.523 0.36 25.65 ?  101 ASN   A HB3  1 
ATOM   2066 H  HD21 A ASN   A 1 101 ? 16.144 2.189   -9.794  0.64 21.85 ?  101 ASN   A HD21 1 
ATOM   2067 H  HD21 B ASN   A 1 101 ? 17.050 2.305   -10.274 0.36 26.17 ?  101 ASN   A HD21 1 
ATOM   2068 H  HD22 A ASN   A 1 101 ? 17.498 2.772   -9.583  0.64 21.85 ?  101 ASN   A HD22 1 
ATOM   2069 H  HD22 B ASN   A 1 101 ? 18.379 2.919   -10.547 0.36 26.17 ?  101 ASN   A HD22 1 
ATOM   2070 N  N    A LYS   A 1 102 ? 21.637 1.294   -13.136 0.64 22.98 ?  102 LYS   A N    1 
ATOM   2071 N  N    B LYS   A 1 102 ? 21.850 0.682   -13.693 0.36 23.25 ?  102 LYS   A N    1 
ATOM   2072 C  CA   A LYS   A 1 102 ? 22.923 1.500   -13.792 0.64 24.76 ?  102 LYS   A CA   1 
ATOM   2073 C  CA   B LYS   A 1 102 ? 23.180 0.806   -14.272 0.36 24.18 ?  102 LYS   A CA   1 
ATOM   2074 C  C    A LYS   A 1 102 ? 23.244 0.422   -14.818 0.64 25.59 ?  102 LYS   A C    1 
ATOM   2075 C  C    B LYS   A 1 102 ? 23.537 -0.377  -15.164 0.36 23.18 ?  102 LYS   A C    1 
ATOM   2076 O  O    A LYS   A 1 102 ? 24.298 0.498   -15.458 0.64 26.09 ?  102 LYS   A O    1 
ATOM   2077 O  O    B LYS   A 1 102 ? 24.692 -0.497  -15.583 0.36 22.96 ?  102 LYS   A O    1 
ATOM   2078 C  CB   A LYS   A 1 102 ? 24.057 1.547   -12.759 0.64 26.21 ?  102 LYS   A CB   1 
ATOM   2079 C  CB   B LYS   A 1 102 ? 24.232 0.943   -13.166 0.36 25.88 ?  102 LYS   A CB   1 
ATOM   2080 C  CG   A LYS   A 1 102 ? 23.953 2.668   -11.746 0.64 27.35 ?  102 LYS   A CG   1 
ATOM   2081 C  CG   B LYS   A 1 102 ? 24.026 2.134   -12.241 0.36 27.53 ?  102 LYS   A CG   1 
ATOM   2082 C  CD   A LYS   A 1 102 ? 25.113 2.606   -10.762 0.64 28.70 ?  102 LYS   A CD   1 
ATOM   2083 C  CD   B LYS   A 1 102 ? 25.186 2.286   -11.263 0.36 29.05 ?  102 LYS   A CD   1 
ATOM   2084 C  CE   A LYS   A 1 102 ? 25.029 3.708   -9.721  0.64 29.69 ?  102 LYS   A CE   1 
ATOM   2085 C  CE   B LYS   A 1 102 ? 24.998 3.493   -10.357 0.36 30.30 ?  102 LYS   A CE   1 
ATOM   2086 N  NZ   A LYS   A 1 102 ? 26.108 3.578   -8.700  0.64 30.31 ?  102 LYS   A NZ   1 
ATOM   2087 N  NZ   B LYS   A 1 102 ? 26.255 3.858   -9.643  0.36 30.94 ?  102 LYS   A NZ   1 
ATOM   2088 H  H    A LYS   A 1 102 ? 21.641 0.613   -12.607 0.64 27.69 ?  102 LYS   A H    1 
ATOM   2089 H  H    B LYS   A 1 102 ? 21.841 0.260   -12.945 0.36 28.02 ?  102 LYS   A H    1 
ATOM   2090 H  HA   A LYS   A 1 102 ? 22.913 2.339   -14.263 0.64 29.83 ?  102 LYS   A HA   1 
ATOM   2091 H  HA   B LYS   A 1 102 ? 23.213 1.617   -14.805 0.36 29.13 ?  102 LYS   A HA   1 
ATOM   2092 H  HB2  A LYS   A 1 102 ? 24.065 0.709   -12.270 0.64 31.56 ?  102 LYS   A HB2  1 
ATOM   2093 H  HB2  B LYS   A 1 102 ? 24.211 0.144   -12.620 0.36 31.17 ?  102 LYS   A HB2  1 
ATOM   2094 H  HB3  A LYS   A 1 102 ? 24.899 1.654   -13.230 0.64 31.56 ?  102 LYS   A HB3  1 
ATOM   2095 H  HB3  B LYS   A 1 102 ? 25.108 1.036   -13.577 0.36 31.17 ?  102 LYS   A HB3  1 
ATOM   2096 H  HG2  A LYS   A 1 102 ? 23.983 3.521   -12.207 0.64 32.93 ?  102 LYS   A HG2  1 
ATOM   2097 H  HG2  B LYS   A 1 102 ? 23.967 2.944   -12.768 0.36 33.15 ?  102 LYS   A HG2  1 
ATOM   2098 H  HG3  A LYS   A 1 102 ? 23.123 2.579   -11.252 0.64 32.93 ?  102 LYS   A HG3  1 
ATOM   2099 H  HG3  B LYS   A 1 102 ? 23.211 2.006   -11.731 0.36 33.15 ?  102 LYS   A HG3  1 
ATOM   2100 H  HD2  A LYS   A 1 102 ? 25.095 1.752   -10.303 0.64 34.55 ?  102 LYS   A HD2  1 
ATOM   2101 H  HD2  B LYS   A 1 102 ? 25.243 1.494   -10.705 0.36 34.97 ?  102 LYS   A HD2  1 
ATOM   2102 H  HD3  A LYS   A 1 102 ? 25.947 2.708   -11.248 0.64 34.55 ?  102 LYS   A HD3  1 
ATOM   2103 H  HD3  B LYS   A 1 102 ? 26.011 2.406   -11.760 0.36 34.97 ?  102 LYS   A HD3  1 
ATOM   2104 H  HE2  A LYS   A 1 102 ? 25.125 4.569   -10.160 0.64 35.74 ?  102 LYS   A HE2  1 
ATOM   2105 H  HE2  B LYS   A 1 102 ? 24.722 4.253   -10.892 0.36 36.48 ?  102 LYS   A HE2  1 
ATOM   2106 H  HE3  A LYS   A 1 102 ? 24.172 3.656   -9.270  0.64 35.74 ?  102 LYS   A HE3  1 
ATOM   2107 H  HE3  B LYS   A 1 102 ? 24.322 3.289   -9.691  0.36 36.48 ?  102 LYS   A HE3  1 
ATOM   2108 H  HZ1  A LYS   A 1 102 ? 26.041 4.232   -8.102  0.64 36.49 ?  102 LYS   A HZ1  1 
ATOM   2109 H  HZ1  B LYS   A 1 102 ? 26.116 4.566   -9.122  0.36 37.25 ?  102 LYS   A HZ1  1 
ATOM   2110 H  HZ2  A LYS   A 1 102 ? 26.038 2.794   -8.283  0.64 36.49 ?  102 LYS   A HZ2  1 
ATOM   2111 H  HZ2  B LYS   A 1 102 ? 26.528 3.177   -9.139  0.36 37.25 ?  102 LYS   A HZ2  1 
ATOM   2112 H  HZ3  A LYS   A 1 102 ? 26.905 3.625   -9.094  0.64 36.49 ?  102 LYS   A HZ3  1 
ATOM   2113 H  HZ3  B LYS   A 1 102 ? 26.893 4.055   -10.232 0.36 37.25 ?  102 LYS   A HZ3  1 
ATOM   2114 N  N    A GLY   A 1 103 ? 22.380 -0.579  -14.986 0.64 26.52 ?  103 GLY   A N    1 
ATOM   2115 N  N    B GLY   A 1 103 ? 22.582 -1.260  -15.451 0.36 22.87 ?  103 GLY   A N    1 
ATOM   2116 C  CA   A GLY   A 1 103 ? 22.635 -1.656  -15.924 0.64 27.14 ?  103 GLY   A CA   1 
ATOM   2117 C  CA   B GLY   A 1 103 ? 22.863 -2.424  -16.266 0.36 22.27 ?  103 GLY   A CA   1 
ATOM   2118 C  C    A GLY   A 1 103 ? 23.514 -2.765  -15.396 0.64 27.51 ?  103 GLY   A C    1 
ATOM   2119 C  C    B GLY   A 1 103 ? 23.640 -3.520  -15.572 0.36 21.43 ?  103 GLY   A C    1 
ATOM   2120 O  O    A GLY   A 1 103 ? 24.155 -3.458  -16.191 0.64 28.36 ?  103 GLY   A O    1 
ATOM   2121 O  O    B GLY   A 1 103 ? 24.070 -4.469  -16.235 0.36 21.49 ?  103 GLY   A O    1 
ATOM   2122 H  H    A GLY   A 1 103 ? 21.640 -0.665  -14.562 0.64 31.94 ?  103 GLY   A H    1 
ATOM   2123 H  H    B GLY   A 1 103 ? 21.766 -1.200  -15.183 0.36 27.56 ?  103 GLY   A H    1 
ATOM   2124 H  HA2  A GLY   A 1 103 ? 21.786 -2.035  -16.218 0.64 32.68 ?  103 GLY   A HA2  1 
ATOM   2125 H  HA2  B GLY   A 1 103 ? 22.028 -2.808  -16.566 0.36 26.84 ?  103 GLY   A HA2  1 
ATOM   2126 H  HA3  A GLY   A 1 103 ? 23.085 -1.304  -16.704 0.64 32.68 ?  103 GLY   A HA3  1 
ATOM   2127 H  HA3  B GLY   A 1 103 ? 23.363 -2.136  -17.048 0.36 26.84 ?  103 GLY   A HA3  1 
ATOM   2128 N  N    A GLU   A 1 104 ? 23.573 -2.954  -14.081 0.64 26.39 ?  104 GLU   A N    1 
ATOM   2129 N  N    B GLU   A 1 104 ? 23.818 -3.433  -14.258 0.36 20.40 ?  104 GLU   A N    1 
ATOM   2130 C  CA   A GLU   A 1 104 ? 24.445 -3.957  -13.485 0.64 25.19 ?  104 GLU   A CA   1 
ATOM   2131 C  CA   B GLU   A 1 104 ? 24.679 -4.368  -13.549 0.36 19.29 ?  104 GLU   A CA   1 
ATOM   2132 C  C    A GLU   A 1 104 ? 23.754 -5.317  -13.398 0.64 25.40 ?  104 GLU   A C    1 
ATOM   2133 C  C    B GLU   A 1 104 ? 23.990 -5.721  -13.382 0.36 19.25 ?  104 GLU   A C    1 
ATOM   2134 O  O    A GLU   A 1 104 ? 22.527 -5.413  -13.299 0.64 25.40 ?  104 GLU   A O    1 
ATOM   2135 O  O    B GLU   A 1 104 ? 22.786 -5.802  -13.116 0.36 18.95 ?  104 GLU   A O    1 
ATOM   2136 C  CB   A GLU   A 1 104 ? 24.940 -3.478  -12.116 0.64 23.38 ?  104 GLU   A CB   1 
ATOM   2137 C  CB   B GLU   A 1 104 ? 25.100 -3.772  -12.203 0.36 18.79 ?  104 GLU   A CB   1 
ATOM   2138 C  CG   A GLU   A 1 104 ? 25.945 -2.326  -12.256 0.64 22.38 ?  104 GLU   A CG   1 
ATOM   2139 C  CG   B GLU   A 1 104 ? 25.774 -2.406  -12.365 0.36 18.99 ?  104 GLU   A CG   1 
ATOM   2140 C  CD   A GLU   A 1 104 ? 26.212 -1.523  -10.986 0.64 21.30 ?  104 GLU   A CD   1 
ATOM   2141 C  CD   B GLU   A 1 104 ? 26.229 -1.769  -11.061 0.36 19.00 ?  104 GLU   A CD   1 
ATOM   2142 O  OE1  A GLU   A 1 104 ? 25.611 -1.805  -9.928  0.64 19.65 ?  104 GLU   A OE1  1 
ATOM   2143 O  OE1  B GLU   A 1 104 ? 25.712 -2.128  -9.984  0.36 18.64 ?  104 GLU   A OE1  1 
ATOM   2144 O  OE2  A GLU   A 1 104 ? 27.033 -0.578  -11.070 0.64 22.01 -1 104 GLU   A OE2  1 
ATOM   2145 O  OE2  B GLU   A 1 104 ? 27.112 -0.885  -11.126 0.36 19.67 -1 104 GLU   A OE2  1 
ATOM   2146 H  H    A GLU   A 1 104 ? 23.123 -2.499  -13.505 0.64 31.79 ?  104 GLU   A H    1 
ATOM   2147 H  H    B GLU   A 1 104 ? 23.442 -2.840  -13.756 0.36 24.60 ?  104 GLU   A H    1 
ATOM   2148 H  HA   A GLU   A 1 104 ? 25.217 -4.065  -14.056 0.64 30.34 ?  104 GLU   A HA   1 
ATOM   2149 H  HA   B GLU   A 1 104 ? 25.486 -4.504  -14.071 0.36 23.26 ?  104 GLU   A HA   1 
ATOM   2150 H  HB2  A GLU   A 1 104 ? 24.183 -3.167  -11.597 0.64 28.18 ?  104 GLU   A HB2  1 
ATOM   2151 H  HB2  B GLU   A 1 104 ? 24.318 -3.655  -11.645 0.36 22.66 ?  104 GLU   A HB2  1 
ATOM   2152 H  HB3  A GLU   A 1 104 ? 25.377 -4.216  -11.663 0.64 28.18 ?  104 GLU   A HB3  1 
ATOM   2153 H  HB3  B GLU   A 1 104 ? 25.735 -4.367  -11.775 0.36 22.66 ?  104 GLU   A HB3  1 
ATOM   2154 H  HG2  A GLU   A 1 104 ? 26.788 -2.694  -12.560 0.64 26.97 ?  104 GLU   A HG2  1 
ATOM   2155 H  HG2  B GLU   A 1 104 ? 26.557 -2.507  -12.928 0.36 22.90 ?  104 GLU   A HG2  1 
ATOM   2156 H  HG3  A GLU   A 1 104 ? 25.603 -1.702  -12.913 0.64 26.97 ?  104 GLU   A HG3  1 
ATOM   2157 H  HG3  B GLU   A 1 104 ? 25.148 -1.796  -12.786 0.36 22.90 ?  104 GLU   A HG3  1 
ATOM   2158 N  N    A ASP   A 1 105 ? 24.568 -6.373  -13.445 0.64 26.28 ?  105 ASP   A N    1 
ATOM   2159 N  N    B ASP   A 1 105 ? 24.774 -6.783  -13.561 0.36 20.19 ?  105 ASP   A N    1 
ATOM   2160 C  CA   A ASP   A 1 105 ? 24.073 -7.739  -13.590 0.64 27.24 ?  105 ASP   A CA   1 
ATOM   2161 C  CA   B ASP   A 1 105 ? 24.269 -8.152  -13.600 0.36 21.24 ?  105 ASP   A CA   1 
ATOM   2162 C  C    A ASP   A 1 105 ? 23.389 -8.200  -12.306 0.64 25.21 ?  105 ASP   A C    1 
ATOM   2163 C  C    B ASP   A 1 105 ? 23.522 -8.505  -12.320 0.36 20.74 ?  105 ASP   A C    1 
ATOM   2164 O  O    A ASP   A 1 105 ? 24.014 -8.244  -11.243 0.64 23.67 ?  105 ASP   A O    1 
ATOM   2165 O  O    B ASP   A 1 105 ? 24.106 -8.520  -11.233 0.36 19.34 ?  105 ASP   A O    1 
ATOM   2166 C  CB   A ASP   A 1 105 ? 25.245 -8.660  -13.926 0.64 30.17 ?  105 ASP   A CB   1 
ATOM   2167 C  CB   B ASP   A 1 105 ? 25.463 -9.088  -13.790 0.36 22.97 ?  105 ASP   A CB   1 
ATOM   2168 C  CG   A ASP   A 1 105 ? 24.807 -10.075 -14.225 0.64 32.55 ?  105 ASP   A CG   1 
ATOM   2169 C  CG   B ASP   A 1 105 ? 25.073 -10.549 -13.838 0.36 24.32 ?  105 ASP   A CG   1 
ATOM   2170 O  OD1  A ASP   A 1 105 ? 23.583 -10.312 -14.310 0.64 33.12 ?  105 ASP   A OD1  1 
ATOM   2171 O  OD1  B ASP   A 1 105 ? 23.870 -10.844 -13.978 0.36 24.70 ?  105 ASP   A OD1  1 
ATOM   2172 O  OD2  A ASP   A 1 105 ? 25.687 -10.949 -14.383 0.64 33.63 -1 105 ASP   A OD2  1 
ATOM   2173 O  OD2  B ASP   A 1 105 ? 25.982 -11.404 -13.735 0.36 25.13 -1 105 ASP   A OD2  1 
ATOM   2174 H  H    A ASP   A 1 105 ? 25.427 -6.324  -13.398 0.64 31.66 ?  105 ASP   A H    1 
ATOM   2175 H  H    B ASP   A 1 105 ? 25.620 -6.725  -13.678 0.36 24.34 ?  105 ASP   A H    1 
ATOM   2176 H  HA   A ASP   A 1 105 ? 23.433 -7.788  -14.316 0.64 32.81 ?  105 ASP   A HA   1 
ATOM   2177 H  HA   B ASP   A 1 105 ? 23.660 -8.250  -14.349 0.36 25.60 ?  105 ASP   A HA   1 
ATOM   2178 H  HB2  A ASP   A 1 105 ? 25.700 -8.328  -14.717 0.64 36.32 ?  105 ASP   A HB2  1 
ATOM   2179 H  HB2  B ASP   A 1 105 ? 25.904 -8.863  -14.623 0.36 27.68 ?  105 ASP   A HB2  1 
ATOM   2180 H  HB3  A ASP   A 1 105 ? 25.864 -8.679  -13.176 0.64 36.32 ?  105 ASP   A HB3  1 
ATOM   2181 H  HB3  B ASP   A 1 105 ? 26.072 -8.971  -13.047 0.36 27.68 ?  105 ASP   A HB3  1 
ATOM   2182 N  N    A ILE   A 1 106 ? 22.110 -8.573  -12.411 0.64 24.67 ?  106 ILE   A N    1 
ATOM   2183 N  N    B ILE   A 1 106 ? 22.231 -8.819  -12.455 0.36 21.51 ?  106 ILE   A N    1 
ATOM   2184 C  CA   A ILE   A 1 106 ? 21.347 -8.983  -11.238 0.64 23.54 ?  106 ILE   A CA   1 
ATOM   2185 C  CA   B ILE   A 1 106 ? 21.426 -9.171  -11.292 0.36 22.33 ?  106 ILE   A CA   1 
ATOM   2186 C  C    A ILE   A 1 106 ? 21.881 -10.275 -10.633 0.64 22.48 ?  106 ILE   A C    1 
ATOM   2187 C  C    B ILE   A 1 106 ? 21.932 -10.446 -10.635 0.36 22.52 ?  106 ILE   A C    1 
ATOM   2188 O  O    A ILE   A 1 106 ? 21.665 -10.526 -9.443  0.64 21.96 ?  106 ILE   A O    1 
ATOM   2189 O  O    B ILE   A 1 106 ? 21.705 -10.653 -9.439  0.36 22.49 ?  106 ILE   A O    1 
ATOM   2190 C  CB   A ILE   A 1 106 ? 19.842 -9.071  -11.570 0.64 24.87 ?  106 ILE   A CB   1 
ATOM   2191 C  CB   B ILE   A 1 106 ? 19.927 -9.258  -11.659 0.36 23.35 ?  106 ILE   A CB   1 
ATOM   2192 C  CG1  A ILE   A 1 106 ? 19.003 -9.151  -10.291 0.64 25.39 ?  106 ILE   A CG1  1 
ATOM   2193 C  CG1  B ILE   A 1 106 ? 19.057 -9.274  -10.399 0.36 23.95 ?  106 ILE   A CG1  1 
ATOM   2194 C  CG2  A ILE   A 1 106 ? 19.554 -10.273 -12.457 0.64 25.22 ?  106 ILE   A CG2  1 
ATOM   2195 C  CG2  B ILE   A 1 106 ? 19.644 -10.500 -12.473 0.36 23.58 ?  106 ILE   A CG2  1 
ATOM   2196 C  CD1  A ILE   A 1 106 ? 19.164 -7.955  -9.375  0.64 25.96 ?  106 ILE   A CD1  1 
ATOM   2197 C  CD1  B ILE   A 1 106 ? 19.045 -7.968  -9.640  0.36 24.32 ?  106 ILE   A CD1  1 
ATOM   2198 H  H    A ILE   A 1 106 ? 21.671 -8.593  -13.145 0.64 29.72 ?  106 ILE   A H    1 
ATOM   2199 H  H    B ILE   A 1 106 ? 21.810 -8.836  -13.201 0.36 25.92 ?  106 ILE   A H    1 
ATOM   2200 H  HA   A ILE   A 1 106 ? 21.459 -8.302  -10.565 0.64 28.36 ?  106 ILE   A HA   1 
ATOM   2201 H  HA   B ILE   A 1 106 ? 21.523 -8.465  -10.639 0.36 26.91 ?  106 ILE   A HA   1 
ATOM   2202 H  HB   A ILE   A 1 106 ? 19.589 -8.270  -12.053 0.64 29.96 ?  106 ILE   A HB   1 
ATOM   2203 H  HB   B ILE   A 1 106 ? 19.692 -8.478  -12.187 0.36 28.14 ?  106 ILE   A HB   1 
ATOM   2204 H  HG12 A ILE   A 1 106 ? 18.066 -9.210  -10.537 0.64 30.59 ?  106 ILE   A HG12 1 
ATOM   2205 H  HG12 B ILE   A 1 106 ? 18.143 -9.470  -10.656 0.36 28.85 ?  106 ILE   A HG12 1 
ATOM   2206 H  HG13 A ILE   A 1 106 ? 19.261 -9.943  -9.795  0.64 30.59 ?  106 ILE   A HG13 1 
ATOM   2207 H  HG13 B ILE   A 1 106 ? 19.383 -9.961  -9.799  0.36 28.85 ?  106 ILE   A HG13 1 
ATOM   2208 H  HG21 A ILE   A 1 106 ? 18.655 -10.194 -12.810 0.64 30.38 ?  106 ILE   A HG21 1 
ATOM   2209 H  HG21 B ILE   A 1 106 ? 18.764 -10.417 -12.871 0.36 28.41 ?  106 ILE   A HG21 1 
ATOM   2210 H  HG22 A ILE   A 1 106 ? 20.196 -10.287 -13.183 0.64 30.38 ?  106 ILE   A HG22 1 
ATOM   2211 H  HG22 B ILE   A 1 106 ? 20.317 -10.578 -13.164 0.36 28.41 ?  106 ILE   A HG22 1 
ATOM   2212 H  HG23 A ILE   A 1 106 ? 19.634 -11.082 -11.929 0.64 30.38 ?  106 ILE   A HG23 1 
ATOM   2213 H  HG23 B ILE   A 1 106 ? 19.673 -11.271 -11.887 0.36 28.41 ?  106 ILE   A HG23 1 
ATOM   2214 H  HD11 A ILE   A 1 106 ? 18.428 -7.939  -8.747  0.64 31.26 ?  106 ILE   A HD11 1 
ATOM   2215 H  HD11 B ILE   A 1 106 ? 18.352 -8.005  -8.963  0.36 29.30 ?  106 ILE   A HD11 1 
ATOM   2216 H  HD12 A ILE   A 1 106 ? 20.005 -8.033  -8.897  0.64 31.26 ?  106 ILE   A HD12 1 
ATOM   2217 H  HD12 B ILE   A 1 106 ? 19.909 -7.836  -9.220  0.36 29.30 ?  106 ILE   A HD12 1 
ATOM   2218 H  HD13 A ILE   A 1 106 ? 19.161 -7.145  -9.910  0.64 31.26 ?  106 ILE   A HD13 1 
ATOM   2219 H  HD13 B ILE   A 1 106 ? 18.862 -7.244  -10.259 0.36 29.30 ?  106 ILE   A HD13 1 
ATOM   2220 N  N    A GLN   A 1 107 ? 22.592 -11.092 -11.419 0.64 23.22 ?  107 GLN   A N    1 
ATOM   2221 N  N    B GLN   A 1 107 ? 22.629 -11.306 -11.385 0.36 23.07 ?  107 GLN   A N    1 
ATOM   2222 C  CA   A GLN   A 1 107 ? 23.189 -12.318 -10.891 0.64 25.19 ?  107 GLN   A CA   1 
ATOM   2223 C  CA   B GLN   A 1 107 ? 23.245 -12.474 -10.770 0.36 24.21 ?  107 GLN   A CA   1 
ATOM   2224 C  C    A GLN   A 1 107 ? 24.153 -12.026 -9.747  0.64 22.71 ?  107 GLN   A C    1 
ATOM   2225 C  C    B GLN   A 1 107 ? 24.267 -12.079 -9.715  0.36 22.06 ?  107 GLN   A C    1 
ATOM   2226 O  O    A GLN   A 1 107 ? 24.346 -12.870 -8.865  0.64 23.88 ?  107 GLN   A O    1 
ATOM   2227 O  O    B GLN   A 1 107 ? 24.622 -12.908 -8.871  0.36 22.81 ?  107 GLN   A O    1 
ATOM   2228 C  CB   A GLN   A 1 107 ? 23.903 -13.072 -12.019 0.64 29.41 ?  107 GLN   A CB   1 
ATOM   2229 C  CB   B GLN   A 1 107 ? 23.902 -13.373 -11.824 0.36 27.40 ?  107 GLN   A CB   1 
ATOM   2230 C  CG   A GLN   A 1 107 ? 23.033 -13.313 -13.248 0.64 33.92 ?  107 GLN   A CG   1 
ATOM   2231 C  CG   B GLN   A 1 107 ? 23.033 -13.675 -13.041 0.36 30.62 ?  107 GLN   A CG   1 
ATOM   2232 C  CD   A GLN   A 1 107 ? 21.800 -14.135 -12.934 0.64 37.28 ?  107 GLN   A CD   1 
ATOM   2233 C  CD   B GLN   A 1 107 ? 21.595 -14.002 -12.688 0.36 33.32 ?  107 GLN   A CD   1 
ATOM   2234 O  OE1  A GLN   A 1 107 ? 21.890 -15.199 -12.319 0.64 38.49 ?  107 GLN   A OE1  1 
ATOM   2235 O  OE1  B GLN   A 1 107 ? 21.325 -14.744 -11.744 0.36 34.37 ?  107 GLN   A OE1  1 
ATOM   2236 N  NE2  A GLN   A 1 107 ? 20.637 -13.643 -13.349 0.64 38.77 ?  107 GLN   A NE2  1 
ATOM   2237 N  NE2  B GLN   A 1 107 ? 20.661 -13.442 -13.451 0.36 34.38 ?  107 GLN   A NE2  1 
ATOM   2238 H  H    A GLN   A 1 107 ? 22.745 -10.958 -12.252 0.64 27.98 ?  107 GLN   A H    1 
ATOM   2239 H  H    B GLN   A 1 107 ? 22.760 -11.234 -12.231 0.36 27.79 ?  107 GLN   A H    1 
ATOM   2240 H  HA   A GLN   A 1 107 ? 22.496 -12.893 -10.544 0.64 30.35 ?  107 GLN   A HA   1 
ATOM   2241 H  HA   B GLN   A 1 107 ? 22.559 -12.992 -10.332 0.36 29.17 ?  107 GLN   A HA   1 
ATOM   2242 H  HB2  A GLN   A 1 107 ? 24.677 -12.562 -12.305 0.64 35.40 ?  107 GLN   A HB2  1 
ATOM   2243 H  HB2  B GLN   A 1 107 ? 24.711 -12.944 -12.141 0.36 32.99 ?  107 GLN   A HB2  1 
ATOM   2244 H  HB3  A GLN   A 1 107 ? 24.188 -13.941 -11.690 0.64 35.40 ?  107 GLN   A HB3  1 
ATOM   2245 H  HB3  B GLN   A 1 107 ? 24.127 -14.222 -11.409 0.36 32.99 ?  107 GLN   A HB3  1 
ATOM   2246 H  HG2  A GLN   A 1 107 ? 22.743 -12.461 -13.610 0.64 40.82 ?  107 GLN   A HG2  1 
ATOM   2247 H  HG2  B GLN   A 1 107 ? 23.024 -12.906 -13.627 0.36 36.86 ?  107 GLN   A HG2  1 
ATOM   2248 H  HG3  A GLN   A 1 107 ? 23.550 -13.794 -13.912 0.64 40.82 ?  107 GLN   A HG3  1 
ATOM   2249 H  HG3  B GLN   A 1 107 ? 23.405 -14.439 -13.509 0.36 36.86 ?  107 GLN   A HG3  1 
ATOM   2250 H  HE21 A GLN   A 1 107 ? 20.612 -12.896 -13.775 0.64 46.64 ?  107 GLN   A HE21 1 
ATOM   2251 H  HE21 B GLN   A 1 107 ? 20.890 -12.927 -14.102 0.36 41.37 ?  107 GLN   A HE21 1 
ATOM   2252 H  HE22 A GLN   A 1 107 ? 19.908 -14.072 -13.193 0.64 46.64 ?  107 GLN   A HE22 1 
ATOM   2253 H  HE22 B GLN   A 1 107 ? 19.829 -13.596 -13.298 0.36 41.37 ?  107 GLN   A HE22 1 
ATOM   2254 N  N    . LEU   A 1 108 ? 24.744 -10.829 -9.731  1.00 19.40 ?  108 LEU   A N    1 
ATOM   2255 C  CA   . LEU   A 1 108 ? 25.657 -10.404 -8.681  1.00 16.24 ?  108 LEU   A CA   1 
ATOM   2256 C  C    . LEU   A 1 108 ? 24.956 -10.232 -7.343  1.00 14.06 ?  108 LEU   A C    1 
ATOM   2257 O  O    . LEU   A 1 108 ? 25.639 -10.072 -6.329  1.00 14.19 ?  108 LEU   A O    1 
ATOM   2258 C  CB   . LEU   A 1 108 ? 26.386 -9.114  -9.086  1.00 16.12 ?  108 LEU   A CB   1 
ATOM   2259 C  CG   . LEU   A 1 108 ? 27.389 -9.311  -10.225 1.00 17.94 ?  108 LEU   A CG   1 
ATOM   2260 C  CD1  . LEU   A 1 108 ? 27.854 -7.976  -10.786 1.00 18.48 ?  108 LEU   A CD1  1 
ATOM   2261 C  CD2  . LEU   A 1 108 ? 28.583 -10.128 -9.754  1.00 19.53 ?  108 LEU   A CD2  1 
ATOM   2262 H  H    A LEU   A 1 108 ? 24.620 -10.231 -10.328 0.64 23.40 ?  108 LEU   A H    1 
ATOM   2263 H  H    B LEU   A 1 108 ? 24.570 -10.239 -10.323 0.36 23.40 ?  108 LEU   A H    1 
ATOM   2264 H  HA   . LEU   A 1 108 ? 26.330 -11.090 -8.559  1.00 19.60 ?  108 LEU   A HA   1 
ATOM   2265 H  HB2  . LEU   A 1 108 ? 25.730 -8.462  -9.380  1.00 19.46 ?  108 LEU   A HB2  1 
ATOM   2266 H  HB3  . LEU   A 1 108 ? 26.870 -8.771  -8.320  1.00 19.46 ?  108 LEU   A HB3  1 
ATOM   2267 H  HG   . LEU   A 1 108 ? 26.961 -9.805  -10.942 1.00 21.64 ?  108 LEU   A HG   1 
ATOM   2268 H  HD11 . LEU   A 1 108 ? 28.474 -8.139  -11.519 1.00 22.29 ?  108 LEU   A HD11 1 
ATOM   2269 H  HD12 . LEU   A 1 108 ? 27.085 -7.484  -11.109 1.00 22.29 ?  108 LEU   A HD12 1 
ATOM   2270 H  HD13 . LEU   A 1 108 ? 28.300 -7.475  -10.085 1.00 22.29 ?  108 LEU   A HD13 1 
ATOM   2271 H  HD21 . LEU   A 1 108 ? 29.274 -10.096 -10.432 1.00 23.55 ?  108 LEU   A HD21 1 
ATOM   2272 H  HD22 . LEU   A 1 108 ? 28.914 -9.749  -8.924  1.00 23.55 ?  108 LEU   A HD22 1 
ATOM   2273 H  HD23 . LEU   A 1 108 ? 28.302 -11.045 -9.609  1.00 23.55 ?  108 LEU   A HD23 1 
ATOM   2274 N  N    . LEU   A 1 109 ? 23.622 -10.284 -7.304  1.00 13.20 ?  109 LEU   A N    1 
ATOM   2275 C  CA   . LEU   A 1 109 ? 22.927 -10.160 -6.030  1.00 12.54 ?  109 LEU   A CA   1 
ATOM   2276 C  C    . LEU   A 1 109 ? 23.274 -11.311 -5.092  1.00 12.16 ?  109 LEU   A C    1 
ATOM   2277 O  O    . LEU   A 1 109 ? 23.404 -11.112 -3.880  1.00 12.77 ?  109 LEU   A O    1 
ATOM   2278 C  CB   . LEU   A 1 109 ? 21.422 -10.084 -6.276  1.00 13.49 ?  109 LEU   A CB   1 
ATOM   2279 C  CG   . LEU   A 1 109 ? 20.537 -9.777  -5.073  1.00 13.53 ?  109 LEU   A CG   1 
ATOM   2280 C  CD1  . LEU   A 1 109 ? 20.993 -8.505  -4.380  1.00 13.74 ?  109 LEU   A CD1  1 
ATOM   2281 C  CD2  . LEU   A 1 109 ? 19.079 -9.661  -5.513  1.00 14.95 ?  109 LEU   A CD2  1 
ATOM   2282 H  H    . LEU   A 1 109 ? 23.109 -10.388 -7.985  1.00 15.95 ?  109 LEU   A H    1 
ATOM   2283 H  HA   . LEU   A 1 109 ? 23.205 -9.335  -5.602  1.00 15.16 ?  109 LEU   A HA   1 
ATOM   2284 H  HB2  . LEU   A 1 109 ? 21.259 -9.389  -6.932  1.00 16.30 ?  109 LEU   A HB2  1 
ATOM   2285 H  HB3  . LEU   A 1 109 ? 21.129 -10.935 -6.631  1.00 16.30 ?  109 LEU   A HB3  1 
ATOM   2286 H  HG   . LEU   A 1 109 ? 20.597 -10.502 -4.436  1.00 16.35 ?  109 LEU   A HG   1 
ATOM   2287 H  HD11 . LEU   A 1 109 ? 20.310 -8.217  -3.755  1.00 16.60 ?  109 LEU   A HD11 1 
ATOM   2288 H  HD12 . LEU   A 1 109 ? 21.823 -8.676  -3.914  1.00 16.60 ?  109 LEU   A HD12 1 
ATOM   2289 H  HD13 . LEU   A 1 109 ? 21.129 -7.810  -5.053  1.00 16.60 ?  109 LEU   A HD13 1 
ATOM   2290 H  HD21 . LEU   A 1 109 ? 18.540 -9.361  -4.762  1.00 18.05 ?  109 LEU   A HD21 1 
ATOM   2291 H  HD22 . LEU   A 1 109 ? 19.013 -9.022  -6.240  1.00 18.05 ?  109 LEU   A HD22 1 
ATOM   2292 H  HD23 . LEU   A 1 109 ? 18.767 -10.532 -5.813  1.00 18.05 ?  109 LEU   A HD23 1 
ATOM   2293 N  N    . LYS   A 1 110 ? 23.425 -12.527 -5.626  1.00 11.99 ?  110 LYS   A N    1 
ATOM   2294 C  CA   . LYS   A 1 110 ? 23.795 -13.643 -4.762  1.00 11.97 ?  110 LYS   A CA   1 
ATOM   2295 C  C    . LYS   A 1 110 ? 25.176 -13.421 -4.159  1.00 11.69 ?  110 LYS   A C    1 
ATOM   2296 O  O    . LYS   A 1 110 ? 25.375 -13.620 -2.959  1.00 11.95 ?  110 LYS   A O    1 
ATOM   2297 C  CB   . LYS   A 1 110 ? 23.715 -14.971 -5.521  1.00 12.86 ?  110 LYS   A CB   1 
ATOM   2298 C  CG   . LYS   A 1 110 ? 23.922 -16.183 -4.614  1.00 13.36 ?  110 LYS   A CG   1 
ATOM   2299 C  CD   . LYS   A 1 110 ? 23.695 -17.504 -5.327  1.00 13.85 ?  110 LYS   A CD   1 
ATOM   2300 C  CE   . LYS   A 1 110 ? 23.797 -18.680 -4.369  1.00 14.41 ?  110 LYS   A CE   1 
ATOM   2301 N  NZ   . LYS   A 1 110 ? 22.607 -18.798 -3.490  1.00 14.82 ?  110 LYS   A NZ   1 
ATOM   2302 H  H    . LYS   A 1 110 ? 23.323 -12.724 -6.452  1.00 14.51 ?  110 LYS   A H    1 
ATOM   2303 H  HA   . LYS   A 1 110 ? 23.157 -13.692 -4.029  1.00 14.48 ?  110 LYS   A HA   1 
ATOM   2304 H  HB2  . LYS   A 1 110 ? 22.838 -15.052 -5.928  1.00 15.55 ?  110 LYS   A HB2  1 
ATOM   2305 H  HB3  . LYS   A 1 110 ? 24.403 -14.988 -6.201  1.00 15.55 ?  110 LYS   A HB3  1 
ATOM   2306 H  HG2  . LYS   A 1 110 ? 24.832 -16.173 -4.277  1.00 16.15 ?  110 LYS   A HG2  1 
ATOM   2307 H  HG3  . LYS   A 1 110 ? 23.297 -16.132 -3.872  1.00 16.15 ?  110 LYS   A HG3  1 
ATOM   2308 H  HD2  . LYS   A 1 110 ? 22.813 -17.510 -5.719  1.00 16.73 ?  110 LYS   A HD2  1 
ATOM   2309 H  HD3  . LYS   A 1 110 ? 24.374 -17.615 -6.012  1.00 16.73 ?  110 LYS   A HD3  1 
ATOM   2310 H  HE2  . LYS   A 1 110 ? 23.879 -19.500 -4.880  1.00 17.40 ?  110 LYS   A HE2  1 
ATOM   2311 H  HE3  . LYS   A 1 110 ? 24.579 -18.563 -3.802  1.00 17.40 ?  110 LYS   A HE3  1 
ATOM   2312 H  HZ1  . LYS   A 1 110 ? 22.694 -19.490 -2.945  1.00 17.90 ?  110 LYS   A HZ1  1 
ATOM   2313 H  HZ2  . LYS   A 1 110 ? 22.513 -18.054 -3.006  1.00 17.90 ?  110 LYS   A HZ2  1 
ATOM   2314 H  HZ3  . LYS   A 1 110 ? 21.875 -18.907 -3.988  1.00 17.90 ?  110 LYS   A HZ3  1 
ATOM   2315 N  N    . SER   A 1 111 ? 26.135 -12.986 -4.978  1.00 11.66 ?  111 SER   A N    1 
ATOM   2316 C  CA   . SER   A 1 111 ? 27.465 -12.678 -4.461  1.00 11.89 ?  111 SER   A CA   1 
ATOM   2317 C  C    . SER   A 1 111 ? 27.400 -11.629 -3.358  1.00 11.60 ?  111 SER   A C    1 
ATOM   2318 O  O    . SER   A 1 111 ? 28.096 -11.733 -2.343  1.00 12.16 ?  111 SER   A O    1 
ATOM   2319 C  CB   . SER   A 1 111 ? 28.360 -12.191 -5.600  1.00 13.06 ?  111 SER   A CB   1 
ATOM   2320 O  OG   . SER   A 1 111 ? 28.461 -13.189 -6.607  1.00 14.88 ?  111 SER   A OG   1 
ATOM   2321 H  H    . SER   A 1 111 ? 26.035 -12.862 -5.818  1.00 14.10 ?  111 SER   A H    1 
ATOM   2322 H  HA   . SER   A 1 111 ? 27.858 -13.482 -4.093  1.00 14.39 ?  111 SER   A HA   1 
ATOM   2323 H  HB2  . SER   A 1 111 ? 27.968 -11.395 -5.995  1.00 15.79 ?  111 SER   A HB2  1 
ATOM   2324 H  HB3  . SER   A 1 111 ? 29.240 -11.989 -5.250  1.00 15.79 ?  111 SER   A HB3  1 
ATOM   2325 H  HG   . SER   A 1 111 ? 28.972 -12.914 -7.226  1.00 17.97 ?  111 SER   A HG   1 
ATOM   2326 N  N    . ALA   A 1 112 ? 26.553 -10.613 -3.533  1.00 11.63 ?  112 ALA   A N    1 
ATOM   2327 C  CA   . ALA   A 1 112 ? 26.412 -9.574  -2.515  1.00 11.83 ?  112 ALA   A CA   1 
ATOM   2328 C  C    . ALA   A 1 112 ? 25.927 -10.165 -1.191  1.00 11.29 ?  112 ALA   A C    1 
ATOM   2329 O  O    . ALA   A 1 112 ? 26.476 -9.868  -0.121  1.00 11.75 ?  112 ALA   A O    1 
ATOM   2330 C  CB   . ALA   A 1 112 ? 25.456 -8.485  -3.009  1.00 12.29 ?  112 ALA   A CB   1 
ATOM   2331 H  H    . ALA   A 1 112 ? 26.054 -10.502 -4.224  1.00 14.08 ?  112 ALA   A H    1 
ATOM   2332 H  HA   . ALA   A 1 112 ? 27.277 -9.157  -2.363  1.00 14.31 ?  112 ALA   A HA   1 
ATOM   2333 H  HB1  . ALA   A 1 112 ? 25.384 -7.792  -2.329  1.00 14.87 ?  112 ALA   A HB1  1 
ATOM   2334 H  HB2  . ALA   A 1 112 ? 25.803 -8.102  -3.830  1.00 14.87 ?  112 ALA   A HB2  1 
ATOM   2335 H  HB3  . ALA   A 1 112 ? 24.583 -8.877  -3.170  1.00 14.87 ?  112 ALA   A HB3  1 
ATOM   2336 N  N    . TYR   A 1 113 ? 24.888 -11.004 -1.241  1.00 11.40 ?  113 TYR   A N    1 
ATOM   2337 C  CA   . TYR   A 1 113 ? 24.377 -11.608 -0.014  1.00 11.37 ?  113 TYR   A CA   1 
ATOM   2338 C  C    . TYR   A 1 113 ? 25.381 -12.563 0.632   1.00 11.30 ?  113 TYR   A C    1 
ATOM   2339 O  O    . TYR   A 1 113 ? 25.336 -12.750 1.851   1.00 11.84 ?  113 TYR   A O    1 
ATOM   2340 C  CB   . TYR   A 1 113 ? 23.061 -12.336 -0.287  1.00 11.49 ?  113 TYR   A CB   1 
ATOM   2341 C  CG   . TYR   A 1 113 ? 21.849 -11.439 -0.209  1.00 11.18 ?  113 TYR   A CG   1 
ATOM   2342 C  CD1  . TYR   A 1 113 ? 21.483 -10.844 0.992   1.00 11.55 ?  113 TYR   A CD1  1 
ATOM   2343 C  CD2  . TYR   A 1 113 ? 21.046 -11.217 -1.324  1.00 11.46 ?  113 TYR   A CD2  1 
ATOM   2344 C  CE1  . TYR   A 1 113 ? 20.359 -10.042 1.081   1.00 11.86 ?  113 TYR   A CE1  1 
ATOM   2345 C  CE2  . TYR   A 1 113 ? 19.895 -10.413 -1.238  1.00 11.70 ?  113 TYR   A CE2  1 
ATOM   2346 C  CZ   . TYR   A 1 113 ? 19.568 -9.836  -0.031  1.00 11.68 ?  113 TYR   A CZ   1 
ATOM   2347 O  OH   . TYR   A 1 113 ? 18.439 -9.047  0.091   1.00 12.28 ?  113 TYR   A OH   1 
ATOM   2348 H  H    . TYR   A 1 113 ? 24.480 -11.233 -1.960  1.00 13.79 ?  113 TYR   A H    1 
ATOM   2349 H  HA   . TYR   A 1 113 ? 24.201 -10.901 0.622   1.00 13.76 ?  113 TYR   A HA   1 
ATOM   2350 H  HB2  . TYR   A 1 113 ? 23.087 -12.712 -1.178  1.00 13.90 ?  113 TYR   A HB2  1 
ATOM   2351 H  HB3  . TYR   A 1 113 ? 22.951 -13.038 0.369   1.00 13.90 ?  113 TYR   A HB3  1 
ATOM   2352 H  HD1  . TYR   A 1 113 ? 22.004 -10.989 1.748   1.00 13.98 ?  113 TYR   A HD1  1 
ATOM   2353 H  HD2  . TYR   A 1 113 ? 21.263 -11.617 -2.132  1.00 13.87 ?  113 TYR   A HD2  1 
ATOM   2354 H  HE1  . TYR   A 1 113 ? 20.130 -9.655  1.894   1.00 14.35 ?  113 TYR   A HE1  1 
ATOM   2355 H  HE2  . TYR   A 1 113 ? 19.363 -10.266 -1.986  1.00 14.16 ?  113 TYR   A HE2  1 
ATOM   2356 H  HH   . TYR   A 1 113 ? 18.058 -8.996  -0.666  1.00 14.85 ?  113 TYR   A HH   1 
ATOM   2357 N  N    . GLU   A 1 114 ? 26.283 -13.184 -0.147  1.00 11.54 ?  114 GLU   A N    1 
ATOM   2358 C  CA   . GLU   A 1 114 ? 27.279 -14.077 0.453   1.00 11.60 ?  114 GLU   A CA   1 
ATOM   2359 C  C    . GLU   A 1 114 ? 28.124 -13.364 1.505   1.00 11.73 ?  114 GLU   A C    1 
ATOM   2360 O  O    . GLU   A 1 114 ? 28.596 -13.995 2.460   1.00 12.05 ?  114 GLU   A O    1 
ATOM   2361 C  CB   . GLU   A 1 114 ? 28.150 -14.726 -0.632  1.00 11.73 ?  114 GLU   A CB   1 
ATOM   2362 C  CG   . GLU   A 1 114 ? 27.384 -15.785 -1.421  1.00 12.45 ?  114 GLU   A CG   1 
ATOM   2363 C  CD   . GLU   A 1 114 ? 28.094 -16.314 -2.657  1.00 12.68 ?  114 GLU   A CD   1 
ATOM   2364 O  OE1  . GLU   A 1 114 ? 29.056 -15.687 -3.147  1.00 13.06 ?  114 GLU   A OE1  1 
ATOM   2365 O  OE2  . GLU   A 1 114 ? 27.655 -17.377 -3.151  1.00 13.94 -1 114 GLU   A OE2  1 
ATOM   2366 H  H    . GLU   A 1 114 ? 26.337 -13.095 -1.007  1.00 13.96 ?  114 GLU   A H    1 
ATOM   2367 H  HA   . GLU   A 1 114 ? 26.802 -14.788 0.901   1.00 14.03 ?  114 GLU   A HA   1 
ATOM   2368 H  HB2  . GLU   A 1 114 ? 28.444 -14.047 -1.258  1.00 14.20 ?  114 GLU   A HB2  1 
ATOM   2369 H  HB3  . GLU   A 1 114 ? 28.906 -15.157 -0.216  1.00 14.20 ?  114 GLU   A HB3  1 
ATOM   2370 H  HG2  . GLU   A 1 114 ? 27.210 -16.538 -0.836  1.00 15.06 ?  114 GLU   A HG2  1 
ATOM   2371 H  HG3  . GLU   A 1 114 ? 26.537 -15.401 -1.711  1.00 15.06 ?  114 GLU   A HG3  1 
ATOM   2372 N  N    . ASN   A 1 115 ? 28.307 -12.047 1.372   1.00 11.45 ?  115 ASN   A N    1 
ATOM   2373 C  CA   . ASN   A 1 115 ? 29.073 -11.317 2.379   1.00 11.86 ?  115 ASN   A CA   1 
ATOM   2374 C  C    . ASN   A 1 115 ? 28.457 -11.450 3.766   1.00 11.32 ?  115 ASN   A C    1 
ATOM   2375 O  O    . ASN   A 1 115 ? 29.173 -11.382 4.772   1.00 12.01 ?  115 ASN   A O    1 
ATOM   2376 C  CB   . ASN   A 1 115 ? 29.184 -9.842  2.002   1.00 11.87 ?  115 ASN   A CB   1 
ATOM   2377 C  CG   . ASN   A 1 115 ? 29.983 -9.627  0.743   1.00 12.24 ?  115 ASN   A CG   1 
ATOM   2378 O  OD1  . ASN   A 1 115 ? 31.202 -9.723  0.762   1.00 15.55 ?  115 ASN   A OD1  1 
ATOM   2379 N  ND2  . ASN   A 1 115 ? 29.310 -9.335  -0.356  1.00 11.90 ?  115 ASN   A ND2  1 
ATOM   2380 H  H    . ASN   A 1 115 ? 27.993 -11.558 0.733   1.00 13.86 ?  115 ASN   A H    1 
ATOM   2381 H  HA   . ASN   A 1 115 ? 29.964 -11.684 2.418   1.00 14.35 ?  115 ASN   A HA   1 
ATOM   2382 H  HB2  . ASN   A 1 115 ? 28.293 -9.476  1.871   1.00 14.36 ?  115 ASN   A HB2  1 
ATOM   2383 H  HB3  . ASN   A 1 115 ? 29.627 -9.364  2.728   1.00 14.36 ?  115 ASN   A HB3  1 
ATOM   2384 H  HD21 . ASN   A 1 115 ? 29.723 -9.203  -1.097  1.00 14.40 ?  115 ASN   A HD21 1 
ATOM   2385 H  HD22 . ASN   A 1 115 ? 28.447 -9.297  -0.334  1.00 14.40 ?  115 ASN   A HD22 1 
ATOM   2386 N  N    . PHE   A 1 116 ? 27.130 -11.618 3.844   1.00 11.71 ?  116 PHE   A N    1 
ATOM   2387 C  CA   . PHE   A 1 116 ? 26.471 -11.719 5.144   1.00 11.53 ?  116 PHE   A CA   1 
ATOM   2388 C  C    . PHE   A 1 116 ? 26.945 -12.949 5.916   1.00 11.83 ?  116 PHE   A C    1 
ATOM   2389 O  O    . PHE   A 1 116 ? 26.876 -12.970 7.147   1.00 12.34 ?  116 PHE   A O    1 
ATOM   2390 C  CB   . PHE   A 1 116 ? 24.943 -11.846 4.998   1.00 11.73 ?  116 PHE   A CB   1 
ATOM   2391 C  CG   . PHE   A 1 116 ? 24.189 -10.594 4.537   1.00 11.27 ?  116 PHE   A CG   1 
ATOM   2392 C  CD1  . PHE   A 1 116 ? 24.770 -9.570  3.802   1.00 11.26 ?  116 PHE   A CD1  1 
ATOM   2393 C  CD2  . PHE   A 1 116 ? 22.833 -10.489 4.844   1.00 12.11 ?  116 PHE   A CD2  1 
ATOM   2394 C  CE1  . PHE   A 1 116 ? 24.007 -8.491  3.383   1.00 11.60 ?  116 PHE   A CE1  1 
ATOM   2395 C  CE2  . PHE   A 1 116 ? 22.077 -9.415  4.437   1.00 12.19 ?  116 PHE   A CE2  1 
ATOM   2396 C  CZ   . PHE   A 1 116 ? 22.658 -8.412  3.706   1.00 11.33 ?  116 PHE   A CZ   1 
ATOM   2397 H  H    . PHE   A 1 116 ? 26.594 -11.659 3.169   1.00 14.17 ?  116 PHE   A H    1 
ATOM   2398 H  HA   . PHE   A 1 116 ? 26.658 -10.929 5.674   1.00 13.95 ?  116 PHE   A HA   1 
ATOM   2399 H  HB2  . PHE   A 1 116 ? 24.755 -12.549 4.354   1.00 14.19 ?  116 PHE   A HB2  1 
ATOM   2400 H  HB3  . PHE   A 1 116 ? 24.574 -12.102 5.861   1.00 14.19 ?  116 PHE   A HB3  1 
ATOM   2401 H  HD1  . PHE   A 1 116 ? 25.667 -9.632  3.575   1.00 13.63 ?  116 PHE   A HD1  1 
ATOM   2402 H  HD2  . PHE   A 1 116 ? 22.421 -11.176 5.330   1.00 14.65 ?  116 PHE   A HD2  1 
ATOM   2403 H  HE1  . PHE   A 1 116 ? 24.408 -7.809  2.896   1.00 14.04 ?  116 PHE   A HE1  1 
ATOM   2404 H  HE2  . PHE   A 1 116 ? 21.171 -9.371  4.658   1.00 14.74 ?  116 PHE   A HE2  1 
ATOM   2405 H  HZ   . PHE   A 1 116 ? 22.154 -7.677  3.438   1.00 13.71 ?  116 PHE   A HZ   1 
ATOM   2406 N  N    . ASN   A 1 117 ? 27.392 -13.998 5.213   1.00 12.18 ?  117 ASN   A N    1 
ATOM   2407 C  CA   . ASN   A 1 117 ? 27.760 -15.242 5.882   1.00 12.54 ?  117 ASN   A CA   1 
ATOM   2408 C  C    . ASN   A 1 117 ? 29.016 -15.123 6.725   1.00 12.88 ?  117 ASN   A C    1 
ATOM   2409 O  O    . ASN   A 1 117 ? 29.309 -16.042 7.498   1.00 13.83 ?  117 ASN   A O    1 
ATOM   2410 C  CB   . ASN   A 1 117 ? 27.878 -16.365 4.858   1.00 12.59 ?  117 ASN   A CB   1 
ATOM   2411 C  CG   . ASN   A 1 117 ? 26.526 -16.757 4.323   1.00 12.32 ?  117 ASN   A CG   1 
ATOM   2412 O  OD1  . ASN   A 1 117 ? 25.547 -16.778 5.071   1.00 13.43 ?  117 ASN   A OD1  1 
ATOM   2413 N  ND2  . ASN   A 1 117 ? 26.442 -17.014 3.032   1.00 12.21 ?  117 ASN   A ND2  1 
ATOM   2414 H  H    . ASN   A 1 117 ? 27.472 -14.012 4.352   1.00 14.73 ?  117 ASN   A H    1 
ATOM   2415 H  HA   . ASN   A 1 117 ? 27.033 -15.478 6.479   1.00 15.16 ?  117 ASN   A HA   1 
ATOM   2416 H  HB2  . ASN   A 1 117 ? 28.424 -16.062 4.112   1.00 15.22 ?  117 ASN   A HB2  1 
ATOM   2417 H  HB3  . ASN   A 1 117 ? 28.274 -17.137 5.277   1.00 15.22 ?  117 ASN   A HB3  1 
ATOM   2418 H  HD21 . ASN   A 1 117 ? 25.691 -17.237 2.690   1.00 14.77 ?  117 ASN   A HD21 1 
ATOM   2419 H  HD22 . ASN   A 1 117 ? 27.150 -16.978 2.541   1.00 14.77 ?  117 ASN   A HD22 1 
ATOM   2420 N  N    . GLN   A 1 118 ? 29.745 -14.013 6.613   1.00 12.79 ?  118 GLN   A N    1 
ATOM   2421 C  CA   . GLN   A 1 118 ? 30.922 -13.775 7.435   1.00 13.63 ?  118 GLN   A CA   1 
ATOM   2422 C  C    . GLN   A 1 118 ? 30.576 -13.200 8.803   1.00 13.78 ?  118 GLN   A C    1 
ATOM   2423 O  O    . GLN   A 1 118 ? 31.491 -12.911 9.583   1.00 15.02 ?  118 GLN   A O    1 
ATOM   2424 C  CB   . GLN   A 1 118 ? 31.921 -12.875 6.695   1.00 13.80 ?  118 GLN   A CB   1 
ATOM   2425 C  CG   . GLN   A 1 118 ? 32.393 -13.455 5.377   1.00 13.70 ?  118 GLN   A CG   1 
ATOM   2426 C  CD   . GLN   A 1 118 ? 33.227 -14.712 5.560   1.00 13.92 ?  118 GLN   A CD   1 
ATOM   2427 O  OE1  . GLN   A 1 118 ? 34.089 -14.777 6.448   1.00 14.91 ?  118 GLN   A OE1  1 
ATOM   2428 N  NE2  . GLN   A 1 118 ? 32.988 -15.711 4.711   1.00 13.79 ?  118 GLN   A NE2  1 
ATOM   2429 H  H    . GLN   A 1 118 ? 29.567 -13.367 6.064   1.00 15.46 ?  118 GLN   A H    1 
ATOM   2430 H  HA   . GLN   A 1 118 ? 31.353 -14.633 7.582   1.00 16.47 ?  118 GLN   A HA   1 
ATOM   2431 H  HB2  . GLN   A 1 118 ? 31.495 -12.025 6.516   1.00 16.67 ?  118 GLN   A HB2  1 
ATOM   2432 H  HB3  . GLN   A 1 118 ? 32.695 -12.748 7.262   1.00 16.67 ?  118 GLN   A HB3  1 
ATOM   2433 H  HG2  . GLN   A 1 118 ? 31.621 -13.678 4.830   1.00 16.56 ?  118 GLN   A HG2  1 
ATOM   2434 H  HG3  . GLN   A 1 118 ? 32.939 -12.795 4.921   1.00 16.56 ?  118 GLN   A HG3  1 
ATOM   2435 H  HE21 . GLN   A 1 118 ? 32.377 -15.625 4.103   1.00 16.66 ?  118 GLN   A HE21 1 
ATOM   2436 H  HE22 . GLN   A 1 118 ? 33.428 -16.445 4.768   1.00 16.66 ?  118 GLN   A HE22 1 
ATOM   2437 N  N    . HIS   A 1 119 ? 29.287 -13.047 9.116   1.00 13.27 ?  119 HIS   A N    1 
ATOM   2438 C  CA   . HIS   A 1 119 ? 28.836 -12.436 10.362  1.00 13.57 ?  119 HIS   A CA   1 
ATOM   2439 C  C    . HIS   A 1 119 ? 27.694 -13.252 10.941  1.00 13.94 ?  119 HIS   A C    1 
ATOM   2440 O  O    . HIS   A 1 119 ? 26.747 -13.593 10.227  1.00 14.44 ?  119 HIS   A O    1 
ATOM   2441 C  CB   . HIS   A 1 119 ? 28.385 -11.003 10.089  1.00 14.14 ?  119 HIS   A CB   1 
ATOM   2442 C  CG   . HIS   A 1 119 ? 29.468 -10.193 9.473   1.00 15.18 ?  119 HIS   A CG   1 
ATOM   2443 N  ND1  . HIS   A 1 119 ? 30.436 -9.570  10.225  1.00 17.28 ?  119 HIS   A ND1  1 
ATOM   2444 C  CD2  . HIS   A 1 119 ? 29.808 -10.007 8.178   1.00 16.06 ?  119 HIS   A CD2  1 
ATOM   2445 C  CE1  . HIS   A 1 119 ? 31.306 -8.992  9.416   1.00 17.56 ?  119 HIS   A CE1  1 
ATOM   2446 N  NE2  . HIS   A 1 119 ? 30.954 -9.251  8.168   1.00 17.28 ?  119 HIS   A NE2  1 
ATOM   2447 H  H    . HIS   A 1 119 ? 28.636 -13.306 8.609   1.00 16.04 ?  119 HIS   A H    1 
ATOM   2448 H  HA   . HIS   A 1 119 ? 29.567 -12.427 11.000  1.00 16.40 ?  119 HIS   A HA   1 
ATOM   2449 H  HB2  . HIS   A 1 119 ? 27.630 -11.024 9.483   1.00 17.09 ?  119 HIS   A HB2  1 
ATOM   2450 H  HB3  . HIS   A 1 119 ? 28.134 -10.592 10.929  1.00 17.09 ?  119 HIS   A HB3  1 
ATOM   2451 H  HD2  . HIS   A 1 119 ? 29.352 -10.331 7.432   1.00 19.38 ?  119 HIS   A HD2  1 
ATOM   2452 H  HE1  . HIS   A 1 119 ? 32.040 -8.487  9.676   1.00 21.19 ?  119 HIS   A HE1  1 
ATOM   2453 H  HE2  . HIS   A 1 119 ? 31.358 -8.965  7.463   1.00 20.86 ?  119 HIS   A HE2  1 
ATOM   2454 N  N    . GLU   A 1 120 ? 27.775 -13.547 12.240  1.00 15.09 ?  120 GLU   A N    1 
ATOM   2455 C  CA   . GLU   A 1 120 ? 26.821 -14.481 12.836  1.00 17.27 ?  120 GLU   A CA   1 
ATOM   2456 C  C    . GLU   A 1 120 ? 25.402 -13.921 12.889  1.00 15.48 ?  120 GLU   A C    1 
ATOM   2457 O  O    . GLU   A 1 120 ? 24.431 -14.686 12.772  1.00 15.84 ?  120 GLU   A O    1 
ATOM   2458 C  CB   . GLU   A 1 120 ? 27.286 -14.877 14.239  1.00 22.70 ?  120 GLU   A CB   1 
ATOM   2459 C  CG   . GLU   A 1 120 ? 28.479 -15.821 14.254  1.00 29.49 ?  120 GLU   A CG   1 
ATOM   2460 C  CD   . GLU   A 1 120 ? 28.642 -16.537 15.579  1.00 35.96 ?  120 GLU   A CD   1 
ATOM   2461 O  OE1  . GLU   A 1 120 ? 28.162 -16.010 16.605  1.00 38.51 ?  120 GLU   A OE1  1 
ATOM   2462 O  OE2  . GLU   A 1 120 ? 29.248 -17.629 15.592  1.00 41.23 -1 120 GLU   A OE2  1 
ATOM   2463 H  H    . GLU   A 1 120 ? 28.364 -13.227 12.788  1.00 18.23 ?  120 GLU   A H    1 
ATOM   2464 H  HA   . GLU   A 1 120 ? 26.808 -15.288 12.304  1.00 20.83 ?  120 GLU   A HA   1 
ATOM   2465 H  HB2  . GLU   A 1 120 ? 27.545 -14.083 14.733  1.00 27.35 ?  120 GLU   A HB2  1 
ATOM   2466 H  HB3  . GLU   A 1 120 ? 26.559 -15.327 14.702  1.00 27.35 ?  120 GLU   A HB3  1 
ATOM   2467 H  HG2  . GLU   A 1 120 ? 28.367 -16.487 13.558  1.00 35.51 ?  120 GLU   A HG2  1 
ATOM   2468 H  HG3  . GLU   A 1 120 ? 29.291 -15.316 14.107  1.00 35.51 ?  120 GLU   A HG3  1 
ATOM   2469 N  N    . VAL   A 1 121 ? 25.268 -12.611 13.098  1.00 14.85 ?  121 VAL   A N    1 
ATOM   2470 C  CA   . VAL   A 1 121 ? 23.974 -11.944 13.215  1.00 14.71 ?  121 VAL   A CA   1 
ATOM   2471 C  C    . VAL   A 1 121 ? 24.087 -10.564 12.576  1.00 13.45 ?  121 VAL   A C    1 
ATOM   2472 O  O    . VAL   A 1 121 ? 25.056 -9.837  12.821  1.00 14.05 ?  121 VAL   A O    1 
ATOM   2473 C  CB   . VAL   A 1 121 ? 23.536 -11.793 14.689  1.00 17.70 ?  121 VAL   A CB   1 
ATOM   2474 C  CG1  . VAL   A 1 121 ? 22.140 -11.183 14.778  1.00 18.16 ?  121 VAL   A CG1  1 
ATOM   2475 C  CG2  . VAL   A 1 121 ? 23.570 -13.120 15.428  1.00 19.92 ?  121 VAL   A CG2  1 
ATOM   2476 H  H    . VAL   A 1 121 ? 25.934 -12.071 13.177  1.00 17.93 ?  121 VAL   A H    1 
ATOM   2477 H  HA   . VAL   A 1 121 ? 23.301 -12.461 12.743  1.00 17.76 ?  121 VAL   A HA   1 
ATOM   2478 H  HB   . VAL   A 1 121 ? 24.146 -11.193 15.139  1.00 21.35 ?  121 VAL   A HB   1 
ATOM   2479 H  HG11 . VAL   A 1 121 ? 21.829 -11.228 15.698  1.00 21.91 ?  121 VAL   A HG11 1 
ATOM   2480 H  HG12 . VAL   A 1 121 ? 22.176 -10.258 14.490  1.00 21.91 ?  121 VAL   A HG12 1 
ATOM   2481 H  HG13 . VAL   A 1 121 ? 21.535 -11.684 14.206  1.00 21.91 ?  121 VAL   A HG13 1 
ATOM   2482 H  HG21 . VAL   A 1 121 ? 23.215 -12.995 16.327  1.00 24.02 ?  121 VAL   A HG21 1 
ATOM   2483 H  HG22 . VAL   A 1 121 ? 23.021 -13.766 14.952  1.00 24.02 ?  121 VAL   A HG22 1 
ATOM   2484 H  HG23 . VAL   A 1 121 ? 24.483 -13.435 15.478  1.00 24.02 ?  121 VAL   A HG23 1 
ATOM   2485 N  N    . LEU   A 1 122 ? 23.075 -10.179 11.791  1.00 12.64 ?  122 LEU   A N    1 
ATOM   2486 C  CA   . LEU   A 1 122 ? 23.077 -8.882  11.120  1.00 12.48 ?  122 LEU   A CA   1 
ATOM   2487 C  C    . LEU   A 1 122 ? 21.679 -8.285  11.071  1.00 12.33 ?  122 LEU   A C    1 
ATOM   2488 O  O    . LEU   A 1 122 ? 20.687 -9.003  10.934  1.00 13.40 ?  122 LEU   A O    1 
ATOM   2489 C  CB   . LEU   A 1 122 ? 23.522 -8.979  9.658   1.00 13.71 ?  122 LEU   A CB   1 
ATOM   2490 C  CG   . LEU   A 1 122 ? 24.729 -9.836  9.304   1.00 13.65 ?  122 LEU   A CG   1 
ATOM   2491 C  CD1  . LEU   A 1 122 ? 24.324 -11.286 9.086   1.00 14.38 ?  122 LEU   A CD1  1 
ATOM   2492 C  CD2  . LEU   A 1 122 ? 25.412 -9.274  8.068   1.00 13.06 ?  122 LEU   A CD2  1 
ATOM   2493 H  H    . LEU   A 1 122 ? 22.367 -10.652 11.636  1.00 15.29 ?  122 LEU   A H    1 
ATOM   2494 H  HA   . LEU   A 1 122 ? 23.668 -8.269  11.588  1.00 15.09 ?  122 LEU   A HA   1 
ATOM   2495 H  HB2  . LEU   A 1 122 ? 22.785 -9.331  9.145   1.00 16.57 ?  122 LEU   A HB2  1 
ATOM   2496 H  HB3  . LEU   A 1 122 ? 23.730 -8.086  9.350   1.00 16.57 ?  122 LEU   A HB3  1 
ATOM   2497 H  HG   . LEU   A 1 122 ? 25.376 -9.816  10.031  1.00 16.50 ?  122 LEU   A HG   1 
ATOM   2498 H  HD11 . LEU   A 1 122 ? 25.097 -11.803 8.808   1.00 17.37 ?  122 LEU   A HD11 1 
ATOM   2499 H  HD12 . LEU   A 1 122 ? 23.972 -11.646 9.917   1.00 17.37 ?  122 LEU   A HD12 1 
ATOM   2500 H  HD13 . LEU   A 1 122 ? 23.640 -11.324 8.397   1.00 17.37 ?  122 LEU   A HD13 1 
ATOM   2501 H  HD21 . LEU   A 1 122 ? 26.158 -9.853  7.818   1.00 15.79 ?  122 LEU   A HD21 1 
ATOM   2502 H  HD22 . LEU   A 1 122 ? 24.774 -9.234  7.341   1.00 15.79 ?  122 LEU   A HD22 1 
ATOM   2503 H  HD23 . LEU   A 1 122 ? 25.748 -8.385  8.266   1.00 15.79 ?  122 LEU   A HD23 1 
ATOM   2504 N  N    A LEU   A 1 123 ? 21.620 -6.958  11.155  0.64 12.00 ?  123 LEU   A N    1 
ATOM   2505 N  N    B LEU   A 1 123 ? 21.623 -6.959  11.197  0.36 11.88 ?  123 LEU   A N    1 
ATOM   2506 C  CA   A LEU   A 1 123 ? 20.455 -6.169  10.769  0.64 11.44 ?  123 LEU   A CA   1 
ATOM   2507 C  CA   B LEU   A 1 123 ? 20.451 -6.159  10.866  0.36 11.49 ?  123 LEU   A CA   1 
ATOM   2508 C  C    A LEU   A 1 123 ? 20.703 -5.654  9.359   0.64 10.99 ?  123 LEU   A C    1 
ATOM   2509 C  C    B LEU   A 1 123 ? 20.682 -5.602  9.465   0.36 10.66 ?  123 LEU   A C    1 
ATOM   2510 O  O    A LEU   A 1 123 ? 21.797 -5.155  9.075   0.64 10.94 ?  123 LEU   A O    1 
ATOM   2511 O  O    B LEU   A 1 123 ? 21.629 -4.836  9.256   0.36 10.44 ?  123 LEU   A O    1 
ATOM   2512 C  CB   A LEU   A 1 123 ? 20.310 -4.982  11.722  0.64 12.14 ?  123 LEU   A CB   1 
ATOM   2513 C  CB   B LEU   A 1 123 ? 20.291 -5.021  11.878  0.36 12.21 ?  123 LEU   A CB   1 
ATOM   2514 C  CG   A LEU   A 1 123 ? 19.247 -3.931  11.400  0.64 13.19 ?  123 LEU   A CG   1 
ATOM   2515 C  CG   B LEU   A 1 123 ? 19.320 -3.896  11.498  0.36 12.67 ?  123 LEU   A CG   1 
ATOM   2516 C  CD1  A LEU   A 1 123 ? 17.865 -4.561  11.403  0.64 13.75 ?  123 LEU   A CD1  1 
ATOM   2517 C  CD1  B LEU   A 1 123 ? 17.876 -4.390  11.434  0.36 13.05 ?  123 LEU   A CD1  1 
ATOM   2518 C  CD2  A LEU   A 1 123 ? 19.319 -2.773  12.395  0.64 13.88 ?  123 LEU   A CD2  1 
ATOM   2519 C  CD2  B LEU   A 1 123 ? 19.454 -2.726  12.461  0.36 13.05 ?  123 LEU   A CD2  1 
ATOM   2520 H  H    A LEU   A 1 123 ? 22.277 -6.473  11.433  0.64 14.52 ?  123 LEU   A H    1 
ATOM   2521 H  H    B LEU   A 1 123 ? 22.284 -6.480  11.473  0.36 14.37 ?  123 LEU   A H    1 
ATOM   2522 H  HA   A LEU   A 1 123 ? 19.654 -6.715  10.781  0.64 13.84 ?  123 LEU   A HA   1 
ATOM   2523 H  HA   B LEU   A 1 123 ? 19.651 -6.702  10.870  0.36 13.90 ?  123 LEU   A HA   1 
ATOM   2524 H  HB2  A LEU   A 1 123 ? 20.095 -5.336  12.600  0.64 14.68 ?  123 LEU   A HB2  1 
ATOM   2525 H  HB2  B LEU   A 1 123 ? 19.973 -5.400  12.719  0.36 14.77 ?  123 LEU   A HB2  1 
ATOM   2526 H  HB3  A LEU   A 1 123 ? 21.158 -4.524  11.760  0.64 14.68 ?  123 LEU   A HB3  1 
ATOM   2527 H  HB3  B LEU   A 1 123 ? 21.158 -4.611  12.027  0.36 14.77 ?  123 LEU   A HB3  1 
ATOM   2528 H  HG   A LEU   A 1 123 ? 19.409 -3.569  10.514  0.64 15.95 ?  123 LEU   A HG   1 
ATOM   2529 H  HG   B LEU   A 1 123 ? 19.550 -3.564  10.619  0.36 15.32 ?  123 LEU   A HG   1 
ATOM   2530 H  HD11 A LEU   A 1 123 ? 17.203 -3.872  11.244  0.64 16.61 ?  123 LEU   A HD11 1 
ATOM   2531 H  HD11 B LEU   A 1 123 ? 17.297 -3.648  11.198  0.36 15.77 ?  123 LEU   A HD11 1 
ATOM   2532 H  HD12 A LEU   A 1 123 ? 17.823 -5.230  10.703  0.64 16.61 ?  123 LEU   A HD12 1 
ATOM   2533 H  HD12 B LEU   A 1 123 ? 17.808 -5.088  10.762  0.36 15.77 ?  123 LEU   A HD12 1 
ATOM   2534 H  HD13 A LEU   A 1 123 ? 17.711 -4.975  12.268  0.64 16.61 ?  123 LEU   A HD13 1 
ATOM   2535 H  HD13 B LEU   A 1 123 ? 17.622 -4.743  12.302  0.36 15.77 ?  123 LEU   A HD13 1 
ATOM   2536 H  HD21 A LEU   A 1 123 ? 18.638 -2.117  12.173  0.64 16.77 ?  123 LEU   A HD21 1 
ATOM   2537 H  HD21 B LEU   A 1 123 ? 18.829 -2.031  12.200  0.36 15.78 ?  123 LEU   A HD21 1 
ATOM   2538 H  HD22 A LEU   A 1 123 ? 19.164 -3.115  13.292  0.64 16.77 ?  123 LEU   A HD22 1 
ATOM   2539 H  HD22 B LEU   A 1 123 ? 19.252 -3.032  13.359  0.36 15.78 ?  123 LEU   A HD22 1 
ATOM   2540 H  HD23 A LEU   A 1 123 ? 20.197 -2.365  12.346  0.64 16.77 ?  123 LEU   A HD23 1 
ATOM   2541 H  HD23 B LEU   A 1 123 ? 20.362 -2.389  12.421  0.36 15.78 ?  123 LEU   A HD23 1 
ATOM   2542 N  N    A ALA   A 1 124 ? 19.703 -5.750  8.476   0.64 10.58 ?  124 ALA   A N    1 
ATOM   2543 N  N    B ALA   A 1 124 ? 19.844 -5.991  8.509   0.36 10.21 ?  124 ALA   A N    1 
ATOM   2544 C  CA   A ALA   A 1 124 ? 20.000 -5.503  7.071   0.64 10.32 ?  124 ALA   A CA   1 
ATOM   2545 C  CA   B ALA   A 1 124 ? 20.079 -5.682  7.108   0.36 10.60 ?  124 ALA   A CA   1 
ATOM   2546 C  C    A ALA   A 1 124 ? 18.761 -5.098  6.285   0.64 10.32 ?  124 ALA   A C    1 
ATOM   2547 C  C    B ALA   A 1 124 ? 18.858 -5.101  6.416   0.36 10.39 ?  124 ALA   A C    1 
ATOM   2548 O  O    A ALA   A 1 124 ? 17.644 -5.526  6.612   0.64 10.79 ?  124 ALA   A O    1 
ATOM   2549 O  O    B ALA   A 1 124 ? 17.722 -5.271  6.874   0.36 10.65 ?  124 ALA   A O    1 
ATOM   2550 C  CB   A ALA   A 1 124 ? 20.625 -6.745  6.432   0.64 10.99 ?  124 ALA   A CB   1 
ATOM   2551 C  CB   B ALA   A 1 124 ? 20.533 -6.924  6.326   0.36 11.03 ?  124 ALA   A CB   1 
ATOM   2552 H  H    A ALA   A 1 124 ? 18.885 -5.932  8.665   0.64 12.81 ?  124 ALA   A H    1 
ATOM   2553 H  H    B ALA   A 1 124 ? 19.132 -6.449  8.649   0.36 12.37 ?  124 ALA   A H    1 
ATOM   2554 H  HA   A ALA   A 1 124 ? 20.649 -4.784  7.026   0.64 12.50 ?  124 ALA   A HA   1 
ATOM   2555 H  HA   B ALA   A 1 124 ? 20.790 -5.033  7.057   0.36 12.84 ?  124 ALA   A HA   1 
ATOM   2556 H  HB1  A ALA   A 1 124 ? 20.817 -6.560  5.501   0.64 13.31 ?  124 ALA   A HB1  1 
ATOM   2557 H  HB1  B ALA   A 1 124 ? 20.678 -6.677  5.395   0.36 13.35 ?  124 ALA   A HB1  1 
ATOM   2558 H  HB2  A ALA   A 1 124 ? 21.451 -6.961  6.901   0.64 13.31 ?  124 ALA   A HB2  1 
ATOM   2559 H  HB2  B ALA   A 1 124 ? 21.361 -7.256  6.708   0.36 13.35 ?  124 ALA   A HB2  1 
ATOM   2560 H  HB3  A ALA   A 1 124 ? 20.005 -7.485  6.505   0.64 13.31 ?  124 ALA   A HB3  1 
ATOM   2561 H  HB3  B ALA   A 1 124 ? 19.846 -7.606  6.380   0.36 13.35 ?  124 ALA   A HB3  1 
ATOM   2562 N  N    A PRO   A 1 125 ? 18.942 -4.327  5.216   0.64 10.72 ?  125 PRO   A N    1 
ATOM   2563 N  N    B PRO   A 1 125 ? 19.072 -4.407  5.289   0.36 9.80  ?  125 PRO   A N    1 
ATOM   2564 C  CA   A PRO   A 1 125 ? 17.896 -4.126  4.214   0.64 10.98 ?  125 PRO   A CA   1 
ATOM   2565 C  CA   B PRO   A 1 125 ? 17.966 -4.031  4.407   0.36 10.38 ?  125 PRO   A CA   1 
ATOM   2566 C  C    A PRO   A 1 125 ? 17.970 -5.208  3.142   0.64 10.96 ?  125 PRO   A C    1 
ATOM   2567 C  C    B PRO   A 1 125 ? 17.893 -5.015  3.253   0.36 10.78 ?  125 PRO   A C    1 
ATOM   2568 O  O    A PRO   A 1 125 ? 18.946 -5.956  3.038   0.64 11.40 ?  125 PRO   A O    1 
ATOM   2569 O  O    B PRO   A 1 125 ? 18.783 -5.864  3.122   0.36 11.22 ?  125 PRO   A O    1 
ATOM   2570 C  CB   A PRO   A 1 125 ? 18.321 -2.789  3.598   0.64 11.16 ?  125 PRO   A CB   1 
ATOM   2571 C  CB   B PRO   A 1 125 ? 18.413 -2.656  3.905   0.36 10.27 ?  125 PRO   A CB   1 
ATOM   2572 C  CG   A PRO   A 1 125 ? 19.835 -2.931  3.541   0.64 11.31 ?  125 PRO   A CG   1 
ATOM   2573 C  CG   B PRO   A 1 125 ? 19.919 -2.844  3.736   0.36 10.37 ?  125 PRO   A CG   1 
ATOM   2574 C  CD   A PRO   A 1 125 ? 20.175 -3.591  4.869   0.64 11.31 ?  125 PRO   A CD   1 
ATOM   2575 C  CD   B PRO   A 1 125 ? 20.350 -3.858  4.798   0.36 9.75  ?  125 PRO   A CD   1 
ATOM   2576 H  HA   A PRO   A 1 125 ? 17.007 -4.079  4.611   0.64 13.29 ?  125 PRO   A HA   1 
ATOM   2577 H  HA   B PRO   A 1 125 ? 17.120 -3.975  4.883   0.36 12.57 ?  125 PRO   A HA   1 
ATOM   2578 H  HB2  A PRO   A 1 125 ? 17.934 -2.699  2.714   0.64 13.51 ?  125 PRO   A HB2  1 
ATOM   2579 H  HB2  B PRO   A 1 125 ? 17.982 -2.452  3.058   0.36 12.44 ?  125 PRO   A HB2  1 
ATOM   2580 H  HB3  A PRO   A 1 125 ? 18.051 -2.061  4.179   0.64 13.51 ?  125 PRO   A HB3  1 
ATOM   2581 H  HB3  B PRO   A 1 125 ? 18.211 -1.977  4.570   0.36 12.44 ?  125 PRO   A HB3  1 
ATOM   2582 H  HG2  A PRO   A 1 125 ? 20.090 -3.501  2.796   0.64 13.69 ?  125 PRO   A HG2  1 
ATOM   2583 H  HG2  B PRO   A 1 125 ? 20.101 -3.183  2.846   0.36 12.56 ?  125 PRO   A HG2  1 
ATOM   2584 H  HG3  A PRO   A 1 125 ? 20.246 -2.057  3.468   0.64 13.69 ?  125 PRO   A HG3  1 
ATOM   2585 H  HG3  B PRO   A 1 125 ? 20.366 -1.994  3.873   0.36 12.56 ?  125 PRO   A HG3  1 
ATOM   2586 H  HD2  A PRO   A 1 125 ? 20.918 -4.200  4.773   0.64 13.68 ?  125 PRO   A HD2  1 
ATOM   2587 H  HD2  B PRO   A 1 125 ? 20.897 -4.551  4.394   0.36 11.81 ?  125 PRO   A HD2  1 
ATOM   2588 H  HD3  A PRO   A 1 125 ? 20.355 -2.914  5.548   0.64 13.68 ?  125 PRO   A HD3  1 
ATOM   2589 H  HD3  B PRO   A 1 125 ? 20.822 -3.406  5.515   0.36 11.81 ?  125 PRO   A HD3  1 
ATOM   2590 N  N    A LEU   A 1 126 ? 16.926 -5.256  2.321   0.64 10.91 ?  126 LEU   A N    1 
ATOM   2591 N  N    B LEU   A 1 126 ? 16.877 -4.919  2.400   0.36 11.32 ?  126 LEU   A N    1 
ATOM   2592 C  CA   A LEU   A 1 126 ? 16.949 -6.079  1.121   0.64 11.09 ?  126 LEU   A CA   1 
ATOM   2593 C  CA   B LEU   A 1 126 ? 16.831 -5.747  1.197   0.36 11.01 ?  126 LEU   A CA   1 
ATOM   2594 C  C    A LEU   A 1 126 ? 17.865 -5.457  0.070   0.64 11.36 ?  126 LEU   A C    1 
ATOM   2595 C  C    B LEU   A 1 126 ? 17.801 -5.174  0.169   0.36 10.83 ?  126 LEU   A C    1 
ATOM   2596 O  O    A LEU   A 1 126 ? 17.619 -4.349  -0.415  0.64 12.21 ?  126 LEU   A O    1 
ATOM   2597 O  O    B LEU   A 1 126 ? 17.596 -4.069  -0.341  0.36 11.61 ?  126 LEU   A O    1 
ATOM   2598 C  CB   A LEU   A 1 126 ? 15.538 -6.236  0.579   0.64 11.24 ?  126 LEU   A CB   1 
ATOM   2599 C  CB   B LEU   A 1 126 ? 15.418 -5.780  0.628   0.36 12.01 ?  126 LEU   A CB   1 
ATOM   2600 C  CG   A LEU   A 1 126 ? 14.644 -7.184  1.378   0.64 12.05 ?  126 LEU   A CG   1 
ATOM   2601 C  CG   B LEU   A 1 126 ? 14.412 -6.710  1.302   0.36 12.34 ?  126 LEU   A CG   1 
ATOM   2602 C  CD1  A LEU   A 1 126 ? 13.207 -7.053  0.920   0.64 13.67 ?  126 LEU   A CD1  1 
ATOM   2603 C  CD1  B LEU   A 1 126 ? 13.045 -6.537  0.658   0.36 12.61 ?  126 LEU   A CD1  1 
ATOM   2604 C  CD2  A LEU   A 1 126 ? 15.131 -8.621  1.235   0.64 11.93 ?  126 LEU   A CD2  1 
ATOM   2605 C  CD2  B LEU   A 1 126 ? 14.856 -8.161  1.218   0.36 12.76 ?  126 LEU   A CD2  1 
ATOM   2606 H  H    A LEU   A 1 126 ? 16.202 -4.812  2.433   0.64 13.21 ?  126 LEU   A H    1 
ATOM   2607 H  H    B LEU   A 1 126 ? 16.201 -4.387  2.496   0.36 13.70 ?  126 LEU   A H    1 
ATOM   2608 H  HA   A LEU   A 1 126 ? 17.294 -6.958  1.339   0.64 13.42 ?  126 LEU   A HA   1 
ATOM   2609 H  HA   B LEU   A 1 126 ? 17.107 -6.651  1.421   0.36 13.32 ?  126 LEU   A HA   1 
ATOM   2610 H  HB2  A LEU   A 1 126 ? 15.106 -5.365  0.579   0.64 13.61 ?  126 LEU   A HB2  1 
ATOM   2611 H  HB2  B LEU   A 1 126 ? 15.053 -4.883  0.678   0.36 14.53 ?  126 LEU   A HB2  1 
ATOM   2612 H  HB3  A LEU   A 1 126 ? 15.584 -6.575  -0.327  0.64 13.61 ?  126 LEU   A HB3  1 
ATOM   2613 H  HB3  B LEU   A 1 126 ? 15.477 -6.051  -0.299  0.36 14.53 ?  126 LEU   A HB3  1 
ATOM   2614 H  HG   A LEU   A 1 126 ? 14.679 -6.947  2.318   0.64 14.57 ?  126 LEU   A HG   1 
ATOM   2615 H  HG   B LEU   A 1 126 ? 14.328 -6.472  2.239   0.36 14.92 ?  126 LEU   A HG   1 
ATOM   2616 H  HD11 A LEU   A 1 126 ? 12.653 -7.664  1.431   0.64 16.52 ?  126 LEU   A HD11 1 
ATOM   2617 H  HD11 B LEU   A 1 126 ? 12.410 -7.130  1.092   0.36 15.24 ?  126 LEU   A HD11 1 
ATOM   2618 H  HD12 A LEU   A 1 126 ? 12.912 -6.141  1.063   0.64 16.52 ?  126 LEU   A HD12 1 
ATOM   2619 H  HD12 B LEU   A 1 126 ? 12.759 -5.616  0.759   0.36 15.24 ?  126 LEU   A HD12 1 
ATOM   2620 H  HD13 A LEU   A 1 126 ? 13.156 -7.274  -0.024  0.64 16.52 ?  126 LEU   A HD13 1 
ATOM   2621 H  HD13 B LEU   A 1 126 ? 13.110 -6.761  -0.286  0.36 15.24 ?  126 LEU   A HD13 1 
ATOM   2622 H  HD21 A LEU   A 1 126 ? 14.466 -9.221  1.603   0.64 14.44 ?  126 LEU   A HD21 1 
ATOM   2623 H  HD21 B LEU   A 1 126 ? 14.124 -8.732  1.496   0.36 15.43 ?  126 LEU   A HD21 1 
ATOM   2624 H  HD22 A LEU   A 1 126 ? 15.270 -8.813  0.294   0.64 14.44 ?  126 LEU   A HD22 1 
ATOM   2625 H  HD22 B LEU   A 1 126 ? 15.101 -8.359  0.300   0.36 15.43 ?  126 LEU   A HD22 1 
ATOM   2626 H  HD23 A LEU   A 1 126 ? 15.968 -8.718  1.718   0.64 14.44 ?  126 LEU   A HD23 1 
ATOM   2627 H  HD23 B LEU   A 1 126 ? 15.619 -8.289  1.801   0.36 15.43 ?  126 LEU   A HD23 1 
ATOM   2628 N  N    A LEU   A 1 127 ? 18.913 -6.189  -0.293  0.64 11.09 ?  127 LEU   A N    1 
ATOM   2629 N  N    B LEU   A 1 127 ? 18.855 -5.918  -0.152  0.36 10.46 ?  127 LEU   A N    1 
ATOM   2630 C  CA   A LEU   A 1 127 ? 19.906 -5.677  -1.224  0.64 10.55 ?  127 LEU   A CA   1 
ATOM   2631 C  CA   B LEU   A 1 127 ? 19.842 -5.406  -1.092  0.36 10.39 ?  127 LEU   A CA   1 
ATOM   2632 C  C    A LEU   A 1 127 ? 19.299 -5.484  -2.605  0.64 10.50 ?  127 LEU   A C    1 
ATOM   2633 C  C    B LEU   A 1 127 ? 19.261 -5.320  -2.498  0.36 10.57 ?  127 LEU   A C    1 
ATOM   2634 O  O    A LEU   A 1 127 ? 18.482 -6.287  -3.070  0.64 10.68 ?  127 LEU   A O    1 
ATOM   2635 O  O    B LEU   A 1 127 ? 18.395 -6.106  -2.894  0.36 11.06 ?  127 LEU   A O    1 
ATOM   2636 C  CB   A LEU   A 1 127 ? 21.084 -6.646  -1.308  0.64 11.15 ?  127 LEU   A CB   1 
ATOM   2637 C  CB   B LEU   A 1 127 ? 21.085 -6.293  -1.111  0.36 10.82 ?  127 LEU   A CB   1 
ATOM   2638 C  CG   A LEU   A 1 127 ? 21.858 -6.900  -0.017  0.64 11.45 ?  127 LEU   A CG   1 
ATOM   2639 C  CG   B LEU   A 1 127 ? 21.908 -6.316  0.179   0.36 11.00 ?  127 LEU   A CG   1 
ATOM   2640 C  CD1  A LEU   A 1 127 ? 22.947 -7.909  -0.289  0.64 11.84 ?  127 LEU   A CD1  1 
ATOM   2641 C  CD1  B LEU   A 1 127 ? 23.061 -7.297  0.053   0.36 11.40 ?  127 LEU   A CD1  1 
ATOM   2642 C  CD2  A LEU   A 1 127 ? 22.457 -5.616  0.519   0.64 12.38 ?  127 LEU   A CD2  1 
ATOM   2643 C  CD2  B LEU   A 1 127 ? 22.420 -4.922  0.534   0.36 11.33 ?  127 LEU   A CD2  1 
ATOM   2644 H  H    A LEU   A 1 127 ? 19.065 -6.986  -0.009  0.64 13.43 ?  127 LEU   A H    1 
ATOM   2645 H  H    B LEU   A 1 127 ? 19.018 -6.707  0.155   0.36 12.67 ?  127 LEU   A H    1 
ATOM   2646 H  HA   A LEU   A 1 127 ? 20.233 -4.822  -0.903  0.64 12.78 ?  127 LEU   A HA   1 
ATOM   2647 H  HA   B LEU   A 1 127 ? 20.103 -4.514  -0.812  0.36 12.59 ?  127 LEU   A HA   1 
ATOM   2648 H  HB2  A LEU   A 1 127 ? 20.749 -7.502  -1.616  0.64 13.50 ?  127 LEU   A HB2  1 
ATOM   2649 H  HB2  B LEU   A 1 127 ? 20.803 -7.201  -1.300  0.36 13.10 ?  127 LEU   A HB2  1 
ATOM   2650 H  HB3  A LEU   A 1 127 ? 21.716 -6.296  -1.954  0.64 13.50 ?  127 LEU   A HB3  1 
ATOM   2651 H  HB3  B LEU   A 1 127 ? 21.662 -5.979  -1.826  0.36 13.10 ?  127 LEU   A HB3  1 
ATOM   2652 H  HG   A LEU   A 1 127 ? 21.256 -7.268  0.655   0.64 13.86 ?  127 LEU   A HG   1 
ATOM   2653 H  HG   B LEU   A 1 127 ? 21.337 -6.614  0.903   0.36 13.31 ?  127 LEU   A HG   1 
ATOM   2654 H  HD11 A LEU   A 1 127 ? 23.407 -8.112  0.541   0.64 14.32 ?  127 LEU   A HD11 1 
ATOM   2655 H  HD11 B LEU   A 1 127 ? 23.587 -7.264  0.866   0.36 13.79 ?  127 LEU   A HD11 1 
ATOM   2656 H  HD12 A LEU   A 1 127 ? 22.546 -8.720  -0.648  0.64 14.32 ?  127 LEU   A HD12 1 
ATOM   2657 H  HD12 B LEU   A 1 127 ? 22.700 -8.189  -0.074  0.36 13.79 ?  127 LEU   A HD12 1 
ATOM   2658 H  HD13 A LEU   A 1 127 ? 23.568 -7.538  -0.932  0.64 14.32 ?  127 LEU   A HD13 1 
ATOM   2659 H  HD13 B LEU   A 1 127 ? 23.605 -7.046  -0.707  0.36 13.79 ?  127 LEU   A HD13 1 
ATOM   2660 H  HD21 A LEU   A 1 127 ? 23.033 -5.829  1.269   0.64 14.97 ?  127 LEU   A HD21 1 
ATOM   2661 H  HD21 B LEU   A 1 127 ? 23.057 -4.998  1.262   0.36 13.71 ?  127 LEU   A HD21 1 
ATOM   2662 H  HD22 A LEU   A 1 127 ? 22.975 -5.198  -0.187  0.64 14.97 ?  127 LEU   A HD22 1 
ATOM   2663 H  HD22 B LEU   A 1 127 ? 22.852 -4.535  -0.244  0.36 13.71 ?  127 LEU   A HD22 1 
ATOM   2664 H  HD23 A LEU   A 1 127 ? 21.743 -5.028  0.801   0.64 14.97 ?  127 LEU   A HD23 1 
ATOM   2665 H  HD23 B LEU   A 1 127 ? 21.672 -4.367  0.806   0.36 13.71 ?  127 LEU   A HD23 1 
ATOM   2666 N  N    A SER   A 1 128 ? 19.713 -4.408  -3.261  0.64 10.84 ?  128 SER   A N    1 
ATOM   2667 N  N    B SER   A 1 128 ? 19.752 -4.337  -3.249  0.36 10.77 ?  128 SER   A N    1 
ATOM   2668 C  CA   A SER   A 1 128 ? 19.297 -4.016  -4.599  0.64 11.16 ?  128 SER   A CA   1 
ATOM   2669 C  CA   B SER   A 1 128 ? 19.396 -4.032  -4.631  0.36 10.39 ?  128 SER   A CA   1 
ATOM   2670 C  C    A SER   A 1 128 ? 17.829 -3.594  -4.682  0.64 11.71 ?  128 SER   A C    1 
ATOM   2671 C  C    B SER   A 1 128 ? 17.962 -3.545  -4.811  0.36 10.23 ?  128 SER   A C    1 
ATOM   2672 O  O    A SER   A 1 128 ? 17.351 -3.315  -5.783  0.64 12.82 ?  128 SER   A O    1 
ATOM   2673 O  O    B SER   A 1 128 ? 17.593 -3.187  -5.933  0.36 10.17 ?  128 SER   A O    1 
ATOM   2674 C  CB   A SER   A 1 128 ? 19.645 -5.060  -5.672  0.64 11.48 ?  128 SER   A CB   1 
ATOM   2675 C  CB   B SER   A 1 128 ? 19.705 -5.172  -5.613  0.36 10.47 ?  128 SER   A CB   1 
ATOM   2676 O  OG   A SER   A 1 128 ? 21.049 -5.299  -5.696  0.64 12.15 ?  128 SER   A OG   1 
ATOM   2677 O  OG   B SER   A 1 128 ? 21.108 -5.340  -5.758  0.36 11.05 ?  128 SER   A OG   1 
ATOM   2678 H  H    A SER   A 1 128 ? 20.291 -3.856  -2.924  0.64 13.13 ?  128 SER   A H    1 
ATOM   2679 H  H    B SER   A 1 128 ? 20.351 -3.792  -2.951  0.36 13.04 ?  128 SER   A H    1 
ATOM   2680 H  HA   A SER   A 1 128 ? 19.811 -3.232  -4.822  0.64 13.51 ?  128 SER   A HA   1 
ATOM   2681 H  HA   B SER   A 1 128 ? 19.953 -3.290  -4.900  0.36 12.58 ?  128 SER   A HA   1 
ATOM   2682 H  HB2  A SER   A 1 128 ? 19.182 -5.887  -5.478  0.64 13.89 ?  128 SER   A HB2  1 
ATOM   2683 H  HB2  B SER   A 1 128 ? 19.311 -5.989  -5.279  0.36 12.68 ?  128 SER   A HB2  1 
ATOM   2684 H  HB3  A SER   A 1 128 ? 19.368 -4.719  -6.540  0.64 13.89 ?  128 SER   A HB3  1 
ATOM   2685 H  HB3  B SER   A 1 128 ? 19.320 -4.945  -6.479  0.36 12.68 ?  128 SER   A HB3  1 
ATOM   2686 H  HG   A SER   A 1 128 ? 21.457 -4.581  -5.857  0.64 14.69 ?  128 SER   A HG   1 
ATOM   2687 H  HG   B SER   A 1 128 ? 21.447 -4.620  -6.032  0.36 13.38 ?  128 SER   A HG   1 
ATOM   2688 N  N    A ALA   A 1 129 ? 17.109 -3.529  -3.561  0.64 12.33 ?  129 ALA   A N    1 
ATOM   2689 N  N    B ALA   A 1 129 ? 17.153 -3.496  -3.754  0.36 10.95 ?  129 ALA   A N    1 
ATOM   2690 C  CA   A ALA   A 1 129 ? 15.734 -3.052  -3.546  0.64 12.51 ?  129 ALA   A CA   1 
ATOM   2691 C  CA   B ALA   A 1 129 ? 15.793 -2.983  -3.844  0.36 11.49 ?  129 ALA   A CA   1 
ATOM   2692 C  C    A ALA   A 1 129 ? 15.707 -1.523  -3.516  0.64 12.37 ?  129 ALA   A C    1 
ATOM   2693 C  C    B ALA   A 1 129 ? 15.817 -1.458  -3.721  0.36 11.38 ?  129 ALA   A C    1 
ATOM   2694 O  O    A ALA   A 1 129 ? 16.740 -0.851  -3.596  0.64 12.64 ?  129 ALA   A O    1 
ATOM   2695 O  O    B ALA   A 1 129 ? 16.876 -0.825  -3.703  0.36 11.43 ?  129 ALA   A O    1 
ATOM   2696 C  CB   A ALA   A 1 129 ? 14.973 -3.658  -2.363  0.64 13.69 ?  129 ALA   A CB   1 
ATOM   2697 C  CB   B ALA   A 1 129 ? 14.902 -3.667  -2.806  0.36 12.46 ?  129 ALA   A CB   1 
ATOM   2698 H  H    A ALA   A 1 129 ? 17.401 -3.761  -2.784  0.64 14.91 ?  129 ALA   A H    1 
ATOM   2699 H  H    B ALA   A 1 129 ? 17.372 -3.752  -2.963  0.36 13.25 ?  129 ALA   A H    1 
ATOM   2700 H  HA   A ALA   A 1 129 ? 15.294 -3.339  -4.359  0.64 15.13 ?  129 ALA   A HA   1 
ATOM   2701 H  HA   B ALA   A 1 129 ? 15.438 -3.194  -4.717  0.36 13.90 ?  129 ALA   A HA   1 
ATOM   2702 H  HB1  A ALA   A 1 129 ? 14.056 -3.335  -2.381  0.64 16.55 ?  129 ALA   A HB1  1 
ATOM   2703 H  HB1  B ALA   A 1 129 ? 14.002 -3.308  -2.876  0.36 15.07 ?  129 ALA   A HB1  1 
ATOM   2704 H  HB2  A ALA   A 1 129 ? 14.986 -4.622  -2.440  0.64 16.55 ?  129 ALA   A HB2  1 
ATOM   2705 H  HB2  B ALA   A 1 129 ? 14.893 -4.620  -2.976  0.36 15.07 ?  129 ALA   A HB2  1 
ATOM   2706 H  HB3  A ALA   A 1 129 ? 15.402 -3.383  -1.537  0.64 16.55 ?  129 ALA   A HB3  1 
ATOM   2707 H  HB3  B ALA   A 1 129 ? 15.256 -3.492  -1.918  0.36 15.07 ?  129 ALA   A HB3  1 
ATOM   2708 N  N    A GLY   A 1 130 ? 14.504 -0.966  -3.413  0.64 12.52 ?  130 GLY   A N    1 
ATOM   2709 N  N    B GLY   A 1 130 ? 14.641 -0.846  -3.647  0.36 11.84 ?  130 GLY   A N    1 
ATOM   2710 C  CA   A GLY   A 1 130 ? 14.367 0.481   -3.370  0.64 12.79 ?  130 GLY   A CA   1 
ATOM   2711 C  CA   B GLY   A 1 130 ? 14.587 0.604   -3.573  0.36 12.48 ?  130 GLY   A CA   1 
ATOM   2712 C  C    A GLY   A 1 130 ? 14.977 1.129   -4.598  0.64 12.17 ?  130 GLY   A C    1 
ATOM   2713 C  C    B GLY   A 1 130 ? 15.228 1.228   -4.794  0.36 12.60 ?  130 GLY   A C    1 
ATOM   2714 O  O    A GLY   A 1 130 ? 14.754 0.693   -5.731  0.64 12.47 ?  130 GLY   A O    1 
ATOM   2715 O  O    B GLY   A 1 130 ? 14.999 0.807   -5.932  0.36 13.20 ?  130 GLY   A O    1 
ATOM   2716 H  H    A GLY   A 1 130 ? 13.762 -1.399  -3.371  0.64 15.14 ?  130 GLY   A H    1 
ATOM   2717 H  H    B GLY   A 1 130 ? 13.878 -1.242  -3.643  0.36 14.32 ?  130 GLY   A H    1 
ATOM   2718 H  HA2  A GLY   A 1 130 ? 13.424 0.718   -3.326  0.64 15.46 ?  130 GLY   A HA2  1 
ATOM   2719 H  HA2  B GLY   A 1 130 ? 13.663 0.896   -3.519  0.36 15.09 ?  130 GLY   A HA2  1 
ATOM   2720 H  HA3  A GLY   A 1 130 ? 14.811 0.830   -2.587  0.64 15.46 ?  130 GLY   A HA3  1 
ATOM   2721 H  HA3  B GLY   A 1 130 ? 15.063 0.917   -2.788  0.36 15.09 ?  130 GLY   A HA3  1 
ATOM   2722 N  N    A ILE   A 1 131 ? 15.753 2.196   -4.374  0.64 12.37 ?  131 ILE   A N    1 
ATOM   2723 N  N    B ILE   A 1 131 ? 16.063 2.242   -4.555  0.36 12.43 ?  131 ILE   A N    1 
ATOM   2724 C  CA   A ILE   A 1 131 ? 16.317 2.977   -5.475  0.64 12.19 ?  131 ILE   A CA   1 
ATOM   2725 C  CA   B ILE   A 1 131 ? 16.659 3.009   -5.643  0.36 12.47 ?  131 ILE   A CA   1 
ATOM   2726 C  C    A ILE   A 1 131 ? 17.373 2.227   -6.280  0.64 12.20 ?  131 ILE   A C    1 
ATOM   2727 C  C    B ILE   A 1 131 ? 17.634 2.206   -6.490  0.36 12.34 ?  131 ILE   A C    1 
ATOM   2728 O  O    A ILE   A 1 131 ? 17.799 2.733   -7.325  0.64 13.00 ?  131 ILE   A O    1 
ATOM   2729 O  O    B ILE   A 1 131 ? 18.047 2.689   -7.552  0.36 12.81 ?  131 ILE   A O    1 
ATOM   2730 C  CB   A ILE   A 1 131 ? 16.822 4.367   -5.022  0.64 13.44 ?  131 ILE   A CB   1 
ATOM   2731 C  CB   B ILE   A 1 131 ? 17.317 4.308   -5.131  0.36 13.03 ?  131 ILE   A CB   1 
ATOM   2732 C  CG1  A ILE   A 1 131 ? 18.045 4.257   -4.104  0.64 14.74 ?  131 ILE   A CG1  1 
ATOM   2733 C  CG1  B ILE   A 1 131 ? 18.520 4.004   -4.228  0.36 13.77 ?  131 ILE   A CG1  1 
ATOM   2734 C  CG2  A ILE   A 1 131 ? 15.694 5.151   -4.346  0.64 13.99 ?  131 ILE   A CG2  1 
ATOM   2735 C  CG2  B ILE   A 1 131 ? 16.299 5.156   -4.389  0.36 13.37 ?  131 ILE   A CG2  1 
ATOM   2736 C  CD1  A ILE   A 1 131 ? 18.699 5.602   -3.789  0.64 15.77 ?  131 ILE   A CD1  1 
ATOM   2737 C  CD1  B ILE   A 1 131 ? 19.180 5.258   -3.646  0.36 14.37 ?  131 ILE   A CD1  1 
ATOM   2738 H  H    A ILE   A 1 131 ? 15.949 2.493   -3.591  0.64 14.96 ?  131 ILE   A H    1 
ATOM   2739 H  H    B ILE   A 1 131 ? 16.293 2.504   -3.771  0.36 15.03 ?  131 ILE   A H    1 
ATOM   2740 H  HA   A ILE   A 1 131 ? 15.595 3.150   -6.094  0.64 14.75 ?  131 ILE   A HA   1 
ATOM   2741 H  HA   B ILE   A 1 131 ? 15.946 3.274   -6.237  0.36 15.09 ?  131 ILE   A HA   1 
ATOM   2742 H  HB   A ILE   A 1 131 ? 17.087 4.857   -5.811  0.64 16.24 ?  131 ILE   A HB   1 
ATOM   2743 H  HB   B ILE   A 1 131 ? 17.623 4.809   -5.901  0.36 15.75 ?  131 ILE   A HB   1 
ATOM   2744 H  HG12 A ILE   A 1 131 ? 17.774 3.853   -3.264  0.64 17.81 ?  131 ILE   A HG12 1 
ATOM   2745 H  HG12 B ILE   A 1 131 ? 18.225 3.455   -3.486  0.36 16.64 ?  131 ILE   A HG12 1 
ATOM   2746 H  HG13 A ILE   A 1 131 ? 18.715 3.699   -4.533  0.64 17.81 ?  131 ILE   A HG13 1 
ATOM   2747 H  HG13 B ILE   A 1 131 ? 19.192 3.532   -4.742  0.36 16.64 ?  131 ILE   A HG13 1 
ATOM   2748 H  HG21 A ILE   A 1 131 ? 15.992 6.059   -4.181  0.64 16.90 ?  131 ILE   A HG21 1 
ATOM   2749 H  HG21 B ILE   A 1 131 ? 16.662 6.046   -4.263  0.36 16.16 ?  131 ILE   A HG21 1 
ATOM   2750 H  HG22 A ILE   A 1 131 ? 14.921 5.159   -4.933  0.64 16.90 ?  131 ILE   A HG22 1 
ATOM   2751 H  HG22 B ILE   A 1 131 ? 15.486 5.202   -4.916  0.36 16.16 ?  131 ILE   A HG22 1 
ATOM   2752 H  HG23 A ILE   A 1 131 ? 15.465 4.719   -3.507  0.64 16.90 ?  131 ILE   A HG23 1 
ATOM   2753 H  HG23 B ILE   A 1 131 ? 16.114 4.745   -3.531  0.36 16.16 ?  131 ILE   A HG23 1 
ATOM   2754 H  HD11 A ILE   A 1 131 ? 19.518 5.448   -3.291  0.64 19.03 ?  131 ILE   A HD11 1 
ATOM   2755 H  HD11 B ILE   A 1 131 ? 20.058 5.027   -3.303  0.36 17.36 ?  131 ILE   A HD11 1 
ATOM   2756 H  HD12 A ILE   A 1 131 ? 18.900 6.058   -4.622  0.64 19.03 ?  131 ILE   A HD12 1 
ATOM   2757 H  HD12 B ILE   A 1 131 ? 19.264 5.926   -4.345  0.36 17.36 ?  131 ILE   A HD12 1 
ATOM   2758 H  HD13 A ILE   A 1 131 ? 18.087 6.136   -3.260  0.64 19.03 ?  131 ILE   A HD13 1 
ATOM   2759 H  HD13 B ILE   A 1 131 ? 18.626 5.606   -2.928  0.36 17.36 ?  131 ILE   A HD13 1 
ATOM   2760 N  N    A PHE   A 1 132 ? 17.806 1.036   -5.840  0.64 11.91 ?  132 PHE   A N    1 
ATOM   2761 N  N    B PHE   A 1 132 ? 18.013 0.994   -6.063  0.36 12.26 ?  132 PHE   A N    1 
ATOM   2762 C  CA   A PHE   A 1 132 ? 18.674 0.197   -6.663  0.64 11.86 ?  132 PHE   A CA   1 
ATOM   2763 C  CA   B PHE   A 1 132 ? 18.923 0.171   -6.857  0.36 12.38 ?  132 PHE   A CA   1 
ATOM   2764 C  C    A PHE   A 1 132 ? 17.909 -0.556  -7.756  0.64 11.88 ?  132 PHE   A C    1 
ATOM   2765 C  C    B PHE   A 1 132 ? 18.228 -0.581  -7.994  0.36 13.34 ?  132 PHE   A C    1 
ATOM   2766 O  O    A PHE   A 1 132 ? 18.536 -1.177  -8.620  0.64 12.50 ?  132 PHE   A O    1 
ATOM   2767 O  O    B PHE   A 1 132 ? 18.919 -1.153  -8.846  0.36 14.31 ?  132 PHE   A O    1 
ATOM   2768 C  CB   A PHE   A 1 132 ? 19.475 -0.785  -5.794  0.64 11.90 ?  132 PHE   A CB   1 
ATOM   2769 C  CB   B PHE   A 1 132 ? 19.703 -0.802  -5.963  0.36 11.31 ?  132 PHE   A CB   1 
ATOM   2770 C  CG   A PHE   A 1 132 ? 20.730 -0.201  -5.166  0.64 11.93 ?  132 PHE   A CG   1 
ATOM   2771 C  CG   B PHE   A 1 132 ? 20.873 -0.176  -5.236  0.36 10.99 ?  132 PHE   A CG   1 
ATOM   2772 C  CD1  A PHE   A 1 132 ? 20.665 0.864   -4.281  0.64 13.00 ?  132 PHE   A CD1  1 
ATOM   2773 C  CD1  B PHE   A 1 132 ? 20.678 0.805   -4.275  0.36 11.87 ?  132 PHE   A CD1  1 
ATOM   2774 C  CD2  A PHE   A 1 132 ? 21.971 -0.769  -5.423  0.64 12.45 ?  132 PHE   A CD2  1 
ATOM   2775 C  CD2  B PHE   A 1 132 ? 22.167 -0.599  -5.495  0.36 11.03 ?  132 PHE   A CD2  1 
ATOM   2776 C  CE1  A PHE   A 1 132 ? 21.820 1.368   -3.690  0.64 13.59 ?  132 PHE   A CE1  1 
ATOM   2777 C  CE1  B PHE   A 1 132 ? 21.755 1.361   -3.601  0.36 12.15 ?  132 PHE   A CE1  1 
ATOM   2778 C  CE2  A PHE   A 1 132 ? 23.127 -0.268  -4.834  0.64 12.81 ?  132 PHE   A CE2  1 
ATOM   2779 C  CE2  B PHE   A 1 132 ? 23.245 -0.047  -4.824  0.36 11.27 ?  132 PHE   A CE2  1 
ATOM   2780 C  CZ   A PHE   A 1 132 ? 23.046 0.802   -3.967  0.64 13.28 ?  132 PHE   A CZ   1 
ATOM   2781 C  CZ   B PHE   A 1 132 ? 23.037 0.933   -3.877  0.36 11.82 ?  132 PHE   A CZ   1 
ATOM   2782 H  H    A PHE   A 1 132 ? 17.602 0.691   -5.078  0.64 14.41 ?  132 PHE   A H    1 
ATOM   2783 H  H    B PHE   A 1 132 ? 17.765 0.629   -5.317  0.36 14.82 ?  132 PHE   A H    1 
ATOM   2784 H  HA   A PHE   A 1 132 ? 19.317 0.771   -7.104  0.64 14.35 ?  132 PHE   A HA   1 
ATOM   2785 H  HA   B PHE   A 1 132 ? 19.576 0.762   -7.254  0.36 14.98 ?  132 PHE   A HA   1 
ATOM   2786 H  HB2  A PHE   A 1 132 ? 18.907 -1.099  -5.072  0.64 14.39 ?  132 PHE   A HB2  1 
ATOM   2787 H  HB2  B PHE   A 1 132 ? 19.104 -1.161  -5.292  0.36 13.69 ?  132 PHE   A HB2  1 
ATOM   2788 H  HB3  A PHE   A 1 132 ? 19.746 -1.539  -6.344  0.64 14.39 ?  132 PHE   A HB3  1 
ATOM   2789 H  HB3  B PHE   A 1 132 ? 20.050 -1.525  -6.513  0.36 13.69 ?  132 PHE   A HB3  1 
ATOM   2790 H  HD1  A PHE   A 1 132 ? 19.844 1.246   -4.084  0.64 15.72 ?  132 PHE   A HD1  1 
ATOM   2791 H  HD1  B PHE   A 1 132 ? 19.817 1.096   -4.082  0.36 14.36 ?  132 PHE   A HD1  1 
ATOM   2792 H  HD2  A PHE   A 1 132 ? 22.038 -1.494  -6.006  0.64 15.05 ?  132 PHE   A HD2  1 
ATOM   2793 H  HD2  B PHE   A 1 132 ? 22.316 -1.264  -6.133  0.36 13.35 ?  132 PHE   A HD2  1 
ATOM   2794 H  HE1  A PHE   A 1 132 ? 21.763 2.089   -3.104  0.64 16.43 ?  132 PHE   A HE1  1 
ATOM   2795 H  HE1  B PHE   A 1 132 ? 21.614 2.023   -2.963  0.36 14.69 ?  132 PHE   A HE1  1 
ATOM   2796 H  HE2  A PHE   A 1 132 ? 23.957 -0.652  -5.027  0.64 15.49 ?  132 PHE   A HE2  1 
ATOM   2797 H  HE2  B PHE   A 1 132 ? 24.110 -0.338  -5.016  0.36 13.64 ?  132 PHE   A HE2  1 
ATOM   2798 H  HZ   A PHE   A 1 132 ? 23.818 1.145   -3.574  0.64 16.05 ?  132 PHE   A HZ   1 
ATOM   2799 H  HZ   B PHE   A 1 132 ? 23.761 1.307   -3.430  0.36 14.30 ?  132 PHE   A HZ   1 
ATOM   2800 N  N    A GLY   A 1 133 ? 16.578 -0.525  -7.741  0.64 11.96 ?  133 GLY   A N    1 
ATOM   2801 N  N    B GLY   A 1 133 ? 16.893 -0.620  -8.024  0.36 13.13 ?  133 GLY   A N    1 
ATOM   2802 C  CA   A GLY   A 1 133 ? 15.785 -0.887  -8.904  0.64 12.69 ?  133 GLY   A CA   1 
ATOM   2803 C  CA   B GLY   A 1 133 ? 16.148 -0.993  -9.209  0.36 13.34 ?  133 GLY   A CA   1 
ATOM   2804 C  C    A GLY   A 1 133 ? 15.528 -2.359  -9.151  0.64 13.48 ?  133 GLY   A C    1 
ATOM   2805 C  C    B GLY   A 1 133 ? 15.535 -2.382  -9.203  0.36 13.42 ?  133 GLY   A C    1 
ATOM   2806 O  O    A GLY   A 1 133 ? 15.003 -2.692  -10.220 0.64 14.50 ?  133 GLY   A O    1 
ATOM   2807 O  O    B GLY   A 1 133 ? 14.587 -2.621  -9.961  0.36 13.59 ?  133 GLY   A O    1 
ATOM   2808 H  H    A GLY   A 1 133 ? 16.111 -0.289  -7.066  0.64 14.47 ?  133 GLY   A H    1 
ATOM   2809 H  H    B GLY   A 1 133 ? 16.396 -0.437  -7.348  0.36 15.87 ?  133 GLY   A H    1 
ATOM   2810 H  HA2  A GLY   A 1 133 ? 14.919 -0.463  -8.830  0.64 15.34 ?  133 GLY   A HA2  1 
ATOM   2811 H  HA2  B GLY   A 1 133 ? 15.418 -0.376  -9.319  0.36 16.13 ?  133 GLY   A HA2  1 
ATOM   2812 H  HA3  A GLY   A 1 133 ? 16.218 -0.536  -9.699  0.64 15.34 ?  133 GLY   A HA3  1 
ATOM   2813 H  HA3  B GLY   A 1 133 ? 16.722 -0.899  -9.986  0.36 16.13 ?  133 GLY   A HA3  1 
ATOM   2814 N  N    A ALA   A 1 134 ? 15.871 -3.252  -8.224  0.64 13.28 ?  134 ALA   A N    1 
ATOM   2815 N  N    B ALA   A 1 134 ? 16.033 -3.297  -8.378  0.36 13.25 ?  134 ALA   A N    1 
ATOM   2816 C  CA   A ALA   A 1 134 ? 15.567 -4.663  -8.416  0.64 14.31 ?  134 ALA   A CA   1 
ATOM   2817 C  CA   B ALA   A 1 134 ? 15.585 -4.679  -8.461  0.36 13.49 ?  134 ALA   A CA   1 
ATOM   2818 C  C    A ALA   A 1 134 ? 14.205 -5.004  -7.813  0.64 14.60 ?  134 ALA   A C    1 
ATOM   2819 C  C    B ALA   A 1 134 ? 14.257 -4.877  -7.732  0.36 13.59 ?  134 ALA   A C    1 
ATOM   2820 O  O    A ALA   A 1 134 ? 13.615 -4.228  -7.057  0.64 15.51 ?  134 ALA   A O    1 
ATOM   2821 O  O    B ALA   A 1 134 ? 13.851 -4.077  -6.883  0.36 13.91 ?  134 ALA   A O    1 
ATOM   2822 C  CB   A ALA   A 1 134 ? 16.657 -5.550  -7.813  0.64 15.11 ?  134 ALA   A CB   1 
ATOM   2823 C  CB   B ALA   A 1 134 ? 16.636 -5.619  -7.878  0.36 13.77 ?  134 ALA   A CB   1 
ATOM   2824 H  H    A ALA   A 1 134 ? 16.281 -3.066  -7.486  0.64 16.05 ?  134 ALA   A H    1 
ATOM   2825 H  H    B ALA   A 1 134 ? 16.622 -3.142  -7.772  0.36 16.02 ?  134 ALA   A H    1 
ATOM   2826 H  HA   A ALA   A 1 134 ? 15.529 -4.850  -9.367  0.64 17.29 ?  134 ALA   A HA   1 
ATOM   2827 H  HA   B ALA   A 1 134 ? 15.454 -4.909  -9.394  0.36 16.30 ?  134 ALA   A HA   1 
ATOM   2828 H  HB1  A ALA   A 1 134 ? 16.440 -6.479  -7.991  0.64 18.24 ?  134 ALA   A HB1  1 
ATOM   2829 H  HB1  B ALA   A 1 134 ? 16.313 -6.529  -7.947  0.36 16.64 ?  134 ALA   A HB1  1 
ATOM   2830 H  HB2  A ALA   A 1 134 ? 17.509 -5.327  -8.223  0.64 18.24 ?  134 ALA   A HB2  1 
ATOM   2831 H  HB2  B ALA   A 1 134 ? 17.459 -5.517  -8.383  0.36 16.64 ?  134 ALA   A HB2  1 
ATOM   2832 H  HB3  A ALA   A 1 134 ? 16.699 -5.395  -6.859  0.64 18.24 ?  134 ALA   A HB3  1 
ATOM   2833 H  HB3  B ALA   A 1 134 ? 16.785 -5.385  -6.950  0.36 16.64 ?  134 ALA   A HB3  1 
ATOM   2834 N  N    A ASP   A 1 135 ? 13.705 -6.185  -8.169  0.64 14.66 ?  135 ASP   A N    1 
ATOM   2835 N  N    B ASP   A 1 135 ? 13.585 -5.974  -8.079  0.36 14.15 ?  135 ASP   A N    1 
ATOM   2836 C  CA   A ASP   A 1 135 ? 12.453 -6.692  -7.615  0.64 14.97 ?  135 ASP   A CA   1 
ATOM   2837 C  CA   B ASP   A 1 135 ? 12.318 -6.334  -7.459  0.36 14.59 ?  135 ASP   A CA   1 
ATOM   2838 C  C    A ASP   A 1 135 ? 12.690 -7.124  -6.174  0.64 14.39 ?  135 ASP   A C    1 
ATOM   2839 C  C    B ASP   A 1 135 ? 12.576 -6.825  -6.039  0.36 13.79 ?  135 ASP   A C    1 
ATOM   2840 O  O    A ASP   A 1 135 ? 13.497 -8.030  -5.938  0.64 14.22 ?  135 ASP   A O    1 
ATOM   2841 O  O    B ASP   A 1 135 ? 13.299 -7.815  -5.858  0.36 13.35 ?  135 ASP   A O    1 
ATOM   2842 C  CB   A ASP   A 1 135 ? 11.993 -7.885  -8.449  0.64 17.11 ?  135 ASP   A CB   1 
ATOM   2843 C  CB   B ASP   A 1 135 ? 11.655 -7.434  -8.283  0.36 15.77 ?  135 ASP   A CB   1 
ATOM   2844 C  CG   A ASP   A 1 135 ? 10.694 -8.512  -7.948  0.64 18.85 ?  135 ASP   A CG   1 
ATOM   2845 C  CG   B ASP   A 1 135 ? 10.249 -7.761  -7.803  0.36 16.95 ?  135 ASP   A CG   1 
ATOM   2846 O  OD1  A ASP   A 1 135 ? 10.149 -8.076  -6.915  0.64 18.68 ?  135 ASP   A OD1  1 
ATOM   2847 O  OD1  B ASP   A 1 135 ? 9.913  -7.435  -6.642  0.36 17.08 ?  135 ASP   A OD1  1 
ATOM   2848 O  OD2  A ASP   A 1 135 ? 10.213 -9.458  -8.606  0.64 21.10 -1 135 ASP   A OD2  1 
ATOM   2849 O  OD2  B ASP   A 1 135 ? 9.481  -8.354  -8.589  0.36 17.94 -1 135 ASP   A OD2  1 
ATOM   2850 H  H    A ASP   A 1 135 ? 14.075 -6.715  -8.736  0.64 17.71 ?  135 ASP   A H    1 
ATOM   2851 H  H    B ASP   A 1 135 ? 13.843 -6.531  -8.677  0.36 17.09 ?  135 ASP   A H    1 
ATOM   2852 H  HA   A ASP   A 1 135 ? 11.777 -5.996  -7.651  0.64 18.07 ?  135 ASP   A HA   1 
ATOM   2853 H  HA   B ASP   A 1 135 ? 11.725 -5.563  -7.450  0.36 17.62 ?  135 ASP   A HA   1 
ATOM   2854 H  HB2  A ASP   A 1 135 ? 11.843 -7.592  -9.357  0.64 20.65 ?  135 ASP   A HB2  1 
ATOM   2855 H  HB2  B ASP   A 1 135 ? 11.615 -7.147  -9.213  0.36 19.04 ?  135 ASP   A HB2  1 
ATOM   2856 H  HB3  A ASP   A 1 135 ? 12.681 -8.566  -8.423  0.64 20.65 ?  135 ASP   A HB3  1 
ATOM   2857 H  HB3  B ASP   A 1 135 ? 12.182 -8.243  -8.212  0.36 19.04 ?  135 ASP   A HB3  1 
ATOM   2858 N  N    A PRO   A 1 136 ? 12.030 -6.512  -5.188  0.64 14.25 ?  136 PRO   A N    1 
ATOM   2859 N  N    B PRO   A 1 136 ? 12.026 -6.172  -5.013  0.36 13.64 ?  136 PRO   A N    1 
ATOM   2860 C  CA   A PRO   A 1 136 ? 12.277 -6.912  -3.792  0.64 14.43 ?  136 PRO   A CA   1 
ATOM   2861 C  CA   B PRO   A 1 136 ? 12.273 -6.626  -3.634  0.36 13.64 ?  136 PRO   A CA   1 
ATOM   2862 C  C    A PRO   A 1 136 ? 11.856 -8.336  -3.472  0.64 13.67 ?  136 PRO   A C    1 
ATOM   2863 C  C    B PRO   A 1 136 ? 11.831 -8.055  -3.360  0.36 13.11 ?  136 PRO   A C    1 
ATOM   2864 O  O    A PRO   A 1 136 ? 12.467 -8.963  -2.599  0.64 13.61 ?  136 PRO   A O    1 
ATOM   2865 O  O    B PRO   A 1 136 ? 12.394 -8.705  -2.470  0.36 12.44 ?  136 PRO   A O    1 
ATOM   2866 C  CB   A PRO   A 1 136 ? 11.482 -5.879  -2.983  0.64 15.38 ?  136 PRO   A CB   1 
ATOM   2867 C  CB   B PRO   A 1 136 ? 11.501 -5.604  -2.785  0.36 14.33 ?  136 PRO   A CB   1 
ATOM   2868 C  CG   A PRO   A 1 136 ? 10.421 -5.391  -3.931  0.64 15.96 ?  136 PRO   A CG   1 
ATOM   2869 C  CG   B PRO   A 1 136 ? 10.521 -4.979  -3.735  0.36 14.86 ?  136 PRO   A CG   1 
ATOM   2870 C  CD   A PRO   A 1 136 ? 11.037 -5.429  -5.294  0.64 15.06 ?  136 PRO   A CD   1 
ATOM   2871 C  CD   B PRO   A 1 136 ? 11.201 -4.956  -5.052  0.36 14.09 ?  136 PRO   A CD   1 
ATOM   2872 H  HA   A PRO   A 1 136 ? 13.220 -6.816  -3.576  0.64 17.43 ?  136 PRO   A HA   1 
ATOM   2873 H  HA   B PRO   A 1 136 ? 13.216 -6.546  -3.427  0.36 16.48 ?  136 PRO   A HA   1 
ATOM   2874 H  HB2  A PRO   A 1 136 ? 11.082 -6.304  -2.207  0.64 18.57 ?  136 PRO   A HB2  1 
ATOM   2875 H  HB2  B PRO   A 1 136 ? 11.036 -6.054  -2.063  0.36 17.31 ?  136 PRO   A HB2  1 
ATOM   2876 H  HB3  A PRO   A 1 136 ? 12.068 -5.154  -2.712  0.64 18.57 ?  136 PRO   A HB3  1 
ATOM   2877 H  HB3  B PRO   A 1 136 ? 12.111 -4.933  -2.437  0.36 17.31 ?  136 PRO   A HB3  1 
ATOM   2878 H  HG2  A PRO   A 1 136 ? 9.656  -5.978  -3.888  0.64 19.27 ?  136 PRO   A HG2  1 
ATOM   2879 H  HG2  B PRO   A 1 136 ? 9.722  -5.527  -3.784  0.36 17.95 ?  136 PRO   A HG2  1 
ATOM   2880 H  HG3  A PRO   A 1 136 ? 10.177 -4.483  -3.699  0.64 19.27 ?  136 PRO   A HG3  1 
ATOM   2881 H  HG3  B PRO   A 1 136 ? 10.305 -4.080  -3.445  0.36 17.95 ?  136 PRO   A HG3  1 
ATOM   2882 H  HD2  A PRO   A 1 136 ? 10.367 -5.659  -5.960  0.64 18.19 ?  136 PRO   A HD2  1 
ATOM   2883 H  HD2  B PRO   A 1 136 ? 10.545 -5.005  -5.767  0.36 17.02 ?  136 PRO   A HD2  1 
ATOM   2884 H  HD3  A PRO   A 1 136 ? 11.471 -4.588  -5.502  0.64 18.19 ?  136 PRO   A HD3  1 
ATOM   2885 H  HD3  B PRO   A 1 136 ? 11.762 -4.167  -5.137  0.36 17.02 ?  136 PRO   A HD3  1 
ATOM   2886 N  N    A ILE   A 1 137 ? 10.810 -8.857  -4.117  0.64 13.83 ?  137 ILE   A N    1 
ATOM   2887 N  N    B ILE   A 1 137 ? 10.830 -8.562  -4.085  0.36 13.51 ?  137 ILE   A N    1 
ATOM   2888 C  CA   A ILE   A 1 137 ? 10.446 -10.256 -3.910  0.64 14.05 ?  137 ILE   A CA   1 
ATOM   2889 C  CA   B ILE   A 1 137 ? 10.426 -9.956  -3.917  0.36 13.87 ?  137 ILE   A CA   1 
ATOM   2890 C  C    A ILE   A 1 137 ? 11.601 -11.156 -4.321  0.64 13.38 ?  137 ILE   A C    1 
ATOM   2891 C  C    B ILE   A 1 137 ? 11.588 -10.880 -4.260  0.36 13.58 ?  137 ILE   A C    1 
ATOM   2892 O  O    A ILE   A 1 137 ? 11.918 -12.140 -3.643  0.64 13.68 ?  137 ILE   A O    1 
ATOM   2893 O  O    B ILE   A 1 137 ? 11.886 -11.837 -3.534  0.36 13.61 ?  137 ILE   A O    1 
ATOM   2894 C  CB   A ILE   A 1 137 ? 9.144  -10.597 -4.660  0.64 15.60 ?  137 ILE   A CB   1 
ATOM   2895 C  CB   B ILE   A 1 137 ? 9.189  -10.263 -4.780  0.36 14.93 ?  137 ILE   A CB   1 
ATOM   2896 C  CG1  A ILE   A 1 137 ? 7.976  -9.760  -4.126  0.64 17.34 ?  137 ILE   A CG1  1 
ATOM   2897 C  CG1  B ILE   A 1 137 ? 7.996  -9.403  -4.355  0.36 16.26 ?  137 ILE   A CG1  1 
ATOM   2898 C  CG2  A ILE   A 1 137 ? 8.830  -12.090 -4.539  0.64 16.06 ?  137 ILE   A CG2  1 
ATOM   2899 C  CG2  B ILE   A 1 137 ? 8.830  -11.746 -4.704  0.36 15.11 ?  137 ILE   A CG2  1 
ATOM   2900 C  CD1  A ILE   A 1 137 ? 6.693  -9.919  -4.913  0.64 19.07 ?  137 ILE   A CD1  1 
ATOM   2901 C  CD1  B ILE   A 1 137 ? 6.731  -9.731  -5.116  0.36 17.47 ?  137 ILE   A CD1  1 
ATOM   2902 H  H    A ILE   A 1 137 ? 10.308 -8.435  -4.666  0.64 16.71 ?  137 ILE   A H    1 
ATOM   2903 H  H    B ILE   A 1 137 ? 10.378 -8.122  -4.672  0.36 16.33 ?  137 ILE   A H    1 
ATOM   2904 H  HA   A ILE   A 1 137 ? 10.291 -10.412 -2.969  0.64 16.98 ?  137 ILE   A HA   1 
ATOM   2905 H  HA   B ILE   A 1 137 ? 10.186 -10.104 -2.990  0.36 16.76 ?  137 ILE   A HA   1 
ATOM   2906 H  HB   A ILE   A 1 137 ? 9.263  -10.393 -5.598  0.64 18.83 ?  137 ILE   A HB   1 
ATOM   2907 H  HB   B ILE   A 1 137 ? 9.397  -10.045 -5.701  0.36 18.03 ?  137 ILE   A HB   1 
ATOM   2908 H  HG12 A ILE   A 1 137 ? 7.801  -10.018 -3.208  0.64 20.93 ?  137 ILE   A HG12 1 
ATOM   2909 H  HG12 B ILE   A 1 137 ? 7.824  -9.542  -3.410  0.36 19.62 ?  137 ILE   A HG12 1 
ATOM   2910 H  HG13 A ILE   A 1 137 ? 8.232  -8.822  -4.158  0.64 20.93 ?  137 ILE   A HG13 1 
ATOM   2911 H  HG13 B ILE   A 1 137 ? 8.205  -8.467  -4.517  0.36 19.62 ?  137 ILE   A HG13 1 
ATOM   2912 H  HG21 A ILE   A 1 137 ? 7.932  -12.266 -4.865  0.64 19.39 ?  137 ILE   A HG21 1 
ATOM   2913 H  HG21 B ILE   A 1 137 ? 8.754  -12.087 -5.608  0.36 18.25 ?  137 ILE   A HG21 1 
ATOM   2914 H  HG22 A ILE   A 1 137 ? 9.468  -12.592 -5.068  0.64 19.39 ?  137 ILE   A HG22 1 
ATOM   2915 H  HG22 B ILE   A 1 137 ? 9.512  -12.230 -4.223  0.36 18.25 ?  137 ILE   A HG22 1 
ATOM   2916 H  HG23 A ILE   A 1 137 ? 8.893  -12.349 -3.608  0.64 19.39 ?  137 ILE   A HG23 1 
ATOM   2917 H  HG23 B ILE   A 1 137 ? 7.986  -11.843 -4.242  0.36 18.25 ?  137 ILE   A HG23 1 
ATOM   2918 H  HD11 A ILE   A 1 137 ? 5.978  -10.159 -4.305  0.64 23.00 ?  137 ILE   A HD11 1 
ATOM   2919 H  HD11 B ILE   A 1 137 ? 6.017  -9.879  -4.479  0.36 21.08 ?  137 ILE   A HD11 1 
ATOM   2920 H  HD12 A ILE   A 1 137 ? 6.496  -9.078  -5.349  0.64 23.00 ?  137 ILE   A HD12 1 
ATOM   2921 H  HD12 B ILE   A 1 137 ? 6.521  -8.990  -5.694  0.36 21.08 ?  137 ILE   A HD12 1 
ATOM   2922 H  HD13 A ILE   A 1 137 ? 6.807  -10.611 -5.583  0.64 23.00 ?  137 ILE   A HD13 1 
ATOM   2923 H  HD13 B ILE   A 1 137 ? 6.864  -10.528 -5.653  0.36 21.08 ?  137 ILE   A HD13 1 
ATOM   2924 N  N    A HIS   A 1 138 ? 12.257 -10.820 -5.433  0.64 13.89 ?  138 HIS   A N    1 
ATOM   2925 N  N    B HIS   A 1 138 ? 12.249 -10.608 -5.386  0.36 13.99 ?  138 HIS   A N    1 
ATOM   2926 C  CA   A HIS   A 1 138 ? 13.457 -11.545 -5.832  0.64 14.01 ?  138 HIS   A CA   1 
ATOM   2927 C  CA   B HIS   A 1 138 ? 13.371 -11.432 -5.825  0.36 13.74 ?  138 HIS   A CA   1 
ATOM   2928 C  C    A HIS   A 1 138 ? 14.582 -11.371 -4.816  0.64 13.53 ?  138 HIS   A C    1 
ATOM   2929 C  C    B HIS   A 1 138 ? 14.539 -11.343 -4.849  0.36 13.44 ?  138 HIS   A C    1 
ATOM   2930 O  O    A HIS   A 1 138 ? 15.249 -12.348 -4.449  0.64 13.91 ?  138 HIS   A O    1 
ATOM   2931 O  O    B HIS   A 1 138 ? 15.194 -12.351 -4.552  0.36 13.73 ?  138 HIS   A O    1 
ATOM   2932 C  CB   A HIS   A 1 138 ? 13.895 -11.110 -7.228  0.64 15.10 ?  138 HIS   A CB   1 
ATOM   2933 C  CB   B HIS   A 1 138 ? 13.791 -10.982 -7.225  0.36 14.01 ?  138 HIS   A CB   1 
ATOM   2934 C  CG   A HIS   A 1 138 ? 15.148 -11.783 -7.690  0.64 16.33 ?  138 HIS   A CG   1 
ATOM   2935 C  CG   B HIS   A 1 138 ? 15.080 -11.577 -7.694  0.36 14.51 ?  138 HIS   A CG   1 
ATOM   2936 N  ND1  A HIS   A 1 138 ? 15.228 -13.143 -7.898  0.64 17.71 ?  138 HIS   A ND1  1 
ATOM   2937 N  ND1  B HIS   A 1 138 ? 15.216 -12.912 -8.008  0.36 15.33 ?  138 HIS   A ND1  1 
ATOM   2938 C  CD2  A HIS   A 1 138 ? 16.378 -11.287 -7.957  0.64 16.72 ?  138 HIS   A CD2  1 
ATOM   2939 C  CD2  B HIS   A 1 138 ? 16.292 -11.014 -7.910  0.36 14.61 ?  138 HIS   A CD2  1 
ATOM   2940 C  CE1  A HIS   A 1 138 ? 16.451 -13.454 -8.288  0.64 18.19 ?  138 HIS   A CE1  1 
ATOM   2941 C  CE1  B HIS   A 1 138 ? 16.458 -13.145 -8.395  0.36 15.43 ?  138 HIS   A CE1  1 
ATOM   2942 N  NE2  A HIS   A 1 138 ? 17.170 -12.347 -8.330  0.64 17.44 ?  138 HIS   A NE2  1 
ATOM   2943 N  NE2  B HIS   A 1 138 ? 17.132 -12.010 -8.344  0.36 14.89 ?  138 HIS   A NE2  1 
ATOM   2944 H  H    A HIS   A 1 138 ? 12.026 -10.186 -5.971  0.64 16.79 ?  138 HIS   A H    1 
ATOM   2945 H  H    B HIS   A 1 138 ? 12.062 -9.952  -5.914  0.36 16.90 ?  138 HIS   A H    1 
ATOM   2946 H  HA   A HIS   A 1 138 ? 13.244 -12.488 -5.880  0.64 16.92 ?  138 HIS   A HA   1 
ATOM   2947 H  HA   B HIS   A 1 138 ? 13.085 -12.355 -5.879  0.36 16.60 ?  138 HIS   A HA   1 
ATOM   2948 H  HB2  A HIS   A 1 138 ? 13.188 -11.326 -7.864  0.64 18.23 ?  138 HIS   A HB2  1 
ATOM   2949 H  HB2  B HIS   A 1 138 ? 13.099 -11.240 -7.858  0.36 16.93 ?  138 HIS   A HB2  1 
ATOM   2950 H  HB3  A HIS   A 1 138 ? 14.051 -10.153 -7.229  0.64 18.23 ?  138 HIS   A HB3  1 
ATOM   2951 H  HB3  B HIS   A 1 138 ? 13.891 -10.017 -7.229  0.36 16.93 ?  138 HIS   A HB3  1 
ATOM   2952 H  HD1  A HIS   A 1 138 ? 14.578 -13.700 -7.798  0.64 21.37 ?  138 HIS   A HD1  1 
ATOM   2953 H  HD1  B HIS   A 1 138 ? 14.589 -13.500 -7.959  0.36 18.51 ?  138 HIS   A HD1  1 
ATOM   2954 H  HD2  A HIS   A 1 138 ? 16.631 -10.392 -7.901  0.64 20.18 ?  138 HIS   A HD2  1 
ATOM   2955 H  HD2  B HIS   A 1 138 ? 16.513 -10.120 -7.788  0.36 17.65 ?  138 HIS   A HD2  1 
ATOM   2956 H  HE1  A HIS   A 1 138 ? 16.754 -14.306 -8.493  0.64 21.94 ?  138 HIS   A HE1  1 
ATOM   2957 H  HE1  B HIS   A 1 138 ? 16.797 -13.972 -8.656  0.36 18.63 ?  138 HIS   A HE1  1 
ATOM   2958 N  N    . SER   A 1 139 ? 14.810 -10.143 -4.341  1.00 12.94 ?  139 SER   A N    1 
ATOM   2959 C  CA   . SER   A 1 139 ? 15.878 -9.952  -3.369  1.00 12.69 ?  139 SER   A CA   1 
ATOM   2960 C  C    . SER   A 1 139 ? 15.654 -10.790 -2.116  1.00 12.59 ?  139 SER   A C    1 
ATOM   2961 O  O    . SER   A 1 139 ? 16.603 -11.373 -1.576  1.00 12.63 ?  139 SER   A O    1 
ATOM   2962 C  CB   . SER   A 1 139 ? 16.008 -8.475  -3.012  1.00 12.92 ?  139 SER   A CB   1 
ATOM   2963 O  OG   . SER   A 1 139 ? 17.080 -8.290  -2.106  1.00 13.14 ?  139 SER   A OG   1 
ATOM   2964 H  H    A SER   A 1 139 ? 14.375 -9.431  -4.553  0.64 15.64 ?  139 SER   A H    1 
ATOM   2965 H  H    B SER   A 1 139 ? 14.384 -9.421  -4.539  0.36 15.64 ?  139 SER   A H    1 
ATOM   2966 H  HA   . SER   A 1 139 ? 16.718 -10.235 -3.764  1.00 15.34 ?  139 SER   A HA   1 
ATOM   2967 H  HB2  . SER   A 1 139 ? 16.185 -7.964  -3.814  1.00 15.62 ?  139 SER   A HB2  1 
ATOM   2968 H  HB3  . SER   A 1 139 ? 15.182 -8.172  -2.598  1.00 15.62 ?  139 SER   A HB3  1 
ATOM   2969 H  HG   . SER   A 1 139 ? 17.149 -7.473  -1.896  1.00 15.88 ?  139 SER   A HG   1 
ATOM   2970 N  N    . LEU   A 1 140 ? 14.413 -10.856 -1.632  1.00 12.31 ?  140 LEU   A N    1 
ATOM   2971 C  CA   . LEU   A 1 140 ? 14.137 -11.669 -0.452  1.00 12.50 ?  140 LEU   A CA   1 
ATOM   2972 C  C    . LEU   A 1 140 ? 14.406 -13.144 -0.729  1.00 12.40 ?  140 LEU   A C    1 
ATOM   2973 O  O    . LEU   A 1 140 ? 14.956 -13.857 0.122   1.00 13.30 ?  140 LEU   A O    1 
ATOM   2974 C  CB   . LEU   A 1 140 ? 12.693 -11.446 0.000   1.00 12.78 ?  140 LEU   A CB   1 
ATOM   2975 C  CG   . LEU   A 1 140 ? 12.218 -12.295 1.177   1.00 13.45 ?  140 LEU   A CG   1 
ATOM   2976 C  CD1  . LEU   A 1 140 ? 13.122 -12.138 2.388   1.00 13.96 ?  140 LEU   A CD1  1 
ATOM   2977 C  CD2  . LEU   A 1 140 ? 10.762 -11.956 1.525   1.00 14.07 ?  140 LEU   A CD2  1 
ATOM   2978 H  H    . LEU   A 1 140 ? 13.730 -10.446 -1.957  1.00 14.89 ?  140 LEU   A H    1 
ATOM   2979 H  HA   . LEU   A 1 140 ? 14.718 -11.391 0.270   1.00 15.12 ?  140 LEU   A HA   1 
ATOM   2980 H  HB2  . LEU   A 1 140 ? 12.589 -10.523 0.262   1.00 15.45 ?  140 LEU   A HB2  1 
ATOM   2981 H  HB3  . LEU   A 1 140 ? 12.103 -11.642 -0.746  1.00 15.45 ?  140 LEU   A HB3  1 
ATOM   2982 H  HG   . LEU   A 1 140 ? 12.229 -13.234 0.916   1.00 16.26 ?  140 LEU   A HG   1 
ATOM   2983 H  HD11 . LEU   A 1 140 ? 12.733 -12.615 3.139   1.00 16.86 ?  140 LEU   A HD11 1 
ATOM   2984 H  HD12 . LEU   A 1 140 ? 13.992 -12.517 2.176   1.00 16.86 ?  140 LEU   A HD12 1 
ATOM   2985 H  HD13 . LEU   A 1 140 ? 13.208 -11.200 2.595   1.00 16.86 ?  140 LEU   A HD13 1 
ATOM   2986 H  HD21 . LEU   A 1 140 ? 10.474 -12.511 2.275   1.00 17.00 ?  140 LEU   A HD21 1 
ATOM   2987 H  HD22 . LEU   A 1 140 ? 10.702 -11.022 1.769   1.00 17.00 ?  140 LEU   A HD22 1 
ATOM   2988 H  HD23 . LEU   A 1 140 ? 10.196 -12.136 0.756   1.00 17.00 ?  140 LEU   A HD23 1 
ATOM   2989 N  N    . ARG   A 1 141 ? 14.018 -13.619 -1.916  1.00 12.92 ?  141 ARG   A N    1 
ATOM   2990 C  CA   . ARG   A 1 141 ? 14.261 -15.009 -2.285  1.00 14.21 ?  141 ARG   A CA   1 
ATOM   2991 C  C    . ARG   A 1 141 ? 15.757 -15.315 -2.300  1.00 13.53 ?  141 ARG   A C    1 
ATOM   2992 O  O    . ARG   A 1 141 ? 16.208 -16.330 -1.752  1.00 13.99 ?  141 ARG   A O    1 
ATOM   2993 C  CB   . ARG   A 1 141 ? 13.635 -15.263 -3.660  1.00 15.55 ?  141 ARG   A CB   1 
ATOM   2994 C  CG   . ARG   A 1 141 ? 13.607 -16.713 -4.109  1.00 18.26 ?  141 ARG   A CG   1 
ATOM   2995 C  CD   . ARG   A 1 141 ? 12.579 -17.475 -3.332  1.00 20.33 ?  141 ARG   A CD   1 
ATOM   2996 N  NE   . ARG   A 1 141 ? 13.194 -18.229 -2.255  1.00 20.98 ?  141 ARG   A NE   1 
ATOM   2997 C  CZ   . ARG   A 1 141 ? 12.516 -18.813 -1.275  1.00 21.83 ?  141 ARG   A CZ   1 
ATOM   2998 N  NH1  . ARG   A 1 141 ? 11.220 -18.609 -1.114  1.00 21.08 ?  141 ARG   A NH1  1 
ATOM   2999 N  NH2  . ARG   A 1 141 ? 13.157 -19.620 -0.434  1.00 23.33 ?  141 ARG   A NH2  1 
ATOM   3000 H  H    . ARG   A 1 141 ? 13.615 -13.156 -2.522  1.00 15.62 ?  141 ARG   A H    1 
ATOM   3001 H  HA   . ARG   A 1 141 ? 13.837 -15.593 -1.643  1.00 17.17 ?  141 ARG   A HA   1 
ATOM   3002 H  HB2  . ARG   A 1 141 ? 12.718 -14.942 -3.650  1.00 18.77 ?  141 ARG   A HB2  1 
ATOM   3003 H  HB3  . ARG   A 1 141 ? 14.138 -14.766 -4.325  1.00 18.77 ?  141 ARG   A HB3  1 
ATOM   3004 H  HG2  . ARG   A 1 141 ? 13.379 -16.759 -5.054  1.00 22.02 ?  141 ARG   A HG2  1 
ATOM   3005 H  HG3  . ARG   A 1 141 ? 14.477 -17.120 -3.956  1.00 22.02 ?  141 ARG   A HG3  1 
ATOM   3006 H  HD2  . ARG   A 1 141 ? 11.945 -16.854 -2.935  1.00 24.51 ?  141 ARG   A HD2  1 
ATOM   3007 H  HD3  . ARG   A 1 141 ? 12.115 -18.090 -3.923  1.00 24.51 ?  141 ARG   A HD3  1 
ATOM   3008 H  HE   . ARG   A 1 141 ? 14.035 -18.390 -2.307  1.00 25.29 ?  141 ARG   A HE   1 
ATOM   3009 H  HH11 . ARG   A 1 141 ? 10.787 -18.104 -1.659  1.00 25.41 ?  141 ARG   A HH11 1 
ATOM   3010 H  HH12 . ARG   A 1 141 ? 10.798 -18.998 -0.469  1.00 25.41 ?  141 ARG   A HH12 1 
ATOM   3011 H  HH21 . ARG   A 1 141 ? 14.000 -19.758 -0.526  1.00 28.11 ?  141 ARG   A HH21 1 
ATOM   3012 H  HH22 . ARG   A 1 141 ? 12.730 -19.995 0.215   1.00 28.11 ?  141 ARG   A HH22 1 
ATOM   3013 N  N    . VAL   A 1 142 ? 16.550 -14.447 -2.930  1.00 13.07 ?  142 VAL   A N    1 
ATOM   3014 C  CA   . VAL   A 1 142 ? 17.994 -14.661 -2.955  1.00 12.99 ?  142 VAL   A CA   1 
ATOM   3015 C  C    . VAL   A 1 142 ? 18.560 -14.641 -1.541  1.00 12.55 ?  142 VAL   A C    1 
ATOM   3016 O  O    . VAL   A 1 142 ? 19.427 -15.453 -1.195  1.00 13.20 ?  142 VAL   A O    1 
ATOM   3017 C  CB   . VAL   A 1 142 ? 18.695 -13.644 -3.876  1.00 13.38 ?  142 VAL   A CB   1 
ATOM   3018 C  CG1  . VAL   A 1 142 ? 20.205 -13.869 -3.845  1.00 13.50 ?  142 VAL   A CG1  1 
ATOM   3019 C  CG2  . VAL   A 1 142 ? 18.191 -13.772 -5.299  1.00 14.49 ?  142 VAL   A CG2  1 
ATOM   3020 H  H    . VAL   A 1 142 ? 16.285 -13.729 -3.343  1.00 15.79 ?  142 VAL   A H    1 
ATOM   3021 H  HA   . VAL   A 1 142 ? 18.164 -15.536 -3.326  1.00 15.71 ?  142 VAL   A HA   1 
ATOM   3022 H  HB   . VAL   A 1 142 ? 18.522 -12.738 -3.567  1.00 16.17 ?  142 VAL   A HB   1 
ATOM   3023 H  HG11 . VAL   A 1 142 ? 20.615 -13.380 -4.577  1.00 16.32 ?  142 VAL   A HG11 1 
ATOM   3024 H  HG12 . VAL   A 1 142 ? 20.561 -13.549 -3.000  1.00 16.32 ?  142 VAL   A HG12 1 
ATOM   3025 H  HG13 . VAL   A 1 142 ? 20.385 -14.817 -3.943  1.00 16.32 ?  142 VAL   A HG13 1 
ATOM   3026 H  HG21 . VAL   A 1 142 ? 18.672 -13.138 -5.859  1.00 17.51 ?  142 VAL   A HG21 1 
ATOM   3027 H  HG22 . VAL   A 1 142 ? 18.362 -14.676 -5.606  1.00 17.51 ?  142 VAL   A HG22 1 
ATOM   3028 H  HG23 . VAL   A 1 142 ? 17.248 -13.582 -5.313  1.00 17.51 ?  142 VAL   A HG23 1 
ATOM   3029 N  N    . CYS   A 1 143 ? 18.088 -13.716 -0.704  1.00 12.33 ?  143 CYS   A N    1 
ATOM   3030 C  CA   . CYS   A 1 143 ? 18.551 -13.665 0.679   1.00 12.51 ?  143 CYS   A CA   1 
ATOM   3031 C  C    . CYS   A 1 143 ? 18.325 -15.004 1.375   1.00 12.87 ?  143 CYS   A C    1 
ATOM   3032 O  O    . CYS   A 1 143 ? 19.245 -15.587 1.953   1.00 12.66 ?  143 CYS   A O    1 
ATOM   3033 C  CB   . CYS   A 1 143 ? 17.822 -12.548 1.421   1.00 12.68 ?  143 CYS   A CB   1 
ATOM   3034 S  SG   . CYS   A 1 143 ? 18.314 -12.369 3.143   1.00 13.11 ?  143 CYS   A SG   1 
ATOM   3035 H  H    . CYS   A 1 143 ? 17.507 -13.118 -0.912  1.00 14.91 ?  143 CYS   A H    1 
ATOM   3036 H  HA   . CYS   A 1 143 ? 19.500 -13.477 0.691   1.00 15.12 ?  143 CYS   A HA   1 
ATOM   3037 H  HB2  . CYS   A 1 143 ? 17.998 -11.707 0.970   1.00 15.33 ?  143 CYS   A HB2  1 
ATOM   3038 H  HB3  . CYS   A 1 143 ? 16.871 -12.732 1.400   1.00 15.33 ?  143 CYS   A HB3  1 
ATOM   3039 H  HG   . CYS   A 1 143 ? 17.715 -11.443 3.610   1.00 15.85 ?  143 CYS   A HG   1 
ATOM   3040 N  N    . VAL   A 1 144 ? 17.093 -15.510 1.322   1.00 13.54 ?  144 VAL   A N    1 
ATOM   3041 C  CA   . VAL   A 1 144 ? 16.753 -16.744 2.024   1.00 14.59 ?  144 VAL   A CA   1 
ATOM   3042 C  C    . VAL   A 1 144 ? 17.565 -17.915 1.493   1.00 14.33 ?  144 VAL   A C    1 
ATOM   3043 O  O    . VAL   A 1 144 ? 17.941 -18.820 2.249   1.00 14.98 ?  144 VAL   A O    1 
ATOM   3044 C  CB   . VAL   A 1 144 ? 15.235 -16.986 1.916   1.00 17.27 ?  144 VAL   A CB   1 
ATOM   3045 C  CG1  . VAL   A 1 144 ? 14.878 -18.416 2.263   1.00 19.26 ?  144 VAL   A CG1  1 
ATOM   3046 C  CG2  . VAL   A 1 144 ? 14.494 -15.978 2.799   1.00 17.19 ?  144 VAL   A CG2  1 
ATOM   3047 H  H    . VAL   A 1 144 ? 16.434 -15.151 0.887   1.00 16.36 ?  144 VAL   A H    1 
ATOM   3048 H  HA   . VAL   A 1 144 ? 16.965 -16.635 2.956   1.00 17.63 ?  144 VAL   A HA   1 
ATOM   3049 H  HB   . VAL   A 1 144 ? 14.955 -16.823 0.997   1.00 20.84 ?  144 VAL   A HB   1 
ATOM   3050 H  HG11 . VAL   A 1 144 ? 13.927 -18.464 2.456   1.00 23.23 ?  144 VAL   A HG11 1 
ATOM   3051 H  HG12 . VAL   A 1 144 ? 15.089 -18.987 1.510   1.00 23.23 ?  144 VAL   A HG12 1 
ATOM   3052 H  HG13 . VAL   A 1 144 ? 15.385 -18.684 3.043   1.00 23.23 ?  144 VAL   A HG13 1 
ATOM   3053 H  HG21 . VAL   A 1 144 ? 13.537 -16.139 2.739   1.00 20.74 ?  144 VAL   A HG21 1 
ATOM   3054 H  HG22 . VAL   A 1 144 ? 14.786 -16.082 3.718   1.00 20.74 ?  144 VAL   A HG22 1 
ATOM   3055 H  HG23 . VAL   A 1 144 ? 14.690 -15.074 2.494   1.00 20.74 ?  144 VAL   A HG23 1 
ATOM   3056 N  N    . ASP   A 1 145 ? 17.828 -17.933 0.188   1.00 14.77 ?  145 ASP   A N    1 
ATOM   3057 C  CA   . ASP   A 1 145 ? 18.539 -19.038 -0.443  1.00 15.19 ?  145 ASP   A CA   1 
ATOM   3058 C  C    . ASP   A 1 145 ? 20.061 -18.895 -0.398  1.00 15.03 ?  145 ASP   A C    1 
ATOM   3059 O  O    . ASP   A 1 145 ? 20.762 -19.790 -0.885  1.00 16.64 ?  145 ASP   A O    1 
ATOM   3060 C  CB   . ASP   A 1 145 ? 18.092 -19.179 -1.899  1.00 16.74 ?  145 ASP   A CB   1 
ATOM   3061 C  CG   . ASP   A 1 145 ? 16.644 -19.618 -2.029  1.00 18.74 ?  145 ASP   A CG   1 
ATOM   3062 O  OD1  . ASP   A 1 145 ? 16.079 -20.160 -1.054  1.00 19.22 ?  145 ASP   A OD1  1 
ATOM   3063 O  OD2  . ASP   A 1 145 ? 16.069 -19.404 -3.113  1.00 20.05 -1 145 ASP   A OD2  1 
ATOM   3064 H  H    . ASP   A 1 145 ? 17.585 -17.315 -0.366  1.00 17.84 ?  145 ASP   A H    1 
ATOM   3065 H  HA   . ASP   A 1 145 ? 18.304 -19.859 0.014   1.00 18.34 ?  145 ASP   A HA   1 
ATOM   3066 H  HB2  . ASP   A 1 145 ? 18.197 -18.321 -2.346  1.00 20.20 ?  145 ASP   A HB2  1 
ATOM   3067 H  HB3  . ASP   A 1 145 ? 18.642 -19.847 -2.336  1.00 20.20 ?  145 ASP   A HB3  1 
ATOM   3068 N  N    . THR   A 1 146 ? 20.592 -17.804 0.155   1.00 13.55 ?  146 THR   A N    1 
ATOM   3069 C  CA   . THR   A 1 146 ? 22.032 -17.554 0.175   1.00 12.78 ?  146 THR   A CA   1 
ATOM   3070 C  C    . THR   A 1 146 ? 22.578 -17.379 1.580   1.00 12.71 ?  146 THR   A C    1 
ATOM   3071 O  O    . THR   A 1 146 ? 23.656 -17.908 1.894   1.00 14.02 ?  146 THR   A O    1 
ATOM   3072 C  CB   . THR   A 1 146 ? 22.363 -16.302 -0.660  1.00 12.91 ?  146 THR   A CB   1 
ATOM   3073 O  OG1  . THR   A 1 146 ? 21.835 -16.461 -1.979  1.00 13.45 ?  146 THR   A OG1  1 
ATOM   3074 C  CG2  . THR   A 1 146 ? 23.866 -16.084 -0.753  1.00 13.46 ?  146 THR   A CG2  1 
ATOM   3075 H  H    . THR   A 1 146 ? 20.127 -17.181 0.527   1.00 16.38 ?  146 THR   A H    1 
ATOM   3076 H  HA   . THR   A 1 146 ? 22.490 -18.303 -0.226  1.00 15.45 ?  146 THR   A HA   1 
ATOM   3077 H  HB   . THR   A 1 146 ? 21.970 -15.516 -0.240  1.00 15.61 ?  146 THR   A HB   1 
ATOM   3078 H  HG1  . THR   A 1 146 ? 20.998 -16.529 -1.942  1.00 16.25 ?  146 THR   A HG1  1 
ATOM   3079 H  HG21 . THR   A 1 146 ? 24.062 -15.406 -1.417  1.00 16.26 ?  146 THR   A HG21 1 
ATOM   3080 H  HG22 . THR   A 1 146 ? 24.218 -15.797 0.104   1.00 16.26 ?  146 THR   A HG22 1 
ATOM   3081 H  HG23 . THR   A 1 146 ? 24.302 -16.912 -1.012  1.00 16.26 ?  146 THR   A HG23 1 
ATOM   3082 N  N    . VAL   A 1 147 ? 21.904 -16.591 2.411   1.00 12.66 ?  147 VAL   A N    1 
ATOM   3083 C  CA   . VAL   A 1 147 ? 22.393 -16.294 3.750   1.00 12.86 ?  147 VAL   A CA   1 
ATOM   3084 C  C    . VAL   A 1 147 ? 22.071 -17.462 4.670   1.00 13.28 ?  147 VAL   A C    1 
ATOM   3085 O  O    . VAL   A 1 147 ? 20.928 -17.935 4.723   1.00 13.78 ?  147 VAL   A O    1 
ATOM   3086 C  CB   . VAL   A 1 147 ? 21.780 -14.985 4.269   1.00 13.05 ?  147 VAL   A CB   1 
ATOM   3087 C  CG1  . VAL   A 1 147 ? 22.320 -14.670 5.646   1.00 13.78 ?  147 VAL   A CG1  1 
ATOM   3088 C  CG2  . VAL   A 1 147 ? 22.045 -13.842 3.297   1.00 13.13 ?  147 VAL   A CG2  1 
ATOM   3089 H  H    . VAL   A 1 147 ? 21.151 -16.216 2.223   1.00 15.31 ?  147 VAL   A H    1 
ATOM   3090 H  HA   . VAL   A 1 147 ? 23.358 -16.185 3.716   1.00 15.55 ?  147 VAL   A HA   1 
ATOM   3091 H  HB   . VAL   A 1 147 ? 20.822 -15.095 4.346   1.00 15.77 ?  147 VAL   A HB   1 
ATOM   3092 H  HG11 . VAL   A 1 147 ? 22.074 -13.765 5.881   1.00 16.66 ?  147 VAL   A HG11 1 
ATOM   3093 H  HG12 . VAL   A 1 147 ? 21.938 -15.295 6.284   1.00 16.66 ?  147 VAL   A HG12 1 
ATOM   3094 H  HG13 . VAL   A 1 147 ? 23.286 -14.760 5.633   1.00 16.66 ?  147 VAL   A HG13 1 
ATOM   3095 H  HG21 . VAL   A 1 147 ? 21.725 -13.016 3.692   1.00 15.87 ?  147 VAL   A HG21 1 
ATOM   3096 H  HG22 . VAL   A 1 147 ? 22.995 -13.786 3.129   1.00 15.87 ?  147 VAL   A HG22 1 
ATOM   3097 H  HG23 . VAL   A 1 147 ? 21.568 -14.019 2.471   1.00 15.87 ?  147 VAL   A HG23 1 
ATOM   3098 N  N    . ARG   A 1 148 ? 23.089 -17.929 5.391   1.00 13.61 ?  148 ARG   A N    1 
ATOM   3099 C  CA   . ARG   A 1 148 ? 22.956 -19.005 6.357   1.00 13.74 ?  148 ARG   A CA   1 
ATOM   3100 C  C    . ARG   A 1 148 ? 23.080 -18.531 7.793   1.00 13.91 ?  148 ARG   A C    1 
ATOM   3101 O  O    . ARG   A 1 148 ? 22.677 -19.260 8.708   1.00 15.73 ?  148 ARG   A O    1 
ATOM   3102 C  CB   . ARG   A 1 148 ? 23.997 -20.102 6.087   1.00 14.52 ?  148 ARG   A CB   1 
ATOM   3103 C  CG   . ARG   A 1 148 ? 23.852 -20.742 4.717   1.00 15.80 ?  148 ARG   A CG   1 
ATOM   3104 C  CD   . ARG   A 1 148 ? 24.942 -21.773 4.434   1.00 16.49 ?  148 ARG   A CD   1 
ATOM   3105 N  NE   . ARG   A 1 148 ? 26.279 -21.191 4.466   1.00 16.46 ?  148 ARG   A NE   1 
ATOM   3106 C  CZ   . ARG   A 1 148 ? 26.795 -20.456 3.489   1.00 15.40 ?  148 ARG   A CZ   1 
ATOM   3107 N  NH1  . ARG   A 1 148 ? 26.121 -20.223 2.374   1.00 16.12 ?  148 ARG   A NH1  1 
ATOM   3108 N  NH2  . ARG   A 1 148 ? 28.013 -19.932 3.639   1.00 15.94 ?  148 ARG   A NH2  1 
ATOM   3109 H  H    . ARG   A 1 148 ? 23.894 -17.622 5.325   1.00 16.44 ?  148 ARG   A H    1 
ATOM   3110 H  HA   . ARG   A 1 148 ? 22.081 -19.400 6.254   1.00 16.60 ?  148 ARG   A HA   1 
ATOM   3111 H  HB2  . ARG   A 1 148 ? 24.884 -19.725 6.145   1.00 17.54 ?  148 ARG   A HB2  1 
ATOM   3112 H  HB3  . ARG   A 1 148 ? 23.889 -20.806 6.749   1.00 17.54 ?  148 ARG   A HB3  1 
ATOM   3113 H  HG2  . ARG   A 1 148 ? 22.991 -21.185 4.665   1.00 19.08 ?  148 ARG   A HG2  1 
ATOM   3114 H  HG3  . ARG   A 1 148 ? 23.908 -20.046 4.041   1.00 19.08 ?  148 ARG   A HG3  1 
ATOM   3115 H  HD2  . ARG   A 1 148 ? 24.898 -22.466 5.107   1.00 19.90 ?  148 ARG   A HD2  1 
ATOM   3116 H  HD3  . ARG   A 1 148 ? 24.794 -22.151 3.553   1.00 19.90 ?  148 ARG   A HD3  1 
ATOM   3117 H  HE   . ARG   A 1 148 ? 26.762 -21.331 5.159   1.00 19.87 ?  148 ARG   A HE   1 
ATOM   3118 H  HH11 . ARG   A 1 148 ? 25.332 -20.540 2.268   1.00 19.46 ?  148 ARG   A HH11 1 
ATOM   3119 H  HH12 . ARG   A 1 148 ? 26.472 -19.732 1.756   1.00 19.46 ?  148 ARG   A HH12 1 
ATOM   3120 H  HH21 . ARG   A 1 148 ? 28.455 -20.073 4.360   1.00 19.24 ?  148 ARG   A HH21 1 
ATOM   3121 H  HH22 . ARG   A 1 148 ? 28.354 -19.448 3.012   1.00 19.24 ?  148 ARG   A HH22 1 
ATOM   3122 N  N    . THR   A 1 149 ? 23.628 -17.337 8.004   1.00 14.11 ?  149 THR   A N    1 
ATOM   3123 C  CA   . THR   A 1 149 ? 23.704 -16.737 9.322   1.00 14.34 ?  149 THR   A CA   1 
ATOM   3124 C  C    . THR   A 1 149 ? 22.378 -16.037 9.629   1.00 13.62 ?  149 THR   A C    1 
ATOM   3125 O  O    . THR   A 1 149 ? 21.447 -16.025 8.816   1.00 14.18 ?  149 THR   A O    1 
ATOM   3126 C  CB   . THR   A 1 149 ? 24.906 -15.801 9.381   1.00 14.77 ?  149 THR   A CB   1 
ATOM   3127 O  OG1  . THR   A 1 149 ? 24.777 -14.862 8.314   1.00 14.50 ?  149 THR   A OG1  1 
ATOM   3128 C  CG2  . THR   A 1 149 ? 26.218 -16.599 9.250   1.00 15.38 ?  149 THR   A CG2  1 
ATOM   3129 H  H    . THR   A 1 149 ? 23.970 -16.843 7.382   1.00 17.04 ?  149 THR   A H    1 
ATOM   3130 H  HA   . THR   A 1 149 ? 23.830 -17.444 9.976   1.00 17.32 ?  149 THR   A HA   1 
