data_7HFJ
# 
_entry.id   7HFJ 
# 
_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   7HFJ         pdb_00007hfj 10.2210/pdb7hfj/pdb 
WWPDB D_1001407409 ?            ?                   
# 
_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                        7HFJ 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                                     18178.766 2   
'3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn '(1R,4S,5R)-4-{[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}-2-oxabicyclo[3.1.1]heptan-4-ol' 260.292   1   ? ? 
? ?                                                                                    
3 non-polymer syn 'CHLORIDE ION'                                                                                 35.453    1   ? ? 
? ?                                                                                    
4 water       nat water                                                                                          18.015    411 ? ? 
? ?                                                                                    
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(1R,4S,5R)-4-{[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}-2-oxabicyclo[3.1.1]heptan-4-ol' A1BBK 
3 'CHLORIDE ION'                                                                                 CL    
4 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 
A1BBK non-polymer         . '(1R,4S,5R)-4-{[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}-2-oxabicyclo[3.1.1]heptan-4-ol' ? 
'C13 H16 N4 O2'  260.292 
ALA   'L-peptide linking' y ALANINE                                                                                        ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                       ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                     ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                ? 
'C4 H7 N O4'     133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                                                 ? 
'Cl -1'          35.453  
CYS   'L-peptide linking' y CYSTEINE                                                                                       ? 
'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                      ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                        ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                      ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                          ? 
'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                     ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                        ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                         ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                     ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                  ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                        ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                         ? 
'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                      ? 
'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                                                       ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                         ? 
'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1BBK 1   201 201  A1BBK LA1 A . 
D 3 CL    1   202 1    CL    CL  A . 
E 4 HOH   1   301 292  HOH   HOH A . 
E 4 HOH   2   302 196  HOH   HOH A . 
E 4 HOH   3   303 1289 HOH   HOH A . 
E 4 HOH   4   304 209  HOH   HOH A . 
E 4 HOH   5   305 1301 HOH   HOH A . 
E 4 HOH   6   306 625  HOH   HOH A . 
E 4 HOH   7   307 661  HOH   HOH A . 
E 4 HOH   8   308 109  HOH   HOH A . 
E 4 HOH   9   309 409  HOH   HOH A . 
E 4 HOH   10  310 662  HOH   HOH A . 
E 4 HOH   11  311 153  HOH   HOH A . 
E 4 HOH   12  312 337  HOH   HOH A . 
E 4 HOH   13  313 93   HOH   HOH A . 
E 4 HOH   14  314 124  HOH   HOH A . 
E 4 HOH   15  315 247  HOH   HOH A . 
E 4 HOH   16  316 136  HOH   HOH A . 
E 4 HOH   17  317 49   HOH   HOH A . 
E 4 HOH   18  318 35   HOH   HOH A . 
E 4 HOH   19  319 1295 HOH   HOH A . 
E 4 HOH   20  320 229  HOH   HOH A . 
E 4 HOH   21  321 34   HOH   HOH A . 
E 4 HOH   22  322 469  HOH   HOH A . 
E 4 HOH   23  323 76   HOH   HOH A . 
E 4 HOH   24  324 105  HOH   HOH A . 
E 4 HOH   25  325 86   HOH   HOH A . 
E 4 HOH   26  326 36   HOH   HOH A . 
E 4 HOH   27  327 164  HOH   HOH A . 
E 4 HOH   28  328 236  HOH   HOH A . 
E 4 HOH   29  329 199  HOH   HOH A . 
E 4 HOH   30  330 1300 HOH   HOH A . 
E 4 HOH   31  331 15   HOH   HOH A . 
E 4 HOH   32  332 57   HOH   HOH A . 
E 4 HOH   33  333 85   HOH   HOH A . 
E 4 HOH   34  334 151  HOH   HOH A . 
E 4 HOH   35  335 1296 HOH   HOH A . 
E 4 HOH   36  336 630  HOH   HOH A . 
E 4 HOH   37  337 1283 HOH   HOH A . 
E 4 HOH   38  338 17   HOH   HOH A . 
E 4 HOH   39  339 155  HOH   HOH A . 
E 4 HOH   40  340 493  HOH   HOH A . 
E 4 HOH   41  341 218  HOH   HOH A . 
E 4 HOH   42  342 964  HOH   HOH A . 
E 4 HOH   43  343 165  HOH   HOH A . 
E 4 HOH   44  344 354  HOH   HOH A . 
E 4 HOH   45  345 102  HOH   HOH A . 
E 4 HOH   46  346 1290 HOH   HOH A . 
E 4 HOH   47  347 132  HOH   HOH A . 
E 4 HOH   48  348 225  HOH   HOH A . 
E 4 HOH   49  349 393  HOH   HOH A . 
E 4 HOH   50  350 140  HOH   HOH A . 
E 4 HOH   51  351 461  HOH   HOH A . 
E 4 HOH   52  352 42   HOH   HOH A . 
E 4 HOH   53  353 33   HOH   HOH A . 
E 4 HOH   54  354 18   HOH   HOH A . 
E 4 HOH   55  355 192  HOH   HOH A . 
E 4 HOH   56  356 241  HOH   HOH A . 
E 4 HOH   57  357 169  HOH   HOH A . 
E 4 HOH   58  358 92   HOH   HOH A . 
E 4 HOH   59  359 939  HOH   HOH A . 
E 4 HOH   60  360 148  HOH   HOH A . 
E 4 HOH   61  361 320  HOH   HOH A . 
E 4 HOH   62  362 2    HOH   HOH A . 
E 4 HOH   63  363 396  HOH   HOH A . 
E 4 HOH   64  364 66   HOH   HOH A . 
E 4 HOH   65  365 26   HOH   HOH A . 
E 4 HOH   66  366 19   HOH   HOH A . 
E 4 HOH   67  367 139  HOH   HOH A . 
E 4 HOH   68  368 46   HOH   HOH A . 
E 4 HOH   69  369 56   HOH   HOH A . 
E 4 HOH   70  370 5    HOH   HOH A . 
E 4 HOH   71  371 27   HOH   HOH A . 
E 4 HOH   72  372 45   HOH   HOH A . 
E 4 HOH   73  373 1309 HOH   HOH A . 
E 4 HOH   74  374 81   HOH   HOH A . 
E 4 HOH   75  375 138  HOH   HOH A . 
E 4 HOH   76  376 186  HOH   HOH A . 
E 4 HOH   77  377 351  HOH   HOH A . 
E 4 HOH   78  378 3    HOH   HOH A . 
E 4 HOH   79  379 6    HOH   HOH A . 
E 4 HOH   80  380 39   HOH   HOH A . 
E 4 HOH   81  381 162  HOH   HOH A . 
E 4 HOH   82  382 4    HOH   HOH A . 
E 4 HOH   83  383 154  HOH   HOH A . 
E 4 HOH   84  384 366  HOH   HOH A . 
E 4 HOH   85  385 21   HOH   HOH A . 
E 4 HOH   86  386 1313 HOH   HOH A . 
E 4 HOH   87  387 78   HOH   HOH A . 
E 4 HOH   88  388 12   HOH   HOH A . 
E 4 HOH   89  389 159  HOH   HOH A . 
E 4 HOH   90  390 134  HOH   HOH A . 
E 4 HOH   91  391 67   HOH   HOH A . 
E 4 HOH   92  392 116  HOH   HOH A . 
E 4 HOH   93  393 278  HOH   HOH A . 
E 4 HOH   94  394 195  HOH   HOH A . 
E 4 HOH   95  395 24   HOH   HOH A . 
E 4 HOH   96  396 4    HOH   HOH A . 
E 4 HOH   97  397 74   HOH   HOH A . 
E 4 HOH   98  398 1310 HOH   HOH A . 
E 4 HOH   99  399 83   HOH   HOH A . 
E 4 HOH   100 400 58   HOH   HOH A . 
E 4 HOH   101 401 303  HOH   HOH A . 
E 4 HOH   102 402 296  HOH   HOH A . 
E 4 HOH   103 403 1275 HOH   HOH A . 
E 4 HOH   104 404 70   HOH   HOH A . 
E 4 HOH   105 405 115  HOH   HOH A . 
E 4 HOH   106 406 7    HOH   HOH A . 
E 4 HOH   107 407 281  HOH   HOH A . 
E 4 HOH   108 408 68   HOH   HOH A . 
E 4 HOH   109 409 1308 HOH   HOH A . 
E 4 HOH   110 410 405  HOH   HOH A . 
E 4 HOH   111 411 381  HOH   HOH A . 
E 4 HOH   112 412 25   HOH   HOH A . 
E 4 HOH   113 413 123  HOH   HOH A . 
E 4 HOH   114 414 333  HOH   HOH A . 
E 4 HOH   115 415 125  HOH   HOH A . 
E 4 HOH   116 416 121  HOH   HOH A . 
E 4 HOH   117 417 1068 HOH   HOH A . 
E 4 HOH   118 418 397  HOH   HOH A . 
E 4 HOH   119 419 95   HOH   HOH A . 
E 4 HOH   120 420 1315 HOH   HOH A . 
E 4 HOH   121 421 8    HOH   HOH A . 
E 4 HOH   122 422 122  HOH   HOH A . 
E 4 HOH   123 423 53   HOH   HOH A . 
E 4 HOH   124 424 51   HOH   HOH A . 
E 4 HOH   125 425 96   HOH   HOH A . 
E 4 HOH   126 426 1222 HOH   HOH A . 
E 4 HOH   127 427 1279 HOH   HOH A . 
E 4 HOH   128 428 212  HOH   HOH A . 
E 4 HOH   129 429 156  HOH   HOH A . 
E 4 HOH   130 430 582  HOH   HOH A . 
E 4 HOH   131 431 16   HOH   HOH A . 
E 4 HOH   132 432 188  HOH   HOH A . 
E 4 HOH   133 433 80   HOH   HOH A . 
E 4 HOH   134 434 1286 HOH   HOH A . 
E 4 HOH   135 435 71   HOH   HOH A . 
E 4 HOH   136 436 1094 HOH   HOH A . 
E 4 HOH   137 437 94   HOH   HOH A . 
E 4 HOH   138 438 73   HOH   HOH A . 
E 4 HOH   139 439 3    HOH   HOH A . 
E 4 HOH   140 440 576  HOH   HOH A . 
E 4 HOH   141 441 40   HOH   HOH A . 
E 4 HOH   142 442 104  HOH   HOH A . 
E 4 HOH   143 443 97   HOH   HOH A . 
E 4 HOH   144 444 1238 HOH   HOH A . 
E 4 HOH   145 445 944  HOH   HOH A . 
E 4 HOH   146 446 1189 HOH   HOH A . 
E 4 HOH   147 447 2    HOH   HOH A . 
E 4 HOH   148 448 952  HOH   HOH A . 
E 4 HOH   149 449 79   HOH   HOH A . 
E 4 HOH   150 450 1134 HOH   HOH A . 
E 4 HOH   151 451 509  HOH   HOH A . 
E 4 HOH   152 452 107  HOH   HOH A . 
E 4 HOH   153 453 330  HOH   HOH A . 
E 4 HOH   154 454 1119 HOH   HOH A . 
E 4 HOH   155 455 726  HOH   HOH A . 
E 4 HOH   156 456 163  HOH   HOH A . 
E 4 HOH   157 457 408  HOH   HOH A . 
E 4 HOH   158 458 280  HOH   HOH A . 
E 4 HOH   159 459 756  HOH   HOH A . 
E 4 HOH   160 460 126  HOH   HOH A . 
E 4 HOH   161 461 319  HOH   HOH A . 
E 4 HOH   162 462 361  HOH   HOH A . 
E 4 HOH   163 463 556  HOH   HOH A . 
E 4 HOH   164 464 342  HOH   HOH A . 
E 4 HOH   165 465 250  HOH   HOH A . 
E 4 HOH   166 466 63   HOH   HOH A . 
E 4 HOH   167 467 801  HOH   HOH A . 
E 4 HOH   168 468 1307 HOH   HOH A . 
E 4 HOH   169 469 1276 HOH   HOH A . 
E 4 HOH   170 470 370  HOH   HOH A . 
E 4 HOH   171 471 135  HOH   HOH A . 
E 4 HOH   172 472 1287 HOH   HOH A . 
E 4 HOH   173 473 202  HOH   HOH A . 
E 4 HOH   174 474 1306 HOH   HOH A . 
E 4 HOH   175 475 224  HOH   HOH A . 
E 4 HOH   176 476 674  HOH   HOH A . 
E 4 HOH   177 477 208  HOH   HOH A . 
E 4 HOH   178 478 941  HOH   HOH A . 
E 4 HOH   179 479 919  HOH   HOH A . 
E 4 HOH   180 480 318  HOH   HOH A . 
E 4 HOH   181 481 152  HOH   HOH A . 
E 4 HOH   182 482 1284 HOH   HOH A . 
E 4 HOH   183 483 695  HOH   HOH A . 
E 4 HOH   184 484 1299 HOH   HOH A . 
E 4 HOH   185 485 267  HOH   HOH A . 
E 4 HOH   186 486 331  HOH   HOH A . 
E 4 HOH   187 487 315  HOH   HOH A . 
E 4 HOH   188 488 1314 HOH   HOH A . 
E 4 HOH   189 489 805  HOH   HOH A . 
E 4 HOH   190 490 309  HOH   HOH A . 
E 4 HOH   191 491 521  HOH   HOH A . 
E 4 HOH   192 492 981  HOH   HOH A . 
E 4 HOH   193 493 711  HOH   HOH A . 
E 4 HOH   194 494 263  HOH   HOH A . 
E 4 HOH   195 495 326  HOH   HOH A . 
E 4 HOH   196 496 180  HOH   HOH A . 
E 4 HOH   197 497 363  HOH   HOH A . 
E 4 HOH   198 498 1071 HOH   HOH A . 
E 4 HOH   199 499 356  HOH   HOH A . 
E 4 HOH   200 500 5    HOH   HOH A . 
E 4 HOH   201 501 371  HOH   HOH A . 
E 4 HOH   202 502 313  HOH   HOH A . 
E 4 HOH   203 503 429  HOH   HOH A . 
E 4 HOH   204 504 185  HOH   HOH A . 
E 4 HOH   205 505 376  HOH   HOH A . 
E 4 HOH   206 506 772  HOH   HOH A . 
E 4 HOH   207 507 1074 HOH   HOH A . 
E 4 HOH   208 508 1292 HOH   HOH A . 
E 4 HOH   209 509 346  HOH   HOH A . 
E 4 HOH   210 510 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 240  HOH   HOH B . 
F 4 HOH   3   203 205  HOH   HOH B . 