ATOM   3131 H  HB   . THR   A 1 149 ? 24.901 -15.338 10.230  1.00 17.84 ?  149 THR   A HB   1 
ATOM   3132 H  HG1  . THR   A 1 149 ? 25.431 -14.335 8.319   1.00 17.51 ?  149 THR   A HG1  1 
ATOM   3133 H  HG21 . THR   A 1 149 ? 26.976 -15.999 9.309   1.00 18.57 ?  149 THR   A HG21 1 
ATOM   3134 H  HG22 . THR   A 1 149 ? 26.283 -17.259 9.961   1.00 18.57 ?  149 THR   A HG22 1 
ATOM   3135 H  HG23 . THR   A 1 149 ? 26.247 -17.061 8.395   1.00 18.57 ?  149 THR   A HG23 1 
ATOM   3136 N  N    . ASN   A 1 150 ? 22.256 -15.499 10.837  1.00 13.97 ?  150 ASN   A N    1 
ATOM   3137 C  CA   . ASN   A 1 150 ? 20.974 -14.978 11.316  1.00 14.44 ?  150 ASN   A CA   1 
ATOM   3138 C  C    . ASN   A 1 150 ? 20.797 -13.540 10.847  1.00 13.60 ?  150 ASN   A C    1 
ATOM   3139 O  O    . ASN   A 1 150 ? 21.543 -12.645 11.262  1.00 14.99 ?  150 ASN   A O    1 
ATOM   3140 C  CB   . ASN   A 1 150 ? 20.899 -15.089 12.835  1.00 17.07 ?  150 ASN   A CB   1 
ATOM   3141 C  CG   . ASN   A 1 150 ? 20.801 -16.522 13.298  1.00 21.28 ?  150 ASN   A CG   1 
ATOM   3142 O  OD1  . ASN   A 1 150 ? 20.196 -17.352 12.623  1.00 22.52 ?  150 ASN   A OD1  1 
ATOM   3143 N  ND2  . ASN   A 1 150 ? 21.403 -16.827 14.446  1.00 23.88 ?  150 ASN   A ND2  1 
ATOM   3144 H  H    . ASN   A 1 150 ? 22.894 -15.438 11.407  1.00 16.89 ?  150 ASN   A H    1 
ATOM   3145 H  HA   . ASN   A 1 150 ? 20.250 -15.519 10.947  1.00 17.44 ?  150 ASN   A HA   1 
ATOM   3146 H  HB2  . ASN   A 1 150 ? 21.697 -14.706 13.225  1.00 20.60 ?  150 ASN   A HB2  1 
ATOM   3147 H  HB3  . ASN   A 1 150 ? 20.110 -14.623 13.154  1.00 20.60 ?  150 ASN   A HB3  1 
ATOM   3148 H  HD21 . ASN   A 1 150 ? 21.380 -17.635 14.756  1.00 28.78 ?  150 ASN   A HD21 1 
ATOM   3149 H  HD22 . ASN   A 1 150 ? 21.821 -16.219 14.892  1.00 28.78 ?  150 ASN   A HD22 1 
ATOM   3150 N  N    . VAL   A 1 151 ? 19.806 -13.315 9.990   1.00 13.14 ?  151 VAL   A N    1 
ATOM   3151 C  CA   . VAL   A 1 151 ? 19.591 -12.011 9.382   1.00 12.98 ?  151 VAL   A CA   1 
ATOM   3152 C  C    . VAL   A 1 151 ? 18.210 -11.483 9.747   1.00 12.87 ?  151 VAL   A C    1 
ATOM   3153 O  O    . VAL   A 1 151 ? 17.194 -12.187 9.609   1.00 14.32 ?  151 VAL   A O    1 
ATOM   3154 C  CB   . VAL   A 1 151 ? 19.880 -12.013 7.866   1.00 14.56 ?  151 VAL   A CB   1 
ATOM   3155 C  CG1  . VAL   A 1 151 ? 19.067 -13.052 7.136   1.00 15.64 ?  151 VAL   A CG1  1 
ATOM   3156 C  CG2  . VAL   A 1 151 ? 19.679 -10.611 7.271   1.00 14.66 ?  151 VAL   A CG2  1 
ATOM   3157 H  H    . VAL   A 1 151 ? 19.240 -13.917 9.739   1.00 15.88 ?  151 VAL   A H    1 
ATOM   3158 H  HA   . VAL   A 1 151 ? 20.238 -11.401 9.771   1.00 15.69 ?  151 VAL   A HA   1 
ATOM   3159 H  HB   . VAL   A 1 151 ? 20.816 -12.243 7.732   1.00 17.59 ?  151 VAL   A HB   1 
ATOM   3160 H  HG11 . VAL   A 1 151 ? 19.236 -12.986 6.183   1.00 18.88 ?  151 VAL   A HG11 1 
ATOM   3161 H  HG12 . VAL   A 1 151 ? 19.325 -13.937 7.452   1.00 18.88 ?  151 VAL   A HG12 1 
ATOM   3162 H  HG13 . VAL   A 1 151 ? 18.124 -12.904 7.315   1.00 18.88 ?  151 VAL   A HG13 1 
ATOM   3163 H  HG21 . VAL   A 1 151 ? 19.995 -10.611 6.351   1.00 17.71 ?  151 VAL   A HG21 1 
ATOM   3164 H  HG22 . VAL   A 1 151 ? 18.735 -10.391 7.292   1.00 17.71 ?  151 VAL   A HG22 1 
ATOM   3165 H  HG23 . VAL   A 1 151 ? 20.184 -9.971  7.792   1.00 17.71 ?  151 VAL   A HG23 1 
ATOM   3166 N  N    A TYR   A 1 152 ? 18.190 -10.240 10.210  0.64 13.23 ?  152 TYR   A N    1 
ATOM   3167 N  N    B TYR   A 1 152 ? 18.199 -10.236 10.225  0.36 12.68 ?  152 TYR   A N    1 
ATOM   3168 C  CA   A TYR   A 1 152 ? 16.980 -9.513  10.555  0.64 13.05 ?  152 TYR   A CA   1 
ATOM   3169 C  CA   B TYR   A 1 152 ? 17.013 -9.512  10.658  0.36 12.09 ?  152 TYR   A CA   1 
ATOM   3170 C  C    A TYR   A 1 152 ? 16.782 -8.428  9.503   0.64 12.20 ?  152 TYR   A C    1 
ATOM   3171 C  C    B TYR   A 1 152 ? 16.823 -8.360  9.688   0.36 11.11 ?  152 TYR   A C    1 
ATOM   3172 O  O    A TYR   A 1 152 ? 17.530 -7.442  9.462   0.64 12.69 ?  152 TYR   A O    1 
ATOM   3173 O  O    B TYR   A 1 152 ? 17.638 -7.430  9.649   0.36 11.42 ?  152 TYR   A O    1 
ATOM   3174 C  CB   A TYR   A 1 152 ? 17.114 -8.968  11.974  0.64 13.99 ?  152 TYR   A CB   1 
ATOM   3175 C  CB   B TYR   A 1 152 ? 17.207 -9.004  12.083  0.36 12.94 ?  152 TYR   A CB   1 
ATOM   3176 C  CG   A TYR   A 1 152 ? 17.114 -10.102 12.971  0.64 14.53 ?  152 TYR   A CG   1 
ATOM   3177 C  CG   B TYR   A 1 152 ? 17.110 -10.110 13.095  0.36 13.72 ?  152 TYR   A CG   1 
ATOM   3178 C  CD1  A TYR   A 1 152 ? 18.283 -10.781 13.302  0.64 15.99 ?  152 TYR   A CD1  1 
ATOM   3179 C  CD1  B TYR   A 1 152 ? 18.187 -10.952 13.344  0.36 14.67 ?  152 TYR   A CD1  1 
ATOM   3180 C  CD2  A TYR   A 1 152 ? 15.930 -10.539 13.541  0.64 15.15 ?  152 TYR   A CD2  1 
ATOM   3181 C  CD2  B TYR   A 1 152 ? 15.930 -10.335 13.786  0.36 13.95 ?  152 TYR   A CD2  1 
ATOM   3182 C  CE1  A TYR   A 1 152 ? 18.274 -11.846 14.190  0.64 16.99 ?  152 TYR   A CE1  1 
ATOM   3183 C  CE1  B TYR   A 1 152 ? 18.094 -11.981 14.259  0.36 15.87 ?  152 TYR   A CE1  1 
ATOM   3184 C  CE2  A TYR   A 1 152 ? 15.906 -11.610 14.432  0.64 16.15 ?  152 TYR   A CE2  1 
ATOM   3185 C  CE2  B TYR   A 1 152 ? 15.825 -11.364 14.706  0.36 15.09 ?  152 TYR   A CE2  1 
ATOM   3186 C  CZ   A TYR   A 1 152 ? 17.082 -12.257 14.752  0.64 17.09 ?  152 TYR   A CZ   1 
ATOM   3187 C  CZ   B TYR   A 1 152 ? 16.910 -12.183 14.940  0.36 16.26 ?  152 TYR   A CZ   1 
ATOM   3188 O  OH   A TYR   A 1 152 ? 17.067 -13.323 15.634  0.64 18.67 ?  152 TYR   A OH   1 
ATOM   3189 O  OH   B TYR   A 1 152 ? 16.815 -13.210 15.852  0.36 18.05 ?  152 TYR   A OH   1 
ATOM   3190 H  H    A TYR   A 1 152 ? 18.911 -9.771  10.328  0.64 15.99 ?  152 TYR   A H    1 
ATOM   3191 H  H    B TYR   A 1 152 ? 18.917 -9.753  10.289  0.36 15.34 ?  152 TYR   A H    1 
ATOM   3192 H  HA   A TYR   A 1 152 ? 16.229 -10.126 10.522  0.64 15.77 ?  152 TYR   A HA   1 
ATOM   3193 H  HA   B TYR   A 1 152 ? 16.239 -10.088 10.622  0.36 14.63 ?  152 TYR   A HA   1 
ATOM   3194 H  HB2  A TYR   A 1 152 ? 17.950 -8.495  12.059  0.64 16.91 ?  152 TYR   A HB2  1 
ATOM   3195 H  HB2  B TYR   A 1 152 ? 18.086 -8.602  12.160  0.36 15.65 ?  152 TYR   A HB2  1 
ATOM   3196 H  HB3  A TYR   A 1 152 ? 16.368 -8.390  12.168  0.64 16.91 ?  152 TYR   A HB3  1 
ATOM   3197 H  HB3  B TYR   A 1 152 ? 16.520 -8.351  12.283  0.36 15.65 ?  152 TYR   A HB3  1 
ATOM   3198 H  HD1  A TYR   A 1 152 ? 19.085 -10.516 12.925  0.64 19.30 ?  152 TYR   A HD1  1 
ATOM   3199 H  HD1  B TYR   A 1 152 ? 18.986 -10.816 12.881  0.36 17.72 ?  152 TYR   A HD1  1 
ATOM   3200 H  HD2  A TYR   A 1 152 ? 15.128 -10.117 13.326  0.64 18.30 ?  152 TYR   A HD2  1 
ATOM   3201 H  HD2  B TYR   A 1 152 ? 15.193 -9.786  13.626  0.36 16.85 ?  152 TYR   A HD2  1 
ATOM   3202 H  HE1  A TYR   A 1 152 ? 19.063 -12.284 14.413  0.64 20.51 ?  152 TYR   A HE1  1 
ATOM   3203 H  HE1  B TYR   A 1 152 ? 18.828 -12.529 14.416  0.36 19.16 ?  152 TYR   A HE1  1 
ATOM   3204 H  HE2  A TYR   A 1 152 ? 15.099 -11.886 14.816  0.64 19.50 ?  152 TYR   A HE2  1 
ATOM   3205 H  HE2  B TYR   A 1 152 ? 15.028 -11.500 15.166  0.36 18.23 ?  152 TYR   A HE2  1 
ATOM   3206 H  HH   A TYR   A 1 152 ? 16.282 -13.459 15.912  0.64 22.52 ?  152 TYR   A HH   1 
ATOM   3207 H  HH   B TYR   A 1 152 ? 16.076 -13.174 16.240  0.36 21.78 ?  152 TYR   A HH   1 
ATOM   3208 N  N    A LEU   A 1 153 ? 15.797 -8.642  8.629   0.64 11.70 ?  153 LEU   A N    1 
ATOM   3209 N  N    B LEU   A 1 153 ? 15.755 -8.427  8.902   0.36 10.86 ?  153 LEU   A N    1 
ATOM   3210 C  CA   A LEU   A 1 153 ? 15.540 -7.769  7.490   0.64 11.44 ?  153 LEU   A CA   1 
ATOM   3211 C  CA   B LEU   A 1 153 ? 15.513 -7.488  7.819   0.36 10.35 ?  153 LEU   A CA   1 
ATOM   3212 C  C    A LEU   A 1 153 ? 14.546 -6.679  7.871   0.64 11.23 ?  153 LEU   A C    1 
ATOM   3213 C  C    B LEU   A 1 153 ? 14.528 -6.420  8.270   0.36 10.77 ?  153 LEU   A C    1 
ATOM   3214 O  O    A LEU   A 1 153 ? 13.426 -6.972  8.307   0.64 12.08 ?  153 LEU   A O    1 
ATOM   3215 O  O    B LEU   A 1 153 ? 13.455 -6.735  8.799   0.36 10.95 ?  153 LEU   A O    1 
ATOM   3216 C  CB   A LEU   A 1 153 ? 14.979 -8.581  6.322   0.64 11.21 ?  153 LEU   A CB   1 
ATOM   3217 C  CB   B LEU   A 1 153 ? 14.948 -8.216  6.599   0.36 10.12 ?  153 LEU   A CB   1 
ATOM   3218 C  CG   A LEU   A 1 153 ? 15.946 -9.567  5.661   0.64 11.73 ?  153 LEU   A CG   1 
ATOM   3219 C  CG   B LEU   A 1 153 ? 15.839 -9.279  5.958   0.36 10.43 ?  153 LEU   A CG   1 
ATOM   3220 C  CD1  A LEU   A 1 153 ? 15.190 -10.486 4.711   0.64 11.83 ?  153 LEU   A CD1  1 
ATOM   3221 C  CD1  B LEU   A 1 153 ? 15.020 -10.103 4.973   0.36 10.55 ?  153 LEU   A CD1  1 
ATOM   3222 C  CD2  A LEU   A 1 153 ? 17.048 -8.826  4.922   0.64 12.16 ?  153 LEU   A CD2  1 
ATOM   3223 C  CD2  B LEU   A 1 153 ? 17.034 -8.639  5.269   0.36 11.07 ?  153 LEU   A CD2  1 
ATOM   3224 H  H    A LEU   A 1 153 ? 15.254 -9.318  8.679   0.64 14.15 ?  153 LEU   A H    1 
ATOM   3225 H  H    B LEU   A 1 153 ? 15.135 -9.019  8.982   0.36 13.15 ?  153 LEU   A H    1 
ATOM   3226 H  HA   A LEU   A 1 153 ? 16.367 -7.362  7.213   0.64 13.84 ?  153 LEU   A HA   1 
ATOM   3227 H  HA   B LEU   A 1 153 ? 16.341 -7.055  7.571   0.36 12.54 ?  153 LEU   A HA   1 
ATOM   3228 H  HB2  A LEU   A 1 153 ? 14.217 -9.097  6.643   0.64 13.57 ?  153 LEU   A HB2  1 
ATOM   3229 H  HB2  B LEU   A 1 153 ? 14.126 -8.653  6.863   0.36 12.25 ?  153 LEU   A HB2  1 
ATOM   3230 H  HB3  A LEU   A 1 153 ? 14.684 -7.967  5.636   0.64 13.57 ?  153 LEU   A HB3  1 
ATOM   3231 H  HB3  B LEU   A 1 153 ? 14.758 -7.556  5.915   0.36 12.25 ?  153 LEU   A HB3  1 
ATOM   3232 H  HG   A LEU   A 1 153 ? 16.359 -10.121 6.348   0.64 14.19 ?  153 LEU   A HG   1 
ATOM   3233 H  HG   B LEU   A 1 153 ? 16.172 -9.876  6.648   0.36 12.63 ?  153 LEU   A HG   1 
ATOM   3234 H  HD11 A LEU   A 1 153 ? 15.733 -11.269 4.528   0.64 14.31 ?  153 LEU   A HD11 1 
ATOM   3235 H  HD11 B LEU   A 1 153 ? 15.594 -10.769 4.564   0.36 12.77 ?  153 LEU   A HD11 1 
ATOM   3236 H  HD12 A LEU   A 1 153 ? 14.357 -10.754 5.127   0.64 14.31 ?  153 LEU   A HD12 1 
ATOM   3237 H  HD12 B LEU   A 1 153 ? 14.295 -10.536 5.449   0.36 12.77 ?  153 LEU   A HD12 1 
ATOM   3238 H  HD13 A LEU   A 1 153 ? 15.011 -10.005 3.889   0.64 14.31 ?  153 LEU   A HD13 1 
ATOM   3239 H  HD13 B LEU   A 1 153 ? 14.662 -9.512  4.291   0.36 12.77 ?  153 LEU   A HD13 1 
ATOM   3240 H  HD21 A LEU   A 1 153 ? 17.651 -9.473  4.530   0.64 14.71 ?  153 LEU   A HD21 1 
ATOM   3241 H  HD21 B LEU   A 1 153 ? 17.567 -9.335  4.852   0.36 13.39 ?  153 LEU   A HD21 1 
ATOM   3242 H  HD22 A LEU   A 1 153 ? 16.642 -8.284  4.231   0.64 14.71 ?  153 LEU   A HD22 1 
ATOM   3243 H  HD22 B LEU   A 1 153 ? 16.714 -8.020  4.596   0.36 13.39 ?  153 LEU   A HD22 1 
ATOM   3244 H  HD23 A LEU   A 1 153 ? 17.523 -8.268  5.552   0.64 14.71 ?  153 LEU   A HD23 1 
ATOM   3245 H  HD23 B LEU   A 1 153 ? 17.564 -8.167  5.929   0.36 13.39 ?  153 LEU   A HD23 1 
ATOM   3246 N  N    A ALA   A 1 154 ? 14.942 -5.426  7.670   0.64 11.47 ?  154 ALA   A N    1 
ATOM   3247 N  N    B ALA   A 1 154 ? 14.897 -5.160  8.054   0.36 10.74 ?  154 ALA   A N    1 
ATOM   3248 C  CA   A ALA   A 1 154 ? 14.086 -4.274  7.916   0.64 11.85 ?  154 ALA   A CA   1 
ATOM   3249 C  CA   B ALA   A 1 154 ? 14.019 -4.018  8.268   0.36 11.35 ?  154 ALA   A CA   1 
ATOM   3250 C  C    A ALA   A 1 154 ? 13.576 -3.759  6.577   0.64 11.47 ?  154 ALA   A C    1 
ATOM   3251 C  C    B ALA   A 1 154 ? 13.611 -3.489  6.900   0.36 11.47 ?  154 ALA   A C    1 
ATOM   3252 O  O    A ALA   A 1 154 ? 14.370 -3.391  5.707   0.64 12.18 ?  154 ALA   A O    1 
ATOM   3253 O  O    B ALA   A 1 154 ? 14.470 -3.083  6.112   0.36 11.74 ?  154 ALA   A O    1 
ATOM   3254 C  CB   A ALA   A 1 154 ? 14.862 -3.179  8.642   0.64 12.33 ?  154 ALA   A CB   1 
ATOM   3255 C  CB   B ALA   A 1 154 ? 14.737 -2.929  9.066   0.36 11.65 ?  154 ALA   A CB   1 
ATOM   3256 H  H    A ALA   A 1 154 ? 15.720 -5.222  7.374   0.64 13.88 ?  154 ALA   A H    1 
ATOM   3257 H  H    B ALA   A 1 154 ? 15.680 -4.932  7.769   0.36 13.00 ?  154 ALA   A H    1 
ATOM   3258 H  HA   A ALA   A 1 154 ? 13.324 -4.544  8.462   0.64 14.34 ?  154 ALA   A HA   1 
ATOM   3259 H  HA   B ALA   A 1 154 ? 13.225 -4.291  8.750   0.36 13.74 ?  154 ALA   A HA   1 
ATOM   3260 H  HB1  A ALA   A 1 154 ? 14.270 -2.429  8.793   0.64 14.91 ?  154 ALA   A HB1  1 
ATOM   3261 H  HB1  B ALA   A 1 154 ? 14.132 -2.182  9.197   0.36 14.09 ?  154 ALA   A HB1  1 
ATOM   3262 H  HB2  A ALA   A 1 154 ? 15.180 -3.530  9.489   0.64 14.91 ?  154 ALA   A HB2  1 
ATOM   3263 H  HB2  B ALA   A 1 154 ? 15.005 -3.294  9.923   0.36 14.09 ?  154 ALA   A HB2  1 
ATOM   3264 H  HB3  A ALA   A 1 154 ? 15.610 -2.912  8.089   0.64 14.91 ?  154 ALA   A HB3  1 
ATOM   3265 H  HB3  B ALA   A 1 154 ? 15.519 -2.639  8.570   0.36 14.09 ?  154 ALA   A HB3  1 
ATOM   3266 N  N    A VAL   A 1 155 ? 12.256 -3.759  6.410   0.34 10.08 ?  155 VAL   A N    1 
ATOM   3267 N  N    B VAL   A 1 155 ? 12.312 -3.520  6.609   0.36 11.85 ?  155 VAL   A N    1 
ATOM   3268 C  CA   A VAL   A 1 155 ? 11.591 -3.257  5.213   0.34 12.03 ?  155 VAL   A CA   1 
ATOM   3269 C  CA   B VAL   A 1 155 ? 11.771 -3.032  5.344   0.36 14.45 ?  155 VAL   A CA   1 
ATOM   3270 C  CA   T VAL   A 1 155 ? 11.614 -3.294  5.227   0.30 13.38 ?  155 VAL   A CA   1 
ATOM   3271 C  C    A VAL   A 1 155 ? 10.912 -1.943  5.583   0.34 13.25 ?  155 VAL   A C    1 
ATOM   3272 C  C    B VAL   A 1 155 ? 10.955 -1.775  5.628   0.36 16.63 ?  155 VAL   A C    1 
ATOM   3273 C  C    T VAL   A 1 155 ? 10.997 -1.924  5.537   0.30 13.26 ?  155 VAL   A C    1 
ATOM   3274 O  O    A VAL   A 1 155 ? 9.990  -1.931  6.408   0.34 13.86 ?  155 VAL   A O    1 
ATOM   3275 O  O    B VAL   A 1 155 ? 9.923  -1.838  6.307   0.36 17.13 ?  155 VAL   A O    1 
ATOM   3276 O  O    T VAL   A 1 155 ? 10.152 -1.800  6.422   0.30 13.50 ?  155 VAL   A O    1 
ATOM   3277 C  CB   A VAL   A 1 155 ? 10.574 -4.278  4.677   0.34 12.47 ?  155 VAL   A CB   1 
ATOM   3278 C  CB   B VAL   A 1 155 ? 10.923 -4.101  4.638   0.36 14.57 ?  155 VAL   A CB   1 
ATOM   3279 C  CB   T VAL   A 1 155 ? 10.572 -4.326  4.738   0.30 13.34 ?  155 VAL   A CB   1 
ATOM   3280 C  CG1  A VAL   A 1 155 ? 9.891  -3.748  3.423   0.34 12.81 ?  155 VAL   A CG1  1 
ATOM   3281 C  CG1  B VAL   A 1 155 ? 10.342 -3.543  3.350   0.36 14.72 ?  155 VAL   A CG1  1 
ATOM   3282 C  CG1  T VAL   A 1 155 ? 9.840  -3.805  3.511   0.30 13.36 ?  155 VAL   A CG1  1 
ATOM   3283 C  CG2  A VAL   A 1 155 ? 11.253 -5.617  4.401   0.34 12.80 ?  155 VAL   A CG2  1 
ATOM   3284 C  CG2  B VAL   A 1 155 ? 11.761 -5.343  4.354   0.36 14.51 ?  155 VAL   A CG2  1 
ATOM   3285 C  CG2  T VAL   A 1 155 ? 11.243 -5.665  4.434   0.30 13.63 ?  155 VAL   A CG2  1 
ATOM   3286 H  H    A VAL   A 1 155 ? 11.706 -4.076  6.995   0.34 12.22 ?  155 VAL   A H    1 
ATOM   3287 H  H    B VAL   A 1 155 ? 11.710 -3.825  7.144   0.36 14.33 ?  155 VAL   A H    1 
ATOM   3288 H  HA   A VAL   A 1 155 ? 12.248 -3.086  4.524   0.34 14.55 ?  155 VAL   A HA   1 
ATOM   3289 H  HA   B VAL   A 1 155 ? 12.502 -2.792  4.755   0.36 17.45 ?  155 VAL   A HA   1 
ATOM   3290 H  HB   A VAL   A 1 155 ? 9.888  -4.423  5.350   0.34 15.08 ?  155 VAL   A HB   1 
ATOM   3291 H  HB   B VAL   A 1 155 ? 10.188 -4.357  5.216   0.36 17.60 ?  155 VAL   A HB   1 
ATOM   3292 H  HB   T VAL   A 1 155 ? 9.920  -4.472  5.440   0.30 16.12 ?  155 VAL   A HB   1 
ATOM   3293 H  HG11 A VAL   A 1 155 ? 9.360  -4.457  3.030   0.34 15.49 ?  155 VAL   A HG11 1 
ATOM   3294 H  HG11 B VAL   A 1 155 ? 9.994  -4.275  2.819   0.36 17.78 ?  155 VAL   A HG11 1 
ATOM   3295 H  HG11 T VAL   A 1 155 ? 9.301  -4.518  3.137   0.30 16.15 ?  155 VAL   A HG11 1 
ATOM   3296 H  HG12 A VAL   A 1 155 ? 9.319  -3.001  3.662   0.34 15.49 ?  155 VAL   A HG12 1 
ATOM   3297 H  HG12 B VAL   A 1 155 ? 9.627  -2.923  3.565   0.36 17.78 ?  155 VAL   A HG12 1 
ATOM   3298 H  HG12 T VAL   A 1 155 ? 9.272  -3.063  3.772   0.30 16.15 ?  155 VAL   A HG12 1 
ATOM   3299 H  HG13 A VAL   A 1 155 ? 10.570 -3.457  2.794   0.34 15.49 ?  155 VAL   A HG13 1 
ATOM   3300 H  HG13 B VAL   A 1 155 ? 11.043 -3.084  2.860   0.36 17.78 ?  155 VAL   A HG13 1 
ATOM   3301 H  HG13 T VAL   A 1 155 ? 10.494 -3.508  2.856   0.30 16.15 ?  155 VAL   A HG13 1 
ATOM   3302 H  HG21 A VAL   A 1 155 ? 10.612 -6.215  3.986   0.34 15.48 ?  155 VAL   A HG21 1 
ATOM   3303 H  HG21 B VAL   A 1 155 ? 11.214 -5.989  3.878   0.36 17.53 ?  155 VAL   A HG21 1 
ATOM   3304 H  HG21 T VAL   A 1 155 ? 10.569 -6.295  4.131   0.30 16.47 ?  155 VAL   A HG21 1 
ATOM   3305 H  HG22 A VAL   A 1 155 ? 12.003 -5.470  3.803   0.34 15.48 ?  155 VAL   A HG22 1 
ATOM   3306 H  HG22 B VAL   A 1 155 ? 12.524 -5.093  3.812   0.36 17.53 ?  155 VAL   A HG22 1 
ATOM   3307 H  HG22 T VAL   A 1 155 ? 11.907 -5.535  3.737   0.30 16.47 ?  155 VAL   A HG22 1 
ATOM   3308 H  HG23 A VAL   A 1 155 ? 11.565 -5.993  5.238   0.34 15.48 ?  155 VAL   A HG23 1 
ATOM   3309 H  HG23 B VAL   A 1 155 ? 12.060 -5.722  5.195   0.36 17.53 ?  155 VAL   A HG23 1 
ATOM   3310 H  HG23 T VAL   A 1 155 ? 11.669 -5.997  5.239   0.30 16.47 ?  155 VAL   A HG23 1 
ATOM   3311 N  N    A PHE   A 1 156 ? 11.358 -0.836  4.976   0.34 14.07 ?  156 PHE   A N    1 
ATOM   3312 N  N    B PHE   A 1 156 ? 11.411 -0.640  5.101   0.36 18.49 ?  156 PHE   A N    1 
ATOM   3313 N  N    T PHE   A 1 156 ? 11.433 -0.900  4.797   0.30 13.44 ?  156 PHE   A N    1 
ATOM   3314 C  CA   A PHE   A 1 156 ? 10.841 0.478   5.363   0.34 14.89 ?  156 PHE   A CA   1 
ATOM   3315 C  CA   B PHE   A 1 156 ? 10.803 0.668   5.372   0.36 20.73 ?  156 PHE   A CA   1 
ATOM   3316 C  CA   T PHE   A 1 156 ? 11.014 0.472   5.085   0.30 13.46 ?  156 PHE   A CA   1 
ATOM   3317 C  C    A PHE   A 1 156 ? 9.377  0.643   4.968   0.34 14.42 ?  156 PHE   A C    1 
ATOM   3318 C  C    B PHE   A 1 156 ? 9.641  0.982   4.426   0.36 21.82 ?  156 PHE   A C    1 
ATOM   3319 C  C    T PHE   A 1 156 ? 9.552  0.701   4.724   0.30 13.93 ?  156 PHE   A C    1 
ATOM   3320 O  O    A PHE   A 1 156 ? 8.559  1.138   5.757   0.34 14.62 ?  156 PHE   A O    1 
ATOM   3321 O  O    B PHE   A 1 156 ? 9.597  2.047   3.810   0.36 22.53 ?  156 PHE   A O    1 
ATOM   3322 O  O    T PHE   A 1 156 ? 8.813  1.355   5.471   0.30 14.05 ?  156 PHE   A O    1 
ATOM   3323 C  CB   A PHE   A 1 156 ? 11.690 1.593   4.743   0.34 15.81 ?  156 PHE   A CB   1 
ATOM   3324 C  CB   B PHE   A 1 156 ? 11.877 1.752   5.302   0.36 21.94 ?  156 PHE   A CB   1 
ATOM   3325 C  CB   T PHE   A 1 156 ? 11.895 1.441   4.295   0.30 12.80 ?  156 PHE   A CB   1 
ATOM   3326 C  CG   A PHE   A 1 156 ? 11.179 2.980   5.050   0.34 16.79 ?  156 PHE   A CG   1 
ATOM   3327 C  CG   B PHE   A 1 156 ? 11.451 3.093   5.859   0.36 23.02 ?  156 PHE   A CG   1 
ATOM   3328 C  CG   T PHE   A 1 156 ? 11.554 2.896   4.504   0.30 12.83 ?  156 PHE   A CG   1 
ATOM   3329 C  CD1  A PHE   A 1 156 ? 11.128 3.432   6.358   0.34 17.29 ?  156 PHE   A CD1  1 
ATOM   3330 C  CD1  B PHE   A 1 156 ? 10.282 3.238   6.592   0.36 23.48 ?  156 PHE   A CD1  1 
ATOM   3331 C  CD1  T PHE   A 1 156 ? 11.953 3.548   5.662   0.30 13.52 ?  156 PHE   A CD1  1 
ATOM   3332 C  CD2  A PHE   A 1 156 ? 10.752 3.826   4.037   0.34 17.26 ?  156 PHE   A CD2  1 
ATOM   3333 C  CD2  B PHE   A 1 156 ? 12.237 4.214   5.642   0.36 23.22 ?  156 PHE   A CD2  1 
ATOM   3334 C  CD2  T PHE   A 1 156 ? 10.859 3.611   3.541   0.30 13.32 ?  156 PHE   A CD2  1 
ATOM   3335 C  CE1  A PHE   A 1 156 ? 10.660 4.696   6.653   0.34 17.59 ?  156 PHE   A CE1  1 
ATOM   3336 C  CE1  B PHE   A 1 156 ? 9.908  4.475   7.096   0.36 23.67 ?  156 PHE   A CE1  1 
ATOM   3337 C  CE1  T PHE   A 1 156 ? 11.653 4.880   5.862   0.30 13.99 ?  156 PHE   A CE1  1 
ATOM   3338 C  CE2  A PHE   A 1 156 ? 10.280 5.096   4.326   0.34 17.75 ?  156 PHE   A CE2  1 
ATOM   3339 C  CE2  B PHE   A 1 156 ? 11.869 5.450   6.141   0.36 23.48 ?  156 PHE   A CE2  1 
ATOM   3340 C  CE2  T PHE   A 1 156 ? 10.558 4.947   3.734   0.30 13.90 ?  156 PHE   A CE2  1 
ATOM   3341 C  CZ   A PHE   A 1 156 ? 10.239 5.532   5.635   0.34 17.88 ?  156 PHE   A CZ   1 
ATOM   3342 C  CZ   B PHE   A 1 156 ? 10.704 5.582   6.869   0.36 23.65 ?  156 PHE   A CZ   1 
ATOM   3343 C  CZ   T PHE   A 1 156 ? 10.956 5.581   4.898   0.30 14.17 ?  156 PHE   A CZ   1 
ATOM   3344 H  H    A PHE   A 1 156 ? 11.952 -0.828  4.349   0.34 17.00 ?  156 PHE   A H    1 
ATOM   3345 H  H    B PHE   A 1 156 ? 12.097 -0.600  4.584   0.36 22.30 ?  156 PHE   A H    1 
ATOM   3346 H  H    T PHE   A 1 156 ? 11.971 -0.984  4.134   0.30 16.24 ?  156 PHE   A H    1 
ATOM   3347 H  HA   A PHE   A 1 156 ? 10.906 0.563   6.325   0.34 17.98 ?  156 PHE   A HA   1 
ATOM   3348 H  HA   B PHE   A 1 156 ? 10.455 0.646   6.276   0.36 24.99 ?  156 PHE   A HA   1 
ATOM   3349 H  HA   T PHE   A 1 156 ? 11.133 0.643   6.034   0.30 16.27 ?  156 PHE   A HA   1 
ATOM   3350 H  HB2  A PHE   A 1 156 ? 12.600 1.526   5.086   0.34 19.09 ?  156 PHE   A HB2  1 
ATOM   3351 H  HB2  B PHE   A 1 156 ? 12.650 1.461   5.810   0.36 26.45 ?  156 PHE   A HB2  1 
ATOM   3352 H  HB2  T PHE   A 1 156 ? 12.817 1.302   4.564   0.30 15.48 ?  156 PHE   A HB2  1 
ATOM   3353 H  HB3  A PHE   A 1 156 ? 11.699 1.483   3.779   0.34 19.09 ?  156 PHE   A HB3  1 
ATOM   3354 H  HB3  B PHE   A 1 156 ? 12.128 1.887   4.374   0.36 26.45 ?  156 PHE   A HB3  1 
ATOM   3355 H  HB3  T PHE   A 1 156 ? 11.795 1.238   3.352   0.30 15.48 ?  156 PHE   A HB3  1 
ATOM   3356 H  HD1  A PHE   A 1 156 ? 11.413 2.874   7.049   0.34 20.87 ?  156 PHE   A HD1  1 
ATOM   3357 H  HD1  B PHE   A 1 156 ? 9.741  2.500   6.751   0.36 28.29 ?  156 PHE   A HD1  1 
ATOM   3358 H  HD1  T PHE   A 1 156 ? 12.417 3.073   6.320   0.30 16.34 ?  156 PHE   A HD1  1 
ATOM   3359 H  HD2  A PHE   A 1 156 ? 10.783 3.534   3.154   0.34 20.83 ?  156 PHE   A HD2  1 
ATOM   3360 H  HD2  B PHE   A 1 156 ? 13.024 4.135   5.153   0.36 27.98 ?  156 PHE   A HD2  1 
ATOM   3361 H  HD2  T PHE   A 1 156 ? 10.589 3.179   2.763   0.30 16.10 ?  156 PHE   A HD2  1 
ATOM   3362 H  HE1  A PHE   A 1 156 ? 10.633 4.987   7.537   0.34 21.23 ?  156 PHE   A HE1  1 
ATOM   3363 H  HE1  B PHE   A 1 156 ? 9.121  4.560   7.587   0.36 28.52 ?  156 PHE   A HE1  1 
ATOM   3364 H  HE1  T PHE   A 1 156 ? 11.917 5.300   6.647   0.30 16.90 ?  156 PHE   A HE1  1 
ATOM   3365 H  HE2  A PHE   A 1 156 ? 10.001 5.654   3.639   0.34 21.42 ?  156 PHE   A HE2  1 
ATOM   3366 H  HE2  B PHE   A 1 156 ? 12.407 6.192   5.986   0.36 28.29 ?  156 PHE   A HE2  1 
ATOM   3367 H  HE2  T PHE   A 1 156 ? 10.087 5.412   3.088   0.30 16.80 ?  156 PHE   A HE2  1 
ATOM   3368 H  HZ   A PHE   A 1 156 ? 9.924  6.384   5.834   0.34 21.58 ?  156 PHE   A HZ   1 
ATOM   3369 H  HZ   B PHE   A 1 156 ? 10.454 6.413   7.206   0.36 28.50 ?  156 PHE   A HZ   1 
ATOM   3370 H  HZ   T PHE   A 1 156 ? 10.751 6.475   5.034   0.30 17.11 ?  156 PHE   A HZ   1 
ATOM   3371 N  N    A ASP   A 1 157 ? 9.037  0.261   3.742   0.34 14.56 ?  157 ASP   A N    1 
ATOM   3372 N  N    B ASP   A 1 157 ? 8.682  0.062   4.305   0.36 21.84 ?  157 ASP   A N    1 
ATOM   3373 N  N    T ASP   A 1 157 ? 9.132  0.200   3.569   0.30 14.17 ?  157 ASP   A N    1 
ATOM   3374 C  CA   A ASP   A 1 157 ? 7.715  0.527   3.188   0.34 15.98 ?  157 ASP   A CA   1 
ATOM   3375 C  CA   B ASP   A 1 157 ? 7.452  0.331   3.563   0.36 22.15 ?  157 ASP   A CA   1 
ATOM   3376 C  CA   T ASP   A 1 157 ? 7.825  0.499   3.004   0.30 15.12 ?  157 ASP   A CA   1 
ATOM   3377 C  C    A ASP   A 1 157 ? 6.723  -0.507  3.713   0.34 16.57 ?  157 ASP   A C    1 
ATOM   3378 C  C    B ASP   A 1 157 ? 6.402  -0.732  3.864   0.36 21.93 ?  157 ASP   A C    1 
ATOM   3379 C  C    T ASP   A 1 157 ? 6.795  -0.470  3.573   0.30 15.75 ?  157 ASP   A C    1 
ATOM   3380 O  O    A ASP   A 1 157 ? 6.875  -1.706  3.452   0.34 16.33 ?  157 ASP   A O    1 
ATOM   3381 O  O    B ASP   A 1 157 ? 6.645  -1.929  3.677   0.36 21.80 ?  157 ASP   A O    1 
ATOM   3382 O  O    T ASP   A 1 157 ? 6.898  -1.684  3.358   0.30 15.48 ?  157 ASP   A O    1 
ATOM   3383 C  CB   A ASP   A 1 157 ? 7.799  0.467   1.665   0.34 17.16 ?  157 ASP   A CB   1 
ATOM   3384 C  CB   B ASP   A 1 157 ? 7.716  0.414   2.057   0.36 22.84 ?  157 ASP   A CB   1 
ATOM   3385 C  CB   T ASP   A 1 157 ? 7.920  0.339   1.489   0.30 15.33 ?  157 ASP   A CB   1 
ATOM   3386 C  CG   A ASP   A 1 157 ? 6.534  0.956   0.991   0.34 18.51 ?  157 ASP   A CG   1 
ATOM   3387 C  CG   B ASP   A 1 157 ? 6.497  0.849   1.273   0.36 23.44 ?  157 ASP   A CG   1 
ATOM   3388 C  CG   T ASP   A 1 157 ? 6.780  0.987   0.762   0.30 15.08 ?  157 ASP   A CG   1 
ATOM   3389 O  OD1  A ASP   A 1 157 ? 6.206  2.156   1.110   0.34 19.91 ?  157 ASP   A OD1  1 
ATOM   3390 O  OD1  B ASP   A 1 157 ? 5.552  0.045   1.142   0.36 23.27 ?  157 ASP   A OD1  1 
ATOM   3391 O  OD1  T ASP   A 1 157 ? 5.674  0.414   0.795   0.30 15.14 ?  157 ASP   A OD1  1 
ATOM   3392 O  OD2  A ASP   A 1 157 ? 5.856  0.129   0.345   0.34 18.35 -1 157 ASP   A OD2  1 
ATOM   3393 O  OD2  B ASP   A 1 157 ? 6.480  2.002   0.794   0.36 23.95 -1 157 ASP   A OD2  1 
ATOM   3394 O  OD2  T ASP   A 1 157 ? 6.982  2.065   0.166   0.30 15.04 -1 157 ASP   A OD2  1 
ATOM   3395 H  H    A ASP   A 1 157 ? 9.569  -0.158  3.203   0.34 17.59 ?  157 ASP   A H    1 
ATOM   3396 H  H    B ASP   A 1 157 ? 8.720  -0.727  4.647   0.36 26.33 ?  157 ASP   A H    1 
ATOM   3397 H  H    T ASP   A 1 157 ? 9.608  -0.322  3.075   0.30 17.12 ?  157 ASP   A H    1 
ATOM   3398 H  HA   A ASP   A 1 157 ? 7.427  1.417   3.452   0.34 19.29 ?  157 ASP   A HA   1 
ATOM   3399 H  HA   B ASP   A 1 157 ? 7.095  1.187   3.848   0.36 26.70 ?  157 ASP   A HA   1 
ATOM   3400 H  HA   T ASP   A 1 157 ? 7.570  1.414   3.218   0.30 18.26 ?  157 ASP   A HA   1 
ATOM   3401 H  HB2  A ASP   A 1 157 ? 8.571  0.986   1.370   0.34 20.71 ?  157 ASP   A HB2  1 
ATOM   3402 H  HB2  B ASP   A 1 157 ? 8.418  1.056   1.889   0.36 27.53 ?  157 ASP   A HB2  1 
ATOM   3403 H  HB2  T ASP   A 1 157 ? 8.752  0.724   1.181   0.30 18.51 ?  157 ASP   A HB2  1 
ATOM   3404 H  HB3  A ASP   A 1 157 ? 7.915  -0.458  1.395   0.34 20.71 ?  157 ASP   A HB3  1 
ATOM   3405 H  HB3  B ASP   A 1 157 ? 7.970  -0.460  1.729   0.36 27.53 ?  157 ASP   A HB3  1 
ATOM   3406 H  HB3  T ASP   A 1 157 ? 7.901  -0.609  1.280   0.30 18.51 ?  157 ASP   A HB3  1 
ATOM   3407 N  N    A LYS   A 1 158 ? 5.708  -0.047  4.453   0.34 17.95 ?  158 LYS   A N    1 
ATOM   3408 N  N    B LYS   A 1 158 ? 5.226  -0.295  4.318   0.36 21.96 ?  158 LYS   A N    1 
ATOM   3409 N  N    T LYS   A 1 158 ? 5.801  0.061   4.293   0.30 17.07 ?  158 LYS   A N    1 
ATOM   3410 C  CA   A LYS   A 1 158 ? 4.739  -0.980  5.025   0.34 18.90 ?  158 LYS   A CA   1 
ATOM   3411 C  CA   B LYS   A 1 158 ? 4.207  -1.226  4.795   0.36 22.00 ?  158 LYS   A CA   1 
ATOM   3412 C  CA   T LYS   A 1 158 ? 4.811  -0.814  4.918   0.30 18.50 ?  158 LYS   A CA   1 
ATOM   3413 C  C    A LYS   A 1 158 ? 3.989  -1.728  3.933   0.34 18.31 ?  158 LYS   A C    1 
ATOM   3414 C  C    B LYS   A 1 158 ? 3.644  -2.069  3.656   0.36 20.98 ?  158 LYS   A C    1 
ATOM   3415 C  C    T LYS   A 1 158 ? 4.041  -1.609  3.873   0.30 18.20 ?  158 LYS   A C    1 
ATOM   3416 O  O    A LYS   A 1 158 ? 3.761  -2.938  4.043   0.34 18.58 ?  158 LYS   A O    1 
ATOM   3417 O  O    B LYS   A 1 158 ? 3.609  -3.303  3.742   0.36 20.63 ?  158 LYS   A O    1 
ATOM   3418 O  O    T LYS   A 1 158 ? 3.788  -2.805  4.055   0.30 18.37 ?  158 LYS   A O    1 
ATOM   3419 C  CB   A LYS   A 1 158 ? 3.758  -0.246  5.942   0.34 20.48 ?  158 LYS   A CB   1 
ATOM   3420 C  CB   B LYS   A 1 158 ? 3.101  -0.443  5.507   0.36 23.24 ?  158 LYS   A CB   1 
ATOM   3421 C  CB   T LYS   A 1 158 ? 3.849  -0.012  5.798   0.30 20.50 ?  158 LYS   A CB   1 
ATOM   3422 C  CG   A LYS   A 1 158 ? 2.526  -1.070  6.357   0.34 22.08 ?  158 LYS   A CG   1 
ATOM   3423 C  CG   B LYS   A 1 158 ? 1.929  -1.279  6.010   0.36 24.36 ?  158 LYS   A CG   1 
ATOM   3424 C  CG   T LYS   A 1 158 ? 2.629  -0.807  6.276   0.30 22.28 ?  158 LYS   A CG   1 
ATOM   3425 C  CD   A LYS   A 1 158 ? 2.881  -2.356  7.112   0.34 23.42 ?  158 LYS   A CD   1 
ATOM   3426 C  CD   B LYS   A 1 158 ? 2.374  -2.374  6.971   0.36 25.12 ?  158 LYS   A CD   1 
ATOM   3427 C  CD   T LYS   A 1 158 ? 3.021  -2.026  7.109   0.30 23.83 ?  158 LYS   A CD   1 
ATOM   3428 C  CE   A LYS   A 1 158 ? 1.632  -3.033  7.676   0.34 24.22 ?  158 LYS   A CE   1 
ATOM   3429 C  CE   B LYS   A 1 158 ? 1.182  -3.155  7.514   0.36 25.57 ?  158 LYS   A CE   1 
ATOM   3430 C  CE   T LYS   A 1 158 ? 1.792  -2.840  7.512   0.30 24.86 ?  158 LYS   A CE   1 
ATOM   3431 N  NZ   A LYS   A 1 158 ? 1.919  -4.360  8.299   0.34 24.58 ?  158 LYS   A NZ   1 
ATOM   3432 N  NZ   B LYS   A 1 158 ? 1.591  -4.404  8.222   0.36 25.74 ?  158 LYS   A NZ   1 
ATOM   3433 N  NZ   T LYS   A 1 158 ? 2.140  -4.046  8.318   0.30 25.34 ?  158 LYS   A NZ   1 
ATOM   3434 H  H    A LYS   A 1 158 ? 5.570  0.781   4.632   0.34 21.65 ?  158 LYS   A H    1 
ATOM   3435 H  H    B LYS   A 1 158 ? 4.997  0.530   4.358   0.36 26.47 ?  158 LYS   A H    1 
ATOM   3436 H  H    T LYS   A 1 158 ? 5.682  0.903   4.431   0.30 20.60 ?  158 LYS   A H    1 
ATOM   3437 H  HA   A LYS   A 1 158 ? 5.217  -1.632  5.561   0.34 22.80 ?  158 LYS   A HA   1 
ATOM   3438 H  HA   B LYS   A 1 158 ? 4.610  -1.828  5.440   0.36 26.52 ?  158 LYS   A HA   1 
ATOM   3439 H  HA   T LYS   A 1 158 ? 5.274  -1.446  5.491   0.30 22.32 ?  158 LYS   A HA   1 
ATOM   3440 H  HB2  A LYS   A 1 158 ? 4.224  0.020   6.751   0.34 24.70 ?  158 LYS   A HB2  1 
ATOM   3441 H  HB2  B LYS   A 1 158 ? 3.489  0.006   6.276   0.36 28.00 ?  158 LYS   A HB2  1 
ATOM   3442 H  HB2  T LYS   A 1 158 ? 4.327  0.293   6.587   0.30 24.71 ?  158 LYS   A HB2  1 
ATOM   3443 H  HB3  A LYS   A 1 158 ? 3.440  0.544   5.479   0.34 24.70 ?  158 LYS   A HB3  1 
ATOM   3444 H  HB3  B LYS   A 1 158 ? 2.746  0.218   4.892   0.36 28.00 ?  158 LYS   A HB3  1 
ATOM   3445 H  HB3  T LYS   A 1 158 ? 3.526  0.750   5.295   0.30 24.71 ?  158 LYS   A HB3  1 
ATOM   3446 H  HG2  A LYS   A 1 158 ? 1.977  -0.529  6.941   0.34 26.61 ?  158 LYS   A HG2  1 
ATOM   3447 H  HG2  B LYS   A 1 158 ? 1.307  -0.699  6.479   0.36 29.35 ?  158 LYS   A HG2  1 
ATOM   3448 H  HG2  T LYS   A 1 158 ? 2.081  -0.235  6.832   0.30 26.85 ?  158 LYS   A HG2  1 
ATOM   3449 H  HG3  A LYS   A 1 158 ? 2.018  -1.314  5.566   0.34 26.61 ?  158 LYS   A HG3  1 
ATOM   3450 H  HG3  B LYS   A 1 158 ? 1.487  -1.697  5.255   0.36 29.35 ?  158 LYS   A HG3  1 
ATOM   3451 H  HG3  T LYS   A 1 158 ? 2.113  -1.114  5.512   0.30 26.85 ?  158 LYS   A HG3  1 
ATOM   3452 H  HD2  A LYS   A 1 158 ? 3.319  -2.977  6.509   0.34 28.22 ?  158 LYS   A HD2  1 
ATOM   3453 H  HD2  B LYS   A 1 158 ? 2.956  -2.993  6.505   0.36 30.26 ?  158 LYS   A HD2  1 
ATOM   3454 H  HD2  T LYS   A 1 158 ? 3.606  -2.601  6.593   0.30 28.71 ?  158 LYS   A HD2  1 
ATOM   3455 H  HD3  A LYS   A 1 158 ? 3.461  -2.142  7.856   0.34 28.22 ?  158 LYS   A HD3  1 
ATOM   3456 H  HD3  B LYS   A 1 158 ? 2.843  -1.970  7.720   0.36 30.26 ?  158 LYS   A HD3  1 
ATOM   3457 H  HD3  T LYS   A 1 158 ? 3.467  -1.732  7.919   0.30 28.71 ?  158 LYS   A HD3  1 
ATOM   3458 H  HE2  A LYS   A 1 158 ? 1.241  -2.460  8.356   0.34 29.18 ?  158 LYS   A HE2  1 
ATOM   3459 H  HE2  B LYS   A 1 158 ? 0.701  -2.596  8.144   0.36 30.80 ?  158 LYS   A HE2  1 
ATOM   3460 H  HE2  T LYS   A 1 158 ? 1.200  -2.285  8.043   0.30 29.95 ?  158 LYS   A HE2  1 
ATOM   3461 H  HE3  A LYS   A 1 158 ? 0.997  -3.171  6.958   0.34 29.18 ?  158 LYS   A HE3  1 
ATOM   3462 H  HE3  B LYS   A 1 158 ? 0.602  -3.400  6.778   0.36 30.80 ?  158 LYS   A HE3  1 
ATOM   3463 H  HE3  T LYS   A 1 158 ? 1.334  -3.140  6.711   0.30 29.95 ?  158 LYS   A HE3  1 
ATOM   3464 H  HZ1  A LYS   A 1 158 ? 1.167  -4.718  8.614   0.34 29.61 ?  158 LYS   A HZ1  1 
ATOM   3465 H  HZ1  B LYS   A 1 158 ? 0.871  -4.832  8.523   0.36 31.01 ?  158 LYS   A HZ1  1 
ATOM   3466 H  HZ1  T LYS   A 1 158 ? 1.401  -4.494  8.532   0.30 30.52 ?  158 LYS   A HZ1  1 
ATOM   3467 H  HZ2  A LYS   A 1 158 ? 2.268  -4.911  7.692   0.34 29.61 ?  158 LYS   A HZ2  1 
ATOM   3468 H  HZ2  B LYS   A 1 158 ? 2.032  -4.940  7.664   0.36 31.01 ?  158 LYS   A HZ2  1 
ATOM   3469 H  HZ2  T LYS   A 1 158 ? 2.675  -4.581  7.849   0.30 30.52 ?  158 LYS   A HZ2  1 
ATOM   3470 H  HZ3  A LYS   A 1 158 ? 2.497  -4.265  8.969   0.34 29.61 ?  158 LYS   A HZ3  1 
ATOM   3471 H  HZ3  B LYS   A 1 158 ? 2.119  -4.206  8.910   0.36 31.01 ?  158 LYS   A HZ3  1 
ATOM   3472 H  HZ3  T LYS   A 1 158 ? 2.557  -3.803  9.065   0.30 30.52 ?  158 LYS   A HZ3  1 
ATOM   3473 N  N    A ASN   A 1 159 ? 3.589  -1.027  2.873   0.34 18.02 ?  159 ASN   A N    1 
ATOM   3474 N  N    B ASN   A 1 159 ? 3.194  -1.424  2.577   0.36 20.83 ?  159 ASN   A N    1 
ATOM   3475 N  N    T ASN   A 1 159 ? 3.652  -0.966  2.779   0.30 18.37 ?  159 ASN   A N    1 
ATOM   3476 C  CA   A ASN   A 1 159 ? 2.888  -1.704  1.789   0.34 17.88 ?  159 ASN   A CA   1 
ATOM   3477 C  CA   B ASN   A 1 159 ? 2.638  -2.173  1.455   0.36 20.86 ?  159 ASN   A CA   1 
ATOM   3478 C  CA   T ASN   A 1 159 ? 2.910  -1.660  1.736   0.30 18.67 ?  159 ASN   A CA   1 
ATOM   3479 C  C    A ASN   A 1 159 ? 3.760  -2.786  1.163   0.34 17.34 ?  159 ASN   A C    1 
ATOM   3480 C  C    B ASN   A 1 159 ? 3.652  -3.177  0.923   0.36 19.20 ?  159 ASN   A C    1 
ATOM   3481 C  C    T ASN   A 1 159 ? 3.735  -2.778  1.103   0.30 18.80 ?  159 ASN   A C    1 
ATOM   3482 O  O    A ASN   A 1 159 ? 3.283  -3.892  0.884   0.34 17.24 ?  159 ASN   A O    1 
ATOM   3483 O  O    B ASN   A 1 159 ? 3.308  -4.330  0.634   0.36 18.76 ?  159 ASN   A O    1 
ATOM   3484 O  O    T ASN   A 1 159 ? 3.196  -3.826  0.755   0.30 18.82 ?  159 ASN   A O    1 
ATOM   3485 C  CB   A ASN   A 1 159 ? 2.404  -0.690  0.752   0.34 18.79 ?  159 ASN   A CB   1 
ATOM   3486 C  CB   B ASN   A 1 159 ? 2.183  -1.208  0.357   0.36 22.81 ?  159 ASN   A CB   1 
ATOM   3487 C  CB   T ASN   A 1 159 ? 2.411  -0.679  0.674   0.30 19.33 ?  159 ASN   A CB   1 
ATOM   3488 C  CG   A ASN   A 1 159 ? 1.159  0.054   1.204   0.34 20.15 ?  159 ASN   A CG   1 
ATOM   3489 C  CG   B ASN   A 1 159 ? 1.079  -0.275  0.824   0.36 24.76 ?  159 ASN   A CG   1 
ATOM   3490 C  CG   T ASN   A 1 159 ? 1.183  0.092   1.127   0.30 20.30 ?  159 ASN   A CG   1 
ATOM   3491 O  OD1  A ASN   A 1 159 ? 0.334  -0.490  1.936   0.34 20.86 ?  159 ASN   A OD1  1 
ATOM   3492 O  OD1  B ASN   A 1 159 ? 1.345  0.792   1.376   0.36 25.38 ?  159 ASN   A OD1  1 
ATOM   3493 O  OD1  T ASN   A 1 159 ? 0.385  -0.405  1.920   0.30 20.88 ?  159 ASN   A OD1  1 
ATOM   3494 N  ND2  A ASN   A 1 159 ? 1.018  1.301   0.769   0.34 20.40 ?  159 ASN   A ND2  1 
ATOM   3495 N  ND2  B ASN   A 1 159 ? -0.168 -0.675  0.605   0.36 25.52 ?  159 ASN   A ND2  1 
ATOM   3496 N  ND2  T ASN   A 1 159 ? 1.025  1.309   0.624   0.30 20.50 ?  159 ASN   A ND2  1 
ATOM   3497 H  H    A ASN   A 1 159 ? 3.709  -0.183  2.762   0.34 21.74 ?  159 ASN   A H    1 
ATOM   3498 H  H    B ASN   A 1 159 ? 3.213  -0.574  2.469   0.36 25.11 ?  159 ASN   A H    1 
ATOM   3499 H  H    T ASN   A 1 159 ? 3.796  -0.134  2.625   0.30 22.16 ?  159 ASN   A H    1 
ATOM   3500 H  HA   A ASN   A 1 159 ? 2.106  -2.141  2.160   0.34 21.57 ?  159 ASN   A HA   1 
ATOM   3501 H  HA   B ASN   A 1 159 ? 1.861  -2.667  1.752   0.36 25.15 ?  159 ASN   A HA   1 
ATOM   3502 H  HA   T ASN   A 1 159 ? 2.135  -2.075  2.139   0.30 22.52 ?  159 ASN   A HA   1 
ATOM   3503 H  HB2  A ASN   A 1 159 ? 3.100  -0.036  0.596   0.34 22.67 ?  159 ASN   A HB2  1 
ATOM   3504 H  HB2  B ASN   A 1 159 ? 2.935  -0.661  0.078   0.36 27.49 ?  159 ASN   A HB2  1 
ATOM   3505 H  HB2  T ASN   A 1 159 ? 3.111  -0.040  0.478   0.30 23.31 ?  159 ASN   A HB2  1 
ATOM   3506 H  HB3  A ASN   A 1 159 ? 2.191  -1.157  -0.071  0.34 22.67 ?  159 ASN   A HB3  1 
ATOM   3507 H  HB3  B ASN   A 1 159 ? 1.843  -1.713  -0.398  0.36 27.49 ?  159 ASN   A HB3  1 
ATOM   3508 H  HB3  T ASN   A 1 159 ? 2.179  -1.176  -0.128  0.30 23.31 ?  159 ASN   A HB3  1 
ATOM   3509 H  HD21 A ASN   A 1 159 ? 0.328  1.760   0.997   0.34 24.59 ?  159 ASN   A HD21 1 
ATOM   3510 H  HD21 B ASN   A 1 159 ? -0.830 -0.180  0.849   0.36 30.74 ?  159 ASN   A HD21 1 
ATOM   3511 H  HD21 T ASN   A 1 159 ? 0.342  1.780   0.850   0.30 24.72 ?  159 ASN   A HD21 1 
ATOM   3512 H  HD22 A ASN   A 1 159 ? 1.617  1.647   0.261   0.34 24.59 ?  159 ASN   A HD22 1 
ATOM   3513 H  HD22 B ASN   A 1 159 ? -0.315 -1.427  0.217   0.36 30.74 ?  159 ASN   A HD22 1 
ATOM   3514 H  HD22 T ASN   A 1 159 ? 1.603  1.623   0.074   0.30 24.72 ?  159 ASN   A HD22 1 
ATOM   3515 N  N    A LEU   A 1 160 ? 5.047  -2.503  0.959   0.34 16.91 ?  160 LEU   A N    1 
ATOM   3516 N  N    B LEU   A 1 160 ? 4.914  -2.764  0.817   0.36 18.14 ?  160 LEU   A N    1 
ATOM   3517 N  N    T LEU   A 1 160 ? 5.039  -2.570  0.963   0.30 18.91 ?  160 LEU   A N    1 
ATOM   3518 C  CA   A LEU   A 1 160 ? 5.925  -3.533  0.413   0.34 16.62 ?  160 LEU   A CA   1 
ATOM   3519 C  CA   B LEU   A 1 160 ? 5.956  -3.685  0.385   0.36 17.34 ?  160 LEU   A CA   1 
ATOM   3520 C  CA   T LEU   A 1 160 ? 5.899  -3.615  0.418   0.30 18.89 ?  160 LEU   A CA   1 
ATOM   3521 C  C    A LEU   A 1 160 ? 6.095  -4.688  1.392   0.34 15.81 ?  160 LEU   A C    1 
ATOM   3522 C  C    B LEU   A 1 160 ? 6.124  -4.820  1.388   0.36 16.02 ?  160 LEU   A C    1 
ATOM   3523 O  O    A LEU   A 1 160 ? 6.095  -5.856  0.986   0.34 15.37 ?  160 LEU   A O    1 
ATOM   3524 O  O    B LEU   A 1 160 ? 6.164  -5.999  1.016   0.36 15.64 ?  160 LEU   A O    1 
ATOM   3525 C  CB   A LEU   A 1 160 ? 7.281  -2.943  0.037   0.34 16.99 ?  160 LEU   A CB   1 
ATOM   3526 C  CB   B LEU   A 1 160 ? 7.270  -2.923  0.210   0.36 17.90 ?  160 LEU   A CB   1 
ATOM   3527 C  CB   T LEU   A 1 160 ? 7.266  -3.056  0.036   0.30 18.72 ?  160 LEU   A CB   1 
ATOM   3528 C  CG   A LEU   A 1 160 ? 8.321  -3.990  -0.367  0.34 17.87 ?  160 LEU   A CG   1 
ATOM   3529 C  CG   B LEU   A 1 160 ? 8.404  -3.810  -0.286  0.36 18.87 ?  160 LEU   A CG   1 
ATOM   3530 C  CG   T LEU   A 1 160 ? 8.293  -4.105  -0.389  0.30 18.97 ?  160 LEU   A CG   1 
ATOM   3531 C  CD1  A LEU   A 1 160 ? 7.843  -4.793  -1.567  0.34 18.53 ?  160 LEU   A CD1  1 
ATOM   3532 C  CD1  B LEU   A 1 160 ? 7.945  -4.523  -1.537  0.36 19.48 ?  160 LEU   A CD1  1 
ATOM   3533 C  CD1  T LEU   A 1 160 ? 7.820  -4.863  -1.616  0.30 19.37 ?  160 LEU   A CD1  1 
ATOM   3534 C  CD2  A LEU   A 1 160 ? 9.650  -3.326  -0.655  0.34 18.05 ?  160 LEU   A CD2  1 
ATOM   3535 C  CD2  B LEU   A 1 160 ? 9.656  -2.999  -0.552  0.36 19.04 ?  160 LEU   A CD2  1 
ATOM   3536 C  CD2  T LEU   A 1 160 ? 9.634  -3.445  -0.647  0.30 18.90 ?  160 LEU   A CD2  1 
ATOM   3537 H  H    A LEU   A 1 160 ? 5.424  -1.748  1.129   0.34 20.41 ?  160 LEU   A H    1 
ATOM   3538 H  H    B LEU   A 1 160 ? 5.188  -1.967  0.993   0.36 21.88 ?  160 LEU   A H    1 
ATOM   3539 H  H    T LEU   A 1 160 ? 5.448  -1.841  1.176   0.30 22.81 ?  160 LEU   A H    1 
ATOM   3540 H  HA   A LEU   A 1 160 ? 5.522  -3.885  -0.391  0.34 20.06 ?  160 LEU   A HA   1 
ATOM   3541 H  HA   B LEU   A 1 160 ? 5.693  -4.055  -0.470  0.36 20.93 ?  160 LEU   A HA   1 
ATOM   3542 H  HB2  A LEU   A 1 160 ? 7.163  -2.331  -0.711  0.34 20.50 ?  160 LEU   A HB2  1 
ATOM   3543 H  HB2  B LEU   A 1 160 ? 7.147  -2.205  -0.436  0.36 21.59 ?  160 LEU   A HB2  1 
ATOM   3544 H  HB2  T LEU   A 1 160 ? 7.156  -2.428  -0.698  0.30 22.58 ?  160 LEU   A HB2  1 
ATOM   3545 H  HB3  A LEU   A 1 160 ? 7.634  -2.464  0.800   0.34 20.50 ?  160 LEU   A HB3  1 
ATOM   3546 H  HB3  B LEU   A 1 160 ? 7.537  -2.548  1.067   0.36 21.59 ?  160 LEU   A HB3  1 
ATOM   3547 H  HB3  T LEU   A 1 160 ? 7.634  -2.599  0.806   0.30 22.58 ?  160 LEU   A HB3  1 
ATOM   3548 H  HG   A LEU   A 1 160 ? 8.461  -4.604  0.369   0.34 21.56 ?  160 LEU   A HG   1 
ATOM   3549 H  HG   B LEU   A 1 160 ? 8.614  -4.475  0.389   0.36 22.76 ?  160 LEU   A HG   1 
ATOM   3550 H  HG   T LEU   A 1 160 ? 8.409  -4.741  0.333   0.30 22.88 ?  160 LEU   A HG   1 
ATOM   3551 H  HD11 A LEU   A 1 160 ? 8.562  -5.371  -1.863  0.34 22.35 ?  160 LEU   A HD11 1 
ATOM   3552 H  HD11 B LEU   A 1 160 ? 8.709  -4.927  -1.954  0.36 23.49 ?  160 LEU   A HD11 1 
ATOM   3553 H  HD11 T LEU   A 1 160 ? 8.523  -5.466  -1.902  0.30 23.36 ?  160 LEU   A HD11 1 
ATOM   3554 H  HD12 A LEU   A 1 160 ? 7.076  -5.326  -1.306  0.34 22.35 ?  160 LEU   A HD12 1 
ATOM   3555 H  HD12 B LEU   A 1 160 ? 7.305  -5.212  -1.296  0.36 23.49 ?  160 LEU   A HD12 1 
ATOM   3556 H  HD12 T LEU   A 1 160 ? 7.024  -5.366  -1.388  0.30 23.36 ?  160 LEU   A HD12 1 
ATOM   3557 H  HD13 A LEU   A 1 160 ? 7.595  -4.180  -2.277  0.34 22.35 ?  160 LEU   A HD13 1 
ATOM   3558 H  HD13 B LEU   A 1 160 ? 7.533  -3.877  -2.135  0.36 23.49 ?  160 LEU   A HD13 1 
ATOM   3559 H  HD13 T LEU   A 1 160 ? 7.622  -4.227  -2.321  0.30 23.36 ?  160 LEU   A HD13 1 
ATOM   3560 H  HD21 A LEU   A 1 160 ? 10.294 -4.007  -0.906  0.34 21.78 ?  160 LEU   A HD21 1 
ATOM   3561 H  HD21 B LEU   A 1 160 ? 10.383 -3.602  -0.774  0.36 22.97 ?  160 LEU   A HD21 1 
ATOM   3562 H  HD21 T LEU   A 1 160 ? 10.274 -4.123  -0.914  0.30 22.80 ?  160 LEU   A HD21 1 
ATOM   3563 H  HD22 A LEU   A 1 160 ? 9.537  -2.694  -1.382  0.34 21.78 ?  160 LEU   A HD22 1 
ATOM   3564 H  HD22 B LEU   A 1 160 ? 9.489  -2.396  -1.294  0.36 22.97 ?  160 LEU   A HD22 1 
ATOM   3565 H  HD22 T LEU   A 1 160 ? 9.533  -2.789  -1.355  0.30 22.80 ?  160 LEU   A HD22 1 
ATOM   3566 H  HD23 A LEU   A 1 160 ? 9.953  -2.863  0.142   0.34 21.78 ?  160 LEU   A HD23 1 
ATOM   3567 H  HD23 B LEU   A 1 160 ? 9.881  -2.491  0.244   0.36 22.97 ?  160 LEU   A HD23 1 
ATOM   3568 H  HD23 T LEU   A 1 160 ? 9.935  -3.008  0.166   0.30 22.80 ?  160 LEU   A HD23 1 
ATOM   3569 N  N    A TYR   A 1 161 ? 6.253  -4.383  2.681   0.64 16.19 ?  161 TYR   A N    1 
ATOM   3570 N  N    B TYR   A 1 161 ? 6.235  -4.475  2.671   0.36 15.70 ?  161 TYR   A N    1 
ATOM   3571 C  CA   A TYR   A 1 161 ? 6.385  -5.441  3.678   0.64 16.08 ?  161 TYR   A CA   1 
ATOM   3572 C  CA   B TYR   A 1 161 ? 6.353  -5.488  3.715   0.36 15.20 ?  161 TYR   A CA   1 
ATOM   3573 C  C    A TYR   A 1 161 ? 5.214  -6.411  3.603   0.64 16.85 ?  161 TYR   A C    1 
ATOM   3574 C  C    B TYR   A 1 161 ? 5.202  -6.486  3.655   0.36 15.61 ?  161 TYR   A C    1 
ATOM   3575 O  O    A TYR   A 1 161 ? 5.404  -7.630  3.508   0.64 16.24 ?  161 TYR   A O    1 
ATOM   3576 O  O    B TYR   A 1 161 ? 5.405  -7.692  3.838   0.36 15.27 ?  161 TYR   A O    1 
ATOM   3577 C  CB   A TYR   A 1 161 ? 6.489  -4.847  5.082   0.64 16.29 ?  161 TYR   A CB   1 
ATOM   3578 C  CB   B TYR   A 1 161 ? 6.412  -4.802  5.083   0.36 15.16 ?  161 TYR   A CB   1 
ATOM   3579 C  CG   A TYR   A 1 161 ? 6.383  -5.903  6.153   0.64 15.65 ?  161 TYR   A CG   1 
ATOM   3580 C  CG   B TYR   A 1 161 ? 6.335  -5.743  6.264   0.36 14.73 ?  161 TYR   A CG   1 
ATOM   3581 C  CD1  A TYR   A 1 161 ? 7.485  -6.667  6.503   0.64 15.21 ?  161 TYR   A CD1  1 
ATOM   3582 C  CD1  B TYR   A 1 161 ? 7.472  -6.379  6.751   0.36 14.33 ?  161 TYR   A CD1  1 
ATOM   3583 C  CD2  A TYR   A 1 161 ? 5.178  -6.152  6.803   0.64 15.50 ?  161 TYR   A CD2  1 
ATOM   3584 C  CD2  B TYR   A 1 161 ? 5.128  -5.981  6.907   0.36 14.69 ?  161 TYR   A CD2  1 
ATOM   3585 C  CE1  A TYR   A 1 161 ? 7.397  -7.640  7.470   0.64 14.66 ?  161 TYR   A CE1  1 
ATOM   3586 C  CE1  B TYR   A 1 161 ? 7.402  -7.240  7.834   0.36 14.27 ?  161 TYR   A CE1  1 
ATOM   3587 C  CE2  A TYR   A 1 161 ? 5.082  -7.128  7.775   0.64 14.99 ?  161 TYR   A CE2  1 
ATOM   3588 C  CE2  B TYR   A 1 161 ? 5.049  -6.838  7.989   0.36 14.71 ?  161 TYR   A CE2  1 
ATOM   3589 C  CZ   A TYR   A 1 161 ? 6.196  -7.869  8.102   0.64 14.31 ?  161 TYR   A CZ   1 
ATOM   3590 C  CZ   B TYR   A 1 161 ? 6.187  -7.465  8.449   0.36 14.81 ?  161 TYR   A CZ   1 
ATOM   3591 O  OH   A TYR   A 1 161 ? 6.126  -8.842  9.069   0.64 14.38 ?  161 TYR   A OH   1 
ATOM   3592 O  OH   B TYR   A 1 161 ? 6.113  -8.319  9.527   0.36 15.75 ?  161 TYR   A OH   1 
ATOM   3593 H  H    A TYR   A 1 161 ? 6.274  -3.586  3.002   0.64 19.54 ?  161 TYR   A H    1 
ATOM   3594 H  H    B TYR   A 1 161 ? 6.245  -3.667  2.956   0.36 18.95 ?  161 TYR   A H    1 
ATOM   3595 H  HA   A TYR   A 1 161 ? 7.193  -5.942  3.507   0.64 19.41 ?  161 TYR   A HA   1 
ATOM   3596 H  HA   B TYR   A 1 161 ? 7.176  -5.978  3.585   0.36 18.36 ?  161 TYR   A HA   1 
ATOM   3597 H  HB2  A TYR   A 1 161 ? 7.350  -4.406  5.179   0.64 19.66 ?  161 TYR   A HB2  1 
ATOM   3598 H  HB2  B TYR   A 1 161 ? 7.250  -4.317  5.146   0.36 18.31 ?  161 TYR   A HB2  1 
ATOM   3599 H  HB3  A TYR   A 1 161 ? 5.772  -4.208  5.218   0.64 19.66 ?  161 TYR   A HB3  1 
ATOM   3600 H  HB3  B TYR   A 1 161 ? 5.671  -4.181  5.152   0.36 18.31 ?  161 TYR   A HB3  1 
ATOM   3601 H  HD1  A TYR   A 1 161 ? 8.298  -6.521  6.078   0.64 18.36 ?  161 TYR   A HD1  1 
ATOM   3602 H  HD1  B TYR   A 1 161 ? 8.293  -6.230  6.339   0.36 17.31 ?  161 TYR   A HD1  1 
ATOM   3603 H  HD2  A TYR   A 1 161 ? 4.423  -5.655  6.586   0.64 18.72 ?  161 TYR   A HD2  1 
ATOM   3604 H  HD2  B TYR   A 1 161 ? 4.356  -5.563  6.600   0.36 17.75 ?  161 TYR   A HD2  1 
ATOM   3605 H  HE1  A TYR   A 1 161 ? 8.145  -8.150  7.692   0.64 17.71 ?  161 TYR   A HE1  1 
ATOM   3606 H  HE1  B TYR   A 1 161 ? 8.170  -7.660  8.151   0.36 17.24 ?  161 TYR   A HE1  1 
ATOM   3607 H  HE2  A TYR   A 1 161 ? 4.267  -7.288  8.204   0.64 18.10 ?  161 TYR   A HE2  1 
ATOM   3608 H  HE2  B TYR   A 1 161 ? 4.229  -6.988  8.408   0.36 17.77 ?  161 TYR   A HE2  1 
ATOM   3609 H  HH   A TYR   A 1 161 ? 5.336  -8.895  9.373   0.64 17.37 ?  161 TYR   A HH   1 
ATOM   3610 H  HH   B TYR   A 1 161 ? 6.869  -8.627  9.708   0.36 19.02 ?  161 TYR   A HH   1 
ATOM   3611 N  N    A ASP   A 1 162 ? 3.985  -5.885  3.654   0.64 17.71 ?  162 ASP   A N    1 
ATOM   3612 N  N    B ASP   A 1 162 ? 3.984  -6.005  3.389   0.36 16.22 ?  162 ASP   A N    1 
ATOM   3613 C  CA   A ASP   A 1 162 ? 2.817  -6.756  3.564   0.64 18.91 ?  162 ASP   A CA   1 
ATOM   3614 C  CA   B ASP   A 1 162 ? 2.831  -6.902  3.338   0.36 17.27 ?  162 ASP   A CA   1 
ATOM   3615 C  C    A ASP   A 1 162 ? 2.863  -7.592  2.294   0.64 18.81 ?  162 ASP   A C    1 
ATOM   3616 C  C    B ASP   A 1 162 ? 2.884  -7.810  2.114   0.36 17.37 ?  162 ASP   A C    1 
ATOM   3617 O  O    A ASP   A 1 162 ? 2.528  -8.783  2.311   0.64 19.32 ?  162 ASP   A O    1 
ATOM   3618 O  O    B ASP   A 1 162 ? 2.535  -8.994  2.198   0.36 17.55 ?  162 ASP   A O    1 
ATOM   3619 C  CB   A ASP   A 1 162 ? 1.523  -5.936  3.614   0.64 20.35 ?  162 ASP   A CB   1 
ATOM   3620 C  CB   B ASP   A 1 162 ? 1.529  -6.095  3.365   0.36 18.59 ?  162 ASP   A CB   1 
ATOM   3621 C  CG   A ASP   A 1 162 ? 1.230  -5.364  4.990   0.64 22.13 ?  162 ASP   A CG   1 
ATOM   3622 C  CG   B ASP   A 1 162 ? 1.233  -5.497  4.724   0.36 19.91 ?  162 ASP   A CG   1 
ATOM   3623 O  OD1  A ASP   A 1 162 ? 1.854  -5.795  5.980   0.64 23.06 ?  162 ASP   A OD1  1 
ATOM   3624 O  OD1  B ASP   A 1 162 ? 1.870  -5.904  5.717   0.36 20.64 ?  162 ASP   A OD1  1 
ATOM   3625 O  OD2  A ASP   A 1 162 ? 0.353  -4.478  5.076   0.64 23.65 -1 162 ASP   A OD2  1 
ATOM   3626 O  OD2  B ASP   A 1 162 ? 0.343  -4.624  4.797   0.36 20.72 -1 162 ASP   A OD2  1 
ATOM   3627 H  H    A ASP   A 1 162 ? 3.805  -5.042  3.729   0.64 21.37 ?  162 ASP   A H    1 
ATOM   3628 H  H    B ASP   A 1 162 ? 3.801  -5.177  3.238   0.36 19.58 ?  162 ASP   A H    1 
ATOM   3629 H  HA   A ASP   A 1 162 ? 2.816  -7.360  4.316   0.64 22.81 ?  162 ASP   A HA   1 
ATOM   3630 H  HA   B ASP   A 1 162 ? 2.840  -7.469  4.120   0.36 20.84 ?  162 ASP   A HA   1 
ATOM   3631 H  HB2  A ASP   A 1 162 ? 1.591  -5.190  3.003   0.64 24.54 ?  162 ASP   A HB2  1 
ATOM   3632 H  HB2  B ASP   A 1 162 ? 1.583  -5.372  2.722   0.36 22.42 ?  162 ASP   A HB2  1 
ATOM   3633 H  HB3  A ASP   A 1 162 ? 0.778  -6.507  3.366   0.64 24.54 ?  162 ASP   A HB3  1 
ATOM   3634 H  HB3  B ASP   A 1 162 ? 0.784  -6.675  3.157   0.36 22.42 ?  162 ASP   A HB3  1 
ATOM   3635 N  N    A LYS   A 1 163 ? 3.285  -6.988  1.180   0.64 19.29 ?  163 LYS   A N    1 
ATOM   3636 N  N    B LYS   A 1 163 ? 3.314  -7.278  0.966   0.36 18.03 ?  163 LYS   A N    1 
ATOM   3637 C  CA   A LYS   A 1 163 ? 3.382  -7.750  -0.060  0.64 20.05 ?  163 LYS   A CA   1 
ATOM   3638 C  CA   B LYS   A 1 163 ? 3.415  -8.105  -0.233  0.36 18.79 ?  163 LYS   A CA   1 
ATOM   3639 C  C    A LYS   A 1 163 ? 4.448  -8.834  0.037   0.64 19.07 ?  163 LYS   A C    1 
ATOM   3640 C  C    B LYS   A 1 163 ? 4.521  -9.146  -0.091  0.36 17.79 ?  163 LYS   A C    1 
ATOM   3641 O  O    A LYS   A 1 163 ? 4.273  -9.930  -0.506  0.64 18.88 ?  163 LYS   A O    1 
ATOM   3642 O  O    B LYS   A 1 163 ? 4.366  -10.291 -0.530  0.36 18.23 ?  163 LYS   A O    1 
ATOM   3643 C  CB   A LYS   A 1 163 ? 3.661  -6.828  -1.248  0.64 22.42 ?  163 LYS   A CB   1 
ATOM   3644 C  CB   B LYS   A 1 163 ? 3.649  -7.220  -1.459  0.36 21.06 ?  163 LYS   A CB   1 
ATOM   3645 C  CG   A LYS   A 1 163 ? 3.722  -7.576  -2.574  0.64 24.94 ?  163 LYS   A CG   1 
ATOM   3646 C  CG   B LYS   A 1 163 ? 3.577  -7.967  -2.782  0.36 23.44 ?  163 LYS   A CG   1 
ATOM   3647 C  CD   A LYS   A 1 163 ? 4.140  -6.682  -3.724  0.64 27.24 ?  163 LYS   A CD   1 
ATOM   3648 C  CD   B LYS   A 1 163 ? 3.506  -7.020  -3.976  0.36 25.50 ?  163 LYS   A CD   1 
ATOM   3649 C  CE   A LYS   A 1 163 ? 4.072  -7.431  -5.048  0.64 29.11 ?  163 LYS   A CE   1 
ATOM   3650 C  CE   B LYS   A 1 163 ? 4.886  -6.731  -4.548  0.36 27.11 ?  163 LYS   A CE   1 
ATOM   3651 N  NZ   A LYS   A 1 163 ? 4.681  -6.659  -6.165  0.64 30.17 ?  163 LYS   A NZ   1 
ATOM   3652 N  NZ   B LYS   A 1 163 ? 4.831  -6.169  -5.929  0.36 28.06 ?  163 LYS   A NZ   1 
ATOM   3653 H  H    A LYS   A 1 163 ? 3.512  -6.153  1.117   0.64 23.26 ?  163 LYS   A H    1 
ATOM   3654 H  H    B LYS   A 1 163 ? 3.547  -6.455  0.858   0.36 21.75 ?  163 LYS   A H    1 
ATOM   3655 H  HA   A LYS   A 1 163 ? 2.534  -8.186  -0.219  0.64 24.17 ?  163 LYS   A HA   1 
ATOM   3656 H  HA   B LYS   A 1 163 ? 2.576  -8.574  -0.363  0.36 22.66 ?  163 LYS   A HA   1 
ATOM   3657 H  HB2  A LYS   A 1 163 ? 2.945  -6.169  -1.313  0.64 27.02 ?  163 LYS   A HB2  1 
ATOM   3658 H  HB2  B LYS   A 1 163 ? 2.970  -6.524  -1.477  0.36 25.39 ?  163 LYS   A HB2  1 
ATOM   3659 H  HB3  A LYS   A 1 163 ? 4.507  -6.380  -1.116  0.64 27.02 ?  163 LYS   A HB3  1 
ATOM   3660 H  HB3  B LYS   A 1 163 ? 4.527  -6.816  -1.395  0.36 25.39 ?  163 LYS   A HB3  1 
ATOM   3661 H  HG2  A LYS   A 1 163 ? 4.369  -8.295  -2.509  0.64 30.05 ?  163 LYS   A HG2  1 
ATOM   3662 H  HG2  B LYS   A 1 163 ? 4.370  -8.518  -2.877  0.36 28.24 ?  163 LYS   A HG2  1 
ATOM   3663 H  HG3  A LYS   A 1 163 ? 2.844  -7.938  -2.776  0.64 30.05 ?  163 LYS   A HG3  1 
ATOM   3664 H  HG3  B LYS   A 1 163 ? 2.783  -8.521  -2.791  0.36 28.24 ?  163 LYS   A HG3  1 
ATOM   3665 H  HD2  A LYS   A 1 163 ? 3.542  -5.921  -3.774  0.64 32.80 ?  163 LYS   A HD2  1 
ATOM   3666 H  HD2  B LYS   A 1 163 ? 2.966  -7.425  -4.673  0.36 30.72 ?  163 LYS   A HD2  1 
ATOM   3667 H  HD3  A LYS   A 1 163 ? 5.053  -6.387  -3.586  0.64 32.80 ?  163 LYS   A HD3  1 
ATOM   3668 H  HD3  B LYS   A 1 163 ? 3.113  -6.177  -3.696  0.36 30.72 ?  163 LYS   A HD3  1 
ATOM   3669 H  HE2  A LYS   A 1 163 ? 4.545  -8.274  -4.963  0.64 35.05 ?  163 LYS   A HE2  1 
ATOM   3670 H  HE2  B LYS   A 1 163 ? 5.336  -6.087  -3.982  0.36 32.65 ?  163 LYS   A HE2  1 
ATOM   3671 H  HE3  A LYS   A 1 163 ? 3.144  -7.597  -5.270  0.64 35.05 ?  163 LYS   A HE3  1 
ATOM   3672 H  HE3  B LYS   A 1 163 ? 5.394  -7.554  -4.578  0.36 32.65 ?  163 LYS   A HE3  1 
ATOM   3673 H  HZ1  A LYS   A 1 163 ? 4.627  -7.123  -6.922  0.64 36.32 ?  163 LYS   A HZ1  1 
ATOM   3674 H  HZ1  B LYS   A 1 163 ? 5.655  -6.017  -6.230  0.36 33.79 ?  163 LYS   A HZ1  1 
ATOM   3675 H  HZ2  A LYS   A 1 163 ? 4.252  -5.885  -6.268  0.64 36.32 ?  163 LYS   A HZ2  1 
ATOM   3676 H  HZ2  B LYS   A 1 163 ? 4.427  -6.744  -6.476  0.36 33.79 ?  163 LYS   A HZ2  1 
ATOM   3677 H  HZ3  A LYS   A 1 163 ? 5.538  -6.492  -5.989  0.64 36.32 ?  163 LYS   A HZ3  1 
ATOM   3678 H  HZ3  B LYS   A 1 163 ? 4.377  -5.404  -5.928  0.36 33.79 ?  163 LYS   A HZ3  1 
ATOM   3679 N  N    A LEU   A 1 164 ? 5.567  -8.547  0.708   0.64 17.59 ?  164 LEU   A N    1 
ATOM   3680 N  N    B LEU   A 1 164 ? 5.643  -8.763  0.523   0.36 16.01 ?  164 LEU   A N    1 
ATOM   3681 C  CA   A LEU   A 1 164 ? 6.635  -9.540  0.808   0.64 17.06 ?  164 LEU   A CA   1 
ATOM   3682 C  CA   B LEU   A 1 164 ? 6.742  -9.700  0.742   0.36 15.38 ?  164 LEU   A CA   1 
ATOM   3683 C  C    A LEU   A 1 164 ? 6.205  -10.731 1.652   0.64 17.37 ?  164 LEU   A C    1 
ATOM   3684 C  C    B LEU   A 1 164 ? 6.305  -10.855 1.632   0.36 15.66 ?  164 LEU   A C    1 
ATOM   3685 O  O    A LEU   A 1 164 ? 6.508  -11.881 1.315   0.64 17.82 ?  164 LEU   A O    1 
ATOM   3686 O  O    B LEU   A 1 164 ? 6.597  -12.023 1.347   0.36 15.67 ?  164 LEU   A O    1 
ATOM   3687 C  CB   A LEU   A 1 164 ? 7.883  -8.904  1.405   0.64 16.74 ?  164 LEU   A CB   1 
ATOM   3688 C  CB   B LEU   A 1 164 ? 7.918  -8.967  1.386   0.36 15.04 ?  164 LEU   A CB   1 
ATOM   3689 C  CG   A LEU   A 1 164 ? 8.623  -7.963  0.462   0.64 16.72 ?  164 LEU   A CG   1 
ATOM   3690 C  CG   B LEU   A 1 164 ? 8.723  -7.997  0.519   0.36 14.86 ?  164 LEU   A CG   1 
ATOM   3691 C  CD1  A LEU   A 1 164 ? 9.628  -7.149  1.247   0.64 16.34 ?  164 LEU   A CD1  1 
ATOM   3692 C  CD1  B LEU   A 1 164 ? 9.502  -7.019  1.391   0.36 14.75 ?  164 LEU   A CD1  1 
ATOM   3693 C  CD2  A LEU   A 1 164 ? 9.317  -8.741  -0.646  0.64 16.83 ?  164 LEU   A CD2  1 
ATOM   3694 C  CD2  B LEU   A 1 164 ? 9.673  -8.753  -0.395  0.36 14.54 ?  164 LEU   A CD2  1 
ATOM   3695 H  H    A LEU   A 1 164 ? 5.733  -7.791  1.105   0.64 21.22 ?  164 LEU   A H    1 
ATOM   3696 H  H    B LEU   A 1 164 ? 5.789  -7.969  0.819   0.36 19.33 ?  164 LEU   A H    1 
ATOM   3697 H  HA   A LEU   A 1 164 ? 6.855  -9.855  -0.081  0.64 20.59 ?  164 LEU   A HA   1 
ATOM   3698 H  HA   B LEU   A 1 164 ? 7.032  -10.060 -0.110  0.36 18.57 ?  164 LEU   A HA   1 
ATOM   3699 H  HB2  A LEU   A 1 164 ? 7.634  -8.391  2.188   0.64 20.21 ?  164 LEU   A HB2  1 
ATOM   3700 H  HB2  B LEU   A 1 164 ? 7.578  -8.456  2.135   0.36 18.17 ?  164 LEU   A HB2  1 
ATOM   3701 H  HB3  A LEU   A 1 164 ? 8.503  -9.606  1.655   0.64 20.21 ?  164 LEU   A HB3  1 
ATOM   3702 H  HB3  B LEU   A 1 164 ? 8.541  -9.633  1.711   0.36 18.17 ?  164 LEU   A HB3  1 
ATOM   3703 H  HG   A LEU   A 1 164 ? 7.992  -7.349  0.053   0.64 20.17 ?  164 LEU   A HG   1 
ATOM   3704 H  HG   B LEU   A 1 164 ? 8.116  -7.483  -0.035  0.36 17.94 ?  164 LEU   A HG   1 
ATOM   3705 H  HD11 A LEU   A 1 164 ? 10.104 -6.562  0.642   0.64 19.73 ?  164 LEU   A HD11 1 
ATOM   3706 H  HD11 B LEU   A 1 164 ? 10.013 -6.421  0.821   0.36 17.82 ?  164 LEU   A HD11 1 
ATOM   3707 H  HD12 A LEU   A 1 164 ? 9.155  -6.625  1.914   0.64 19.73 ?  164 LEU   A HD12 1 
ATOM   3708 H  HD12 B LEU   A 1 164 ? 8.876  -6.504  1.927   0.36 17.82 ?  164 LEU   A HD12 1 
ATOM   3709 H  HD13 A LEU   A 1 164 ? 10.249 -7.753  1.682   0.64 19.73 ?  164 LEU   A HD13 1 
ATOM   3710 H  HD13 B LEU   A 1 164 ? 10.100 -7.515  1.970   0.36 17.82 ?  164 LEU   A HD13 1 
ATOM   3711 H  HD21 A LEU   A 1 164 ? 9.876  -8.135  -1.158  0.64 20.31 ?  164 LEU   A HD21 1 
ATOM   3712 H  HD21 B LEU   A 1 164 ? 10.167 -8.115  -0.935  0.36 17.56 ?  164 LEU   A HD21 1 
ATOM   3713 H  HD22 A LEU   A 1 164 ? 9.863  -9.437  -0.247  0.64 20.31 ?  164 LEU   A HD22 1 
ATOM   3714 H  HD22 B LEU   A 1 164 ? 10.286 -9.272  0.147   0.36 17.56 ?  164 LEU   A HD22 1 
ATOM   3715 H  HD23 A LEU   A 1 164 ? 8.645  -9.137  -1.222  0.64 20.31 ?  164 LEU   A HD23 1 
ATOM   3716 H  HD23 B LEU   A 1 164 ? 9.156  -9.340  -0.967  0.36 17.56 ?  164 LEU   A HD23 1 
ATOM   3717 N  N    A VAL   A 1 165 ? 5.522  -10.470 2.765   0.64 16.82 ?  165 VAL   A N    1 
ATOM   3718 N  N    B VAL   A 1 165 ? 5.620  -10.543 2.733   0.36 15.46 ?  165 VAL   A N    1 
ATOM   3719 C  CA   A VAL   A 1 165 ? 5.037  -11.555 3.611   0.64 16.37 ?  165 VAL   A CA   1 
ATOM   3720 C  CA   B VAL   A 1 165 ? 5.180  -11.586 3.652   0.36 15.43 ?  165 VAL   A CA   1 
ATOM   3721 C  C    A VAL   A 1 165 ? 4.021  -12.399 2.853   0.64 16.61 ?  165 VAL   A C    1 
ATOM   3722 C  C    B VAL   A 1 165 ? 4.116  -12.459 3.005   0.36 15.50 ?  165 VAL   A C    1 
ATOM   3723 O  O    A VAL   A 1 165 ? 4.149  -13.626 2.757   0.64 16.60 ?  165 VAL   A O    1 
ATOM   3724 O  O    B VAL   A 1 165 ? 4.161  -13.692 3.102   0.36 15.11 ?  165 VAL   A O    1 
ATOM   3725 C  CB   A VAL   A 1 165 ? 4.448  -10.984 4.914   0.64 16.93 ?  165 VAL   A CB   1 
ATOM   3726 C  CB   B VAL   A 1 165 ? 4.687  -10.965 4.971   0.36 15.73 ?  165 VAL   A CB   1 
ATOM   3727 C  CG1  A VAL   A 1 165 ? 3.728  -12.072 5.702   0.64 17.36 ?  165 VAL   A CG1  1 
ATOM   3728 C  CG1  B VAL   A 1 165 ? 3.994  -12.015 5.828   0.36 16.11 ?  165 VAL   A CG1  1 
ATOM   3729 C  CG2  A VAL   A 1 165 ? 5.541  -10.322 5.750   0.64 17.27 ?  165 VAL   A CG2  1 
ATOM   3730 C  CG2  B VAL   A 1 165 ? 5.846  -10.337 5.724   0.36 16.06 ?  165 VAL   A CG2  1 
ATOM   3731 H  H    A VAL   A 1 165 ? 5.324  -9.679  3.045   0.64 20.30 ?  165 VAL   A H    1 
ATOM   3732 H  H    B VAL   A 1 165 ? 5.407  -9.742  2.969   0.36 18.67 ?  165 VAL   A H    1 
ATOM   3733 H  HA   A VAL   A 1 165 ? 5.786  -12.124 3.849   0.64 19.76 ?  165 VAL   A HA   1 
ATOM   3734 H  HA   B VAL   A 1 165 ? 5.936  -12.152 3.863   0.36 18.63 ?  165 VAL   A HA   1 
ATOM   3735 H  HB   A VAL   A 1 165 ? 3.800  -10.300 4.691   0.64 20.43 ?  165 VAL   A HB   1 
ATOM   3736 H  HB   B VAL   A 1 165 ? 4.040  -10.267 4.774   0.36 18.99 ?  165 VAL   A HB   1 
ATOM   3737 H  HG11 A VAL   A 1 165 ? 3.612  -11.772 6.617   0.64 20.95 ?  165 VAL   A HG11 1 
ATOM   3738 H  HG11 B VAL   A 1 165 ? 3.961  -11.699 6.744   0.36 19.44 ?  165 VAL   A HG11 1 
ATOM   3739 H  HG12 A VAL   A 1 165 ? 2.862  -12.233 5.296   0.64 20.95 ?  165 VAL   A HG12 1 
ATOM   3740 H  HG12 B VAL   A 1 165 ? 3.093  -12.156 5.495   0.36 19.44 ?  165 VAL   A HG12 1 
ATOM   3741 H  HG13 A VAL   A 1 165 ? 4.262  -12.880 5.684   0.64 20.95 ?  165 VAL   A HG13 1 
ATOM   3742 H  HG13 B VAL   A 1 165 ? 4.499  -12.841 5.783   0.36 19.44 ?  165 VAL   A HG13 1 
ATOM   3743 H  HG21 A VAL   A 1 165 ? 5.158  -10.006 6.583   0.64 20.85 ?  165 VAL   A HG21 1 
ATOM   3744 H  HG21 B VAL   A 1 165 ? 5.514  -9.942  6.546   0.36 19.39 ?  165 VAL   A HG21 1 
ATOM   3745 H  HG22 A VAL   A 1 165 ? 6.241  -10.969 5.931   0.64 20.85 ?  165 VAL   A HG22 1 
ATOM   3746 H  HG22 B VAL   A 1 165 ? 6.498  -11.025 5.927   0.36 19.39 ?  165 VAL   A HG22 1 
ATOM   3747 H  HG23 A VAL   A 1 165 ? 5.910  -9.571  5.253   0.64 20.85 ?  165 VAL   A HG23 1 
ATOM   3748 H  HG23 B VAL   A 1 165 ? 6.249  -9.653  5.167   0.36 19.39 ?  165 VAL   A HG23 1 
ATOM   3749 N  N    A SER   A 1 166 ? 3.007  -11.745 2.284   0.64 16.83 ?  166 SER   A N    1 
ATOM   3750 N  N    B SER   A 1 166 ? 3.146  -11.839 2.330   0.36 16.02 ?  166 SER   A N    1 
ATOM   3751 C  CA   A SER   A 1 166 ? 1.906  -12.474 1.665   0.64 17.27 ?  166 SER   A CA   1 
ATOM   3752 C  CA   B SER   A 1 166 ? 1.995  -12.591 1.847   0.36 16.71 ?  166 SER   A CA   1 
ATOM   3753 C  C    A SER   A 1 166 ? 2.357  -13.267 0.448   0.64 17.20 ?  166 SER   A C    1 
ATOM   3754 C  C    B SER   A 1 166 ? 2.355  -13.577 0.740   0.36 16.99 ?  166 SER   A C    1 
ATOM   3755 O  O    A SER   A 1 166 ? 1.697  -14.242 0.072   0.64 18.84 ?  166 SER   A O    1 
ATOM   3756 O  O    B SER   A 1 166 ? 1.639  -14.566 0.559   0.36 17.84 ?  166 SER   A O    1 
ATOM   3757 C  CB   A SER   A 1 166 ? 0.796  -11.504 1.259   0.64 17.85 ?  166 SER   A CB   1 
ATOM   3758 C  CB   B SER   A 1 166 ? 0.868  -11.634 1.423   0.36 17.33 ?  166 SER   A CB   1 
ATOM   3759 O  OG   A SER   A 1 166 ? 0.167  -10.937 2.395   0.64 18.42 ?  166 SER   A OG   1 
ATOM   3760 O  OG   B SER   A 1 166 ? 1.211  -10.888 0.269   0.36 17.99 ?  166 SER   A OG   1 
ATOM   3761 H  H    A SER   A 1 166 ? 2.933  -10.890 2.251   0.64 20.31 ?  166 SER   A H    1 
ATOM   3762 H  H    B SER   A 1 166 ? 3.131  -10.996 2.146   0.36 19.34 ?  166 SER   A H    1 
ATOM   3763 H  HA   A SER   A 1 166 ? 1.533  -13.096 2.313   0.64 20.84 ?  166 SER   A HA   1 
ATOM   3764 H  HA   B SER   A 1 166 ? 1.649  -13.114 2.579   0.36 20.17 ?  166 SER   A HA   1 
ATOM   3765 H  HB2  A SER   A 1 166 ? 1.179  -10.795 0.719   0.64 21.54 ?  166 SER   A HB2  1 
ATOM   3766 H  HB2  B SER   A 1 166 ? 0.071  -12.148 1.225   0.36 20.91 ?  166 SER   A HB2  1 
ATOM   3767 H  HB3  A SER   A 1 166 ? 0.128  -11.986 0.746   0.64 21.54 ?  166 SER   A HB3  1 
ATOM   3768 H  HB3  B SER   A 1 166 ? 0.682  -11.018 2.159   0.36 20.91 ?  166 SER   A HB3  1 
ATOM   3769 H  HG   A SER   A 1 166 ? -0.432 -10.401 2.156   0.64 22.22 ?  166 SER   A HG   1 
ATOM   3770 H  HG   B SER   A 1 166 ? 0.587  -10.357 0.070   0.36 21.71 ?  166 SER   A HG   1 
ATOM   3771 N  N    A SER   A 1 167 ? 3.447  -12.861 -0.198  0.64 16.22 ?  167 SER   A N    1 
ATOM   3772 N  N    B SER   A 1 167 ? 3.469  -13.376 0.034   0.36 17.24 ?  167 SER   A N    1 
ATOM   3773 C  CA   A SER   A 1 167 ? 3.928  -13.563 -1.378  0.64 16.53 ?  167 SER   A CA   1 
ATOM   3774 C  CA   B SER   A 1 167 ? 3.794  -14.191 -1.132  0.36 17.23 ?  167 SER   A CA   1 
ATOM   3775 C  C    A SER   A 1 167 ? 5.074  -14.519 -1.077  0.64 17.07 ?  167 SER   A C    1 
ATOM   3776 C  C    B SER   A 1 167 ? 4.983  -15.118 -0.896  0.36 17.32 ?  167 SER   A C    1 
ATOM   3777 O  O    A SER   A 1 167 ? 5.572  -15.169 -2.001  0.64 18.74 ?  167 SER   A O    1 
ATOM   3778 O  O    B SER   A 1 167 ? 5.597  -15.583 -1.861  0.36 18.03 ?  167 SER   A O    1 
ATOM   3779 C  CB   A SER   A 1 167 ? 4.352  -12.562 -2.463  0.64 16.52 ?  167 SER   A CB   1 
ATOM   3780 C  CB   B SER   A 1 167 ? 4.033  -13.308 -2.359  0.36 17.79 ?  167 SER   A CB   1 
ATOM   3781 O  OG   A SER   A 1 167 ? 5.428  -11.751 -2.016  0.64 16.57 ?  167 SER   A OG   1 
ATOM   3782 O  OG   B SER   A 1 167 ? 5.244  -12.576 -2.253  0.36 18.30 ?  167 SER   A OG   1 
ATOM   3783 H  H    A SER   A 1 167 ? 3.905  -12.164 0.019   0.64 19.58 ?  167 SER   A H    1 
ATOM   3784 H  H    B SER   A 1 167 ? 4.061  -12.786 0.230   0.36 20.81 ?  167 SER   A H    1 
ATOM   3785 H  HA   A SER   A 1 167 ? 3.193  -14.080 -1.741  0.64 19.95 ?  167 SER   A HA   1 
ATOM   3786 H  HA   B SER   A 1 167 ? 3.038  -14.761 -1.329  0.36 20.80 ?  167 SER   A HA   1 
ATOM   3787 H  HB2  A SER   A 1 167 ? 4.631  -13.054 -3.250  0.64 19.94 ?  167 SER   A HB2  1 
ATOM   3788 H  HB2  B SER   A 1 167 ? 4.074  -13.875 -3.145  0.36 21.46 ?  167 SER   A HB2  1 
ATOM   3789 H  HB3  A SER   A 1 167 ? 3.587  -11.996 -2.689  0.64 19.94 ?  167 SER   A HB3  1 
ATOM   3790 H  HB3  B SER   A 1 167 ? 3.291  -12.686 -2.443  0.36 21.46 ?  167 SER   A HB3  1 
ATOM   3791 H  HG   A SER   A 1 167 ? 5.175  -11.307 -1.344  0.64 20.00 ?  167 SER   A HG   1 
ATOM   3792 H  HG   B SER   A 1 167 ? 5.217  -12.076 -1.579  0.36 22.07 ?  167 SER   A HG   1 
ATOM   3793 N  N    A PHE   A 1 168 ? 5.499  -14.631 0.180   0.64 16.44 ?  168 PHE   A N    1 
ATOM   3794 N  N    B PHE   A 1 168 ? 5.298  -15.434 0.360   0.36 16.83 ?  168 PHE   A N    1 
ATOM   3795 C  CA   A PHE   A 1 168 ? 6.675  -15.434 0.490   0.64 16.89 ?  168 PHE   A CA   1 
ATOM   3796 C  CA   B PHE   A 1 168 ? 6.557  -16.113 0.656   0.36 16.85 ?  168 PHE   A CA   1 
ATOM   3797 C  C    A PHE   A 1 168 ? 6.363  -16.920 0.383   0.64 17.93 ?  168 PHE   A C    1 
ATOM   3798 C  C    B PHE   A 1 168 ? 6.477  -17.633 0.530   0.36 18.49 ?  168 PHE   A C    1 
ATOM   3799 O  O    A PHE   A 1 168 ? 5.359  -17.401 0.920   0.64 19.47 ?  168 PHE   A O    1 
ATOM   3800 O  O    B PHE   A 1 168 ? 7.238  -18.233 -0.236  0.36 18.78 ?  168 PHE   A O    1 
ATOM   3801 C  CB   A PHE   A 1 168 ? 7.192  -15.137 1.894   0.64 16.65 ?  168 PHE   A CB   1 
ATOM   3802 C  CB   B PHE   A 1 168 ? 7.066  -15.734 2.049   0.36 16.35 ?  168 PHE   A CB   1 
ATOM   3803 C  CG   A PHE   A 1 168 ? 8.449  -15.886 2.224   0.64 16.99 ?  168 PHE   A CG   1 
ATOM   3804 C  CG   B PHE   A 1 168 ? 8.390  -16.355 2.384   0.36 15.50 ?  168 PHE   A CG   1 
ATOM   3805 C  CD1  A PHE   A 1 168 ? 9.652  -15.496 1.669   0.64 17.53 ?  168 PHE   A CD1  1 
ATOM   3806 C  CD1  B PHE   A 1 168 ? 9.538  -15.953 1.725   0.36 15.27 ?  168 PHE   A CD1  1 
ATOM   3807 C  CD2  A PHE   A 1 168 ? 8.428  -16.996 3.052   0.64 16.96 ?  168 PHE   A CD2  1 
ATOM   3808 C  CD2  B PHE   A 1 168 ? 8.488  -17.352 3.341   0.36 15.03 ?  168 PHE   A CD2  1 
ATOM   3809 C  CE1  A PHE   A 1 168 ? 10.813 -16.186 1.949   0.64 17.63 ?  168 PHE   A CE1  1 
ATOM   3810 C  CE1  B PHE   A 1 168 ? 10.758 -16.525 2.019   0.36 15.02 ?  168 PHE   A CE1  1 
ATOM   3811 C  CE2  A PHE   A 1 168 ? 9.590  -17.688 3.336   0.64 17.32 ?  168 PHE   A CE2  1 
ATOM   3812 C  CE2  B PHE   A 1 168 ? 9.708  -17.926 3.641   0.36 15.13 ?  168 PHE   A CE2  1 
ATOM   3813 C  CZ   A PHE   A 1 168 ? 10.781 -17.282 2.783   0.64 17.40 ?  168 PHE   A CZ   1 
ATOM   3814 C  CZ   B PHE   A 1 168 ? 10.844 -17.512 2.979   0.36 15.29 ?  168 PHE   A CZ   1 
ATOM   3815 H  H    A PHE   A 1 168 ? 5.132  -14.246 0.860   0.64 19.85 ?  168 PHE   A H    1 
ATOM   3816 H  H    B PHE   A 1 168 ? 4.805  -15.272 1.050   0.36 20.31 ?  168 PHE   A H    1 
ATOM   3817 H  HA   A PHE   A 1 168 ? 7.377  -15.215 -0.146  0.64 20.38 ?  168 PHE   A HA   1 
ATOM   3818 H  HA   B PHE   A 1 168 ? 7.218  -15.811 0.014   0.36 20.34 ?  168 PHE   A HA   1 
ATOM   3819 H  HB2  A PHE   A 1 168 ? 7.376  -14.187 1.970   0.64 20.10 ?  168 PHE   A HB2  1 
ATOM   3820 H  HB2  B PHE   A 1 168 ? 7.167  -14.773 2.091   0.36 19.74 ?  168 PHE   A HB2  1 
ATOM   3821 H  HB3  A PHE   A 1 168 ? 6.511  -15.393 2.537   0.64 20.10 ?  168 PHE   A HB3  1 
ATOM   3822 H  HB3  B PHE   A 1 168 ? 6.420  -16.033 2.707   0.36 19.74 ?  168 PHE   A HB3  1 
ATOM   3823 H  HD1  A PHE   A 1 168 ? 9.682  -14.756 1.104   0.64 21.15 ?  168 PHE   A HD1  1 
ATOM   3824 H  HD1  B PHE   A 1 168 ? 9.486  -15.288 1.075   0.36 18.44 ?  168 PHE   A HD1  1 
ATOM   3825 H  HD2  A PHE   A 1 168 ? 7.623  -17.273 3.427   0.64 20.47 ?  168 PHE   A HD2  1 
ATOM   3826 H  HD2  B PHE   A 1 168 ? 7.721  -17.636 3.787   0.36 18.15 ?  168 PHE   A HD2  1 
ATOM   3827 H  HE1  A PHE   A 1 168 ? 11.622 -15.911 1.576   0.64 21.28 ?  168 PHE   A HE1  1 
ATOM   3828 H  HE1  B PHE   A 1 168 ? 11.525 -16.242 1.572   0.36 18.14 ?  168 PHE   A HE1  1 
ATOM   3829 H  HE2  A PHE   A 1 168 ? 9.563  -18.428 3.899   0.64 20.90 ?  168 PHE   A HE2  1 
ATOM   3830 H  HE2  B PHE   A 1 168 ? 9.762  -18.593 4.287   0.36 18.27 ?  168 PHE   A HE2  1 
ATOM   3831 H  HZ   A PHE   A 1 168 ? 11.566 -17.747 2.973   0.64 20.99 ?  168 PHE   A HZ   1 
ATOM   3832 H  HZ   B PHE   A 1 168 ? 11.668 -17.897 3.180   0.36 18.46 ?  168 PHE   A HZ   1 
ATOM   3833 N  N    A LEU   A 1 169 ? 7.254  -17.655 -0.275  0.64 19.10 ?  169 LEU   A N    1 
ATOM   3834 N  N    B LEU   A 1 169 ? 5.613  -18.272 1.314   0.36 20.19 ?  169 LEU   A N    1 
ATOM   3835 C  CA   A LEU   A 1 169 ? 7.055  -19.088 -0.448  0.64 20.91 ?  169 LEU   A CA   1 
ATOM   3836 C  CA   B LEU   A 1 169 ? 5.588  -19.733 1.361   0.36 22.35 ?  169 LEU   A CA   1 
ATOM   3837 C  C    A LEU   A 1 169 ? 7.872  -19.881 0.566   0.64 21.03 ?  169 LEU   A C    1 
ATOM   3838 C  C    B LEU   A 1 169 ? 4.949  -20.341 0.114   0.36 23.36 ?  169 LEU   A C    1 
ATOM   3839 O  O    A LEU   A 1 169 ? 7.298  -20.446 1.502   0.64 21.44 ?  169 LEU   A O    1 
ATOM   3840 O  O    B LEU   A 1 169 ? 5.287  -21.459 -0.278  0.36 23.94 ?  169 LEU   A O    1 
ATOM   3841 C  CB   A LEU   A 1 169 ? 7.386  -19.515 -1.881  0.64 22.16 ?  169 LEU   A CB   1 
ATOM   3842 C  CB   B LEU   A 1 169 ? 4.853  -20.223 2.612   0.36 23.03 ?  169 LEU   A CB   1 
ATOM   3843 C  CG   A LEU   A 1 169 ? 7.103  -20.982 -2.227  0.64 23.36 ?  169 LEU   A CG   1 
ATOM   3844 C  CG   B LEU   A 1 169 ? 5.207  -21.635 3.087   0.36 23.55 ?  169 LEU   A CG   1 
ATOM   3845 C  CD1  A LEU   A 1 169 ? 5.685  -21.374 -1.842  0.64 23.89 ?  169 LEU   A CD1  1 
ATOM   3846 C  CD1  B LEU   A 1 169 ? 6.624  -21.660 3.642   0.36 23.85 ?  169 LEU   A CD1  1 
ATOM   3847 C  CD2  A LEU   A 1 169 ? 7.339  -21.245 -3.708  0.64 23.77 ?  169 LEU   A CD2  1 
ATOM   3848 C  CD2  B LEU   A 1 169 ? 4.214  -22.128 4.129   0.36 23.77 ?  169 LEU   A CD2  1 
ATOM   3849 O  OXT  A LEU   A 1 169 ? 9.100  -19.969 0.488   0.64 21.08 -1 169 LEU   A OXT  1 
ATOM   3850 O  OXT  B LEU   A 1 169 ? 4.082  -19.743 -0.526  0.36 23.60 -1 169 LEU   A OXT  1 
ATOM   3851 H  H    A LEU   A 1 169 ? 7.982  -17.349 -0.626  0.64 23.04 ?  169 LEU   A H    1 
ATOM   3852 H  H    B LEU   A 1 169 ? 5.049  -17.887 1.842   0.36 24.35 ?  169 LEU   A H    1 
ATOM   3853 H  HA   A LEU   A 1 169 ? 6.127  -19.292 -0.282  0.64 25.21 ?  169 LEU   A HA   1 
ATOM   3854 H  HA   B LEU   A 1 169 ? 6.503  -20.050 1.408   0.36 26.93 ?  169 LEU   A HA   1 
ATOM   3855 H  HB2  A LEU   A 1 169 ? 6.861  -18.972 -2.491  0.64 26.71 ?  169 LEU   A HB2  1 
ATOM   3856 H  HB2  B LEU   A 1 169 ? 5.059  -19.624 3.342   0.36 27.76 ?  169 LEU   A HB2  1 
ATOM   3857 H  HB3  A LEU   A 1 169 ? 8.328  -19.361 -2.041  0.64 26.71 ?  169 LEU   A HB3  1 
ATOM   3858 H  HB3  B LEU   A 1 169 ? 3.901  -20.208 2.435   0.36 27.76 ?  169 LEU   A HB3  1 
ATOM   3859 H  HG   A LEU   A 1 169 ? 7.711  -21.547 -1.727  0.64 28.14 ?  169 LEU   A HG   1 
ATOM   3860 H  HG   B LEU   A 1 169 ? 5.174  -22.241 2.331   0.36 28.37 ?  169 LEU   A HG   1 
ATOM   3861 H  HD11 A LEU   A 1 169 ? 5.474  -22.234 -2.236  0.64 28.78 ?  169 LEU   A HD11 1 
ATOM   3862 H  HD11 B LEU   A 1 169 ? 6.783  -22.519 4.063   0.36 28.73 ?  169 LEU   A HD11 1 
ATOM   3863 H  HD12 A LEU   A 1 169 ? 5.623  -21.430 -0.875  0.64 28.78 ?  169 LEU   A HD12 1 
ATOM   3864 H  HD12 B LEU   A 1 169 ? 7.253  -21.528 2.915   0.36 28.73 ?  169 LEU   A HD12 1 
ATOM   3865 H  HD13 A LEU   A 1 169 ? 5.069  -20.700 -2.173  0.64 28.78 ?  169 LEU   A HD13 1 
ATOM   3866 H  HD13 B LEU   A 1 169 ? 6.722  -20.950 4.296   0.36 28.73 ?  169 LEU   A HD13 1 
ATOM   3867 H  HD21 A LEU   A 1 169 ? 7.158  -22.180 -3.896  0.64 28.64 ?  169 LEU   A HD21 1 
ATOM   3868 H  HD21 B LEU   A 1 169 ? 4.469  -23.021 4.410   0.36 28.64 ?  169 LEU   A HD21 1 
ATOM   3869 H  HD22 A LEU   A 1 169 ? 6.741  -20.683 -4.227  0.64 28.64 ?  169 LEU   A HD22 1 
ATOM   3870 H  HD22 B LEU   A 1 169 ? 4.230  -21.526 4.890   0.36 28.64 ?  169 LEU   A HD22 1 
ATOM   3871 H  HD23 A LEU   A 1 169 ? 8.260  -21.035 -3.922  0.64 28.64 ?  169 LEU   A HD23 1 
ATOM   3872 H  HD23 B LEU   A 1 169 ? 3.328  -22.143 3.737   0.36 28.64 ?  169 LEU   A HD23 1 
ATOM   3873 N  N    . SER   B 1 1   ? 50.795 -9.258  -23.697 1.00 27.24 ?  1   SER   B N    1 
ATOM   3874 C  CA   . SER   B 1 1   ? 51.263 -10.284 -22.747 1.00 27.04 ?  1   SER   B CA   1 
ATOM   3875 C  C    . SER   B 1 1   ? 50.209 -11.360 -22.538 1.00 26.09 ?  1   SER   B C    1 
ATOM   3876 O  O    . SER   B 1 1   ? 49.016 -11.182 -22.844 1.00 26.24 ?  1   SER   B O    1 
ATOM   3877 C  CB   . SER   B 1 1   ? 51.645 -9.660  -21.406 1.00 28.01 ?  1   SER   B CB   1 
ATOM   3878 O  OG   . SER   B 1 1   ? 50.496 -9.426  -20.614 1.00 30.02 ?  1   SER   B OG   1 
ATOM   3879 H  H1   . SER   B 1 1   ? 50.748 -9.617  -24.506 1.00 32.80 ?  1   SER   B H1   1 
ATOM   3880 H  H2   . SER   B 1 1   ? 49.997 -8.973  -23.442 1.00 32.80 ?  1   SER   B H2   1 
ATOM   3881 H  H3   . SER   B 1 1   ? 51.373 -8.583  -23.699 1.00 32.80 ?  1   SER   B H3   1 
ATOM   3882 H  HA   . SER   B 1 1   ? 52.055 -10.698 -23.118 1.00 32.56 ?  1   SER   B HA   1 
ATOM   3883 H  HB2  . SER   B 1 1   ? 52.231 -10.271 -20.933 1.00 33.73 ?  1   SER   B HB2  1 
ATOM   3884 H  HB3  . SER   B 1 1   ? 52.102 -8.818  -21.564 1.00 33.73 ?  1   SER   B HB3  1 
ATOM   3885 H  HG   . SER   B 1 1   ? 50.681 -8.875  -20.003 1.00 36.14 ?  1   SER   B HG   1 
ATOM   3886 N  N    A MET   B 1 2   ? 50.659 -12.488 -22.002 0.64 26.16 ?  2   MET   B N    1 
ATOM   3887 N  N    B MET   B 1 2   ? 50.663 -12.487 -22.007 0.36 25.44 ?  2   MET   B N    1 
ATOM   3888 C  CA   A MET   B 1 2   ? 49.838 -13.682 -21.850 0.64 26.41 ?  2   MET   B CA   1 
ATOM   3889 C  CA   B MET   B 1 2   ? 49.838 -13.671 -21.829 0.36 24.92 ?  2   MET   B CA   1 
ATOM   3890 C  C    A MET   B 1 2   ? 49.575 -13.896 -20.365 0.64 24.16 ?  2   MET   B C    1 
ATOM   3891 C  C    B MET   B 1 2   ? 49.582 -13.843 -20.343 0.36 23.33 ?  2   MET   B C    1 
ATOM   3892 O  O    A MET   B 1 2   ? 50.495 -14.218 -19.608 0.64 24.27 ?  2   MET   B O    1 
ATOM   3893 O  O    B MET   B 1 2   ? 50.515 -14.073 -19.567 0.36 23.25 ?  2   MET   B O    1 
ATOM   3894 C  CB   A MET   B 1 2   ? 50.567 -14.875 -22.459 0.64 29.84 ?  2   MET   B CB   1 
ATOM   3895 C  CB   B MET   B 1 2   ? 50.567 -14.875 -22.399 0.36 26.56 ?  2   MET   B CB   1 
ATOM   3896 C  CG   A MET   B 1 2   ? 49.725 -16.130 -22.607 0.64 33.15 ?  2   MET   B CG   1 
ATOM   3897 C  CG   B MET   B 1 2   ? 49.670 -16.031 -22.822 0.36 27.86 ?  2   MET   B CG   1 
ATOM   3898 S  SD   A MET   B 1 2   ? 50.585 -17.378 -23.583 0.64 36.18 ?  2   MET   B SD   1 
ATOM   3899 S  SD   B MET   B 1 2   ? 50.549 -17.143 -23.925 0.36 29.15 ?  2   MET   B SD   1 
ATOM   3900 C  CE   A MET   B 1 2   ? 51.102 -16.376 -24.973 0.64 36.30 ?  2   MET   B CE   1 
ATOM   3901 C  CE   B MET   B 1 2   ? 51.597 -15.975 -24.769 0.36 29.26 ?  2   MET   B CE   1 
ATOM   3902 H  H    A MET   B 1 2   ? 51.466 -12.595 -21.713 0.64 31.50 ?  2   MET   B H    1 
ATOM   3903 H  H    B MET   B 1 2   ? 51.476 -12.601 -21.736 0.36 30.64 ?  2   MET   B H    1 
ATOM   3904 H  HA   A MET   B 1 2   ? 49.001 -13.570 -22.323 0.64 31.80 ?  2   MET   B HA   1 
ATOM   3905 H  HA   B MET   B 1 2   ? 49.006 -13.576 -22.315 0.36 30.02 ?  2   MET   B HA   1 
ATOM   3906 H  HB2  A MET   B 1 2   ? 50.875 -14.601 -23.335 0.64 35.92 ?  2   MET   B HB2  1 
ATOM   3907 H  HB2  B MET   B 1 2   ? 51.030 -14.503 -23.156 0.36 31.99 ?  2   MET   B HB2  1 
ATOM   3908 H  HB3  A MET   B 1 2   ? 51.327 -15.108 -21.907 0.64 35.92 ?  2   MET   B HB3  1 
ATOM   3909 H  HB3  B MET   B 1 2   ? 51.206 -15.232 -21.768 0.36 31.99 ?  2   MET   B HB3  1 
ATOM   3910 H  HG2  A MET   B 1 2   ? 49.542 -16.500 -21.727 0.64 39.89 ?  2   MET   B HG2  1 
ATOM   3911 H  HG2  B MET   B 1 2   ? 49.388 -16.533 -22.033 0.36 33.55 ?  2   MET   B HG2  1 
ATOM   3912 H  HG3  A MET   B 1 2   ? 48.896 -15.915 -23.062 0.64 39.89 ?  2   MET   B HG3  1 
ATOM   3913 H  HG3  B MET   B 1 2   ? 48.898 -15.702 -23.302 0.36 33.55 ?  2   MET   B HG3  1 
ATOM   3914 H  HE1  A MET   B 1 2   ? 51.265 -16.952 -25.726 0.64 43.68 ?  2   MET   B HE1  1 
ATOM   3915 H  HE1  B MET   B 1 2   ? 51.951 -16.424 -25.516 0.36 35.22 ?  2   MET   B HE1  1 
ATOM   3916 H  HE2  A MET   B 1 2   ? 50.393 -15.743 -25.180 0.64 43.68 ?  2   MET   B HE2  1 
ATOM   3917 H  HE2  B MET   B 1 2   ? 51.056 -15.214 -25.055 0.36 35.22 ?  2   MET   B HE2  1 
ATOM   3918 H  HE3  A MET   B 1 2   ? 51.914 -15.891 -24.740 0.64 43.68 ?  2   MET   B HE3  1 
ATOM   3919 H  HE3  B MET   B 1 2   ? 52.325 -15.679 -24.184 0.36 35.22 ?  2   MET   B HE3  1 
ATOM   3920 N  N    . VAL   B 1 3   ? 48.323 -13.704 -19.949 1.00 22.03 ?  3   VAL   B N    1 
ATOM   3921 C  CA   . VAL   B 1 3   ? 47.906 -13.939 -18.576 1.00 20.56 ?  3   VAL   B CA   1 
ATOM   3922 C  C    . VAL   B 1 3   ? 46.667 -14.823 -18.600 1.00 18.67 ?  3   VAL   B C    1 
ATOM   3923 O  O    . VAL   B 1 3   ? 45.934 -14.889 -19.591 1.00 19.53 ?  3   VAL   B O    1 
ATOM   3924 C  CB   . VAL   B 1 3   ? 47.637 -12.630 -17.800 1.00 21.99 ?  3   VAL   B CB   1 
ATOM   3925 C  CG1  . VAL   B 1 3   ? 48.919 -11.796 -17.676 1.00 22.30 ?  3   VAL   B CG1  1 
ATOM   3926 C  CG2  . VAL   B 1 3   ? 46.529 -11.832 -18.470 1.00 22.83 ?  3   VAL   B CG2  1 
ATOM   3927 H  H    A VAL   B 1 3   ? 47.688 -13.440 -20.466 0.64 26.55 ?  3   VAL   B H    1 
ATOM   3928 H  H    B VAL   B 1 3   ? 47.685 -13.462 -20.473 0.36 26.55 ?  3   VAL   B H    1 
ATOM   3929 H  HA   . VAL   B 1 3   ? 48.606 -14.423 -18.111 1.00 24.79 ?  3   VAL   B HA   1 
ATOM   3930 H  HB   . VAL   B 1 3   ? 47.345 -12.859 -16.904 1.00 26.51 ?  3   VAL   B HB   1 
ATOM   3931 H  HG11 . VAL   B 1 3   ? 48.716 -10.991 -17.179 1.00 26.88 ?  3   VAL   B HG11 1 
ATOM   3932 H  HG12 . VAL   B 1 3   ? 49.586 -12.320 -17.206 1.00 26.88 ?  3   VAL   B HG12 1 
ATOM   3933 H  HG13 . VAL   B 1 3   ? 49.232 -11.574 -18.563 1.00 26.88 ?  3   VAL   B HG13 1 
ATOM   3934 H  HG21 . VAL   B 1 3   ? 46.469 -10.964 -18.048 1.00 27.52 ?  3   VAL   B HG21 1 
ATOM   3935 H  HG22 . VAL   B 1 3   ? 46.735 -11.733 -19.412 1.00 27.52 ?  3   VAL   B HG22 1 
ATOM   3936 H  HG23 . VAL   B 1 3   ? 45.689 -12.310 -18.366 1.00 27.52 ?  3   VAL   B HG23 1 
ATOM   3937 N  N    . ASN   B 1 4   ? 46.451 -15.523 -17.491 1.00 16.51 ?  4   ASN   B N    1 
ATOM   3938 C  CA   . ASN   B 1 4   ? 45.310 -16.429 -17.364 1.00 16.05 ?  4   ASN   B CA   1 
ATOM   3939 C  C    . ASN   B 1 4   ? 45.245 -17.397 -18.542 1.00 16.45 ?  4   ASN   B C    1 
ATOM   3940 O  O    . ASN   B 1 4   ? 44.183 -17.651 -19.104 1.00 17.07 ?  4   ASN   B O    1 
ATOM   3941 C  CB   . ASN   B 1 4   ? 43.997 -15.655 -17.206 1.00 15.59 ?  4   ASN   B CB   1 
ATOM   3942 C  CG   . ASN   B 1 4   ? 43.955 -14.842 -15.923 1.00 15.10 ?  4   ASN   B CG   1 
ATOM   3943 O  OD1  . ASN   B 1 4   ? 44.230 -15.356 -14.839 1.00 14.80 ?  4   ASN   B OD1  1 
ATOM   3944 N  ND2  . ASN   B 1 4   ? 43.628 -13.559 -16.046 1.00 15.80 ?  4   ASN   B ND2  1 
ATOM   3945 H  H    . ASN   B 1 4   ? 46.960 -15.505 -16.799 1.00 19.93 ?  4   ASN   B H    1 
ATOM   3946 H  HA   . ASN   B 1 4   ? 45.433 -16.960 -16.564 1.00 19.37 ?  4   ASN   B HA   1 
ATOM   3947 H  HB2  . ASN   B 1 4   ? 43.896 -15.044 -17.953 1.00 18.82 ?  4   ASN   B HB2  1 
ATOM   3948 H  HB3  . ASN   B 1 4   ? 43.259 -16.284 -17.188 1.00 18.82 ?  4   ASN   B HB3  1 
ATOM   3949 H  HD21 . ASN   B 1 4   ? 43.598 -13.055 -15.347 1.00 19.07 ?  4   ASN   B HD21 1 
ATOM   3950 H  HD22 . ASN   B 1 4   ? 43.450 -13.226 -16.819 1.00 19.07 ?  4   ASN   B HD22 1 
ATOM   3951 N  N    . SER   B 1 5   ? 46.402 -17.940 -18.925 1.00 17.43 ?  5   SER   B N    1 
ATOM   3952 C  CA   . SER   B 1 5   ? 46.493 -18.860 -20.060 1.00 19.89 ?  5   SER   B CA   1 
ATOM   3953 C  C    . SER   B 1 5   ? 46.492 -20.276 -19.501 1.00 21.42 ?  5   SER   B C    1 
ATOM   3954 O  O    . SER   B 1 5   ? 47.523 -20.937 -19.393 1.00 23.05 ?  5   SER   B O    1 
ATOM   3955 C  CB   . SER   B 1 5   ? 47.742 -18.571 -20.889 1.00 21.53 ?  5   SER   B CB   1 
ATOM   3956 O  OG   . SER   B 1 5   ? 48.916 -18.702 -20.107 1.00 24.56 ?  5   SER   B OG   1 
ATOM   3957 H  H    . SER   B 1 5   ? 47.157 -17.793 -18.541 1.00 21.03 ?  5   SER   B H    1 
ATOM   3958 H  HA   . SER   B 1 5   ? 45.716 -18.755 -20.628 1.00 23.98 ?  5   SER   B HA   1 
ATOM   3959 H  HB2  . SER   B 1 5   ? 47.778 -19.197 -21.632 1.00 25.95 ?  5   SER   B HB2  1 
ATOM   3960 H  HB3  . SER   B 1 5   ? 47.681 -17.664 -21.228 1.00 25.95 ?  5   SER   B HB3  1 
ATOM   3961 H  HG   . SER   B 1 5   ? 48.987 -19.491 -19.830 1.00 29.58 ?  5   SER   B HG   1 
ATOM   3962 N  N    . PHE   B 1 6   ? 45.302 -20.729 -19.115 1.00 22.17 ?  6   PHE   B N    1 
ATOM   3963 C  CA   . PHE   B 1 6   ? 45.122 -22.068 -18.574 1.00 21.91 ?  6   PHE   B CA   1 
ATOM   3964 C  C    . PHE   B 1 6   ? 45.045 -23.062 -19.722 1.00 25.59 ?  6   PHE   B C    1 
ATOM   3965 O  O    . PHE   B 1 6   ? 44.343 -22.823 -20.708 1.00 27.35 ?  6   PHE   B O    1 
ATOM   3966 C  CB   . PHE   B 1 6   ? 43.838 -22.129 -17.748 1.00 19.93 ?  6   PHE   B CB   1 
ATOM   3967 C  CG   . PHE   B 1 6   ? 43.857 -21.256 -16.524 1.00 17.54 ?  6   PHE   B CG   1 
ATOM   3968 C  CD1  . PHE   B 1 6   ? 44.366 -21.731 -15.328 1.00 16.44 ?  6   PHE   B CD1  1 
ATOM   3969 C  CD2  . PHE   B 1 6   ? 43.366 -19.961 -16.573 1.00 16.81 ?  6   PHE   B CD2  1 
ATOM   3970 C  CE1  . PHE   B 1 6   ? 44.370 -20.933 -14.194 1.00 15.85 ?  6   PHE   B CE1  1 
ATOM   3971 C  CE2  . PHE   B 1 6   ? 43.379 -19.152 -15.451 1.00 17.30 ?  6   PHE   B CE2  1 
ATOM   3972 C  CZ   . PHE   B 1 6   ? 43.885 -19.631 -14.262 1.00 16.41 ?  6   PHE   B CZ   1 
ATOM   3973 H  H    . PHE   B 1 6   ? 44.572 -20.277 -19.165 1.00 26.72 ?  6   PHE   B H    1 
ATOM   3974 H  HA   . PHE   B 1 6   ? 45.872 -22.302 -18.008 1.00 26.41 ?  6   PHE   B HA   1 
ATOM   3975 H  HB2  . PHE   B 1 6   ? 43.094 -21.845 -18.302 1.00 24.04 ?  6   PHE   B HB2  1 
ATOM   3976 H  HB3  . PHE   B 1 6   ? 43.696 -23.045 -17.456 1.00 24.04 ?  6   PHE   B HB3  1 
ATOM   3977 H  HD1  . PHE   B 1 6   ? 44.700 -22.598 -15.279 1.00 19.85 ?  6   PHE   B HD1  1 
ATOM   3978 H  HD2  . PHE   B 1 6   ? 43.019 -19.636 -17.369 1.00 20.28 ?  6   PHE   B HD2  1 
ATOM   3979 H  HE1  . PHE   B 1 6   ? 44.724 -21.252 -13.394 1.00 19.14 ?  6   PHE   B HE1  1 
ATOM   3980 H  HE2  . PHE   B 1 6   ? 43.039 -18.288 -15.498 1.00 20.87 ?  6   PHE   B HE2  1 
ATOM   3981 H  HZ   . PHE   B 1 6   ? 43.891 -19.091 -13.504 1.00 19.81 ?  6   PHE   B HZ   1 
ATOM   3982 N  N    . SER   B 1 7   ? 45.781 -24.166 -19.602 1.00 26.99 ?  7   SER   B N    1 
ATOM   3983 C  CA   . SER   B 1 7   ? 45.854 -25.159 -20.664 1.00 30.33 ?  7   SER   B CA   1 
ATOM   3984 C  C    . SER   B 1 7   ? 45.776 -26.560 -20.075 1.00 29.26 ?  7   SER   B C    1 
ATOM   3985 O  O    . SER   B 1 7   ? 46.368 -26.840 -19.029 1.00 29.65 ?  7   SER   B O    1 
ATOM   3986 C  CB   . SER   B 1 7   ? 47.154 -25.008 -21.467 1.00 33.74 ?  7   SER   B CB   1 
ATOM   3987 O  OG   . SER   B 1 7   ? 47.128 -25.814 -22.632 1.00 36.08 ?  7   SER   B OG   1 
ATOM   3988 H  H    . SER   B 1 7   ? 46.261 -24.356 -18.911 1.00 32.50 ?  7   SER   B H    1 
ATOM   3989 H  HA   . SER   B 1 7   ? 45.108 -25.042 -21.268 1.00 36.51 ?  7   SER   B HA   1 
ATOM   3990 H  HB2  . SER   B 1 7   ? 47.258 -24.078 -21.728 1.00 40.61 ?  7   SER   B HB2  1 
ATOM   3991 H  HB3  . SER   B 1 7   ? 47.903 -25.280 -20.913 1.00 40.61 ?  7   SER   B HB3  1 
ATOM   3992 H  HG   . SER   B 1 7   ? 47.844 -25.720 -23.062 1.00 43.41 ?  7   SER   B HG   1 
ATOM   3993 N  N    . GLY   B 1 8   ? 45.042 -27.437 -20.757 1.00 28.08 ?  8   GLY   B N    1 
ATOM   3994 C  CA   . GLY   B 1 8   ? 44.987 -28.829 -20.371 1.00 27.13 ?  8   GLY   B CA   1 
ATOM   3995 C  C    . GLY   B 1 8   ? 44.045 -29.148 -19.241 1.00 25.48 ?  8   GLY   B C    1 
ATOM   3996 O  O    . GLY   B 1 8   ? 44.182 -30.211 -18.621 1.00 26.73 ?  8   GLY   B O    1 
ATOM   3997 H  H    . GLY   B 1 8   ? 44.575 -27.240 -21.450 1.00 33.82 ?  8   GLY   B H    1 
ATOM   3998 H  HA2  . GLY   B 1 8   ? 44.712 -29.354 -21.133 1.00 32.67 ?  8   GLY   B HA2  1 
ATOM   3999 H  HA3  . GLY   B 1 8   ? 45.871 -29.117 -20.103 1.00 32.67 ?  8   GLY   B HA3  1 
ATOM   4000 N  N    . TYR   B 1 9   ? 43.068 -28.287 -18.965 1.00 23.57 ?  9   TYR   B N    1 
ATOM   4001 C  CA   . TYR   B 1 9   ? 42.119 -28.562 -17.900 1.00 21.73 ?  9   TYR   B CA   1 
ATOM   4002 C  C    . TYR   B 1 9   ? 40.934 -29.357 -18.416 1.00 21.26 ?  9   TYR   B C    1 
ATOM   4003 O  O    . TYR   B 1 9   ? 40.521 -29.230 -19.572 1.00 22.75 ?  9   TYR   B O    1 
ATOM   4004 C  CB   . TYR   B 1 9   ? 41.616 -27.277 -17.251 1.00 20.88 ?  9   TYR   B CB   1 
ATOM   4005 C  CG   . TYR   B 1 9   ? 42.642 -26.654 -16.339 1.00 20.18 ?  9   TYR   B CG   1 
ATOM   4006 C  CD1  . TYR   B 1 9   ? 43.742 -25.983 -16.857 1.00 20.51 ?  9   TYR   B CD1  1 
ATOM   4007 C  CD2  . TYR   B 1 9   ? 42.526 -26.751 -14.962 1.00 19.30 ?  9   TYR   B CD2  1 
ATOM   4008 C  CE1  . TYR   B 1 9   ? 44.695 -25.424 -16.029 1.00 20.49 ?  9   TYR   B CE1  1 
ATOM   4009 C  CE2  . TYR   B 1 9   ? 43.474 -26.193 -14.122 1.00 19.75 ?  9   TYR   B CE2  1 
ATOM   4010 C  CZ   . TYR   B 1 9   ? 44.557 -25.526 -14.663 1.00 20.29 ?  9   TYR   B CZ   1 
ATOM   4011 O  OH   . TYR   B 1 9   ? 45.509 -24.975 -13.841 1.00 20.42 ?  9   TYR   B OH   1 
ATOM   4012 H  H    . TYR   B 1 9   ? 42.918 -27.551 -19.390 1.00 28.40 ?  9   TYR   B H    1 
ATOM   4013 H  HA   . TYR   B 1 9   ? 42.549 -29.089 -17.214 1.00 26.19 ?  9   TYR   B HA   1 
ATOM   4014 H  HB2  . TYR   B 1 9   ? 41.387 -26.629 -17.937 1.00 25.18 ?  9   TYR   B HB2  1 
ATOM   4015 H  HB3  . TYR   B 1 9   ? 40.838 -27.488 -16.717 1.00 25.18 ?  9   TYR   B HB3  1 
ATOM   4016 H  HD1  . TYR   B 1 9   ? 43.837 -25.914 -17.780 1.00 24.72 ?  9   TYR   B HD1  1 
ATOM   4017 H  HD2  . TYR   B 1 9   ? 41.793 -27.202 -14.596 1.00 23.28 ?  9   TYR   B HD2  1 
ATOM   4018 H  HE1  . TYR   B 1 9   ? 45.419 -24.980 -16.392 1.00 24.70 ?  9   TYR   B HE1  1 
ATOM   4019 H  HE2  . TYR   B 1 9   ? 43.372 -26.269 -13.199 1.00 23.81 ?  9   TYR   B HE2  1 
ATOM   4020 H  HH   . TYR   B 1 9   ? 46.096 -24.604 -14.301 1.00 24.62 ?  9   TYR   B HH   1 
ATOM   4021 N  N    . LEU   B 1 10  ? 40.400 -30.196 -17.535 1.00 19.68 ?  10  LEU   B N    1 
ATOM   4022 C  CA   . LEU   B 1 10  ? 39.193 -30.956 -17.802 1.00 19.59 ?  10  LEU   B CA   1 
ATOM   4023 C  C    . LEU   B 1 10  ? 38.008 -30.185 -17.239 1.00 19.06 ?  10  LEU   B C    1 
ATOM   4024 O  O    . LEU   B 1 10  ? 38.030 -29.764 -16.079 1.00 18.57 ?  10  LEU   B O    1 
ATOM   4025 C  CB   . LEU   B 1 10  ? 39.298 -32.323 -17.126 1.00 20.46 ?  10  LEU   B CB   1 
ATOM   4026 C  CG   . LEU   B 1 10  ? 38.156 -33.287 -17.433 1.00 21.95 ?  10  LEU   B CG   1 
ATOM   4027 C  CD1  . LEU   B 1 10  ? 38.252 -33.775 -18.873 1.00 23.14 ?  10  LEU   B CD1  1 
ATOM   4028 C  CD2  . LEU   B 1 10  ? 38.150 -34.453 -16.461 1.00 22.89 ?  10  LEU   B CD2  1 
ATOM   4029 H  H    . LEU   B 1 10  ? 40.722 -30.340 -16.748 1.00 23.73 ?  10  LEU   B H    1 
ATOM   4030 H  HA   . LEU   B 1 10  ? 39.071 -31.078 -18.754 1.00 23.63 ?  10  LEU   B HA   1 
ATOM   4031 H  HB2  . LEU   B 1 10  ? 40.123 -32.746 -17.415 1.00 24.67 ?  10  LEU   B HB2  1 
ATOM   4032 H  HB3  . LEU   B 1 10  ? 39.320 -32.194 -16.164 1.00 24.67 ?  10  LEU   B HB3  1 
ATOM   4033 H  HG   . LEU   B 1 10  ? 37.313 -32.817 -17.336 1.00 26.45 ?  10  LEU   B HG   1 
ATOM   4034 H  HD11 . LEU   B 1 10  ? 37.562 -34.438 -19.026 1.00 27.88 ?  10  LEU   B HD11 1 
ATOM   4035 H  HD12 . LEU   B 1 10  ? 38.122 -33.019 -19.470 1.00 27.88 ?  10  LEU   B HD12 1 
ATOM   4036 H  HD13 . LEU   B 1 10  ? 39.127 -34.164 -19.016 1.00 27.88 ?  10  LEU   B HD13 1 
ATOM   4037 H  HD21 . LEU   B 1 10  ? 37.415 -35.043 -16.686 1.00 27.59 ?  10  LEU   B HD21 1 
ATOM   4038 H  HD22 . LEU   B 1 10  ? 38.992 -34.923 -16.532 1.00 27.59 ?  10  LEU   B HD22 1 
ATOM   4039 H  HD23 . LEU   B 1 10  ? 38.035 -34.106 -15.562 1.00 27.59 ?  10  LEU   B HD23 1 
ATOM   4040 N  N    . LYS   B 1 11  ? 36.983 -30.001 -18.063 1.00 20.33 ?  11  LYS   B N    1 
ATOM   4041 C  CA   . LYS   B 1 11  ? 35.782 -29.290 -17.652 1.00 22.27 ?  11  LYS   B CA   1 
ATOM   4042 C  C    . LYS   B 1 11  ? 34.911 -30.216 -16.809 1.00 21.11 ?  11  LYS   B C    1 
ATOM   4043 O  O    . LYS   B 1 11  ? 34.536 -31.305 -17.260 1.00 22.60 ?  11  LYS   B O    1 
ATOM   4044 C  CB   . LYS   B 1 11  ? 35.030 -28.834 -18.903 1.00 26.13 ?  11  LYS   B CB   1 
ATOM   4045 C  CG   . LYS   B 1 11  ? 33.876 -27.882 -18.662 1.00 29.58 ?  11  LYS   B CG   1 
ATOM   4046 C  CD   . LYS   B 1 11  ? 33.132 -27.607 -19.964 1.00 32.20 ?  11  LYS   B CD   1 
ATOM   4047 C  CE   . LYS   B 1 11  ? 32.122 -26.483 -19.811 1.00 34.07 ?  11  LYS   B CE   1 
ATOM   4048 N  NZ   . LYS   B 1 11  ? 32.785 -25.164 -19.629 1.00 35.23 ?  11  LYS   B NZ   1 
ATOM   4049 H  H    . LYS   B 1 11  ? 36.952 -30.288 -18.876 1.00 24.52 ?  11  LYS   B H    1 
ATOM   4050 H  HA   . LYS   B 1 11  ? 36.020 -28.512 -17.126 1.00 26.84 ?  11  LYS   B HA   1 
ATOM   4051 H  HB2  . LYS   B 1 11  ? 35.658 -28.383 -19.491 1.00 31.47 ?  11  LYS   B HB2  1 
ATOM   4052 H  HB3  . LYS   B 1 11  ? 34.672 -29.615 -19.351 1.00 31.47 ?  11  LYS   B HB3  1 
ATOM   4053 H  HG2  . LYS   B 1 11  ? 33.255 -28.279 -18.033 1.00 35.61 ?  11  LYS   B HG2  1 
ATOM   4054 H  HG3  . LYS   B 1 11  ? 34.216 -27.041 -18.320 1.00 35.61 ?  11  LYS   B HG3  1 
ATOM   4055 H  HD2  . LYS   B 1 11  ? 33.771 -27.350 -20.649 1.00 38.75 ?  11  LYS   B HD2  1 
ATOM   4056 H  HD3  . LYS   B 1 11  ? 32.657 -28.409 -20.236 1.00 38.75 ?  11  LYS   B HD3  1 
ATOM   4057 H  HE2  . LYS   B 1 11  ? 31.570 -26.438 -20.608 1.00 41.00 ?  11  LYS   B HE2  1 
ATOM   4058 H  HE3  . LYS   B 1 11  ? 31.570 -26.659 -19.033 1.00 41.00 ?  11  LYS   B HE3  1 
ATOM   4059 H  HZ1  . LYS   B 1 11  ? 32.173 -24.522 -19.557 1.00 42.39 ?  11  LYS   B HZ1  1 
ATOM   4060 H  HZ2  . LYS   B 1 11  ? 33.284 -25.173 -18.893 1.00 42.39 ?  11  LYS   B HZ2  1 
ATOM   4061 H  HZ3  . LYS   B 1 11  ? 33.307 -24.988 -20.330 1.00 42.39 ?  11  LYS   B HZ3  1 
ATOM   4062 N  N    . LEU   B 1 12  ? 34.590 -29.790 -15.586 1.00 19.26 ?  12  LEU   B N    1 
ATOM   4063 C  CA   . LEU   B 1 12  ? 33.634 -30.497 -14.739 1.00 18.37 ?  12  LEU   B CA   1 
ATOM   4064 C  C    . LEU   B 1 12  ? 32.243 -29.889 -14.827 1.00 18.24 ?  12  LEU   B C    1 
ATOM   4065 O  O    . LEU   B 1 12  ? 31.257 -30.609 -14.997 1.00 18.49 ?  12  LEU   B O    1 
ATOM   4066 C  CB   . LEU   B 1 12  ? 34.100 -30.515 -13.277 1.00 17.60 ?  12  LEU   B CB   1 
ATOM   4067 C  CG   . LEU   B 1 12  ? 35.444 -31.193 -13.001 1.00 17.75 ?  12  LEU   B CG   1 
ATOM   4068 C  CD1  . LEU   B 1 12  ? 35.809 -31.135 -11.527 1.00 18.23 ?  12  LEU   B CD1  1 
ATOM   4069 C  CD2  . LEU   B 1 12  ? 35.434 -32.632 -13.492 1.00 18.41 ?  12  LEU   B CD2  1 
ATOM   4070 H  H    . LEU   B 1 12  ? 34.910 -29.078 -15.225 1.00 23.22 ?  12  LEU   B H    1 
ATOM   4071 H  HA   . LEU   B 1 12  ? 33.562 -31.414 -15.044 1.00 22.16 ?  12  LEU   B HA   1 
ATOM   4072 H  HB2  . LEU   B 1 12  ? 34.166 -29.598 -12.971 1.00 21.24 ?  12  LEU   B HB2  1 
ATOM   4073 H  HB3  . LEU   B 1 12  ? 33.427 -30.979 -12.752 1.00 21.24 ?  12  LEU   B HB3  1 
ATOM   4074 H  HG   . LEU   B 1 12  ? 36.131 -30.719 -13.492 1.00 21.41 ?  12  LEU   B HG   1 
ATOM   4075 H  HD11 . LEU   B 1 12  ? 36.670 -31.570 -11.398 1.00 21.99 ?  12  LEU   B HD11 1 
ATOM   4076 H  HD12 . LEU   B 1 12  ? 35.867 -30.207 -11.248 1.00 21.99 ?  12  LEU   B HD12 1 
ATOM   4077 H  HD13 . LEU   B 1 12  ? 35.129 -31.594 -11.010 1.00 21.99 ?  12  LEU   B HD13 1 
ATOM   4078 H  HD21 . LEU   B 1 12  ? 36.240 -33.073 -13.185 1.00 22.21 ?  12  LEU   B HD21 1 
ATOM   4079 H  HD22 . LEU   B 1 12  ? 34.652 -33.082 -13.135 1.00 22.21 ?  12  LEU   B HD22 1 
ATOM   4080 H  HD23 . LEU   B 1 12  ? 35.403 -32.634 -14.461 1.00 22.21 ?  12  LEU   B HD23 1 
ATOM   4081 N  N    . THR   B 1 13  ? 32.150 -28.571 -14.701 1.00 18.22 ?  13  THR   B N    1 
ATOM   4082 C  CA   . THR   B 1 13  ? 30.927 -27.820 -14.918 1.00 18.38 ?  13  THR   B CA   1 
ATOM   4083 C  C    . THR   B 1 13  ? 31.267 -26.629 -15.809 1.00 20.31 ?  13  THR   B C    1 
ATOM   4084 O  O    . THR   B 1 13  ? 32.415 -26.444 -16.229 1.00 21.39 ?  13  THR   B O    1 
ATOM   4085 C  CB   . THR   B 1 13  ? 30.324 -27.336 -13.594 1.00 17.93 ?  13  THR   B CB   1 
ATOM   4086 O  OG1  . THR   B 1 13  ? 31.163 -26.311 -13.048 1.00 17.40 ?  13  THR   B OG1  1 
ATOM   4087 C  CG2  . THR   B 1 13  ? 30.203 -28.487 -12.594 1.00 18.33 ?  13  THR   B CG2  1 
ATOM   4088 H  H    . THR   B 1 13  ? 32.811 -28.068 -14.474 1.00 21.98 ?  13  THR   B H    1 
ATOM   4089 H  HA   . THR   B 1 13  ? 30.270 -28.380 -15.362 1.00 22.17 ?  13  THR   B HA   1 
ATOM   4090 H  HB   . THR   B 1 13  ? 29.431 -26.975 -13.751 1.00 21.63 ?  13  THR   B HB   1 
ATOM   4091 H  HG1  . THR   B 1 13  ? 30.846 -25.546 -13.241 1.00 21.00 ?  13  THR   B HG1  1 
ATOM   4092 H  HG21 . THR   B 1 13  ? 29.692 -28.205 -11.818 1.00 22.11 ?  13  THR   B HG21 1 
ATOM   4093 H  HG22 . THR   B 1 13  ? 29.752 -29.239 -13.009 1.00 22.11 ?  13  THR   B HG22 1 
ATOM   4094 H  HG23 . THR   B 1 13  ? 31.085 -28.768 -12.306 1.00 22.11 ?  13  THR   B HG23 1 
ATOM   4095 N  N    A ASP   B 1 14  ? 30.257 -25.803 -16.084 0.64 21.25 ?  14  ASP   B N    1 
ATOM   4096 N  N    B ASP   B 1 14  ? 30.262 -25.790 -16.077 0.36 21.03 ?  14  ASP   B N    1 
ATOM   4097 C  CA   A ASP   B 1 14  ? 30.481 -24.647 -16.944 0.64 22.56 ?  14  ASP   B CA   1 
ATOM   4098 C  CA   B ASP   B 1 14  ? 30.475 -24.642 -16.952 0.36 21.76 ?  14  ASP   B CA   1 
ATOM   4099 C  C    A ASP   B 1 14  ? 31.590 -23.749 -16.409 0.64 20.85 ?  14  ASP   B C    1 
ATOM   4100 C  C    B ASP   B 1 14  ? 31.463 -23.634 -16.381 0.36 20.04 ?  14  ASP   B C    1 
ATOM   4101 O  O    A ASP   B 1 14  ? 32.284 -23.089 -17.193 0.64 22.07 ?  14  ASP   B O    1 
ATOM   4102 O  O    B ASP   B 1 14  ? 31.909 -22.744 -17.115 0.36 20.24 ?  14  ASP   B O    1 
ATOM   4103 C  CB   A ASP   B 1 14  ? 29.184 -23.856 -17.115 0.64 25.77 ?  14  ASP   B CB   1 
ATOM   4104 C  CB   B ASP   B 1 14  ? 29.155 -23.925 -17.233 0.36 24.26 ?  14  ASP   B CB   1 
ATOM   4105 C  CG   A ASP   B 1 14  ? 28.190 -24.543 -18.029 0.64 28.80 ?  14  ASP   B CG   1 
ATOM   4106 C  CG   B ASP   B 1 14  ? 28.300 -24.658 -18.250 0.36 26.43 ?  14  ASP   B CG   1 
ATOM   4107 O  OD1  A ASP   B 1 14  ? 28.538 -25.559 -18.674 0.64 29.85 ?  14  ASP   B OD1  1 
ATOM   4108 O  OD1  B ASP   B 1 14  ? 28.873 -25.324 -19.139 0.36 27.22 ?  14  ASP   B OD1  1 
ATOM   4109 O  OD2  A ASP   B 1 14  ? 27.040 -24.062 -18.093 0.64 30.16 -1 14  ASP   B OD2  1 
ATOM   4110 O  OD2  B ASP   B 1 14  ? 27.058 -24.576 -18.160 0.36 27.28 -1 14  ASP   B OD2  1 
ATOM   4111 H  H    A ASP   B 1 14  ? 29.454 -25.877 -15.781 0.64 25.62 ?  14  ASP   B H    1 
ATOM   4112 H  H    B ASP   B 1 14  ? 29.462 -25.861 -15.769 0.36 25.35 ?  14  ASP   B H    1 
ATOM   4113 H  HA   A ASP   B 1 14  ? 30.759 -24.952 -17.816 0.64 27.19 ?  14  ASP   B HA   1 
ATOM   4114 H  HA   B ASP   B 1 14  ? 30.824 -24.960 -17.799 0.36 26.23 ?  14  ASP   B HA   1 
ATOM   4115 H  HB2  A ASP   B 1 14  ? 28.746 -23.761 -16.257 0.64 31.03 ?  14  ASP   B HB2  1 
ATOM   4116 H  HB2  B ASP   B 1 14  ? 28.654 -23.853 -16.405 0.36 29.23 ?  14  ASP   B HB2  1 
ATOM   4117 H  HB3  A ASP   B 1 14  ? 29.384 -22.983 -17.487 0.64 31.03 ?  14  ASP   B HB3  1 
ATOM   4118 H  HB3  B ASP   B 1 14  ? 29.351 -23.032 -17.573 0.36 29.23 ?  14  ASP   B HB3  1 
ATOM   4119 N  N    . ASN   B 1 15  ? 31.789 -23.723 -15.089 1.00 18.51 ?  15  ASN   B N    1 
ATOM   4120 C  CA   . ASN   B 1 15  ? 32.746 -22.804 -14.482 1.00 16.46 ?  15  ASN   B CA   1 
ATOM   4121 C  C    . ASN   B 1 15  ? 33.838 -23.454 -13.642 1.00 15.13 ?  15  ASN   B C    1 
ATOM   4122 O  O    . ASN   B 1 15  ? 34.684 -22.723 -13.112 1.00 15.25 ?  15  ASN   B O    1 
ATOM   4123 C  CB   . ASN   B 1 15  ? 32.026 -21.750 -13.626 1.00 16.29 ?  15  ASN   B CB   1 
ATOM   4124 C  CG   . ASN   B 1 15  ? 31.410 -22.344 -12.381 1.00 15.89 ?  15  ASN   B CG   1 
ATOM   4125 O  OD1  . ASN   B 1 15  ? 30.465 -23.133 -12.464 1.00 17.43 ?  15  ASN   B OD1  1 
ATOM   4126 N  ND2  . ASN   B 1 15  ? 31.938 -21.992 -11.226 1.00 14.48 ?  15  ASN   B ND2  1 
ATOM   4127 H  H    A ASN   B 1 15  ? 31.383 -24.234 -14.525 0.64 22.32 ?  15  ASN   B H    1 
ATOM   4128 H  H    B ASN   B 1 15  ? 31.437 -24.283 -14.537 0.36 22.32 ?  15  ASN   B H    1 
ATOM   4129 H  HA   . ASN   B 1 15  ? 33.194 -22.321 -15.184 1.00 19.87 ?  15  ASN   B HA   1 
ATOM   4130 H  HB2  . ASN   B 1 15  ? 32.665 -21.068 -13.351 1.00 19.66 ?  15  ASN   B HB2  1 
ATOM   4131 H  HB3  . ASN   B 1 15  ? 31.316 -21.336 -14.149 1.00 19.66 ?  15  ASN   B HB3  1 
ATOM   4132 H  HD21 . ASN   B 1 15  ? 31.618 -22.296 -10.486 1.00 17.50 ?  15  ASN   B HD21 1 
ATOM   4133 H  HD22 . ASN   B 1 15  ? 32.608 -21.445 -11.203 1.00 17.50 ?  15  ASN   B HD22 1 
ATOM   4134 N  N    . VAL   B 1 16  ? 33.852 -24.777 -13.493 1.00 14.76 ?  16  VAL   B N    1 
ATOM   4135 C  CA   . VAL   B 1 16  ? 34.851 -25.464 -12.680 1.00 14.60 ?  16  VAL   B CA   1 
ATOM   4136 C  C    . VAL   B 1 16  ? 35.639 -26.406 -13.574 1.00 14.85 ?  16  VAL   B C    1 
ATOM   4137 O  O    . VAL   B 1 16  ? 35.059 -27.292 -14.224 1.00 15.59 ?  16  VAL   B O    1 
ATOM   4138 C  CB   . VAL   B 1 16  ? 34.221 -26.225 -11.504 1.00 15.06 ?  16  VAL   B CB   1 
ATOM   4139 C  CG1  . VAL   B 1 16  ? 35.301 -26.970 -10.714 1.00 14.63 ?  16  VAL   B CG1  1 
ATOM   4140 C  CG2  . VAL   B 1 16  ? 33.425 -25.276 -10.613 1.00 15.56 ?  16  VAL   B CG2  1 
ATOM   4141 H  H    . VAL   B 1 16  ? 33.271 -25.308 -13.852 1.00 17.83 ?  16  VAL   B H    1 
ATOM   4142 H  HA   . VAL   B 1 16  ? 35.462 -24.808 -12.315 1.00 17.63 ?  16  VAL   B HA   1 
ATOM   4143 H  HB   . VAL   B 1 16  ? 33.604 -26.888 -11.855 1.00 18.18 ?  16  VAL   B HB   1 
ATOM   4144 H  HG11 . VAL   B 1 16  ? 34.924 -27.265 -9.869  1.00 17.67 ?  16  VAL   B HG11 1 
ATOM   4145 H  HG12 . VAL   B 1 16  ? 35.600 -27.736 -11.226 1.00 17.67 ?  16  VAL   B HG12 1 
ATOM   4146 H  HG13 . VAL   B 1 16  ? 36.043 -26.368 -10.550 1.00 17.67 ?  16  VAL   B HG13 1 
ATOM   4147 H  HG21 . VAL   B 1 16  ? 33.085 -25.769 -9.849  1.00 18.78 ?  16  VAL   B HG21 1 
ATOM   4148 H  HG22 . VAL   B 1 16  ? 34.003 -24.560 -10.315 1.00 18.78 ?  16  VAL   B HG22 1 
ATOM   4149 H  HG23 . VAL   B 1 16  ? 32.683 -24.911 -11.124 1.00 18.78 ?  16  VAL   B HG23 1 
ATOM   4150 N  N    . TYR   B 1 17  ? 36.963 -26.237 -13.560 1.00 15.18 ?  17  TYR   B N    1 
ATOM   4151 C  CA   . TYR   B 1 17  ? 37.910 -26.987 -14.371 1.00 15.50 ?  17  TYR   B CA   1 
ATOM   4152 C  C    . TYR   B 1 17  ? 38.963 -27.598 -13.454 1.00 14.34 ?  17  TYR   B C    1 
ATOM   4153 O  O    . TYR   B 1 17  ? 39.246 -27.065 -12.379 1.00 14.69 ?  17  TYR   B O    1 
ATOM   4154 C  CB   . TYR   B 1 17  ? 38.613 -26.062 -15.376 1.00 18.07 ?  17  TYR   B CB   1 
ATOM   4155 C  CG   . TYR   B 1 17  ? 37.682 -25.292 -16.282 1.00 21.33 ?  17  TYR   B CG   1 
ATOM   4156 C  CD1  . TYR   B 1 17  ? 37.104 -24.097 -15.872 1.00 22.83 ?  17  TYR   B CD1  1 
ATOM   4157 C  CD2  . TYR   B 1 17  ? 37.388 -25.758 -17.555 1.00 23.19 ?  17  TYR   B CD2  1 
ATOM   4158 C  CE1  . TYR   B 1 17  ? 36.253 -23.390 -16.706 1.00 24.56 ?  17  TYR   B CE1  1 
ATOM   4159 C  CE2  . TYR   B 1 17  ? 36.542 -25.060 -18.395 1.00 24.68 ?  17  TYR   B CE2  1 
ATOM   4160 C  CZ   . TYR   B 1 17  ? 35.976 -23.879 -17.965 1.00 25.41 ?  17  TYR   B CZ   1 
ATOM   4161 O  OH   . TYR   B 1 17  ? 35.135 -23.184 -18.803 1.00 26.71 ?  17  TYR   B OH   1 
ATOM   4162 H  H    . TYR   B 1 17  ? 37.356 -25.650 -13.061 1.00 18.33 ?  17  TYR   B H    1 
ATOM   4163 H  HA   . TYR   B 1 17  ? 37.443 -27.694 -14.853 1.00 18.72 ?  17  TYR   B HA   1 
ATOM   4164 H  HB2  . TYR   B 1 17  ? 39.152 -25.422 -14.889 1.00 21.80 ?  17  TYR   B HB2  1 
ATOM   4165 H  HB3  . TYR   B 1 17  ? 39.175 -26.605 -15.944 1.00 21.80 ?  17  TYR   B HB3  1 
ATOM   4166 H  HD1  . TYR   B 1 17  ? 37.287 -23.765 -15.024 1.00 27.51 ?  17  TYR   B HD1  1 
ATOM   4167 H  HD2  . TYR   B 1 17  ? 37.763 -26.554 -17.850 1.00 27.95 ?  17  TYR   B HD2  1 
ATOM   4168 H  HE1  . TYR   B 1 17  ? 35.869 -22.590 -16.421 1.00 29.59 ?  17  TYR   B HE1  1 
ATOM   4169 H  HE2  . TYR   B 1 17  ? 36.350 -25.386 -19.247 1.00 29.73 ?  17  TYR   B HE2  1 
ATOM   4170 H  HH   . TYR   B 1 17  ? 35.051 -23.588 -19.535 1.00 32.16 ?  17  TYR   B HH   1 
ATOM   4171 N  N    . ILE   B 1 18  ? 39.569 -28.707 -13.882 1.00 14.38 ?  18  ILE   B N    1 
ATOM   4172 C  CA   . ILE   B 1 18  ? 40.500 -29.427 -13.018 1.00 14.49 ?  18  ILE   B CA   1 
ATOM   4173 C  C    . ILE   B 1 18  ? 41.662 -29.980 -13.835 1.00 14.82 ?  18  ILE   B C    1 
ATOM   4174 O  O    . ILE   B 1 18  ? 41.502 -30.372 -14.995 1.00 16.43 ?  18  ILE   B O    1 
ATOM   4175 C  CB   . ILE   B 1 18  ? 39.755 -30.528 -12.217 1.00 15.10 ?  18  ILE   B CB   1 
ATOM   4176 C  CG1  . ILE   B 1 18  ? 40.624 -31.073 -11.078 1.00 15.51 ?  18  ILE   B CG1  1 
ATOM   4177 C  CG2  . ILE   B 1 18  ? 39.253 -31.647 -13.142 1.00 15.62 ?  18  ILE   B CG2  1 
ATOM   4178 C  CD1  . ILE   B 1 18  ? 39.830 -31.887 -10.061 1.00 16.81 ?  18  ILE   B CD1  1 
ATOM   4179 H  H    . ILE   B 1 18  ? 39.455 -29.059 -14.656 1.00 17.37 ?  18  ILE   B H    1 
ATOM   4180 H  HA   . ILE   B 1 18  ? 40.859 -28.808 -12.368 1.00 17.51 ?  18  ILE   B HA   1 
ATOM   4181 H  HB   . ILE   B 1 18  ? 38.973 -30.126 -11.808 1.00 18.23 ?  18  ILE   B HB   1 
ATOM   4182 H  HG12 . ILE   B 1 18  ? 41.310 -31.645 -11.448 1.00 18.72 ?  18  ILE   B HG12 1 
ATOM   4183 H  HG13 . ILE   B 1 18  ? 41.027 -30.325 -10.609 1.00 18.72 ?  18  ILE   B HG13 1 
ATOM   4184 H  HG21 . ILE   B 1 18  ? 38.668 -32.237 -12.638 1.00 18.86 ?  18  ILE   B HG21 1 
ATOM   4185 H  HG22 . ILE   B 1 18  ? 38.759 -31.245 -13.874 1.00 18.86 ?  18  ILE   B HG22 1 
ATOM   4186 H  HG23 . ILE   B 1 18  ? 40.010 -32.142 -13.482 1.00 18.86 ?  18  ILE   B HG23 1 
ATOM   4187 H  HD11 . ILE   B 1 18  ? 40.425 -32.164 -9.346  1.00 20.29 ?  18  ILE   B HD11 1 
ATOM   4188 H  HD12 . ILE   B 1 18  ? 39.116 -31.337 -9.702  1.00 20.29 ?  18  ILE   B HD12 1 
ATOM   4189 H  HD13 . ILE   B 1 18  ? 39.458 -32.666 -10.501 1.00 20.29 ?  18  ILE   B HD13 1 
ATOM   4190 N  N    . LYS   B 1 19  ? 42.839 -30.022 -13.207 1.00 15.46 ?  19  LYS   B N    1 
ATOM   4191 C  CA   . LYS   B 1 19  ? 44.052 -30.484 -13.864 1.00 16.25 ?  19  LYS   B CA   1 
ATOM   4192 C  C    . LYS   B 1 19  ? 44.956 -31.164 -12.847 1.00 16.09 ?  19  LYS   B C    1 
ATOM   4193 O  O    . LYS   B 1 19  ? 45.041 -30.740 -11.694 1.00 15.40 ?  19  LYS   B O    1 
ATOM   4194 C  CB   . LYS   B 1 19  ? 44.812 -29.312 -14.496 1.00 17.81 ?  19  LYS   B CB   1 
ATOM   4195 C  CG   . LYS   B 1 19  ? 45.992 -29.720 -15.363 1.00 19.55 ?  19  LYS   B CG   1 
ATOM   4196 C  CD   . LYS   B 1 19  ? 46.732 -28.495 -15.885 1.00 21.56 ?  19  LYS   B CD   1 
ATOM   4197 C  CE   . LYS   B 1 19  ? 47.884 -28.881 -16.793 1.00 23.25 ?  19  LYS   B CE   1 
ATOM   4198 N  NZ   . LYS   B 1 19  ? 48.660 -27.697 -17.248 1.00 24.34 ?  19  LYS   B NZ   1 
ATOM   4199 H  H    . LYS   B 1 19  ? 42.947 -29.782 -12.384 1.00 18.67 ?  19  LYS   B H    1 
ATOM   4200 H  HA   . LYS   B 1 19  ? 43.816 -31.118 -14.556 1.00 19.62 ?  19  LYS   B HA   1 
ATOM   4201 H  HB2  . LYS   B 1 19  ? 44.196 -28.814 -15.055 1.00 21.49 ?  19  LYS   B HB2  1 
ATOM   4202 H  HB3  . LYS   B 1 19  ? 45.143 -28.738 -13.784 1.00 21.49 ?  19  LYS   B HB3  1 
ATOM   4203 H  HG2  . LYS   B 1 19  ? 46.603 -30.254 -14.836 1.00 23.58 ?  19  LYS   B HG2  1 
ATOM   4204 H  HG3  . LYS   B 1 19  ? 45.661 -30.232 -16.120 1.00 23.58 ?  19  LYS   B HG3  1 
ATOM   4205 H  HD2  . LYS   B 1 19  ? 46.114 -27.940 -16.390 1.00 25.98 ?  19  LYS   B HD2  1 
ATOM   4206 H  HD3  . LYS   B 1 19  ? 47.088 -27.995 -15.132 1.00 25.98 ?  19  LYS   B HD3  1 
ATOM   4207 H  HE2  . LYS   B 1 19  ? 48.482 -29.473 -16.310 1.00 28.02 ?  19  LYS   B HE2  1 
ATOM   4208 H  HE3  . LYS   B 1 19  ? 47.530 -29.335 -17.576 1.00 28.02 ?  19  LYS   B HE3  1 
ATOM   4209 H  HZ1  . LYS   B 1 19  ? 49.302 -27.952 -17.808 1.00 29.32 ?  19  LYS   B HZ1  1 
ATOM   4210 H  HZ2  . LYS   B 1 19  ? 48.122 -27.123 -17.666 1.00 29.32 ?  19  LYS   B HZ2  1 
ATOM   4211 H  HZ3  . LYS   B 1 19  ? 49.030 -27.290 -16.549 1.00 29.32 ?  19  LYS   B HZ3  1 
ATOM   4212 N  N    . ASN   B 1 20  ? 45.636 -32.216 -13.284 1.00 17.35 ?  20  ASN   B N    1 
ATOM   4213 C  CA   . ASN   B 1 20  ? 46.665 -32.854 -12.468 1.00 18.32 ?  20  ASN   B CA   1 
ATOM   4214 C  C    . ASN   B 1 20  ? 47.943 -32.040 -12.646 1.00 18.75 ?  20  ASN   B C    1 
ATOM   4215 O  O    . ASN   B 1 20  ? 48.608 -32.131 -13.683 1.00 20.77 ?  20  ASN   B O    1 
ATOM   4216 C  CB   . ASN   B 1 20  ? 46.837 -34.306 -12.911 1.00 19.95 ?  20  ASN   B CB   1 
ATOM   4217 C  CG   . ASN   B 1 20  ? 47.990 -35.017 -12.220 1.00 21.54 ?  20  ASN   B CG   1 
ATOM   4218 O  OD1  . ASN   B 1 20  ? 48.641 -35.883 -12.818 1.00 23.93 ?  20  ASN   B OD1  1 
ATOM   4219 N  ND2  . ASN   B 1 20  ? 48.235 -34.685 -10.961 1.00 21.19 ?  20  ASN   B ND2  1 
ATOM   4220 H  H    . ASN   B 1 20  ? 45.522 -32.577 -14.055 1.00 20.93 ?  20  ASN   B H    1 
ATOM   4221 H  HA   . ASN   B 1 20  ? 46.389 -32.836 -11.535 1.00 22.10 ?  20  ASN   B HA   1 
ATOM   4222 H  HB2  . ASN   B 1 20  ? 46.019 -34.792 -12.708 1.00 24.05 ?  20  ASN   B HB2  1 
ATOM   4223 H  HB3  . ASN   B 1 20  ? 46.999 -34.320 -13.864 1.00 24.05 ?  20  ASN   B HB3  1 
ATOM   4224 H  HD21 . ASN   B 1 20  ? 48.880 -35.056 -10.536 1.00 25.55 ?  20  ASN   B HD21 1 
ATOM   4225 H  HD22 . ASN   B 1 20  ? 47.757 -34.080 -10.567 1.00 25.55 ?  20  ASN   B HD22 1 
ATOM   4226 N  N    . ALA   B 1 21  ? 48.288 -31.227 -11.643 1.00 18.25 ?  21  ALA   B N    1 
ATOM   4227 C  CA   . ALA   B 1 21  ? 49.411 -30.314 -11.793 1.00 19.06 ?  21  ALA   B CA   1 
ATOM   4228 C  C    . ALA   B 1 21  ? 49.880 -29.817 -10.435 1.00 17.77 ?  21  ALA   B C    1 
ATOM   4229 O  O    . ALA   B 1 21  ? 49.141 -29.846 -9.445  1.00 17.69 ?  21  ALA   B O    1 
ATOM   4230 C  CB   . ALA   B 1 21  ? 49.041 -29.130 -12.684 1.00 20.38 ?  21  ALA   B CB   1 
ATOM   4231 H  H    . ALA   B 1 21  ? 47.887 -31.190 -10.874 1.00 22.02 ?  21  ALA   B H    1 
ATOM   4232 H  HA   . ALA   B 1 21  ? 50.144 -30.794 -12.205 1.00 22.98 ?  21  ALA   B HA   1 
ATOM   4233 H  HB1  . ALA   B 1 21  ? 49.834 -28.596 -12.820 1.00 24.57 ?  21  ALA   B HB1  1 
ATOM   4234 H  HB2  . ALA   B 1 21  ? 48.717 -29.473 -13.528 1.00 24.57 ?  21  ALA   B HB2  1 
ATOM   4235 H  HB3  . ALA   B 1 21  ? 48.351 -28.612 -12.244 1.00 24.57 ?  21  ALA   B HB3  1 
ATOM   4236 N  N    . ASP   B 1 22  ? 51.137 -29.368 -10.421 1.00 17.10 ?  22  ASP   B N    1 
ATOM   4237 C  CA   . ASP   B 1 22  ? 51.749 -28.669 -9.297  1.00 16.35 ?  22  ASP   B CA   1 
ATOM   4238 C  C    . ASP   B 1 22  ? 51.339 -27.200 -9.381  1.00 14.76 ?  22  ASP   B C    1 
ATOM   4239 O  O    . ASP   B 1 22  ? 51.648 -26.527 -10.368 1.00 15.23 ?  22  ASP   B O    1 
ATOM   4240 C  CB   . ASP   B 1 22  ? 53.268 -28.845 -9.453  1.00 17.46 ?  22  ASP   B CB   1 
ATOM   4241 C  CG   . ASP   B 1 22  ? 54.094 -28.085 -8.421  1.00 19.25 ?  22  ASP   B CG   1 
ATOM   4242 O  OD1  . ASP   B 1 22  ? 53.729 -26.969 -8.022  1.00 19.19 ?  22  ASP   B OD1  1 
ATOM   4243 O  OD2  . ASP   B 1 22  ? 55.165 -28.601 -8.035  1.00 21.58 -1 22  ASP   B OD2  1 
ATOM   4244 H  H    . ASP   B 1 22  ? 51.676 -29.462 -11.087 1.00 20.63 ?  22  ASP   B H    1 
ATOM   4245 H  HA   . ASP   B 1 22  ? 51.461 -29.051 -8.453  1.00 19.73 ?  22  ASP   B HA   1 
ATOM   4246 H  HB2  . ASP   B 1 22  ? 53.490 -29.782 -9.373  1.00 21.07 ?  22  ASP   B HB2  1 
ATOM   4247 H  HB3  . ASP   B 1 22  ? 53.534 -28.513 -10.326 1.00 21.07 ?  22  ASP   B HB3  1 
ATOM   4248 N  N    . ILE   B 1 23  ? 50.625 -26.708 -8.360  1.00 14.02 ?  23  ILE   B N    1 
ATOM   4249 C  CA   . ILE   B 1 23  ? 50.036 -25.365 -8.424  1.00 13.27 ?  23  ILE   B CA   1 
ATOM   4250 C  C    . ILE   B 1 23  ? 51.094 -24.278 -8.565  1.00 13.02 ?  23  ILE   B C    1 
ATOM   4251 O  O    . ILE   B 1 23  ? 50.833 -23.239 -9.180  1.00 12.67 ?  23  ILE   B O    1 
ATOM   4252 C  CB   . ILE   B 1 23  ? 49.099 -25.115 -7.225  1.00 13.68 ?  23  ILE   B CB   1 
ATOM   4253 C  CG1  . ILE   B 1 23  ? 48.272 -23.847 -7.438  1.00 14.57 ?  23  ILE   B CG1  1 
ATOM   4254 C  CG2  . ILE   B 1 23  ? 49.865 -25.075 -5.919  1.00 14.74 ?  23  ILE   B CG2  1 
ATOM   4255 C  CD1  . ILE   B 1 23  ? 47.130 -23.675 -6.441  1.00 14.96 ?  23  ILE   B CD1  1 
ATOM   4256 H  H    . ILE   B 1 23  ? 50.468 -27.132 -7.630  1.00 16.94 ?  23  ILE   B H    1 
ATOM   4257 H  HA   . ILE   B 1 23  ? 49.489 -25.324 -9.220  1.00 16.04 ?  23  ILE   B HA   1 
ATOM   4258 H  HB   . ILE   B 1 23  ? 48.478 -25.861 -7.180  1.00 16.53 ?  23  ILE   B HB   1 
ATOM   4259 H  HG12 . ILE   B 1 23  ? 48.858 -23.075 -7.351  1.00 17.60 ?  23  ILE   B HG12 1 
ATOM   4260 H  HG13 . ILE   B 1 23  ? 47.891 -23.864 -8.331  1.00 17.60 ?  23  ILE   B HG13 1 
ATOM   4261 H  HG21 . ILE   B 1 23  ? 49.234 -25.059 -5.183  1.00 17.80 ?  23  ILE   B HG21 1 
ATOM   4262 H  HG22 . ILE   B 1 23  ? 50.425 -25.865 -5.858  1.00 17.80 ?  23  ILE   B HG22 1 
ATOM   4263 H  HG23 . ILE   B 1 23  ? 50.416 -24.277 -5.902  1.00 17.80 ?  23  ILE   B HG23 1 
ATOM   4264 H  HD11 . ILE   B 1 23  ? 46.620 -22.888 -6.678  1.00 18.07 ?  23  ILE   B HD11 1 
ATOM   4265 H  HD12 . ILE   B 1 23  ? 46.561 -24.463 -6.485  1.00 18.07 ?  23  ILE   B HD12 1 
ATOM   4266 H  HD13 . ILE   B 1 23  ? 47.499 -23.584 -5.552  1.00 18.07 ?  23  ILE   B HD13 1 
ATOM   4267 N  N    . VAL   B 1 24  ? 52.289 -24.483 -8.002  1.00 13.28 ?  24  VAL   B N    1 
ATOM   4268 C  CA   . VAL   B 1 24  ? 53.365 -23.505 -8.170  1.00 13.82 ?  24  VAL   B CA   1 
ATOM   4269 C  C    . VAL   B 1 24  ? 53.822 -23.462 -9.622  1.00 14.03 ?  24  VAL   B C    1 
ATOM   4270 O  O    . VAL   B 1 24  ? 53.969 -22.385 -10.216 1.00 14.56 ?  24  VAL   B O    1 
ATOM   4271 C  CB   . VAL   B 1 24  ? 54.537 -23.815 -7.219  1.00 14.60 ?  24  VAL   B CB   1 
ATOM   4272 C  CG1  . VAL   B 1 24  ? 55.747 -22.944 -7.553  1.00 15.36 ?  24  VAL   B CG1  1 
ATOM   4273 C  CG2  . VAL   B 1 24  ? 54.117 -23.612 -5.781  1.00 15.65 ?  24  VAL   B CG2  1 
ATOM   4274 H  H    . VAL   B 1 24  ? 52.499 -25.168 -7.523  1.00 16.06 ?  24  VAL   B H    1 
ATOM   4275 H  HA   . VAL   B 1 24  ? 53.028 -22.629 -7.938  1.00 16.69 ?  24  VAL   B HA   1 
ATOM   4276 H  HB   . VAL   B 1 24  ? 54.800 -24.746 -7.322  1.00 17.64 ?  24  VAL   B HB   1 
ATOM   4277 H  HG11 . VAL   B 1 24  ? 56.344 -22.933 -6.790  1.00 18.55 ?  24  VAL   B HG11 1 
ATOM   4278 H  HG12 . VAL   B 1 24  ? 56.200 -23.318 -8.323  1.00 18.55 ?  24  VAL   B HG12 1 
ATOM   4279 H  HG13 . VAL   B 1 24  ? 55.438 -22.046 -7.746  1.00 18.55 ?  24  VAL   B HG13 1 
ATOM   4280 H  HG21 . VAL   B 1 24  ? 54.841 -23.875 -5.194  1.00 18.90 ?  24  VAL   B HG21 1 
ATOM   4281 H  HG22 . VAL   B 1 24  ? 53.906 -22.673 -5.645  1.00 18.90 ?  24  VAL   B HG22 1 
ATOM   4282 H  HG23 . VAL   B 1 24  ? 53.331 -24.154 -5.600  1.00 18.90 ?  24  VAL   B HG23 1 
ATOM   4283 N  N    . GLU   B 1 25  ? 54.084 -24.635 -10.208 1.00 15.14 ?  25  GLU   B N    1 
ATOM   4284 C  CA   . GLU   B 1 25  ? 54.477 -24.667 -11.611 1.00 16.82 ?  25  GLU   B CA   1 
ATOM   4285 C  C    . GLU   B 1 25  ? 53.368 -24.126 -12.498 1.00 15.33 ?  25  GLU   B C    1 
ATOM   4286 O  O    . GLU   B 1 25  ? 53.633 -23.409 -13.471 1.00 16.25 ?  25  GLU   B O    1 
ATOM   4287 C  CB   . GLU   B 1 25  ? 54.875 -26.084 -12.018 1.00 21.10 ?  25  GLU   B CB   1 
ATOM   4288 C  CG   . GLU   B 1 25  ? 56.175 -26.532 -11.371 1.00 26.28 ?  25  GLU   B CG   1 
ATOM   4289 C  CD   . GLU   B 1 25  ? 57.284 -25.492 -11.467 1.00 30.90 ?  25  GLU   B CD   1 
ATOM   4290 O  OE1  . GLU   B 1 25  ? 57.680 -25.141 -12.600 1.00 32.41 ?  25  GLU   B OE1  1 
ATOM   4291 O  OE2  . GLU   B 1 25  ? 57.748 -25.008 -10.409 1.00 32.28 -1 25  GLU   B OE2  1 
ATOM   4292 H  H    . GLU   B 1 25  ? 54.041 -25.403 -9.823  1.00 18.29 ?  25  GLU   B H    1 
ATOM   4293 H  HA   . GLU   B 1 25  ? 55.233 -24.077 -11.734 1.00 20.31 ?  25  GLU   B HA   1 
ATOM   4294 H  HB2  . GLU   B 1 25  ? 54.175 -26.700 -11.743 1.00 25.44 ?  25  GLU   B HB2  1 
ATOM   4295 H  HB3  . GLU   B 1 25  ? 54.985 -26.117 -12.981 1.00 25.44 ?  25  GLU   B HB3  1 
ATOM   4296 H  HG2  . GLU   B 1 25  ? 56.019 -26.693 -10.434 1.00 31.65 ?  25  GLU   B HG2  1 
ATOM   4297 H  HG3  . GLU   B 1 25  ? 56.481 -27.336 -11.813 1.00 31.65 ?  25  GLU   B HG3  1 
ATOM   4298 N  N    . GLU   B 1 26  ? 52.116 -24.448 -12.168 1.00 14.42 ?  26  GLU   B N    1 
ATOM   4299 C  CA   . GLU   B 1 26  ? 50.990 -23.925 -12.933 1.00 15.11 ?  26  GLU   B CA   1 
ATOM   4300 C  C    . GLU   B 1 26  ? 50.943 -22.406 -12.859 1.00 14.24 ?  26  GLU   B C    1 
ATOM   4301 O  O    . GLU   B 1 26  ? 50.754 -21.732 -13.876 1.00 15.37 ?  26  GLU   B O    1 
ATOM   4302 C  CB   . GLU   B 1 26  ? 49.677 -24.509 -12.410 1.00 16.85 ?  26  GLU   B CB   1 
ATOM   4303 C  CG   . GLU   B 1 26  ? 49.223 -25.779 -13.101 1.00 20.52 ?  26  GLU   B CG   1 
ATOM   4304 C  CD   . GLU   B 1 26  ? 48.983 -25.612 -14.602 1.00 22.40 ?  26  GLU   B CD   1 
ATOM   4305 O  OE1  . GLU   B 1 26  ? 48.005 -24.956 -15.021 1.00 22.95 ?  26  GLU   B OE1  1 
ATOM   4306 O  OE2  . GLU   B 1 26  ? 49.776 -26.174 -15.367 1.00 24.60 -1 26  GLU   B OE2  1 
ATOM   4307 H  H    . GLU   B 1 26  ? 51.893 -24.969 -11.517 1.00 17.43 ?  26  GLU   B H    1 
ATOM   4308 H  HA   . GLU   B 1 26  ? 51.089 -24.179 -13.862 1.00 18.25 ?  26  GLU   B HA   1 
ATOM   4309 H  HB2  . GLU   B 1 26  ? 49.781 -24.709 -11.464 1.00 20.34 ?  26  GLU   B HB2  1 
ATOM   4310 H  HB3  . GLU   B 1 26  ? 48.976 -23.844 -12.521 1.00 20.34 ?  26  GLU   B HB3  1 
ATOM   4311 H  HG2  . GLU   B 1 26  ? 49.914 -26.442 -13.000 1.00 24.75 ?  26  GLU   B HG2  1 
ATOM   4312 H  HG3  . GLU   B 1 26  ? 48.399 -26.081 -12.686 1.00 24.75 ?  26  GLU   B HG3  1 
ATOM   4313 N  N    . ALA   B 1 27  ? 51.091 -21.850 -11.655 1.00 13.32 ?  27  ALA   B N    1 
ATOM   4314 C  CA   . ALA   B 1 27  ? 51.052 -20.400 -11.513 1.00 13.85 ?  27  ALA   B CA   1 
ATOM   4315 C  C    . ALA   B 1 27  ? 52.124 -19.739 -12.370 1.00 14.82 ?  27  ALA   B C    1 
ATOM   4316 O  O    . ALA   B 1 27  ? 51.863 -18.734 -13.045 1.00 15.55 ?  27  ALA   B O    1 
ATOM   4317 C  CB   . ALA   B 1 27  ? 51.198 -20.012 -10.041 1.00 13.62 ?  27  ALA   B CB   1 
ATOM   4318 H  H    . ALA   B 1 27  ? 51.206 -22.286 -10.918 1.00 16.09 ?  27  ALA   B H    1 
ATOM   4319 H  HA   . ALA   B 1 27  ? 50.193 -20.080 -11.816 1.00 16.73 ?  27  ALA   B HA   1 
ATOM   4320 H  HB1  . ALA   B 1 27  ? 51.162 -19.045 -9.964  1.00 16.46 ?  27  ALA   B HB1  1 
ATOM   4321 H  HB2  . ALA   B 1 27  ? 50.464 -20.406 -9.536  1.00 16.46 ?  27  ALA   B HB2  1 
ATOM   4322 H  HB3  . ALA   B 1 27  ? 52.043 -20.341 -9.703  1.00 16.46 ?  27  ALA   B HB3  1 
ATOM   4323 N  N    . LYS   B 1 28  ? 53.336 -20.298 -12.370 1.00 16.07 ?  28  LYS   B N    1 
ATOM   4324 C  CA   . LYS   B 1 28  ? 54.415 -19.687 -13.138 1.00 18.17 ?  28  LYS   B CA   1 
ATOM   4325 C  C    . LYS   B 1 28  ? 54.160 -19.765 -14.638 1.00 18.96 ?  28  LYS   B C    1 
ATOM   4326 O  O    . LYS   B 1 28  ? 54.571 -18.865 -15.381 1.00 20.12 ?  28  LYS   B O    1 
ATOM   4327 C  CB   . LYS   B 1 28  ? 55.763 -20.300 -12.746 1.00 20.70 ?  28  LYS   B CB   1 
ATOM   4328 C  CG   . LYS   B 1 28  ? 56.167 -19.942 -11.318 1.00 24.55 ?  28  LYS   B CG   1 
ATOM   4329 C  CD   . LYS   B 1 28  ? 57.594 -20.346 -10.973 1.00 28.47 ?  28  LYS   B CD   1 
ATOM   4330 C  CE   . LYS   B 1 28  ? 57.710 -21.827 -10.701 1.00 31.11 ?  28  LYS   B CE   1 
ATOM   4331 N  NZ   . LYS   B 1 28  ? 59.069 -22.179 -10.201 1.00 34.15 ?  28  LYS   B NZ   1 
ATOM   4332 H  H    . LYS   B 1 28  ? 53.553 -21.016 -11.945 1.00 19.40 ?  28  LYS   B H    1 
ATOM   4333 H  HA   . LYS   B 1 28  ? 54.456 -18.749 -12.911 1.00 21.92 ?  28  LYS   B HA   1 
ATOM   4334 H  HB2  . LYS   B 1 28  ? 55.709 -21.266 -12.807 1.00 24.96 ?  28  LYS   B HB2  1 
ATOM   4335 H  HB3  . LYS   B 1 28  ? 56.453 -19.967 -13.344 1.00 24.96 ?  28  LYS   B HB3  1 
ATOM   4336 H  HG2  . LYS   B 1 28  ? 56.090 -18.980 -11.207 1.00 29.57 ?  28  LYS   B HG2  1 
ATOM   4337 H  HG3  . LYS   B 1 28  ? 55.569 -20.393 -10.704 1.00 29.57 ?  28  LYS   B HG3  1 
ATOM   4338 H  HD2  . LYS   B 1 28  ? 58.175 -20.124 -11.718 1.00 34.28 ?  28  LYS   B HD2  1 
ATOM   4339 H  HD3  . LYS   B 1 28  ? 57.873 -19.865 -10.178 1.00 34.28 ?  28  LYS   B HD3  1 
ATOM   4340 H  HE2  . LYS   B 1 28  ? 57.061 -22.080 -10.026 1.00 37.45 ?  28  LYS   B HE2  1 
ATOM   4341 H  HE3  . LYS   B 1 28  ? 57.550 -22.317 -11.522 1.00 37.45 ?  28  LYS   B HE3  1 
ATOM   4342 H  HZ1  . LYS   B 1 28  ? 59.119 -23.053 -10.046 1.00 41.10 ?  28  LYS   B HZ1  1 
ATOM   4343 H  HZ2  . LYS   B 1 28  ? 59.682 -21.956 -10.806 1.00 41.10 ?  28  LYS   B HZ2  1 
ATOM   4344 H  HZ3  . LYS   B 1 28  ? 59.237 -21.740 -9.445  1.00 41.10 ?  28  LYS   B HZ3  1 
ATOM   4345 N  N    . LYS   B 1 29  ? 53.449 -20.796 -15.096 1.00 20.13 ?  29  LYS   B N    1 
ATOM   4346 C  CA   . LYS   B 1 29  ? 53.159 -20.956 -16.517 1.00 23.04 ?  29  LYS   B CA   1 
ATOM   4347 C  C    . LYS   B 1 29  ? 51.908 -20.202 -16.960 1.00 21.88 ?  29  LYS   B C    1 
ATOM   4348 O  O    . LYS   B 1 29  ? 51.910 -19.583 -18.029 1.00 23.25 ?  29  LYS   B O    1 
ATOM   4349 C  CB   . LYS   B 1 29  ? 53.013 -22.441 -16.857 1.00 27.77 ?  29  LYS   B CB   1 
ATOM   4350 C  CG   . LYS   B 1 29  ? 52.940 -22.728 -18.347 1.00 32.19 ?  29  LYS   B CG   1 
ATOM   4351 C  CD   . LYS   B 1 29  ? 53.156 -24.206 -18.642 1.00 36.07 ?  29  LYS   B CD   1 
ATOM   4352 C  CE   . LYS   B 1 29  ? 51.996 -25.056 -18.152 1.00 38.30 ?  29  LYS   B CE   1 
ATOM   4353 N  NZ   . LYS   B 1 29  ? 52.227 -26.507 -18.405 1.00 39.57 ?  29  LYS   B NZ   1 
ATOM   4354 H  H    . LYS   B 1 29  ? 53.123 -21.422 -14.599 1.00 24.27 ?  29  LYS   B H    1 
ATOM   4355 H  HA   . LYS   B 1 29  ? 53.902 -20.609 -17.028 1.00 27.76 ?  29  LYS   B HA   1 
ATOM   4356 H  HB2  . LYS   B 1 29  ? 53.781 -22.917 -16.502 1.00 33.44 ?  29  LYS   B HB2  1 
ATOM   4357 H  HB3  . LYS   B 1 29  ? 52.201 -22.778 -16.451 1.00 33.44 ?  29  LYS   B HB3  1 
ATOM   4358 H  HG2  . LYS   B 1 29  ? 52.063 -22.476 -18.678 1.00 38.74 ?  29  LYS   B HG2  1 
ATOM   4359 H  HG3  . LYS   B 1 29  ? 53.629 -22.221 -18.805 1.00 38.74 ?  29  LYS   B HG3  1 
ATOM   4360 H  HD2  . LYS   B 1 29  ? 53.241 -24.331 -19.600 1.00 43.41 ?  29  LYS   B HD2  1 
ATOM   4361 H  HD3  . LYS   B 1 29  ? 53.963 -24.507 -18.193 1.00 43.41 ?  29  LYS   B HD3  1 
ATOM   4362 H  HE2  . LYS   B 1 29  ? 51.886 -24.929 -17.197 1.00 46.08 ?  29  LYS   B HE2  1 
ATOM   4363 H  HE3  . LYS   B 1 29  ? 51.187 -24.791 -18.619 1.00 46.08 ?  29  LYS   B HE3  1 
ATOM   4364 H  HZ1  . LYS   B 1 29  ? 51.534 -26.982 -18.110 1.00 47.59 ?  29  LYS   B HZ1  1 
ATOM   4365 H  HZ2  . LYS   B 1 29  ? 52.326 -26.653 -19.278 1.00 47.59 ?  29  LYS   B HZ2  1 
ATOM   4366 H  HZ3  . LYS   B 1 29  ? 52.963 -26.776 -17.982 1.00 47.59 ?  29  LYS   B HZ3  1 
ATOM   4367 N  N    . VAL   B 1 30  ? 50.837 -20.258 -16.163 1.00 19.96 ?  30  VAL   B N    1 
ATOM   4368 C  CA   . VAL   B 1 30  ? 49.552 -19.655 -16.529 1.00 19.90 ?  30  VAL   B CA   1 
ATOM   4369 C  C    . VAL   B 1 30  ? 49.566 -18.142 -16.369 1.00 18.67 ?  30  VAL   B C    1 
ATOM   4370 O  O    . VAL   B 1 30  ? 48.829 -17.425 -17.069 1.00 19.53 ?  30  VAL   B O    1 
ATOM   4371 C  CB   . VAL   B 1 30  ? 48.454 -20.261 -15.631 1.00 21.00 ?  30  VAL   B CB   1 
ATOM   4372 C  CG1  . VAL   B 1 30  ? 47.170 -19.446 -15.702 1.00 21.70 ?  30  VAL   B CG1  1 
ATOM   4373 C  CG2  . VAL   B 1 30  ? 48.199 -21.717 -15.999 1.00 21.70 ?  30  VAL   B CG2  1 
ATOM   4374 H  H    . VAL   B 1 30  ? 50.819 -20.669 -15.399 1.00 24.06 ?  30  VAL   B H    1 
ATOM   4375 H  HA   . VAL   B 1 30  ? 49.340 -19.882 -17.450 1.00 24.00 ?  30  VAL   B HA   1 
ATOM   4376 H  HB   . VAL   B 1 30  ? 48.758 -20.249 -14.709 1.00 25.32 ?  30  VAL   B HB   1 
ATOM   4377 H  HG11 . VAL   B 1 30  ? 46.427 -20.023 -15.462 1.00 26.15 ?  30  VAL   B HG11 1 
ATOM   4378 H  HG12 . VAL   B 1 30  ? 47.225 -18.709 -15.077 1.00 26.15 ?  30  VAL   B HG12 1 
ATOM   4379 H  HG13 . VAL   B 1 30  ? 47.048 -19.124 -16.603 1.00 26.15 ?  30  VAL   B HG13 1 
ATOM   4380 H  HG21 . VAL   B 1 30  ? 47.508 -22.079 -15.415 1.00 26.16 ?  30  VAL   B HG21 1 
ATOM   4381 H  HG22 . VAL   B 1 30  ? 47.898 -21.763 -16.922 1.00 26.16 ?  30  VAL   B HG22 1 
ATOM   4382 H  HG23 . VAL   B 1 30  ? 49.017 -22.222 -15.891 1.00 26.16 ?  30  VAL   B HG23 1 
ATOM   4383 N  N    A LYS   B 1 31  ? 50.367 -17.634 -15.439 0.64 18.19 ?  31  LYS   B N    1 
ATOM   4384 N  N    B LYS   B 1 31  ? 50.369 -17.641 -15.438 0.36 18.46 ?  31  LYS   B N    1 
ATOM   4385 C  CA   A LYS   B 1 31  ? 50.382 -16.222 -15.077 0.64 18.26 ?  31  LYS   B CA   1 
ATOM   4386 C  CA   B LYS   B 1 31  ? 50.381 -16.231 -15.072 0.36 18.54 ?  31  LYS   B CA   1 
ATOM   4387 C  C    A LYS   B 1 31  ? 48.990 -15.714 -14.685 0.64 16.41 ?  31  LYS   B C    1 
ATOM   4388 C  C    B LYS   B 1 31  ? 48.976 -15.743 -14.707 0.36 16.50 ?  31  LYS   B C    1 
ATOM   4389 O  O    A LYS   B 1 31  ? 48.465 -14.779 -15.299 0.64 17.27 ?  31  LYS   B O    1 
ATOM   4390 O  O    B LYS   B 1 31  ? 48.423 -14.863 -15.373 0.36 16.71 ?  31  LYS   B O    1 
ATOM   4391 C  CB   A LYS   B 1 31  ? 51.001 -15.373 -16.180 0.64 21.07 ?  31  LYS   B CB   1 
ATOM   4392 C  CB   B LYS   B 1 31  ? 51.000 -15.384 -16.176 0.36 20.95 ?  31  LYS   B CB   1 
ATOM   4393 C  CG   A LYS   B 1 31  ? 52.445 -15.768 -16.487 0.64 24.07 ?  31  LYS   B CG   1 
ATOM   4394 C  CG   B LYS   B 1 31  ? 52.402 -15.859 -16.543 0.36 23.07 ?  31  LYS   B CG   1 
ATOM   4395 C  CD   A LYS   B 1 31  ? 53.013 -14.978 -17.648 0.64 26.99 ?  31  LYS   B CD   1 
ATOM   4396 C  CD   B LYS   B 1 31  ? 52.973 -15.111 -17.726 0.36 25.07 ?  31  LYS   B CD   1 
ATOM   4397 C  CE   A LYS   B 1 31  ? 54.485 -15.281 -17.842 0.64 28.78 ?  31  LYS   B CE   1 
ATOM   4398 C  CE   B LYS   B 1 31  ? 54.447 -15.426 -17.900 0.36 26.56 ?  31  LYS   B CE   1 
ATOM   4399 N  NZ   A LYS   B 1 31  ? 55.276 -14.924 -16.631 0.64 29.65 ?  31  LYS   B NZ   1 
ATOM   4400 N  NZ   B LYS   B 1 31  ? 55.228 -15.076 -16.680 0.36 27.44 ?  31  LYS   B NZ   1 
ATOM   4401 H  H    A LYS   B 1 31  ? 50.935 -18.112 -14.998 0.64 21.95 ?  31  LYS   B H    1 
ATOM   4402 H  H    B LYS   B 1 31  ? 50.936 -18.118 -14.998 0.36 22.27 ?  31  LYS   B H    1 
ATOM   4403 H  HA   A LYS   B 1 31  ? 50.939 -16.135 -14.298 0.64 22.03 ?  31  LYS   B HA   1 
ATOM   4404 H  HA   B LYS   B 1 31  ? 50.936 -16.138 -14.292 0.36 22.36 ?  31  LYS   B HA   1 
ATOM   4405 H  HB2  A LYS   B 1 31  ? 50.480 -15.478 -16.991 0.64 25.40 ?  31  LYS   B HB2  1 
ATOM   4406 H  HB2  B LYS   B 1 31  ? 50.448 -15.433 -16.969 0.36 25.25 ?  31  LYS   B HB2  1 
ATOM   4407 H  HB3  A LYS   B 1 31  ? 50.995 -14.449 -15.894 0.64 25.40 ?  31  LYS   B HB3  1 
ATOM   4408 H  HB3  B LYS   B 1 31  ? 51.065 -14.468 -15.866 0.36 25.25 ?  31  LYS   B HB3  1 
ATOM   4409 H  HG2  A LYS   B 1 31  ? 52.988 -15.601 -15.702 0.64 29.00 ?  31  LYS   B HG2  1 
ATOM   4410 H  HG2  B LYS   B 1 31  ? 52.987 -15.723 -15.781 0.36 27.80 ?  31  LYS   B HG2  1 
ATOM   4411 H  HG3  A LYS   B 1 31  ? 52.474 -16.712 -16.717 0.64 29.00 ?  31  LYS   B HG3  1 
ATOM   4412 H  HG3  B LYS   B 1 31  ? 52.372 -16.802 -16.772 0.36 27.80 ?  31  LYS   B HG3  1 
ATOM   4413 H  HD2  A LYS   B 1 31  ? 52.537 -15.219 -18.458 0.64 32.50 ?  31  LYS   B HD2  1 
ATOM   4414 H  HD2  B LYS   B 1 31  ? 52.504 -15.381 -18.531 0.36 30.20 ?  31  LYS   B HD2  1 
ATOM   4415 H  HD3  A LYS   B 1 31  ? 52.913 -14.032 -17.465 0.64 32.50 ?  31  LYS   B HD3  1 
ATOM   4416 H  HD3  B LYS   B 1 31  ? 52.877 -14.159 -17.580 0.36 30.20 ?  31  LYS   B HD3  1 
ATOM   4417 H  HE2  A LYS   B 1 31  ? 54.597 -16.230 -18.012 0.64 34.65 ?  31  LYS   B HE2  1 
ATOM   4418 H  HE2  B LYS   B 1 31  ? 54.555 -16.376 -18.067 0.36 31.98 ?  31  LYS   B HE2  1 
ATOM   4419 H  HE3  A LYS   B 1 31  ? 54.821 -14.764 -18.590 0.64 34.65 ?  31  LYS   B HE3  1 
ATOM   4420 H  HE3  B LYS   B 1 31  ? 54.798 -14.913 -18.644 0.36 31.98 ?  31  LYS   B HE3  1 
ATOM   4421 H  HZ1  A LYS   B 1 31  ? 56.146 -15.007 -16.800 0.64 35.69 ?  31  LYS   B HZ1  1 
ATOM   4422 H  HZ1  B LYS   B 1 31  ? 56.099 -15.109 -16.856 0.36 33.05 ?  31  LYS   B HZ1  1 
ATOM   4423 H  HZ2  A LYS   B 1 31  ? 55.106 -14.084 -16.393 0.64 35.69 ?  31  LYS   B HZ2  1 
ATOM   4424 H  HZ2  B LYS   B 1 31  ? 55.018 -14.254 -16.411 0.36 33.05 ?  31  LYS   B HZ2  1 
ATOM   4425 H  HZ3  A LYS   B 1 31  ? 55.061 -15.464 -15.956 0.64 35.69 ?  31  LYS   B HZ3  1 
ATOM   4426 H  HZ3  B LYS   B 1 31  ? 55.043 -15.649 -16.024 0.36 33.05 ?  31  LYS   B HZ3  1 
ATOM   4427 N  N    . PRO   B 1 32  ? 48.375 -16.305 -13.657 1.00 14.85 ?  32  PRO   B N    1 
ATOM   4428 C  CA   . PRO   B 1 32  ? 47.002 -15.934 -13.298 1.00 14.06 ?  32  PRO   B CA   1 
ATOM   4429 C  C    . PRO   B 1 32  ? 46.922 -14.592 -12.587 1.00 13.91 ?  32  PRO   B C    1 
ATOM   4430 O  O    . PRO   B 1 32  ? 47.846 -14.171 -11.883 1.00 15.23 ?  32  PRO   B O    1 
ATOM   4431 C  CB   . PRO   B 1 32  ? 46.596 -17.051 -12.329 1.00 13.95 ?  32  PRO   B CB   1 
ATOM   4432 C  CG   . PRO   B 1 32  ? 47.897 -17.402 -11.646 1.00 14.41 ?  32  PRO   B CG   1 
ATOM   4433 C  CD   . PRO   B 1 32  ? 48.950 -17.285 -12.711 1.00 14.73 ?  32  PRO   B CD   1 
ATOM   4434 H  HA   . PRO   B 1 32  ? 46.420 -15.945 -14.082 1.00 16.98 ?  32  PRO   B HA   1 
ATOM   4435 H  HB2  . PRO   B 1 32  ? 45.943 -16.714 -11.692 1.00 16.86 ?  32  PRO   B HB2  1 
ATOM   4436 H  HB3  . PRO   B 1 32  ? 46.240 -17.809 -12.820 1.00 16.86 ?  32  PRO   B HB3  1 
ATOM   4437 H  HG2  . PRO   B 1 32  ? 48.065 -16.775 -10.923 1.00 17.41 ?  32  PRO   B HG2  1 
ATOM   4438 H  HG3  . PRO   B 1 32  ? 47.852 -18.310 -11.304 1.00 17.41 ?  32  PRO   B HG3  1 
ATOM   4439 H  HD2  . PRO   B 1 32  ? 49.770 -16.943 -12.327 1.00 17.79 ?  32  PRO   B HD2  1 
ATOM   4440 H  HD3  . PRO   B 1 32  ? 49.080 -18.140 -13.140 1.00 17.79 ?  32  PRO   B HD3  1 
ATOM   4441 N  N    . THR   B 1 33  ? 45.766 -13.940 -12.749 1.00 13.50 ?  33  THR   B N    1 
ATOM   4442 C  CA   . THR   B 1 33  ? 45.474 -12.761 -11.941 1.00 13.59 ?  33  THR   B CA   1 
ATOM   4443 C  C    . THR   B 1 33  ? 45.433 -13.113 -10.459 1.00 13.31 ?  33  THR   B C    1 
ATOM   4444 O  O    . THR   B 1 33  ? 45.909 -12.335 -9.619  1.00 14.53 ?  33  THR   B O    1 
ATOM   4445 C  CB   . THR   B 1 33  ? 44.155 -12.126 -12.392 1.00 14.39 ?  33  THR   B CB   1 
ATOM   4446 O  OG1  . THR   B 1 33  ? 44.198 -11.875 -13.800 1.00 14.06 ?  33  THR   B OG1  1 
ATOM   4447 C  CG2  . THR   B 1 33  ? 43.887 -10.829 -11.642 1.00 15.49 ?  33  THR   B CG2  1 
ATOM   4448 H  H    . THR   B 1 33  ? 45.147 -14.157 -13.310 1.00 16.32 ?  33  THR   B H    1 
ATOM   4449 H  HA   . THR   B 1 33  ? 46.173 -12.109 -12.072 1.00 16.43 ?  33  THR   B HA   1 
ATOM   4450 H  HB   . THR   B 1 33  ? 43.420 -12.740 -12.203 1.00 17.39 ?  33  THR   B HB   1 
ATOM   4451 H  HG1  . THR   B 1 33  ? 43.481 -11.510 -14.049 1.00 16.99 ?  33  THR   B HG1  1 
ATOM   4452 H  HG21 . THR   B 1 33  ? 43.127 -10.374 -12.029 1.00 18.71 ?  33  THR   B HG21 1 
ATOM   4453 H  HG22 . THR   B 1 33  ? 43.702 -11.016 -10.707 1.00 18.71 ?  33  THR   B HG22 1 
ATOM   4454 H  HG23 . THR   B 1 33  ? 44.666 -10.253 -11.700 1.00 18.71 ?  33  THR   B HG23 1 
ATOM   4455 N  N    . VAL   B 1 34  ? 44.880 -14.284 -10.118 1.00 12.39 ?  34  VAL   B N    1 
ATOM   4456 C  CA   . VAL   B 1 34  ? 44.681 -14.681 -8.727  1.00 12.05 ?  34  VAL   B CA   1 
ATOM   4457 C  C    . VAL   B 1 34  ? 45.104 -16.134 -8.558  1.00 11.19 ?  34  VAL   B C    1 
ATOM   4458 O  O    . VAL   B 1 34  ? 44.578 -17.025 -9.239  1.00 11.92 ?  34  VAL   B O    1 
ATOM   4459 C  CB   . VAL   B 1 34  ? 43.208 -14.530 -8.286  1.00 13.24 ?  34  VAL   B CB   1 
ATOM   4460 C  CG1  . VAL   B 1 34  ? 43.032 -14.992 -6.846  1.00 13.77 ?  34  VAL   B CG1  1 
ATOM   4461 C  CG2  . VAL   B 1 34  ? 42.721 -13.099 -8.461  1.00 14.41 ?  34  VAL   B CG2  1 
ATOM   4462 H  H    . VAL   B 1 34  ? 44.619 -14.878 -10.683 1.00 14.98 ?  34  VAL   B H    1 
ATOM   4463 H  HA   . VAL   B 1 34  ? 45.234 -14.130 -8.147  1.00 14.57 ?  34  VAL   B HA   1 
ATOM   4464 H  HB   . VAL   B 1 34  ? 42.659 -15.094 -8.849  1.00 16.01 ?  34  VAL   B HB   1 
ATOM   4465 H  HG11 . VAL   B 1 34  ? 42.177 -14.673 -6.512  1.00 16.63 ?  34  VAL   B HG11 1 
ATOM   4466 H  HG12 . VAL   B 1 34  ? 43.048 -15.964 -6.818  1.00 16.63 ?  34  VAL   B HG12 1 
ATOM   4467 H  HG13 . VAL   B 1 34  ? 43.750 -14.634 -6.303  1.00 16.63 ?  34  VAL   B HG13 1 
ATOM   4468 H  HG21 . VAL   B 1 34  ? 41.801 -13.035 -8.157  1.00 17.41 ?  34  VAL   B HG21 1 
ATOM   4469 H  HG22 . VAL   B 1 34  ? 43.282 -12.503 -7.937  1.00 17.41 ?  34  VAL   B HG22 1 
ATOM   4470 H  HG23 . VAL   B 1 34  ? 42.773 -12.855 -9.400  1.00 17.41 ?  34  VAL   B HG23 1 
ATOM   4471 N  N    . VAL   B 1 35  ? 46.009 -16.383 -7.614  1.00 10.53 ?  35  VAL   B N    1 
ATOM   4472 C  CA   . VAL   B 1 35  ? 46.240 -17.725 -7.095  1.00 10.37 ?  35  VAL   B CA   1 
ATOM   4473 C  C    . VAL   B 1 35  ? 45.703 -17.776 -5.675  1.00 10.10 ?  35  VAL   B C    1 
ATOM   4474 O  O    . VAL   B 1 35  ? 45.920 -16.850 -4.886  1.00 10.42 ?  35  VAL   B O    1 
ATOM   4475 C  CB   . VAL   B 1 35  ? 47.722 -18.157 -7.176  1.00 11.38 ?  35  VAL   B CB   1 
ATOM   4476 C  CG1  . VAL   B 1 35  ? 48.629 -17.304 -6.266  1.00 11.71 ?  35  VAL   B CG1  1 
ATOM   4477 C  CG2  . VAL   B 1 35  ? 47.857 -19.649 -6.843  1.00 12.08 ?  35  VAL   B CG2  1 
ATOM   4478 H  H    . VAL   B 1 35  ? 46.514 -15.782 -7.258  1.00 12.75 ?  35  VAL   B H    1 
ATOM   4479 H  HA   . VAL   B 1 35  ? 45.725 -18.355 -7.621  1.00 12.56 ?  35  VAL   B HA   1 
ATOM   4480 H  HB   . VAL   B 1 35  ? 48.026 -18.038 -8.090  1.00 13.78 ?  35  VAL   B HB   1 
ATOM   4481 H  HG11 . VAL   B 1 35  ? 49.550 -17.544 -6.441  1.00 14.16 ?  35  VAL   B HG11 1 
ATOM   4482 H  HG12 . VAL   B 1 35  ? 48.476 -16.374 -6.463  1.00 14.16 ?  35  VAL   B HG12 1 
ATOM   4483 H  HG13 . VAL   B 1 35  ? 48.404 -17.497 -5.341  1.00 14.16 ?  35  VAL   B HG13 1 
ATOM   4484 H  HG21 . VAL   B 1 35  ? 48.778 -19.923 -6.954  1.00 14.62 ?  35  VAL   B HG21 1 
ATOM   4485 H  HG22 . VAL   B 1 35  ? 47.575 -19.800 -5.924  1.00 14.62 ?  35  VAL   B HG22 1 
ATOM   4486 H  HG23 . VAL   B 1 35  ? 47.286 -20.165 -7.443  1.00 14.62 ?  35  VAL   B HG23 1 
ATOM   4487 N  N    . VAL   B 1 36  ? 44.981 -18.855 -5.357  1.00 9.96  ?  36  VAL   B N    1 
ATOM   4488 C  CA   . VAL   B 1 36  ? 44.432 -19.053 -4.026  1.00 9.76  ?  36  VAL   B CA   1 
ATOM   4489 C  C    . VAL   B 1 36  ? 45.441 -19.814 -3.171  1.00 9.77  ?  36  VAL   B C    1 
ATOM   4490 O  O    . VAL   B 1 36  ? 45.985 -20.848 -3.589  1.00 10.57 ?  36  VAL   B O    1 
ATOM   4491 C  CB   . VAL   B 1 36  ? 43.091 -19.810 -4.100  1.00 10.45 ?  36  VAL   B CB   1 
ATOM   4492 C  CG1  . VAL   B 1 36  ? 42.590 -20.169 -2.706  1.00 11.17 ?  36  VAL   B CG1  1 
ATOM   4493 C  CG2  . VAL   B 1 36  ? 42.060 -18.981 -4.852  1.00 10.98 ?  36  VAL   B CG2  1 
ATOM   4494 H  H    . VAL   B 1 36  ? 44.806 -19.495 -5.900  1.00 12.07 ?  36  VAL   B H    1 
ATOM   4495 H  HA   . VAL   B 1 36  ? 44.268 -18.191 -3.610  1.00 11.83 ?  36  VAL   B HA   1 
ATOM   4496 H  HB   . VAL   B 1 36  ? 43.223 -20.634 -4.589  1.00 12.65 ?  36  VAL   B HB   1 
ATOM   4497 H  HG11 . VAL   B 1 36  ? 41.649 -20.405 -2.761  1.00 13.52 ?  36  VAL   B HG11 1 
ATOM   4498 H  HG12 . VAL   B 1 36  ? 43.098 -20.917 -2.364  1.00 13.52 ?  36  VAL   B HG12 1 
ATOM   4499 H  HG13 . VAL   B 1 36  ? 42.696 -19.397 -2.122  1.00 13.52 ?  36  VAL   B HG13 1 
ATOM   4500 H  HG21 . VAL   B 1 36  ? 41.218 -19.462 -4.872  1.00 13.29 ?  36  VAL   B HG21 1 
ATOM   4501 H  HG22 . VAL   B 1 36  ? 41.943 -18.130 -4.396  1.00 13.29 ?  36  VAL   B HG22 1 
ATOM   4502 H  HG23 . VAL   B 1 36  ? 42.375 -18.827 -5.757  1.00 13.29 ?  36  VAL   B HG23 1 
ATOM   4503 N  N    . ASN   B 1 37  ? 45.659 -19.317 -1.955  1.00 10.26 ?  37  ASN   B N    1 
ATOM   4504 C  CA   . ASN   B 1 37  ? 46.407 -20.044 -0.941  1.00 10.57 ?  37  ASN   B CA   1 
ATOM   4505 C  C    . ASN   B 1 37  ? 45.461 -20.716 0.043   1.00 10.41 ?  37  ASN   B C    1 
ATOM   4506 O  O    . ASN   B 1 37  ? 44.449 -20.135 0.452   1.00 10.91 ?  37  ASN   B O    1 
ATOM   4507 C  CB   . ASN   B 1 37  ? 47.335 -19.099 -0.179  1.00 10.56 ?  37  ASN   B CB   1 
ATOM   4508 C  CG   . ASN   B 1 37  ? 48.186 -19.817 0.834   1.00 10.95 ?  37  ASN   B CG   1 
ATOM   4509 O  OD1  . ASN   B 1 37  ? 48.531 -20.992 0.660   1.00 11.50 ?  37  ASN   B OD1  1 
ATOM   4510 N  ND2  . ASN   B 1 37  ? 48.542 -19.110 1.901   1.00 10.79 ?  37  ASN   B ND2  1 
ATOM   4511 H  H    . ASN   B 1 37  ? 45.372 -18.549 -1.685  1.00 12.43 ?  37  ASN   B H    1 
ATOM   4512 H  HA   . ASN   B 1 37  ? 46.945 -20.730 -1.360  1.00 12.80 ?  37  ASN   B HA   1 
ATOM   4513 H  HB2  . ASN   B 1 37  ? 47.927 -18.667 -0.814  1.00 12.78 ?  37  ASN   B HB2  1 
ATOM   4514 H  HB3  . ASN   B 1 37  ? 46.805 -18.439 0.289   1.00 12.78 ?  37  ASN   B HB3  1 
ATOM   4515 H  HD21 . ASN   B 1 37  ? 49.043 -19.462 2.506   1.00 13.06 ?  37  ASN   B HD21 1 
ATOM   4516 H  HD22 . ASN   B 1 37  ? 48.295 -18.293 1.982   1.00 13.06 ?  37  ASN   B HD22 1 
ATOM   4517 N  N    . ALA   B 1 38  ? 45.814 -21.947 0.420   1.00 10.62 ?  38  ALA   B N    1 
ATOM   4518 C  CA   . ALA   B 1 38  ? 45.156 -22.689 1.497   1.00 10.99 ?  38  ALA   B CA   1 
ATOM   4519 C  C    . ALA   B 1 38  ? 45.736 -22.200 2.822   1.00 10.94 ?  38  ALA   B C    1 
ATOM   4520 O  O    . ALA   B 1 38  ? 46.637 -22.809 3.408   1.00 11.71 ?  38  ALA   B O    1 
ATOM   4521 C  CB   . ALA   B 1 38  ? 45.383 -24.184 1.317   1.00 12.40 ?  38  ALA   B CB   1 
ATOM   4522 H  H    . ALA   B 1 38  ? 46.466 -22.385 0.068   1.00 12.86 ?  38  ALA   B H    1 
ATOM   4523 H  HA   . ALA   B 1 38  ? 44.203 -22.509 1.489   1.00 13.30 ?  38  ALA   B HA   1 
ATOM   4524 H  HB1  . ALA   B 1 38  ? 44.933 -24.661 2.041   1.00 15.00 ?  38  ALA   B HB1  1 
ATOM   4525 H  HB2  . ALA   B 1 38  ? 45.009 -24.459 0.467   1.00 15.00 ?  38  ALA   B HB2  1 
ATOM   4526 H  HB3  . ALA   B 1 38  ? 46.330 -24.370 1.345   1.00 15.00 ?  38  ALA   B HB3  1 
ATOM   4527 N  N    . ALA   B 1 39  ? 45.223 -21.057 3.280   1.00 10.76 ?  39  ALA   B N    1 
ATOM   4528 C  CA   . ALA   B 1 39  ? 45.772 -20.325 4.413   1.00 11.19 ?  39  ALA   B CA   1 
ATOM   4529 C  C    . ALA   B 1 39  ? 45.152 -20.767 5.739   1.00 11.13 ?  39  ALA   B C    1 
ATOM   4530 O  O    . ALA   B 1 39  ? 44.122 -21.441 5.785   1.00 12.22 ?  39  ALA   B O    1 
ATOM   4531 C  CB   . ALA   B 1 39  ? 45.539 -18.820 4.217   1.00 11.90 ?  39  ALA   B CB   1 
ATOM   4532 H  H    . ALA   B 1 39  ? 44.533 -20.678 2.934   1.00 13.02 ?  39  ALA   B H    1 
ATOM   4533 H  HA   . ALA   B 1 39  ? 46.725 -20.479 4.460   1.00 13.54 ?  39  ALA   B HA   1 
ATOM   4534 H  HB1  . ALA   B 1 39  ? 45.909 -18.341 4.976   1.00 14.39 ?  39  ALA   B HB1  1 
ATOM   4535 H  HB2  . ALA   B 1 39  ? 45.983 -18.536 3.401   1.00 14.39 ?  39  ALA   B HB2  1 
ATOM   4536 H  HB3  . ALA   B 1 39  ? 44.587 -18.650 4.150   1.00 14.39 ?  39  ALA   B HB3  1 
ATOM   4537 N  N    . ASN   B 1 40  ? 45.794 -20.355 6.830   1.00 11.72 ?  40  ASN   B N    1 
ATOM   4538 C  CA   . ASN   B 1 40  ? 45.230 -20.399 8.171   1.00 12.39 ?  40  ASN   B CA   1 
ATOM   4539 C  C    . ASN   B 1 40  ? 45.047 -18.970 8.692   1.00 12.03 ?  40  ASN   B C    1 
ATOM   4540 O  O    . ASN   B 1 40  ? 45.453 -17.993 8.053   1.00 12.23 ?  40  ASN   B O    1 
ATOM   4541 C  CB   . ASN   B 1 40  ? 46.081 -21.273 9.108   1.00 13.06 ?  40  ASN   B CB   1 
ATOM   4542 C  CG   . ASN   B 1 40  ? 47.537 -20.869 9.131   1.00 14.34 ?  40  ASN   B CG   1 
ATOM   4543 O  OD1  . ASN   B 1 40  ? 47.858 -19.687 9.207   1.00 16.43 ?  40  ASN   B OD1  1 
ATOM   4544 N  ND2  . ASN   B 1 40  ? 48.428 -21.843 9.071   1.00 14.75 ?  40  ASN   B ND2  1 
ATOM   4545 H  H    . ASN   B 1 40  ? 46.592 -20.039 6.811   1.00 14.18 ?  40  ASN   B H    1 
ATOM   4546 H  HA   . ASN   B 1 40  ? 44.348 -20.800 8.122   1.00 14.98 ?  40  ASN   B HA   1 
ATOM   4547 H  HB2  . ASN   B 1 40  ? 45.733 -21.197 10.011  1.00 15.79 ?  40  ASN   B HB2  1 
ATOM   4548 H  HB3  . ASN   B 1 40  ? 46.030 -22.195 8.810   1.00 15.79 ?  40  ASN   B HB3  1 
ATOM   4549 H  HD21 . ASN   B 1 40  ? 49.269 -21.660 9.080   1.00 17.82 ?  40  ASN   B HD21 1 
ATOM   4550 H  HD22 . ASN   B 1 40  ? 48.165 -22.659 9.017   1.00 17.82 ?  40  ASN   B HD22 1 
ATOM   4551 N  N    . VAL   B 1 41  ? 44.402 -18.843 9.854   1.00 12.67 ?  41  VAL   B N    1 
ATOM   4552 C  CA   . VAL   B 1 41  ? 43.943 -17.522 10.294  1.00 13.56 ?  41  VAL   B CA   1 
ATOM   4553 C  C    . VAL   B 1 41  ? 45.093 -16.567 10.589  1.00 13.33 ?  41  VAL   B C    1 
ATOM   4554 O  O    . VAL   B 1 41  ? 44.915 -15.346 10.500  1.00 13.46 ?  41  VAL   B O    1 
ATOM   4555 C  CB   . VAL   B 1 41  ? 42.962 -17.592 11.480  1.00 15.20 ?  41  VAL   B CB   1 
ATOM   4556 C  CG1  . VAL   B 1 41  ? 41.654 -18.260 11.067  1.00 15.15 ?  41  VAL   B CG1  1 
ATOM   4557 C  CG2  . VAL   B 1 41  ? 43.598 -18.285 12.676  1.00 16.37 ?  41  VAL   B CG2  1 
ATOM   4558 H  H    . VAL   B 1 41  ? 44.226 -19.483 10.393  1.00 15.32 ?  41  VAL   B H    1 
ATOM   4559 H  HA   . VAL   B 1 41  ? 43.452 -17.126 9.560   1.00 16.39 ?  41  VAL   B HA   1 
ATOM   4560 H  HB   . VAL   B 1 41  ? 42.744 -16.687 11.754  1.00 18.35 ?  41  VAL   B HB   1 
ATOM   4561 H  HG11 . VAL   B 1 41  ? 41.046 -18.264 11.823  1.00 18.30 ?  41  VAL   B HG11 1 
ATOM   4562 H  HG12 . VAL   B 1 41  ? 41.263 -17.765 10.331  1.00 18.30 ?  41  VAL   B HG12 1 
ATOM   4563 H  HG13 . VAL   B 1 41  ? 41.840 -19.173 10.790  1.00 18.30 ?  41  VAL   B HG13 1 
ATOM   4564 H  HG21 . VAL   B 1 41  ? 42.961 -18.303 13.407  1.00 19.76 ?  41  VAL   B HG21 1 
ATOM   4565 H  HG22 . VAL   B 1 41  ? 43.837 -19.192 12.427  1.00 19.76 ?  41  VAL   B HG22 1 
ATOM   4566 H  HG23 . VAL   B 1 41  ? 44.391 -17.794 12.941  1.00 19.76 ?  41  VAL   B HG23 1 
ATOM   4567 N  N    . TYR   B 1 42  ? 46.263 -17.082 10.972  1.00 13.43 ?  42  TYR   B N    1 
ATOM   4568 C  CA   . TYR   B 1 42  ? 47.416 -16.233 11.238  1.00 13.64 ?  42  TYR   B CA   1 
ATOM   4569 C  C    . TYR   B 1 42  ? 48.381 -16.164 10.057  1.00 13.16 ?  42  TYR   B C    1 
ATOM   4570 O  O    . TYR   B 1 42  ? 49.472 -15.595 10.191  1.00 14.45 ?  42  TYR   B O    1 
ATOM   4571 C  CB   . TYR   B 1 42  ? 48.109 -16.636 12.546  1.00 15.75 ?  42  TYR   B CB   1 
ATOM   4572 C  CG   . TYR   B 1 42  ? 47.506 -15.951 13.772  1.00 15.97 ?  42  TYR   B CG   1 
ATOM   4573 C  CD1  . TYR   B 1 42  ? 47.707 -14.592 13.996  1.00 15.36 ?  42  TYR   B CD1  1 
ATOM   4574 C  CD2  . TYR   B 1 42  ? 46.735 -16.652 14.689  1.00 17.49 ?  42  TYR   B CD2  1 
ATOM   4575 C  CE1  . TYR   B 1 42  ? 47.165 -13.955 15.095  1.00 16.09 ?  42  TYR   B CE1  1 
ATOM   4576 C  CE2  . TYR   B 1 42  ? 46.194 -16.022 15.799  1.00 17.95 ?  42  TYR   B CE2  1 
ATOM   4577 C  CZ   . TYR   B 1 42  ? 46.408 -14.668 15.995  1.00 18.04 ?  42  TYR   B CZ   1 
ATOM   4578 O  OH   . TYR   B 1 42  ? 45.877 -14.019 17.093  1.00 20.80 ?  42  TYR   B OH   1 
ATOM   4579 H  H    . TYR   B 1 42  ? 46.415 -17.930 11.068  1.00 16.23 ?  42  TYR   B H    1 
ATOM   4580 H  HA   . TYR   B 1 42  ? 47.088 -15.335 11.368  1.00 16.48 ?  42  TYR   B HA   1 
ATOM   4581 H  HB2  . TYR   B 1 42  ? 48.027 -17.594 12.667  1.00 19.02 ?  42  TYR   B HB2  1 
ATOM   4582 H  HB3  . TYR   B 1 42  ? 49.045 -16.387 12.495  1.00 19.02 ?  42  TYR   B HB3  1 
ATOM   4583 H  HD1  . TYR   B 1 42  ? 48.219 -14.102 13.385  1.00 18.55 ?  42  TYR   B HD1  1 
ATOM   4584 H  HD2  . TYR   B 1 42  ? 46.587 -17.564 14.556  1.00 21.11 ?  42  TYR   B HD2  1 
ATOM   4585 H  HE1  . TYR   B 1 42  ? 47.315 -13.045 15.223  1.00 19.43 ?  42  TYR   B HE1  1 
ATOM   4586 H  HE2  . TYR   B 1 42  ? 45.679 -16.507 16.400  1.00 21.65 ?  42  TYR   B HE2  1 
ATOM   4587 H  HH   . TYR   B 1 42  ? 46.094 -13.212 17.072  1.00 25.07 ?  42  TYR   B HH   1 
ATOM   4588 N  N    . LEU   B 1 43  ? 47.983 -16.678 8.894   1.00 12.39 ?  43  LEU   B N    1 
ATOM   4589 C  CA   . LEU   B 1 43  ? 48.796 -16.605 7.683   1.00 12.04 ?  43  LEU   B CA   1 
ATOM   4590 C  C    . LEU   B 1 43  ? 50.208 -17.115 7.940   1.00 12.21 ?  43  LEU   B C    1 
ATOM   4591 O  O    . LEU   B 1 43  ? 51.193 -16.526 7.491   1.00 12.86 ?  43  LEU   B O    1 
ATOM   4592 C  CB   . LEU   B 1 43  ? 48.815 -15.204 7.073   1.00 12.17 ?  43  LEU   B CB   1 
ATOM   4593 C  CG   . LEU   B 1 43  ? 47.459 -14.592 6.704   1.00 12.69 ?  43  LEU   B CG   1 
ATOM   4594 C  CD1  . LEU   B 1 43  ? 47.681 -13.194 6.120   1.00 13.75 ?  43  LEU   B CD1  1 
ATOM   4595 C  CD2  . LEU   B 1 43  ? 46.687 -15.478 5.734   1.00 12.70 ?  43  LEU   B CD2  1 
ATOM   4596 H  H    . LEU   B 1 43  ? 47.239 -17.091 8.781   1.00 14.98 ?  43  LEU   B H    1 
ATOM   4597 H  HA   . LEU   B 1 43  ? 48.399 -17.198 7.021   1.00 14.57 ?  43  LEU   B HA   1 
ATOM   4598 H  HB2  . LEU   B 1 43  ? 49.241 -14.608 7.705   1.00 14.72 ?  43  LEU   B HB2  1 
ATOM   4599 H  HB3  . LEU   B 1 43  ? 49.342 -15.240 6.259   1.00 14.72 ?  43  LEU   B HB3  1 
ATOM   4600 H  HG   . LEU   B 1 43  ? 46.931 -14.492 7.509   1.00 15.34 ?  43  LEU   B HG   1 
ATOM   4601 H  HD11 . LEU   B 1 43  ? 46.819 -12.808 5.892   1.00 16.62 ?  43  LEU   B HD11 1 
ATOM   4602 H  HD12 . LEU   B 1 43  ? 48.123 -12.640 6.785   1.00 16.62 ?  43  LEU   B HD12 1 
ATOM   4603 H  HD13 . LEU   B 1 43  ? 48.233 -13.264 5.328   1.00 16.62 ?  43  LEU   B HD13 1 
ATOM   4604 H  HD21 . LEU   B 1 43  ? 45.885 -15.011 5.451   1.00 15.35 ?  43  LEU   B HD21 1 
ATOM   4605 H  HD22 . LEU   B 1 43  ? 47.247 -15.669 4.966   1.00 15.35 ?  43  LEU   B HD22 1 
ATOM   4606 H  HD23 . LEU   B 1 43  ? 46.449 -16.302 6.184   1.00 15.35 ?  43  LEU   B HD23 1 
ATOM   4607 N  N    . LYS   B 1 44  ? 50.305 -18.236 8.657   1.00 12.37 ?  44  LYS   B N    1 
ATOM   4608 C  CA   . LYS   B 1 44  ? 51.571 -18.915 8.899   1.00 12.93 ?  44  LYS   B CA   1 
ATOM   4609 C  C    . LYS   B 1 44  ? 51.692 -20.033 7.873   1.00 12.41 ?  44  LYS   B C    1 
ATOM   4610 O  O    . LYS   B 1 44  ? 51.000 -21.051 7.966   1.00 13.73 ?  44  LYS   B O    1 
ATOM   4611 C  CB   . LYS   B 1 44  ? 51.631 -19.428 10.336  1.00 14.96 ?  44  LYS   B CB   1 
ATOM   4612 C  CG   . LYS   B 1 44  ? 51.837 -18.318 11.353  1.00 17.61 ?  44  LYS   B CG   1 
ATOM   4613 C  CD   . LYS   B 1 44  ? 53.028 -17.451 10.930  1.00 20.97 ?  44  LYS   B CD   1 
ATOM   4614 C  CE   . LYS   B 1 44  ? 53.549 -16.580 12.039  1.00 23.92 ?  44  LYS   B CE   1 
ATOM   4615 N  NZ   . LYS   B 1 44  ? 54.734 -15.786 11.635  1.00 25.14 ?  44  LYS   B NZ   1 
ATOM   4616 H  H    . LYS   B 1 44  ? 49.633 -18.620 9.027   1.00 14.97 ?  44  LYS   B H    1 
ATOM   4617 H  HA   . LYS   B 1 44  ? 52.304 -18.300 8.734   1.00 15.63 ?  44  LYS   B HA   1 
ATOM   4618 H  HB2  . LYS   B 1 44  ? 50.789 -19.869 10.548  1.00 18.06 ?  44  LYS   B HB2  1 
ATOM   4619 H  HB3  . LYS   B 1 44  ? 52.363 -20.054 10.421  1.00 18.06 ?  44  LYS   B HB3  1 
ATOM   4620 H  HG2  . LYS   B 1 44  ? 51.046 -17.765 11.401  1.00 21.25 ?  44  LYS   B HG2  1 
ATOM   4621 H  HG3  . LYS   B 1 44  ? 52.036 -18.711 12.222  1.00 21.25 ?  44  LYS   B HG3  1 
ATOM   4622 H  HD2  . LYS   B 1 44  ? 53.744 -18.034 10.618  1.00 25.29 ?  44  LYS   B HD2  1 
ATOM   4623 H  HD3  . LYS   B 1 44  ? 52.742 -16.867 10.208  1.00 25.29 ?  44  LYS   B HD3  1 
ATOM   4624 H  HE2  . LYS   B 1 44  ? 52.855 -15.952 12.269  1.00 28.81 ?  44  LYS   B HE2  1 
ATOM   4625 H  HE3  . LYS   B 1 44  ? 53.785 -17.135 12.800  1.00 28.81 ?  44  LYS   B HE3  1 
ATOM   4626 H  HZ1  . LYS   B 1 44  ? 55.001 -15.276 12.314  1.00 30.28 ?  44  LYS   B HZ1  1 
ATOM   4627 H  HZ2  . LYS   B 1 44  ? 55.399 -16.324 11.396  1.00 30.28 ?  44  LYS   B HZ2  1 
ATOM   4628 H  HZ3  . LYS   B 1 44  ? 54.526 -15.260 10.945  1.00 30.28 ?  44  LYS   B HZ3  1 
ATOM   4629 N  N    . HIS   B 1 45  ? 52.549 -19.818 6.876   1.00 12.19 ?  45  HIS   B N    1 
ATOM   4630 C  CA   . HIS   B 1 45  ? 52.573 -20.650 5.673   1.00 12.35 ?  45  HIS   B CA   1 
ATOM   4631 C  C    . HIS   B 1 45  ? 53.593 -21.774 5.836   1.00 14.64 ?  45  HIS   B C    1 
ATOM   4632 O  O    . HIS   B 1 45  ? 54.657 -21.789 5.225   1.00 16.91 ?  45  HIS   B O    1 
ATOM   4633 C  CB   . HIS   B 1 45  ? 52.889 -19.794 4.459   1.00 12.24 ?  45  HIS   B CB   1 
ATOM   4634 C  CG   . HIS   B 1 45  ? 52.018 -18.594 4.344   1.00 12.09 ?  45  HIS   B CG   1 
ATOM   4635 N  ND1  . HIS   B 1 45  ? 50.641 -18.673 4.291   1.00 12.11 ?  45  HIS   B ND1  1 
ATOM   4636 C  CD2  . HIS   B 1 45  ? 52.333 -17.279 4.284   1.00 13.03 ?  45  HIS   B CD2  1 
ATOM   4637 C  CE1  . HIS   B 1 45  ? 50.152 -17.451 4.186   1.00 12.12 ?  45  HIS   B CE1  1 
ATOM   4638 N  NE2  . HIS   B 1 45  ? 51.154 -16.587 4.178   1.00 12.62 ?  45  HIS   B NE2  1 
ATOM   4639 H  H    . HIS   B 1 45  ? 53.123 -19.176 6.866   1.00 14.74 ?  45  HIS   B H    1 
ATOM   4640 H  HA   . HIS   B 1 45  ? 51.694 -21.045 5.543   1.00 14.94 ?  45  HIS   B HA   1 
ATOM   4641 H  HB2  . HIS   B 1 45  ? 53.808 -19.495 4.516   1.00 14.80 ?  45  HIS   B HB2  1 
ATOM   4642 H  HB3  . HIS   B 1 45  ? 52.767 -20.333 3.657   1.00 14.80 ?  45  HIS   B HB3  1 
ATOM   4643 H  HD2  . HIS   B 1 45  ? 53.187 -16.910 4.307   1.00 15.75 ?  45  HIS   B HD2  1 
ATOM   4644 H  HE1  . HIS   B 1 45  ? 49.250 -17.236 4.116   1.00 14.66 ?  45  HIS   B HE1  1 
ATOM   4645 H  HE2  . HIS   B 1 45  ? 51.075 -15.733 4.128   1.00 15.26 ?  45  HIS   B HE2  1 
ATOM   4646 N  N    A GLY   B 1 46  ? 53.221 -22.751 6.659   0.64 15.50 ?  46  GLY   B N    1 
ATOM   4647 N  N    B GLY   B 1 46  ? 53.235 -22.731 6.681   0.36 15.40 ?  46  GLY   B N    1 
ATOM   4648 C  CA   A GLY   B 1 46  ? 54.149 -23.793 7.060   0.64 17.03 ?  46  GLY   B CA   1 
ATOM   4649 C  CA   B GLY   B 1 46  ? 54.158 -23.791 7.024   0.36 16.39 ?  46  GLY   B CA   1 
ATOM   4650 C  C    A GLY   B 1 46  ? 54.208 -25.033 6.190   0.64 18.24 ?  46  GLY   B C    1 
ATOM   4651 C  C    B GLY   B 1 46  ? 54.190 -24.931 6.026   0.36 17.29 ?  46  GLY   B C    1 
ATOM   4652 O  O    A GLY   B 1 46  ? 55.297 -25.504 5.847   0.64 20.77 ?  46  GLY   B O    1 
ATOM   4653 O  O    B GLY   B 1 46  ? 55.219 -25.194 5.394   0.36 17.92 ?  46  GLY   B O    1 
ATOM   4654 H  H    A GLY   B 1 46  ? 52.435 -22.818 7.010   0.64 18.71 ?  46  GLY   B H    1 
ATOM   4655 H  H    B GLY   B 1 46  ? 52.464 -22.781 7.069   0.36 18.60 ?  46  GLY   B H    1 
ATOM   4656 H  HA2  A GLY   B 1 46  ? 55.039 -23.411 7.097   0.64 20.55 ?  46  GLY   B HA2  1 
ATOM   4657 H  HA2  B GLY   B 1 46  ? 55.049 -23.417 7.088   0.36 19.79 ?  46  GLY   B HA2  1 
ATOM   4658 H  HA3  A GLY   B 1 46  ? 53.914 -24.085 7.953   0.64 20.55 ?  46  GLY   B HA3  1 
ATOM   4659 H  HA3  B GLY   B 1 46  ? 53.916 -24.140 7.898   0.36 19.79 ?  46  GLY   B HA3  1 
ATOM   4660 N  N    . GLY   B 1 47  ? 53.052 -25.600 5.850   1.00 17.94 ?  47  GLY   B N    1 
ATOM   4661 C  CA   . GLY   B 1 47  ? 52.997 -26.869 5.152   1.00 16.10 ?  47  GLY   B CA   1 
ATOM   4662 C  C    . GLY   B 1 47  ? 52.074 -26.852 3.949   1.00 14.15 ?  47  GLY   B C    1 
ATOM   4663 O  O    . GLY   B 1 47  ? 51.414 -25.854 3.659   1.00 14.31 ?  47  GLY   B O    1 
ATOM   4664 H  H    A GLY   B 1 47  ? 52.277 -25.277 6.043   0.64 21.65 ?  47  GLY   B H    1 
ATOM   4665 H  H    B GLY   B 1 47  ? 52.283 -25.327 6.129   0.36 21.65 ?  47  GLY   B H    1 
ATOM   4666 H  HA2  . GLY   B 1 47  ? 53.885 -27.115 4.849   1.00 19.43 ?  47  GLY   B HA2  1 
ATOM   4667 H  HA3  . GLY   B 1 47  ? 52.688 -27.558 5.765   1.00 19.43 ?  47  GLY   B HA3  1 
ATOM   4668 N  N    . GLY   B 1 48  ? 52.029 -27.991 3.262   1.00 13.58 ?  48  GLY   B N    1 
ATOM   4669 C  CA   . GLY   B 1 48  ? 51.097 -28.137 2.160   1.00 12.99 ?  48  GLY   B CA   1 
ATOM   4670 C  C    . GLY   B 1 48  ? 51.241 -27.033 1.136   1.00 12.35 ?  48  GLY   B C    1 
ATOM   4671 O  O    . GLY   B 1 48  ? 52.347 -26.573 0.823   1.00 13.18 ?  48  GLY   B O    1 
ATOM   4672 H  H    . GLY   B 1 48  ? 52.523 -28.673 3.410   1.00 16.41 ?  48  GLY   B H    1 
ATOM   4673 H  HA2  . GLY   B 1 48  ? 51.248 -28.990 1.719   1.00 15.70 ?  48  GLY   B HA2  1 
ATOM   4674 H  HA3  . GLY   B 1 48  ? 50.188 -28.124 2.495   1.00 15.70 ?  48  GLY   B HA3  1 
ATOM   4675 N  N    . VAL   B 1 49  ? 50.095 -26.600 0.604   1.00 12.41 ?  49  VAL   B N    1 
ATOM   4676 C  CA   . VAL   B 1 49  ? 50.079 -25.581 -0.442  1.00 12.27 ?  49  VAL   B CA   1 
ATOM   4677 C  C    . VAL   B 1 49  ? 50.733 -24.292 0.044   1.00 11.43 ?  49  VAL   B C    1 
ATOM   4678 O  O    . VAL   B 1 49  ? 51.523 -23.669 -0.675  1.00 12.15 ?  49  VAL   B O    1 
ATOM   4679 C  CB   . VAL   B 1 49  ? 48.635 -25.332 -0.924  1.00 13.49 ?  49  VAL   B CB   1 
ATOM   4680 C  CG1  . VAL   B 1 49  ? 48.566 -24.087 -1.802  1.00 13.72 ?  49  VAL   B CG1  1 
ATOM   4681 C  CG2  . VAL   B 1 49  ? 48.090 -26.551 -1.669  1.00 14.78 ?  49  VAL   B CG2  1 
ATOM   4682 H  H    . VAL   B 1 49  ? 49.308 -26.880 0.832   1.00 15.00 ?  49  VAL   B H    1 
ATOM   4683 H  HA   . VAL   B 1 49  ? 50.582 -25.904 -1.202  1.00 14.84 ?  49  VAL   B HA   1 
ATOM   4684 H  HB   . VAL   B 1 49  ? 48.065 -25.181 -0.156  1.00 16.30 ?  49  VAL   B HB   1 
ATOM   4685 H  HG11 . VAL   B 1 49  ? 47.739 -24.101 -2.312  1.00 16.57 ?  49  VAL   B HG11 1 
ATOM   4686 H  HG12 . VAL   B 1 49  ? 48.583 -23.296 -1.235  1.00 16.57 ?  49  VAL   B HG12 1 
ATOM   4687 H  HG13 . VAL   B 1 49  ? 49.323 -24.079 -2.405  1.00 16.57 ?  49  VAL   B HG13 1 
ATOM   4688 H  HG21 . VAL   B 1 49  ? 47.182 -26.367 -1.961  1.00 17.85 ?  49  VAL   B HG21 1 
ATOM   4689 H  HG22 . VAL   B 1 49  ? 48.652 -26.728 -2.442  1.00 17.85 ?  49  VAL   B HG22 1 
ATOM   4690 H  HG23 . VAL   B 1 49  ? 48.097 -27.314 -1.073  1.00 17.85 ?  49  VAL   B HG23 1 
ATOM   4691 N  N    . ALA   B 1 50  ? 50.387 -23.850 1.252   1.00 11.60 ?  50  ALA   B N    1 
ATOM   4692 C  CA   . ALA   B 1 50  ? 50.909 -22.573 1.728   1.00 11.28 ?  50  ALA   B CA   1 
ATOM   4693 C  C    . ALA   B 1 50  ? 52.428 -22.604 1.836   1.00 11.65 ?  50  ALA   B C    1 
ATOM   4694 O  O    . ALA   B 1 50  ? 53.108 -21.637 1.464   1.00 11.45 ?  50  ALA   B O    1 
ATOM   4695 C  CB   . ALA   B 1 50  ? 50.281 -22.215 3.072   1.00 11.58 ?  50  ALA   B CB   1 
ATOM   4696 H  H    . ALA   B 1 50  ? 49.860 -24.253 1.799   1.00 14.04 ?  50  ALA   B H    1 
ATOM   4697 H  HA   . ALA   B 1 50  ? 50.677 -21.878 1.097   1.00 13.66 ?  50  ALA   B HA   1 
ATOM   4698 H  HB1  . ALA   B 1 50  ? 50.641 -21.363 3.373   1.00 14.01 ?  50  ALA   B HB1  1 
ATOM   4699 H  HB2  . ALA   B 1 50  ? 49.319 -22.143 2.961   1.00 14.01 ?  50  ALA   B HB2  1 
ATOM   4700 H  HB3  . ALA   B 1 50  ? 50.489 -22.907 3.716   1.00 14.01 ?  50  ALA   B HB3  1 
ATOM   4701 N  N    . GLY   B 1 51  ? 52.979 -23.695 2.362   1.00 11.90 ?  51  GLY   B N    1 
ATOM   4702 C  CA   . GLY   B 1 51  ? 54.423 -23.798 2.435   1.00 12.46 ?  51  GLY   B CA   1 
ATOM   4703 C  C    . GLY   B 1 51  ? 55.069 -23.749 1.066   1.00 12.44 ?  51  GLY   B C    1 
ATOM   4704 O  O    . GLY   B 1 51  ? 56.111 -23.112 0.883   1.00 13.53 ?  51  GLY   B O    1 
ATOM   4705 H  H    . GLY   B 1 51  ? 52.549 -24.370 2.677   1.00 14.39 ?  51  GLY   B H    1 
ATOM   4706 H  HA2  . GLY   B 1 51  ? 54.778 -23.069 2.967   1.00 15.06 ?  51  GLY   B HA2  1 
ATOM   4707 H  HA3  . GLY   B 1 51  ? 54.670 -24.636 2.860   1.00 15.06 ?  51  GLY   B HA3  1 
ATOM   4708 N  N    . ALA   B 1 52  ? 54.465 -24.418 0.087   1.00 12.21 ?  52  ALA   B N    1 
ATOM   4709 C  CA   . ALA   B 1 52  ? 55.029 -24.425 -1.255  1.00 12.67 ?  52  ALA   B CA   1 
ATOM   4710 C  C    . ALA   B 1 52  ? 54.950 -23.047 -1.904  1.00 12.00 ?  52  ALA   B C    1 
ATOM   4711 O  O    . ALA   B 1 52  ? 55.921 -22.592 -2.527  1.00 12.75 ?  52  ALA   B O    1 
ATOM   4712 C  CB   . ALA   B 1 52  ? 54.327 -25.469 -2.115  1.00 13.53 ?  52  ALA   B CB   1 
ATOM   4713 H  H    . ALA   B 1 52  ? 53.732 -24.864 0.172   1.00 14.77 ?  52  ALA   B H    1 
ATOM   4714 H  HA   . ALA   B 1 52  ? 55.962 -24.667 -1.198  1.00 15.32 ?  52  ALA   B HA   1 
ATOM   4715 H  HB1  . ALA   B 1 52  ? 54.720 -25.463 -3.004  1.00 16.35 ?  52  ALA   B HB1  1 
ATOM   4716 H  HB2  . ALA   B 1 52  ? 54.455 -26.346 -1.710  1.00 16.35 ?  52  ALA   B HB2  1 
ATOM   4717 H  HB3  . ALA   B 1 52  ? 53.384 -25.264 -2.166  1.00 16.35 ?  52  ALA   B HB3  1 
ATOM   4718 N  N    . LEU   B 1 53  ? 53.801 -22.370 -1.796  1.00 11.68 ?  53  LEU   B N    1 
ATOM   4719 C  CA   . LEU   B 1 53  ? 53.697 -21.030 -2.369  1.00 12.03 ?  53  LEU   B CA   1 
ATOM   4720 C  C    . LEU   B 1 53  ? 54.708 -20.090 -1.722  1.00 11.69 ?  53  LEU   B C    1 
ATOM   4721 O  O    . LEU   B 1 53  ? 55.412 -19.340 -2.410  1.00 12.44 ?  53  LEU   B O    1 
ATOM   4722 C  CB   . LEU   B 1 53  ? 52.276 -20.480 -2.207  1.00 12.58 ?  53  LEU   B CB   1 
ATOM   4723 C  CG   . LEU   B 1 53  ? 51.136 -21.206 -2.930  1.00 12.46 ?  53  LEU   B CG   1 
ATOM   4724 C  CD1  . LEU   B 1 53  ? 49.785 -20.605 -2.562  1.00 14.07 ?  53  LEU   B CD1  1 
ATOM   4725 C  CD2  . LEU   B 1 53  ? 51.328 -21.198 -4.442  1.00 14.43 ?  53  LEU   B CD2  1 
ATOM   4726 H  H    . LEU   B 1 53  ? 53.089 -22.654 -1.406  1.00 14.13 ?  53  LEU   B H    1 
ATOM   4727 H  HA   . LEU   B 1 53  ? 53.896 -21.076 -3.321  1.00 14.55 ?  53  LEU   B HA   1 
ATOM   4728 H  HB2  . LEU   B 1 53  ? 52.062 -20.487 -1.265  1.00 15.22 ?  53  LEU   B HB2  1 
ATOM   4729 H  HB3  . LEU   B 1 53  ? 52.274 -19.565 -2.529  1.00 15.22 ?  53  LEU   B HB3  1 
ATOM   4730 H  HG   . LEU   B 1 53  ? 51.126 -22.130 -2.643  1.00 15.07 ?  53  LEU   B HG   1 
ATOM   4731 H  HD11 . LEU   B 1 53  ? 49.084 -21.090 -3.030  1.00 17.00 ?  53  LEU   B HD11 1 
ATOM   4732 H  HD12 . LEU   B 1 53  ? 49.654 -20.688 -1.602  1.00 17.00 ?  53  LEU   B HD12 1 
ATOM   4733 H  HD13 . LEU   B 1 53  ? 49.769 -19.672 -2.818  1.00 17.00 ?  53  LEU   B HD13 1 
ATOM   4734 H  HD21 . LEU   B 1 53  ? 50.627 -21.730 -4.852  1.00 17.43 ?  53  LEU   B HD21 1 
ATOM   4735 H  HD22 . LEU   B 1 53  ? 51.277 -20.285 -4.763  1.00 17.43 ?  53  LEU   B HD22 1 
ATOM   4736 H  HD23 . LEU   B 1 53  ? 52.194 -21.578 -4.654  1.00 17.43 ?  53  LEU   B HD23 1 
ATOM   4737 N  N    . ASN   B 1 54  ? 54.797 -20.116 -0.396  1.00 11.24 ?  54  ASN   B N    1 
ATOM   4738 C  CA   . ASN   B 1 54  ? 55.710 -19.203 0.275   1.00 12.25 ?  54  ASN   B CA   1 
ATOM   4739 C  C    . ASN   B 1 54  ? 57.157 -19.482 -0.118  1.00 12.42 ?  54  ASN   B C    1 
ATOM   4740 O  O    . ASN   B 1 54  ? 57.940 -18.549 -0.347  1.00 12.78 ?  54  ASN   B O    1 
ATOM   4741 C  CB   . ASN   B 1 54  ? 55.544 -19.279 1.786   1.00 12.90 ?  54  ASN   B CB   1 
ATOM   4742 C  CG   . ASN   B 1 54  ? 56.519 -18.364 2.501   1.00 13.08 ?  54  ASN   B CG   1 
ATOM   4743 O  OD1  . ASN   B 1 54  ? 56.535 -17.154 2.259   1.00 13.28 ?  54  ASN   B OD1  1 
ATOM   4744 N  ND2  . ASN   B 1 54  ? 57.358 -18.936 3.359   1.00 14.55 ?  54  ASN   B ND2  1 
ATOM   4745 H  H    . ASN   B 1 54  ? 54.351 -20.642 0.122   1.00 13.60 ?  54  ASN   B H    1 
ATOM   4746 H  HA   . ASN   B 1 54  ? 55.498 -18.299 0.001   1.00 14.82 ?  54  ASN   B HA   1 
ATOM   4747 H  HB2  . ASN   B 1 54  ? 54.642 -19.005 2.026   1.00 15.59 ?  54  ASN   B HB2  1 
ATOM   4748 H  HB3  . ASN   B 1 54  ? 55.706 -20.187 2.085   1.00 15.59 ?  54  ASN   B HB3  1 
ATOM   4749 H  HD21 . ASN   B 1 54  ? 57.932 -18.456 3.785   1.00 17.57 ?  54  ASN   B HD21 1 
ATOM   4750 H  HD22 . ASN   B 1 54  ? 57.326 -19.786 3.496   1.00 17.57 ?  54  ASN   B HD22 1 
ATOM   4751 N  N    . LYS   B 1 55  ? 57.540 -20.761 -0.179  1.00 13.00 ?  55  LYS   B N    1 
ATOM   4752 C  CA   . LYS   B 1 55  ? 58.893 -21.106 -0.599  1.00 14.18 ?  55  LYS   B CA   1 
ATOM   4753 C  C    . LYS   B 1 55  ? 59.187 -20.564 -1.991  1.00 13.80 ?  55  LYS   B C    1 
ATOM   4754 O  O    . LYS   B 1 55  ? 60.287 -20.059 -2.246  1.00 14.63 ?  55  LYS   B O    1 
ATOM   4755 C  CB   . LYS   B 1 55  ? 59.084 -22.623 -0.552  1.00 15.75 ?  55  LYS   B CB   1 
ATOM   4756 C  CG   . LYS   B 1 55  ? 60.455 -23.093 -1.007  1.00 19.70 ?  55  LYS   B CG   1 
ATOM   4757 C  CD   . LYS   B 1 55  ? 60.622 -24.591 -0.817  1.00 23.04 ?  55  LYS   B CD   1 
ATOM   4758 C  CE   . LYS   B 1 55  ? 60.733 -24.966 0.660   1.00 25.65 ?  55  LYS   B CE   1 
ATOM   4759 N  NZ   . LYS   B 1 55  ? 61.101 -26.389 0.851   1.00 27.21 ?  55  LYS   B NZ   1 
ATOM   4760 H  H    . LYS   B 1 55  ? 57.033 -21.433 0.004   1.00 15.72 ?  55  LYS   B H    1 
ATOM   4761 H  HA   . LYS   B 1 55  ? 59.522 -20.703 0.014   1.00 17.13 ?  55  LYS   B HA   1 
ATOM   4762 H  HB2  . LYS   B 1 55  ? 58.955 -22.918 0.363   1.00 19.02 ?  55  LYS   B HB2  1 
ATOM   4763 H  HB3  . LYS   B 1 55  ? 58.423 -23.040 -1.126  1.00 19.02 ?  55  LYS   B HB3  1 
ATOM   4764 H  HG2  . LYS   B 1 55  ? 60.567 -22.894 -1.950  1.00 23.75 ?  55  LYS   B HG2  1 
ATOM   4765 H  HG3  . LYS   B 1 55  ? 61.138 -22.641 -0.486  1.00 23.75 ?  55  LYS   B HG3  1 
ATOM   4766 H  HD2  . LYS   B 1 55  ? 59.853 -25.052 -1.189  1.00 27.76 ?  55  LYS   B HD2  1 
ATOM   4767 H  HD3  . LYS   B 1 55  ? 61.434 -24.885 -1.262  1.00 27.76 ?  55  LYS   B HD3  1 
ATOM   4768 H  HE2  . LYS   B 1 55  ? 61.414 -24.409 1.074   1.00 30.89 ?  55  LYS   B HE2  1 
ATOM   4769 H  HE3  . LYS   B 1 55  ? 59.874 -24.809 1.088   1.00 30.89 ?  55  LYS   B HE3  1 
ATOM   4770 H  HZ1  . LYS   B 1 55  ? 61.121 -26.580 1.719   1.00 32.77 ?  55  LYS   B HZ1  1 
ATOM   4771 H  HZ2  . LYS   B 1 55  ? 60.501 -26.910 0.452   1.00 32.77 ?  55  LYS   B HZ2  1 
ATOM   4772 H  HZ3  . LYS   B 1 55  ? 61.901 -26.543 0.499   1.00 32.77 ?  55  LYS   B HZ3  1 
ATOM   4773 N  N    . ALA   B 1 56  ? 58.214 -20.648 -2.903  1.00 13.25 ?  56  ALA   B N    1 
ATOM   4774 C  CA   . ALA   B 1 56  ? 58.437 -20.154 -4.256  1.00 14.32 ?  56  ALA   B CA   1 
ATOM   4775 C  C    . ALA   B 1 56  ? 58.717 -18.659 -4.261  1.00 14.00 ?  56  ALA   B C    1 
ATOM   4776 O  O    . ALA   B 1 56  ? 59.450 -18.170 -5.131  1.00 14.90 ?  56  ALA   B O    1 
ATOM   4777 C  CB   . ALA   B 1 56  ? 57.240 -20.481 -5.148  1.00 15.28 ?  56  ALA   B CB   1 
ATOM   4778 H  H    . ALA   B 1 56  ? 57.424 -20.967 -2.763  1.00 16.02 ?  56  ALA   B H    1 
ATOM   4779 H  HA   . ALA   B 1 56  ? 59.211 -20.595 -4.627  1.00 17.30 ?  56  ALA   B HA   1 
ATOM   4780 H  HB1  . ALA   B 1 56  ? 57.412 -20.148 -6.045  1.00 18.45 ?  56  ALA   B HB1  1 
ATOM   4781 H  HB2  . ALA   B 1 56  ? 57.120 -21.443 -5.173  1.00 18.45 ?  56  ALA   B HB2  1 
ATOM   4782 H  HB3  . ALA   B 1 56  ? 56.446 -20.058 -4.787  1.00 18.45 ?  56  ALA   B HB3  1 
ATOM   4783 N  N    . THR   B 1 57  ? 58.153 -17.920 -3.302  1.00 13.71 ?  57  THR   B N    1 
ATOM   4784 C  CA   . THR   B 1 57  ? 58.389 -16.484 -3.183  1.00 13.64 ?  57  THR   B CA   1 
ATOM   4785 C  C    . THR   B 1 57  ? 59.638 -16.152 -2.371  1.00 14.41 ?  57  THR   B C    1 
ATOM   4786 O  O    . THR   B 1 57  ? 59.882 -14.973 -2.082  1.00 14.84 ?  57  THR   B O    1 
ATOM   4787 C  CB   . THR   B 1 57  ? 57.184 -15.754 -2.553  1.00 13.06 ?  57  THR   B CB   1 
ATOM   4788 O  OG1  . THR   B 1 57  ? 57.159 -15.966 -1.135  1.00 13.63 ?  57  THR   B OG1  1 
ATOM   4789 C  CG2  . THR   B 1 57  ? 55.869 -16.181 -3.191  1.00 13.02 ?  57  THR   B CG2  1 
ATOM   4790 H  H    . THR   B 1 57  ? 57.611 -18.230 -2.708  1.00 16.57 ?  57  THR   B H    1 
ATOM   4791 H  HA   . THR   B 1 57  ? 58.509 -16.122 -4.075  1.00 16.48 ?  57  THR   B HA   1 
ATOM   4792 H  HB   . THR   B 1 57  ? 57.283 -14.805 -2.725  1.00 15.79 ?  57  THR   B HB   1 
ATOM   4793 H  HG1  . THR   B 1 57  ? 57.084 -16.787 -0.973  1.00 16.48 ?  57  THR   B HG1  1 
ATOM   4794 H  HG21 . THR   B 1 57  ? 55.141 -15.639 -2.852  1.00 15.73 ?  57  THR   B HG21 1 
ATOM   4795 H  HG22 . THR   B 1 57  ? 55.914 -16.081 -4.156  1.00 15.73 ?  57  THR   B HG22 1 
ATOM   4796 H  HG23 . THR   B 1 57  ? 55.686 -17.113 -2.986  1.00 15.73 ?  57  THR   B HG23 1 
ATOM   4797 N  N    . ASN   B 1 58  ? 60.430 -17.156 -2.003  1.00 15.19 ?  58  ASN   B N    1 
ATOM   4798 C  CA   . ASN   B 1 58  ? 61.629 -16.938 -1.199  1.00 18.34 ?  58  ASN   B CA   1 
ATOM   4799 C  C    . ASN   B 1 58  ? 61.293 -16.224 0.111   1.00 15.69 ?  58  ASN   B C    1 
ATOM   4800 O  O    . ASN   B 1 58  ? 62.036 -15.354 0.577   1.00 16.38 ?  58  ASN   B O    1 
ATOM   4801 C  CB   . ASN   B 1 58  ? 62.716 -16.196 -1.985  1.00 26.58 ?  58  ASN   B CB   1 
ATOM   4802 C  CG   . ASN   B 1 58  ? 64.094 -16.360 -1.371  1.00 36.15 ?  58  ASN   B CG   1 
ATOM   4803 O  OD1  . ASN   B 1 58  ? 64.390 -17.378 -0.744  1.00 38.79 ?  58  ASN   B OD1  1 
ATOM   4804 N  ND2  . ASN   B 1 58  ? 64.944 -15.356 -1.547  1.00 43.00 ?  58  ASN   B ND2  1 
ATOM   4805 H  H    . ASN   B 1 58  ? 60.290 -17.983 -2.207  1.00 18.34 ?  58  ASN   B H    1 
ATOM   4806 H  HA   . ASN   B 1 58  ? 61.991 -17.810 -0.975  1.00 22.12 ?  58  ASN   B HA   1 
ATOM   4807 H  HB2  . ASN   B 1 58  ? 62.750 -16.545 -2.894  1.00 32.01 ?  58  ASN   B HB2  1 
ATOM   4808 H  HB3  . ASN   B 1 58  ? 62.509 -15.251 -2.003  1.00 32.01 ?  58  ASN   B HB3  1 
ATOM   4809 H  HD21 . ASN   B 1 58  ? 65.739 -15.402 -1.220  1.00 51.72 ?  58  ASN   B HD21 1 
ATOM   4810 H  HD22 . ASN   B 1 58  ? 64.701 -14.660 -1.989  1.00 51.72 ?  58  ASN   B HD22 1 
ATOM   4811 N  N    . ASN   B 1 59  ? 60.168 -16.607 0.716   1.00 14.75 ?  59  ASN   B N    1 
ATOM   4812 C  CA   . ASN   B 1 59  ? 59.692 -16.135 2.018   1.00 14.54 ?  59  ASN   B CA   1 
ATOM   4813 C  C    . ASN   B 1 59  ? 59.098 -14.730 1.963   1.00 14.14 ?  59  ASN   B C    1 
ATOM   4814 O  O    . ASN   B 1 59  ? 58.665 -14.224 3.006   1.00 14.45 ?  59  ASN   B O    1 
ATOM   4815 C  CB   . ASN   B 1 59  ? 60.762 -16.202 3.123   1.00 15.70 ?  59  ASN   B CB   1 
ATOM   4816 C  CG   . ASN   B 1 59  ? 60.172 -16.374 4.507   1.00 16.68 ?  59  ASN   B CG   1 
ATOM   4817 O  OD1  . ASN   B 1 59  ? 59.351 -17.264 4.739   1.00 16.96 ?  59  ASN   B OD1  1 
ATOM   4818 N  ND2  . ASN   B 1 59  ? 60.585 -15.520 5.436   1.00 17.70 ?  59  ASN   B ND2  1 
ATOM   4819 H  H    . ASN   B 1 59  ? 59.629 -17.187 0.368   1.00 17.82 ?  59  ASN   B H    1 
ATOM   4820 H  HA   . ASN   B 1 59  ? 58.982 -16.731 2.296   1.00 17.56 ?  59  ASN   B HA   1 
ATOM   4821 H  HB2  . ASN   B 1 59  ? 61.349 -16.958 2.961   1.00 18.96 ?  59  ASN   B HB2  1 
ATOM   4822 H  HB3  . ASN   B 1 59  ? 61.273 -15.379 3.125   1.00 18.96 ?  59  ASN   B HB3  1 
ATOM   4823 H  HD21 . ASN   B 1 59  ? 60.276 -15.574 6.239   1.00 21.35 ?  59  ASN   B HD21 1 
ATOM   4824 H  HD22 . ASN   B 1 59  ? 61.153 -14.909 5.236   1.00 21.35 ?  59  ASN   B HD22 1 
ATOM   4825 N  N    . ALA   B 1 60  ? 59.035 -14.091 0.792   1.00 13.92 ?  60  ALA   B N    1 
ATOM   4826 C  CA   . ALA   B 1 60  ? 58.440 -12.757 0.714   1.00 13.95 ?  60  ALA   B CA   1 
ATOM   4827 C  C    . ALA   B 1 60  ? 56.969 -12.779 1.109   1.00 13.17 ?  60  ALA   B C    1 
ATOM   4828 O  O    . ALA   B 1 60  ? 56.464 -11.825 1.715   1.00 13.65 ?  60  ALA   B O    1 
ATOM   4829 C  CB   . ALA   B 1 60  ? 58.606 -12.179 -0.691  1.00 15.01 ?  60  ALA   B CB   1 
ATOM   4830 H  H    . ALA   B 1 60  ? 59.324 -14.407 0.044   1.00 16.82 ?  60  ALA   B H    1 
ATOM   4831 H  HA   . ALA   B 1 60  ? 58.903 -12.177 1.334   1.00 16.85 ?  60  ALA   B HA   1 
ATOM   4832 H  HB1  . ALA   B 1 60  ? 58.207 -11.299 -0.716  1.00 18.13 ?  60  ALA   B HB1  1 
ATOM   4833 H  HB2  . ALA   B 1 60  ? 59.554 -12.122 -0.898  1.00 18.13 ?  60  ALA   B HB2  1 
ATOM   4834 H  HB3  . ALA   B 1 60  ? 58.166 -12.765 -1.328  1.00 18.13 ?  60  ALA   B HB3  1 
ATOM   4835 N  N    . MET   B 1 61  ? 56.262 -13.857 0.764   1.00 12.54 ?  61  MET   B N    1 
ATOM   4836 C  CA   . MET   B 1 61  ? 54.866 -13.978 1.158   1.00 12.17 ?  61  MET   B CA   1 
ATOM   4837 C  C    . MET   B 1 61  ? 54.726 -13.985 2.680   1.00 12.07 ?  61  MET   B C    1 
ATOM   4838 O  O    . MET   B 1 61  ? 53.821 -13.341 3.231   1.00 11.90 ?  61  MET   B O    1 
ATOM   4839 C  CB   . MET   B 1 61  ? 54.285 -15.248 0.532   1.00 12.13 ?  61  MET   B CB   1 
ATOM   4840 C  CG   . MET   B 1 61  ? 52.848 -15.546 0.952   1.00 11.80 ?  61  MET   B CG   1 
ATOM   4841 S  SD   . MET   B 1 61  ? 52.201 -17.048 0.178   1.00 12.38 ?  61  MET   B SD   1 
ATOM   4842 C  CE   . MET   B 1 61  ? 51.923 -16.441 -1.482  1.00 13.59 ?  61  MET   B CE   1 
ATOM   4843 H  H    . MET   B 1 61  ? 56.567 -14.527 0.307   1.00 15.16 ?  61  MET   B H    1 
ATOM   4844 H  HA   . MET   B 1 61  ? 54.375 -13.226 0.796   1.00 14.72 ?  61  MET   B HA   1 
ATOM   4845 H  HB2  . MET   B 1 61  ? 54.289 -15.155 -0.436  1.00 14.67 ?  61  MET   B HB2  1 
ATOM   4846 H  HB3  . MET   B 1 61  ? 54.829 -16.007 0.789   1.00 14.67 ?  61  MET   B HB3  1 
ATOM   4847 H  HG2  . MET   B 1 61  ? 52.818 -15.677 1.916   1.00 14.28 ?  61  MET   B HG2  1 
ATOM   4848 H  HG3  . MET   B 1 61  ? 52.280 -14.802 0.702   1.00 14.28 ?  61  MET   B HG3  1 
ATOM   4849 H  HE1  . MET   B 1 61  ? 51.534 -17.151 -2.015  1.00 16.43 ?  61  MET   B HE1  1 
ATOM   4850 H  HE2  . MET   B 1 61  ? 51.312 -15.684 -1.446  1.00 16.43 ?  61  MET   B HE2  1 
ATOM   4851 H  HE3  . MET   B 1 61  ? 52.768 -16.161 -1.866  1.00 16.43 ?  61  MET   B HE3  1 
ATOM   4852 N  N    . GLN   B 1 62  ? 55.607 -14.704 3.382   1.00 12.46 ?  62  GLN   B N    1 
ATOM   4853 C  CA   . GLN   B 1 62  ? 55.498 -14.762 4.836   1.00 12.81 ?  62  GLN   B CA   1 
ATOM   4854 C  C    . GLN   B 1 62  ? 55.781 -13.407 5.471   1.00 12.77 ?  62  GLN   B C    1 
ATOM   4855 O  O    . GLN   B 1 62  ? 55.089 -13.003 6.412   1.00 13.24 ?  62  GLN   B O    1 
ATOM   4856 C  CB   . GLN   B 1 62  ? 56.443 -15.822 5.403   1.00 13.01 ?  62  GLN   B CB   1 
ATOM   4857 C  CG   . GLN   B 1 62  ? 56.225 -16.076 6.882   1.00 13.27 ?  62  GLN   B CG   1 
ATOM   4858 C  CD   . GLN   B 1 62  ? 54.850 -16.668 7.134   1.00 12.73 ?  62  GLN   B CD   1 
ATOM   4859 O  OE1  . GLN   B 1 62  ? 54.591 -17.823 6.781   1.00 13.00 ?  62  GLN   B OE1  1 
ATOM   4860 N  NE2  . GLN   B 1 62  ? 53.944 -15.871 7.697   1.00 13.02 ?  62  GLN   B NE2  1 
ATOM   4861 H  H    . GLN   B 1 62  ? 56.258 -15.154 3.043   1.00 15.07 ?  62  GLN   B H    1 
ATOM   4862 H  HA   . GLN   B 1 62  ? 54.589 -15.017 5.066   1.00 15.49 ?  62  GLN   B HA   1 
ATOM   4863 H  HB2  . GLN   B 1 62  ? 56.305 -16.659 4.934   1.00 15.73 ?  62  GLN   B HB2  1 
ATOM   4864 H  HB3  . GLN   B 1 62  ? 57.360 -15.523 5.282   1.00 15.73 ?  62  GLN   B HB3  1 
ATOM   4865 H  HG2  . GLN   B 1 62  ? 56.894 -16.704 7.199   1.00 16.04 ?  62  GLN   B HG2  1 
ATOM   4866 H  HG3  . GLN   B 1 62  ? 56.297 -15.239 7.369   1.00 16.04 ?  62  GLN   B HG3  1 
ATOM   4867 H  HE21 . GLN   B 1 62  ? 54.158 -15.065 7.912   1.00 15.74 ?  62  GLN   B HE21 1 
ATOM   4868 H  HE22 . GLN   B 1 62  ? 53.153 -16.163 7.849   1.00 15.74 ?  62  GLN   B HE22 1 
ATOM   4869 N  N    . VAL   B 1 63  ? 56.797 -12.695 4.982   1.00 13.22 ?  63  VAL   B N    1 
ATOM   4870 C  CA   . VAL   B 1 63  ? 57.102 -11.377 5.536   1.00 14.30 ?  63  VAL   B CA   1 
ATOM   4871 C  C    . VAL   B 1 63  ? 55.913 -10.442 5.349   1.00 13.64 ?  63  VAL   B C    1 
ATOM   4872 O  O    . VAL   B 1 63  ? 55.501 -9.726  6.275   1.00 14.36 ?  63  VAL   B O    1 
ATOM   4873 C  CB   . VAL   B 1 63  ? 58.394 -10.820 4.913   1.00 15.71 ?  63  VAL   B CB   1 
ATOM   4874 C  CG1  . VAL   B 1 63  ? 58.622 -9.376  5.349   1.00 16.25 ?  63  VAL   B CG1  1 
ATOM   4875 C  CG2  . VAL   B 1 63  ? 59.574 -11.694 5.314   1.00 16.37 ?  63  VAL   B CG2  1 
ATOM   4876 H  H    . VAL   B 1 63  ? 57.309 -12.947 4.335   1.00 15.98 ?  63  VAL   B H    1 
ATOM   4877 H  HA   . VAL   B 1 63  ? 57.253 -11.475 6.484   1.00 17.27 ?  63  VAL   B HA   1 
ATOM   4878 H  HB   . VAL   B 1 63  ? 58.327 -10.844 3.946   1.00 18.96 ?  63  VAL   B HB   1 
ATOM   4879 H  HG11 . VAL   B 1 63  ? 59.540 -9.131  5.160   1.00 19.62 ?  63  VAL   B HG11 1 
ATOM   4880 H  HG12 . VAL   B 1 63  ? 58.017 -8.802  4.857   1.00 19.62 ?  63  VAL   B HG12 1 
ATOM   4881 H  HG13 . VAL   B 1 63  ? 58.450 -9.307  6.301   1.00 19.62 ?  63  VAL   B HG13 1 
ATOM   4882 H  HG21 . VAL   B 1 63  ? 60.388 -11.321 4.938   1.00 19.76 ?  63  VAL   B HG21 1 
ATOM   4883 H  HG22 . VAL   B 1 63  ? 59.640 -11.709 6.285   1.00 19.76 ?  63  VAL   B HG22 1 
ATOM   4884 H  HG23 . VAL   B 1 63  ? 59.437 -12.593 4.980   1.00 19.76 ?  63  VAL   B HG23 1 
ATOM   4885 N  N    . GLU   B 1 64  ? 55.346 -10.433 4.143   1.00 13.00 ?  64  GLU   B N    1 
ATOM   4886 C  CA   . GLU   B 1 64  ? 54.183 -9.595  3.867   1.00 12.64 ?  64  GLU   B CA   1 
ATOM   4887 C  C    . GLU   B 1 64  ? 52.996 -9.996  4.739   1.00 12.02 ?  64  GLU   B C    1 
ATOM   4888 O  O    . GLU   B 1 64  ? 52.250 -9.137  5.237   1.00 12.57 ?  64  GLU   B O    1 
ATOM   4889 C  CB   . GLU   B 1 64  ? 53.826 -9.737  2.387   1.00 12.80 ?  64  GLU   B CB   1 
ATOM   4890 C  CG   . GLU   B 1 64  ? 52.559 -9.003  1.950   1.00 13.19 ?  64  GLU   B CG   1 
ATOM   4891 C  CD   . GLU   B 1 64  ? 52.027 -9.504  0.613   1.00 13.65 ?  64  GLU   B CD   1 
ATOM   4892 O  OE1  . GLU   B 1 64  ? 52.192 -10.716 0.304   1.00 14.52 ?  64  GLU   B OE1  1 
ATOM   4893 O  OE2  . GLU   B 1 64  ? 51.409 -8.693  -0.118  1.00 14.61 -1 64  GLU   B OE2  1 
ATOM   4894 H  H    . GLU   B 1 64  ? 55.611 -10.904 3.467   1.00 15.71 ?  64  GLU   B H    1 
ATOM   4895 H  HA   . GLU   B 1 64  ? 54.399 -8.668  4.044   1.00 15.28 ?  64  GLU   B HA   1 
ATOM   4896 H  HB2  . GLU   B 1 64  ? 54.554 -9.381  1.853   1.00 15.47 ?  64  GLU   B HB2  1 
ATOM   4897 H  HB3  . GLU   B 1 64  ? 53.700 -10.673 2.184   1.00 15.47 ?  64  GLU   B HB3  1 
ATOM   4898 H  HG2  . GLU   B 1 64  ? 51.857 -9.132  2.613   1.00 15.95 ?  64  GLU   B HG2  1 
ATOM   4899 H  HG3  . GLU   B 1 64  ? 52.753 -8.057  1.862   1.00 15.95 ?  64  GLU   B HG3  1 
ATOM   4900 N  N    . SER   B 1 65  ? 52.810 -11.301 4.929   1.00 12.16 ?  65  SER   B N    1 
ATOM   4901 C  CA   . SER   B 1 65  ? 51.702 -11.807 5.728   1.00 12.22 ?  65  SER   B CA   1 
ATOM   4902 C  C    . SER   B 1 65  ? 51.834 -11.405 7.190   1.00 12.42 ?  65  SER   B C    1 
ATOM   4903 O  O    . SER   B 1 65  ? 50.834 -11.037 7.825   1.00 12.74 ?  65  SER   B O    1 
ATOM   4904 C  CB   . SER   B 1 65  ? 51.629 -13.328 5.598   1.00 12.50 ?  65  SER   B CB   1 
ATOM   4905 O  OG   . SER   B 1 65  ? 51.276 -13.725 4.281   1.00 12.51 ?  65  SER   B OG   1 
ATOM   4906 H  H    . SER   B 1 65  ? 53.316 -11.919 4.606   1.00 14.70 ?  65  SER   B H    1 
ATOM   4907 H  HA   . SER   B 1 65  ? 50.871 -11.436 5.390   1.00 14.78 ?  65  SER   B HA   1 
ATOM   4908 H  HB2  . SER   B 1 65  ? 52.491 -13.705 5.816   1.00 15.11 ?  65  SER   B HB2  1 
ATOM   4909 H  HB3  . SER   B 1 65  ? 50.955 -13.661 6.217   1.00 15.11 ?  65  SER   B HB3  1 
ATOM   4910 H  HG   . SER   B 1 65  ? 51.842 -13.431 3.731   1.00 15.13 ?  65  SER   B HG   1 
ATOM   4911 N  N    . ASP   B 1 66  ? 53.041 -11.507 7.758   1.00 12.96 ?  66  ASP   B N    1 
ATOM   4912 C  CA   . ASP   B 1 66  ? 53.223 -11.117 9.153   1.00 13.00 ?  66  ASP   B CA   1 
ATOM   4913 C  C    . ASP   B 1 66  ? 52.913 -9.638  9.349   1.00 12.95 ?  66  ASP   B C    1 
ATOM   4914 O  O    . ASP   B 1 66  ? 52.342 -9.244  10.373  1.00 13.59 ?  66  ASP   B O    1 
ATOM   4915 C  CB   . ASP   B 1 66  ? 54.650 -11.429 9.615   1.00 14.06 ?  66  ASP   B CB   1 
ATOM   4916 C  CG   . ASP   B 1 66  ? 54.913 -12.921 9.782   1.00 15.96 ?  66  ASP   B CG   1 
ATOM   4917 O  OD1  . ASP   B 1 66  ? 53.959 -13.730 9.712   1.00 16.70 ?  66  ASP   B OD1  1 
ATOM   4918 O  OD2  . ASP   B 1 66  ? 56.094 -13.286 9.999   1.00 18.72 -1 66  ASP   B OD2  1 
ATOM   4919 H  H    . ASP   B 1 66  ? 53.745 -11.803 7.370   1.00 15.66 ?  66  ASP   B H    1 
ATOM   4920 H  HA   . ASP   B 1 66  ? 52.613 -11.619 9.713   1.00 15.71 ?  66  ASP   B HA   1 
ATOM   4921 H  HB2  . ASP   B 1 66  ? 55.278 -11.093 8.960   1.00 16.99 ?  66  ASP   B HB2  1 
ATOM   4922 H  HB3  . ASP   B 1 66  ? 54.807 -11.000 10.475  1.00 16.99 ?  66  ASP   B HB3  1 
ATOM   4923 N  N    . ASP   B 1 67  ? 53.298 -8.797  8.387   1.00 12.91 ?  67  ASP   B N    1 
ATOM   4924 C  CA   . ASP   B 1 67  ? 52.951 -7.385  8.468   1.00 13.36 ?  67  ASP   B CA   1 
ATOM   4925 C  C    . ASP   B 1 67  ? 51.439 -7.178  8.393   1.00 13.70 ?  67  ASP   B C    1 
ATOM   4926 O  O    . ASP   B 1 67  ? 50.880 -6.369  9.144   1.00 14.29 ?  67  ASP   B O    1 
ATOM   4927 C  CB   . ASP   B 1 67  ? 53.662 -6.616  7.361   1.00 14.76 ?  67  ASP   B CB   1 
ATOM   4928 C  CG   . ASP   B 1 67  ? 53.238 -5.174  7.313   1.00 16.27 ?  67  ASP   B CG   1 
ATOM   4929 O  OD1  . ASP   B 1 67  ? 53.735 -4.359  8.124   1.00 17.87 ?  67  ASP   B OD1  1 
ATOM   4930 O  OD2  . ASP   B 1 67  ? 52.374 -4.873  6.475   1.00 17.16 -1 67  ASP   B OD2  1 
ATOM   4931 H  H    . ASP   B 1 67  ? 53.758 -9.017  7.695   1.00 15.60 ?  67  ASP   B H    1 
ATOM   4932 H  HA   . ASP   B 1 67  ? 53.256 -7.030  9.317   1.00 16.15 ?  67  ASP   B HA   1 
ATOM   4933 H  HB2  . ASP   B 1 67  ? 54.622 -6.649  7.515   1.00 17.83 ?  67  ASP   B HB2  1 
ATOM   4934 H  HB3  . ASP   B 1 67  ? 53.455 -7.028  6.503   1.00 17.83 ?  67  ASP   B HB3  1 
ATOM   4935 N  N    . TYR   B 1 68  ? 50.757 -7.907  7.500   1.00 13.28 ?  68  TYR   B N    1 
ATOM   4936 C  CA   . TYR   B 1 68  ? 49.300 -7.821  7.428   1.00 14.17 ?  68  TYR   B CA   1 
ATOM   4937 C  C    . TYR   B 1 68  ? 48.663 -8.163  8.772   1.00 13.59 ?  68  TYR   B C    1 
ATOM   4938 O  O    . TYR   B 1 68  ? 47.731 -7.482  9.219   1.00 14.30 ?  68  TYR   B O    1 
ATOM   4939 C  CB   . TYR   B 1 68  ? 48.764 -8.749  6.329   1.00 14.96 ?  68  TYR   B CB   1 
ATOM   4940 C  CG   . TYR   B 1 68  ? 47.260 -8.899  6.387   1.00 15.86 ?  68  TYR   B CG   1 
ATOM   4941 C  CD1  . TYR   B 1 68  ? 46.671 -9.859  7.202   1.00 16.68 ?  68  TYR   B CD1  1 
ATOM   4942 C  CD2  . TYR   B 1 68  ? 46.430 -8.060  5.660   1.00 16.84 ?  68  TYR   B CD2  1 
ATOM   4943 C  CE1  . TYR   B 1 68  ? 45.305 -9.982  7.291   1.00 17.68 ?  68  TYR   B CE1  1 
ATOM   4944 C  CE2  . TYR   B 1 68  ? 45.047 -8.188  5.735   1.00 17.20 ?  68  TYR   B CE2  1 
ATOM   4945 C  CZ   . TYR   B 1 68  ? 44.504 -9.147  6.554   1.00 17.69 ?  68  TYR   B CZ   1 
ATOM   4946 O  OH   . TYR   B 1 68  ? 43.136 -9.266  6.642   1.00 18.90 ?  68  TYR   B OH   1 
ATOM   4947 H  H    . TYR   B 1 68  ? 51.115 -8.459  6.937   1.00 16.05 ?  68  TYR   B H    1 
ATOM   4948 H  HA   . TYR   B 1 68  ? 49.055 -6.914  7.201   1.00 17.12 ?  68  TYR   B HA   1 
ATOM   4949 H  HB2  . TYR   B 1 68  ? 48.992 -8.381  5.464   1.00 18.07 ?  68  TYR   B HB2  1 
ATOM   4950 H  HB3  . TYR   B 1 68  ? 49.155 -9.629  6.435   1.00 18.07 ?  68  TYR   B HB3  1 
ATOM   4951 H  HD1  . TYR   B 1 68  ? 47.209 -10.430 7.704   1.00 20.13 ?  68  TYR   B HD1  1 
ATOM   4952 H  HD2  . TYR   B 1 68  ? 46.800 -7.404  5.119   1.00 20.33 ?  68  TYR   B HD2  1 
ATOM   4953 H  HE1  . TYR   B 1 68  ? 44.919 -10.642 7.830   1.00 21.34 ?  68  TYR   B HE1  1 
ATOM   4954 H  HE2  . TYR   B 1 68  ? 44.491 -7.621  5.248   1.00 20.76 ?  68  TYR   B HE2  1 
ATOM   4955 H  HH   . TYR   B 1 68  ? 42.750 -8.708  6.136   1.00 22.79 ?  68  TYR   B HH   1 
ATOM   4956 N  N    . ILE   B 1 69  ? 49.140 -9.231  9.420   1.00 13.25 ?  69  ILE   B N    1 
ATOM   4957 C  CA   . ILE   B 1 69  ? 48.577 -9.654  10.700  1.00 14.24 ?  69  ILE   B CA   1 
ATOM   4958 C  C    . ILE   B 1 69  ? 48.837 -8.610  11.780  1.00 13.84 ?  69  ILE   B C    1 
ATOM   4959 O  O    . ILE   B 1 69  ? 47.971 -8.335  12.617  1.00 14.12 ?  69  ILE   B O    1 
ATOM   4960 C  CB   . ILE   B 1 69  ? 49.149 -11.031 11.092  1.00 15.03 ?  69  ILE   B CB   1 
ATOM   4961 C  CG1  . ILE   B 1 69  ? 48.622 -12.132 10.163  1.00 15.50 ?  69  ILE   B CG1  1 
ATOM   4962 C  CG2  . ILE   B 1 69  ? 48.856 -11.346 12.554  1.00 15.96 ?  69  ILE   B CG2  1 
ATOM   4963 C  CD1  . ILE   B 1 69  ? 47.151 -12.453 10.330  1.00 15.91 ?  69  ILE   B CD1  1 
ATOM   4964 H  H    . ILE   B 1 69  ? 49.786 -9.722  9.141   1.00 16.02 ?  69  ILE   B H    1 
ATOM   4965 H  HA   . ILE   B 1 69  ? 47.616 -9.747  10.601  1.00 17.20 ?  69  ILE   B HA   1 
ATOM   4966 H  HB   . ILE   B 1 69  ? 50.113 -10.989 10.988  1.00 18.15 ?  69  ILE   B HB   1 
ATOM   4967 H  HG12 . ILE   B 1 69  ? 48.765 -11.851 9.244   1.00 18.72 ?  69  ILE   B HG12 1 
ATOM   4968 H  HG13 . ILE   B 1 69  ? 49.127 -12.944 10.335  1.00 18.72 ?  69  ILE   B HG13 1 
ATOM   4969 H  HG21 . ILE   B 1 69  ? 48.991 -12.296 12.702  1.00 19.27 ?  69  ILE   B HG21 1 
ATOM   4970 H  HG22 . ILE   B 1 69  ? 49.459 -10.839 13.120  1.00 19.27 ?  69  ILE   B HG22 1 
ATOM   4971 H  HG23 . ILE   B 1 69  ? 47.936 -11.111 12.751  1.00 19.27 ?  69  ILE   B HG23 1 
ATOM   4972 H  HD11 . ILE   B 1 69  ? 46.916 -13.149 9.698   1.00 19.20 ?  69  ILE   B HD11 1 
ATOM   4973 H  HD12 . ILE   B 1 69  ? 46.997 -12.760 11.235  1.00 19.20 ?  69  ILE   B HD12 1 
ATOM   4974 H  HD13 . ILE   B 1 69  ? 46.632 -11.655 10.153  1.00 19.20 ?  69  ILE   B HD13 1 
ATOM   4975 N  N    . ALA   B 1 70  ? 50.037 -8.028  11.803  1.00 13.83 ?  70  ALA   B N    1 
ATOM   4976 C  CA   . ALA   B 1 70  ? 50.321 -6.988  12.786  1.00 13.46 ?  70  ALA   B CA   1 
ATOM   4977 C  C    . ALA   B 1 70  ? 49.320 -5.845  12.679  1.00 13.94 ?  70  ALA   B C    1 
ATOM   4978 O  O    . ALA   B 1 70  ? 48.880 -5.298  13.695  1.00 14.40 ?  70  ALA   B O    1 
ATOM   4979 C  CB   . ALA   B 1 70  ? 51.747 -6.473  12.603  1.00 14.04 ?  70  ALA   B CB   1 
ATOM   4980 H  H    . ALA   B 1 70  ? 50.677 -8.217  11.273  1.00 16.71 ?  70  ALA   B H    1 
ATOM   4981 H  HA   . ALA   B 1 70  ? 50.249 -7.364  13.676  1.00 16.27 ?  70  ALA   B HA   1 
ATOM   4982 H  HB1  . ALA   B 1 70  ? 51.935 -5.811  13.288  1.00 16.96 ?  70  ALA   B HB1  1 
ATOM   4983 H  HB2  . ALA   B 1 70  ? 52.366 -7.217  12.689  1.00 16.96 ?  70  ALA   B HB2  1 
ATOM   4984 H  HB3  . ALA   B 1 70  ? 51.833 -6.074  11.724  1.00 16.96 ?  70  ALA   B HB3  1 
ATOM   4985 N  N    . THR   B 1 71  ? 48.945 -5.478  11.455  1.00 14.46 ?  71  THR   B N    1 
ATOM   4986 C  CA   . THR   B 1 71  ? 48.051 -4.346  11.247  1.00 15.48 ?  71  THR   B CA   1 
ATOM   4987 C  C    . THR   B 1 71  ? 46.584 -4.716  11.451  1.00 16.10 ?  71  THR   B C    1 
ATOM   4988 O  O    . THR   B 1 71  ? 45.799 -3.900  11.958  1.00 17.49 ?  71  THR   B O    1 
ATOM   4989 C  CB   . THR   B 1 71  ? 48.271 -3.777  9.841   1.00 17.27 ?  71  THR   B CB   1 
ATOM   4990 O  OG1  . THR   B 1 71  ? 49.589 -3.227  9.749   1.00 19.33 ?  71  THR   B OG1  1 
ATOM   4991 C  CG2  . THR   B 1 71  ? 47.246 -2.700  9.510   1.00 18.05 ?  71  THR   B CG2  1 
ATOM   4992 H  H    . THR   B 1 71  ? 49.203 -5.865  10.730  1.00 17.46 ?  71  THR   B H    1 
ATOM   4993 H  HA   . THR   B 1 71  ? 48.271 -3.648  11.881  1.00 18.69 ?  71  THR   B HA   1 
ATOM   4994 H  HB   . THR   B 1 71  ? 48.190 -4.484  9.185   1.00 20.83 ?  71  THR   B HB   1 
ATOM   4995 H  HG1  . THR   B 1 71  ? 49.720 -2.892  8.984   1.00 23.31 ?  71  THR   B HG1  1 
ATOM   4996 H  HG21 . THR   B 1 71  ? 47.549 -2.172  8.751   1.00 21.78 ?  71  THR   B HG21 1 
ATOM   4997 H  HG22 . THR   B 1 71  ? 46.395 -3.104  9.290   1.00 21.78 ?  71  THR   B HG22 1 
ATOM   4998 H  HG23 . THR   B 1 71  ? 47.130 -2.106  10.271  1.00 21.78 ?  71  THR   B HG23 1 
ATOM   4999 N  N    . ASN   B 1 72  ? 46.193 -5.932  11.059  1.00 15.91 ?  72  ASN   B N    1 
ATOM   5000 C  CA   . ASN   B 1 72  ? 44.790 -6.295  10.937  1.00 16.06 ?  72  ASN   B CA   1 
ATOM   5001 C  C    . ASN   B 1 72  ? 44.324 -7.390  11.885  1.00 16.44 ?  72  ASN   B C    1 
ATOM   5002 O  O    . ASN   B 1 72  ? 43.108 -7.542  12.060  1.00 17.93 ?  72  ASN   B O    1 
ATOM   5003 C  CB   . ASN   B 1 72  ? 44.477 -6.725  9.495   1.00 17.08 ?  72  ASN   B CB   1 
ATOM   5004 C  CG   . ASN   B 1 72  ? 44.750 -5.622  8.497   1.00 17.96 ?  72  ASN   B CG   1 
ATOM   5005 O  OD1  . ASN   B 1 72  ? 45.761 -5.630  7.787   1.00 18.91 ?  72  ASN   B OD1  1 
ATOM   5006 N  ND2  . ASN   B 1 72  ? 43.870 -4.641  8.464   1.00 19.62 ?  72  ASN   B ND2  1 
ATOM   5007 H  H    . ASN   B 1 72  ? 46.737 -6.578  10.856  1.00 19.21 ?  72  ASN   B H    1 
ATOM   5008 H  HA   . ASN   B 1 72  ? 44.258 -5.509  11.124  1.00 19.39 ?  72  ASN   B HA   1 
ATOM   5009 H  HB2  . ASN   B 1 72  ? 45.035 -7.486  9.263   1.00 20.61 ?  72  ASN   B HB2  1 
ATOM   5010 H  HB3  . ASN   B 1 72  ? 43.542 -6.965  9.432   1.00 20.61 ?  72  ASN   B HB3  1 
ATOM   5011 H  HD21 . ASN   B 1 72  ? 43.975 -3.985  7.916   1.00 23.66 ?  72  ASN   B HD21 1 
ATOM   5012 H  HD22 . ASN   B 1 72  ? 43.178 -4.662  8.976   1.00 23.66 ?  72  ASN   B HD22 1 
ATOM   5013 N  N    . GLY   B 1 73  ? 45.227 -8.149  12.497  1.00 16.02 ?  73  GLY   B N    1 
ATOM   5014 C  CA   . GLY   B 1 73  ? 44.828 -9.287  13.290  1.00 15.44 ?  73  GLY   B CA   1 
ATOM   5015 C  C    . GLY   B 1 73  ? 44.459 -10.471 12.423  1.00 14.41 ?  73  GLY   B C    1 
ATOM   5016 O  O    . GLY   B 1 73  ? 44.442 -10.386 11.192  1.00 14.24 ?  73  GLY   B O    1 
ATOM   5017 H  H    . GLY   B 1 73  ? 46.079 -8.019  12.467  1.00 19.34 ?  73  GLY   B H    1 
ATOM   5018 H  HA2  . GLY   B 1 73  ? 45.556 -9.543  13.877  1.00 18.65 ?  73  GLY   B HA2  1 
ATOM   5019 H  HA3  . GLY   B 1 73  ? 44.061 -9.049  13.835  1.00 18.65 ?  73  GLY   B HA3  1 
ATOM   5020 N  N    . PRO   B 1 74  ? 44.152 -11.597 13.062  1.00 14.65 ?  74  PRO   B N    1 
ATOM   5021 C  CA   . PRO   B 1 74  ? 43.898 -12.830 12.317  1.00 14.02 ?  74  PRO   B CA   1 
ATOM   5022 C  C    . PRO   B 1 74  ? 42.601 -12.769 11.523  1.00 13.42 ?  74  PRO   B C    1 
ATOM   5023 O  O    . PRO   B 1 74  ? 41.658 -12.033 11.841  1.00 14.75 ?  74  PRO   B O    1 
ATOM   5024 C  CB   . PRO   B 1 74  ? 43.817 -13.894 13.419  1.00 14.94 ?  74  PRO   B CB   1 
ATOM   5025 C  CG   . PRO   B 1 74  ? 43.380 -13.145 14.629  1.00 16.71 ?  74  PRO   B CG   1 
ATOM   5026 C  CD   . PRO   B 1 74  ? 44.042 -11.801 14.517  1.00 16.37 ?  74  PRO   B CD   1 
ATOM   5027 H  HA   . PRO   B 1 74  ? 44.641 -13.026 11.722  1.00 16.94 ?  74  PRO   B HA   1 
ATOM   5028 H  HB2  . PRO   B 1 74  ? 43.164 -14.569 13.173  1.00 18.05 ?  74  PRO   B HB2  1 
ATOM   5029 H  HB3  . PRO   B 1 74  ? 44.691 -14.293 13.554  1.00 18.05 ?  74  PRO   B HB3  1 
ATOM   5030 H  HG2  . PRO   B 1 74  ? 42.414 -13.056 14.624  1.00 20.16 ?  74  PRO   B HG2  1 
ATOM   5031 H  HG3  . PRO   B 1 74  ? 43.679 -13.611 15.424  1.00 20.16 ?  74  PRO   B HG3  1 
ATOM   5032 H  HD2  . PRO   B 1 74  ? 43.480 -11.116 14.921  1.00 19.76 ?  74  PRO   B HD2  1 
ATOM   5033 H  HD3  . PRO   B 1 74  ? 44.921 -11.821 14.923  1.00 19.76 ?  74  PRO   B HD3  1 
ATOM   5034 N  N    . LEU   B 1 75  ? 42.571 -13.581 10.469  1.00 12.94 ?  75  LEU   B N    1 
ATOM   5035 C  CA   . LEU   B 1 75  ? 41.361 -13.793 9.696   1.00 13.09 ?  75  LEU   B CA   1 
ATOM   5036 C  C    . LEU   B 1 75  ? 40.379 -14.649 10.494  1.00 13.31 ?  75  LEU   B C    1 
ATOM   5037 O  O    . LEU   B 1 75  ? 40.714 -15.216 11.534  1.00 14.16 ?  75  LEU   B O    1 
ATOM   5038 C  CB   . LEU   B 1 75  ? 41.688 -14.502 8.381   1.00 12.96 ?  75  LEU   B CB   1 
ATOM   5039 C  CG   . LEU   B 1 75  ? 42.529 -13.742 7.350   1.00 14.64 ?  75  LEU   B CG   1 
ATOM   5040 C  CD1  . LEU   B 1 75  ? 42.711 -14.563 6.078   1.00 15.93 ?  75  LEU   B CD1  1 
ATOM   5041 C  CD2  . LEU   B 1 75  ? 41.934 -12.392 7.027   1.00 17.92 ?  75  LEU   B CD2  1 
ATOM   5042 H  H    . LEU   B 1 75  ? 43.246 -14.033 10.180  1.00 15.65 ?  75  LEU   B H    1 
ATOM   5043 H  HA   . LEU   B 1 75  ? 40.941 -12.944 9.499   1.00 15.82 ?  75  LEU   B HA   1 
ATOM   5044 H  HB2  . LEU   B 1 75  ? 42.169 -15.319 8.589   1.00 15.67 ?  75  LEU   B HB2  1 
ATOM   5045 H  HB3  . LEU   B 1 75  ? 40.851 -14.733 7.944   1.00 15.67 ?  75  LEU   B HB3  1 
ATOM   5046 H  HG   . LEU   B 1 75  ? 43.411 -13.590 7.726   1.00 17.69 ?  75  LEU   B HG   1 
ATOM   5047 H  HD11 . LEU   B 1 75  ? 43.252 -14.055 5.448   1.00 19.24 ?  75  LEU   B HD11 1 
ATOM   5048 H  HD12 . LEU   B 1 75  ? 43.159 -15.394 6.297   1.00 19.24 ?  75  LEU   B HD12 1 
ATOM   5049 H  HD13 . LEU   B 1 75  ? 41.842 -14.746 5.690   1.00 19.24 ?  75  LEU   B HD13 1 
ATOM   5050 H  HD21 . LEU   B 1 75  ? 42.436 -11.990 6.302   1.00 21.62 ?  75  LEU   B HD21 1 
ATOM   5051 H  HD22 . LEU   B 1 75  ? 41.009 -12.510 6.767   1.00 21.62 ?  75  LEU   B HD22 1 
ATOM   5052 H  HD23 . LEU   B 1 75  ? 41.987 -11.827 7.816   1.00 21.62 ?  75  LEU   B HD23 1 
ATOM   5053 N  N    . LYS   B 1 76  ? 39.148 -14.733 9.989   1.00 14.64 ?  76  LYS   B N    1 
ATOM   5054 C  CA   . LYS   B 1 76  ? 38.162 -15.691 10.472  1.00 16.10 ?  76  LYS   B CA   1 
ATOM   5055 C  C    . LYS   B 1 76  ? 38.251 -16.964 9.635   1.00 14.95 ?  76  LYS   B C    1 
ATOM   5056 O  O    . LYS   B 1 76  ? 38.526 -16.910 8.438   1.00 14.51 ?  76  LYS   B O    1 
ATOM   5057 C  CB   . LYS   B 1 76  ? 36.744 -15.126 10.305  1.00 17.87 ?  76  LYS   B CB   1 
ATOM   5058 C  CG   . LYS   B 1 76  ? 36.475 -13.737 10.907  1.00 19.77 ?  76  LYS   B CG   1 
ATOM   5059 C  CD   . LYS   B 1 76  ? 35.060 -13.228 10.568  1.00 20.94 ?  76  LYS   B CD   1 
ATOM   5060 C  CE   . LYS   B 1 76  ? 34.805 -11.836 11.132  1.00 22.49 ?  76  LYS   B CE   1 
ATOM   5061 N  NZ   . LYS   B 1 76  ? 33.503 -11.259 10.694  1.00 23.25 ?  76  LYS   B NZ   1 
ATOM   5062 H  H    . LYS   B 1 76  ? 38.858 -14.242 9.347   1.00 17.68 ?  76  LYS   B H    1 
ATOM   5063 H  HA   . LYS   B 1 76  ? 38.322 -15.910 11.403  1.00 19.43 ?  76  LYS   B HA   1 
ATOM   5064 H  HB2  . LYS   B 1 76  ? 36.553 -15.072 9.356   1.00 21.57 ?  76  LYS   B HB2  1 
ATOM   5065 H  HB3  . LYS   B 1 76  ? 36.124 -15.745 10.722  1.00 21.57 ?  76  LYS   B HB3  1 
ATOM   5066 H  HG2  . LYS   B 1 76  ? 36.561 -13.788 11.871  1.00 23.84 ?  76  LYS   B HG2  1 
ATOM   5067 H  HG3  . LYS   B 1 76  ? 37.121 -13.107 10.547  1.00 23.84 ?  76  LYS   B HG3  1 
ATOM   5068 H  HD2  . LYS   B 1 76  ? 34.960 -13.190 9.603   1.00 25.25 ?  76  LYS   B HD2  1 
ATOM   5069 H  HD3  . LYS   B 1 76  ? 34.407 -13.835 10.947  1.00 25.25 ?  76  LYS   B HD3  1 
ATOM   5070 H  HE2  . LYS   B 1 76  ? 34.802 -11.886 12.100  1.00 27.10 ?  76  LYS   B HE2  1 
ATOM   5071 H  HE3  . LYS   B 1 76  ? 35.512 -11.242 10.833  1.00 27.10 ?  76  LYS   B HE3  1 
ATOM   5072 H  HZ1  . LYS   B 1 76  ? 33.394 -10.447 11.046  1.00 28.02 ?  76  LYS   B HZ1  1 
ATOM   5073 H  HZ2  . LYS   B 1 76  ? 33.478 -11.192 9.807   1.00 28.02 ?  76  LYS   B HZ2  1 
ATOM   5074 H  HZ3  . LYS   B 1 76  ? 32.831 -11.779 10.962  1.00 28.02 ?  76  LYS   B HZ3  1 
ATOM   5075 N  N    . VAL   B 1 77  ? 38.007 -18.117 10.266  1.00 15.39 ?  77  VAL   B N    1 
ATOM   5076 C  CA   . VAL   B 1 77  ? 37.800 -19.332 9.484   1.00 15.58 ?  77  VAL   B CA   1 
ATOM   5077 C  C    . VAL   B 1 77  ? 36.608 -19.103 8.569   1.00 14.36 ?  77  VAL   B C    1 
ATOM   5078 O  O    . VAL   B 1 77  ? 35.541 -18.661 9.016   1.00 14.41 ?  77  VAL   B O    1 
ATOM   5079 C  CB   . VAL   B 1 77  ? 37.598 -20.550 10.397  1.00 17.26 ?  77  VAL   B CB   1 
ATOM   5080 C  CG1  . VAL   B 1 77  ? 37.306 -21.785 9.554   1.00 17.81 ?  77  VAL   B CG1  1 
ATOM   5081 C  CG2  . VAL   B 1 77  ? 38.830 -20.777 11.265  1.00 18.85 ?  77  VAL   B CG2  1 
ATOM   5082 H  H    . VAL   B 1 77  ? 37.954 -18.221 11.113  1.00 18.58 ?  77  VAL   B H    1 
ATOM   5083 H  HA   . VAL   B 1 77  ? 38.571 -19.493 8.925   1.00 18.81 ?  77  VAL   B HA   1 
ATOM   5084 H  HB   . VAL   B 1 77  ? 36.833 -20.391 10.975  1.00 20.83 ?  77  VAL   B HB   1 
ATOM   5085 H  HG11 . VAL   B 1 77  ? 37.352 -22.569 10.124  1.00 21.49 ?  77  VAL   B HG11 1 
ATOM   5086 H  HG12 . VAL   B 1 77  ? 36.412 -21.712 9.175   1.00 21.49 ?  77  VAL   B HG12 1 
ATOM   5087 H  HG13 . VAL   B 1 77  ? 37.961 -21.848 8.847   1.00 21.49 ?  77  VAL   B HG13 1 
ATOM   5088 H  HG21 . VAL   B 1 77  ? 38.692 -21.572 11.797  1.00 22.74 ?  77  VAL   B HG21 1 
ATOM   5089 H  HG22 . VAL   B 1 77  ? 39.599 -20.886 10.688  1.00 22.74 ?  77  VAL   B HG22 1 
ATOM   5090 H  HG23 . VAL   B 1 77  ? 38.949 -20.005 11.840  1.00 22.74 ?  77  VAL   B HG23 1 
ATOM   5091 N  N    . GLY   B 1 78  ? 36.786 -19.382 7.278   1.00 13.68 ?  78  GLY   B N    1 
ATOM   5092 C  CA   . GLY   B 1 78  ? 35.806 -19.057 6.267   1.00 13.36 ?  78  GLY   B CA   1 
ATOM   5093 C  C    . GLY   B 1 78  ? 36.051 -17.741 5.562   1.00 12.75 ?  78  GLY   B C    1 
ATOM   5094 O  O    . GLY   B 1 78  ? 35.367 -17.459 4.574   1.00 13.20 ?  78  GLY   B O    1 
ATOM   5095 H  H    . GLY   B 1 78  ? 37.480 -19.778 6.960   1.00 16.53 ?  78  GLY   B H    1 
ATOM   5096 H  HA2  . GLY   B 1 78  ? 35.793 -19.750 5.593   1.00 16.15 ?  78  GLY   B HA2  1 
ATOM   5097 H  HA3  . GLY   B 1 78  ? 34.926 -19.012 6.674   1.00 16.15 ?  78  GLY   B HA3  1 
ATOM   5098 N  N    . GLY   B 1 79  ? 37.004 -16.935 6.043   1.00 12.41 ?  79  GLY   B N    1 
ATOM   5099 C  CA   . GLY   B 1 79  ? 37.303 -15.641 5.463   1.00 12.30 ?  79  GLY   B CA   1 
ATOM   5100 C  C    . GLY   B 1 79  ? 38.543 -15.664 4.576   1.00 12.24 ?  79  GLY   B C    1 
ATOM   5101 O  O    . GLY   B 1 79  ? 39.162 -16.701 4.339   1.00 12.66 ?  79  GLY   B O    1 
ATOM   5102 H  H    . GLY   B 1 79  ? 37.503 -17.123 6.717   1.00 15.01 ?  79  GLY   B H    1 
ATOM   5103 H  HA2  . GLY   B 1 79  ? 36.548 -15.342 4.928   1.00 14.88 ?  79  GLY   B HA2  1 
ATOM   5104 H  HA3  . GLY   B 1 79  ? 37.450 -14.994 6.169   1.00 14.88 ?  79  GLY   B HA3  1 
ATOM   5105 N  N    . SER   B 1 80  ? 38.906 -14.473 4.094   1.00 11.96 ?  80  SER   B N    1 
ATOM   5106 C  CA   . SER   B 1 80  ? 40.018 -14.342 3.161   1.00 11.44 ?  80  SER   B CA   1 
ATOM   5107 C  C    . SER   B 1 80  ? 40.599 -12.937 3.221   1.00 11.73 ?  80  SER   B C    1 
ATOM   5108 O  O    . SER   B 1 80  ? 39.980 -12.002 3.734   1.00 12.91 ?  80  SER   B O    1 
ATOM   5109 C  CB   . SER   B 1 80  ? 39.576 -14.635 1.723   1.00 11.82 ?  80  SER   B CB   1 
ATOM   5110 O  OG   . SER   B 1 80  ? 38.736 -13.609 1.223   1.00 12.96 ?  80  SER   B OG   1 
ATOM   5111 H  H    . SER   B 1 80  ? 38.531 -13.728 4.295   1.00 14.47 ?  80  SER   B H    1 
ATOM   5112 H  HA   . SER   B 1 80  ? 40.709 -14.976 3.408   1.00 13.85 ?  80  SER   B HA   1 
ATOM   5113 H  HB2  . SER   B 1 80  ? 40.361 -14.693 1.156   1.00 14.30 ?  80  SER   B HB2  1 
ATOM   5114 H  HB3  . SER   B 1 80  ? 39.091 -15.473 1.705   1.00 14.30 ?  80  SER   B HB3  1 
ATOM   5115 H  HG   . SER   B 1 80  ? 38.046 -13.541 1.709   1.00 15.67 ?  80  SER   B HG   1 
ATOM   5116 N  N    . CYS   B 1 81  ? 41.788 -12.797 2.639   1.00 11.33 ?  81  CYS   B N    1 
ATOM   5117 C  CA   . CYS   B 1 81  ? 42.340 -11.486 2.329   1.00 11.40 ?  81  CYS   B CA   1 
ATOM   5118 C  C    . CYS   B 1 81  ? 43.108 -11.566 1.018   1.00 10.92 ?  81  CYS   B C    1 
ATOM   5119 O  O    . CYS   B 1 81  ? 43.617 -12.627 0.640   1.00 11.94 ?  81  CYS   B O    1 
ATOM   5120 C  CB   . CYS   B 1 81  ? 43.233 -10.933 3.452   1.00 12.15 ?  81  CYS   B CB   1 
ATOM   5121 S  SG   . CYS   B 1 81  ? 44.746 -11.865 3.699   1.00 12.64 ?  81  CYS   B SG   1 
ATOM   5122 H  H    . CYS   B 1 81  ? 42.299 -13.455 2.407   1.00 13.71 ?  81  CYS   B H    1 
ATOM   5123 H  HA   . CYS   B 1 81  ? 41.606 -10.864 2.202   1.00 13.80 ?  81  CYS   B HA   1 
ATOM   5124 H  HB2  . CYS   B 1 81  ? 43.478 -10.019 3.238   1.00 14.70 ?  81  CYS   B HB2  1 
ATOM   5125 H  HB3  . CYS   B 1 81  ? 42.729 -10.945 4.286   1.00 14.70 ?  81  CYS   B HB3  1 
ATOM   5126 H  HG   . CYS   B 1 81  ? 45.366 -11.362 4.602   1.00 15.29 ?  81  CYS   B HG   1 
ATOM   5127 N  N    . VAL   B 1 82  ? 43.210 -10.423 0.341   1.00 11.09 ?  82  VAL   B N    1 
ATOM   5128 C  CA   . VAL   B 1 82  ? 43.979 -10.299 -0.897  1.00 11.67 ?  82  VAL   B CA   1 
ATOM   5129 C  C    . VAL   B 1 82  ? 45.320 -9.658  -0.577  1.00 11.86 ?  82  VAL   B C    1 
ATOM   5130 O  O    . VAL   B 1 82  ? 45.369 -8.542  -0.043  1.00 12.73 ?  82  VAL   B O    1 
ATOM   5131 C  CB   . VAL   B 1 82  ? 43.232 -9.461  -1.947  1.00 12.40 ?  82  VAL   B CB   1 
ATOM   5132 C  CG1  . VAL   B 1 82  ? 44.070 -9.319  -3.210  1.00 13.81 ?  82  VAL   B CG1  1 
ATOM   5133 C  CG2  . VAL   B 1 82  ? 41.876 -10.073 -2.256  1.00 13.65 ?  82  VAL   B CG2  1 
ATOM   5134 H  H    . VAL   B 1 82  ? 42.831 -9.683  0.581   1.00 13.43 ?  82  VAL   B H    1 
ATOM   5135 H  HA   . VAL   B 1 82  ? 44.137 -11.180 -1.265  1.00 14.12 ?  82  VAL   B HA   1 
ATOM   5136 H  HB   . VAL   B 1 82  ? 43.078 -8.575  -1.593  1.00 15.00 ?  82  VAL   B HB   1 
ATOM   5137 H  HG11 . VAL   B 1 82  ? 43.507 -8.994  -3.930  1.00 16.69 ?  82  VAL   B HG11 1 
ATOM   5138 H  HG12 . VAL   B 1 82  ? 44.789 -8.686  -3.045  1.00 16.69 ?  82  VAL   B HG12 1 
ATOM   5139 H  HG13 . VAL   B 1 82  ? 44.439 -10.184 -3.446  1.00 16.69 ?  82  VAL   B HG13 1 
ATOM   5140 H  HG21 . VAL   B 1 82  ? 41.441 -9.555  -2.953  1.00 16.50 ?  82  VAL   B HG21 1 
ATOM   5141 H  HG22 . VAL   B 1 82  ? 41.999 -10.989 -2.558  1.00 16.50 ?  82  VAL   B HG22 1 
ATOM   5142 H  HG23 . VAL   B 1 82  ? 41.331 -10.065 -1.452  1.00 16.50 ?  82  VAL   B HG23 1 
ATOM   5143 N  N    . LEU   B 1 83  ? 46.400 -10.343 -0.944  1.00 11.19 ?  83  LEU   B N    1 
ATOM   5144 C  CA   . LEU   B 1 83  ? 47.759 -9.834  -0.825  1.00 11.23 ?  83  LEU   B CA   1 
ATOM   5145 C  C    . LEU   B 1 83  ? 48.459 -9.985  -2.176  1.00 11.18 ?  83  LEU   B C    1 
ATOM   5146 O  O    . LEU   B 1 83  ? 47.857 -10.403 -3.168  1.00 11.02 ?  83  LEU   B O    1 
ATOM   5147 C  CB   . LEU   B 1 83  ? 48.508 -10.516 0.329   1.00 11.91 ?  83  LEU   B CB   1 
ATOM   5148 C  CG   . LEU   B 1 83  ? 48.008 -10.151 1.731   1.00 12.77 ?  83  LEU   B CG   1 
ATOM   5149 C  CD1  . LEU   B 1 83  ? 48.648 -11.015 2.797   1.00 13.51 ?  83  LEU   B CD1  1 
ATOM   5150 C  CD2  . LEU   B 1 83  ? 48.210 -8.658  2.050   1.00 13.71 ?  83  LEU   B CD2  1 
ATOM   5151 H  H    . LEU   B 1 83  ? 46.360 -11.142 -1.273  1.00 13.54 ?  83  LEU   B H    1 
ATOM   5152 H  HA   . LEU   B 1 83  ? 47.712 -8.892  -0.629  1.00 13.60 ?  83  LEU   B HA   1 
ATOM   5153 H  HB2  . LEU   B 1 83  ? 48.428 -11.476 0.230   1.00 14.40 ?  83  LEU   B HB2  1 
ATOM   5154 H  HB3  . LEU   B 1 83  ? 49.444 -10.262 0.277   1.00 14.40 ?  83  LEU   B HB3  1 
ATOM   5155 H  HG   . LEU   B 1 83  ? 47.055 -10.320 1.760   1.00 15.44 ?  83  LEU   B HG   1 
ATOM   5156 H  HD11 . LEU   B 1 83  ? 48.299 -10.756 3.664   1.00 16.33 ?  83  LEU   B HD11 1 
ATOM   5157 H  HD12 . LEU   B 1 83  ? 48.432 -11.945 2.619   1.00 16.33 ?  83  LEU   B HD12 1 
ATOM   5158 H  HD13 . LEU   B 1 83  ? 49.608 -10.888 2.774   1.00 16.33 ?  83  LEU   B HD13 1 
ATOM   5159 H  HD21 . LEU   B 1 83  ? 48.003 -8.507  2.985   1.00 16.57 ?  83  LEU   B HD21 1 
ATOM   5160 H  HD22 . LEU   B 1 83  ? 49.129 -8.418  1.868   1.00 16.57 ?  83  LEU   B HD22 1 
ATOM   5161 H  HD23 . LEU   B 1 83  ? 47.612 -8.134  1.492   1.00 16.57 ?  83  LEU   B HD23 1 
ATOM   5162 N  N    . SER   B 1 84  ? 49.734 -9.612  -2.228  1.00 12.16 ?  84  SER   B N    1 
ATOM   5163 C  CA   . SER   B 1 84  ? 50.471 -9.733  -3.476  1.00 12.26 ?  84  SER   B CA   1 
ATOM   5164 C  C    . SER   B 1 84  ? 50.633 -11.195 -3.881  1.00 11.38 ?  84  SER   B C    1 
ATOM   5165 O  O    . SER   B 1 84  ? 50.746 -12.088 -3.042  1.00 11.28 ?  84  SER   B O    1 
ATOM   5166 C  CB   . SER   B 1 84  ? 51.860 -9.115  -3.333  1.00 14.27 ?  84  SER   B CB   1 
ATOM   5167 O  OG   . SER   B 1 84  ? 52.603 -9.329  -4.517  1.00 15.68 ?  84  SER   B OG   1 
ATOM   5168 H  H    . SER   B 1 84  ? 50.178 -9.274  -1.572  1.00 14.71 ?  84  SER   B H    1 
ATOM   5169 H  HA   . SER   B 1 84  ? 49.998 -9.267  -4.182  1.00 14.83 ?  84  SER   B HA   1 
ATOM   5170 H  HB2  . SER   B 1 84  ? 51.769 -8.159  -3.173  1.00 17.24 ?  84  SER   B HB2  1 
ATOM   5171 H  HB3  . SER   B 1 84  ? 52.321 -9.532  -2.589  1.00 17.24 ?  84  SER   B HB3  1 
ATOM   5172 H  HG   . SER   B 1 84  ? 53.370 -8.976  -4.441  1.00 18.93 ?  84  SER   B HG   1 
ATOM   5173 N  N    . GLY   B 1 85  ? 50.690 -11.423 -5.186  1.00 12.42 ?  85  GLY   B N    1 
ATOM   5174 C  CA   . GLY   B 1 85  ? 51.044 -12.713 -5.728  1.00 13.18 ?  85  GLY   B CA   1 
ATOM   5175 C  C    . GLY   B 1 85  ? 52.516 -12.904 -6.032  1.00 12.72 ?  85  GLY   B C    1 
ATOM   5176 O  O    . GLY   B 1 85  ? 52.897 -13.983 -6.489  1.00 12.94 ?  85  GLY   B O    1 
ATOM   5177 H  H    . GLY   B 1 85  ? 50.533 -10.833 -5.787  1.00 15.02 ?  85  GLY   B H    1 
ATOM   5178 H  HA2  . GLY   B 1 85  ? 50.782 -13.406 -5.097  1.00 15.93 ?  85  GLY   B HA2  1 
ATOM   5179 H  HA3  . GLY   B 1 85  ? 50.555 -12.860 -6.549  1.00 15.93 ?  85  GLY   B HA3  1 
ATOM   5180 N  N    . HIS   B 1 86  ? 53.366 -11.902 -5.810  1.00 12.73 ?  86  HIS   B N    1 
ATOM   5181 C  CA   . HIS   B 1 86  ? 54.827 -12.068 -5.895  1.00 12.29 ?  86  HIS   B CA   1 
ATOM   5182 C  C    . HIS   B 1 86  ? 55.200 -12.583 -7.283  1.00 12.69 ?  86  HIS   B C    1 
ATOM   5183 O  O    . HIS   B 1 86  ? 54.807 -11.969 -8.289  1.00 13.60 ?  86  HIS   B O    1 
ATOM   5184 C  CB   . HIS   B 1 86  ? 55.320 -12.905 -4.714  1.00 12.79 ?  86  HIS   B CB   1 
ATOM   5185 C  CG   . HIS   B 1 86  ? 55.006 -12.295 -3.388  1.00 13.00 ?  86  HIS   B CG   1 
ATOM   5186 N  ND1  . HIS   B 1 86  ? 55.837 -11.390 -2.764  1.00 14.73 ?  86  HIS   B ND1  1 
ATOM   5187 C  CD2  . HIS   B 1 86  ? 53.924 -12.434 -2.584  1.00 13.24 ?  86  HIS   B CD2  1 
ATOM   5188 C  CE1  . HIS   B 1 86  ? 55.277 -10.997 -1.634  1.00 14.51 ?  86  HIS   B CE1  1 
ATOM   5189 N  NE2  . HIS   B 1 86  ? 54.114 -11.613 -1.502  1.00 13.56 ?  86  HIS   B NE2  1 
ATOM   5190 H  H    . HIS   B 1 86  ? 53.123 -11.105 -5.612  1.00 15.39 ?  86  HIS   B H    1 
ATOM   5191 H  HA   . HIS   B 1 86  ? 55.234 -11.195 -5.803  1.00 14.86 ?  86  HIS   B HA   1 
ATOM   5192 H  HB2  . HIS   B 1 86  ? 54.906 -13.779 -4.748  1.00 15.47 ?  86  HIS   B HB2  1 
ATOM   5193 H  HB3  . HIS   B 1 86  ? 56.287 -12.995 -4.772  1.00 15.47 ?  86  HIS   B HB3  1 
ATOM   5194 H  HD2  . HIS   B 1 86  ? 53.176 -12.967 -2.746  1.00 16.00 ?  86  HIS   B HD2  1 
ATOM   5195 H  HE1  . HIS   B 1 86  ? 55.647 -10.402 -1.022  1.00 17.53 ?  86  HIS   B HE1  1 
ATOM   5196 H  HE2  . HIS   B 1 86  ? 53.572 -11.525 -0.837  1.00 16.39 ?  86  HIS   B HE2  1 
ATOM   5197 N  N    . ASN   B 1 87  ? 55.969 -13.666 -7.389  1.00 13.39 ?  87  ASN   B N    1 
ATOM   5198 C  CA   . ASN   B 1 87  ? 56.367 -14.243 -8.666  1.00 14.16 ?  87  ASN   B CA   1 
ATOM   5199 C  C    . ASN   B 1 87  ? 55.381 -15.286 -9.169  1.00 13.77 ?  87  ASN   B C    1 
ATOM   5200 O  O    . ASN   B 1 87  ? 55.699 -16.002 -10.125 1.00 15.59 ?  87  ASN   B O    1 
ATOM   5201 C  CB   . ASN   B 1 87  ? 57.762 -14.872 -8.548  1.00 15.97 ?  87  ASN   B CB   1 
ATOM   5202 C  CG   . ASN   B 1 87  ? 57.815 -15.987 -7.512  1.00 16.71 ?  87  ASN   B CG   1 
ATOM   5203 O  OD1  . ASN   B 1 87  ? 57.176 -15.906 -6.460  1.00 16.07 ?  87  ASN   B OD1  1 
ATOM   5204 N  ND2  . ASN   B 1 87  ? 58.562 -17.052 -7.820  1.00 18.75 ?  87  ASN   B ND2  1 
ATOM   5205 H  H    . ASN   B 1 87  ? 56.281 -14.099 -6.714  1.00 16.18 ?  87  ASN   B H    1 
ATOM   5206 H  HA   . ASN   B 1 87  ? 56.414 -13.537 -9.325  1.00 17.11 ?  87  ASN   B HA   1 
ATOM   5207 H  HB2  . ASN   B 1 87  ? 58.013 -15.245 -9.409  1.00 19.28 ?  87  ASN   B HB2  1 
ATOM   5208 H  HB3  . ASN   B 1 87  ? 58.395 -14.188 -8.285  1.00 19.28 ?  87  ASN   B HB3  1 
ATOM   5209 H  HD21 . ASN   B 1 87  ? 58.625 -17.708 -7.271  1.00 22.61 ?  87  ASN   B HD21 1 
ATOM   5210 H  HD22 . ASN   B 1 87  ? 58.990 -17.075 -8.568  1.00 22.61 ?  87  ASN   B HD22 1 
ATOM   5211 N  N    . LEU   B 1 88  ? 54.199 -15.383 -8.552  1.00 12.61 ?  88  LEU   B N    1 
ATOM   5212 C  CA   . LEU   B 1 88  ? 53.218 -16.414 -8.875  1.00 12.83 ?  88  LEU   B CA   1 
ATOM   5213 C  C    . LEU   B 1 88  ? 51.988 -15.897 -9.599  1.00 12.66 ?  88  LEU   B C    1 
ATOM   5214 O  O    . LEU   B 1 88  ? 51.384 -16.644 -10.378 1.00 14.61 ?  88  LEU   B O    1 
ATOM   5215 C  CB   . LEU   B 1 88  ? 52.748 -17.094 -7.587  1.00 13.72 ?  88  LEU   B CB   1 
ATOM   5216 C  CG   . LEU   B 1 88  ? 53.863 -17.766 -6.797  1.00 16.13 ?  88  LEU   B CG   1 
ATOM   5217 C  CD1  . LEU   B 1 88  ? 53.370 -18.149 -5.413  1.00 17.60 ?  88  LEU   B CD1  1 
ATOM   5218 C  CD2  . LEU   B 1 88  ? 54.370 -18.982 -7.551  1.00 19.16 ?  88  LEU   B CD2  1 
ATOM   5219 H  H    . LEU   B 1 88  ? 53.938 -14.848 -7.920  1.00 15.25 ?  88  LEU   B H    1 
ATOM   5220 H  HA   . LEU   B 1 88  ? 53.634 -17.078 -9.433  1.00 15.51 ?  88  LEU   B HA   1 
ATOM   5221 H  HB2  . LEU   B 1 88  ? 52.333 -16.434 -7.009  1.00 16.58 ?  88  LEU   B HB2  1 
ATOM   5222 H  HB3  . LEU   B 1 88  ? 52.096 -17.779 -7.817  1.00 16.58 ?  88  LEU   B HB3  1 
ATOM   5223 H  HG   . LEU   B 1 88  ? 54.598 -17.145 -6.693  1.00 19.47 ?  88  LEU   B HG   1 
ATOM   5224 H  HD11 . LEU   B 1 88  ? 54.040 -18.699 -4.979  1.00 21.23 ?  88  LEU   B HD11 1 
ATOM   5225 H  HD12 . LEU   B 1 88  ? 53.215 -17.344 -4.897  1.00 21.23 ?  88  LEU   B HD12 1 
ATOM   5226 H  HD13 . LEU   B 1 88  ? 52.542 -18.649 -5.503  1.00 21.23 ?  88  LEU   B HD13 1 
ATOM   5227 H  HD21 . LEU   B 1 88  ? 55.001 -19.458 -6.990  1.00 23.10 ?  88  LEU   B HD21 1 
ATOM   5228 H  HD22 . LEU   B 1 88  ? 53.619 -19.556 -7.767  1.00 23.10 ?  88  LEU   B HD22 1 
ATOM   5229 H  HD23 . LEU   B 1 88  ? 54.808 -18.688 -8.365  1.00 23.10 ?  88  LEU   B HD23 1 
ATOM   5230 N  N    . ALA   B 1 89  ? 51.586 -14.662 -9.332  1.00 12.07 ?  89  ALA   B N    1 
ATOM   5231 C  CA   . ALA   B 1 89  ? 50.296 -14.164 -9.782  1.00 11.37 ?  89  ALA   B CA   1 
ATOM   5232 C  C    . ALA   B 1 89  ? 50.269 -12.675 -9.496  1.00 11.81 ?  89  ALA   B C    1 
ATOM   5233 O  O    . ALA   B 1 89  ? 51.107 -12.160 -8.755  1.00 12.57 ?  89  ALA   B O    1 
ATOM   5234 C  CB   . ALA   B 1 89  ? 49.158 -14.850 -9.031  1.00 11.75 ?  89  ALA   B CB   1 
ATOM   5235 H  H    . ALA   B 1 89  ? 52.038 -14.081 -8.883  1.00 14.61 ?  89  ALA   B H    1 
ATOM   5236 H  HA   . ALA   B 1 89  ? 50.186 -14.309 -10.738 1.00 13.76 ?  89  ALA   B HA   1 
ATOM   5237 H  HB1  . ALA   B 1 89  ? 48.309 -14.515 -9.367  1.00 14.21 ?  89  ALA   B HB1  1 
ATOM   5238 H  HB2  . ALA   B 1 89  ? 49.216 -15.807 -9.186  1.00 14.21 ?  89  ALA   B HB2  1 
ATOM   5239 H  HB3  . ALA   B 1 89  ? 49.243 -14.659 -8.089  1.00 14.21 ?  89  ALA   B HB3  1 
ATOM   5240 N  N    . LYS   B 1 90  ? 49.283 -11.982 -10.061 1.00 12.89 ?  90  LYS   B N    1 
ATOM   5241 C  CA   . LYS   B 1 90  ? 49.100 -10.593 -9.656  1.00 13.05 ?  90  LYS   B CA   1 
ATOM   5242 C  C    . LYS   B 1 90  ? 48.774 -10.517 -8.167  1.00 12.72 ?  90  LYS   B C    1 
ATOM   5243 O  O    . LYS   B 1 90  ? 49.415 -9.766  -7.414  1.00 13.82 ?  90  LYS   B O    1 
ATOM   5244 C  CB   . LYS   B 1 90  ? 48.029 -9.925  -10.518 1.00 14.59 ?  90  LYS   B CB   1 
ATOM   5245 C  CG   . LYS   B 1 90  ? 47.730 -8.489  -10.136 1.00 14.97 ?  90  LYS   B CG   1 
ATOM   5246 C  CD   . LYS   B 1 90  ? 48.946 -7.598  -10.196 1.00 17.26 ?  90  LYS   B CD   1 
ATOM   5247 C  CE   . LYS   B 1 90  ? 48.502 -6.175  -9.970  1.00 19.29 ?  90  LYS   B CE   1 
ATOM   5248 N  NZ   . LYS   B 1 90  ? 49.655 -5.255  -9.860  1.00 18.98 ?  90  LYS   B NZ   1 
ATOM   5249 H  H    . LYS   B 1 90  ? 48.731 -12.280 -10.656 1.00 15.59 ?  90  LYS   B H    1 
ATOM   5250 H  HA   . LYS   B 1 90  ? 49.929 -10.120 -9.803  1.00 15.78 ?  90  LYS   B HA   1 
ATOM   5251 H  HB2  . LYS   B 1 90  ? 48.328 -9.924  -11.445 1.00 17.63 ?  90  LYS   B HB2  1 
ATOM   5252 H  HB3  . LYS   B 1 90  ? 47.204 -10.429 -10.447 1.00 17.63 ?  90  LYS   B HB3  1 
ATOM   5253 H  HG2  . LYS   B 1 90  ? 47.067 -8.129  -10.750 1.00 18.08 ?  90  LYS   B HG2  1 
ATOM   5254 H  HG3  . LYS   B 1 90  ? 47.380 -8.466  -9.230  1.00 18.08 ?  90  LYS   B HG3  1 
ATOM   5255 H  HD2  . LYS   B 1 90  ? 49.571 -7.846  -9.495  1.00 20.83 ?  90  LYS   B HD2  1 
ATOM   5256 H  HD3  . LYS   B 1 90  ? 49.363 -7.666  -11.069 1.00 20.83 ?  90  LYS   B HD3  1 
ATOM   5257 H  HE2  . LYS   B 1 90  ? 47.958 -5.880  -10.720 1.00 23.26 ?  90  LYS   B HE2  1 
ATOM   5258 H  HE3  . LYS   B 1 90  ? 47.995 -6.114  -9.146  1.00 23.26 ?  90  LYS   B HE3  1 
ATOM   5259 H  HZ1  . LYS   B 1 90  ? 49.378 -4.420  -9.731  1.00 22.90 ?  90  LYS   B HZ1  1 
ATOM   5260 H  HZ2  . LYS   B 1 90  ? 50.175 -5.496  -9.178  1.00 22.90 ?  90  LYS   B HZ2  1 