F 4 HOH   4   204 398  HOH   HOH B . 
F 4 HOH   5   205 1249 HOH   HOH B . 
F 4 HOH   6   206 416  HOH   HOH B . 
F 4 HOH   7   207 358  HOH   HOH B . 
F 4 HOH   8   208 549  HOH   HOH B . 
F 4 HOH   9   209 364  HOH   HOH B . 
F 4 HOH   10  210 531  HOH   HOH B . 
F 4 HOH   11  211 50   HOH   HOH B . 
F 4 HOH   12  212 120  HOH   HOH B . 
F 4 HOH   13  213 232  HOH   HOH B . 
F 4 HOH   14  214 1312 HOH   HOH B . 
F 4 HOH   15  215 758  HOH   HOH B . 
F 4 HOH   16  216 264  HOH   HOH B . 
F 4 HOH   17  217 743  HOH   HOH B . 
F 4 HOH   18  218 900  HOH   HOH B . 
F 4 HOH   19  219 353  HOH   HOH B . 
F 4 HOH   20  220 75   HOH   HOH B . 
F 4 HOH   21  221 452  HOH   HOH B . 
F 4 HOH   22  222 1278 HOH   HOH B . 
F 4 HOH   23  223 1140 HOH   HOH B . 
F 4 HOH   24  224 77   HOH   HOH B . 
F 4 HOH   25  225 391  HOH   HOH B . 
F 4 HOH   26  226 54   HOH   HOH B . 
F 4 HOH   27  227 300  HOH   HOH B . 
F 4 HOH   28  228 82   HOH   HOH B . 
F 4 HOH   29  229 332  HOH   HOH B . 
F 4 HOH   30  230 252  HOH   HOH B . 
F 4 HOH   31  231 131  HOH   HOH B . 
F 4 HOH   32  232 69   HOH   HOH B . 
F 4 HOH   33  233 110  HOH   HOH B . 
F 4 HOH   34  234 444  HOH   HOH B . 
F 4 HOH   35  235 60   HOH   HOH B . 
F 4 HOH   36  236 128  HOH   HOH B . 
F 4 HOH   37  237 127  HOH   HOH B . 
F 4 HOH   38  238 172  HOH   HOH B . 
F 4 HOH   39  239 272  HOH   HOH B . 
F 4 HOH   40  240 343  HOH   HOH B . 
F 4 HOH   41  241 299  HOH   HOH B . 
F 4 HOH   42  242 133  HOH   HOH B . 
F 4 HOH   43  243 52   HOH   HOH B . 
F 4 HOH   44  244 129  HOH   HOH B . 
F 4 HOH   45  245 150  HOH   HOH B . 
F 4 HOH   46  246 654  HOH   HOH B . 
F 4 HOH   47  247 1    HOH   HOH B . 
F 4 HOH   48  248 325  HOH   HOH B . 
F 4 HOH   49  249 9    HOH   HOH B . 
F 4 HOH   50  250 41   HOH   HOH B . 
F 4 HOH   51  251 30   HOH   HOH B . 
F 4 HOH   52  252 143  HOH   HOH B . 
F 4 HOH   53  253 166  HOH   HOH B . 
F 4 HOH   54  254 47   HOH   HOH B . 
F 4 HOH   55  255 14   HOH   HOH B . 
F 4 HOH   56  256 181  HOH   HOH B . 
F 4 HOH   57  257 72   HOH   HOH B . 
F 4 HOH   58  258 271  HOH   HOH B . 
F 4 HOH   59  259 144  HOH   HOH B . 
F 4 HOH   60  260 723  HOH   HOH B . 
F 4 HOH   61  261 31   HOH   HOH B . 
F 4 HOH   62  262 231  HOH   HOH B . 
F 4 HOH   63  263 103  HOH   HOH B . 
F 4 HOH   64  264 147  HOH   HOH B . 
F 4 HOH   65  265 89   HOH   HOH B . 
F 4 HOH   66  266 62   HOH   HOH B . 
F 4 HOH   67  267 10   HOH   HOH B . 
F 4 HOH   68  268 287  HOH   HOH B . 
F 4 HOH   69  269 243  HOH   HOH B . 
F 4 HOH   70  270 61   HOH   HOH B . 
F 4 HOH   71  271 347  HOH   HOH B . 
F 4 HOH   72  272 242  HOH   HOH B . 
F 4 HOH   73  273 302  HOH   HOH B . 
F 4 HOH   74  274 11   HOH   HOH B . 
F 4 HOH   75  275 207  HOH   HOH B . 
F 4 HOH   76  276 59   HOH   HOH B . 
F 4 HOH   77  277 84   HOH   HOH B . 
F 4 HOH   78  278 1305 HOH   HOH B . 
F 4 HOH   79  279 20   HOH   HOH B . 
F 4 HOH   80  280 960  HOH   HOH B . 
F 4 HOH   81  281 117  HOH   HOH B . 
F 4 HOH   82  282 276  HOH   HOH B . 
F 4 HOH   83  283 221  HOH   HOH B . 
F 4 HOH   84  284 22   HOH   HOH B . 
F 4 HOH   85  285 1277 HOH   HOH B . 
F 4 HOH   86  286 99   HOH   HOH B . 
F 4 HOH   87  287 175  HOH   HOH B . 
F 4 HOH   88  288 114  HOH   HOH B . 
F 4 HOH   89  289 137  HOH   HOH B . 
F 4 HOH   90  290 43   HOH   HOH B . 
F 4 HOH   91  291 235  HOH   HOH B . 
F 4 HOH   92  292 1285 HOH   HOH B . 
F 4 HOH   93  293 1066 HOH   HOH B . 
F 4 HOH   94  294 88   HOH   HOH B . 
F 4 HOH   95  295 297  HOH   HOH B . 
F 4 HOH   96  296 13   HOH   HOH B . 
F 4 HOH   97  297 106  HOH   HOH B . 
F 4 HOH   98  298 1106 HOH   HOH B . 
F 4 HOH   99  299 282  HOH   HOH B . 
F 4 HOH   100 300 160  HOH   HOH B . 
F 4 HOH   101 301 216  HOH   HOH B . 
F 4 HOH   102 302 1274 HOH   HOH B . 
F 4 HOH   103 303 1291 HOH   HOH B . 
F 4 HOH   104 304 118  HOH   HOH B . 
F 4 HOH   105 305 112  HOH   HOH B . 
F 4 HOH   106 306 32   HOH   HOH B . 
F 4 HOH   107 307 197  HOH   HOH B . 
F 4 HOH   108 308 316  HOH   HOH B . 
F 4 HOH   109 309 220  HOH   HOH B . 
F 4 HOH   110 310 182  HOH   HOH B . 
F 4 HOH   111 311 101  HOH   HOH B . 
F 4 HOH   112 312 215  HOH   HOH B . 
F 4 HOH   113 313 311  HOH   HOH B . 
F 4 HOH   114 314 38   HOH   HOH B . 
F 4 HOH   115 315 44   HOH   HOH B . 
F 4 HOH   116 316 142  HOH   HOH B . 
F 4 HOH   117 317 55   HOH   HOH B . 
F 4 HOH   118 318 177  HOH   HOH B . 
F 4 HOH   119 319 37   HOH   HOH B . 
F 4 HOH   120 320 48   HOH   HOH B . 
F 4 HOH   121 321 91   HOH   HOH B . 
F 4 HOH   122 322 170  HOH   HOH B . 
F 4 HOH   123 323 387  HOH   HOH B . 
F 4 HOH   124 324 23   HOH   HOH B . 
F 4 HOH   125 325 28   HOH   HOH B . 
F 4 HOH   126 326 1294 HOH   HOH B . 
F 4 HOH   127 327 100  HOH   HOH B . 
F 4 HOH   128 328 635  HOH   HOH B . 
F 4 HOH   129 329 445  HOH   HOH B . 
F 4 HOH   130 330 717  HOH   HOH B . 
F 4 HOH   131 331 161  HOH   HOH B . 
F 4 HOH   132 332 29   HOH   HOH B . 
F 4 HOH   133 333 98   HOH   HOH B . 
F 4 HOH   134 334 87   HOH   HOH B . 
F 4 HOH   135 335 704  HOH   HOH B . 
F 4 HOH   136 336 141  HOH   HOH B . 
F 4 HOH   137 337 65   HOH   HOH B . 
F 4 HOH   138 338 334  HOH   HOH B . 
F 4 HOH   139 339 234  HOH   HOH B . 
F 4 HOH   140 340 341  HOH   HOH B . 
F 4 HOH   141 341 1293 HOH   HOH B . 
F 4 HOH   142 342 178  HOH   HOH B . 
F 4 HOH   143 343 1126 HOH   HOH B . 
F 4 HOH   144 344 362  HOH   HOH B . 
F 4 HOH   145 345 619  HOH   HOH B . 
F 4 HOH   146 346 90   HOH   HOH B . 
F 4 HOH   147 347 1280 HOH   HOH B . 
F 4 HOH   148 348 463  HOH   HOH B . 
F 4 HOH   149 349 623  HOH   HOH B . 
F 4 HOH   150 350 1304 HOH   HOH B . 
F 4 HOH   151 351 191  HOH   HOH B . 
F 4 HOH   152 352 339  HOH   HOH B . 
F 4 HOH   153 353 1046 HOH   HOH B . 
F 4 HOH   154 354 1077 HOH   HOH B . 
F 4 HOH   155 355 335  HOH   HOH B . 
F 4 HOH   156 356 304  HOH   HOH B . 
F 4 HOH   157 357 203  HOH   HOH B . 
F 4 HOH   158 358 290  HOH   HOH B . 
F 4 HOH   159 359 541  HOH   HOH B . 
F 4 HOH   160 360 389  HOH   HOH B . 
F 4 HOH   161 361 291  HOH   HOH B . 
F 4 HOH   162 362 718  HOH   HOH B . 
F 4 HOH   163 363 283  HOH   HOH B . 
F 4 HOH   164 364 1072 HOH   HOH B . 
F 4 HOH   165 365 615  HOH   HOH B . 
F 4 HOH   166 366 479  HOH   HOH B . 
F 4 HOH   167 367 1316 HOH   HOH B . 
F 4 HOH   168 368 340  HOH   HOH B . 
F 4 HOH   169 369 898  HOH   HOH B . 
F 4 HOH   170 370 373  HOH   HOH B . 
F 4 HOH   171 371 667  HOH   HOH B . 
F 4 HOH   172 372 310  HOH   HOH B . 
F 4 HOH   173 373 190  HOH   HOH B . 
F 4 HOH   174 374 431  HOH   HOH B . 
F 4 HOH   175 375 1303 HOH   HOH B . 
F 4 HOH   176 376 418  HOH   HOH B . 
F 4 HOH   177 377 1000 HOH   HOH B . 
F 4 HOH   178 378 149  HOH   HOH B . 
F 4 HOH   179 379 183  HOH   HOH B . 
F 4 HOH   180 380 1173 HOH   HOH B . 
F 4 HOH   181 381 1311 HOH   HOH B . 
F 4 HOH   182 382 1163 HOH   HOH B . 
F 4 HOH   183 383 176  HOH   HOH B . 
F 4 HOH   184 384 491  HOH   HOH B . 
F 4 HOH   185 385 424  HOH   HOH B . 
F 4 HOH   186 386 1298 HOH   HOH B . 
F 4 HOH   187 387 470  HOH   HOH B . 
F 4 HOH   188 388 248  HOH   HOH B . 
F 4 HOH   189 389 265  HOH   HOH B . 
F 4 HOH   190 390 350  HOH   HOH B . 
F 4 HOH   191 391 184  HOH   HOH B . 
F 4 HOH   192 392 360  HOH   HOH B . 
F 4 HOH   193 393 355  HOH   HOH B . 
F 4 HOH   194 394 410  HOH   HOH B . 
F 4 HOH   195 395 157  HOH   HOH B . 
F 4 HOH   196 396 314  HOH   HOH B . 
F 4 HOH   197 397 274  HOH   HOH B . 
F 4 HOH   198 398 566  HOH   HOH B . 
F 4 HOH   199 399 792  HOH   HOH B . 
F 4 HOH   200 400 321  HOH   HOH B . 