ATOM   5261 H  HZ3  . LYS   B 1 90  ? 50.141 -5.282  -10.610 1.00 22.90 ?  90  LYS   B HZ3  1 
ATOM   5262 N  N    . HIS   B 1 91  ? 47.805 -11.329 -7.723  1.00 11.18 ?  91  HIS   B N    1 
ATOM   5263 C  CA   . HIS   B 1 91  ? 47.344 -11.355 -6.349  1.00 11.54 ?  91  HIS   B CA   1 
ATOM   5264 C  C    . HIS   B 1 91  ? 47.339 -12.783 -5.831  1.00 10.64 ?  91  HIS   B C    1 
ATOM   5265 O  O    . HIS   B 1 91  ? 47.113 -13.739 -6.585  1.00 11.01 ?  91  HIS   B O    1 
ATOM   5266 C  CB   . HIS   B 1 91  ? 45.894 -10.870 -6.230  1.00 13.16 ?  91  HIS   B CB   1 
ATOM   5267 C  CG   . HIS   B 1 91  ? 45.684 -9.464  -6.675  1.00 16.16 ?  91  HIS   B CG   1 
ATOM   5268 N  ND1  . HIS   B 1 91  ? 46.284 -8.385  -6.063  1.00 18.47 ?  91  HIS   B ND1  1 
ATOM   5269 C  CD2  . HIS   B 1 91  ? 44.898 -8.953  -7.650  1.00 18.40 ?  91  HIS   B CD2  1 
ATOM   5270 C  CE1  . HIS   B 1 91  ? 45.900 -7.269  -6.659  1.00 19.58 ?  91  HIS   B CE1  1 
ATOM   5271 N  NE2  . HIS   B 1 91  ? 45.053 -7.587  -7.622  1.00 19.82 ?  91  HIS   B NE2  1 
ATOM   5272 H  H    . HIS   B 1 91  ? 47.385 -11.889 -8.224  1.00 13.53 ?  91  HIS   B H    1 
ATOM   5273 H  HA   . HIS   B 1 91  ? 47.920 -10.797 -5.787  1.00 13.97 ?  91  HIS   B HA   1 
ATOM   5274 H  HB2  . HIS   B 1 91  ? 45.330 -11.437 -6.774  1.00 15.91 ?  91  HIS   B HB2  1 
ATOM   5275 H  HB3  . HIS   B 1 91  ? 45.619 -10.929 -5.299  1.00 15.91 ?  91  HIS   B HB3  1 
ATOM   5276 H  HD1  . HIS   B 1 91  ? 46.834 -8.429  -5.400  1.00 22.28 ?  91  HIS   B HD1  1 
ATOM   5277 H  HD2  . HIS   B 1 91  ? 44.363 -9.427  -8.238  1.00 22.19 ?  91  HIS   B HD2  1 
ATOM   5278 H  HE1  . HIS   B 1 91  ? 46.176 -6.407  -6.432  1.00 23.61 ?  91  HIS   B HE1  1 
ATOM   5279 N  N    . CYS   B 1 92  ? 47.526 -12.915 -4.527  1.00 10.38 ?  92  CYS   B N    1 
ATOM   5280 C  CA   . CYS   B 1 92  ? 47.217 -14.148 -3.816  1.00 10.17 ?  92  CYS   B CA   1 
ATOM   5281 C  C    . CYS   B 1 92  ? 46.000 -13.908 -2.935  1.00 10.01 ?  92  CYS   B C    1 
ATOM   5282 O  O    . CYS   B 1 92  ? 46.000 -13.000 -2.095  1.00 11.12 ?  92  CYS   B O    1 
ATOM   5283 C  CB   . CYS   B 1 92  ? 48.388 -14.599 -2.951  1.00 10.67 ?  92  CYS   B CB   1 
ATOM   5284 S  SG   . CYS   B 1 92  ? 48.043 -16.140 -2.058  1.00 10.89 ?  92  CYS   B SG   1 
ATOM   5285 H  H    . CYS   B 1 92  ? 47.858 -12.296 -4.021  1.00 12.57 ?  92  CYS   B H    1 
ATOM   5286 H  HA   . CYS   B 1 92  ? 47.017 -14.846 -4.458  1.00 12.32 ?  92  CYS   B HA   1 
ATOM   5287 H  HB2  . CYS   B 1 92  ? 49.161 -14.737 -3.511  1.00 12.92 ?  92  CYS   B HB2  1 
ATOM   5288 H  HB3  . CYS   B 1 92  ? 48.570 -13.908 -2.291  1.00 12.92 ?  92  CYS   B HB3  1 
ATOM   5289 H  HG   . CYS   B 1 92  ? 49.014 -16.442 -1.424  1.00 13.19 ?  92  CYS   B HG   1 
ATOM   5290 N  N    . LEU   B 1 93  ? 44.967 -14.717 -3.139  1.00 10.20 ?  93  LEU   B N    1 
ATOM   5291 C  CA   . LEU   B 1 93  ? 43.789 -14.724 -2.281  1.00 10.42 ?  93  LEU   B CA   1 
ATOM   5292 C  C    . LEU   B 1 93  ? 44.011 -15.788 -1.215  1.00 9.90  ?  93  LEU   B C    1 
ATOM   5293 O  O    . LEU   B 1 93  ? 43.961 -16.991 -1.506  1.00 10.45 ?  93  LEU   B O    1 
ATOM   5294 C  CB   . LEU   B 1 93  ? 42.533 -15.022 -3.093  1.00 10.56 ?  93  LEU   B CB   1 
ATOM   5295 C  CG   . LEU   B 1 93  ? 41.230 -15.029 -2.291  1.00 11.40 ?  93  LEU   B CG   1 
ATOM   5296 C  CD1  . LEU   B 1 93  ? 40.875 -13.637 -1.809  1.00 11.96 ?  93  LEU   B CD1  1 
ATOM   5297 C  CD2  . LEU   B 1 93  ? 40.102 -15.630 -3.108  1.00 11.42 ?  93  LEU   B CD2  1 
ATOM   5298 H  H    . LEU   B 1 93  ? 44.922 -15.297 -3.785  1.00 12.35 ?  93  LEU   B H    1 
ATOM   5299 H  HA   . LEU   B 1 93  ? 43.694 -13.859 -1.853  1.00 12.62 ?  93  LEU   B HA   1 
ATOM   5300 H  HB2  . LEU   B 1 93  ? 42.446 -14.342 -3.783  1.00 12.79 ?  93  LEU   B HB2  1 
ATOM   5301 H  HB3  . LEU   B 1 93  ? 42.631 -15.891 -3.505  1.00 12.79 ?  93  LEU   B HB3  1 
ATOM   5302 H  HG   . LEU   B 1 93  ? 41.348 -15.587 -1.511  1.00 13.79 ?  93  LEU   B HG   1 
ATOM   5303 H  HD11 . LEU   B 1 93  ? 40.019 -13.662 -1.361  1.00 14.47 ?  93  LEU   B HD11 1 
ATOM   5304 H  HD12 . LEU   B 1 93  ? 41.563 -13.329 -1.198  1.00 14.47 ?  93  LEU   B HD12 1 
ATOM   5305 H  HD13 . LEU   B 1 93  ? 40.828 -13.038 -2.577  1.00 14.47 ?  93  LEU   B HD13 1 
ATOM   5306 H  HD21 . LEU   B 1 93  ? 39.286 -15.620 -2.580  1.00 13.82 ?  93  LEU   B HD21 1 
ATOM   5307 H  HD22 . LEU   B 1 93  ? 39.975 -15.106 -3.916  1.00 13.82 ?  93  LEU   B HD22 1 
ATOM   5308 H  HD23 . LEU   B 1 93  ? 40.329 -16.545 -3.343  1.00 13.82 ?  93  LEU   B HD23 1 
ATOM   5309 N  N    . HIS   B 1 94  ? 44.286 -15.351 0.007   1.00 9.91  ?  94  HIS   B N    1 
ATOM   5310 C  CA   . HIS   B 1 94  ? 44.508 -16.256 1.126   1.00 9.87  ?  94  HIS   B CA   1 
ATOM   5311 C  C    . HIS   B 1 94  ? 43.145 -16.610 1.705   1.00 10.76 ?  94  HIS   B C    1 
ATOM   5312 O  O    . HIS   B 1 94  ? 42.474 -15.736 2.256   1.00 11.89 ?  94  HIS   B O    1 
ATOM   5313 C  CB   . HIS   B 1 94  ? 45.377 -15.578 2.183   1.00 10.74 ?  94  HIS   B CB   1 
ATOM   5314 C  CG   . HIS   B 1 94  ? 46.758 -15.277 1.714   1.00 10.71 ?  94  HIS   B CG   1 
ATOM   5315 N  ND1  . HIS   B 1 94  ? 47.783 -16.193 1.804   1.00 10.90 ?  94  HIS   B ND1  1 
ATOM   5316 C  CD2  . HIS   B 1 94  ? 47.270 -14.173 1.116   1.00 10.97 ?  94  HIS   B CD2  1 
ATOM   5317 C  CE1  . HIS   B 1 94  ? 48.876 -15.646 1.299   1.00 10.77 ?  94  HIS   B CE1  1 
ATOM   5318 N  NE2  . HIS   B 1 94  ? 48.593 -14.426 0.871   1.00 10.96 ?  94  HIS   B NE2  1 
ATOM   5319 H  H    . HIS   B 1 94  ? 44.357 -14.516 0.212   1.00 12.01 ?  94  HIS   B H    1 
ATOM   5320 H  HA   . HIS   B 1 94  ? 44.943 -17.065 0.819   1.00 11.95 ?  94  HIS   B HA   1 
ATOM   5321 H  HB2  . HIS   B 1 94  ? 44.960 -14.745 2.442   1.00 13.00 ?  94  HIS   B HB2  1 
ATOM   5322 H  HB3  . HIS   B 1 94  ? 45.445 -16.169 2.950   1.00 13.00 ?  94  HIS   B HB3  1 
ATOM   5323 H  HD2  . HIS   B 1 94  ? 46.814 -13.393 0.912   1.00 13.29 ?  94  HIS   B HD2  1 
ATOM   5324 H  HE1  . HIS   B 1 94  ? 49.707 -16.070 1.245   1.00 13.04 ?  94  HIS   B HE1  1 
ATOM   5325 H  HE2  . HIS   B 1 94  ? 49.152 -13.893 0.501   1.00 13.27 ?  94  HIS   B HE2  1 
ATOM   5326 N  N    . VAL   B 1 95  ? 42.711 -17.868 1.558   1.00 10.23 ?  95  VAL   B N    1 
ATOM   5327 C  CA   . VAL   B 1 95  ? 41.382 -18.305 1.991   1.00 10.45 ?  95  VAL   B CA   1 
ATOM   5328 C  C    . VAL   B 1 95  ? 41.551 -19.339 3.089   1.00 10.79 ?  95  VAL   B C    1 
ATOM   5329 O  O    . VAL   B 1 95  ? 42.324 -20.292 2.936   1.00 11.38 ?  95  VAL   B O    1 
ATOM   5330 C  CB   . VAL   B 1 95  ? 40.562 -18.908 0.834   1.00 10.96 ?  95  VAL   B CB   1 
ATOM   5331 C  CG1  . VAL   B 1 95  ? 39.186 -19.364 1.321   1.00 12.19 ?  95  VAL   B CG1  1 
ATOM   5332 C  CG2  . VAL   B 1 95  ? 40.432 -17.925 -0.303  1.00 10.98 ?  95  VAL   B CG2  1 
ATOM   5333 H  H    . VAL   B 1 95  ? 43.174 -18.495 1.198   1.00 12.39 ?  95  VAL   B H    1 
ATOM   5334 H  HA   . VAL   B 1 95  ? 40.888 -17.550 2.353   1.00 12.65 ?  95  VAL   B HA   1 
ATOM   5335 H  HB   . VAL   B 1 95  ? 41.024 -19.685 0.493   1.00 13.26 ?  95  VAL   B HB   1 
ATOM   5336 H  HG11 . VAL   B 1 95  ? 38.622 -19.558 0.549   1.00 14.74 ?  95  VAL   B HG11 1 
ATOM   5337 H  HG12 . VAL   B 1 95  ? 39.282 -20.166 1.858   1.00 14.74 ?  95  VAL   B HG12 1 
ATOM   5338 H  HG13 . VAL   B 1 95  ? 38.778 -18.658 1.847   1.00 14.74 ?  95  VAL   B HG13 1 
ATOM   5339 H  HG21 . VAL   B 1 95  ? 39.858 -18.312 -0.988  1.00 13.30 ?  95  VAL   B HG21 1 
ATOM   5340 H  HG22 . VAL   B 1 95  ? 40.029 -17.107 0.033   1.00 13.30 ?  95  VAL   B HG22 1 
ATOM   5341 H  HG23 . VAL   B 1 95  ? 41.306 -17.744 -0.665  1.00 13.30 ?  95  VAL   B HG23 1 
ATOM   5342 N  N    . VAL   B 1 96  ? 40.817 -19.168 4.182   1.00 11.24 ?  96  VAL   B N    1 
ATOM   5343 C  CA   . VAL   B 1 96  ? 40.900 -20.078 5.323   1.00 11.80 ?  96  VAL   B CA   1 
ATOM   5344 C  C    . VAL   B 1 96  ? 39.710 -21.034 5.278   1.00 12.29 ?  96  VAL   B C    1 
ATOM   5345 O  O    . VAL   B 1 96  ? 38.593 -20.681 5.670   1.00 13.10 ?  96  VAL   B O    1 
ATOM   5346 C  CB   . VAL   B 1 96  ? 40.946 -19.327 6.658   1.00 12.45 ?  96  VAL   B CB   1 
ATOM   5347 C  CG1  . VAL   B 1 96  ? 41.121 -20.320 7.800   1.00 13.32 ?  96  VAL   B CG1  1 
ATOM   5348 C  CG2  . VAL   B 1 96  ? 42.064 -18.295 6.668   1.00 13.15 ?  96  VAL   B CG2  1 
ATOM   5349 H  H    . VAL   B 1 96  ? 40.257 -18.529 4.295   1.00 13.60 ?  96  VAL   B H    1 
ATOM   5350 H  HA   . VAL   B 1 96  ? 41.710 -20.608 5.252   1.00 14.28 ?  96  VAL   B HA   1 
ATOM   5351 H  HB   . VAL   B 1 96  ? 40.106 -18.864 6.792   1.00 15.06 ?  96  VAL   B HB   1 
ATOM   5352 H  HG11 . VAL   B 1 96  ? 41.316 -19.830 8.616   1.00 16.10 ?  96  VAL   B HG11 1 
ATOM   5353 H  HG12 . VAL   B 1 96  ? 40.305 -20.830 7.910   1.00 16.10 ?  96  VAL   B HG12 1 
ATOM   5354 H  HG13 . VAL   B 1 96  ? 41.860 -20.915 7.592   1.00 16.10 ?  96  VAL   B HG13 1 
ATOM   5355 H  HG21 . VAL   B 1 96  ? 42.108 -17.882 7.546   1.00 15.90 ?  96  VAL   B HG21 1 
ATOM   5356 H  HG22 . VAL   B 1 96  ? 42.905 -18.733 6.467   1.00 15.90 ?  96  VAL   B HG22 1 
ATOM   5357 H  HG23 . VAL   B 1 96  ? 41.877 -17.618 5.996   1.00 15.90 ?  96  VAL   B HG23 1 
ATOM   5358 N  N    . GLY   B 1 97  ? 39.945 -22.269 4.838   1.00 12.24 ?  97  GLY   B N    1 
ATOM   5359 C  CA   . GLY   B 1 97  ? 38.973 -23.326 4.991   1.00 13.30 ?  97  GLY   B CA   1 
ATOM   5360 C  C    . GLY   B 1 97  ? 39.098 -23.942 6.368   1.00 13.88 ?  97  GLY   B C    1 
ATOM   5361 O  O    . GLY   B 1 97  ? 40.140 -23.818 7.028   1.00 14.41 ?  97  GLY   B O    1 
ATOM   5362 H  H    . GLY   B 1 97  ? 40.672 -22.510 4.434   1.00 14.80 ?  97  GLY   B H    1 
ATOM   5363 H  HA2  . GLY   B 1 97  ? 38.079 -22.958 4.873   1.00 16.07 ?  97  GLY   B HA2  1 
ATOM   5364 H  HA3  . GLY   B 1 97  ? 39.118 -24.007 4.313   1.00 16.07 ?  97  GLY   B HA3  1 
ATOM   5365 N  N    . PRO   B 1 98  ? 38.049 -24.622 6.830   1.00 14.85 ?  98  PRO   B N    1 
ATOM   5366 C  CA   . PRO   B 1 98  ? 38.140 -25.314 8.118   1.00 15.58 ?  98  PRO   B CA   1 
ATOM   5367 C  C    . PRO   B 1 98  ? 39.164 -26.439 8.076   1.00 15.46 ?  98  PRO   B C    1 
ATOM   5368 O  O    . PRO   B 1 98  ? 39.270 -27.179 7.098   1.00 15.82 ?  98  PRO   B O    1 
ATOM   5369 C  CB   . PRO   B 1 98  ? 36.719 -25.850 8.330   1.00 16.00 ?  98  PRO   B CB   1 
ATOM   5370 C  CG   . PRO   B 1 98  ? 36.153 -25.980 6.961   1.00 15.84 ?  98  PRO   B CG   1 
ATOM   5371 C  CD   . PRO   B 1 98  ? 36.725 -24.803 6.206   1.00 15.02 ?  98  PRO   B CD   1 
ATOM   5372 H  HA   . PRO   B 1 98  ? 38.369 -24.690 8.818   1.00 18.81 ?  98  PRO   B HA   1 
ATOM   5373 H  HB2  . PRO   B 1 98  ? 36.759 -26.713 8.769   1.00 19.31 ?  98  PRO   B HB2  1 
ATOM   5374 H  HB3  . PRO   B 1 98  ? 36.208 -25.216 8.853   1.00 19.31 ?  98  PRO   B HB3  1 
ATOM   5375 H  HG2  . PRO   B 1 98  ? 36.444 -26.818 6.563   1.00 19.13 ?  98  PRO   B HG2  1 
ATOM   5376 H  HG3  . PRO   B 1 98  ? 35.187 -25.932 6.997   1.00 19.13 ?  98  PRO   B HG3  1 
ATOM   5377 H  HD2  . PRO   B 1 98  ? 36.810 -25.016 5.259   1.00 18.14 ?  98  PRO   B HD2  1 
ATOM   5378 H  HD3  . PRO   B 1 98  ? 36.177 -24.014 6.341   1.00 18.14 ?  98  PRO   B HD3  1 
ATOM   5379 N  N    . ASN   B 1 99  ? 39.917 -26.563 9.158   1.00 16.65 ?  99  ASN   B N    1 
ATOM   5380 C  CA   . ASN   B 1 99  ? 40.894 -27.637 9.320   1.00 18.08 ?  99  ASN   B CA   1 
ATOM   5381 C  C    . ASN   B 1 99  ? 40.271 -28.720 10.200  1.00 20.59 ?  99  ASN   B C    1 
ATOM   5382 O  O    . ASN   B 1 99  ? 40.205 -28.579 11.423  1.00 21.33 ?  99  ASN   B O    1 
ATOM   5383 C  CB   . ASN   B 1 99  ? 42.166 -27.080 9.944   1.00 18.32 ?  99  ASN   B CB   1 
ATOM   5384 C  CG   . ASN   B 1 99  ? 43.300 -28.081 9.948   1.00 19.00 ?  99  ASN   B CG   1 
ATOM   5385 O  OD1  . ASN   B 1 99  ? 43.081 -29.272 10.118  1.00 19.91 ?  99  ASN   B OD1  1 
ATOM   5386 N  ND2  . ASN   B 1 99  ? 44.518 -27.603 9.756   1.00 18.80 ?  99  ASN   B ND2  1 
ATOM   5387 H  H    . ASN   B 1 99  ? 39.877 -26.029 9.826   1.00 20.10 ?  99  ASN   B H    1 
ATOM   5388 H  HA   . ASN   B 1 99  ? 41.105 -28.027 8.458   1.00 21.81 ?  99  ASN   B HA   1 
ATOM   5389 H  HB2  . ASN   B 1 99  ? 42.445 -26.305 9.443   1.00 22.10 ?  99  ASN   B HB2  1 
ATOM   5390 H  HB3  . ASN   B 1 99  ? 41.977 -26.837 10.866  1.00 22.10 ?  99  ASN   B HB3  1 
ATOM   5391 H  HD21 . ASN   B 1 99  ? 45.192 -28.133 9.744   1.00 22.68 ?  99  ASN   B HD21 1 
ATOM   5392 H  HD22 . ASN   B 1 99  ? 44.626 -26.759 9.639   1.00 22.68 ?  99  ASN   B HD22 1 
ATOM   5393 N  N    A VAL   B 1 100 ? 39.805 -29.804 9.572   0.64 22.21 ?  100 VAL   B N    1 
ATOM   5394 N  N    B VAL   B 1 100 ? 39.816 -29.805 9.565   0.36 22.42 ?  100 VAL   B N    1 
ATOM   5395 C  CA   A VAL   B 1 100 ? 39.185 -30.889 10.331  0.64 24.84 ?  100 VAL   B CA   1 
ATOM   5396 C  CA   B VAL   B 1 100 ? 39.189 -30.903 10.300  0.36 24.70 ?  100 VAL   B CA   1 
ATOM   5397 C  C    A VAL   B 1 100 ? 40.193 -31.546 11.263  0.64 25.45 ?  100 VAL   B C    1 
ATOM   5398 C  C    B VAL   B 1 100 ? 40.186 -31.573 11.237  0.36 25.36 ?  100 VAL   B C    1 
ATOM   5399 O  O    A VAL   B 1 100 ? 39.828 -32.039 12.338  0.64 26.11 ?  100 VAL   B O    1 
ATOM   5400 O  O    B VAL   B 1 100 ? 39.805 -32.095 12.292  0.36 25.70 ?  100 VAL   B O    1 
ATOM   5401 C  CB   A VAL   B 1 100 ? 38.529 -31.909 9.379   0.64 27.11 ?  100 VAL   B CB   1 
ATOM   5402 C  CB   B VAL   B 1 100 ? 38.553 -31.905 9.314   0.36 26.33 ?  100 VAL   B CB   1 
ATOM   5403 C  CG1  A VAL   B 1 100 ? 38.024 -33.118 10.156  0.64 28.00 ?  100 VAL   B CG1  1 
ATOM   5404 C  CG1  B VAL   B 1 100 ? 38.031 -33.132 10.050  0.36 26.89 ?  100 VAL   B CG1  1 
ATOM   5405 C  CG2  A VAL   B 1 100 ? 37.390 -31.258 8.614   0.64 27.51 ?  100 VAL   B CG2  1 
ATOM   5406 C  CG2  B VAL   B 1 100 ? 37.431 -31.236 8.535   0.36 26.69 ?  100 VAL   B CG2  1 
ATOM   5407 H  H    A VAL   B 1 100 ? 39.828 -29.928 8.721   0.64 26.76 ?  100 VAL   B H    1 
ATOM   5408 H  H    B VAL   B 1 100 ? 39.855 -29.925 8.714   0.36 27.02 ?  100 VAL   B H    1 
ATOM   5409 H  HA   A VAL   B 1 100 ? 38.474 -30.514 10.877  0.64 29.92 ?  100 VAL   B HA   1 
ATOM   5410 H  HA   B VAL   B 1 100 ? 38.471 -30.541 10.841  0.36 29.76 ?  100 VAL   B HA   1 
ATOM   5411 H  HB   A VAL   B 1 100 ? 39.189 -32.219 8.739   0.64 32.64 ?  100 VAL   B HB   1 
ATOM   5412 H  HB   B VAL   B 1 100 ? 39.225 -32.200 8.680   0.36 31.72 ?  100 VAL   B HB   1 
ATOM   5413 H  HG11 A VAL   B 1 100 ? 37.431 -33.634 9.586   0.64 33.72 ?  100 VAL   B HG11 1 
ATOM   5414 H  HG11 B VAL   B 1 100 ? 37.456 -33.637 9.451   0.36 32.39 ?  100 VAL   B HG11 1 
ATOM   5415 H  HG12 A VAL   B 1 100 ? 38.779 -33.666 10.425  0.64 33.72 ?  100 VAL   B HG12 1 
ATOM   5416 H  HG12 B VAL   B 1 100 ? 38.780 -33.682 10.326  0.36 32.39 ?  100 VAL   B HG12 1 
ATOM   5417 H  HG13 A VAL   B 1 100 ? 37.540 -32.812 10.940  0.64 33.72 ?  100 VAL   B HG13 1 
ATOM   5418 H  HG13 B VAL   B 1 100 ? 37.524 -32.844 10.825  0.36 32.39 ?  100 VAL   B HG13 1 
ATOM   5419 H  HG21 A VAL   B 1 100 ? 36.986 -31.917 8.027   0.64 33.13 ?  100 VAL   B HG21 1 
ATOM   5420 H  HG21 B VAL   B 1 100 ? 37.030 -31.887 7.938   0.36 32.14 ?  100 VAL   B HG21 1 
ATOM   5421 H  HG22 A VAL   B 1 100 ? 36.730 -30.933 9.248   0.64 33.13 ?  100 VAL   B HG22 1 
ATOM   5422 H  HG22 B VAL   B 1 100 ? 36.766 -30.907 9.160   0.36 32.14 ?  100 VAL   B HG22 1 
ATOM   5423 H  HG23 A VAL   B 1 100 ? 37.741 -30.521 8.093   0.64 33.13 ?  100 VAL   B HG23 1 
ATOM   5424 H  HG23 B VAL   B 1 100 ? 37.799 -30.500 8.023   0.36 32.14 ?  100 VAL   B HG23 1 
ATOM   5425 N  N    . ASN   B 1 101 ? 41.468 -31.587 10.867  1.00 25.81 ?  101 ASN   B N    1 
ATOM   5426 C  CA   . ASN   B 1 101 ? 42.508 -32.127 11.741  1.00 27.76 ?  101 ASN   B CA   1 
ATOM   5427 C  C    . ASN   B 1 101 ? 42.717 -31.289 12.997  1.00 30.04 ?  101 ASN   B C    1 
ATOM   5428 O  O    . ASN   B 1 101 ? 43.365 -31.766 13.937  1.00 31.09 ?  101 ASN   B O    1 
ATOM   5429 C  CB   . ASN   B 1 101 ? 43.827 -32.264 10.977  1.00 27.55 ?  101 ASN   B CB   1 
ATOM   5430 C  CG   . ASN   B 1 101 ? 43.820 -33.431 10.007  1.00 27.03 ?  101 ASN   B CG   1 
ATOM   5431 O  OD1  . ASN   B 1 101 ? 43.161 -34.435 10.244  1.00 27.94 ?  101 ASN   B OD1  1 
ATOM   5432 N  ND2  . ASN   B 1 101 ? 44.546 -33.297 8.906   1.00 26.41 ?  101 ASN   B ND2  1 
ATOM   5433 H  H    A ASN   B 1 101 ? 41.746 -31.329 10.097  0.64 31.08 ?  101 ASN   B H    1 
ATOM   5434 H  H    B ASN   B 1 101 ? 41.756 -31.302 10.110  0.36 31.08 ?  101 ASN   B H    1 
ATOM   5435 H  HA   . ASN   B 1 101 ? 42.239 -33.010 12.026  1.00 33.42 ?  101 ASN   B HA   1 
ATOM   5436 H  HB2  . ASN   B 1 101 ? 43.991 -31.457 10.468  1.00 33.18 ?  101 ASN   B HB2  1 
ATOM   5437 H  HB3  . ASN   B 1 101 ? 44.546 -32.407 11.613  1.00 33.18 ?  101 ASN   B HB3  1 
ATOM   5438 H  HD21 . ASN   B 1 101 ? 44.569 -33.933 8.327   1.00 31.80 ?  101 ASN   B HD21 1 
ATOM   5439 H  HD22 . ASN   B 1 101 ? 44.986 -32.573 8.768   1.00 31.80 ?  101 ASN   B HD22 1 
ATOM   5440 N  N    . LYS   B 1 102 ? 42.201 -30.059 13.026  1.00 32.51 ?  102 LYS   B N    1 
ATOM   5441 C  CA   . LYS   B 1 102 ? 42.172 -29.228 14.223  1.00 35.55 ?  102 LYS   B CA   1 
ATOM   5442 C  C    . LYS   B 1 102 ? 40.788 -29.179 14.861  1.00 34.82 ?  102 LYS   B C    1 
ATOM   5443 O  O    . LYS   B 1 102 ? 40.567 -28.381 15.776  1.00 35.29 ?  102 LYS   B O    1 
ATOM   5444 C  CB   . LYS   B 1 102 ? 42.622 -27.803 13.897  1.00 38.96 ?  102 LYS   B CB   1 
ATOM   5445 C  CG   . LYS   B 1 102 ? 44.083 -27.654 13.511  1.00 42.38 ?  102 LYS   B CG   1 
ATOM   5446 C  CD   . LYS   B 1 102 ? 44.343 -26.243 13.007  1.00 45.07 ?  102 LYS   B CD   1 
ATOM   5447 C  CE   . LYS   B 1 102 ? 45.823 -25.945 12.856  1.00 47.18 ?  102 LYS   B CE   1 
ATOM   5448 N  NZ   . LYS   B 1 102 ? 46.039 -24.545 12.384  1.00 48.40 ?  102 LYS   B NZ   1 
ATOM   5449 H  H    . LYS   B 1 102 ? 41.850 -29.672 12.342  1.00 39.13 ?  102 LYS   B H    1 
ATOM   5450 H  HA   . LYS   B 1 102 ? 42.791 -29.592 14.873  1.00 42.77 ?  102 LYS   B HA   1 
ATOM   5451 H  HB2  . LYS   B 1 102 ? 42.091 -27.471 13.157  1.00 46.87 ?  102 LYS   B HB2  1 
ATOM   5452 H  HB3  . LYS   B 1 102 ? 42.472 -27.245 14.678  1.00 46.87 ?  102 LYS   B HB3  1 
ATOM   5453 H  HG2  . LYS   B 1 102 ? 44.644 -27.813 14.287  1.00 50.97 ?  102 LYS   B HG2  1 
ATOM   5454 H  HG3  . LYS   B 1 102 ? 44.298 -28.280 12.802  1.00 50.97 ?  102 LYS   B HG3  1 
ATOM   5455 H  HD2  . LYS   B 1 102 ? 43.923 -26.135 12.139  1.00 54.19 ?  102 LYS   B HD2  1 
ATOM   5456 H  HD3  . LYS   B 1 102 ? 43.970 -25.608 13.638  1.00 54.19 ?  102 LYS   B HD3  1 
ATOM   5457 H  HE2  . LYS   B 1 102 ? 46.262 -26.049 13.715  1.00 56.73 ?  102 LYS   B HE2  1 
ATOM   5458 H  HE3  . LYS   B 1 102 ? 46.209 -26.551 12.204  1.00 56.73 ?  102 LYS   B HE3  1 
ATOM   5459 H  HZ1  . LYS   B 1 102 ? 46.909 -24.383 12.300  1.00 58.20 ?  102 LYS   B HZ1  1 
ATOM   5460 H  HZ2  . LYS   B 1 102 ? 45.644 -24.426 11.595  1.00 58.20 ?  102 LYS   B HZ2  1 
ATOM   5461 H  HZ3  . LYS   B 1 102 ? 45.692 -23.970 12.969  1.00 58.20 ?  102 LYS   B HZ3  1 
ATOM   5462 N  N    . GLY   B 1 103 ? 39.850 -29.995 14.388  1.00 33.75 ?  103 GLY   B N    1 
ATOM   5463 C  CA   . GLY   B 1 103 ? 38.522 -30.047 14.966  1.00 33.05 ?  103 GLY   B CA   1 
ATOM   5464 C  C    . GLY   B 1 103 ? 37.572 -28.965 14.508  1.00 31.90 ?  103 GLY   B C    1 
ATOM   5465 O  O    . GLY   B 1 103 ? 36.481 -28.840 15.077  1.00 32.27 ?  103 GLY   B O    1 
ATOM   5466 H  H    . GLY   B 1 103 ? 39.962 -30.530 13.726  1.00 40.62 ?  103 GLY   B H    1 
ATOM   5467 H  HA2  . GLY   B 1 103 ? 38.121 -30.902 14.751  1.00 39.78 ?  103 GLY   B HA2  1 
ATOM   5468 H  HA3  . GLY   B 1 103 ? 38.599 -29.988 15.932  1.00 39.78 ?  103 GLY   B HA3  1 
ATOM   5469 N  N    A GLU   B 1 104 ? 37.951 -28.172 13.508  0.64 30.80 ?  104 GLU   B N    1 
ATOM   5470 N  N    B GLU   B 1 104 ? 37.933 -28.191 13.489  0.36 31.25 ?  104 GLU   B N    1 
ATOM   5471 C  CA   A GLU   B 1 104 ? 37.112 -27.074 13.055  0.64 29.55 ?  104 GLU   B CA   1 
ATOM   5472 C  CA   B GLU   B 1 104 ? 37.074 -27.114 13.022  0.36 30.40 ?  104 GLU   B CA   1 
ATOM   5473 C  C    A GLU   B 1 104 ? 35.924 -27.601 12.248  0.64 29.65 ?  104 GLU   B C    1 
ATOM   5474 C  C    B GLU   B 1 104 ? 35.916 -27.663 12.192  0.36 30.36 ?  104 GLU   B C    1 
ATOM   5475 O  O    A GLU   B 1 104 ? 35.959 -28.692 11.670  0.64 30.00 ?  104 GLU   B O    1 
ATOM   5476 O  O    B GLU   B 1 104 ? 36.000 -28.744 11.601  0.36 30.51 ?  104 GLU   B O    1 
ATOM   5477 C  CB   A GLU   B 1 104 ? 37.945 -26.077 12.245  0.64 28.26 ?  104 GLU   B CB   1 
ATOM   5478 C  CB   B GLU   B 1 104 ? 37.893 -26.098 12.226  0.36 29.54 ?  104 GLU   B CB   1 
ATOM   5479 C  CG   A GLU   B 1 104 ? 39.056 -25.436 13.074  0.64 26.93 ?  104 GLU   B CG   1 
ATOM   5480 C  CG   B GLU   B 1 104 ? 38.991 -25.454 13.065  0.36 28.65 ?  104 GLU   B CG   1 
ATOM   5481 C  CD   A GLU   B 1 104 ? 39.984 -24.550 12.271  0.64 25.45 ?  104 GLU   B CD   1 
ATOM   5482 C  CD   B GLU   B 1 104 ? 39.933 -24.583 12.260  0.36 27.78 ?  104 GLU   B CD   1 
ATOM   5483 O  OE1  A GLU   B 1 104 ? 39.969 -24.613 11.025  0.64 23.55 ?  104 GLU   B OE1  1 
ATOM   5484 O  OE1  B GLU   B 1 104 ? 39.867 -24.609 11.013  0.36 27.10 ?  104 GLU   B OE1  1 
ATOM   5485 O  OE2  A GLU   B 1 104 ? 40.739 -23.784 12.903  0.64 25.51 -1 104 GLU   B OE2  1 
ATOM   5486 O  OE2  B GLU   B 1 104 ? 40.745 -23.868 12.882  0.36 27.65 -1 104 GLU   B OE2  1 
ATOM   5487 H  H    A GLU   B 1 104 ? 38.695 -28.246 13.084  0.64 37.08 ?  104 GLU   B H    1 
ATOM   5488 H  H    B GLU   B 1 104 ? 38.672 -28.266 13.057  0.36 37.61 ?  104 GLU   B H    1 
ATOM   5489 H  HA   A GLU   B 1 104 ? 36.766 -26.604 13.830  0.64 35.58 ?  104 GLU   B HA   1 
ATOM   5490 H  HA   B GLU   B 1 104 ? 36.700 -26.657 13.788  0.36 36.60 ?  104 GLU   B HA   1 
ATOM   5491 H  HB2  A GLU   B 1 104 ? 38.357 -26.536 11.496  0.64 34.03 ?  104 GLU   B HB2  1 
ATOM   5492 H  HB2  B GLU   B 1 104 ? 38.311 -26.543 11.473  0.36 35.56 ?  104 GLU   B HB2  1 
ATOM   5493 H  HB3  A GLU   B 1 104 ? 37.368 -25.366 11.921  0.64 34.03 ?  104 GLU   B HB3  1 
ATOM   5494 H  HB3  B GLU   B 1 104 ? 37.305 -25.392 11.911  0.36 35.56 ?  104 GLU   B HB3  1 
ATOM   5495 H  HG2  A GLU   B 1 104 ? 38.661 -24.887 13.770  0.64 32.43 ?  104 GLU   B HG2  1 
ATOM   5496 H  HG2  B GLU   B 1 104 ? 38.582 -24.898 13.748  0.36 34.50 ?  104 GLU   B HG2  1 
ATOM   5497 H  HG3  A GLU   B 1 104 ? 39.599 -26.132 13.476  0.64 32.43 ?  104 GLU   B HG3  1 
ATOM   5498 H  HG3  B GLU   B 1 104 ? 39.518 -26.152 13.486  0.36 34.50 ?  104 GLU   B HG3  1 
ATOM   5499 N  N    A ASP   B 1 105 ? 34.859 -26.803 12.221  0.64 29.59 ?  105 ASP   B N    1 
ATOM   5500 N  N    B ASP   B 1 105 ? 34.825 -26.901 12.160  0.36 30.39 ?  105 ASP   B N    1 
ATOM   5501 C  CA   A ASP   B 1 105 ? 33.580 -27.249 11.679  0.64 30.16 ?  105 ASP   B CA   1 
ATOM   5502 C  CA   B ASP   B 1 105 ? 33.564 -27.374 11.600  0.36 30.42 ?  105 ASP   B CA   1 
ATOM   5503 C  C    A ASP   B 1 105 ? 33.637 -27.306 10.157  0.64 27.98 ?  105 ASP   B C    1 
ATOM   5504 C  C    B ASP   B 1 105 ? 33.640 -27.388 10.077  0.36 29.21 ?  105 ASP   B C    1 
ATOM   5505 O  O    A ASP   B 1 105 ? 33.805 -26.277 9.494   0.64 26.97 ?  105 ASP   B O    1 
ATOM   5506 O  O    B ASP   B 1 105 ? 33.846 -26.344 9.448   0.36 28.88 ?  105 ASP   B O    1 
ATOM   5507 C  CB   A ASP   B 1 105 ? 32.472 -26.300 12.132  0.64 33.24 ?  105 ASP   B CB   1 
ATOM   5508 C  CB   B ASP   B 1 105 ? 32.417 -26.481 12.071  0.36 31.82 ?  105 ASP   B CB   1 
ATOM   5509 C  CG   A ASP   B 1 105 ? 31.097 -26.750 11.681  0.64 35.60 ?  105 ASP   B CG   1 
ATOM   5510 C  CG   B ASP   B 1 105 ? 31.054 -27.047 11.716  0.36 32.72 ?  105 ASP   B CG   1 
ATOM   5511 O  OD1  A ASP   B 1 105 ? 30.978 -27.874 11.150  0.64 35.90 ?  105 ASP   B OD1  1 
ATOM   5512 O  OD1  B ASP   B 1 105 ? 31.000 -28.071 11.002  0.36 32.92 ?  105 ASP   B OD1  1 
ATOM   5513 O  OD2  A ASP   B 1 105 ? 30.133 -25.971 11.848  0.64 36.97 -1 105 ASP   B OD2  1 
ATOM   5514 O  OD2  B ASP   B 1 105 ? 30.034 -26.474 12.157  0.36 33.10 -1 105 ASP   B OD2  1 
ATOM   5515 H  H    A ASP   B 1 105 ? 34.853 -25.995 12.512  0.64 35.63 ?  105 ASP   B H    1 
ATOM   5516 H  H    B ASP   B 1 105 ? 34.792 -26.096 12.456  0.36 36.58 ?  105 ASP   B H    1 
ATOM   5517 H  HA   A ASP   B 1 105 ? 33.379 -28.137 12.015  0.64 36.31 ?  105 ASP   B HA   1 
ATOM   5518 H  HA   B ASP   B 1 105 ? 33.389 -28.278 11.906  0.36 36.62 ?  105 ASP   B HA   1 
ATOM   5519 H  HB2  A ASP   B 1 105 ? 32.486 -26.236 13.103  0.64 40.00 ?  105 ASP   B HB2  1 
ATOM   5520 H  HB2  B ASP   B 1 105 ? 32.462 -26.389 13.037  0.36 38.29 ?  105 ASP   B HB2  1 
ATOM   5521 H  HB3  A ASP   B 1 105 ? 32.621 -25.427 11.741  0.64 40.00 ?  105 ASP   B HB3  1 
ATOM   5522 H  HB3  B ASP   B 1 105 ? 32.503 -25.607 11.654  0.36 38.29 ?  105 ASP   B HB3  1 
ATOM   5523 N  N    A ILE   B 1 106 ? 33.460 -28.509 9.605   0.64 27.32 ?  106 ILE   B N    1 
ATOM   5524 N  N    B ILE   B 1 106 ? 33.457 -28.573 9.489   0.36 28.47 ?  106 ILE   B N    1 
ATOM   5525 C  CA   A ILE   B 1 106 ? 33.463 -28.696 8.159   0.64 26.32 ?  106 ILE   B CA   1 
ATOM   5526 C  CA   B ILE   B 1 106 ? 33.467 -28.719 8.038   0.36 27.76 ?  106 ILE   B CA   1 
ATOM   5527 C  C    A ILE   B 1 106 ? 32.373 -27.875 7.478   0.64 25.11 ?  106 ILE   B C    1 
ATOM   5528 C  C    B ILE   B 1 106 ? 32.368 -27.898 7.377   0.36 26.86 ?  106 ILE   B C    1 
ATOM   5529 O  O    A ILE   B 1 106 ? 32.489 -27.559 6.289   0.64 24.19 ?  106 ILE   B O    1 
ATOM   5530 O  O    B ILE   B 1 106 ? 32.448 -27.607 6.179   0.36 26.51 ?  106 ILE   B O    1 
ATOM   5531 C  CB   A ILE   B 1 106 ? 33.355 -30.203 7.831   0.64 27.16 ?  106 ILE   B CB   1 
ATOM   5532 C  CB   B ILE   B 1 106 ? 33.373 -30.218 7.668   0.36 28.15 ?  106 ILE   B CB   1 
ATOM   5533 C  CG1  A ILE   B 1 106 ? 33.612 -30.461 6.346   0.64 27.81 ?  106 ILE   B CG1  1 
ATOM   5534 C  CG1  B ILE   B 1 106 ? 33.661 -30.437 6.181   0.36 28.50 ?  106 ILE   B CG1  1 
ATOM   5535 C  CG2  A ILE   B 1 106 ? 31.990 -30.746 8.240   0.64 27.72 ?  106 ILE   B CG2  1 
ATOM   5536 C  CG2  B ILE   B 1 106 ? 32.004 -30.777 8.035   0.36 28.45 ?  106 ILE   B CG2  1 
ATOM   5537 C  CD1  A ILE   B 1 106 ? 34.984 -30.027 5.886   0.64 27.93 ?  106 ILE   B CD1  1 
ATOM   5538 C  CD1  B ILE   B 1 106 ? 35.028 -29.960 5.750   0.36 28.65 ?  106 ILE   B CD1  1 
ATOM   5539 H  H    A ILE   B 1 106 ? 33.335 -29.231 10.055  0.64 32.90 ?  106 ILE   B H    1 
ATOM   5540 H  H    B ILE   B 1 106 ? 33.332 -29.308 9.913   0.36 34.28 ?  106 ILE   B H    1 
ATOM   5541 H  HA   A ILE   B 1 106 ? 34.310 -28.383 7.821   0.64 31.70 ?  106 ILE   B HA   1 
ATOM   5542 H  HA   B ILE   B 1 106 ? 34.312 -28.385 7.709   0.36 33.43 ?  106 ILE   B HA   1 
ATOM   5543 H  HB   A ILE   B 1 106 ? 34.029 -30.675 8.345   0.64 32.71 ?  106 ILE   B HB   1 
ATOM   5544 H  HB   B ILE   B 1 106 ? 34.040 -30.698 8.180   0.36 33.90 ?  106 ILE   B HB   1 
ATOM   5545 H  HG12 A ILE   B 1 106 ? 33.534 -31.414 6.177   0.64 33.48 ?  106 ILE   B HG12 1 
ATOM   5546 H  HG12 B ILE   B 1 106 ? 33.609 -31.389 5.990   0.36 34.31 ?  106 ILE   B HG12 1 
ATOM   5547 H  HG13 A ILE   B 1 106 ? 32.956 -29.979 5.822   0.64 33.48 ?  106 ILE   B HG13 1 
ATOM   5548 H  HG13 B ILE   B 1 106 ? 33.001 -29.962 5.656   0.36 34.31 ?  106 ILE   B HG13 1 
ATOM   5549 H  HG21 A ILE   B 1 106 ? 31.999 -31.713 8.164   0.64 33.38 ?  106 ILE   B HG21 1 
ATOM   5550 H  HG21 B ILE   B 1 106 ? 32.024 -31.743 7.942   0.36 34.26 ?  106 ILE   B HG21 1 
ATOM   5551 H  HG22 A ILE   B 1 106 ? 31.810 -30.490 9.159   0.64 33.38 ?  106 ILE   B HG22 1 
ATOM   5552 H  HG22 B ILE   B 1 106 ? 31.801 -30.539 8.953   0.36 34.26 ?  106 ILE   B HG22 1 
ATOM   5553 H  HG23 A ILE   B 1 106 ? 31.312 -30.375 7.655   0.64 33.38 ?  106 ILE   B HG23 1 
ATOM   5554 H  HG23 B ILE   B 1 106 ? 31.336 -30.402 7.440   0.36 34.26 ?  106 ILE   B HG23 1 
ATOM   5555 H  HD11 A ILE   B 1 106 ? 35.172 -30.434 5.027   0.64 33.63 ?  106 ILE   B HD11 1 
ATOM   5556 H  HD11 B ILE   B 1 106 ? 35.241 -30.355 4.891   0.36 34.50 ?  106 ILE   B HD11 1 
ATOM   5557 H  HD12 A ILE   B 1 106 ? 35.000 -29.060 5.804   0.64 33.63 ?  106 ILE   B HD12 1 
ATOM   5558 H  HD12 B ILE   B 1 106 ? 35.016 -28.993 5.676   0.36 34.50 ?  106 ILE   B HD12 1 
ATOM   5559 H  HD13 A ILE   B 1 106 ? 35.643 -30.315 6.538   0.64 33.63 ?  106 ILE   B HD13 1 
ATOM   5560 H  HD13 B ILE   B 1 106 ? 35.681 -30.236 6.412   0.36 34.50 ?  106 ILE   B HD13 1 
ATOM   5561 N  N    A GLN   B 1 107 ? 31.315 -27.510 8.206   0.64 25.45 ?  107 GLN   B N    1 
ATOM   5562 N  N    B GLN   B 1 107 ? 31.337 -27.508 8.132   0.36 26.73 ?  107 GLN   B N    1 
ATOM   5563 C  CA   A GLN   B 1 107 ? 30.244 -26.710 7.619   0.64 25.72 ?  107 GLN   B CA   1 
ATOM   5564 C  CA   B GLN   B 1 107 ? 30.254 -26.713 7.565   0.36 26.59 ?  107 GLN   B CA   1 
ATOM   5565 C  C    A GLN   B 1 107 ? 30.737 -25.364 7.102   0.64 23.69 ?  107 GLN   B C    1 
ATOM   5566 C  C    B GLN   B 1 107 ? 30.727 -25.340 7.104   0.36 24.24 ?  107 GLN   B C    1 
ATOM   5567 O  O    A GLN   B 1 107 ? 30.099 -24.786 6.217   0.64 24.06 ?  107 GLN   B O    1 
ATOM   5568 O  O    B GLN   B 1 107 ? 30.062 -24.719 6.269   0.36 24.47 ?  107 GLN   B O    1 
ATOM   5569 C  CB   A GLN   B 1 107 ? 29.128 -26.499 8.647   0.64 28.97 ?  107 GLN   B CB   1 
ATOM   5570 C  CB   B GLN   B 1 107 ? 29.126 -26.570 8.591   0.36 28.96 ?  107 GLN   B CB   1 
ATOM   5571 C  CG   A GLN   B 1 107 ? 27.809 -25.990 8.066   0.64 32.33 ?  107 GLN   B CG   1 
ATOM   5572 C  CG   B GLN   B 1 107 ? 27.800 -26.077 8.022   0.36 31.33 ?  107 GLN   B CG   1 
ATOM   5573 C  CD   A GLN   B 1 107 ? 27.749 -24.476 7.959   0.64 34.81 ?  107 GLN   B CD   1 
ATOM   5574 C  CD   B GLN   B 1 107 ? 27.680 -24.564 8.030   0.36 33.12 ?  107 GLN   B CD   1 
ATOM   5575 O  OE1  A GLN   B 1 107 ? 28.580 -23.767 8.529   0.64 35.72 ?  107 GLN   B OE1  1 
ATOM   5576 O  OE1  B GLN   B 1 107 ? 28.494 -23.866 8.637   0.36 33.74 ?  107 GLN   B OE1  1 
ATOM   5577 N  NE2  A GLN   B 1 107 ? 26.758 -23.972 7.227   0.64 35.77 ?  107 GLN   B NE2  1 
ATOM   5578 N  NE2  B GLN   B 1 107 ? 26.656 -24.048 7.356   0.36 33.87 ?  107 GLN   B NE2  1 
ATOM   5579 H  H    A GLN   B 1 107 ? 31.197 -27.709 9.030   0.64 30.65 ?  107 GLN   B H    1 
ATOM   5580 H  H    B GLN   B 1 107 ? 31.242 -27.688 8.965   0.36 32.19 ?  107 GLN   B H    1 
ATOM   5581 H  HA   A GLN   B 1 107 ? 29.864 -27.196 6.869   0.64 30.97 ?  107 GLN   B HA   1 
ATOM   5582 H  HA   B GLN   B 1 107 ? 29.894 -27.178 6.795   0.36 32.02 ?  107 GLN   B HA   1 
ATOM   5583 H  HB2  A GLN   B 1 107 ? 28.947 -27.344 9.081   0.64 34.88 ?  107 GLN   B HB2  1 
ATOM   5584 H  HB2  B GLN   B 1 107 ? 28.964 -27.436 8.989   0.36 34.86 ?  107 GLN   B HB2  1 
ATOM   5585 H  HB3  A GLN   B 1 107 ? 29.430 -25.852 9.304   0.64 34.88 ?  107 GLN   B HB3  1 
ATOM   5586 H  HB3  B GLN   B 1 107 ? 29.405 -25.943 9.276   0.36 34.86 ?  107 GLN   B HB3  1 
ATOM   5587 H  HG2  A GLN   B 1 107 ? 27.692 -26.355 7.176   0.64 38.91 ?  107 GLN   B HG2  1 
ATOM   5588 H  HG2  B GLN   B 1 107 ? 27.715 -26.378 7.104   0.36 37.71 ?  107 GLN   B HG2  1 
ATOM   5589 H  HG3  A GLN   B 1 107 ? 27.080 -26.280 8.640   0.64 38.91 ?  107 GLN   B HG3  1 
ATOM   5590 H  HG3  B GLN   B 1 107 ? 27.073 -26.440 8.557   0.36 37.71 ?  107 GLN   B HG3  1 
ATOM   5591 H  HE21 A GLN   B 1 107 ? 26.195 -24.499 6.842   0.64 43.04 ?  107 GLN   B HE21 1 
ATOM   5592 H  HE21 B GLN   B 1 107 ? 26.107 -24.566 6.943   0.36 40.76 ?  107 GLN   B HE21 1 
ATOM   5593 H  HE22 A GLN   B 1 107 ? 26.675 -23.120 7.137   0.64 43.04 ?  107 GLN   B HE22 1 
ATOM   5594 H  HE22 B GLN   B 1 107 ? 26.543 -23.196 7.333   0.36 40.76 ?  107 GLN   B HE22 1 
ATOM   5595 N  N    . LEU   B 1 108 ? 31.858 -24.856 7.621   1.00 21.91 ?  108 LEU   B N    1 
ATOM   5596 C  CA   . LEU   B 1 108 ? 32.396 -23.558 7.211   1.00 19.48 ?  108 LEU   B CA   1 
ATOM   5597 C  C    . LEU   B 1 108 ? 33.046 -23.580 5.836   1.00 16.79 ?  108 LEU   B C    1 
ATOM   5598 O  O    . LEU   B 1 108 ? 33.476 -22.520 5.353   1.00 16.06 ?  108 LEU   B O    1 
ATOM   5599 C  CB   . LEU   B 1 108 ? 33.391 -23.055 8.255   1.00 20.11 ?  108 LEU   B CB   1 
ATOM   5600 C  CG   . LEU   B 1 108 ? 32.773 -22.572 9.568   1.00 21.66 ?  108 LEU   B CG   1 
ATOM   5601 C  CD1  . LEU   B 1 108 ? 33.812 -22.551 10.672  1.00 22.22 ?  108 LEU   B CD1  1 
ATOM   5602 C  CD2  . LEU   B 1 108 ? 32.171 -21.189 9.382   1.00 22.57 ?  108 LEU   B CD2  1 
ATOM   5603 H  H    A LEU   B 1 108 ? 32.319 -25.245 8.229   0.64 26.41 ?  108 LEU   B H    1 
ATOM   5604 H  H    B LEU   B 1 108 ? 32.321 -25.256 8.220   0.36 26.41 ?  108 LEU   B H    1 
ATOM   5605 H  HA   . LEU   B 1 108 ? 31.666 -22.924 7.174   1.00 23.49 ?  108 LEU   B HA   1 
ATOM   5606 H  HB2  . LEU   B 1 108 ? 33.999 -23.777 8.474   1.00 24.25 ?  108 LEU   B HB2  1 
ATOM   5607 H  HB3  . LEU   B 1 108 ? 33.883 -22.314 7.878   1.00 24.25 ?  108 LEU   B HB3  1 
ATOM   5608 H  HG   . LEU   B 1 108 ? 32.060 -23.177 9.833   1.00 26.11 ?  108 LEU   B HG   1 
ATOM   5609 H  HD11 . LEU   B 1 108 ? 33.388 -22.276 11.501  1.00 26.78 ?  108 LEU   B HD11 1 
ATOM   5610 H  HD12 . LEU   B 1 108 ? 34.186 -23.439 10.770  1.00 26.78 ?  108 LEU   B HD12 1 
ATOM   5611 H  HD13 . LEU   B 1 108 ? 34.510 -21.921 10.434  1.00 26.78 ?  108 LEU   B HD13 1 
ATOM   5612 H  HD21 . LEU   B 1 108 ? 31.804 -20.886 10.228  1.00 27.20 ?  108 LEU   B HD21 1 
ATOM   5613 H  HD22 . LEU   B 1 108 ? 32.865 -20.580 9.087   1.00 27.20 ?  108 LEU   B HD22 1 
ATOM   5614 H  HD23 . LEU   B 1 108 ? 31.467 -21.236 8.716   1.00 27.20 ?  108 LEU   B HD23 1 
ATOM   5615 N  N    . LEU   B 1 109 ? 33.101 -24.746 5.195   1.00 15.81 ?  109 LEU   B N    1 
ATOM   5616 C  CA   . LEU   B 1 109 ? 33.735 -24.855 3.887   1.00 14.82 ?  109 LEU   B CA   1 
ATOM   5617 C  C    . LEU   B 1 109 ? 32.974 -24.073 2.824   1.00 14.18 ?  109 LEU   B C    1 
ATOM   5618 O  O    . LEU   B 1 109 ? 33.595 -23.478 1.933   1.00 13.87 ?  109 LEU   B O    1 
ATOM   5619 C  CB   . LEU   B 1 109 ? 33.848 -26.330 3.505   1.00 15.13 ?  109 LEU   B CB   1 
ATOM   5620 C  CG   . LEU   B 1 109 ? 34.645 -26.679 2.250   1.00 14.73 ?  109 LEU   B CG   1 
ATOM   5621 C  CD1  . LEU   B 1 109 ? 36.020 -26.016 2.268   1.00 14.38 ?  109 LEU   B CD1  1 
ATOM   5622 C  CD2  . LEU   B 1 109 ? 34.790 -28.191 2.128   1.00 15.57 ?  109 LEU   B CD2  1 
ATOM   5623 H  H    . LEU   B 1 109 ? 32.794 -25.491 5.493   1.00 19.08 ?  109 LEU   B H    1 
ATOM   5624 H  HA   . LEU   B 1 109 ? 34.631 -24.494 3.936   1.00 17.90 ?  109 LEU   B HA   1 
ATOM   5625 H  HB2  . LEU   B 1 109 ? 34.268 -26.803 4.239   1.00 18.28 ?  109 LEU   B HB2  1 
ATOM   5626 H  HB3  . LEU   B 1 109 ? 32.953 -26.682 3.372   1.00 18.28 ?  109 LEU   B HB3  1 
ATOM   5627 H  HG   . LEU   B 1 109 ? 34.166 -26.370 1.462   1.00 17.79 ?  109 LEU   B HG   1 
ATOM   5628 H  HD11 . LEU   B 1 109 ? 36.560 -26.387 1.552   1.00 17.38 ?  109 LEU   B HD11 1 
ATOM   5629 H  HD12 . LEU   B 1 109 ? 35.907 -25.064 2.138   1.00 17.38 ?  109 LEU   B HD12 1 
ATOM   5630 H  HD13 . LEU   B 1 109 ? 36.439 -26.192 3.124   1.00 17.38 ?  109 LEU   B HD13 1 
ATOM   5631 H  HD21 . LEU   B 1 109 ? 35.362 -28.399 1.368   1.00 18.80 ?  109 LEU   B HD21 1 
ATOM   5632 H  HD22 . LEU   B 1 109 ? 35.187 -28.539 2.941   1.00 18.80 ?  109 LEU   B HD22 1 
ATOM   5633 H  HD23 . LEU   B 1 109 ? 33.913 -28.588 1.993   1.00 18.80 ?  109 LEU   B HD23 1 
ATOM   5634 N  N    . LYS   B 1 110 ? 31.639 -24.041 2.900   1.00 13.91 ?  110 LYS   B N    1 
ATOM   5635 C  CA   . LYS   B 1 110 ? 30.883 -23.275 1.913   1.00 13.97 ?  110 LYS   B CA   1 
ATOM   5636 C  C    . LYS   B 1 110 ? 31.228 -21.787 2.003   1.00 13.66 ?  110 LYS   B C    1 
ATOM   5637 O  O    . LYS   B 1 110 ? 31.487 -21.138 0.984   1.00 13.30 ?  110 LYS   B O    1 
ATOM   5638 C  CB   . LYS   B 1 110 ? 29.376 -23.523 2.061   1.00 14.43 ?  110 LYS   B CB   1 
ATOM   5639 C  CG   . LYS   B 1 110 ? 28.566 -22.897 0.930   1.00 14.70 ?  110 LYS   B CG   1 
ATOM   5640 C  CD   . LYS   B 1 110 ? 27.099 -23.332 0.953   1.00 15.08 ?  110 LYS   B CD   1 
ATOM   5641 C  CE   . LYS   B 1 110 ? 26.335 -22.798 -0.261  1.00 15.87 ?  110 LYS   B CE   1 
ATOM   5642 N  NZ   . LYS   B 1 110 ? 26.661 -23.529 -1.514  1.00 16.12 ?  110 LYS   B NZ   1 
ATOM   5643 H  H    . LYS   B 1 110 ? 31.166 -24.447 3.485   1.00 16.81 ?  110 LYS   B H    1 
ATOM   5644 H  HA   . LYS   B 1 110 ? 31.141 -23.574 1.023   1.00 16.88 ?  110 LYS   B HA   1 
ATOM   5645 H  HB2  . LYS   B 1 110 ? 29.213 -24.481 2.049   1.00 17.43 ?  110 LYS   B HB2  1 
ATOM   5646 H  HB3  . LYS   B 1 110 ? 29.073 -23.143 2.896   1.00 17.43 ?  110 LYS   B HB3  1 
ATOM   5647 H  HG2  . LYS   B 1 110 ? 28.586 -21.931 1.018   1.00 17.75 ?  110 LYS   B HG2  1 
ATOM   5648 H  HG3  . LYS   B 1 110 ? 28.938 -23.164 0.077   1.00 17.75 ?  110 LYS   B HG3  1 
ATOM   5649 H  HD2  . LYS   B 1 110 ? 27.048 -24.304 0.940   1.00 18.21 ?  110 LYS   B HD2  1 
ATOM   5650 H  HD3  . LYS   B 1 110 ? 26.670 -22.990 1.756   1.00 18.21 ?  110 LYS   B HD3  1 
ATOM   5651 H  HE2  . LYS   B 1 110 ? 25.382 -22.885 -0.103  1.00 19.16 ?  110 LYS   B HE2  1 
ATOM   5652 H  HE3  . LYS   B 1 110 ? 26.566 -21.865 -0.391  1.00 19.16 ?  110 LYS   B HE3  1 
ATOM   5653 H  HZ1  . LYS   B 1 110 ? 26.202 -23.190 -2.194  1.00 19.46 ?  110 LYS   B HZ1  1 
ATOM   5654 H  HZ2  . LYS   B 1 110 ? 27.532 -23.461 -1.688  1.00 19.46 ?  110 LYS   B HZ2  1 
ATOM   5655 H  HZ3  . LYS   B 1 110 ? 26.453 -24.392 -1.425  1.00 19.46 ?  110 LYS   B HZ3  1 
ATOM   5656 N  N    . SER   B 1 111 ? 31.248 -21.235 3.224   1.00 13.92 ?  111 SER   B N    1 
ATOM   5657 C  CA   . SER   B 1 111 ? 31.639 -19.837 3.401   1.00 13.93 ?  111 SER   B CA   1 
ATOM   5658 C  C    . SER   B 1 111 ? 33.019 -19.579 2.810   1.00 13.35 ?  111 SER   B C    1 
ATOM   5659 O  O    . SER   B 1 111 ? 33.247 -18.547 2.161   1.00 13.36 ?  111 SER   B O    1 
ATOM   5660 C  CB   . SER   B 1 111 ? 31.636 -19.476 4.886   1.00 15.17 ?  111 SER   B CB   1 
ATOM   5661 O  OG   . SER   B 1 111 ? 30.332 -19.473 5.424   1.00 16.74 ?  111 SER   B OG   1 
ATOM   5662 H  H    . SER   B 1 111 ? 31.051 -21.653 3.948   1.00 16.82 ?  111 SER   B H    1 
ATOM   5663 H  HA   . SER   B 1 111 ? 31.004 -19.270 2.946   1.00 16.83 ?  111 SER   B HA   1 
ATOM   5664 H  HB2  . SER   B 1 111 ? 32.160 -20.134 5.370   1.00 18.32 ?  111 SER   B HB2  1 
ATOM   5665 H  HB3  . SER   B 1 111 ? 32.022 -18.599 4.995   1.00 18.32 ?  111 SER   B HB3  1 
ATOM   5666 H  HG   . SER   B 1 111 ? 30.352 -19.263 6.242   1.00 20.21 ?  111 SER   B HG   1 
ATOM   5667 N  N    . ALA   B 1 112 ? 33.952 -20.504 3.023   1.00 13.22 ?  112 ALA   B N    1 
ATOM   5668 C  CA   . ALA   B 1 112 ? 35.298 -20.330 2.487   1.00 12.95 ?  112 ALA   B CA   1 
ATOM   5669 C  C    . ALA   B 1 112 ? 35.274 -20.234 0.964   1.00 12.24 ?  112 ALA   B C    1 
ATOM   5670 O  O    . ALA   B 1 112 ? 35.903 -19.345 0.372   1.00 12.38 ?  112 ALA   B O    1 
ATOM   5671 C  CB   . ALA   B 1 112 ? 36.196 -21.476 2.962   1.00 13.69 ?  112 ALA   B CB   1 
ATOM   5672 H  H    . ALA   B 1 112 ? 33.832 -21.235 3.474   1.00 15.97 ?  112 ALA   B H    1 
ATOM   5673 H  HA   . ALA   B 1 112 ? 35.661 -19.503 2.834   1.00 15.66 ?  112 ALA   B HA   1 
ATOM   5674 H  HB1  . ALA   B 1 112 ? 37.089 -21.340 2.602   1.00 16.54 ?  112 ALA   B HB1  1 
ATOM   5675 H  HB2  . ALA   B 1 112 ? 36.232 -21.469 3.933   1.00 16.54 ?  112 ALA   B HB2  1 
ATOM   5676 H  HB3  . ALA   B 1 112 ? 35.836 -22.315 2.649   1.00 16.54 ?  112 ALA   B HB3  1 
ATOM   5677 N  N    . TYR   B 1 113 ? 34.542 -21.143 0.309   1.00 12.41 ?  113 TYR   B N    1 
ATOM   5678 C  CA   . TYR   B 1 113 ? 34.468 -21.101 -1.146  1.00 12.04 ?  113 TYR   B CA   1 
ATOM   5679 C  C    . TYR   B 1 113 ? 33.757 -19.852 -1.663  1.00 11.82 ?  113 TYR   B C    1 
ATOM   5680 O  O    . TYR   B 1 113 ? 34.026 -19.422 -2.789  1.00 11.71 ?  113 TYR   B O    1 
ATOM   5681 C  CB   . TYR   B 1 113 ? 33.793 -22.360 -1.686  1.00 12.00 ?  113 TYR   B CB   1 
ATOM   5682 C  CG   . TYR   B 1 113 ? 34.758 -23.507 -1.946  1.00 12.70 ?  113 TYR   B CG   1 
ATOM   5683 C  CD1  . TYR   B 1 113 ? 35.760 -23.395 -2.902  1.00 13.30 ?  113 TYR   B CD1  1 
ATOM   5684 C  CD2  . TYR   B 1 113 ? 34.650 -24.703 -1.254  1.00 12.94 ?  113 TYR   B CD2  1 
ATOM   5685 C  CE1  . TYR   B 1 113 ? 36.642 -24.431 -3.148  1.00 12.95 ?  113 TYR   B CE1  1 
ATOM   5686 C  CE2  . TYR   B 1 113 ? 35.524 -25.753 -1.497  1.00 13.14 ?  113 TYR   B CE2  1 
ATOM   5687 C  CZ   . TYR   B 1 113 ? 36.510 -25.612 -2.447  1.00 13.04 ?  113 TYR   B CZ   1 
ATOM   5688 O  OH   . TYR   B 1 113 ? 37.395 -26.637 -2.711  1.00 13.92 ?  113 TYR   B OH   1 
ATOM   5689 H  H    . TYR   B 1 113 ? 34.077 -21.772 0.683   1.00 15.01 ?  113 TYR   B H    1 
ATOM   5690 H  HA   . TYR   B 1 113 ? 35.370 -21.084 -1.485  1.00 14.57 ?  113 TYR   B HA   1 
ATOM   5691 H  HB2  . TYR   B 1 113 ? 33.136 -22.671 -1.039  1.00 14.52 ?  113 TYR   B HB2  1 
ATOM   5692 H  HB3  . TYR   B 1 113 ? 33.351 -22.144 -2.521  1.00 14.52 ?  113 TYR   B HB3  1 
ATOM   5693 H  HD1  . TYR   B 1 113 ? 35.852 -22.596 -3.376  1.00 16.08 ?  113 TYR   B HD1  1 
ATOM   5694 H  HD2  . TYR   B 1 113 ? 33.978 -24.804 -0.622  1.00 15.65 ?  113 TYR   B HD2  1 
ATOM   5695 H  HE1  . TYR   B 1 113 ? 37.310 -24.336 -3.794  1.00 15.66 ?  113 TYR   B HE1  1 
ATOM   5696 H  HE2  . TYR   B 1 113 ? 35.431 -26.554 -1.032  1.00 15.88 ?  113 TYR   B HE2  1 
ATOM   5697 H  HH   . TYR   B 1 113 ? 37.208 -27.304 -2.239  1.00 16.82 ?  113 TYR   B HH   1 
ATOM   5698 N  N    . GLU   B 1 114 ? 32.833 -19.272 -0.884  1.00 11.88 ?  114 GLU   B N    1 
ATOM   5699 C  CA   . GLU   B 1 114 ? 32.150 -18.062 -1.338  1.00 11.80 ?  114 GLU   B CA   1 
ATOM   5700 C  C    . GLU   B 1 114 ? 33.135 -16.941 -1.637  1.00 11.74 ?  114 GLU   B C    1 
ATOM   5701 O  O    . GLU   B 1 114 ? 32.856 -16.082 -2.476  1.00 11.97 ?  114 GLU   B O    1 
ATOM   5702 C  CB   . GLU   B 1 114 ? 31.094 -17.628 -0.316  1.00 12.73 ?  114 GLU   B CB   1 
ATOM   5703 C  CG   . GLU   B 1 114 ? 29.872 -18.544 -0.389  1.00 12.67 ?  114 GLU   B CG   1 
ATOM   5704 C  CD   . GLU   B 1 114 ? 28.849 -18.361 0.719   1.00 12.83 ?  114 GLU   B CD   1 
ATOM   5705 O  OE1  . GLU   B 1 114 ? 29.136 -17.738 1.761   1.00 13.54 ?  114 GLU   B OE1  1 
ATOM   5706 O  OE2  . GLU   B 1 114 ? 27.726 -18.901 0.553   1.00 13.36 -1 114 GLU   B OE2  1 
ATOM   5707 H  H    . GLU   B 1 114 ? 32.582 -19.563 -0.110  1.00 14.37 ?  114 GLU   B H    1 
ATOM   5708 H  HA   . GLU   B 1 114 ? 31.689 -18.261 -2.161  1.00 14.27 ?  114 GLU   B HA   1 
ATOM   5709 H  HB2  . GLU   B 1 114 ? 31.464 -17.682 0.581   1.00 15.39 ?  114 GLU   B HB2  1 
ATOM   5710 H  HB3  . GLU   B 1 114 ? 30.808 -16.723 -0.509  1.00 15.39 ?  114 GLU   B HB3  1 
ATOM   5711 H  HG2  . GLU   B 1 114 ? 29.424 -18.384 -1.229  1.00 15.33 ?  114 GLU   B HG2  1 
ATOM   5712 H  HG3  . GLU   B 1 114 ? 30.181 -19.462 -0.349  1.00 15.33 ?  114 GLU   B HG3  1 
ATOM   5713 N  N    . ASN   B 1 115 ? 34.300 -16.933 -0.984  1.00 11.69 ?  115 ASN   B N    1 
ATOM   5714 C  CA   . ASN   B 1 115 ? 35.293 -15.903 -1.285  1.00 11.28 ?  115 ASN   B CA   1 
ATOM   5715 C  C    . ASN   B 1 115 ? 35.698 -15.924 -2.751  1.00 11.24 ?  115 ASN   B C    1 
ATOM   5716 O  O    . ASN   B 1 115 ? 36.090 -14.884 -3.302  1.00 11.82 ?  115 ASN   B O    1 
ATOM   5717 C  CB   . ASN   B 1 115 ? 36.528 -16.074 -0.399  1.00 12.12 ?  115 ASN   B CB   1 
ATOM   5718 C  CG   . ASN   B 1 115 ? 36.255 -15.804 1.063   1.00 12.53 ?  115 ASN   B CG   1 
ATOM   5719 O  OD1  . ASN   B 1 115 ? 36.255 -14.658 1.507   1.00 14.35 ?  115 ASN   B OD1  1 
ATOM   5720 N  ND2  . ASN   B 1 115 ? 36.091 -16.872 1.838   1.00 12.76 ?  115 ASN   B ND2  1 
ATOM   5721 H  H    . ASN   B 1 115 ? 34.535 -17.491 -0.368  1.00 14.15 ?  115 ASN   B H    1 
ATOM   5722 H  HA   . ASN   B 1 115 ? 34.916 -15.031 -1.095  1.00 13.65 ?  115 ASN   B HA   1 
ATOM   5723 H  HB2  . ASN   B 1 115 ? 36.857 -16.984 -0.485  1.00 14.66 ?  115 ASN   B HB2  1 
ATOM   5724 H  HB3  . ASN   B 1 115 ? 37.215 -15.451 -0.690  1.00 14.66 ?  115 ASN   B HB3  1 
ATOM   5725 H  HD21 . ASN   B 1 115 ? 35.944 -16.776 2.680   1.00 15.43 ?  115 ASN   B HD21 1 
ATOM   5726 H  HD22 . ASN   B 1 115 ? 36.116 -17.663 1.496   1.00 15.43 ?  115 ASN   B HD22 1 
ATOM   5727 N  N    . PHE   B 1 116 ? 35.677 -17.103 -3.385  1.00 11.11 ?  116 PHE   B N    1 
ATOM   5728 C  CA   . PHE   B 1 116 ? 36.111 -17.194 -4.776  1.00 11.66 ?  116 PHE   B CA   1 
ATOM   5729 C  C    . PHE   B 1 116 ? 35.207 -16.372 -5.692  1.00 11.25 ?  116 PHE   B C    1 
ATOM   5730 O  O    . PHE   B 1 116 ? 35.641 -15.943 -6.767  1.00 11.73 ?  116 PHE   B O    1 
ATOM   5731 C  CB   . PHE   B 1 116 ? 36.079 -18.641 -5.301  1.00 11.15 ?  116 PHE   B CB   1 
ATOM   5732 C  CG   . PHE   B 1 116 ? 37.147 -19.600 -4.744  1.00 11.06 ?  116 PHE   B CG   1 
ATOM   5733 C  CD1  . PHE   B 1 116 ? 37.796 -19.416 -3.534  1.00 11.95 ?  116 PHE   B CD1  1 
ATOM   5734 C  CD2  . PHE   B 1 116 ? 37.447 -20.741 -5.472  1.00 11.52 ?  116 PHE   B CD2  1 
ATOM   5735 C  CE1  . PHE   B 1 116 ? 38.728 -20.354 -3.076  1.00 11.95 ?  116 PHE   B CE1  1 
ATOM   5736 C  CE2  . PHE   B 1 116 ? 38.375 -21.675 -5.022  1.00 11.54 ?  116 PHE   B CE2  1 
ATOM   5737 C  CZ   . PHE   B 1 116 ? 39.005 -21.488 -3.826  1.00 11.42 ?  116 PHE   B CZ   1 
ATOM   5738 H  H    . PHE   B 1 116 ? 35.423 -17.853 -3.038  1.00 13.44 ?  116 PHE   B H    1 
ATOM   5739 H  HA   . PHE   B 1 116 ? 37.019 -16.866 -4.856  1.00 14.10 ?  116 PHE   B HA   1 
ATOM   5740 H  HB2  . PHE   B 1 116 ? 35.208 -19.023 -5.087  1.00 13.50 ?  116 PHE   B HB2  1 
ATOM   5741 H  HB3  . PHE   B 1 116 ? 36.185 -18.619 -6.264  1.00 13.50 ?  116 PHE   B HB3  1 
ATOM   5742 H  HD1  . PHE   B 1 116 ? 37.600 -18.661 -3.020  1.00 14.45 ?  116 PHE   B HD1  1 
ATOM   5743 H  HD2  . PHE   B 1 116 ? 37.010 -20.896 -6.280  1.00 13.94 ?  116 PHE   B HD2  1 
ATOM   5744 H  HE1  . PHE   B 1 116 ? 39.161 -20.215 -2.265  1.00 14.46 ?  116 PHE   B HE1  1 
ATOM   5745 H  HE2  . PHE   B 1 116 ? 38.555 -22.429 -5.529  1.00 13.96 ?  116 PHE   B HE2  1 
ATOM   5746 H  HZ   . PHE   B 1 116 ? 39.633 -22.101 -3.529  1.00 13.82 ?  116 PHE   B HZ   1 
ATOM   5747 N  N    . ASN   B 1 117 ? 33.938 -16.173 -5.311  1.00 11.80 ?  117 ASN   B N    1 
ATOM   5748 C  CA   . ASN   B 1 117 ? 32.990 -15.469 -6.176  1.00 11.97 ?  117 ASN   B CA   1 
ATOM   5749 C  C    . ASN   B 1 117 ? 33.308 -13.990 -6.333  1.00 12.16 ?  117 ASN   B C    1 
ATOM   5750 O  O    . ASN   B 1 117 ? 32.706 -13.341 -7.193  1.00 13.38 ?  117 ASN   B O    1 
ATOM   5751 C  CB   . ASN   B 1 117 ? 31.568 -15.693 -5.675  1.00 12.14 ?  117 ASN   B CB   1 
ATOM   5752 C  CG   . ASN   B 1 117 ? 31.112 -17.104 -5.930  1.00 12.48 ?  117 ASN   B CG   1 
ATOM   5753 O  OD1  . ASN   B 1 117 ? 31.462 -17.691 -6.953  1.00 13.19 ?  117 ASN   B OD1  1 
ATOM   5754 N  ND2  . ASN   B 1 117 ? 30.375 -17.678 -4.990  1.00 12.36 ?  117 ASN   B ND2  1 
ATOM   5755 H  H    . ASN   B 1 117 ? 33.608 -16.442 -4.561  1.00 14.27 ?  117 ASN   B H    1 
ATOM   5756 H  HA   . ASN   B 1 117 ? 33.048 -15.871 -7.055  1.00 14.48 ?  117 ASN   B HA   1 
ATOM   5757 H  HB2  . ASN   B 1 117 ? 31.534 -15.530 -4.716  1.00 14.69 ?  117 ASN   B HB2  1 
ATOM   5758 H  HB3  . ASN   B 1 117 ? 30.969 -15.082 -6.135  1.00 14.69 ?  117 ASN   B HB3  1 
ATOM   5759 H  HD21 . ASN   B 1 117 ? 30.088 -18.483 -5.102  1.00 14.95 ?  117 ASN   B HD21 1 
ATOM   5760 H  HD22 . ASN   B 1 117 ? 30.152 -17.238 -4.286  1.00 14.95 ?  117 ASN   B HD22 1 
ATOM   5761 N  N    . GLN   B 1 118 ? 34.245 -13.459 -5.555  1.00 11.85 ?  118 GLN   B N    1 
ATOM   5762 C  CA   . GLN   B 1 118 ? 34.673 -12.073 -5.698  1.00 12.45 ?  118 GLN   B CA   1 
ATOM   5763 C  C    . GLN   B 1 118 ? 35.744 -11.887 -6.766  1.00 12.67 ?  118 GLN   B C    1 
ATOM   5764 O  O    . GLN   B 1 118 ? 36.218 -10.763 -6.949  1.00 14.10 ?  118 GLN   B O    1 
ATOM   5765 C  CB   . GLN   B 1 118 ? 35.151 -11.533 -4.346  1.00 13.23 ?  118 GLN   B CB   1 
ATOM   5766 C  CG   . GLN   B 1 118 ? 34.075 -11.572 -3.274  1.00 13.00 ?  118 GLN   B CG   1 
ATOM   5767 C  CD   . GLN   B 1 118 ? 32.901 -10.668 -3.603  1.00 12.96 ?  118 GLN   B CD   1 
ATOM   5768 O  OE1  . GLN   B 1 118 ? 33.088 -9.527  -4.039  1.00 13.96 ?  118 GLN   B OE1  1 
ATOM   5769 N  NE2  . GLN   B 1 118 ? 31.686 -11.166 -3.401  1.00 13.63 ?  118 GLN   B NE2  1 
ATOM   5770 H  H    . GLN   B 1 118 ? 34.659 -13.881 -4.930  1.00 14.34 ?  118 GLN   B H    1 
ATOM   5771 H  HA   . GLN   B 1 118 ? 33.909 -11.542 -5.973  1.00 15.06 ?  118 GLN   B HA   1 
ATOM   5772 H  HB2  . GLN   B 1 118 ? 35.899 -12.060 -4.040  1.00 15.99 ?  118 GLN   B HB2  1 
ATOM   5773 H  HB3  . GLN   B 1 118 ? 35.423 -10.603 -4.457  1.00 15.99 ?  118 GLN   B HB3  1 
ATOM   5774 H  HG2  . GLN   B 1 118 ? 33.742 -12.479 -3.190  1.00 15.71 ?  118 GLN   B HG2  1 
ATOM   5775 H  HG3  . GLN   B 1 118 ? 34.453 -11.276 -2.431  1.00 15.71 ?  118 GLN   B HG3  1 
ATOM   5776 H  HE21 . GLN   B 1 118 ? 31.600 -11.966 -3.093  1.00 16.47 ?  118 GLN   B HE21 1 
ATOM   5777 H  HE22 . GLN   B 1 118 ? 30.996 -10.693 -3.573  1.00 16.47 ?  118 GLN   B HE22 1 
ATOM   5778 N  N    . HIS   B 1 119 ? 36.102 -12.947 -7.490  1.00 11.72 ?  119 HIS   B N    1 
ATOM   5779 C  CA   . HIS   B 1 119 ? 37.138 -12.897 -8.511  1.00 12.07 ?  119 HIS   B CA   1 
ATOM   5780 C  C    . HIS   B 1 119 ? 36.660 -13.633 -9.749  1.00 11.92 ?  119 HIS   B C    1 
ATOM   5781 O  O    . HIS   B 1 119 ? 36.149 -14.749 -9.646  1.00 13.19 ?  119 HIS   B O    1 
ATOM   5782 C  CB   . HIS   B 1 119 ? 38.423 -13.525 -7.967  1.00 12.80 ?  119 HIS   B CB   1 
ATOM   5783 C  CG   . HIS   B 1 119 ? 38.902 -12.836 -6.736  1.00 14.17 ?  119 HIS   B CG   1 
ATOM   5784 N  ND1  . HIS   B 1 119 ? 39.701 -11.714 -6.781  1.00 15.45 ?  119 HIS   B ND1  1 
ATOM   5785 C  CD2  . HIS   B 1 119 ? 38.607 -13.039 -5.431  1.00 15.11 ?  119 HIS   B CD2  1 
ATOM   5786 C  CE1  . HIS   B 1 119 ? 39.917 -11.287 -5.551  1.00 16.57 ?  119 HIS   B CE1  1 
ATOM   5787 N  NE2  . HIS   B 1 119 ? 39.253 -12.063 -4.714  1.00 16.55 ?  119 HIS   B NE2  1 
ATOM   5788 H  H    . HIS   B 1 119 ? 35.741 -13.730 -7.416  1.00 14.18 ?  119 HIS   B H    1 
ATOM   5789 H  HA   . HIS   B 1 119 ? 37.317 -11.972 -8.749  1.00 14.60 ?  119 HIS   B HA   1 
ATOM   5790 H  HB2  . HIS   B 1 119 ? 38.260 -14.453 -7.755  1.00 15.47 ?  119 HIS   B HB2  1 
ATOM   5791 H  HB3  . HIS   B 1 119 ? 39.120 -13.454 -8.644  1.00 15.47 ?  119 HIS   B HB3  1 
ATOM   5792 H  HD2  . HIS   B 1 119 ? 38.073 -13.720 -5.086  1.00 18.24 ?  119 HIS   B HD2  1 
ATOM   5793 H  HE1  . HIS   B 1 119 ? 40.452 -10.564 -5.305  1.00 20.00 ?  119 HIS   B HE1  1 
ATOM   5794 H  HE2  . HIS   B 1 119 ? 39.259 -11.998 -3.853  1.00 19.98 ?  119 HIS   B HE2  1 
ATOM   5795 N  N    . GLU   B 1 120 ? 36.820 -13.017 -10.919 1.00 12.80 ?  120 GLU   B N    1 
ATOM   5796 C  CA   . GLU   B 1 120 ? 36.234 -13.599 -12.122 1.00 14.65 ?  120 GLU   B CA   1 
ATOM   5797 C  C    . GLU   B 1 120 ? 36.909 -14.902 -12.534 1.00 13.48 ?  120 GLU   B C    1 
ATOM   5798 O  O    . GLU   B 1 120 ? 36.247 -15.778 -13.104 1.00 13.63 ?  120 GLU   B O    1 
ATOM   5799 C  CB   . GLU   B 1 120 ? 36.244 -12.587 -13.265 1.00 19.56 ?  120 GLU   B CB   1 
ATOM   5800 C  CG   . GLU   B 1 120 ? 35.266 -11.443 -13.058 1.00 25.56 ?  120 GLU   B CG   1 
ATOM   5801 C  CD   . GLU   B 1 120 ? 35.161 -10.531 -14.264 1.00 31.23 ?  120 GLU   B CD   1 
ATOM   5802 O  OE1  . GLU   B 1 120 ? 36.161 -10.399 -15.003 1.00 33.34 ?  120 GLU   B OE1  1 
ATOM   5803 O  OE2  . GLU   B 1 120 ? 34.076 -9.950  -14.475 1.00 34.56 -1 120 GLU   B OE2  1 
ATOM   5804 H  H    . GLU   B 1 120 ? 37.249 -12.277 -11.041 1.00 15.47 ?  120 GLU   B H    1 
ATOM   5805 H  HA   . GLU   B 1 120 ? 35.309 -13.806 -11.931 1.00 17.69 ?  120 GLU   B HA   1 
ATOM   5806 H  HB2  . GLU   B 1 120 ? 37.128 -12.205 -13.348 1.00 23.59 ?  120 GLU   B HB2  1 
ATOM   5807 H  HB3  . GLU   B 1 120 ? 35.996 -13.038 -14.088 1.00 23.59 ?  120 GLU   B HB3  1 
ATOM   5808 H  HG2  . GLU   B 1 120 ? 34.379 -11.805 -12.888 1.00 30.79 ?  120 GLU   B HG2  1 
ATOM   5809 H  HG3  . GLU   B 1 120 ? 35.553 -10.909 -12.301 1.00 30.79 ?  120 GLU   B HG3  1 
ATOM   5810 N  N    . VAL   B 1 121 ? 38.209 -15.046 -12.270 1.00 12.84 ?  121 VAL   B N    1 
ATOM   5811 C  CA   . VAL   B 1 121 ? 38.950 -16.259 -12.610 1.00 12.73 ?  121 VAL   B CA   1 
ATOM   5812 C  C    . VAL   B 1 121 ? 40.061 -16.459 -11.589 1.00 11.99 ?  121 VAL   B C    1 
ATOM   5813 O  O    . VAL   B 1 121 ? 40.735 -15.500 -11.197 1.00 12.55 ?  121 VAL   B O    1 
ATOM   5814 C  CB   . VAL   B 1 121 ? 39.467 -16.214 -14.066 1.00 14.35 ?  121 VAL   B CB   1 
ATOM   5815 C  CG1  . VAL   B 1 121 ? 40.332 -14.984 -14.311 1.00 15.94 ?  121 VAL   B CG1  1 
ATOM   5816 C  CG2  . VAL   B 1 121 ? 40.212 -17.497 -14.418 1.00 16.14 ?  121 VAL   B CG2  1 
ATOM   5817 H  H    . VAL   B 1 121 ? 38.696 -14.440 -11.899 1.00 15.52 ?  121 VAL   B H    1 
ATOM   5818 H  HA   . VAL   B 1 121 ? 38.339 -17.010 -12.541 1.00 15.39 ?  121 VAL   B HA   1 
ATOM   5819 H  HB   . VAL   B 1 121 ? 38.698 -16.155 -14.664 1.00 17.34 ?  121 VAL   B HB   1 
ATOM   5820 H  HG11 . VAL   B 1 121 ? 40.646 -14.996 -15.228 1.00 19.24 ?  121 VAL   B HG11 1 
ATOM   5821 H  HG12 . VAL   B 1 121 ? 39.799 -14.186 -14.156 1.00 19.24 ?  121 VAL   B HG12 1 
ATOM   5822 H  HG13 . VAL   B 1 121 ? 41.084 -15.003 -13.701 1.00 19.24 ?  121 VAL   B HG13 1 
ATOM   5823 H  HG21 . VAL   B 1 121 ? 40.412 -17.496 -15.368 1.00 19.48 ?  121 VAL   B HG21 1 
ATOM   5824 H  HG22 . VAL   B 1 121 ? 41.036 -17.533 -13.908 1.00 19.48 ?  121 VAL   B HG22 1 
ATOM   5825 H  HG23 . VAL   B 1 121 ? 39.653 -18.260 -14.201 1.00 19.48 ?  121 VAL   B HG23 1 
ATOM   5826 N  N    . LEU   B 1 122 ? 40.245 -17.711 -11.153 1.00 11.58 ?  122 LEU   B N    1 
ATOM   5827 C  CA   . LEU   B 1 122 ? 41.233 -18.062 -10.137 1.00 11.45 ?  122 LEU   B CA   1 
ATOM   5828 C  C    . LEU   B 1 122 ? 41.885 -19.393 -10.464 1.00 11.33 ?  122 LEU   B C    1 
ATOM   5829 O  O    . LEU   B 1 122 ? 41.221 -20.312 -10.964 1.00 12.40 ?  122 LEU   B O    1 
ATOM   5830 C  CB   . LEU   B 1 122 ? 40.584 -18.288 -8.754  1.00 12.91 ?  122 LEU   B CB   1 
ATOM   5831 C  CG   . LEU   B 1 122 ? 39.542 -17.270 -8.268  1.00 12.99 ?  122 LEU   B CG   1 
ATOM   5832 C  CD1  . LEU   B 1 122 ? 38.145 -17.634 -8.745  1.00 14.17 ?  122 LEU   B CD1  1 
ATOM   5833 C  CD2  . LEU   B 1 122 ? 39.567 -17.148 -6.761  1.00 12.61 ?  122 LEU   B CD2  1 
ATOM   5834 H  H    . LEU   B 1 122 ? 39.797 -18.389 -11.440 1.00 14.01 ?  122 LEU   B H    1 
ATOM   5835 H  HA   . LEU   B 1 122 ? 41.911 -17.370 -10.067 1.00 13.86 ?  122 LEU   B HA   1 
ATOM   5836 H  HB2  . LEU   B 1 122 ? 40.147 -19.149 -8.767  1.00 15.60 ?  122 LEU   B HB2  1 
ATOM   5837 H  HB3  . LEU   B 1 122 ? 41.290 -18.294 -8.092  1.00 15.60 ?  122 LEU   B HB3  1 
ATOM   5838 H  HG   . LEU   B 1 122 ? 39.755 -16.400 -8.636  1.00 15.70 ?  122 LEU   B HG   1 
ATOM   5839 H  HD11 . LEU   B 1 122 ? 37.508 -16.999 -8.378  1.00 17.12 ?  122 LEU   B HD11 1 
ATOM   5840 H  HD12 . LEU   B 1 122 ? 38.121 -17.596 -9.716  1.00 17.12 ?  122 LEU   B HD12 1 
ATOM   5841 H  HD13 . LEU   B 1 122 ? 37.929 -18.529 -8.444  1.00 17.12 ?  122 LEU   B HD13 1 
ATOM   5842 H  HD21 . LEU   B 1 122 ? 38.883 -16.519 -6.479  1.00 15.25 ?  122 LEU   B HD21 1 
ATOM   5843 H  HD22 . LEU   B 1 122 ? 39.398 -18.018 -6.367  1.00 15.25 ?  122 LEU   B HD22 1 
ATOM   5844 H  HD23 . LEU   B 1 122 ? 40.442 -16.827 -6.485  1.00 15.25 ?  122 LEU   B HD23 1 
ATOM   5845 N  N    . LEU   B 1 123 ? 43.170 -19.506 -10.106 1.00 10.86 ?  123 LEU   B N    1 
ATOM   5846 C  CA   . LEU   B 1 123 ? 43.876 -20.776 -9.981  1.00 11.19 ?  123 LEU   B CA   1 
ATOM   5847 C  C    . LEU   B 1 123 ? 43.845 -21.165 -8.507  1.00 10.86 ?  123 LEU   B C    1 
ATOM   5848 O  O    . LEU   B 1 123 ? 44.196 -20.338 -7.655  1.00 11.05 ?  123 LEU   B O    1 
ATOM   5849 C  CB   . LEU   B 1 123 ? 45.324 -20.601 -10.443 1.00 11.73 ?  123 LEU   B CB   1 
ATOM   5850 C  CG   . LEU   B 1 123 ? 46.274 -21.780 -10.195 1.00 11.94 ?  123 LEU   B CG   1 
ATOM   5851 C  CD1  . LEU   B 1 123 ? 45.853 -23.037 -10.965 1.00 12.90 ?  123 LEU   B CD1  1 
ATOM   5852 C  CD2  . LEU   B 1 123 ? 47.679 -21.375 -10.570 1.00 12.78 ?  123 LEU   B CD2  1 
ATOM   5853 H  H    . LEU   B 1 123 ? 43.667 -18.829 -9.920  1.00 13.15 ?  123 LEU   B H    1 
ATOM   5854 H  HA   . LEU   B 1 123 ? 43.438 -21.467 -10.503 1.00 13.55 ?  123 LEU   B HA   1 
ATOM   5855 H  HB2  . LEU   B 1 123 ? 45.312 -20.441 -11.397 1.00 14.19 ?  123 LEU   B HB2  1 
ATOM   5856 H  HB3  . LEU   B 1 123 ? 45.694 -19.835 -9.987  1.00 14.19 ?  123 LEU   B HB3  1 
ATOM   5857 H  HG   . LEU   B 1 123 ? 46.275 -21.998 -9.249  1.00 14.44 ?  123 LEU   B HG   1 
ATOM   5858 H  HD11 . LEU   B 1 123 ? 46.492 -23.742 -10.783 1.00 15.60 ?  123 LEU   B HD11 1 
ATOM   5859 H  HD12 . LEU   B 1 123 ? 44.969 -23.301 -10.668 1.00 15.60 ?  123 LEU   B HD12 1 
ATOM   5860 H  HD13 . LEU   B 1 123 ? 45.841 -22.831 -11.911 1.00 15.60 ?  123 LEU   B HD13 1 
ATOM   5861 H  HD21 . LEU   B 1 123 ? 48.276 -22.121 -10.416 1.00 15.45 ?  123 LEU   B HD21 1 
ATOM   5862 H  HD22 . LEU   B 1 123 ? 47.693 -21.126 -11.509 1.00 15.45 ?  123 LEU   B HD22 1 
ATOM   5863 H  HD23 . LEU   B 1 123 ? 47.944 -20.617 -10.025 1.00 15.45 ?  123 LEU   B HD23 1 
ATOM   5864 N  N    . ALA   B 1 124 ? 43.415 -22.396 -8.197  1.00 10.66 ?  124 ALA   B N    1 
ATOM   5865 C  CA   . ALA   B 1 124 ? 43.160 -22.712 -6.799  1.00 10.90 ?  124 ALA   B CA   1 
ATOM   5866 C  C    . ALA   B 1 124 ? 43.430 -24.170 -6.462  1.00 10.43 ?  124 ALA   B C    1 
ATOM   5867 O  O    . ALA   B 1 124 ? 43.294 -25.049 -7.325  1.00 11.34 ?  124 ALA   B O    1 
ATOM   5868 C  CB   . ALA   B 1 124 ? 41.707 -22.388 -6.426  1.00 11.53 ?  124 ALA   B CB   1 
ATOM   5869 H  H    . ALA   B 1 124 ? 43.260 -23.038 -8.753  1.00 12.90 ?  124 ALA   B H    1 
ATOM   5870 H  HA   . ALA   B 1 124 ? 43.734 -22.155 -6.250  1.00 13.19 ?  124 ALA   B HA   1 
ATOM   5871 H  HB1  . ALA   B 1 124 ? 41.557 -22.600 -5.492  1.00 13.95 ?  124 ALA   B HB1  1 
ATOM   5872 H  HB2  . ALA   B 1 124 ? 41.544 -21.440 -6.578  1.00 13.95 ?  124 ALA   B HB2  1 
ATOM   5873 H  HB3  . ALA   B 1 124 ? 41.111 -22.914 -6.985  1.00 13.95 ?  124 ALA   B HB3  1 
ATOM   5874 N  N    . PRO   B 1 125 ? 43.729 -24.458 -5.199  1.00 10.82 ?  125 PRO   B N    1 
ATOM   5875 C  CA   . PRO   B 1 125 ? 43.661 -25.820 -4.671  1.00 11.51 ?  125 PRO   B CA   1 
ATOM   5876 C  C    . PRO   B 1 125 ? 42.260 -26.096 -4.126  1.00 11.63 ?  125 PRO   B C    1 
ATOM   5877 O  O    . PRO   B 1 125 ? 41.464 -25.179 -3.921  1.00 12.22 ?  125 PRO   B O    1 
ATOM   5878 C  CB   . PRO   B 1 125 ? 44.646 -25.748 -3.500  1.00 12.70 ?  125 PRO   B CB   1 
ATOM   5879 C  CG   . PRO   B 1 125 ? 44.398 -24.366 -2.935  1.00 12.58 ?  125 PRO   B CG   1 
ATOM   5880 C  CD   . PRO   B 1 125 ? 44.056 -23.490 -4.136  1.00 11.62 ?  125 PRO   B CD   1 
ATOM   5881 H  HA   . PRO   B 1 125 ? 43.933 -26.491 -5.317  1.00 13.93 ?  125 PRO   B HA   1 
ATOM   5882 H  HB2  . PRO   B 1 125 ? 44.437 -26.433 -2.840  1.00 15.35 ?  125 PRO   B HB2  1 
ATOM   5883 H  HB3  . PRO   B 1 125 ? 45.556 -25.836 -3.816  1.00 15.35 ?  125 PRO   B HB3  1 
ATOM   5884 H  HG2  . PRO   B 1 125 ? 43.650 -24.391 -2.312  1.00 15.21 ?  125 PRO   B HG2  1 
ATOM   5885 H  HG3  . PRO   B 1 125 ? 45.197 -24.042 -2.487  1.00 15.21 ?  125 PRO   B HG3  1 
ATOM   5886 H  HD2  . PRO   B 1 125 ? 43.294 -22.926 -3.942  1.00 14.06 ?  125 PRO   B HD2  1 
ATOM   5887 H  HD3  . PRO   B 1 125 ? 44.833 -22.956 -4.390  1.00 14.06 ?  125 PRO   B HD3  1 
ATOM   5888 N  N    . LEU   B 1 126 ? 41.990 -27.375 -3.847  1.00 12.31 ?  126 LEU   B N    1 
ATOM   5889 C  CA   . LEU   B 1 126 ? 40.771 -27.739 -3.128  1.00 13.03 ?  126 LEU   B CA   1 
ATOM   5890 C  C    . LEU   B 1 126 ? 40.893 -27.337 -1.666  1.00 12.91 ?  126 LEU   B C    1 
ATOM   5891 O  O    . LEU   B 1 126 ? 41.787 -27.801 -0.953  1.00 14.86 ?  126 LEU   B O    1 
ATOM   5892 C  CB   . LEU   B 1 126 ? 40.509 -29.237 -3.235  1.00 14.17 ?  126 LEU   B CB   1 
ATOM   5893 C  CG   . LEU   B 1 126 ? 39.993 -29.731 -4.588  1.00 15.18 ?  126 LEU   B CG   1 
ATOM   5894 C  CD1  . LEU   B 1 126 ? 40.028 -31.240 -4.660  1.00 17.15 ?  126 LEU   B CD1  1 
ATOM   5895 C  CD2  . LEU   B 1 126 ? 38.581 -29.238 -4.849  1.00 15.58 ?  126 LEU   B CD2  1 
ATOM   5896 H  H    . LEU   B 1 126 ? 42.495 -28.042 -4.050  1.00 14.89 ?  126 LEU   B H    1 
ATOM   5897 H  HA   . LEU   B 1 126 ? 40.020 -27.264 -3.512  1.00 15.75 ?  126 LEU   B HA   1 
ATOM   5898 H  HB2  . LEU   B 1 126 ? 41.338 -29.704 -3.051  1.00 17.13 ?  126 LEU   B HB2  1 
ATOM   5899 H  HB3  . LEU   B 1 126 ? 39.847 -29.478 -2.569  1.00 17.13 ?  126 LEU   B HB3  1 
ATOM   5900 H  HG   . LEU   B 1 126 ? 40.571 -29.384 -5.288  1.00 18.33 ?  126 LEU   B HG   1 
ATOM   5901 H  HD11 . LEU   B 1 126 ? 39.699 -31.520 -5.528  1.00 20.70 ?  126 LEU   B HD11 1 
ATOM   5902 H  HD12 . LEU   B 1 126 ? 40.937 -31.545 -4.534  1.00 20.70 ?  126 LEU   B HD12 1 
ATOM   5903 H  HD13 . LEU   B 1 126 ? 39.457 -31.600 -3.960  1.00 20.70 ?  126 LEU   B HD13 1 
ATOM   5904 H  HD21 . LEU   B 1 126 ? 38.251 -29.647 -5.662  1.00 18.81 ?  126 LEU   B HD21 1 
ATOM   5905 H  HD22 . LEU   B 1 126 ? 38.019 -29.479 -4.100  1.00 18.81 ?  126 LEU   B HD22 1 
ATOM   5906 H  HD23 . LEU   B 1 126 ? 38.599 -28.270 -4.952  1.00 18.81 ?  126 LEU   B HD23 1 
ATOM   5907 N  N    . LEU   B 1 127 ? 39.964 -26.505 -1.206  1.00 13.08 ?  127 LEU   B N    1 
ATOM   5908 C  CA   . LEU   B 1 127 ? 40.017 -26.012 0.159   1.00 13.57 ?  127 LEU   B CA   1 
ATOM   5909 C  C    . LEU   B 1 127 ? 39.746 -27.133 1.152   1.00 13.18 ?  127 LEU   B C    1 
ATOM   5910 O  O    . LEU   B 1 127 ? 38.922 -28.025 0.920   1.00 13.73 ?  127 LEU   B O    1 
ATOM   5911 C  CB   . LEU   B 1 127 ? 38.999 -24.889 0.366   1.00 14.23 ?  127 LEU   B CB   1 
ATOM   5912 C  CG   . LEU   B 1 127 ? 39.184 -23.626 -0.476  1.00 14.50 ?  127 LEU   B CG   1 
ATOM   5913 C  CD1  . LEU   B 1 127 ? 38.072 -22.653 -0.160  1.00 14.79 ?  127 LEU   B CD1  1 
ATOM   5914 C  CD2  . LEU   B 1 127 ? 40.550 -22.976 -0.244  1.00 14.90 ?  127 LEU   B CD2  1 
ATOM   5915 H  H    . LEU   B 1 127 ? 39.299 -26.200 -1.665  1.00 15.81 ?  127 LEU   B H    1 
ATOM   5916 H  HA   . LEU   B 1 127 ? 40.904 -25.652 0.336   1.00 16.39 ?  127 LEU   B HA   1 
ATOM   5917 H  HB2  . LEU   B 1 127 ? 38.119 -25.237 0.167   1.00 17.19 ?  127 LEU   B HB2  1 
ATOM   5918 H  HB3  . LEU   B 1 127 ? 39.034 -24.615 1.297   1.00 17.19 ?  127 LEU   B HB3  1 
ATOM   5919 H  HG   . LEU   B 1 127 ? 39.112 -23.854 -1.412  1.00 17.52 ?  127 LEU   B HG   1 
ATOM   5920 H  HD11 . LEU   B 1 127 ? 38.195 -21.845 -0.689  1.00 17.86 ?  127 LEU   B HD11 1 
ATOM   5921 H  HD12 . LEU   B 1 127 ? 37.219 -23.059 -0.376  1.00 17.86 ?  127 LEU   B HD12 1 
ATOM   5922 H  HD13 . LEU   B 1 127 ? 38.101 -22.429 0.785   1.00 17.86 ?  127 LEU   B HD13 1 
ATOM   5923 H  HD21 . LEU   B 1 127 ? 40.587 -22.131 -0.722  1.00 18.00 ?  127 LEU   B HD21 1 
ATOM   5924 H  HD22 . LEU   B 1 127 ? 40.672 -22.820 0.707   1.00 18.00 ?  127 LEU   B HD22 1 
ATOM   5925 H  HD23 . LEU   B 1 127 ? 41.241 -23.572 -0.572  1.00 18.00 ?  127 LEU   B HD23 1 
ATOM   5926 N  N    . SER   B 1 128 ? 40.429 -27.053 2.283   1.00 13.14 ?  128 SER   B N    1 
ATOM   5927 C  CA   . SER   B 1 128 ? 40.310 -27.966 3.407   1.00 13.89 ?  128 SER   B CA   1 
ATOM   5928 C  C    . SER   B 1 128 ? 40.797 -29.374 3.089   1.00 15.09 ?  128 SER   B C    1 
ATOM   5929 O  O    . SER   B 1 128 ? 40.693 -30.249 3.943   1.00 16.32 ?  128 SER   B O    1 
ATOM   5930 C  CB   . SER   B 1 128 ? 38.904 -27.968 4.024   1.00 14.19 ?  128 SER   B CB   1 
ATOM   5931 O  OG   . SER   B 1 128 ? 38.592 -26.690 4.563   1.00 14.66 ?  128 SER   B OG   1 
ATOM   5932 H  H    . SER   B 1 128 ? 41.003 -26.427 2.431   1.00 15.88 ?  128 SER   B H    1 
ATOM   5933 H  HA   . SER   B 1 128 ? 40.894 -27.633 4.094   1.00 16.78 ?  128 SER   B HA   1 
ATOM   5934 H  HB2  . SER   B 1 128 ? 38.252 -28.204 3.342   1.00 17.15 ?  128 SER   B HB2  1 
ATOM   5935 H  HB3  . SER   B 1 128 ? 38.877 -28.631 4.741   1.00 17.15 ?  128 SER   B HB3  1 
ATOM   5936 H  HG   . SER   B 1 128 ? 39.153 -26.485 5.147   1.00 17.71 ?  128 SER   B HG   1 
ATOM   5937 N  N    . ALA   B 1 129 ? 41.374 -29.601 1.907   1.00 16.16 ?  129 ALA   B N    1 
ATOM   5938 C  CA   . ALA   B 1 129 ? 41.921 -30.899 1.548   1.00 16.66 ?  129 ALA   B CA   1 
ATOM   5939 C  C    . ALA   B 1 129 ? 43.314 -31.076 2.144   1.00 15.94 ?  129 ALA   B C    1 
ATOM   5940 O  O    . ALA   B 1 129 ? 43.875 -30.176 2.783   1.00 15.93 ?  129 ALA   B O    1 
ATOM   5941 C  CB   . ALA   B 1 129 ? 41.974 -31.049 0.030   1.00 18.67 ?  129 ALA   B CB   1 
ATOM   5942 H  H    . ALA   B 1 129 ? 41.459 -29.007 1.288   1.00 19.50 ?  129 ALA   B H    1 
ATOM   5943 H  HA   . ALA   B 1 129 ? 41.348 -31.594 1.901   1.00 20.11 ?  129 ALA   B HA   1 
ATOM   5944 H  HB1  . ALA   B 1 129 ? 42.332 -31.925 -0.189  1.00 22.53 ?  129 ALA   B HB1  1 
ATOM   5945 H  HB2  . ALA   B 1 129 ? 41.079 -30.958 -0.329  1.00 22.53 ?  129 ALA   B HB2  1 
ATOM   5946 H  HB3  . ALA   B 1 129 ? 42.550 -30.358 -0.337  1.00 22.53 ?  129 ALA   B HB3  1 
ATOM   5947 N  N    . GLY   B 1 130 ? 43.882 -32.258 1.909   1.00 15.70 ?  130 GLY   B N    1 
ATOM   5948 C  CA   . GLY   B 1 130 ? 45.268 -32.497 2.265   1.00 16.51 ?  130 GLY   B CA   1 
ATOM   5949 C  C    . GLY   B 1 130 ? 45.484 -32.407 3.756   1.00 16.56 ?  130 GLY   B C    1 
ATOM   5950 O  O    . GLY   B 1 130 ? 44.783 -33.048 4.552   1.00 17.17 ?  130 GLY   B O    1 
ATOM   5951 H  H    . GLY   B 1 130 ? 43.490 -32.928 1.538   1.00 18.95 ?  130 GLY   B H    1 
ATOM   5952 H  HA2  . GLY   B 1 130 ? 45.533 -33.382 1.971   1.00 19.93 ?  130 GLY   B HA2  1 
ATOM   5953 H  HA3  . GLY   B 1 130 ? 45.836 -31.843 1.828   1.00 19.93 ?  130 GLY   B HA3  1 
ATOM   5954 N  N    . ILE   B 1 131 ? 46.458 -31.577 4.144   1.00 17.07 ?  131 ILE   B N    1 
ATOM   5955 C  CA   . ILE   B 1 131 ? 46.819 -31.442 5.546   1.00 17.98 ?  131 ILE   B CA   1 
ATOM   5956 C  C    . ILE   B 1 131 ? 45.703 -30.841 6.380   1.00 17.28 ?  131 ILE   B C    1 
ATOM   5957 O  O    . ILE   B 1 131 ? 45.776 -30.904 7.610   1.00 18.80 ?  131 ILE   B O    1 
ATOM   5958 C  CB   . ILE   B 1 131 ? 48.139 -30.659 5.733   1.00 20.02 ?  131 ILE   B CB   1 
ATOM   5959 C  CG1  . ILE   B 1 131 ? 47.967 -29.175 5.368   1.00 21.05 ?  131 ILE   B CG1  1 
ATOM   5960 C  CG2  . ILE   B 1 131 ? 49.249 -31.291 4.904   1.00 21.06 ?  131 ILE   B CG2  1 
ATOM   5961 C  CD1  . ILE   B 1 131 ? 49.184 -28.319 5.680   1.00 22.15 ?  131 ILE   B CD1  1 
ATOM   5962 H  H    . ILE   B 1 131 ? 46.916 -31.075 3.619   1.00 20.60 ?  131 ILE   B H    1 
ATOM   5963 H  HA   . ILE   B 1 131 ? 46.963 -32.327 5.900   1.00 21.69 ?  131 ILE   B HA   1 
ATOM   5964 H  HB   . ILE   B 1 131 ? 48.386 -30.708 6.670   1.00 24.14 ?  131 ILE   B HB   1 
ATOM   5965 H  HG12 . ILE   B 1 131 ? 47.787 -29.107 4.418   1.00 25.38 ?  131 ILE   B HG12 1 
ATOM   5966 H  HG13 . ILE   B 1 131 ? 47.217 -28.805 5.867   1.00 25.38 ?  131 ILE   B HG13 1 
ATOM   5967 H  HG21 . ILE   B 1 131 ? 50.091 -30.889 5.155   1.00 25.39 ?  131 ILE   B HG21 1 
ATOM   5968 H  HG22 . ILE   B 1 131 ? 49.261 -32.241 5.079   1.00 25.39 ?  131 ILE   B HG22 1 
ATOM   5969 H  HG23 . ILE   B 1 131 ? 49.066 -31.126 3.965   1.00 25.39 ?  131 ILE   B HG23 1 
ATOM   5970 H  HD11 . ILE   B 1 131 ? 48.964 -27.388 5.516   1.00 26.70 ?  131 ILE   B HD11 1 
ATOM   5971 H  HD12 . ILE   B 1 131 ? 49.424 -28.443 6.612   1.00 26.70 ?  131 ILE   B HD12 1 
ATOM   5972 H  HD13 . ILE   B 1 131 ? 49.916 -28.593 5.109   1.00 26.70 ?  131 ILE   B HD13 1 
ATOM   5973 N  N    . PHE   B 1 132 ? 44.672 -30.259 5.749   1.00 15.66 ?  132 PHE   B N    1 
ATOM   5974 C  CA   . PHE   B 1 132 ? 43.511 -29.751 6.474   1.00 16.31 ?  132 PHE   B CA   1 
ATOM   5975 C  C    . PHE   B 1 132 ? 42.486 -30.838 6.800   1.00 17.62 ?  132 PHE   B C    1 
ATOM   5976 O  O    . PHE   B 1 132 ? 41.577 -30.588 7.598   1.00 19.27 ?  132 PHE   B O    1 
ATOM   5977 C  CB   . PHE   B 1 132 ? 42.836 -28.621 5.685   1.00 15.32 ?  132 PHE   B CB   1 
ATOM   5978 C  CG   . PHE   B 1 132 ? 43.531 -27.283 5.795   1.00 15.22 ?  132 PHE   B CG   1 
ATOM   5979 C  CD1  . PHE   B 1 132 ? 44.823 -27.098 5.326   1.00 15.93 ?  132 PHE   B CD1  1 
ATOM   5980 C  CD2  . PHE   B 1 132 ? 42.857 -26.188 6.318   1.00 15.02 ?  132 PHE   B CD2  1 
ATOM   5981 C  CE1  . PHE   B 1 132 ? 45.441 -25.856 5.419   1.00 16.73 ?  132 PHE   B CE1  1 
ATOM   5982 C  CE2  . PHE   B 1 132 ? 43.466 -24.941 6.402   1.00 15.41 ?  132 PHE   B CE2  1 
ATOM   5983 C  CZ   . PHE   B 1 132 ? 44.756 -24.782 5.955   1.00 16.27 ?  132 PHE   B CZ   1 
ATOM   5984 H  H    . PHE   B 1 132 ? 44.619 -30.148 4.895   1.00 18.91 ?  132 PHE   B H    1 
ATOM   5985 H  HA   . PHE   B 1 132 ? 43.812 -29.374 7.313   1.00 19.69 ?  132 PHE   B HA   1 
ATOM   5986 H  HB2  . PHE   B 1 132 ? 42.823 -28.863 4.748   1.00 18.50 ?  132 PHE   B HB2  1 
ATOM   5987 H  HB3  . PHE   B 1 132 ? 41.927 -28.509 6.010   1.00 18.50 ?  132 PHE   B HB3  1 
ATOM   5988 H  HD1  . PHE   B 1 132 ? 45.287 -27.823 4.970   1.00 19.24 ?  132 PHE   B HD1  1 
ATOM   5989 H  HD2  . PHE   B 1 132 ? 41.983 -26.291 6.626   1.00 18.14 ?  132 PHE   B HD2  1 
ATOM   5990 H  HE1  . PHE   B 1 132 ? 46.313 -25.751 5.115   1.00 20.19 ?  132 PHE   B HE1  1 
ATOM   5991 H  HE2  . PHE   B 1 132 ? 43.006 -24.220 6.771   1.00 18.61 ?  132 PHE   B HE2  1 
ATOM   5992 H  HZ   . PHE   B 1 132 ? 45.169 -23.947 6.019   1.00 19.64 ?  132 PHE   B HZ   1 
ATOM   5993 N  N    . GLY   B 1 133 ? 42.592 -32.031 6.203   1.00 17.23 ?  133 GLY   B N    1 
ATOM   5994 C  CA   . GLY   B 1 133 ? 41.877 -33.197 6.697   1.00 18.27 ?  133 GLY   B CA   1 
ATOM   5995 C  C    . GLY   B 1 133 ? 40.478 -33.458 6.163   1.00 18.62 ?  133 GLY   B C    1 
ATOM   5996 O  O    . GLY   B 1 133 ? 39.890 -34.480 6.531   1.00 20.36 ?  133 GLY   B O    1 
ATOM   5997 H  H    . GLY   B 1 133 ? 43.086 -32.183 5.514   1.00 20.79 ?  133 GLY   B H    1 
ATOM   5998 H  HA2  . GLY   B 1 133 ? 42.416 -33.980 6.507   1.00 22.04 ?  133 GLY   B HA2  1 
ATOM   5999 H  HA3  . GLY   B 1 133 ? 41.807 -33.118 7.660   1.00 22.04 ?  133 GLY   B HA3  1 
ATOM   6000 N  N    . ALA   B 1 134 ? 39.917 -32.591 5.327   1.00 17.72 ?  134 ALA   B N    1 
ATOM   6001 C  CA   . ALA   B 1 134 ? 38.593 -32.881 4.799   1.00 17.79 ?  134 ALA   B CA   1 
ATOM   6002 C  C    . ALA   B 1 134 ? 38.681 -33.875 3.646   1.00 17.75 ?  134 ALA   B C    1 
ATOM   6003 O  O    . ALA   B 1 134 ? 39.735 -34.065 3.031   1.00 18.65 ?  134 ALA   B O    1 
ATOM   6004 C  CB   . ALA   B 1 134 ? 37.906 -31.603 4.323   1.00 17.95 ?  134 ALA   B CB   1 
ATOM   6005 H  H    . ALA   B 1 134 ? 40.271 -31.846 5.063   1.00 21.38 ?  134 ALA   B H    1 
ATOM   6006 H  HA   . ALA   B 1 134 ? 38.054 -33.269 5.505   1.00 21.46 ?  134 ALA   B HA   1 
ATOM   6007 H  HB1  . ALA   B 1 134 ? 37.021 -31.829 3.996   1.00 21.66 ?  134 ALA   B HB1  1 
ATOM   6008 H  HB2  . ALA   B 1 134 ? 37.837 -30.984 5.066   1.00 21.66 ?  134 ALA   B HB2  1 
ATOM   6009 H  HB3  . ALA   B 1 134 ? 38.432 -31.209 3.610   1.00 21.66 ?  134 ALA   B HB3  1 
ATOM   6010 N  N    . ASP   B 1 135 ? 37.547 -34.505 3.358   1.00 18.11 ?  135 ASP   B N    1 
ATOM   6011 C  CA   . ASP   B 1 135 ? 37.439 -35.393 2.210   1.00 18.78 ?  135 ASP   B CA   1 
ATOM   6012 C  C    . ASP   B 1 135 ? 37.538 -34.558 0.941   1.00 17.59 ?  135 ASP   B C    1 
ATOM   6013 O  O    . ASP   B 1 135 ? 36.686 -33.684 0.717   1.00 17.38 ?  135 ASP   B O    1 
ATOM   6014 C  CB   . ASP   B 1 135 ? 36.097 -36.118 2.257   1.00 20.62 ?  135 ASP   B CB   1 
ATOM   6015 C  CG   . ASP   B 1 135 ? 35.929 -37.127 1.137   1.00 22.23 ?  135 ASP   B CG   1 
ATOM   6016 O  OD1  . ASP   B 1 135 ? 36.788 -37.177 0.231   1.00 22.17 ?  135 ASP   B OD1  1 
ATOM   6017 O  OD2  . ASP   B 1 135 ? 34.939 -37.894 1.179   1.00 25.10 -1 135 ASP   B OD2  1 
ATOM   6018 H  H    . ASP   B 1 135 ? 36.825 -34.438 3.821   1.00 21.85 ?  135 ASP   B H    1 
ATOM   6019 H  HA   . ASP   B 1 135 ? 38.155 -36.050 2.240   1.00 22.65 ?  135 ASP   B HA   1 
ATOM   6020 H  HB2  . ASP   B 1 135 ? 36.026 -36.592 3.096   1.00 24.86 ?  135 ASP   B HB2  1 
ATOM   6021 H  HB3  . ASP   B 1 135 ? 35.389 -35.464 2.176   1.00 24.86 ?  135 ASP   B HB3  1 
ATOM   6022 N  N    . PRO   B 1 136 ? 38.549 -34.766 0.097   1.00 17.71 ?  136 PRO   B N    1 
ATOM   6023 C  CA   . PRO   B 1 136 ? 38.650 -33.947 -1.119  1.00 17.03 ?  136 PRO   B CA   1 
ATOM   6024 C  C    . PRO   B 1 136 ? 37.460 -34.099 -2.046  1.00 16.32 ?  136 PRO   B C    1 
ATOM   6025 O  O    . PRO   B 1 136 ? 37.139 -33.149 -2.768  1.00 15.75 ?  136 PRO   B O    1 
ATOM   6026 C  CB   . PRO   B 1 136 ? 39.963 -34.422 -1.761  1.00 17.91 ?  136 PRO   B CB   1 
ATOM   6027 C  CG   . PRO   B 1 136 ? 40.167 -35.807 -1.218  1.00 19.08 ?  136 PRO   B CG   1 
ATOM   6028 C  CD   . PRO   B 1 136 ? 39.616 -35.779 0.176   1.00 18.79 ?  136 PRO   B CD   1 
ATOM   6029 H  HA   . PRO   B 1 136 ? 38.737 -33.012 -0.885  1.00 20.55 ?  136 PRO   B HA   1 
ATOM   6030 H  HB2  . PRO   B 1 136 ? 39.872 -34.440 -2.728  1.00 21.61 ?  136 PRO   B HB2  1 
ATOM   6031 H  HB3  . PRO   B 1 136 ? 40.687 -33.835 -1.495  1.00 21.61 ?  136 PRO   B HB3  1 
ATOM   6032 H  HG2  . PRO   B 1 136 ? 39.682 -36.451 -1.760  1.00 23.01 ?  136 PRO   B HG2  1 
ATOM   6033 H  HG3  . PRO   B 1 136 ? 41.114 -36.020 -1.202  1.00 23.01 ?  136 PRO   B HG3  1 
ATOM   6034 H  HD2  . PRO   B 1 136 ? 39.246 -36.644 0.414   1.00 22.67 ?  136 PRO   B HD2  1 
ATOM   6035 H  HD3  . PRO   B 1 136 ? 40.297 -35.498 0.809   1.00 22.67 ?  136 PRO   B HD3  1 
ATOM   6036 N  N    . ILE   B 1 137 ? 36.798 -35.263 -2.047  1.00 16.70 ?  137 ILE   B N    1 
ATOM   6037 C  CA   . ILE   B 1 137 ? 35.577 -35.434 -2.833  1.00 16.93 ?  137 ILE   B CA   1 
ATOM   6038 C  C    . ILE   B 1 137 ? 34.504 -34.462 -2.358  1.00 16.82 ?  137 ILE   B C    1 
ATOM   6039 O  O    . ILE   B 1 137 ? 33.792 -33.847 -3.163  1.00 16.29 ?  137 ILE   B O    1 
ATOM   6040 C  CB   . ILE   B 1 137 ? 35.105 -36.901 -2.766  1.00 18.81 ?  137 ILE   B CB   1 
ATOM   6041 C  CG1  . ILE   B 1 137 ? 36.116 -37.809 -3.471  1.00 20.91 ?  137 ILE   B CG1  1 
ATOM   6042 C  CG2  . ILE   B 1 137 ? 33.703 -37.046 -3.364  1.00 19.34 ?  137 ILE   B CG2  1 
ATOM   6043 C  CD1  . ILE   B 1 137 ? 35.790 -39.287 -3.378  1.00 23.19 ?  137 ILE   B CD1  1 
ATOM   6044 H  H    . ILE   B 1 137 ? 37.034 -35.965 -1.609  1.00 20.15 ?  137 ILE   B H    1 
ATOM   6045 H  HA   . ILE   B 1 137 ? 35.768 -35.232 -3.764  1.00 20.43 ?  137 ILE   B HA   1 
ATOM   6046 H  HB   . ILE   B 1 137 ? 35.059 -37.164 -1.839  1.00 22.68 ?  137 ILE   B HB   1 
ATOM   6047 H  HG12 . ILE   B 1 137 ? 36.149 -37.577 -4.412  1.00 25.20 ?  137 ILE   B HG12 1 
ATOM   6048 H  HG13 . ILE   B 1 137 ? 36.988 -37.677 -3.069  1.00 25.20 ?  137 ILE   B HG13 1 
ATOM   6049 H  HG21 . ILE   B 1 137 ? 33.447 -37.984 -3.377  1.00 23.32 ?  137 ILE   B HG21 1 
ATOM   6050 H  HG22 . ILE   B 1 137 ? 33.066 -36.558 -2.820  1.00 23.32 ?  137 ILE   B HG22 1 
ATOM   6051 H  HG23 . ILE   B 1 137 ? 33.701 -36.696 -4.269  1.00 23.32 ?  137 ILE   B HG23 1 
ATOM   6052 H  HD11 . ILE   B 1 137 ? 36.445 -39.775 -3.898  1.00 27.94 ?  137 ILE   B HD11 1 
ATOM   6053 H  HD12 . ILE   B 1 137 ? 35.827 -39.566 -2.448  1.00 27.94 ?  137 ILE   B HD12 1 
ATOM   6054 H  HD13 . ILE   B 1 137 ? 34.906 -39.455 -3.739  1.00 27.94 ?  137 ILE   B HD13 1 
ATOM   6055 N  N    . HIS   B 1 138 ? 34.377 -34.305 -1.043  1.00 16.95 ?  138 HIS   B N    1 
ATOM   6056 C  CA   . HIS   B 1 138 ? 33.427 -33.341 -0.509  1.00 17.43 ?  138 HIS   B CA   1 
ATOM   6057 C  C    . HIS   B 1 138 ? 33.841 -31.912 -0.842  1.00 16.43 ?  138 HIS   B C    1 
ATOM   6058 O  O    . HIS   B 1 138 ? 32.993 -31.074 -1.165  1.00 16.71 ?  138 HIS   B O    1 
ATOM   6059 C  CB   . HIS   B 1 138 ? 33.315 -33.509 0.999   1.00 18.71 ?  138 HIS   B CB   1 
ATOM   6060 C  CG   . HIS   B 1 138 ? 32.384 -32.527 1.633   1.00 19.59 ?  138 HIS   B CG   1 
ATOM   6061 N  ND1  . HIS   B 1 138 ? 31.044 -32.459 1.311   1.00 20.85 ?  138 HIS   B ND1  1 
ATOM   6062 C  CD2  . HIS   B 1 138 ? 32.601 -31.552 2.546   1.00 20.01 ?  138 HIS   B CD2  1 
ATOM   6063 C  CE1  . HIS   B 1 138 ? 30.475 -31.494 2.010   1.00 20.83 ?  138 HIS   B CE1  1 
ATOM   6064 N  NE2  . HIS   B 1 138 ? 31.396 -30.934 2.772   1.00 20.46 ?  138 HIS   B NE2  1 
ATOM   6065 H  H    . HIS   B 1 138 ? 34.824 -34.739 -0.452  1.00 20.45 ?  138 HIS   B H    1 
ATOM   6066 H  HA   . HIS   B 1 138 ? 32.552 -33.508 -0.898  1.00 21.04 ?  138 HIS   B HA   1 
ATOM   6067 H  HB2  . HIS   B 1 138 ? 32.984 -34.399 1.195   1.00 22.57 ?  138 HIS   B HB2  1 
ATOM   6068 H  HB3  . HIS   B 1 138 ? 34.189 -33.384 1.396   1.00 22.57 ?  138 HIS   B HB3  1 
ATOM   6069 H  HD1  . HIS   B 1 138 ? 30.640 -32.970 0.748   1.00 25.13 ?  138 HIS   B HD1  1 
ATOM   6070 H  HD2  . HIS   B 1 138 ? 33.404 -31.347 2.961   1.00 24.13 ?  138 HIS   B HD2  1 
ATOM   6071 H  HE1  . HIS   B 1 138 ? 29.569 -31.261 1.979   1.00 25.11 ?  138 HIS   B HE1  1 
ATOM   6072 N  N    . SER   B 1 139 ? 35.135 -31.605 -0.757  1.00 15.87 ?  139 SER   B N    1 
ATOM   6073 C  CA   . SER   B 1 139 ? 35.579 -30.258 -1.085  1.00 15.15 ?  139 SER   B CA   1 
ATOM   6074 C  C    . SER   B 1 139 ? 35.247 -29.916 -2.527  1.00 14.37 ?  139 SER   B C    1 
ATOM   6075 O  O    . SER   B 1 139 ? 34.799 -28.802 -2.815  1.00 14.35 ?  139 SER   B O    1 
ATOM   6076 C  CB   . SER   B 1 139 ? 37.075 -30.123 -0.815  1.00 15.48 ?  139 SER   B CB   1 
ATOM   6077 O  OG   . SER   B 1 139 ? 37.490 -28.788 -1.057  1.00 15.73 ?  139 SER   B OG   1 
ATOM   6078 H  H    . SER   B 1 139 ? 35.752 -32.148 -0.522  1.00 19.16 ?  139 SER   B H    1 
ATOM   6079 H  HA   . SER   B 1 139 ? 35.109 -29.628 -0.520  1.00 18.30 ?  139 SER   B HA   1 
ATOM   6080 H  HB2  . SER   B 1 139 ? 37.249 -30.350 0.113   1.00 18.69 ?  139 SER   B HB2  1 
ATOM   6081 H  HB3  . SER   B 1 139 ? 37.562 -30.719 -1.402  1.00 18.69 ?  139 SER   B HB3  1 
ATOM   6082 H  HG   . SER   B 1 139 ? 38.318 -28.715 -0.899  1.00 18.99 ?  139 SER   B HG   1 
ATOM   6083 N  N    . LEU   B 1 140 ? 35.430 -30.867 -3.444  1.00 14.07 ?  140 LEU   B N    1 
ATOM   6084 C  CA   . LEU   B 1 140 ? 35.071 -30.619 -4.834  1.00 13.90 ?  140 LEU   B CA   1 
ATOM   6085 C  C    . LEU   B 1 140 ? 33.570 -30.387 -4.971  1.00 14.24 ?  140 LEU   B C    1 
ATOM   6086 O  O    . LEU   B 1 140 ? 33.135 -29.500 -5.713  1.00 14.57 ?  140 LEU   B O    1 
ATOM   6087 C  CB   . LEU   B 1 140 ? 35.543 -31.782 -5.707  1.00 14.08 ?  140 LEU   B CB   1 
ATOM   6088 C  CG   . LEU   B 1 140 ? 35.180 -31.677 -7.182  1.00 14.61 ?  140 LEU   B CG   1 
ATOM   6089 C  CD1  . LEU   B 1 140 ? 35.746 -30.408 -7.780  1.00 15.05 ?  140 LEU   B CD1  1 
ATOM   6090 C  CD2  . LEU   B 1 140 ? 35.668 -32.912 -7.917  1.00 15.56 ?  140 LEU   B CD2  1 
ATOM   6091 H  H    . LEU   B 1 140 ? 35.752 -31.648 -3.292  1.00 17.00 ?  140 LEU   B H    1 
ATOM   6092 H  HA   . LEU   B 1 140 ? 35.528 -29.818 -5.139  1.00 16.80 ?  140 LEU   B HA   1 
ATOM   6093 H  HB2  . LEU   B 1 140 ? 36.511 -31.843 -5.653  1.00 17.01 ?  140 LEU   B HB2  1 
ATOM   6094 H  HB3  . LEU   B 1 140 ? 35.148 -32.604 -5.374  1.00 17.01 ?  140 LEU   B HB3  1 
ATOM   6095 H  HG   . LEU   B 1 140 ? 34.215 -31.634 -7.267  1.00 17.65 ?  140 LEU   B HG   1 
ATOM   6096 H  HD11 . LEU   B 1 140 ? 35.632 -30.436 -8.741  1.00 18.17 ?  140 LEU   B HD11 1 
ATOM   6097 H  HD12 . LEU   B 1 140 ? 35.268 -29.642 -7.415  1.00 18.17 ?  140 LEU   B HD12 1 
ATOM   6098 H  HD13 . LEU   B 1 140 ? 36.687 -30.345 -7.557  1.00 18.17 ?  140 LEU   B HD13 1 
ATOM   6099 H  HD21 . LEU   B 1 140 ? 35.428 -32.828 -8.853  1.00 18.78 ?  140 LEU   B HD21 1 
ATOM   6100 H  HD22 . LEU   B 1 140 ? 36.626 -32.973 -7.820  1.00 18.78 ?  140 LEU   B HD22 1 
ATOM   6101 H  HD23 . LEU   B 1 140 ? 35.237 -33.688 -7.530  1.00 18.78 ?  140 LEU   B HD23 1 
ATOM   6102 N  N    . ARG   B 1 141 ? 32.768 -31.181 -4.258  1.00 14.19 ?  141 ARG   B N    1 
ATOM   6103 C  CA   . ARG   B 1 141 ? 31.318 -31.002 -4.237  1.00 15.52 ?  141 ARG   B CA   1 
ATOM   6104 C  C    . ARG   B 1 141 ? 30.942 -29.590 -3.812  1.00 15.11 ?  141 ARG   B C    1 
ATOM   6105 O  O    . ARG   B 1 141 ? 30.140 -28.913 -4.475  1.00 15.31 ?  141 ARG   B O    1 
ATOM   6106 C  CB   . ARG   B 1 141 ? 30.733 -32.024 -3.254  1.00 16.69 ?  141 ARG   B CB   1 
ATOM   6107 C  CG   . ARG   B 1 141 ? 29.265 -31.908 -2.930  1.00 18.41 ?  141 ARG   B CG   1 
ATOM   6108 C  CD   . ARG   B 1 141 ? 28.472 -32.554 -3.986  1.00 19.84 ?  141 ARG   B CD   1 
ATOM   6109 N  NE   . ARG   B 1 141 ? 28.205 -31.647 -5.091  1.00 20.00 ?  141 ARG   B NE   1 
ATOM   6110 C  CZ   . ARG   B 1 141 ? 28.190 -32.006 -6.366  1.00 19.42 ?  141 ARG   B CZ   1 
ATOM   6111 N  NH1  . ARG   B 1 141 ? 28.620 -33.196 -6.756  1.00 19.19 ?  141 ARG   B NH1  1 
ATOM   6112 N  NH2  . ARG   B 1 141 ? 27.731 -31.150 -7.274  1.00 20.00 ?  141 ARG   B NH2  1 
ATOM   6113 H  H    . ARG   B 1 141 ? 33.046 -31.829 -3.771  1.00 17.15 ?  141 ARG   B H    1 
ATOM   6114 H  HA   . ARG   B 1 141 ? 30.952 -31.167 -5.116  1.00 18.74 ?  141 ARG   B HA   1 
ATOM   6115 H  HB2  . ARG   B 1 141 ? 30.889 -32.910 -3.615  1.00 20.14 ?  141 ARG   B HB2  1 
ATOM   6116 H  HB3  . ARG   B 1 141 ? 31.214 -31.941 -2.416  1.00 20.14 ?  141 ARG   B HB3  1 
ATOM   6117 H  HG2  . ARG   B 1 141 ? 29.093 -32.346 -2.086  1.00 22.21 ?  141 ARG   B HG2  1 
ATOM   6118 H  HG3  . ARG   B 1 141 ? 29.010 -30.967 -2.875  1.00 22.21 ?  141 ARG   B HG3  1 
ATOM   6119 H  HD2  . ARG   B 1 141 ? 28.957 -33.328 -4.320  1.00 23.93 ?  141 ARG   B HD2  1 
ATOM   6120 H  HD3  . ARG   B 1 141 ? 27.631 -32.839 -3.607  1.00 23.93 ?  141 ARG   B HD3  1 
ATOM   6121 H  HE   . ARG   B 1 141 ? 28.033 -30.826 -4.901  1.00 24.12 ?  141 ARG   B HE   1 
ATOM   6122 H  HH11 . ARG   B 1 141 ? 28.908 -33.769 -6.182  1.00 23.14 ?  141 ARG   B HH11 1 
ATOM   6123 H  HH12 . ARG   B 1 141 ? 28.609 -33.402 -7.589  1.00 23.14 ?  141 ARG   B HH12 1 
ATOM   6124 H  HH21 . ARG   B 1 141 ? 27.453 -30.371 -7.032  1.00 24.12 ?  141 ARG   B HH21 1 
ATOM   6125 H  HH22 . ARG   B 1 141 ? 27.734 -31.362 -8.108  1.00 24.12 ?  141 ARG   B HH22 1 
ATOM   6126 N  N    . VAL   B 1 142 ? 31.487 -29.139 -2.684  1.00 14.80 ?  142 VAL   B N    1 
ATOM   6127 C  CA   . VAL   B 1 142 ? 31.148 -27.805 -2.203  1.00 14.54 ?  142 VAL   B CA   1 
ATOM   6128 C  C    . VAL   B 1 142 ? 31.625 -26.748 -3.193  1.00 14.18 ?  142 VAL   B C    1 
ATOM   6129 O  O    . VAL   B 1 142 ? 30.925 -25.762 -3.455  1.00 14.62 ?  142 VAL   B O    1 
ATOM   6130 C  CB   . VAL   B 1 142 ? 31.695 -27.576 -0.781  1.00 15.02 ?  142 VAL   B CB   1 
ATOM   6131 C  CG1  . VAL   B 1 142 ? 31.381 -26.156 -0.309  1.00 15.26 ?  142 VAL   B CG1  1 
ATOM   6132 C  CG2  . VAL   B 1 142 ? 31.114 -28.604 0.178   1.00 15.50 ?  142 VAL   B CG2  1 
ATOM   6133 H  H    . VAL   B 1 142 ? 32.050 -29.571 -2.192  1.00 17.87 ?  142 VAL   B H    1 
ATOM   6134 H  HA   . VAL   B 1 142 ? 30.188 -27.736 -2.148  1.00 17.56 ?  142 VAL   B HA   1 
ATOM   6135 H  HB   . VAL   B 1 142 ? 32.661 -27.684 -0.786  1.00 18.14 ?  142 VAL   B HB   1 
ATOM   6136 H  HG11 . VAL   B 1 142 ? 31.567 -26.089 0.639   1.00 18.42 ?  142 VAL   B HG11 1 
ATOM   6137 H  HG12 . VAL   B 1 142 ? 31.940 -25.529 -0.799  1.00 18.42 ?  142 VAL   B HG12 1 
ATOM   6138 H  HG13 . VAL   B 1 142 ? 30.446 -25.968 -0.479  1.00 18.42 ?  142 VAL   B HG13 1 
ATOM   6139 H  HG21 . VAL   B 1 142 ? 31.426 -28.413 1.075   1.00 18.71 ?  142 VAL   B HG21 1 
ATOM   6140 H  HG22 . VAL   B 1 142 ? 30.147 -28.553 0.143   1.00 18.71 ?  142 VAL   B HG22 1 
ATOM   6141 H  HG23 . VAL   B 1 142 ? 31.409 -29.489 -0.094  1.00 18.71 ?  142 VAL   B HG23 1 
ATOM   6142 N  N    . CYS   B 1 143 ? 32.809 -26.945 -3.776  1.00 13.88 ?  143 CYS   B N    1 
ATOM   6143 C  CA   . CYS   B 1 143 ? 33.303 -26.009 -4.783  1.00 13.72 ?  143 CYS   B CA   1 
ATOM   6144 C  C    . CYS   B 1 143 ? 32.300 -25.869 -5.922  1.00 13.58 ?  143 CYS   B C    1 
ATOM   6145 O  O    . CYS   B 1 143 ? 31.901 -24.759 -6.289  1.00 13.63 ?  143 CYS   B O    1 
ATOM   6146 C  CB   . CYS   B 1 143 ? 34.660 -26.495 -5.304  1.00 13.83 ?  143 CYS   B CB   1 
ATOM   6147 S  SG   . CYS   B 1 143 ? 35.415 -25.397 -6.525  1.00 13.85 ?  143 CYS   B SG   1 
ATOM   6148 H  H    . CYS   B 1 143 ? 33.340 -27.597 -3.605  1.00 16.77 ?  143 CYS   B H    1 
ATOM   6149 H  HA   . CYS   B 1 143 ? 33.433 -25.136 -4.380  1.00 16.59 ?  143 CYS   B HA   1 
ATOM   6150 H  HB2  . CYS   B 1 143 ? 35.278 -26.580 -4.557  1.00 16.71 ?  143 CYS   B HB2  1 
ATOM   6151 H  HB3  . CYS   B 1 143 ? 34.543 -27.362 -5.721  1.00 16.71 ?  143 CYS   B HB3  1 
ATOM   6152 H  HG   . CYS   B 1 143 ? 36.494 -25.828 -6.835  1.00 16.74 ?  143 CYS   B HG   1 
ATOM   6153 N  N    . VAL   B 1 144 ? 31.891 -26.995 -6.504  1.00 14.32 ?  144 VAL   B N    1 
ATOM   6154 C  CA   . VAL   B 1 144 ? 30.984 -26.938 -7.644  1.00 15.05 ?  144 VAL   B CA   1 
ATOM   6155 C  C    . VAL   B 1 144 ? 29.646 -26.321 -7.268  1.00 15.44 ?  144 VAL   B C    1 
ATOM   6156 O  O    . VAL   B 1 144 ? 29.034 -25.611 -8.077  1.00 16.54 ?  144 VAL   B O    1 
ATOM   6157 C  CB   . VAL   B 1 144 ? 30.822 -28.348 -8.224  1.00 17.60 ?  144 VAL   B CB   1 
ATOM   6158 C  CG1  . VAL   B 1 144 ? 29.547 -28.471 -9.053  1.00 20.03 ?  144 VAL   B CG1  1 
ATOM   6159 C  CG2  . VAL   B 1 144 ? 32.062 -28.739 -9.028  1.00 18.08 ?  144 VAL   B CG2  1 
ATOM   6160 H  H    . VAL   B 1 144 ? 32.124 -27.788 -6.266  1.00 17.29 ?  144 VAL   B H    1 
ATOM   6161 H  HA   . VAL   B 1 144 ? 31.374 -26.380 -8.332  1.00 18.17 ?  144 VAL   B HA   1 
ATOM   6162 H  HB   . VAL   B 1 144 ? 30.748 -28.977 -7.489  1.00 21.24 ?  144 VAL   B HB   1 
ATOM   6163 H  HG11 . VAL   B 1 144 ? 29.619 -29.258 -9.620  1.00 24.15 ?  144 VAL   B HG11 1 
ATOM   6164 H  HG12 . VAL   B 1 144 ? 28.789 -28.568 -8.456  1.00 24.15 ?  144 VAL   B HG12 1 
ATOM   6165 H  HG13 . VAL   B 1 144 ? 29.447 -27.680 -9.601  1.00 24.15 ?  144 VAL   B HG13 1 
ATOM   6166 H  HG21 . VAL   B 1 144 ? 31.943 -29.635 -9.381  1.00 21.82 ?  144 VAL   B HG21 1 
ATOM   6167 H  HG22 . VAL   B 1 144 ? 32.173 -28.110 -9.761  1.00 21.82 ?  144 VAL   B HG22 1 
ATOM   6168 H  HG23 . VAL   B 1 144 ? 32.837 -28.710 -8.449  1.00 21.82 ?  144 VAL   B HG23 1 
ATOM   6169 N  N    . ASP   B 1 145 ? 29.175 -26.562 -6.048  1.00 15.72 ?  145 ASP   B N    1 
ATOM   6170 C  CA   . ASP   B 1 145 ? 27.867 -26.088 -5.621  1.00 16.18 ?  145 ASP   B CA   1 
ATOM   6171 C  C    . ASP   B 1 145 ? 27.897 -24.664 -5.085  1.00 15.72 ?  145 ASP   B C    1 
ATOM   6172 O  O    . ASP   B 1 145 ? 26.835 -24.121 -4.756  1.00 17.50 ?  145 ASP   B O    1 
ATOM   6173 C  CB   . ASP   B 1 145 ? 27.283 -27.001 -4.536  1.00 18.07 ?  145 ASP   B CB   1 
ATOM   6174 C  CG   . ASP   B 1 145 ? 26.927 -28.382 -5.042  1.00 19.62 ?  145 ASP   B CG   1 
ATOM   6175 O  OD1  . ASP   B 1 145 ? 26.821 -28.583 -6.268  1.00 19.59 ?  145 ASP   B OD1  1 
ATOM   6176 O  OD2  . ASP   B 1 145 ? 26.743 -29.264 -4.185  1.00 21.42 -1 145 ASP   B OD2  1 
ATOM   6177 H  H    . ASP   B 1 145 ? 29.607 -26.987 -5.438  1.00 18.98 ?  145 ASP   B H    1 
ATOM   6178 H  HA   . ASP   B 1 145 ? 27.270 -26.086 -6.380  1.00 19.53 ?  145 ASP   B HA   1 
ATOM   6179 H  HB2  . ASP   B 1 145 ? 27.930 -27.108 -3.832  1.00 21.79 ?  145 ASP   B HB2  1 
ATOM   6180 H  HB3  . ASP   B 1 145 ? 26.471 -26.591 -4.189  1.00 21.79 ?  145 ASP   B HB3  1 
ATOM   6181 N  N    . THR   B 1 146 ? 29.073 -24.046 -4.983  1.00 14.17 ?  146 THR   B N    1 
ATOM   6182 C  CA   . THR   B 1 146 ? 29.201 -22.722 -4.381  1.00 13.78 ?  146 THR   B CA   1 
ATOM   6183 C  C    . THR   B 1 146 ? 29.835 -21.696 -5.302  1.00 13.44 ?  146 THR   B C    1 
ATOM   6184 O  O    . THR   B 1 146 ? 29.385 -20.535 -5.347  1.00 13.64 ?  146 THR   B O    1 
ATOM   6185 C  CB   . THR   B 1 146 ? 30.033 -22.819 -3.093  1.00 13.78 ?  146 THR   B CB   1 
ATOM   6186 O  OG1  . THR   B 1 146 ? 29.461 -23.808 -2.231  1.00 14.45 ?  146 THR   B OG1  1 
ATOM   6187 C  CG2  . THR   B 1 146 ? 30.103 -21.472 -2.380  1.00 14.13 ?  146 THR   B CG2  1 
ATOM   6188 H  H    . THR   B 1 146 ? 29.826 -24.366 -5.263  1.00 17.11 ?  146 THR   B H    1 
ATOM   6189 H  HA   . THR   B 1 146 ? 28.328 -22.389 -4.143  1.00 16.65 ?  146 THR   B HA   1 
ATOM   6190 H  HB   . THR   B 1 146 ? 30.941 -23.077 -3.316  1.00 16.65 ?  146 THR   B HB   1 
ATOM   6191 H  HG1  . THR   B 1 146 ? 29.494 -24.567 -2.606  1.00 17.46 ?  146 THR   B HG1  1 
ATOM   6192 H  HG21 . THR   B 1 146 ? 30.445 -21.589 -1.481  1.00 17.07 ?  146 THR   B HG21 1 
ATOM   6193 H  HG22 . THR   B 1 146 ? 30.693 -20.868 -2.862  1.00 17.07 ?  146 THR   B HG22 1 
ATOM   6194 H  HG23 . THR   B 1 146 ? 29.219 -21.076 -2.332  1.00 17.07 ?  146 THR   B HG23 1 
ATOM   6195 N  N    . VAL   B 1 147 ? 30.905 -22.069 -5.996  1.00 13.32 ?  147 VAL   B N    1 
ATOM   6196 C  CA   . VAL   B 1 147 ? 31.630 -21.128 -6.838  1.00 12.99 ?  147 VAL   B CA   1 
ATOM   6197 C  C    . VAL   B 1 147 ? 30.898 -20.996 -8.160  1.00 13.05 ?  147 VAL   B C    1 
ATOM   6198 O  O    . VAL   B 1 147 ? 30.532 -22.001 -8.784  1.00 14.19 ?  147 VAL   B O    1 
ATOM   6199 C  CB   . VAL   B 1 147 ? 33.083 -21.589 -7.041  1.00 13.11 ?  147 VAL   B CB   1 
ATOM   6200 C  CG1  . VAL   B 1 147 ? 33.850 -20.563 -7.863  1.00 12.69 ?  147 VAL   B CG1  1 
ATOM   6201 C  CG2  . VAL   B 1 147 ? 33.765 -21.806 -5.697  1.00 12.94 ?  147 VAL   B CG2  1 
ATOM   6202 H  H    . VAL   B 1 147 ? 31.231 -22.868 -6.004  1.00 16.10 ?  147 VAL   B H    1 
ATOM   6203 H  HA   . VAL   B 1 147 ? 31.651 -20.259 -6.410  1.00 15.71 ?  147 VAL   B HA   1 
ATOM   6204 H  HB   . VAL   B 1 147 ? 33.091 -22.432 -7.528  1.00 15.84 ?  147 VAL   B HB   1 
ATOM   6205 H  HG11 . VAL   B 1 147 ? 34.791 -20.786 -7.854  1.00 15.35 ?  147 VAL   B HG11 1 
ATOM   6206 H  HG12 . VAL   B 1 147 ? 33.515 -20.566 -8.773  1.00 15.35 ?  147 VAL   B HG12 1 
ATOM   6207 H  HG13 . VAL   B 1 147 ? 33.716 -19.683 -7.466  1.00 15.35 ?  147 VAL   B HG13 1 
ATOM   6208 H  HG21 . VAL   B 1 147 ? 34.704 -22.003 -5.846  1.00 15.64 ?  147 VAL   B HG21 1 
ATOM   6209 H  HG22 . VAL   B 1 147 ? 33.677 -20.998 -5.167  1.00 15.64 ?  147 VAL   B HG22 1 
ATOM   6210 H  HG23 . VAL   B 1 147 ? 33.341 -22.549 -5.241  1.00 15.64 ?  147 VAL   B HG23 1 
ATOM   6211 N  N    . ARG   B 1 148 ? 30.689 -19.749 -8.585  1.00 12.96 ?  148 ARG   B N    1 
ATOM   6212 C  CA   . ARG   B 1 148 ? 30.066 -19.440 -9.862  1.00 13.53 ?  148 ARG   B CA   1 
ATOM   6213 C  C    . ARG   B 1 148 ? 31.025 -18.767 -10.834 1.00 13.37 ?  148 ARG   B C    1 
ATOM   6214 O  O    . ARG   B 1 148 ? 30.739 -18.739 -12.032 1.00 15.05 ?  148 ARG   B O    1 
ATOM   6215 C  CB   . ARG   B 1 148 ? 28.827 -18.551 -9.654  1.00 13.75 ?  148 ARG   B CB   1 
ATOM   6216 C  CG   . ARG   B 1 148 ? 27.748 -19.253 -8.837  1.00 14.36 ?  148 ARG   B CG   1 
ATOM   6217 C  CD   . ARG   B 1 148 ? 26.543 -18.360 -8.523  1.00 15.41 ?  148 ARG   B CD   1 
ATOM   6218 N  NE   . ARG   B 1 148 ? 26.932 -17.161 -7.792  1.00 15.47 ?  148 ARG   B NE   1 
ATOM   6219 C  CZ   . ARG   B 1 148 ? 27.231 -17.129 -6.500  1.00 14.37 ?  148 ARG   B CZ   1 
ATOM   6220 N  NH1  . ARG   B 1 148 ? 27.164 -18.215 -5.744  1.00 14.44 ?  148 ARG   B NH1  1 
ATOM   6221 N  NH2  . ARG   B 1 148 ? 27.634 -15.982 -5.960  1.00 14.11 ?  148 ARG   B NH2  1 
ATOM   6222 H  H    . ARG   B 1 148 ? 30.912 -19.045 -8.136  1.00 15.66 ?  148 ARG   B H    1 
ATOM   6223 H  HA   . ARG   B 1 148 ? 29.771 -20.264 -10.270 1.00 16.35 ?  148 ARG   B HA   1 
ATOM   6224 H  HB2  . ARG   B 1 148 ? 29.085 -17.746 -9.180  1.00 16.62 ?  148 ARG   B HB2  1 
ATOM   6225 H  HB3  . ARG   B 1 148 ? 28.450 -18.324 -10.519 1.00 16.62 ?  148 ARG   B HB3  1 
ATOM   6226 H  HG2  . ARG   B 1 148 ? 27.425 -20.023 -9.339  1.00 17.35 ?  148 ARG   B HG2  1 
ATOM   6227 H  HG3  . ARG   B 1 148 ? 28.127 -19.548 -7.997  1.00 17.35 ?  148 ARG   B HG3  1 
ATOM   6228 H  HD2  . ARG   B 1 148 ? 26.125 -18.090 -9.354  1.00 18.61 ?  148 ARG   B HD2  1 
ATOM   6229 H  HD3  . ARG   B 1 148 ? 25.911 -18.861 -7.980  1.00 18.61 ?  148 ARG   B HD3  1 
ATOM   6230 H  HE   . ARG   B 1 148 ? 26.985 -16.431 -8.232  1.00 18.67 ?  148 ARG   B HE   1 
ATOM   6231 H  HH11 . ARG   B 1 148 ? 26.902 -18.965 -6.079  1.00 17.45 ?  148 ARG   B HH11 1 
ATOM   6232 H  HH12 . ARG   B 1 148 ? 27.356 -18.169 -4.906  1.00 17.45 ?  148 ARG   B HH12 1 
ATOM   6233 H  HH21 . ARG   B 1 148 ? 27.691 -15.278 -6.447  1.00 17.05 ?  148 ARG   B HH21 1 
ATOM   6234 H  HH22 . ARG   B 1 148 ? 27.832 -15.948 -5.125  1.00 17.05 ?  148 ARG   B HH22 1 
ATOM   6235 N  N    . THR   B 1 149 ? 32.134 -18.211 -10.346 1.00 13.06 ?  149 THR   B N    1 
ATOM   6236 C  CA   . THR   B 1 149 ? 33.175 -17.645 -11.191 1.00 13.30 ?  149 THR   B CA   1 
ATOM   6237 C  C    . THR   B 1 149 ? 34.058 -18.787 -11.704 1.00 12.97 ?  149 THR   B C    1 
ATOM   6238 O  O    . THR   B 1 149 ? 33.862 -19.957 -11.363 1.00 13.27 ?  149 THR   B O    1 
ATOM   6239 C  CB   . THR   B 1 149 ? 33.946 -16.591 -10.404 1.00 13.20 ?  149 THR   B CB   1 
ATOM   6240 O  OG1  . THR   B 1 149 ? 34.404 -17.198 -9.196  1.00 13.33 ?  149 THR   B OG1  1 
ATOM   6241 C  CG2  . THR   B 1 149 ? 33.054 -15.386 -10.100 1.00 13.96 ?  149 THR   B CG2  1 
ATOM   6242 H  H    . THR   B 1 149 ? 32.299 -18.145 -9.508  1.00 15.79 ?  149 THR   B H    1 
ATOM   6243 H  HA   . THR   B 1 149 ? 32.766 -17.209 -11.956 1.00 16.08 ?  149 THR   B HA   1 
ATOM   6244 H  HB   . THR   B 1 149 ? 34.707 -16.296 -10.918 1.00 15.95 ?  149 THR   B HB   1 
ATOM   6245 H  HG1  . THR   B 1 149 ? 34.824 -16.629 -8.728  1.00 16.11 ?  149 THR   B HG1  1 
ATOM   6246 H  HG21 . THR   B 1 149 ? 33.559 -14.717 -9.607  1.00 16.87 ?  149 THR   B HG21 1 
ATOM   6247 H  HG22 . THR   B 1 149 ? 32.738 -14.992 -10.927 1.00 16.87 ?  149 THR   B HG22 1 
ATOM   6248 H  HG23 . THR   B 1 149 ? 32.291 -15.657 -9.567  1.00 16.87 ?  149 THR   B HG23 1 
ATOM   6249 N  N    . ASN   B 1 150 ? 35.026 -18.466 -12.553 1.00 12.95 ?  150 ASN   B N    1 
ATOM   6250 C  CA   . ASN   B 1 150 ? 35.789 -19.496 -13.250 1.00 13.21 ?  150 ASN   B CA   1 
ATOM   6251 C  C    . ASN   B 1 150 ? 36.956 -19.944 -12.378 1.00 12.94 ?  150 ASN   B C    1 
ATOM   6252 O  O    . ASN   B 1 150 ? 37.889 -19.173 -12.130 1.00 13.35 ?  150 ASN   B O    1 
ATOM   6253 C  CB   . ASN   B 1 150 ? 36.258 -18.974 -14.602 1.00 15.15 ?  150 ASN   B CB   1 
ATOM   6254 C  CG   . ASN   B 1 150 ? 35.112 -18.749 -15.542 1.00 17.71 ?  150 ASN   B CG   1 
ATOM   6255 O  OD1  . ASN   B 1 150 ? 34.216 -19.578 -15.634 1.00 18.73 ?  150 ASN   B OD1  1 
ATOM   6256 N  ND2  . ASN   B 1 150 ? 35.107 -17.611 -16.220 1.00 19.49 ?  150 ASN   B ND2  1 
ATOM   6257 H  H    . ASN   B 1 150 ? 35.268 -17.659 -12.737 1.00 15.65 ?  150 ASN   B H    1 
ATOM   6258 H  HA   . ASN   B 1 150 ? 35.212 -20.262 -13.408 1.00 15.96 ?  150 ASN   B HA   1 
ATOM   6259 H  HB2  . ASN   B 1 150 ? 36.713 -18.127 -14.476 1.00 18.29 ?  150 ASN   B HB2  1 
ATOM   6260 H  HB3  . ASN   B 1 150 ? 36.851 -19.621 -15.006 1.00 18.29 ?  150 ASN   B HB3  1 
ATOM   6261 H  HD21 . ASN   B 1 150 ? 34.468 -17.430 -16.771 1.00 23.51 ?  150 ASN   B HD21 1 
ATOM   6262 H  HD22 . ASN   B 1 150 ? 35.753 -17.048 -16.122 1.00 23.51 ?  150 ASN   B HD22 1 
ATOM   6263 N  N    . VAL   B 1 151 ? 36.911 -21.191 -11.917 1.00 12.75 ?  151 VAL   B N    1 
ATOM   6264 C  CA   . VAL   B 1 151 ? 37.926 -21.721 -11.017 1.00 12.98 ?  151 VAL   B CA   1 
ATOM   6265 C  C    . VAL   B 1 151 ? 38.632 -22.893 -11.684 1.00 12.82 ?  151 VAL   B C    1 
ATOM   6266 O  O    . VAL   B 1 151 ? 37.988 -23.823 -12.190 1.00 13.73 ?  151 VAL   B O    1 
ATOM   6267 C  CB   . VAL   B 1 151 ? 37.360 -22.060 -9.622  1.00 14.19 ?  151 VAL   B CB   1 
ATOM   6268 C  CG1  . VAL   B 1 151 ? 36.194 -23.047 -9.706  1.00 15.30 ?  151 VAL   B CG1  1 
ATOM   6269 C  CG2  . VAL   B 1 151 ? 38.468 -22.553 -8.701  1.00 14.38 ?  151 VAL   B CG2  1 
ATOM   6270 H  H    . VAL   B 1 151 ? 36.293 -21.756 -12.126 1.00 15.41 ?  151 VAL   B H    1 
ATOM   6271 H  HA   . VAL   B 1 151 ? 38.589 -21.028 -10.885 1.00 15.70 ?  151 VAL   B HA   1 
ATOM   6272 H  HB   . VAL   B 1 151 ? 37.009 -21.241 -9.237  1.00 17.14 ?  151 VAL   B HB   1 
ATOM   6273 H  HG11 . VAL   B 1 151 ? 35.872 -23.234 -8.810  1.00 18.48 ?  151 VAL   B HG11 1 
ATOM   6274 H  HG12 . VAL   B 1 151 ? 35.478 -22.654 -10.236 1.00 18.48 ?  151 VAL   B HG12 1 
ATOM   6275 H  HG13 . VAL   B 1 151 ? 36.499 -23.867 -10.125 1.00 18.48 ?  151 VAL   B HG13 1 
ATOM   6276 H  HG21 . VAL   B 1 151 ? 38.111 -22.630 -7.800  1.00 17.38 ?  151 VAL   B HG21 1 
ATOM   6277 H  HG22 . VAL   B 1 151 ? 38.775 -23.418 -9.009  1.00 17.38 ?  151 VAL   B HG22 1 
ATOM   6278 H  HG23 . VAL   B 1 151 ? 39.195 -21.913 -8.713  1.00 17.38 ?  151 VAL   B HG23 1 
ATOM   6279 N  N    . TYR   B 1 152 ? 39.963 -22.807 -11.705 1.00 12.44 ?  152 TYR   B N    1 
ATOM   6280 C  CA   . TYR   B 1 152 ? 40.865 -23.789 -12.289 1.00 12.75 ?  152 TYR   B CA   1 
ATOM   6281 C  C    . TYR   B 1 152 ? 41.589 -24.467 -11.132 1.00 11.85 ?  152 TYR   B C    1 
ATOM   6282 O  O    . TYR   B 1 152 ? 42.441 -23.852 -10.481 1.00 12.40 ?  152 TYR   B O    1 
ATOM   6283 C  CB   . TYR   B 1 152 ? 41.834 -23.086 -13.240 1.00 13.46 ?  152 TYR   B CB   1 
ATOM   6284 C  CG   . TYR   B 1 152 ? 41.152 -22.628 -14.507 1.00 14.06 ?  152 TYR   B CG   1 
ATOM   6285 C  CD1  . TYR   B 1 152 ? 40.487 -21.405 -14.572 1.00 14.36 ?  152 TYR   B CD1  1 
ATOM   6286 C  CD2  . TYR   B 1 152 ? 41.151 -23.433 -15.632 1.00 15.10 ?  152 TYR   B CD2  1 
ATOM   6287 C  CE1  . TYR   B 1 152 ? 39.846 -21.004 -15.729 1.00 15.81 ?  152 TYR   B CE1  1 
ATOM   6288 C  CE2  . TYR   B 1 152 ? 40.511 -23.047 -16.789 1.00 15.87 ?  152 TYR   B CE2  1 
ATOM   6289 C  CZ   . TYR   B 1 152 ? 39.863 -21.828 -16.837 1.00 16.10 ?  152 TYR   B CZ   1 
ATOM   6290 O  OH   . TYR   B 1 152 ? 39.231 -21.449 -17.997 1.00 18.61 ?  152 TYR   B OH   1 
ATOM   6291 H  H    . TYR   B 1 152 ? 40.395 -22.140 -11.358 1.00 15.04 ?  152 TYR   B H    1 
ATOM   6292 H  HA   . TYR   B 1 152 ? 40.355 -24.452 -12.783 1.00 15.42 ?  152 TYR   B HA   1 
ATOM   6293 H  HB2  . TYR   B 1 152 ? 42.202 -22.306 -12.794 1.00 16.26 ?  152 TYR   B HB2  1 
ATOM   6294 H  HB3  . TYR   B 1 152 ? 42.544 -23.698 -13.481 1.00 16.26 ?  152 TYR   B HB3  1 
ATOM   6295 H  HD1  . TYR   B 1 152 ? 40.472 -20.849 -13.825 1.00 17.35 ?  152 TYR   B HD1  1 
ATOM   6296 H  HD2  . TYR   B 1 152 ? 41.580 -24.259 -15.601 1.00 18.24 ?  152 TYR   B HD2  1 
ATOM   6297 H  HE1  . TYR   B 1 152 ? 39.409 -20.184 -15.764 1.00 19.08 ?  152 TYR   B HE1  1 
ATOM   6298 H  HE2  . TYR   B 1 152 ? 40.524 -23.601 -17.535 1.00 19.16 ?  152 TYR   B HE2  1 
ATOM   6299 H  HH   . TYR   B 1 152 ? 39.331 -22.043 -18.583 1.00 22.45 ?  152 TYR   B HH   1 
ATOM   6300 N  N    . LEU   B 1 153 ? 41.221 -25.723 -10.861 1.00 12.04 ?  153 LEU   B N    1 
ATOM   6301 C  CA   . LEU   B 1 153 ? 41.729 -26.472 -9.722  1.00 12.04 ?  153 LEU   B CA   1 
ATOM   6302 C  C    . LEU   B 1 153 ? 42.963 -27.270 -10.119 1.00 12.36 ?  153 LEU   B C    1 
ATOM   6303 O  O    . LEU   B 1 153 ? 42.949 -27.997 -11.115 1.00 13.37 ?  153 LEU   B O    1 
ATOM   6304 C  CB   . LEU   B 1 153 ? 40.652 -27.428 -9.201  1.00 12.42 ?  153 LEU   B CB   1 
ATOM   6305 C  CG   . LEU   B 1 153 ? 39.396 -26.763 -8.634  1.00 13.05 ?  153 LEU   B CG   1 
ATOM   6306 C  CD1  . LEU   B 1 153 ? 38.288 -27.800 -8.464  1.00 14.16 ?  153 LEU   B CD1  1 
ATOM   6307 C  CD2  . LEU   B 1 153 ? 39.698 -26.093 -7.304  1.00 13.47 ?  153 LEU   B CD2  1 
ATOM   6308 H  H    . LEU   B 1 153 ? 40.643 -26.166 -11.334 1.00 14.56 ?  153 LEU   B H    1 
ATOM   6309 H  HA   . LEU   B 1 153 ? 41.962 -25.854 -9.016  1.00 14.56 ?  153 LEU   B HA   1 
ATOM   6310 H  HB2  . LEU   B 1 153 ? 40.371 -28.004 -9.925  1.00 15.02 ?  153 LEU   B HB2  1 
ATOM   6311 H  HB3  . LEU   B 1 153 ? 41.038 -27.963 -8.488  1.00 15.02 ?  153 LEU   B HB3  1 
ATOM   6312 H  HG   . LEU   B 1 153 ? 39.080 -26.079 -9.250  1.00 15.78 ?  153 LEU   B HG   1 
ATOM   6313 H  HD11 . LEU   B 1 153 ? 37.483 -27.349 -8.160  1.00 17.11 ?  153 LEU   B HD11 1 
ATOM   6314 H  HD12 . LEU   B 1 153 ? 38.130 -28.225 -9.316  1.00 17.11 ?  153 LEU   B HD12 1 
ATOM   6315 H  HD13 . LEU   B 1 153 ? 38.573 -28.450 -7.807  1.00 17.11 ?  153 LEU   B HD13 1 
ATOM   6316 H  HD21 . LEU   B 1 153 ? 38.885 -25.715 -6.938  1.00 16.27 ?  153 LEU   B HD21 1 
ATOM   6317 H  HD22 . LEU   B 1 153 ? 40.064 -26.752 -6.693  1.00 16.27 ?  153 LEU   B HD22 1 
ATOM   6318 H  HD23 . LEU   B 1 153 ? 40.353 -25.384 -7.448  1.00 16.27 ?  153 LEU   B HD23 1 
ATOM   6319 N  N    . ALA   B 1 154 ? 44.015 -27.156 -9.316  1.00 12.42 ?  154 ALA   B N    1 
ATOM   6320 C  CA   . ALA   B 1 154 ? 45.243 -27.921 -9.497  1.00 13.75 ?  154 ALA   B CA   1 
ATOM   6321 C  C    . ALA   B 1 154 ? 45.310 -28.997 -8.422  1.00 14.13 ?  154 ALA   B C    1 
ATOM   6322 O  O    . ALA   B 1 154 ? 45.243 -28.692 -7.223  1.00 15.43 ?  154 ALA   B O    1 
ATOM   6323 C  CB   . ALA   B 1 154 ? 46.462 -27.005 -9.423  1.00 14.20 ?  154 ALA   B CB   1 
ATOM   6324 H  H    . ALA   B 1 154 ? 44.035 -26.627 -8.638  1.00 15.02 ?  154 ALA   B H    1 
ATOM   6325 H  HA   . ALA   B 1 154 ? 45.233 -28.349 -10.363 1.00 16.61 ?  154 ALA   B HA   1 
ATOM   6326 H  HB1  . ALA   B 1 154 ? 47.265 -27.535 -9.543  1.00 17.16 ?  154 ALA   B HB1  1 
ATOM   6327 H  HB2  . ALA   B 1 154 ? 46.400 -26.335 -10.124 1.00 17.16 ?  154 ALA   B HB2  1 
ATOM   6328 H  HB3  . ALA   B 1 154 ? 46.483 -26.569 -8.554  1.00 17.16 ?  154 ALA   B HB3  1 
ATOM   6329 N  N    . VAL   B 1 155 ? 45.429 -30.247 -8.851  1.00 13.28 ?  155 VAL   B N    1 
ATOM   6330 C  CA   . VAL   B 1 155 ? 45.534 -31.392 -7.955  1.00 13.58 ?  155 VAL   B CA   1 
ATOM   6331 C  C    . VAL   B 1 155 ? 46.875 -32.063 -8.234  1.00 13.21 ?  155 VAL   B C    1 
ATOM   6332 O  O    . VAL   B 1 155 ? 47.106 -32.561 -9.344  1.00 15.07 ?  155 VAL   B O    1 
ATOM   6333 C  CB   . VAL   B 1 155 ? 44.379 -32.388 -8.151  1.00 15.08 ?  155 VAL   B CB   1 
ATOM   6334 C  CG1  . VAL   B 1 155 ? 44.555 -33.591 -7.233  1.00 15.24 ?  155 VAL   B CG1  1 
ATOM   6335 C  CG2  . VAL   B 1 155 ? 43.041 -31.699 -7.897  1.00 16.01 ?  155 VAL   B CG2  1 
ATOM   6336 H  H    . VAL   B 1 155 ? 45.462 -30.469 -9.685  1.00 16.05 ?  155 VAL   B H    1 
ATOM   6337 H  HA   . VAL   B 1 155 ? 45.525 -31.091 -7.034  1.00 16.42 ?  155 VAL   B HA   1 
ATOM   6338 H  HB   . VAL   B 1 155 ? 44.383 -32.702 -9.069  1.00 18.21 ?  155 VAL   B HB   1 
ATOM   6339 H  HG11 . VAL   B 1 155 ? 43.728 -34.100 -7.212  1.00 18.41 ?  155 VAL   B HG11 1 
ATOM   6340 H  HG12 . VAL   B 1 155 ? 45.274 -34.152 -7.571  1.00 18.41 ?  155 VAL   B HG12 1 
ATOM   6341 H  HG13 . VAL   B 1 155 ? 44.772 -33.282 -6.339  1.00 18.41 ?  155 VAL   B HG13 1 
ATOM   6342 H  HG21 . VAL   B 1 155 ? 42.331 -32.355 -7.980  1.00 19.33 ?  155 VAL   B HG21 1 
ATOM   6343 H  HG22 . VAL   B 1 155 ? 43.045 -31.329 -7.000  1.00 19.33 ?  155 VAL   B HG22 1 
ATOM   6344 H  HG23 . VAL   B 1 155 ? 42.920 -30.993 -8.548  1.00 19.33 ?  155 VAL   B HG23 1 
ATOM   6345 N  N    . PHE   B 1 156 ? 47.740 -32.105 -7.220  1.00 14.10 ?  156 PHE   B N    1 
ATOM   6346 C  CA   . PHE   B 1 156 ? 49.116 -32.561 -7.421  1.00 15.23 ?  156 PHE   B CA   1 
ATOM   6347 C  C    . PHE   B 1 156 ? 49.210 -34.061 -7.701  1.00 16.54 ?  156 PHE   B C    1 
ATOM   6348 O  O    . PHE   B 1 156 ? 49.925 -34.491 -8.616  1.00 18.33 ?  156 PHE   B O    1 
ATOM   6349 C  CB   . PHE   B 1 156 ? 49.945 -32.189 -6.194  1.00 15.46 ?  156 PHE   B CB   1 
ATOM   6350 C  CG   . PHE   B 1 156 ? 51.374 -32.649 -6.256  1.00 16.01 ?  156 PHE   B CG   1 
ATOM   6351 C  CD1  . PHE   B 1 156 ? 52.254 -32.106 -7.174  1.00 17.37 ?  156 PHE   B CD1  1 
ATOM   6352 C  CD2  . PHE   B 1 156 ? 51.838 -33.612 -5.383  1.00 16.35 ?  156 PHE   B CD2  1 
ATOM   6353 C  CE1  . PHE   B 1 156 ? 53.577 -32.515 -7.223  1.00 18.05 ?  156 PHE   B CE1  1 
ATOM   6354 C  CE2  . PHE   B 1 156 ? 53.157 -34.027 -5.430  1.00 17.56 ?  156 PHE   B CE2  1 
ATOM   6355 C  CZ   . PHE   B 1 156 ? 54.018 -33.480 -6.355  1.00 18.14 ?  156 PHE   B CZ   1 
ATOM   6356 H  H    . PHE   B 1 156 ? 47.551 -31.886 -6.410  1.00 17.03 ?  156 PHE   B H    1 
ATOM   6357 H  HA   . PHE   B 1 156 ? 49.486 -32.091 -8.182  1.00 18.39 ?  156 PHE   B HA   1 
ATOM   6358 H  HB2  . PHE   B 1 156 ? 49.949 -31.224 -6.103  1.00 18.67 ?  156 PHE   B HB2  1 
ATOM   6359 H  HB3  . PHE   B 1 156 ? 49.540 -32.590 -5.408  1.00 18.67 ?  156 PHE   B HB3  1 
ATOM   6360 H  HD1  . PHE   B 1 156 ? 51.956 -31.447 -7.764  1.00 20.96 ?  156 PHE   B HD1  1 
ATOM   6361 H  HD2  . PHE   B 1 156 ? 51.255 -33.986 -4.762  1.00 19.73 ?  156 PHE   B HD2  1 
ATOM   6362 H  HE1  . PHE   B 1 156 ? 54.160 -32.143 -7.848  1.00 21.78 ?  156 PHE   B HE1  1 
ATOM   6363 H  HE2  . PHE   B 1 156 ? 53.458 -34.686 -4.842  1.00 21.19 ?  156 PHE   B HE2  1 
ATOM   6364 H  HZ   . PHE   B 1 156 ? 54.907 -33.764 -6.386  1.00 21.89 ?  156 PHE   B HZ   1 
ATOM   6365 N  N    . ASP   B 1 157 ? 48.550 -34.876 -6.890  1.00 16.97 ?  157 ASP   B N    1 
ATOM   6366 C  CA   . ASP   B 1 157 ? 48.694 -36.324 -6.984  1.00 18.33 ?  157 ASP   B CA   1 
ATOM   6367 C  C    . ASP   B 1 157 ? 47.779 -36.874 -8.072  1.00 18.68 ?  157 ASP   B C    1 
ATOM   6368 O  O    . ASP   B 1 157 ? 46.553 -36.759 -7.970  1.00 18.07 ?  157 ASP   B O    1 
ATOM   6369 C  CB   . ASP   B 1 157 ? 48.333 -36.938 -5.638  1.00 19.72 ?  157 ASP   B CB   1 
ATOM   6370 C  CG   . ASP   B 1 157 ? 48.478 -38.448 -5.622  1.00 21.61 ?  157 ASP   B CG   1 
ATOM   6371 O  OD1  . ASP   B 1 157 ? 48.818 -39.045 -6.671  1.00 22.38 ?  157 ASP   B OD1  1 
ATOM   6372 O  OD2  . ASP   B 1 157 ? 48.264 -39.034 -4.546  1.00 23.59 -1 157 ASP   B OD2  1 
ATOM   6373 H  H    . ASP   B 1 157 ? 48.017 -34.616 -6.273  1.00 20.48 ?  157 ASP   B H    1 
ATOM   6374 H  HA   . ASP   B 1 157 ? 49.611 -36.556 -7.199  1.00 22.11 ?  157 ASP   B HA   1 
ATOM   6375 H  HB2  . ASP   B 1 157 ? 48.901 -36.554 -4.956  1.00 23.79 ?  157 ASP   B HB2  1 
ATOM   6376 H  HB3  . ASP   B 1 157 ? 47.400 -36.731 -5.442  1.00 23.79 ?  157 ASP   B HB3  1 
ATOM   6377 N  N    . LYS   B 1 158 ? 48.373 -37.504 -9.094  1.00 19.61 ?  158 LYS   B N    1 
ATOM   6378 C  CA   . LYS   B 1 158 ? 47.598 -38.117 -10.176 1.00 20.68 ?  158 LYS   B CA   1 
ATOM   6379 C  C    . LYS   B 1 158 ? 46.533 -39.080 -9.648  1.00 20.60 ?  158 LYS   B C    1 
ATOM   6380 O  O    . LYS   B 1 158 ? 45.429 -39.164 -10.203 1.00 20.74 ?  158 LYS   B O    1 
ATOM   6381 C  CB   . LYS   B 1 158 ? 48.548 -38.835 -11.147 1.00 22.55 ?  158 LYS   B CB   1 
ATOM   6382 C  CG   . LYS   B 1 158 ? 47.871 -39.741 -12.169 1.00 24.89 ?  158 LYS   B CG   1 
ATOM   6383 C  CD   . LYS   B 1 158 ? 47.002 -38.966 -13.141 1.00 27.06 ?  158 LYS   B CD   1 
ATOM   6384 C  CE   . LYS   B 1 158 ? 46.412 -39.886 -14.198 1.00 28.49 ?  158 LYS   B CE   1 
ATOM   6385 N  NZ   . LYS   B 1 158 ? 45.329 -39.223 -14.979 1.00 28.53 ?  158 LYS   B NZ   1 
ATOM   6386 H  H    . LYS   B 1 158 ? 49.229 -37.596 -9.180  1.00 23.65 ?  158 LYS   B H    1 
ATOM   6387 H  HA   . LYS   B 1 158 ? 47.151 -37.417 -10.675 1.00 24.94 ?  158 LYS   B HA   1 
ATOM   6388 H  HB2  . LYS   B 1 158 ? 49.050 -38.166 -11.646 1.00 27.17 ?  158 LYS   B HB2  1 
ATOM   6389 H  HB3  . LYS   B 1 158 ? 49.165 -39.381 -10.636 1.00 27.17 ?  158 LYS   B HB3  1 
ATOM   6390 H  HG2  . LYS   B 1 158 ? 48.557 -40.196 -12.684 1.00 29.98 ?  158 LYS   B HG2  1 
ATOM   6391 H  HG3  . LYS   B 1 158 ? 47.319 -40.398 -11.716 1.00 29.98 ?  158 LYS   B HG3  1 
ATOM   6392 H  HD2  . LYS   B 1 158 ? 46.273 -38.547 -12.659 1.00 32.58 ?  158 LYS   B HD2  1 
ATOM   6393 H  HD3  . LYS   B 1 158 ? 47.540 -38.294 -13.589 1.00 32.58 ?  158 LYS   B HD3  1 
ATOM   6394 H  HE2  . LYS   B 1 158 ? 47.109 -40.149 -14.817 1.00 34.30 ?  158 LYS   B HE2  1 
ATOM   6395 H  HE3  . LYS   B 1 158 ? 46.036 -40.669 -13.766 1.00 34.30 ?  158 LYS   B HE3  1 
ATOM   6396 H  HZ1  . LYS   B 1 158 ? 45.003 -39.785 -15.587 1.00 34.36 ?  158 LYS   B HZ1  1 
ATOM   6397 H  HZ2  . LYS   B 1 158 ? 44.670 -38.972 -14.435 1.00 34.36 ?  158 LYS   B HZ2  1 
ATOM   6398 H  HZ3  . LYS   B 1 158 ? 45.650 -38.503 -15.393 1.00 34.36 ?  158 LYS   B HZ3  1 
ATOM   6399 N  N    . ASN   B 1 159 ? 46.850 -39.838 -8.596  1.00 20.64 ?  159 ASN   B N    1 
ATOM   6400 C  CA   . ASN   B 1 159 ? 45.889 -40.814 -8.088  1.00 21.12 ?  159 ASN   B CA   1 
ATOM   6401 C  C    . ASN   B 1 159 ? 44.699 -40.138 -7.405  1.00 20.07 ?  159 ASN   B C    1 
ATOM   6402 O  O    . ASN   B 1 159 ? 43.567 -40.633 -7.500  1.00 20.48 ?  159 ASN   B O    1 
ATOM   6403 C  CB   . ASN   B 1 159 ? 46.593 -41.798 -7.157  1.00 22.92 ?  159 ASN   B CB   1 
ATOM   6404 C  CG   . ASN   B 1 159 ? 47.626 -42.643 -7.881  1.00 25.23 ?  159 ASN   B CG   1 
ATOM   6405 O  OD1  . ASN   B 1 159 ? 47.383 -43.139 -8.991  1.00 25.79 ?  159 ASN   B OD1  1 
ATOM   6406 N  ND2  . ASN   B 1 159 ? 48.786 -42.819 -7.254  1.00 25.94 ?  159 ASN   B ND2  1 
ATOM   6407 H  H    . ASN   B 1 159 ? 47.595 -39.798 -8.174  1.00 24.88 ?  159 ASN   B H    1 
ATOM   6408 H  HA   . ASN   B 1 159 ? 45.549 -41.318 -8.844  1.00 25.46 ?  159 ASN   B HA   1 
ATOM   6409 H  HB2  . ASN   B 1 159 ? 47.045 -41.307 -6.456  1.00 27.62 ?  159 ASN   B HB2  1 
ATOM   6410 H  HB3  . ASN   B 1 159 ? 45.935 -42.398 -6.781  1.00 27.62 ?  159 ASN   B HB3  1 
ATOM   6411 H  HD21 . ASN   B 1 159 ? 49.409 -43.290 -7.622  1.00 31.25 ?  159 ASN   B HD21 1 
ATOM   6412 H  HD22 . ASN   B 1 159 ? 48.916 -42.477 -6.476  1.00 31.25 ?  159 ASN   B HD22 1 
ATOM   6413 N  N    . LEU   B 1 160 ? 44.920 -39.010 -6.723  1.00 19.08 ?  160 LEU   B N    1 
ATOM   6414 C  CA   . LEU   B 1 160 ? 43.787 -38.267 -6.185  1.00 18.23 ?  160 LEU   B CA   1 
ATOM   6415 C  C    . LEU   B 1 160 ? 43.000 -37.600 -7.304  1.00 17.59 ?  160 LEU   B C    1 
ATOM   6416 O  O    . LEU   B 1 160 ? 41.763 -37.600 -7.288  1.00 17.36 ?  160 LEU   B O    1 
ATOM   6417 C  CB   . LEU   B 1 160 ? 44.252 -37.237 -5.157  1.00 17.86 ?  160 LEU   B CB   1 
ATOM   6418 C  CG   . LEU   B 1 160 ? 43.127 -36.336 -4.632  1.00 17.36 ?  160 LEU   B CG   1 
ATOM   6419 C  CD1  . LEU   B 1 160 ? 42.006 -37.172 -4.024  1.00 18.44 ?  160 LEU   B CD1  1 
ATOM   6420 C  CD2  . LEU   B 1 160 ? 43.665 -35.343 -3.618  1.00 17.36 ?  160 LEU   B CD2  1 
ATOM   6421 H  H    . LEU   B 1 160 ? 45.696 -38.667 -6.564  1.00 23.01 ?  160 LEU   B H    1 
ATOM   6422 H  HA   . LEU   B 1 160 ? 43.196 -38.891 -5.741  1.00 21.99 ?  160 LEU   B HA   1 
ATOM   6423 H  HB2  . LEU   B 1 160 ? 44.637 -37.710 -4.400  1.00 21.54 ?  160 LEU   B HB2  1 
ATOM   6424 H  HB3  . LEU   B 1 160 ? 44.924 -36.670 -5.565  1.00 21.54 ?  160 LEU   B HB3  1 
ATOM   6425 H  HG   . LEU   B 1 160 ? 42.754 -35.835 -5.372  1.00 20.95 ?  160 LEU   B HG   1 
ATOM   6426 H  HD11 . LEU   B 1 160 ? 41.384 -36.584 -3.574  1.00 22.24 ?  160 LEU   B HD11 1 
ATOM   6427 H  HD12 . LEU   B 1 160 ? 41.548 -37.660 -4.729  1.00 22.24 ?  160 LEU   B HD12 1 
ATOM   6428 H  HD13 . LEU   B 1 160 ? 42.388 -37.801 -3.387  1.00 22.24 ?  160 LEU   B HD13 1 
ATOM   6429 H  HD21 . LEU   B 1 160 ? 42.939 -34.772 -3.326  1.00 20.94 ?  160 LEU   B HD21 1 
ATOM   6430 H  HD22 . LEU   B 1 160 ? 44.031 -35.830 -2.864  1.00 20.94 ?  160 LEU   B HD22 1 
ATOM   6431 H  HD23 . LEU   B 1 160 ? 44.359 -34.812 -4.039  1.00 20.94 ?  160 LEU   B HD23 1 
ATOM   6432 N  N    . TYR   B 1 161 ? 43.702 -37.037 -8.292  1.00 17.73 ?  161 TYR   B N    1 
ATOM   6433 C  CA   . TYR   B 1 161 ? 43.027 -36.471 -9.456  1.00 17.46 ?  161 TYR   B CA   1 
ATOM   6434 C  C    . TYR   B 1 161 ? 42.078 -37.491 -10.075 1.00 17.45 ?  161 TYR   B C    1 
ATOM   6435 O  O    . TYR   B 1 161 ? 40.905 -37.194 -10.327 1.00 17.50 ?  161 TYR   B O    1 
ATOM   6436 C  CB   . TYR   B 1 161 ? 44.061 -35.989 -10.480 1.00 17.87 ?  161 TYR   B CB   1 
ATOM   6437 C  CG   . TYR   B 1 161 ? 43.478 -35.521 -11.794 1.00 18.39 ?  161 TYR   B CG   1 
ATOM   6438 C  CD1  . TYR   B 1 161 ? 43.078 -34.200 -11.965 1.00 18.55 ?  161 TYR   B CD1  1 
ATOM   6439 C  CD2  . TYR   B 1 161 ? 43.321 -36.397 -12.865 1.00 19.19 ?  161 TYR   B CD2  1 
ATOM   6440 C  CE1  . TYR   B 1 161 ? 42.546 -33.764 -13.155 1.00 19.70 ?  161 TYR   B CE1  1 
ATOM   6441 C  CE2  . TYR   B 1 161 ? 42.781 -35.968 -14.061 1.00 20.05 ?  161 TYR   B CE2  1 
ATOM   6442 C  CZ   . TYR   B 1 161 ? 42.397 -34.650 -14.199 1.00 20.31 ?  161 TYR   B CZ   1 
ATOM   6443 O  OH   . TYR   B 1 161 ? 41.858 -34.213 -15.385 1.00 22.58 ?  161 TYR   B OH   1 
ATOM   6444 H  H    . TYR   B 1 161 ? 44.557 -36.983 -8.321  1.00 21.39 ?  161 TYR   B H    1 
ATOM   6445 H  HA   . TYR   B 1 161 ? 42.499 -35.708 -9.179  1.00 21.06 ?  161 TYR   B HA   1 
ATOM   6446 H  HB2  . TYR   B 1 161 ? 44.549 -35.242 -10.097 1.00 21.56 ?  161 TYR   B HB2  1 
ATOM   6447 H  HB3  . TYR   B 1 161 ? 44.672 -36.714 -10.674 1.00 21.56 ?  161 TYR   B HB3  1 
ATOM   6448 H  HD1  . TYR   B 1 161 ? 43.174 -33.593 -11.266 1.00 22.38 ?  161 TYR   B HD1  1 
ATOM   6449 H  HD2  . TYR   B 1 161 ? 43.574 -37.287 -12.775 1.00 23.15 ?  161 TYR   B HD2  1 
ATOM   6450 H  HE1  . TYR   B 1 161 ? 42.283 -32.873 -13.253 1.00 23.76 ?  161 TYR   B HE1  1 
ATOM   6451 H  HE2  . TYR   B 1 161 ? 42.678 -36.563 -14.771 1.00 24.17 ?  161 TYR   B HE2  1 
ATOM   6452 H  HH   . TYR   B 1 161 ? 41.824 -34.844 -15.939 1.00 27.21 ?  161 TYR   B HH   1 
ATOM   6453 N  N    . ASP   B 1 162 ? 42.569 -38.713 -10.306 1.00 17.95 ?  162 ASP   B N    1 
ATOM   6454 C  CA   . ASP   B 1 162 ? 41.740 -39.745 -10.920 1.00 18.20 ?  162 ASP   B CA   1 
ATOM   6455 C  C    . ASP   B 1 162 ? 40.535 -40.084 -10.049 1.00 17.74 ?  162 ASP   B C    1 
ATOM   6456 O  O    . ASP   B 1 162 ? 39.429 -40.297 -10.561 1.00 18.28 ?  162 ASP   B O    1 
ATOM   6457 C  CB   . ASP   B 1 162 ? 42.567 -41.007 -11.175 1.00 19.78 ?  162 ASP   B CB   1 
ATOM   6458 C  CG   . ASP   B 1 162 ? 43.578 -40.842 -12.294 1.00 21.31 ?  162 ASP   B CG   1 
ATOM   6459 O  OD1  . ASP   B 1 162 ? 43.461 -39.901 -13.098 1.00 21.54 ?  162 ASP   B OD1  1 
ATOM   6460 O  OD2  . ASP   B 1 162 ? 44.485 -41.694 -12.386 1.00 22.95 -1 162 ASP   B OD2  1 
ATOM   6461 H  H    . ASP   B 1 162 ? 43.371 -38.959 -10.124 1.00 21.66 ?  162 ASP   B H    1 
ATOM   6462 H  HA   . ASP   B 1 162 ? 41.412 -39.426 -11.774 1.00 21.95 ?  162 ASP   B HA   1 
ATOM   6463 H  HB2  . ASP   B 1 162 ? 43.065 -41.232 -10.375 1.00 23.85 ?  162 ASP   B HB2  1 
ATOM   6464 H  HB3  . ASP   B 1 162 ? 41.976 -41.734 -11.419 1.00 23.85 ?  162 ASP   B HB3  1 
ATOM   6465 N  N    A LYS   B 1 163 ? 40.729 -40.156 -8.731  0.64 16.88 ?  163 LYS   B N    1 
ATOM   6466 N  N    B LYS   B 1 163 ? 40.728 -40.147 -8.729  0.36 17.50 ?  163 LYS   B N    1 
ATOM   6467 C  CA   A LYS   B 1 163 ? 39.603 -40.431 -7.844  0.64 17.50 ?  163 LYS   B CA   1 
ATOM   6468 C  CA   B LYS   B 1 163 ? 39.606 -40.429 -7.838  0.36 17.91 ?  163 LYS   B CA   1 
ATOM   6469 C  C    A LYS   B 1 163 ? 38.565 -39.316 -7.908  0.64 16.44 ?  163 LYS   B C    1 
ATOM   6470 C  C    B LYS   B 1 163 ? 38.568 -39.314 -7.889  0.36 16.65 ?  163 LYS   B C    1 
ATOM   6471 O  O    A LYS   B 1 163 ? 37.353 -39.580 -7.911  0.64 17.20 ?  163 LYS   B O    1 
ATOM   6472 O  O    B LYS   B 1 163 ? 37.358 -39.577 -7.865  0.36 16.91 ?  163 LYS   B O    1 
ATOM   6473 C  CB   A LYS   B 1 163 ? 40.088 -40.617 -6.408  0.64 20.14 ?  163 LYS   B CB   1 
ATOM   6474 C  CB   B LYS   B 1 163 ? 40.108 -40.619 -6.408  0.36 20.13 ?  163 LYS   B CB   1 
ATOM   6475 C  CG   A LYS   B 1 163 ? 39.014 -41.176 -5.495  0.64 24.28 ?  163 LYS   B CG   1 
ATOM   6476 C  CG   B LYS   B 1 163 ? 39.041 -41.126 -5.460  0.36 23.10 ?  163 LYS   B CG   1 
ATOM   6477 C  CD   A LYS   B 1 163 ? 39.420 -41.168 -4.033  0.64 27.56 ?  163 LYS   B CD   1 
ATOM   6478 C  CD   B LYS   B 1 163 ? 39.555 -41.267 -4.039  0.36 25.82 ?  163 LYS   B CD   1 
ATOM   6479 C  CE   A LYS   B 1 163 ? 38.353 -41.846 -3.184  0.64 29.38 ?  163 LYS   B CE   1 
ATOM   6480 C  CE   B LYS   B 1 163 ? 38.505 -41.926 -3.157  0.36 27.43 ?  163 LYS   B CE   1 
ATOM   6481 N  NZ   A LYS   B 1 163 ? 38.471 -41.508 -1.739  0.64 30.97 ?  163 LYS   B NZ   1 
ATOM   6482 N  NZ   B LYS   B 1 163 ? 38.761 -41.710 -1.707  0.36 28.03 ?  163 LYS   B NZ   1 
ATOM   6483 H  H    A LYS   B 1 163 ? 41.489 -40.053 -8.338  0.64 20.37 ?  163 LYS   B H    1 
ATOM   6484 H  H    B LYS   B 1 163 ? 41.485 -40.036 -8.336  0.36 21.12 ?  163 LYS   B H    1 
ATOM   6485 H  HA   A LYS   B 1 163 ? 39.178 -41.253 -8.128  0.64 21.12 ?  163 LYS   B HA   1 
ATOM   6486 H  HA   B LYS   B 1 163 ? 39.178 -41.251 -8.122  0.36 21.61 ?  163 LYS   B HA   1 
ATOM   6487 H  HB2  A LYS   B 1 163 ? 40.836 -41.237 -6.405  0.64 24.28 ?  163 LYS   B HB2  1 
ATOM   6488 H  HB2  B LYS   B 1 163 ? 40.833 -41.265 -6.414  0.36 24.28 ?  163 LYS   B HB2  1 
ATOM   6489 H  HB3  A LYS   B 1 163 ? 40.367 -39.760 -6.054  0.64 24.28 ?  163 LYS   B HB3  1 
ATOM   6490 H  HB3  B LYS   B 1 163 ? 40.427 -39.768 -6.071  0.36 24.28 ?  163 LYS   B HB3  1 
ATOM   6491 H  HG2  A LYS   B 1 163 ? 38.210 -40.642 -5.584  0.64 29.25 ?  163 LYS   B HG2  1 
ATOM   6492 H  HG2  B LYS   B 1 163 ? 38.298 -40.502 -5.450  0.36 27.83 ?  163 LYS   B HG2  1 
ATOM   6493 H  HG3  A LYS   B 1 163 ? 38.830 -42.096 -5.749  0.64 29.25 ?  163 LYS   B HG3  1 
ATOM   6494 H  HG3  B LYS   B 1 163 ? 38.738 -41.999 -5.758  0.36 27.83 ?  163 LYS   B HG3  1 
ATOM   6495 H  HD2  A LYS   B 1 163 ? 40.253 -41.656 -3.925  0.64 33.19 ?  163 LYS   B HD2  1 
ATOM   6496 H  HD2  B LYS   B 1 163 ? 40.352 -41.822 -4.036  0.36 31.10 ?  163 LYS   B HD2  1 
ATOM   6497 H  HD3  A LYS   B 1 163 ? 39.521 -40.253 -3.730  0.64 33.19 ?  163 LYS   B HD3  1 
ATOM   6498 H  HD3  B LYS   B 1 163 ? 39.753 -40.389 -3.678  0.36 31.10 ?  163 LYS   B HD3  1 
ATOM   6499 H  HE2  A LYS   B 1 163 ? 37.475 -41.573 -3.491  0.64 35.37 ?  163 LYS   B HE2  1 
ATOM   6500 H  HE2  B LYS   B 1 163 ? 37.634 -41.557 -3.371  0.36 33.03 ?  163 LYS   B HE2  1 
ATOM   6501 H  HE3  A LYS   B 1 163 ? 38.446 -42.806 -3.273  0.64 35.37 ?  163 LYS   B HE3  1 
ATOM   6502 H  HE3  B LYS   B 1 163 ? 38.509 -42.882 -3.325  0.36 33.03 ?  163 LYS   B HE3  1 
ATOM   6503 H  HZ1  A LYS   B 1 163 ? 37.832 -41.920 -1.278  0.64 37.28 ?  163 LYS   B HZ1  1 
ATOM   6504 H  HZ1  B LYS   B 1 163 ? 38.127 -42.108 -1.225  0.36 33.75 ?  163 LYS   B HZ1  1 
ATOM   6505 H  HZ2  A LYS   B 1 163 ? 39.264 -41.768 -1.432  0.64 37.28 ?  163 LYS   B HZ2  1 
ATOM   6506 H  HZ2  B LYS   B 1 163 ? 39.551 -42.050 -1.483  0.36 33.75 ?  163 LYS   B HZ2  1 
ATOM   6507 H  HZ3  A LYS   B 1 163 ? 38.390 -40.629 -1.625  0.64 37.28 ?  163 LYS   B HZ3  1 
ATOM   6508 H  HZ3  B LYS   B 1 163 ? 38.758 -40.839 -1.524  0.36 33.75 ?  163 LYS   B HZ3  1 
ATOM   6509 N  N    . LEU   B 1 164 ? 39.025 -38.062 -7.951  1.00 15.63 ?  164 LEU   B N    1 
ATOM   6510 C  CA   . LEU   B 1 164 ? 38.112 -36.926 -8.006  1.00 15.21 ?  164 LEU   B CA   1 
ATOM   6511 C  C    . LEU   B 1 164 ? 37.329 -36.909 -9.314  1.00 15.49 ?  164 LEU   B C    1 
ATOM   6512 O  O    . LEU   B 1 164 ? 36.104 -36.719 -9.314  1.00 16.61 ?  164 LEU   B O    1 
ATOM   6513 C  CB   . LEU   B 1 164 ? 38.911 -35.635 -7.839  1.00 14.58 ?  164 LEU   B CB   1 
ATOM   6514 C  CG   . LEU   B 1 164 ? 39.434 -35.351 -6.434  1.00 15.27 ?  164 LEU   B CG   1 
ATOM   6515 C  CD1  . LEU   B 1 164 ? 40.515 -34.280 -6.495  1.00 15.45 ?  164 LEU   B CD1  1 
ATOM   6516 C  CD2  . LEU   B 1 164 ? 38.316 -34.905 -5.510  1.00 16.85 ?  164 LEU   B CD2  1 
ATOM   6517 H  H    A LEU   B 1 164 ? 39.861 -37.844 -7.946  0.64 18.87 ?  164 LEU   B H    1 
ATOM   6518 H  H    B LEU   B 1 164 ? 39.862 -37.845 -7.963  0.36 18.87 ?  164 LEU   B H    1 
ATOM   6519 H  HA   . LEU   B 1 164 ? 37.482 -36.989 -7.280  1.00 18.37 ?  164 LEU   B HA   1 
ATOM   6520 H  HB2  . LEU   B 1 164 ? 39.682 -35.670 -8.431  1.00 17.61 ?  164 LEU   B HB2  1 
ATOM   6521 H  HB3  . LEU   B 1 164 ? 38.348 -34.890 -8.092  1.00 17.61 ?  164 LEU   B HB3  1 
ATOM   6522 H  HG   . LEU   B 1 164 ? 39.838 -36.150 -6.068  1.00 18.43 ?  164 LEU   B HG   1 
ATOM   6523 H  HD11 . LEU   B 1 164 ? 40.834 -34.092 -5.596  1.00 18.66 ?  164 LEU   B HD11 1 
ATOM   6524 H  HD12 . LEU   B 1 164 ? 41.252 -34.595 -7.044  1.00 18.66 ?  164 LEU   B HD12 1 
ATOM   6525 H  HD13 . LEU   B 1 164 ? 40.142 -33.469 -6.883  1.00 18.66 ?  164 LEU   B HD13 1 
ATOM   6526 H  HD21 . LEU   B 1 164 ? 38.687 -34.687 -4.641  1.00 20.33 ?  164 LEU   B HD21 1 
ATOM   6527 H  HD22 . LEU   B 1 164 ? 37.881 -34.126 -5.890  1.00 20.33 ?  164 LEU   B HD22 1 
ATOM   6528 H  HD23 . LEU   B 1 164 ? 37.678 -35.632 -5.425  1.00 20.33 ?  164 LEU   B HD23 1 
ATOM   6529 N  N    . VAL   B 1 165 ? 38.021 -37.081 -10.441 1.00 17.02 ?  165 VAL   B N    1 
ATOM   6530 C  CA   . VAL   B 1 165 ? 37.362 -37.026 -11.742 1.00 18.57 ?  165 VAL   B CA   1 
ATOM   6531 C  C    . VAL   B 1 165 ? 36.431 -38.221 -11.915 1.00 20.43 ?  165 VAL   B C    1 
ATOM   6532 O  O    . VAL   B 1 165 ? 35.264 -38.078 -12.303 1.00 21.76 ?  165 VAL   B O    1 
ATOM   6533 C  CB   . VAL   B 1 165 ? 38.407 -36.956 -12.872 1.00 19.33 ?  165 VAL   B CB   1 
ATOM   6534 C  CG1  . VAL   B 1 165 ? 37.740 -37.073 -14.222 1.00 20.55 ?  165 VAL   B CG1  1 
ATOM   6535 C  CG2  . VAL   B 1 165 ? 39.202 -35.662 -12.785 1.00 19.12 ?  165 VAL   B CG2  1 
ATOM   6536 H  H    . VAL   B 1 165 ? 38.874 -37.228 -10.481 1.00 20.55 ?  165 VAL   B H    1 
ATOM   6537 H  HA   . VAL   B 1 165 ? 36.828 -36.222 -11.790 1.00 22.40 ?  165 VAL   B HA   1 
ATOM   6538 H  HB   . VAL   B 1 165 ? 39.036 -37.690 -12.777 1.00 23.31 ?  165 VAL   B HB   1 
ATOM   6539 H  HG11 . VAL   B 1 165 ? 38.354 -36.777 -14.908 1.00 24.78 ?  165 VAL   B HG11 1 
ATOM   6540 H  HG12 . VAL   B 1 165 ? 37.508 -38.006 -14.373 1.00 24.78 ?  165 VAL   B HG12 1 
ATOM   6541 H  HG13 . VAL   B 1 165 ? 36.941 -36.529 -14.228 1.00 24.78 ?  165 VAL   B HG13 1 
ATOM   6542 H  HG21 . VAL   B 1 165 ? 39.836 -35.625 -13.521 1.00 23.06 ?  165 VAL   B HG21 1 
ATOM   6543 H  HG22 . VAL   B 1 165 ? 38.591 -34.909 -12.842 1.00 23.06 ?  165 VAL   B HG22 1 
ATOM   6544 H  HG23 . VAL   B 1 165 ? 39.680 -35.634 -11.941 1.00 23.06 ?  165 VAL   B HG23 1 
ATOM   6545 N  N    . SER   B 1 166 ? 36.941 -39.424 -11.628 1.00 21.04 ?  166 SER   B N    1 
ATOM   6546 C  CA   . SER   B 1 166 ? 36.189 -40.637 -11.918 1.00 22.05 ?  166 SER   B CA   1 
ATOM   6547 C  C    . SER   B 1 166 ? 34.930 -40.727 -11.072 1.00 22.30 ?  166 SER   B C    1 
ATOM   6548 O  O    . SER   B 1 166 ? 33.965 -41.361 -11.491 1.00 23.63 ?  166 SER   B O    1 
ATOM   6549 C  CB   . SER   B 1 166 ? 37.056 -41.888 -11.735 1.00 23.08 ?  166 SER   B CB   1 
ATOM   6550 O  OG   . SER   B 1 166 ? 37.403 -42.100 -10.376 1.00 23.30 ?  166 SER   B OG   1 
ATOM   6551 H  H    . SER   B 1 166 ? 37.716 -39.560 -11.271 1.00 25.36 ?  166 SER   B H    1 
ATOM   6552 H  HA   . SER   B 1 166 ? 35.915 -40.613 -12.848 1.00 26.58 ?  166 SER   B HA   1 
ATOM   6553 H  HB2  . SER   B 1 166 ? 36.562 -42.660 -12.055 1.00 27.81 ?  166 SER   B HB2  1 
ATOM   6554 H  HB3  . SER   B 1 166 ? 37.870 -41.784 -12.253 1.00 27.81 ?  166 SER   B HB3  1 
ATOM   6555 H  HG   . SER   B 1 166 ? 37.834 -41.440 -10.087 1.00 28.08 ?  166 SER   B HG   1 
ATOM   6556 N  N    . SER   B 1 167 ? 34.910 -40.110 -9.894  1.00 20.77 ?  167 SER   B N    1 
ATOM   6557 C  CA   . SER   B 1 167 ? 33.759 -40.168 -9.001  1.00 20.29 ?  167 SER   B CA   1 
ATOM   6558 C  C    . SER   B 1 167 ? 32.844 -38.945 -9.092  1.00 19.82 ?  167 SER   B C    1 
ATOM   6559 O  O    . SER   B 1 167 ? 31.769 -38.948 -8.483  1.00 20.31 ?  167 SER   B O    1 
ATOM   6560 C  CB   . SER   B 1 167 ? 34.221 -40.357 -7.550  1.00 20.25 ?  167 SER   B CB   1 
ATOM   6561 O  OG   . SER   B 1 167 ? 34.886 -39.194 -7.077  1.00 20.03 ?  167 SER   B OG   1 
ATOM   6562 H  H    . SER   B 1 167 ? 35.561 -39.649 -9.589  1.00 25.04 ?  167 SER   B H    1 
ATOM   6563 H  HA   . SER   B 1 167 ? 33.228 -40.947 -9.235  1.00 24.46 ?  167 SER   B HA   1 
ATOM   6564 H  HB2  . SER   B 1 167 ? 33.448 -40.534 -6.991  1.00 24.41 ?  167 SER   B HB2  1 
ATOM   6565 H  HB3  . SER   B 1 167 ? 34.832 -41.118 -7.511  1.00 24.41 ?  167 SER   B HB3  1 
ATOM   6566 H  HG   . SER   B 1 167 ? 35.565 -39.046 -7.549  1.00 24.16 ?  167 SER   B HG   1 
ATOM   6567 N  N    . PHE   B 1 168 ? 33.224 -37.906 -9.838  1.00 19.46 ?  168 PHE   B N    1 
ATOM   6568 C  CA   . PHE   B 1 168 ? 32.384 -36.709 -9.905  1.00 18.58 ?  168 PHE   B CA   1 
ATOM   6569 C  C    . PHE   B 1 168 ? 31.079 -36.971 -10.651 1.00 16.32 ?  168 PHE   B C    1 
ATOM   6570 O  O    . PHE   B 1 168 ? 30.031 -36.382 -10.315 1.00 17.00 ?  168 PHE   B O    1 
ATOM   6571 C  CB   . PHE   B 1 168 ? 33.150 -35.566 -10.567 1.00 19.35 ?  168 PHE   B CB   1 
ATOM   6572 C  CG   . PHE   B 1 168 ? 32.341 -34.316 -10.712 1.00 19.38 ?  168 PHE   B CG   1 
ATOM   6573 C  CD1  . PHE   B 1 168 ? 31.993 -33.575 -9.593  1.00 20.58 ?  168 PHE   B CD1  1 
ATOM   6574 C  CD2  . PHE   B 1 168 ? 31.903 -33.894 -11.953 1.00 18.79 ?  168 PHE   B CD2  1 
ATOM   6575 C  CE1  . PHE   B 1 168 ? 31.228 -32.431 -9.705  1.00 20.71 ?  168 PHE   B CE1  1 
ATOM   6576 C  CE2  . PHE   B 1 168 ? 31.150 -32.733 -12.080 1.00 19.95 ?  168 PHE   B CE2  1 
ATOM   6577 C  CZ   . PHE   B 1 168 ? 30.806 -32.001 -10.951 1.00 20.16 ?  168 PHE   B CZ   1 
ATOM   6578 H  H    . PHE   B 1 168 ? 33.945 -37.868 -10.298 1.00 23.47 ?  168 PHE   B H    1 
ATOM   6579 H  HA   . PHE   B 1 168 ? 32.152 -36.437 -9.006  1.00 22.41 ?  168 PHE   B HA   1 
ATOM   6580 H  HB2  . PHE   B 1 168 ? 33.924 -35.357 -10.026 1.00 23.33 ?  168 PHE   B HB2  1 
ATOM   6581 H  HB3  . PHE   B 1 168 ? 33.425 -35.843 -11.453 1.00 23.33 ?  168 PHE   B HB3  1 
ATOM   6582 H  HD1  . PHE   B 1 168 ? 32.269 -33.865 -8.753  1.00 24.81 ?  168 PHE   B HD1  1 
ATOM   6583 H  HD2  . PHE   B 1 168 ? 32.132 -34.375 -12.711 1.00 22.67 ?  168 PHE   B HD2  1 
ATOM   6584 H  HE1  . PHE   B 1 168 ? 31.003 -31.947 -8.946  1.00 24.97 ?  168 PHE   B HE1  1 
ATOM   6585 H  HE2  . PHE   B 1 168 ? 30.862 -32.451 -12.921 1.00 24.06 ?  168 PHE   B HE2  1 
ATOM   6586 H  HZ   . PHE   B 1 168 ? 30.293 -31.230 -11.033 1.00 24.31 ?  168 PHE   B HZ   1 
ATOM   6587 N  N    . LEU   B 1 169 ? 31.122 -37.844 -11.657 1.00 16.67 ?  169 LEU   B N    1 
ATOM   6588 C  CA   . LEU   B 1 169 ? 29.951 -38.161 -12.463 1.00 18.64 ?  169 LEU   B CA   1 
ATOM   6589 C  C    . LEU   B 1 169 ? 29.937 -39.602 -12.949 1.00 21.44 ?  169 LEU   B C    1 
ATOM   6590 O  O    . LEU   B 1 169 ? 29.030 -40.018 -13.674 1.00 23.77 ?  169 LEU   B O    1 
ATOM   6591 C  CB   . LEU   B 1 169 ? 29.881 -37.233 -13.674 1.00 20.45 ?  169 LEU   B CB   1 
ATOM   6592 C  CG   . LEU   B 1 169 ? 28.621 -36.379 -13.787 1.00 23.12 ?  169 LEU   B CG   1 
ATOM   6593 C  CD1  . LEU   B 1 169 ? 28.558 -35.758 -15.165 1.00 24.11 ?  169 LEU   B CD1  1 
ATOM   6594 C  CD2  . LEU   B 1 169 ? 27.366 -37.188 -13.505 1.00 22.89 ?  169 LEU   B CD2  1 
ATOM   6595 O  OXT  . LEU   B 1 169 ? 30.838 -40.370 -12.638 1.00 22.52 -1 169 LEU   B OXT  1 
ATOM   6596 H  H    . LEU   B 1 169 ? 31.833 -38.266 -11.905 1.00 20.12 ?  169 LEU   B H    1 
ATOM   6597 H  HA   . LEU   B 1 169 ? 29.167 -38.017 -11.920 1.00 22.48 ?  169 LEU   B HA   1 
ATOM   6598 H  HB2  . LEU   B 1 169 ? 30.636 -36.625 -13.646 1.00 24.66 ?  169 LEU   B HB2  1 
ATOM   6599 H  HB3  . LEU   B 1 169 ? 29.931 -37.769 -14.482 1.00 24.66 ?  169 LEU   B HB3  1 
ATOM   6600 H  HG   . LEU   B 1 169 ? 28.664 -35.657 -13.138 1.00 27.86 ?  169 LEU   B HG   1 
ATOM   6601 H  HD11 . LEU   B 1 169 ? 27.773 -35.191 -15.219 1.00 29.04 ?  169 LEU   B HD11 1 
ATOM   6602 H  HD12 . LEU   B 1 169 ? 29.359 -35.232 -15.307 1.00 29.04 ?  169 LEU   B HD12 1 
ATOM   6603 H  HD13 . LEU   B 1 169 ? 28.502 -36.467 -15.823 1.00 29.04 ?  169 LEU   B HD13 1 
ATOM   6604 H  HD21 . LEU   B 1 169 ? 26.612 -36.774 -13.948 1.00 27.58 ?  169 LEU   B HD21 1 
ATOM   6605 H  HD22 . LEU   B 1 169 ? 27.493 -38.091 -13.843 1.00 27.58 ?  169 LEU   B HD22 1 
ATOM   6606 H  HD23 . LEU   B 1 169 ? 27.217 -37.214 -12.548 1.00 27.58 ?  169 LEU   B HD23 1 
HETATM 6607 C  C1   T TFA   C 2 .   ? 12.134 -1.267  1.438   0.30 11.35 ?  201 TFA   A C1   1 
HETATM 6608 C  C2   T TFA   C 2 .   ? 12.738 -1.716  0.085   0.30 13.34 ?  201 TFA   A C2   1 
HETATM 6609 O  O    T TFA   C 2 .   ? 12.851 -1.540  2.408   0.30 9.77  ?  201 TFA   A O    1 
HETATM 6610 F  F1   T TFA   C 2 .   ? 12.774 -3.061  0.043   0.30 14.75 ?  201 TFA   A F1   1 
HETATM 6611 F  F2   T TFA   C 2 .   ? 12.025 -1.334  -0.985  0.30 13.92 ?  201 TFA   A F2   1 
HETATM 6612 F  F3   T TFA   C 2 .   ? 13.973 -1.244  -0.108  0.30 14.34 ?  201 TFA   A F3   1 
HETATM 6613 O  OXT  T TFA   C 2 .   ? 11.039 -0.708  1.366   0.30 11.69 ?  201 TFA   A OXT  1 
HETATM 6614 N  N2   B A1A81 D 3 .   ? 14.861 -0.202  3.969   0.36 16.26 ?  202 A1A81 A N2   1 
HETATM 6615 C  C3   B A1A81 D 3 .   ? 13.626 -0.137  -0.230  0.36 22.37 ?  202 A1A81 A C3   1 
HETATM 6616 C  C6   B A1A81 D 3 .   ? 10.544 0.717   -0.526  0.36 23.70 ?  202 A1A81 A C6   1 
HETATM 6617 C  C9   B A1A81 D 3 .   ? 14.911 -0.089  5.341   0.36 15.58 ?  202 A1A81 A C9   1 
HETATM 6618 C  C12  B A1A81 D 3 .   ? 15.704 3.539   3.502   0.36 13.91 ?  202 A1A81 A C12  1 
HETATM 6619 C  C1   B A1A81 D 3 .   ? 15.617 -1.481  0.626   0.36 22.39 ?  202 A1A81 A C1   1 
HETATM 6620 C  C10  B A1A81 D 3 .   ? 15.403 2.099   5.253   0.36 14.10 ?  202 A1A81 A C10  1 
HETATM 6621 C  C11  B A1A81 D 3 .   ? 15.387 2.152   3.810   0.36 14.79 ?  202 A1A81 A C11  1 
HETATM 6622 C  C13  B A1A81 D 3 .   ? 15.873 4.232   4.695   0.36 13.55 ?  202 A1A81 A C13  1 
HETATM 6623 C  C2   B A1A81 D 3 .   ? 14.466 -0.491  1.065   0.36 21.21 ?  202 A1A81 A C2   1 
HETATM 6624 C  C4   B A1A81 D 3 .   ? 12.649 1.056   -0.033  0.36 23.25 ?  202 A1A81 A C4   1 
HETATM 6625 C  C5   B A1A81 D 3 .   ? 11.374 0.762   0.794   0.36 23.58 ?  202 A1A81 A C5   1 
HETATM 6626 C  C7   B A1A81 D 3 .   ? 11.743 1.400   -1.244  0.36 23.61 ?  202 A1A81 A C7   1 
HETATM 6627 C  C8   B A1A81 D 3 .   ? 15.089 0.893   3.169   0.36 16.60 ?  202 A1A81 A C8   1 
HETATM 6628 N  N1   B A1A81 D 3 .   ? 15.025 0.710   1.769   0.36 19.00 ?  202 A1A81 A N1   1 
HETATM 6629 N  N3   B A1A81 D 3 .   ? 15.170 1.018   6.042   0.36 14.84 ?  202 A1A81 A N3   1 
HETATM 6630 N  N4   B A1A81 D 3 .   ? 15.697 3.339   5.707   0.36 13.20 ?  202 A1A81 A N4   1 
HETATM 6631 O  O1   B A1A81 D 3 .   ? 16.515 -0.770  -0.192  0.36 23.13 ?  202 A1A81 A O1   1 
HETATM 6632 H  H6   B A1A81 D 3 .   ? 14.278 0.069   -1.087  0.36 26.96 ?  202 A1A81 A H6   1 
HETATM 6633 H  H5   B A1A81 D 3 .   ? 13.059 -1.018  -0.609  0.36 26.96 ?  202 A1A81 A H5   1 
HETATM 6634 H  H10  B A1A81 D 3 .   ? 10.244 -0.285  -0.907  0.36 28.56 ?  202 A1A81 A H10  1 
HETATM 6635 H  H11  B A1A81 D 3 .   ? 9.595  1.282   -0.533  0.36 28.56 ?  202 A1A81 A H11  1 
HETATM 6636 H  H15  B A1A81 D 3 .   ? 14.712 -0.985  5.972   0.36 18.81 ?  202 A1A81 A H15  1 
HETATM 6637 H  H16  B A1A81 D 3 .   ? 15.788 4.014   2.551   0.36 16.80 ?  202 A1A81 A H16  1 
HETATM 6638 H  H4   B A1A81 D 3 .   ? 16.143 -1.891  1.512   0.36 26.98 ?  202 A1A81 A H4   1 
HETATM 6639 H  H3   B A1A81 D 3 .   ? 15.197 -2.363  0.081   0.36 26.98 ?  202 A1A81 A H3   1 
HETATM 6640 H  H17  B A1A81 D 3 .   ? 16.115 5.241   4.989   0.36 16.38 ?  202 A1A81 A H17  1 
HETATM 6641 H  H1   B A1A81 D 3 .   ? 13.754 -1.008  1.743   0.36 25.56 ?  202 A1A81 A H1   1 
HETATM 6642 H  H7   B A1A81 D 3 .   ? 13.128 1.988   0.342   0.36 28.02 ?  202 A1A81 A H7   1 
HETATM 6643 H  H8   B A1A81 D 3 .   ? 11.445 -0.171  1.389   0.36 28.41 ?  202 A1A81 A H8   1 
HETATM 6644 H  H9   B A1A81 D 3 .   ? 11.172 1.556   1.526   0.36 28.41 ?  202 A1A81 A H9   1 
HETATM 6645 H  H13  B A1A81 D 3 .   ? 11.703 2.483   -1.435  0.36 28.45 ?  202 A1A81 A H13  1 
HETATM 6646 H  H12  B A1A81 D 3 .   ? 12.075 0.947   -2.193  0.36 28.45 ?  202 A1A81 A H12  1 
HETATM 6647 H  H14  B A1A81 D 3 .   ? 15.375 1.444   1.159   0.36 22.92 ?  202 A1A81 A H14  1 
HETATM 6648 H  H18  B A1A81 D 3 .   ? 15.770 3.585   6.709   0.36 15.95 ?  202 A1A81 A H18  1 
HETATM 6649 H  H2   B A1A81 D 3 .   ? 17.298 -1.313  -0.365  0.36 27.87 ?  202 A1A81 A H2   1 
HETATM 6650 CL CL   B CL    E 4 .   ? 16.017 2.691   -1.132  0.36 19.86 ?  203 CL    A CL   1 
HETATM 6651 O  O    . HOH   F 5 .   ? 4.692  3.761   0.531   1.00 22.67 ?  301 HOH   A O    1 
HETATM 6652 O  O    . HOH   F 5 .   ? 14.726 -4.583  20.499  1.00 45.86 ?  302 HOH   A O    1 
HETATM 6653 O  O    . HOH   F 5 .   ? 17.052 -17.981 15.004  1.00 26.31 ?  303 HOH   A O    1 
HETATM 6654 O  O    . HOH   F 5 .   ? 14.649 -13.920 16.657  1.00 25.44 ?  304 HOH   A O    1 
HETATM 6655 O  O    . HOH   F 5 .   ? 6.833  -7.979  11.814  1.00 18.82 ?  305 HOH   A O    1 
HETATM 6656 O  O    . HOH   F 5 .   ? 11.940 0.351   14.714  1.00 33.38 ?  306 HOH   A O    1 
HETATM 6657 O  O    . HOH   F 5 .   ? 18.666 -2.357  -16.406 1.00 46.03 ?  307 HOH   A O    1 
HETATM 6658 O  O    . HOH   F 5 .   ? 34.307 -1.839  12.541  1.00 35.39 ?  308 HOH   A O    1 
HETATM 6659 O  O    . HOH   F 5 .   ? 8.878  -12.098 17.103  1.00 44.22 ?  309 HOH   A O    1 
HETATM 6660 O  O    . HOH   F 5 .   ? 7.636  -6.313  -6.613  1.00 40.22 ?  310 HOH   A O    1 
HETATM 6661 O  O    . HOH   F 5 .   ? 15.058 -12.221 18.623  1.00 40.20 ?  311 HOH   A O    1 
HETATM 6662 O  O    . HOH   F 5 .   ? 11.754 -10.809 -10.114 1.00 44.71 ?  312 HOH   A O    1 
HETATM 6663 O  O    . HOH   F 5 .   ? 13.881 -4.894  17.361  1.00 27.28 ?  313 HOH   A O    1 
HETATM 6664 O  O    . HOH   F 5 .   ? 28.960 0.479   -9.706  1.00 22.03 ?  314 HOH   A O    1 
HETATM 6665 O  O    . HOH   F 5 .   ? 28.123 -6.280  19.614  1.00 40.94 ?  315 HOH   A O    1 
HETATM 6666 O  O    . HOH   F 5 .   ? 14.984 4.002   17.636  1.00 40.13 ?  316 HOH   A O    1 
HETATM 6667 O  O    . HOH   F 5 .   ? 30.228 -13.346 -8.531  1.00 21.32 ?  317 HOH   A O    1 
HETATM 6668 O  O    . HOH   F 5 .   ? 42.456 10.574  5.119   1.00 19.91 ?  318 HOH   A O    1 
HETATM 6669 O  O    . HOH   F 5 .   ? 14.153 -4.508  -11.918 1.00 33.49 ?  319 HOH   A O    1 
HETATM 6670 O  O    . HOH   F 5 .   ? 9.154  -10.048 19.316  1.00 38.96 ?  320 HOH   A O    1 
HETATM 6671 O  O    . HOH   F 5 .   ? 19.887 -12.486 -8.938  1.00 25.57 ?  321 HOH   A O    1 
HETATM 6672 O  O    . HOH   F 5 .   ? 36.155 -5.074  -0.514  1.00 28.50 ?  322 HOH   A O    1 
HETATM 6673 O  O    . HOH   F 5 .   ? -0.640 -8.434  2.118   1.00 41.46 ?  323 HOH   A O    1 
HETATM 6674 O  O    . HOH   F 5 .   ? -0.461 -2.927  2.933   1.00 36.27 ?  324 HOH   A O    1 
HETATM 6675 O  O    A HOH   F 5 .   ? 14.629 -3.624  3.077   0.64 13.89 ?  325 HOH   A O    1 
HETATM 6676 O  O    . HOH   F 5 .   ? 38.273 10.154  7.145   1.00 41.92 ?  326 HOH   A O    1 
HETATM 6677 O  O    . HOH   F 5 .   ? 7.905  -12.527 -0.917  1.00 21.05 ?  327 HOH   A O    1 
HETATM 6678 O  O    . HOH   F 5 .   ? 0.656  -4.303  0.106   1.00 29.45 ?  328 HOH   A O    1 
HETATM 6679 O  O    . HOH   F 5 .   ? 26.472 -19.325 -1.767  1.00 14.50 ?  329 HOH   A O    1 
HETATM 6680 O  O    . HOH   F 5 .   ? 34.004 -1.043  -8.919  1.00 26.68 ?  330 HOH   A O    1 
HETATM 6681 O  O    . HOH   F 5 .   ? 13.581 -15.209 -7.526  1.00 25.42 ?  331 HOH   A O    1 
HETATM 6682 O  O    . HOH   F 5 .   ? 9.839  -21.368 5.671   1.00 19.28 ?  332 HOH   A O    1 
HETATM 6683 O  O    . HOH   F 5 .   ? 22.301 5.434   18.964  1.00 39.38 ?  333 HOH   A O    1 
HETATM 6684 O  O    A HOH   F 5 .   ? 3.583  -9.420  9.704   0.64 24.61 ?  334 HOH   A O    1 
HETATM 6685 O  O    . HOH   F 5 .   ? 22.709 12.505  1.620   1.00 15.16 ?  335 HOH   A O    1 
HETATM 6686 O  O    . HOH   F 5 .   ? 20.626 -19.724 -5.055  1.00 26.95 ?  336 HOH   A O    1 
HETATM 6687 O  O    . HOH   F 5 .   ? 31.012 -18.102 7.831   1.00 20.41 ?  337 HOH   A O    1 
HETATM 6688 O  O    . HOH   F 5 .   ? 27.350 13.793  2.842   1.00 30.17 ?  338 HOH   A O    1 
HETATM 6689 O  O    . HOH   F 5 .   ? 37.529 2.782   10.225  1.00 27.38 ?  339 HOH   A O    1 
HETATM 6690 O  O    . HOH   F 5 .   ? 44.338 7.123   6.423   1.00 26.53 ?  340 HOH   A O    1 
HETATM 6691 O  O    . HOH   F 5 .   ? 18.646 -19.378 13.551  1.00 35.74 ?  341 HOH   A O    1 
HETATM 6692 O  O    . HOH   F 5 .   ? 15.174 -21.497 14.224  1.00 18.89 ?  342 HOH   A O    1 
HETATM 6693 O  O    . HOH   F 5 .   ? 21.295 -2.303  -2.356  1.00 15.57 ?  343 HOH   A O    1 
HETATM 6694 O  O    . HOH   F 5 .   ? 39.767 -1.033  -5.160  1.00 22.10 ?  344 HOH   A O    1 
HETATM 6695 O  O    . HOH   F 5 .   ? 28.581 -10.676 -14.009 1.00 43.96 ?  345 HOH   A O    1 
HETATM 6696 O  O    B HOH   F 5 .   ? 12.012 -1.513  -3.735  0.36 19.54 ?  346 HOH   A O    1 
HETATM 6697 O  O    . HOH   F 5 .   ? 13.224 -1.444  -6.673  1.00 16.79 ?  347 HOH   A O    1 
HETATM 6698 O  O    . HOH   F 5 .   ? 42.592 4.304   5.477   1.00 32.25 ?  348 HOH   A O    1 
HETATM 6699 O  O    . HOH   F 5 .   ? 38.560 4.995   7.009   1.00 15.65 ?  349 HOH   A O    1 
HETATM 6700 O  O    . HOH   F 5 .   ? 18.853 -21.970 6.967   1.00 32.94 ?  350 HOH   A O    1 
HETATM 6701 O  O    . HOH   F 5 .   ? 35.756 -12.663 6.862   1.00 15.96 ?  351 HOH   A O    1 
HETATM 6702 O  O    . HOH   F 5 .   ? 26.864 11.444  1.628   1.00 16.80 ?  352 HOH   A O    1 
HETATM 6703 O  O    . HOH   F 5 .   ? 28.389 -0.144  -13.427 1.00 33.48 ?  353 HOH   A O    1 
HETATM 6704 O  O    A HOH   F 5 .   ? 14.269 0.606   6.775   0.64 17.19 ?  354 HOH   A O    1 
HETATM 6705 O  O    . HOH   F 5 .   ? 31.826 -9.335  -6.681  1.00 23.26 ?  355 HOH   A O    1 
HETATM 6706 O  O    . HOH   F 5 .   ? 14.346 -21.188 -4.279  1.00 28.73 ?  356 HOH   A O    1 
HETATM 6707 O  O    . HOH   F 5 .   ? 22.136 -19.274 11.398  1.00 36.01 ?  357 HOH   A O    1 
HETATM 6708 O  O    . HOH   F 5 .   ? 31.063 -13.944 -2.466  1.00 14.09 ?  358 HOH   A O    1 
HETATM 6709 O  O    . HOH   F 5 .   ? 24.039 -2.085  -2.100  1.00 10.64 ?  359 HOH   A O    1 
HETATM 6710 O  O    . HOH   F 5 .   ? 37.338 11.981  4.955   1.00 27.62 ?  360 HOH   A O    1 
HETATM 6711 O  O    . HOH   F 5 .   ? 43.976 8.451   -3.030  1.00 27.46 ?  361 HOH   A O    1 
HETATM 6712 O  O    . HOH   F 5 .   ? 31.675 8.225   14.888  1.00 25.08 ?  362 HOH   A O    1 
HETATM 6713 O  O    . HOH   F 5 .   ? 21.224 10.235  14.997  1.00 35.05 ?  363 HOH   A O    1 
HETATM 6714 O  O    . HOH   F 5 .   ? 17.136 -17.757 -5.068  1.00 27.40 ?  364 HOH   A O    1 
HETATM 6715 O  O    . HOH   F 5 .   ? 24.571 2.006   -7.013  1.00 19.24 ?  365 HOH   A O    1 
HETATM 6716 O  O    . HOH   F 5 .   ? 33.643 -7.151  4.334   1.00 16.55 ?  366 HOH   A O    1 
HETATM 6717 O  O    . HOH   F 5 .   ? 30.799 3.108   8.273   1.00 12.15 ?  367 HOH   A O    1 
HETATM 6718 O  O    . HOH   F 5 .   ? 25.693 -0.769  -7.358  1.00 15.81 ?  368 HOH   A O    1 
HETATM 6719 O  O    . HOH   F 5 .   ? 37.250 -2.820  9.710   1.00 41.68 ?  369 HOH   A O    1 
HETATM 6720 O  O    . HOH   F 5 .   ? 21.857 -21.898 8.461   1.00 29.90 ?  370 HOH   A O    1 
HETATM 6721 O  O    . HOH   F 5 .   ? 16.940 -19.224 4.869   1.00 15.85 ?  371 HOH   A O    1 
HETATM 6722 O  O    . HOH   F 5 .   ? 24.420 3.594   -1.811  1.00 15.26 ?  372 HOH   A O    1 
HETATM 6723 O  O    . HOH   F 5 .   ? 14.487 -24.670 11.606  1.00 39.10 ?  373 HOH   A O    1 
HETATM 6724 O  O    A HOH   F 5 .   ? 8.168  -21.362 3.979   0.64 32.91 ?  374 HOH   A O    1 
HETATM 6725 O  O    . HOH   F 5 .   ? 18.567 9.491   8.987   1.00 22.20 ?  375 HOH   A O    1 
HETATM 6726 O  O    B HOH   F 5 .   ? 14.874 -2.933  3.358   0.36 19.74 ?  376 HOH   A O    1 
HETATM 6727 O  O    . HOH   F 5 .   ? 33.507 -16.941 8.109   1.00 19.89 ?  377 HOH   A O    1 
HETATM 6728 O  O    . HOH   F 5 .   ? 27.438 -6.081  -14.014 1.00 37.36 ?  378 HOH   A O    1 
HETATM 6729 O  O    A HOH   F 5 .   ? 17.494 -1.688  0.422   0.64 17.51 ?  379 HOH   A O    1 
HETATM 6730 O  O    . HOH   F 5 .   ? 27.431 -10.599 14.081  1.00 18.19 ?  380 HOH   A O    1 
HETATM 6731 O  O    . HOH   F 5 .   ? 43.378 7.829   2.724   1.00 27.00 ?  381 HOH   A O    1 
HETATM 6732 O  O    B HOH   F 5 .   ? 10.969 2.255   11.983  0.36 22.92 ?  382 HOH   A O    1 
HETATM 6733 O  O    . HOH   F 5 .   ? 16.509 -22.058 0.957   1.00 27.66 ?  383 HOH   A O    1 
HETATM 6734 O  O    T HOH   F 5 .   ? 15.404 -0.393  2.364   0.30 12.30 ?  384 HOH   A O    1 
HETATM 6735 O  O    A HOH   F 5 .   ? 11.064 -0.348  1.907   0.34 20.05 ?  385 HOH   A O    1 
HETATM 6736 O  O    . HOH   F 5 .   ? 31.789 -7.301  -9.851  1.00 21.70 ?  386 HOH   A O    1 
HETATM 6737 O  O    . HOH   F 5 .   ? 6.398  -5.419  11.074  1.00 19.00 ?  387 HOH   A O    1 
HETATM 6738 O  O    . HOH   F 5 .   ? 24.149 -7.717  14.420  1.00 17.55 ?  388 HOH   A O    1 
HETATM 6739 O  O    . HOH   F 5 .   ? 24.632 -17.487 12.741  1.00 25.00 ?  389 HOH   A O    1 
HETATM 6740 O  O    . HOH   F 5 .   ? 21.759 -13.735 -8.197  1.00 39.51 ?  390 HOH   A O    1 
HETATM 6741 O  O    . HOH   F 5 .   ? 15.489 11.815  7.902   1.00 40.23 ?  391 HOH   A O    1 
HETATM 6742 O  O    . HOH   F 5 .   ? 22.586 -11.881 21.783  1.00 46.91 ?  392 HOH   A O    1 
HETATM 6743 O  O    B HOH   F 5 .   ? 8.160  4.187   1.355   0.36 26.71 ?  393 HOH   A O    1 
HETATM 6744 O  O    . HOH   F 5 .   ? 14.030 -23.038 7.426   1.00 18.66 ?  394 HOH   A O    1 
HETATM 6745 O  O    . HOH   F 5 .   ? 21.349 3.080   -0.287  1.00 13.31 ?  395 HOH   A O    1 
HETATM 6746 O  O    . HOH   F 5 .   ? 18.911 -0.720  -1.694  1.00 14.75 ?  396 HOH   A O    1 
HETATM 6747 O  O    . HOH   F 5 .   ? 37.532 -2.008  5.829   1.00 26.35 ?  397 HOH   A O    1 
HETATM 6748 O  O    . HOH   F 5 .   ? 14.536 -0.523  -12.194 1.00 22.21 ?  398 HOH   A O    1 
HETATM 6749 O  O    . HOH   F 5 .   ? 32.753 -9.247  5.961   1.00 19.79 ?  399 HOH   A O    1 
HETATM 6750 O  O    . HOH   F 5 .   ? 23.476 11.396  4.082   1.00 12.54 ?  400 HOH   A O    1 
HETATM 6751 O  O    . HOH   F 5 .   ? 27.321 2.354   18.739  1.00 29.84 ?  401 HOH   A O    1 
HETATM 6752 O  O    . HOH   F 5 .   ? 31.007 6.176   -12.277 1.00 27.50 ?  402 HOH   A O    1 
HETATM 6753 O  O    . HOH   F 5 .   ? 30.005 -10.063 13.018  1.00 22.11 ?  403 HOH   A O    1 
HETATM 6754 O  O    . HOH   F 5 .   ? 23.941 -15.693 -9.185  1.00 37.36 ?  404 HOH   A O    1 
HETATM 6755 O  O    . HOH   F 5 .   ? 30.692 1.906   16.705  1.00 21.38 ?  405 HOH   A O    1 
HETATM 6756 O  O    . HOH   F 5 .   ? 15.158 -8.067  -9.783  1.00 23.05 ?  406 HOH   A O    1 
HETATM 6757 O  O    . HOH   F 5 .   ? 20.541 -20.002 2.761   1.00 19.28 ?  407 HOH   A O    1 
HETATM 6758 O  O    . HOH   F 5 .   ? 6.687  -3.176  12.800  1.00 29.27 ?  408 HOH   A O    1 
HETATM 6759 O  O    . HOH   F 5 .   ? 16.194 16.656  8.563   1.00 35.68 ?  409 HOH   A O    1 
HETATM 6760 O  O    A HOH   F 5 .   ? 15.794 -0.915  5.248   0.64 18.16 ?  410 HOH   A O    1 
HETATM 6761 O  O    . HOH   F 5 .   ? 32.660 -4.215  -9.862  1.00 29.18 ?  411 HOH   A O    1 
HETATM 6762 O  O    . HOH   F 5 .   ? 30.283 -12.896 13.534  1.00 20.46 ?  412 HOH   A O    1 
HETATM 6763 O  O    . HOH   F 5 .   ? 44.893 -0.637  3.077   1.00 40.09 ?  413 HOH   A O    1 
HETATM 6764 O  O    . HOH   F 5 .   ? 40.901 -8.260  -6.768  1.00 36.26 ?  414 HOH   A O    1 
HETATM 6765 O  O    . HOH   F 5 .   ? 23.911 -20.258 -1.353  1.00 17.04 ?  415 HOH   A O    1 
HETATM 6766 O  O    . HOH   F 5 .   ? 5.354  2.841   4.981   1.00 35.26 ?  416 HOH   A O    1 
HETATM 6767 O  O    . HOH   F 5 .   ? 26.929 4.187   -0.667  1.00 12.82 ?  417 HOH   A O    1 
HETATM 6768 O  O    . HOH   F 5 .   ? 38.132 -1.333  -1.920  1.00 19.16 ?  418 HOH   A O    1 
HETATM 6769 O  O    . HOH   F 5 .   ? 15.863 2.119   24.710  1.00 41.42 ?  419 HOH   A O    1 
HETATM 6770 O  O    . HOH   F 5 .   ? 10.369 -13.707 -1.735  1.00 16.94 ?  420 HOH   A O    1 
HETATM 6771 O  O    A HOH   F 5 .   ? 11.024 1.592   12.723  0.64 19.89 ?  421 HOH   A O    1 
HETATM 6772 O  O    A HOH   F 5 .   ? 24.098 3.975   -4.934  0.64 17.57 ?  422 HOH   A O    1 
HETATM 6773 O  O    . HOH   F 5 .   ? 32.516 -10.634 3.211   1.00 31.87 ?  423 HOH   A O    1 
HETATM 6774 O  O    . HOH   F 5 .   ? 35.096 -5.228  -3.094  1.00 17.79 ?  424 HOH   A O    1 
HETATM 6775 O  O    . HOH   F 5 .   ? 41.622 1.536   5.026   1.00 37.62 ?  425 HOH   A O    1 
HETATM 6776 O  O    . HOH   F 5 .   ? 27.936 0.830   -7.163  1.00 14.18 ?  426 HOH   A O    1 
HETATM 6777 O  O    . HOH   F 5 .   ? 36.727 -4.941  5.398   1.00 23.69 ?  427 HOH   A O    1 
HETATM 6778 O  O    . HOH   F 5 .   ? 11.633 -10.675 16.952  1.00 25.11 ?  428 HOH   A O    1 
HETATM 6779 O  O    A HOH   F 5 .   ? 20.108 4.560   -7.568  0.64 16.42 ?  429 HOH   A O    1 
HETATM 6780 O  O    . HOH   F 5 .   ? 16.197 -14.181 20.129  1.00 50.05 ?  430 HOH   A O    1 
HETATM 6781 O  O    . HOH   F 5 .   ? 15.967 6.847   2.941   1.00 19.44 ?  431 HOH   A O    1 
HETATM 6782 O  O    . HOH   F 5 .   ? 22.604 8.199   18.372  1.00 47.65 ?  432 HOH   A O    1 
HETATM 6783 O  O    . HOH   F 5 .   ? 19.398 -11.013 23.999  1.00 67.69 ?  433 HOH   A O    1 
HETATM 6784 O  O    . HOH   F 5 .   ? 23.490 -7.983  17.087  1.00 22.01 ?  434 HOH   A O    1 
HETATM 6785 O  O    . HOH   F 5 .   ? 18.457 4.900   -15.155 1.00 48.38 ?  435 HOH   A O    1 
HETATM 6786 O  O    . HOH   F 5 .   ? 18.345 -15.973 16.330  1.00 37.57 ?  436 HOH   A O    1 
HETATM 6787 O  O    B HOH   F 5 .   ? 11.831 6.659   10.351  0.36 28.30 ?  437 HOH   A O    1 
HETATM 6788 O  O    A HOH   F 5 .   ? 16.261 2.973   -1.465  0.64 17.89 ?  438 HOH   A O    1 
HETATM 6789 O  O    . HOH   F 5 .   ? 23.324 -20.910 1.341   1.00 19.32 ?  439 HOH   A O    1 
HETATM 6790 O  O    . HOH   F 5 .   ? 23.178 7.590   -3.228  1.00 32.34 ?  440 HOH   A O    1 
HETATM 6791 O  O    . HOH   F 5 .   ? 10.363 -22.198 -1.208  1.00 50.20 ?  441 HOH   A O    1 
HETATM 6792 O  O    . HOH   F 5 .   ? 27.118 -3.136  19.359  1.00 37.32 ?  442 HOH   A O    1 
HETATM 6793 O  O    . HOH   F 5 .   ? 37.719 -8.814  -3.427  1.00 23.40 ?  443 HOH   A O    1 
HETATM 6794 O  O    . HOH   F 5 .   ? 21.239 -9.191  21.314  1.00 49.45 ?  444 HOH   A O    1 
HETATM 6795 O  O    . HOH   F 5 .   ? 34.404 -8.099  -0.569  1.00 27.91 ?  445 HOH   A O    1 
HETATM 6796 O  O    . HOH   F 5 .   ? 18.869 1.973   -0.708  1.00 13.71 ?  446 HOH   A O    1 
HETATM 6797 O  O    . HOH   F 5 .   ? 9.433  -16.237 -2.014  1.00 38.68 ?  447 HOH   A O    1 
HETATM 6798 O  O    A HOH   F 5 .   ? 14.023 -0.308  3.438   0.34 25.62 ?  448 HOH   A O    1 
HETATM 6799 O  O    . HOH   F 5 .   ? 31.309 -12.752 0.012   1.00 20.31 ?  449 HOH   A O    1 
HETATM 6800 O  O    . HOH   F 5 .   ? -1.524 -4.889  7.573   1.00 44.04 ?  450 HOH   A O    1 
HETATM 6801 O  O    . HOH   F 5 .   ? 30.602 14.772  2.736   1.00 18.93 ?  451 HOH   A O    1 
HETATM 6802 O  O    . HOH   F 5 .   ? 20.566 -17.725 24.827  1.00 50.72 ?  452 HOH   A O    1 
HETATM 6803 O  O    . HOH   F 5 .   ? 21.467 -14.696 17.916  1.00 52.88 ?  453 HOH   A O    1 
HETATM 6804 O  O    . HOH   F 5 .   ? 29.787 -1.940  -12.740 1.00 44.97 ?  454 HOH   A O    1 
HETATM 6805 O  O    . HOH   F 5 .   ? 29.831 -16.039 10.787  1.00 34.38 ?  455 HOH   A O    1 
HETATM 6806 O  O    . HOH   F 5 .   ? 32.432 -15.881 10.888  1.00 29.39 ?  456 HOH   A O    1 
HETATM 6807 O  O    . HOH   F 5 .   ? 27.762 6.985   -6.585  1.00 38.02 ?  457 HOH   A O    1 
HETATM 6808 O  O    . HOH   F 5 .   ? 25.402 8.242   -4.857  1.00 31.21 ?  458 HOH   A O    1 
HETATM 6809 O  O    . HOH   F 5 .   ? 24.846 5.687   20.749  1.00 52.91 ?  459 HOH   A O    1 
HETATM 6810 O  O    . HOH   F 5 .   ? 19.869 -17.338 -5.057  1.00 24.23 ?  460 HOH   A O    1 
HETATM 6811 O  O    . HOH   F 5 .   ? 23.151 -22.300 -3.352  1.00 36.03 ?  461 HOH   A O    1 
HETATM 6812 O  O    . HOH   F 5 .   ? 24.600 14.683  7.777   1.00 35.81 ?  462 HOH   A O    1 
HETATM 6813 O  O    . HOH   F 5 .   ? 15.707 -21.484 3.669   1.00 24.33 ?  463 HOH   A O    1 
HETATM 6814 O  O    . HOH   F 5 .   ? 18.764 10.892  11.292  1.00 32.05 ?  464 HOH   A O    1 
HETATM 6815 O  O    . HOH   F 5 .   ? 26.906 11.703  -1.391  1.00 33.51 ?  465 HOH   A O    1 
HETATM 6816 O  O    A HOH   F 5 .   ? 21.974 5.284   -5.857  0.64 27.64 ?  466 HOH   A O    1 
HETATM 6817 O  O    . HOH   F 5 .   ? 39.615 -7.014  -3.452  1.00 43.15 ?  467 HOH   A O    1 
HETATM 6818 O  O    . HOH   F 5 .   ? 27.459 -11.347 16.587  1.00 37.61 ?  468 HOH   A O    1 
HETATM 6819 O  O    . HOH   F 5 .   ? 11.973 -13.411 16.374  1.00 53.13 ?  469 HOH   A O    1 
HETATM 6820 O  O    . HOH   F 5 .   ? 12.296 1.651   17.295  1.00 40.54 ?  470 HOH   A O    1 
HETATM 6821 O  O    . HOH   F 5 .   ? 10.990 -15.020 -6.109  1.00 35.50 ?  471 HOH   A O    1 
HETATM 6822 O  O    . HOH   F 5 .   ? 23.461 13.738  5.512   1.00 18.54 ?  472 HOH   A O    1 
HETATM 6823 O  O    . HOH   F 5 .   ? 25.828 10.794  -3.802  1.00 26.18 ?  473 HOH   A O    1 
HETATM 6824 O  O    . HOH   F 5 .   ? 18.099 -16.190 -8.884  1.00 40.82 ?  474 HOH   A O    1 
HETATM 6825 O  O    . HOH   F 5 .   ? 15.701 -17.075 -7.013  1.00 30.16 ?  475 HOH   A O    1 
HETATM 6826 O  O    . HOH   F 5 .   ? 16.793 -20.490 16.107  1.00 29.42 ?  476 HOH   A O    1 
HETATM 6827 O  O    . HOH   F 5 .   ? 17.423 -18.685 19.818  1.00 52.42 ?  477 HOH   A O    1 
HETATM 6828 O  O    . HOH   F 5 .   ? 13.981 -10.294 -10.934 1.00 32.73 ?  478 HOH   A O    1 
HETATM 6829 O  O    . HOH   F 5 .   ? 28.852 9.072   17.509  1.00 37.70 ?  479 HOH   A O    1 
HETATM 6830 O  O    . HOH   F 5 .   ? 23.119 11.830  -4.076  1.00 18.94 ?  480 HOH   A O    1 
HETATM 6831 O  O    . HOH   F 5 .   ? 35.255 7.457   12.240  1.00 44.25 ?  481 HOH   A O    1 
HETATM 6832 O  O    . HOH   F 5 .   ? 30.831 0.720   19.144  1.00 41.24 ?  482 HOH   A O    1 
HETATM 6833 O  O    . HOH   F 5 .   ? 41.038 -3.977  -0.387  1.00 38.34 ?  483 HOH   A O    1 
HETATM 6834 O  O    . HOH   F 5 .   ? 28.607 -4.705  -12.305 1.00 36.23 ?  484 HOH   A O    1 
HETATM 6835 O  O    . HOH   F 5 .   ? 44.564 10.437  -1.600  1.00 31.26 ?  485 HOH   A O    1 
HETATM 6836 O  O    . HOH   F 5 .   ? 23.187 -12.825 19.320  1.00 43.97 ?  486 HOH   A O    1 
HETATM 6837 O  O    . HOH   F 5 .   ? 28.668 -7.950  -15.265 1.00 48.76 ?  487 HOH   A O    1 
HETATM 6838 O  O    . HOH   F 5 .   ? 41.771 9.375   -3.987  1.00 30.74 ?  488 HOH   A O    1 
HETATM 6839 O  O    . HOH   F 5 .   ? 39.180 2.431   7.454   1.00 32.18 ?  489 HOH   A O    1 
HETATM 6840 O  O    . HOH   F 5 .   ? 18.443 -23.149 1.878   1.00 42.79 ?  490 HOH   A O    1 
HETATM 6841 O  O    . HOH   F 5 .   ? 31.457 -0.558  -10.589 1.00 30.28 ?  491 HOH   A O    1 
HETATM 6842 O  O    . HOH   F 5 .   ? 13.926 -25.204 8.887   1.00 32.98 ?  492 HOH   A O    1 
HETATM 6843 O  O    . HOH   F 5 .   ? 8.085  -3.207  -5.804  1.00 44.06 ?  493 HOH   A O    1 
HETATM 6844 O  O    . HOH   F 5 .   ? 15.989 -6.845  -11.916 1.00 42.77 ?  494 HOH   A O    1 
HETATM 6845 O  O    . HOH   F 5 .   ? 40.556 -0.268  -7.823  1.00 35.42 ?  495 HOH   A O    1 
HETATM 6846 O  O    . HOH   F 5 .   ? 16.166 -23.376 5.776   1.00 27.57 ?  496 HOH   A O    1 
HETATM 6847 O  O    . HOH   F 5 .   ? 20.018 -22.330 4.189   1.00 28.00 ?  497 HOH   A O    1 
HETATM 6848 O  O    B HOH   F 5 .   ? 14.799 7.734   4.706   0.36 27.77 ?  498 HOH   A O    1 
HETATM 6849 O  O    . HOH   F 5 .   ? 20.491 -16.033 -7.403  1.00 28.60 ?  499 HOH   A O    1 
HETATM 6850 O  O    . HOH   F 5 .   ? 30.749 -5.831  -11.866 1.00 47.21 ?  500 HOH   A O    1 
HETATM 6851 O  O    . HOH   F 5 .   ? 37.366 -6.616  7.622   1.00 25.44 ?  501 HOH   A O    1 
HETATM 6852 O  O    . HOH   F 5 .   ? 23.139 -23.775 1.597   1.00 31.51 ?  502 HOH   A O    1 
HETATM 6853 O  O    . HOH   F 5 .   ? 39.525 -0.005  6.624   1.00 30.06 ?  503 HOH   A O    1 
HETATM 6854 O  O    . HOH   F 5 .   ? 37.991 13.944  6.759   1.00 43.42 ?  504 HOH   A O    1 
HETATM 6855 O  O    . HOH   F 5 .   ? 30.726 5.851   -14.751 1.00 33.58 ?  505 HOH   A O    1 
HETATM 6856 O  O    . HOH   F 5 .   ? 29.018 14.439  0.827   1.00 46.94 ?  506 HOH   A O    1 
HETATM 6857 O  O    . HOH   F 5 .   ? 21.996 -24.006 4.512   1.00 26.92 ?  507 HOH   A O    1 
HETATM 6858 O  O    . HOH   F 5 .   ? 36.456 -6.501  10.200  1.00 46.39 ?  508 HOH   A O    1 
HETATM 6859 O  O    T HOH   F 5 .   ? 11.923 -2.122  -3.679  0.30 12.13 ?  509 HOH   A O    1 
HETATM 6860 O  O    A HOH   F 5 .   ? 14.852 8.682   4.859   0.64 39.01 ?  510 HOH   A O    1 
HETATM 6861 O  O    . HOH   F 5 .   ? 17.320 -6.537  -14.233 1.00 39.91 ?  511 HOH   A O    1 
HETATM 6862 O  O    . HOH   F 5 .   ? 24.077 9.067   -7.202  1.00 37.01 ?  512 HOH   A O    1 
HETATM 6863 O  O    . HOH   F 5 .   ? 15.776 -12.231 27.400  1.00 46.22 ?  513 HOH   A O    1 
HETATM 6864 O  O    . HOH   F 5 .   ? 16.375 -21.106 18.762  1.00 38.28 ?  514 HOH   A O    1 
HETATM 6865 O  O    . HOH   F 5 .   ? 14.740 -22.751 19.823  1.00 34.99 ?  515 HOH   A O    1 
HETATM 6866 O  O    . HOH   G 5 .   ? 29.818 -22.439 5.515   1.00 21.18 ?  201 HOH   B O    1 
HETATM 6867 O  O    . HOH   G 5 .   ? 41.724 -36.015 -17.123 1.00 33.21 ?  202 HOH   B O    1 
HETATM 6868 O  O    . HOH   G 5 .   ? 27.695 -29.180 -1.819  1.00 35.68 ?  203 HOH   B O    1 
HETATM 6869 O  O    . HOH   G 5 .   ? 41.346 -7.838  5.474   1.00 39.96 ?  204 HOH   B O    1 
HETATM 6870 O  O    . HOH   G 5 .   ? 59.162 -18.679 6.878   1.00 35.51 ?  205 HOH   B O    1 
HETATM 6871 O  O    . HOH   G 5 .   ? 48.109 -6.878  15.579  1.00 31.04 ?  206 HOH   B O    1 
HETATM 6872 O  O    . HOH   G 5 .   ? 37.972 -39.442 -0.160  1.00 38.67 ?  207 HOH   B O    1 
HETATM 6873 O  O    . HOH   G 5 .   ? 47.401 -7.426  -3.918  1.00 39.18 ?  208 HOH   B O    1 
HETATM 6874 O  O    . HOH   G 5 .   ? 29.897 -26.262 4.075   1.00 28.73 ?  209 HOH   B O    1 
HETATM 6875 O  O    . HOH   G 5 .   ? 27.860 -41.820 -15.156 1.00 34.88 ?  210 HOH   B O    1 
HETATM 6876 O  O    . HOH   G 5 .   ? 49.397 -22.725 -19.762 1.00 47.23 ?  211 HOH   B O    1 
HETATM 6877 O  O    . HOH   G 5 .   ? 52.930 -13.462 -20.369 1.00 35.18 ?  212 HOH   B O    1 
HETATM 6878 O  O    . HOH   G 5 .   ? 57.712 -24.476 5.044   1.00 36.03 ?  213 HOH   B O    1 
HETATM 6879 O  O    . HOH   G 5 .   ? 50.185 -3.354  7.196   1.00 35.34 ?  214 HOH   B O    1 
HETATM 6880 O  O    . HOH   G 5 .   ? 30.915 -28.755 4.379   1.00 28.24 ?  215 HOH   B O    1 
HETATM 6881 O  O    . HOH   G 5 .   ? 56.351 -19.709 7.307   1.00 32.29 ?  216 HOH   B O    1 
HETATM 6882 O  O    . HOH   G 5 .   ? 54.496 -9.388  -8.706  1.00 19.36 ?  217 HOH   B O    1 
HETATM 6883 O  O    . HOH   G 5 .   ? 30.211 -41.027 -8.035  1.00 17.69 ?  218 HOH   B O    1 
HETATM 6884 O  O    . HOH   G 5 .   ? 57.161 -26.889 -7.664  1.00 39.60 ?  219 HOH   B O    1 
HETATM 6885 O  O    . HOH   G 5 .   ? 58.232 -12.930 8.462   1.00 30.92 ?  220 HOH   B O    1 
HETATM 6886 O  O    . HOH   G 5 .   ? 37.096 -19.850 -18.137 1.00 37.78 ?  221 HOH   B O    1 
HETATM 6887 O  O    . HOH   G 5 .   ? 34.542 -36.394 -7.166  1.00 19.04 ?  222 HOH   B O    1 
HETATM 6888 O  O    . HOH   G 5 .   ? 55.360 -16.531 -14.323 1.00 32.39 ?  223 HOH   B O    1 
HETATM 6889 O  O    . HOH   G 5 .   ? 44.413 -7.223  2.087   1.00 32.93 ?  224 HOH   B O    1 
HETATM 6890 O  O    . HOH   G 5 .   ? 56.682 -30.792 -7.713  1.00 30.44 ?  225 HOH   B O    1 
HETATM 6891 O  O    . HOH   G 5 .   ? 41.512 -39.204 -14.824 1.00 23.41 ?  226 HOH   B O    1 
HETATM 6892 O  O    . HOH   G 5 .   ? 45.114 -34.973 6.867   1.00 43.40 ?  227 HOH   B O    1 
HETATM 6893 O  O    . HOH   G 5 .   ? 50.765 -6.085  0.159   1.00 27.17 ?  228 HOH   B O    1 
HETATM 6894 O  O    . HOH   G 5 .   ? 32.798 -43.795 -11.306 1.00 21.03 ?  229 HOH   B O    1 
HETATM 6895 O  O    . HOH   G 5 .   ? 35.985 -43.323 -8.423  1.00 32.42 ?  230 HOH   B O    1 
HETATM 6896 O  O    . HOH   G 5 .   ? 25.411 -25.923 -1.261  1.00 32.63 ?  231 HOH   B O    1 
HETATM 6897 O  O    . HOH   G 5 .   ? 34.856 -24.629 13.853  1.00 33.85 ?  232 HOH   B O    1 
HETATM 6898 O  O    . HOH   G 5 .   ? 57.403 -16.286 -12.226 1.00 19.12 ?  233 HOH   B O    1 
HETATM 6899 O  O    . HOH   G 5 .   ? 51.670 -6.466  4.380   1.00 19.52 ?  234 HOH   B O    1 
HETATM 6900 O  O    . HOH   G 5 .   ? 50.738 -12.979 -0.466  1.00 12.09 ?  235 HOH   B O    1 
HETATM 6901 O  O    . HOH   G 5 .   ? 35.106 -8.004  -3.014  1.00 18.34 ?  236 HOH   B O    1 
HETATM 6902 O  O    . HOH   G 5 .   ? 41.348 -9.630  13.101  1.00 22.06 ?  237 HOH   B O    1 
HETATM 6903 O  O    . HOH   G 5 .   ? 39.294 -10.885 6.133   1.00 25.00 ?  238 HOH   B O    1 
HETATM 6904 O  O    . HOH   G 5 .   ? 40.635 -16.048 14.137  1.00 24.36 ?  239 HOH   B O    1 
HETATM 6905 O  O    . HOH   G 5 .   ? 46.404 -1.561  13.244  1.00 27.74 ?  240 HOH   B O    1 
HETATM 6906 O  O    . HOH   G 5 .   ? 48.603 -36.500 -15.485 1.00 44.34 ?  241 HOH   B O    1 
HETATM 6907 O  O    . HOH   G 5 .   ? 42.556 -25.370 2.680   1.00 15.88 ?  242 HOH   B O    1 
HETATM 6908 O  O    . HOH   G 5 .   ? 44.510 -27.714 -0.646  1.00 23.14 ?  243 HOH   B O    1 
HETATM 6909 O  O    . HOH   G 5 .   ? 39.494 -11.110 0.380   1.00 16.58 ?  244 HOH   B O    1 
HETATM 6910 O  O    . HOH   G 5 .   ? 44.913 -43.602 -10.456 1.00 28.87 ?  245 HOH   B O    1 
HETATM 6911 O  O    . HOH   G 5 .   ? 29.803 -34.190 -0.426  1.00 36.40 ?  246 HOH   B O    1 
HETATM 6912 O  O    . HOH   G 5 .   ? 50.940 -39.982 -8.150  1.00 34.11 ?  247 HOH   B O    1 
HETATM 6913 O  O    . HOH   G 5 .   ? 28.384 -19.692 -13.098 1.00 24.32 ?  248 HOH   B O    1 
HETATM 6914 O  O    . HOH   G 5 .   ? 43.078 -43.265 -8.160  1.00 29.20 ?  249 HOH   B O    1 
HETATM 6915 O  O    . HOH   G 5 .   ? 34.224 -18.459 11.430  1.00 25.69 ?  250 HOH   B O    1 
HETATM 6916 O  O    . HOH   G 5 .   ? 42.635 -22.866 3.882   1.00 12.13 ?  251 HOH   B O    1 
HETATM 6917 O  O    . HOH   G 5 .   ? 51.551 -13.838 11.060  1.00 26.09 ?  252 HOH   B O    1 
HETATM 6918 O  O    . HOH   G 5 .   ? 48.030 -24.540 -17.753 1.00 31.47 ?  253 HOH   B O    1 
HETATM 6919 O  O    . HOH   G 5 .   ? 43.206 -32.428 -17.025 1.00 24.09 ?  254 HOH   B O    1 
HETATM 6920 O  O    . HOH   G 5 .   ? 57.626 -24.378 -3.796  1.00 21.15 ?  255 HOH   B O    1 
HETATM 6921 O  O    . HOH   G 5 .   ? 40.331 -12.769 -11.501 1.00 15.60 ?  256 HOH   B O    1 
HETATM 6922 O  O    . HOH   G 5 .   ? 41.859 -23.508 9.312   1.00 18.73 ?  257 HOH   B O    1 
HETATM 6923 O  O    . HOH   G 5 .   ? 38.487 -11.086 -2.215  1.00 19.54 ?  258 HOH   B O    1 
HETATM 6924 O  O    . HOH   G 5 .   ? 58.203 -10.658 -4.062  1.00 19.77 ?  259 HOH   B O    1 
HETATM 6925 O  O    . HOH   G 5 .   ? 42.355 -34.707 3.779   1.00 25.87 ?  260 HOH   B O    1 
HETATM 6926 O  O    . HOH   G 5 .   ? 31.787 -17.913 -14.494 1.00 31.35 ?  261 HOH   B O    1 
HETATM 6927 O  O    . HOH   G 5 .   ? 29.718 -25.249 -10.787 1.00 17.54 ?  262 HOH   B O    1 
HETATM 6928 O  O    . HOH   G 5 .   ? 56.137 -23.602 -14.719 1.00 26.24 ?  263 HOH   B O    1 
HETATM 6929 O  O    . HOH   G 5 .   ? 49.743 -0.460  10.209  1.00 30.03 ?  264 HOH   B O    1 
HETATM 6930 O  O    . HOH   G 5 .   ? 38.900 -11.935 12.375  1.00 36.71 ?  265 HOH   B O    1 
HETATM 6931 O  O    . HOH   G 5 .   ? 30.852 -15.716 2.703   1.00 14.33 ?  266 HOH   B O    1 
HETATM 6932 O  O    . HOH   G 5 .   ? 27.131 -31.855 -9.934  1.00 20.78 ?  267 HOH   B O    1 
HETATM 6933 O  O    . HOH   G 5 .   ? 57.506 -9.222  1.443   1.00 19.79 ?  268 HOH   B O    1 
HETATM 6934 O  O    . HOH   G 5 .   ? 49.330 -28.705 -6.847  1.00 15.77 ?  269 HOH   B O    1 
HETATM 6935 O  O    . HOH   G 5 .   ? 30.561 -42.242 -10.546 1.00 29.16 ?  270 HOH   B O    1 
HETATM 6936 O  O    . HOH   G 5 .   ? 48.025 -22.775 5.866   1.00 17.73 ?  271 HOH   B O    1 
HETATM 6937 O  O    . HOH   G 5 .   ? 42.333 -9.908  9.377   1.00 21.05 ?  272 HOH   B O    1 
HETATM 6938 O  O    . HOH   G 5 .   ? 28.463 -30.877 -14.685 1.00 29.60 ?  273 HOH   B O    1 
HETATM 6939 O  O    . HOH   G 5 .   ? 46.858 -29.557 9.846   1.00 32.90 ?  274 HOH   B O    1 
HETATM 6940 O  O    . HOH   G 5 .   ? 34.960 -33.390 -19.124 1.00 33.10 ?  275 HOH   B O    1 
HETATM 6941 O  O    . HOH   G 5 .   ? 43.373 -15.795 -12.177 1.00 14.34 ?  276 HOH   B O    1 
HETATM 6942 O  O    . HOH   G 5 .   ? 28.254 -34.381 -9.385  1.00 18.63 ?  277 HOH   B O    1 
HETATM 6943 O  O    . HOH   G 5 .   ? 46.625 -31.262 -4.754  1.00 22.88 ?  278 HOH   B O    1 
HETATM 6944 O  O    . HOH   G 5 .   ? 56.935 -8.628  8.474   1.00 19.66 ?  279 HOH   B O    1 
HETATM 6945 O  O    . HOH   G 5 .   ? 27.957 -22.900 -7.972  1.00 18.31 ?  280 HOH   B O    1 
HETATM 6946 O  O    . HOH   G 5 .   ? 59.786 -15.269 8.158   1.00 33.11 ?  281 HOH   B O    1 
HETATM 6947 O  O    . HOH   G 5 .   ? 34.456 -12.756 2.658   1.00 23.91 ?  282 HOH   B O    1 
HETATM 6948 O  O    . HOH   G 5 .   ? 41.169 -5.498  11.517  1.00 45.96 ?  283 HOH   B O    1 
HETATM 6949 O  O    . HOH   G 5 .   ? 48.403 -25.058 3.141   1.00 13.68 ?  284 HOH   B O    1 
HETATM 6950 O  O    . HOH   G 5 .   ? 49.947 -24.677 5.830   1.00 33.24 ?  285 HOH   B O    1 
HETATM 6951 O  O    . HOH   G 5 .   ? 36.804 -12.758 -1.504  1.00 27.12 ?  286 HOH   B O    1 
HETATM 6952 O  O    . HOH   G 5 .   ? 33.525 -15.324 -13.913 1.00 21.70 ?  287 HOH   B O    1 
HETATM 6953 O  O    . HOH   G 5 .   ? 27.568 -26.687 -15.565 1.00 32.83 ?  288 HOH   B O    1 
HETATM 6954 O  O    . HOH   G 5 .   ? 45.295 -33.419 -15.890 1.00 24.58 ?  289 HOH   B O    1 
HETATM 6955 O  O    . HOH   G 5 .   ? 47.079 -33.991 -4.564  1.00 17.95 ?  290 HOH   B O    1 
HETATM 6956 O  O    . HOH   G 5 .   ? 52.524 -10.388 13.026  1.00 22.94 ?  291 HOH   B O    1 
HETATM 6957 O  O    . HOH   G 5 .   ? 48.701 -20.026 5.965   1.00 14.04 ?  292 HOH   B O    1 
HETATM 6958 O  O    . HOH   G 5 .   ? 37.508 -18.086 13.125  1.00 31.87 ?  293 HOH   B O    1 
HETATM 6959 O  O    . HOH   G 5 .   ? 51.231 -37.613 -9.588  1.00 26.87 ?  294 HOH   B O    1 
HETATM 6960 O  O    . HOH   G 5 .   ? 44.621 -27.472 2.029   1.00 15.69 ?  295 HOH   B O    1 
HETATM 6961 O  O    . HOH   G 5 .   ? 42.717 -12.295 -18.499 1.00 30.12 ?  296 HOH   B O    1 
HETATM 6962 O  O    . HOH   G 5 .   ? 42.909 -20.294 -20.730 1.00 35.55 ?  297 HOH   B O    1 
HETATM 6963 O  O    . HOH   G 5 .   ? 57.143 -12.040 12.410  1.00 36.82 ?  298 HOH   B O    1 
HETATM 6964 O  O    . HOH   G 5 .   ? 45.932 -40.425 -3.499  1.00 30.16 ?  299 HOH   B O    1 
HETATM 6965 O  O    . HOH   G 5 .   ? 52.595 -35.668 -8.654  1.00 29.27 ?  300 HOH   B O    1 
HETATM 6966 O  O    . HOH   G 5 .   ? 35.062 -33.577 4.603   1.00 29.59 ?  301 HOH   B O    1 
HETATM 6967 O  O    . HOH   G 5 .   ? 42.352 -9.869  -14.882 1.00 39.23 ?  302 HOH   B O    1 
HETATM 6968 O  O    . HOH   G 5 .   ? 52.505 -29.276 -13.015 1.00 25.15 ?  303 HOH   B O    1 
HETATM 6969 O  O    . HOH   G 5 .   ? 51.702 -6.019  -7.896  1.00 46.84 ?  304 HOH   B O    1 
HETATM 6970 O  O    . HOH   G 5 .   ? 53.480 -30.201 4.554   1.00 19.12 ?  305 HOH   B O    1 
HETATM 6971 O  O    . HOH   G 5 .   ? 44.042 -29.356 -4.620  1.00 23.54 ?  306 HOH   B O    1 
HETATM 6972 O  O    . HOH   G 5 .   ? 37.293 -35.671 7.261   1.00 32.77 ?  307 HOH   B O    1 
HETATM 6973 O  O    . HOH   G 5 .   ? 53.089 -16.065 -12.714 1.00 27.13 ?  308 HOH   B O    1 
HETATM 6974 O  O    . HOH   G 5 .   ? 25.939 -21.469 -3.503  1.00 17.05 ?  309 HOH   B O    1 
HETATM 6975 O  O    . HOH   G 5 .   ? 37.865 -10.258 -10.761 1.00 17.94 ?  310 HOH   B O    1 
HETATM 6976 O  O    . HOH   G 5 .   ? 40.250 -10.841 -9.553  1.00 17.35 ?  311 HOH   B O    1 
HETATM 6977 O  O    . HOH   G 5 .   ? 62.715 -13.578 4.765   1.00 26.57 ?  312 HOH   B O    1 
HETATM 6978 O  O    . HOH   G 5 .   ? 43.200 -21.415 10.702  1.00 16.49 ?  313 HOH   B O    1 
HETATM 6979 O  O    . HOH   G 5 .   ? 43.492 -15.386 18.199  1.00 31.26 ?  314 HOH   B O    1 
HETATM 6980 O  O    . HOH   G 5 .   ? 32.807 -34.609 -5.861  1.00 17.20 ?  315 HOH   B O    1 
HETATM 6981 O  O    . HOH   G 5 .   ? 59.969 -17.155 -10.440 1.00 34.02 ?  316 HOH   B O    1 
HETATM 6982 O  O    . HOH   G 5 .   ? 51.359 -33.054 -10.792 1.00 42.01 ?  317 HOH   B O    1 
HETATM 6983 O  O    . HOH   G 5 .   ? 48.607 -12.031 -14.160 1.00 27.19 ?  318 HOH   B O    1 
HETATM 6984 O  O    . HOH   G 5 .   ? 41.744 -8.038  1.363   1.00 23.91 ?  319 HOH   B O    1 
HETATM 6985 O  O    . HOH   G 5 .   ? 26.341 -21.040 -6.221  1.00 16.98 ?  320 HOH   B O    1 
HETATM 6986 O  O    . HOH   G 5 .   ? 37.117 -30.584 -20.988 1.00 32.02 ?  321 HOH   B O    1 
HETATM 6987 O  O    . HOH   G 5 .   ? 53.641 -12.598 -22.210 1.00 33.15 ?  322 HOH   B O    1 
HETATM 6988 O  O    . HOH   G 5 .   ? 38.329 -12.725 7.932   1.00 18.75 ?  323 HOH   B O    1 
HETATM 6989 O  O    . HOH   G 5 .   ? 62.878 -20.208 -0.746  1.00 36.82 ?  324 HOH   B O    1 
HETATM 6990 O  O    . HOH   G 5 .   ? 38.393 -9.363  -13.290 1.00 27.38 ?  325 HOH   B O    1 
HETATM 6991 O  O    . HOH   G 5 .   ? 36.727 -12.414 4.302   1.00 18.27 ?  326 HOH   B O    1 
HETATM 6992 O  O    . HOH   G 5 .   ? 44.606 -24.599 9.645   1.00 21.03 ?  327 HOH   B O    1 
HETATM 6993 O  O    . HOH   G 5 .   ? 44.149 -1.738  7.645   1.00 46.17 ?  328 HOH   B O    1 
HETATM 6994 O  O    . HOH   G 5 .   ? 57.627 -22.053 3.285   1.00 29.59 ?  329 HOH   B O    1 
HETATM 6995 O  O    . HOH   G 5 .   ? 47.192 -24.482 8.225   1.00 25.61 ?  330 HOH   B O    1 
HETATM 6996 O  O    . HOH   G 5 .   ? 43.120 -34.626 0.167   1.00 21.39 ?  331 HOH   B O    1 
HETATM 6997 O  O    . HOH   G 5 .   ? 48.045 -32.687 -16.620 1.00 42.69 ?  332 HOH   B O    1 
HETATM 6998 O  O    . HOH   G 5 .   ? 27.932 -14.805 -9.451  1.00 36.30 ?  333 HOH   B O    1 
HETATM 6999 O  O    . HOH   G 5 .   ? 33.595 -31.204 11.076  1.00 34.59 ?  334 HOH   B O    1 
HETATM 7000 O  O    . HOH   G 5 .   ? 41.210 -24.477 15.874  1.00 45.52 ?  335 HOH   B O    1 
HETATM 7001 O  O    . HOH   G 5 .   ? 47.473 -27.437 2.042   1.00 15.06 ?  336 HOH   B O    1 
HETATM 7002 O  O    . HOH   G 5 .   ? 37.013 -15.142 -16.504 1.00 42.06 ?  337 HOH   B O    1 
HETATM 7003 O  O    . HOH   G 5 .   ? 42.817 -43.530 -14.313 1.00 42.52 ?  338 HOH   B O    1 
HETATM 7004 O  O    . HOH   G 5 .   ? 45.702 -36.294 -16.080 1.00 35.15 ?  339 HOH   B O    1 
HETATM 7005 O  O    . HOH   G 5 .   ? 46.825 -19.884 12.333  1.00 29.62 ?  340 HOH   B O    1 
HETATM 7006 O  O    . HOH   G 5 .   ? 38.472 -12.211 -16.246 1.00 45.33 ?  341 HOH   B O    1 
HETATM 7007 O  O    . HOH   G 5 .   ? 37.042 -45.197 -9.673  1.00 37.70 ?  342 HOH   B O    1 
HETATM 7008 O  O    . HOH   G 5 .   ? 28.900 -42.937 -12.364 1.00 38.26 ?  343 HOH   B O    1 
HETATM 7009 O  O    . HOH   G 5 .   ? 39.497 -23.606 -20.373 1.00 36.54 ?  344 HOH   B O    1 
HETATM 7010 O  O    . HOH   G 5 .   ? 34.502 -10.326 7.709   1.00 23.41 ?  345 HOH   B O    1 
HETATM 7011 O  O    . HOH   G 5 .   ? 32.994 -14.678 1.076   1.00 19.16 ?  346 HOH   B O    1 
HETATM 7012 O  O    . HOH   G 5 .   ? 38.536 -22.381 15.032  1.00 41.98 ?  347 HOH   B O    1 
HETATM 7013 O  O    . HOH   G 5 .   ? 27.735 -26.590 -0.558  1.00 31.36 ?  348 HOH   B O    1 
HETATM 7014 O  O    . HOH   G 5 .   ? 39.847 -44.303 -11.165 1.00 38.73 ?  349 HOH   B O    1 
HETATM 7015 O  O    . HOH   G 5 .   ? 40.423 -43.516 -9.060  1.00 26.21 ?  350 HOH   B O    1 
HETATM 7016 O  O    . HOH   G 5 .   ? 33.723 -9.518  -8.905  1.00 32.65 ?  351 HOH   B O    1 
HETATM 7017 O  O    . HOH   G 5 .   ? 62.576 -20.103 -4.795  1.00 42.77 ?  352 HOH   B O    1 
HETATM 7018 O  O    . HOH   G 5 .   ? 55.643 -8.250  10.856  1.00 23.68 ?  353 HOH   B O    1 
HETATM 7019 O  O    . HOH   G 5 .   ? 44.188 -37.344 -17.688 1.00 33.66 ?  354 HOH   B O    1 
HETATM 7020 O  O    . HOH   G 5 .   ? 36.075 -8.591  -9.706  1.00 34.00 ?  355 HOH   B O    1 
HETATM 7021 O  O    . HOH   G 5 .   ? 23.179 -23.613 6.874   1.00 35.35 ?  356 HOH   B O    1 
HETATM 7022 O  O    . HOH   G 5 .   ? 56.601 -7.275  3.122   1.00 26.18 ?  357 HOH   B O    1 
HETATM 7023 O  O    . HOH   G 5 .   ? 34.096 -7.737  11.459  1.00 38.66 ?  358 HOH   B O    1 
HETATM 7024 O  O    . HOH   G 5 .   ? 56.914 -21.592 -16.312 1.00 38.80 ?  359 HOH   B O    1 
HETATM 7025 O  O    . HOH   G 5 .   ? 61.529 -19.913 1.768   1.00 37.35 ?  360 HOH   B O    1 
HETATM 7026 O  O    . HOH   G 5 .   ? 27.137 -25.957 -11.336 1.00 33.57 ?  361 HOH   B O    1 
HETATM 7027 O  O    . HOH   G 5 .   ? 40.252 -8.827  9.876   1.00 35.80 ?  362 HOH   B O    1 
HETATM 7028 O  O    . HOH   G 5 .   ? 43.201 -12.688 -21.146 1.00 42.32 ?  363 HOH   B O    1 
HETATM 7029 O  O    . HOH   G 5 .   ? 54.208 -5.730  3.009   1.00 35.14 ?  364 HOH   B O    1 
HETATM 7030 O  O    . HOH   G 5 .   ? 40.201 -11.334 -13.941 1.00 33.69 ?  365 HOH   B O    1 
HETATM 7031 O  O    . HOH   G 5 .   ? 32.530 -23.645 14.118  1.00 39.94 ?  366 HOH   B O    1 
HETATM 7032 O  O    . HOH   G 5 .   ? 48.336 -26.491 8.858   1.00 40.89 ?  367 HOH   B O    1 
HETATM 7033 O  O    . HOH   G 5 .   ? 36.160 -8.657  9.023   1.00 35.07 ?  368 HOH   B O    1 
HETATM 7034 O  O    . HOH   G 5 .   ? 58.924 -10.424 9.240   1.00 37.54 ?  369 HOH   B O    1 
HETATM 7035 O  O    . HOH   G 5 .   ? 39.902 -6.984  7.885   1.00 37.80 ?  370 HOH   B O    1 
HETATM 7036 O  O    . HOH   G 5 .   ? 56.094 -7.806  -0.634  1.00 31.90 ?  371 HOH   B O    1 
HETATM 7037 O  O    . HOH   G 5 .   ? 52.058 -12.926 13.387  1.00 29.98 ?  372 HOH   B O    1 
HETATM 7038 O  O    . HOH   G 5 .   ? 41.824 -10.004 -17.420 1.00 54.20 ?  373 HOH   B O    1 
HETATM 7039 O  O    . HOH   G 5 .   ? 63.029 -12.356 6.934   1.00 37.49 ?  374 HOH   B O    1 
HETATM 7040 O  O    . HOH   G 5 .   ? 38.003 -10.578 10.093  1.00 29.09 ?  375 HOH   B O    1 
HETATM 7041 O  O    . HOH   G 5 .   ? 36.524 -22.850 13.322  1.00 31.39 ?  376 HOH   B O    1 
HETATM 7042 O  O    . HOH   G 5 .   ? 41.828 -6.700  -4.845  1.00 46.00 ?  377 HOH   B O    1 
HETATM 7043 O  O    . HOH   G 5 .   ? 44.080 -5.595  -3.551  1.00 42.88 ?  378 HOH   B O    1 
HETATM 7044 O  O    . HOH   G 5 .   ? 42.606 -17.102 -23.134 1.00 43.12 ?  379 HOH   B O    1 
HETATM 7045 O  O    . HOH   G 5 .   ? 40.109 -7.663  3.224   1.00 34.42 ?  380 HOH   B O    1 
HETATM 7046 O  O    . HOH   G 5 .   ? 39.655 -14.037 15.680  1.00 48.53 ?  381 HOH   B O    1 
HETATM 7047 O  O    . HOH   G 5 .   ? 52.857 -29.884 7.244   1.00 23.45 ?  382 HOH   B O    1 
HETATM 7048 O  O    . HOH   G 5 .   ? 25.824 -18.843 -11.838 1.00 38.95 ?  383 HOH   B O    1 
HETATM 7049 O  O    . HOH   G 5 .   ? 46.763 -5.374  2.882   1.00 38.23 ?  384 HOH   B O    1 
HETATM 7050 O  O    . HOH   G 5 .   ? 60.514 -22.273 2.901   1.00 47.61 ?  385 HOH   B O    1 
HETATM 7051 O  O    . HOH   G 5 .   ? 23.916 -20.878 -7.634  1.00 29.23 ?  386 HOH   B O    1 
HETATM 7052 O  O    . HOH   G 5 .   ? 35.265 -20.345 13.295  1.00 33.02 ?  387 HOH   B O    1 
HETATM 7053 O  O    . HOH   G 5 .   ? 35.402 -33.732 7.385   1.00 40.95 ?  388 HOH   B O    1 
HETATM 7054 O  O    . HOH   G 5 .   ? 40.930 -9.784  15.850  1.00 45.04 ?  389 HOH   B O    1 
HETATM 7055 O  O    . HOH   G 5 .   ? 40.735 -6.607  -0.865  1.00 24.46 ?  390 HOH   B O    1 
HETATM 7056 O  O    . HOH   G 5 .   ? 44.111 -31.717 -3.697  1.00 37.73 ?  391 HOH   B O    1 
HETATM 7057 O  O    . HOH   G 5 .   ? 27.926 -27.078 2.227   1.00 31.42 ?  392 HOH   B O    1 
HETATM 7058 O  O    . HOH   G 5 .   ? 26.624 -27.988 -13.430 1.00 35.99 ?  393 HOH   B O    1 
HETATM 7059 O  O    . HOH   G 5 .   ? 24.633 -20.597 -10.515 1.00 40.57 ?  394 HOH   B O    1 
HETATM 7060 O  O    . HOH   G 5 .   ? 50.651 -30.820 8.716   1.00 29.47 ?  395 HOH   B O    1 
HETATM 7061 O  O    . HOH   G 5 .   ? 34.360 -33.503 9.637   1.00 35.50 ?  396 HOH   B O    1 
HETATM 7062 O  O    . HOH   G 5 .   ? 26.850 -30.693 -12.585 1.00 28.72 ?  397 HOH   B O    1 
HETATM 7063 O  O    . HOH   G 5 .   ? 57.725 -6.559  -2.340  1.00 34.76 ?  398 HOH   B O    1 
HETATM 7064 O  O    . HOH   G 5 .   ? 45.734 -20.147 15.246  1.00 48.89 ?  399 HOH   B O    1 
HETATM 7065 O  O    . HOH   G 5 .   ? 40.896 -11.776 -22.289 1.00 38.86 ?  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   . VAL   A 3   ? 0.6630 0.6831 0.7692 -0.0251 -0.0463 0.1032  3   VAL   A N   
2    C  CA  . VAL   A 3   ? 0.6572 0.6778 0.7533 -0.0262 -0.0464 0.1020  3   VAL   A CA  
3    C  C   . VAL   A 3   ? 0.6276 0.6533 0.7088 -0.0343 -0.0455 0.1040  3   VAL   A C   
4    O  O   . VAL   A 3   ? 0.6333 0.6568 0.7268 -0.0329 -0.0469 0.1075  3   VAL   A O   
5    C  CB  . VAL   A 3   ? 0.6745 0.6921 0.7703 -0.0212 -0.0449 0.1005  3   VAL   A CB  
6    C  CG1 . VAL   A 3   ? 0.6821 0.7001 0.7752 -0.0209 -0.0439 0.1008  3   VAL   A CG1 
7    C  CG2 . VAL   A 3   ? 0.6784 0.6932 0.7755 -0.0181 -0.0437 0.1007  3   VAL   A CG2 
16   N  N   . ASN   A 4   ? 0.5872 0.6213 0.6302 -0.0443 -0.0404 0.1026  4   ASN   A N   
17   C  CA  . ASN   A 4   ? 0.5449 0.5855 0.5376 -0.0562 -0.0340 0.0962  4   ASN   A CA  
18   C  C   . ASN   A 4   ? 0.4879 0.5403 0.4726 -0.0693 -0.0169 0.0616  4   ASN   A C   
19   O  O   . ASN   A 4   ? 0.4922 0.5430 0.4726 -0.0679 -0.0204 0.0658  4   ASN   A O   
20   C  CB  . ASN   A 4   ? 0.5568 0.5918 0.5028 -0.0568 -0.0446 0.1228  4   ASN   A CB  
21   C  CG  . ASN   A 4   ? 0.5658 0.5940 0.4697 -0.0594 -0.0520 0.1493  4   ASN   A CG  
22   O  OD1 . ASN   A 4   ? 0.5710 0.5934 0.4504 -0.0592 -0.0544 0.1620  4   ASN   A OD1 
23   N  ND2 . ASN   A 4   ? 0.5672 0.5947 0.4562 -0.0608 -0.0549 0.1605  4   ASN   A ND2 
30   N  N   A SER   A 5   ? 0.4518 0.5171 0.4370 -0.0820 -0.0073 0.0410  5   SER   A N   
31   N  N   B SER   A 5   ? 0.4606 0.5116 0.4477 -0.0726 -0.0065 0.0438  5   SER   A N   
32   C  CA  A SER   A 5   ? 0.4137 0.4922 0.4019 -0.0919 0.0026  0.0228  5   SER   A CA  
33   C  CA  B SER   A 5   ? 0.4312 0.4811 0.4206 -0.0738 0.0043  0.0277  5   SER   A CA  
34   C  C   A SER   A 5   ? 0.3705 0.4580 0.3518 -0.1004 0.0149  0.0134  5   SER   A C   
35   C  C   B SER   A 5   ? 0.3972 0.4438 0.3763 -0.0751 0.0156  0.0186  5   SER   A C   
36   O  O   A SER   A 5   ? 0.3748 0.4665 0.3541 -0.0940 0.0145  0.0040  5   SER   A O   
37   O  O   B SER   A 5   ? 0.4005 0.4485 0.3795 -0.0698 0.0175  0.0131  5   SER   A O   
38   C  CB  A SER   A 5   ? 0.4199 0.4997 0.4101 -0.0926 0.0030  0.0153  5   SER   A CB  
39   C  CB  B SER   A 5   ? 0.4358 0.4864 0.4301 -0.0731 0.0054  0.0220  5   SER   A CB  
40   O  OG  A SER   A 5   ? 0.4242 0.5039 0.4202 -0.0931 0.0058  0.0109  5   SER   A OG  
41   O  OG  B SER   A 5   ? 0.4386 0.4894 0.4393 -0.0725 0.0069  0.0185  5   SER   A OG  
52   N  N   A PHE   A 6   ? 0.3185 0.4135 0.3005 -0.1150 0.0297  0.0182  6   PHE   A N   
53   N  N   B PHE   A 6   ? 0.3573 0.4006 0.3297 -0.0820 0.0260  0.0182  6   PHE   A N   
54   C  CA  A PHE   A 6   ? 0.2720 0.3685 0.2520 -0.1238 0.0378  0.0267  6   PHE   A CA  
55   C  CA  B PHE   A 6   ? 0.3186 0.3571 0.2850 -0.0860 0.0336  0.0199  6   PHE   A CA  
56   C  C   A PHE   A 6   ? 0.2618 0.3555 0.2397 -0.1290 0.0484  0.0169  6   PHE   A C   
57   C  C   B PHE   A 6   ? 0.3081 0.3395 0.2764 -0.0858 0.0479  0.0171  6   PHE   A C   
58   O  O   A PHE   A 6   ? 0.2694 0.3664 0.2733 -0.1281 0.0528  0.0245  6   PHE   A O   
59   O  O   B PHE   A 6   ? 0.3096 0.3400 0.2838 -0.0841 0.0507  0.0248  6   PHE   A O   
60   C  CB  A PHE   A 6   ? 0.2490 0.3404 0.2171 -0.1180 0.0323  0.0444  6   PHE   A CB  
61   C  CB  B PHE   A 6   ? 0.2958 0.3334 0.2527 -0.0854 0.0236  0.0222  6   PHE   A CB  
62   C  CG  A PHE   A 6   ? 0.2338 0.3222 0.1995 -0.1055 0.0251  0.0495  6   PHE   A CG  
63   C  CG  B PHE   A 6   ? 0.2763 0.3149 0.2299 -0.0824 0.0136  0.0213  6   PHE   A CG  
64   C  CD1 A PHE   A 6   ? 0.2267 0.3134 0.1955 -0.0957 0.0205  0.0478  6   PHE   A CD1 
65   C  CD1 B PHE   A 6   ? 0.2675 0.3067 0.2203 -0.0791 0.0103  0.0223  6   PHE   A CD1 
66   C  CD2 A PHE   A 6   ? 0.2402 0.3195 0.2132 -0.0892 0.0192  0.0533  6   PHE   A CD2 
67   C  CD2 B PHE   A 6   ? 0.2726 0.3083 0.2314 -0.0773 0.0081  0.0208  6   PHE   A CD2 
68   C  CE1 A PHE   A 6   ? 0.2271 0.3095 0.2010 -0.0889 0.0263  0.0522  6   PHE   A CE1 
69   C  CE1 B PHE   A 6   ? 0.2635 0.3017 0.2208 -0.0774 0.0090  0.0215  6   PHE   A CE1 
70   C  CE2 A PHE   A 6   ? 0.2403 0.3160 0.2198 -0.0834 0.0198  0.0492  6   PHE   A CE2 
71   C  CE2 B PHE   A 6   ? 0.2681 0.3022 0.2315 -0.0763 0.0074  0.0186  6   PHE   A CE2 
72   C  CZ  A PHE   A 6   ? 0.2349 0.3101 0.2067 -0.0860 0.0196  0.0462  6   PHE   A CZ  
73   C  CZ  B PHE   A 6   ? 0.2650 0.3001 0.2237 -0.0765 0.0065  0.0174  6   PHE   A CZ  
92   N  N   A SER   A 7   ? 0.2467 0.3327 0.2100 -0.1295 0.0543  0.0028  7   SER   A N   
93   N  N   B SER   A 7   ? 0.2972 0.3205 0.2690 -0.0849 0.0531  0.0034  7   SER   A N   
94   C  CA  A SER   A 7   ? 0.2432 0.3218 0.2089 -0.1165 0.0509  -0.0233 7   SER   A CA  
95   C  CA  B SER   A 7   ? 0.2916 0.3051 0.2703 -0.0753 0.0499  -0.0131 7   SER   A CA  
96   C  C   A SER   A 7   ? 0.2284 0.2851 0.1755 -0.1048 0.0610  -0.0210 7   SER   A C   
97   C  C   B SER   A 7   ? 0.2798 0.2883 0.2514 -0.0626 0.0538  -0.0144 7   SER   A C   
98   O  O   A SER   A 7   ? 0.2479 0.2732 0.1784 -0.1047 0.0613  -0.0187 7   SER   A O   
99   O  O   B SER   A 7   ? 0.2887 0.2912 0.2469 -0.0576 0.0535  -0.0144 7   SER   A O   
100  C  CB  A SER   A 7   ? 0.2617 0.3475 0.2452 -0.1038 0.0476  -0.0310 7   SER   A CB  
101  C  CB  B SER   A 7   ? 0.2949 0.3043 0.2951 -0.0819 0.0423  -0.0247 7   SER   A CB  
102  O  OG  A SER   A 7   ? 0.2801 0.3643 0.2738 -0.0906 0.0430  -0.0348 7   SER   A OG  
103  O  OG  B SER   A 7   ? 0.2978 0.3051 0.3120 -0.0861 0.0313  -0.0359 7   SER   A OG  
114  N  N   A GLY   A 8   ? 0.2032 0.2563 0.1741 -0.0919 0.0471  -0.0310 8   GLY   A N   
115  N  N   B GLY   A 8   ? 0.2618 0.2722 0.2352 -0.0495 0.0538  -0.0125 8   GLY   A N   
116  C  CA  A GLY   A 8   ? 0.1865 0.2319 0.1732 -0.0716 0.0454  -0.0224 8   GLY   A CA  
117  C  CA  B GLY   A 8   ? 0.2446 0.2530 0.2219 -0.0373 0.0487  -0.0102 8   GLY   A CA  
118  C  C   A GLY   A 8   ? 0.1726 0.2166 0.1794 -0.0461 0.0351  -0.0206 8   GLY   A C   
119  C  C   B GLY   A 8   ? 0.2234 0.2323 0.2017 -0.0280 0.0424  -0.0082 8   GLY   A C   
120  O  O   A GLY   A 8   ? 0.1829 0.2199 0.1949 -0.0264 0.0399  -0.0392 8   GLY   A O   
121  O  O   B GLY   A 8   ? 0.2259 0.2351 0.2082 -0.0186 0.0475  -0.0181 8   GLY   A O   
128  N  N   A TYR   A 9   ? 0.1553 0.2025 0.1706 -0.0316 0.0359  -0.0122 9   TYR   A N   
129  N  N   B TYR   A 9   ? 0.2006 0.2094 0.1920 -0.0262 0.0301  0.0045  9   TYR   A N   
130  C  CA  A TYR   A 9   ? 0.1471 0.1827 0.1538 -0.0328 0.0219  -0.0060 9   TYR   A CA  
131  C  CA  B TYR   A 9   ? 0.1855 0.1882 0.1776 -0.0220 0.0320  0.0108  9   TYR   A CA  
132  C  C   A TYR   A 9   ? 0.1472 0.1607 0.1335 -0.0276 0.0247  0.0100  9   TYR   A C   
133  C  C   B TYR   A 9   ? 0.1839 0.1747 0.1726 -0.0164 0.0363  0.0127  9   TYR   A C   
134  O  O   A TYR   A 9   ? 0.1738 0.1743 0.1544 -0.0238 0.0083  0.0048  9   TYR   A O   
135  O  O   B TYR   A 9   ? 0.1968 0.1837 0.1909 -0.0166 0.0264  0.0173  9   TYR   A O   
136  C  CB  A TYR   A 9   ? 0.1402 0.1874 0.1657 -0.0280 0.0244  -0.0184 9   TYR   A CB  
137  C  CB  B TYR   A 9   ? 0.1741 0.1873 0.1796 -0.0234 0.0255  0.0044  9   TYR   A CB  
138  C  CG  A TYR   A 9   ? 0.1423 0.1793 0.1765 -0.0135 0.0367  -0.0231 9   TYR   A CG  
139  C  CG  B TYR   A 9   ? 0.1636 0.1866 0.1710 -0.0225 0.0253  -0.0015 9   TYR   A CG  
140  C  CD1 A TYR   A 9   ? 0.1446 0.1777 0.1834 -0.0177 0.0458  -0.0241 9   TYR   A CD1 
141  C  CD1 B TYR   A 9   ? 0.1641 0.1836 0.1767 -0.0237 0.0280  -0.0092 9   TYR   A CD1 
142  C  CD2 A TYR   A 9   ? 0.1485 0.1756 0.1904 -0.0076 0.0253  -0.0114 9   TYR   A CD2 
143  C  CD2 B TYR   A 9   ? 0.1572 0.1886 0.1600 -0.0163 0.0199  0.0003  9   TYR   A CD2 
144  C  CE1 A TYR   A 9   ? 0.1534 0.1785 0.2083 -0.0121 0.0412  -0.0291 9   TYR   A CE1 
145  C  CE1 B TYR   A 9   ? 0.1584 0.1831 0.1679 -0.0262 0.0303  -0.0147 9   TYR   A CE1 
146  C  CE2 A TYR   A 9   ? 0.1490 0.1771 0.1979 -0.0075 0.0307  -0.0134 9   TYR   A CE2 
147  C  CE2 B TYR   A 9   ? 0.1512 0.1880 0.1612 -0.0144 0.0295  -0.0018 9   TYR   A CE2 
148  C  CZ  A TYR   A 9   ? 0.1492 0.1792 0.2154 -0.0197 0.0427  -0.0193 9   TYR   A CZ  
149  C  CZ  B TYR   A 9   ? 0.1476 0.1837 0.1695 -0.0194 0.0463  -0.0123 9   TYR   A CZ  
150  O  OH  A TYR   A 9   ? 0.1623 0.1890 0.2386 -0.0262 0.0423  -0.0251 9   TYR   A OH  
151  O  OH  B TYR   A 9   ? 0.1392 0.1805 0.1857 -0.0216 0.0651  -0.0096 9   TYR   A OH  
170  N  N   A LEU   A 10  ? 0.1456 0.1445 0.1482 -0.0241 0.0211  0.0130  10  LEU   A N   
171  N  N   B LEU   A 10  ? 0.1784 0.1611 0.1656 -0.0153 0.0394  0.0013  10  LEU   A N   
172  C  CA  A LEU   A 10  ? 0.1309 0.1415 0.1556 -0.0174 0.0222  0.0207  10  LEU   A CA  
173  C  CA  B LEU   A 10  ? 0.1778 0.1621 0.1742 -0.0107 0.0322  -0.0069 10  LEU   A CA  
174  C  C   A LEU   A 10  ? 0.1280 0.1347 0.1658 -0.0160 0.0239  0.0236  10  LEU   A C   
175  C  C   B LEU   A 10  ? 0.1686 0.1515 0.1671 -0.0100 0.0274  0.0010  10  LEU   A C   
176  O  O   A LEU   A 10  ? 0.1344 0.1255 0.1734 -0.0176 0.0391  0.0255  10  LEU   A O   
177  O  O   B LEU   A 10  ? 0.1709 0.1403 0.1529 -0.0111 0.0388  0.0037  10  LEU   A O   
178  C  CB  A LEU   A 10  ? 0.1293 0.1475 0.1734 -0.0115 0.0054  0.0340  10  LEU   A CB  
179  C  CB  B LEU   A 10  ? 0.1864 0.1689 0.1885 -0.0125 0.0140  -0.0093 10  LEU   A CB  
180  C  CG  A LEU   A 10  ? 0.1519 0.1595 0.2284 0.0029  -0.0120 0.0365  10  LEU   A CG  
181  C  CG  B LEU   A 10  ? 0.1958 0.1807 0.2164 -0.0166 -0.0090 -0.0125 10  LEU   A CG  
182  C  CD1 A LEU   A 10  ? 0.1709 0.1611 0.2465 -0.0079 -0.0067 0.0213  10  LEU   A CD1 
183  C  CD1 B LEU   A 10  ? 0.1973 0.1849 0.2320 -0.0275 -0.0081 -0.0144 10  LEU   A CD1 
184  C  CD2 A LEU   A 10  ? 0.1639 0.1783 0.2353 0.0100  0.0007  0.0361  10  LEU   A CD2 
185  C  CD2 B LEU   A 10  ? 0.2081 0.1905 0.2288 -0.0069 -0.0235 -0.0190 10  LEU   A CD2 
208  N  N   A LYS   A 11  ? 0.1345 0.1376 0.1778 -0.0136 0.0279  0.0317  11  LYS   A N   
209  N  N   B LYS   A 11  ? 0.1652 0.1488 0.1638 -0.0157 0.0184  0.0045  11  LYS   A N   
210  C  CA  A LYS   A 11  ? 0.1319 0.1329 0.1898 -0.0189 0.0251  0.0230  11  LYS   A CA  
211  C  CA  B LYS   A 11  ? 0.1579 0.1387 0.1628 -0.0209 0.0169  0.0085  11  LYS   A CA  
212  C  C   A LYS   A 11  ? 0.1299 0.1391 0.1868 -0.0164 0.0309  0.0084  11  LYS   A C   
213  C  C   B LYS   A 11  ? 0.1502 0.1278 0.1622 -0.0215 0.0222  0.0061  11  LYS   A C   
214  O  O   A LYS   A 11  ? 0.1366 0.1615 0.2248 -0.0351 0.0319  -0.0014 11  LYS   A O   
215  O  O   B LYS   A 11  ? 0.1494 0.1229 0.1776 -0.0225 0.0219  -0.0109 11  LYS   A O   
216  C  CB  A LYS   A 11  ? 0.1381 0.1353 0.1921 -0.0152 0.0211  0.0169  11  LYS   A CB  
217  C  CB  B LYS   A 11  ? 0.1620 0.1351 0.1599 -0.0197 0.0135  0.0066  11  LYS   A CB  
218  C  CG  A LYS   A 11  ? 0.1485 0.1376 0.1991 -0.0150 0.0162  0.0317  11  LYS   A CG  
219  C  CG  B LYS   A 11  ? 0.1660 0.1420 0.1492 -0.0140 0.0224  0.0166  11  LYS   A CG  
220  C  CD  A LYS   A 11  ? 0.1566 0.1440 0.2028 -0.0111 0.0143  0.0354  11  LYS   A CD  
221  C  CD  B LYS   A 11  ? 0.1656 0.1514 0.1478 -0.0066 0.0326  0.0247  11  LYS   A CD  
222  C  CE  A LYS   A 11  ? 0.1631 0.1419 0.2095 0.0012  0.0181  0.0363  11  LYS   A CE  
223  C  CE  B LYS   A 11  ? 0.1660 0.1516 0.1370 -0.0008 0.0330  0.0309  11  LYS   A CE  
224  N  NZ  A LYS   A 11  ? 0.1665 0.1401 0.2094 0.0070  0.0259  0.0265  11  LYS   A NZ  
225  N  NZ  B LYS   A 11  ? 0.1635 0.1504 0.1360 0.0103  0.0306  0.0318  11  LYS   A NZ  
252  N  N   A LEU   A 12  ? 0.1281 0.1297 0.1678 -0.0226 0.0232  0.0068  12  LEU   A N   
253  N  N   B LEU   A 12  ? 0.1467 0.1335 0.1620 -0.0082 0.0187  0.0007  12  LEU   A N   
254  C  CA  A LEU   A 12  ? 0.1294 0.1345 0.1567 -0.0158 0.0066  0.0122  12  LEU   A CA  
255  C  CA  B LEU   A 12  ? 0.1446 0.1437 0.1664 -0.0031 0.0226  0.0015  12  LEU   A CA  
256  C  C   A LEU   A 12  ? 0.1340 0.1304 0.1704 -0.0218 0.0087  0.0203  12  LEU   A C   
257  C  C   B LEU   A 12  ? 0.1395 0.1420 0.1685 -0.0010 0.0263  -0.0019 12  LEU   A C   
258  O  O   A LEU   A 12  ? 0.1410 0.1312 0.1842 -0.0159 0.0199  0.0092  12  LEU   A O   
259  O  O   B LEU   A 12  ? 0.1459 0.1445 0.1653 0.0071  0.0181  -0.0074 12  LEU   A O   
260  C  CB  A LEU   A 12  ? 0.1357 0.1338 0.1658 -0.0132 -0.0057 0.0142  12  LEU   A CB  
261  C  CB  B LEU   A 12  ? 0.1539 0.1499 0.1841 -0.0023 0.0262  -0.0019 12  LEU   A CB  
262  C  CG  A LEU   A 12  ? 0.1465 0.1432 0.1805 -0.0038 0.0095  0.0124  12  LEU   A CG  
263  C  CG  B LEU   A 12  ? 0.1579 0.1531 0.2123 0.0009  0.0307  -0.0027 12  LEU   A CG  
264  C  CD1 A LEU   A 12  ? 0.1594 0.1424 0.1877 0.0118  0.0275  0.0385  12  LEU   A CD1 
265  C  CD1 B LEU   A 12  ? 0.1564 0.1612 0.2201 0.0091  0.0409  -0.0030 12  LEU   A CD1 
266  C  CD2 A LEU   A 12  ? 0.1465 0.1549 0.1976 -0.0087 0.0011  0.0151  12  LEU   A CD2 
267  C  CD2 B LEU   A 12  ? 0.1597 0.1555 0.2168 0.0003  0.0289  -0.0101 12  LEU   A CD2 
290  N  N   A THR   A 13  ? 0.1280 0.1251 0.1922 -0.0193 0.0124  0.0179  13  THR   A N   
291  N  N   B THR   A 13  ? 0.1352 0.1380 0.1827 -0.0083 0.0261  0.0046  13  THR   A N   
292  C  CA  A THR   A 13  ? 0.1282 0.1334 0.2079 -0.0116 0.0238  0.0151  13  THR   A CA  
293  C  CA  B THR   A 13  ? 0.1376 0.1422 0.1860 -0.0152 0.0305  0.0081  13  THR   A CA  
294  C  C   A THR   A 13  ? 0.1321 0.1399 0.2157 -0.0130 0.0133  0.0353  13  THR   A C   
295  C  C   B THR   A 13  ? 0.1456 0.1517 0.1888 -0.0186 0.0286  0.0220  13  THR   A C   
296  O  O   A THR   A 13  ? 0.1347 0.1415 0.2086 -0.0122 0.0105  0.0318  13  THR   A O   
297  O  O   B THR   A 13  ? 0.1527 0.1532 0.1841 -0.0189 0.0185  0.0362  13  THR   A O   
298  C  CB  A THR   A 13  ? 0.1385 0.1460 0.2241 -0.0072 0.0265  0.0180  13  THR   A CB  
299  C  CB  B THR   A 13  ? 0.1354 0.1490 0.1901 -0.0091 0.0351  0.0108  13  THR   A CB  
300  O  OG1 A THR   A 13  ? 0.1427 0.1356 0.2378 -0.0073 0.0139  0.0185  13  THR   A OG1 
301  O  OG1 B THR   A 13  ? 0.1241 0.1494 0.1989 -0.0186 0.0480  0.0301  13  THR   A OG1 
302  C  CG2 A THR   A 13  ? 0.1521 0.1589 0.2392 0.0009  0.0317  0.0086  13  THR   A CG2 
303  C  CG2 B THR   A 13  ? 0.1417 0.1554 0.1954 0.0034  0.0321  0.0048  13  THR   A CG2 
318  N  N   A ASP   A 14  ? 0.1344 0.1476 0.2378 -0.0173 0.0071  0.0563  14  ASP   A N   
319  N  N   B ASP   A 14  ? 0.1479 0.1583 0.2056 -0.0254 0.0272  0.0315  14  ASP   A N   
320  C  CA  A ASP   A 14  ? 0.1398 0.1583 0.2579 -0.0154 -0.0062 0.0658  14  ASP   A CA  
321  C  CA  B ASP   A 14  ? 0.1621 0.1660 0.2208 -0.0231 0.0073  0.0423  14  ASP   A CA  
322  C  C   A ASP   A 14  ? 0.1451 0.1628 0.2330 -0.0190 -0.0130 0.0644  14  ASP   A C   
323  C  C   B ASP   A 14  ? 0.1532 0.1583 0.2111 -0.0299 -0.0086 0.0574  14  ASP   A C   
324  O  O   A ASP   A 14  ? 0.1588 0.1749 0.2428 -0.0169 -0.0086 0.0691  14  ASP   A O   
325  O  O   B ASP   A 14  ? 0.1560 0.1510 0.2057 -0.0295 -0.0206 0.0688  14  ASP   A O   
326  C  CB  A ASP   A 14  ? 0.1529 0.1699 0.3115 -0.0270 -0.0028 0.0844  14  ASP   A CB  
327  C  CB  B ASP   A 14  ? 0.1860 0.1812 0.2570 -0.0151 -0.0023 0.0389  14  ASP   A CB  
328  C  CG  A ASP   A 14  ? 0.1761 0.1987 0.3837 -0.0273 0.0102  0.0661  14  ASP   A CG  
329  C  CG  B ASP   A 14  ? 0.2087 0.2085 0.2949 -0.0081 -0.0047 0.0234  14  ASP   A CG  
330  O  OD1 A ASP   A 14  ? 0.1897 0.1975 0.4022 -0.0313 0.0065  0.0782  14  ASP   A OD1 
331  O  OD1 B ASP   A 14  ? 0.2234 0.2161 0.3051 -0.0049 -0.0153 0.0250  14  ASP   A OD1 
332  O  OD2 A ASP   A 14  ? 0.1985 0.2164 0.4087 -0.0364 -0.0013 0.0449  14  ASP   A OD2 
333  O  OD2 B ASP   A 14  ? 0.2179 0.2191 0.3110 -0.0075 -0.0073 0.0130  14  ASP   A OD2 
342  N  N   . ASN   A 15  ? 0.1436 0.1557 0.2243 -0.0295 -0.0075 0.0651  15  ASN   A N   
343  C  CA  . ASN   A 15  ? 0.1465 0.1579 0.2390 -0.0247 -0.0109 0.0559  15  ASN   A CA  
344  C  C   . ASN   A 15  ? 0.1400 0.1555 0.2469 -0.0264 -0.0047 0.0491  15  ASN   A C   
345  O  O   . ASN   A 15  ? 0.1460 0.1559 0.3011 -0.0225 -0.0247 0.0544  15  ASN   A O   
346  C  CB  . ASN   A 15  ? 0.1428 0.1610 0.2344 -0.0162 -0.0028 0.0525  15  ASN   A CB  
347  C  CG  . ASN   A 15  ? 0.1397 0.1683 0.2480 -0.0141 0.0065  0.0370  15  ASN   A CG  
348  O  OD1 . ASN   A 15  ? 0.1561 0.1719 0.2613 -0.0264 -0.0024 0.0432  15  ASN   A OD1 
349  N  ND2 . ASN   A 15  ? 0.1426 0.1774 0.2330 -0.0166 0.0125  0.0363  15  ASN   A ND2 
357  N  N   A VAL   A 16  ? 0.1399 0.1482 0.2215 -0.0252 0.0059  0.0473  16  VAL   A N   
358  N  N   B VAL   A 16  ? 0.1336 0.1536 0.2093 -0.0200 0.0048  0.0497  16  VAL   A N   
359  C  CA  A VAL   A 16  ? 0.1375 0.1514 0.2049 -0.0201 0.0099  0.0310  16  VAL   A CA  
360  C  CA  B VAL   A 16  ? 0.1339 0.1500 0.1683 -0.0119 0.0082  0.0446  16  VAL   A CA  
361  C  C   A VAL   A 16  ? 0.1303 0.1496 0.1826 -0.0267 0.0013  0.0219  16  VAL   A C   
362  C  C   B VAL   A 16  ? 0.1314 0.1591 0.1521 -0.0162 0.0056  0.0387  16  VAL   A C   
363  O  O   A VAL   A 16  ? 0.1279 0.1457 0.1570 -0.0316 0.0072  0.0209  16  VAL   A O   
364  O  O   B VAL   A 16  ? 0.1313 0.1670 0.1353 -0.0189 0.0086  0.0358  16  VAL   A O   
365  C  CB  A VAL   A 16  ? 0.1501 0.1565 0.2053 -0.0029 0.0293  0.0272  16  VAL   A CB  
366  C  CB  B VAL   A 16  ? 0.1445 0.1383 0.1566 0.0062  0.0168  0.0337  16  VAL   A CB  
367  C  CG1 A VAL   A 16  ? 0.1621 0.1635 0.2043 -0.0030 0.0246  0.0226  16  VAL   A CG1 
368  C  CG1 B VAL   A 16  ? 0.1521 0.1327 0.1497 0.0091  0.0196  0.0237  16  VAL   A CG1 
369  C  CG2 A VAL   A 16  ? 0.1567 0.1664 0.2105 0.0009  0.0496  0.0211  16  VAL   A CG2 
370  C  CG2 B VAL   A 16  ? 0.1478 0.1453 0.1700 0.0154  0.0345  0.0333  16  VAL   A CG2 
389  N  N   A TYR   A 17  ? 0.1308 0.1374 0.1855 -0.0165 0.0129  0.0310  17  TYR   A N   
390  N  N   B TYR   A 17  ? 0.1355 0.1531 0.1549 -0.0164 0.0048  0.0360  17  TYR   A N   
391  C  CA  A TYR   A 17  ? 0.1390 0.1417 0.1680 -0.0228 0.0090  0.0281  17  TYR   A CA  
392  C  CA  B TYR   A 17  ? 0.1344 0.1513 0.1451 -0.0206 -0.0030 0.0304  17  TYR   A CA  
393  C  C   A TYR   A 17  ? 0.1425 0.1324 0.1753 -0.0203 0.0069  0.0169  17  TYR   A C   
394  C  C   B TYR   A 17  ? 0.1251 0.1463 0.1341 -0.0224 0.0032  0.0289  17  TYR   A C   
395  O  O   A TYR   A 17  ? 0.1307 0.1269 0.1756 -0.0236 0.0155  0.0212  17  TYR   A O   
396  O  O   B TYR   A 17  ? 0.1167 0.1519 0.1262 -0.0243 0.0019  0.0305  17  TYR   A O   
397  C  CB  A TYR   A 17  ? 0.1522 0.1489 0.1727 -0.0336 -0.0059 0.0350  17  TYR   A CB  
398  C  CB  B TYR   A 17  ? 0.1493 0.1551 0.1609 -0.0237 -0.0096 0.0334  17  TYR   A CB  
399  C  CG  A TYR   A 17  ? 0.1786 0.1616 0.2010 -0.0425 -0.0252 0.0402  17  TYR   A CG  
400  C  CG  B TYR   A 17  ? 0.1657 0.1628 0.1783 -0.0259 -0.0237 0.0282  17  TYR   A CG  
401  C  CD1 A TYR   A 17  ? 0.1877 0.1683 0.2226 -0.0395 -0.0278 0.0357  17  TYR   A CD1 
402  C  CD1 B TYR   A 17  ? 0.1771 0.1669 0.1904 -0.0147 -0.0260 0.0320  17  TYR   A CD1 
403  C  CD2 A TYR   A 17  ? 0.1918 0.1642 0.1928 -0.0550 -0.0270 0.0606  17  TYR   A CD2 
404  C  CD2 B TYR   A 17  ? 0.1720 0.1711 0.1788 -0.0283 -0.0236 0.0319  17  TYR   A CD2 
405  C  CE1 A TYR   A 17  ? 0.1934 0.1689 0.2308 -0.0437 -0.0364 0.0400  17  TYR   A CE1 
406  C  CE1 B TYR   A 17  ? 0.1827 0.1701 0.2004 -0.0148 -0.0230 0.0397  17  TYR   A CE1 
407  C  CE2 A TYR   A 17  ? 0.2019 0.1651 0.2158 -0.0529 -0.0401 0.0456  17  TYR   A CE2 
408  C  CE2 B TYR   A 17  ? 0.1811 0.1742 0.1905 -0.0199 -0.0254 0.0334  17  TYR   A CE2 
409  C  CZ  A TYR   A 17  ? 0.2002 0.1649 0.2277 -0.0496 -0.0417 0.0450  17  TYR   A CZ  
410  C  CZ  B TYR   A 17  ? 0.1818 0.1738 0.1945 -0.0164 -0.0283 0.0423  17  TYR   A CZ  
411  O  OH  A TYR   A 17  ? 0.2115 0.1644 0.2321 -0.0385 -0.0384 0.0412  17  TYR   A OH  
412  O  OH  B TYR   A 17  ? 0.1836 0.1784 0.2061 -0.0090 -0.0264 0.0504  17  TYR   A OH  
431  N  N   A ILE   A 18  ? 0.1478 0.1395 0.1670 -0.0187 0.0151  0.0295  18  ILE   A N   
432  N  N   B ILE   A 18  ? 0.1173 0.1438 0.1326 -0.0226 0.0152  0.0303  18  ILE   A N   
433  C  CA  A ILE   A 18  ? 0.1474 0.1370 0.1581 -0.0130 0.0195  0.0221  18  ILE   A CA  
434  C  CA  B ILE   A 18  ? 0.1201 0.1408 0.1247 -0.0125 0.0245  0.0150  18  ILE   A CA  
435  C  C   A ILE   A 18  ? 0.1479 0.1409 0.1708 -0.0230 0.0231  0.0135  18  ILE   A C   
436  C  C   B ILE   A 18  ? 0.1205 0.1483 0.1174 -0.0170 0.0166  0.0106  18  ILE   A C   
437  O  O   A ILE   A 18  ? 0.1437 0.1534 0.1797 -0.0298 0.0291  0.0178  18  ILE   A O   
438  O  O   B ILE   A 18  ? 0.1233 0.1550 0.1347 -0.0237 0.0232  0.0027  18  ILE   A O   
439  C  CB  A ILE   A 18  ? 0.1463 0.1357 0.1471 0.0011  0.0209  0.0233  18  ILE   A CB  
440  C  CB  B ILE   A 18  ? 0.1290 0.1307 0.1151 -0.0070 0.0369  0.0142  18  ILE   A CB  
441  C  CG1 A ILE   A 18  ? 0.1543 0.1414 0.1478 0.0171  0.0062  0.0196  18  ILE   A CG1 
442  C  CG1 B ILE   A 18  ? 0.1467 0.1404 0.1228 -0.0113 0.0480  0.0092  18  ILE   A CG1 
443  C  CG2 A ILE   A 18  ? 0.1481 0.1382 0.1517 0.0064  0.0129  0.0101  18  ILE   A CG2 
444  C  CG2 B ILE   A 18  ? 0.1455 0.1374 0.1222 -0.0111 0.0441  0.0179  18  ILE   A CG2 
445  C  CD1 A ILE   A 18  ? 0.1766 0.1531 0.1593 0.0268  0.0078  0.0197  18  ILE   A CD1 
446  C  CD1 B ILE   A 18  ? 0.1597 0.1541 0.1418 -0.0046 0.0540  -0.0006 18  ILE   A CD1 
469  N  N   A LYS   A 19  ? 0.1548 0.1480 0.1735 -0.0224 0.0222  0.0065  19  LYS   A N   
470  N  N   B LYS   A 19  ? 0.1302 0.1509 0.1128 -0.0103 0.0335  0.0088  19  LYS   A N   
471  C  CA  A LYS   A 19  ? 0.1621 0.1600 0.1686 -0.0218 0.0253  0.0105  19  LYS   A CA  
472  C  CA  B LYS   A 19  ? 0.1454 0.1580 0.1302 -0.0070 0.0421  0.0087  19  LYS   A CA  
473  C  C   A LYS   A 19  ? 0.1485 0.1581 0.1949 -0.0101 0.0294  0.0216  19  LYS   A C   
474  C  C   B LYS   A 19  ? 0.1486 0.1574 0.1584 -0.0007 0.0335  0.0118  19  LYS   A C   
475  O  O   A LYS   A 19  ? 0.1403 0.1585 0.1956 -0.0057 0.0258  0.0297  19  LYS   A O   
476  O  O   B LYS   A 19  ? 0.1457 0.1533 0.1651 -0.0028 0.0293  0.0149  19  LYS   A O   
477  C  CB  A LYS   A 19  ? 0.1883 0.1814 0.1799 -0.0235 0.0226  0.0045  19  LYS   A CB  
478  C  CB  B LYS   A 19  ? 0.1578 0.1625 0.1372 -0.0092 0.0502  -0.0036 19  LYS   A CB  
479  C  CG  A LYS   A 19  ? 0.2137 0.1941 0.1993 -0.0248 0.0257  -0.0057 19  LYS   A CG  
480  C  CG  B LYS   A 19  ? 0.1862 0.1811 0.1481 -0.0042 0.0514  -0.0139 19  LYS   A CG  
481  C  CD  A LYS   A 19  ? 0.2337 0.2030 0.2167 -0.0264 0.0346  -0.0161 19  LYS   A CD  
482  C  CD  B LYS   A 19  ? 0.2117 0.1931 0.1670 -0.0056 0.0537  -0.0149 19  LYS   A CD  
483  C  CE  A LYS   A 19  ? 0.2493 0.2064 0.2287 -0.0286 0.0421  -0.0239 19  LYS   A CE  
484  C  CE  B LYS   A 19  ? 0.2271 0.2036 0.1813 -0.0075 0.0496  -0.0178 19  LYS   A CE  
485  N  NZ  A LYS   A 19  ? 0.2577 0.2072 0.2349 -0.0351 0.0553  -0.0276 19  LYS   A NZ  
486  N  NZ  B LYS   A 19  ? 0.2342 0.2072 0.1939 -0.0086 0.0491  -0.0248 19  LYS   A NZ  
513  N  N   A ASN   A 20  ? 0.1530 0.1638 0.2193 -0.0160 0.0276  0.0319  20  ASN   A N   
514  N  N   B ASN   A 20  ? 0.1638 0.1700 0.1792 0.0083  0.0339  0.0151  20  ASN   A N   
515  C  CA  A ASN   A 20  ? 0.1655 0.1794 0.2431 0.0020  0.0448  0.0343  20  ASN   A CA  
516  C  CA  B ASN   A 20  ? 0.1775 0.1845 0.2037 0.0180  0.0403  0.0149  20  ASN   A CA  
517  C  C   A ASN   A 20  ? 0.1871 0.1806 0.2501 -0.0068 0.0600  0.0271  20  ASN   A C   
518  C  C   B ASN   A 20  ? 0.1886 0.1881 0.2105 0.0128  0.0604  0.0080  20  ASN   A C   
519  O  O   A ASN   A 20  ? 0.2061 0.1813 0.2607 -0.0175 0.0646  0.0209  20  ASN   A O   
520  O  O   B ASN   A 20  ? 0.1971 0.1882 0.2273 0.0132  0.0638  0.0027  20  ASN   A O   
521  C  CB  A ASN   A 20  ? 0.1741 0.1980 0.2605 0.0166  0.0521  0.0509  20  ASN   A CB  
522  C  CB  B ASN   A 20  ? 0.1893 0.1983 0.2273 0.0293  0.0302  0.0261  20  ASN   A CB  
523  C  CG  A ASN   A 20  ? 0.1845 0.2074 0.2793 0.0303  0.0707  0.0584  20  ASN   A CG  
524  C  CG  B ASN   A 20  ? 0.2019 0.2080 0.2545 0.0424  0.0246  0.0296  20  ASN   A CG  
525  O  OD1 A ASN   A 20  ? 0.2163 0.2137 0.3073 0.0454  0.0865  0.0452  20  ASN   A OD1 
526  O  OD1 B ASN   A 20  ? 0.2281 0.2212 0.2826 0.0375  0.0277  0.0178  20  ASN   A OD1 
527  N  ND2 A ASN   A 20  ? 0.1821 0.2098 0.2952 0.0274  0.0583  0.0731  20  ASN   A ND2 
528  N  ND2 B ASN   A 20  ? 0.1997 0.2040 0.2554 0.0562  0.0110  0.0447  20  ASN   A ND2 
541  N  N   A ALA   A 21  ? 0.1897 0.1832 0.2409 -0.0027 0.0524  0.0162  21  ALA   A N   
542  N  N   B ALA   A 21  ? 0.1940 0.1933 0.2128 0.0125  0.0543  0.0025  21  ALA   A N   
543  C  CA  A ALA   A 21  ? 0.1913 0.1792 0.2365 -0.0099 0.0413  0.0225  21  ALA   A CA  
544  C  CA  B ALA   A 21  ? 0.1992 0.1961 0.2161 0.0064  0.0524  0.0055  21  ALA   A CA  
545  C  C   A ALA   A 21  ? 0.1788 0.1834 0.2359 -0.0115 0.0363  0.0292  21  ALA   A C   
546  C  C   B ALA   A 21  ? 0.1883 0.1940 0.2059 0.0059  0.0652  0.0122  21  ALA   A C   
547  O  O   A ALA   A 21  ? 0.1749 0.1888 0.2477 -0.0052 0.0293  0.0345  21  ALA   A O   
548  O  O   B ALA   A 21  ? 0.1859 0.1907 0.2202 0.0135  0.0652  0.0106  21  ALA   A O   
549  C  CB  A ALA   A 21  ? 0.2006 0.1746 0.2378 -0.0158 0.0367  0.0302  21  ALA   A CB  
550  C  CB  B ALA   A 21  ? 0.2082 0.1963 0.2356 0.0046  0.0422  0.0041  21  ALA   A CB  
561  N  N   A ASP   A 22  ? 0.1763 0.1764 0.2424 -0.0174 0.0364  0.0353  22  ASP   A N   
562  N  N   B ASP   A 22  ? 0.1857 0.1921 0.2009 -0.0003 0.0677  0.0206  22  ASP   A N   
563  C  CA  A ASP   A 22  ? 0.1777 0.1782 0.2372 -0.0105 0.0306  0.0418  22  ASP   A CA  
564  C  CA  B ASP   A 22  ? 0.1857 0.1880 0.2057 -0.0040 0.0610  0.0338  22  ASP   A CA  
565  C  C   A ASP   A 22  ? 0.1660 0.1766 0.1990 -0.0064 0.0284  0.0274  22  ASP   A C   
566  C  C   B ASP   A 22  ? 0.1699 0.1820 0.1824 -0.0175 0.0630  0.0280  22  ASP   A C   
567  O  O   A ASP   A 22  ? 0.1702 0.1832 0.2086 -0.0100 0.0251  0.0192  22  ASP   A O   
568  O  O   B ASP   A 22  ? 0.1686 0.1851 0.1880 -0.0238 0.0618  0.0082  22  ASP   A O   
569  C  CB  A ASP   A 22  ? 0.1928 0.1810 0.2886 -0.0144 0.0169  0.0348  22  ASP   A CB  
570  C  CB  B ASP   A 22  ? 0.2059 0.1942 0.2392 0.0070  0.0513  0.0298  22  ASP   A CB  
571  C  CG  A ASP   A 22  ? 0.2150 0.1904 0.3412 -0.0173 -0.0093 0.0382  22  ASP   A CG  
572  C  CG  B ASP   A 22  ? 0.2169 0.1965 0.2643 0.0111  0.0437  0.0355  22  ASP   A CG  
573  O  OD1 A ASP   A 22  ? 0.2127 0.1934 0.3614 -0.0344 -0.0184 0.0477  22  ASP   A OD1 
574  O  OD1 B ASP   A 22  ? 0.2192 0.1963 0.2582 0.0082  0.0455  0.0355  22  ASP   A OD1 
575  O  OD2 A ASP   A 22  ? 0.2410 0.1977 0.3705 -0.0066 -0.0176 0.0313  22  ASP   A OD2 
576  O  OD2 B ASP   A 22  ? 0.2209 0.2022 0.2842 0.0123  0.0414  0.0337  22  ASP   A OD2 
585  N  N   A ILE   A 23  ? 0.1643 0.1704 0.1884 -0.0004 0.0325  0.0190  23  ILE   A N   
586  N  N   B ILE   A 23  ? 0.1639 0.1737 0.1758 -0.0151 0.0559  0.0238  23  ILE   A N   
587  C  CA  A ILE   A 23  ? 0.1658 0.1609 0.1783 -0.0040 0.0327  0.0185  23  ILE   A CA  
588  C  CA  B ILE   A 23  ? 0.1585 0.1728 0.1535 -0.0181 0.0442  0.0217  23  ILE   A CA  
589  C  C   A ILE   A 23  ? 0.1634 0.1720 0.1807 -0.0067 0.0447  0.0140  23  ILE   A C   
590  C  C   B ILE   A 23  ? 0.1663 0.1778 0.1580 -0.0285 0.0391  0.0068  23  ILE   A C   
591  O  O   A ILE   A 23  ? 0.1706 0.1835 0.1896 -0.0091 0.0402  0.0011  23  ILE   A O   
592  O  O   B ILE   A 23  ? 0.1684 0.1740 0.1565 -0.0247 0.0322  0.0009  23  ILE   A O   
593  C  CB  A ILE   A 23  ? 0.1798 0.1591 0.1710 0.0021  0.0322  0.0118  23  ILE   A CB  
594  C  CB  B ILE   A 23  ? 0.1565 0.1675 0.1418 -0.0066 0.0282  0.0286  23  ILE   A CB  
595  C  CG1 A ILE   A 23  ? 0.1817 0.1560 0.1749 0.0051  0.0258  0.0086  23  ILE   A CG1 
596  C  CG1 B ILE   A 23  ? 0.1577 0.1645 0.1406 -0.0055 0.0122  0.0248  23  ILE   A CG1 
597  C  CG2 A ILE   A 23  ? 0.1889 0.1657 0.1705 0.0089  0.0368  0.0252  23  ILE   A CG2 
598  C  CG2 B ILE   A 23  ? 0.1599 0.1656 0.1430 0.0059  0.0167  0.0270  23  ILE   A CG2 
599  C  CD1 A ILE   A 23  ? 0.1842 0.1552 0.1791 0.0022  0.0088  0.0090  23  ILE   A CD1 
600  C  CD1 B ILE   A 23  ? 0.1560 0.1616 0.1432 -0.0030 0.0002  0.0197  23  ILE   A CD1 
623  N  N   A VAL   A 24  ? 0.1715 0.1754 0.1890 -0.0146 0.0457  0.0145  24  VAL   A N   
624  N  N   B VAL   A 24  ? 0.1801 0.1868 0.1743 -0.0404 0.0407  0.0009  24  VAL   A N   
625  C  CA  A VAL   A 24  ? 0.1894 0.1882 0.2100 -0.0187 0.0418  0.0005  24  VAL   A CA  
626  C  CA  B VAL   A 24  ? 0.2007 0.1963 0.2016 -0.0448 0.0412  -0.0043 24  VAL   A CA  
627  C  C   A VAL   A 24  ? 0.1963 0.2101 0.2093 -0.0316 0.0393  -0.0037 24  VAL   A C   
628  C  C   B VAL   A 24  ? 0.2081 0.2145 0.2107 -0.0453 0.0411  -0.0187 24  VAL   A C   
629  O  O   A VAL   A 24  ? 0.2081 0.2175 0.2207 -0.0339 0.0432  -0.0028 24  VAL   A O   
630  O  O   B VAL   A 24  ? 0.2150 0.2200 0.2261 -0.0413 0.0440  -0.0139 24  VAL   A O   
631  C  CB  A VAL   A 24  ? 0.1956 0.1858 0.2338 -0.0114 0.0444  0.0051  24  VAL   A CB  
632  C  CB  B VAL   A 24  ? 0.2094 0.1946 0.2307 -0.0463 0.0405  0.0048  24  VAL   A CB  
633  C  CG1 A VAL   A 24  ? 0.1989 0.1919 0.2400 -0.0045 0.0455  -0.0037 24  VAL   A CG1 
634  C  CG1 B VAL   A 24  ? 0.2182 0.2002 0.2464 -0.0416 0.0340  0.0023  24  VAL   A CG1 
635  C  CG2 A VAL   A 24  ? 0.2117 0.1912 0.2386 -0.0108 0.0561  0.0201  24  VAL   A CG2 
636  C  CG2 B VAL   A 24  ? 0.2144 0.1916 0.2275 -0.0472 0.0466  0.0119  24  VAL   A CG2 
655  N  N   A GLU   A 25  ? 0.1976 0.2313 0.2024 -0.0432 0.0516  -0.0129 25  GLU   A N   
656  N  N   B GLU   A 25  ? 0.2091 0.2285 0.2138 -0.0493 0.0502  -0.0281 25  GLU   A N   
657  C  CA  A GLU   A 25  ? 0.2117 0.2574 0.2072 -0.0280 0.0565  -0.0219 25  GLU   A CA  
658  C  CA  B GLU   A 25  ? 0.2158 0.2479 0.2195 -0.0561 0.0511  -0.0296 25  GLU   A CA  
659  C  C   A GLU   A 25  ? 0.1992 0.2620 0.1822 -0.0422 0.0595  -0.0206 25  GLU   A C   
660  C  C   B GLU   A 25  ? 0.2142 0.2584 0.2034 -0.0525 0.0557  -0.0282 25  GLU   A C   
661  O  O   A GLU   A 25  ? 0.2007 0.2735 0.2037 -0.0445 0.0572  -0.0175 25  GLU   A O   
662  O  O   B GLU   A 25  ? 0.2160 0.2613 0.2107 -0.0526 0.0617  -0.0346 25  GLU   A O   
663  C  CB  A GLU   A 25  ? 0.2352 0.2829 0.2512 -0.0162 0.0477  -0.0202 25  GLU   A CB  
664  C  CB  B GLU   A 25  ? 0.2243 0.2567 0.2487 -0.0613 0.0519  -0.0306 25  GLU   A CB  
665  C  CG  A GLU   A 25  ? 0.2648 0.3061 0.3117 -0.0162 0.0250  -0.0249 25  GLU   A CG  
666  C  CG  B GLU   A 25  ? 0.2396 0.2666 0.2953 -0.0638 0.0405  -0.0284 25  GLU   A CG  
667  C  CD  A GLU   A 25  ? 0.2859 0.3247 0.3637 -0.0198 0.0127  -0.0264 25  GLU   A CD  
668  C  CD  B GLU   A 25  ? 0.2483 0.2753 0.3427 -0.0652 0.0275  -0.0285 25  GLU   A CD  
669  O  OE1 A GLU   A 25  ? 0.2948 0.3311 0.3756 -0.0193 0.0022  -0.0342 25  GLU   A OE1 
670  O  OE1 B GLU   A 25  ? 0.2510 0.2768 0.3633 -0.0656 0.0233  -0.0306 25  GLU   A OE1 
671  O  OE2 A GLU   A 25  ? 0.2908 0.3330 0.3962 -0.0226 0.0083  -0.0334 25  GLU   A OE2 