F 4 HOH   201 401 558  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           7HFJ 
_cell.length_a           88.685 
_cell.length_b           88.685 
_cell.length_c           39.335 
_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                         7HFJ 
_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          7HFJ 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.13 
_exptl_crystal.density_percent_sol   42.27 
_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   2023-10-07 
_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                     7HFJ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.340 
_reflns.d_resolution_high            0.990 
_reflns.number_obs                   169539 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.700 
_reflns.pdbx_Rmerge_I_obs            0.070 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        9.400 
_reflns.B_iso_Wilson_estimate        12.550 
_reflns.pdbx_redundancy              6.300 
_reflns.pdbx_Rrim_I_all              0.077 
_reflns.pdbx_Rpim_I_all              0.030 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1061461 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 0.990 1.010  ? 31750 7900 ? 1.833 ? ? ? 4.000 ? 0.400  ? ? ? ? ? ? 94.700 2.106 1.010 0.377 
1 2 5.420 44.340 ? 7679  1127 ? 0.045 ? ? ? 6.800 ? 30.800 ? ? ? ? ? ? 99.800 0.049 0.018 0.998 
# 
_refine.entry_id                                 7HFJ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9900 
_refine.ls_d_res_low                             44.3400 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.4300 
_refine.ls_number_reflns_obs                     169021 
_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                          0.1464 
_refine.ls_R_factor_R_work                       0.1457 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1600 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  8139 
_refine.ls_number_reflns_R_work                  160882 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.3229 
_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                            0.1300 
_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                                87.010 
_refine.B_iso_min                                9.770 
_refine.pdbx_overall_phase_error                 18.6000 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       0.9900 
_refine_hist.d_res_low                        44.3400 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.number_atoms_solvent             411 
_refine_hist.number_atoms_total               2989 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           19.05 
_refine_hist.pdbx_B_iso_mean_solvent          32.61 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
0.9900 1.0000  30 86.0000  4638 . 0.4743 0.4495 . 218 0.0000 4856 . 'X-RAY DIFFRACTION' 
1.0000 1.0100  30 98.0000  5232 . 0.4160 0.4045 . 273 0.0000 5505 . 'X-RAY DIFFRACTION' 
1.0100 1.0300  30 100.0000 5406 . 0.3626 0.3600 . 230 0.0000 5636 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5364 . 0.3160 0.3062 . 299 0.0000 5663 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5312 . 0.2767 0.2868 . 284 0.0000 5596 . 'X-RAY DIFFRACTION' 
1.0500 1.0700  30 100.0000 5379 . 0.2494 0.2575 . 314 0.0000 5693 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 5325 . 0.2368 0.2588 . 270 0.0000 5595 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 5393 . 0.2178 0.2542 . 247 0.0000 5640 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5386 . 0.1962 0.2136 . 281 0.0000 5667 . 'X-RAY DIFFRACTION' 
1.1200 1.1300  30 100.0000 5352 . 0.1790 0.1929 . 240 0.0000 5592 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 5432 . 0.1673 0.1793 . 269 0.0000 5701 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 5307 . 0.1502 0.1896 . 272 0.0000 5579 . 'X-RAY DIFFRACTION' 
1.1700 1.2000  30 100.0000 5432 . 0.1410 0.1700 . 268 0.0000 5700 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 100.0000 5304 . 0.1281 0.1612 . 295 0.0000 5599 . 'X-RAY DIFFRACTION' 
1.2200 1.2500  30 100.0000 5410 . 0.1254 0.1504 . 261 0.0000 5671 . 'X-RAY DIFFRACTION' 
1.2500 1.2800  30 100.0000 5386 . 0.1271 0.1516 . 258 0.0000 5644 . 'X-RAY DIFFRACTION' 
1.2800 1.3100  30 100.0000 5358 . 0.1229 0.1408 . 285 0.0000 5643 . 'X-RAY DIFFRACTION' 
1.3100 1.3400  30 100.0000 5382 . 0.1254 0.1502 . 270 0.0000 5652 . 'X-RAY DIFFRACTION' 
1.3400 1.3800  30 100.0000 5376 . 0.1249 0.1481 . 283 0.0000 5659 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 5412 . 0.1269 0.1616 . 251 0.0000 5663 . 'X-RAY DIFFRACTION' 
1.4300 1.4800  30 100.0000 5385 . 0.1207 0.1254 . 272 0.0000 5657 . 'X-RAY DIFFRACTION' 
1.4800 1.5400  30 100.0000 5390 . 0.1140 0.1202 . 287 0.0000 5677 . 'X-RAY DIFFRACTION' 
1.5400 1.6100  30 100.0000 5375 . 0.1144 0.1280 . 271 0.0000 5646 . 'X-RAY DIFFRACTION' 
1.6100 1.6900  30 100.0000 5425 . 0.1208 0.1476 . 265 0.0000 5690 . 'X-RAY DIFFRACTION' 
1.6900 1.8000  30 100.0000 5428 . 0.1292 0.1386 . 265 0.0000 5693 . 'X-RAY DIFFRACTION' 
1.8000 1.9400  30 100.0000 5405 . 0.1275 0.1306 . 291 0.0000 5696 . 'X-RAY DIFFRACTION' 
1.9400 2.1300  30 100.0000 5394 . 0.1328 0.1327 . 275 0.0000 5669 . 'X-RAY DIFFRACTION' 
2.1300 2.4400  30 100.0000 5411 . 0.1330 0.1439 . 298 0.0000 5709 . 'X-RAY DIFFRACTION' 
2.4400 3.0700  30 100.0000 5477 . 0.1465 0.1662 . 278 0.0000 5755 . 'X-RAY DIFFRACTION' 
3.0800 44.3400 30 100.0000 5606 . 0.1508 0.1699 . 269 0.0000 5875 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HFJ 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0004313' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HFJ 
_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 4 ? 
# 
_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 7HFJ A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HFJ 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 7HFJ SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HFJ MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HFJ SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HFJ 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 
2 1 B,F     
# 
_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 TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HFJ 
_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    210 
_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    307 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.91   -132.12 
2 1 SER A 128 ? B 70.95   -4.91   
3 1 ASP A 157 ? B -168.32 114.02  
4 1 HIS B 86  ? ? 57.31   -127.76 
# 
_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 508 ? 5.87 . 
2 1 O ? A HOH 509 ? 5.99 . 
3 1 O ? A HOH 510 ? 7.63 . 
4 1 O ? B HOH 401 ? 6.54 . 
# 
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 
A1BBK N2   N  Y N 1   
A1BBK C3   C  Y N 2   
A1BBK C6   C  Y N 3   
A1BBK C9   C  N N 4   
A1BBK C12  C  N N 5   
A1BBK C1   C  N S 6   
A1BBK C10  C  N N 7   
A1BBK C11  C  N N 8   
A1BBK C13  C  N N 9   
A1BBK C2   C  N N 10  
A1BBK C4   C  Y N 11  
A1BBK C5   C  Y N 12  
A1BBK C7   C  Y N 13  
A1BBK C8   C  Y N 14  
A1BBK N1   N  N N 15  
A1BBK N3   N  Y N 16  
A1BBK N4   N  Y N 17  
A1BBK O1   O  N N 18  
A1BBK O2   O  N N 19  
A1BBK H7   H  N N 20  
A1BBK H6   H  N N 21  
A1BBK H10  H  N N 22  
A1BBK H9   H  N N 23  
A1BBK H14  H  N N 24  
A1BBK H11  H  N N 25  
A1BBK H13  H  N N 26  
A1BBK H12  H  N N 27  
A1BBK H15  H  N N 28  
A1BBK H16  H  N N 29  
A1BBK H2   H  N N 30  
A1BBK H3   H  N N 31  
A1BBK H5   H  N N 32  
A1BBK H8   H  N N 33  
A1BBK H4   H  N N 34  
A1BBK H1   H  N N 35  
ALA   N    N  N N 36  
ALA   CA   C  N S 37  
ALA   C    C  N N 38  
ALA   O    O  N N 39  
ALA   CB   C  N N 40  
ALA   OXT  O  N N 41  
ALA   H    H  N N 42  
ALA   H2   H  N N 43  
ALA   HA   H  N N 44  
ALA   HB1  H  N N 45  
ALA   HB2  H  N N 46  
ALA   HB3  H  N N 47  
ALA   HXT  H  N N 48  
ARG   N    N  N N 49  
ARG   CA   C  N S 50  
ARG   C    C  N N 51  
ARG   O    O  N N 52  
ARG   CB   C  N N 53  
ARG   CG   C  N N 54  
ARG   CD   C  N N 55  
ARG   NE   N  N N 56  
ARG   CZ   C  N N 57  
ARG   NH1  N  N N 58  
ARG   NH2  N  N N 59  
ARG   OXT  O  N N 60  
ARG   H    H  N N 61  
ARG   H2   H  N N 62  
ARG   HA   H  N N 63  
ARG   HB2  H  N N 64  
ARG   HB3  H  N N 65  
ARG   HG2  H  N N 66  
ARG   HG3  H  N N 67  
ARG   HD2  H  N N 68  
ARG   HD3  H  N N 69  
ARG   HE   H  N N 70  
ARG   HH11 H  N N 71  
ARG   HH12 H  N N 72  
ARG   HH21 H  N N 73  
ARG   HH22 H  N N 74  
ARG   HXT  H  N N 75  
ASN   N    N  N N 76  
ASN   CA   C  N S 77  
ASN   C    C  N N 78  
ASN   O    O  N N 79  
ASN   CB   C  N N 80  
ASN   CG   C  N N 81  
ASN   OD1  O  N N 82  
ASN   ND2  N  N N 83  
ASN   OXT  O  N N 84  
ASN   H    H  N N 85  
ASN   H2   H  N N 86  
ASN   HA   H  N N 87  
ASN   HB2  H  N N 88  
ASN   HB3  H  N N 89  
ASN   HD21 H  N N 90  
ASN   HD22 H  N N 91  
ASN   HXT  H  N N 92  
ASP   N    N  N N 93  
ASP   CA   C  N S 94  
ASP   C    C  N N 95  
ASP   O    O  N N 96  
ASP   CB   C  N N 97  
ASP   CG   C  N N 98  
ASP   OD1  O  N N 99  
ASP   OD2  O  N N 100 
ASP   OXT  O  N N 101 
ASP   H    H  N N 102 
ASP   H2   H  N N 103 
ASP   HA   H  N N 104 
ASP   HB2  H  N N 105 
ASP   HB3  H  N N 106 
ASP   HD2  H  N N 107 
ASP   HXT  H  N N 108 
CL    CL   CL N N 109 
CYS   N    N  N N 110 
CYS   CA   C  N R 111 
CYS   C    C  N N 112 
CYS   O    O  N N 113 
CYS   CB   C  N N 114 
CYS   SG   S  N N 115 
CYS   OXT  O  N N 116 
CYS   H    H  N N 117 
CYS   H2   H  N N 118 
CYS   HA   H  N N 119 
CYS   HB2  H  N N 120 
CYS   HB3  H  N N 121 
CYS   HG   H  N N 122 
CYS   HXT  H  N N 123 
GLN   N    N  N N 124 
GLN   CA   C  N S 125 
GLN   C    C  N N 126 
GLN   O    O  N N 127 
GLN   CB   C  N N 128 
GLN   CG   C  N N 129 
GLN   CD   C  N N 130 
GLN   OE1  O  N N 131 
GLN   NE2  N  N N 132 
GLN   OXT  O  N N 133 
GLN   H    H  N N 134 
GLN   H2   H  N N 135 
GLN   HA   H  N N 136 
GLN   HB2  H  N N 137 
GLN   HB3  H  N N 138 
GLN   HG2  H  N N 139 
GLN   HG3  H  N N 140 
GLN   HE21 H  N N 141 