672  O  OE2 B GLU   A 25  ? 0.2569 0.2822 0.3581 -0.0606 0.0250  -0.0245 25  GLU   A OE2 
685  N  N   A GLU   A 26  ? 0.1896 0.2549 0.1868 -0.0590 0.0601  -0.0215 26  GLU   A N   
686  N  N   B GLU   A 26  ? 0.2098 0.2633 0.1914 -0.0512 0.0574  -0.0257 26  GLU   A N   
687  C  CA  A GLU   A 26  ? 0.1980 0.2557 0.1802 -0.0718 0.0609  -0.0115 26  GLU   A CA  
688  C  CA  B GLU   A 26  ? 0.2167 0.2717 0.1811 -0.0447 0.0544  -0.0192 26  GLU   A CA  
689  C  C   A GLU   A 26  ? 0.1965 0.2506 0.1587 -0.0710 0.0579  -0.0079 26  GLU   A C   
690  C  C   B GLU   A 26  ? 0.2174 0.2655 0.1707 -0.0409 0.0491  -0.0144 26  GLU   A C   
691  O  O   A GLU   A 26  ? 0.2076 0.2519 0.1475 -0.0750 0.0641  -0.0092 26  GLU   A O   
692  O  O   B GLU   A 26  ? 0.2188 0.2612 0.1635 -0.0445 0.0533  -0.0157 26  GLU   A O   
693  C  CB  A GLU   A 26  ? 0.2175 0.2573 0.2096 -0.0820 0.0598  -0.0019 26  GLU   A CB  
694  C  CB  B GLU   A 26  ? 0.2252 0.2836 0.1904 -0.0452 0.0430  -0.0177 26  GLU   A CB  
695  C  CG  A GLU   A 26  ? 0.2465 0.2769 0.2744 -0.0856 0.0492  -0.0167 26  GLU   A CG  
696  C  CG  B GLU   A 26  ? 0.2328 0.2930 0.1968 -0.0485 0.0411  -0.0191 26  GLU   A CG  
697  C  CD  A GLU   A 26  ? 0.2618 0.2877 0.3160 -0.0998 0.0563  -0.0249 26  GLU   A CD  
698  C  CD  B GLU   A 26  ? 0.2371 0.3001 0.1867 -0.0586 0.0447  -0.0168 26  GLU   A CD  
699  O  OE1 A GLU   A 26  ? 0.2575 0.3049 0.3126 -0.0997 0.0737  -0.0559 26  GLU   A OE1 
700  O  OE1 B GLU   A 26  ? 0.2430 0.3114 0.1806 -0.0546 0.0511  -0.0202 26  GLU   A OE1 
701  O  OE2 A GLU   A 26  ? 0.2785 0.2933 0.3264 -0.1022 0.0484  -0.0153 26  GLU   A OE2 
702  O  OE2 B GLU   A 26  ? 0.2336 0.2985 0.1544 -0.0698 0.0548  -0.0133 26  GLU   A OE2 
715  N  N   A ALA   A 27  ? 0.1837 0.2409 0.1594 -0.0731 0.0516  0.0026  27  ALA   A N   
716  N  N   B ALA   A 27  ? 0.2147 0.2642 0.1693 -0.0343 0.0418  -0.0044 27  ALA   A N   
717  C  CA  A ALA   A 27  ? 0.1931 0.2505 0.1528 -0.0685 0.0491  0.0014  27  ALA   A CA  
718  C  CA  B ALA   A 27  ? 0.2217 0.2712 0.1660 -0.0280 0.0349  0.0002  27  ALA   A CA  
719  C  C   A ALA   A 27  ? 0.2231 0.2673 0.1664 -0.0814 0.0517  -0.0112 27  ALA   A C   
720  C  C   B ALA   A 27  ? 0.2404 0.2881 0.1861 -0.0231 0.0275  -0.0061 27  ALA   A C   
721  O  O   A ALA   A 27  ? 0.2313 0.2625 0.1740 -0.0846 0.0383  -0.0036 27  ALA   A O   
722  O  O   B ALA   A 27  ? 0.2367 0.2852 0.1883 -0.0206 0.0200  -0.0035 27  ALA   A O   
723  C  CB  A ALA   A 27  ? 0.1747 0.2411 0.1623 -0.0652 0.0329  -0.0040 27  ALA   A CB  
724  C  CB  B ALA   A 27  ? 0.2121 0.2655 0.1561 -0.0313 0.0338  0.0013  27  ALA   A CB  
735  N  N   A LYS   A 28  ? 0.2579 0.2971 0.1883 -0.0798 0.0411  -0.0437 28  LYS   A N   
736  N  N   B LYS   A 28  ? 0.2673 0.3086 0.2135 -0.0191 0.0195  -0.0200 28  LYS   A N   
737  C  CA  A LYS   A 28  ? 0.2983 0.3328 0.2213 -0.0711 0.0432  -0.0577 28  LYS   A CA  
738  C  CA  B LYS   A 28  ? 0.2964 0.3306 0.2488 -0.0134 0.0140  -0.0293 28  LYS   A CA  
739  C  C   A LYS   A 28  ? 0.3126 0.3590 0.2157 -0.0753 0.0631  -0.0447 28  LYS   A C   
740  C  C   B LYS   A 28  ? 0.3135 0.3479 0.2525 -0.0171 0.0182  -0.0240 28  LYS   A C   
741  O  O   A LYS   A 28  ? 0.3158 0.3668 0.2421 -0.0730 0.0469  -0.0423 28  LYS   A O   
742  O  O   B LYS   A 28  ? 0.3158 0.3510 0.2595 -0.0158 0.0114  -0.0240 28  LYS   A O   
743  C  CB  A LYS   A 28  ? 0.3200 0.3453 0.2796 -0.0557 0.0337  -0.0672 28  LYS   A CB  
744  C  CB  B LYS   A 28  ? 0.3094 0.3369 0.2873 -0.0044 0.0079  -0.0371 28  LYS   A CB  
745  C  CG  A LYS   A 28  ? 0.3381 0.3552 0.3417 -0.0408 0.0292  -0.0733 28  LYS   A CG  
746  C  CG  B LYS   A 28  ? 0.3227 0.3427 0.3334 0.0026  0.0051  -0.0404 28  LYS   A CG  
747  C  CD  A LYS   A 28  ? 0.3547 0.3685 0.4024 -0.0289 0.0212  -0.0787 28  LYS   A CD  
748  C  CD  B LYS   A 28  ? 0.3344 0.3516 0.3779 0.0074  0.0009  -0.0432 28  LYS   A CD  
749  C  CE  A LYS   A 28  ? 0.3657 0.3768 0.4538 -0.0217 0.0133  -0.0817 28  LYS   A CE  
750  C  CE  B LYS   A 28  ? 0.3428 0.3583 0.4179 0.0088  -0.0030 -0.0449 28  LYS   A CE  
751  N  NZ  A LYS   A 28  ? 0.3738 0.3812 0.4791 -0.0164 0.0109  -0.0784 28  LYS   A NZ  
752  N  NZ  B LYS   A 28  ? 0.3474 0.3619 0.4367 0.0111  -0.0046 -0.0454 28  LYS   A NZ  
779  N  N   A LYS   A 29  ? 0.3200 0.3775 0.2064 -0.0847 0.0956  -0.0226 29  LYS   A N   
780  N  N   B LYS   A 29  ? 0.3267 0.3616 0.2609 -0.0238 0.0301  -0.0140 29  LYS   A N   
781  C  CA  A LYS   A 29  ? 0.3390 0.4003 0.2339 -0.0870 0.1061  -0.0069 29  LYS   A CA  
782  C  CA  B LYS   A 29  ? 0.3427 0.3756 0.2820 -0.0294 0.0362  -0.0046 29  LYS   A CA  
783  C  C   A LYS   A 29  ? 0.3442 0.3941 0.2124 -0.0956 0.0918  0.0023  29  LYS   A C   
784  C  C   B LYS   A 29  ? 0.3465 0.3711 0.2649 -0.0396 0.0301  0.0030  29  LYS   A C   
785  O  O   A LYS   A 29  ? 0.3533 0.4019 0.2274 -0.0870 0.0846  -0.0044 29  LYS   A O   
786  O  O   B LYS   A 29  ? 0.3495 0.3742 0.2669 -0.0395 0.0296  0.0023  29  LYS   A O   
787  C  CB  A LYS   A 29  ? 0.3527 0.4272 0.2950 -0.0759 0.1140  -0.0043 29  LYS   A CB  
788  C  CB  B LYS   A 29  ? 0.3537 0.3912 0.3321 -0.0231 0.0424  -0.0025 29  LYS   A CB  
789  C  CG  A LYS   A 29  ? 0.3691 0.4483 0.3632 -0.0640 0.1130  -0.0046 29  LYS   A CG  
790  C  CG  B LYS   A 29  ? 0.3646 0.4030 0.3785 -0.0164 0.0466  -0.0021 29  LYS   A CG  
791  C  CD  A LYS   A 29  ? 0.3823 0.4633 0.4224 -0.0550 0.1112  -0.0056 29  LYS   A CD  
792  C  CD  B LYS   A 29  ? 0.3723 0.4113 0.4202 -0.0111 0.0491  -0.0004 29  LYS   A CD  
793  C  CE  A LYS   A 29  ? 0.3915 0.4727 0.4660 -0.0489 0.1092  -0.0045 29  LYS   A CE  
794  C  CE  B LYS   A 29  ? 0.3781 0.4177 0.4510 -0.0081 0.0506  0.0005  29  LYS   A CE  
795  N  NZ  A LYS   A 29  ? 0.3956 0.4780 0.4914 -0.0448 0.1049  -0.0053 29  LYS   A NZ  
796  N  NZ  B LYS   A 29  ? 0.3813 0.4211 0.4690 -0.0067 0.0497  0.0013  29  LYS   A NZ  
823  N  N   A VAL   A 30  ? 0.3347 0.3788 0.1931 -0.1131 0.0901  0.0149  30  VAL   A N   
824  N  N   B VAL   A 30  ? 0.3455 0.3628 0.2499 -0.0501 0.0282  0.0097  30  VAL   A N   
825  C  CA  A VAL   A 30  ? 0.3301 0.3611 0.1816 -0.1297 0.0597  0.0289  30  VAL   A CA  
826  C  CA  B VAL   A 30  ? 0.3441 0.3524 0.2368 -0.0606 0.0159  0.0197  30  VAL   A CA  
827  C  C   A VAL   A 30  ? 0.3301 0.3466 0.1528 -0.1278 0.0405  0.0419  30  VAL   A C   
828  C  C   B VAL   A 30  ? 0.3433 0.3450 0.2213 -0.0663 0.0070  0.0239  30  VAL   A C   
829  O  O   A VAL   A 30  ? 0.3377 0.3502 0.1627 -0.1266 0.0343  0.0391  30  VAL   A O   
830  O  O   B VAL   A 30  ? 0.3445 0.3458 0.2200 -0.0657 0.0061  0.0243  30  VAL   A O   
831  C  CB  A VAL   A 30  ? 0.3252 0.3521 0.2162 -0.1440 0.0392  0.0299  30  VAL   A CB  
832  C  CB  B VAL   A 30  ? 0.3426 0.3475 0.2505 -0.0650 0.0102  0.0237  30  VAL   A CB  
833  C  CG1 A VAL   A 30  ? 0.3315 0.3521 0.2345 -0.1443 0.0286  0.0322  30  VAL   A CG1 
834  C  CG1 B VAL   A 30  ? 0.3457 0.3477 0.2579 -0.0655 0.0073  0.0249  30  VAL   A CG1 
835  C  CG2 A VAL   A 30  ? 0.3200 0.3472 0.2307 -0.1524 0.0405  0.0317  30  VAL   A CG2 
836  C  CG2 B VAL   A 30  ? 0.3404 0.3441 0.2552 -0.0672 0.0106  0.0277  30  VAL   A CG2 
855  N  N   A LYS   A 31  ? 0.3238 0.3335 0.1371 -0.1316 0.0162  0.0400  31  LYS   A N   
856  N  N   B LYS   A 31  ? 0.3397 0.3360 0.2151 -0.0728 -0.0043 0.0253  31  LYS   A N   
857  C  CA  A LYS   A 31  ? 0.3323 0.3327 0.1648 -0.1110 -0.0107 0.0398  31  LYS   A CA  
858  C  CA  B LYS   A 31  ? 0.3385 0.3314 0.2226 -0.0734 -0.0174 0.0297  31  LYS   A CA  
859  C  C   A LYS   A 31  ? 0.3110 0.3156 0.1322 -0.0933 -0.0184 0.0664  31  LYS   A C   
860  C  C   B LYS   A 31  ? 0.3139 0.3109 0.1716 -0.0780 -0.0219 0.0520  31  LYS   A C   
861  O  O   A LYS   A 31  ? 0.3158 0.3279 0.1459 -0.0833 -0.0228 0.0751  31  LYS   A O   
862  O  O   B LYS   A 31  ? 0.3202 0.3169 0.1756 -0.0708 -0.0284 0.0612  31  LYS   A O   
863  C  CB  A LYS   A 31  ? 0.3638 0.3522 0.2659 -0.1008 -0.0248 0.0183  31  LYS   A CB  
864  C  CB  B LYS   A 31  ? 0.3596 0.3479 0.3002 -0.0676 -0.0240 0.0149  31  LYS   A CB  
865  C  CG  A LYS   A 31  ? 0.3968 0.3708 0.3813 -0.0855 -0.0394 0.0048  31  LYS   A CG  
866  C  CG  B LYS   A 31  ? 0.3796 0.3629 0.3818 -0.0595 -0.0315 0.0050  31  LYS   A CG  
867  C  CD  A LYS   A 31  ? 0.4240 0.3862 0.4675 -0.0739 -0.0555 -0.0098 31  LYS   A CD  
868  C  CD  B LYS   A 31  ? 0.3962 0.3744 0.4451 -0.0530 -0.0399 -0.0052 31  LYS   A CD  
869  C  CE  A LYS   A 31  ? 0.4419 0.3980 0.5297 -0.0656 -0.0664 -0.0184 31  LYS   A CE  
870  C  CE  B LYS   A 31  ? 0.4083 0.3823 0.4935 -0.0482 -0.0455 -0.0110 31  LYS   A CE  
871  N  NZ  A LYS   A 31  ? 0.4507 0.4038 0.5572 -0.0613 -0.0714 -0.0228 31  LYS   A NZ  
872  N  NZ  B LYS   A 31  ? 0.4156 0.3855 0.5147 -0.0454 -0.0479 -0.0139 31  LYS   A NZ  
899  N  N   . PRO   A 32  ? 0.2799 0.2851 0.1352 -0.0931 -0.0188 0.0564  32  PRO   A N   
900  C  CA  . PRO   A 32  ? 0.2609 0.2626 0.1574 -0.0850 -0.0271 0.0652  32  PRO   A CA  
901  C  C   . PRO   A 32  ? 0.2549 0.2562 0.1680 -0.0673 -0.0349 0.0727  32  PRO   A C   
902  O  O   . PRO   A 32  ? 0.2508 0.2484 0.1793 -0.0652 -0.0406 0.0708  32  PRO   A O   
903  C  CB  . PRO   A 32  ? 0.2479 0.2626 0.1644 -0.0863 -0.0253 0.0505  32  PRO   A CB  
904  C  CG  . PRO   A 32  ? 0.2459 0.2680 0.1268 -0.0814 -0.0429 0.0336  32  PRO   A CG  
905  C  CD  . PRO   A 32  ? 0.2534 0.2717 0.1199 -0.0898 -0.0354 0.0431  32  PRO   A CD  
913  N  N   . THR   A 33  ? 0.2627 0.2546 0.1525 -0.0619 -0.0338 0.0769  33  THR   A N   
914  C  CA  . THR   A 33  ? 0.2597 0.2512 0.1580 -0.0522 -0.0406 0.0831  33  THR   A CA  
915  C  C   . THR   A 33  ? 0.2250 0.2293 0.1547 -0.0520 -0.0430 0.0665  33  THR   A C   
916  O  O   . THR   A 33  ? 0.2211 0.2324 0.1642 -0.0540 -0.0494 0.0660  33  THR   A O   
917  C  CB  . THR   A 33  ? 0.2854 0.2752 0.1749 -0.0412 -0.0489 0.0970  33  THR   A CB  
918  O  OG1 . THR   A 33  ? 0.3073 0.2915 0.2094 -0.0259 -0.0473 0.1025  33  THR   A OG1 
919  C  CG2 . THR   A 33  ? 0.2889 0.2868 0.1954 -0.0327 -0.0531 0.0998  33  THR   A CG2 
927  N  N   . VAL   A 34  ? 0.1978 0.2111 0.1406 -0.0478 -0.0372 0.0623  34  VAL   A N   
928  C  CA  . VAL   A 34  ? 0.1811 0.1891 0.1390 -0.0379 -0.0223 0.0555  34  VAL   A CA  
929  C  C   . VAL   A 34  ? 0.1658 0.1783 0.1295 -0.0311 -0.0127 0.0363  34  VAL   A C   
930  O  O   . VAL   A 34  ? 0.1654 0.1793 0.1626 -0.0383 -0.0095 0.0411  34  VAL   A O   
931  C  CB  . VAL   A 34  ? 0.1819 0.1895 0.1632 -0.0372 -0.0154 0.0400  34  VAL   A CB  
932  C  CG1 . VAL   A 34  ? 0.1878 0.1871 0.1703 -0.0352 0.0005  0.0288  34  VAL   A CG1 
933  C  CG2 . VAL   A 34  ? 0.1913 0.2050 0.1803 -0.0315 -0.0222 0.0379  34  VAL   A CG2 
943  N  N   . VAL   A 35  ? 0.1547 0.1688 0.1246 -0.0346 -0.0162 0.0342  35  VAL   A N   
944  C  CA  . VAL   A 35  ? 0.1474 0.1632 0.1186 -0.0300 -0.0051 0.0276  35  VAL   A CA  
945  C  C   . VAL   A 35  ? 0.1345 0.1479 0.1310 -0.0196 -0.0007 0.0241  35  VAL   A C   
946  O  O   . VAL   A 35  ? 0.1311 0.1583 0.1406 -0.0223 0.0084  0.0229  35  VAL   A O   
947  C  CB  . VAL   A 35  ? 0.1513 0.1678 0.1439 -0.0187 0.0055  0.0110  35  VAL   A CB  
948  C  CG1 . VAL   A 35  ? 0.1671 0.1773 0.1445 -0.0124 0.0038  0.0090  35  VAL   A CG1 
949  C  CG2 . VAL   A 35  ? 0.1506 0.1684 0.1690 -0.0140 0.0106  0.0072  35  VAL   A CG2 
959  N  N   . VAL   A 36  ? 0.1223 0.1410 0.1210 -0.0209 0.0030  0.0250  36  VAL   A N   
960  C  CA  . VAL   A 36  ? 0.1227 0.1337 0.1198 -0.0117 0.0008  0.0176  36  VAL   A CA  
961  C  C   . VAL   A 36  ? 0.1184 0.1370 0.1346 -0.0195 0.0114  0.0198  36  VAL   A C   
962  O  O   . VAL   A 36  ? 0.1224 0.1335 0.1547 -0.0129 0.0149  0.0218  36  VAL   A O   
963  C  CB  . VAL   A 36  ? 0.1256 0.1235 0.1290 -0.0136 -0.0039 0.0192  36  VAL   A CB  
964  C  CG1 . VAL   A 36  ? 0.1332 0.1254 0.1538 -0.0172 0.0058  0.0083  36  VAL   A CG1 
965  C  CG2 . VAL   A 36  ? 0.1337 0.1357 0.1507 -0.0148 -0.0029 0.0231  36  VAL   A CG2 
975  N  N   . ASN   A 37  ? 0.1203 0.1209 0.1122 -0.0082 0.0048  0.0173  37  ASN   A N   
976  C  CA  . ASN   A 37  ? 0.1174 0.1178 0.1158 -0.0054 0.0070  0.0214  37  ASN   A CA  
977  C  C   . ASN   A 37  ? 0.1184 0.1202 0.1207 -0.0027 0.0098  0.0291  37  ASN   A C   
978  O  O   . ASN   A 37  ? 0.1307 0.1298 0.1157 0.0077  0.0116  0.0118  37  ASN   A O   
979  C  CB  . ASN   A 37  ? 0.1232 0.1239 0.1223 -0.0081 0.0028  0.0181  37  ASN   A CB  
980  C  CG  . ASN   A 37  ? 0.1206 0.1187 0.1380 -0.0064 0.0007  0.0124  37  ASN   A CG  
981  O  OD1 . ASN   A 37  ? 0.1157 0.1256 0.1526 -0.0023 0.0059  0.0170  37  ASN   A OD1 
982  N  ND2 . ASN   A 37  ? 0.1226 0.1196 0.1537 -0.0029 -0.0006 0.0235  37  ASN   A ND2 
989  N  N   A ALA   A 38  ? 0.1122 0.1258 0.1300 -0.0003 0.0105  0.0103  38  ALA   A N   
990  N  N   B ALA   A 38  ? 0.1219 0.1285 0.1274 -0.0054 0.0056  0.0202  38  ALA   A N   
991  C  CA  A ALA   A 38  ? 0.1216 0.1197 0.1305 -0.0012 0.0023  0.0042  38  ALA   A CA  
992  C  CA  B ALA   A 38  ? 0.1341 0.1317 0.1336 -0.0114 -0.0019 0.0187  38  ALA   A CA  
993  C  C   A ALA   A 38  ? 0.1172 0.1241 0.1236 -0.0003 -0.0014 -0.0000 38  ALA   A C   
994  C  C   B ALA   A 38  ? 0.1290 0.1324 0.1348 -0.0105 -0.0035 0.0155  38  ALA   A C   
995  O  O   A ALA   A 38  ? 0.1158 0.1127 0.1266 -0.0006 -0.0123 -0.0022 38  ALA   A O   
996  O  O   B ALA   A 38  ? 0.1208 0.1264 0.1360 -0.0113 -0.0124 0.0225  38  ALA   A O   
997  C  CB  A ALA   A 38  ? 0.1202 0.1349 0.1446 -0.0152 -0.0061 0.0041  38  ALA   A CB  
998  C  CB  B ALA   A 38  ? 0.1435 0.1367 0.1377 -0.0119 -0.0102 0.0119  38  ALA   A CB  
1009 N  N   A ALA   A 39  ? 0.1129 0.1229 0.1338 -0.0021 0.0031  0.0090  39  ALA   A N   
1010 N  N   B ALA   A 39  ? 0.1323 0.1348 0.1432 -0.0091 0.0046  0.0225  39  ALA   A N   
1011 C  CA  A ALA   A 39  ? 0.1193 0.1203 0.1320 0.0031  0.0025  0.0098  39  ALA   A CA  
1012 C  CA  B ALA   A 39  ? 0.1386 0.1384 0.1441 -0.0059 0.0066  0.0212  39  ALA   A CA  
1013 C  C   A ALA   A 39  ? 0.1269 0.1173 0.1387 0.0026  -0.0006 0.0078  39  ALA   A C   
1014 C  C   B ALA   A 39  ? 0.1336 0.1300 0.1322 -0.0068 0.0133  0.0143  39  ALA   A C   
1015 O  O   A ALA   A 39  ? 0.1352 0.1172 0.1497 0.0016  -0.0050 0.0038  39  ALA   A O   
1016 O  O   B ALA   A 39  ? 0.1292 0.1297 0.1228 -0.0116 0.0217  0.0157  39  ALA   A O   
1017 C  CB  A ALA   A 39  ? 0.1161 0.1214 0.1427 0.0061  -0.0132 -0.0041 39  ALA   A CB  
1018 C  CB  B ALA   A 39  ? 0.1520 0.1494 0.1662 -0.0046 0.0035  0.0062  39  ALA   A CB  
1029 N  N   . ASN   A 40  ? 0.1369 0.1268 0.1307 -0.0067 0.0181  0.0061  40  ASN   A N   
1030 C  CA  . ASN   A 40  ? 0.1410 0.1217 0.1416 -0.0022 0.0148  0.0059  40  ASN   A CA  
1031 C  C   . ASN   A 40  ? 0.1437 0.1117 0.1266 -0.0064 0.0207  0.0165  40  ASN   A C   
1032 O  O   . ASN   A 40  ? 0.1369 0.1194 0.1349 -0.0049 0.0216  0.0183  40  ASN   A O   
1033 C  CB  . ASN   A 40  ? 0.1520 0.1273 0.1652 0.0033  -0.0013 0.0097  40  ASN   A CB  
1034 C  CG  . ASN   A 40  ? 0.1590 0.1285 0.1895 0.0037  0.0021  0.0126  40  ASN   A CG  
1035 O  OD1 . ASN   A 40  ? 0.1664 0.1267 0.1942 -0.0023 0.0069  0.0085  40  ASN   A OD1 
1036 N  ND2 . ASN   A 40  ? 0.1619 0.1418 0.2194 0.0037  0.0009  -0.0080 40  ASN   A ND2 
1044 N  N   . VAL   A 41  ? 0.1506 0.1183 0.1349 -0.0059 0.0202  0.0148  41  VAL   A N   
1045 C  CA  . VAL   A 41  ? 0.1581 0.1230 0.1544 -0.0058 0.0336  0.0096  41  VAL   A CA  
1046 C  C   . VAL   A 41  ? 0.1495 0.1248 0.1586 -0.0033 0.0377  0.0142  41  VAL   A C   
1047 O  O   . VAL   A 41  ? 0.1526 0.1183 0.1842 -0.0004 0.0328  0.0110  41  VAL   A O   
1048 C  CB  . VAL   A 41  ? 0.1704 0.1396 0.1540 -0.0131 0.0492  0.0050  41  VAL   A CB  
1049 C  CG1 . VAL   A 41  ? 0.1798 0.1443 0.1760 -0.0063 0.0455  0.0029  41  VAL   A CG1 
1050 C  CG2 . VAL   A 41  ? 0.2005 0.1513 0.1467 -0.0190 0.0542  0.0110  41  VAL   A CG2 
1060 N  N   . TYR   A 42  ? 0.1359 0.1151 0.1765 -0.0029 0.0357  0.0279  42  TYR   A N   
1061 C  CA  . TYR   A 42  ? 0.1392 0.1150 0.1763 -0.0029 0.0380  0.0226  42  TYR   A CA  
1062 C  C   . TYR   A 42  ? 0.1293 0.1183 0.1714 -0.0003 0.0340  0.0272  42  TYR   A C   
1063 O  O   . TYR   A 42  ? 0.1301 0.1210 0.1891 -0.0137 0.0246  0.0073  42  TYR   A O   
1064 C  CB  . TYR   A 42  ? 0.1581 0.1267 0.1532 0.0000  0.0389  0.0285  42  TYR   A CB  
1065 C  CG  . TYR   A 42  ? 0.1765 0.1341 0.1659 0.0008  0.0236  0.0352  42  TYR   A CG  
1066 C  CD1 . TYR   A 42  ? 0.1889 0.1460 0.1698 -0.0137 0.0356  0.0294  42  TYR   A CD1 
1067 C  CD2 . TYR   A 42  ? 0.1921 0.1550 0.1908 -0.0027 0.0176  0.0247  42  TYR   A CD2 
1068 C  CE1 . TYR   A 42  ? 0.2029 0.1629 0.1742 -0.0123 0.0408  0.0227  42  TYR   A CE1 
1069 C  CE2 . TYR   A 42  ? 0.2109 0.1689 0.1945 -0.0102 0.0246  0.0266  42  TYR   A CE2 
1070 C  CZ  . TYR   A 42  ? 0.2213 0.1768 0.1769 -0.0180 0.0422  0.0167  42  TYR   A CZ  
1071 O  OH  . TYR   A 42  ? 0.2390 0.2001 0.2034 -0.0313 0.0443  0.0083  42  TYR   A OH  
1081 N  N   . LEU   A 43  ? 0.1340 0.1180 0.1557 -0.0055 0.0187  0.0074  43  LEU   A N   
1082 C  CA  . LEU   A 43  ? 0.1267 0.1200 0.1540 -0.0051 0.0161  0.0062  43  LEU   A CA  
1083 C  C   . LEU   A 43  ? 0.1223 0.1224 0.1588 -0.0052 0.0103  0.0130  43  LEU   A C   
1084 O  O   . LEU   A 43  ? 0.1425 0.1232 0.1779 0.0009  -0.0007 0.0039  43  LEU   A O   
1085 C  CB  . LEU   A 43  ? 0.1324 0.1176 0.1665 -0.0088 0.0169  0.0100  43  LEU   A CB  
1086 C  CG  . LEU   A 43  ? 0.1356 0.1184 0.1672 -0.0056 0.0130  0.0074  43  LEU   A CG  
1087 C  CD1 . LEU   A 43  ? 0.1376 0.1316 0.1835 -0.0063 -0.0052 0.0128  43  LEU   A CD1 
1088 C  CD2 . LEU   A 43  ? 0.1556 0.1223 0.1671 -0.0020 0.0153  0.0177  43  LEU   A CD2 
1100 N  N   A LYS   A 44  ? 0.1308 0.1224 0.1500 -0.0035 0.0097  0.0129  44  LYS   A N   
1101 N  N   B LYS   A 44  ? 0.1321 0.1288 0.1568 -0.0031 0.0074  0.0105  44  LYS   A N   
1102 C  CA  A LYS   A 44  ? 0.1463 0.1205 0.1525 -0.0045 0.0100  0.0218  44  LYS   A CA  
1103 C  CA  B LYS   A 44  ? 0.1453 0.1334 0.1657 -0.0034 0.0050  0.0127  44  LYS   A CA  
1104 C  C   A LYS   A 44  ? 0.1333 0.1243 0.1423 0.0018  0.0068  0.0138  44  LYS   A C   
1105 C  C   B LYS   A 44  ? 0.1320 0.1299 0.1510 -0.0012 0.0031  0.0113  44  LYS   A C   
1106 O  O   A LYS   A 44  ? 0.1448 0.1375 0.1531 0.0029  0.0039  0.0004  44  LYS   A O   
1107 O  O   B LYS   A 44  ? 0.1361 0.1375 0.1542 -0.0040 0.0033  0.0062  44  LYS   A O   
1108 C  CB  A LYS   A 44  ? 0.1814 0.1317 0.1932 -0.0010 0.0309  0.0330  44  LYS   A CB  
1109 C  CB  B LYS   A 44  ? 0.1747 0.1488 0.2064 0.0004  0.0147  0.0148  44  LYS   A CB  
1110 C  CG  A LYS   A 44  ? 0.2174 0.1688 0.2625 -0.0060 0.0538  0.0477  44  LYS   A CG  
1111 C  CG  B LYS   A 44  ? 0.2010 0.1746 0.2637 0.0001  0.0270  0.0229  44  LYS   A CG  
1112 C  CD  A LYS   A 44  ? 0.2532 0.2248 0.3542 -0.0084 0.0401  0.0333  44  LYS   A CD  
1113 C  CD  B LYS   A 44  ? 0.2275 0.2094 0.3248 -0.0059 0.0199  0.0207  44  LYS   A CD  
1114 C  CE  A LYS   A 44  ? 0.2709 0.2564 0.4144 -0.0127 0.0367  0.0277  44  LYS   A CE  
1115 C  CE  B LYS   A 44  ? 0.2412 0.2339 0.3641 -0.0132 0.0156  0.0223  44  LYS   A CE  
1116 N  NZ  A LYS   A 44  ? 0.2777 0.2719 0.4446 -0.0187 0.0408  0.0308  44  LYS   A NZ  
1117 N  NZ  B LYS   A 44  ? 0.2489 0.2504 0.3865 -0.0225 0.0188  0.0249  44  LYS   A NZ  
1144 N  N   . HIS   A 45  ? 0.1220 0.1225 0.1470 0.0008  -0.0025 0.0161  45  HIS   A N   
1145 C  CA  . HIS   A 45  ? 0.1220 0.1180 0.1474 0.0011  -0.0049 0.0130  45  HIS   A CA  
1146 C  C   . HIS   A 45  ? 0.1307 0.1347 0.1571 0.0065  0.0022  0.0117  45  HIS   A C   
1147 O  O   . HIS   A 45  ? 0.1518 0.1479 0.1908 0.0268  -0.0052 -0.0057 45  HIS   A O   
1148 C  CB  . HIS   A 45  ? 0.1258 0.1182 0.1541 0.0011  -0.0026 0.0096  45  HIS   A CB  
1149 C  CG  . HIS   A 45  ? 0.1186 0.1207 0.1417 -0.0060 0.0071  0.0145  45  HIS   A CG  
1150 N  ND1 . HIS   A 45  ? 0.1144 0.1292 0.1617 -0.0048 -0.0023 0.0219  45  HIS   A ND1 
1151 C  CD2 . HIS   A 45  ? 0.1189 0.1258 0.1371 -0.0114 -0.0015 0.0154  45  HIS   A CD2 
1152 C  CE1 . HIS   A 45  ? 0.1194 0.1332 0.1353 -0.0083 -0.0050 0.0290  45  HIS   A CE1 
1153 N  NE2 . HIS   A 45  ? 0.1208 0.1351 0.1379 -0.0070 0.0018  0.0276  45  HIS   A NE2 
1162 N  N   A GLY   A 46  ? 0.1498 0.1388 0.1793 0.0069  -0.0175 0.0204  46  GLY   A N   
1163 N  N   B GLY   A 46  ? 0.1433 0.1400 0.1655 0.0185  -0.0110 0.0203  46  GLY   A N   
1164 C  CA  A GLY   A 46  ? 0.1536 0.1479 0.1902 0.0064  -0.0196 0.0242  46  GLY   A CA  
1165 C  CA  B GLY   A 46  ? 0.1506 0.1421 0.1708 0.0201  -0.0209 0.0262  46  GLY   A CA  
1166 C  C   A GLY   A 46  ? 0.1539 0.1423 0.1985 0.0117  -0.0239 0.0237  46  GLY   A C   
1167 C  C   B GLY   A 46  ? 0.1554 0.1354 0.1714 0.0257  -0.0309 0.0257  46  GLY   A C   
1168 O  O   A GLY   A 46  ? 0.1587 0.1514 0.2322 0.0135  -0.0279 0.0043  46  GLY   A O   
1169 O  O   B GLY   A 46  ? 0.1565 0.1312 0.1982 0.0228  -0.0380 0.0302  46  GLY   A O   
1176 N  N   A GLY   A 47  ? 0.1598 0.1418 0.1807 0.0118  -0.0247 0.0092  47  GLY   A N   
1177 N  N   B GLY   A 47  ? 0.1571 0.1370 0.1598 0.0284  -0.0355 0.0050  47  GLY   A N   
1178 C  CA  A GLY   A 47  ? 0.1556 0.1423 0.1765 0.0153  -0.0467 -0.0110 47  GLY   A CA  
1179 C  CA  B GLY   A 47  ? 0.1588 0.1436 0.1611 0.0305  -0.0523 -0.0108 47  GLY   A CA  
1180 C  C   A GLY   A 47  ? 0.1480 0.1331 0.1820 0.0126  -0.0524 -0.0146 47  GLY   A C   
1181 C  C   B GLY   A 47  ? 0.1540 0.1448 0.1596 0.0258  -0.0512 -0.0249 47  GLY   A C   
1182 O  O   A GLY   A 47  ? 0.1453 0.1248 0.1933 0.0179  -0.0552 0.0085  47  GLY   A O   
1183 O  O   B GLY   A 47  ? 0.1529 0.1417 0.1639 0.0282  -0.0450 -0.0123 47  GLY   A O   
1190 N  N   A GLY   A 48  ? 0.1425 0.1341 0.1855 0.0151  -0.0544 -0.0167 48  GLY   A N   
1191 N  N   B GLY   A 48  ? 0.1527 0.1532 0.1701 0.0235  -0.0491 -0.0251 48  GLY   A N   
1192 C  CA  A GLY   A 48  ? 0.1392 0.1296 0.2035 0.0077  -0.0458 -0.0163 48  GLY   A CA  
1193 C  CA  B GLY   A 48  ? 0.1507 0.1527 0.1777 0.0172  -0.0338 -0.0263 48  GLY   A CA  
1194 C  C   A GLY   A 48  ? 0.1309 0.1317 0.1847 0.0034  -0.0166 -0.0058 48  GLY   A C   
1195 C  C   B GLY   A 48  ? 0.1421 0.1517 0.1697 0.0084  -0.0109 -0.0134 48  GLY   A C   
1196 O  O   A GLY   A 48  ? 0.1486 0.1296 0.1820 0.0050  -0.0103 -0.0076 48  GLY   A O   
1197 O  O   B GLY   A 48  ? 0.1555 0.1541 0.1642 0.0024  -0.0050 -0.0171 48  GLY   A O   
1204 N  N   A VAL   A 49  ? 0.1125 0.1281 0.1882 0.0013  -0.0100 -0.0105 49  VAL   A N   
1205 N  N   B VAL   A 49  ? 0.1276 0.1441 0.1720 0.0007  -0.0099 -0.0086 49  VAL   A N   
1206 C  CA  A VAL   A 49  ? 0.1314 0.1293 0.1772 -0.0008 0.0126  -0.0045 49  VAL   A CA  
1207 C  CA  B VAL   A 49  ? 0.1139 0.1371 0.1567 -0.0033 -0.0005 0.0002  49  VAL   A CA  
1208 C  C   A VAL   A 49  ? 0.1266 0.1172 0.1482 0.0013  0.0092  0.0033  49  VAL   A C   
1209 C  C   B VAL   A 49  ? 0.1112 0.1231 0.1345 -0.0002 0.0083  -0.0062 49  VAL   A C   
1210 O  O   A VAL   A 49  ? 0.1357 0.1247 0.1450 -0.0017 0.0154  0.0095  49  VAL   A O   
1211 O  O   B VAL   A 49  ? 0.1117 0.1137 0.1400 0.0048  0.0093  -0.0042 49  VAL   A O   
1212 C  CB  A VAL   A 49  ? 0.1445 0.1365 0.1864 -0.0031 0.0256  -0.0115 49  VAL   A CB  
1213 C  CB  B VAL   A 49  ? 0.1051 0.1309 0.1595 0.0016  -0.0005 0.0010  49  VAL   A CB  
1214 C  CG1 A VAL   A 49  ? 0.1459 0.1306 0.1962 -0.0004 0.0351  -0.0157 49  VAL   A CG1 
1215 C  CG1 B VAL   A 49  ? 0.0971 0.1242 0.1524 0.0141  -0.0030 -0.0055 49  VAL   A CG1 
1216 C  CG2 A VAL   A 49  ? 0.1528 0.1416 0.2235 -0.0222 0.0333  -0.0113 49  VAL   A CG2 
1217 C  CG2 B VAL   A 49  ? 0.1077 0.1360 0.1682 0.0022  0.0095  0.0050  49  VAL   A CG2 
1236 N  N   A ALA   A 50  ? 0.1182 0.1177 0.1390 -0.0027 -0.0138 0.0146  50  ALA   A N   
1237 N  N   B ALA   A 50  ? 0.1146 0.1245 0.1122 0.0010  0.0054  -0.0048 50  ALA   A N   
1238 C  CA  A ALA   A 50  ? 0.1126 0.1136 0.1420 -0.0086 -0.0035 0.0202  50  ALA   A CA  
1239 C  CA  B ALA   A 50  ? 0.1201 0.1240 0.1037 -0.0042 -0.0026 -0.0014 50  ALA   A CA  
1240 C  C   A ALA   A 50  ? 0.1143 0.1186 0.1506 -0.0068 -0.0010 0.0146  50  ALA   A C   
1241 C  C   B ALA   A 50  ? 0.1243 0.1270 0.0911 -0.0053 0.0012  -0.0102 50  ALA   A C   
1242 O  O   A ALA   A 50  ? 0.1126 0.1171 0.1672 0.0003  -0.0021 0.0142  50  ALA   A O   
1243 O  O   B ALA   A 50  ? 0.1247 0.1290 0.0782 -0.0063 0.0053  -0.0167 50  ALA   A O   
1244 C  CB  A ALA   A 50  ? 0.1081 0.1157 0.1483 -0.0067 -0.0038 0.0040  50  ALA   A CB  
1245 C  CB  B ALA   A 50  ? 0.1205 0.1219 0.1222 0.0016  -0.0014 -0.0023 50  ALA   A CB  
1256 N  N   A GLY   A 51  ? 0.1212 0.1124 0.1594 0.0039  -0.0063 0.0117  51  GLY   A N   
1257 N  N   B GLY   A 51  ? 0.1283 0.1240 0.1162 0.0009  -0.0048 -0.0117 51  GLY   A N   
1258 C  CA  A GLY   A 51  ? 0.1344 0.1119 0.1554 0.0090  -0.0182 0.0144  51  GLY   A CA  
1259 C  CA  B GLY   A 51  ? 0.1358 0.1256 0.1273 0.0027  -0.0124 -0.0094 51  GLY   A CA  
1260 C  C   A GLY   A 51  ? 0.1213 0.1205 0.1608 0.0107  -0.0008 -0.0045 51  GLY   A C   
1261 C  C   B GLY   A 51  ? 0.1279 0.1310 0.1424 0.0044  -0.0037 -0.0112 51  GLY   A C   
1262 O  O   A GLY   A 51  ? 0.1229 0.1299 0.1832 0.0029  -0.0017 -0.0113 51  GLY   A O   
1263 O  O   B GLY   A 51  ? 0.1320 0.1369 0.1496 0.0001  -0.0096 -0.0146 51  GLY   A O   
1270 N  N   . ALA   A 52  ? 0.1199 0.1364 0.1504 0.0039  -0.0005 -0.0105 52  ALA   A N   
1271 C  CA  . ALA   A 52  ? 0.1181 0.1439 0.1713 -0.0054 0.0038  -0.0129 52  ALA   A CA  
1272 C  C   . ALA   A 52  ? 0.1191 0.1393 0.1509 -0.0102 0.0099  -0.0105 52  ALA   A C   
1273 O  O   . ALA   A 52  ? 0.1277 0.1502 0.1740 -0.0042 0.0075  -0.0144 52  ALA   A O   
1274 C  CB  . ALA   A 52  ? 0.1314 0.1775 0.1839 -0.0132 0.0006  -0.0083 52  ALA   A CB  
1281 N  N   A LEU   A 53  ? 0.1216 0.1371 0.1469 -0.0105 0.0042  -0.0038 53  LEU   A N   
1282 N  N   B LEU   A 53  ? 0.1187 0.1375 0.1406 -0.0084 0.0014  -0.0030 53  LEU   A N   
1283 C  CA  A LEU   A 53  ? 0.1351 0.1424 0.1315 -0.0095 0.0061  0.0006  53  LEU   A CA  
1284 C  CA  B LEU   A 53  ? 0.1259 0.1392 0.1267 -0.0055 -0.0016 0.0026  53  LEU   A CA  
1285 C  C   A LEU   A 53  ? 0.1353 0.1458 0.1041 -0.0031 0.0107  0.0003  53  LEU   A C   
1286 C  C   B LEU   A 53  ? 0.1296 0.1418 0.1125 -0.0005 -0.0002 0.0019  53  LEU   A C   
1287 O  O   A LEU   A 53  ? 0.1467 0.1608 0.1216 -0.0180 0.0124  -0.0016 53  LEU   A O   
1288 O  O   B LEU   A 53  ? 0.1393 0.1518 0.1221 -0.0064 -0.0024 -0.0012 53  LEU   A O   
1289 C  CB  A LEU   A 53  ? 0.1469 0.1436 0.1488 -0.0140 0.0046  0.0055  53  LEU   A CB  
1290 C  CB  B LEU   A 53  ? 0.1279 0.1352 0.1268 -0.0063 -0.0042 0.0052  53  LEU   A CB  
1291 C  CG  A LEU   A 53  ? 0.1523 0.1496 0.1670 -0.0142 0.0092  0.0156  53  LEU   A CG  
1292 C  CG  B LEU   A 53  ? 0.1247 0.1334 0.1262 -0.0062 -0.0105 0.0097  53  LEU   A CG  
1293 C  CD1 A LEU   A 53  ? 0.1530 0.1556 0.1632 -0.0029 0.0144  0.0209  53  LEU   A CD1 
1294 C  CD1 B LEU   A 53  ? 0.1325 0.1393 0.1309 -0.0092 -0.0058 -0.0027 53  LEU   A CD1 
1295 C  CD2 A LEU   A 53  ? 0.1574 0.1630 0.1703 -0.0133 0.0023  0.0170  53  LEU   A CD2 
1296 C  CD2 B LEU   A 53  ? 0.1208 0.1320 0.1168 -0.0037 -0.0068 0.0070  53  LEU   A CD2 
1319 N  N   . ASN   A 54  ? 0.1265 0.1357 0.1186 -0.0021 -0.0020 0.0028  54  ASN   A N   
1320 C  CA  . ASN   A 54  ? 0.1111 0.1310 0.1490 -0.0066 -0.0037 0.0020  54  ASN   A CA  
1321 C  C   . ASN   A 54  ? 0.1233 0.1327 0.1411 -0.0120 -0.0011 -0.0027 54  ASN   A C   
1322 O  O   . ASN   A 54  ? 0.1240 0.1415 0.1500 -0.0092 -0.0037 -0.0075 54  ASN   A O   
1323 C  CB  . ASN   A 54  ? 0.1084 0.1285 0.1618 -0.0082 -0.0062 0.0058  54  ASN   A CB  
1324 C  CG  . ASN   A 54  ? 0.1173 0.1356 0.1486 -0.0019 -0.0021 0.0006  54  ASN   A CG  
1325 O  OD1 . ASN   A 54  ? 0.1188 0.1346 0.1461 -0.0036 -0.0043 0.0030  54  ASN   A OD1 
1326 N  ND2 . ASN   A 54  ? 0.1287 0.1412 0.1597 -0.0115 -0.0133 0.0162  54  ASN   A ND2 
1334 N  N   . LYS   A 55  ? 0.1249 0.1358 0.1439 -0.0049 -0.0049 -0.0081 55  LYS   A N   
1335 C  CA  . LYS   A 55  ? 0.1345 0.1460 0.1644 0.0068  -0.0014 -0.0179 55  LYS   A CA  
1336 C  C   . LYS   A 55  ? 0.1330 0.1525 0.1597 -0.0023 0.0056  -0.0205 55  LYS   A C   
1337 O  O   . LYS   A 55  ? 0.1380 0.1626 0.1707 0.0027  -0.0040 -0.0312 55  LYS   A O   
1338 C  CB  . LYS   A 55  ? 0.1415 0.1569 0.1787 0.0141  -0.0054 -0.0264 55  LYS   A CB  
1339 C  CG  . LYS   A 55  ? 0.1546 0.1877 0.1905 0.0332  -0.0174 -0.0248 55  LYS   A CG  
1340 C  CD  . LYS   A 55  ? 0.1740 0.2218 0.2029 0.0422  -0.0132 -0.0275 55  LYS   A CD  
1341 C  CE  . LYS   A 55  ? 0.1933 0.2512 0.2211 0.0529  -0.0159 -0.0278 55  LYS   A CE  
1342 N  NZ  . LYS   A 55  ? 0.2020 0.2614 0.2412 0.0577  -0.0177 -0.0216 55  LYS   A NZ  
1356 N  N   . ALA   A 56  ? 0.1399 0.1580 0.1532 -0.0135 0.0046  -0.0223 56  ALA   A N   
1357 C  CA  . ALA   A 56  ? 0.1487 0.1763 0.1530 -0.0181 0.0132  -0.0186 56  ALA   A CA  
1358 C  C   . ALA   A 56  ? 0.1522 0.1927 0.1337 -0.0152 0.0146  -0.0258 56  ALA   A C   
1359 O  O   . ALA   A 56  ? 0.1556 0.2199 0.1459 -0.0010 0.0185  -0.0234 56  ALA   A O   
1360 C  CB  . ALA   A 56  ? 0.1519 0.1995 0.1592 -0.0282 0.0068  -0.0141 56  ALA   A CB  
1366 N  N   . THR   A 57  ? 0.1372 0.1702 0.1374 -0.0165 0.0117  -0.0188 57  THR   A N   
1367 C  CA  . THR   A 57  ? 0.1419 0.1610 0.1410 -0.0145 -0.0035 -0.0122 57  THR   A CA  
1368 C  C   . THR   A 57  ? 0.1413 0.1709 0.1464 -0.0074 -0.0023 -0.0222 57  THR   A C   
1369 O  O   . THR   A 57  ? 0.1362 0.1736 0.1652 -0.0115 -0.0114 -0.0298 57  THR   A O   
1370 C  CB  . THR   A 57  ? 0.1353 0.1616 0.1418 -0.0177 0.0041  -0.0043 57  THR   A CB  
1371 O  OG1 . THR   A 57  ? 0.1302 0.1573 0.1441 -0.0094 0.0043  -0.0097 57  THR   A OG1 
1372 C  CG2 . THR   A 57  ? 0.1427 0.1660 0.1306 -0.0108 0.0043  0.0025  57  THR   A CG2 
1380 N  N   . ASN   A 58  ? 0.1448 0.1666 0.1692 -0.0061 0.0063  -0.0328 58  ASN   A N   
1381 C  CA  . ASN   A 58  ? 0.1637 0.1612 0.1915 -0.0112 0.0137  -0.0423 58  ASN   A CA  
1382 C  C   . ASN   A 58  ? 0.1397 0.1502 0.1833 -0.0066 -0.0008 -0.0276 58  ASN   A C   
1383 O  O   . ASN   A 58  ? 0.1446 0.1602 0.1880 -0.0164 -0.0039 -0.0305 58  ASN   A O   
1384 C  CB  . ASN   A 58  ? 0.2057 0.1760 0.2271 -0.0160 0.0323  -0.0572 58  ASN   A CB  
1385 C  CG  . ASN   A 58  ? 0.2437 0.2040 0.2987 -0.0062 0.0389  -0.0367 58  ASN   A CG  
1386 O  OD1 . ASN   A 58  ? 0.2746 0.1994 0.3412 0.0266  0.0643  -0.0292 58  ASN   A OD1 
1387 N  ND2 . ASN   A 58  ? 0.2502 0.2172 0.3231 -0.0076 0.0324  -0.0328 58  ASN   A ND2 
1394 N  N   . ASN   A 59  ? 0.1230 0.1428 0.1710 -0.0073 -0.0100 -0.0132 59  ASN   A N   
1395 C  CA  . ASN   A 59  ? 0.1259 0.1285 0.1678 -0.0024 -0.0054 -0.0095 59  ASN   A CA  
1396 C  C   . ASN   A 59  ? 0.1278 0.1312 0.1611 -0.0068 -0.0097 -0.0022 59  ASN   A C   
1397 O  O   . ASN   A 59  ? 0.1300 0.1370 0.1523 -0.0091 -0.0021 0.0050  59  ASN   A O   
1398 C  CB  . ASN   A 59  ? 0.1354 0.1288 0.1697 0.0040  -0.0140 -0.0147 59  ASN   A CB  
1399 C  CG  . ASN   A 59  ? 0.1391 0.1356 0.1702 -0.0004 -0.0236 -0.0019 59  ASN   A CG  
1400 O  OD1 . ASN   A 59  ? 0.1522 0.1392 0.1602 -0.0133 -0.0213 0.0008  59  ASN   A OD1 
1401 N  ND2 . ASN   A 59  ? 0.1437 0.1362 0.1954 -0.0101 -0.0158 0.0020  59  ASN   A ND2 
1408 N  N   . ALA   A 60  ? 0.1201 0.1404 0.1548 -0.0026 -0.0020 0.0012  60  ALA   A N   
1409 C  CA  . ALA   A 60  ? 0.1255 0.1387 0.1639 -0.0067 -0.0069 0.0031  60  ALA   A CA  
1410 C  C   . ALA   A 60  ? 0.1254 0.1319 0.1652 -0.0051 -0.0068 0.0003  60  ALA   A C   
1411 O  O   . ALA   A 60  ? 0.1200 0.1305 0.1865 -0.0061 -0.0123 -0.0078 60  ALA   A O   
1412 C  CB  . ALA   A 60  ? 0.1353 0.1542 0.1669 -0.0049 -0.0148 -0.0161 60  ALA   A CB  
1418 N  N   . MET   A 61  ? 0.1218 0.1281 0.1471 -0.0101 -0.0020 -0.0069 61  MET   A N   
1419 C  CA  . MET   A 61  ? 0.1194 0.1252 0.1524 -0.0102 0.0050  0.0057  61  MET   A CA  
1420 C  C   . MET   A 61  ? 0.1187 0.1245 0.1579 -0.0081 -0.0062 -0.0027 61  MET   A C   
1421 O  O   . MET   A 61  ? 0.1240 0.1239 0.1710 -0.0059 0.0050  0.0054  61  MET   A O   
1422 C  CB  . MET   A 61  ? 0.1305 0.1251 0.1352 -0.0051 0.0004  -0.0003 61  MET   A CB  
1423 C  CG  . MET   A 61  ? 0.1296 0.1327 0.1508 -0.0024 -0.0013 0.0077  61  MET   A CG  
1424 S  SD  . MET   A 61  ? 0.1300 0.1367 0.1910 -0.0103 -0.0005 -0.0149 61  MET   A SD  
1425 C  CE  . MET   A 61  ? 0.1548 0.1470 0.2101 -0.0170 0.0159  -0.0096 61  MET   A CE  
1435 N  N   . GLN   A 62  ? 0.1214 0.1174 0.1610 -0.0150 -0.0062 -0.0028 62  GLN   A N   
1436 C  CA  . GLN   A 62  ? 0.1223 0.1175 0.1668 -0.0096 0.0000  0.0040  62  GLN   A CA  
1437 C  C   . GLN   A 62  ? 0.1251 0.1108 0.1671 -0.0022 0.0029  0.0057  62  GLN   A C   
1438 O  O   . GLN   A 62  ? 0.1264 0.1269 0.1573 -0.0006 0.0084  0.0022  62  GLN   A O   
1439 C  CB  . GLN   A 62  ? 0.1211 0.1176 0.1619 -0.0061 0.0007  0.0054  62  GLN   A CB  
1440 C  CG  . GLN   A 62  ? 0.1283 0.1194 0.1591 -0.0022 -0.0003 0.0196  62  GLN   A CG  
1441 C  CD  . GLN   A 62  ? 0.1361 0.1207 0.1516 -0.0031 0.0078  0.0141  62  GLN   A CD  
1442 O  OE1 . GLN   A 62  ? 0.1363 0.1321 0.1604 -0.0036 -0.0001 0.0041  62  GLN   A OE1 
1443 N  NE2 . GLN   A 62  ? 0.1428 0.1254 0.1653 0.0025  0.0023  -0.0003 62  GLN   A NE2 
1452 N  N   . VAL   A 63  ? 0.1190 0.1200 0.1803 -0.0100 0.0100  -0.0165 63  VAL   A N   
1453 C  CA  . VAL   A 63  ? 0.1234 0.1318 0.2034 -0.0103 0.0047  -0.0181 63  VAL   A CA  
1454 C  C   . VAL   A 63  ? 0.1128 0.1310 0.1840 -0.0128 -0.0044 -0.0112 63  VAL   A C   
1455 O  O   . VAL   A 63  ? 0.1143 0.1290 0.2042 -0.0164 -0.0016 -0.0097 63  VAL   A O   
1456 C  CB  . VAL   A 63  ? 0.1394 0.1483 0.2244 -0.0129 -0.0086 -0.0328 63  VAL   A CB  
1457 C  CG1 . VAL   A 63  ? 0.1514 0.1698 0.2502 -0.0122 -0.0136 -0.0499 63  VAL   A CG1 
1458 C  CG2 . VAL   A 63  ? 0.1450 0.1406 0.2297 -0.0139 0.0075  -0.0313 63  VAL   A CG2 
1468 N  N   . GLU   A 64  ? 0.1212 0.1370 0.1694 -0.0073 -0.0019 -0.0086 64  GLU   A N   
1469 C  CA  . GLU   A 64  ? 0.1181 0.1356 0.1709 -0.0061 -0.0099 0.0012  64  GLU   A CA  
1470 C  C   . GLU   A 64  ? 0.1124 0.1245 0.1807 -0.0083 -0.0004 0.0058  64  GLU   A C   
1471 O  O   . GLU   A 64  ? 0.1207 0.1281 0.1882 -0.0054 -0.0002 0.0047  64  GLU   A O   
1472 C  CB  . GLU   A 64  ? 0.1226 0.1441 0.1720 -0.0067 -0.0009 -0.0051 64  GLU   A CB  
1473 C  CG  . GLU   A 64  ? 0.1360 0.1475 0.1853 -0.0099 0.0002  0.0068  64  GLU   A CG  
1474 C  CD  . GLU   A 64  ? 0.1475 0.1586 0.1930 -0.0153 0.0058  0.0005  64  GLU   A CD  
1475 O  OE1 . GLU   A 64  ? 0.1446 0.1653 0.2092 -0.0227 0.0176  0.0051  64  GLU   A OE1 
1476 O  OE2 . GLU   A 64  ? 0.1623 0.1563 0.1968 -0.0253 -0.0089 0.0042  64  GLU   A OE2 
1483 N  N   . SER   A 65  ? 0.1095 0.1266 0.1636 -0.0011 0.0021  0.0023  65  SER   A N   
1484 C  CA  . SER   A 65  ? 0.1215 0.1239 0.1636 -0.0040 -0.0020 -0.0047 65  SER   A CA  
1485 C  C   . SER   A 65  ? 0.1238 0.1289 0.1576 -0.0080 0.0022  -0.0047 65  SER   A C   
1486 O  O   . SER   A 65  ? 0.1312 0.1329 0.1726 -0.0011 0.0164  -0.0106 65  SER   A O   
1487 C  CB  . SER   A 65  ? 0.1171 0.1243 0.1722 -0.0085 -0.0049 0.0080  65  SER   A CB  
1488 O  OG  . SER   A 65  ? 0.1175 0.1364 0.1701 -0.0115 -0.0061 0.0168  65  SER   A OG  
1494 N  N   . ASP   A 66  ? 0.1231 0.1234 0.1612 -0.0028 0.0142  0.0054  66  ASP   A N   
1495 C  CA  . ASP   A 66  ? 0.1342 0.1405 0.1776 -0.0016 0.0139  0.0198  66  ASP   A CA  
1496 C  C   . ASP   A 66  ? 0.1287 0.1306 0.1889 -0.0070 0.0113  0.0201  66  ASP   A C   
1497 O  O   . ASP   A 66  ? 0.1344 0.1443 0.2021 -0.0039 0.0278  0.0195  66  ASP   A O   
1498 C  CB  . ASP   A 66  ? 0.1414 0.1467 0.2199 0.0056  0.0165  0.0335  66  ASP   A CB  
1499 C  CG  . ASP   A 66  ? 0.1651 0.1581 0.2499 0.0013  0.0026  0.0442  66  ASP   A CG  
1500 O  OD1 . ASP   A 66  ? 0.1651 0.1860 0.2187 -0.0090 -0.0015 0.0527  66  ASP   A OD1 
1501 O  OD2 . ASP   A 66  ? 0.1796 0.1687 0.3255 0.0161  -0.0158 0.0250  66  ASP   A OD2 
1506 N  N   . ASP   A 67  ? 0.1269 0.1353 0.1996 -0.0058 0.0140  0.0237  67  ASP   A N   
1507 C  CA  . ASP   A 67  ? 0.1256 0.1537 0.2025 -0.0091 0.0106  0.0248  67  ASP   A CA  
1508 C  C   . ASP   A 67  ? 0.1234 0.1503 0.2053 -0.0026 0.0105  0.0265  67  ASP   A C   
1509 O  O   . ASP   A 67  ? 0.1222 0.1596 0.2238 0.0027  0.0258  0.0313  67  ASP   A O   
1510 C  CB  . ASP   A 67  ? 0.1316 0.1601 0.2378 -0.0113 -0.0081 0.0335  67  ASP   A CB  
1511 C  CG  . ASP   A 67  ? 0.1309 0.1743 0.2772 -0.0150 -0.0249 0.0438  67  ASP   A CG  
1512 O  OD1 . ASP   A 67  ? 0.1394 0.1921 0.3407 -0.0170 -0.0370 0.0562  67  ASP   A OD1 
1513 O  OD2 . ASP   A 67  ? 0.1345 0.1799 0.2698 -0.0022 -0.0147 0.0296  67  ASP   A OD2 
1518 N  N   . TYR   A 68  ? 0.1266 0.1374 0.2097 0.0028  0.0183  0.0255  68  TYR   A N   
1519 C  CA  . TYR   A 68  ? 0.1397 0.1371 0.2013 0.0027  0.0211  0.0269  68  TYR   A CA  
1520 C  C   . TYR   A 68  ? 0.1334 0.1389 0.1943 -0.0002 0.0249  0.0159  68  TYR   A C   
1521 O  O   . TYR   A 68  ? 0.1401 0.1419 0.1973 0.0040  0.0271  0.0166  68  TYR   A O   
1522 C  CB  . TYR   A 68  ? 0.1381 0.1303 0.2142 0.0061  0.0404  0.0351  68  TYR   A CB  
1523 C  CG  . TYR   A 68  ? 0.1456 0.1489 0.2397 -0.0044 0.0509  0.0324  68  TYR   A CG  
1524 C  CD1 . TYR   A 68  ? 0.1536 0.1560 0.2720 -0.0260 0.0411  -0.0075 68  TYR   A CD1 
1525 C  CD2 . TYR   A 68  ? 0.1679 0.1543 0.2685 0.0033  0.0522  0.0405  68  TYR   A CD2 
1526 C  CE1 . TYR   A 68  ? 0.1659 0.1680 0.3071 -0.0242 0.0573  -0.0186 68  TYR   A CE1 
1527 C  CE2 . TYR   A 68  ? 0.1668 0.1609 0.2998 -0.0019 0.0679  0.0099  68  TYR   A CE2 
1528 C  CZ  . TYR   A 68  ? 0.1692 0.1637 0.3182 -0.0242 0.0558  -0.0209 68  TYR   A CZ  
1529 O  OH  . TYR   A 68  ? 0.1935 0.1642 0.3348 -0.0205 0.0331  -0.0416 68  TYR   A OH  
1539 N  N   . ILE   A 69  ? 0.1259 0.1302 0.1915 -0.0041 0.0238  0.0207  69  ILE   A N   
1540 C  CA  . ILE   A 69  ? 0.1326 0.1336 0.1836 0.0001  0.0184  0.0055  69  ILE   A CA  
1541 C  C   . ILE   A 69  ? 0.1358 0.1357 0.1734 0.0087  0.0245  0.0162  69  ILE   A C   
1542 O  O   . ILE   A 69  ? 0.1443 0.1451 0.1809 -0.0024 0.0242  0.0183  69  ILE   A O   
1543 C  CB  . ILE   A 69  ? 0.1437 0.1548 0.1931 0.0065  0.0122  0.0033  69  ILE   A CB  
1544 C  CG1 . ILE   A 69  ? 0.1380 0.1632 0.1990 0.0077  0.0209  -0.0164 69  ILE   A CG1 
1545 C  CG2 . ILE   A 69  ? 0.1685 0.1717 0.2113 0.0152  0.0003  -0.0034 69  ILE   A CG2 
1546 C  CD1 . ILE   A 69  ? 0.1449 0.1769 0.2106 -0.0024 0.0158  -0.0217 69  ILE   A CD1 
1558 N  N   . ALA   A 70  ? 0.1431 0.1340 0.1988 -0.0051 0.0257  0.0187  70  ALA   A N   
1559 C  CA  . ALA   A 70  ? 0.1482 0.1455 0.2166 -0.0149 0.0340  0.0239  70  ALA   A CA  
1560 C  C   . ALA   A 70  ? 0.1422 0.1617 0.2140 -0.0127 0.0313  0.0224  70  ALA   A C   
1561 O  O   . ALA   A 70  ? 0.1615 0.1972 0.2463 0.0065  0.0563  0.0418  70  ALA   A O   
1562 C  CB  . ALA   A 70  ? 0.1500 0.1418 0.2397 -0.0169 0.0314  0.0118  70  ALA   A CB  
1568 N  N   . THR   A 71  ? 0.1354 0.1648 0.2015 -0.0055 0.0251  0.0242  71  THR   A N   
1569 C  CA  . THR   A 71  ? 0.1445 0.1778 0.2324 0.0065  0.0234  0.0221  71  THR   A CA  
1570 C  C   . THR   A 71  ? 0.1336 0.1714 0.2497 0.0103  0.0296  0.0242  71  THR   A C   
1571 O  O   . THR   A 71  ? 0.1383 0.1980 0.2967 0.0043  0.0391  -0.0059 71  THR   A O   
1572 C  CB  . THR   A 71  ? 0.1680 0.1966 0.2686 0.0142  -0.0125 0.0352  71  THR   A CB  
1573 O  OG1 . THR   A 71  ? 0.1968 0.2140 0.2876 0.0032  -0.0280 0.0283  71  THR   A OG1 
1574 C  CG2 . THR   A 71  ? 0.1818 0.2146 0.2958 0.0225  -0.0230 0.0422  71  THR   A CG2 
1582 N  N   . ASN   A 72  ? 0.1387 0.1515 0.2272 0.0110  0.0298  0.0261  72  ASN   A N   
1583 C  CA  . ASN   A 72  ? 0.1424 0.1535 0.2316 0.0185  0.0372  0.0277  72  ASN   A CA  
1584 C  C   . ASN   A 72  ? 0.1538 0.1531 0.2285 0.0100  0.0483  0.0179  72  ASN   A C   
1585 O  O   . ASN   A 72  ? 0.1746 0.1512 0.2511 0.0162  0.0494  0.0032  72  ASN   A O   
1586 C  CB  . ASN   A 72  ? 0.1640 0.1621 0.2307 0.0159  0.0399  0.0243  72  ASN   A CB  
1587 C  CG  . ASN   A 72  ? 0.1907 0.1761 0.2315 0.0191  0.0319  0.0223  72  ASN   A CG  
1588 O  OD1 . ASN   A 72  ? 0.2081 0.2111 0.2511 0.0253  0.0410  0.0349  72  ASN   A OD1 
1589 N  ND2 . ASN   A 72  ? 0.2066 0.1721 0.2330 0.0497  0.0079  0.0074  72  ASN   A ND2 
1596 N  N   . GLY   A 73  ? 0.1530 0.1503 0.2178 0.0044  0.0465  0.0123  73  GLY   A N   
1597 C  CA  . GLY   A 73  ? 0.1561 0.1466 0.2049 -0.0050 0.0399  0.0115  73  GLY   A CA  
1598 C  C   . GLY   A 73  ? 0.1608 0.1397 0.1900 0.0016  0.0462  0.0243  73  GLY   A C   
1599 O  O   . GLY   A 73  ? 0.1651 0.1442 0.2001 0.0138  0.0362  0.0350  73  GLY   A O   
1603 N  N   . PRO   A 74  ? 0.1707 0.1399 0.1970 -0.0136 0.0546  0.0120  74  PRO   A N   
1604 C  CA  . PRO   A 74  ? 0.1682 0.1393 0.2009 -0.0014 0.0415  0.0201  74  PRO   A CA  
1605 C  C   . PRO   A 74  ? 0.1599 0.1251 0.1836 -0.0001 0.0320  0.0069  74  PRO   A C   
1606 O  O   . PRO   A 74  ? 0.1675 0.1311 0.2081 0.0018  0.0385  -0.0047 74  PRO   A O   
1607 C  CB  . PRO   A 74  ? 0.1842 0.1656 0.2203 -0.0012 0.0442  0.0235  74  PRO   A CB  
1608 C  CG  . PRO   A 74  ? 0.2091 0.2022 0.2627 -0.0255 0.0365  0.0045  74  PRO   A CG  
1609 C  CD  . PRO   A 74  ? 0.1877 0.1759 0.2185 -0.0306 0.0403  -0.0032 74  PRO   A CD  
1617 N  N   . LEU   A 75  ? 0.1576 0.1200 0.1778 0.0008  0.0253  0.0076  75  LEU   A N   
1618 C  CA  . LEU   A 75  ? 0.1592 0.1175 0.1666 0.0001  0.0118  0.0131  75  LEU   A CA  
1619 C  C   . LEU   A 75  ? 0.1704 0.1362 0.1615 0.0072  0.0110  0.0113  75  LEU   A C   
1620 O  O   . LEU   A 75  ? 0.1934 0.1516 0.1653 0.0129  0.0118  0.0079  75  LEU   A O   
1621 C  CB  . LEU   A 75  ? 0.1624 0.1218 0.1672 -0.0070 0.0116  0.0152  75  LEU   A CB  
1622 C  CG  . LEU   A 75  ? 0.1779 0.1607 0.1773 -0.0369 0.0036  0.0210  75  LEU   A CG  
1623 C  CD1 . LEU   A 75  ? 0.1872 0.2132 0.1838 -0.0374 -0.0001 0.0005  75  LEU   A CD1 
1624 C  CD2 . LEU   A 75  ? 0.2084 0.2019 0.2242 -0.0150 0.0037  0.0344  75  LEU   A CD2 
1636 N  N   . LYS   A 76  ? 0.1690 0.1335 0.1774 -0.0028 0.0084  -0.0032 76  LYS   A N   
1637 C  CA  . LYS   A 76  ? 0.1654 0.1528 0.1796 -0.0089 0.0133  -0.0125 76  LYS   A CA  
1638 C  C   . LYS   A 76  ? 0.1555 0.1337 0.1499 -0.0015 0.0102  0.0055  76  LYS   A C   
1639 O  O   . LYS   A 76  ? 0.1628 0.1284 0.1561 -0.0041 0.0148  0.0140  76  LYS   A O   
1640 C  CB  . LYS   A 76  ? 0.1657 0.1752 0.2177 0.0037  0.0128  -0.0380 76  LYS   A CB  
1641 C  CG  . LYS   A 76  ? 0.1755 0.1700 0.2666 0.0094  0.0082  -0.0324 76  LYS   A CG  
1642 C  CD  . LYS   A 76  ? 0.1793 0.1646 0.3174 0.0141  -0.0023 -0.0369 76  LYS   A CD  
1643 C  CE  . LYS   A 76  ? 0.1939 0.1895 0.3696 0.0008  0.0009  -0.0411 76  LYS   A CE  
1644 N  NZ  . LYS   A 76  ? 0.1927 0.1858 0.4010 -0.0151 -0.0049 -0.0544 76  LYS   A NZ  
1658 N  N   . VAL   A 77  ? 0.1701 0.1415 0.1430 -0.0007 0.0203  0.0169  77  VAL   A N   
1659 C  CA  . VAL   A 77  ? 0.1666 0.1437 0.1412 0.0063  0.0158  0.0088  77  VAL   A CA  
1660 C  C   . VAL   A 77  ? 0.1671 0.1378 0.1517 0.0072  0.0148  0.0069  77  VAL   A C   
1661 O  O   . VAL   A 77  ? 0.1702 0.1421 0.1512 0.0137  0.0290  -0.0048 77  VAL   A O   
1662 C  CB  . VAL   A 77  ? 0.1833 0.1596 0.1498 0.0063  0.0176  0.0189  77  VAL   A CB  
1663 C  CG1 . VAL   A 77  ? 0.1842 0.1765 0.1672 0.0179  0.0149  0.0021  77  VAL   A CG1 
1664 C  CG2 . VAL   A 77  ? 0.2108 0.1693 0.1689 -0.0001 0.0063  0.0217  77  VAL   A CG2 
1674 N  N   . GLY   A 78  ? 0.1569 0.1278 0.1511 0.0007  0.0254  0.0034  78  GLY   A N   
1675 C  CA  . GLY   A 78  ? 0.1506 0.1331 0.1616 -0.0013 0.0318  0.0070  78  GLY   A CA  
1676 C  C   . GLY   A 78  ? 0.1410 0.1262 0.1584 0.0051  0.0264  0.0111  78  GLY   A C   
1677 O  O   . GLY   A 78  ? 0.1359 0.1313 0.1906 0.0001  0.0180  0.0296  78  GLY   A O   
1681 N  N   . GLY   A 79  ? 0.1450 0.1207 0.1521 -0.0007 0.0191  0.0121  79  GLY   A N   
1682 C  CA  . GLY   A 79  ? 0.1458 0.1278 0.1583 0.0003  0.0198  0.0158  79  GLY   A CA  
1683 C  C   . GLY   A 79  ? 0.1324 0.1257 0.1616 -0.0028 0.0114  0.0121  79  GLY   A C   
1684 O  O   . GLY   A 79  ? 0.1343 0.1325 0.1700 0.0138  0.0121  0.0106  79  GLY   A O   
1688 N  N   . SER   A 80  ? 0.1282 0.1308 0.1844 0.0043  0.0145  -0.0011 80  SER   A N   
1689 C  CA  . SER   A 80  ? 0.1299 0.1271 0.1739 -0.0000 0.0108  0.0036  80  SER   A CA  
1690 C  C   . SER   A 80  ? 0.1224 0.1322 0.1652 -0.0036 0.0035  0.0124  80  SER   A C   
1691 O  O   . SER   A 80  ? 0.1239 0.1573 0.1936 0.0022  0.0081  0.0017  80  SER   A O   
1692 C  CB  . SER   A 80  ? 0.1424 0.1295 0.2000 -0.0082 0.0082  0.0102  80  SER   A CB  
1693 O  OG  . SER   A 80  ? 0.1648 0.1293 0.2365 0.0062  -0.0039 0.0298  80  SER   A OG  
1699 N  N   . CYS   A 81  ? 0.1192 0.1251 0.1781 -0.0022 -0.0067 0.0220  81  CYS   A N   
1700 C  CA  . CYS   A 81  ? 0.1195 0.1394 0.1690 -0.0045 -0.0078 0.0275  81  CYS   A CA  
1701 C  C   . CYS   A 81  ? 0.1156 0.1357 0.1666 -0.0127 -0.0003 0.0323  81  CYS   A C   
1702 O  O   . CYS   A 81  ? 0.1150 0.1637 0.1837 -0.0032 -0.0016 0.0400  81  CYS   A O   
1703 C  CB  . CYS   A 81  ? 0.1277 0.1437 0.1858 -0.0171 -0.0019 0.0313  81  CYS   A CB  
1704 S  SG  . CYS   A 81  ? 0.1408 0.1305 0.1766 -0.0139 0.0005  0.0172  81  CYS   A SG  
1710 N  N   . VAL   A 82  ? 0.1222 0.1389 0.1729 0.0001  -0.0099 0.0278  82  VAL   A N   
1711 C  CA  . VAL   A 82  ? 0.1365 0.1461 0.1687 -0.0029 -0.0062 0.0297  82  VAL   A CA  
1712 C  C   . VAL   A 82  ? 0.1330 0.1489 0.1733 -0.0055 -0.0109 0.0301  82  VAL   A C   
1713 O  O   . VAL   A 82  ? 0.1281 0.1601 0.1962 -0.0027 -0.0071 0.0076  82  VAL   A O   
1714 C  CB  . VAL   A 82  ? 0.1628 0.1599 0.1816 0.0035  -0.0011 0.0385  82  VAL   A CB  
1715 C  CG1 . VAL   A 82  ? 0.1835 0.1773 0.2128 0.0046  0.0036  0.0374  82  VAL   A CG1 
1716 C  CG2 . VAL   A 82  ? 0.1661 0.1640 0.2099 0.0021  -0.0024 0.0319  82  VAL   A CG2 
1726 N  N   . LEU   A 83  ? 0.1271 0.1466 0.1595 -0.0125 -0.0046 0.0206  83  LEU   A N   
1727 C  CA  . LEU   A 83  ? 0.1306 0.1472 0.1551 -0.0144 -0.0073 0.0122  83  LEU   A CA  
1728 C  C   . LEU   A 83  ? 0.1360 0.1521 0.1527 -0.0109 -0.0106 0.0238  83  LEU   A C   
1729 O  O   . LEU   A 83  ? 0.1460 0.1589 0.1587 -0.0204 -0.0048 0.0284  83  LEU   A O   
1730 C  CB  . LEU   A 83  ? 0.1387 0.1545 0.1657 -0.0131 -0.0149 0.0123  83  LEU   A CB  
1731 C  CG  . LEU   A 83  ? 0.1482 0.1597 0.1742 -0.0105 0.0052  0.0119  83  LEU   A CG  
1732 C  CD1 . LEU   A 83  ? 0.1623 0.1636 0.1834 -0.0256 0.0001  0.0256  83  LEU   A CD1 
1733 C  CD2 . LEU   A 83  ? 0.1491 0.1771 0.1874 -0.0063 0.0118  0.0212  83  LEU   A CD2 
1745 N  N   . SER   A 84  ? 0.1490 0.1530 0.1578 -0.0119 -0.0145 0.0232  84  SER   A N   
1746 C  CA  . SER   A 84  ? 0.1613 0.1603 0.1472 -0.0145 -0.0149 0.0259  84  SER   A CA  
1747 C  C   . SER   A 84  ? 0.1651 0.1576 0.1385 -0.0238 -0.0008 0.0208  84  SER   A C   
1748 O  O   . SER   A 84  ? 0.1583 0.1716 0.1333 -0.0176 -0.0079 0.0195  84  SER   A O   
1749 C  CB  . SER   A 84  ? 0.1619 0.1818 0.1541 -0.0096 -0.0173 0.0037  84  SER   A CB  
1750 O  OG  . SER   A 84  ? 0.1657 0.2042 0.1680 -0.0158 -0.0219 -0.0078 84  SER   A OG  
1756 N  N   . GLY   A 85  ? 0.1774 0.1774 0.1390 -0.0273 0.0060  0.0148  85  GLY   A N   
1757 C  CA  . GLY   A 85  ? 0.1764 0.1872 0.1512 -0.0324 0.0148  0.0033  85  GLY   A CA  
1758 C  C   . GLY   A 85  ? 0.1704 0.1945 0.1377 -0.0294 -0.0056 0.0082  85  GLY   A C   
1759 O  O   . GLY   A 85  ? 0.1726 0.2012 0.1570 -0.0363 0.0067  -0.0112 85  GLY   A O   
1763 N  N   . HIS   A 86  ? 0.1711 0.1862 0.1340 -0.0242 -0.0092 0.0151  86  HIS   A N   
1764 C  CA  . HIS   A 86  ? 0.1873 0.1967 0.1252 -0.0246 -0.0009 0.0122  86  HIS   A CA  
1765 C  C   . HIS   A 86  ? 0.2123 0.2090 0.1200 -0.0321 -0.0117 0.0044  86  HIS   A C   
1766 O  O   . HIS   A 86  ? 0.2190 0.2304 0.1343 -0.0273 0.0035  0.0045  86  HIS   A O   
1767 C  CB  . HIS   A 86  ? 0.1859 0.1895 0.1419 -0.0195 -0.0008 0.0115  86  HIS   A CB  
1768 C  CG  . HIS   A 86  ? 0.1801 0.1854 0.1453 -0.0143 0.0003  0.0144  86  HIS   A CG  
1769 N  ND1 . HIS   A 86  ? 0.1888 0.1801 0.1884 -0.0243 -0.0021 0.0102  86  HIS   A ND1 
1770 C  CD2 . HIS   A 86  ? 0.1785 0.1774 0.1319 0.0010  0.0062  0.0126  86  HIS   A CD2 
1771 C  CE1 . HIS   A 86  ? 0.1776 0.1775 0.1791 -0.0140 0.0109  0.0167  86  HIS   A CE1 
1772 N  NE2 . HIS   A 86  ? 0.1792 0.1738 0.1569 0.0050  0.0123  0.0264  86  HIS   A NE2 
1780 N  N   . ASN   A 87  ? 0.2267 0.2179 0.1315 -0.0283 0.0179  -0.0073 87  ASN   A N   
1781 C  CA  . ASN   A 87  ? 0.2435 0.2287 0.1430 -0.0280 0.0384  -0.0128 87  ASN   A CA  
1782 C  C   . ASN   A 87  ? 0.2390 0.2439 0.1750 -0.0350 0.0512  0.0076  87  ASN   A C   
1783 O  O   . ASN   A 87  ? 0.2698 0.2630 0.2135 -0.0467 0.0839  0.0013  87  ASN   A O   
1784 C  CB  . ASN   A 87  ? 0.2639 0.2351 0.1515 -0.0206 0.0401  -0.0154 87  ASN   A CB  
1785 C  CG  . ASN   A 87  ? 0.2776 0.2443 0.1551 -0.0076 0.0498  -0.0077 87  ASN   A CG  
1786 O  OD1 . ASN   A 87  ? 0.2951 0.2464 0.1591 0.0095  0.0455  -0.0012 87  ASN   A OD1 
1787 N  ND2 . ASN   A 87  ? 0.2818 0.2641 0.1671 -0.0050 0.0504  0.0003  87  ASN   A ND2 
1794 N  N   A LEU   A 88  ? 0.2158 0.2335 0.1581 -0.0362 0.0337  0.0148  88  LEU   A N   
1795 N  N   B LEU   A 88  ? 0.2217 0.2382 0.1654 -0.0346 0.0392  0.0078  88  LEU   A N   
1796 C  CA  A LEU   A 88  ? 0.1989 0.2309 0.1720 -0.0371 0.0311  0.0293  88  LEU   A CA  
1797 C  CA  B LEU   A 88  ? 0.2071 0.2358 0.1767 -0.0332 0.0363  0.0127  88  LEU   A CA  
1798 C  C   A LEU   A 88  ? 0.1880 0.2306 0.1700 -0.0351 0.0311  0.0288  88  LEU   A C   
1799 C  C   B LEU   A 88  ? 0.1941 0.2321 0.1679 -0.0318 0.0335  0.0206  88  LEU   A C   
1800 O  O   A LEU   A 88  ? 0.1927 0.2293 0.2057 -0.0336 0.0368  0.0383  88  LEU   A O   
1801 O  O   B LEU   A 88  ? 0.1962 0.2313 0.1852 -0.0302 0.0416  0.0335  88  LEU   A O   
1802 C  CB  A LEU   A 88  ? 0.2021 0.2332 0.1828 -0.0432 -0.0040 0.0417  88  LEU   A CB  
1803 C  CB  B LEU   A 88  ? 0.2103 0.2394 0.1898 -0.0351 0.0202  0.0088  88  LEU   A CB  
1804 C  CG  A LEU   A 88  ? 0.2188 0.2417 0.2095 -0.0462 -0.0110 0.0500  88  LEU   A CG  
1805 C  CG  B LEU   A 88  ? 0.2178 0.2452 0.2059 -0.0348 0.0159  0.0045  88  LEU   A CG  
1806 C  CD1 A LEU   A 88  ? 0.2277 0.2454 0.2032 -0.0460 -0.0188 0.0507  88  LEU   A CD1 
1807 C  CD1 B LEU   A 88  ? 0.2205 0.2486 0.2012 -0.0328 0.0142  -0.0012 88  LEU   A CD1 
1808 C  CD2 A LEU   A 88  ? 0.2315 0.2512 0.2474 -0.0399 -0.0095 0.0417  88  LEU   A CD2 
1809 C  CD2 B LEU   A 88  ? 0.2238 0.2496 0.2237 -0.0307 0.0168  0.0007  88  LEU   A CD2 
1832 N  N   . ALA   A 89  ? 0.1874 0.2265 0.1544 -0.0283 0.0225  0.0161  89  ALA   A N   
1833 C  CA  . ALA   A 89  ? 0.1941 0.2217 0.1379 -0.0245 0.0055  0.0274  89  ALA   A CA  
1834 C  C   . ALA   A 89  ? 0.2071 0.2245 0.1548 -0.0238 -0.0141 0.0308  89  ALA   A C   
1835 O  O   . ALA   A 89  ? 0.2044 0.2149 0.1973 -0.0359 -0.0174 0.0016  89  ALA   A O   
1836 C  CB  . ALA   A 89  ? 0.1873 0.2180 0.1327 -0.0194 0.0045  0.0324  89  ALA   A CB  
1843 N  N   . LYS   A 90  ? 0.2170 0.2433 0.1583 -0.0331 -0.0262 0.0350  90  LYS   A N   
1844 C  CA  . LYS   A 90  ? 0.2231 0.2558 0.1577 -0.0286 -0.0377 0.0383  90  LYS   A CA  
1845 C  C   . LYS   A 90  ? 0.1979 0.2362 0.1469 -0.0295 -0.0317 0.0230  90  LYS   A C   
1846 O  O   . LYS   A 90  ? 0.1974 0.2544 0.1784 -0.0269 -0.0391 0.0080  90  LYS   A O   
1847 C  CB  . LYS   A 90  ? 0.2495 0.2905 0.1990 -0.0268 -0.0419 0.0585  90  LYS   A CB  
1848 C  CG  . LYS   A 90  ? 0.2980 0.3293 0.3076 -0.0234 -0.0371 0.0588  90  LYS   A CG  
1849 C  CD  . LYS   A 90  ? 0.3491 0.3722 0.4053 -0.0232 -0.0268 0.0650  90  LYS   A CD  
1850 C  CE  . LYS   A 90  ? 0.3743 0.3940 0.4911 -0.0246 -0.0164 0.0625  90  LYS   A CE  
1851 N  NZ  . LYS   A 90  ? 0.4119 0.4119 0.5369 -0.0271 -0.0073 0.0544  90  LYS   A NZ  
1865 N  N   . HIS   A 91  ? 0.1849 0.2033 0.1177 -0.0316 -0.0393 0.0356  91  HIS   A N   
1866 C  CA  . HIS   A 91  ? 0.1739 0.1803 0.1389 -0.0222 -0.0337 0.0345  91  HIS   A CA  
1867 C  C   . HIS   A 91  ? 0.1550 0.1689 0.1303 -0.0178 -0.0195 0.0323  91  HIS   A C   
1868 O  O   . HIS   A 91  ? 0.1504 0.1839 0.1480 -0.0275 -0.0059 0.0305  91  HIS   A O   
1869 C  CB  . HIS   A 91  ? 0.1946 0.2099 0.1772 -0.0005 -0.0519 0.0379  91  HIS   A CB  
1870 C  CG  . HIS   A 91  ? 0.2429 0.2611 0.2532 0.0120  -0.0700 0.0265  91  HIS   A CG  
1871 N  ND1 . HIS   A 91  ? 0.2525 0.2867 0.2954 0.0213  -0.0854 -0.0003 91  HIS   A ND1 
1872 C  CD2 . HIS   A 91  ? 0.2668 0.2809 0.2726 0.0227  -0.0844 0.0311  91  HIS   A CD2 
1873 C  CE1 . HIS   A 91  ? 0.2658 0.2979 0.3132 0.0269  -0.0839 0.0070  91  HIS   A CE1 
1874 N  NE2 . HIS   A 91  ? 0.2765 0.2965 0.3019 0.0315  -0.0920 0.0191  91  HIS   A NE2 
1882 N  N   . CYS   A 92  ? 0.1455 0.1631 0.1276 -0.0242 -0.0133 0.0251  92  CYS   A N   
1883 C  CA  . CYS   A 92  ? 0.1396 0.1538 0.1314 -0.0182 -0.0039 0.0196  92  CYS   A CA  
1884 C  C   . CYS   A 92  ? 0.1336 0.1462 0.1402 -0.0156 -0.0023 0.0179  92  CYS   A C   
1885 O  O   . CYS   A 92  ? 0.1354 0.1519 0.1547 -0.0237 -0.0094 0.0182  92  CYS   A O   
1886 C  CB  . CYS   A 92  ? 0.1376 0.1531 0.1465 -0.0101 -0.0132 0.0141  92  CYS   A CB  
1887 S  SG  . CYS   A 92  ? 0.1359 0.1394 0.1487 -0.0136 -0.0055 0.0147  92  CYS   A SG  
1893 N  N   . LEU   A 93  ? 0.1330 0.1321 0.1457 -0.0110 0.0049  0.0183  93  LEU   A N   
1894 C  CA  . LEU   A 93  ? 0.1228 0.1293 0.1417 -0.0093 0.0029  0.0216  93  LEU   A CA  
1895 C  C   . LEU   A 93  ? 0.1213 0.1204 0.1390 -0.0047 0.0029  0.0149  93  LEU   A C   
1896 O  O   . LEU   A 93  ? 0.1154 0.1291 0.1427 -0.0067 -0.0042 0.0177  93  LEU   A O   
1897 C  CB  . LEU   A 93  ? 0.1305 0.1322 0.1612 -0.0080 -0.0059 0.0311  93  LEU   A CB  
1898 C  CG  . LEU   A 93  ? 0.1396 0.1304 0.1700 -0.0023 -0.0007 0.0282  93  LEU   A CG  
1899 C  CD1 . LEU   A 93  ? 0.1422 0.1353 0.1847 0.0018  -0.0000 0.0190  93  LEU   A CD1 
1900 C  CD2 . LEU   A 93  ? 0.1473 0.1269 0.1922 -0.0125 -0.0028 0.0221  93  LEU   A CD2 
1912 N  N   . HIS   A 94  ? 0.1131 0.1173 0.1421 -0.0038 0.0086  0.0204  94  HIS   A N   
1913 C  CA  . HIS   A 94  ? 0.1120 0.1161 0.1409 -0.0071 0.0007  0.0240  94  HIS   A CA  
1914 C  C   . HIS   A 94  ? 0.1122 0.1167 0.1471 -0.0062 0.0017  0.0107  94  HIS   A C   
1915 O  O   . HIS   A 94  ? 0.1117 0.1392 0.1802 -0.0021 -0.0036 -0.0013 94  HIS   A O   
1916 C  CB  . HIS   A 94  ? 0.1142 0.1173 0.1534 -0.0062 -0.0067 0.0112  94  HIS   A CB  
1917 C  CG  . HIS   A 94  ? 0.1197 0.1190 0.1290 -0.0057 -0.0040 0.0213  94  HIS   A CG  
1918 N  ND1 . HIS   A 94  ? 0.1215 0.1205 0.1398 -0.0033 -0.0027 0.0192  94  HIS   A ND1 
1919 C  CD2 . HIS   A 94  ? 0.1281 0.1280 0.1420 -0.0072 -0.0062 0.0093  94  HIS   A CD2 
1920 C  CE1 . HIS   A 94  ? 0.1221 0.1238 0.1397 -0.0117 -0.0088 0.0122  94  HIS   A CE1 
1921 N  NE2 . HIS   A 94  ? 0.1278 0.1274 0.1473 -0.0125 -0.0060 0.0084  94  HIS   A NE2 
1929 N  N   . VAL   A 95  ? 0.1098 0.1118 0.1276 -0.0028 0.0041  0.0038  95  VAL   A N   
1930 C  CA  . VAL   A 95  ? 0.1207 0.1170 0.1371 -0.0051 0.0091  0.0134  95  VAL   A CA  
1931 C  C   . VAL   A 95  ? 0.1179 0.1124 0.1330 -0.0105 0.0049  0.0094  95  VAL   A C   
1932 O  O   . VAL   A 95  ? 0.1260 0.1281 0.1303 0.0078  0.0033  0.0102  95  VAL   A O   
1933 C  CB  . VAL   A 95  ? 0.1207 0.1183 0.1524 -0.0081 0.0039  0.0157  95  VAL   A CB  
1934 C  CG1 . VAL   A 95  ? 0.1348 0.1160 0.1684 -0.0150 0.0041  0.0083  95  VAL   A CG1 
1935 C  CG2 . VAL   A 95  ? 0.1275 0.1244 0.1662 -0.0159 0.0079  0.0282  95  VAL   A CG2 
1945 N  N   . VAL   A 96  ? 0.1205 0.1144 0.1256 -0.0012 0.0098  0.0164  96  VAL   A N   
1946 C  CA  . VAL   A 96  ? 0.1316 0.1171 0.1341 0.0008  0.0090  0.0231  96  VAL   A CA  
1947 C  C   . VAL   A 96  ? 0.1345 0.1255 0.1346 -0.0068 0.0144  0.0180  96  VAL   A C   
1948 O  O   . VAL   A 96  ? 0.1428 0.1294 0.1676 -0.0076 0.0202  -0.0029 96  VAL   A O   
1949 C  CB  . VAL   A 96  ? 0.1317 0.1243 0.1482 -0.0024 0.0190  0.0202  96  VAL   A CB  
1950 C  CG1 . VAL   A 96  ? 0.1420 0.1333 0.1320 -0.0060 0.0234  0.0108  96  VAL   A CG1 
1951 C  CG2 . VAL   A 96  ? 0.1325 0.1309 0.1665 -0.0119 0.0165  0.0124  96  VAL   A CG2 
1961 N  N   . GLY   A 97  ? 0.1328 0.1292 0.1345 -0.0082 0.0085  0.0142  97  GLY   A N   
1962 C  CA  . GLY   A 97  ? 0.1475 0.1419 0.1351 -0.0051 0.0002  0.0114  97  GLY   A CA  
1963 C  C   . GLY   A 97  ? 0.1482 0.1530 0.1271 -0.0059 0.0006  0.0048  97  GLY   A C   
1964 O  O   . GLY   A 97  ? 0.1587 0.1541 0.1548 -0.0087 -0.0033 0.0164  97  GLY   A O   
1968 N  N   . PRO   A 98  ? 0.1461 0.1567 0.1158 -0.0010 -0.0012 0.0150  98  PRO   A N   
1969 C  CA  . PRO   A 98  ? 0.1583 0.1852 0.1412 -0.0118 0.0026  0.0099  98  PRO   A CA  
1970 C  C   . PRO   A 98  ? 0.1668 0.2003 0.1273 -0.0200 -0.0047 0.0284  98  PRO   A C   
1971 O  O   . PRO   A 98  ? 0.1551 0.1753 0.1560 -0.0096 -0.0056 0.0225  98  PRO   A O   
1972 C  CB  . PRO   A 98  ? 0.1665 0.1940 0.1352 0.0003  -0.0029 -0.0111 98  PRO   A CB  
1973 C  CG  . PRO   A 98  ? 0.1682 0.1858 0.1461 0.0010  -0.0017 -0.0143 98  PRO   A CG  
1974 C  CD  . PRO   A 98  ? 0.1542 0.1605 0.1325 0.0039  -0.0036 0.0001  98  PRO   A CD  
1982 N  N   A ASN   A 99  ? 0.1700 0.2266 0.1213 -0.0208 0.0051  0.0485  99  ASN   A N   
1983 N  N   B ASN   A 99  ? 0.1915 0.2132 0.1361 -0.0123 -0.0188 0.0447  99  ASN   A N   
1984 C  CA  A ASN   A 99  ? 0.1843 0.2425 0.1205 -0.0297 -0.0028 0.0598  99  ASN   A CA  
1985 C  CA  B ASN   A 99  ? 0.2198 0.2181 0.1459 -0.0084 -0.0342 0.0517  99  ASN   A CA  
1986 C  C   A ASN   A 99  ? 0.1942 0.2696 0.1110 -0.0446 -0.0004 0.0613  99  ASN   A C   
1987 C  C   B ASN   A 99  ? 0.2402 0.2172 0.1552 -0.0033 -0.0346 0.0433  99  ASN   A C   
1988 O  O   A ASN   A 99  ? 0.2006 0.2796 0.1189 -0.0464 -0.0022 0.0563  99  ASN   A O   
1989 O  O   B ASN   A 99  ? 0.2431 0.1986 0.1541 -0.0009 -0.0452 0.0277  99  ASN   A O   
1990 C  CB  A ASN   A 99  ? 0.1862 0.2283 0.1210 -0.0285 -0.0157 0.0653  99  ASN   A CB  
1991 C  CB  B ASN   A 99  ? 0.2284 0.2217 0.1597 -0.0113 -0.0465 0.0648  99  ASN   A CB  
1992 C  CG  A ASN   A 99  ? 0.1840 0.2190 0.1139 -0.0274 -0.0279 0.0512  99  ASN   A CG  
1993 C  CG  B ASN   A 99  ? 0.2342 0.2250 0.1737 -0.0151 -0.0483 0.0826  99  ASN   A CG  
1994 O  OD1 A ASN   A 99  ? 0.1921 0.2307 0.1091 -0.0162 -0.0266 0.0388  99  ASN   A OD1 
1995 O  OD1 B ASN   A 99  ? 0.2422 0.2368 0.1647 -0.0219 -0.0441 0.0876  99  ASN   A OD1 
1996 N  ND2 A ASN   A 99  ? 0.1865 0.2179 0.1244 -0.0217 -0.0328 0.0606  99  ASN   A ND2 
1997 N  ND2 B ASN   A 99  ? 0.2349 0.2252 0.1836 -0.0057 -0.0617 0.0787  99  ASN   A ND2 
2010 N  N   A VAL   A 100 ? 0.2059 0.2817 0.1274 -0.0563 -0.0292 0.0487  100 VAL   A N   
2011 N  N   B VAL   A 100 ? 0.2548 0.2371 0.1743 0.0008  -0.0337 0.0440  100 VAL   A N   
2012 C  CA  A VAL   A 100 ? 0.2259 0.2934 0.1537 -0.0626 -0.0386 0.0431  100 VAL   A CA  
2013 C  CA  B VAL   A 100 ? 0.2674 0.2559 0.2111 0.0034  -0.0256 0.0372  100 VAL   A CA  
2014 C  C   A VAL   A 100 ? 0.2339 0.2951 0.1330 -0.0677 -0.0344 0.0606  100 VAL   A C   
2015 C  C   B VAL   A 100 ? 0.2801 0.2610 0.2188 0.0097  -0.0263 0.0437  100 VAL   A C   
2016 O  O   A VAL   A 100 ? 0.2490 0.2949 0.1537 -0.0588 -0.0049 0.0596  100 VAL   A O   
2017 O  O   B VAL   A 100 ? 0.2807 0.2541 0.2285 0.0135  -0.0254 0.0445  100 VAL   A O   
2018 C  CB  A VAL   A 100 ? 0.2435 0.3012 0.2041 -0.0639 -0.0475 0.0291  100 VAL   A CB  
2019 C  CB  B VAL   A 100 ? 0.2683 0.2659 0.2371 0.0045  -0.0223 0.0242  100 VAL   A CB  
2020 C  CG1 A VAL   A 100 ? 0.2443 0.3086 0.2314 -0.0626 -0.0454 0.0234  100 VAL   A CG1 
2021 C  CG1 B VAL   A 100 ? 0.2670 0.2665 0.2461 0.0062  -0.0176 0.0211  100 VAL   A CG1 
2022 C  CG2 A VAL   A 100 ? 0.2508 0.3004 0.2043 -0.0679 -0.0561 0.0211  100 VAL   A CG2 
2023 C  CG2 B VAL   A 100 ? 0.2697 0.2722 0.2411 0.0014  -0.0236 0.0182  100 VAL   A CG2 
2042 N  N   A ASN   A 101 ? 0.2356 0.3071 0.1404 -0.0731 -0.0333 0.0806  101 ASN   A N   
2043 N  N   B ASN   A 101 ? 0.2929 0.2689 0.2240 0.0105  -0.0290 0.0466  101 ASN   A N   
2044 C  CA  A ASN   A 101 ? 0.2550 0.3168 0.1496 -0.0735 -0.0315 0.0986  101 ASN   A CA  
2045 C  CA  B ASN   A 101 ? 0.3063 0.2722 0.2293 0.0110  -0.0239 0.0471  101 ASN   A CA  
2046 C  C   A ASN   A 101 ? 0.2813 0.3442 0.1733 -0.0775 -0.0079 0.1163  101 ASN   A C   
2047 C  C   B ASN   A 101 ? 0.3191 0.2811 0.2382 0.0100  -0.0160 0.0590  101 ASN   A C   
2048 O  O   A ASN   A 101 ? 0.2959 0.3462 0.2169 -0.0733 -0.0163 0.1063  101 ASN   A O   
2049 O  O   B ASN   A 101 ? 0.3237 0.2798 0.2291 0.0093  -0.0227 0.0724  101 ASN   A O   
2050 C  CB  A ASN   A 101 ? 0.2536 0.3003 0.1536 -0.0677 -0.0413 0.0854  101 ASN   A CB  
2051 C  CB  B ASN   A 101 ? 0.3054 0.2685 0.2345 0.0095  -0.0237 0.0360  101 ASN   A CB  
2052 C  CG  A ASN   A 101 ? 0.2523 0.2823 0.1602 -0.0646 -0.0459 0.0546  101 ASN   A CG  
2053 C  CG  B ASN   A 101 ? 0.3069 0.2695 0.2424 0.0043  -0.0253 0.0305  101 ASN   A CG  
2054 O  OD1 A ASN   A 101 ? 0.2464 0.2816 0.1695 -0.0466 -0.0449 0.0250  101 ASN   A OD1 
2055 O  OD1 B ASN   A 101 ? 0.3114 0.2714 0.2523 -0.0005 -0.0250 0.0312  101 ASN   A OD1 
2056 N  ND2 A ASN   A 101 ? 0.2541 0.2718 0.1622 -0.0741 -0.0444 0.0581  101 ASN   A ND2 
2057 N  ND2 B ASN   A 101 ? 0.3053 0.2703 0.2492 0.0057  -0.0239 0.0198  101 ASN   A ND2 
2070 N  N   A LYS   A 102 ? 0.2891 0.3740 0.2098 -0.0853 0.0097  0.1161  102 LYS   A N   
2071 N  N   B LYS   A 102 ? 0.3275 0.2924 0.2636 0.0083  0.0001  0.0594  102 LYS   A N   
2072 C  CA  A LYS   A 102 ? 0.3046 0.4009 0.2353 -0.0827 0.0048  0.1076  102 LYS   A CA  
2073 C  CA  B LYS   A 102 ? 0.3367 0.3044 0.2776 0.0022  0.0115  0.0570  102 LYS   A CA  
2074 C  C   A LYS   A 102 ? 0.3143 0.4221 0.2360 -0.0704 0.0087  0.0938  102 LYS   A C   
2075 C  C   B LYS   A 102 ? 0.3321 0.2999 0.2488 0.0067  0.0119  0.0741  102 LYS   A C   
2076 O  O   A LYS   A 102 ? 0.3158 0.4299 0.2457 -0.0658 0.0127  0.0879  102 LYS   A O   
2077 O  O   B LYS   A 102 ? 0.3350 0.2971 0.2402 0.0089  0.0176  0.0900  102 LYS   A O   
2078 C  CB  A LYS   A 102 ? 0.3150 0.4064 0.2743 -0.0871 -0.0053 0.0973  102 LYS   A CB  
2079 C  CB  B LYS   A 102 ? 0.3493 0.3187 0.3152 -0.0057 0.0135  0.0390  102 LYS   A CB  
2080 C  CG  A LYS   A 102 ? 0.3242 0.4076 0.3071 -0.0910 -0.0173 0.0834  102 LYS   A CG  
2081 C  CG  B LYS   A 102 ? 0.3591 0.3300 0.3570 -0.0132 0.0157  0.0236  102 LYS   A CG  
2082 C  CD  A LYS   A 102 ? 0.3363 0.4105 0.3436 -0.0933 -0.0286 0.0648  102 LYS   A CD  
2083 C  CD  B LYS   A 102 ? 0.3682 0.3406 0.3948 -0.0190 0.0157  0.0096  102 LYS   A CD  
2084 C  CE  A LYS   A 102 ? 0.3466 0.4132 0.3683 -0.0958 -0.0367 0.0550  102 LYS   A CE  
2085 C  CE  B LYS   A 102 ? 0.3745 0.3479 0.4289 -0.0240 0.0133  -0.0003 102 LYS   A CE  
2086 N  NZ  A LYS   A 102 ? 0.3529 0.4135 0.3852 -0.1011 -0.0338 0.0472  102 LYS   A NZ  
2087 N  NZ  B LYS   A 102 ? 0.3778 0.3519 0.4460 -0.0269 0.0128  -0.0072 102 LYS   A NZ  
2114 N  N   A GLY   A 103 ? 0.3214 0.4357 0.2508 -0.0578 0.0061  0.0698  103 GLY   A N   
2115 N  N   B GLY   A 103 ? 0.3245 0.3031 0.2413 0.0105  0.0003  0.0663  103 GLY   A N   
2116 C  CA  A GLY   A 103 ? 0.3298 0.4449 0.2564 -0.0453 0.0075  0.0518  103 GLY   A CA  
2117 C  CA  B GLY   A 103 ? 0.3175 0.2996 0.2291 0.0123  -0.0078 0.0731  103 GLY   A CA  
2118 C  C   A GLY   A 103 ? 0.3339 0.4520 0.2594 -0.0392 0.0160  0.0428  103 GLY   A C   
2119 C  C   B GLY   A 103 ? 0.3078 0.2943 0.2120 0.0101  -0.0100 0.0707  103 GLY   A C   
2120 O  O   A GLY   A 103 ? 0.3462 0.4552 0.2762 -0.0380 0.0191  0.0353  103 GLY   A O   
2121 O  O   B GLY   A 103 ? 0.3142 0.2940 0.2083 0.0092  -0.0141 0.0771  103 GLY   A O   
2128 N  N   A GLU   A 104 ? 0.3206 0.4514 0.2308 -0.0412 0.0294  0.0381  104 GLU   A N   
2129 N  N   B GLU   A 104 ? 0.2907 0.2878 0.1967 0.0081  -0.0156 0.0652  104 GLU   A N   
2130 C  CA  A GLU   A 104 ? 0.3017 0.4456 0.2098 -0.0490 0.0346  0.0300  104 GLU   A CA  
2131 C  CA  B GLU   A 104 ? 0.2739 0.2802 0.1786 0.0010  -0.0243 0.0505  104 GLU   A CA  
2132 C  C   A GLU   A 104 ? 0.3039 0.4542 0.2072 -0.0473 0.0357  0.0090  104 GLU   A C   
2133 C  C   B GLU   A 104 ? 0.2686 0.2778 0.1852 0.0063  -0.0221 0.0267  104 GLU   A C   
2134 O  O   A GLU   A 104 ? 0.2964 0.4548 0.2138 -0.0480 0.0220  0.0085  104 GLU   A O   
2135 O  O   B GLU   A 104 ? 0.2634 0.2660 0.1905 0.0099  -0.0264 0.0293  104 GLU   A O   
2136 C  CB  A GLU   A 104 ? 0.2743 0.4285 0.1857 -0.0574 0.0429  0.0510  104 GLU   A CB  
2137 C  CB  B GLU   A 104 ? 0.2646 0.2777 0.1715 -0.0095 -0.0289 0.0585  104 GLU   A CB  
2138 C  CG  A GLU   A 104 ? 0.2525 0.4120 0.1858 -0.0602 0.0402  0.0690  104 GLU   A CG  
2139 C  CG  B GLU   A 104 ? 0.2592 0.2818 0.1806 -0.0148 -0.0410 0.0594  104 GLU   A CG  
2140 C  CD  A GLU   A 104 ? 0.2293 0.3977 0.1825 -0.0647 0.0409  0.0821  104 GLU   A CD  
2141 C  CD  B GLU   A 104 ? 0.2506 0.2832 0.1881 -0.0166 -0.0510 0.0614  104 GLU   A CD  
2142 O  OE1 A GLU   A 104 ? 0.2105 0.3793 0.1567 -0.0647 0.0304  0.0819  104 GLU   A OE1 
2143 O  OE1 B GLU   A 104 ? 0.2444 0.2825 0.1813 -0.0134 -0.0596 0.0635  104 GLU   A OE1 
2144 O  OE2 A GLU   A 104 ? 0.2419 0.3936 0.2006 -0.0607 0.0398  0.0952  104 GLU   A OE2 
2145 O  OE2 B GLU   A 104 ? 0.2569 0.2842 0.2062 -0.0202 -0.0480 0.0580  104 GLU   A OE2 
2158 N  N   A ASP   A 105 ? 0.3126 0.4607 0.2253 -0.0423 0.0431  -0.0169 105 ASP   A N   
2159 N  N   B ASP   A 105 ? 0.2751 0.2896 0.2024 0.0040  -0.0160 0.0028  105 ASP   A N   
2160 C  CA  A ASP   A 105 ? 0.3174 0.4649 0.2528 -0.0390 0.0491  -0.0409 105 ASP   A CA  
2161 C  CA  B ASP   A 105 ? 0.2800 0.3003 0.2266 0.0050  -0.0047 -0.0267 105 ASP   A CA  
2162 C  C   A ASP   A 105 ? 0.2886 0.4486 0.2206 -0.0501 0.0446  -0.0636 105 ASP   A C   
2163 C  C   B ASP   A 105 ? 0.2762 0.3025 0.2094 -0.0078 -0.0012 -0.0387 105 ASP   A C   
2164 O  O   A ASP   A 105 ? 0.2746 0.4457 0.1793 -0.0530 0.0485  -0.0908 105 ASP   A O   
2165 O  O   B ASP   A 105 ? 0.2687 0.2994 0.1667 -0.0107 -0.0037 -0.0509 105 ASP   A O   
2166 C  CB  A ASP   A 105 ? 0.3458 0.4797 0.3208 -0.0257 0.0533  -0.0439 105 ASP   A CB  
2167 C  CB  B ASP   A 105 ? 0.2898 0.3093 0.2738 0.0160  -0.0003 -0.0398 105 ASP   A CB  
2168 C  CG  A ASP   A 105 ? 0.3678 0.4898 0.3792 -0.0155 0.0554  -0.0478 105 ASP   A CG  
2169 C  CG  B ASP   A 105 ? 0.2988 0.3155 0.3098 0.0261  0.0015  -0.0509 105 ASP   A CG  
2170 O  OD1 A ASP   A 105 ? 0.3733 0.4954 0.3896 -0.0161 0.0553  -0.0552 105 ASP   A OD1 
2171 O  OD1 B ASP   A 105 ? 0.3063 0.3161 0.3162 0.0255  -0.0010 -0.0570 105 ASP   A OD1 
2172 O  OD2 A ASP   A 105 ? 0.3825 0.4924 0.4028 -0.0100 0.0591  -0.0420 105 ASP   A OD2 
2173 O  OD2 B ASP   A 105 ? 0.2997 0.3191 0.3361 0.0295  -0.0012 -0.0494 105 ASP   A OD2 
2182 N  N   A ILE   A 106 ? 0.2715 0.4312 0.2345 -0.0614 0.0191  -0.0661 106 ILE   A N   
2183 N  N   B ILE   A 106 ? 0.2766 0.3068 0.2338 -0.0160 -0.0015 -0.0392 106 ILE   A N   
2184 C  CA  A ILE   A 106 ? 0.2447 0.4097 0.2399 -0.0787 -0.0136 -0.0817 106 ILE   A CA  
2185 C  CA  B ILE   A 106 ? 0.2752 0.3138 0.2593 -0.0304 -0.0061 -0.0453 106 ILE   A CA  
2186 C  C   A ILE   A 106 ? 0.2275 0.3828 0.2437 -0.0978 -0.0120 -0.1022 106 ILE   A C   
2187 C  C   B ILE   A 106 ? 0.2754 0.3141 0.2662 -0.0410 0.0043  -0.0480 106 ILE   A C   
2188 O  O   A ILE   A 106 ? 0.2080 0.3753 0.2512 -0.1051 0.0071  -0.1007 106 ILE   A O   
2189 O  O   B ILE   A 106 ? 0.2713 0.3155 0.2676 -0.0437 0.0084  -0.0475 106 ILE   A O   
2190 C  CB  A ILE   A 106 ? 0.2463 0.4186 0.2801 -0.0668 -0.0335 -0.0537 106 ILE   A CB  
2191 C  CB  B ILE   A 106 ? 0.2774 0.3240 0.2860 -0.0305 -0.0182 -0.0358 106 ILE   A CB  
2192 C  CG1 A ILE   A 106 ? 0.2379 0.4233 0.3036 -0.0548 -0.0388 -0.0327 106 ILE   A CG1 
2193 C  CG1 B ILE   A 106 ? 0.2734 0.3319 0.3046 -0.0265 -0.0223 -0.0259 106 ILE   A CG1 
2194 C  CG2 A ILE   A 106 ? 0.2527 0.4197 0.2859 -0.0655 -0.0401 -0.0530 106 ILE   A CG2 
2195 C  CG2 B ILE   A 106 ? 0.2804 0.3245 0.2911 -0.0316 -0.0219 -0.0382 106 ILE   A CG2 
2196 C  CD1 A ILE   A 106 ? 0.2393 0.4253 0.3216 -0.0418 -0.0305 -0.0222 106 ILE   A CD1 
2197 C  CD1 B ILE   A 106 ? 0.2723 0.3353 0.3165 -0.0217 -0.0197 -0.0230 106 ILE   A CD1 
2220 N  N   A GLN   A 107 ? 0.2460 0.3639 0.2723 -0.0906 0.0068  -0.1118 107 GLN   A N   
2221 N  N   B GLN   A 107 ? 0.2811 0.3089 0.2864 -0.0440 0.0188  -0.0530 107 GLN   A N   
2222 C  CA  A GLN   A 107 ? 0.2684 0.3441 0.3446 -0.0726 0.0293  -0.1027 107 GLN   A CA  
2223 C  CA  B GLN   A 107 ? 0.2861 0.3060 0.3278 -0.0450 0.0322  -0.0591 107 GLN   A CA  
2224 C  C   A GLN   A 107 ? 0.2424 0.2946 0.3258 -0.0614 0.0540  -0.0837 107 GLN   A C   
2225 C  C   B GLN   A 107 ? 0.2547 0.2778 0.3058 -0.0491 0.0494  -0.0644 107 GLN   A C   
2226 O  O   A GLN   A 107 ? 0.2448 0.2860 0.3766 -0.0563 0.0675  -0.0826 107 GLN   A O   
2227 O  O   B GLN   A 107 ? 0.2592 0.2753 0.3320 -0.0496 0.0503  -0.0612 107 GLN   A O   
2228 C  CB  A GLN   A 107 ? 0.3089 0.3714 0.4370 -0.0728 0.0190  -0.1018 107 GLN   A CB  
2229 C  CB  B GLN   A 107 ? 0.3168 0.3297 0.3945 -0.0452 0.0235  -0.0549 107 GLN   A CB  
2230 C  CG  A GLN   A 107 ? 0.3505 0.4036 0.5347 -0.0672 0.0112  -0.0929 107 GLN   A CG  
2231 C  CG  B GLN   A 107 ? 0.3464 0.3533 0.4637 -0.0442 0.0169  -0.0491 107 GLN   A CG  
2232 C  CD  A GLN   A 107 ? 0.3760 0.4234 0.6172 -0.0621 0.0099  -0.0807 107 GLN   A CD  
2233 C  CD  B GLN   A 107 ? 0.3705 0.3742 0.5214 -0.0418 0.0140  -0.0413 107 GLN   A CD  
2234 O  OE1 A GLN   A 107 ? 0.3816 0.4321 0.6487 -0.0579 0.0117  -0.0790 107 GLN   A OE1 
2235 O  OE1 B GLN   A 107 ? 0.3804 0.3790 0.5466 -0.0393 0.0141  -0.0381 107 GLN   A OE1 
2236 N  NE2 A GLN   A 107 ? 0.3929 0.4333 0.6471 -0.0633 0.0064  -0.0770 107 GLN   A NE2 
2237 N  NE2 B GLN   A 107 ? 0.3801 0.3832 0.5428 -0.0433 0.0125  -0.0401 107 GLN   A NE2 
2254 N  N   . LEU   A 108 ? 0.2181 0.2504 0.2687 -0.0545 0.0545  -0.0764 108 LEU   A N   
2255 C  CA  . LEU   A 108 ? 0.1920 0.1975 0.2274 -0.0233 0.0417  -0.0358 108 LEU   A CA  
2256 C  C   . LEU   A 108 ? 0.1651 0.1496 0.2196 -0.0105 0.0345  -0.0077 108 LEU   A C   
2257 O  O   . LEU   A 108 ? 0.1556 0.1420 0.2415 -0.0015 0.0444  0.0010  108 LEU   A O   
2258 C  CB  . LEU   A 108 ? 0.1932 0.2055 0.2139 -0.0268 0.0507  -0.0264 108 LEU   A CB  
2259 C  CG  . LEU   A 108 ? 0.2063 0.2326 0.2426 -0.0257 0.0577  -0.0229 108 LEU   A CG  
2260 C  CD1 . LEU   A 108 ? 0.2211 0.2370 0.2441 -0.0315 0.0608  -0.0177 108 LEU   A CD1 
2261 C  CD2 . LEU   A 108 ? 0.2093 0.2530 0.2797 -0.0187 0.0566  -0.0169 108 LEU   A CD2 
2274 N  N   . LEU   A 109 ? 0.1477 0.1425 0.2113 0.0050  0.0221  0.0109  109 LEU   A N   
2275 C  CA  . LEU   A 109 ? 0.1470 0.1380 0.1915 0.0005  0.0178  0.0157  109 LEU   A CA  
2276 C  C   . LEU   A 109 ? 0.1372 0.1319 0.1929 -0.0093 0.0175  0.0071  109 LEU   A C   
2277 O  O   . LEU   A 109 ? 0.1499 0.1270 0.2083 -0.0015 0.0058  0.0084  109 LEU   A O   
2278 C  CB  . LEU   A 109 ? 0.1522 0.1466 0.2137 0.0134  0.0064  0.0294  109 LEU   A CB  
2279 C  CG  . LEU   A 109 ? 0.1418 0.1532 0.2189 0.0074  0.0155  0.0370  109 LEU   A CG  
2280 C  CD1 . LEU   A 109 ? 0.1444 0.1401 0.2374 -0.0012 0.0179  0.0186  109 LEU   A CD1 
2281 C  CD2 . LEU   A 109 ? 0.1391 0.1768 0.2520 0.0076  0.0115  0.0422  109 LEU   A CD2 
2293 N  N   . LYS   A 110 ? 0.1368 0.1300 0.1889 -0.0074 0.0054  0.0039  110 LYS   A N   
2294 C  CA  . LYS   A 110 ? 0.1368 0.1239 0.1941 -0.0050 0.0006  0.0083  110 LYS   A CA  
2295 C  C   . LYS   A 110 ? 0.1357 0.1210 0.1874 -0.0065 0.0017  -0.0019 110 LYS   A C   
2296 O  O   . LYS   A 110 ? 0.1275 0.1227 0.2037 -0.0072 0.0069  -0.0062 110 LYS   A O   
2297 C  CB  . LYS   A 110 ? 0.1417 0.1317 0.2154 -0.0038 -0.0125 -0.0018 110 LYS   A CB  
2298 C  CG  . LYS   A 110 ? 0.1454 0.1289 0.2334 -0.0065 -0.0186 -0.0005 110 LYS   A CG  
2299 C  CD  . LYS   A 110 ? 0.1465 0.1391 0.2405 -0.0126 -0.0089 -0.0046 110 LYS   A CD  
2300 C  CE  . LYS   A 110 ? 0.1520 0.1417 0.2537 -0.0134 0.0087  -0.0078 110 LYS   A CE  
2301 N  NZ  . LYS   A 110 ? 0.1581 0.1467 0.2583 -0.0208 0.0166  -0.0015 110 LYS   A NZ  
2315 N  N   . SER   A 111 ? 0.1347 0.1244 0.1838 -0.0017 0.0056  0.0054  111 SER   A N   
2316 C  CA  . SER   A 111 ? 0.1269 0.1275 0.1974 -0.0028 0.0127  0.0036  111 SER   A CA  
2317 C  C   . SER   A 111 ? 0.1237 0.1219 0.1953 -0.0078 0.0116  0.0081  111 SER   A C   
2318 O  O   . SER   A 111 ? 0.1370 0.1171 0.2080 -0.0038 0.0126  0.0076  111 SER   A O   
2319 C  CB  . SER   A 111 ? 0.1417 0.1423 0.2124 0.0001  0.0175  -0.0074 111 SER   A CB  
2320 O  OG  . SER   A 111 ? 0.1934 0.1669 0.2049 0.0043  0.0220  -0.0151 111 SER   A OG  
2326 N  N   . ALA   A 112 ? 0.1286 0.1167 0.1967 -0.0035 0.0180  0.0111  112 ALA   A N   
2327 C  CA  . ALA   A 112 ? 0.1331 0.1154 0.2009 -0.0055 0.0221  0.0063  112 ALA   A CA  
2328 C  C   . ALA   A 112 ? 0.1249 0.1129 0.1909 -0.0020 0.0111  0.0063  112 ALA   A C   
2329 O  O   . ALA   A 112 ? 0.1284 0.1134 0.2048 -0.0128 0.0143  0.0115  112 ALA   A O   
2330 C  CB  . ALA   A 112 ? 0.1440 0.1176 0.2054 -0.0011 0.0189  0.0041  112 ALA   A CB  
2336 N  N   . TYR   A 113 ? 0.1176 0.1200 0.1955 -0.0044 0.0150  0.0125  113 TYR   A N   
2337 C  CA  . TYR   A 113 ? 0.1190 0.1187 0.1945 -0.0041 0.0197  0.0186  113 TYR   A CA  
2338 C  C   . TYR   A 113 ? 0.1172 0.1179 0.1940 -0.0131 0.0182  0.0145  113 TYR   A C   
2339 O  O   . TYR   A 113 ? 0.1253 0.1191 0.2053 -0.0064 0.0179  0.0119  113 TYR   A O   
2340 C  CB  . TYR   A 113 ? 0.1182 0.1269 0.1915 -0.0065 0.0057  0.0253  113 TYR   A CB  
2341 C  CG  . TYR   A 113 ? 0.1195 0.1252 0.1802 -0.0093 0.0111  0.0198  113 TYR   A CG  
2342 C  CD1 . TYR   A 113 ? 0.1215 0.1348 0.1825 -0.0009 0.0164  0.0240  113 TYR   A CD1 
2343 C  CD2 . TYR   A 113 ? 0.1277 0.1351 0.1725 -0.0102 0.0080  0.0204  113 TYR   A CD2 
2344 C  CE1 . TYR   A 113 ? 0.1257 0.1427 0.1823 -0.0060 0.0155  0.0271  113 TYR   A CE1 
2345 C  CE2 . TYR   A 113 ? 0.1272 0.1413 0.1760 -0.0077 0.0086  0.0240  113 TYR   A CE2 
2346 C  CZ  . TYR   A 113 ? 0.1218 0.1415 0.1805 0.0003  0.0140  0.0260  113 TYR   A CZ  
2347 O  OH  . TYR   A 113 ? 0.1226 0.1479 0.1960 0.0080  0.0109  0.0297  113 TYR   A OH  
2357 N  N   . GLU   A 114 ? 0.1218 0.1189 0.1977 -0.0061 0.0161  0.0128  114 GLU   A N   
2358 C  CA  . GLU   A 114 ? 0.1217 0.1112 0.2077 0.0023  0.0114  0.0187  114 GLU   A CA  
2359 C  C   . GLU   A 114 ? 0.1161 0.1173 0.2124 0.0019  0.0138  0.0180  114 GLU   A C   
2360 O  O   . GLU   A 114 ? 0.1315 0.1162 0.2101 0.0008  0.0077  0.0133  114 GLU   A O   
2361 C  CB  . GLU   A 114 ? 0.1225 0.1169 0.2064 -0.0078 0.0072  0.0179  114 GLU   A CB  
2362 C  CG  . GLU   A 114 ? 0.1352 0.1194 0.2185 0.0033  0.0090  0.0090  114 GLU   A CG  
2363 C  CD  . GLU   A 114 ? 0.1420 0.1173 0.2226 -0.0006 0.0053  0.0062  114 GLU   A CD  
2364 O  OE1 . GLU   A 114 ? 0.1425 0.1178 0.2357 -0.0082 0.0192  0.0006  114 GLU   A OE1 
2365 O  OE2 . GLU   A 114 ? 0.1643 0.1269 0.2386 -0.0083 0.0064  -0.0092 114 GLU   A OE2 
2372 N  N   . ASN   A 115 ? 0.1257 0.1211 0.1884 -0.0078 0.0104  0.0125  115 ASN   A N   
2373 C  CA  . ASN   A 115 ? 0.1253 0.1281 0.1974 -0.0115 0.0113  0.0110  115 ASN   A CA  
2374 C  C   . ASN   A 115 ? 0.1234 0.1186 0.1881 -0.0149 0.0085  0.0142  115 ASN   A C   
2375 O  O   . ASN   A 115 ? 0.1270 0.1325 0.1968 -0.0133 0.0080  0.0280  115 ASN   A O   
2376 C  CB  . ASN   A 115 ? 0.1297 0.1321 0.1891 -0.0177 0.0157  0.0075  115 ASN   A CB  
2377 C  CG  . ASN   A 115 ? 0.1307 0.1505 0.1838 -0.0193 0.0216  0.0104  115 ASN   A CG  
2378 O  OD1 . ASN   A 115 ? 0.1378 0.2461 0.2071 -0.0182 0.0266  0.0217  115 ASN   A OD1 
2379 N  ND2 . ASN   A 115 ? 0.1338 0.1301 0.1883 -0.0142 0.0289  0.0112  115 ASN   A ND2 
2386 N  N   . PHE   A 116 ? 0.1236 0.1207 0.2006 -0.0063 0.0102  0.0243  116 PHE   A N   
2387 C  CA  . PHE   A 116 ? 0.1226 0.1332 0.1824 -0.0039 0.0142  0.0195  116 PHE   A CA  
2388 C  C   . PHE   A 116 ? 0.1230 0.1345 0.1920 -0.0080 0.0161  0.0263  116 PHE   A C   
2389 O  O   . PHE   A 116 ? 0.1276 0.1414 0.1997 -0.0054 0.0094  0.0332  116 PHE   A O   
2390 C  CB  . PHE   A 116 ? 0.1232 0.1257 0.1966 -0.0085 0.0168  0.0245  116 PHE   A CB  
2391 C  CG  . PHE   A 116 ? 0.1235 0.1195 0.1851 -0.0013 0.0147  0.0176  116 PHE   A CG  
2392 C  CD1 . PHE   A 116 ? 0.1291 0.1197 0.1791 -0.0058 0.0133  0.0155  116 PHE   A CD1 
2393 C  CD2 . PHE   A 116 ? 0.1279 0.1321 0.2002 -0.0071 0.0193  0.0220  116 PHE   A CD2 
2394 C  CE1 . PHE   A 116 ? 0.1332 0.1176 0.1901 -0.0194 0.0070  0.0132  116 PHE   A CE1 
2395 C  CE2 . PHE   A 116 ? 0.1284 0.1302 0.2046 -0.0040 0.0158  0.0165  116 PHE   A CE2 
2396 C  CZ  . PHE   A 116 ? 0.1340 0.1161 0.1802 -0.0046 0.0057  0.0176  116 PHE   A CZ  
2406 N  N   . ASN   A 117 ? 0.1226 0.1258 0.2144 -0.0098 0.0155  0.0276  117 ASN   A N   
2407 C  CA  . ASN   A 117 ? 0.1268 0.1279 0.2217 -0.0074 0.0119  0.0358  117 ASN   A CA  
2408 C  C   . ASN   A 117 ? 0.1278 0.1385 0.2231 -0.0054 0.0150  0.0347  117 ASN   A C   
2409 O  O   . ASN   A 117 ? 0.1374 0.1490 0.2389 -0.0074 -0.0031 0.0482  117 ASN   A O   
2410 C  CB  . ASN   A 117 ? 0.1266 0.1344 0.2173 -0.0024 0.0100  0.0377  117 ASN   A CB  
2411 C  CG  . ASN   A 117 ? 0.1236 0.1293 0.2154 -0.0034 0.0111  0.0355  117 ASN   A CG  
2412 O  OD1 . ASN   A 117 ? 0.1238 0.1542 0.2323 -0.0147 0.0070  0.0316  117 ASN   A OD1 
2413 N  ND2 . ASN   A 117 ? 0.1269 0.1286 0.2085 -0.0028 0.0058  0.0256  117 ASN   A ND2 
2420 N  N   . GLN   A 118 ? 0.1271 0.1362 0.2226 -0.0069 0.0005  0.0361  118 GLN   A N   
2421 C  CA  . GLN   A 118 ? 0.1305 0.1521 0.2354 -0.0055 -0.0086 0.0299  118 GLN   A CA  
2422 C  C   . GLN   A 118 ? 0.1349 0.1604 0.2284 -0.0108 -0.0018 0.0383  118 GLN   A C   
2423 O  O   . GLN   A 118 ? 0.1310 0.1934 0.2463 -0.0037 -0.0089 0.0215  118 GLN   A O   
2424 C  CB  . GLN   A 118 ? 0.1271 0.1557 0.2414 -0.0083 0.0103  0.0354  118 GLN   A CB  
2425 C  CG  . GLN   A 118 ? 0.1226 0.1582 0.2397 -0.0095 0.0095  0.0366  118 GLN   A CG  
2426 C  CD  . GLN   A 118 ? 0.1193 0.1536 0.2560 -0.0031 0.0092  0.0256  118 GLN   A CD  
2427 O  OE1 . GLN   A 118 ? 0.1234 0.1641 0.2791 0.0058  0.0049  0.0216  118 GLN   A OE1 
2428 N  NE2 . GLN   A 118 ? 0.1356 0.1496 0.2388 0.0032  0.0019  0.0368  118 GLN   A NE2 
2437 N  N   . HIS   A 119 ? 0.1396 0.1527 0.2119 -0.0049 0.0040  0.0415  119 HIS   A N   
2438 C  CA  . HIS   A 119 ? 0.1457 0.1596 0.2103 -0.0057 0.0010  0.0466  119 HIS   A CA  
2439 C  C   . HIS   A 119 ? 0.1543 0.1698 0.2055 -0.0060 0.0001  0.0577  119 HIS   A C   
2440 O  O   . HIS   A 119 ? 0.1551 0.1803 0.2131 -0.0205 -0.0033 0.0563  119 HIS   A O   
2441 C  CB  . HIS   A 119 ? 0.1502 0.1607 0.2265 -0.0058 0.0142  0.0442  119 HIS   A CB  
2442 C  CG  . HIS   A 119 ? 0.1468 0.1686 0.2616 0.0017  0.0116  0.0501  119 HIS   A CG  
2443 N  ND1 . HIS   A 119 ? 0.1577 0.1883 0.3104 -0.0094 0.0111  0.0341  119 HIS   A ND1 
2444 C  CD2 . HIS   A 119 ? 0.1633 0.1731 0.2737 0.0103  0.0348  0.0668  119 HIS   A CD2 
2445 C  CE1 . HIS   A 119 ? 0.1641 0.1886 0.3145 -0.0150 0.0334  0.0615  119 HIS   A CE1 
2446 N  NE2 . HIS   A 119 ? 0.1753 0.1810 0.3004 -0.0007 0.0490  0.0749  119 HIS   A NE2 
2454 N  N   . GLU   A 120 ? 0.1624 0.1981 0.2130 -0.0087 -0.0092 0.0849  120 GLU   A N   
2455 C  CA  . GLU   A 120 ? 0.1881 0.2338 0.2341 -0.0053 -0.0099 0.1221  120 GLU   A CA  
2456 C  C   . GLU   A 120 ? 0.1611 0.2160 0.2111 -0.0180 -0.0065 0.1061  120 GLU   A C   
2457 O  O   . GLU   A 120 ? 0.1631 0.2138 0.2248 -0.0198 -0.0090 0.1016  120 GLU   A O   
2458 C  CB  . GLU   A 120 ? 0.2627 0.3019 0.2977 0.0129  -0.0093 0.1631  120 GLU   A CB  
2459 C  CG  . GLU   A 120 ? 0.3486 0.3686 0.4034 0.0242  -0.0043 0.1648  120 GLU   A CG  
2460 C  CD  . GLU   A 120 ? 0.4249 0.4259 0.5157 0.0349  0.0041  0.1491  120 GLU   A CD  
2461 O  OE1 . GLU   A 120 ? 0.4626 0.4531 0.5473 0.0378  0.0069  0.1421  120 GLU   A OE1 
2462 O  OE2 . GLU   A 120 ? 0.4989 0.4989 0.5686 0.0381  0.0064  0.1405  120 GLU   A OE2 
2469 N  N   . VAL   A 121 ? 0.1586 0.2184 0.1871 -0.0145 0.0010  0.0873  121 VAL   A N   
2470 C  CA  . VAL   A 121 ? 0.1663 0.2199 0.1725 -0.0160 0.0128  0.0828  121 VAL   A CA  
2471 C  C   . VAL   A 121 ? 0.1544 0.2009 0.1556 -0.0199 0.0068  0.0593  121 VAL   A C   
2472 O  O   . VAL   A 121 ? 0.1566 0.2010 0.1763 -0.0299 -0.0043 0.0559  121 VAL   A O   
2473 C  CB  . VAL   A 121 ? 0.2090 0.2542 0.2091 -0.0039 0.0267  0.0848  121 VAL   A CB  
2474 C  CG1 . VAL   A 121 ? 0.2143 0.2685 0.2070 0.0014  0.0395  0.0889  121 VAL   A CG1 
2475 C  CG2 . VAL   A 121 ? 0.2329 0.2706 0.2532 -0.0144 0.0221  0.0669  121 VAL   A CG2 
2485 N  N   . LEU   A 122 ? 0.1422 0.1796 0.1586 -0.0240 0.0044  0.0553  122 LEU   A N   
2486 C  CA  . LEU   A 122 ? 0.1524 0.1617 0.1601 -0.0234 0.0195  0.0449  122 LEU   A CA  
2487 C  C   . LEU   A 122 ? 0.1444 0.1612 0.1628 -0.0273 0.0019  0.0450  122 LEU   A C   
2488 O  O   . LEU   A 122 ? 0.1451 0.1711 0.1931 -0.0302 0.0011  0.0508  122 LEU   A O   
2489 C  CB  . LEU   A 122 ? 0.1694 0.1575 0.1940 -0.0140 0.0076  0.0553  122 LEU   A CB  
2490 C  CG  . LEU   A 122 ? 0.1669 0.1626 0.1892 -0.0091 0.0171  0.0375  122 LEU   A CG  
2491 C  CD1 . LEU   A 122 ? 0.1851 0.1631 0.1983 -0.0118 0.0180  0.0366  122 LEU   A CD1 
2492 C  CD2 . LEU   A 122 ? 0.1617 0.1567 0.1779 -0.0075 0.0274  0.0292  122 LEU   A CD2 
2504 N  N   A LEU   A 123 ? 0.1379 0.1560 0.1621 -0.0288 -0.0017 0.0386  123 LEU   A N   
2505 N  N   B LEU   A 123 ? 0.1422 0.1547 0.1545 -0.0256 -0.0002 0.0331  123 LEU   A N   
2506 C  CA  A LEU   A 123 ? 0.1368 0.1551 0.1426 -0.0248 0.0017  0.0424  123 LEU   A CA  
2507 C  CA  B LEU   A 123 ? 0.1439 0.1527 0.1399 -0.0208 0.0010  0.0253  123 LEU   A CA  
2508 C  C   A LEU   A 123 ? 0.1305 0.1404 0.1464 -0.0228 0.0041  0.0436  123 LEU   A C   
2509 C  C   B LEU   A 123 ? 0.1410 0.1422 0.1220 -0.0159 0.0105  0.0176  123 LEU   A C   
2510 O  O   A LEU   A 123 ? 0.1193 0.1377 0.1588 -0.0230 0.0031  0.0341  123 LEU   A O   
2511 O  O   B LEU   A 123 ? 0.1383 0.1394 0.1190 -0.0108 0.0207  0.0058  123 LEU   A O   
2512 C  CB  A LEU   A 123 ? 0.1496 0.1743 0.1372 -0.0275 0.0171  0.0388  123 LEU   A CB  
2513 C  CB  B LEU   A 123 ? 0.1523 0.1630 0.1489 -0.0256 -0.0035 0.0245  123 LEU   A CB  
2514 C  CG  A LEU   A 123 ? 0.1573 0.1924 0.1516 -0.0156 0.0225  0.0202  123 LEU   A CG  
2515 C  CG  B LEU   A 123 ? 0.1563 0.1723 0.1528 -0.0259 0.0003  0.0210  123 LEU   A CG  
2516 C  CD1 A LEU   A 123 ? 0.1614 0.1980 0.1629 -0.0066 0.0260  0.0103  123 LEU   A CD1 
2517 C  CD1 B LEU   A 123 ? 0.1622 0.1758 0.1577 -0.0215 0.0000  0.0193  123 LEU   A CD1 
2518 C  CD2 A LEU   A 123 ? 0.1693 0.2021 0.1559 -0.0093 0.0147  0.0207  123 LEU   A CD2 
2519 C  CD2 B LEU   A 123 ? 0.1610 0.1774 0.1576 -0.0237 0.0004  0.0208  123 LEU   A CD2 
2542 N  N   A ALA   A 124 ? 0.1291 0.1310 0.1417 -0.0151 0.0056  0.0349  124 ALA   A N   
2543 N  N   B ALA   A 124 ? 0.1391 0.1334 0.1156 -0.0115 0.0116  0.0092  124 ALA   A N   
2544 C  CA  A ALA   A 124 ? 0.1201 0.1259 0.1460 -0.0112 0.0029  0.0336  124 ALA   A CA  
2545 C  CA  B ALA   A 124 ? 0.1395 0.1400 0.1234 -0.0185 0.0007  0.0173  124 ALA   A CA  
2546 C  C   A ALA   A 124 ? 0.1157 0.1298 0.1466 -0.0140 0.0032  0.0307  124 ALA   A C   
2547 C  C   B ALA   A 124 ? 0.1406 0.1446 0.1095 -0.0137 0.0068  0.0274  124 ALA   A C   
2548 O  O   A ALA   A 124 ? 0.1132 0.1265 0.1702 -0.0220 0.0069  0.0217  124 ALA   A O   
2549 O  O   B ALA   A 124 ? 0.1459 0.1516 0.1072 -0.0127 0.0127  0.0278  124 ALA   A O   
2550 C  CB  A ALA   A 124 ? 0.1226 0.1254 0.1697 -0.0109 0.0076  0.0260  124 ALA   A CB  
2551 C  CB  B ALA   A 124 ? 0.1381 0.1400 0.1408 -0.0209 -0.0026 0.0154  124 ALA   A CB  
2562 N  N   A PRO   A 125 ? 0.1137 0.1355 0.1582 -0.0162 0.0005  0.0270  125 PRO   A N   
2563 N  N   B PRO   A 125 ? 0.1306 0.1367 0.1052 -0.0089 0.0014  0.0387  125 PRO   A N   
2564 C  CA  A PRO   A 125 ? 0.1183 0.1353 0.1636 -0.0100 0.0007  0.0221  125 PRO   A CA  
2565 C  CA  B PRO   A 125 ? 0.1334 0.1379 0.1230 -0.0062 0.0060  0.0285  125 PRO   A CA  
2566 C  C   A PRO   A 125 ? 0.1109 0.1325 0.1729 -0.0105 0.0040  0.0199  125 PRO   A C   
2567 C  C   B PRO   A 125 ? 0.1346 0.1421 0.1327 -0.0089 0.0109  0.0177  125 PRO   A C   
2568 O  O   A PRO   A 125 ? 0.1159 0.1353 0.1821 -0.0023 -0.0037 0.0192  125 PRO   A O   
2569 O  O   B PRO   A 125 ? 0.1398 0.1462 0.1404 -0.0081 0.0095  0.0234  125 PRO   A O   
2570 C  CB  A PRO   A 125 ? 0.1357 0.1359 0.1524 -0.0160 0.0038  0.0138  125 PRO   A CB  
2571 C  CB  B PRO   A 125 ? 0.1373 0.1343 0.1185 -0.0072 0.0067  0.0293  125 PRO   A CB  
2572 C  CG  A PRO   A 125 ? 0.1358 0.1319 0.1621 -0.0187 0.0034  0.0199  125 PRO   A CG  
2573 C  CG  B PRO   A 125 ? 0.1340 0.1273 0.1328 -0.0075 0.0086  0.0368  125 PRO   A CG  
2574 C  CD  A PRO   A 125 ? 0.1197 0.1377 0.1722 -0.0135 0.0132  0.0191  125 PRO   A CD  
2575 C  CD  B PRO   A 125 ? 0.1231 0.1224 0.1248 -0.0041 0.0109  0.0414  125 PRO   A CD  
2590 N  N   A LEU   A 126 ? 0.1088 0.1282 0.1777 -0.0041 0.0040  0.0184  126 LEU   A N   
2591 N  N   B LEU   A 126 ? 0.1403 0.1448 0.1449 -0.0121 0.0078  0.0054  126 LEU   A N   
2592 C  CA  A LEU   A 126 ? 0.1183 0.1260 0.1771 -0.0074 -0.0006 0.0202  126 LEU   A CA  
2593 C  CA  B LEU   A 126 ? 0.1333 0.1342 0.1507 -0.0038 0.0118  0.0023  126 LEU   A CA  
2594 C  C   A LEU   A 126 ? 0.1266 0.1226 0.1826 -0.0046 -0.0081 0.0152  126 LEU   A C   
2595 C  C   B LEU   A 126 ? 0.1338 0.1234 0.1542 0.0056  0.0223  0.0026  126 LEU   A C   
2596 O  O   A LEU   A 126 ? 0.1400 0.1226 0.2013 0.0062  0.0108  0.0211  126 LEU   A O   
2597 O  O   B LEU   A 126 ? 0.1538 0.1216 0.1657 0.0056  0.0366  0.0165  126 LEU   A O   
2598 C  CB  A LEU   A 126 ? 0.1283 0.1273 0.1715 -0.0023 0.0025  0.0184  126 LEU   A CB  
2599 C  CB  B LEU   A 126 ? 0.1365 0.1452 0.1746 -0.0099 0.0058  -0.0072 126 LEU   A CB  
2600 C  CG  A LEU   A 126 ? 0.1260 0.1402 0.1914 0.0028  0.0164  0.0239  126 LEU   A CG  
2601 C  CG  B LEU   A 126 ? 0.1316 0.1488 0.1884 -0.0045 0.0090  -0.0054 126 LEU   A CG  
2602 C  CD1 A LEU   A 126 ? 0.1304 0.1594 0.2297 0.0024  0.0089  0.0388  126 LEU   A CD1 
2603 C  CD1 B LEU   A 126 ? 0.1354 0.1420 0.2015 -0.0113 0.0003  -0.0094 126 LEU   A CD1 
2604 C  CD2 A LEU   A 126 ? 0.1368 0.1338 0.1828 -0.0022 0.0162  0.0258  126 LEU   A CD2 
2605 C  CD2 B LEU   A 126 ? 0.1255 0.1541 0.2053 0.0027  0.0051  0.0027  126 LEU   A CD2 
2628 N  N   A LEU   A 127 ? 0.1273 0.1308 0.1634 0.0004  -0.0020 0.0123  127 LEU   A N   
2629 N  N   B LEU   A 127 ? 0.1256 0.1270 0.1450 0.0074  0.0211  0.0070  127 LEU   A N   
2630 C  CA  A LEU   A 127 ? 0.1257 0.1317 0.1435 -0.0048 -0.0052 0.0066  127 LEU   A CA  
2631 C  CA  B LEU   A 127 ? 0.1216 0.1350 0.1382 0.0081  0.0096  0.0155  127 LEU   A CA  
2632 C  C   A LEU   A 127 ? 0.1259 0.1277 0.1455 -0.0034 -0.0016 0.0051  127 LEU   A C   
2633 C  C   B LEU   A 127 ? 0.1258 0.1361 0.1396 0.0035  0.0079  0.0036  127 LEU   A C   
2634 O  O   A LEU   A 127 ? 0.1336 0.1253 0.1470 -0.0106 -0.0058 0.0076  127 LEU   A O   
2635 O  O   B LEU   A 127 ? 0.1294 0.1429 0.1480 -0.0015 0.0194  0.0046  127 LEU   A O   
2636 C  CB  A LEU   A 127 ? 0.1338 0.1348 0.1553 0.0075  0.0051  0.0006  127 LEU   A CB  
2637 C  CB  B LEU   A 127 ? 0.1264 0.1483 0.1365 0.0050  0.0041  0.0107  127 LEU   A CB  
2638 C  CG  A LEU   A 127 ? 0.1412 0.1310 0.1628 0.0065  0.0007  0.0146  127 LEU   A CG  
2639 C  CG  B LEU   A 127 ? 0.1269 0.1572 0.1338 0.0086  -0.0063 0.0202  127 LEU   A CG  
2640 C  CD1 A LEU   A 127 ? 0.1431 0.1233 0.1834 0.0026  -0.0047 0.0066  127 LEU   A CD1 
2641 C  CD1 B LEU   A 127 ? 0.1300 0.1600 0.1431 0.0124  0.0120  0.0281  127 LEU   A CD1 
2642 C  CD2 A LEU   A 127 ? 0.1515 0.1324 0.1865 0.0114  -0.0098 0.0155  127 LEU   A CD2 
2643 C  CD2 B LEU   A 127 ? 0.1281 0.1658 0.1365 0.0069  -0.0253 0.0152  127 LEU   A CD2 
2666 N  N   A SER   A 128 ? 0.1326 0.1318 0.1475 -0.0093 -0.0055 0.0115  128 SER   A N   
2667 N  N   B SER   A 128 ? 0.1284 0.1374 0.1432 -0.0043 0.0010  0.0103  128 SER   A N   
2668 C  CA  A SER   A 128 ? 0.1447 0.1380 0.1414 -0.0060 -0.0018 0.0147  128 SER   A CA  
2669 C  CA  B SER   A 128 ? 0.1281 0.1321 0.1345 -0.0091 -0.0071 0.0123  128 SER   A CA  
2670 C  C   A SER   A 128 ? 0.1510 0.1432 0.1506 0.0014  0.0057  0.0233  128 SER   A C   
2671 C  C   B SER   A 128 ? 0.1271 0.1292 0.1325 -0.0091 -0.0167 0.0192  128 SER   A C   
2672 O  O   A SER   A 128 ? 0.1658 0.1545 0.1668 0.0046  0.0133  0.0145  128 SER   A O   
2673 O  O   B SER   A 128 ? 0.1254 0.1280 0.1331 -0.0079 -0.0204 0.0075  128 SER   A O   
2674 C  CB  A SER   A 128 ? 0.1448 0.1498 0.1415 -0.0078 0.0029  0.0116  128 SER   A CB  
2675 C  CB  B SER   A 128 ? 0.1283 0.1366 0.1330 -0.0112 -0.0068 0.0088  128 SER   A CB  
2676 O  OG  A SER   A 128 ? 0.1470 0.1642 0.1503 -0.0054 0.0112  0.0143  128 SER   A OG  
2677 O  OG  B SER   A 128 ? 0.1258 0.1481 0.1460 -0.0094 -0.0016 0.0087  128 SER   A OG  
2688 N  N   A ALA   A 129 ? 0.1453 0.1537 0.1693 0.0033  0.0031  0.0343  129 ALA   A N   
2689 N  N   B ALA   A 129 ? 0.1324 0.1387 0.1449 -0.0032 -0.0228 0.0253  129 ALA   A N   
2690 C  CA  A ALA   A 129 ? 0.1372 0.1579 0.1803 0.0063  0.0077  0.0377  129 ALA   A CA  
2691 C  CA  B ALA   A 129 ? 0.1352 0.1450 0.1562 0.0023  -0.0266 0.0294  129 ALA   A CA  
2692 C  C   A ALA   A 129 ? 0.1415 0.1568 0.1716 0.0030  0.0072  0.0180  129 ALA   A C   
2693 C  C   B ALA   A 129 ? 0.1402 0.1471 0.1451 0.0017  -0.0341 0.0101  129 ALA   A C   
2694 O  O   A ALA   A 129 ? 0.1470 0.1600 0.1735 0.0011  0.0086  0.0243  129 ALA   A O   
2695 O  O   B ALA   A 129 ? 0.1433 0.1479 0.1432 -0.0016 -0.0280 0.0069  129 ALA   A O   
2696 C  CB  A ALA   A 129 ? 0.1407 0.1763 0.2032 0.0156  0.0107  0.0574  129 ALA   A CB  
2697 C  CB  B ALA   A 129 ? 0.1391 0.1625 0.1720 0.0048  -0.0192 0.0384  129 ALA   A CB  
2708 N  N   A GLY   A 130 ? 0.1465 0.1493 0.1801 -0.0023 0.0115  0.0162  130 GLY   A N   
2709 N  N   B GLY   A 130 ? 0.1483 0.1542 0.1473 0.0031  -0.0305 0.0114  130 GLY   A N   
2710 C  CA  A GLY   A 130 ? 0.1613 0.1449 0.1796 0.0013  0.0217  0.0115  130 GLY   A CA  
2711 C  CA  B GLY   A 130 ? 0.1603 0.1551 0.1588 0.0034  -0.0267 0.0063  130 GLY   A CA  
2712 C  C   A GLY   A 130 ? 0.1614 0.1359 0.1651 0.0041  0.0190  0.0092  130 GLY   A C   
2713 C  C   B GLY   A 130 ? 0.1635 0.1525 0.1629 0.0064  -0.0338 0.0142  130 GLY   A C   
2714 O  O   A GLY   A 130 ? 0.1661 0.1368 0.1708 -0.0001 0.0114  0.0080  130 GLY   A O   
2715 O  O   B GLY   A 130 ? 0.1676 0.1570 0.1769 0.0104  -0.0328 0.0139  130 GLY   A O   
2722 N  N   A ILE   A 131 ? 0.1703 0.1350 0.1648 -0.0002 0.0067  0.0077  131 ILE   A N   
2723 N  N   B ILE   A 131 ? 0.1653 0.1480 0.1587 -0.0005 -0.0314 0.0232  131 ILE   A N   
2724 C  CA  A ILE   A 131 ? 0.1767 0.1365 0.1501 -0.0048 -0.0096 0.0025  131 ILE   A CA  
2725 C  CA  B ILE   A 131 ? 0.1702 0.1456 0.1582 -0.0034 -0.0353 0.0220  131 ILE   A CA  
2726 C  C   A ILE   A 131 ? 0.1724 0.1417 0.1493 -0.0057 -0.0022 0.0145  131 ILE   A C   
2727 C  C   B ILE   A 131 ? 0.1689 0.1460 0.1540 -0.0036 -0.0257 0.0236  131 ILE   A C   
2728 O  O   A ILE   A 131 ? 0.1827 0.1470 0.1641 -0.0021 -0.0091 0.0263  131 ILE   A O   
2729 O  O   B ILE   A 131 ? 0.1758 0.1488 0.1622 -0.0051 -0.0271 0.0302  131 ILE   A O   
2730 C  CB  A ILE   A 131 ? 0.1887 0.1493 0.1726 -0.0080 -0.0205 -0.0128 131 ILE   A CB  
2731 C  CB  B ILE   A 131 ? 0.1695 0.1535 0.1719 -0.0025 -0.0425 0.0109  131 ILE   A CB  
2732 C  CG1 A ILE   A 131 ? 0.1976 0.1789 0.1836 -0.0109 -0.0346 -0.0169 131 ILE   A CG1 
2733 C  CG1 B ILE   A 131 ? 0.1670 0.1715 0.1846 0.0020  -0.0498 0.0067  131 ILE   A CG1 
2734 C  CG2 A ILE   A 131 ? 0.1962 0.1404 0.1949 0.0004  -0.0161 -0.0287 131 ILE   A CG2 
2735 C  CG2 B ILE   A 131 ? 0.1735 0.1498 0.1848 -0.0079 -0.0314 0.0034  131 ILE   A CG2 
2736 C  CD1 A ILE   A 131 ? 0.2028 0.1868 0.2095 -0.0114 -0.0415 -0.0214 131 ILE   A CD1 
2737 C  CD1 B ILE   A 131 ? 0.1696 0.1788 0.1978 0.0064  -0.0556 -0.0007 131 ILE   A CD1 
2760 N  N   A PHE   A 132 ? 0.1613 0.1427 0.1484 -0.0075 0.0023  0.0167  132 PHE   A N   
2761 N  N   B PHE   A 132 ? 0.1597 0.1449 0.1611 0.0043  -0.0199 0.0192  132 PHE   A N   
2762 C  CA  A PHE   A 132 ? 0.1628 0.1509 0.1370 -0.0111 0.0037  0.0121  132 PHE   A CA  
2763 C  CA  B PHE   A 132 ? 0.1604 0.1467 0.1635 0.0038  -0.0104 0.0151  132 PHE   A CA  
2764 C  C   A PHE   A 132 ? 0.1584 0.1702 0.1226 -0.0099 0.0005  0.0082  132 PHE   A C   
2765 C  C   B PHE   A 132 ? 0.1652 0.1621 0.1797 0.0051  -0.0070 0.0159  132 PHE   A C   
2766 O  O   A PHE   A 132 ? 0.1603 0.1851 0.1294 -0.0138 -0.0020 0.0048  132 PHE   A O   
2767 O  O   B PHE   A 132 ? 0.1747 0.1759 0.1932 0.0027  0.0079  0.0189  132 PHE   A O   
2768 C  CB  A PHE   A 132 ? 0.1674 0.1408 0.1437 -0.0061 -0.0089 0.0181  132 PHE   A CB  
2769 C  CB  B PHE   A 132 ? 0.1520 0.1354 0.1425 -0.0001 -0.0083 0.0229  132 PHE   A CB  
2770 C  CG  A PHE   A 132 ? 0.1686 0.1414 0.1433 0.0002  -0.0073 0.0178  132 PHE   A CG  
2771 C  CG  B PHE   A 132 ? 0.1532 0.1335 0.1308 -0.0001 -0.0136 0.0094  132 PHE   A CG  
2772 C  CD1 A PHE   A 132 ? 0.1688 0.1556 0.1696 0.0055  -0.0114 0.0031  132 PHE   A CD1 
2773 C  CD1 B PHE   A 132 ? 0.1566 0.1443 0.1501 0.0044  -0.0099 -0.0045 132 PHE   A CD1 
2774 C  CD2 A PHE   A 132 ? 0.1648 0.1504 0.1577 -0.0045 0.0055  0.0121  132 PHE   A CD2 
2775 C  CD2 B PHE   A 132 ? 0.1511 0.1374 0.1304 0.0014  -0.0158 -0.0090 132 PHE   A CD2 
2776 C  CE1 A PHE   A 132 ? 0.1746 0.1625 0.1793 0.0029  -0.0198 0.0068  132 PHE   A CE1 
2777 C  CE1 B PHE   A 132 ? 0.1606 0.1489 0.1521 0.0038  -0.0133 -0.0098 132 PHE   A CE1 
2778 C  CE2 A PHE   A 132 ? 0.1623 0.1551 0.1694 -0.0073 -0.0059 0.0151  132 PHE   A CE2 
2779 C  CE2 B PHE   A 132 ? 0.1486 0.1431 0.1365 0.0048  -0.0187 -0.0137 132 PHE   A CE2 
2780 C  CZ  A PHE   A 132 ? 0.1677 0.1596 0.1772 -0.0072 -0.0191 0.0167  132 PHE   A CZ  
2781 C  CZ  B PHE   A 132 ? 0.1551 0.1466 0.1474 -0.0006 -0.0173 -0.0113 132 PHE   A CZ  
2800 N  N   A GLY   A 133 ? 0.1589 0.1719 0.1238 -0.0086 -0.0142 0.0159  133 GLY   A N   
2801 N  N   B GLY   A 133 ? 0.1629 0.1622 0.1737 0.0006  -0.0169 0.0159  133 GLY   A N   
2802 C  CA  A GLY   A 133 ? 0.1659 0.1834 0.1327 -0.0121 -0.0182 0.0072  133 GLY   A CA  
2803 C  CA  B GLY   A 133 ? 0.1684 0.1691 0.1695 -0.0049 -0.0170 0.0063  133 GLY   A CA  
2804 C  C   A GLY   A 133 ? 0.1832 0.1929 0.1362 -0.0189 -0.0308 -0.0014 133 GLY   A C   
2805 C  C   B GLY   A 133 ? 0.1688 0.1738 0.1673 0.0003  -0.0205 -0.0082 133 GLY   A C   
2806 O  O   A GLY   A 133 ? 0.1960 0.2074 0.1474 -0.0159 -0.0248 -0.0130 133 GLY   A O   
2807 O  O   B GLY   A 133 ? 0.1622 0.1831 0.1710 0.0086  -0.0142 -0.0301 133 GLY   A O   
2814 N  N   A ALA   A 134 ? 0.1864 0.1768 0.1414 -0.0230 -0.0251 -0.0061 134 ALA   A N   
2815 N  N   B ALA   A 134 ? 0.1719 0.1621 0.1695 0.0015  -0.0168 -0.0044 134 ALA   A N   
2816 C  CA  A ALA   A 134 ? 0.1873 0.1765 0.1799 -0.0186 -0.0262 -0.0049 134 ALA   A CA  
2817 C  CA  B ALA   A 134 ? 0.1728 0.1579 0.1817 -0.0001 -0.0195 -0.0026 134 ALA   A CA  
2818 C  C   A ALA   A 134 ? 0.1849 0.1801 0.1898 -0.0178 -0.0212 0.0068  134 ALA   A C   
2819 C  C   B ALA   A 134 ? 0.1733 0.1577 0.1855 -0.0033 -0.0173 0.0024  134 ALA   A C   
2820 O  O   A ALA   A 134 ? 0.1945 0.1882 0.2064 -0.0233 -0.0156 0.0055  134 ALA   A O   
2821 O  O   B ALA   A 134 ? 0.1717 0.1603 0.1967 -0.0071 -0.0101 0.0074  134 ALA   A O   
2822 C  CB  A ALA   A 134 ? 0.1953 0.1725 0.2062 -0.0131 -0.0230 -0.0174 134 ALA   A CB  
2823 C  CB  B ALA   A 134 ? 0.1774 0.1533 0.1926 0.0018  -0.0167 -0.0111 134 ALA   A CB  
2834 N  N   A ASP   A 135 ? 0.1884 0.1749 0.1938 -0.0142 -0.0172 0.0186  135 ASP   A N   
2835 N  N   B ASP   A 135 ? 0.1866 0.1600 0.1909 -0.0073 -0.0197 0.0068  135 ASP   A N   
2836 C  CA  A ASP   A 135 ? 0.1820 0.1771 0.2095 -0.0166 -0.0252 0.0276  135 ASP   A CA  
2837 C  CA  B ASP   A 135 ? 0.1864 0.1621 0.2058 -0.0082 -0.0255 0.0035  135 ASP   A CA  
2838 C  C   A ASP   A 135 ? 0.1676 0.1659 0.2133 -0.0115 -0.0191 0.0385  135 ASP   A C   
2839 C  C   B ASP   A 135 ? 0.1685 0.1518 0.2035 -0.0014 -0.0188 -0.0005 135 ASP   A C   
2840 O  O   A ASP   A 135 ? 0.1580 0.1611 0.2211 -0.0091 -0.0212 0.0419  135 ASP   A O   
2841 O  O   B ASP   A 135 ? 0.1591 0.1439 0.2040 -0.0005 -0.0203 0.0033  135 ASP   A O   
2842 C  CB  A ASP   A 135 ? 0.2008 0.2029 0.2464 -0.0307 -0.0410 0.0117  135 ASP   A CB  
2843 C  CB  B ASP   A 135 ? 0.1994 0.1778 0.2221 -0.0141 -0.0388 0.0046  135 ASP   A CB  
2844 C  CG  A ASP   A 135 ? 0.2130 0.2261 0.2773 -0.0508 -0.0519 0.0073  135 ASP   A CG  
2845 C  CG  B ASP   A 135 ? 0.2068 0.1951 0.2421 -0.0155 -0.0426 0.0059  135 ASP   A CG  
2846 O  OD1 A ASP   A 135 ? 0.2039 0.2338 0.2721 -0.0649 -0.0669 0.0226  135 ASP   A OD1 
2847 O  OD1 B ASP   A 135 ? 0.2075 0.1924 0.2489 -0.0090 -0.0480 0.0075  135 ASP   A OD1 
2848 O  OD2 A ASP   A 135 ? 0.2367 0.2471 0.3177 -0.0483 -0.0393 -0.0006 135 ASP   A OD2 
2849 O  OD2 B ASP   A 135 ? 0.2121 0.2087 0.2607 -0.0212 -0.0393 0.0049  135 ASP   A OD2 
2858 N  N   A PRO   A 136 ? 0.1552 0.1585 0.2278 -0.0035 -0.0104 0.0459  136 PRO   A N   
2859 N  N   B PRO   A 136 ? 0.1598 0.1494 0.2090 0.0043  -0.0074 -0.0042 136 PRO   A N   
2860 C  CA  A PRO   A 136 ? 0.1492 0.1593 0.2396 -0.0091 -0.0020 0.0295  136 PRO   A CA  
2861 C  CA  B PRO   A 136 ? 0.1531 0.1588 0.2063 0.0019  0.0020  -0.0134 136 PRO   A CA  
2862 C  C   A PRO   A 136 ? 0.1269 0.1569 0.2355 -0.0029 -0.0035 0.0285  136 PRO   A C   
2863 C  C   B PRO   A 136 ? 0.1415 0.1644 0.1923 0.0099  0.0059  -0.0054 136 PRO   A C   
2864 O  O   A PRO   A 136 ? 0.1231 0.1596 0.2346 -0.0117 -0.0021 0.0257  136 PRO   A O   
2865 O  O   B PRO   A 136 ? 0.1368 0.1572 0.1785 0.0244  0.0207  -0.0129 136 PRO   A O   
2866 C  CB  A PRO   A 136 ? 0.1697 0.1585 0.2559 -0.0067 0.0030  0.0252  136 PRO   A CB  
2867 C  CB  B PRO   A 136 ? 0.1669 0.1563 0.2212 0.0035  0.0059  -0.0187 136 PRO   A CB  
2868 C  CG  A PRO   A 136 ? 0.1789 0.1606 0.2669 0.0010  -0.0036 0.0274  136 PRO   A CG  
2869 C  CG  B PRO   A 136 ? 0.1770 0.1510 0.2365 0.0093  0.0012  -0.0140 136 PRO   A CG  
2870 C  CD  A PRO   A 136 ? 0.1701 0.1591 0.2430 0.0030  -0.0086 0.0395  136 PRO   A CD  
2871 C  CD  B PRO   A 136 ? 0.1669 0.1441 0.2243 0.0094  -0.0001 -0.0041 136 PRO   A CD  
2886 N  N   A ILE   A 137 ? 0.1242 0.1561 0.2450 -0.0059 -0.0128 0.0327  137 ILE   A N   
2887 N  N   B ILE   A 137 ? 0.1413 0.1696 0.2026 0.0024  -0.0007 0.0035  137 ILE   A N   
2888 C  CA  A ILE   A 137 ? 0.1305 0.1645 0.2390 -0.0143 -0.0201 0.0380  137 ILE   A CA  
2889 C  CA  B ILE   A 137 ? 0.1463 0.1792 0.2016 -0.0012 -0.0021 0.0120  137 ILE   A CA  
2890 C  C   A ILE   A 137 ? 0.1339 0.1609 0.2138 -0.0155 -0.0224 0.0313  137 ILE   A C   
2891 C  C   B ILE   A 137 ? 0.1429 0.1771 0.1958 -0.0084 0.0025  0.0035  137 ILE   A C   
2892 O  O   A ILE   A 137 ? 0.1445 0.1504 0.2251 -0.0147 -0.0160 0.0276  137 ILE   A O   
2893 O  O   B ILE   A 137 ? 0.1406 0.1743 0.2021 -0.0137 0.0086  -0.0003 137 ILE   A O   
2894 C  CB  A ILE   A 137 ? 0.1392 0.1853 0.2681 -0.0141 -0.0383 0.0405  137 ILE   A CB  
2895 C  CB  B ILE   A 137 ? 0.1567 0.1895 0.2210 -0.0008 -0.0144 0.0226  137 ILE   A CB  
2896 C  CG1 A ILE   A 137 ? 0.1465 0.2166 0.2959 -0.0083 -0.0329 0.0472  137 ILE   A CG1 
2897 C  CG1 B ILE   A 137 ? 0.1646 0.2093 0.2438 0.0105  -0.0255 0.0284  137 ILE   A CG1 
2898 C  CG2 A ILE   A 137 ? 0.1509 0.1845 0.2747 -0.0190 -0.0490 0.0294  137 ILE   A CG2 
2899 C  CG2 B ILE   A 137 ? 0.1652 0.1864 0.2226 -0.0016 -0.0138 0.0215  137 ILE   A CG2 
2900 C  CD1 A ILE   A 137 ? 0.1622 0.2408 0.3216 -0.0033 -0.0268 0.0401  137 ILE   A CD1 
2901 C  CD1 B ILE   A 137 ? 0.1745 0.2245 0.2648 0.0110  -0.0247 0.0296  137 ILE   A CD1 
2924 N  N   A HIS   A 138 ? 0.1383 0.1773 0.2123 -0.0125 -0.0106 0.0270  138 HIS   A N   
2925 N  N   B HIS   A 138 ? 0.1444 0.1844 0.2026 -0.0071 0.0097  -0.0030 138 HIS   A N   
2926 C  CA  A HIS   A 138 ? 0.1452 0.1849 0.2021 -0.0117 -0.0056 0.0230  138 HIS   A CA  
2927 C  CA  B HIS   A 138 ? 0.1467 0.1810 0.1943 -0.0091 0.0112  -0.0008 138 HIS   A CA  
2928 C  C   A HIS   A 138 ? 0.1384 0.1761 0.1995 -0.0041 -0.0016 0.0299  138 HIS   A C   
2929 C  C   B HIS   A 138 ? 0.1412 0.1741 0.1955 -0.0040 0.0078  0.0159  138 HIS   A C   
2930 O  O   A HIS   A 138 ? 0.1495 0.1783 0.2007 -0.0105 0.0001  0.0279  138 HIS   A O   
2931 O  O   B HIS   A 138 ? 0.1492 0.1769 0.1955 -0.0074 0.0066  0.0143  138 HIS   A O   
2932 C  CB  A HIS   A 138 ? 0.1641 0.2065 0.2031 -0.0093 -0.0174 0.0189  138 HIS   A CB  
2933 C  CB  B HIS   A 138 ? 0.1515 0.1897 0.1912 -0.0075 0.0098  -0.0180 138 HIS   A CB  
2934 C  CG  A HIS   A 138 ? 0.1849 0.2188 0.2167 -0.0204 -0.0147 0.0143  138 HIS   A CG  
2935 C  CG  B HIS   A 138 ? 0.1595 0.1948 0.1970 -0.0118 0.0059  -0.0307 138 HIS   A CG  
2936 N  ND1 A HIS   A 138 ? 0.1980 0.2296 0.2453 -0.0260 -0.0123 0.0047  138 HIS   A ND1 
2937 N  ND1 B HIS   A 138 ? 0.1688 0.2004 0.2132 -0.0126 0.0023  -0.0369 138 HIS   A ND1 
2938 C  CD2 A HIS   A 138 ? 0.1887 0.2256 0.2210 -0.0181 -0.0139 0.0175  138 HIS   A CD2 
2939 C  CD2 B HIS   A 138 ? 0.1594 0.1968 0.1988 -0.0083 0.0076  -0.0333 138 HIS   A CD2 
2940 C  CE1 A HIS   A 138 ? 0.2029 0.2388 0.2493 -0.0152 -0.0146 0.0087  138 HIS   A CE1 
2941 C  CE1 B HIS   A 138 ? 0.1693 0.2030 0.2139 -0.0077 0.0012  -0.0351 138 HIS   A CE1 
2942 N  NE2 A HIS   A 138 ? 0.1948 0.2382 0.2298 -0.0150 -0.0049 0.0121  138 HIS   A NE2 
2943 N  NE2 B HIS   A 138 ? 0.1626 0.2027 0.2003 -0.0051 0.0082  -0.0384 138 HIS   A NE2 
2958 N  N   . SER   A 139 ? 0.1278 0.1636 0.2002 -0.0024 0.0018  0.0289  139 SER   A N   
2959 C  CA  . SER   A 139 ? 0.1264 0.1572 0.1986 -0.0073 0.0035  0.0316  139 SER   A CA  