GLN   HE22 H  N N 142 
GLN   HXT  H  N N 143 
GLU   N    N  N N 144 
GLU   CA   C  N S 145 
GLU   C    C  N N 146 
GLU   O    O  N N 147 
GLU   CB   C  N N 148 
GLU   CG   C  N N 149 
GLU   CD   C  N N 150 
GLU   OE1  O  N N 151 
GLU   OE2  O  N N 152 
GLU   OXT  O  N N 153 
GLU   H    H  N N 154 
GLU   H2   H  N N 155 
GLU   HA   H  N N 156 
GLU   HB2  H  N N 157 
GLU   HB3  H  N N 158 
GLU   HG2  H  N N 159 
GLU   HG3  H  N N 160 
GLU   HE2  H  N N 161 
GLU   HXT  H  N N 162 
GLY   N    N  N N 163 
GLY   CA   C  N N 164 
GLY   C    C  N N 165 
GLY   O    O  N N 166 
GLY   OXT  O  N N 167 
GLY   H    H  N N 168 
GLY   H2   H  N N 169 
GLY   HA2  H  N N 170 
GLY   HA3  H  N N 171 
GLY   HXT  H  N N 172 
HIS   N    N  N N 173 
HIS   CA   C  N S 174 
HIS   C    C  N N 175 
HIS   O    O  N N 176 
HIS   CB   C  N N 177 
HIS   CG   C  Y N 178 
HIS   ND1  N  Y N 179 
HIS   CD2  C  Y N 180 
HIS   CE1  C  Y N 181 
HIS   NE2  N  Y N 182 
HIS   OXT  O  N N 183 
HIS   H    H  N N 184 
HIS   H2   H  N N 185 
HIS   HA   H  N N 186 
HIS   HB2  H  N N 187 
HIS   HB3  H  N N 188 
HIS   HD1  H  N N 189 
HIS   HD2  H  N N 190 
HIS   HE1  H  N N 191 
HIS   HE2  H  N N 192 
HIS   HXT  H  N N 193 
HOH   O    O  N N 194 
HOH   H1   H  N N 195 
HOH   H2   H  N N 196 
ILE   N    N  N N 197 
ILE   CA   C  N S 198 
ILE   C    C  N N 199 
ILE   O    O  N N 200 
ILE   CB   C  N S 201 
ILE   CG1  C  N N 202 
ILE   CG2  C  N N 203 
ILE   CD1  C  N N 204 
ILE   OXT  O  N N 205 
ILE   H    H  N N 206 
ILE   H2   H  N N 207 
ILE   HA   H  N N 208 
ILE   HB   H  N N 209 
ILE   HG12 H  N N 210 
ILE   HG13 H  N N 211 
ILE   HG21 H  N N 212 
ILE   HG22 H  N N 213 
ILE   HG23 H  N N 214 
ILE   HD11 H  N N 215 
ILE   HD12 H  N N 216 
ILE   HD13 H  N N 217 
ILE   HXT  H  N N 218 
LEU   N    N  N N 219 
LEU   CA   C  N S 220 
LEU   C    C  N N 221 
LEU   O    O  N N 222 
LEU   CB   C  N N 223 
LEU   CG   C  N N 224 
LEU   CD1  C  N N 225 
LEU   CD2  C  N N 226 
LEU   OXT  O  N N 227 
LEU   H    H  N N 228 
LEU   H2   H  N N 229 
LEU   HA   H  N N 230 
LEU   HB2  H  N N 231 
LEU   HB3  H  N N 232 
LEU   HG   H  N N 233 
LEU   HD11 H  N N 234 
LEU   HD12 H  N N 235 
LEU   HD13 H  N N 236 
LEU   HD21 H  N N 237 
LEU   HD22 H  N N 238 
LEU   HD23 H  N N 239 
LEU   HXT  H  N N 240 
LYS   N    N  N N 241 
LYS   CA   C  N S 242 
LYS   C    C  N N 243 
LYS   O    O  N N 244 
LYS   CB   C  N N 245 
LYS   CG   C  N N 246 
LYS   CD   C  N N 247 
LYS   CE   C  N N 248 
LYS   NZ   N  N N 249 
LYS   OXT  O  N N 250 
LYS   H    H  N N 251 
LYS   H2   H  N N 252 
LYS   HA   H  N N 253 
LYS   HB2  H  N N 254 
LYS   HB3  H  N N 255 
LYS   HG2  H  N N 256 
LYS   HG3  H  N N 257 
LYS   HD2  H  N N 258 
LYS   HD3  H  N N 259 
LYS   HE2  H  N N 260 
LYS   HE3  H  N N 261 
LYS   HZ1  H  N N 262 
LYS   HZ2  H  N N 263 
LYS   HZ3  H  N N 264 
LYS   HXT  H  N N 265 
MET   N    N  N N 266 
MET   CA   C  N S 267 
MET   C    C  N N 268 
MET   O    O  N N 269 
MET   CB   C  N N 270 
MET   CG   C  N N 271 
MET   SD   S  N N 272 
MET   CE   C  N N 273 
MET   OXT  O  N N 274 
MET   H    H  N N 275 
MET   H2   H  N N 276 
MET   HA   H  N N 277 
MET   HB2  H  N N 278 
MET   HB3  H  N N 279 
MET   HG2  H  N N 280 
MET   HG3  H  N N 281 
MET   HE1  H  N N 282 
MET   HE2  H  N N 283 
MET   HE3  H  N N 284 
MET   HXT  H  N N 285 
PHE   N    N  N N 286 
PHE   CA   C  N S 287 
PHE   C    C  N N 288 
PHE   O    O  N N 289 
PHE   CB   C  N N 290 
PHE   CG   C  Y N 291 
PHE   CD1  C  Y N 292 
PHE   CD2  C  Y N 293 
PHE   CE1  C  Y N 294 
PHE   CE2  C  Y N 295 
PHE   CZ   C  Y N 296 
PHE   OXT  O  N N 297 
PHE   H    H  N N 298 
PHE   H2   H  N N 299 
PHE   HA   H  N N 300 
PHE   HB2  H  N N 301 
PHE   HB3  H  N N 302 
PHE   HD1  H  N N 303 
PHE   HD2  H  N N 304 
PHE   HE1  H  N N 305 
PHE   HE2  H  N N 306 
PHE   HZ   H  N N 307 
PHE   HXT  H  N N 308 
PRO   N    N  N N 309 
PRO   CA   C  N S 310 
PRO   C    C  N N 311 
PRO   O    O  N N 312 
PRO   CB   C  N N 313 
PRO   CG   C  N N 314 
PRO   CD   C  N N 315 
PRO   OXT  O  N N 316 
PRO   H    H  N N 317 
PRO   HA   H  N N 318 
PRO   HB2  H  N N 319 
PRO   HB3  H  N N 320 
PRO   HG2  H  N N 321 
PRO   HG3  H  N N 322 
PRO   HD2  H  N N 323 
PRO   HD3  H  N N 324 
PRO   HXT  H  N N 325 
SER   N    N  N N 326 
SER   CA   C  N S 327 
SER   C    C  N N 328 
SER   O    O  N N 329 
SER   CB   C  N N 330 
SER   OG   O  N N 331 
SER   OXT  O  N N 332 
SER   H    H  N N 333 
SER   H2   H  N N 334 
SER   HA   H  N N 335 
SER   HB2  H  N N 336 
SER   HB3  H  N N 337 
SER   HG   H  N N 338 
SER   HXT  H  N N 339 
THR   N    N  N N 340 
THR   CA   C  N S 341 
THR   C    C  N N 342 
THR   O    O  N N 343 
THR   CB   C  N R 344 
THR   OG1  O  N N 345 
THR   CG2  C  N N 346 
THR   OXT  O  N N 347 
THR   H    H  N N 348 
THR   H2   H  N N 349 
THR   HA   H  N N 350 
THR   HB   H  N N 351 
THR   HG1  H  N N 352 
THR   HG21 H  N N 353 
THR   HG22 H  N N 354 
THR   HG23 H  N N 355 
THR   HXT  H  N N 356 
TYR   N    N  N N 357 
TYR   CA   C  N S 358 
TYR   C    C  N N 359 
TYR   O    O  N N 360 
TYR   CB   C  N N 361 
TYR   CG   C  Y N 362 
TYR   CD1  C  Y N 363 
TYR   CD2  C  Y N 364 
TYR   CE1  C  Y N 365 
TYR   CE2  C  Y N 366 
TYR   CZ   C  Y N 367 
TYR   OH   O  N N 368 
TYR   OXT  O  N N 369 
TYR   H    H  N N 370 
TYR   H2   H  N N 371 
TYR   HA   H  N N 372 
TYR   HB2  H  N N 373 
TYR   HB3  H  N N 374 
TYR   HD1  H  N N 375 
TYR   HD2  H  N N 376 
TYR   HE1  H  N N 377 
TYR   HE2  H  N N 378 
TYR   HH   H  N N 379 
TYR   HXT  H  N N 380 
VAL   N    N  N N 381 
VAL   CA   C  N S 382 
VAL   C    C  N N 383 
VAL   O    O  N N 384 
VAL   CB   C  N N 385 
VAL   CG1  C  N N 386 
VAL   CG2  C  N N 387 
VAL   OXT  O  N N 388 
VAL   H    H  N N 389 
VAL   H2   H  N N 390 
VAL   HA   H  N N 391 
VAL   HB   H  N N 392 
VAL   HG11 H  N N 393 
VAL   HG12 H  N N 394 
VAL   HG13 H  N N 395 
VAL   HG21 H  N N 396 
VAL   HG22 H  N N 397 
VAL   HG23 H  N N 398 
VAL   HXT  H  N N 399 
# 
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 
A1BBK O2  C10  sing N N 1   
A1BBK O2  C9   sing N N 2   
A1BBK C10 C13  sing N N 3   
A1BBK C10 C11  sing N N 4   
A1BBK C13 C12  sing N N 5   
A1BBK C9  C1   sing N N 6   
A1BBK C11 C12  sing N N 7   
A1BBK C12 C1   sing N N 8   
A1BBK C1  C2   sing N N 9   
A1BBK C1  O1   sing N N 10  
A1BBK C2  N1   sing N N 11  
A1BBK N1  C3   sing N N 12  
A1BBK C3  N4   doub Y N 13  
A1BBK C3  C4   sing Y N 14  
A1BBK C5  C4   sing Y N 15  
A1BBK C5  C6   doub Y N 16  
A1BBK N4  C8   sing Y N 17  
A1BBK C4  C7   doub Y N 18  
A1BBK C6  N2   sing Y N 19  
A1BBK C8  N3   doub Y N 20  
A1BBK C7  N2   sing Y N 21  
A1BBK C7  N3   sing Y N 22  
A1BBK N2  H7   sing N N 23  
A1BBK C6  H6   sing N N 24  
A1BBK C9  H10  sing N N 25  
A1BBK C9  H9   sing N N 26  
A1BBK C12 H14  sing N N 27  
A1BBK C10 H11  sing N N 28  
A1BBK C11 H13  sing N N 29  
A1BBK C11 H12  sing N N 30  
A1BBK C13 H15  sing N N 31  
A1BBK C13 H16  sing N N 32  
A1BBK C2  H2   sing N N 33  
A1BBK C2  H3   sing N N 34  
A1BBK C5  H5   sing N N 35  
A1BBK C8  H8   sing N N 36  
A1BBK N1  H4   sing N N 37  
A1BBK O1  H1   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 
THR   N   CA   sing N N 328 
THR   N   H    sing N N 329 
THR   N   H2   sing N N 330 
THR   CA  C    sing N N 331 
THR   CA  CB   sing N N 332 
THR   CA  HA   sing N N 333 
THR   C   O    doub N N 334 
THR   C   OXT  sing N N 335 
THR   CB  OG1  sing N N 336 
THR   CB  CG2  sing N N 337 
THR   CB  HB   sing N N 338 
THR   OG1 HG1  sing N N 339 
THR   CG2 HG21 sing N N 340 
THR   CG2 HG22 sing N N 341 
THR   CG2 HG23 sing N N 342 
THR   OXT HXT  sing N N 343 
TYR   N   CA   sing N N 344 
TYR   N   H    sing N N 345 
TYR   N   H2   sing N N 346 
TYR   CA  C    sing N N 347 
TYR   CA  CB   sing N N 348 
TYR   CA  HA   sing N N 349 
TYR   C   O    doub N N 350 
TYR   C   OXT  sing N N 351 
TYR   CB  CG   sing N N 352 
TYR   CB  HB2  sing N N 353 
TYR   CB  HB3  sing N N 354 
TYR   CG  CD1  doub Y N 355 
TYR   CG  CD2  sing Y N 356 
TYR   CD1 CE1  sing Y N 357 
TYR   CD1 HD1  sing N N 358 
TYR   CD2 CE2  doub Y N 359 
TYR   CD2 HD2  sing N N 360 
TYR   CE1 CZ   doub Y N 361 
TYR   CE1 HE1  sing N N 362 
TYR   CE2 CZ   sing Y N 363 
TYR   CE2 HE2  sing N N 364 
TYR   CZ  OH   sing N N 365 
TYR   OH  HH   sing N N 366 
TYR   OXT HXT  sing N N 367 
VAL   N   CA   sing N N 368 
VAL   N   H    sing N N 369 
VAL   N   H2   sing N N 370 
VAL   CA  C    sing N N 371 
VAL   CA  CB   sing N N 372 
VAL   CA  HA   sing N N 373 
VAL   C   O    doub N N 374 
VAL   C   OXT  sing N N 375 
VAL   CB  CG1  sing N N 376 
VAL   CB  CG2  sing N N 377 
VAL   CB  HB   sing N N 378 
VAL   CG1 HG11 sing N N 379 
VAL   CG1 HG12 sing N N 380 
VAL   CG1 HG13 sing N N 381 
VAL   CG2 HG21 sing N N 382 
VAL   CG2 HG22 sing N N 383 
VAL   CG2 HG23 sing N N 384 
VAL   OXT HXT  sing N N 385 
# 
_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                    7HFJ 
_atom_sites.fract_transf_matrix[1][1]   0.011276 
_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]   0.011276 
_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]   0.025423 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    A VAL   A 1 3   ? 19.597 -16.159 22.185  0.62 65.92 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.540 -15.899 22.331  0.38 64.17 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.624 -15.088 22.357  0.62 65.39 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.562 -14.836 22.521  0.38 63.60 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.272 -13.735 22.076  0.62 63.24 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.205 -13.477 22.265  0.38 61.35 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.371 -13.454 22.556  0.62 63.94 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.235 -13.149 22.855  0.38 61.87 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 17.991 -15.127 23.765  0.62 66.58 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 17.933 -14.899 23.926  0.38 64.84 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 16.968 -14.011 23.921  0.62 66.83 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 16.897 -13.798 24.094  0.38 65.14 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.348 -16.483 24.025  0.62 66.92 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.312 -16.266 24.172  0.38 65.23 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.911 -15.211 21.715  0.62 78.49 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.847 -14.951 21.879  0.38 76.34 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.684 -14.993 24.430  0.62 79.92 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.627 -14.765 24.590  0.38 77.83 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.459 -14.161 24.733  0.62 80.22 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.389 -13.965 24.903  0.38 78.18 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.431 -13.161 23.975  0.62 80.22 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.350 -12.943 24.160  0.38 78.18 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.374 -14.018 23.154  0.62 80.22 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.304 -13.802 23.326  0.38 78.18 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.900 -16.461 24.886  0.62 80.32 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 16.853 -16.254 25.027  0.38 78.30 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.705 -16.668 23.323  0.62 80.32 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.681 -16.458 23.461  0.38 78.30 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.038 -17.165 24.030  0.62 80.32 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.013 -16.936 24.182  0.38 78.30 ?  3   VAL   A HG23 1 
ATOM   31   N  N    A ASN   A 1 4   ? 18.590 -12.904 21.289  0.62 59.92 ?  4   ASN   A N    1 
ATOM   32   N  N    B ASN   A 1 4   ? 18.595 -12.691 21.382  0.38 58.15 ?  4   ASN   A N    1 
ATOM   33   C  CA   A ASN   A 1 4   ? 19.033 -11.546 20.999  0.62 56.10 ?  4   ASN   A CA   1 
ATOM   34   C  CA   B ASN   A 1 4   ? 19.062 -11.349 21.061  0.38 54.58 ?  4   ASN   A CA   1 
ATOM   35   C  C    A ASN   A 1 4   ? 17.881 -10.576 21.253  0.62 52.35 ?  4   ASN   A C    1 
ATOM   36   C  C    B ASN   A 1 4   ? 17.953 -10.335 21.320  0.38 51.16 ?  4   ASN   A C    1 
ATOM   37   O  O    A ASN   A 1 4   ? 16.789 -10.971 21.674  0.62 52.45 ?  4   ASN   A O    1 
ATOM   38   O  O    B ASN   A 1 4   ? 16.817 -10.688 21.648  0.38 51.24 ?  4   ASN   A O    1 
ATOM   39   C  CB   A ASN   A 1 4   ? 19.604 -11.421 19.579  0.62 55.67 ?  4   ASN   A CB   1 
ATOM   40   C  CB   B ASN   A 1 4   ? 19.576 -11.263 19.617  0.38 54.20 ?  4   ASN   A CB   1 
ATOM   41   C  CG   A ASN   A 1 4   ? 18.629 -11.870 18.511  0.62 55.14 ?  4   ASN   A CG   1 
ATOM   42   C  CG   B ASN   A 1 4   ? 18.564 -11.752 18.603  0.38 53.75 ?  4   ASN   A CG   1 
ATOM   43   O  OD1  A ASN   A 1 4   ? 17.459 -11.486 18.517  0.62 55.02 ?  4   ASN   A OD1  1 
ATOM   44   O  OD1  B ASN   A 1 4   ? 17.378 -11.433 18.685  0.38 53.63 ?  4   ASN   A OD1  1 
ATOM   45   N  ND2  A ASN   A 1 4   ? 19.109 -12.692 17.584  0.62 54.92 ?  4   ASN   A ND2  1 
ATOM   46   N  ND2  B ASN   A 1 4   ? 19.033 -12.530 17.634  0.38 53.58 ?  4   ASN   A ND2  1 
ATOM   47   H  H    A ASN   A 1 4   ? 17.850 -13.115 20.906  0.62 71.92 ?  4   ASN   A H    1 
ATOM   48   H  H    B ASN   A 1 4   ? 17.889 -12.923 20.949  0.38 69.80 ?  4   ASN   A H    1 
ATOM   49   H  HA   A ASN   A 1 4   ? 19.745 -11.321 21.612  0.62 67.34 ?  4   ASN   A HA   1 
ATOM   50   H  HA   B ASN   A 1 4   ? 19.804 -11.134 21.637  0.38 65.52 ?  4   ASN   A HA   1 
ATOM   51   H  HB2  A ASN   A 1 4   ? 19.831 -10.492 19.409  0.62 66.82 ?  4   ASN   A HB2  1 
ATOM   52   H  HB2  B ASN   A 1 4   ? 19.790 -10.337 19.412  0.38 65.06 ?  4   ASN   A HB2  1 
ATOM   53   H  HB3  A ASN   A 1 4   ? 20.399 -11.972 19.509  0.62 66.82 ?  4   ASN   A HB3  1 
ATOM   54   H  HB3  B ASN   A 1 4   ? 20.372 -11.810 19.531  0.38 65.06 ?  4   ASN   A HB3  1 
ATOM   55   H  HD21 A ASN   A 1 4   ? 18.598 -12.975 16.953  0.62 65.93 ?  4   ASN   A HD21 1 
ATOM   56   H  HD21 B ASN   A 1 4   ? 18.501 -12.831 17.029  0.38 64.32 ?  4   ASN   A HD21 1 
ATOM   57   H  HD22 A ASN   A 1 4   ? 19.932 -12.942 17.614  0.62 65.93 ?  4   ASN   A HD22 1 
ATOM   58   H  HD22 B ASN   A 1 4   ? 19.869 -12.734 17.611  0.38 64.32 ?  4   ASN   A HD22 1 
ATOM   59   N  N    A SER   A 1 5   ? 18.131 -9.291  20.992  0.62 48.18 ?  5   SER   A N    1 
ATOM   60   N  N    B SER   A 1 5   ? 18.297 -9.056  21.172  0.38 47.41 ?  5   SER   A N    1 
ATOM   61   C  CA   A SER   A 1 5   ? 17.234 -8.216  21.399  0.62 43.76 ?  5   SER   A CA   1 
ATOM   62   C  CA   B SER   A 1 5   ? 17.395 -7.958  21.497  0.38 43.56 ?  5   SER   A CA   1 
ATOM   63   C  C    A SER   A 1 5   ? 16.391 -7.661  20.252  0.62 38.40 ?  5   SER   A C    1 
ATOM   64   C  C    B SER   A 1 5   ? 16.506 -7.549  20.329  0.38 39.07 ?  5   SER   A C    1 
ATOM   65   O  O    A SER   A 1 5   ? 15.829 -6.568  20.385  0.62 38.36 ?  5   SER   A O    1 
ATOM   66   O  O    B SER   A 1 5   ? 15.783 -6.553  20.438  0.38 38.95 ?  5   SER   A O    1 
ATOM   67   C  CB   A SER   A 1 5   ? 18.026 -7.084  22.053  0.62 44.76 ?  5   SER   A CB   1 
ATOM   68   C  CB   B SER   A 1 5   ? 18.182 -6.747  22.006  0.38 44.29 ?  5   SER   A CB   1 
ATOM   69   O  OG   A SER   A 1 5   ? 19.015 -6.580  21.173  0.62 45.25 ?  5   SER   A OG   1 
ATOM   70   O  OG   B SER   A 1 5   ? 19.053 -6.245  21.009  0.38 44.62 ?  5   SER   A OG   1 
ATOM   71   H  H    A SER   A 1 5   ? 18.830 -9.019  20.575  0.62 57.84 ?  5   SER   A H    1 
ATOM   72   H  H    B SER   A 1 5   ? 19.058 -8.797  20.872  0.38 56.91 ?  5   SER   A H    1 
ATOM   73   H  HA   A SER   A 1 5   ? 16.630 -8.569  22.072  0.62 52.53 ?  5   SER   A HA   1 
ATOM   74   H  HA   B SER   A 1 5   ? 16.813 -8.243  22.218  0.38 52.29 ?  5   SER   A HA   1 
ATOM   75   H  HB2  A SER   A 1 5   ? 17.414 -6.365  22.282  0.62 53.74 ?  5   SER   A HB2  1 
ATOM   76   H  HB2  B SER   A 1 5   ? 17.556 -6.050  22.263  0.38 53.16 ?  5   SER   A HB2  1 
ATOM   77   H  HB3  A SER   A 1 5   ? 18.456 -7.420  22.853  0.62 53.74 ?  5   SER   A HB3  1 
ATOM   78   H  HB3  B SER   A 1 5   ? 18.709 -7.015  22.775  0.38 53.16 ?  5   SER   A HB3  1 
ATOM   79   H  HG   A SER   A 1 5   ? 19.441 -5.959  21.545  0.62 54.33 ?  5   SER   A HG   1 
ATOM   80   H  HG   B SER   A 1 5   ? 19.471 -5.578  21.305  0.38 53.57 ?  5   SER   A HG   1 
ATOM   81   N  N    A PHE   A 1 6   ? 16.294 -8.372  19.132  0.62 32.85 ?  6   PHE   A N    1 
ATOM   82   N  N    B PHE   A 1 6   ? 16.546 -8.279  19.218  0.38 34.65 ?  6   PHE   A N    1 
ATOM   83   C  CA   A PHE   A 1 6   ? 15.392 -7.955  18.066  0.62 27.44 ?  6   PHE   A CA   1 
ATOM   84   C  CA   B PHE   A 1 6   ? 15.580 -8.057  18.154  0.38 30.51 ?  6   PHE   A CA   1 
ATOM   85   C  C    A PHE   A 1 6   ? 13.954 -8.302  18.436  0.62 26.35 ?  6   PHE   A C    1 
ATOM   86   C  C    B PHE   A 1 6   ? 14.211 -8.544  18.609  0.38 29.46 ?  6   PHE   A C    1 
ATOM   87   O  O    A PHE   A 1 6   ? 13.678 -9.382  18.963  0.62 27.31 ?  6   PHE   A O    1 
ATOM   88   O  O    B PHE   A 1 6   ? 14.087 -9.609  19.219  0.38 30.00 ?  6   PHE   A O    1 
ATOM   89   C  CB   A PHE   A 1 6   ? 15.768 -8.638  16.753  0.62 24.22 ?  6   PHE   A CB   1 
ATOM   90   C  CB   B PHE   A 1 6   ? 15.992 -8.822  16.897  0.38 27.96 ?  6   PHE   A CB   1 
ATOM   91   C  CG   A PHE   A 1 6   ? 17.044 -8.121  16.146  0.62 21.68 ?  6   PHE   A CG   1 
ATOM   92   C  CG   B PHE   A 1 6   ? 17.304 -8.375  16.310  0.38 25.79 ?  6   PHE   A CG   1 
ATOM   93   C  CD1  A PHE   A 1 6   ? 17.064 -6.918  15.460  0.62 20.97 ?  6   PHE   A CD1  1 
ATOM   94   C  CD1  B PHE   A 1 6   ? 17.373 -7.255  15.499  0.38 24.95 ?  6   PHE   A CD1  1 
ATOM   95   C  CD2  A PHE   A 1 6   ? 18.220 -8.843  16.253  0.62 21.51 ?  6   PHE   A CD2  1 
ATOM   96   C  CD2  B PHE   A 1 6   ? 18.465 -9.086  16.560  0.38 25.30 ?  6   PHE   A CD2  1 
ATOM   97   C  CE1  A PHE   A 1 6   ? 18.239 -6.441  14.897  0.62 20.51 ?  6   PHE   A CE1  1 
ATOM   98   C  CE1  B PHE   A 1 6   ? 18.579 -6.848  14.955  0.38 24.60 ?  6   PHE   A CE1  1 
ATOM   99   C  CE2  A PHE   A 1 6   ? 19.392 -8.377  15.694  0.62 21.49 ?  6   PHE   A CE2  1 
ATOM   100  C  CE2  B PHE   A 1 6   ? 19.672 -8.687  16.020  0.38 24.80 ?  6   PHE   A CE2  1 
ATOM   101  C  CZ   A PHE   A 1 6   ? 19.403 -7.173  15.014  0.62 20.86 ?  6   PHE   A CZ   1 
ATOM   102  C  CZ   B PHE   A 1 6   ? 19.731 -7.565  15.217  0.38 24.60 ?  6   PHE   A CZ   1 
ATOM   103  H  H    A PHE   A 1 6   ? 16.738 -9.093  18.963  0.62 39.44 ?  6   PHE   A H    1 
ATOM   104  H  H    B PHE   A 1 6   ? 17.115 -8.903  19.058  0.38 41.60 ?  6   PHE   A H    1 
ATOM   105  H  HA   A PHE   A 1 6   ? 15.454 -6.998  17.949  0.62 32.94 ?  6   PHE   A HA   1 
ATOM   106  H  HA   B PHE   A 1 6   ? 15.525 -7.112  17.946  0.38 36.63 ?  6   PHE   A HA   1 
ATOM   107  H  HB2  A PHE   A 1 6   ? 15.879 -9.587  16.915  0.62 29.09 ?  6   PHE   A HB2  1 
ATOM   108  H  HB2  B PHE   A 1 6   ? 16.072 -9.763  17.119  0.38 33.57 ?  6   PHE   A HB2  1 
ATOM   109  H  HB3  A PHE   A 1 6   ? 15.054 -8.494  16.112  0.62 29.09 ?  6   PHE   A HB3  1 
ATOM   110  H  HB3  B PHE   A 1 6   ? 15.307 -8.705  16.220  0.38 33.57 ?  6   PHE   A HB3  1 
ATOM   111  H  HD1  A PHE   A 1 6   ? 16.280 -6.419  15.378  0.62 25.18 ?  6   PHE   A HD1  1 
ATOM   112  H  HD1  B PHE   A 1 6   ? 16.603 -6.768  15.320  0.38 29.96 ?  6   PHE   A HD1  1 
ATOM   113  H  HD2  A PHE   A 1 6   ? 18.220 -9.653  16.710  0.62 25.83 ?  6   PHE   A HD2  1 
ATOM   114  H  HD2  B PHE   A 1 6   ? 18.432 -9.841  17.099  0.38 30.38 ?  6   PHE   A HD2  1 
ATOM   115  H  HE1  A PHE   A 1 6   ? 18.242 -5.627  14.439  0.62 24.63 ?  6   PHE   A HE1  1 
ATOM   116  H  HE1  B PHE   A 1 6   ? 18.616 -6.092  14.414  0.38 29.54 ?  6   PHE   A HE1  1 
ATOM   117  H  HE2  A PHE   A 1 6   ? 20.176 -8.869  15.776  0.62 25.81 ?  6   PHE   A HE2  1 
ATOM   118  H  HE2  B PHE   A 1 6   ? 20.447 -9.173  16.198  0.38 29.78 ?  6   PHE   A HE2  1 