2960 C  C   . SER   A 139 ? 0.1260 0.1540 0.1985 -0.0092 0.0064  0.0244  139 SER   A C   
2961 O  O   . SER   A 139 ? 0.1202 0.1457 0.2140 -0.0126 0.0020  0.0265  139 SER   A O   
2962 C  CB  . SER   A 139 ? 0.1295 0.1614 0.2000 -0.0141 -0.0064 0.0321  139 SER   A CB  
2963 O  OG  . SER   A 139 ? 0.1372 0.1634 0.1986 -0.0201 -0.0085 0.0465  139 SER   A OG  
2970 N  N   . LEU   A 140 ? 0.1225 0.1582 0.1870 -0.0063 0.0044  0.0374  140 LEU   A N   
2971 C  CA  . LEU   A 140 ? 0.1222 0.1571 0.1957 -0.0074 0.0011  0.0266  140 LEU   A CA  
2972 C  C   . LEU   A 140 ? 0.1142 0.1624 0.1944 -0.0123 0.0010  0.0312  140 LEU   A C   
2973 O  O   . LEU   A 140 ? 0.1244 0.1613 0.2197 -0.0069 0.0003  0.0341  140 LEU   A O   
2974 C  CB  . LEU   A 140 ? 0.1281 0.1617 0.1956 -0.0103 0.0066  0.0317  140 LEU   A CB  
2975 C  CG  . LEU   A 140 ? 0.1290 0.1785 0.2036 -0.0151 0.0030  0.0451  140 LEU   A CG  
2976 C  CD1 . LEU   A 140 ? 0.1369 0.1765 0.2169 -0.0101 -0.0044 0.0405  140 LEU   A CD1 
2977 C  CD2 . LEU   A 140 ? 0.1256 0.1993 0.2096 -0.0133 0.0112  0.0466  140 LEU   A CD2 
2989 N  N   . ARG   A 141 ? 0.1247 0.1663 0.1998 -0.0112 -0.0022 0.0236  141 ARG   A N   
2990 C  CA  . ARG   A 141 ? 0.1374 0.1764 0.2260 -0.0184 -0.0020 0.0019  141 ARG   A CA  
2991 C  C   . ARG   A 141 ? 0.1396 0.1524 0.2221 -0.0196 -0.0017 0.0042  141 ARG   A C   
2992 O  O   . ARG   A 141 ? 0.1379 0.1530 0.2408 -0.0176 0.0053  0.0123  141 ARG   A O   
2993 C  CB  . ARG   A 141 ? 0.1468 0.1981 0.2458 -0.0215 -0.0082 -0.0217 141 ARG   A CB  
2994 C  CG  . ARG   A 141 ? 0.1815 0.2308 0.2813 -0.0216 0.0069  -0.0152 141 ARG   A CG  
2995 C  CD  . ARG   A 141 ? 0.2137 0.2529 0.3057 -0.0246 0.0057  -0.0221 141 ARG   A CD  
2996 N  NE  . ARG   A 141 ? 0.2044 0.2697 0.3229 -0.0215 0.0000  -0.0217 141 ARG   A NE  
2997 C  CZ  . ARG   A 141 ? 0.2133 0.2918 0.3245 -0.0398 0.0068  -0.0159 141 ARG   A CZ  
2998 N  NH1 . ARG   A 141 ? 0.1976 0.2952 0.3081 -0.0567 0.0308  -0.0248 141 ARG   A NH1 
2999 N  NH2 . ARG   A 141 ? 0.2265 0.3072 0.3526 -0.0363 -0.0120 -0.0055 141 ARG   A NH2 
3013 N  N   . VAL   A 142 ? 0.1306 0.1555 0.2103 -0.0143 -0.0019 0.0066  142 VAL   A N   
3014 C  CA  . VAL   A 142 ? 0.1340 0.1481 0.2115 -0.0103 0.0138  0.0083  142 VAL   A CA  
3015 C  C   . VAL   A 142 ? 0.1159 0.1419 0.2189 -0.0128 0.0084  0.0116  142 VAL   A C   
3016 O  O   . VAL   A 142 ? 0.1243 0.1463 0.2311 -0.0015 0.0120  0.0147  142 VAL   A O   
3017 C  CB  . VAL   A 142 ? 0.1403 0.1594 0.2085 -0.0079 0.0110  0.0168  142 VAL   A CB  
3018 C  CG1 . VAL   A 142 ? 0.1496 0.1566 0.2068 -0.0092 0.0223  0.0049  142 VAL   A CG1 
3019 C  CG2 . VAL   A 142 ? 0.1499 0.1797 0.2211 -0.0036 0.0108  0.0181  142 VAL   A CG2 
3029 N  N   . CYS   A 143 ? 0.1241 0.1405 0.2037 -0.0138 -0.0013 0.0197  143 CYS   A N   
3030 C  CA  . CYS   A 143 ? 0.1216 0.1391 0.2145 -0.0102 0.0050  0.0250  143 CYS   A CA  
3031 C  C   . CYS   A 143 ? 0.1253 0.1441 0.2198 -0.0102 0.0021  0.0365  143 CYS   A C   
3032 O  O   . CYS   A 143 ? 0.1227 0.1432 0.2152 -0.0095 0.0009  0.0372  143 CYS   A O   
3033 C  CB  . CYS   A 143 ? 0.1305 0.1445 0.2067 -0.0092 0.0155  0.0376  143 CYS   A CB  
3034 S  SG  . CYS   A 143 ? 0.1494 0.1578 0.1910 0.0007  0.0106  0.0245  143 CYS   A SG  
3040 N  N   . VAL   A 144 ? 0.1231 0.1486 0.2428 -0.0088 0.0053  0.0470  144 VAL   A N   
3041 C  CA  . VAL   A 144 ? 0.1309 0.1555 0.2682 -0.0082 0.0170  0.0444  144 VAL   A CA  
3042 C  C   . VAL   A 144 ? 0.1312 0.1445 0.2688 -0.0235 -0.0092 0.0383  144 VAL   A C   
3043 O  O   . VAL   A 144 ? 0.1473 0.1508 0.2710 -0.0096 -0.0089 0.0410  144 VAL   A O   
3044 C  CB  . VAL   A 144 ? 0.1575 0.1825 0.3162 -0.0055 0.0339  0.0500  144 VAL   A CB  
3045 C  CG1 . VAL   A 144 ? 0.1743 0.2013 0.3562 -0.0171 0.0144  0.0451  144 VAL   A CG1 
3046 C  CG2 . VAL   A 144 ? 0.1404 0.1943 0.3184 -0.0054 0.0429  0.0635  144 VAL   A CG2 
3056 N  N   . ASP   A 145 ? 0.1382 0.1408 0.2820 -0.0147 -0.0008 0.0358  145 ASP   A N   
3057 C  CA  . ASP   A 145 ? 0.1488 0.1469 0.2813 -0.0205 0.0039  0.0186  145 ASP   A CA  
3058 C  C   . ASP   A 145 ? 0.1512 0.1404 0.2793 -0.0101 -0.0007 0.0071  145 ASP   A C   
3059 O  O   . ASP   A 145 ? 0.1654 0.1470 0.3197 -0.0128 -0.0060 -0.0232 145 ASP   A O   
3060 C  CB  . ASP   A 145 ? 0.1627 0.1729 0.3003 -0.0255 -0.0146 0.0160  145 ASP   A CB  
3061 C  CG  . ASP   A 145 ? 0.1799 0.2109 0.3211 -0.0460 -0.0291 0.0189  145 ASP   A CG  
3062 O  OD1 . ASP   A 145 ? 0.1709 0.2314 0.3281 -0.0578 -0.0187 0.0254  145 ASP   A OD1 
3063 O  OD2 . ASP   A 145 ? 0.1968 0.2361 0.3289 -0.0545 -0.0414 0.0117  145 ASP   A OD2 
3068 N  N   . THR   A 146 ? 0.1375 0.1320 0.2455 -0.0129 0.0018  0.0117  146 THR   A N   
3069 C  CA  . THR   A 146 ? 0.1320 0.1297 0.2237 -0.0105 0.0053  0.0071  146 THR   A CA  
3070 C  C   . THR   A 146 ? 0.1248 0.1289 0.2294 -0.0051 0.0137  0.0174  146 THR   A C   
3071 O  O   . THR   A 146 ? 0.1407 0.1444 0.2475 0.0026  -0.0000 0.0187  146 THR   A O   
3072 C  CB  . THR   A 146 ? 0.1300 0.1333 0.2271 -0.0027 0.0040  0.0125  146 THR   A CB  
3073 O  OG1 . THR   A 146 ? 0.1281 0.1493 0.2336 -0.0006 0.0009  0.0048  146 THR   A OG1 
3074 C  CG2 . THR   A 146 ? 0.1266 0.1366 0.2481 -0.0108 0.0045  0.0179  146 THR   A CG2 
3082 N  N   . VAL   A 147 ? 0.1242 0.1362 0.2206 -0.0024 0.0108  0.0175  147 VAL   A N   
3083 C  CA  . VAL   A 147 ? 0.1267 0.1384 0.2238 -0.0079 0.0267  0.0309  147 VAL   A CA  
3084 C  C   . VAL   A 147 ? 0.1269 0.1398 0.2379 -0.0101 0.0208  0.0393  147 VAL   A C   
3085 O  O   . VAL   A 147 ? 0.1284 0.1442 0.2511 -0.0146 0.0148  0.0415  147 VAL   A O   
3086 C  CB  . VAL   A 147 ? 0.1408 0.1387 0.2162 -0.0121 0.0231  0.0288  147 VAL   A CB  
3087 C  CG1 . VAL   A 147 ? 0.1675 0.1441 0.2122 -0.0096 0.0183  0.0347  147 VAL   A CG1 
3088 C  CG2 . VAL   A 147 ? 0.1464 0.1366 0.2157 -0.0087 0.0111  0.0246  147 VAL   A CG2 
3098 N  N   . ARG   A 148 ? 0.1264 0.1385 0.2520 -0.0133 0.0182  0.0519  148 ARG   A N   
3099 C  CA  . ARG   A 148 ? 0.1375 0.1420 0.2425 -0.0184 0.0048  0.0600  148 ARG   A CA  
3100 C  C   . ARG   A 148 ? 0.1496 0.1444 0.2344 -0.0200 0.0029  0.0751  148 ARG   A C   
3101 O  O   . ARG   A 148 ? 0.1783 0.1616 0.2578 -0.0252 0.0149  0.0702  148 ARG   A O   
3102 C  CB  . ARG   A 148 ? 0.1464 0.1473 0.2579 -0.0061 0.0212  0.0601  148 ARG   A CB  
3103 C  CG  . ARG   A 148 ? 0.1576 0.1505 0.2922 -0.0099 0.0364  0.0482  148 ARG   A CG  
3104 C  CD  . ARG   A 148 ? 0.1732 0.1486 0.3046 -0.0018 0.0446  0.0662  148 ARG   A CD  
3105 N  NE  . ARG   A 148 ? 0.1669 0.1524 0.3063 0.0092  0.0520  0.0606  148 ARG   A NE  
3106 C  CZ  . ARG   A 148 ? 0.1615 0.1362 0.2872 0.0057  0.0457  0.0568  148 ARG   A CZ  
3107 N  NH1 . ARG   A 148 ? 0.1712 0.1379 0.3035 -0.0108 0.0415  0.0309  148 ARG   A NH1 
3108 N  NH2 . ARG   A 148 ? 0.1551 0.1570 0.2933 0.0149  0.0519  0.0616  148 ARG   A NH2 
3122 N  N   . THR   A 149 ? 0.1514 0.1601 0.2245 -0.0188 -0.0036 0.0619  149 THR   A N   
3123 C  CA  . THR   A 149 ? 0.1530 0.1650 0.2267 -0.0181 -0.0008 0.0600  149 THR   A CA  
3124 C  C   . THR   A 149 ? 0.1445 0.1631 0.2100 -0.0219 0.0063  0.0715  149 THR   A C   
3125 O  O   . THR   A 149 ? 0.1441 0.1723 0.2223 -0.0237 0.0024  0.0634  149 THR   A O   
3126 C  CB  . THR   A 149 ? 0.1485 0.1731 0.2397 -0.0214 0.0025  0.0562  149 THR   A CB  
3127 O  OG1 . THR   A 149 ? 0.1482 0.1597 0.2430 -0.0282 0.0031  0.0483  149 THR   A OG1 
3128 C  CG2 . THR   A 149 ? 0.1468 0.1873 0.2503 -0.0109 -0.0109 0.0420  149 THR   A CG2 
3136 N  N   . ASN   A 150 ? 0.1478 0.1725 0.2107 -0.0095 0.0025  0.0757  150 ASN   A N   
3137 C  CA  . ASN   A 150 ? 0.1626 0.1761 0.2099 -0.0140 0.0080  0.0638  150 ASN   A CA  
3138 C  C   . ASN   A 150 ? 0.1421 0.1677 0.2069 -0.0209 0.0043  0.0546  150 ASN   A C   
3139 O  O   . ASN   A 150 ? 0.1520 0.1809 0.2366 -0.0221 -0.0146 0.0505  150 ASN   A O   
3140 C  CB  . ASN   A 150 ? 0.2067 0.2038 0.2380 -0.0219 0.0231  0.0784  150 ASN   A CB  
3141 C  CG  . ASN   A 150 ? 0.2608 0.2357 0.3118 -0.0216 0.0070  0.0756  150 ASN   A CG  
3142 O  OD1 . ASN   A 150 ? 0.2865 0.2437 0.3254 -0.0303 0.0050  0.0840  150 ASN   A OD1 
3143 N  ND2 . ASN   A 150 ? 0.2950 0.2642 0.3483 -0.0169 -0.0005 0.0649  150 ASN   A ND2 
3150 N  N   . VAL   A 151 ? 0.1359 0.1543 0.2089 -0.0210 0.0049  0.0531  151 VAL   A N   
3151 C  CA  . VAL   A 151 ? 0.1460 0.1576 0.1895 -0.0212 0.0052  0.0487  151 VAL   A CA  
3152 C  C   . VAL   A 151 ? 0.1367 0.1527 0.1996 -0.0227 0.0045  0.0561  151 VAL   A C   
3153 O  O   . VAL   A 151 ? 0.1455 0.1607 0.2377 -0.0197 0.0086  0.0486  151 VAL   A O   
3154 C  CB  . VAL   A 151 ? 0.1773 0.1740 0.2020 -0.0117 0.0030  0.0451  151 VAL   A CB  
3155 C  CG1 . VAL   A 151 ? 0.1708 0.1999 0.2234 -0.0149 -0.0030 0.0342  151 VAL   A CG1 
3156 C  CG2 . VAL   A 151 ? 0.1910 0.1673 0.1986 -0.0070 0.0182  0.0343  151 VAL   A CG2 
3166 N  N   A TYR   A 152 ? 0.1386 0.1526 0.2116 -0.0241 0.0108  0.0605  152 TYR   A N   
3167 N  N   B TYR   A 152 ? 0.1393 0.1561 0.1866 -0.0218 0.0017  0.0535  152 TYR   A N   
3168 C  CA  A TYR   A 152 ? 0.1418 0.1617 0.1923 -0.0245 0.0095  0.0566  152 TYR   A CA  
3169 C  CA  B TYR   A 152 ? 0.1419 0.1636 0.1539 -0.0210 -0.0067 0.0451  152 TYR   A CA  
3170 C  C   A TYR   A 152 ? 0.1370 0.1468 0.1799 -0.0251 0.0201  0.0425  152 TYR   A C   
3171 C  C   B TYR   A 152 ? 0.1342 0.1546 0.1335 -0.0242 -0.0070 0.0367  152 TYR   A C   
3172 O  O   A TYR   A 152 ? 0.1453 0.1514 0.1855 -0.0293 0.0215  0.0438  152 TYR   A O   
3173 O  O   B TYR   A 152 ? 0.1374 0.1598 0.1369 -0.0265 -0.0048 0.0327  152 TYR   A O   
3174 C  CB  A TYR   A 152 ? 0.1569 0.1789 0.1959 -0.0261 0.0205  0.0685  152 TYR   A CB  
3175 C  CB  B TYR   A 152 ? 0.1551 0.1766 0.1601 -0.0164 -0.0005 0.0409  152 TYR   A CB  
3176 C  CG  A TYR   A 152 ? 0.1660 0.2003 0.1858 -0.0342 0.0248  0.0749  152 TYR   A CG  
3177 C  CG  B TYR   A 152 ? 0.1656 0.1929 0.1626 -0.0201 0.0114  0.0417  152 TYR   A CG  
3178 C  CD1 A TYR   A 152 ? 0.1803 0.2220 0.2051 -0.0267 0.0147  0.0765  152 TYR   A CD1 
3179 C  CD1 B TYR   A 152 ? 0.1759 0.2042 0.1772 -0.0169 0.0182  0.0516  152 TYR   A CD1 
3180 C  CD2 A TYR   A 152 ? 0.1725 0.2083 0.1950 -0.0456 0.0231  0.0625  152 TYR   A CD2 
3181 C  CD2 B TYR   A 152 ? 0.1696 0.1998 0.1606 -0.0289 0.0095  0.0326  152 TYR   A CD2 
3182 C  CE1 A TYR   A 152 ? 0.2036 0.2359 0.2062 -0.0231 0.0063  0.0895  152 TYR   A CE1 
3183 C  CE1 B TYR   A 152 ? 0.1950 0.2163 0.1918 -0.0149 0.0080  0.0526  152 TYR   A CE1 
3184 C  CE2 A TYR   A 152 ? 0.1906 0.2203 0.2028 -0.0476 0.0252  0.0675  152 TYR   A CE2 
3185 C  CE2 B TYR   A 152 ? 0.1870 0.2121 0.1743 -0.0270 0.0111  0.0370  152 TYR   A CE2 
3186 C  CZ  A TYR   A 152 ? 0.2144 0.2338 0.2010 -0.0324 0.0119  0.0893  152 TYR   A CZ  
3187 C  CZ  B TYR   A 152 ? 0.2030 0.2214 0.1933 -0.0218 0.0085  0.0526  152 TYR   A CZ  
3188 O  OH  A TYR   A 152 ? 0.2423 0.2475 0.2198 -0.0198 0.0183  0.1040  152 TYR   A OH  
3189 O  OH  B TYR   A 152 ? 0.2226 0.2384 0.2249 -0.0217 0.0138  0.0646  152 TYR   A OH  
3208 N  N   A LEU   A 153 ? 0.1355 0.1390 0.1699 -0.0229 0.0255  0.0322  153 LEU   A N   
3209 N  N   B LEU   A 153 ? 0.1330 0.1432 0.1365 -0.0262 -0.0026 0.0316  153 LEU   A N   
3210 C  CA  A LEU   A 153 ? 0.1323 0.1306 0.1718 -0.0119 0.0220  0.0292  153 LEU   A CA  
3211 C  CA  B LEU   A 153 ? 0.1329 0.1325 0.1280 -0.0170 0.0053  0.0140  153 LEU   A CA  
3212 C  C   A LEU   A 153 ? 0.1343 0.1318 0.1604 -0.0074 0.0255  0.0161  153 LEU   A C   
3213 C  C   B LEU   A 153 ? 0.1367 0.1396 0.1328 -0.0076 0.0170  0.0114  153 LEU   A C   
3214 O  O   A LEU   A 153 ? 0.1394 0.1418 0.1777 -0.0153 0.0338  0.0108  153 LEU   A O   
3215 O  O   B LEU   A 153 ? 0.1385 0.1500 0.1276 -0.0138 0.0309  0.0087  153 LEU   A O   
3216 C  CB  A LEU   A 153 ? 0.1251 0.1190 0.1820 -0.0124 0.0217  0.0188  153 LEU   A CB  
3217 C  CB  B LEU   A 153 ? 0.1265 0.1258 0.1320 -0.0099 0.0014  0.0094  153 LEU   A CB  
3218 C  CG  A LEU   A 153 ? 0.1281 0.1292 0.1883 -0.0138 0.0292  0.0133  153 LEU   A CG  
3219 C  CG  B LEU   A 153 ? 0.1312 0.1285 0.1364 0.0018  0.0039  0.0042  153 LEU   A CG  
3220 C  CD1 A LEU   A 153 ? 0.1357 0.1218 0.1921 -0.0031 0.0204  0.0099  153 LEU   A CD1 
3221 C  CD1 B LEU   A 153 ? 0.1347 0.1299 0.1362 0.0075  0.0063  0.0052  153 LEU   A CD1 
3222 C  CD2 A LEU   A 153 ? 0.1390 0.1452 0.1778 -0.0241 0.0329  -0.0093 153 LEU   A CD2 
3223 C  CD2 B LEU   A 153 ? 0.1386 0.1322 0.1497 -0.0020 -0.0007 -0.0028 153 LEU   A CD2 
3246 N  N   A ALA   A 154 ? 0.1379 0.1274 0.1704 -0.0049 0.0255  0.0265  154 ALA   A N   
3247 N  N   B ALA   A 154 ? 0.1384 0.1408 0.1288 -0.0049 0.0262  0.0067  154 ALA   A N   
3248 C  CA  A ALA   A 154 ? 0.1456 0.1278 0.1769 -0.0059 0.0313  0.0225  154 ALA   A CA  
3249 C  CA  B ALA   A 154 ? 0.1422 0.1432 0.1459 -0.0039 0.0287  0.0050  154 ALA   A CA  
3250 C  C   A ALA   A 154 ? 0.1353 0.1254 0.1752 -0.0023 0.0272  0.0260  154 ALA   A C   
3251 C  C   B ALA   A 154 ? 0.1415 0.1489 0.1452 -0.0055 0.0177  0.0197  154 ALA   A C   
3252 O  O   A ALA   A 154 ? 0.1487 0.1380 0.1761 -0.0133 0.0196  0.0207  154 ALA   A O   
3253 O  O   B ALA   A 154 ? 0.1528 0.1558 0.1375 -0.0085 0.0151  0.0137  154 ALA   A O   
3254 C  CB  A ALA   A 154 ? 0.1575 0.1334 0.1774 0.0078  0.0349  0.0071  154 ALA   A CB  
3255 C  CB  B ALA   A 154 ? 0.1418 0.1445 0.1563 0.0016  0.0256  -0.0124 154 ALA   A CB  
3266 N  N   A VAL   A 155 ? 0.1205 0.1075 0.1552 0.0083  0.0321  0.0437  155 VAL   A N   
3267 N  N   B VAL   A 155 ? 0.1412 0.1521 0.1569 -0.0027 0.0193  0.0438  155 VAL   A N   
3268 C  CA  A VAL   A 155 ? 0.1384 0.1308 0.1879 0.0069  0.0198  0.0484  155 VAL   A CA  
3269 C  CA  B VAL   A 155 ? 0.1697 0.1789 0.2003 0.0046  0.0039  0.0411  155 VAL   A CA  
3270 C  CA  T VAL   A 155 ? 0.1570 0.1633 0.1879 -0.0216 0.0396  0.0556  155 VAL   A CA  
3271 C  C   A VAL   A 155 ? 0.1485 0.1446 0.2104 0.0244  0.0222  0.0566  155 VAL   A C   
3272 C  C   B VAL   A 155 ? 0.1933 0.1988 0.2396 0.0163  0.0038  0.0454  155 VAL   A C   
3273 C  C   T VAL   A 155 ? 0.1608 0.1654 0.1777 -0.0086 0.0526  0.0639  155 VAL   A C   
3274 O  O   A VAL   A 155 ? 0.1447 0.1477 0.2342 0.0336  0.0250  0.0560  155 VAL   A O   
3275 O  O   B VAL   A 155 ? 0.1912 0.2055 0.2542 0.0203  0.0113  0.0453  155 VAL   A O   
3276 O  O   T VAL   A 155 ? 0.1581 0.1729 0.1819 -0.0053 0.0608  0.0604  155 VAL   A O   
3277 C  CB  A VAL   A 155 ? 0.1425 0.1373 0.1939 0.0072  0.0049  0.0390  155 VAL   A CB  
3278 C  CB  B VAL   A 155 ? 0.1671 0.1853 0.2012 0.0055  -0.0013 0.0323  155 VAL   A CB  
3279 C  CB  T VAL   A 155 ? 0.1547 0.1630 0.1892 -0.0211 0.0242  0.0496  155 VAL   A CB  
3280 C  CG1 A VAL   A 155 ? 0.1514 0.1425 0.1929 0.0086  0.0026  0.0380  155 VAL   A CG1 
3281 C  CG1 B VAL   A 155 ? 0.1642 0.1884 0.2069 0.0040  -0.0041 0.0327  155 VAL   A CG1 
3282 C  CG1 T VAL   A 155 ? 0.1590 0.1653 0.1834 -0.0197 0.0213  0.0516  155 VAL   A CG1 
3283 C  CG2 A VAL   A 155 ? 0.1472 0.1428 0.1965 0.0109  -0.0072 0.0316  155 VAL   A CG2 
3284 C  CG2 B VAL   A 155 ? 0.1664 0.1850 0.1999 0.0050  -0.0028 0.0287  155 VAL   A CG2 
3285 C  CG2 T VAL   A 155 ? 0.1582 0.1672 0.1925 -0.0164 0.0139  0.0432  155 VAL   A CG2 
3311 N  N   A PHE   A 156 ? 0.1594 0.1548 0.2204 0.0280  0.0277  0.0655  156 PHE   A N   
3312 N  N   B PHE   A 156 ? 0.2180 0.2136 0.2708 0.0224  0.0015  0.0442  156 PHE   A N   
3313 N  N   T PHE   A 156 ? 0.1702 0.1604 0.1799 -0.0013 0.0565  0.0745  156 PHE   A N   
3314 C  CA  A PHE   A 156 ? 0.1727 0.1617 0.2312 0.0322  0.0284  0.0694  156 PHE   A CA  
3315 C  CA  B PHE   A 156 ? 0.2456 0.2338 0.3082 0.0255  0.0012  0.0368  156 PHE   A CA  
3316 C  CA  T PHE   A 156 ? 0.1850 0.1543 0.1721 0.0072  0.0521  0.0747  156 PHE   A CA  
3317 C  C   A PHE   A 156 ? 0.1661 0.1637 0.2179 0.0375  0.0416  0.0789  156 PHE   A C   
3318 C  C   B PHE   A 156 ? 0.2622 0.2467 0.3200 0.0292  0.0027  0.0421  156 PHE   A C   
3319 C  C   T PHE   A 156 ? 0.1802 0.1650 0.1841 0.0129  0.0582  0.0720  156 PHE   A C   
3320 O  O   A PHE   A 156 ? 0.1712 0.1698 0.2146 0.0251  0.0466  0.0670  156 PHE   A O   
3321 O  O   B PHE   A 156 ? 0.2720 0.2527 0.3315 0.0205  0.0018  0.0382  156 PHE   A O   
3322 O  O   T PHE   A 156 ? 0.1844 0.1623 0.1870 0.0110  0.0653  0.0598  156 PHE   A O   
3323 C  CB  A PHE   A 156 ? 0.1860 0.1718 0.2429 0.0282  0.0157  0.0635  156 PHE   A CB  
3324 C  CB  B PHE   A 156 ? 0.2562 0.2491 0.3283 0.0196  0.0025  0.0228  156 PHE   A CB  
3325 C  CB  T PHE   A 156 ? 0.1929 0.1414 0.1521 0.0076  0.0418  0.0673  156 PHE   A CB  
3326 C  CG  A PHE   A 156 ? 0.2015 0.1791 0.2572 0.0275  0.0022  0.0537  156 PHE   A CG  
3327 C  CG  B PHE   A 156 ? 0.2660 0.2626 0.3460 0.0164  0.0015  0.0053  156 PHE   A CG  
3328 C  CG  T PHE   A 156 ? 0.1984 0.1331 0.1559 0.0110  0.0271  0.0655  156 PHE   A CG  
3329 C  CD1 A PHE   A 156 ? 0.2087 0.1842 0.2642 0.0264  0.0132  0.0471  156 PHE   A CD1 
3330 C  CD1 B PHE   A 156 ? 0.2697 0.2676 0.3547 0.0157  -0.0015 -0.0010 156 PHE   A CD1 
3331 C  CD1 T PHE   A 156 ? 0.2003 0.1315 0.1819 0.0127  0.0216  0.0492  156 PHE   A CD1 
3332 C  CD2 A PHE   A 156 ? 0.2124 0.1865 0.2569 0.0316  -0.0049 0.0541  156 PHE   A CD2 
3333 C  CD2 B PHE   A 156 ? 0.2668 0.2677 0.3476 0.0151  0.0003  -0.0017 156 PHE   A CD2 
3334 C  CD2 T PHE   A 156 ? 0.2057 0.1326 0.1679 0.0131  0.0175  0.0766  156 PHE   A CD2 
3335 C  CE1 A PHE   A 156 ? 0.2151 0.1868 0.2666 0.0265  0.0182  0.0461  156 PHE   A CE1 
3336 C  CE1 B PHE   A 156 ? 0.2711 0.2706 0.3577 0.0154  -0.0058 -0.0076 156 PHE   A CE1 
3337 C  CE1 T PHE   A 156 ? 0.2026 0.1335 0.1953 0.0129  0.0196  0.0401  156 PHE   A CE1 
3338 C  CE2 A PHE   A 156 ? 0.2213 0.1928 0.2603 0.0315  -0.0017 0.0462  156 PHE   A CE2 
3339 C  CE2 B PHE   A 156 ? 0.2693 0.2699 0.3531 0.0145  -0.0016 -0.0061 156 PHE   A CE2 
3340 C  CE2 T PHE   A 156 ? 0.2097 0.1356 0.1830 0.0115  0.0162  0.0688  156 PHE   A CE2 
3341 C  CZ  A PHE   A 156 ? 0.2225 0.1940 0.2630 0.0307  0.0149  0.0440  156 PHE   A CZ  
3342 C  CZ  B PHE   A 156 ? 0.2711 0.2719 0.3557 0.0156  -0.0055 -0.0105 156 PHE   A CZ  
3343 C  CZ  T PHE   A 156 ? 0.2054 0.1303 0.2025 0.0061  0.0223  0.0533  156 PHE   A CZ  
3371 N  N   A ASP   A 157 ? 0.1618 0.1717 0.2199 0.0498  0.0389  0.0833  157 ASP   A N   
3372 N  N   B ASP   A 157 ? 0.2676 0.2496 0.3127 0.0364  -0.0002 0.0553  157 ASP   A N   
3373 N  N   T ASP   A 157 ? 0.1668 0.1789 0.1928 0.0140  0.0506  0.0817  157 ASP   A N   
3374 C  CA  A ASP   A 157 ? 0.1744 0.1949 0.2379 0.0528  0.0348  0.0862  157 ASP   A CA  
3375 C  CA  B ASP   A 157 ? 0.2721 0.2562 0.3134 0.0351  -0.0006 0.0663  157 ASP   A CA  
3376 C  CA  T ASP   A 157 ? 0.1652 0.1984 0.2110 0.0211  0.0422  0.0843  157 ASP   A CA  
3377 C  C   A ASP   A 157 ? 0.1649 0.2107 0.2539 0.0506  0.0388  0.0916  157 ASP   A C   
3378 C  C   B ASP   A 157 ? 0.2607 0.2587 0.3137 0.0328  -0.0013 0.0709  157 ASP   A C   
3379 C  C   T ASP   A 157 ? 0.1649 0.2129 0.2205 0.0256  0.0466  0.0899  157 ASP   A C   
3380 O  O   A ASP   A 157 ? 0.1620 0.2083 0.2501 0.0497  0.0426  0.0946  157 ASP   A O   
3381 O  O   B ASP   A 157 ? 0.2598 0.2566 0.3119 0.0315  -0.0038 0.0758  157 ASP   A O   
3382 O  O   T ASP   A 157 ? 0.1590 0.2120 0.2172 0.0281  0.0544  0.0876  157 ASP   A O   
3383 C  CB  A ASP   A 157 ? 0.1944 0.2045 0.2531 0.0597  0.0270  0.0791  157 ASP   A CB  
3384 C  CB  B ASP   A 157 ? 0.2842 0.2603 0.3235 0.0355  -0.0018 0.0694  157 ASP   A CB  
3385 C  CB  T ASP   A 157 ? 0.1626 0.2007 0.2190 0.0281  0.0392  0.0839  157 ASP   A CB  
3386 C  CG  A ASP   A 157 ? 0.2140 0.2124 0.2770 0.0626  0.0178  0.0798  157 ASP   A CG  
3387 C  CG  B ASP   A 157 ? 0.2939 0.2607 0.3359 0.0362  -0.0075 0.0819  157 ASP   A CG  
3388 C  CG  T ASP   A 157 ? 0.1558 0.1949 0.2221 0.0353  0.0302  0.0908  157 ASP   A CG  
3389 O  OD1 A ASP   A 157 ? 0.2288 0.2232 0.3045 0.0579  0.0063  0.0651  157 ASP   A OD1 
3390 O  OD1 B ASP   A 157 ? 0.2955 0.2546 0.3341 0.0389  -0.0079 0.1010  157 ASP   A OD1 
3391 O  OD1 T ASP   A 157 ? 0.1523 0.1873 0.2356 0.0352  0.0341  0.0846  157 ASP   A OD1 
3392 O  OD2 A ASP   A 157 ? 0.2134 0.2066 0.2774 0.0625  0.0257  0.0907  157 ASP   A OD2 
3393 O  OD2 B ASP   A 157 ? 0.2980 0.2635 0.3487 0.0309  -0.0086 0.0779  157 ASP   A OD2 
3394 O  OD2 T ASP   A 157 ? 0.1506 0.1965 0.2244 0.0386  0.0195  0.0957  157 ASP   A OD2 
3407 N  N   A LYS   A 158 ? 0.1704 0.2339 0.2777 0.0446  0.0486  0.0763  158 LYS   A N   
3408 N  N   B LYS   A 158 ? 0.2524 0.2646 0.3174 0.0298  -0.0024 0.0659  158 LYS   A N   
3409 N  N   T LYS   A 158 ? 0.1802 0.2308 0.2377 0.0241  0.0536  0.0822  158 LYS   A N   
3410 C  CA  A LYS   A 158 ? 0.1729 0.2536 0.2918 0.0439  0.0567  0.0686  158 LYS   A CA  
3411 C  CA  B LYS   A 158 ? 0.2479 0.2735 0.3147 0.0261  0.0057  0.0640  158 LYS   A CA  
3412 C  CA  T LYS   A 158 ? 0.1931 0.2484 0.2614 0.0267  0.0521  0.0700  158 LYS   A CA  
3413 C  C   A LYS   A 158 ? 0.1610 0.2568 0.2779 0.0494  0.0492  0.0692  158 LYS   A C   
3414 C  C   B LYS   A 158 ? 0.2281 0.2750 0.2943 0.0306  -0.0061 0.0710  158 LYS   A C   
3415 C  C   T LYS   A 158 ? 0.1889 0.2480 0.2548 0.0315  0.0433  0.0634  158 LYS   A C   
3416 O  O   A LYS   A 158 ? 0.1573 0.2621 0.2866 0.0491  0.0504  0.0650  158 LYS   A O   
3417 O  O   B LYS   A 158 ? 0.2222 0.2751 0.2867 0.0210  -0.0054 0.0716  158 LYS   A O   
3418 O  O   T LYS   A 158 ? 0.1859 0.2496 0.2627 0.0344  0.0423  0.0566  158 LYS   A O   
3419 C  CB  A LYS   A 158 ? 0.1881 0.2663 0.3239 0.0380  0.0775  0.0618  158 LYS   A CB  
3420 C  CB  B LYS   A 158 ? 0.2619 0.2826 0.3384 0.0188  0.0233  0.0588  158 LYS   A CB  
3421 C  CB  T LYS   A 158 ? 0.2116 0.2641 0.3032 0.0224  0.0623  0.0580  158 LYS   A CB  
3422 C  CG  A LYS   A 158 ? 0.2046 0.2777 0.3566 0.0375  0.0877  0.0605  158 LYS   A CG  
3423 C  CG  B LYS   A 158 ? 0.2723 0.2913 0.3619 0.0118  0.0402  0.0592  158 LYS   A CG  
3424 C  CG  T LYS   A 158 ? 0.2278 0.2765 0.3423 0.0219  0.0691  0.0551  158 LYS   A CG  
3425 C  CD  A LYS   A 158 ? 0.2195 0.2879 0.3825 0.0411  0.0966  0.0615  158 LYS   A CD  
3426 C  CD  B LYS   A 158 ? 0.2790 0.2982 0.3771 0.0049  0.0552  0.0661  158 LYS   A CD  
3427 C  CD  T LYS   A 158 ? 0.2424 0.2857 0.3772 0.0252  0.0711  0.0549  158 LYS   A CD  
3428 C  CE  A LYS   A 158 ? 0.2284 0.2912 0.4008 0.0391  0.1029  0.0719  158 LYS   A CE  
3429 C  CE  B LYS   A 158 ? 0.2827 0.3010 0.3878 0.0048  0.0634  0.0752  158 LYS   A CE  
3430 C  CE  T LYS   A 158 ? 0.2516 0.2882 0.4049 0.0252  0.0692  0.0585  158 LYS   A CE  
3431 N  NZ  A LYS   A 158 ? 0.2320 0.2926 0.4093 0.0373  0.1107  0.0764  158 LYS   A NZ  
3432 N  NZ  B LYS   A 158 ? 0.2837 0.3033 0.3912 0.0055  0.0680  0.0786  158 LYS   A NZ  
3433 N  NZ  T LYS   A 158 ? 0.2557 0.2886 0.4183 0.0259  0.0701  0.0584  158 LYS   A NZ  
3473 N  N   A ASN   A 159 ? 0.1572 0.2527 0.2746 0.0462  0.0329  0.0699  159 ASN   A N   
3474 N  N   B ASN   A 159 ? 0.2195 0.2788 0.2930 0.0430  -0.0133 0.0734  159 ASN   A N   
3475 N  N   T ASN   A 159 ? 0.1914 0.2457 0.2608 0.0274  0.0307  0.0584  159 ASN   A N   
3476 C  CA  A ASN   A 159 ? 0.1609 0.2527 0.2656 0.0402  0.0095  0.0754  159 ASN   A CA  
3477 C  CA  B ASN   A 159 ? 0.2127 0.2836 0.2962 0.0484  -0.0182 0.0732  159 ASN   A CA  
3478 C  CA  T ASN   A 159 ? 0.2005 0.2465 0.2625 0.0211  0.0163  0.0587  159 ASN   A CA  
3479 C  C   A ASN   A 159 ? 0.1537 0.2547 0.2503 0.0346  0.0126  0.0685  159 ASN   A C   
3480 C  C   B ASN   A 159 ? 0.1837 0.2785 0.2672 0.0528  -0.0146 0.0796  159 ASN   A C   
3481 C  C   T ASN   A 159 ? 0.2050 0.2495 0.2596 0.0157  0.0227  0.0486  159 ASN   A C   
3482 O  O   A ASN   A 159 ? 0.1501 0.2514 0.2535 0.0403  0.0013  0.0445  159 ASN   A O   
3483 O  O   B ASN   A 159 ? 0.1667 0.2829 0.2634 0.0673  -0.0275 0.0812  159 ASN   A O   
3484 O  O   T ASN   A 159 ? 0.2054 0.2451 0.2644 0.0177  0.0178  0.0308  159 ASN   A O   
3485 C  CB  A ASN   A 159 ? 0.1743 0.2540 0.2857 0.0357  -0.0096 0.0825  159 ASN   A CB  
3486 C  CB  B ASN   A 159 ? 0.2354 0.2932 0.3380 0.0465  -0.0247 0.0624  159 ASN   A CB  
3487 C  CB  T ASN   A 159 ? 0.2076 0.2472 0.2795 0.0182  0.0008  0.0668  159 ASN   A CB  
3488 C  CG  A ASN   A 159 ? 0.1880 0.2606 0.3169 0.0360  -0.0111 0.0783  159 ASN   A CG  
3489 C  CG  B ASN   A 159 ? 0.2573 0.3033 0.3802 0.0384  -0.0279 0.0441  159 ASN   A CG  
3490 C  CG  T ASN   A 159 ? 0.2154 0.2517 0.3042 0.0190  -0.0031 0.0660  159 ASN   A CG  
3491 O  OD1 A ASN   A 159 ? 0.1892 0.2695 0.3340 0.0382  -0.0033 0.0824  159 ASN   A OD1 
3492 O  OD1 B ASN   A 159 ? 0.2629 0.3047 0.3967 0.0329  -0.0314 0.0390  159 ASN   A OD1 
3493 O  OD1 T ASN   A 159 ? 0.2150 0.2594 0.3189 0.0216  0.0049  0.0685  159 ASN   A OD1 
3494 N  ND2 A ASN   A 159 ? 0.1912 0.2610 0.3227 0.0386  -0.0211 0.0774  159 ASN   A ND2 
3495 N  ND2 B ASN   A 159 ? 0.2675 0.3084 0.3937 0.0358  -0.0311 0.0360  159 ASN   A ND2 
3496 N  ND2 T ASN   A 159 ? 0.2173 0.2522 0.3096 0.0209  -0.0130 0.0674  159 ASN   A ND2 
3515 N  N   A LEU   A 160 ? 0.1493 0.2562 0.2370 0.0254  0.0176  0.0836  160 LEU   A N   
3516 N  N   B LEU   A 160 ? 0.1744 0.2688 0.2459 0.0408  -0.0099 0.0889  160 LEU   A N   
3517 N  N   T LEU   A 160 ? 0.2074 0.2529 0.2581 0.0092  0.0278  0.0560  160 LEU   A N   
3518 C  CA  A LEU   A 160 ? 0.1508 0.2569 0.2236 0.0125  0.0335  0.0906  160 LEU   A CA  
3519 C  CA  B LEU   A 160 ? 0.1708 0.2592 0.2289 0.0326  0.0084  0.0897  160 LEU   A CA  
3520 C  CA  T LEU   A 160 ? 0.2128 0.2537 0.2511 0.0011  0.0370  0.0614  160 LEU   A CA  
3521 C  C   A LEU   A 160 ? 0.1336 0.2533 0.2137 0.0056  0.0340  0.0897  160 LEU   A C   
3522 C  C   B LEU   A 160 ? 0.1489 0.2510 0.2086 0.0257  0.0134  0.0874  160 LEU   A C   
3523 O  O   A LEU   A 160 ? 0.1197 0.2589 0.2055 0.0030  0.0232  0.0919  160 LEU   A O   
3524 O  O   B LEU   A 160 ? 0.1360 0.2567 0.2014 0.0226  0.0063  0.0910  160 LEU   A O   
3525 C  CB  A LEU   A 160 ? 0.1619 0.2590 0.2244 0.0088  0.0356  0.0926  160 LEU   A CB  
3526 C  CB  B LEU   A 160 ? 0.1855 0.2577 0.2367 0.0321  0.0118  0.0822  160 LEU   A CB  
3527 C  CB  T LEU   A 160 ? 0.2148 0.2536 0.2428 -0.0058 0.0415  0.0646  160 LEU   A CB  
3528 C  CG  A LEU   A 160 ? 0.1723 0.2629 0.2438 0.0021  0.0351  0.0777  160 LEU   A CG  
3529 C  CG  B LEU   A 160 ? 0.1987 0.2590 0.2594 0.0307  0.0137  0.0579  160 LEU   A CG  
3530 C  CG  T LEU   A 160 ? 0.2183 0.2552 0.2473 -0.0146 0.0428  0.0575  160 LEU   A CG  
3531 C  CD1 A LEU   A 160 ? 0.1822 0.2657 0.2561 -0.0024 0.0381  0.0719  160 LEU   A CD1 
3532 C  CD1 B LEU   A 160 ? 0.2092 0.2595 0.2713 0.0253  0.0174  0.0472  160 LEU   A CD1 
3533 C  CD1 T LEU   A 160 ? 0.2238 0.2577 0.2544 -0.0169 0.0436  0.0530  160 LEU   A CD1 
3534 C  CD2 A LEU   A 160 ? 0.1734 0.2619 0.2504 0.0002  0.0378  0.0705  160 LEU   A CD2 
3535 C  CD2 B LEU   A 160 ? 0.1991 0.2592 0.2652 0.0336  0.0203  0.0477  160 LEU   A CD2 
3536 C  CD2 T LEU   A 160 ? 0.2175 0.2531 0.2476 -0.0187 0.0467  0.0553  160 LEU   A CD2 
3569 N  N   A TYR   A 161 ? 0.1475 0.2417 0.2259 0.0020  0.0361  0.0880  161 TYR   A N   
3570 N  N   B TYR   A 161 ? 0.1546 0.2351 0.2067 0.0214  0.0190  0.0796  161 TYR   A N   
3571 C  CA  A TYR   A 161 ? 0.1509 0.2375 0.2225 -0.0010 0.0334  0.0830  161 TYR   A CA  
3572 C  CA  B TYR   A 161 ? 0.1546 0.2227 0.2005 0.0161  0.0252  0.0758  161 TYR   A CA  
3573 C  C   A TYR   A 161 ? 0.1516 0.2613 0.2273 -0.0037 0.0258  0.0778  161 TYR   A C   
3574 C  C   B TYR   A 161 ? 0.1513 0.2349 0.2070 0.0112  0.0198  0.0800  161 TYR   A C   
3575 O  O   A TYR   A 161 ? 0.1483 0.2641 0.2045 -0.0037 0.0152  0.0832  161 TYR   A O   
3576 O  O   B TYR   A 161 ? 0.1474 0.2337 0.1992 0.0064  0.0205  0.0859  161 TYR   A O   
3577 C  CB  A TYR   A 161 ? 0.1592 0.2246 0.2350 -0.0033 0.0288  0.0669  161 TYR   A CB  
3578 C  CB  B TYR   A 161 ? 0.1633 0.2084 0.2044 0.0105  0.0303  0.0590  161 TYR   A CB  
3579 C  CG  A TYR   A 161 ? 0.1522 0.2130 0.2294 -0.0005 0.0137  0.0444  161 TYR   A CG  
3580 C  CG  B TYR   A 161 ? 0.1634 0.1944 0.2019 0.0111  0.0265  0.0385  161 TYR   A CG  
3581 C  CD1 A TYR   A 161 ? 0.1465 0.2045 0.2268 -0.0025 0.0062  0.0343  161 TYR   A CD1 
3582 C  CD1 B TYR   A 161 ? 0.1616 0.1838 0.1992 0.0089  0.0229  0.0299  161 TYR   A CD1 
3583 C  CD2 A TYR   A 161 ? 0.1521 0.2110 0.2259 0.0114  0.0058  0.0370  161 TYR   A CD2 
3584 C  CD2 B TYR   A 161 ? 0.1654 0.1896 0.2033 0.0154  0.0278  0.0327  161 TYR   A CD2 
3585 C  CE1 A TYR   A 161 ? 0.1494 0.1923 0.2152 -0.0022 -0.0001 0.0344  161 TYR   A CE1 
3586 C  CE1 B TYR   A 161 ? 0.1645 0.1797 0.1979 0.0099  0.0197  0.0236  161 TYR   A CE1 
3587 C  CE2 A TYR   A 161 ? 0.1513 0.1977 0.2204 0.0061  0.0032  0.0366  161 TYR   A CE2 
3588 C  CE2 B TYR   A 161 ? 0.1667 0.1834 0.2088 0.0095  0.0289  0.0297  161 TYR   A CE2 
3589 C  CZ  A TYR   A 161 ? 0.1554 0.1868 0.2017 -0.0046 -0.0029 0.0376  161 TYR   A CZ  
3590 C  CZ  B TYR   A 161 ? 0.1729 0.1797 0.2103 0.0084  0.0220  0.0257  161 TYR   A CZ  
3591 O  OH  A TYR   A 161 ? 0.1733 0.1763 0.1966 -0.0096 -0.0029 0.0434  161 TYR   A OH  
3592 O  OH  B TYR   A 161 ? 0.1887 0.1788 0.2310 0.0076  0.0115  0.0214  161 TYR   A OH  
3611 N  N   A ASP   A 162 ? 0.1492 0.2863 0.2374 0.0019  0.0347  0.0713  162 ASP   A N   
3612 N  N   B ASP   A 162 ? 0.1484 0.2523 0.2157 0.0123  0.0209  0.0794  162 ASP   A N   
3613 C  CA  A ASP   A 162 ? 0.1500 0.3141 0.2544 0.0036  0.0398  0.0538  162 ASP   A CA  
3614 C  CA  B ASP   A 162 ? 0.1494 0.2734 0.2332 0.0073  0.0230  0.0627  162 ASP   A CA  
3615 C  C   A ASP   A 162 ? 0.1422 0.3203 0.2521 -0.0011 0.0309  0.0490  162 ASP   A C   
3616 C  C   B ASP   A 162 ? 0.1412 0.2823 0.2363 0.0024  0.0159  0.0615  162 ASP   A C   
3617 O  O   A ASP   A 162 ? 0.1452 0.3226 0.2663 0.0043  0.0320  0.0351  162 ASP   A O   
3618 O  O   B ASP   A 162 ? 0.1364 0.2821 0.2484 -0.0028 0.0145  0.0540  162 ASP   A O   
3619 C  CB  A ASP   A 162 ? 0.1599 0.3361 0.2773 0.0131  0.0500  0.0378  162 ASP   A CB  
3620 C  CB  B ASP   A 162 ? 0.1613 0.2867 0.2583 0.0090  0.0232  0.0439  162 ASP   A CB  
3621 C  CG  A ASP   A 162 ? 0.1750 0.3589 0.3070 0.0207  0.0573  0.0259  162 ASP   A CG  
3622 C  CG  B ASP   A 162 ? 0.1759 0.3009 0.2799 0.0126  0.0260  0.0275  162 ASP   A CG  
3623 O  OD1 A ASP   A 162 ? 0.1901 0.3699 0.3162 0.0141  0.0631  0.0261  162 ASP   A OD1 
3624 O  OD1 B ASP   A 162 ? 0.1869 0.3085 0.2889 0.0092  0.0327  0.0227  162 ASP   A OD1 
3625 O  OD2 A ASP   A 162 ? 0.1912 0.3693 0.3381 0.0333  0.0540  0.0110  162 ASP   A OD2 
3626 O  OD2 B ASP   A 162 ? 0.1867 0.3052 0.2956 0.0210  0.0241  0.0135  162 ASP   A OD2 
3635 N  N   A LYS   A 163 ? 0.1507 0.3288 0.2533 -0.0034 0.0169  0.0520  163 LYS   A N   
3636 N  N   B LYS   A 163 ? 0.1489 0.2920 0.2442 0.0050  0.0048  0.0623  163 LYS   A N   
3637 C  CA  A LYS   A 163 ? 0.1636 0.3363 0.2619 -0.0028 -0.0001 0.0469  163 LYS   A CA  
3638 C  CA  B LYS   A 163 ? 0.1620 0.3024 0.2495 0.0041  -0.0007 0.0540  163 LYS   A CA  
3639 C  C   A LYS   A 163 ? 0.1560 0.3209 0.2478 -0.0087 0.0108  0.0503  163 LYS   A C   
3640 C  C   B LYS   A 163 ? 0.1501 0.2968 0.2290 -0.0009 0.0038  0.0491  163 LYS   A C   
3641 O  O   A LYS   A 163 ? 0.1476 0.3187 0.2510 -0.0093 0.0181  0.0357  163 LYS   A O   
3642 O  O   B LYS   A 163 ? 0.1509 0.3079 0.2339 -0.0040 -0.0007 0.0485  163 LYS   A O   
3643 C  CB  A LYS   A 163 ? 0.1981 0.3569 0.2968 0.0124  -0.0167 0.0383  163 LYS   A CB  
3644 C  CB  B LYS   A 163 ? 0.1942 0.3162 0.2898 0.0137  -0.0087 0.0494  163 LYS   A CB  
3645 C  CG  A LYS   A 163 ? 0.2252 0.3735 0.3490 0.0158  -0.0130 0.0317  163 LYS   A CG  
3646 C  CG  B LYS   A 163 ? 0.2223 0.3303 0.3379 0.0117  -0.0075 0.0470  163 LYS   A CG  
3647 C  CD  A LYS   A 163 ? 0.2490 0.3881 0.3978 0.0134  -0.0097 0.0283  163 LYS   A CD  
3648 C  CD  B LYS   A 163 ? 0.2469 0.3420 0.3800 0.0090  -0.0059 0.0456  163 LYS   A CD  
3649 C  CE  A LYS   A 163 ? 0.2677 0.3973 0.4409 0.0094  -0.0055 0.0266  163 LYS   A CE  
3650 C  CE  B LYS   A 163 ? 0.2649 0.3505 0.4148 0.0064  -0.0047 0.0468  163 LYS   A CE  
3651 N  NZ  A LYS   A 163 ? 0.2780 0.4041 0.4643 0.0044  -0.0086 0.0253  163 LYS   A NZ  
3652 N  NZ  B LYS   A 163 ? 0.2764 0.3555 0.4343 0.0039  -0.0055 0.0430  163 LYS   A NZ  
3679 N  N   A LEU   A 164 ? 0.1388 0.2984 0.2311 -0.0150 0.0129  0.0535  164 LEU   A N   
3680 N  N   B LEU   A 164 ? 0.1308 0.2753 0.2022 -0.0027 0.0064  0.0437  164 LEU   A N   
3681 C  CA  A LEU   A 164 ? 0.1483 0.2807 0.2192 -0.0320 0.0230  0.0561  164 LEU   A CA  
3682 C  CA  B LEU   A 164 ? 0.1326 0.2593 0.1925 -0.0096 0.0183  0.0430  164 LEU   A CA  
3683 C  C   A LEU   A 164 ? 0.1602 0.2808 0.2189 -0.0374 0.0203  0.0531  164 LEU   A C   
3684 C  C   B LEU   A 164 ? 0.1407 0.2600 0.1943 -0.0089 0.0246  0.0381  164 LEU   A C   
3685 O  O   A LEU   A 164 ? 0.1676 0.2839 0.2257 -0.0411 0.0358  0.0435  164 LEU   A O   
3686 O  O   B LEU   A 164 ? 0.1443 0.2640 0.1872 -0.0143 0.0463  0.0287  164 LEU   A O   
3687 C  CB  A LEU   A 164 ? 0.1469 0.2676 0.2217 -0.0317 0.0233  0.0528  164 LEU   A CB  
3688 C  CB  B LEU   A 164 ? 0.1331 0.2468 0.1916 -0.0115 0.0174  0.0427  164 LEU   A CB  
3689 C  CG  A LEU   A 164 ? 0.1512 0.2551 0.2288 -0.0228 0.0220  0.0548  164 LEU   A CG  
3690 C  CG  B LEU   A 164 ? 0.1366 0.2348 0.1930 -0.0081 0.0150  0.0441  164 LEU   A CG  
3691 C  CD1 A LEU   A 164 ? 0.1420 0.2478 0.2311 -0.0088 0.0258  0.0642  164 LEU   A CD1 
3692 C  CD1 B LEU   A 164 ? 0.1380 0.2291 0.1934 -0.0080 0.0160  0.0545  164 LEU   A CD1 
3693 C  CD2 A LEU   A 164 ? 0.1619 0.2535 0.2240 -0.0250 0.0215  0.0495  164 LEU   A CD2 
3694 C  CD2 B LEU   A 164 ? 0.1329 0.2310 0.1886 -0.0080 0.0125  0.0370  164 LEU   A CD2 
3717 N  N   A VAL   A 165 ? 0.1553 0.2777 0.2062 -0.0370 0.0161  0.0655  165 VAL   A N   
3718 N  N   B VAL   A 165 ? 0.1398 0.2569 0.1907 -0.0046 0.0245  0.0427  165 VAL   A N   
3719 C  CA  A VAL   A 165 ? 0.1610 0.2791 0.1820 -0.0382 0.0135  0.0750  165 VAL   A CA  
3720 C  CA  B VAL   A 165 ? 0.1441 0.2580 0.1841 -0.0033 0.0269  0.0422  165 VAL   A CA  
3721 C  C   A VAL   A 165 ? 0.1560 0.2872 0.1880 -0.0270 0.0150  0.0662  165 VAL   A C   
3722 C  C   B VAL   A 165 ? 0.1369 0.2630 0.1891 -0.0077 0.0280  0.0420  165 VAL   A C   
3723 O  O   A VAL   A 165 ? 0.1560 0.2905 0.1841 -0.0291 0.0146  0.0574  165 VAL   A O   
3724 O  O   B VAL   A 165 ? 0.1333 0.2620 0.1786 -0.0112 0.0281  0.0426  165 VAL   A O   
3725 C  CB  A VAL   A 165 ? 0.1737 0.2766 0.1928 -0.0495 0.0191  0.0714  165 VAL   A CB  
3726 C  CB  B VAL   A 165 ? 0.1533 0.2563 0.1881 0.0015  0.0281  0.0365  165 VAL   A CB  
3727 C  CG1 A VAL   A 165 ? 0.1777 0.2820 0.1998 -0.0507 0.0161  0.0553  165 VAL   A CG1 
3728 C  CG1 B VAL   A 165 ? 0.1585 0.2575 0.1960 0.0023  0.0223  0.0289  165 VAL   A CG1 
3729 C  CG2 A VAL   A 165 ? 0.1795 0.2785 0.1983 -0.0477 0.0162  0.0748  165 VAL   A CG2 
3730 C  CG2 B VAL   A 165 ? 0.1579 0.2583 0.1940 0.0059  0.0219  0.0314  165 VAL   A CG2 
3749 N  N   A SER   A 166 ? 0.1457 0.2893 0.2043 -0.0181 0.0167  0.0580  166 SER   A N   
3750 N  N   B SER   A 166 ? 0.1296 0.2671 0.2120 -0.0128 0.0276  0.0430  166 SER   A N   
3751 C  CA  A SER   A 166 ? 0.1524 0.2923 0.2115 -0.0185 0.0153  0.0504  166 SER   A CA  
3752 C  CA  B SER   A 166 ? 0.1368 0.2731 0.2250 -0.0165 0.0206  0.0384  166 SER   A CA  
3753 C  C   A SER   A 166 ? 0.1518 0.2900 0.2120 -0.0116 0.0064  0.0487  166 SER   A C   
3754 C  C   B SER   A 166 ? 0.1438 0.2787 0.2232 -0.0277 0.0198  0.0375  166 SER   A C   
3755 O  O   A SER   A 166 ? 0.1724 0.3043 0.2390 -0.0260 0.0144  0.0376  166 SER   A O   
3756 O  O   B SER   A 166 ? 0.1504 0.2860 0.2413 -0.0497 0.0301  0.0335  166 SER   A O   
3757 C  CB  A SER   A 166 ? 0.1560 0.2937 0.2286 -0.0196 0.0082  0.0438  166 SER   A CB  
3758 C  CB  B SER   A 166 ? 0.1407 0.2732 0.2446 -0.0120 0.0098  0.0297  166 SER   A CB  
3759 O  OG  A SER   A 166 ? 0.1639 0.2954 0.2406 -0.0150 0.0128  0.0481  166 SER   A OG  
3760 O  OG  B SER   A 166 ? 0.1489 0.2745 0.2602 -0.0032 0.0012  0.0292  166 SER   A OG  
3771 N  N   A SER   A 167 ? 0.1503 0.2734 0.1926 0.0101  -0.0030 0.0621  167 SER   A N   
3772 N  N   B SER   A 167 ? 0.1551 0.2736 0.2265 -0.0156 0.0211  0.0385  167 SER   A N   
3773 C  CA  A SER   A 167 ? 0.1676 0.2599 0.2007 0.0105  -0.0082 0.0494  167 SER   A CA  
3774 C  CA  B SER   A 167 ? 0.1736 0.2707 0.2104 -0.0095 0.0254  0.0351  167 SER   A CA  
3775 C  C   A SER   A 167 ? 0.1774 0.2538 0.2176 0.0159  0.0148  0.0522  167 SER   A C   
3776 C  C   B SER   A 167 ? 0.1714 0.2723 0.2143 0.0017  0.0270  0.0306  167 SER   A C   
3777 O  O   A SER   A 167 ? 0.2019 0.2630 0.2473 0.0265  0.0014  0.0521  167 SER   A O   
3778 O  O   B SER   A 167 ? 0.1808 0.2773 0.2269 0.0061  0.0184  0.0328  167 SER   A O   
3779 C  CB  A SER   A 167 ? 0.1636 0.2519 0.2121 0.0057  0.0045  0.0470  167 SER   A CB  
3780 C  CB  B SER   A 167 ? 0.1909 0.2688 0.2162 -0.0106 0.0314  0.0218  167 SER   A CB  
3781 O  OG  A SER   A 167 ? 0.1679 0.2491 0.2127 -0.0033 0.0164  0.0325  167 SER   A OG  
3782 O  OG  B SER   A 167 ? 0.2043 0.2700 0.2208 -0.0106 0.0371  0.0138  167 SER   A OG  
3793 N  N   A PHE   A 168 ? 0.1631 0.2416 0.2201 0.0220  0.0206  0.0555  168 PHE   A N   
3794 N  N   B PHE   A 168 ? 0.1641 0.2668 0.2085 0.0082  0.0267  0.0222  168 PHE   A N   
3795 C  CA  A PHE   A 168 ? 0.1613 0.2427 0.2378 0.0149  0.0258  0.0604  168 PHE   A CA  
3796 C  CA  B PHE   A 168 ? 0.1683 0.2639 0.2082 0.0068  0.0258  0.0162  168 PHE   A CA  
3797 C  C   A PHE   A 168 ? 0.1648 0.2510 0.2656 0.0044  0.0568  0.0475  168 PHE   A C   
3798 C  C   B PHE   A 168 ? 0.1841 0.2752 0.2432 0.0028  0.0416  0.0134  168 PHE   A C   
3799 O  O   A PHE   A 168 ? 0.1763 0.2566 0.3068 0.0008  0.0591  0.0483  168 PHE   A O   
3800 O  O   B PHE   A 168 ? 0.1857 0.2764 0.2516 -0.0001 0.0531  0.0046  168 PHE   A O   
3801 C  CB  A PHE   A 168 ? 0.1624 0.2388 0.2315 0.0110  0.0144  0.0684  168 PHE   A CB  
3802 C  CB  B PHE   A 168 ? 0.1684 0.2536 0.1994 -0.0023 0.0081  0.0188  168 PHE   A CB  
3803 C  CG  A PHE   A 168 ? 0.1628 0.2457 0.2371 0.0093  0.0073  0.0611  168 PHE   A CG  
3804 C  CG  B PHE   A 168 ? 0.1603 0.2394 0.1890 -0.0102 -0.0079 0.0239  168 PHE   A CG  
3805 C  CD1 A PHE   A 168 ? 0.1668 0.2530 0.2462 0.0010  0.0105  0.0588  168 PHE   A CD1 
3806 C  CD1 B PHE   A 168 ? 0.1584 0.2362 0.1855 -0.0146 -0.0121 0.0274  168 PHE   A CD1 
3807 C  CD2 A PHE   A 168 ? 0.1601 0.2490 0.2354 0.0097  0.0235  0.0614  168 PHE   A CD2 
3808 C  CD2 B PHE   A 168 ? 0.1581 0.2324 0.1804 -0.0067 -0.0151 0.0244  168 PHE   A CD2 
3809 C  CE1 A PHE   A 168 ? 0.1650 0.2556 0.2494 0.0041  0.0165  0.0613  168 PHE   A CE1 
3810 C  CE1 B PHE   A 168 ? 0.1511 0.2326 0.1869 -0.0181 -0.0180 0.0238  168 PHE   A CE1 
3811 C  CE2 A PHE   A 168 ? 0.1680 0.2472 0.2428 0.0134  0.0252  0.0656  168 PHE   A CE2 
3812 C  CE2 B PHE   A 168 ? 0.1605 0.2297 0.1846 -0.0052 -0.0221 0.0271  168 PHE   A CE2 
3813 C  CZ  A PHE   A 168 ? 0.1630 0.2521 0.2458 0.0085  0.0228  0.0637  168 PHE   A CZ  
3814 C  CZ  B PHE   A 168 ? 0.1584 0.2311 0.1913 -0.0112 -0.0144 0.0241  168 PHE   A CZ  
3833 N  N   A LEU   A 169 ? 0.1851 0.2522 0.2886 -0.0077 0.0608  0.0240  169 LEU   A N   
3834 N  N   B LEU   A 169 ? 0.2046 0.2901 0.2726 0.0062  0.0387  0.0180  169 LEU   A N   
3835 C  CA  A LEU   A 169 ? 0.2170 0.2624 0.3151 0.0017  0.0441  0.0142  169 LEU   A CA  
3836 C  CA  B LEU   A 169 ? 0.2317 0.3063 0.3111 0.0082  0.0328  0.0159  169 LEU   A CA  
3837 C  C   A LEU   A 169 ? 0.2114 0.2602 0.3276 -0.0001 0.0467  0.0272  169 LEU   A C   
3838 C  C   B LEU   A 169 ? 0.2428 0.3127 0.3321 0.0101  0.0301  0.0146  169 LEU   A C   
3839 O  O   A LEU   A 169 ? 0.2133 0.2666 0.3346 0.0014  0.0393  0.0220  169 LEU   A O   
3840 O  O   B LEU   A 169 ? 0.2520 0.3150 0.3425 0.0065  0.0295  0.0154  169 LEU   A O   
3841 C  CB  A LEU   A 169 ? 0.2426 0.2763 0.3232 0.0086  0.0403  -0.0114 169 LEU   A CB  
3842 C  CB  B LEU   A 169 ? 0.2441 0.3124 0.3187 0.0090  0.0320  0.0157  169 LEU   A CB  
3843 C  CG  A LEU   A 169 ? 0.2699 0.2887 0.3288 0.0100  0.0410  -0.0411 169 LEU   A CG  
3844 C  CG  B LEU   A 169 ? 0.2533 0.3139 0.3275 0.0098  0.0339  0.0176  169 LEU   A CG  
3845 C  CD1 A LEU   A 169 ? 0.2850 0.2890 0.3337 0.0071  0.0367  -0.0474 169 LEU   A CD1 
3846 C  CD1 B LEU   A 169 ? 0.2557 0.3135 0.3368 0.0099  0.0304  0.0166  169 LEU   A CD1 
3847 C  CD2 A LEU   A 169 ? 0.2765 0.2970 0.3297 0.0106  0.0404  -0.0484 169 LEU   A CD2 
3848 C  CD2 B LEU   A 169 ? 0.2598 0.3172 0.3263 0.0065  0.0356  0.0195  169 LEU   A CD2 
3849 O  OXT A LEU   A 169 ? 0.2045 0.2644 0.3322 -0.0034 0.0520  0.0352  169 LEU   A OXT 
3850 O  OXT B LEU   A 169 ? 0.2427 0.3160 0.3379 0.0097  0.0267  0.0127  169 LEU   A OXT 
3873 N  N   . SER   B 1   ? 0.3452 0.3359 0.3537 -0.1079 -0.0778 0.0439  1   SER   B N   
3874 C  CA  . SER   B 1   ? 0.3361 0.3425 0.3486 -0.1149 -0.0906 0.0393  1   SER   B CA  
3875 C  C   . SER   B 1   ? 0.3070 0.3486 0.3357 -0.1112 -0.0947 0.0592  1   SER   B C   
3876 O  O   . SER   B 1   ? 0.3179 0.3519 0.3271 -0.1015 -0.0868 0.0530  1   SER   B O   
3877 C  CB  . SER   B 1   ? 0.3480 0.3351 0.3813 -0.1200 -0.0846 0.0108  1   SER   B CB  
3878 O  OG  . SER   B 1   ? 0.3652 0.3471 0.4283 -0.1157 -0.0642 -0.0041 1   SER   B OG  
3886 N  N   A MET   B 2   ? 0.2951 0.3517 0.3470 -0.1107 -0.0906 0.0849  2   MET   B N   
3887 N  N   B MET   B 2   ? 0.2927 0.3433 0.3306 -0.1060 -0.0910 0.0870  2   MET   B N   
3888 C  CA  A MET   B 2   ? 0.2878 0.3529 0.3626 -0.0958 -0.0876 0.1036  2   MET   B CA  
3889 C  CA  B MET   B 2   ? 0.2810 0.3389 0.3268 -0.0921 -0.0890 0.1117  2   MET   B CA  
3890 C  C   A MET   B 2   ? 0.2564 0.3320 0.3295 -0.0814 -0.0957 0.1342  2   MET   B C   
3891 C  C   B MET   B 2   ? 0.2557 0.3209 0.3097 -0.0836 -0.0932 0.1348  2   MET   B C   
3892 O  O   A MET   B 2   ? 0.2537 0.3416 0.3270 -0.0683 -0.1081 0.1405  2   MET   B O   
3893 O  O   B MET   B 2   ? 0.2552 0.3235 0.3045 -0.0770 -0.1011 0.1390  2   MET   B O   
3894 C  CB  A MET   B 2   ? 0.3191 0.3795 0.4350 -0.0803 -0.0673 0.0813  2   MET   B CB  
3895 C  CB  B MET   B 2   ? 0.2991 0.3564 0.3535 -0.0761 -0.0782 0.1068  2   MET   B CB  
3896 C  CG  A MET   B 2   ? 0.3455 0.4035 0.5104 -0.0631 -0.0480 0.0695  2   MET   B CG  
3897 C  CG  B MET   B 2   ? 0.3128 0.3705 0.3754 -0.0587 -0.0703 0.1115  2   MET   B CG  
3898 S  SD  A MET   B 2   ? 0.3709 0.4254 0.5782 -0.0470 -0.0313 0.0576  2   MET   B SD  
3899 S  SD  B MET   B 2   ? 0.3264 0.3855 0.3956 -0.0422 -0.0663 0.1148  2   MET   B SD  
3900 C  CE  A MET   B 2   ? 0.3694 0.4278 0.5822 -0.0479 -0.0225 0.0535  2   MET   B CE  
3901 C  CE  B MET   B 2   ? 0.3262 0.3857 0.3997 -0.0431 -0.0597 0.1066  2   MET   B CE  
3920 N  N   . VAL   B 3   ? 0.2334 0.3005 0.3032 -0.0843 -0.0890 0.1483  3   VAL   B N   
3921 C  CA  . VAL   B 3   ? 0.2187 0.2630 0.2994 -0.0701 -0.0787 0.1298  3   VAL   B CA  
3922 C  C   . VAL   B 3   ? 0.1987 0.2526 0.2579 -0.0682 -0.0748 0.1106  3   VAL   B C   
3923 O  O   . VAL   B 3   ? 0.1963 0.2707 0.2749 -0.0725 -0.0777 0.1182  3   VAL   B O   
3924 C  CB  . VAL   B 3   ? 0.2305 0.2497 0.3556 -0.0712 -0.0722 0.1095  3   VAL   B CB  
3925 C  CG1 . VAL   B 3   ? 0.2361 0.2389 0.3725 -0.0726 -0.0703 0.1095  3   VAL   B CG1 
3926 C  CG2 . VAL   B 3   ? 0.2347 0.2542 0.3787 -0.0675 -0.0597 0.1133  3   VAL   B CG2 
3937 N  N   . ASN   B 4   ? 0.1890 0.2183 0.2200 -0.0664 -0.0635 0.0887  4   ASN   B N   
3938 C  CA  . ASN   B 4   ? 0.1931 0.2167 0.1999 -0.0597 -0.0525 0.0545  4   ASN   B CA  
3939 C  C   . ASN   B 4   ? 0.1929 0.2283 0.2038 -0.0616 -0.0420 0.0408  4   ASN   B C   
3940 O  O   . ASN   B 4   ? 0.1905 0.2391 0.2188 -0.0584 -0.0361 0.0252  4   ASN   B O   
3941 C  CB  . ASN   B 4   ? 0.1919 0.2090 0.1912 -0.0580 -0.0695 0.0444  4   ASN   B CB  
3942 C  CG  . ASN   B 4   ? 0.1946 0.1920 0.1871 -0.0545 -0.0619 0.0395  4   ASN   B CG  
3943 O  OD1 . ASN   B 4   ? 0.1981 0.1717 0.1926 -0.0470 -0.0611 0.0340  4   ASN   B OD1 
3944 N  ND2 . ASN   B 4   ? 0.2134 0.2016 0.1853 -0.0350 -0.0418 0.0262  4   ASN   B ND2 
3951 N  N   . SER   B 5   ? 0.2110 0.2496 0.2014 -0.0611 -0.0316 0.0341  5   SER   B N   
3952 C  CA  . SER   B 5   ? 0.2420 0.2869 0.2267 -0.0558 -0.0092 0.0370  5   SER   B CA  
3953 C  C   . SER   B 5   ? 0.2620 0.2941 0.2580 -0.0755 0.0155  0.0405  5   SER   B C   
3954 O  O   . SER   B 5   ? 0.2770 0.2834 0.3155 -0.0695 0.0469  0.0283  5   SER   B O   
3955 C  CB  . SER   B 5   ? 0.2559 0.3114 0.2509 -0.0455 0.0015  0.0475  5   SER   B CB  
3956 O  OG  . SER   B 5   ? 0.2846 0.3388 0.3096 -0.0306 0.0008  0.0496  5   SER   B OG  
3962 N  N   . PHE   B 6   ? 0.2816 0.3178 0.2431 -0.0867 0.0293  0.0509  6   PHE   B N   
3963 C  CA  . PHE   B 6   ? 0.2927 0.3251 0.2146 -0.1061 0.0332  0.0300  6   PHE   B CA  
3964 C  C   . PHE   B 6   ? 0.3454 0.3619 0.2651 -0.1119 0.0550  -0.0009 6   PHE   B C   
3965 O  O   . PHE   B 6   ? 0.3611 0.3914 0.2867 -0.0981 0.0420  -0.0190 6   PHE   B O   
3966 C  CB  . PHE   B 6   ? 0.2641 0.3011 0.1922 -0.0963 0.0050  0.0250  6   PHE   B CB  
3967 C  CG  . PHE   B 6   ? 0.2293 0.2613 0.1758 -0.0858 -0.0148 0.0184  6   PHE   B CG  
3968 C  CD1 . PHE   B 6   ? 0.2256 0.2275 0.1716 -0.0788 -0.0301 0.0147  6   PHE   B CD1 
3969 C  CD2 . PHE   B 6   ? 0.2035 0.2578 0.1773 -0.0681 -0.0165 0.0455  6   PHE   B CD2 
3970 C  CE1 . PHE   B 6   ? 0.2178 0.2048 0.1797 -0.0651 -0.0318 0.0155  6   PHE   B CE1 
3971 C  CE2 . PHE   B 6   ? 0.2038 0.2387 0.2148 -0.0558 -0.0082 0.0417  6   PHE   B CE2 
3972 C  CZ  . PHE   B 6   ? 0.2087 0.2142 0.2007 -0.0525 -0.0213 0.0198  6   PHE   B CZ  
3982 N  N   . SER   B 7   ? 0.3890 0.3561 0.2804 -0.1379 0.0844  -0.0231 7   SER   B N   
3983 C  CA  . SER   B 7   ? 0.4327 0.3790 0.3406 -0.1404 0.1099  -0.0288 7   SER   B CA  
3984 C  C   . SER   B 7   ? 0.4310 0.3569 0.3238 -0.1422 0.1246  -0.0498 7   SER   B C   
3985 O  O   . SER   B 7   ? 0.4400 0.3510 0.3356 -0.1475 0.1246  -0.0535 7   SER   B O   
3986 C  CB  . SER   B 7   ? 0.4553 0.4076 0.4192 -0.1378 0.1305  -0.0148 7   SER   B CB  
3987 O  OG  . SER   B 7   ? 0.4555 0.4457 0.4698 -0.1367 0.1425  -0.0092 7   SER   B OG  
3993 N  N   . GLY   B 8   ? 0.4198 0.3368 0.3104 -0.1242 0.1270  -0.0689 8   GLY   B N   
3994 C  CA  . GLY   B 8   ? 0.4047 0.3153 0.3108 -0.1124 0.1259  -0.0789 8   GLY   B CA  
3995 C  C   . GLY   B 8   ? 0.3871 0.2841 0.2970 -0.1098 0.1292  -0.0707 8   GLY   B C   
3996 O  O   . GLY   B 8   ? 0.3983 0.2907 0.3265 -0.1014 0.1326  -0.0742 8   GLY   B O   
4000 N  N   . TYR   B 9   ? 0.3692 0.2596 0.2666 -0.0984 0.1040  -0.0808 9   TYR   B N   
4001 C  CA  . TYR   B 9   ? 0.3455 0.2299 0.2502 -0.0870 0.0775  -0.0615 9   TYR   B CA  
4002 C  C   . TYR   B 9   ? 0.3385 0.2270 0.2424 -0.0774 0.0457  -0.0457 9   TYR   B C   
4003 O  O   . TYR   B 9   ? 0.3451 0.2453 0.2741 -0.0757 0.0448  -0.0371 9   TYR   B O   
4004 C  CB  . TYR   B 9   ? 0.3358 0.2059 0.2518 -0.0820 0.0721  -0.0573 9   TYR   B CB  
4005 C  CG  . TYR   B 9   ? 0.3234 0.1889 0.2543 -0.0869 0.0591  -0.0566 9   TYR   B CG  
4006 C  CD1 . TYR   B 9   ? 0.3225 0.1905 0.2661 -0.0958 0.0598  -0.0528 9   TYR   B CD1 
4007 C  CD2 . TYR   B 9   ? 0.3105 0.1874 0.2354 -0.0797 0.0513  -0.0546 9   TYR   B CD2 
4008 C  CE1 . TYR   B 9   ? 0.3145 0.1993 0.2646 -0.0944 0.0650  -0.0694 9   TYR   B CE1 
4009 C  CE2 . TYR   B 9   ? 0.3103 0.1875 0.2524 -0.0746 0.0552  -0.0522 9   TYR   B CE2 
4010 C  CZ  . TYR   B 9   ? 0.3100 0.1996 0.2612 -0.0824 0.0600  -0.0740 9   TYR   B CZ  
4011 O  OH  . TYR   B 9   ? 0.3024 0.2069 0.2667 -0.0906 0.0658  -0.0845 9   TYR   B OH  
4021 N  N   . LEU   B 10  ? 0.3265 0.1980 0.2233 -0.0772 0.0197  -0.0444 10  LEU   B N   
4022 C  CA  . LEU   B 10  ? 0.3236 0.1965 0.2243 -0.0879 -0.0178 -0.0360 10  LEU   B CA  
4023 C  C   . LEU   B 10  ? 0.3013 0.1964 0.2265 -0.0873 -0.0366 -0.0319 10  LEU   B C   
4024 O  O   . LEU   B 10  ? 0.2824 0.1981 0.2251 -0.0731 -0.0357 -0.0168 10  LEU   B O   
4025 C  CB  . LEU   B 10  ? 0.3416 0.1928 0.2430 -0.0914 -0.0368 -0.0229 10  LEU   B CB  
4026 C  CG  . LEU   B 10  ? 0.3582 0.2032 0.2725 -0.0831 -0.0612 -0.0150 10  LEU   B CG  
4027 C  CD1 . LEU   B 10  ? 0.3693 0.2165 0.2932 -0.0751 -0.0534 -0.0095 10  LEU   B CD1 
4028 C  CD2 . LEU   B 10  ? 0.3659 0.2089 0.2950 -0.0805 -0.0530 0.0076  10  LEU   B CD2 
4040 N  N   . LYS   B 11  ? 0.3131 0.2247 0.2348 -0.0805 -0.0413 -0.0290 11  LYS   B N   
4041 C  CA  . LYS   B 11  ? 0.3238 0.2525 0.2698 -0.0661 -0.0450 -0.0283 11  LYS   B CA  
4042 C  C   . LYS   B 11  ? 0.2978 0.2317 0.2725 -0.0815 -0.0556 -0.0372 11  LYS   B C   
4043 O  O   . LYS   B 11  ? 0.3117 0.2512 0.2956 -0.0985 -0.0586 -0.0647 11  LYS   B O   
4044 C  CB  . LYS   B 11  ? 0.3576 0.3012 0.3341 -0.0421 -0.0403 -0.0213 11  LYS   B CB  
4045 C  CG  . LYS   B 11  ? 0.3875 0.3320 0.4045 -0.0277 -0.0453 -0.0246 11  LYS   B CG  
4046 C  CD  . LYS   B 11  ? 0.4088 0.3540 0.4605 -0.0170 -0.0457 -0.0289 11  LYS   B CD  
4047 C  CE  . LYS   B 11  ? 0.4228 0.3704 0.5014 -0.0103 -0.0405 -0.0287 11  LYS   B CE  
4048 N  NZ  . LYS   B 11  ? 0.4314 0.3815 0.5257 -0.0056 -0.0363 -0.0235 11  LYS   B NZ  
4062 N  N   . LEU   B 12  ? 0.2601 0.2019 0.2697 -0.0664 -0.0531 -0.0324 12  LEU   B N   
4063 C  CA  . LEU   B 12  ? 0.2424 0.1802 0.2755 -0.0571 -0.0454 -0.0277 12  LEU   B CA  
4064 C  C   . LEU   B 12  ? 0.2301 0.1802 0.2828 -0.0613 -0.0615 -0.0193 12  LEU   B C   
4065 O  O   . LEU   B 12  ? 0.2274 0.1824 0.2927 -0.0669 -0.0802 -0.0135 12  LEU   B O   
4066 C  CB  . LEU   B 12  ? 0.2399 0.1567 0.2723 -0.0448 -0.0411 -0.0312 12  LEU   B CB  
4067 C  CG  . LEU   B 12  ? 0.2414 0.1537 0.2792 -0.0443 -0.0307 -0.0201 12  LEU   B CG  
4068 C  CD1 . LEU   B 12  ? 0.2530 0.1546 0.2851 -0.0318 -0.0250 0.0022  12  LEU   B CD1 
4069 C  CD2 . LEU   B 12  ? 0.2506 0.1639 0.2850 -0.0386 -0.0216 -0.0238 12  LEU   B CD2 
4081 N  N   . THR   B 13  ? 0.2238 0.1839 0.2847 -0.0606 -0.0560 -0.0352 13  THR   B N   
4082 C  CA  . THR   B 13  ? 0.2216 0.1915 0.2852 -0.0638 -0.0655 -0.0203 13  THR   B CA  
4083 C  C   . THR   B 13  ? 0.2648 0.2098 0.2971 -0.0720 -0.0905 -0.0097 13  THR   B C   
4084 O  O   . THR   B 13  ? 0.2853 0.2097 0.3177 -0.0738 -0.0618 -0.0041 13  THR   B O   
4085 C  CB  . THR   B 13  ? 0.1995 0.1931 0.2886 -0.0508 -0.0624 -0.0101 13  THR   B CB  
4086 O  OG1 . THR   B 13  ? 0.1828 0.1844 0.2940 -0.0431 -0.0537 -0.0120 13  THR   B OG1 
4087 C  CG2 . THR   B 13  ? 0.2080 0.2011 0.2873 -0.0493 -0.0577 0.0023  13  THR   B CG2 
4095 N  N   A ASP   B 14  ? 0.2762 0.2230 0.3083 -0.0756 -0.1208 0.0006  14  ASP   B N   
4096 N  N   B ASP   B 14  ? 0.2745 0.2216 0.3029 -0.0704 -0.0975 0.0003  14  ASP   B N   
4097 C  CA  A ASP   B 14  ? 0.2861 0.2406 0.3306 -0.0731 -0.1191 0.0172  14  ASP   B CA  
4098 C  CA  B ASP   B 14  ? 0.2795 0.2320 0.3153 -0.0666 -0.0918 0.0128  14  ASP   B CA  
4099 C  C   A ASP   B 14  ? 0.2727 0.2249 0.2945 -0.0768 -0.1027 0.0202  14  ASP   B C   
4100 C  C   B ASP   B 14  ? 0.2634 0.2139 0.2840 -0.0681 -0.0924 0.0142  14  ASP   B C   
4101 O  O   A ASP   B 14  ? 0.2957 0.2413 0.3018 -0.0728 -0.0914 0.0338  14  ASP   B O   
4102 O  O   B ASP   B 14  ? 0.2755 0.2121 0.2814 -0.0626 -0.0867 0.0153  14  ASP   B O   
4103 C  CB  A ASP   B 14  ? 0.3041 0.2742 0.4006 -0.0684 -0.1230 0.0191  14  ASP   B CB  
4104 C  CB  B ASP   B 14  ? 0.2961 0.2576 0.3681 -0.0597 -0.0804 0.0173  14  ASP   B CB  
4105 C  CG  A ASP   B 14  ? 0.3241 0.3021 0.4680 -0.0646 -0.1181 0.0081  14  ASP   B CG  
4106 C  CG  B ASP   B 14  ? 0.3115 0.2781 0.4146 -0.0530 -0.0695 0.0128  14  ASP   B CG  
4107 O  OD1 A ASP   B 14  ? 0.3352 0.3098 0.4891 -0.0736 -0.1161 -0.0039 14  ASP   B OD1 
4108 O  OD1 B ASP   B 14  ? 0.3158 0.2866 0.4319 -0.0507 -0.0621 0.0101  14  ASP   B OD1 
4109 O  OD2 A ASP   B 14  ? 0.3274 0.3170 0.5017 -0.0609 -0.1158 0.0099  14  ASP   B OD2 
4110 O  OD2 B ASP   B 14  ? 0.3163 0.2838 0.4363 -0.0568 -0.0703 0.0112  14  ASP   B OD2 
4119 N  N   . ASN   B 15  ? 0.2358 0.1970 0.2703 -0.0656 -0.1002 0.0134  15  ASN   B N   
4120 C  CA  . ASN   B 15  ? 0.1911 0.1715 0.2629 -0.0437 -0.0761 0.0106  15  ASN   B CA  
4121 C  C   . ASN   B 15  ? 0.1747 0.1564 0.2439 -0.0276 -0.0575 0.0022  15  ASN   B C   
4122 O  O   . ASN   B 15  ? 0.1713 0.1513 0.2569 -0.0295 -0.0592 -0.0083 15  ASN   B O   
4123 C  CB  . ASN   B 15  ? 0.1805 0.1638 0.2747 -0.0262 -0.0687 0.0141  15  ASN   B CB  
4124 C  CG  . ASN   B 15  ? 0.1629 0.1591 0.2819 -0.0310 -0.0448 0.0123  15  ASN   B CG  
4125 O  OD1 . ASN   B 15  ? 0.1719 0.1891 0.3012 -0.0483 -0.0433 0.0267  15  ASN   B OD1 
4126 N  ND2 . ASN   B 15  ? 0.1580 0.1350 0.2574 -0.0203 -0.0138 -0.0084 15  ASN   B ND2 
4134 N  N   . VAL   B 16  ? 0.1816 0.1427 0.2367 -0.0349 -0.0620 0.0035  16  VAL   B N   
4135 C  CA  . VAL   B 16  ? 0.1870 0.1434 0.2244 -0.0315 -0.0509 -0.0198 16  VAL   B CA  
4136 C  C   . VAL   B 16  ? 0.1814 0.1582 0.2247 -0.0388 -0.0491 -0.0120 16  VAL   B C   
4137 O  O   . VAL   B 16  ? 0.1799 0.1667 0.2456 -0.0379 -0.0456 -0.0244 16  VAL   B O   
4138 C  CB  . VAL   B 16  ? 0.1883 0.1407 0.2431 -0.0208 -0.0376 -0.0163 16  VAL   B CB  
4139 C  CG1 . VAL   B 16  ? 0.1937 0.1348 0.2273 -0.0034 -0.0288 -0.0068 16  VAL   B CG1 
4140 C  CG2 . VAL   B 16  ? 0.1867 0.1441 0.2603 -0.0162 -0.0303 -0.0135 16  VAL   B CG2 
4150 N  N   . TYR   B 17  ? 0.1865 0.1686 0.2216 -0.0371 -0.0464 -0.0168 17  TYR   B N   
4151 C  CA  . TYR   B 17  ? 0.1943 0.1859 0.2088 -0.0464 -0.0383 0.0036  17  TYR   B CA  
4152 C  C   . TYR   B 17  ? 0.1835 0.1538 0.2075 -0.0469 -0.0257 -0.0086 17  TYR   B C   
4153 O  O   . TYR   B 17  ? 0.1757 0.1609 0.2214 -0.0380 -0.0306 -0.0358 17  TYR   B O   
4154 C  CB  . TYR   B 17  ? 0.2260 0.2291 0.2314 -0.0321 -0.0429 0.0341  17  TYR   B CB  
4155 C  CG  . TYR   B 17  ? 0.2563 0.2776 0.2766 -0.0267 -0.0561 0.0356  17  TYR   B CG  
4156 C  CD1 . TYR   B 17  ? 0.2770 0.2952 0.2952 -0.0240 -0.0636 0.0421  17  TYR   B CD1 
4157 C  CD2 . TYR   B 17  ? 0.2749 0.3064 0.2999 -0.0160 -0.0614 0.0349  17  TYR   B CD2 
4158 C  CE1 . TYR   B 17  ? 0.2953 0.3208 0.3171 -0.0144 -0.0724 0.0390  17  TYR   B CE1 
4159 C  CE2 . TYR   B 17  ? 0.2903 0.3277 0.3196 -0.0039 -0.0797 0.0416  17  TYR   B CE2 
4160 C  CZ  . TYR   B 17  ? 0.3048 0.3326 0.3281 -0.0038 -0.0839 0.0395  17  TYR   B CZ  
4161 O  OH  . TYR   B 17  ? 0.3194 0.3456 0.3497 0.0055  -0.0913 0.0363  17  TYR   B OH  
4171 N  N   . ILE   B 18  ? 0.1933 0.1532 0.1998 -0.0374 -0.0142 -0.0205 18  ILE   B N   
4172 C  CA  . ILE   B 18  ? 0.2040 0.1489 0.1978 -0.0389 -0.0053 -0.0306 18  ILE   B CA  
4173 C  C   . ILE   B 18  ? 0.2174 0.1544 0.1915 -0.0535 -0.0017 -0.0364 18  ILE   B C   
4174 O  O   . ILE   B 18  ? 0.2411 0.1723 0.2107 -0.0464 0.0020  -0.0496 18  ILE   B O   
4175 C  CB  . ILE   B 18  ? 0.2062 0.1502 0.2173 -0.0479 -0.0174 -0.0200 18  ILE   B CB  
4176 C  CG1 . ILE   B 18  ? 0.2049 0.1570 0.2273 -0.0521 -0.0106 -0.0127 18  ILE   B CG1 
4177 C  CG2 . ILE   B 18  ? 0.2109 0.1572 0.2254 -0.0462 -0.0229 -0.0116 18  ILE   B CG2 
4178 C  CD1 . ILE   B 18  ? 0.2120 0.1880 0.2389 -0.0483 -0.0230 0.0082  18  ILE   B CD1 
4190 N  N   . LYS   B 19  ? 0.2172 0.1569 0.2133 -0.0355 0.0363  -0.0361 19  LYS   B N   
4191 C  CA  . LYS   B 19  ? 0.2238 0.1578 0.2360 -0.0337 0.0363  -0.0456 19  LYS   B CA  
4192 C  C   . LYS   B 19  ? 0.2026 0.1516 0.2573 -0.0309 0.0406  -0.0531 19  LYS   B C   
4193 O  O   . LYS   B 19  ? 0.1893 0.1597 0.2360 -0.0231 0.0269  -0.0515 19  LYS   B O   
4194 C  CB  . LYS   B 19  ? 0.2511 0.1803 0.2454 -0.0393 0.0433  -0.0381 19  LYS   B CB  
4195 C  CG  . LYS   B 19  ? 0.2771 0.2009 0.2649 -0.0484 0.0426  -0.0377 19  LYS   B CG  
4196 C  CD  . LYS   B 19  ? 0.3054 0.2319 0.2817 -0.0546 0.0494  -0.0339 19  LYS   B CD  
4197 C  CE  . LYS   B 19  ? 0.3320 0.2611 0.2904 -0.0551 0.0433  -0.0316 19  LYS   B CE  
4198 N  NZ  . LYS   B 19  ? 0.3498 0.2783 0.2965 -0.0612 0.0473  -0.0231 19  LYS   B NZ  
4212 N  N   . ASN   B 20  ? 0.1961 0.1718 0.2913 -0.0261 0.0409  -0.0666 20  ASN   B N   
4213 C  CA  . ASN   B 20  ? 0.1925 0.1843 0.3192 -0.0213 0.0465  -0.0860 20  ASN   B CA  
4214 C  C   . ASN   B 20  ? 0.1957 0.2018 0.3150 -0.0252 0.0556  -0.0981 20  ASN   B C   
4215 O  O   . ASN   B 20  ? 0.2163 0.2426 0.3303 -0.0458 0.0545  -0.0968 20  ASN   B O   
4216 C  CB  . ASN   B 20  ? 0.2204 0.1878 0.3496 0.0007  0.0354  -0.0861 20  ASN   B CB  
4217 C  CG  . ASN   B 20  ? 0.2517 0.1973 0.3693 0.0306  0.0354  -0.0950 20  ASN   B CG  
4218 O  OD1 . ASN   B 20  ? 0.2863 0.2259 0.3969 0.0457  0.0346  -0.0901 20  ASN   B OD1 
4219 N  ND2 . ASN   B 20  ? 0.2394 0.1994 0.3663 0.0308  0.0248  -0.0902 20  ASN   B ND2 
4226 N  N   . ALA   B 21  ? 0.1989 0.1811 0.3136 -0.0327 0.0557  -0.0784 21  ALA   B N   
4227 C  CA  . ALA   B 21  ? 0.2117 0.1905 0.3219 -0.0339 0.0474  -0.0575 21  ALA   B CA  
4228 C  C   . ALA   B 21  ? 0.2117 0.1627 0.3009 -0.0240 0.0518  -0.0467 21  ALA   B C   
4229 O  O   . ALA   B 21  ? 0.2150 0.1570 0.3002 -0.0330 0.0435  -0.0400 21  ALA   B O   
4230 C  CB  . ALA   B 21  ? 0.2249 0.2200 0.3295 -0.0494 0.0448  -0.0384 21  ALA   B CB  
4236 N  N   . ASP   B 22  ? 0.2056 0.1522 0.2919 -0.0220 0.0442  -0.0384 22  ASP   B N   
4237 C  CA  . ASP   B 22  ? 0.1983 0.1460 0.2768 -0.0095 0.0334  -0.0275 22  ASP   B CA  
4238 C  C   . ASP   B 22  ? 0.1844 0.1437 0.2328 -0.0186 0.0227  -0.0139 22  ASP   B C   
4239 O  O   . ASP   B 22  ? 0.1863 0.1516 0.2406 -0.0167 0.0191  -0.0112 22  ASP   B O   
4240 C  CB  . ASP   B 22  ? 0.2035 0.1488 0.3112 -0.0077 0.0289  -0.0071 22  ASP   B CB  
4241 C  CG  . ASP   B 22  ? 0.2042 0.1757 0.3515 -0.0040 0.0056  -0.0075 22  ASP   B CG  
4242 O  OD1 . ASP   B 22  ? 0.2134 0.1684 0.3476 -0.0057 -0.0222 -0.0055 22  ASP   B OD1 
4243 O  OD2 . ASP   B 22  ? 0.2090 0.2090 0.4020 0.0097  -0.0156 -0.0211 22  ASP   B OD2 
4248 N  N   . ILE   B 23  ? 0.1825 0.1420 0.2082 -0.0150 0.0053  0.0097  23  ILE   B N   
4249 C  CA  . ILE   B 23  ? 0.1721 0.1410 0.1911 -0.0146 -0.0082 0.0027  23  ILE   B CA  
4250 C  C   . ILE   B 23  ? 0.1627 0.1433 0.1888 -0.0120 -0.0147 0.0012  23  ILE   B C   
4251 O  O   . ILE   B 23  ? 0.1590 0.1427 0.1798 -0.0120 -0.0086 0.0142  23  ILE   B O   
4252 C  CB  . ILE   B 23  ? 0.1656 0.1467 0.2073 -0.0199 -0.0068 0.0130  23  ILE   B CB  
4253 C  CG1 . ILE   B 23  ? 0.1706 0.1557 0.2273 -0.0112 0.0050  0.0242  23  ILE   B CG1 
4254 C  CG2 . ILE   B 23  ? 0.1732 0.1718 0.2148 -0.0188 -0.0026 0.0123  23  ILE   B CG2 
4255 C  CD1 . ILE   B 23  ? 0.1731 0.1672 0.2281 -0.0060 0.0045  0.0236  23  ILE   B CD1 
4267 N  N   . VAL   B 24  ? 0.1637 0.1411 0.1999 -0.0154 -0.0099 0.0015  24  VAL   B N   
4268 C  CA  . VAL   B 24  ? 0.1622 0.1470 0.2157 -0.0064 -0.0207 -0.0015 24  VAL   B CA  
4269 C  C   . VAL   B 24  ? 0.1569 0.1493 0.2267 -0.0115 -0.0119 0.0095  24  VAL   B C   
4270 O  O   . VAL   B 24  ? 0.1536 0.1602 0.2392 -0.0178 -0.0093 0.0084  24  VAL   B O   
4271 C  CB  . VAL   B 24  ? 0.1708 0.1671 0.2170 0.0019  -0.0253 -0.0031 24  VAL   B CB  
4272 C  CG1 . VAL   B 24  ? 0.1712 0.1705 0.2419 -0.0134 -0.0255 0.0012  24  VAL   B CG1 
4273 C  CG2 . VAL   B 24  ? 0.1797 0.1969 0.2182 0.0054  -0.0264 -0.0191 24  VAL   B CG2 
4283 N  N   . GLU   B 25  ? 0.1797 0.1633 0.2324 -0.0120 0.0031  0.0142  25  GLU   B N   
4284 C  CA  . GLU   B 25  ? 0.1955 0.1906 0.2532 -0.0074 0.0184  0.0005  25  GLU   B CA  
4285 C  C   . GLU   B 25  ? 0.1825 0.1816 0.2182 -0.0180 0.0178  0.0018  25  GLU   B C   
4286 O  O   . GLU   B 25  ? 0.1867 0.1953 0.2353 -0.0150 0.0166  0.0031  25  GLU   B O   
4287 C  CB  . GLU   B 25  ? 0.2351 0.2395 0.3272 0.0145  0.0215  -0.0076 25  GLU   B CB  
4288 C  CG  . GLU   B 25  ? 0.2736 0.2976 0.4271 0.0269  0.0108  -0.0126 25  GLU   B CG  
4289 C  CD  . GLU   B 25  ? 0.3231 0.3475 0.5036 0.0232  0.0077  -0.0122 25  GLU   B CD  
4290 O  OE1 . GLU   B 25  ? 0.3359 0.3597 0.5359 0.0296  0.0156  -0.0103 25  GLU   B OE1 
4291 O  OE2 . GLU   B 25  ? 0.3275 0.3627 0.5363 0.0216  0.0060  -0.0157 25  GLU   B OE2 
4298 N  N   . GLU   B 26  ? 0.1798 0.1759 0.1924 -0.0319 0.0049  -0.0010 26  GLU   B N   
4299 C  CA  . GLU   B 26  ? 0.1851 0.1886 0.2004 -0.0376 -0.0127 0.0058  26  GLU   B CA  
4300 C  C   . GLU   B 26  ? 0.1716 0.1847 0.1849 -0.0248 0.0067  0.0227  26  GLU   B C   
4301 O  O   . GLU   B 26  ? 0.1868 0.2044 0.1927 -0.0250 0.0034  0.0272  26  GLU   B O   
4302 C  CB  . GLU   B 26  ? 0.2168 0.2042 0.2191 -0.0527 -0.0045 0.0236  26  GLU   B CB  
4303 C  CG  . GLU   B 26  ? 0.2603 0.2457 0.2738 -0.0587 0.0110  -0.0022 26  GLU   B CG  
4304 C  CD  . GLU   B 26  ? 0.2885 0.2731 0.2897 -0.0795 0.0247  -0.0393 26  GLU   B CD  
4305 O  OE1 . GLU   B 26  ? 0.3143 0.2670 0.2907 -0.0923 0.0670  -0.0382 26  GLU   B OE1 
4306 O  OE2 . GLU   B 26  ? 0.2893 0.3140 0.3315 -0.0725 0.0207  -0.0346 26  GLU   B OE2 
4313 N  N   . ALA   B 27  ? 0.1533 0.1655 0.1871 -0.0225 0.0058  0.0224  27  ALA   B N   
4314 C  CA  . ALA   B 27  ? 0.1553 0.1676 0.2031 -0.0157 -0.0001 0.0314  27  ALA   B CA  
4315 C  C   . ALA   B 27  ? 0.1581 0.1789 0.2259 -0.0194 0.0048  0.0430  27  ALA   B C   
4316 O  O   . ALA   B 27  ? 0.1667 0.1837 0.2406 -0.0099 0.0070  0.0486  27  ALA   B O   
4317 C  CB  . ALA   B 27  ? 0.1675 0.1447 0.2052 -0.0207 0.0026  0.0282  27  ALA   B CB  
4323 N  N   . LYS   B 28  ? 0.1512 0.1963 0.2632 -0.0218 0.0151  0.0584  28  LYS   B N   
4324 C  CA  . LYS   B 28  ? 0.1674 0.2341 0.2889 -0.0123 0.0462  0.0873  28  LYS   B CA  
4325 C  C   . LYS   B 28  ? 0.1935 0.2486 0.2783 -0.0084 0.0592  0.0740  28  LYS   B C   
4326 O  O   . LYS   B 28  ? 0.2223 0.2525 0.2898 -0.0104 0.0650  0.0757  28  LYS   B O   
4327 C  CB  . LYS   B 28  ? 0.1880 0.2686 0.3300 -0.0035 0.0695  0.0995  28  LYS   B CB  
4328 C  CG  . LYS   B 28  ? 0.2282 0.3257 0.3788 0.0030  0.0672  0.1122  28  LYS   B CG  
4329 C  CD  . LYS   B 28  ? 0.2696 0.3808 0.4313 0.0052  0.0820  0.1176  28  LYS   B CD  
4330 C  CE  . LYS   B 28  ? 0.2987 0.4141 0.4694 0.0127  0.0828  0.1191  28  LYS   B CE  
4331 N  NZ  . LYS   B 28  ? 0.3530 0.4497 0.4949 0.0215  0.0857  0.1245  28  LYS   B NZ  
4345 N  N   . LYS   B 29  ? 0.2105 0.2744 0.2797 0.0110  0.0579  0.0620  29  LYS   B N   
4346 C  CA  . LYS   B 29  ? 0.2577 0.3103 0.3074 0.0117  0.0543  0.0624  29  LYS   B CA  
4347 C  C   . LYS   B 29  ? 0.2498 0.3094 0.2720 0.0101  0.0394  0.0733  29  LYS   B C   
4348 O  O   . LYS   B 29  ? 0.2667 0.3312 0.2854 0.0166  0.0381  0.0851  29  LYS   B O   
4349 C  CB  . LYS   B 29  ? 0.3185 0.3471 0.3895 0.0118  0.0585  0.0526  29  LYS   B CB  
4350 C  CG  . LYS   B 29  ? 0.3700 0.3811 0.4718 0.0099  0.0642  0.0488  29  LYS   B CG  
4351 C  CD  . LYS   B 29  ? 0.4144 0.4137 0.5426 0.0080  0.0729  0.0393  29  LYS   B CD  
4352 C  CE  . LYS   B 29  ? 0.4351 0.4269 0.5932 0.0050  0.0813  0.0347  29  LYS   B CE  
4353 N  NZ  . LYS   B 29  ? 0.4602 0.4273 0.6158 0.0036  0.0861  0.0326  29  LYS   B NZ  
4367 N  N   . VAL   B 30  ? 0.2187 0.2845 0.2551 -0.0054 0.0266  0.0670  30  VAL   B N   
4368 C  CA  . VAL   B 30  ? 0.2063 0.2709 0.2791 -0.0169 -0.0065 0.0719  30  VAL   B CA  
4369 C  C   . VAL   B 30  ? 0.1866 0.2587 0.2640 -0.0178 -0.0054 0.0870  30  VAL   B C   
4370 O  O   . VAL   B 30  ? 0.2029 0.2747 0.2643 -0.0102 -0.0016 0.1009  30  VAL   B O   
4371 C  CB  . VAL   B 30  ? 0.2122 0.2694 0.3164 -0.0284 -0.0311 0.0764  30  VAL   B CB  
4372 C  CG1 . VAL   B 30  ? 0.2213 0.2810 0.3221 -0.0258 -0.0274 0.0688  30  VAL   B CG1 
4373 C  CG2 . VAL   B 30  ? 0.2222 0.2658 0.3366 -0.0384 -0.0386 0.0653  30  VAL   B CG2 
4383 N  N   A LYS   B 31  ? 0.1733 0.2300 0.2881 -0.0342 -0.0046 0.0978  31  LYS   B N   
4384 N  N   B LYS   B 31  ? 0.1880 0.2401 0.2735 -0.0247 -0.0143 0.0803  31  LYS   B N   
4385 C  CA  A LYS   B 31  ? 0.1572 0.2268 0.3100 -0.0442 -0.0069 0.0979  31  LYS   B CA  
4386 C  CA  B LYS   B 31  ? 0.1885 0.2325 0.2834 -0.0294 -0.0244 0.0698  31  LYS   B CA  
4387 C  C   A LYS   B 31  ? 0.1551 0.1897 0.2785 -0.0402 -0.0270 0.0862  31  LYS   B C   
4388 C  C   B LYS   B 31  ? 0.1777 0.1941 0.2549 -0.0336 -0.0419 0.0617  31  LYS   B C   
4389 O  O   A LYS   B 31  ? 0.1571 0.2008 0.2985 -0.0321 -0.0131 0.1022  31  LYS   B O   
4390 O  O   B LYS   B 31  ? 0.1808 0.1985 0.2556 -0.0313 -0.0447 0.0632  31  LYS   B O   
4391 C  CB  A LYS   B 31  ? 0.1683 0.2716 0.3607 -0.0395 0.0236  0.1093  31  LYS   B CB  
4392 C  CB  B LYS   B 31  ? 0.2073 0.2643 0.3243 -0.0224 -0.0123 0.0668  31  LYS   B CB  
4393 C  CG  A LYS   B 31  ? 0.1914 0.3157 0.4074 -0.0362 0.0349  0.1022  31  LYS   B CG  
4394 C  CG  B LYS   B 31  ? 0.2262 0.2880 0.3623 -0.0204 -0.0062 0.0542  31  LYS   B CG  
4395 C  CD  A LYS   B 31  ? 0.2232 0.3540 0.4483 -0.0296 0.0265  0.0893  31  LYS   B CD  
4396 C  CD  B LYS   B 31  ? 0.2448 0.3111 0.3965 -0.0197 -0.0072 0.0436  31  LYS   B CD  
4397 C  CE  A LYS   B 31  ? 0.2389 0.3733 0.4814 -0.0256 0.0167  0.0789  31  LYS   B CE  
4398 C  CE  B LYS   B 31  ? 0.2584 0.3262 0.4245 -0.0190 -0.0082 0.0367  31  LYS   B CE  
4399 N  NZ  A LYS   B 31  ? 0.2493 0.3785 0.4986 -0.0168 0.0068  0.0666  31  LYS   B NZ  
4400 N  NZ  B LYS   B 31  ? 0.2687 0.3353 0.4387 -0.0150 -0.0130 0.0292  31  LYS   B NZ  
4427 N  N   . PRO   B 32  ? 0.1717 0.1618 0.2307 -0.0382 -0.0502 0.0538  32  PRO   B N   
4428 C  CA  . PRO   B 32  ? 0.1847 0.1518 0.1976 -0.0391 -0.0468 0.0328  32  PRO   B CA  
4429 C  C   . PRO   B 32  ? 0.1944 0.1396 0.1945 -0.0409 -0.0607 0.0367  32  PRO   B C   
4430 O  O   . PRO   B 32  ? 0.2032 0.1426 0.2327 -0.0458 -0.0814 0.0357  32  PRO   B O   
4431 C  CB  . PRO   B 32  ? 0.1976 0.1490 0.1836 -0.0445 -0.0431 0.0151  32  PRO   B CB  
4432 C  CG  . PRO   B 32  ? 0.2138 0.1384 0.1952 -0.0332 -0.0575 0.0188  32  PRO   B CG  
4433 C  CD  . PRO   B 32  ? 0.2013 0.1437 0.2148 -0.0283 -0.0668 0.0263  32  PRO   B CD  
4441 N  N   . THR   B 33  ? 0.1985 0.1333 0.1812 -0.0349 -0.0592 0.0261  33  THR   B N   
4442 C  CA  . THR   B 33  ? 0.2028 0.1384 0.1752 -0.0381 -0.0530 0.0287  33  THR   B CA  
4443 C  C   . THR   B 33  ? 0.2061 0.1299 0.1697 -0.0393 -0.0524 0.0242  33  THR   B C   
4444 O  O   . THR   B 33  ? 0.2327 0.1309 0.1883 -0.0466 -0.0609 0.0180  33  THR   B O   
4445 C  CB  . THR   B 33  ? 0.2105 0.1492 0.1872 -0.0206 -0.0568 0.0311  33  THR   B CB  
4446 O  OG1 . THR   B 33  ? 0.1891 0.1576 0.1876 -0.0210 -0.0469 0.0359  33  THR   B OG1 
4447 C  CG2 . THR   B 33  ? 0.2340 0.1542 0.2004 -0.0156 -0.0610 0.0295  33  THR   B CG2 
4455 N  N   . VAL   B 34  ? 0.1838 0.1265 0.1604 -0.0381 -0.0459 0.0217  34  VAL   B N   
4456 C  CA  . VAL   B 34  ? 0.1694 0.1298 0.1584 -0.0316 -0.0388 0.0099  34  VAL   B CA  
4457 C  C   . VAL   B 34  ? 0.1522 0.1262 0.1468 -0.0329 -0.0240 0.0126  34  VAL   B C   
4458 O  O   . VAL   B 34  ? 0.1721 0.1288 0.1521 -0.0289 -0.0408 0.0089  34  VAL   B O   
4459 C  CB  . VAL   B 34  ? 0.1764 0.1352 0.1915 -0.0144 -0.0374 0.0099  34  VAL   B CB  
4460 C  CG1 . VAL   B 34  ? 0.1697 0.1531 0.2002 -0.0127 -0.0289 0.0047  34  VAL   B CG1 
4461 C  CG2 . VAL   B 34  ? 0.1830 0.1383 0.2263 -0.0092 -0.0330 0.0117  34  VAL   B CG2 
4471 N  N   . VAL   B 35  ? 0.1434 0.1218 0.1348 -0.0286 -0.0171 0.0110  35  VAL   B N   
4472 C  CA  . VAL   B 35  ? 0.1425 0.1204 0.1313 -0.0252 -0.0130 0.0124  35  VAL   B CA  
4473 C  C   . VAL   B 35  ? 0.1354 0.1155 0.1328 -0.0179 -0.0177 0.0105  35  VAL   B C   
4474 O  O   . VAL   B 35  ? 0.1363 0.1198 0.1399 -0.0265 -0.0047 -0.0072 35  VAL   B O   
4475 C  CB  . VAL   B 35  ? 0.1420 0.1401 0.1505 -0.0202 -0.0048 0.0075  35  VAL   B CB  
4476 C  CG1 . VAL   B 35  ? 0.1320 0.1491 0.1637 -0.0268 -0.0031 0.0014  35  VAL   B CG1 
4477 C  CG2 . VAL   B 35  ? 0.1483 0.1357 0.1752 -0.0106 -0.0051 0.0074  35  VAL   B CG2 
4487 N  N   . VAL   B 36  ? 0.1329 0.1138 0.1318 -0.0207 -0.0136 0.0149  36  VAL   B N   
4488 C  CA  . VAL   B 36  ? 0.1269 0.1089 0.1350 -0.0177 -0.0111 0.0082  36  VAL   B CA  
4489 C  C   . VAL   B 36  ? 0.1227 0.1107 0.1377 -0.0204 -0.0092 0.0086  36  VAL   B C   
4490 O  O   . VAL   B 36  ? 0.1299 0.1243 0.1475 -0.0112 -0.0047 -0.0055 36  VAL   B O   
4491 C  CB  . VAL   B 36  ? 0.1287 0.1189 0.1492 -0.0171 -0.0072 0.0056  36  VAL   B CB  
4492 C  CG1 . VAL   B 36  ? 0.1252 0.1345 0.1647 -0.0225 -0.0040 0.0055  36  VAL   B CG1 
4493 C  CG2 . VAL   B 36  ? 0.1369 0.1252 0.1551 -0.0144 -0.0146 0.0133  36  VAL   B CG2 
4503 N  N   . ASN   B 37  ? 0.1273 0.1174 0.1453 -0.0074 -0.0102 0.0072  37  ASN   B N   
4504 C  CA  . ASN   B 37  ? 0.1262 0.1228 0.1527 -0.0032 -0.0161 0.0054  37  ASN   B CA  
4505 C  C   . ASN   B 37  ? 0.1257 0.1230 0.1470 0.0001  -0.0130 0.0053  37  ASN   B C   
4506 O  O   . ASN   B 37  ? 0.1351 0.1324 0.1470 -0.0021 -0.0037 0.0067  37  ASN   B O   
4507 C  CB  . ASN   B 37  ? 0.1277 0.1271 0.1463 -0.0101 -0.0154 0.0043  37  ASN   B CB  
4508 C  CG  . ASN   B 37  ? 0.1369 0.1288 0.1503 -0.0051 -0.0153 0.0062  37  ASN   B CG  
4509 O  OD1 . ASN   B 37  ? 0.1408 0.1319 0.1642 0.0058  -0.0183 0.0025  37  ASN   B OD1 
4510 N  ND2 . ASN   B 37  ? 0.1386 0.1212 0.1500 -0.0028 -0.0198 0.0090  37  ASN   B ND2 
4517 N  N   . ALA   B 38  ? 0.1375 0.1200 0.1461 0.0053  -0.0010 0.0080  38  ALA   B N   
4518 C  CA  . ALA   B 38  ? 0.1476 0.1247 0.1452 -0.0021 0.0030  0.0142  38  ALA   B CA  
4519 C  C   . ALA   B 38  ? 0.1446 0.1223 0.1488 -0.0012 0.0040  0.0124  38  ALA   B C   
4520 O  O   . ALA   B 38  ? 0.1576 0.1304 0.1571 0.0051  -0.0021 0.0125  38  ALA   B O   
4521 C  CB  . ALA   B 38  ? 0.1718 0.1339 0.1655 -0.0083 0.0102  0.0049  38  ALA   B CB  
4527 N  N   . ALA   B 39  ? 0.1455 0.1230 0.1403 0.0068  -0.0074 0.0080  39  ALA   B N   
4528 C  CA  . ALA   B 39  ? 0.1544 0.1317 0.1391 0.0076  -0.0096 0.0110  39  ALA   B CA  
4529 C  C   . ALA   B 39  ? 0.1604 0.1374 0.1251 0.0073  -0.0101 0.0041  39  ALA   B C   
4530 O  O   . ALA   B 39  ? 0.1663 0.1472 0.1510 -0.0002 -0.0077 0.0121  39  ALA   B O   
4531 C  CB  . ALA   B 39  ? 0.1489 0.1363 0.1669 -0.0030 -0.0009 0.0050  39  ALA   B CB  
4537 N  N   . ASN   B 40  ? 0.1602 0.1574 0.1278 -0.0024 -0.0015 -0.0015 40  ASN   B N   
4538 C  CA  . ASN   B 40  ? 0.1684 0.1633 0.1390 -0.0038 -0.0072 -0.0024 40  ASN   B CA  
4539 C  C   . ASN   B 40  ? 0.1723 0.1588 0.1260 0.0050  -0.0071 0.0026  40  ASN   B C   
4540 O  O   . ASN   B 40  ? 0.1725 0.1541 0.1381 0.0092  -0.0103 0.0009  40  ASN   B O   
4541 C  CB  . ASN   B 40  ? 0.1802 0.1588 0.1572 0.0121  -0.0185 0.0110  40  ASN   B CB  
4542 C  CG  . ASN   B 40  ? 0.1867 0.1628 0.1956 0.0045  -0.0305 0.0197  40  ASN   B CG  
4543 O  OD1 . ASN   B 40  ? 0.1820 0.1591 0.2832 0.0064  -0.0405 0.0271  40  ASN   B OD1 
4544 N  ND2 . ASN   B 40  ? 0.1891 0.1638 0.2075 0.0039  -0.0279 0.0231  40  ASN   B ND2 
4551 N  N   . VAL   B 41  ? 0.1836 0.1617 0.1362 0.0143  0.0044  -0.0041 41  VAL   B N   
4552 C  CA  . VAL   B 41  ? 0.1925 0.1762 0.1465 0.0072  0.0028  -0.0057 41  VAL   B CA  
4553 C  C   . VAL   B 41  ? 0.1902 0.1734 0.1430 0.0132  -0.0035 -0.0084 41  VAL   B C   
4554 O  O   . VAL   B 41  ? 0.1863 0.1727 0.1523 0.0086  -0.0129 -0.0155 41  VAL   B O   
4555 C  CB  . VAL   B 41  ? 0.2063 0.1982 0.1730 -0.0055 0.0180  -0.0261 41  VAL   B CB  
4556 C  CG1 . VAL   B 41  ? 0.2035 0.1984 0.1737 -0.0096 0.0286  -0.0298 41  VAL   B CG1 
4557 C  CG2 . VAL   B 41  ? 0.2230 0.2179 0.1810 -0.0136 0.0104  -0.0277 41  VAL   B CG2 
4567 N  N   . TYR   B 42  ? 0.1969 0.1745 0.1389 0.0130  -0.0181 0.0080  42  TYR   B N   
4568 C  CA  . TYR   B 42  ? 0.1989 0.1776 0.1417 0.0163  -0.0279 -0.0048 42  TYR   B CA  
4569 C  C   . TYR   B 42  ? 0.1798 0.1598 0.1605 0.0174  -0.0233 -0.0062 42  TYR   B C   
4570 O  O   . TYR   B 42  ? 0.1833 0.1674 0.1984 0.0114  -0.0298 -0.0128 42  TYR   B O   
4571 C  CB  . TYR   B 42  ? 0.2228 0.2055 0.1703 0.0201  -0.0358 0.0087  42  TYR   B CB  
4572 C  CG  . TYR   B 42  ? 0.2242 0.2221 0.1605 0.0043  -0.0300 0.0218  42  TYR   B CG  
4573 C  CD1 . TYR   B 42  ? 0.2151 0.2221 0.1466 -0.0007 -0.0202 0.0104  42  TYR   B CD1 
4574 C  CD2 . TYR   B 42  ? 0.2398 0.2334 0.1915 0.0073  -0.0153 0.0275  42  TYR   B CD2 
4575 C  CE1 . TYR   B 42  ? 0.2249 0.2388 0.1478 0.0108  -0.0181 0.0074  42  TYR   B CE1 
4576 C  CE2 . TYR   B 42  ? 0.2406 0.2486 0.1927 0.0182  0.0033  0.0380  42  TYR   B CE2 
4577 C  CZ  . TYR   B 42  ? 0.2480 0.2598 0.1775 0.0315  0.0082  0.0177  42  TYR   B CZ  
4578 O  OH  . TYR   B 42  ? 0.2787 0.2891 0.2223 0.0509  0.0155  0.0297  42  TYR   B OH  
4588 N  N   . LEU   B 43  ? 0.1673 0.1444 0.1590 0.0097  -0.0140 -0.0092 43  LEU   B N   
4589 C  CA  . LEU   B 43  ? 0.1670 0.1497 0.1409 0.0048  -0.0148 0.0006  43  LEU   B CA  
4590 C  C   . LEU   B 43  ? 0.1714 0.1512 0.1412 0.0020  -0.0208 -0.0037 43  LEU   B C   
4591 O  O   . LEU   B 43  ? 0.1672 0.1508 0.1705 0.0036  -0.0262 0.0030  43  LEU   B O   
4592 C  CB  . LEU   B 43  ? 0.1652 0.1424 0.1548 0.0025  -0.0276 -0.0045 43  LEU   B CB  
4593 C  CG  . LEU   B 43  ? 0.1706 0.1407 0.1707 -0.0007 -0.0301 -0.0052 43  LEU   B CG  
4594 C  CD1 . LEU   B 43  ? 0.1761 0.1413 0.2050 0.0029  -0.0451 -0.0099 43  LEU   B CD1 
4595 C  CD2 . LEU   B 43  ? 0.1691 0.1432 0.1701 -0.0068 -0.0266 -0.0024 43  LEU   B CD2 
4607 N  N   . LYS   B 44  ? 0.1672 0.1483 0.1547 0.0100  -0.0162 -0.0088 44  LYS   B N   
4608 C  CA  . LYS   B 44  ? 0.1789 0.1599 0.1526 0.0105  -0.0143 0.0048  44  LYS   B CA  
4609 C  C   . LYS   B 44  ? 0.1695 0.1550 0.1472 0.0075  -0.0172 0.0006  44  LYS   B C   
4610 O  O   . LYS   B 44  ? 0.1937 0.1530 0.1752 -0.0002 -0.0145 0.0019  44  LYS   B O   
4611 C  CB  . LYS   B 44  ? 0.2102 0.1810 0.1771 0.0205  -0.0332 -0.0004 44  LYS   B CB  
4612 C  CG  . LYS   B 44  ? 0.2500 0.2082 0.2110 0.0148  -0.0587 0.0134  44  LYS   B CG  
4613 C  CD  . LYS   B 44  ? 0.2875 0.2319 0.2775 -0.0016 -0.0671 0.0138  44  LYS   B CD  
4614 C  CE  . LYS   B 44  ? 0.3179 0.2612 0.3296 -0.0094 -0.0657 0.0202  44  LYS   B CE  
4615 N  NZ  . LYS   B 44  ? 0.3291 0.2689 0.3571 -0.0079 -0.0683 0.0302  44  LYS   B NZ  
4629 N  N   . HIS   B 45  ? 0.1607 0.1585 0.1440 0.0069  -0.0152 0.0102  45  HIS   B N   
4630 C  CA  . HIS   B 45  ? 0.1665 0.1501 0.1528 0.0097  -0.0107 0.0034  45  HIS   B CA  
4631 C  C   . HIS   B 45  ? 0.1895 0.1707 0.1961 0.0189  -0.0260 -0.0043 45  HIS   B C   
4632 O  O   . HIS   B 45  ? 0.1993 0.2047 0.2387 0.0437  -0.0010 -0.0081 45  HIS   B O   
4633 C  CB  . HIS   B 45  ? 0.1552 0.1493 0.1606 0.0024  -0.0147 -0.0070 45  HIS   B CB  
4634 C  CG  . HIS   B 45  ? 0.1601 0.1463 0.1529 -0.0041 -0.0164 -0.0010 45  HIS   B CG  
4635 N  ND1 . HIS   B 45  ? 0.1629 0.1363 0.1608 -0.0019 -0.0236 -0.0096 45  HIS   B ND1 
4636 C  CD2 . HIS   B 45  ? 0.1693 0.1510 0.1747 -0.0110 -0.0197 0.0001  45  HIS   B CD2 
4637 C  CE1 . HIS   B 45  ? 0.1755 0.1318 0.1531 -0.0023 -0.0299 -0.0089 45  HIS   B CE1 
4638 N  NE2 . HIS   B 45  ? 0.1766 0.1381 0.1649 0.0006  -0.0241 -0.0034 45  HIS   B NE2 
4646 N  N   A GLY   B 46  ? 0.2001 0.1646 0.2242 0.0233  -0.0438 0.0028  46  GLY   B N   
4647 N  N   B GLY   B 46  ? 0.1976 0.1764 0.2111 0.0214  -0.0363 0.0069  46  GLY   B N   
4648 C  CA  A GLY   B 46  ? 0.2078 0.1727 0.2664 0.0227  -0.0501 0.0040  46  GLY   B CA  
4649 C  CA  B GLY   B 46  ? 0.2033 0.1858 0.2338 0.0202  -0.0405 0.0136  46  GLY   B CA  
4650 C  C   A GLY   B 46  ? 0.2044 0.1859 0.3027 0.0294  -0.0438 0.0055  46  GLY   B C   
4651 C  C   B GLY   B 46  ? 0.2020 0.1954 0.2595 0.0227  -0.0351 0.0183  46  GLY   B C   
4652 O  O   A GLY   B 46  ? 0.2142 0.1951 0.3801 0.0351  -0.0217 -0.0187 46  GLY   B O   
4653 O  O   B GLY   B 46  ? 0.2042 0.2017 0.2750 0.0282  -0.0315 0.0284  46  GLY   B O   
4660 N  N   . GLY   B 47  ? 0.2015 0.2009 0.2793 0.0099  -0.0199 0.0074  47  GLY   B N   
4661 C  CA  . GLY   B 47  ? 0.1935 0.1744 0.2437 -0.0005 -0.0177 0.0051  47  GLY   B CA  
4662 C  C   . GLY   B 47  ? 0.1726 0.1551 0.2097 -0.0030 -0.0042 0.0110  47  GLY   B C   
4663 O  O   . GLY   B 47  ? 0.1832 0.1421 0.2185 -0.0024 -0.0161 0.0149  47  GLY   B O   
4668 N  N   . GLY   B 48  ? 0.1545 0.1488 0.2127 0.0011  -0.0116 0.0131  48  GLY   B N   
4669 C  CA  . GLY   B 48  ? 0.1501 0.1401 0.2032 -0.0040 -0.0053 0.0093  48  GLY   B CA  
4670 C  C   . GLY   B 48  ? 0.1457 0.1381 0.1857 -0.0006 0.0043  0.0029  48  GLY   B C   
4671 O  O   . GLY   B 48  ? 0.1422 0.1439 0.2147 0.0034  -0.0095 0.0003  48  GLY   B O   
4675 N  N   . VAL   B 49  ? 0.1479 0.1464 0.1771 0.0072  -0.0022 0.0078  49  VAL   B N   
4676 C  CA  . VAL   B 49  ? 0.1502 0.1509 0.1651 0.0115  -0.0170 -0.0052 49  VAL   B CA  
4677 C  C   . VAL   B 49  ? 0.1423 0.1404 0.1515 0.0136  -0.0103 -0.0065 49  VAL   B C   
4678 O  O   . VAL   B 49  ? 0.1488 0.1457 0.1671 0.0015  -0.0077 0.0023  49  VAL   B O   
4679 C  CB  . VAL   B 49  ? 0.1537 0.1688 0.1899 0.0035  -0.0234 0.0008  49  VAL   B CB  
4680 C  CG1 . VAL   B 49  ? 0.1537 0.1754 0.1920 0.0096  -0.0319 0.0003  49  VAL   B CG1 
4681 C  CG2 . VAL   B 49  ? 0.1663 0.1835 0.2116 -0.0090 -0.0343 -0.0029 49  VAL   B CG2 
4691 N  N   . ALA   B 50  ? 0.1384 0.1374 0.1651 0.0069  -0.0134 -0.0004 50  ALA   B N   
4692 C  CA  . ALA   B 50  ? 0.1374 0.1315 0.1599 0.0095  -0.0099 0.0039  50  ALA   B CA  
4693 C  C   . ALA   B 50  ? 0.1479 0.1325 0.1623 0.0014  -0.0139 -0.0001 50  ALA   B C   
4694 O  O   . ALA   B 50  ? 0.1490 0.1320 0.1542 0.0035  -0.0048 -0.0017 50  ALA   B O   
4695 C  CB  . ALA   B 50  ? 0.1432 0.1332 0.1636 0.0031  -0.0046 0.0116  50  ALA   B CB  
4701 N  N   . GLY   B 51  ? 0.1426 0.1404 0.1690 0.0080  -0.0182 0.0092  51  GLY   B N   
4702 C  CA  . GLY   B 51  ? 0.1450 0.1504 0.1779 0.0156  -0.0198 0.0047  51  GLY   B CA  
4703 C  C   . GLY   B 51  ? 0.1437 0.1426 0.1865 0.0152  -0.0148 0.0040  51  GLY   B C   
4704 O  O   . GLY   B 51  ? 0.1464 0.1585 0.2090 0.0111  -0.0170 -0.0040 51  GLY   B O   
4708 N  N   . ALA   B 52  ? 0.1388 0.1394 0.1858 0.0195  -0.0086 0.0071  52  ALA   B N   
4709 C  CA  . ALA   B 52  ? 0.1474 0.1514 0.1828 0.0175  -0.0035 -0.0051 52  ALA   B CA  
4710 C  C   . ALA   B 52  ? 0.1342 0.1536 0.1681 0.0086  -0.0062 -0.0018 52  ALA   B C   
4711 O  O   . ALA   B 52  ? 0.1404 0.1548 0.1892 0.0106  -0.0002 -0.0003 52  ALA   B O   
4712 C  CB  . ALA   B 52  ? 0.1679 0.1540 0.1922 0.0088  -0.0004 0.0015  52  ALA   B CB  
4718 N  N   . LEU   B 53  ? 0.1305 0.1455 0.1676 0.0152  -0.0026 0.0002  53  LEU   B N   
4719 C  CA  . LEU   B 53  ? 0.1363 0.1544 0.1664 0.0122  -0.0084 -0.0021 53  LEU   B CA  
4720 C  C   . LEU   B 53  ? 0.1456 0.1489 0.1498 0.0108  -0.0024 0.0056  53  LEU   B C   
4721 O  O   . LEU   B 53  ? 0.1490 0.1505 0.1733 0.0029  0.0013  0.0157  53  LEU   B O   
4722 C  CB  . LEU   B 53  ? 0.1392 0.1546 0.1844 0.0067  -0.0096 0.0134  53  LEU   B CB  
4723 C  CG  . LEU   B 53  ? 0.1370 0.1688 0.1676 0.0027  -0.0071 0.0223  53  LEU   B CG  
4724 C  CD1 . LEU   B 53  ? 0.1428 0.1909 0.2009 0.0133  0.0041  0.0083  53  LEU   B CD1 
4725 C  CD2 . LEU   B 53  ? 0.1504 0.2023 0.1953 -0.0126 -0.0096 -0.0111 53  LEU   B CD2 
4737 N  N   . ASN   B 54  ? 0.1394 0.1381 0.1494 0.0051  -0.0051 0.0029  54  ASN   B N   
4738 C  CA  . ASN   B 54  ? 0.1437 0.1518 0.1700 0.0037  -0.0027 -0.0017 54  ASN   B CA  
4739 C  C   . ASN   B 54  ? 0.1384 0.1479 0.1855 -0.0002 -0.0015 0.0044  54  ASN   B C   
4740 O  O   . ASN   B 54  ? 0.1382 0.1539 0.1937 -0.0032 0.0026  0.0025  54  ASN   B O   
4741 C  CB  . ASN   B 54  ? 0.1462 0.1657 0.1781 0.0080  0.0002  0.0049  54  ASN   B CB  
4742 C  CG  . ASN   B 54  ? 0.1462 0.1676 0.1832 0.0054  -0.0134 0.0019  54  ASN   B CG  
4743 O  OD1 . ASN   B 54  ? 0.1458 0.1637 0.1951 -0.0031 -0.0192 -0.0079 54  ASN   B OD1 
4744 N  ND2 . ASN   B 54  ? 0.1647 0.1840 0.2040 -0.0020 -0.0384 0.0159  54  ASN   B ND2 
4751 N  N   . LYS   B 55  ? 0.1373 0.1520 0.2047 0.0045  -0.0027 0.0009  55  LYS   B N   
4752 C  CA  . LYS   B 55  ? 0.1454 0.1678 0.2255 0.0129  -0.0045 -0.0027 55  LYS   B CA  
4753 C  C   . LYS   B 55  ? 0.1387 0.1606 0.2249 0.0105  0.0026  -0.0015 55  LYS   B C   
4754 O  O   . LYS   B 55  ? 0.1345 0.1784 0.2430 0.0078  0.0019  0.0003  55  LYS   B O   
4755 C  CB  . LYS   B 55  ? 0.1594 0.1856 0.2535 0.0241  0.0065  0.0085  55  LYS   B CB  
4756 C  CG  . LYS   B 55  ? 0.2061 0.2144 0.3278 0.0309  0.0216  0.0183  55  LYS   B CG  
4757 C  CD  . LYS   B 55  ? 0.2468 0.2365 0.3919 0.0429  0.0359  0.0248  55  LYS   B CD  
4758 C  CE  . LYS   B 55  ? 0.2724 0.2536 0.4485 0.0458  0.0558  0.0283  55  LYS   B CE  
4759 N  NZ  . LYS   B 55  ? 0.2815 0.2697 0.4828 0.0435  0.0400  0.0433  55  LYS   B NZ  
4773 N  N   . ALA   B 56  ? 0.1380 0.1649 0.2006 0.0048  -0.0017 -0.0076 56  ALA   B N   
4774 C  CA  . ALA   B 56  ? 0.1525 0.1884 0.2032 -0.0004 0.0039  -0.0099 56  ALA   B CA  
4775 C  C   . ALA   B 56  ? 0.1536 0.1846 0.1936 0.0032  0.0118  -0.0020 56  ALA   B C   
4776 O  O   . ALA   B 56  ? 0.1665 0.1947 0.2049 0.0021  0.0280  0.0038  56  ALA   B O   
4777 C  CB  . ALA   B 56  ? 0.1617 0.2111 0.2079 -0.0122 0.0045  -0.0161 56  ALA   B CB  
4783 N  N   . THR   B 57  ? 0.1447 0.1735 0.2028 0.0015  0.0172  0.0027  57  THR   B N   
4784 C  CA  . THR   B 57  ? 0.1522 0.1723 0.1937 -0.0016 0.0142  0.0072  57  THR   B CA  
4785 C  C   . THR   B 57  ? 0.1557 0.1819 0.2100 -0.0008 0.0176  0.0066  57  THR   B C   
4786 O  O   . THR   B 57  ? 0.1619 0.1824 0.2196 -0.0192 0.0148  0.0070  57  THR   B O   
4787 C  CB  . THR   B 57  ? 0.1610 0.1573 0.1780 -0.0047 0.0157  0.0174  57  THR   B CB  
4788 O  OG1 . THR   B 57  ? 0.1600 0.1539 0.2042 -0.0073 0.0108  0.0074  57  THR   B OG1 
4789 C  CG2 . THR   B 57  ? 0.1600 0.1639 0.1707 -0.0060 0.0172  0.0075  57  THR   B CG2 
4797 N  N   . ASN   B 58  ? 0.1391 0.2003 0.2376 -0.0165 0.0038  -0.0099 58  ASN   B N   
4798 C  CA  . ASN   B 58  ? 0.1659 0.2546 0.2763 -0.0343 0.0292  -0.0026 58  ASN   B CA  
4799 C  C   . ASN   B 58  ? 0.1425 0.2258 0.2277 -0.0202 -0.0075 0.0030  58  ASN   B C   
4800 O  O   . ASN   B 58  ? 0.1512 0.2303 0.2408 -0.0178 -0.0058 -0.0106 58  ASN   B O   
4801 C  CB  . ASN   B 58  ? 0.2653 0.3388 0.4059 -0.0491 0.0647  0.0057  58  ASN   B CB  
4802 C  CG  . ASN   B 58  ? 0.4018 0.4170 0.5548 -0.0502 0.0801  0.0262  58  ASN   B CG  
4803 O  OD1 . ASN   B 58  ? 0.4320 0.4320 0.6099 -0.0491 0.0831  0.0335  58  ASN   B OD1 
4804 N  ND2 . ASN   B 58  ? 0.5150 0.5150 0.6039 -0.0536 0.0883  0.0343  58  ASN   B ND2 
4811 N  N   . ASN   B 59  ? 0.1427 0.2049 0.2128 -0.0131 -0.0099 0.0092  59  ASN   B N   
4812 C  CA  . ASN   B 59  ? 0.1460 0.2021 0.2042 -0.0154 -0.0180 0.0133  59  ASN   B CA  
4813 C  C   . ASN   B 59  ? 0.1441 0.1930 0.2002 -0.0199 -0.0138 -0.0026 59  ASN   B C   
4814 O  O   . ASN   B 59  ? 0.1509 0.1960 0.2023 -0.0182 -0.0114 -0.0053 59  ASN   B O   
4815 C  CB  . ASN   B 59  ? 0.1573 0.2190 0.2203 -0.0075 -0.0320 0.0077  59  ASN   B CB  
4816 C  CG  . ASN   B 59  ? 0.1646 0.2353 0.2339 -0.0047 -0.0460 0.0008  59  ASN   B CG  
4817 O  OD1 . ASN   B 59  ? 0.1696 0.2422 0.2327 -0.0036 -0.0309 0.0167  59  ASN   B OD1 
4818 N  ND2 . ASN   B 59  ? 0.1769 0.2447 0.2507 -0.0150 -0.0461 -0.0049 59  ASN   B ND2 
4825 N  N   . ALA   B 60  ? 0.1457 0.1806 0.2025 -0.0195 -0.0022 -0.0002 60  ALA   B N   
4826 C  CA  . ALA   B 60  ? 0.1522 0.1709 0.2067 -0.0189 -0.0019 0.0048  60  ALA   B CA  
4827 C  C   . ALA   B 60  ? 0.1542 0.1592 0.1869 -0.0171 -0.0110 0.0057  60  ALA   B C   
4828 O  O   . ALA   B 60  ? 0.1548 0.1590 0.2047 -0.0211 -0.0008 -0.0068 60  ALA   B O   
4829 C  CB  . ALA   B 60  ? 0.1655 0.1704 0.2344 -0.0162 0.0040  0.0031  60  ALA   B CB  
4835 N  N   . MET   B 61  ? 0.1472 0.1500 0.1792 -0.0116 -0.0016 0.0014  61  MET   B N   
4836 C  CA  . MET   B 61  ? 0.1403 0.1480 0.1742 -0.0121 -0.0152 0.0021  61  MET   B CA  
4837 C  C   . MET   B 61  ? 0.1522 0.1413 0.1651 -0.0122 -0.0196 0.0046  61  MET   B C   
4838 O  O   . MET   B 61  ? 0.1489 0.1422 0.1609 -0.0043 -0.0136 -0.0104 61  MET   B O   
4839 C  CB  . MET   B 61  ? 0.1341 0.1498 0.1770 -0.0046 -0.0100 -0.0044 61  MET   B CB  
4840 C  CG  . MET   B 61  ? 0.1383 0.1488 0.1613 -0.0019 -0.0076 0.0066  61  MET   B CG  
4841 S  SD  . MET   B 61  ? 0.1398 0.1464 0.1842 -0.0032 -0.0083 -0.0081 61  MET   B SD  
4842 C  CE  . MET   B 61  ? 0.1499 0.1652 0.2014 0.0033  -0.0032 -0.0249 61  MET   B CE  
4852 N  N   . GLN   B 62  ? 0.1537 0.1510 0.1688 -0.0095 -0.0322 0.0077  62  GLN   B N   
4853 C  CA  . GLN   B 62  ? 0.1515 0.1579 0.1775 -0.0054 -0.0302 0.0020  62  GLN   B CA  
4854 C  C   . GLN   B 62  ? 0.1482 0.1618 0.1751 -0.0048 -0.0290 -0.0020 62  GLN   B C   
4855 O  O   . GLN   B 62  ? 0.1593 0.1630 0.1809 -0.0022 -0.0322 -0.0135 62  GLN   B O   
4856 C  CB  . GLN   B 62  ? 0.1520 0.1633 0.1791 -0.0016 -0.0182 0.0127  62  GLN   B CB  
4857 C  CG  . GLN   B 62  ? 0.1578 0.1625 0.1839 -0.0014 -0.0255 -0.0033 62  GLN   B CG  
4858 C  CD  . GLN   B 62  ? 0.1630 0.1576 0.1629 0.0055  -0.0271 0.0047  62  GLN   B CD  
4859 O  OE1 . GLN   B 62  ? 0.1615 0.1552 0.1774 0.0021  -0.0262 -0.0026 62  GLN   B OE1 
4860 N  NE2 . GLN   B 62  ? 0.1655 0.1644 0.1649 0.0052  -0.0221 -0.0084 62  GLN   B NE2 
4869 N  N   . VAL   B 63  ? 0.1464 0.1625 0.1935 -0.0103 -0.0307 -0.0136 63  VAL   B N   
4870 C  CA  . VAL   B 63  ? 0.1621 0.1634 0.2178 -0.0176 -0.0350 -0.0102 63  VAL   B CA  
4871 C  C   . VAL   B 63  ? 0.1689 0.1528 0.1966 -0.0178 -0.0414 -0.0194 63  VAL   B C   
4872 O  O   . VAL   B 63  ? 0.1831 0.1500 0.2125 -0.0146 -0.0565 -0.0116 63  VAL   B O   
4873 C  CB  . VAL   B 63  ? 0.1579 0.1844 0.2546 -0.0247 -0.0384 -0.0073 63  VAL   B CB  
4874 C  CG1 . VAL   B 63  ? 0.1665 0.1892 0.2619 -0.0340 -0.0259 -0.0070 63  VAL   B CG1 
4875 C  CG2 . VAL   B 63  ? 0.1540 0.2052 0.2629 -0.0189 -0.0418 -0.0067 63  VAL   B CG2 
4885 N  N   . GLU   B 64  ? 0.1593 0.1448 0.1897 -0.0154 -0.0302 -0.0120 64  GLU   B N   
4886 C  CA  . GLU   B 64  ? 0.1644 0.1423 0.1735 -0.0147 -0.0367 -0.0046 64  GLU   B CA  
4887 C  C   . GLU   B 64  ? 0.1553 0.1415 0.1601 -0.0055 -0.0310 -0.0167 64  GLU   B C   
4888 O  O   . GLU   B 64  ? 0.1626 0.1485 0.1665 -0.0111 -0.0286 -0.0122 64  GLU   B O   
4889 C  CB  . GLU   B 64  ? 0.1636 0.1480 0.1747 -0.0218 -0.0301 0.0023  64  GLU   B CB  
4890 C  CG  . GLU   B 64  ? 0.1726 0.1493 0.1794 -0.0270 -0.0309 -0.0063 64  GLU   B CG  
4891 C  CD  . GLU   B 64  ? 0.1728 0.1605 0.1854 -0.0364 -0.0348 -0.0042 64  GLU   B CD  
4892 O  OE1 . GLU   B 64  ? 0.1742 0.1788 0.1988 -0.0361 -0.0289 -0.0187 64  GLU   B OE1 
4893 O  OE2 . GLU   B 64  ? 0.1882 0.1727 0.1943 -0.0363 -0.0454 -0.0084 64  GLU   B OE2 
4900 N  N   . SER   B 65  ? 0.1574 0.1376 0.1669 -0.0094 -0.0225 -0.0138 65  SER   B N   
4901 C  CA  . SER   B 65  ? 0.1567 0.1364 0.1712 -0.0010 -0.0169 -0.0164 65  SER   B CA  
4902 C  C   . SER   B 65  ? 0.1594 0.1406 0.1720 0.0020  -0.0260 -0.0141 65  SER   B C   
4903 O  O   . SER   B 65  ? 0.1630 0.1492 0.1720 -0.0012 -0.0251 -0.0241 65  SER   B O   
4904 C  CB  . SER   B 65  ? 0.1615 0.1426 0.1707 -0.0128 -0.0227 -0.0079 65  SER   B CB  
4905 O  OG  . SER   B 65  ? 0.1610 0.1431 0.1714 -0.0110 -0.0241 -0.0169 65  SER   B OG  
4911 N  N   . ASP   B 66  ? 0.1722 0.1497 0.1703 -0.0016 -0.0357 -0.0210 66  ASP   B N   
4912 C  CA  . ASP   B 66  ? 0.1772 0.1546 0.1620 -0.0018 -0.0356 -0.0140 66  ASP   B CA  
4913 C  C   . ASP   B 66  ? 0.1832 0.1561 0.1526 -0.0051 -0.0305 -0.0196 66  ASP   B C   
4914 O  O   . ASP   B 66  ? 0.1874 0.1634 0.1657 0.0056  -0.0275 -0.0174 66  ASP   B O   
4915 C  CB  . ASP   B 66  ? 0.1886 0.1652 0.1803 0.0037  -0.0502 -0.0108 66  ASP   B CB  
4916 C  CG  . ASP   B 66  ? 0.2180 0.1827 0.2059 0.0149  -0.0689 0.0031  66  ASP   B CG  
4917 O  OD1 . ASP   B 66  ? 0.2428 0.1811 0.2106 0.0084  -0.0673 0.0064  66  ASP   B OD1 
4918 O  OD2 . ASP   B 66  ? 0.2412 0.2077 0.2623 0.0356  -0.0630 0.0030  66  ASP   B OD2 
4923 N  N   . ASP   B 67  ? 0.1769 0.1487 0.1647 -0.0089 -0.0283 -0.0189 67  ASP   B N   
4924 C  CA  . ASP   B 67  ? 0.1911 0.1453 0.1712 -0.0103 -0.0295 -0.0065 67  ASP   B CA  
4925 C  C   . ASP   B 67  ? 0.1867 0.1511 0.1826 0.0033  -0.0327 -0.0142 67  ASP   B C   
4926 O  O   . ASP   B 67  ? 0.1896 0.1584 0.1949 0.0025  -0.0223 -0.0224 67  ASP   B O   
4927 C  CB  . ASP   B 67  ? 0.2093 0.1547 0.1967 -0.0173 -0.0492 -0.0103 67  ASP   B CB  
4928 C  CG  . ASP   B 67  ? 0.2456 0.1644 0.2080 -0.0134 -0.0710 -0.0156 67  ASP   B CG  
4929 O  OD1 . ASP   B 67  ? 0.2740 0.1697 0.2351 -0.0108 -0.0686 -0.0128 67  ASP   B OD1 
4930 O  OD2 . ASP   B 67  ? 0.2583 0.1726 0.2209 0.0086  -0.0739 -0.0106 67  ASP   B OD2 
4935 N  N   . TYR   B 68  ? 0.1781 0.1507 0.1757 0.0009  -0.0431 -0.0267 68  TYR   B N   
4936 C  CA  . TYR   B 68  ? 0.1764 0.1645 0.1974 0.0040  -0.0393 -0.0310 68  TYR   B CA  
4937 C  C   . TYR   B 68  ? 0.1685 0.1604 0.1876 0.0023  -0.0390 -0.0363 68  TYR   B C   
4938 O  O   . TYR   B 68  ? 0.1772 0.1726 0.1937 0.0114  -0.0359 -0.0485 68  TYR   B O   
4939 C  CB  . TYR   B 68  ? 0.1787 0.1834 0.2064 0.0065  -0.0487 -0.0420 68  TYR   B CB  
4940 C  CG  . TYR   B 68  ? 0.1899 0.2016 0.2113 0.0110  -0.0370 -0.0596 68  TYR   B CG  
4941 C  CD1 . TYR   B 68  ? 0.1913 0.2072 0.2352 -0.0050 -0.0381 -0.0682 68  TYR   B CD1 
4942 C  CD2 . TYR   B 68  ? 0.1918 0.2245 0.2237 0.0185  -0.0497 -0.0503 68  TYR   B CD2 
4943 C  CE1 . TYR   B 68  ? 0.1964 0.2272 0.2483 -0.0042 -0.0332 -0.0665 68  TYR   B CE1 
4944 C  CE2 . TYR   B 68  ? 0.1904 0.2316 0.2317 0.0157  -0.0336 -0.0666 68  TYR   B CE2 
4945 C  CZ  . TYR   B 68  ? 0.1878 0.2367 0.2477 0.0034  -0.0352 -0.0648 68  TYR   B CZ  
4946 O  OH  . TYR   B 68  ? 0.1825 0.2540 0.2815 -0.0031 -0.0296 -0.0396 68  TYR   B OH  
4956 N  N   . ILE   B 69  ? 0.1698 0.1533 0.1804 0.0036  -0.0445 -0.0344 69  ILE   B N   
4957 C  CA  . ILE   B 69  ? 0.1824 0.1594 0.1991 0.0003  -0.0241 -0.0366 69  ILE   B CA  
4958 C  C   . ILE   B 69  ? 0.1768 0.1610 0.1879 0.0079  -0.0369 -0.0293 69  ILE   B C   
4959 O  O   . ILE   B 69  ? 0.1833 0.1709 0.1822 0.0077  -0.0296 -0.0341 69  ILE   B O   
4960 C  CB  . ILE   B 69  ? 0.1876 0.1648 0.2187 -0.0070 -0.0015 -0.0365 69  ILE   B CB  
4961 C  CG1 . ILE   B 69  ? 0.1906 0.1692 0.2293 -0.0055 0.0070  -0.0386 69  ILE   B CG1 
4962 C  CG2 . ILE   B 69  ? 0.2062 0.1725 0.2277 -0.0010 -0.0036 -0.0251 69  ILE   B CG2 
4963 C  CD1 . ILE   B 69  ? 0.1850 0.1781 0.2412 -0.0220 0.0053  -0.0428 69  ILE   B CD1 
4975 N  N   . ALA   B 70  ? 0.1769 0.1596 0.1889 0.0078  -0.0395 -0.0252 70  ALA   B N   
4976 C  CA  . ALA   B 70  ? 0.1789 0.1641 0.1683 0.0023  -0.0476 -0.0255 70  ALA   B CA  
4977 C  C   . ALA   B 70  ? 0.1837 0.1584 0.1873 0.0008  -0.0476 -0.0377 70  ALA   B C   
4978 O  O   . ALA   B 70  ? 0.1907 0.1627 0.1937 0.0087  -0.0435 -0.0285 70  ALA   B O   
4979 C  CB  . ALA   B 70  ? 0.1824 0.1804 0.1706 -0.0035 -0.0494 -0.0250 70  ALA   B CB  
4985 N  N   . THR   B 71  ? 0.1937 0.1608 0.1948 0.0047  -0.0563 -0.0397 71  THR   B N   
4986 C  CA  . THR   B 71  ? 0.2089 0.1660 0.2133 0.0132  -0.0664 -0.0386 71  THR   B CA  
4987 C  C   . THR   B 71  ? 0.2050 0.1716 0.2350 0.0298  -0.0680 -0.0576 71  THR   B C   
4988 O  O   . THR   B 71  ? 0.2150 0.1747 0.2750 0.0361  -0.0624 -0.0633 71  THR   B O   
4989 C  CB  . THR   B 71  ? 0.2339 0.1836 0.2385 0.0024  -0.0716 -0.0171 71  THR   B CB  
4990 O  OG1 . THR   B 71  ? 0.2484 0.2085 0.2773 -0.0167 -0.0737 0.0039  71  THR   B OG1 
4991 C  CG2 . THR   B 71  ? 0.2511 0.1760 0.2589 0.0058  -0.0615 -0.0050 71  THR   B CG2 
4999 N  N   . ASN   B 72  ? 0.1912 0.1785 0.2349 0.0228  -0.0729 -0.0705 72  ASN   B N   
5000 C  CA  . ASN   B 72  ? 0.1880 0.1911 0.2311 0.0202  -0.0520 -0.0766 72  ASN   B CA  
5001 C  C   . ASN   B 72  ? 0.1843 0.1999 0.2403 0.0075  -0.0268 -0.0677 72  ASN   B C   
5002 O  O   . ASN   B 72  ? 0.1866 0.2178 0.2769 0.0096  -0.0117 -0.0723 72  ASN   B O   
5003 C  CB  . ASN   B 72  ? 0.1941 0.2062 0.2486 0.0220  -0.0638 -0.0624 72  ASN   B CB  
5004 C  CG  . ASN   B 72  ? 0.2101 0.2234 0.2489 0.0342  -0.0599 -0.0394 72  ASN   B CG  
5005 O  OD1 . ASN   B 72  ? 0.2315 0.2441 0.2429 0.0235  -0.0430 -0.0465 72  ASN   B OD1 
5006 N  ND2 . ASN   B 72  ? 0.2264 0.2272 0.2919 0.0524  -0.0503 -0.0023 72  ASN   B ND2 
5013 N  N   . GLY   B 73  ? 0.1876 0.2016 0.2194 -0.0019 -0.0284 -0.0657 73  GLY   B N   
5014 C  CA  . GLY   B 73  ? 0.1776 0.2087 0.2005 -0.0072 -0.0198 -0.0525 73  GLY   B CA  
5015 C  C   . GLY   B 73  ? 0.1796 0.2042 0.1637 0.0004  -0.0256 -0.0479 73  GLY   B C   
5016 O  O   . GLY   B 73  ? 0.1731 0.1911 0.1770 0.0030  -0.0144 -0.0332 73  GLY   B O   
5020 N  N   . PRO   B 74  ? 0.1831 0.2131 0.1606 0.0032  -0.0289 -0.0382 74  PRO   B N   
5021 C  CA  . PRO   B 74  ? 0.1746 0.2128 0.1454 0.0077  -0.0215 -0.0268 74  PRO   B CA  
5022 C  C   . PRO   B 74  ? 0.1604 0.1976 0.1520 0.0056  -0.0130 -0.0193 74  PRO   B C   
5023 O  O   . PRO   B 74  ? 0.1668 0.1982 0.1953 0.0081  -0.0098 -0.0286 74  PRO   B O   
5024 C  CB  . PRO   B 74  ? 0.1865 0.2296 0.1516 0.0098  -0.0204 -0.0185 74  PRO   B CB  
5025 C  CG  . PRO   B 74  ? 0.2092 0.2424 0.1831 0.0099  -0.0164 -0.0092 74  PRO   B CG  
5026 C  CD  . PRO   B 74  ? 0.2100 0.2297 0.1824 0.0120  -0.0141 -0.0237 74  PRO   B CD  
5034 N  N   . LEU   B 75  ? 0.1604 0.1854 0.1459 0.0049  -0.0208 -0.0201 75  LEU   B N   
5035 C  CA  . LEU   B 75  ? 0.1662 0.1842 0.1468 0.0043  -0.0141 -0.0041 75  LEU   B CA  
5036 C  C   . LEU   B 75  ? 0.1678 0.1921 0.1458 0.0085  -0.0034 -0.0006 75  LEU   B C   
5037 O  O   . LEU   B 75  ? 0.1830 0.2035 0.1517 0.0024  -0.0045 -0.0009 75  LEU   B O   
5038 C  CB  . LEU   B 75  ? 0.1686 0.1841 0.1398 -0.0100 -0.0212 0.0106  75  LEU   B CB  
5039 C  CG  . LEU   B 75  ? 0.1998 0.1977 0.1588 -0.0353 -0.0140 0.0053  75  LEU   B CG  
5040 C  CD1 . LEU   B 75  ? 0.2312 0.2131 0.1611 -0.0393 0.0075  0.0034  75  LEU   B CD1 
5041 C  CD2 . LEU   B 75  ? 0.2398 0.2202 0.2210 -0.0291 -0.0003 0.0133  75  LEU   B CD2 
5053 N  N   . LYS   B 76  ? 0.1642 0.2152 0.1766 0.0041  0.0024  0.0077  76  LYS   B N   
5054 C  CA  . LYS   B 76  ? 0.1749 0.2251 0.2115 -0.0103 0.0257  0.0063  76  LYS   B CA  
5055 C  C   . LYS   B 76  ? 0.1697 0.2098 0.1884 0.0012  0.0181  0.0343  76  LYS   B C   
5056 O  O   . LYS   B 76  ? 0.1686 0.1932 0.1896 -0.0029 0.0143  0.0326  76  LYS   B O   
5057 C  CB  . LYS   B 76  ? 0.1900 0.2303 0.2588 -0.0173 0.0463  -0.0182 76  LYS   B CB  
5058 C  CG  . LYS   B 76  ? 0.2038 0.2468 0.3007 -0.0075 0.0293  -0.0239 76  LYS   B CG  
5059 C  CD  . LYS   B 76  ? 0.2056 0.2532 0.3370 0.0037  0.0215  -0.0379 76  LYS   B CD  
5060 C  CE  . LYS   B 76  ? 0.2140 0.2667 0.3738 0.0092  0.0048  -0.0447 76  LYS   B CE  
5061 N  NZ  . LYS   B 76  ? 0.2152 0.2689 0.3996 0.0072  -0.0167 -0.0617 76  LYS   B NZ  
5075 N  N   . VAL   B 77  ? 0.1780 0.2211 0.1856 0.0061  0.0167  0.0353  77  VAL   B N   
5076 C  CA  . VAL   B 77  ? 0.1856 0.2128 0.1934 0.0154  0.0210  0.0603  77  VAL   B CA  
5077 C  C   . VAL   B 77  ? 0.1718 0.1879 0.1859 0.0185  0.0295  0.0504  77  VAL   B C   
5078 O  O   . VAL   B 77  ? 0.1730 0.1831 0.1913 0.0277  0.0306  0.0335  77  VAL   B O   
5079 C  CB  . VAL   B 77  ? 0.1969 0.2240 0.2350 0.0139  0.0299  0.0758  77  VAL   B CB  
5080 C  CG1 . VAL   B 77  ? 0.2017 0.2106 0.2645 0.0036  0.0256  0.0824  77  VAL   B CG1 
5081 C  CG2 . VAL   B 77  ? 0.2166 0.2446 0.2551 0.0135  0.0142  0.0827  77  VAL   B CG2 
5091 N  N   . GLY   B 78  ? 0.1675 0.1684 0.1837 0.0147  0.0237  0.0371  78  GLY   B N   
5092 C  CA  . GLY   B 78  ? 0.1616 0.1679 0.1781 0.0110  0.0280  0.0231  78  GLY   B CA  
5093 C  C   . GLY   B 78  ? 0.1555 0.1608 0.1682 0.0151  0.0193  0.0231  78  GLY   B C   
5094 O  O   . GLY   B 78  ? 0.1538 0.1585 0.1892 0.0179  0.0204  0.0285  78  GLY   B O   
5098 N  N   . GLY   B 79  ? 0.1501 0.1654 0.1562 0.0103  0.0102  0.0189  79  GLY   B N   
5099 C  CA  . GLY   B 79  ? 0.1502 0.1530 0.1643 0.0125  0.0102  0.0174  79  GLY   B CA  
5100 C  C   . GLY   B 79  ? 0.1430 0.1454 0.1765 0.0080  0.0047  0.0115  79  GLY   B C   
5101 O  O   . GLY   B 79  ? 0.1500 0.1425 0.1884 0.0104  0.0178  0.0256  79  GLY   B O   
5105 N  N   . SER   B 80  ? 0.1432 0.1354 0.1760 0.0081  0.0187  0.0124  80  SER   B N   
5106 C  CA  . SER   B 80  ? 0.1346 0.1387 0.1615 0.0062  0.0008  0.0078  80  SER   B CA  
5107 C  C   . SER   B 80  ? 0.1385 0.1321 0.1750 0.0053  -0.0043 0.0088  80  SER   B C   
5108 O  O   . SER   B 80  ? 0.1517 0.1358 0.2030 0.0083  0.0058  -0.0018 80  SER   B O   
5109 C  CB  . SER   B 80  ? 0.1372 0.1430 0.1689 -0.0038 0.0030  0.0150  80  SER   B CB  
5110 O  OG  . SER   B 80  ? 0.1447 0.1597 0.1881 0.0004  -0.0062 0.0144  80  SER   B OG  
5116 N  N   . CYS   B 81  ? 0.1342 0.1239 0.1724 -0.0012 -0.0037 0.0048  81  CYS   B N   
5117 C  CA  . CYS   B 81  ? 0.1414 0.1246 0.1673 0.0073  -0.0102 0.0066  81  CYS   B CA  
5118 C  C   . CYS   B 81  ? 0.1344 0.1219 0.1585 -0.0008 -0.0125 0.0058  81  CYS   B C   
5119 O  O   . CYS   B 81  ? 0.1607 0.1222 0.1709 0.0093  0.0000  -0.0021 81  CYS   B O   
5120 C  CB  . CYS   B 81  ? 0.1593 0.1358 0.1667 -0.0038 -0.0093 0.0018  81  CYS   B CB  
5121 S  SG  . CYS   B 81  ? 0.1609 0.1515 0.1679 -0.0052 -0.0265 -0.0076 81  CYS   B SG  
5127 N  N   . VAL   B 82  ? 0.1375 0.1208 0.1632 -0.0054 -0.0136 -0.0035 82  VAL   B N   
5128 C  CA  . VAL   B 82  ? 0.1489 0.1287 0.1657 -0.0078 -0.0130 0.0052  82  VAL   B CA  
5129 C  C   . VAL   B 82  ? 0.1558 0.1177 0.1771 -0.0022 -0.0080 -0.0023 82  VAL   B C   
5130 O  O   . VAL   B 82  ? 0.1631 0.1193 0.2011 -0.0039 -0.0142 -0.0143 82  VAL   B O   
5131 C  CB  . VAL   B 82  ? 0.1571 0.1427 0.1713 -0.0035 -0.0189 0.0110  82  VAL   B CB  
5132 C  CG1 . VAL   B 82  ? 0.1831 0.1694 0.1723 0.0044  -0.0174 0.0134  82  VAL   B CG1 
5133 C  CG2 . VAL   B 82  ? 0.1689 0.1593 0.1904 -0.0072 -0.0356 0.0209  82  VAL   B CG2 
5143 N  N   . LEU   B 83  ? 0.1427 0.1181 0.1644 -0.0139 -0.0221 -0.0094 83  LEU   B N   
5144 C  CA  . LEU   B 83  ? 0.1448 0.1301 0.1519 -0.0143 -0.0214 -0.0057 83  LEU   B CA  
5145 C  C   . LEU   B 83  ? 0.1440 0.1254 0.1554 -0.0208 -0.0208 0.0008  83  LEU   B C   
5146 O  O   . LEU   B 83  ? 0.1458 0.1312 0.1417 -0.0223 -0.0192 0.0117  83  LEU   B O   
5147 C  CB  . LEU   B 83  ? 0.1532 0.1427 0.1565 -0.0130 -0.0262 -0.0107 83  LEU   B CB  
5148 C  CG  . LEU   B 83  ? 0.1689 0.1592 0.1571 -0.0165 -0.0160 -0.0078 83  LEU   B CG  
5149 C  CD1 . LEU   B 83  ? 0.1787 0.1668 0.1679 -0.0080 -0.0229 -0.0034 83  LEU   B CD1 
5150 C  CD2 . LEU   B 83  ? 0.1886 0.1591 0.1734 -0.0131 -0.0170 -0.0182 83  LEU   B CD2 
5162 N  N   . SER   B 84  ? 0.1536 0.1304 0.1782 -0.0258 -0.0240 0.0050  84  SER   B N   
5163 C  CA  . SER   B 84  ? 0.1499 0.1530 0.1631 -0.0245 -0.0127 0.0216  84  SER   B CA  
5164 C  C   . SER   B 84  ? 0.1430 0.1693 0.1199 -0.0231 -0.0165 0.0236  84  SER   B C   
5165 O  O   . SER   B 84  ? 0.1485 0.1559 0.1241 -0.0231 -0.0172 0.0018  84  SER   B O   
5166 C  CB  . SER   B 84  ? 0.1694 0.1606 0.2121 -0.0295 0.0051  0.0139  84  SER   B CB  
5167 O  OG  . SER   B 84  ? 0.1703 0.1747 0.2507 -0.0434 0.0077  0.0197  84  SER   B OG  
5173 N  N   . GLY   B 85  ? 0.1501 0.1876 0.1342 -0.0290 -0.0205 0.0249  85  GLY   B N   
5174 C  CA  . GLY   B 85  ? 0.1512 0.1957 0.1537 -0.0375 -0.0064 -0.0048 85  GLY   B CA  
5175 C  C   . GLY   B 85  ? 0.1483 0.1800 0.1552 -0.0441 -0.0061 0.0027  85  GLY   B C   
5176 O  O   . GLY   B 85  ? 0.1562 0.1750 0.1605 -0.0523 0.0113  -0.0100 85  GLY   B O   
5180 N  N   . HIS   B 86  ? 0.1501 0.1668 0.1668 -0.0320 -0.0212 0.0164  86  HIS   B N   
5181 C  CA  . HIS   B 86  ? 0.1493 0.1640 0.1537 -0.0319 -0.0207 0.0212  86  HIS   B CA  
5182 C  C   . HIS   B 86  ? 0.1486 0.1819 0.1516 -0.0463 -0.0136 0.0353  86  HIS   B C   
5183 O  O   . HIS   B 86  ? 0.1639 0.1935 0.1594 -0.0389 0.0010  0.0313  86  HIS   B O   
5184 C  CB  . HIS   B 86  ? 0.1585 0.1637 0.1639 -0.0237 -0.0217 0.0052  86  HIS   B CB  
5185 C  CG  . HIS   B 86  ? 0.1639 0.1714 0.1585 -0.0104 -0.0355 0.0133  86  HIS   B CG  
5186 N  ND1 . HIS   B 86  ? 0.1741 0.1954 0.1903 -0.0195 -0.0459 -0.0067 86  HIS   B ND1 
5187 C  CD2 . HIS   B 86  ? 0.1642 0.1681 0.1707 -0.0076 -0.0249 0.0129  86  HIS   B CD2 
5188 C  CE1 . HIS   B 86  ? 0.1798 0.1907 0.1809 -0.0140 -0.0202 -0.0245 86  HIS   B CE1 
5189 N  NE2 . HIS   B 86  ? 0.1706 0.1813 0.1635 -0.0008 -0.0204 -0.0051 86  HIS   B NE2 
5197 N  N   . ASN   B 87  ? 0.1494 0.1870 0.1723 -0.0368 -0.0065 0.0294  87  ASN   B N   
5198 C  CA  . ASN   B 87  ? 0.1570 0.2001 0.1809 -0.0396 0.0264  0.0251  87  ASN   B CA  
5199 C  C   . ASN   B 87  ? 0.1721 0.1832 0.1681 -0.0276 0.0318  0.0164  87  ASN   B C   
5200 O  O   . ASN   B 87  ? 0.1985 0.1966 0.1971 -0.0227 0.0494  0.0116  87  ASN   B O   
5201 C  CB  . ASN   B 87  ? 0.1627 0.2421 0.2020 -0.0296 0.0296  0.0184  87  ASN   B CB  
5202 C  CG  . ASN   B 87  ? 0.1687 0.2597 0.2064 -0.0003 0.0315  0.0371  87  ASN   B CG  
5203 O  OD1 . ASN   B 87  ? 0.1634 0.2451 0.2022 0.0036  0.0418  0.0569  87  ASN   B OD1 
5204 N  ND2 . ASN   B 87  ? 0.2005 0.2743 0.2375 0.0083  0.0368  0.0286  87  ASN   B ND2 
5211 N  N   . LEU   B 88  ? 0.1604 0.1707 0.1480 -0.0344 0.0151  0.0087  88  LEU   B N   
5212 C  CA  . LEU   B 88  ? 0.1725 0.1645 0.1504 -0.0372 0.0080  -0.0010 88  LEU   B CA  
5213 C  C   . LEU   B 88  ? 0.1697 0.1536 0.1577 -0.0402 0.0001  0.0019  88  LEU   B C   
5214 O  O   . LEU   B 88  ? 0.1984 0.1611 0.1957 -0.0262 -0.0268 -0.0098 88  LEU   B O   
5215 C  CB  . LEU   B 88  ? 0.1870 0.1658 0.1684 -0.0444 -0.0130 0.0132  88  LEU   B CB  
5216 C  CG  . LEU   B 88  ? 0.2246 0.1970 0.1911 -0.0400 -0.0298 0.0309  88  LEU   B CG  
5217 C  CD1 . LEU   B 88  ? 0.2402 0.2302 0.1981 -0.0500 -0.0292 0.0464  88  LEU   B CD1 
5218 C  CD2 . LEU   B 88  ? 0.2598 0.2227 0.2453 0.0025  -0.0473 0.0072  88  LEU   B CD2 
5230 N  N   . ALA   B 89  ? 0.1559 0.1525 0.1504 -0.0373 0.0163  0.0021  89  ALA   B N   