ATOM   119  H  HZ   A PHE   A 1 6   ? 20.191 -6.854  14.639  0.62 25.05 ?  6   PHE   A HZ   1 
ATOM   120  H  HZ   B PHE   A 1 6   ? 20.544 -7.295  14.852  0.38 29.54 ?  6   PHE   A HZ   1 
ATOM   121  N  N    A SER   A 1 7   ? 13.032 -7.379  18.153  0.62 24.52 ?  7   SER   A N    1 
ATOM   122  N  N    B SER   A 1 7   ? 13.179 -7.758  18.315  0.38 27.88 ?  7   SER   A N    1 
ATOM   123  C  CA   A SER   A 1 7   ? 11.652 -7.489  18.612  0.62 23.93 ?  7   SER   A CA   1 
ATOM   124  C  CA   B SER   A 1 7   ? 11.828 -8.128  18.712  0.38 26.78 ?  7   SER   A CA   1 
ATOM   125  C  C    A SER   A 1 7   ? 10.672 -7.236  17.471  0.62 22.52 ?  7   SER   A C    1 
ATOM   126  C  C    B SER   A 1 7   ? 10.844 -7.614  17.673  0.38 25.09 ?  7   SER   A C    1 
ATOM   127  O  O    A SER   A 1 7   ? 10.900 -6.373  16.619  0.62 22.45 ?  7   SER   A O    1 
ATOM   128  O  O    B SER   A 1 7   ? 11.109 -6.631  16.975  0.38 24.98 ?  7   SER   A O    1 
ATOM   129  C  CB   A SER   A 1 7   ? 11.397 -6.490  19.753  0.62 25.17 ?  7   SER   A CB   1 
ATOM   130  C  CB   B SER   A 1 7   ? 11.479 -7.581  20.102  0.38 27.56 ?  7   SER   A CB   1 
ATOM   131  O  OG   A SER   A 1 7   ? 10.065 -6.579  20.222  0.62 26.53 ?  7   SER   A OG   1 
ATOM   132  O  OG   B SER   A 1 7   ? 10.383 -8.279  20.667  0.38 28.46 ?  7   SER   A OG   1 
ATOM   133  H  H    A SER   A 1 7   ? 13.190 -6.671  17.691  0.62 29.44 ?  7   SER   A H    1 
ATOM   134  H  H    B SER   A 1 7   ? 13.235 -7.011  17.887  0.38 33.47 ?  7   SER   A H    1 
ATOM   135  H  HA   A SER   A 1 7   ? 11.498 -8.381  18.955  0.62 28.74 ?  7   SER   A HA   1 
ATOM   136  H  HA   B SER   A 1 7   ? 11.759 -9.093  18.740  0.38 32.15 ?  7   SER   A HA   1 
ATOM   137  H  HB2  A SER   A 1 7   ? 12.006 -6.689  20.486  0.62 30.23 ?  7   SER   A HB2  1 
ATOM   138  H  HB2  B SER   A 1 7   ? 12.249 -7.682  20.684  0.38 33.09 ?  7   SER   A HB2  1 
ATOM   139  H  HB3  A SER   A 1 7   ? 11.565 -5.591  19.426  0.62 30.23 ?  7   SER   A HB3  1 
ATOM   140  H  HB3  B SER   A 1 7   ? 11.239 -6.647  20.025  0.38 33.09 ?  7   SER   A HB3  1 
ATOM   141  H  HG   A SER   A 1 7   ? 9.947  -6.023  20.841  0.62 31.86 ?  7   SER   A HG   1 
ATOM   142  H  HG   B SER   A 1 7   ? 9.709  -8.217  20.171  0.38 34.18 ?  7   SER   A HG   1 
ATOM   143  N  N    A GLY   A 1 8   ? 9.581  -8.000  17.455  0.62 21.38 ?  8   GLY   A N    1 
ATOM   144  N  N    B GLY   A 1 8   ? 9.706  -8.297  17.572  0.38 23.53 ?  8   GLY   A N    1 
ATOM   145  C  CA   A GLY   A 1 8   ? 8.505  -7.755  16.515  0.62 20.50 ?  8   GLY   A CA   1 
ATOM   146  C  CA   B GLY   A 1 8   ? 8.681  -7.923  16.622  0.38 22.12 ?  8   GLY   A CA   1 
ATOM   147  C  C    A GLY   A 1 8   ? 8.723  -8.282  15.114  0.62 19.24 ?  8   GLY   A C    1 
ATOM   148  C  C    B GLY   A 1 8   ? 8.877  -8.457  15.223  0.38 20.79 ?  8   GLY   A C    1 
ATOM   149  O  O    A GLY   A 1 8   ? 8.029  -7.850  14.190  0.62 20.22 ?  8   GLY   A O    1 
ATOM   150  O  O    B GLY   A 1 8   ? 8.174  -8.017  14.307  0.38 21.13 ?  8   GLY   A O    1 
ATOM   151  H  H    A GLY   A 1 8   ? 9.450  -8.666  17.979  0.62 25.67 ?  8   GLY   A H    1 
ATOM   152  H  H    B GLY   A 1 8   ? 9.509  -8.985  18.048  0.38 28.25 ?  8   GLY   A H    1 
ATOM   153  H  HA2  A GLY   A 1 8   ? 7.692  -8.150  16.869  0.62 24.61 ?  8   GLY   A HA2  1 
ATOM   154  H  HA2  B GLY   A 1 8   ? 7.824  -8.245  16.941  0.38 26.57 ?  8   GLY   A HA2  1 
ATOM   155  H  HA3  A GLY   A 1 8   ? 8.361  -6.796  16.450  0.62 24.61 ?  8   GLY   A HA3  1 
ATOM   156  H  HA3  B GLY   A 1 8   ? 8.637  -6.955  16.571  0.38 26.57 ?  8   GLY   A HA3  1 
ATOM   157  N  N    A TYR   A 1 9   ? 9.674  -9.194  14.919  0.62 17.90 ?  9   TYR   A N    1 
ATOM   158  N  N    B TYR   A 1 9   ? 9.803  -9.391  15.024  0.38 19.32 ?  9   TYR   A N    1 
ATOM   159  C  CA   A TYR   A 1 9   ? 9.961  -9.737  13.599  0.62 16.59 ?  9   TYR   A CA   1 
ATOM   160  C  CA   B TYR   A 1 9   ? 10.092 -9.915  13.698  0.38 17.77 ?  9   TYR   A CA   1 
ATOM   161  C  C    A TYR   A 1 9   ? 9.129  -10.985 13.332  0.62 16.23 ?  9   TYR   A C    1 
ATOM   162  C  C    B TYR   A 1 9   ? 9.215  -11.117 13.386  0.38 17.42 ?  9   TYR   A C    1 
ATOM   163  O  O    A TYR   A 1 9   ? 8.894  -11.799 14.230  0.62 17.49 ?  9   TYR   A O    1 
ATOM   164  O  O    B TYR   A 1 9   ? 8.903  -11.927 14.264  0.38 17.90 ?  9   TYR   A O    1 
ATOM   165  C  CB   A TYR   A 1 9   ? 11.446 -10.094 13.469  0.62 16.90 ?  9   TYR   A CB   1 
ATOM   166  C  CB   B TYR   A 1 9   ? 11.559 -10.329 13.586  0.38 16.97 ?  9   TYR   A CB   1 
ATOM   167  C  CG   A TYR   A 1 9   ? 12.344 -8.893  13.267  0.62 16.74 ?  9   TYR   A CG   1 
ATOM   168  C  CG   B TYR   A 1 9   ? 12.497 -9.157  13.472  0.38 15.77 ?  9   TYR   A CG   1 
ATOM   169  C  CD1  A TYR   A 1 9   ? 12.631 -8.041  14.323  0.62 16.94 ?  9   TYR   A CD1  1 
ATOM   170  C  CD1  B TYR   A 1 9   ? 12.884 -8.447  14.598  0.38 15.40 ?  9   TYR   A CD1  1 
ATOM   171  C  CD2  A TYR   A 1 9   ? 12.882 -8.604  12.021  0.62 16.26 ?  9   TYR   A CD2  1 
ATOM   172  C  CD2  B TYR   A 1 9   ? 12.981 -8.750  12.239  0.38 15.35 ?  9   TYR   A CD2  1 
ATOM   173  C  CE1  A TYR   A 1 9   ? 13.432 -6.934  14.146  0.62 17.04 ?  9   TYR   A CE1  1 
ATOM   174  C  CE1  B TYR   A 1 9   ? 13.731 -7.366  14.500  0.38 15.54 ?  9   TYR   A CE1  1 
ATOM   175  C  CE2  A TYR   A 1 9   ? 13.682 -7.495  11.835  0.62 16.36 ?  9   TYR   A CE2  1 
ATOM   176  C  CE2  B TYR   A 1 9   ? 13.828 -7.673  12.130  0.38 15.42 ?  9   TYR   A CE2  1 
ATOM   177  C  CZ   A TYR   A 1 9   ? 13.950 -6.669  12.901  0.62 16.56 ?  9   TYR   A CZ   1 
ATOM   178  C  CZ   B TYR   A 1 9   ? 14.199 -6.985  13.263  0.38 15.78 ?  9   TYR   A CZ   1 
ATOM   179  O  OH   A TYR   A 1 9   ? 14.738 -5.564  12.722  0.62 17.02 ?  9   TYR   A OH   1 
ATOM   180  O  OH   B TYR   A 1 9   ? 15.046 -5.915  13.150  0.38 16.51 ?  9   TYR   A OH   1 
ATOM   181  H  H    A TYR   A 1 9   ? 10.166 -9.514  15.544  0.62 21.50 ?  9   TYR   A H    1 
ATOM   182  H  H    B TYR   A 1 9   ? 10.280 -9.740  15.650  0.38 23.21 ?  9   TYR   A H    1 
ATOM   183  H  HA   A TYR   A 1 9   ? 9.742  -9.072  12.927  0.62 19.93 ?  9   TYR   A HA   1 
ATOM   184  H  HA   B TYR   A 1 9   ? 9.919  -9.228  13.036  0.38 21.35 ?  9   TYR   A HA   1 
ATOM   185  H  HB2  A TYR   A 1 9   ? 11.729 -10.556 14.273  0.62 20.30 ?  9   TYR   A HB2  1 
ATOM   186  H  HB2  B TYR   A 1 9   ? 11.807 -10.837 14.373  0.38 20.38 ?  9   TYR   A HB2  1 
ATOM   187  H  HB3  A TYR   A 1 9   ? 11.544 -10.674 12.700  0.62 20.30 ?  9   TYR   A HB3  1 
ATOM   188  H  HB3  B TYR   A 1 9   ? 11.666 -10.876 12.792  0.38 20.38 ?  9   TYR   A HB3  1 
ATOM   189  H  HD1  A TYR   A 1 9   ? 12.269 -8.220  15.165  0.62 20.35 ?  9   TYR   A HD1  1 
ATOM   190  H  HD1  B TYR   A 1 9   ? 12.560 -8.704  15.434  0.38 18.50 ?  9   TYR   A HD1  1 
ATOM   191  H  HD2  A TYR   A 1 9   ? 12.692 -9.161  11.301  0.62 19.53 ?  9   TYR   A HD2  1 
ATOM   192  H  HD2  B TYR   A 1 9   ? 12.730 -9.213  11.472  0.38 18.44 ?  9   TYR   A HD2  1 
ATOM   193  H  HE1  A TYR   A 1 9   ? 13.616 -6.374  14.865  0.62 20.47 ?  9   TYR   A HE1  1 
ATOM   194  H  HE1  B TYR   A 1 9   ? 13.984 -6.901  15.263  0.38 18.67 ?  9   TYR   A HE1  1 
ATOM   195  H  HE2  A TYR   A 1 9   ? 14.043 -7.311  10.997  0.62 19.65 ?  9   TYR   A HE2  1 
ATOM   196  H  HE2  B TYR   A 1 9   ? 14.152 -7.414  11.298  0.38 18.52 ?  9   TYR   A HE2  1 
ATOM   197  H  HH   A TYR   A 1 9   ? 14.837 -5.153  13.450  0.62 20.44 ?  9   TYR   A HH   1 
ATOM   198  H  HH   B TYR   A 1 9   ? 15.257 -5.807  12.343  0.38 19.83 ?  9   TYR   A HH   1 
ATOM   199  N  N    A LEU   A 1 10  ? 8.692  -11.127 12.084  0.62 15.83 ?  10  LEU   A N    1 
ATOM   200  N  N    B LEU   A 1 10  ? 8.834  -11.231 12.119  0.38 16.89 ?  10  LEU   A N    1 
ATOM   201  C  CA   A LEU   A 1 10  ? 8.129  -12.380 11.605  0.62 15.31 ?  10  LEU   A CA   1 
ATOM   202  C  CA   B LEU   A 1 10  ? 8.151  -12.409 11.613  0.38 16.44 ?  10  LEU   A CA   1 
ATOM   203  C  C    A LEU   A 1 10  ? 9.272  -13.306 11.205  0.62 14.09 ?  10  LEU   A C    1 
ATOM   204  C  C    B LEU   A 1 10  ? 9.195  -13.366 11.048  0.38 15.36 ?  10  LEU   A C    1 
ATOM   205  O  O    A LEU   A 1 10  ? 10.256 -12.872 10.596  0.62 13.14 ?  10  LEU   A O    1 
ATOM   206  O  O    B LEU   A 1 10  ? 10.016 -12.975 10.212  0.38 14.68 ?  10  LEU   A O    1 
ATOM   207  C  CB   A LEU   A 1 10  ? 7.233  -12.108 10.395  0.62 16.61 ?  10  LEU   A CB   1 
ATOM   208  C  CB   B LEU   A 1 10  ? 7.171  -11.993 10.517  0.38 17.20 ?  10  LEU   A CB   1 
ATOM   209  C  CG   A LEU   A 1 10  ? 6.590  -13.325 9.722   0.62 17.93 ?  10  LEU   A CG   1 
ATOM   210  C  CG   B LEU   A 1 10  ? 6.215  -13.077 10.027  0.38 17.83 ?  10  LEU   A CG   1 
ATOM   211  C  CD1  A LEU   A 1 10  ? 5.509  -13.911 10.609  0.62 18.87 ?  10  LEU   A CD1  1 
ATOM   212  C  CD1  B LEU   A 1 10  ? 5.149  -13.350 11.076  0.38 19.11 ?  10  LEU   A CD1  1 
ATOM   213  C  CD2  A LEU   A 1 10  ? 6.043  -12.975 8.344   0.62 19.71 ?  10  LEU   A CD2  1 
ATOM   214  C  CD2  B LEU   A 1 10  ? 5.577  -12.664 8.707   0.38 18.87 ?  10  LEU   A CD2  1 
ATOM   215  H  H    A LEU   A 1 10  ? 8.722  -10.506 11.481  0.62 19.02 ?  10  LEU   A H    1 
ATOM   216  H  H    B LEU   A 1 10  ? 8.966  -10.624 11.519  0.38 20.29 ?  10  LEU   A H    1 
ATOM   217  H  HA   A LEU   A 1 10  ? 7.603  -12.797 12.305  0.62 18.40 ?  10  LEU   A HA   1 
ATOM   218  H  HA   B LEU   A 1 10  ? 7.663  -12.847 12.329  0.38 19.74 ?  10  LEU   A HA   1 
ATOM   219  H  HB2  A LEU   A 1 10  ? 6.510  -11.526 10.676  0.62 19.95 ?  10  LEU   A HB2  1 
ATOM   220  H  HB2  B LEU   A 1 10  ? 6.628  -11.261 10.853  0.38 20.66 ?  10  LEU   A HB2  1 
ATOM   221  H  HB3  A LEU   A 1 10  ? 7.764  -11.656 9.721   0.62 19.95 ?  10  LEU   A HB3  1 
ATOM   222  H  HB3  B LEU   A 1 10  ? 7.681  -11.688 9.752   0.38 20.66 ?  10  LEU   A HB3  1 
ATOM   223  H  HG   A LEU   A 1 10  ? 7.271  -14.006 9.598   0.62 21.54 ?  10  LEU   A HG   1 
ATOM   224  H  HG   B LEU   A 1 10  ? 6.715  -13.896 9.881   0.38 21.42 ?  10  LEU   A HG   1 
ATOM   225  H  HD11 A LEU   A 1 10  ? 5.179  -14.728 10.207  0.62 22.67 ?  10  LEU   A HD11 1 
ATOM   226  H  HD11 B LEU   A 1 10  ? 4.531  -14.012 10.729  0.38 22.95 ?  10  LEU   A HD11 1 
ATOM   227  H  HD12 A LEU   A 1 10  ? 5.882  -14.096 11.484  0.62 22.67 ?  10  LEU   A HD12 1 
ATOM   228  H  HD12 B LEU   A 1 10  ? 5.575  -13.684 11.881  0.38 22.95 ?  10  LEU   A HD12 1 
ATOM   229  H  HD13 A LEU   A 1 10  ? 4.786  -13.266 10.690  0.62 22.67 ?  10  LEU   A HD13 1 
ATOM   230  H  HD13 B LEU   A 1 10  ? 4.678  -12.525 11.269  0.38 22.95 ?  10  LEU   A HD13 1 
ATOM   231  H  HD21 A LEU   A 1 10  ? 5.648  -13.772 7.955   0.62 23.67 ?  10  LEU   A HD21 1 
ATOM   232  H  HD21 B LEU   A 1 10  ? 4.973  -13.365 8.419   0.38 22.66 ?  10  LEU   A HD21 1 
ATOM   233  H  HD22 A LEU   A 1 10  ? 5.372  -12.284 8.439   0.62 23.67 ?  10  LEU   A HD22 1 
ATOM   234  H  HD22 B LEU   A 1 10  ? 5.090  -11.837 8.838   0.38 22.66 ?  10  LEU   A HD22 1 
ATOM   235  H  HD23 A LEU   A 1 10  ? 6.770  -12.660 7.786   0.62 23.67 ?  10  LEU   A HD23 1 
ATOM   236  H  HD23 B LEU   A 1 10  ? 6.277  -12.537 8.046   0.38 22.66 ?  10  LEU   A HD23 1 
ATOM   237  N  N    A LYS   A 1 11  ? 9.143  -14.584 11.551  0.62 14.97 ?  11  LYS   A N    1 
ATOM   238  N  N    B LYS   A 1 11  ? 9.171  -14.610 11.518  0.38 15.26 ?  11  LYS   A N    1 
ATOM   239  C  CA   A LYS   A 1 11  ? 10.175 -15.576 11.267  0.62 15.02 ?  11  LYS   A CA   1 
ATOM   240  C  CA   B LYS   A 1 11  ? 10.117 -15.619 11.061  0.38 14.78 ?  11  LYS   A CA   1 
ATOM   241  C  C    A LYS   A 1 11  ? 9.851  -16.206 9.919   0.62 14.98 ?  11  LYS   A C    1 
ATOM   242  C  C    B LYS   A 1 11  ? 9.699  -16.119 9.684   0.38 14.38 ?  11  LYS   A C    1 
ATOM   243  O  O    A LYS   A 1 11  ? 8.820  -16.876 9.772   0.62 15.76 ?  11  LYS   A O    1 
ATOM   244  O  O    B LYS   A 1 11  ? 8.527  -16.443 9.465   0.38 14.59 ?  11  LYS   A O    1 
ATOM   245  C  CB   A LYS   A 1 11  ? 10.223 -16.620 12.383  0.62 14.94 ?  11  LYS   A CB   1 
ATOM   246  C  CB   B LYS   A 1 11  ? 10.150 -16.776 12.063  0.38 14.55 ?  11  LYS   A CB   1 
ATOM   247  C  CG   A LYS   A 1 11  ? 11.255 -17.726 12.204  0.62 14.67 ?  11  LYS   A CG   1 
ATOM   248  C  CG   B LYS   A 1 11  ? 11.176 -17.869 11.784  0.38 14.25 ?  11  LYS   A CG   1 
ATOM   249  C  CD   A LYS   A 1 11  ? 11.326 -18.596 13.459  0.62 14.11 ?  11  LYS   A CD   1 
ATOM   250  C  CD   B LYS   A 1 11  ? 11.219 -18.841 12.963  0.38 14.64 ?  11  LYS   A CD   1 
ATOM   251  C  CE   A LYS   A 1 11  ? 12.329 -19.742 13.319  0.62 14.23 ?  11  LYS   A CE   1 
ATOM   252  C  CE   B LYS   A 1 11  ? 12.254 -19.943 12.787  0.38 15.06 ?  11  LYS   A CE   1 
ATOM   253  N  NZ   A LYS   A 1 11  ? 13.708 -19.236 13.075  0.62 14.47 ?  11  LYS   A NZ   1 
ATOM   254  N  NZ   B LYS   A 1 11  ? 13.641 -19.414 12.712  0.38 15.06 ?  11  LYS   A NZ   1 
ATOM   255  H  H    A LYS   A 1 11  ? 8.446  -14.909 11.938  0.62 17.98 ?  11  LYS   A H    1 
ATOM   256  H  H    B LYS   A 1 11  ? 8.610  -14.892 12.106  0.38 18.34 ?  11  LYS   A H    1 
ATOM   257  H  HA   A LYS   A 1 11  ? 11.037 -15.137 11.207  0.62 18.05 ?  11  LYS   A HA   1 
ATOM   258  H  HA   B LYS   A 1 11  ? 11.003 -15.231 10.996  0.38 17.75 ?  11  LYS   A HA   1 
ATOM   259  H  HB2  A LYS   A 1 11  ? 10.426 -16.162 13.216  0.62 17.95 ?  11  LYS   A HB2  1 
ATOM   260  H  HB2  B LYS   A 1 11  ? 10.348 -16.412 12.942  0.38 17.48 ?  11  LYS   A HB2  1 
ATOM   261  H  HB3  A LYS   A 1 11  ? 9.352  -17.037 12.449  0.62 17.95 ?  11  LYS   A HB3  1 
ATOM   262  H  HB3  B LYS   A 1 11  ? 9.276  -17.193 12.077  0.38 17.48 ?  11  LYS   A HB3  1 
ATOM   263  H  HG2  A LYS   A 1 11  ? 11.000 -18.287 11.456  0.62 17.63 ?  11  LYS   A HG2  1 
ATOM   264  H  HG2  B LYS   A 1 11  ? 10.923 -18.361 10.986  0.38 17.12 ?  11  LYS   A HG2  1 
ATOM   265  H  HG3  A LYS   A 1 11  ? 12.128 -17.332 12.053  0.62 17.63 ?  11  LYS   A HG3  1 
ATOM   266  H  HG3  B LYS   A 1 11  ? 12.057 -17.476 11.676  0.38 17.12 ?  11  LYS   A HG3  1 
ATOM   267  H  HD2  A LYS   A 1 11  ? 11.598 -18.047 14.214  0.62 16.96 ?  11  LYS   A HD2  1 
ATOM   268  H  HD2  B LYS   A 1 11  ? 11.438 -18.351 13.771  0.38 17.59 ?  11  LYS   A HD2  1 
ATOM   269  H  HD3  A LYS   A 1 11  ? 10.450 -18.981 13.632  0.62 16.96 ?  11  LYS   A HD3  1 
ATOM   270  H  HD3  B LYS   A 1 11  ? 10.348 -19.262 13.058  0.38 17.59 ?  11  LYS   A HD3  1 
ATOM   271  H  HE2  A LYS   A 1 11  ? 12.337 -20.265 14.138  0.62 17.10 ?  11  LYS   A HE2  1 
ATOM   272  H  HE2  B LYS   A 1 11  ? 12.202 -20.551 13.542  0.38 18.09 ?  11  LYS   A HE2  1 
ATOM   273  H  HE3  A LYS   A 1 11  ? 12.073 -20.301 12.569  0.62 17.10 ?  11  LYS   A HE3  1 
ATOM   274  H  HE3  B LYS   A 1 11  ? 12.068 -20.418 11.963  0.38 18.09 ?  11  LYS   A HE3  1 
ATOM   275  H  HZ1  A LYS   A 1 11  ? 14.275 -19.920 13.009  0.62 17.38 ?  11  LYS   A HZ1  1 
ATOM   276  H  HZ1  B LYS   A 1 11  ? 14.218 -20.087 12.615  0.38 18.09 ?  11  LYS   A HZ1  1 
ATOM   277  H  HZ2  A LYS   A 1 11  ? 13.731 -18.767 12.320  0.62 17.38 ?  11  LYS   A HZ2  1 
ATOM   278  H  HZ2  B LYS   A 1 11  ? 13.720 -18.863 12.019  0.38 18.09 ?  11  LYS   A HZ2  1 
ATOM   279  H  HZ3  A LYS   A 1 11  ? 13.963 -18.714 13.750  0.62 17.38 ?  11  LYS   A HZ3  1 
ATOM   280  H  HZ3  B LYS   A 1 11  ? 13.839 -18.972 13.459  0.38 18.09 ?  11  LYS   A HZ3  1 
ATOM   281  N  N    A LEU   A 1 12  ? 10.711 -15.978 8.923   0.62 14.45 ?  12  LEU   A N    1 
ATOM   282  N  N    B LEU   A 1 12  ? 10.653 -16.172 8.755   0.38 14.08 ?  12  LEU   A N    1 
ATOM   283  C  CA   A LEU   A 1 12  ? 10.484 -16.574 7.612   0.62 14.66 ?  12  LEU   A CA   1 
ATOM   284  C  CA   B LEU   A 1 12  ? 10.418 -16.700 7.412   0.38 14.21 ?  12  LEU   A CA   1 
ATOM   285  C  C    A LEU   A 1 12  ? 11.065 -17.976 7.519   0.62 13.98 ?  12  LEU   A C    1 
ATOM   286  C  C    B LEU   A 1 12  ? 11.040 -18.068 7.173   0.38 13.56 ?  12  LEU   A C    1 
ATOM   287  O  O    A LEU   A 1 12  ? 10.435 -18.874 6.949   0.62 14.42 ?  12  LEU   A O    1 
ATOM   288  O  O    B LEU   A 1 12  ? 10.416 -18.917 6.532   0.38 13.01 ?  12  LEU   A O    1 
ATOM   289  C  CB   A LEU   A 1 12  ? 11.075 -15.703 6.500   0.62 15.72 ?  12  LEU   A CB   1 
ATOM   290  C  CB   B LEU   A 1 12  ? 10.938 -15.724 6.349   0.38 14.42 ?  12  LEU   A CB   1 
ATOM   291  C  CG   A LEU   A 1 12  ? 10.348 -14.396 6.184   0.62 16.97 ?  12  LEU   A CG   1 
ATOM   292  C  CG   B LEU   A 1 12  ? 10.332 -14.316 6.340   0.38 15.02 ?  12  LEU   A CG   1 
ATOM   293  C  CD1  A LEU   A 1 12  ? 11.145 -13.602 5.162   0.62 17.64 ?  12  LEU   A CD1  1 
ATOM   294  C  CD1  B LEU   A 1 12  ? 10.833 -13.514 5.140   0.38 15.46 ?  12  LEU   A CD1  1 
ATOM   295  C  CD2  A LEU   A 1 12  ? 8.924  -14.658 5.690   0.62 17.34 ?  12  LEU   A CD2  1 
ATOM   296  C  CD2  B LEU   A 1 12  ? 8.807  -14.367 6.352   0.38 15.02 ?  12  LEU   A CD2  1 
ATOM   297  H  H    A LEU   A 1 12  ? 11.427 -15.497 8.981   0.62 17.36 ?  12  LEU   A H    1 
ATOM   298  H  H    B LEU   A 1 12  ? 11.453 -15.896 8.883   0.38 16.91 ?  12  LEU   A H    1 
ATOM   299  H  HA   A LEU   A 1 12  ? 9.533  -16.648 7.462   0.62 17.61 ?  12  LEU   A HA   1 
ATOM   300  H  HA   B LEU   A 1 12  ? 9.462  -16.794 7.286   0.38 17.08 ?  12  LEU   A HA   1 
ATOM   301  H  HB2  A LEU   A 1 12  ? 11.983 -15.471 6.748   0.62 18.89 ?  12  LEU   A HB2  1 
ATOM   302  H  HB2  B LEU   A 1 12  ? 11.894 -15.627 6.478   0.38 17.33 ?  12  LEU   A HB2  1 
ATOM   303  H  HB3  A LEU   A 1 12  ? 11.091 -16.227 5.683   0.62 18.89 ?  12  LEU   A HB3  1 
ATOM   304  H  HB3  B LEU   A 1 12  ? 10.771 -16.118 5.480   0.38 17.33 ?  12  LEU   A HB3  1 
ATOM   305  H  HG   A LEU   A 1 12  ? 10.289 -13.870 6.994   0.62 20.39 ?  12  LEU   A HG   1 
ATOM   306  H  HG   B LEU   A 1 12  ? 10.617 -13.852 7.142   0.38 18.05 ?  12  LEU   A HG   1 
ATOM   307  H  HD11 A LEU   A 1 12  ? 10.673 -12.778 4.969   0.62 21.19 ?  12  LEU   A HD11 1 
ATOM   308  H  HD11 B LEU   A 1 12  ? 10.435 -12.628 5.163   0.38 18.57 ?  12  LEU   A HD11 1 
ATOM   309  H  HD12 A LEU   A 1 12  ? 12.021 -13.406 5.531   0.62 21.19 ?  12  LEU   A HD12 1 
ATOM   310  H  HD12 B LEU   A 1 12  ? 11.800 -13.441 5.189   0.38 18.57 ?  12  LEU   A HD12 1 
ATOM   311  H  HD13 A LEU   A 1 12  ? 11.237 -14.130 4.354   0.62 21.19 ?  12  LEU   A HD13 1 
ATOM   312  H  HD13 B LEU   A 1 12  ? 10.577 -13.969 4.323   0.38 18.57 ?  12  LEU   A HD13 1 
ATOM   313  H  HD21 A LEU   A 1 12  ? 8.535  -13.824 5.387   0.62 20.83 ?  12  LEU   A HD21 1 
ATOM   314  H  HD21 B LEU   A 1 12  ? 8.463  -13.472 6.207   0.38 18.05 ?  12  LEU   A HD21 1 
ATOM   315  H  HD22 A LEU   A 1 12  ? 8.956  -15.293 4.955   0.62 20.83 ?  12  LEU   A HD22 1 
ATOM   316  H  HD22 B LEU   A 1 12  ? 8.505  -14.958 5.648   0.38 18.05 ?  12  LEU   A HD22 1 
ATOM   317  H  HD23 A LEU   A 1 12  ? 8.395  -15.025 6.417   0.62 20.83 ?  12  LEU   A HD23 1 
ATOM   318  H  HD23 B LEU   A 1 12  ? 8.510  -14.698 7.215   0.38 18.05 ?  12  LEU   A HD23 1 
ATOM   319  N  N    A THR   A 1 13  ? 12.263 -18.169 8.060   0.62 13.21 ?  13  THR   A N    1 
ATOM   320  N  N    B THR   A 1 13  ? 12.265 -18.295 7.642   0.38 13.38 ?  13  THR   A N    1 
ATOM   321  C  CA   A THR   A 1 13  ? 12.969 -19.437 7.992   0.62 12.95 ?  13  THR   A CA   1 
ATOM   322  C  CA   B THR   A 1 13  ? 12.941 -19.583 7.515   0.38 13.25 ?  13  THR   A CA   1 
ATOM   323  C  C    A THR   A 1 13  ? 13.700 -19.641 9.308   0.62 12.72 ?  13  THR   A C    1 
ATOM   324  C  C    B THR   A 1 13  ? 13.740 -19.820 8.790   0.38 13.13 ?  13  THR   A C    1 
ATOM   325  O  O    A THR   A 1 13  ? 13.569 -18.856 10.254  0.62 13.39 ?  13  THR   A O    1 
ATOM   326  O  O    B THR   A 1 13  ? 13.650 -19.055 9.755   0.38 13.19 ?  13  THR   A O    1 
ATOM   327  C  CB   A THR   A 1 13  ? 13.972 -19.466 6.831   0.62 13.74 ?  13  THR   A CB   1 
ATOM   328  C  CB   B THR   A 1 13  ? 13.866 -19.620 6.290   0.38 13.37 ?  13  THR   A CB   1 
ATOM   329  O  OG1  A THR   A 1 13  ? 14.965 -18.469 7.058   0.62 13.16 ?  13  THR   A OG1  1 