5231 C  CA  . ALA   B 89  ? 0.1577 0.1481 0.1264 -0.0390 0.0021  0.0148  89  ALA   B CA  
5232 C  C   . ALA   B 89  ? 0.1663 0.1527 0.1296 -0.0379 0.0084  0.0080  89  ALA   B C   
5233 O  O   . ALA   B 89  ? 0.1467 0.1639 0.1668 -0.0381 0.0099  -0.0263 89  ALA   B O   
5234 C  CB  . ALA   B 89  ? 0.1539 0.1495 0.1429 -0.0361 0.0047  0.0195  89  ALA   B CB  
5240 N  N   . LYS   B 90  ? 0.2016 0.1397 0.1486 -0.0456 -0.0099 0.0133  90  LYS   B N   
5241 C  CA  . LYS   B 90  ? 0.2158 0.1380 0.1421 -0.0479 -0.0133 0.0138  90  LYS   B CA  
5242 C  C   . LYS   B 90  ? 0.1996 0.1260 0.1579 -0.0416 -0.0138 0.0037  90  LYS   B C   
5243 O  O   . LYS   B 90  ? 0.2098 0.1435 0.1718 -0.0567 -0.0045 0.0020  90  LYS   B O   
5244 C  CB  . LYS   B 90  ? 0.2382 0.1448 0.1715 -0.0393 -0.0034 0.0206  90  LYS   B CB  
5245 C  CG  . LYS   B 90  ? 0.2428 0.1568 0.1690 -0.0212 0.0180  0.0212  90  LYS   B CG  
5246 C  CD  . LYS   B 90  ? 0.2633 0.1766 0.2161 -0.0144 0.0369  0.0015  90  LYS   B CD  
5247 C  CE  . LYS   B 90  ? 0.2740 0.1943 0.2646 -0.0196 0.0386  -0.0161 90  LYS   B CE  
5248 N  NZ  . LYS   B 90  ? 0.2761 0.1874 0.2578 -0.0367 0.0574  -0.0239 90  LYS   B NZ  
5262 N  N   . HIS   B 91  ? 0.1688 0.1216 0.1344 -0.0325 -0.0180 0.0096  91  HIS   B N   
5263 C  CA  . HIS   B 91  ? 0.1569 0.1259 0.1557 -0.0249 -0.0203 0.0055  91  HIS   B CA  
5264 C  C   . HIS   B 91  ? 0.1486 0.1264 0.1291 -0.0261 -0.0081 0.0117  91  HIS   B C   
5265 O  O   . HIS   B 91  ? 0.1636 0.1302 0.1245 -0.0258 -0.0194 0.0003  91  HIS   B O   
5266 C  CB  . HIS   B 91  ? 0.1758 0.1246 0.1997 -0.0140 -0.0178 0.0159  91  HIS   B CB  
5267 C  CG  . HIS   B 91  ? 0.2122 0.1414 0.2603 0.0045  0.0147  0.0271  91  HIS   B CG  
5268 N  ND1 . HIS   B 91  ? 0.2426 0.1471 0.3119 -0.0006 0.0282  0.0082  91  HIS   B ND1 
5269 C  CD2 . HIS   B 91  ? 0.2223 0.1748 0.3019 0.0205  0.0071  0.0555  91  HIS   B CD2 
5270 C  CE1 . HIS   B 91  ? 0.2459 0.1644 0.3335 0.0175  0.0336  0.0112  91  HIS   B CE1 
5271 N  NE2 . HIS   B 91  ? 0.2382 0.1828 0.3322 0.0296  0.0270  0.0577  91  HIS   B NE2 
5279 N  N   . CYS   B 92  ? 0.1425 0.1270 0.1249 -0.0267 -0.0172 0.0059  92  CYS   B N   
5280 C  CA  . CYS   B 92  ? 0.1378 0.1207 0.1280 -0.0243 -0.0151 0.0047  92  CYS   B CA  
5281 C  C   . CYS   B 92  ? 0.1307 0.1118 0.1380 -0.0175 -0.0059 0.0040  92  CYS   B C   
5282 O  O   . CYS   B 92  ? 0.1462 0.1233 0.1532 -0.0182 -0.0036 -0.0005 92  CYS   B O   
5283 C  CB  . CYS   B 92  ? 0.1409 0.1329 0.1316 -0.0136 -0.0086 0.0030  92  CYS   B CB  
5284 S  SG  . CYS   B 92  ? 0.1394 0.1302 0.1442 -0.0139 -0.0140 0.0056  92  CYS   B SG  
5290 N  N   . LEU   B 93  ? 0.1275 0.1223 0.1377 -0.0135 -0.0132 -0.0008 93  LEU   B N   
5291 C  CA  . LEU   B 93  ? 0.1281 0.1192 0.1486 -0.0079 -0.0200 0.0038  93  LEU   B CA  
5292 C  C   . LEU   B 93  ? 0.1248 0.1179 0.1334 -0.0056 -0.0118 0.0144  93  LEU   B C   
5293 O  O   . LEU   B 93  ? 0.1311 0.1148 0.1513 -0.0077 -0.0078 0.0052  93  LEU   B O   
5294 C  CB  . LEU   B 93  ? 0.1292 0.1181 0.1538 -0.0055 -0.0133 0.0055  93  LEU   B CB  
5295 C  CG  . LEU   B 93  ? 0.1278 0.1331 0.1722 -0.0053 -0.0093 0.0141  93  LEU   B CG  
5296 C  CD1 . LEU   B 93  ? 0.1310 0.1437 0.1797 -0.0005 -0.0056 0.0058  93  LEU   B CD1 
5297 C  CD2 . LEU   B 93  ? 0.1290 0.1378 0.1670 -0.0044 -0.0166 0.0047  93  LEU   B CD2 
5309 N  N   . HIS   B 94  ? 0.1296 0.1182 0.1289 -0.0071 -0.0100 0.0082  94  HIS   B N   
5310 C  CA  . HIS   B 94  ? 0.1290 0.1169 0.1289 -0.0025 -0.0084 0.0122  94  HIS   B CA  
5311 C  C   . HIS   B 94  ? 0.1299 0.1210 0.1578 -0.0011 -0.0109 0.0082  94  HIS   B C   
5312 O  O   . HIS   B 94  ? 0.1317 0.1269 0.1930 -0.0025 0.0088  -0.0104 94  HIS   B O   
5313 C  CB  . HIS   B 94  ? 0.1319 0.1260 0.1501 -0.0005 -0.0111 0.0034  94  HIS   B CB  
5314 C  CG  . HIS   B 94  ? 0.1339 0.1205 0.1526 -0.0070 -0.0182 0.0063  94  HIS   B CG  
5315 N  ND1 . HIS   B 94  ? 0.1383 0.1262 0.1495 -0.0094 -0.0184 0.0045  94  HIS   B ND1 
5316 C  CD2 . HIS   B 94  ? 0.1374 0.1261 0.1535 0.0003  -0.0145 0.0071  94  HIS   B CD2 
5317 C  CE1 . HIS   B 94  ? 0.1476 0.1243 0.1374 -0.0119 -0.0260 0.0070  94  HIS   B CE1 
5318 N  NE2 . HIS   B 94  ? 0.1351 0.1320 0.1494 -0.0197 -0.0196 0.0033  94  HIS   B NE2 
5326 N  N   . VAL   B 95  ? 0.1245 0.1142 0.1499 0.0002  -0.0069 0.0045  95  VAL   B N   
5327 C  CA  . VAL   B 95  ? 0.1262 0.1289 0.1419 0.0023  -0.0003 0.0199  95  VAL   B CA  
5328 C  C   . VAL   B 95  ? 0.1336 0.1236 0.1528 -0.0045 0.0082  0.0080  95  VAL   B C   
5329 O  O   . VAL   B 95  ? 0.1393 0.1211 0.1720 0.0034  0.0051  0.0196  95  VAL   B O   
5330 C  CB  . VAL   B 95  ? 0.1314 0.1250 0.1598 -0.0013 -0.0146 0.0064  95  VAL   B CB  
5331 C  CG1 . VAL   B 95  ? 0.1400 0.1419 0.1812 -0.0051 -0.0049 0.0152  95  VAL   B CG1 
5332 C  CG2 . VAL   B 95  ? 0.1387 0.1232 0.1555 0.0018  -0.0175 0.0168  95  VAL   B CG2 
5342 N  N   . VAL   B 96  ? 0.1434 0.1302 0.1534 0.0041  0.0005  0.0199  96  VAL   B N   
5343 C  CA  . VAL   B 96  ? 0.1568 0.1397 0.1520 0.0035  -0.0010 0.0203  96  VAL   B CA  
5344 C  C   . VAL   B 96  ? 0.1582 0.1413 0.1675 0.0060  0.0102  0.0272  96  VAL   B C   
5345 O  O   . VAL   B 96  ? 0.1573 0.1508 0.1895 0.0001  0.0204  0.0113  96  VAL   B O   
5346 C  CB  . VAL   B 96  ? 0.1607 0.1569 0.1556 0.0084  0.0075  0.0147  96  VAL   B CB  
5347 C  CG1 . VAL   B 96  ? 0.1639 0.1789 0.1635 0.0172  0.0044  0.0101  96  VAL   B CG1 
5348 C  CG2 . VAL   B 96  ? 0.1650 0.1629 0.1719 0.0064  0.0130  0.0087  96  VAL   B CG2 
5358 N  N   . GLY   B 97  ? 0.1619 0.1462 0.1569 0.0017  0.0040  0.0301  97  GLY   B N   
5359 C  CA  . GLY   B 97  ? 0.1767 0.1516 0.1769 0.0011  0.0089  0.0253  97  GLY   B CA  
5360 C  C   . GLY   B 97  ? 0.1945 0.1566 0.1762 0.0094  0.0060  0.0249  97  GLY   B C   
5361 O  O   . GLY   B 97  ? 0.2083 0.1664 0.1728 -0.0007 0.0053  0.0170  97  GLY   B O   
5365 N  N   . PRO   B 98  ? 0.2100 0.1598 0.1945 0.0125  0.0300  0.0403  98  PRO   B N   
5366 C  CA  . PRO   B 98  ? 0.2236 0.1783 0.1902 0.0181  0.0458  0.0298  98  PRO   B CA  
5367 C  C   . PRO   B 98  ? 0.2410 0.1798 0.1669 0.0358  0.0444  0.0476  98  PRO   B C   
5368 O  O   . PRO   B 98  ? 0.2288 0.1737 0.1987 0.0303  0.0474  0.0506  98  PRO   B O   
5369 C  CB  . PRO   B 98  ? 0.2099 0.1859 0.2120 0.0148  0.0523  0.0369  98  PRO   B CB  
5370 C  CG  . PRO   B 98  ? 0.2067 0.1807 0.2146 0.0084  0.0429  0.0513  98  PRO   B CG  
5371 C  CD  . PRO   B 98  ? 0.1963 0.1673 0.2071 0.0108  0.0382  0.0509  98  PRO   B CD  
5379 N  N   . ASN   B 99  ? 0.2518 0.2009 0.1799 0.0555  0.0501  0.0318  99  ASN   B N   
5380 C  CA  . ASN   B 99  ? 0.2746 0.2101 0.2022 0.0651  0.0423  0.0572  99  ASN   B CA  
5381 C  C   . ASN   B 99  ? 0.2990 0.2467 0.2366 0.0621  0.0554  0.0949  99  ASN   B C   
5382 O  O   . ASN   B 99  ? 0.3031 0.2566 0.2507 0.0622  0.0386  0.0952  99  ASN   B O   
5383 C  CB  . ASN   B 99  ? 0.2859 0.2054 0.2047 0.0670  0.0286  0.0462  99  ASN   B CB  
5384 C  CG  . ASN   B 99  ? 0.2896 0.2154 0.2169 0.0616  0.0199  0.0405  99  ASN   B CG  
5385 O  OD1 . ASN   B 99  ? 0.2911 0.2212 0.2443 0.0609  0.0297  0.0505  99  ASN   B OD1 
5386 N  ND2 . ASN   B 99  ? 0.2854 0.2094 0.2196 0.0659  -0.0048 0.0349  99  ASN   B ND2 
5393 N  N   A VAL   B 100 ? 0.3164 0.2602 0.2671 0.0492  0.0707  0.1164  100 VAL   B N   
5394 N  N   B VAL   B 100 ? 0.3202 0.2618 0.2700 0.0533  0.0563  0.1067  100 VAL   B N   
5395 C  CA  A VAL   B 100 ? 0.3441 0.2812 0.3186 0.0361  0.0674  0.1304  100 VAL   B CA  
5396 C  CA  B VAL   B 100 ? 0.3463 0.2805 0.3118 0.0430  0.0485  0.1157  100 VAL   B CA  
5397 C  C   A VAL   B 100 ? 0.3673 0.2901 0.3097 0.0429  0.0590  0.1459  100 VAL   B C   
5398 C  C   B VAL   B 100 ? 0.3669 0.2886 0.3083 0.0460  0.0455  0.1351  100 VAL   B C   
5399 O  O   A VAL   B 100 ? 0.3747 0.3017 0.3157 0.0399  0.0636  0.1357  100 VAL   B O   
5400 O  O   B VAL   B 100 ? 0.3709 0.2944 0.3112 0.0421  0.0464  0.1277  100 VAL   B O   
5401 C  CB  A VAL   B 100 ? 0.3506 0.2955 0.3839 0.0129  0.0677  0.1307  100 VAL   B CB  
5402 C  CB  B VAL   B 100 ? 0.3518 0.2917 0.3571 0.0279  0.0436  0.1086  100 VAL   B CB  
5403 C  CG1 A VAL   B 100 ? 0.3540 0.3018 0.4080 0.0054  0.0648  0.1265  100 VAL   B CG1 
5404 C  CG1 B VAL   B 100 ? 0.3543 0.2965 0.3711 0.0229  0.0414  0.1058  100 VAL   B CG1 
5405 C  CG2 A VAL   B 100 ? 0.3510 0.2987 0.3957 0.0068  0.0715  0.1384  100 VAL   B CG2 
5406 C  CG2 B VAL   B 100 ? 0.3524 0.2943 0.3674 0.0239  0.0427  0.1094  100 VAL   B CG2 
5425 N  N   . ASN   B 101 ? 0.3818 0.2925 0.3062 0.0547  0.0424  0.1501  101 ASN   B N   
5426 C  CA  . ASN   B 101 ? 0.4188 0.3092 0.3267 0.0644  0.0276  0.1560  101 ASN   B CA  
5427 C  C   . ASN   B 101 ? 0.4582 0.3498 0.3333 0.0599  0.0126  0.1623  101 ASN   B C   
5428 O  O   . ASN   B 101 ? 0.4622 0.3642 0.3549 0.0645  0.0142  0.1328  101 ASN   B O   
5429 C  CB  . ASN   B 101 ? 0.4183 0.2927 0.3358 0.0677  0.0359  0.1319  101 ASN   B CB  
5430 C  CG  . ASN   B 101 ? 0.4155 0.2744 0.3370 0.0710  0.0373  0.1275  101 ASN   B CG  
5431 O  OD1 . ASN   B 101 ? 0.4216 0.2729 0.3669 0.0666  0.0507  0.1136  101 ASN   B OD1 
5432 N  ND2 . ASN   B 101 ? 0.4062 0.2623 0.3348 0.0752  0.0354  0.1203  101 ASN   B ND2 
5440 N  N   . LYS   B 102 ? 0.4916 0.3862 0.3575 0.0446  0.0143  0.1558  102 LYS   B N   
5441 C  CA  . LYS   B 102 ? 0.5222 0.4283 0.4001 0.0265  0.0194  0.1304  102 LYS   B CA  
5442 C  C   . LYS   B 102 ? 0.5164 0.4284 0.3781 0.0262  0.0222  0.1338  102 LYS   B C   
5443 O  O   . LYS   B 102 ? 0.5256 0.4327 0.3827 0.0253  0.0106  0.1347  102 LYS   B O   
5444 C  CB  . LYS   B 102 ? 0.5530 0.4652 0.4622 0.0131  0.0314  0.0902  102 LYS   B CB  
5445 C  CG  . LYS   B 102 ? 0.5775 0.4953 0.5374 0.0040  0.0406  0.0486  102 LYS   B CG  
5446 C  CD  . LYS   B 102 ? 0.5972 0.5188 0.5963 -0.0034 0.0493  0.0152  102 LYS   B CD  
5447 C  CE  . LYS   B 102 ? 0.6102 0.5355 0.6470 -0.0098 0.0577  -0.0077 102 LYS   B CE  
5448 N  NZ  . LYS   B 102 ? 0.6175 0.5459 0.6757 -0.0133 0.0627  -0.0215 102 LYS   B NZ  
5462 N  N   . GLY   B 103 ? 0.4977 0.4215 0.3633 0.0253  0.0384  0.1255  103 GLY   B N   
5463 C  CA  . GLY   B 103 ? 0.4772 0.4123 0.3663 0.0235  0.0586  0.1079  103 GLY   B CA  
5464 C  C   . GLY   B 103 ? 0.4535 0.4003 0.3583 0.0169  0.0743  0.0844  103 GLY   B C   
5465 O  O   . GLY   B 103 ? 0.4589 0.4078 0.3595 0.0106  0.0760  0.0858  103 GLY   B O   
5469 N  N   A GLU   B 104 ? 0.4365 0.3867 0.3470 0.0186  0.0905  0.0693  104 GLU   B N   
5470 N  N   B GLU   B 104 ? 0.4395 0.3913 0.3564 0.0141  0.0689  0.0664  104 GLU   B N   
5471 C  CA  A GLU   B 104 ? 0.4186 0.3719 0.3324 0.0247  0.0985  0.0523  104 GLU   B CA  
5472 C  CA  B GLU   B 104 ? 0.4245 0.3810 0.3495 0.0130  0.0600  0.0462  104 GLU   B CA  
5473 C  C   A GLU   B 104 ? 0.4184 0.3715 0.3368 0.0067  0.1346  0.0571  104 GLU   B C   
5474 C  C   B GLU   B 104 ? 0.4189 0.3789 0.3556 0.0062  0.0741  0.0415  104 GLU   B C   
5475 O  O   A GLU   B 104 ? 0.4145 0.3718 0.3537 0.0053  0.1375  0.0551  104 GLU   B O   
5476 O  O   B GLU   B 104 ? 0.4159 0.3773 0.3660 0.0051  0.0756  0.0396  104 GLU   B O   
5477 C  CB  A GLU   B 104 ? 0.4025 0.3544 0.3171 0.0485  0.0655  0.0246  104 GLU   B CB  
5478 C  CB  B GLU   B 104 ? 0.4158 0.3706 0.3360 0.0176  0.0370  0.0284  104 GLU   B CB  
5479 C  CG  A GLU   B 104 ? 0.3867 0.3371 0.2993 0.0694  0.0270  -0.0022 104 GLU   B CG  
5480 C  CG  B GLU   B 104 ? 0.4070 0.3600 0.3217 0.0204  0.0131  0.0109  104 GLU   B CG  
5481 C  CD  A GLU   B 104 ? 0.3704 0.3175 0.2791 0.0878  -0.0042 -0.0165 104 GLU   B CD  
5482 C  CD  B GLU   B 104 ? 0.3988 0.3485 0.3082 0.0208  -0.0056 -0.0015 104 GLU   B CD  
5483 O  OE1 A GLU   B 104 ? 0.3512 0.3001 0.2433 0.1023  -0.0038 -0.0180 104 GLU   B OE1 
5484 O  OE1 B GLU   B 104 ? 0.3922 0.3422 0.2953 0.0190  -0.0069 -0.0031 104 GLU   B OE1 
5485 O  OE2 A GLU   B 104 ? 0.3723 0.3181 0.2787 0.0903  -0.0275 -0.0284 104 GLU   B OE2 
5486 O  OE2 B GLU   B 104 ? 0.3980 0.3461 0.3066 0.0222  -0.0189 -0.0102 104 GLU   B OE2 
5499 N  N   A ASP   B 105 ? 0.4172 0.3713 0.3360 -0.0074 0.1678  0.0640  105 ASP   B N   
5500 N  N   B ASP   B 105 ? 0.4146 0.3784 0.3615 0.0007  0.0868  0.0390  105 ASP   B N   
5501 C  CA  A ASP   B 105 ? 0.4188 0.3714 0.3557 -0.0164 0.1884  0.0491  105 ASP   B CA  
5502 C  CA  B ASP   B 105 ? 0.4108 0.3764 0.3686 -0.0035 0.0968  0.0286  105 ASP   B CA  
5503 C  C   A ASP   B 105 ? 0.4002 0.3426 0.3205 -0.0283 0.1948  0.0469  105 ASP   B C   
5504 C  C   B ASP   B 105 ? 0.3988 0.3627 0.3482 -0.0074 0.0983  0.0226  105 ASP   B C   
5505 O  O   A ASP   B 105 ? 0.3843 0.3357 0.3047 -0.0219 0.1922  0.0472  105 ASP   B O   
5506 O  O   B ASP   B 105 ? 0.3966 0.3605 0.3403 -0.0056 0.1018  0.0233  105 ASP   B O   
5507 C  CB  A ASP   B 105 ? 0.4358 0.3947 0.4323 -0.0088 0.1916  0.0274  105 ASP   B CB  
5508 C  CB  B ASP   B 105 ? 0.4147 0.3850 0.4091 -0.0015 0.1034  0.0216  105 ASP   B CB  
5509 C  CG  A ASP   B 105 ? 0.4450 0.4092 0.4983 -0.0047 0.1946  0.0128  105 ASP   B CG  
5510 C  CG  B ASP   B 105 ? 0.4149 0.3881 0.4402 -0.0016 0.1093  0.0181  105 ASP   B CG  
5511 O  OD1 A ASP   B 105 ? 0.4408 0.4129 0.5104 -0.0114 0.2079  0.0160  105 ASP   B OD1 
5512 O  OD1 B ASP   B 105 ? 0.4127 0.3880 0.4502 -0.0049 0.1128  0.0191  105 ASP   B OD1 
5513 O  OD2 A ASP   B 105 ? 0.4523 0.4152 0.5372 0.0046  0.1838  0.0008  105 ASP   B OD2 
5514 O  OD2 B ASP   B 105 ? 0.4137 0.3896 0.4542 -0.0008 0.1126  0.0173  105 ASP   B OD2 
5523 N  N   A ILE   B 106 ? 0.3908 0.3206 0.3266 -0.0332 0.1812  0.0410  106 ILE   B N   
5524 N  N   B ILE   B 106 ? 0.3886 0.3502 0.3430 -0.0085 0.0916  0.0167  106 ILE   B N   
5525 C  CA  A ILE   B 106 ? 0.3748 0.2928 0.3323 -0.0479 0.1825  0.0389  106 ILE   B CA  
5526 C  CA  B ILE   B 106 ? 0.3762 0.3383 0.3405 -0.0106 0.0907  0.0097  106 ILE   B CA  
5527 C  C   A ILE   B 106 ? 0.3467 0.2828 0.3244 -0.0417 0.1762  0.0292  106 ILE   B C   
5528 C  C   B ILE   B 106 ? 0.3569 0.3310 0.3326 -0.0061 0.0895  0.0023  106 ILE   B C   
5529 O  O   A ILE   B 106 ? 0.3370 0.2608 0.3213 -0.0444 0.1762  0.0267  106 ILE   B O   
5530 O  O   B ILE   B 106 ? 0.3544 0.3251 0.3279 -0.0071 0.0853  -0.0022 106 ILE   B O   
5531 C  CB  A ILE   B 106 ? 0.3930 0.2857 0.3533 -0.0582 0.1698  0.0388  106 ILE   B CB  
5532 C  CB  B ILE   B 106 ? 0.3844 0.3382 0.3470 -0.0152 0.0879  0.0089  106 ILE   B CB  
5533 C  CG1 A ILE   B 106 ? 0.4017 0.2882 0.3666 -0.0556 0.1584  0.0277  106 ILE   B CG1 
5534 C  CG1 B ILE   B 106 ? 0.3900 0.3398 0.3529 -0.0147 0.0829  0.0063  106 ILE   B CG1 
5535 C  CG2 A ILE   B 106 ? 0.3973 0.2858 0.3703 -0.0635 0.1693  0.0451  106 ILE   B CG2 
5536 C  CG2 B ILE   B 106 ? 0.3860 0.3399 0.3553 -0.0173 0.0893  0.0097  106 ILE   B CG2 
5537 C  CD1 A ILE   B 106 ? 0.4067 0.2910 0.3636 -0.0528 0.1574  0.0265  106 ILE   B CD1 
5538 C  CD1 B ILE   B 106 ? 0.3935 0.3410 0.3541 -0.0135 0.0816  0.0060  106 ILE   B CD1 
5561 N  N   A GLN   B 107 ? 0.3287 0.2972 0.3410 -0.0385 0.1626  0.0312  107 GLN   B N   
5562 N  N   B GLN   B 107 ? 0.3410 0.3312 0.3436 -0.0040 0.0878  0.0030  107 GLN   B N   
5563 C  CA  A GLN   B 107 ? 0.3087 0.3100 0.3583 -0.0321 0.1435  0.0308  107 GLN   B CA  
5564 C  CA  B GLN   B 107 ? 0.3241 0.3287 0.3574 -0.0021 0.0841  0.0078  107 GLN   B CA  
5565 C  C   A GLN   B 107 ? 0.2801 0.2903 0.3299 -0.0115 0.1153  0.0198  107 GLN   B C   
5566 C  C   B GLN   B 107 ? 0.2917 0.3030 0.3264 0.0055  0.0872  0.0078  107 GLN   B C   
5567 O  O   A GLN   B 107 ? 0.2716 0.2887 0.3537 -0.0063 0.0920  0.0096  107 GLN   B O   
5568 O  O   B GLN   B 107 ? 0.2888 0.3050 0.3360 0.0074  0.0766  0.0027  107 GLN   B O   
5569 C  CB  A GLN   B 107 ? 0.3333 0.3464 0.4212 -0.0358 0.1236  0.0298  107 GLN   B CB  
5570 C  CB  B GLN   B 107 ? 0.3431 0.3523 0.4048 -0.0053 0.0711  0.0087  107 GLN   B CB  
5571 C  CG  A GLN   B 107 ? 0.3608 0.3782 0.4895 -0.0302 0.0914  0.0253  107 GLN   B CG  
5572 C  CG  B GLN   B 107 ? 0.3611 0.3728 0.4566 -0.0041 0.0548  0.0086  107 GLN   B CG  
5573 C  CD  A GLN   B 107 ? 0.3819 0.4010 0.5396 -0.0261 0.0678  0.0240  107 GLN   B CD  
5574 C  CD  B GLN   B 107 ? 0.3756 0.3876 0.4953 -0.0030 0.0418  0.0095  107 GLN   B CD  
5575 O  OE1 A GLN   B 107 ? 0.3875 0.4100 0.5597 -0.0192 0.0624  0.0205  107 GLN   B OE1 
5576 O  OE1 B GLN   B 107 ? 0.3791 0.3931 0.5097 -0.0002 0.0397  0.0093  107 GLN   B OE1 
5577 N  NE2 A GLN   B 107 ? 0.3927 0.4078 0.5584 -0.0256 0.0590  0.0276  107 GLN   B NE2 
5578 N  NE2 B GLN   B 107 ? 0.3833 0.3926 0.5109 -0.0028 0.0372  0.0113  107 GLN   B NE2 
5595 N  N   . LEU   B 108 ? 0.2605 0.2742 0.2977 0.0155  0.0969  0.0122  108 LEU   B N   
5596 C  CA  . LEU   B 108 ? 0.2345 0.2427 0.2631 0.0277  0.0744  0.0245  108 LEU   B CA  
5597 C  C   . LEU   B 108 ? 0.1953 0.1927 0.2500 0.0243  0.0446  0.0344  108 LEU   B C   
5598 O  O   . LEU   B 108 ? 0.1943 0.1761 0.2398 0.0241  0.0395  0.0288  108 LEU   B O   
5599 C  CB  . LEU   B 108 ? 0.2501 0.2636 0.2506 0.0293  0.0756  0.0365  108 LEU   B CB  
5600 C  CG  . LEU   B 108 ? 0.2685 0.2952 0.2592 0.0335  0.0692  0.0146  108 LEU   B CG  
5601 C  CD1 . LEU   B 108 ? 0.2806 0.3119 0.2517 0.0235  0.0679  0.0137  108 LEU   B CD1 
5602 C  CD2 . LEU   B 108 ? 0.2812 0.3066 0.2698 0.0434  0.0609  0.0013  108 LEU   B CD2 
5615 N  N   . LEU   B 109 ? 0.1756 0.1739 0.2510 0.0132  0.0431  0.0258  109 LEU   B N   
5616 C  CA  . LEU   B 109 ? 0.1574 0.1479 0.2577 0.0086  0.0380  0.0338  109 LEU   B CA  
5617 C  C   . LEU   B 109 ? 0.1467 0.1334 0.2586 0.0012  0.0352  0.0224  109 LEU   B C   
5618 O  O   . LEU   B 109 ? 0.1460 0.1328 0.2480 0.0015  0.0369  0.0336  109 LEU   B O   
5619 C  CB  . LEU   B 109 ? 0.1676 0.1401 0.2674 0.0058  0.0276  0.0494  109 LEU   B CB  
5620 C  CG  . LEU   B 109 ? 0.1632 0.1388 0.2578 -0.0006 0.0237  0.0356  109 LEU   B CG  
5621 C  CD1 . LEU   B 109 ? 0.1549 0.1472 0.2445 0.0143  0.0271  0.0329  109 LEU   B CD1 
5622 C  CD2 . LEU   B 109 ? 0.1772 0.1416 0.2728 -0.0007 0.0129  0.0325  109 LEU   B CD2 
5634 N  N   . LYS   B 110 ? 0.1430 0.1325 0.2530 -0.0060 0.0341  0.0254  110 LYS   B N   
5635 C  CA  . LYS   B 110 ? 0.1428 0.1318 0.2563 -0.0022 0.0269  0.0181  110 LYS   B CA  
5636 C  C   . LYS   B 110 ? 0.1404 0.1347 0.2438 -0.0018 0.0331  0.0109  110 LYS   B C   
5637 O  O   . LYS   B 110 ? 0.1362 0.1354 0.2337 -0.0035 0.0207  0.0098  110 LYS   B O   
5638 C  CB  . LYS   B 110 ? 0.1439 0.1316 0.2728 -0.0048 0.0333  0.0180  110 LYS   B CB  
5639 C  CG  . LYS   B 110 ? 0.1464 0.1358 0.2763 -0.0062 0.0147  0.0216  110 LYS   B CG  
5640 C  CD  . LYS   B 110 ? 0.1488 0.1337 0.2905 -0.0106 0.0147  0.0211  110 LYS   B CD  
5641 C  CE  . LYS   B 110 ? 0.1467 0.1507 0.3056 -0.0031 0.0158  0.0146  110 LYS   B CE  
5642 N  NZ  . LYS   B 110 ? 0.1486 0.1649 0.2990 0.0051  0.0058  0.0069  110 LYS   B NZ  
5656 N  N   . SER   B 111 ? 0.1415 0.1344 0.2531 -0.0051 0.0371  0.0210  111 SER   B N   
5657 C  CA  . SER   B 111 ? 0.1506 0.1385 0.2400 -0.0012 0.0332  0.0198  111 SER   B CA  
5658 C  C   . SER   B 111 ? 0.1487 0.1282 0.2302 -0.0012 0.0120  0.0131  111 SER   B C   
5659 O  O   . SER   B 111 ? 0.1399 0.1308 0.2367 0.0019  0.0132  0.0096  111 SER   B O   
5660 C  CB  . SER   B 111 ? 0.1604 0.1609 0.2551 0.0081  0.0460  0.0295  111 SER   B CB  
5661 O  OG  . SER   B 111 ? 0.1784 0.1919 0.2658 0.0118  0.0527  0.0384  111 SER   B OG  
5667 N  N   . ALA   B 112 ? 0.1372 0.1362 0.2287 0.0032  0.0272  0.0258  112 ALA   B N   
5668 C  CA  . ALA   B 112 ? 0.1390 0.1426 0.2105 0.0048  0.0055  0.0087  112 ALA   B CA  
5669 C  C   . ALA   B 112 ? 0.1277 0.1335 0.2039 0.0019  0.0084  0.0060  112 ALA   B C   
5670 O  O   . ALA   B 112 ? 0.1280 0.1312 0.2114 -0.0075 0.0081  0.0042  112 ALA   B O   
5671 C  CB  . ALA   B 112 ? 0.1397 0.1482 0.2321 0.0074  0.0127  0.0160  112 ALA   B CB  
5677 N  N   . TYR   B 113 ? 0.1250 0.1236 0.2230 -0.0030 0.0128  0.0088  113 TYR   B N   
5678 C  CA  . TYR   B 113 ? 0.1235 0.1198 0.2142 -0.0025 0.0118  0.0059  113 TYR   B CA  
5679 C  C   . TYR   B 113 ? 0.1214 0.1189 0.2087 -0.0122 0.0112  0.0049  113 TYR   B C   
5680 O  O   . TYR   B 113 ? 0.1272 0.1188 0.1991 -0.0093 0.0011  -0.0002 113 TYR   B O   
5681 C  CB  . TYR   B 113 ? 0.1290 0.1133 0.2138 -0.0037 0.0195  0.0076  113 TYR   B CB  
5682 C  CG  . TYR   B 113 ? 0.1340 0.1186 0.2301 -0.0061 0.0133  0.0150  113 TYR   B CG  
5683 C  CD1 . TYR   B 113 ? 0.1393 0.1192 0.2469 -0.0071 0.0143  0.0161  113 TYR   B CD1 
5684 C  CD2 . TYR   B 113 ? 0.1392 0.1196 0.2330 -0.0055 0.0081  0.0131  113 TYR   B CD2 
5685 C  CE1 . TYR   B 113 ? 0.1373 0.1245 0.2303 -0.0031 0.0213  0.0049  113 TYR   B CE1 
5686 C  CE2 . TYR   B 113 ? 0.1425 0.1105 0.2462 -0.0031 0.0057  0.0163  113 TYR   B CE2 
5687 C  CZ  . TYR   B 113 ? 0.1316 0.1192 0.2447 0.0062  0.0096  0.0146  113 TYR   B CZ  
5688 O  OH  . TYR   B 113 ? 0.1459 0.1176 0.2653 0.0046  0.0174  0.0138  113 TYR   B OH  
5698 N  N   . GLU   B 114 ? 0.1244 0.1115 0.2156 -0.0070 0.0110  0.0089  114 GLU   B N   
5699 C  CA  . GLU   B 114 ? 0.1201 0.1108 0.2173 0.0022  0.0081  0.0030  114 GLU   B CA  
5700 C  C   . GLU   B 114 ? 0.1227 0.1124 0.2110 0.0024  0.0088  0.0058  114 GLU   B C   
5701 O  O   . GLU   B 114 ? 0.1212 0.1134 0.2202 0.0027  0.0051  0.0100  114 GLU   B O   
5702 C  CB  . GLU   B 114 ? 0.1240 0.1206 0.2389 -0.0022 0.0160  0.0088  114 GLU   B CB  
5703 C  CG  . GLU   B 114 ? 0.1260 0.1184 0.2371 -0.0034 0.0160  0.0094  114 GLU   B CG  
5704 C  CD  . GLU   B 114 ? 0.1247 0.1212 0.2413 -0.0041 0.0096  0.0115  114 GLU   B CD  
5705 O  OE1 . GLU   B 114 ? 0.1245 0.1367 0.2532 -0.0096 0.0234  0.0159  114 GLU   B OE1 
5706 O  OE2 . GLU   B 114 ? 0.1274 0.1393 0.2408 -0.0159 0.0087  0.0127  114 GLU   B OE2 
5713 N  N   . ASN   B 115 ? 0.1289 0.1074 0.2078 -0.0027 -0.0001 0.0044  115 ASN   B N   
5714 C  CA  . ASN   B 115 ? 0.1242 0.1168 0.1876 -0.0061 0.0031  0.0106  115 ASN   B CA  
5715 C  C   . ASN   B 115 ? 0.1166 0.1154 0.1950 -0.0129 -0.0012 0.0041  115 ASN   B C   
5716 O  O   . ASN   B 115 ? 0.1341 0.1168 0.1982 -0.0106 -0.0012 0.0053  115 ASN   B O   
5717 C  CB  . ASN   B 115 ? 0.1328 0.1321 0.1956 -0.0066 0.0020  0.0118  115 ASN   B CB  
5718 C  CG  . ASN   B 115 ? 0.1436 0.1370 0.1953 0.0036  -0.0038 0.0010  115 ASN   B CG  
5719 O  OD1 . ASN   B 115 ? 0.1820 0.1482 0.2149 -0.0004 0.0099  -0.0085 115 ASN   B OD1 
5720 N  ND2 . ASN   B 115 ? 0.1429 0.1503 0.1916 -0.0038 0.0049  0.0095  115 ASN   B ND2 
5727 N  N   . PHE   B 116 ? 0.1210 0.1144 0.1866 -0.0073 0.0021  0.0037  116 PHE   B N   
5728 C  CA  . PHE   B 116 ? 0.1301 0.1198 0.1930 -0.0103 -0.0065 0.0071  116 PHE   B CA  
5729 C  C   . PHE   B 116 ? 0.1281 0.1081 0.1914 -0.0178 -0.0077 0.0080  116 PHE   B C   
5730 O  O   . PHE   B 116 ? 0.1309 0.1213 0.1934 -0.0072 -0.0077 0.0076  116 PHE   B O   
5731 C  CB  . PHE   B 116 ? 0.1285 0.1145 0.1808 -0.0086 -0.0203 0.0075  116 PHE   B CB  
5732 C  CG  . PHE   B 116 ? 0.1214 0.1128 0.1859 -0.0057 -0.0049 0.0067  116 PHE   B CG  
5733 C  CD1 . PHE   B 116 ? 0.1329 0.1205 0.2006 -0.0047 -0.0027 0.0048  116 PHE   B CD1 
5734 C  CD2 . PHE   B 116 ? 0.1223 0.1207 0.1948 -0.0047 -0.0003 -0.0009 116 PHE   B CD2 
5735 C  CE1 . PHE   B 116 ? 0.1334 0.1247 0.1961 -0.0009 -0.0147 0.0091  116 PHE   B CE1 
5736 C  CE2 . PHE   B 116 ? 0.1281 0.1231 0.1873 -0.0029 -0.0012 0.0075  116 PHE   B CE2 
5737 C  CZ  . PHE   B 116 ? 0.1187 0.1234 0.1919 -0.0007 -0.0096 0.0103  116 PHE   B CZ  
5747 N  N   . ASN   B 117 ? 0.1257 0.1164 0.2063 -0.0104 -0.0066 0.0123  117 ASN   B N   
5748 C  CA  . ASN   B 117 ? 0.1311 0.1165 0.2072 -0.0017 -0.0131 0.0073  117 ASN   B CA  
5749 C  C   . ASN   B 117 ? 0.1357 0.1191 0.2074 -0.0002 -0.0157 0.0070  117 ASN   B C   
5750 O  O   . ASN   B 117 ? 0.1445 0.1170 0.2470 -0.0051 -0.0390 0.0136  117 ASN   B O   
5751 C  CB  . ASN   B 117 ? 0.1328 0.1153 0.2133 -0.0010 -0.0026 -0.0058 117 ASN   B CB  
5752 C  CG  . ASN   B 117 ? 0.1290 0.1212 0.2240 0.0057  0.0012  -0.0050 117 ASN   B CG  
5753 O  OD1 . ASN   B 117 ? 0.1469 0.1190 0.2351 -0.0087 0.0020  -0.0016 117 ASN   B OD1 
5754 N  ND2 . ASN   B 117 ? 0.1307 0.1267 0.2121 0.0005  -0.0008 -0.0066 117 ASN   B ND2 
5761 N  N   . GLN   B 118 ? 0.1337 0.1178 0.1987 -0.0074 -0.0171 0.0044  118 GLN   B N   
5762 C  CA  . GLN   B 118 ? 0.1414 0.1124 0.2193 0.0008  -0.0125 0.0045  118 GLN   B CA  
5763 C  C   . GLN   B 118 ? 0.1455 0.1135 0.2225 0.0039  -0.0047 0.0002  118 GLN   B C   
5764 O  O   . GLN   B 118 ? 0.1621 0.1104 0.2633 -0.0037 0.0010  0.0033  118 GLN   B O   
5765 C  CB  . GLN   B 118 ? 0.1458 0.1223 0.2347 0.0027  -0.0130 0.0015  118 GLN   B CB  
5766 C  CG  . GLN   B 118 ? 0.1518 0.1221 0.2200 0.0032  -0.0094 -0.0081 118 GLN   B CG  
5767 C  CD  . GLN   B 118 ? 0.1554 0.1165 0.2205 0.0020  -0.0178 -0.0135 118 GLN   B CD  
5768 O  OE1 . GLN   B 118 ? 0.1651 0.1205 0.2448 0.0048  -0.0011 0.0049  118 GLN   B OE1 
5769 N  NE2 . GLN   B 118 ? 0.1680 0.1232 0.2268 -0.0006 -0.0121 -0.0014 118 GLN   B NE2 
5778 N  N   . HIS   B 119 ? 0.1444 0.1184 0.1825 -0.0072 -0.0161 0.0100  119 HIS   B N   
5779 C  CA  . HIS   B 119 ? 0.1513 0.1307 0.1768 -0.0035 -0.0204 0.0061  119 HIS   B CA  
5780 C  C   . HIS   B 119 ? 0.1586 0.1269 0.1673 -0.0071 -0.0327 0.0110  119 HIS   B C   
5781 O  O   . HIS   B 119 ? 0.1700 0.1292 0.2019 -0.0244 -0.0244 0.0100  119 HIS   B O   
5782 C  CB  . HIS   B 119 ? 0.1603 0.1424 0.1835 -0.0037 -0.0227 0.0016  119 HIS   B CB  
5783 C  CG  . HIS   B 119 ? 0.1668 0.1647 0.2068 0.0048  -0.0416 -0.0175 119 HIS   B CG  
5784 N  ND1 . HIS   B 119 ? 0.1781 0.1783 0.2307 0.0020  -0.0500 -0.0321 119 HIS   B ND1 
5785 C  CD2 . HIS   B 119 ? 0.1814 0.1805 0.2122 0.0324  -0.0500 -0.0237 119 HIS   B CD2 
5786 C  CE1 . HIS   B 119 ? 0.1973 0.1910 0.2413 0.0138  -0.0578 -0.0471 119 HIS   B CE1 
5787 N  NE2 . HIS   B 119 ? 0.1963 0.2022 0.2303 0.0295  -0.0544 -0.0361 119 HIS   B NE2 
5795 N  N   . GLU   B 120 ? 0.1790 0.1351 0.1721 -0.0117 -0.0385 0.0148  120 GLU   B N   
5796 C  CA  . GLU   B 120 ? 0.2063 0.1460 0.2043 -0.0076 -0.0529 0.0312  120 GLU   B CA  
5797 C  C   . GLU   B 120 ? 0.1840 0.1376 0.1904 -0.0191 -0.0428 0.0295  120 GLU   B C   
5798 O  O   . GLU   B 120 ? 0.1745 0.1511 0.1924 -0.0170 -0.0425 0.0175  120 GLU   B O   
5799 C  CB  . GLU   B 120 ? 0.2822 0.1840 0.2769 0.0182  -0.0876 0.0618  120 GLU   B CB  
5800 C  CG  . GLU   B 120 ? 0.3435 0.2600 0.3677 0.0300  -0.1086 0.0782  120 GLU   B CG  
5801 C  CD  . GLU   B 120 ? 0.3806 0.3351 0.4708 0.0329  -0.1123 0.0899  120 GLU   B CD  
5802 O  OE1 . GLU   B 120 ? 0.4023 0.3561 0.5085 0.0278  -0.1043 0.0984  120 GLU   B OE1 
5803 O  OE2 . GLU   B 120 ? 0.4024 0.3904 0.5205 0.0349  -0.1104 0.0855  120 GLU   B OE2 
5810 N  N   . VAL   B 121 ? 0.1702 0.1326 0.1849 -0.0294 -0.0277 0.0249  121 VAL   B N   
5811 C  CA  . VAL   B 121 ? 0.1658 0.1491 0.1687 -0.0211 -0.0314 0.0189  121 VAL   B CA  
5812 C  C   . VAL   B 121 ? 0.1561 0.1431 0.1564 -0.0247 -0.0269 0.0183  121 VAL   B C   
5813 O  O   . VAL   B 121 ? 0.1645 0.1352 0.1771 -0.0351 -0.0360 0.0112  121 VAL   B O   
5814 C  CB  . VAL   B 121 ? 0.1882 0.1853 0.1718 -0.0096 -0.0322 0.0165  121 VAL   B CB  
5815 C  CG1 . VAL   B 121 ? 0.1961 0.1979 0.2117 -0.0200 -0.0146 0.0060  121 VAL   B CG1 
5816 C  CG2 . VAL   B 121 ? 0.2150 0.2150 0.1831 0.0001  -0.0361 0.0072  121 VAL   B CG2 
5826 N  N   . LEU   B 122 ? 0.1488 0.1326 0.1586 -0.0189 -0.0256 0.0179  122 LEU   B N   
5827 C  CA  . LEU   B 122 ? 0.1399 0.1409 0.1542 -0.0235 -0.0260 0.0185  122 LEU   B CA  
5828 C  C   . LEU   B 122 ? 0.1405 0.1274 0.1627 -0.0292 -0.0215 0.0128  122 LEU   B C   
5829 O  O   . LEU   B 122 ? 0.1504 0.1292 0.1915 -0.0340 -0.0283 0.0033  122 LEU   B O   
5830 C  CB  . LEU   B 122 ? 0.1637 0.1467 0.1800 -0.0079 -0.0260 0.0166  122 LEU   B CB  
5831 C  CG  . LEU   B 122 ? 0.1481 0.1525 0.1928 -0.0184 -0.0130 0.0109  122 LEU   B CG  
5832 C  CD1 . LEU   B 122 ? 0.1533 0.1772 0.2079 -0.0224 -0.0211 0.0092  122 LEU   B CD1 
5833 C  CD2 . LEU   B 122 ? 0.1580 0.1570 0.1641 -0.0112 -0.0056 -0.0041 122 LEU   B CD2 
5845 N  N   . LEU   B 123 ? 0.1456 0.1201 0.1471 -0.0253 -0.0196 0.0082  123 LEU   B N   
5846 C  CA  . LEU   B 123 ? 0.1486 0.1217 0.1550 -0.0211 -0.0218 0.0038  123 LEU   B CA  
5847 C  C   . LEU   B 123 ? 0.1459 0.1204 0.1462 -0.0270 -0.0215 0.0032  123 LEU   B C   
5848 O  O   . LEU   B 123 ? 0.1518 0.1222 0.1458 -0.0279 -0.0201 0.0021  123 LEU   B O   
5849 C  CB  . LEU   B 123 ? 0.1509 0.1257 0.1691 -0.0220 -0.0148 -0.0001 123 LEU   B CB  
5850 C  CG  . LEU   B 123 ? 0.1466 0.1301 0.1769 -0.0171 -0.0090 0.0098  123 LEU   B CG  
5851 C  CD1 . LEU   B 123 ? 0.1602 0.1333 0.1969 -0.0127 -0.0053 -0.0037 123 LEU   B CD1 
5852 C  CD2 . LEU   B 123 ? 0.1541 0.1387 0.1925 -0.0177 -0.0054 0.0143  123 LEU   B CD2 
5864 N  N   . ALA   B 124 ? 0.1403 0.1143 0.1503 -0.0199 -0.0097 -0.0020 124 ALA   B N   
5865 C  CA  . ALA   B 124 ? 0.1317 0.1196 0.1628 -0.0193 -0.0183 -0.0063 124 ALA   B CA  
5866 C  C   . ALA   B 124 ? 0.1248 0.1189 0.1528 -0.0224 -0.0142 0.0054  124 ALA   B C   
5867 O  O   . ALA   B 124 ? 0.1422 0.1198 0.1689 -0.0208 -0.0194 0.0014  124 ALA   B O   
5868 C  CB  . ALA   B 124 ? 0.1388 0.1278 0.1715 -0.0071 -0.0093 0.0043  124 ALA   B CB  
5874 N  N   . PRO   B 125 ? 0.1359 0.1190 0.1563 -0.0159 -0.0178 0.0130  125 PRO   B N   
5875 C  CA  . PRO   B 125 ? 0.1483 0.1236 0.1655 -0.0146 -0.0150 0.0259  125 PRO   B CA  
5876 C  C   . PRO   B 125 ? 0.1425 0.1193 0.1801 -0.0082 -0.0054 0.0129  125 PRO   B C   
5877 O  O   . PRO   B 125 ? 0.1488 0.1177 0.1978 -0.0123 -0.0056 0.0139  125 PRO   B O   
5878 C  CB  . PRO   B 125 ? 0.1476 0.1451 0.1898 -0.0226 -0.0185 0.0388  125 PRO   B CB  
5879 C  CG  . PRO   B 125 ? 0.1544 0.1489 0.1747 -0.0336 -0.0190 0.0200  125 PRO   B CG  
5880 C  CD  . PRO   B 125 ? 0.1512 0.1296 0.1609 -0.0295 -0.0113 0.0117  125 PRO   B CD  
5888 N  N   . LEU   B 126 ? 0.1445 0.1163 0.2070 -0.0111 0.0068  0.0193  126 LEU   B N   
5889 C  CA  . LEU   B 126 ? 0.1498 0.1243 0.2210 -0.0069 0.0220  0.0240  126 LEU   B CA  
5890 C  C   . LEU   B 126 ? 0.1415 0.1329 0.2163 -0.0036 0.0283  0.0292  126 LEU   B C   
5891 O  O   . LEU   B 126 ? 0.1655 0.1601 0.2390 0.0134  -0.0020 0.0022  126 LEU   B O   
5892 C  CB  . LEU   B 126 ? 0.1667 0.1254 0.2465 -0.0184 0.0214  0.0136  126 LEU   B CB  
5893 C  CG  . LEU   B 126 ? 0.1841 0.1341 0.2585 -0.0255 0.0189  -0.0098 126 LEU   B CG  
5894 C  CD1 . LEU   B 126 ? 0.2014 0.1449 0.3053 -0.0196 0.0196  -0.0183 126 LEU   B CD1 
5895 C  CD2 . LEU   B 126 ? 0.1839 0.1445 0.2636 -0.0376 0.0115  -0.0099 126 LEU   B CD2 
5907 N  N   . LEU   B 127 ? 0.1418 0.1228 0.2323 0.0019  0.0298  0.0143  127 LEU   B N   
5908 C  CA  . LEU   B 127 ? 0.1443 0.1324 0.2387 -0.0007 0.0373  0.0218  127 LEU   B CA  
5909 C  C   . LEU   B 127 ? 0.1369 0.1248 0.2392 0.0012  0.0194  0.0307  127 LEU   B C   
5910 O  O   . LEU   B 127 ? 0.1414 0.1315 0.2489 -0.0117 0.0118  0.0299  127 LEU   B O   
5911 C  CB  . LEU   B 127 ? 0.1558 0.1288 0.2561 -0.0016 0.0279  0.0303  127 LEU   B CB  
5912 C  CG  . LEU   B 127 ? 0.1606 0.1269 0.2636 0.0045  0.0239  0.0273  127 LEU   B CG  
5913 C  CD1 . LEU   B 127 ? 0.1742 0.1292 0.2584 0.0049  0.0146  0.0207  127 LEU   B CD1 
5914 C  CD2 . LEU   B 127 ? 0.1681 0.1376 0.2605 -0.0150 0.0213  0.0316  127 LEU   B CD2 
5926 N  N   . SER   B 128 ? 0.1367 0.1306 0.2319 -0.0013 0.0042  0.0232  128 SER   B N   
5927 C  CA  . SER   B 128 ? 0.1572 0.1377 0.2327 0.0073  -0.0051 0.0305  128 SER   B CA  
5928 C  C   . SER   B 128 ? 0.1706 0.1423 0.2605 0.0107  -0.0303 0.0263  128 SER   B C   
5929 O  O   . SER   B 128 ? 0.1864 0.1438 0.2898 0.0065  -0.0257 0.0422  128 SER   B O   
5930 C  CB  . SER   B 128 ? 0.1682 0.1423 0.2287 0.0073  0.0039  0.0430  128 SER   B CB  
5931 O  OG  . SER   B 128 ? 0.1699 0.1548 0.2325 0.0134  0.0138  0.0407  128 SER   B OG  
5937 N  N   . ALA   B 129 ? 0.1858 0.1467 0.2814 0.0237  -0.0177 0.0122  129 ALA   B N   
5938 C  CA  . ALA   B 129 ? 0.1956 0.1514 0.2860 0.0284  -0.0137 0.0061  129 ALA   B CA  
5939 C  C   . ALA   B 129 ? 0.1848 0.1464 0.2746 0.0194  0.0073  0.0112  129 ALA   B C   
5940 O  O   . ALA   B 129 ? 0.1772 0.1492 0.2791 0.0193  -0.0035 0.0123  129 ALA   B O   
5941 C  CB  . ALA   B 129 ? 0.2199 0.1764 0.3132 0.0282  0.0014  0.0011  129 ALA   B CB  
5947 N  N   . GLY   B 130 ? 0.1820 0.1442 0.2702 0.0262  0.0052  0.0029  130 GLY   B N   
5948 C  CA  . GLY   B 130 ? 0.1894 0.1534 0.2845 0.0199  0.0282  0.0016  130 GLY   B CA  
5949 C  C   . GLY   B 130 ? 0.1941 0.1594 0.2757 0.0131  0.0184  0.0061  130 GLY   B C   
5950 O  O   . GLY   B 130 ? 0.2038 0.1712 0.2774 0.0161  0.0145  0.0161  130 GLY   B O   
5954 N  N   . ILE   B 131 ? 0.1884 0.1757 0.2844 0.0275  0.0101  0.0010  131 ILE   B N   
5955 C  CA  . ILE   B 131 ? 0.2042 0.1929 0.2860 0.0261  -0.0054 0.0191  131 ILE   B CA  
5956 C  C   . ILE   B 131 ? 0.2138 0.1815 0.2612 0.0175  0.0010  0.0268  131 ILE   B C   
5957 O  O   . ILE   B 131 ? 0.2411 0.2010 0.2722 0.0195  -0.0107 0.0273  131 ILE   B O   
5958 C  CB  . ILE   B 131 ? 0.2084 0.2247 0.3274 0.0251  -0.0122 0.0307  131 ILE   B CB  
5959 C  CG1 . ILE   B 131 ? 0.2159 0.2380 0.3459 0.0027  -0.0054 0.0368  131 ILE   B CG1 
5960 C  CG2 . ILE   B 131 ? 0.2094 0.2447 0.3462 0.0326  -0.0040 0.0263  131 ILE   B CG2 
5961 C  CD1 . ILE   B 131 ? 0.2232 0.2551 0.3635 -0.0154 -0.0092 0.0412  131 ILE   B CD1 
5973 N  N   . PHE   B 132 ? 0.1938 0.1568 0.2445 0.0122  0.0160  0.0314  132 PHE   B N   
5974 C  CA  . PHE   B 132 ? 0.2096 0.1614 0.2487 0.0061  0.0414  0.0235  132 PHE   B CA  
5975 C  C   . PHE   B 132 ? 0.2296 0.1770 0.2628 0.0148  0.0510  0.0239  132 PHE   B C   
5976 O  O   . PHE   B 132 ? 0.2497 0.1954 0.2872 0.0090  0.0643  0.0308  132 PHE   B O   
5977 C  CB  . PHE   B 132 ? 0.1959 0.1597 0.2265 0.0063  0.0461  0.0225  132 PHE   B CB  
5978 C  CG  . PHE   B 132 ? 0.1930 0.1615 0.2236 0.0130  0.0369  0.0197  132 PHE   B CG  
5979 C  CD1 . PHE   B 132 ? 0.1961 0.1613 0.2481 0.0158  0.0308  0.0263  132 PHE   B CD1 
5980 C  CD2 . PHE   B 132 ? 0.1946 0.1709 0.2052 0.0249  0.0350  0.0317  132 PHE   B CD2 
5981 C  CE1 . PHE   B 132 ? 0.2017 0.1739 0.2600 0.0084  0.0215  0.0290  132 PHE   B CE1 
5982 C  CE2 . PHE   B 132 ? 0.1992 0.1770 0.2094 0.0266  0.0209  0.0337  132 PHE   B CE2 
5983 C  CZ  . PHE   B 132 ? 0.2001 0.1771 0.2411 0.0133  0.0044  0.0376  132 PHE   B CZ  
5993 N  N   . GLY   B 133 ? 0.2246 0.1663 0.2637 0.0099  0.0303  0.0475  133 GLY   B N   
5994 C  CA  . GLY   B 133 ? 0.2341 0.1808 0.2792 -0.0105 0.0266  0.0473  133 GLY   B CA  
5995 C  C   . GLY   B 133 ? 0.2411 0.1856 0.2807 -0.0250 0.0314  0.0522  133 GLY   B C   
5996 O  O   . GLY   B 133 ? 0.2615 0.1997 0.3122 -0.0357 0.0369  0.0621  133 GLY   B O   
6000 N  N   . ALA   B 134 ? 0.2249 0.1863 0.2622 -0.0240 0.0324  0.0360  134 ALA   B N   
6001 C  CA  . ALA   B 134 ? 0.2207 0.1833 0.2719 -0.0148 0.0417  0.0242  134 ALA   B CA  
6002 C  C   . ALA   B 134 ? 0.2232 0.1735 0.2779 -0.0109 0.0374  0.0392  134 ALA   B C   
6003 O  O   . ALA   B 134 ? 0.2262 0.1953 0.2873 0.0042  0.0290  0.0331  134 ALA   B O   
6004 C  CB  . ALA   B 134 ? 0.2223 0.1832 0.2766 -0.0070 0.0406  0.0170  134 ALA   B CB  
6010 N  N   . ASP   B 135 ? 0.2368 0.1679 0.2834 -0.0183 0.0257  0.0453  135 ASP   B N   
6011 C  CA  . ASP   B 135 ? 0.2505 0.1615 0.3014 -0.0119 0.0091  0.0463  135 ASP   B CA  
6012 C  C   . ASP   B 135 ? 0.2308 0.1518 0.2858 -0.0047 0.0025  0.0425  135 ASP   B C   
6013 O  O   . ASP   B 135 ? 0.2183 0.1482 0.2939 -0.0042 0.0115  0.0319  135 ASP   B O   
6014 C  CB  . ASP   B 135 ? 0.2830 0.1717 0.3287 -0.0260 0.0080  0.0517  135 ASP   B CB  
6015 C  CG  . ASP   B 135 ? 0.3091 0.1714 0.3640 -0.0457 0.0114  0.0398  135 ASP   B CG  
6016 O  OD1 . ASP   B 135 ? 0.3179 0.1502 0.3742 -0.0299 -0.0058 0.0302  135 ASP   B OD1 
6017 O  OD2 . ASP   B 135 ? 0.3322 0.2059 0.4154 -0.0613 0.0223  0.0212  135 ASP   B OD2 
6022 N  N   . PRO   B 136 ? 0.2262 0.1546 0.2922 0.0166  -0.0138 0.0340  136 PRO   B N   
6023 C  CA  . PRO   B 136 ? 0.2037 0.1418 0.3016 0.0170  -0.0149 0.0163  136 PRO   B CA  
6024 C  C   . PRO   B 136 ? 0.1835 0.1278 0.3086 0.0133  -0.0047 0.0118  136 PRO   B C   
6025 O  O   . PRO   B 136 ? 0.1653 0.1270 0.3062 0.0053  0.0067  0.0176  136 PRO   B O   
6026 C  CB  . PRO   B 136 ? 0.2126 0.1640 0.3042 0.0286  -0.0218 0.0046  136 PRO   B CB  
6027 C  CG  . PRO   B 136 ? 0.2330 0.1765 0.3154 0.0305  -0.0130 0.0084  136 PRO   B CG  
6028 C  CD  . PRO   B 136 ? 0.2348 0.1708 0.3084 0.0339  -0.0090 0.0171  136 PRO   B CD  
6036 N  N   . ILE   B 137 ? 0.1925 0.1256 0.3163 0.0107  -0.0067 0.0146  137 ILE   B N   
6037 C  CA  . ILE   B 137 ? 0.1980 0.1215 0.3238 0.0036  -0.0033 0.0113  137 ILE   B CA  
6038 C  C   . ILE   B 137 ? 0.1900 0.1296 0.3195 -0.0088 0.0083  0.0172  137 ILE   B C   
6039 O  O   . ILE   B 137 ? 0.1811 0.1322 0.3058 -0.0127 0.0075  0.0144  137 ILE   B O   
6040 C  CB  . ILE   B 137 ? 0.2241 0.1288 0.3617 -0.0054 0.0047  0.0108  137 ILE   B CB  
6041 C  CG1 . ILE   B 137 ? 0.2423 0.1497 0.4023 0.0055  0.0131  -0.0050 137 ILE   B CG1 
6042 C  CG2 . ILE   B 137 ? 0.2319 0.1329 0.3700 -0.0294 0.0015  0.0168  137 ILE   B CG2 
6043 C  CD1 . ILE   B 137 ? 0.2633 0.1817 0.4361 0.0214  0.0074  -0.0042 137 ILE   B CD1 
6055 N  N   . HIS   B 138 ? 0.1953 0.1272 0.3214 -0.0059 0.0256  0.0194  138 HIS   B N   
6056 C  CA  . HIS   B 138 ? 0.2052 0.1404 0.3169 -0.0067 0.0362  0.0258  138 HIS   B CA  
6057 C  C   . HIS   B 138 ? 0.1822 0.1385 0.3035 -0.0069 0.0250  0.0268  138 HIS   B C   
6058 O  O   . HIS   B 138 ? 0.1717 0.1410 0.3221 -0.0013 0.0327  0.0362  138 HIS   B O   
6059 C  CB  . HIS   B 138 ? 0.2336 0.1530 0.3244 -0.0107 0.0544  0.0235  138 HIS   B CB  
6060 C  CG  . HIS   B 138 ? 0.2517 0.1653 0.3273 -0.0134 0.0808  0.0380  138 HIS   B CG  
6061 N  ND1 . HIS   B 138 ? 0.2598 0.1826 0.3498 -0.0082 0.0874  0.0304  138 HIS   B ND1 
6062 C  CD2 . HIS   B 138 ? 0.2672 0.1775 0.3157 -0.0130 0.0857  0.0316  138 HIS   B CD2 
6063 C  CE1 . HIS   B 138 ? 0.2636 0.1862 0.3416 -0.0059 0.0866  0.0314  138 HIS   B CE1 
6064 N  NE2 . HIS   B 138 ? 0.2739 0.1762 0.3274 -0.0016 0.0900  0.0218  138 HIS   B NE2 
6072 N  N   . SER   B 139 ? 0.1778 0.1220 0.3030 0.0015  0.0245  0.0211  139 SER   B N   
6073 C  CA  . SER   B 139 ? 0.1797 0.1199 0.2762 -0.0023 0.0238  0.0169  139 SER   B CA  
6074 C  C   . SER   B 139 ? 0.1540 0.1121 0.2801 -0.0041 0.0125  0.0132  139 SER   B C   
6075 O  O   . SER   B 139 ? 0.1524 0.1188 0.2738 -0.0007 0.0049  0.0179  139 SER   B O   
6076 C  CB  . SER   B 139 ? 0.1865 0.1247 0.2770 -0.0003 0.0059  0.0092  139 SER   B CB  
6077 O  OG  . SER   B 139 ? 0.1878 0.1198 0.2899 0.0004  -0.0019 0.0253  139 SER   B OG  
6083 N  N   . LEU   B 140 ? 0.1562 0.1077 0.2706 -0.0058 0.0192  0.0062  140 LEU   B N   
6084 C  CA  . LEU   B 140 ? 0.1510 0.1106 0.2667 -0.0029 0.0161  0.0064  140 LEU   B CA  
6085 C  C   . LEU   B 140 ? 0.1413 0.1158 0.2841 -0.0025 0.0084  0.0022  140 LEU   B C   
6086 O  O   . LEU   B 140 ? 0.1433 0.1251 0.2852 -0.0022 -0.0029 0.0117  140 LEU   B O   
6087 C  CB  . LEU   B 140 ? 0.1491 0.1157 0.2703 -0.0142 0.0167  -0.0072 140 LEU   B CB  
6088 C  CG  . LEU   B 140 ? 0.1589 0.1190 0.2772 -0.0143 0.0046  0.0065  140 LEU   B CG  
6089 C  CD1 . LEU   B 140 ? 0.1667 0.1246 0.2804 -0.0156 0.0187  0.0021  140 LEU   B CD1 
6090 C  CD2 . LEU   B 140 ? 0.1774 0.1295 0.2843 -0.0142 -0.0014 -0.0038 140 LEU   B CD2 
6102 N  N   . ARG   B 141 ? 0.1334 0.1168 0.2890 -0.0093 0.0118  0.0005  141 ARG   B N   
6103 C  CA  . ARG   B 141 ? 0.1457 0.1176 0.3264 -0.0158 0.0180  -0.0004 141 ARG   B CA  
6104 C  C   . ARG   B 141 ? 0.1372 0.1201 0.3170 -0.0167 0.0056  0.0064  141 ARG   B C   
6105 O  O   . ARG   B 141 ? 0.1410 0.1225 0.3181 -0.0138 -0.0040 -0.0079 141 ARG   B O   
6106 C  CB  . ARG   B 141 ? 0.1644 0.1324 0.3374 -0.0243 0.0306  -0.0041 141 ARG   B CB  
6107 C  CG  . ARG   B 141 ? 0.1974 0.1564 0.3458 -0.0225 0.0311  -0.0025 141 ARG   B CG  
6108 C  CD  . ARG   B 141 ? 0.2372 0.1786 0.3381 -0.0157 0.0152  -0.0096 141 ARG   B CD  
6109 N  NE  . ARG   B 141 ? 0.2565 0.1809 0.3227 -0.0378 0.0187  -0.0215 141 ARG   B NE  
6110 C  CZ  . ARG   B 141 ? 0.2656 0.1695 0.3028 -0.0377 0.0301  -0.0280 141 ARG   B CZ  
6111 N  NH1 . ARG   B 141 ? 0.2857 0.1554 0.2881 -0.0356 0.0253  -0.0234 141 ARG   B NH1 
6112 N  NH2 . ARG   B 141 ? 0.2620 0.1858 0.3123 -0.0293 0.0209  -0.0155 141 ARG   B NH2 
6126 N  N   . VAL   B 142 ? 0.1469 0.1145 0.3009 -0.0125 0.0146  0.0003  142 VAL   B N   
6127 C  CA  . VAL   B 142 ? 0.1402 0.1189 0.2935 -0.0067 0.0205  -0.0005 142 VAL   B CA  
6128 C  C   . VAL   B 142 ? 0.1332 0.1136 0.2918 -0.0007 0.0126  0.0008  142 VAL   B C   
6129 O  O   . VAL   B 142 ? 0.1415 0.1127 0.3011 0.0014  0.0181  0.0032  142 VAL   B O   
6130 C  CB  . VAL   B 142 ? 0.1512 0.1305 0.2891 -0.0010 0.0242  0.0128  142 VAL   B CB  
6131 C  CG1 . VAL   B 142 ? 0.1522 0.1299 0.2975 0.0107  0.0244  0.0084  142 VAL   B CG1 
6132 C  CG2 . VAL   B 142 ? 0.1643 0.1312 0.2934 -0.0011 0.0190  0.0153  142 VAL   B CG2 
6142 N  N   . CYS   B 143 ? 0.1282 0.1200 0.2792 -0.0020 0.0073  0.0089  143 CYS   B N   
6143 C  CA  . CYS   B 143 ? 0.1269 0.1152 0.2794 -0.0106 -0.0011 0.0077  143 CYS   B CA  
6144 C  C   . CYS   B 143 ? 0.1240 0.1171 0.2750 -0.0137 0.0012  -0.0008 143 CYS   B C   
6145 O  O   . CYS   B 143 ? 0.1370 0.1236 0.2575 -0.0067 -0.0033 -0.0031 143 CYS   B O   
6146 C  CB  . CYS   B 143 ? 0.1382 0.1226 0.2645 -0.0078 0.0022  0.0032  143 CYS   B CB  
6147 S  SG  . CYS   B 143 ? 0.1405 0.1404 0.2454 -0.0058 0.0027  0.0061  143 CYS   B SG  
6153 N  N   . VAL   B 144 ? 0.1324 0.1172 0.2943 -0.0102 -0.0031 -0.0125 144 VAL   B N   
6154 C  CA  . VAL   B 144 ? 0.1368 0.1259 0.3091 -0.0141 -0.0188 -0.0212 144 VAL   B CA  
6155 C  C   . VAL   B 144 ? 0.1352 0.1305 0.3209 -0.0140 -0.0166 0.0011  144 VAL   B C   
6156 O  O   . VAL   B 144 ? 0.1455 0.1504 0.3327 -0.0044 -0.0195 0.0184  144 VAL   B O   
6157 C  CB  . VAL   B 144 ? 0.1581 0.1450 0.3656 -0.0174 -0.0242 -0.0382 144 VAL   B CB  
6158 C  CG1 . VAL   B 144 ? 0.1821 0.1907 0.3880 -0.0088 -0.0253 -0.0342 144 VAL   B CG1 
6159 C  CG2 . VAL   B 144 ? 0.1710 0.1502 0.3660 -0.0034 -0.0357 -0.0484 144 VAL   B CG2 
6169 N  N   . ASP   B 145 ? 0.1401 0.1275 0.3296 -0.0115 -0.0148 -0.0162 145 ASP   B N   
6170 C  CA  . ASP   B 145 ? 0.1359 0.1300 0.3489 -0.0089 0.0034  -0.0047 145 ASP   B CA  
6171 C  C   . ASP   B 145 ? 0.1320 0.1320 0.3333 -0.0076 -0.0005 -0.0034 145 ASP   B C   
6172 O  O   . ASP   B 145 ? 0.1304 0.1485 0.3858 -0.0126 0.0074  -0.0215 145 ASP   B O   
6173 C  CB  . ASP   B 145 ? 0.1498 0.1385 0.3981 -0.0134 0.0159  -0.0024 145 ASP   B CB  
6174 C  CG  . ASP   B 145 ? 0.1662 0.1437 0.4355 -0.0217 0.0255  -0.0081 145 ASP   B CG  
6175 O  OD1 . ASP   B 145 ? 0.1688 0.1448 0.4307 -0.0209 -0.0099 -0.0067 145 ASP   B OD1 
6176 O  OD2 . ASP   B 145 ? 0.1930 0.1466 0.4743 -0.0310 0.0593  -0.0130 145 ASP   B OD2 
6181 N  N   . THR   B 146 ? 0.1276 0.1220 0.2887 -0.0063 -0.0051 0.0057  146 THR   B N   
6182 C  CA  . THR   B 146 ? 0.1360 0.1244 0.2630 -0.0093 0.0059  0.0025  146 THR   B CA  
6183 C  C   . THR   B 146 ? 0.1328 0.1231 0.2547 -0.0121 -0.0023 0.0032  146 THR   B C   
6184 O  O   . THR   B 146 ? 0.1430 0.1138 0.2615 -0.0088 -0.0092 0.0033  146 THR   B O   
6185 C  CB  . THR   B 146 ? 0.1394 0.1174 0.2668 -0.0097 0.0187  0.0053  146 THR   B CB  
6186 O  OG1 . THR   B 146 ? 0.1426 0.1207 0.2857 -0.0092 0.0151  0.0155  146 THR   B OG1 
6187 C  CG2 . THR   B 146 ? 0.1462 0.1260 0.2647 -0.0034 0.0131  0.0047  146 THR   B CG2 
6195 N  N   . VAL   B 147 ? 0.1363 0.1258 0.2440 -0.0087 0.0058  0.0046  147 VAL   B N   
6196 C  CA  . VAL   B 147 ? 0.1372 0.1199 0.2365 -0.0114 -0.0111 0.0019  147 VAL   B CA  
6197 C  C   . VAL   B 147 ? 0.1306 0.1203 0.2450 -0.0199 -0.0122 -0.0030 147 VAL   B C   
6198 O  O   . VAL   B 147 ? 0.1463 0.1312 0.2617 -0.0213 -0.0374 -0.0112 147 VAL   B O   
6199 C  CB  . VAL   B 147 ? 0.1413 0.1308 0.2260 -0.0066 -0.0135 -0.0009 147 VAL   B CB  
6200 C  CG1 . VAL   B 147 ? 0.1359 0.1418 0.2047 -0.0096 -0.0103 0.0038  147 VAL   B CG1 
6201 C  CG2 . VAL   B 147 ? 0.1402 0.1248 0.2266 -0.0121 -0.0050 -0.0018 147 VAL   B CG2 
6211 N  N   . ARG   B 148 ? 0.1326 0.1201 0.2396 -0.0084 -0.0244 -0.0040 148 ARG   B N   
6212 C  CA  . ARG   B 148 ? 0.1355 0.1336 0.2448 -0.0040 -0.0364 -0.0089 148 ARG   B CA  
6213 C  C   . ARG   B 148 ? 0.1411 0.1407 0.2264 -0.0058 -0.0365 -0.0023 148 ARG   B C   
6214 O  O   . ARG   B 148 ? 0.1635 0.1716 0.2367 -0.0264 -0.0463 0.0022  148 ARG   B O   
6215 C  CB  . ARG   B 148 ? 0.1413 0.1382 0.2432 -0.0046 -0.0395 -0.0166 148 ARG   B CB  
6216 C  CG  . ARG   B 148 ? 0.1422 0.1545 0.2491 -0.0088 -0.0358 -0.0292 148 ARG   B CG  
6217 C  CD  . ARG   B 148 ? 0.1482 0.1719 0.2656 0.0056  -0.0303 -0.0307 148 ARG   B CD  
6218 N  NE  . ARG   B 148 ? 0.1539 0.1678 0.2659 0.0198  -0.0364 -0.0305 148 ARG   B NE  
6219 C  CZ  . ARG   B 148 ? 0.1414 0.1585 0.2461 0.0123  -0.0266 -0.0186 148 ARG   B CZ  
6220 N  NH1 . ARG   B 148 ? 0.1373 0.1682 0.2432 -0.0030 -0.0124 -0.0177 148 ARG   B NH1 
6221 N  NH2 . ARG   B 148 ? 0.1688 0.1430 0.2243 0.0130  -0.0120 -0.0086 148 ARG   B NH2 
6235 N  N   . THR   B 149 ? 0.1446 0.1327 0.2190 -0.0078 -0.0354 -0.0021 149 THR   B N   
6236 C  CA  . THR   B 149 ? 0.1493 0.1414 0.2147 -0.0140 -0.0366 0.0089  149 THR   B CA  
6237 C  C   . THR   B 149 ? 0.1522 0.1345 0.2061 -0.0165 -0.0324 0.0073  149 THR   B C   
6238 O  O   . THR   B 149 ? 0.1605 0.1356 0.2082 -0.0208 -0.0189 0.0073  149 THR   B O   
6239 C  CB  . THR   B 149 ? 0.1546 0.1346 0.2122 -0.0139 -0.0374 0.0049  149 THR   B CB  
6240 O  OG1 . THR   B 149 ? 0.1582 0.1407 0.2075 -0.0240 -0.0408 0.0060  149 THR   B OG1 
6241 C  CG2 . THR   B 149 ? 0.1677 0.1359 0.2269 -0.0116 -0.0278 0.0019  149 THR   B CG2 
6249 N  N   . ASN   B 150 ? 0.1634 0.1362 0.1924 -0.0179 -0.0432 0.0022  150 ASN   B N   
6250 C  CA  . ASN   B 150 ? 0.1709 0.1526 0.1783 -0.0198 -0.0399 -0.0026 150 ASN   B CA  
6251 C  C   . ASN   B 150 ? 0.1576 0.1436 0.1903 -0.0184 -0.0363 -0.0080 150 ASN   B C   
6252 O  O   . ASN   B 150 ? 0.1656 0.1397 0.2020 -0.0288 -0.0487 -0.0049 150 ASN   B O   
6253 C  CB  . ASN   B 150 ? 0.1894 0.1873 0.1988 -0.0274 -0.0535 0.0113  150 ASN   B CB  
6254 C  CG  . ASN   B 150 ? 0.2150 0.2257 0.2321 -0.0257 -0.0548 0.0261  150 ASN   B CG  
6255 O  OD1 . ASN   B 150 ? 0.2226 0.2459 0.2431 -0.0339 -0.0628 0.0194  150 ASN   B OD1 
6256 N  ND2 . ASN   B 150 ? 0.2295 0.2437 0.2675 -0.0173 -0.0493 0.0645  150 ASN   B ND2 
6263 N  N   . VAL   B 151 ? 0.1465 0.1403 0.1976 -0.0234 -0.0407 -0.0024 151 VAL   B N   
6264 C  CA  . VAL   B 151 ? 0.1512 0.1419 0.2002 -0.0309 -0.0274 -0.0058 151 VAL   B CA  
6265 C  C   . VAL   B 151 ? 0.1540 0.1350 0.1979 -0.0339 -0.0374 -0.0055 151 VAL   B C   
6266 O  O   . VAL   B 151 ? 0.1664 0.1472 0.2081 -0.0289 -0.0321 -0.0097 151 VAL   B O   
6267 C  CB  . VAL   B 151 ? 0.1712 0.1542 0.2137 -0.0158 -0.0286 -0.0026 151 VAL   B CB  
6268 C  CG1 . VAL   B 151 ? 0.1806 0.1598 0.2411 -0.0205 -0.0160 -0.0114 151 VAL   B CG1 
6269 C  CG2 . VAL   B 151 ? 0.1859 0.1644 0.1962 -0.0046 -0.0318 0.0061  151 VAL   B CG2 
6279 N  N   . TYR   B 152 ? 0.1486 0.1256 0.1983 -0.0217 -0.0358 0.0031  152 TYR   B N   
6280 C  CA  . TYR   B 152 ? 0.1558 0.1436 0.1851 -0.0275 -0.0229 -0.0026 152 TYR   B CA  
6281 C  C   . TYR   B 152 ? 0.1500 0.1259 0.1744 -0.0185 -0.0181 -0.0095 152 TYR   B C   
6282 O  O   . TYR   B 152 ? 0.1581 0.1287 0.1845 -0.0252 -0.0159 -0.0040 152 TYR   B O   
6283 C  CB  . TYR   B 152 ? 0.1702 0.1586 0.1824 -0.0318 -0.0222 0.0144  152 TYR   B CB  
6284 C  CG  . TYR   B 152 ? 0.1885 0.1677 0.1778 -0.0490 -0.0307 0.0063  152 TYR   B CG  
6285 C  CD1 . TYR   B 152 ? 0.2042 0.1791 0.1622 -0.0390 -0.0366 0.0161  152 TYR   B CD1 
6286 C  CD2 . TYR   B 152 ? 0.2124 0.1835 0.1779 -0.0468 -0.0282 -0.0002 152 TYR   B CD2 
6287 C  CE1 . TYR   B 152 ? 0.2217 0.1962 0.1827 -0.0351 -0.0359 0.0231  152 TYR   B CE1 
6288 C  CE2 . TYR   B 152 ? 0.2247 0.2040 0.1745 -0.0473 -0.0299 -0.0082 152 TYR   B CE2 
6289 C  CZ  . TYR   B 152 ? 0.2245 0.2159 0.1713 -0.0420 -0.0455 0.0230  152 TYR   B CZ  
6290 O  OH  . TYR   B 152 ? 0.2423 0.2522 0.2127 -0.0292 -0.0444 0.0251  152 TYR   B OH  
6300 N  N   . LEU   B 153 ? 0.1557 0.1230 0.1786 -0.0313 -0.0162 -0.0037 153 LEU   B N   
6301 C  CA  . LEU   B 153 ? 0.1566 0.1230 0.1778 -0.0197 -0.0074 -0.0059 153 LEU   B CA  
6302 C  C   . LEU   B 153 ? 0.1538 0.1189 0.1968 -0.0223 -0.0078 -0.0172 153 LEU   B C   
6303 O  O   . LEU   B 153 ? 0.1669 0.1402 0.2011 -0.0153 -0.0107 -0.0301 153 LEU   B O   
6304 C  CB  . LEU   B 153 ? 0.1510 0.1208 0.2003 -0.0283 -0.0075 -0.0059 153 LEU   B CB  
6305 C  CG  . LEU   B 153 ? 0.1492 0.1289 0.2178 -0.0267 -0.0109 -0.0004 153 LEU   B CG  
6306 C  CD1 . LEU   B 153 ? 0.1567 0.1486 0.2327 -0.0209 -0.0013 0.0056  153 LEU   B CD1 
6307 C  CD2 . LEU   B 153 ? 0.1511 0.1433 0.2172 -0.0246 -0.0034 0.0048  153 LEU   B CD2 
6319 N  N   . ALA   B 154 ? 0.1413 0.1253 0.2054 -0.0089 -0.0165 -0.0134 154 ALA   B N   
6320 C  CA  . ALA   B 154 ? 0.1564 0.1402 0.2258 -0.0025 -0.0135 -0.0188 154 ALA   B CA  
6321 C  C   . ALA   B 154 ? 0.1725 0.1430 0.2216 0.0018  -0.0266 -0.0262 154 ALA   B C   
6322 O  O   . ALA   B 154 ? 0.2069 0.1404 0.2389 0.0067  -0.0146 -0.0066 154 ALA   B O   
6323 C  CB  . ALA   B 154 ? 0.1541 0.1503 0.2351 -0.0048 -0.0103 -0.0256 154 ALA   B CB  
6329 N  N   . VAL   B 155 ? 0.1418 0.1330 0.2298 -0.0103 -0.0028 -0.0153 155 VAL   B N   
6330 C  CA  . VAL   B 155 ? 0.1336 0.1299 0.2526 -0.0022 -0.0138 -0.0073 155 VAL   B CA  
6331 C  C   . VAL   B 155 ? 0.1341 0.1299 0.2380 -0.0057 -0.0154 -0.0141 155 VAL   B C   
6332 O  O   . VAL   B 155 ? 0.1560 0.1488 0.2679 -0.0007 -0.0181 -0.0349 155 VAL   B O   
6333 C  CB  . VAL   B 155 ? 0.1414 0.1445 0.2870 -0.0056 -0.0235 0.0050  155 VAL   B CB  
6334 C  CG1 . VAL   B 155 ? 0.1491 0.1417 0.2883 -0.0073 -0.0156 -0.0005 155 VAL   B CG1 
6335 C  CG2 . VAL   B 155 ? 0.1386 0.1617 0.3080 -0.0069 -0.0157 0.0278  155 VAL   B CG2 
6345 N  N   . PHE   B 156 ? 0.1295 0.1431 0.2630 0.0042  -0.0075 -0.0171 156 PHE   B N   
6346 C  CA  . PHE   B 156 ? 0.1337 0.1481 0.2970 0.0050  -0.0115 -0.0164 156 PHE   B CA  
6347 C  C   . PHE   B 156 ? 0.1324 0.1608 0.3354 0.0088  -0.0094 -0.0366 156 PHE   B C   
6348 O  O   . PHE   B 156 ? 0.1576 0.1779 0.3610 0.0199  -0.0044 -0.0510 156 PHE   B O   
6349 C  CB  . PHE   B 156 ? 0.1444 0.1437 0.2995 0.0005  -0.0171 -0.0108 156 PHE   B CB  
6350 C  CG  . PHE   B 156 ? 0.1479 0.1558 0.3047 -0.0066 -0.0150 -0.0013 156 PHE   B CG  
6351 C  CD1 . PHE   B 156 ? 0.1457 0.1834 0.3310 0.0002  -0.0121 0.0371  156 PHE   B CD1 
6352 C  CD2 . PHE   B 156 ? 0.1495 0.1724 0.2993 0.0080  -0.0205 0.0077  156 PHE   B CD2 
6353 C  CE1 . PHE   B 156 ? 0.1482 0.1978 0.3398 -0.0031 -0.0100 0.0413  156 PHE   B CE1 
6354 C  CE2 . PHE   B 156 ? 0.1543 0.1921 0.3208 0.0121  -0.0135 0.0123  156 PHE   B CE2 
6355 C  CZ  . PHE   B 156 ? 0.1451 0.2016 0.3427 0.0111  -0.0194 0.0243  156 PHE   B CZ  
6365 N  N   . ASP   B 157 ? 0.1361 0.1525 0.3561 0.0106  -0.0209 -0.0173 157 ASP   B N   
6366 C  CA  . ASP   B 157 ? 0.1509 0.1576 0.3879 0.0057  -0.0228 -0.0273 157 ASP   B CA  
6367 C  C   . ASP   B 157 ? 0.1516 0.1537 0.4044 0.0082  -0.0241 -0.0479 157 ASP   B C   
6368 O  O   . ASP   B 157 ? 0.1386 0.1558 0.3922 0.0033  -0.0222 -0.0404 157 ASP   B O   
6369 C  CB  . ASP   B 157 ? 0.1790 0.1713 0.3992 -0.0012 -0.0398 -0.0063 157 ASP   B CB  
6370 C  CG  . ASP   B 157 ? 0.2147 0.1827 0.4237 -0.0070 -0.0290 -0.0089 157 ASP   B CG  
6371 O  OD1 . ASP   B 157 ? 0.2277 0.1768 0.4458 0.0004  -0.0310 -0.0047 157 ASP   B OD1 
6372 O  OD2 . ASP   B 157 ? 0.2448 0.2027 0.4488 -0.0051 -0.0110 -0.0129 157 ASP   B OD2 
6377 N  N   . LYS   B 158 ? 0.1555 0.1810 0.4085 0.0074  -0.0151 -0.0750 158 LYS   B N   
6378 C  CA  . LYS   B 158 ? 0.1749 0.1988 0.4123 0.0029  -0.0014 -0.0928 158 LYS   B CA  
6379 C  C   . LYS   B 158 ? 0.1731 0.1845 0.4252 0.0064  -0.0085 -0.0827 158 LYS   B C   
6380 O  O   . LYS   B 158 ? 0.1727 0.1814 0.4340 0.0003  -0.0024 -0.0909 158 LYS   B O   
6381 C  CB  . LYS   B 158 ? 0.2018 0.2461 0.4089 0.0028  0.0167  -0.1163 158 LYS   B CB  
6382 C  CG  . LYS   B 158 ? 0.2397 0.2908 0.4152 0.0059  0.0232  -0.1268 158 LYS   B CG  
6383 C  CD  . LYS   B 158 ? 0.2684 0.3338 0.4258 0.0034  0.0234  -0.1199 158 LYS   B CD  
6384 C  CE  . LYS   B 158 ? 0.2898 0.3564 0.4362 0.0048  0.0192  -0.1177 158 LYS   B CE  
6385 N  NZ  . LYS   B 158 ? 0.2866 0.3620 0.4356 0.0015  0.0175  -0.1196 158 LYS   B NZ  
6399 N  N   . ASN   B 159 ? 0.1744 0.1697 0.4401 0.0053  -0.0175 -0.0679 159 ASN   B N   
6400 C  CA  . ASN   B 159 ? 0.1880 0.1623 0.4521 0.0168  -0.0380 -0.0492 159 ASN   B CA  
6401 C  C   . ASN   B 159 ? 0.1679 0.1476 0.4472 0.0113  -0.0573 -0.0325 159 ASN   B C   
6402 O  O   . ASN   B 159 ? 0.1711 0.1411 0.4661 -0.0067 -0.0651 -0.0247 159 ASN   B O   
6403 C  CB  . ASN   B 159 ? 0.2126 0.1836 0.4747 0.0307  -0.0479 -0.0443 159 ASN   B CB  
6404 C  CG  . ASN   B 159 ? 0.2472 0.2169 0.4944 0.0355  -0.0541 -0.0531 159 ASN   B CG  
6405 O  OD1 . ASN   B 159 ? 0.2637 0.2170 0.4993 0.0382  -0.0538 -0.0663 159 ASN   B OD1 
6406 N  ND2 . ASN   B 159 ? 0.2491 0.2236 0.5130 0.0403  -0.0586 -0.0546 159 ASN   B ND2 
6413 N  N   . LEU   B 160 ? 0.1572 0.1464 0.4215 0.0059  -0.0493 -0.0228 160 LEU   B N   
6414 C  CA  . LEU   B 160 ? 0.1590 0.1482 0.3855 0.0070  -0.0468 -0.0119 160 LEU   B CA  
6415 C  C   . LEU   B 160 ? 0.1526 0.1380 0.3776 -0.0023 -0.0308 -0.0263 160 LEU   B C   
6416 O  O   . LEU   B 160 ? 0.1425 0.1384 0.3786 -0.0044 -0.0372 -0.0213 160 LEU   B O   
6417 C  CB  . LEU   B 160 ? 0.1569 0.1613 0.3603 0.0039  -0.0438 -0.0033 160 LEU   B CB  
6418 C  CG  . LEU   B 160 ? 0.1506 0.1807 0.3284 0.0015  -0.0364 0.0012  160 LEU   B CG  
6419 C  CD1 . LEU   B 160 ? 0.1653 0.2043 0.3309 -0.0060 -0.0292 -0.0025 160 LEU   B CD1 
6420 C  CD2 . LEU   B 160 ? 0.1540 0.1874 0.3180 0.0167  -0.0361 -0.0077 160 LEU   B CD2 
6432 N  N   . TYR   B 161 ? 0.1489 0.1485 0.3762 -0.0099 -0.0035 -0.0459 161 TYR   B N   
6433 C  CA  . TYR   B 161 ? 0.1602 0.1458 0.3573 -0.0170 0.0137  -0.0523 161 TYR   B CA  
6434 C  C   . TYR   B 161 ? 0.1655 0.1451 0.3525 -0.0161 0.0196  -0.0409 161 TYR   B C   
6435 O  O   . TYR   B 161 ? 0.1731 0.1472 0.3447 -0.0225 0.0080  -0.0379 161 TYR   B O   
6436 C  CB  . TYR   B 161 ? 0.1769 0.1592 0.3427 -0.0265 0.0323  -0.0581 161 TYR   B CB  
6437 C  CG  . TYR   B 161 ? 0.2073 0.1615 0.3299 -0.0319 0.0399  -0.0648 161 TYR   B CG  
6438 C  CD1 . TYR   B 161 ? 0.2138 0.1576 0.3336 -0.0428 0.0436  -0.0613 161 TYR   B CD1 
6439 C  CD2 . TYR   B 161 ? 0.2331 0.1696 0.3266 -0.0296 0.0309  -0.0531 161 TYR   B CD2 
6440 C  CE1 . TYR   B 161 ? 0.2361 0.1803 0.3322 -0.0482 0.0392  -0.0614 161 TYR   B CE1 
6441 C  CE2 . TYR   B 161 ? 0.2544 0.1862 0.3211 -0.0346 0.0365  -0.0516 161 TYR   B CE2 
6442 C  CZ  . TYR   B 161 ? 0.2549 0.1900 0.3269 -0.0519 0.0265  -0.0502 161 TYR   B CZ  
6443 O  OH  . TYR   B 161 ? 0.2862 0.2168 0.3548 -0.0491 0.0289  -0.0426 161 TYR   B OH  
6453 N  N   . ASP   B 162 ? 0.1729 0.1446 0.3645 -0.0111 0.0038  -0.0519 162 ASP   B N   
6454 C  CA  . ASP   B 162 ? 0.1787 0.1486 0.3642 -0.0066 -0.0054 -0.0566 162 ASP   B CA  
6455 C  C   . ASP   B 162 ? 0.1745 0.1432 0.3564 -0.0118 -0.0091 -0.0403 162 ASP   B C   
6456 O  O   . ASP   B 162 ? 0.1749 0.1506 0.3692 -0.0189 -0.0242 -0.0346 162 ASP   B O   
6457 C  CB  . ASP   B 162 ? 0.1964 0.1662 0.3890 -0.0029 -0.0153 -0.0717 162 ASP   B CB  
6458 C  CG  . ASP   B 162 ? 0.2021 0.1953 0.4122 0.0062  -0.0085 -0.0869 162 ASP   B CG  
6459 O  OD1 . ASP   B 162 ? 0.2008 0.2106 0.4071 -0.0014 0.0030  -0.0845 162 ASP   B OD1 
6460 O  OD2 . ASP   B 162 ? 0.2146 0.2155 0.4418 0.0224  -0.0028 -0.0827 162 ASP   B OD2 
6465 N  N   A LYS   B 163 ? 0.1714 0.1277 0.3423 -0.0078 -0.0296 -0.0270 163 LYS   B N   
6466 N  N   B LYS   B 163 ? 0.1772 0.1448 0.3429 -0.0114 -0.0209 -0.0245 163 LYS   B N   
6467 C  CA  A LYS   B 163 ? 0.1835 0.1389 0.3427 -0.0139 -0.0277 -0.0009 163 LYS   B CA  
6468 C  CA  B LYS   B 163 ? 0.1846 0.1578 0.3382 -0.0141 -0.0205 -0.0047 163 LYS   B CA  
6469 C  C   A LYS   B 163 ? 0.1538 0.1353 0.3356 -0.0164 -0.0205 0.0053  163 LYS   B C   
6470 C  C   B LYS   B 163 ? 0.1592 0.1447 0.3286 -0.0155 -0.0181 0.0019  163 LYS   B C   
6471 O  O   A LYS   B 163 ? 0.1492 0.1503 0.3541 -0.0207 -0.0214 0.0016  163 LYS   B O   
6472 O  O   B LYS   B 163 ? 0.1561 0.1519 0.3346 -0.0181 -0.0186 0.0016  163 LYS   B O   
6473 C  CB  A LYS   B 163 ? 0.2261 0.1697 0.3695 -0.0067 -0.0331 0.0115  163 LYS   B CB  
6474 C  CB  B LYS   B 163 ? 0.2147 0.1890 0.3613 -0.0104 -0.0236 0.0025  163 LYS   B CB  
6475 C  CG  A LYS   B 163 ? 0.2873 0.2323 0.4029 -0.0088 -0.0184 0.0113  163 LYS   B CG  
6476 C  CG  B LYS   B 163 ? 0.2545 0.2349 0.3881 -0.0106 -0.0168 0.0042  163 LYS   B CG  
6477 C  CD  A LYS   B 163 ? 0.3332 0.2750 0.4391 -0.0179 -0.0096 -0.0020 163 LYS   B CD  
6478 C  CD  B LYS   B 163 ? 0.2880 0.2733 0.4198 -0.0154 -0.0127 -0.0012 163 LYS   B CD  
6479 C  CE  A LYS   B 163 ? 0.3560 0.2934 0.4668 -0.0245 -0.0033 -0.0052 163 LYS   B CE  
6480 C  CE  B LYS   B 163 ? 0.3064 0.2896 0.4461 -0.0197 -0.0090 -0.0025 163 LYS   B CE  
6481 N  NZ  A LYS   B 163 ? 0.3853 0.3082 0.4832 -0.0295 -0.0005 -0.0091 163 LYS   B NZ  
6482 N  NZ  B LYS   B 163 ? 0.3101 0.2935 0.4613 -0.0222 -0.0077 -0.0041 163 LYS   B NZ  
6509 N  N   . LEU   B 164 ? 0.1445 0.1287 0.3206 -0.0126 -0.0215 0.0022  164 LEU   B N   
6510 C  CA  . LEU   B 164 ? 0.1444 0.1271 0.3064 -0.0120 -0.0273 -0.0006 164 LEU   B CA  
6511 C  C   . LEU   B 164 ? 0.1506 0.1296 0.3084 -0.0183 -0.0362 0.0024  164 LEU   B C   
6512 O  O   . LEU   B 164 ? 0.1543 0.1529 0.3241 -0.0151 -0.0364 -0.0015 164 LEU   B O   
6513 C  CB  . LEU   B 164 ? 0.1363 0.1312 0.2865 -0.0083 -0.0279 0.0026  164 LEU   B CB  
6514 C  CG  . LEU   B 164 ? 0.1472 0.1406 0.2923 -0.0092 -0.0188 0.0104  164 LEU   B CG  
6515 C  CD1 . LEU   B 164 ? 0.1591 0.1429 0.2851 -0.0186 -0.0210 -0.0014 164 LEU   B CD1 
6516 C  CD2 . LEU   B 164 ? 0.1609 0.1698 0.3094 -0.0074 0.0043  -0.0078 164 LEU   B CD2 
6529 N  N   . VAL   B 165 ? 0.1883 0.1411 0.3175 -0.0220 -0.0454 0.0025  165 VAL   B N   
6530 C  CA  . VAL   B 165 ? 0.2264 0.1541 0.3252 -0.0341 -0.0632 -0.0029 165 VAL   B CA  
6531 C  C   . VAL   B 165 ? 0.2551 0.1676 0.3534 -0.0434 -0.0914 -0.0043 165 VAL   B C   
6532 O  O   . VAL   B 165 ? 0.2788 0.1824 0.3656 -0.0504 -0.0979 0.0008  165 VAL   B O   
6533 C  CB  . VAL   B 165 ? 0.2504 0.1687 0.3153 -0.0119 -0.0346 -0.0168 165 VAL   B CB  
6534 C  CG1 . VAL   B 165 ? 0.2683 0.1778 0.3348 -0.0140 -0.0187 -0.0152 165 VAL   B CG1 
6535 C  CG2 . VAL   B 165 ? 0.2487 0.1704 0.3074 -0.0017 -0.0244 -0.0142 165 VAL   B CG2 
6545 N  N   . SER   B 166 ? 0.2597 0.1526 0.3871 -0.0416 -0.0960 -0.0227 166 SER   B N   
6546 C  CA  . SER   B 166 ? 0.2552 0.1527 0.4299 -0.0367 -0.0786 -0.0326 166 SER   B CA  
6547 C  C   . SER   B 166 ? 0.2412 0.1635 0.4425 -0.0399 -0.0780 -0.0058 166 SER   B C   
6548 O  O   . SER   B 166 ? 0.2474 0.1891 0.4614 -0.0563 -0.1031 -0.0222 166 SER   B O   
6549 C  CB  . SER   B 166 ? 0.2563 0.1633 0.4573 -0.0264 -0.0643 -0.0410 166 SER   B CB  
6550 O  OG  . SER   B 166 ? 0.2439 0.1627 0.4789 -0.0268 -0.0690 -0.0234 166 SER   B OG  
6556 N  N   . SER   B 167 ? 0.2188 0.1537 0.4168 -0.0465 -0.0768 0.0233  167 SER   B N   
6557 C  CA  . SER   B 167 ? 0.2096 0.1650 0.3962 -0.0337 -0.0575 0.0277  167 SER   B CA  
6558 C  C   . SER   B 167 ? 0.2011 0.1752 0.3767 -0.0527 -0.0547 0.0495  167 SER   B C   
6559 O  O   . SER   B 167 ? 0.2002 0.1904 0.3810 -0.0631 -0.0555 0.0451  167 SER   B O   
6560 C  CB  . SER   B 167 ? 0.1989 0.1696 0.4008 -0.0301 -0.0340 0.0252  167 SER   B CB  
6561 O  OG  . SER   B 167 ? 0.1899 0.1792 0.3921 -0.0231 -0.0173 0.0258  167 SER   B OG  
6567 N  N   . PHE   B 168 ? 0.2003 0.1742 0.3651 -0.0460 -0.0364 0.0624  168 PHE   B N   
6568 C  CA  . PHE   B 168 ? 0.2025 0.1730 0.3303 -0.0466 -0.0364 0.0413  168 PHE   B CA  
6569 C  C   . PHE   B 168 ? 0.1723 0.1610 0.2869 -0.0300 -0.0231 0.0159  168 PHE   B C   
6570 O  O   . PHE   B 168 ? 0.2072 0.1532 0.2856 -0.0030 -0.0247 0.0033  168 PHE   B O   
6571 C  CB  . PHE   B 168 ? 0.2249 0.1796 0.3306 -0.0540 -0.0493 0.0523  168 PHE   B CB  
6572 C  CG  . PHE   B 168 ? 0.2517 0.1644 0.3202 -0.0593 -0.0505 0.0264  168 PHE   B CG  
6573 C  CD1 . PHE   B 168 ? 0.2800 0.1696 0.3323 -0.0543 -0.0498 0.0252  168 PHE   B CD1 
6574 C  CD2 . PHE   B 168 ? 0.2409 0.1567 0.3165 -0.0570 -0.0483 0.0271  168 PHE   B CD2 
6575 C  CE1 . PHE   B 168 ? 0.2897 0.1774 0.3197 -0.0437 -0.0375 0.0292  168 PHE   B CE1 
6576 C  CE2 . PHE   B 168 ? 0.2685 0.1668 0.3229 -0.0373 -0.0499 0.0186  168 PHE   B CE2 
6577 C  CZ  . PHE   B 168 ? 0.2802 0.1624 0.3235 -0.0286 -0.0505 0.0344  168 PHE   B CZ  
6587 N  N   . LEU   B 169 ? 0.1768 0.1729 0.2838 -0.0050 0.0013  0.0034  169 LEU   B N   
6588 C  CA  . LEU   B 169 ? 0.1946 0.1973 0.3163 -0.0046 0.0083  -0.0231 169 LEU   B CA  
6589 C  C   . LEU   B 169 ? 0.2278 0.2221 0.3648 0.0086  0.0052  -0.0505 169 LEU   B C   
6590 O  O   . LEU   B 169 ? 0.2526 0.2434 0.4071 0.0049  0.0014  -0.0697 169 LEU   B O   
6591 C  CB  . LEU   B 169 ? 0.2163 0.2417 0.3192 -0.0121 0.0079  0.0023  169 LEU   B CB  
6592 C  CG  . LEU   B 169 ? 0.2549 0.2806 0.3431 -0.0013 0.0147  0.0051  169 LEU   B CG  
6593 C  CD1 . LEU   B 169 ? 0.2733 0.3003 0.3423 -0.0041 0.0152  0.0169  169 LEU   B CD1 
6594 C  CD2 . LEU   B 169 ? 0.2451 0.2877 0.3368 0.0209  0.0356  -0.0084 169 LEU   B CD2 
6595 O  OXT . LEU   B 169 ? 0.2529 0.2378 0.3648 0.0371  0.0159  -0.0552 169 LEU   B OXT 
6607 C  C1  T TFA   C .   ? 0.1300 0.1577 0.1437 -0.0070 0.0132  0.0190  201 TFA   A C1  
6608 C  C2  T TFA   C .   ? 0.1549 0.1784 0.1737 -0.0185 0.0114  -0.0008 201 TFA   A C2  
6609 O  O   T TFA   C .   ? 0.1053 0.1359 0.1300 -0.0105 0.0139  0.0288  201 TFA   A O   
6610 F  F1  T TFA   C .   ? 0.1656 0.1897 0.2050 -0.0159 0.0027  -0.0066 201 TFA   A F1  
6611 F  F2  T TFA   C .   ? 0.1719 0.1791 0.1778 -0.0214 0.0215  0.0071  201 TFA   A F2  
6612 F  F3  T TFA   C .   ? 0.1614 0.1894 0.1942 -0.0290 0.0253  -0.0070 201 TFA   A F3  
6613 O  OXT T TFA   C .   ? 0.1333 0.1563 0.1547 0.0153  0.0138  0.0204  201 TFA   A OXT 
6614 N  N2  B A1A81 D .   ? 0.1791 0.2201 0.2185 -0.0153 -0.0271 0.0124  202 A1A81 A N2  
6615 C  C3  B A1A81 D .   ? 0.2633 0.2958 0.2907 -0.0121 -0.0231 -0.0032 202 A1A81 A C3  
6616 C  C6  B A1A81 D .   ? 0.2830 0.3176 0.3000 -0.0036 -0.0269 -0.0034 202 A1A81 A C6  
6617 C  C9  B A1A81 D .   ? 0.1685 0.2131 0.2104 -0.0145 -0.0182 0.0263  202 A1A81 A C9  
6618 C  C12 B A1A81 D .   ? 0.1318 0.2033 0.1933 -0.0077 -0.0121 0.0379  202 A1A81 A C12 
6619 C  C1  B A1A81 D .   ? 0.2626 0.2882 0.2999 -0.0135 -0.0102 -0.0084 202 A1A81 A C1  
6620 C  C10 B A1A81 D .   ? 0.1396 0.1985 0.1975 -0.0098 -0.0186 0.0377  202 A1A81 A C10 
6621 C  C11 B A1A81 D .   ? 0.1497 0.2106 0.2017 -0.0097 -0.0176 0.0338  202 A1A81 A C11 
6622 C  C13 B A1A81 D .   ? 0.1252 0.1955 0.1943 -0.0101 -0.0229 0.0470  202 A1A81 A C13 
6623 C  C2  B A1A81 D .   ? 0.2493 0.2783 0.2781 -0.0146 -0.0195 -0.0018 202 A1A81 A C2  
6624 C  C4  B A1A81 D .   ? 0.2764 0.3103 0.2969 -0.0085 -0.0262 -0.0019 202 A1A81 A C4  
6625 C  C5  B A1A81 D .   ? 0.2809 0.3147 0.3003 -0.0063 -0.0276 0.0006  202 A1A81 A C5  
6626 C  C7  B A1A81 D .   ? 0.2814 0.3151 0.3007 -0.0040 -0.0285 -0.0044 202 A1A81 A C7  
6627 C  C8  B A1A81 D .   ? 0.1821 0.2286 0.2199 -0.0117 -0.0235 0.0215  202 A1A81 A C8  
6628 N  N1  B A1A81 D .   ? 0.2175 0.2526 0.2519 -0.0158 -0.0227 0.0092  202 A1A81 A N1  
6629 N  N3  B A1A81 D .   ? 0.1568 0.2054 0.2016 -0.0141 -0.0116 0.0374  202 A1A81 A N3  
6630 N  N4  B A1A81 D .   ? 0.1242 0.1852 0.1921 -0.0020 -0.0200 0.0534  202 A1A81 A N4  
6631 O  O1  B A1A81 D .   ? 0.2750 0.2936 0.3102 -0.0133 -0.0051 -0.0101 202 A1A81 A O1  
6650 CL CL  B CL    E .   ? 0.1885 0.1633 0.4027 -0.0045 -0.0242 -0.0443 203 CL    A CL  
6651 O  O   . HOH   F .   ? 0.2593 0.2256 0.3766 -0.0245 -0.0342 0.0434  301 HOH   A O   
6652 O  O   . HOH   F .   ? 0.4153 0.8279 0.4993 -0.1218 0.0446  0.1094  302 HOH   A O   
6653 O  O   . HOH   F .   ? 0.3009 0.2580 0.4407 -0.0446 -0.1265 0.1169  303 HOH   A O   
6654 O  O   . HOH   F .   ? 0.3394 0.3341 0.2930 -0.1218 -0.0175 0.0839  304 HOH   A O   
6655 O  O   . HOH   F .   ? 0.2140 0.2520 0.2492 -0.0224 0.0341  0.0645  305 HOH   A O   
6656 O  O   . HOH   F .   ? 0.4401 0.3397 0.4885 -0.0462 0.1207  -0.0369 306 HOH   A O   
6657 O  O   . HOH   F .   ? 0.7224 0.5851 0.4413 -0.1318 -0.0294 0.2149  307 HOH   A O   
6658 O  O   . HOH   F .   ? 0.5821 0.4380 0.3245 0.1318  -0.1387 0.0405  308 HOH   A O   
6659 O  O   . HOH   F .   ? 0.6809 0.5360 0.4634 -0.1437 -0.0121 0.2265  309 HOH   A O   
6660 O  O   . HOH   F .   ? 0.2766 0.6721 0.5793 -0.0547 -0.0768 0.2386  310 HOH   A O   
6661 O  O   . HOH   F .   ? 0.6051 0.4051 0.5172 -0.0905 0.1592  0.1171  311 HOH   A O   
6662 O  O   . HOH   F .   ? 0.5566 0.6236 0.5186 -0.1236 -0.1129 -0.0773 312 HOH   A O   
6663 O  O   . HOH   F .   ? 0.3075 0.3857 0.3434 -0.1442 0.0640  -0.0118 313 HOH   A O   
6664 O  O   . HOH   F .   ? 0.2998 0.3496 0.1876 -0.0325 0.0491  0.0538  314 HOH   A O   
6665 O  O   . HOH   F .   ? 0.6574 0.5433 0.3550 -0.0547 -0.0662 0.1108  315 HOH   A O   
6666 O  O   . HOH   F .   ? 0.4422 0.5286 0.5540 0.1607  0.0642  -0.1113 316 HOH   A O   
6667 O  O   . HOH   F .   ? 0.1830 0.3145 0.3125 0.0473  -0.0156 -0.0092 317 HOH   A O   
6668 O  O   . HOH   F .   ? 0.2059 0.1793 0.3713 -0.0401 0.0101  -0.0240 318 HOH   A O   
6669 O  O   . HOH   F .   ? 0.5922 0.3471 0.3330 -0.1322 -0.0946 0.0334  319 HOH   A O   
6670 O  O   . HOH   F .   ? 0.5423 0.4632 0.4750 -0.0329 0.1297  0.2173  320 HOH   A O   
6671 O  O   . HOH   F .   ? 0.1919 0.3736 0.4061 -0.0405 0.0389  -0.1015 321 HOH   A O   
6672 O  O   . HOH   F .   ? 0.3321 0.3632 0.3875 -0.0694 0.1446  0.0225  322 HOH   A O   
6673 O  O   . HOH   F .   ? 0.6108 0.4001 0.5643 0.0348  -0.0201 0.0286  323 HOH   A O   
6674 O  O   . HOH   F .   ? 0.2627 0.5158 0.5996 0.0728  0.0597  0.1093  324 HOH   A O   
6675 O  O   A HOH   F .   ? 0.1318 0.1905 0.2054 0.0410  0.0388  0.0527  325 HOH   A O   
6676 O  O   . HOH   F .   ? 0.6017 0.5434 0.4475 0.0254  0.0294  -0.1070 326 HOH   A O   
6677 O  O   . HOH   F .   ? 0.1576 0.3878 0.2545 0.0011  0.0309  0.0521  327 HOH   A O   
6678 O  O   . HOH   F .   ? 0.2558 0.4781 0.3850 0.0429  -0.0576 0.0509  328 HOH   A O   
6679 O  O   . HOH   F .   ? 0.1484 0.1505 0.2521 -0.0194 0.0044  0.0107  329 HOH   A O   
6680 O  O   . HOH   F .   ? 0.3040 0.4368 0.2729 0.0091  0.0420  0.0127  330 HOH   A O   
6681 O  O   . HOH   F .   ? 0.3142 0.2937 0.3581 -0.0831 0.0060  -0.0403 331 HOH   A O   
6682 O  O   . HOH   F .   ? 0.2521 0.2282 0.2521 -0.0375 0.0088  -0.0081 332 HOH   A O   
6683 O  O   . HOH   F .   ? 0.5087 0.5212 0.4665 0.0083  0.2241  -0.0849 333 HOH   A O   
6684 O  O   A HOH   F .   ? 0.2161 0.3524 0.3663 -0.0269 0.0733  0.1660  334 HOH   A O   
6685 O  O   . HOH   F .   ? 0.1786 0.1683 0.2292 0.0168  -0.0293 0.0277  335 HOH   A O   
6686 O  O   . HOH   F .   ? 0.2867 0.3390 0.3984 -0.0714 -0.0822 -0.0478 336 HOH   A O   
6687 O  O   . HOH   F .   ? 0.2540 0.2235 0.2980 0.0414  0.0316  0.0421  337 HOH   A O   
6688 O  O   . HOH   F .   ? 0.4987 0.1995 0.4482 0.0475  -0.1621 0.0338  338 HOH   A O   
6689 O  O   . HOH   F .   ? 0.2187 0.4299 0.3917 -0.0072 -0.0572 0.1565  339 HOH   A O   
6690 O  O   . HOH   F .   ? 0.2275 0.3942 0.3863 0.0903  -0.0595 -0.0143 340 HOH   A O   
6691 O  O   . HOH   F .   ? 0.4975 0.4067 0.4537 -0.2103 -0.1038 0.1894  341 HOH   A O   
6692 O  O   . HOH   F .   ? 0.1968 0.2244 0.2966 -0.0192 -0.0336 0.0839  342 HOH   A O   
6693 O  O   . HOH   F .   ? 0.1595 0.1684 0.2636 0.0058  -0.0265 -0.0449 343 HOH   A O   
6694 O  O   . HOH   F .   ? 0.1992 0.2006 0.4400 0.0186  0.1018  -0.0095 344 HOH   A O   
6695 O  O   . HOH   F .   ? 0.5980 0.6398 0.4326 0.1920  -0.0151 -0.0244 345 HOH   A O   
6696 O  O   B HOH   F .   ? 0.1862 0.2280 0.3282 0.0068  -0.0560 0.0166  346 HOH   A O   
6697 O  O   . HOH   F .   ? 0.2217 0.1742 0.2420 -0.0096 -0.0519 -0.0004 347 HOH   A O   
6698 O  O   . HOH   F .   ? 0.3825 0.4226 0.4204 0.2061  0.0692  0.0316  348 HOH   A O   
6699 O  O   . HOH   F .   ? 0.1444 0.2188 0.2315 0.0035  -0.0113 0.0569  349 HOH   A O   
6700 O  O   . HOH   F .   ? 0.4890 0.2151 0.5475 0.0482  0.0082  -0.0067 350 HOH   A O   
6701 O  O   . HOH   F .   ? 0.1451 0.1892 0.2720 0.0027  -0.0068 0.0200  351 HOH   A O   
6702 O  O   . HOH   F .   ? 0.2164 0.1713 0.2507 0.0297  -0.0332 -0.0003 352 HOH   A O   
6703 O  O   . HOH   F .   ? 0.4901 0.4913 0.2906 -0.1092 0.1280  0.0483  353 HOH   A O   
6704 O  O   A HOH   F .   ? 0.1770 0.2375 0.2388 0.0130  0.0211  0.0212  354 HOH   A O   
6705 O  O   . HOH   F .   ? 0.3964 0.2068 0.2805 0.1127  0.0661  0.0261  355 HOH   A O   
6706 O  O   . HOH   F .   ? 0.2879 0.3449 0.4588 -0.0642 -0.0888 -0.0810 356 HOH   A O   
6707 O  O   . HOH   F .   ? 0.6242 0.4051 0.3391 -0.0344 -0.0179 0.1568  357 HOH   A O   
6708 O  O   . HOH   F .   ? 0.1575 0.1324 0.2455 -0.0131 0.0152  -0.0045 358 HOH   A O   
6709 O  O   . HOH   F .   ? 0.1292 0.1205 0.1545 -0.0042 0.0128  0.0038  359 HOH   A O   
6710 O  O   . HOH   F .   ? 0.4108 0.2334 0.4051 -0.1057 0.1385  -0.0177 360 HOH   A O   
6711 O  O   . HOH   F .   ? 0.2700 0.4470 0.3265 0.0358  0.0729  0.1934  361 HOH   A O   
6712 O  O   . HOH   F .   ? 0.3230 0.3869 0.2430 -0.1190 0.0025  -0.0712 362 HOH   A O   
6713 O  O   . HOH   F .   ? 0.3143 0.6968 0.3205 0.1309  0.0612  -0.0646 363 HOH   A O   
6714 O  O   . HOH   F .   ? 0.2706 0.4306 0.3400 -0.0477 0.0545  0.0247  364 HOH   A O   
6715 O  O   . HOH   F .   ? 0.1937 0.2102 0.3270 -0.0023 -0.0487 0.0370  365 HOH   A O   
6716 O  O   . HOH   F .   ? 0.1920 0.1947 0.2421 -0.0389 -0.0021 0.0393  366 HOH   A O   
6717 O  O   . HOH   F .   ? 0.1442 0.1540 0.1634 -0.0066 -0.0114 -0.0015 367 HOH   A O   
6718 O  O   . HOH   F .   ? 0.1742 0.2274 0.1991 -0.0135 -0.0001 0.0722  368 HOH   A O   
6719 O  O   . HOH   F .   ? 0.3758 0.7265 0.4815 -0.0402 -0.1544 0.0739  369 HOH   A O   
6720 O  O   . HOH   F .   ? 0.4218 0.2446 0.4698 -0.1274 0.0808  0.0434  370 HOH   A O   
6721 O  O   . HOH   F .   ? 0.1693 0.1797 0.2531 -0.0268 0.0039  0.0487  371 HOH   A O   
6722 O  O   . HOH   F .   ? 0.1924 0.1862 0.2014 0.0018  0.0096  0.0206  372 HOH   A O   
6723 O  O   . HOH   F .   ? 0.4662 0.4103 0.6093 0.0836  0.1806  -0.1251 373 HOH   A O   
6724 O  O   A HOH   F .   ? 0.5138 0.2762 0.4604 -0.0298 -0.1042 0.0796  374 HOH   A O   
6725 O  O   . HOH   F .   ? 0.2086 0.2728 0.3621 0.0383  0.0797  -0.0546 375 HOH   A O   
6726 O  O   B HOH   F .   ? 0.2725 0.2230 0.2545 0.0433  -0.0197 -0.0165 376 HOH   A O   
6727 O  O   . HOH   F .   ? 0.1871 0.2823 0.2865 0.0467  0.0438  0.1062  377 HOH   A O   
6728 O  O   . HOH   F .   ? 0.3829 0.6290 0.4076 -0.0699 0.0110  0.1374  378 HOH   A O   
6729 O  O   A HOH   F .   ? 0.3143 0.1431 0.2081 0.0117  0.0176  -0.0112 379 HOH   A O   
6730 O  O   . HOH   F .   ? 0.1972 0.2437 0.2503 -0.0407 -0.0564 0.0678  380 HOH   A O   
6731 O  O   . HOH   F .   ? 0.2441 0.4268 0.3549 -0.0291 0.0050  0.0984  381 HOH   A O   
6732 O  O   B HOH   F .   ? 0.2988 0.3859 0.1861 -0.0093 -0.0142 0.0686  382 HOH   A O   
6733 O  O   . HOH   F .   ? 0.3295 0.2412 0.4800 -0.0766 -0.0291 0.0249  383 HOH   A O   
6734 O  O   T HOH   F .   ? 0.1072 0.1018 0.2582 -0.0140 0.0118  0.0505  384 HOH   A O   
6735 O  O   A HOH   F .   ? 0.2880 0.2141 0.2596 0.0815  0.0759  0.0454  385 HOH   A O   
6736 O  O   . HOH   F .   ? 0.3016 0.2824 0.2404 0.0292  0.0682  0.0027  386 HOH   A O   
6737 O  O   . HOH   F .   ? 0.1744 0.2563 0.2913 -0.0248 0.0601  0.0648  387 HOH   A O   
6738 O  O   . HOH   F .   ? 0.2667 0.2127 0.1873 -0.0798 0.0131  0.0388  388 HOH   A O   
6739 O  O   . HOH   F .   ? 0.3470 0.2656 0.3373 -0.0059 -0.0249 0.1024  389 HOH   A O   
6740 O  O   . HOH   F .   ? 0.3327 0.6607 0.5076 0.0946  0.1529  0.0419  390 HOH   A O   
6741 O  O   . HOH   F .   ? 0.4118 0.5597 0.5573 0.0662  -0.0727 0.1796  391 HOH   A O   
6742 O  O   . HOH   F .   ? 0.5488 0.5477 0.6859 -0.0750 0.0105  0.1478  392 HOH   A O   
6743 O  O   B HOH   F .   ? 0.3744 0.3413 0.2990 0.0708  -0.0745 -0.0229 393 HOH   A O   
6744 O  O   . HOH   F .   ? 0.2357 0.1893 0.2839 -0.0073 0.0230  0.0296  394 HOH   A O   
6745 O  O   . HOH   F .   ? 0.1573 0.1630 0.1852 0.0230  -0.0316 -0.0288 395 HOH   A O   
6746 O  O   . HOH   F .   ? 0.1721 0.1722 0.2161 0.0027  -0.0431 0.0032  396 HOH   A O   
6747 O  O   . HOH   F .   ? 0.2502 0.3867 0.3644 -0.0325 0.1010  -0.0778 397 HOH   A O   
6748 O  O   . HOH   F .   ? 0.2978 0.3168 0.2294 -0.0365 -0.0626 0.0348  398 HOH   A O   
6749 O  O   . HOH   F .   ? 0.1805 0.1922 0.3793 0.0352  0.0962  0.1044  399 HOH   A O   
6750 O  O   . HOH   F .   ? 0.1309 0.1448 0.2006 -0.0018 -0.0163 0.0101  400 HOH   A O   
6751 O  O   . HOH   F .   ? 0.4406 0.4734 0.2197 -0.0254 0.0816  0.0920  401 HOH   A O   
6752 O  O   . HOH   F .   ? 0.4770 0.2811 0.2869 -0.0997 0.0359  0.0358  402 HOH   A O   
6753 O  O   . HOH   F .   ? 0.1884 0.2649 0.3869 -0.0163 -0.0178 0.0237  403 HOH   A O   
6754 O  O   . HOH   F .   ? 0.6018 0.2818 0.5360 0.1034  -0.0480 -0.0298 404 HOH   A O   
6755 O  O   . HOH   F .   ? 0.3144 0.2724 0.2256 -0.0882 -0.0870 0.0512  405 HOH   A O   
6756 O  O   . HOH   F .   ? 0.2520 0.3036 0.3202 -0.0024 -0.0143 -0.0682 406 HOH   A O   
6757 O  O   . HOH   F .   ? 0.2309 0.1760 0.3258 -0.0026 -0.0285 0.0154  407 HOH   A O   
6758 O  O   . HOH   F .   ? 0.3056 0.3969 0.4098 -0.0656 0.1268  -0.0161 408 HOH   A O   
6759 O  O   . HOH   F .   ? 0.4697 0.4748 0.4112 0.1772  -0.1150 -0.1671 409 HOH   A O   
6760 O  O   A HOH   F .   ? 0.1814 0.1863 0.3223 -0.0084 0.0456  -0.0087 410 HOH   A O   
6761 O  O   . HOH   F .   ? 0.2801 0.6479 0.1806 -0.0286 0.0347  0.0025  411 HOH   A O   
6762 O  O   . HOH   F .   ? 0.2044 0.3009 0.2720 -0.0168 -0.0512 0.0669  412 HOH   A O   
6763 O  O   . HOH   F .   ? 0.6163 0.4133 0.4937 0.1807  -0.1146 0.1442  413 HOH   A O   
6764 O  O   . HOH   F .   ? 0.3056 0.3789 0.6932 -0.0194 0.1162  -0.0543 414 HOH   A O   
6765 O  O   . HOH   F .   ? 0.1503 0.1716 0.3255 -0.0040 0.0073  0.0204  415 HOH   A O   
6766 O  O   . HOH   F .   ? 0.4859 0.4821 0.3718 0.2174  0.0279  -0.0727 416 HOH   A O   
6767 O  O   . HOH   F .   ? 0.1768 0.1401 0.1700 -0.0205 0.0157  0.0030  417 HOH   A O   
6768 O  O   . HOH   F .   ? 0.2473 0.2125 0.2682 -0.0554 -0.0053 0.0690  418 HOH   A O   
6769 O  O   . HOH   F .   ? 0.5734 0.5397 0.4608 0.0076  0.1056  0.0261  419 HOH   A O   
6770 O  O   . HOH   F .   ? 0.1557 0.1942 0.2937 -0.0094 0.0145  0.0326  420 HOH   A O   
6771 O  O   A HOH   F .   ? 0.2490 0.2626 0.2443 -0.0161 0.0895  -0.0120 421 HOH   A O   
6772 O  O   A HOH   F .   ? 0.1673 0.2030 0.2975 0.0087  -0.0444 -0.0385 422 HOH   A O   
6773 O  O   . HOH   F .   ? 0.4281 0.2278 0.5550 -0.0850 -0.2382 0.1079  423 HOH   A O   
6774 O  O   . HOH   F .   ? 0.3250 0.1278 0.2231 0.0042  -0.0575 0.0096  424 HOH   A O   
6775 O  O   . HOH   F .   ? 0.4762 0.6318 0.3213 -0.0981 -0.0198 0.1534  425 HOH   A O   
6776 O  O   . HOH   F .   ? 0.2092 0.1602 0.1694 -0.0060 0.0155  0.0262  426 HOH   A O   
6777 O  O   . HOH   F .   ? 0.2358 0.3925 0.2718 0.1454  -0.0041 0.0198  427 HOH   A O   
6778 O  O   . HOH   F .   ? 0.3432 0.3553 0.2558 -0.0426 -0.0636 0.0288  428 HOH   A O   
6779 O  O   A HOH   F .   ? 0.1964 0.1861 0.2413 0.0049  -0.0157 0.0492  429 HOH   A O   
6780 O  O   . HOH   F .   ? 0.6223 0.6226 0.6566 -0.1536 -0.0547 -0.0646 430 HOH   A O   
6781 O  O   . HOH   F .   ? 0.2075 0.1903 0.3408 0.0166  -0.0690 0.0306  431 HOH   A O   
6782 O  O   . HOH   F .   ? 0.6503 0.7108 0.4494 0.1072  0.2752  -0.0508 432 HOH   A O   
6783 O  O   . HOH   F .   ? 0.9021 0.9352 0.7344 0.0419  -0.0218 -0.0341 433 HOH   A O   
6784 O  O   . HOH   F .   ? 0.3446 0.2892 0.2025 -0.0882 0.0187  0.0886  434 HOH   A O   
6785 O  O   . HOH   F .   ? 0.5766 0.8139 0.4476 0.2097  -0.0897 0.2215  435 HOH   A O   
6786 O  O   . HOH   F .   ? 0.4836 0.4769 0.4670 -0.1262 -0.0849 -0.1184 436 HOH   A O   
6787 O  O   B HOH   F .   ? 0.3684 0.3129 0.3940 0.0326  0.0863  -0.0257 437 HOH   A O   
6788 O  O   A HOH   F .   ? 0.2682 0.1872 0.2245 -0.0157 -0.0635 -0.0033 438 HOH   A O   
6789 O  O   . HOH   F .   ? 0.2515 0.1649 0.3177 0.0071  0.0095  0.0161  439 HOH   A O   
6790 O  O   . HOH   F .   ? 0.2981 0.3749 0.5556 -0.0063 0.1257  -0.1527 440 HOH   A O   
6791 O  O   . HOH   F .   ? 0.6128 0.6914 0.6031 -0.1083 0.0616  0.0570  441 HOH   A O   
6792 O  O   . HOH   F .   ? 0.5411 0.4874 0.3897 -0.0370 -0.1608 0.0199  442 HOH   A O   
6793 O  O   . HOH   F .   ? 0.1791 0.2266 0.4834 -0.0216 -0.0744 0.0649  443 HOH   A O   
6794 O  O   . HOH   F .   ? 0.5449 0.6289 0.7052 -0.1511 -0.0225 -0.1334 444 HOH   A O   
6795 O  O   . HOH   F .   ? 0.3589 0.3698 0.3318 0.2018  -0.0625 -0.0393 445 HOH   A O   
6796 O  O   . HOH   F .   ? 0.1766 0.1556 0.1885 -0.0066 -0.0274 -0.0132 446 HOH   A O   
6797 O  O   . HOH   F .   ? 0.5648 0.3135 0.5912 0.0771  0.0729  -0.0896 447 HOH   A O   
6798 O  O   A HOH   F .   ? 0.4898 0.1812 0.3024 -0.0675 0.0718  0.0563  448 HOH   A O   
6799 O  O   . HOH   F .   ? 0.2209 0.2688 0.2818 -0.0024 -0.0210 -0.0476 449 HOH   A O   
6800 O  O   . HOH   F .   ? 0.7386 0.4286 0.5060 0.1219  0.1144  0.2090  450 HOH   A O   
6801 O  O   . HOH   F .   ? 0.2357 0.1889 0.2946 0.0061  0.0261  0.0369  451 HOH   A O   
6802 O  O   . HOH   F .   ? 0.6556 0.6469 0.6247 0.0776  -0.1199 0.0018  452 HOH   A O   
6803 O  O   . HOH   F .   ? 0.6912 0.5591 0.7591 0.1312  -0.1266 0.1957  453 HOH   A O   
6804 O  O   . HOH   F .   ? 0.6340 0.5961 0.4787 -0.0730 0.0635  0.1004  454 HOH   A O   
6805 O  O   . HOH   F .   ? 0.5160 0.3602 0.4301 0.0419  0.0282  0.0364  455 HOH   A O   
6806 O  O   . HOH   F .   ? 0.3893 0.3290 0.3983 0.0263  0.0344  0.0488  456 HOH   A O   
6807 O  O   . HOH   F .   ? 0.4831 0.4975 0.4638 0.0865  0.0067  0.0985  457 HOH   A O   
6808 O  O   . HOH   F .   ? 0.3381 0.4052 0.4424 0.1441  -0.0459 0.1153  458 HOH   A O   
6809 O  O   . HOH   F .   ? 0.7122 0.7966 0.5014 0.1235  -0.0894 -0.0616 459 HOH   A O   
6810 O  O   . HOH   F .   ? 0.2574 0.2763 0.3871 -0.0482 0.0321  -0.0909 460 HOH   A O   
6811 O  O   . HOH   F .   ? 0.3700 0.4802 0.5189 -0.1672 0.1164  -0.1606 461 HOH   A O   
6812 O  O   . HOH   F .   ? 0.4400 0.4686 0.4519 0.0496  -0.0227 0.0823  462 HOH   A O   
6813 O  O   . HOH   F .   ? 0.2613 0.2965 0.3666 -0.0964 0.0400  -0.0360 463 HOH   A O   
6814 O  O   . HOH   F .   ? 0.2623 0.4623 0.4931 0.0639  0.0026  -0.1927 464 HOH   A O   
6815 O  O   . HOH   F .   ? 0.3382 0.4775 0.4574 -0.0708 0.0030  -0.0150 465 HOH   A O   
6816 O  O   A HOH   F .   ? 0.3125 0.2315 0.5062 0.0849  -0.1959 -0.0708 466 HOH   A O   
6817 O  O   . HOH   F .   ? 0.6194 0.3326 0.6875 0.0729  -0.0470 0.2047  467 HOH   A O   
6818 O  O   . HOH   F .   ? 0.4027 0.6330 0.3931 -0.1065 -0.0926 0.2247  468 HOH   A O   
6819 O  O   . HOH   F .   ? 0.7142 0.6414 0.6631 0.1512  0.1727  0.2596  469 HOH   A O   
6820 O  O   . HOH   F .   ? 0.5737 0.5190 0.4477 -0.0134 0.1024  0.0328  470 HOH   A O   
6821 O  O   . HOH   F .   ? 0.3973 0.5428 0.4085 0.0551  -0.0387 -0.0827 471 HOH   A O   
6822 O  O   . HOH   F .   ? 0.2463 0.1790 0.2790 0.0264  -0.0800 -0.0310 472 HOH   A O   
6823 O  O   . HOH   F .   ? 0.3614 0.2574 0.3761 0.0208  0.1009  -0.0026 473 HOH   A O   
6824 O  O   . HOH   F .   ? 0.5202 0.5110 0.5196 0.0895  -0.0357 -0.0954 474 HOH   A O   
6825 O  O   . HOH   F .   ? 0.3933 0.4705 0.2822 -0.0059 0.0003  -0.0025 475 HOH   A O   
6826 O  O   . HOH   F .   ? 0.4655 0.3028 0.3496 -0.0729 -0.1213 0.0626  476 HOH   A O   
6827 O  O   . HOH   F .   ? 0.7223 0.5855 0.6840 -0.0776 0.0526  -0.1018 477 HOH   A O   
6828 O  O   . HOH   F .   ? 0.4024 0.5188 0.3223 -0.0253 -0.0266 -0.0295 478 HOH   A O   
6829 O  O   . HOH   F .   ? 0.4766 0.4525 0.5035 -0.2394 -0.0610 -0.0166 479 HOH   A O   
6830 O  O   . HOH   F .   ? 0.2485 0.2100 0.2609 0.0191  0.0026  -0.0025 480 HOH   A O   
6831 O  O   . HOH   F .   ? 0.5382 0.5221 0.6210 -0.1987 -0.1326 -0.0036 481 HOH   A O   
6832 O  O   . HOH   F .   ? 0.8410 0.3816 0.3445 -0.0347 -0.1434 0.0637  482 HOH   A O   
6833 O  O   . HOH   F .   ? 0.5931 0.3978 0.4661 0.0067  -0.0166 -0.1086 483 HOH   A O   
6834 O  O   . HOH   F .   ? 0.5736 0.3887 0.4142 -0.0309 0.1357  -0.0350 484 HOH   A O   
6835 O  O   . HOH   F .   ? 0.2986 0.3960 0.4932 0.0005  0.1354  0.1005  485 HOH   A O   
6836 O  O   . HOH   F .   ? 0.5936 0.6527 0.4244 -0.0803 0.1013  0.1386  486 HOH   A O   
6837 O  O   . HOH   F .   ? 0.5754 0.5814 0.6959 0.0769  0.2218  -0.1130 487 HOH   A O   
6838 O  O   . HOH   F .   ? 0.2757 0.5190 0.3732 0.1046  0.1091  0.2358  488 HOH   A O   
6839 O  O   . HOH   F .   ? 0.2534 0.2507 0.7186 -0.0092 -0.1252 0.0386  489 HOH   A O   
6840 O  O   . HOH   F .   ? 0.5518 0.4917 0.5822 0.0626  -0.1175 0.0805  490 HOH   A O   
6841 O  O   . HOH   F .   ? 0.4690 0.3983 0.2832 -0.1105 0.1464  -0.0611 491 HOH   A O   
6842 O  O   . HOH   F .   ? 0.4035 0.3541 0.4955 -0.1086 -0.0415 0.1480  492 HOH   A O   
6843 O  O   . HOH   F .   ? 0.6723 0.5745 0.4273 0.2032  -0.1553 -0.0594 493 HOH   A O   
6844 O  O   . HOH   F .   ? 0.6012 0.4990 0.5250 -0.0816 -0.1161 -0.0614 494 HOH   A O   
6845 O  O   . HOH   F .   ? 0.4940 0.3310 0.5206 -0.0017 0.2654  0.0436  495 HOH   A O   
6846 O  O   . HOH   F .   ? 0.2742 0.2977 0.4756 0.0172  0.1067  0.0051  496 HOH   A O   
6847 O  O   . HOH   F .   ? 0.2829 0.2184 0.5624 0.0081  0.0114  0.0958  497 HOH   A O   
6848 O  O   B HOH   F .   ? 0.2357 0.4369 0.3825 0.0004  0.0686  0.0439  498 HOH   A O   
6849 O  O   . HOH   F .   ? 0.2905 0.4553 0.3409 -0.0143 -0.0251 -0.0782 499 HOH   A O   
6850 O  O   . HOH   F .   ? 0.4213 0.7897 0.5828 -0.0966 -0.0684 0.2247  500 HOH   A O   
6851 O  O   . HOH   F .   ? 0.2418 0.3576 0.3672 0.0604  -0.0619 0.0495  501 HOH   A O   
6852 O  O   . HOH   F .   ? 0.4950 0.2600 0.4423 -0.1512 -0.0065 0.0311  502 HOH   A O   
6853 O  O   . HOH   F .   ? 0.2646 0.4193 0.4583 0.0491  -0.0431 -0.0275 503 HOH   A O   
6854 O  O   . HOH   F .   ? 0.6820 0.3932 0.5743 0.1952  -0.0164 0.0890  504 HOH   A O   
6855 O  O   . HOH   F .   ? 0.6175 0.2633 0.3950 -0.0883 0.0684  0.0485  505 HOH   A O   
6856 O  O   . HOH   F .   ? 0.5776 0.7051 0.5009 0.0967  -0.0588 0.0686  506 HOH   A O   
6857 O  O   . HOH   F .   ? 0.2859 0.2379 0.4990 0.0104  0.0331  0.0703  507 HOH   A O   
6858 O  O   . HOH   F .   ? 0.5318 0.7054 0.5252 0.3152  0.0021  0.1759  508 HOH   A O   
6859 O  O   T HOH   F .   ? 0.1203 0.1134 0.2272 -0.0275 -0.0139 0.0639  509 HOH   A O   
6860 O  O   A HOH   F .   ? 0.3803 0.7520 0.3498 0.2038  0.0443  -0.0761 510 HOH   A O   
6861 O  O   . HOH   F .   ? 0.4951 0.5818 0.4396 -0.0591 -0.0359 -0.1282 511 HOH   A O   
6862 O  O   . HOH   F .   ? 0.2647 0.7007 0.4408 0.0372  0.0223  -0.0927 512 HOH   A O   
6863 O  O   . HOH   F .   ? 0.4966 0.7202 0.5394 -0.0577 -0.0751 0.0900  513 HOH   A O   
6864 O  O   . HOH   F .   ? 0.5151 0.4392 0.5002 0.1163  -0.0310 0.1404  514 HOH   A O   
6865 O  O   . HOH   F .   ? 0.2692 0.4631 0.5972 0.0211  -0.0827 0.2530  515 HOH   A O   
6866 O  O   . HOH   G .   ? 0.2337 0.2312 0.3400 0.0200  0.0808  0.0341  201 HOH   B O   
6867 O  O   . HOH   G .   ? 0.4901 0.3435 0.4283 -0.0269 0.0045  -0.1269 202 HOH   B O   
6868 O  O   . HOH   G .   ? 0.3461 0.3419 0.6677 -0.0678 0.0559  -0.0367 203 HOH   B O   
6869 O  O   . HOH   G .   ? 0.5064 0.5854 0.4267 0.2743  -0.1534 -0.0210 204 HOH   B O   
6870 O  O   . HOH   G .   ? 0.2933 0.6853 0.3707 0.0656  0.0096  0.2238  205 HOH   B O   
6871 O  O   . HOH   G .   ? 0.4312 0.4723 0.2760 0.0199  -0.0583 -0.1169 206 HOH   B O   
6872 O  O   . HOH   G .   ? 0.7068 0.3238 0.4386 0.0743  0.0687  0.0076  207 HOH   B O   
6873 O  O   . HOH   G .   ? 0.4786 0.3971 0.6130 0.0372  -0.0981 0.2575  208 HOH   B O   
6874 O  O   . HOH   G .   ? 0.2926 0.2015 0.5975 0.0196  0.1949  0.0786  209 HOH   B O   
6875 O  O   . HOH   G .   ? 0.2748 0.5335 0.5169 -0.0179 0.1303  -0.1992 210 HOH   B O   
6876 O  O   . HOH   G .   ? 0.6365 0.5746 0.5834 0.1346  0.0571  -0.0257 211 HOH   B O   
6877 O  O   . HOH   G .   ? 0.3753 0.4260 0.5354 -0.1032 0.0163  -0.1377 212 HOH   B O   
6878 O  O   . HOH   G .   ? 0.3221 0.5109 0.5360 0.2143  0.0481  -0.0411 213 HOH   B O   
6879 O  O   . HOH   G .   ? 0.4498 0.4943 0.3988 0.2554  -0.0468 0.0372  214 HOH   B O   
6880 O  O   . HOH   G .   ? 0.3247 0.2258 0.5226 -0.0033 0.1866  0.0431  215 HOH   B O   
6881 O  O   . HOH   G .   ? 0.2820 0.2770 0.6679 0.0553  -0.1088 0.0698  216 HOH   B O   
6882 O  O   . HOH   G .   ? 0.1883 0.2333 0.3139 -0.0085 0.0137  -0.0302 217 HOH   B O   
6883 O  O   . HOH   G .   ? 0.1632 0.2000 0.3090 -0.0158 -0.0037 0.0043  218 HOH   B O   
6884 O  O   . HOH   G .   ? 0.4529 0.4120 0.6396 -0.0421 -0.1609 -0.0779 219 HOH   B O   
6885 O  O   . HOH   G .   ? 0.4215 0.3771 0.3760 0.0105  -0.1111 0.0510  220 HOH   B O   
6886 O  O   . HOH   G .   ? 0.4461 0.6218 0.3677 0.1986  0.0286  0.0059  221 HOH   B O   
6887 O  O   . HOH   G .   ? 0.1652 0.2031 0.3553 -0.0167 0.0085  -0.0034 222 HOH   B O   
6888 O  O   . HOH   G .   ? 0.5757 0.3027 0.3523 -0.1812 0.0358  0.0198  223 HOH   B O   
6889 O  O   . HOH   G .   ? 0.4135 0.4541 0.3834 0.0122  0.0497  -0.1696 224 HOH   B O   
6890 O  O   . HOH   G .   ? 0.3604 0.3097 0.4866 0.0977  -0.0092 0.0206  225 HOH   B O   
6891 O  O   . HOH   G .   ? 0.2259 0.2248 0.4389 -0.0354 -0.0055 -0.0649 226 HOH   B O   
6892 O  O   . HOH   G .   ? 0.6686 0.6351 0.3455 0.0922  0.0117  0.0396  227 HOH   B O   
6893 O  O   . HOH   G .   ? 0.5172 0.2114 0.3037 -0.0082 -0.1023 0.0034  228 HOH   B O   
6894 O  O   . HOH   G .   ? 0.2233 0.2497 0.3262 -0.0555 0.0109  -0.0262 229 HOH   B O   
6895 O  O   . HOH   G .   ? 0.2784 0.3068 0.6464 -0.0283 0.0438  -0.0170 230 HOH   B O   
6896 O  O   . HOH   G .   ? 0.4699 0.3365 0.4333 -0.2308 -0.0230 0.0320  231 HOH   B O   
6897 O  O   . HOH   G .   ? 0.6376 0.3688 0.2798 -0.0644 0.0441  0.0055  232 HOH   B O   
6898 O  O   . HOH   G .   ? 0.2532 0.1760 0.2974 -0.0360 0.1106  -0.0107 233 HOH   B O   
6899 O  O   . HOH   G .   ? 0.3542 0.1738 0.2137 0.0139  -0.0690 -0.0056 234 HOH   B O   
6900 O  O   . HOH   G .   ? 0.1451 0.1407 0.1734 -0.0180 -0.0111 -0.0030 235 HOH   B O   
6901 O  O   . HOH   G .   ? 0.2070 0.1339 0.3560 0.0068  -0.0682 -0.0137 236 HOH   B O   
6902 O  O   . HOH   G .   ? 0.2612 0.2571 0.3199 0.0289  0.0310  -0.0806 237 HOH   B O   
6903 O  O   . HOH   G .   ? 0.2916 0.3666 0.2916 -0.0840 0.0370  -0.0238 238 HOH   B O   
6904 O  O   . HOH   G .   ? 0.3919 0.3025 0.2311 0.0406  0.0535  0.0454  239 HOH   B O   
6905 O  O   . HOH   G .   ? 0.3685 0.2655 0.4201 0.0606  -0.1136 -0.1060 240 HOH   B O   
6906 O  O   . HOH   G .   ? 0.7136 0.5024 0.4688 0.1976  -0.0212 -0.1409 241 HOH   B O   
6907 O  O   . HOH   G .   ? 0.1583 0.1531 0.2919 -0.0003 -0.0008 -0.0039 242 HOH   B O   
6908 O  O   . HOH   G .   ? 0.2150 0.3955 0.2687 -0.0482 -0.0223 0.0555  243 HOH   B O   
6909 O  O   . HOH   G .   ? 0.2163 0.1916 0.2222 -0.0356 -0.0456 0.0199  244 HOH   B O   
6910 O  O   . HOH   G .   ? 0.4015 0.2813 0.4142 0.0920  -0.0305 -0.0591 245 HOH   B O   
6911 O  O   . HOH   G .   ? 0.4068 0.4070 0.5692 -0.1627 -0.0026 0.0963  246 HOH   B O   
6912 O  O   . HOH   G .   ? 0.2452 0.4694 0.5813 0.1397  -0.0651 -0.1180 247 HOH   B O   
6913 O  O   . HOH   G .   ? 0.2230 0.3738 0.3271 -0.0527 -0.0776 -0.0332 248 HOH   B O   
6914 O  O   . HOH   G .   ? 0.3207 0.1693 0.6193 -0.0171 -0.1092 -0.0246 249 HOH   B O   
6915 O  O   . HOH   G .   ? 0.3114 0.4242 0.2403 0.0275  0.0659  0.0321  250 HOH   B O   
6916 O  O   . HOH   G .   ? 0.1505 0.1335 0.1770 -0.0033 -0.0118 0.0091  251 HOH   B O   
6917 O  O   . HOH   G .   ? 0.2985 0.4043 0.2887 -0.0932 -0.0439 -0.0384 252 HOH   B O   
6918 O  O   . HOH   G .   ? 0.4755 0.3664 0.3540 -0.1177 0.0624  -0.1258 253 HOH   B O   
6919 O  O   . HOH   G .   ? 0.3166 0.2553 0.3436 -0.0368 0.0070  -0.0556 254 HOH   B O   
6920 O  O   . HOH   G .   ? 0.2908 0.2070 0.3060 0.0767  0.0660  -0.0073 255 HOH   B O   
6921 O  O   . HOH   G .   ? 0.2114 0.1484 0.2330 -0.0350 -0.0459 0.0283  256 HOH   B O   
6922 O  O   . HOH   G .   ? 0.2755 0.2243 0.2120 0.0234  -0.0159 -0.0041 257 HOH   B O   
6923 O  O   . HOH   G .   ? 0.2448 0.2067 0.2910 0.0796  -0.0829 -0.0636 258 HOH   B O   
6924 O  O   . HOH   G .   ? 0.2240 0.3009 0.2262 -0.0539 0.0309  0.0390  259 HOH   B O   
6925 O  O   . HOH   G .   ? 0.2851 0.2114 0.4864 0.0047  0.0512  0.0564  260 HOH   B O   
6926 O  O   . HOH   G .   ? 0.3389 0.5011 0.3513 -0.0299 -0.1213 0.0947  261 HOH   B O   
6927 O  O   . HOH   G .   ? 0.1606 0.1682 0.3377 -0.0279 -0.0262 0.0204  262 HOH   B O   
6928 O  O   . HOH   G .   ? 0.2584 0.3656 0.3728 0.0333  0.1246  0.0346  263 HOH   B O   
6929 O  O   . HOH   G .   ? 0.4342 0.2636 0.4433 -0.0223 -0.1339 -0.0452 264 HOH   B O   
6930 O  O   . HOH   G .   ? 0.2753 0.4696 0.6498 0.0232  0.0318  -0.1129 265 HOH   B O   
6931 O  O   . HOH   G .   ? 0.1363 0.1664 0.2418 -0.0047 0.0118  0.0192  266 HOH   B O   
6932 O  O   . HOH   G .   ? 0.2187 0.1945 0.3762 -0.0003 -0.0664 -0.0301 267 HOH   B O   
6933 O  O   . HOH   G .   ? 0.2593 0.1882 0.3044 -0.0638 0.0163  -0.0121 268 HOH   B O   
6934 O  O   . HOH   G .   ? 0.2010 0.1532 0.2451 -0.0278 -0.0155 0.0188  269 HOH   B O   
6935 O  O   . HOH   G .   ? 0.4435 0.3756 0.2887 0.0467  -0.0146 -0.0915 270 HOH   B O   
6936 O  O   . HOH   G .   ? 0.2250 0.2183 0.2306 -0.0054 -0.0093 -0.0081 271 HOH   B O   
6937 O  O   . HOH   G .   ? 0.2470 0.2911 0.2618 -0.0477 -0.0802 0.0144  272 HOH   B O   
6938 O  O   . HOH   G .   ? 0.2222 0.4231 0.4795 -0.0279 -0.0258 -0.1514 273 HOH   B O   
6939 O  O   . HOH   G .   ? 0.3422 0.4145 0.4931 0.1360  -0.0752 -0.1148 274 HOH   B O   
6940 O  O   . HOH   G .   ? 0.4301 0.2922 0.5353 0.0225  -0.0051 -0.0522 275 HOH   B O   
6941 O  O   . HOH   G .   ? 0.1828 0.1789 0.1830 -0.0440 -0.0481 0.0098  276 HOH   B O   
6942 O  O   . HOH   G .   ? 0.1831 0.1435 0.3812 -0.0039 -0.0320 -0.0014 277 HOH   B O   
6943 O  O   . HOH   G .   ? 0.2431 0.3804 0.2457 0.1302  -0.0226 -0.0412 278 HOH   B O   
6944 O  O   . HOH   G .   ? 0.2418 0.2526 0.2526 -0.0440 -0.0725 -0.0407 279 HOH   B O   
6945 O  O   . HOH   G .   ? 0.1604 0.1542 0.3810 -0.0140 0.0080  0.0005  280 HOH   B O   
6946 O  O   . HOH   G .   ? 0.2723 0.7256 0.2604 0.0981  -0.0341 -0.0406 281 HOH   B O   
6947 O  O   . HOH   G .   ? 0.2268 0.3356 0.3462 -0.0490 0.0385  -0.0970 282 HOH   B O   
6948 O  O   . HOH   G .   ? 0.2767 0.7461 0.7235 0.1584  -0.0751 -0.1204 283 HOH   B O   
6949 O  O   . HOH   G .   ? 0.1681 0.1538 0.1980 0.0011  0.0039  0.0035  284 HOH   B O   
6950 O  O   . HOH   G .   ? 0.5743 0.3644 0.3242 0.2519  0.1102  0.0825  285 HOH   B O   
6951 O  O   . HOH   G .   ? 0.3806 0.2234 0.4265 -0.1095 -0.2013 0.1010  286 HOH   B O   
6952 O  O   . HOH   G .   ? 0.2422 0.2740 0.3083 0.0101  -0.0811 0.0239  287 HOH   B O   
6953 O  O   . HOH   G .   ? 0.2917 0.4925 0.4633 -0.1127 -0.1157 0.0840  288 HOH   B O   
6954 O  O   . HOH   G .   ? 0.3483 0.2840 0.3016 -0.0366 0.0141  -0.1275 289 HOH   B O   
6955 O  O   . HOH   G .   ? 0.1690 0.2060 0.3070 0.0205  -0.0036 0.0071  290 HOH   B O   
6956 O  O   . HOH   G .   ? 0.3721 0.2666 0.2329 0.0077  -0.0928 -0.0025 291 HOH   B O   
6957 O  O   . HOH   G .   ? 0.1603 0.2023 0.1709 -0.0060 -0.0228 0.0068  292 HOH   B O   
6958 O  O   . HOH   G .   ? 0.4413 0.5161 0.2537 0.0082  0.0529  0.1192  293 HOH   B O   
6959 O  O   . HOH   G .   ? 0.1785 0.3497 0.4927 0.0224  0.0086  -0.1411 294 HOH   B O   
6960 O  O   . HOH   G .   ? 0.1721 0.1649 0.2591 0.0072  0.0056  0.0126  295 HOH   B O   
6961 O  O   . HOH   G .   ? 0.5179 0.3771 0.2495 0.1403  -0.1071 0.0331  296 HOH   B O   
6962 O  O   . HOH   G .   ? 0.4537 0.6568 0.2403 0.0376  -0.1064 0.0335  297 HOH   B O   
6963 O  O   . HOH   G .   ? 0.4313 0.4912 0.4767 0.0049  -0.1645 0.0150  298 HOH   B O   
6964 O  O   . HOH   G .   ? 0.2968 0.3003 0.5487 -0.0335 -0.0822 0.1346  299 HOH   B O   
6965 O  O   . HOH   G .   ? 0.2041 0.2854 0.6225 0.0447  -0.0583 -0.1163 300 HOH   B O   
6966 O  O   . HOH   G .   ? 0.3300 0.3913 0.4030 -0.1523 0.1082  -0.0340 301 HOH   B O   
6967 O  O   . HOH   G .   ? 0.3582 0.7557 0.3767 0.1283  -0.0641 0.1240  302 HOH   B O   
6968 O  O   . HOH   G .   ? 0.2787 0.3030 0.3738 -0.0562 0.1062  -0.1003 303 HOH   B O   
6969 O  O   . HOH   G .   ? 0.5830 0.6433 0.5535 0.3190  -0.0106 -0.0283 304 HOH   B O   
6970 O  O   . HOH   G .   ? 0.2074 0.1564 0.3626 0.0371  -0.0972 -0.0052 305 HOH   B O   
6971 O  O   . HOH   G .   ? 0.3442 0.1853 0.3648 0.0687  0.1073  0.0439  306 HOH   B O   
6972 O  O   . HOH   G .   ? 0.4640 0.3560 0.4250 -0.0696 0.0461  0.1160  307 HOH   B O   
6973 O  O   . HOH   G .   ? 0.5010 0.3001 0.2297 -0.1821 0.0579  -0.0178 308 HOH   B O   
6974 O  O   . HOH   G .   ? 0.1599 0.1443 0.3437 0.0055  -0.0102 -0.0030 309 HOH   B O   
6975 O  O   . HOH   G .   ? 0.2484 0.1461 0.2873 -0.0160 -0.0329 0.0291  310 HOH   B O   
6976 O  O   . HOH   G .   ? 0.2111 0.1621 0.2861 -0.0273 -0.0341 -0.0043 311 HOH   B O   
6977 O  O   . HOH   G .   ? 0.2223 0.3196 0.4678 -0.0247 -0.0355 -0.0212 312 HOH   B O   
6978 O  O   . HOH   G .   ? 0.2217 0.1963 0.2086 -0.0104 0.0193  0.0217  313 HOH   B O   
6979 O  O   . HOH   G .   ? 0.4548 0.4849 0.2482 0.1439  -0.0852 -0.0323 314 HOH   B O   
6980 O  O   . HOH   G .   ? 0.1566 0.1876 0.3092 -0.0260 -0.0152 0.0155  315 HOH   B O   
6981 O  O   . HOH   G .   ? 0.4633 0.3058 0.5234 0.1139  0.2267  0.1666  316 HOH   B O   
6982 O  O   . HOH   G .   ? 0.3827 0.4458 0.7679 -0.0088 -0.1052 0.2292  317 HOH   B O   
6983 O  O   . HOH   G .   ? 0.2235 0.2278 0.5820 -0.0396 -0.0067 0.1426  318 HOH   B O   
6984 O  O   . HOH   G .   ? 0.3955 0.2372 0.2756 0.1442  0.0948  0.0225  319 HOH   B O   
6985 O  O   . HOH   G .   ? 0.1589 0.1588 0.3275 -0.0158 -0.0238 -0.0123 320 HOH   B O   
6986 O  O   . HOH   G .   ? 0.5118 0.4174 0.2875 0.0160  -0.0766 -0.0624 321 HOH   B O   
6987 O  O   . HOH   G .   ? 0.2147 0.5382 0.5068 -0.0516 -0.0110 -0.0026 322 HOH   B O   
6988 O  O   . HOH   G .   ? 0.1683 0.2976 0.2465 -0.0104 -0.0112 0.0802  323 HOH   B O   
6989 O  O   . HOH   G .   ? 0.4327 0.4061 0.5603 0.0615  -0.0254 0.0509  324 HOH   B O   
6990 O  O   . HOH   G .   ? 0.4719 0.2452 0.3231 0.0079  -0.0013 0.0664  325 HOH   B O   
6991 O  O   . HOH   G .   ? 0.1917 0.1966 0.3057 0.0268  0.0438  0.0266  326 HOH   B O   
6992 O  O   . HOH   G .   ? 0.3182 0.2280 0.2528 0.0340  -0.0261 0.0311  327 HOH   B O   
6993 O  O   . HOH   G .   ? 0.5945 0.4783 0.6813 0.1376  -0.1131 0.1714  328 HOH   B O   
6994 O  O   . HOH   G .   ? 0.2930 0.3524 0.4789 -0.0579 -0.1513 0.1495  329 HOH   B O   
6995 O  O   . HOH   G .   ? 0.2681 0.1984 0.5067 0.0076  0.0058  0.0528  330 HOH   B O   
6996 O  O   . HOH   G .   ? 0.1716 0.2928 0.3484 0.0256  -0.0265 -0.0613 331 HOH   B O   
6997 O  O   . HOH   G .   ? 0.6343 0.4458 0.5420 0.0913  0.1140  -0.0470 332 HOH   B O   
6998 O  O   . HOH   G .   ? 0.8203 0.2166 0.3422 0.0337  -0.0923 -0.0289 333 HOH   B O   
6999 O  O   . HOH   G .   ? 0.5503 0.3731 0.3909 0.0293  0.1094  0.1592  334 HOH   B O   
7000 O  O   . HOH   G .   ? 0.5996 0.5636 0.5663 -0.1177 -0.0678 0.1809  335 HOH   B O   
7001 O  O   . HOH   G .   ? 0.1761 0.1419 0.2543 0.0042  -0.0327 0.0069  336 HOH   B O   
7002 O  O   . HOH   G .   ? 0.4691 0.7349 0.3941 -0.0321 -0.0757 0.2057  337 HOH   B O   
7003 O  O   . HOH   G .   ? 0.5449 0.4218 0.6489 -0.0397 -0.0849 -0.1311 338 HOH   B O   
7004 O  O   . HOH   G .   ? 0.5230 0.3659 0.4465 0.0205  0.0603  -0.1535 339 HOH   B O   
7005 O  O   . HOH   G .   ? 0.4690 0.3348 0.3214 0.0588  -0.1158 -0.0822 340 HOH   B O   
7006 O  O   . HOH   G .   ? 0.7382 0.6548 0.3294 -0.0317 -0.0664 0.1183  341 HOH   B O   
7007 O  O   . HOH   G .   ? 0.3750 0.6262 0.4311 -0.1032 -0.0871 -0.0581 342 HOH   B O   
7008 O  O   . HOH   G .   ? 0.2222 0.5935 0.6379 -0.0376 -0.0833 -0.0319 343 HOH   B O   
7009 O  O   . HOH   G .   ? 0.4996 0.5229 0.3657 -0.0031 -0.1167 0.0081  344 HOH   B O   
7010 O  O   . HOH   G .   ? 0.2933 0.1868 0.4095 0.0317  -0.1088 -0.0474 345 HOH   B O   
7011 O  O   . HOH   G .   ? 0.2100 0.1934 0.3246 -0.0045 0.0567  -0.0150 346 HOH   B O   
7012 O  O   . HOH   G .   ? 0.4926 0.5856 0.5169 -0.1204 0.0305  0.1319  347 HOH   B O   
7013 O  O   . HOH   G .   ? 0.2253 0.4430 0.5233 0.0355  0.0399  0.0239  348 HOH   B O   
7014 O  O   . HOH   G .   ? 0.4264 0.5224 0.5227 -0.0034 -0.0923 0.0638  349 HOH   B O   
7015 O  O   . HOH   G .   ? 0.2722 0.2298 0.4941 -0.0247 -0.0925 -0.0439 350 HOH   B O   
7016 O  O   . HOH   G .   ? 0.2429 0.6472 0.3506 0.1578  -0.0533 -0.1331 351 HOH   B O   
7017 O  O   . HOH   G .   ? 0.4368 0.5412 0.6472 -0.0144 0.0180  -0.0372 352 HOH   B O   
7018 O  O   . HOH   G .   ? 0.3540 0.2197 0.3258 -0.0465 -0.0029 -0.0596 353 HOH   B O   
7019 O  O   . HOH   G .   ? 0.3645 0.4428 0.4714 -0.1486 0.0145  -0.0638 354 HOH   B O   
7020 O  O   . HOH   G .   ? 0.5065 0.3755 0.4097 0.0488  0.1203  -0.0702 355 HOH   B O   
7021 O  O   . HOH   G .   ? 0.4830 0.3371 0.5229 -0.1345 0.1158  0.0542  356 HOH   B O   
7022 O  O   . HOH   G .   ? 0.3590 0.2755 0.3604 -0.0989 -0.0166 -0.0608 357 HOH   B O   
7023 O  O   . HOH   G .   ? 0.4823 0.5208 0.4659 0.1514  -0.1199 0.1453  358 HOH   B O   
7024 O  O   . HOH   G .   ? 0.4703 0.3952 0.6087 0.0315  0.0869  0.1313  359 HOH   B O   
7025 O  O   . HOH   G .   ? 0.5398 0.3606 0.5187 -0.0090 -0.1481 -0.0621 360 HOH   B O   
7026 O  O   . HOH   G .   ? 0.2237 0.3779 0.6739 -0.0821 -0.0700 -0.0585 361 HOH   B O   
7027 O  O   . HOH   G .   ? 0.4582 0.5899 0.3121 0.1610  0.0032  0.0342  362 HOH   B O   
7028 O  O   . HOH   G .   ? 0.5643 0.4676 0.5760 -0.0541 0.0160  0.0206  363 HOH   B O   
7029 O  O   . HOH   G .   ? 0.4649 0.3177 0.5525 -0.1445 -0.0650 0.0252  364 HOH   B O   
7030 O  O   . HOH   G .   ? 0.6603 0.2362 0.3838 -0.0218 0.0080  0.0618  365 HOH   B O   
7031 O  O   . HOH   G .   ? 0.6136 0.4855 0.4183 0.1262  0.0302  0.0861  366 HOH   B O   
7032 O  O   . HOH   G .   ? 0.5364 0.5745 0.4427 -0.0924 -0.0508 -0.1054 367 HOH   B O   
7033 O  O   . HOH   G .   ? 0.4254 0.3724 0.5349 0.1130  -0.1655 0.0090  368 HOH   B O   
7034 O  O   . HOH   G .   ? 0.5288 0.5260 0.3716 0.1089  -0.1681 0.0534  369 HOH   B O   
7035 O  O   . HOH   G .   ? 0.3931 0.5559 0.4872 0.2357  0.0909  0.1500  370 HOH   B O   
7036 O  O   . HOH   G .   ? 0.5547 0.3590 0.2983 -0.1013 -0.0889 -0.0520 371 HOH   B O   
7037 O  O   . HOH   G .   ? 0.3877 0.3358 0.4154 0.0888  -0.1222 -0.0574 372 HOH   B O   
7038 O  O   . HOH   G .   ? 0.7540 0.7696 0.5358 0.2050  -0.1460 0.0979  373 HOH   B O   
7039 O  O   . HOH   G .   ? 0.4583 0.5014 0.4648 -0.0909 -0.0577 0.0101  374 HOH   B O   
7040 O  O   . HOH   G .   ? 0.2232 0.4766 0.4056 0.0169  -0.0578 -0.0594 375 HOH   B O   
7041 O  O   . HOH   G .   ? 0.3950 0.5727 0.2251 -0.0777 0.0412  0.0078  376 HOH   B O   
7042 O  O   . HOH   G .   ? 0.4564 0.7293 0.5619 0.1222  0.0395  0.2929  377 HOH   B O   
7043 O  O   . HOH   G .   ? 0.7410 0.3802 0.5079 -0.1254 -0.0845 0.0401  378 HOH   B O   
7044 O  O   . HOH   G .   ? 0.5569 0.6859 0.3957 -0.1412 0.0314  -0.1533 379 HOH   B O   
7045 O  O   . HOH   G .   ? 0.3819 0.4410 0.4848 0.1311  -0.0120 0.0002  380 HOH   B O   
7046 O  O   . HOH   G .   ? 0.5686 0.6583 0.6169 -0.0476 0.2340  0.1032  381 HOH   B O   
7047 O  O   . HOH   G .   ? 0.3242 0.2700 0.2967 0.0028  0.0379  0.0204  382 HOH   B O   
7048 O  O   . HOH   G .   ? 0.5089 0.4958 0.4752 0.0296  -0.0395 -0.0541 383 HOH   B O   
7049 O  O   . HOH   G .   ? 0.6606 0.4186 0.3732 0.1083  0.0823  -0.0260 384 HOH   B O   
7050 O  O   . HOH   G .   ? 0.4428 0.7908 0.5754 0.0752  0.2133  0.0702  385 HOH   B O   
7051 O  O   . HOH   G .   ? 0.2396 0.4417 0.4294 -0.0801 -0.1061 -0.0322 386 HOH   B O   
7052 O  O   . HOH   G .   ? 0.4800 0.3750 0.3995 0.0071  0.0501  -0.0257 387 HOH   B O   
7053 O  O   . HOH   G .   ? 0.6082 0.4444 0.5031 -0.0823 0.0584  -0.0356 388 HOH   B O   
7054 O  O   . HOH   G .   ? 0.7336 0.5410 0.4364 0.1970  -0.0045 0.0267  389 HOH   B O   
7055 O  O   . HOH   G .   ? 0.3751 0.2167 0.3377 0.0569  -0.0303 0.0064  390 HOH   B O   
7056 O  O   . HOH   G .   ? 0.4816 0.4451 0.5067 0.0321  0.0721  0.0646  391 HOH   B O   
7057 O  O   . HOH   G .   ? 0.3942 0.2193 0.5801 -0.0193 0.0981  0.0562  392 HOH   B O   
7058 O  O   . HOH   G .   ? 0.2502 0.4254 0.6920 -0.1189 -0.0715 -0.0404 393 HOH   B O   
7059 O  O   . HOH   G .   ? 0.4608 0.6544 0.4261 0.1550  0.0491  -0.1047 394 HOH   B O   
7060 O  O   . HOH   G .   ? 0.3252 0.3674 0.4270 0.0220  0.0337  -0.0580 395 HOH   B O   
7061 O  O   . HOH   G .   ? 0.4549 0.4460 0.4479 0.0217  0.0910  0.0923  396 HOH   B O   
7062 O  O   . HOH   G .   ? 0.2057 0.2837 0.6019 -0.0684 -0.0895 0.0317  397 HOH   B O   
7063 O  O   . HOH   G .   ? 0.5667 0.4359 0.3182 -0.2429 -0.0602 0.1072  398 HOH   B O   
7064 O  O   . HOH   G .   ? 0.6075 0.5942 0.6558 0.0695  -0.1371 0.1825  399 HOH   B O   
7065 O  O   . HOH   G .   ? 0.5360 0.5754 0.3651 0.1526  -0.0075 -0.0287 400 HOH   B O   
# 