ATOM   330  O  OG1  B THR   A 1 13  ? 15.022 -18.812 6.542   0.38 13.99 ?  13  THR   A OG1  1 
ATOM   331  C  CG2  A THR   A 1 13  ? 13.307 -19.223 5.484   0.62 15.10 ?  13  THR   A CG2  1 
ATOM   332  C  CG2  B THR   A 1 13  ? 13.163 -19.101 5.048   0.38 13.46 ?  13  THR   A CG2  1 
ATOM   333  H  H    A THR   A 1 13  ? 12.701 -17.558 8.488   0.62 15.87 ?  13  THR   A H    1 
ATOM   334  H  H    B THR   A 1 13  ? 12.740 -17.705 8.048   0.38 16.07 ?  13  THR   A H    1 
ATOM   335  H  HA   A THR   A 1 13  ? 12.343 -20.158 7.874   0.62 15.55 ?  13  THR   A HA   1 
ATOM   336  H  HA   B THR   A 1 13  ? 12.282 -20.294 7.425   0.38 15.91 ?  13  THR   A HA   1 
ATOM   337  H  HB   A THR   A 1 13  ? 14.410 -20.329 6.801   0.62 16.51 ?  13  THR   A HB   1 
ATOM   338  H  HB   B THR   A 1 13  ? 14.136 -20.542 6.130   0.38 16.06 ?  13  THR   A HB   1 
ATOM   339  H  HG1  A THR   A 1 13  ? 15.608 -18.779 7.499   0.62 15.82 ?  13  THR   A HG1  1 
ATOM   340  H  HG1  B THR   A 1 13  ? 15.552 -18.855 5.890   0.38 16.81 ?  13  THR   A HG1  1 
ATOM   341  H  HG21 A THR   A 1 13  ? 13.962 -19.315 4.769   0.62 18.14 ?  13  THR   A HG21 1 
ATOM   342  H  HG21 B THR   A 1 13  ? 13.625 -19.419 4.257   0.38 16.17 ?  13  THR   A HG21 1 
ATOM   343  H  HG22 A THR   A 1 13  ? 12.603 -19.874 5.347   0.62 18.14 ?  13  THR   A HG22 1 
ATOM   344  H  HG22 B THR   A 1 13  ? 12.250 -19.420 5.028   0.38 16.17 ?  13  THR   A HG22 1 
ATOM   345  H  HG23 A THR   A 1 13  ? 12.931 -18.333 5.453   0.62 18.14 ?  13  THR   A HG23 1 
ATOM   346  H  HG23 B THR   A 1 13  ? 13.162 -18.132 5.049   0.38 16.17 ?  13  THR   A HG23 1 
ATOM   347  N  N    A ASP   A 1 14  ? 14.505 -20.698 9.345   0.62 13.10 ?  14  ASP   A N    1 
ATOM   348  N  N    B ASP   A 1 14  ? 14.555 -20.877 8.785   0.38 13.91 ?  14  ASP   A N    1 
ATOM   349  C  CA   A ASP   A 1 14  ? 15.345 -20.961 10.499  0.62 14.14 ?  14  ASP   A CA   1 
ATOM   350  C  CA   B ASP   A 1 14  ? 15.384 -21.174 9.947   0.38 14.28 ?  14  ASP   A CA   1 
ATOM   351  C  C    A ASP   A 1 14  ? 16.156 -19.734 10.905  0.62 13.67 ?  14  ASP   A C    1 
ATOM   352  C  C    B ASP   A 1 14  ? 16.249 -19.985 10.350  0.38 12.42 ?  14  ASP   A C    1 
ATOM   353  O  O    A ASP   A 1 14  ? 16.353 -19.482 12.098  0.62 14.13 ?  14  ASP   A O    1 
ATOM   354  O  O    B ASP   A 1 14  ? 16.539 -19.811 11.539  0.38 12.56 ?  14  ASP   A O    1 
ATOM   355  C  CB   A ASP   A 1 14  ? 16.286 -22.112 10.171  0.62 16.91 ?  14  ASP   A CB   1 
ATOM   356  C  CB   B ASP   A 1 14  ? 16.260 -22.398 9.662   0.38 17.28 ?  14  ASP   A CB   1 
ATOM   357  C  CG   A ASP   A 1 14  ? 17.189 -22.436 11.316  0.62 20.78 ?  14  ASP   A CG   1 
ATOM   358  C  CG   B ASP   A 1 14  ? 17.331 -22.594 10.709  0.38 20.39 ?  14  ASP   A CG   1 
ATOM   359  O  OD1  A ASP   A 1 14  ? 16.676 -22.973 12.320  0.62 21.84 ?  14  ASP   A OD1  1 
ATOM   360  O  OD1  B ASP   A 1 14  ? 16.983 -22.631 11.909  0.38 21.37 ?  14  ASP   A OD1  1 
ATOM   361  O  OD2  A ASP   A 1 14  ? 18.392 -22.127 11.226  0.62 22.48 -1 14  ASP   A OD2  1 
ATOM   362  O  OD2  B ASP   A 1 14  ? 18.515 -22.715 10.338  0.38 22.03 -1 14  ASP   A OD2  1 
ATOM   363  H  H    A ASP   A 1 14  ? 14.589 -21.264 8.714   0.62 15.74 ?  14  ASP   A H    1 
ATOM   364  H  H    B ASP   A 1 14  ? 14.656 -21.429 8.131   0.38 16.72 ?  14  ASP   A H    1 
ATOM   365  H  HA   A ASP   A 1 14  ? 14.787 -21.225 11.252  0.62 16.99 ?  14  ASP   A HA   1 
ATOM   366  H  HA   B ASP   A 1 14  ? 14.818 -21.401 10.706  0.38 17.16 ?  14  ASP   A HA   1 
ATOM   367  H  HB2  A ASP   A 1 14  ? 15.756 -22.902 9.960   0.62 20.32 ?  14  ASP   A HB2  1 
ATOM   368  H  HB2  B ASP   A 1 14  ? 15.710 -23.204 9.670   0.38 20.75 ?  14  ASP   A HB2  1 
ATOM   369  H  HB3  A ASP   A 1 14  ? 16.827 -21.869 9.401   0.62 20.32 ?  14  ASP   A HB3  1 
ATOM   370  H  HB3  B ASP   A 1 14  ? 16.677 -22.300 8.789   0.38 20.75 ?  14  ASP   A HB3  1 
ATOM   371  N  N    A ASN   A 1 15  ? 16.639 -18.958 9.931   0.62 13.18 ?  15  ASN   A N    1 
ATOM   372  N  N    B ASN   A 1 15  ? 16.656 -19.144 9.389   0.38 11.41 ?  15  ASN   A N    1 
ATOM   373  C  CA   A ASN   A 1 15  ? 17.611 -17.908 10.206  0.62 13.17 ?  15  ASN   A CA   1 
ATOM   374  C  CA   B ASN   A 1 15  ? 17.642 -18.106 9.671   0.38 11.72 ?  15  ASN   A CA   1 
ATOM   375  C  C    A ASN   A 1 15  ? 17.243 -16.523 9.688   0.62 13.05 ?  15  ASN   A C    1 
ATOM   376  C  C    B ASN   A 1 15  ? 17.291 -16.720 9.134   0.38 12.13 ?  15  ASN   A C    1 
ATOM   377  O  O    A ASN   A 1 15  ? 17.996 -15.583 9.947   0.62 13.42 ?  15  ASN   A O    1 
ATOM   378  O  O    B ASN   A 1 15  ? 18.109 -15.805 9.279   0.38 12.44 ?  15  ASN   A O    1 
ATOM   379  C  CB   A ASN   A 1 15  ? 18.990 -18.288 9.641   0.62 13.30 ?  15  ASN   A CB   1 
ATOM   380  C  CB   B ASN   A 1 15  ? 19.021 -18.525 9.131   0.38 11.65 ?  15  ASN   A CB   1 
ATOM   381  C  CG   A ASN   A 1 15  ? 18.982 -18.448 8.129   0.62 13.49 ?  15  ASN   A CG   1 
ATOM   382  C  CG   B ASN   A 1 15  ? 19.054 -18.573 7.617   0.38 12.19 ?  15  ASN   A CG   1 
ATOM   383  O  OD1  A ASN   A 1 15  ? 18.218 -19.249 7.576   0.62 13.83 ?  15  ASN   A OD1  1 
ATOM   384  O  OD1  B ASN   A 1 15  ? 18.455 -19.456 7.000   0.38 12.35 ?  15  ASN   A OD1  1 
ATOM   385  N  ND2  A ASN   A 1 15  ? 19.822 -17.668 7.449   0.62 14.06 ?  15  ASN   A ND2  1 
ATOM   386  N  ND2  B ASN   A 1 15  ? 19.749 -17.620 7.009   0.38 12.50 ?  15  ASN   A ND2  1 
ATOM   387  H  H    A ASN   A 1 15  ? 16.416 -19.021 9.112   0.62 15.84 ?  15  ASN   A H    1 
ATOM   388  H  H    B ASN   A 1 15  ? 16.368 -19.156 8.573   0.38 13.71 ?  15  ASN   A H    1 
ATOM   389  H  HA   A ASN   A 1 15  ? 17.713 -17.825 11.169  0.62 15.82 ?  15  ASN   A HA   1 
ATOM   390  H  HA   B ASN   A 1 15  ? 17.737 -18.037 10.632  0.38 14.08 ?  15  ASN   A HA   1 
ATOM   391  H  HB2  A ASN   A 1 15  ? 19.628 -17.588 9.868   0.62 15.98 ?  15  ASN   A HB2  1 
ATOM   392  H  HB2  B ASN   A 1 15  ? 19.689 -17.883 9.431   0.38 14.00 ?  15  ASN   A HB2  1 
ATOM   393  H  HB3  A ASN   A 1 15  ? 19.269 -19.127 10.033  0.62 15.98 ?  15  ASN   A HB3  1 
ATOM   394  H  HB3  B ASN   A 1 15  ? 19.252 -19.411 9.474   0.38 14.00 ?  15  ASN   A HB3  1 
ATOM   395  H  HD21 A ASN   A 1 15  ? 19.859 -17.719 6.590   0.62 16.89 ?  15  ASN   A HD21 1 
ATOM   396  H  HD21 B ASN   A 1 15  ? 19.797 -17.611 6.153   0.38 15.02 ?  15  ASN   A HD21 1 
ATOM   397  H  HD22 A ASN   A 1 15  ? 20.338 -17.118 7.866   0.62 16.89 ?  15  ASN   A HD22 1 
ATOM   398  H  HD22 B ASN   A 1 15  ? 20.146 -17.013 7.472   0.38 15.02 ?  15  ASN   A HD22 1 
ATOM   399  N  N    A VAL   A 1 16  ? 16.134 -16.362 8.970   0.62 13.22 ?  16  VAL   A N    1 
ATOM   400  N  N    B VAL   A 1 16  ? 16.117 -16.531 8.531   0.38 12.18 ?  16  VAL   A N    1 
ATOM   401  C  CA   A VAL   A 1 16  ? 15.743 -15.079 8.399   0.62 12.90 ?  16  VAL   A CA   1 
ATOM   402  C  CA   B VAL   A 1 16  ? 15.725 -15.257 7.933   0.38 11.90 ?  16  VAL   A CA   1 
ATOM   403  C  C    A VAL   A 1 16  ? 14.469 -14.594 9.074   0.62 13.31 ?  16  VAL   A C    1 
ATOM   404  C  C    B VAL   A 1 16  ? 14.453 -14.746 8.603   0.38 11.56 ?  16  VAL   A C    1 
ATOM   405  O  O    A VAL   A 1 16  ? 13.495 -15.347 9.217   0.62 13.34 ?  16  VAL   A O    1 
ATOM   406  O  O    B VAL   A 1 16  ? 13.443 -15.458 8.666   0.38 11.15 ?  16  VAL   A O    1 
ATOM   407  C  CB   A VAL   A 1 16  ? 15.587 -15.149 6.871   0.62 13.20 ?  16  VAL   A CB   1 
ATOM   408  C  CB   B VAL   A 1 16  ? 15.537 -15.377 6.409   0.38 12.83 ?  16  VAL   A CB   1 
ATOM   409  C  CG1  A VAL   A 1 16  ? 15.173 -13.779 6.310   0.62 13.68 ?  16  VAL   A CG1  1 
ATOM   410  C  CG1  B VAL   A 1 16  ? 15.085 -14.043 5.828   0.38 13.61 ?  16  VAL   A CG1  1 
ATOM   411  C  CG2  A VAL   A 1 16  ? 16.879 -15.632 6.230   0.62 14.45 ?  16  VAL   A CG2  1 
ATOM   412  C  CG2  B VAL   A 1 16  ? 16.824 -15.845 5.744   0.38 13.10 ?  16  VAL   A CG2  1 
ATOM   413  H  H    A VAL   A 1 16  ? 15.576 -16.996 8.807   0.62 15.88 ?  16  VAL   A H    1 
ATOM   414  H  H    B VAL   A 1 16  ? 15.525 -17.154 8.456   0.38 14.64 ?  16  VAL   A H    1 
ATOM   415  H  HA   A VAL   A 1 16  ? 16.434 -14.429 8.591   0.62 15.50 ?  16  VAL   A HA   1 
ATOM   416  H  HA   B VAL   A 1 16  ? 16.432 -14.615 8.094   0.38 14.31 ?  16  VAL   A HA   1 
ATOM   417  H  HB   A VAL   A 1 16  ? 14.892 -15.785 6.655   0.62 15.86 ?  16  VAL   A HB   1 
ATOM   418  H  HB   B VAL   A 1 16  ? 14.855 -16.040 6.225   0.38 15.41 ?  16  VAL   A HB   1 
ATOM   419  H  HG11 A VAL   A 1 16  ? 15.235 -13.803 5.341   0.62 16.43 ?  16  VAL   A HG11 1 
ATOM   420  H  HG11 B VAL   A 1 16  ? 15.165 -14.075 4.864   0.38 16.35 ?  16  VAL   A HG11 1 
ATOM   421  H  HG12 A VAL   A 1 16  ? 14.258 -13.589 6.574   0.62 16.43 ?  16  VAL   A HG12 1 
ATOM   422  H  HG12 B VAL   A 1 16  ? 14.163 -13.887 6.080   0.38 16.35 ?  16  VAL   A HG12 1 
ATOM   423  H  HG13 A VAL   A 1 16  ? 15.767 -13.098 6.660   0.62 16.43 ?  16  VAL   A HG13 1 
ATOM   424  H  HG13 B VAL   A 1 16  ? 15.651 -13.339 6.183   0.38 16.35 ?  16  VAL   A HG13 1 
ATOM   425  H  HG21 A VAL   A 1 16  ? 16.900 -15.349 5.302   0.62 17.36 ?  16  VAL   A HG21 1 
ATOM   426  H  HG21 B VAL   A 1 16  ? 16.787 -15.635 4.799   0.38 15.74 ?  16  VAL   A HG21 1 
ATOM   427  H  HG22 A VAL   A 1 16  ? 17.633 -15.254 6.708   0.62 17.36 ?  16  VAL   A HG22 1 
ATOM   428  H  HG22 B VAL   A 1 16  ? 17.577 -15.386 6.153   0.38 15.74 ?  16  VAL   A HG22 1 
ATOM   429  H  HG23 A VAL   A 1 16  ? 16.914 -16.600 6.282   0.62 17.36 ?  16  VAL   A HG23 1 
ATOM   430  H  HG23 B VAL   A 1 16  ? 16.919 -16.803 5.869   0.38 15.74 ?  16  VAL   A HG23 1 
ATOM   431  N  N    A TYR   A 1 17  ? 14.485 -13.322 9.465   0.62 13.15 ?  17  TYR   A N    1 
ATOM   432  N  N    B TYR   A 1 17  ? 14.505 -13.498 9.074   0.38 11.57 ?  17  TYR   A N    1 
ATOM   433  C  CA   A TYR   A 1 17  ? 13.399 -12.649 10.160  0.62 13.24 ?  17  TYR   A CA   1 
ATOM   434  C  CA   B TYR   A 1 17  ? 13.402 -12.807 9.733   0.38 12.01 ?  17  TYR   A CA   1 
ATOM   435  C  C    A TYR   A 1 17  ? 13.130 -11.331 9.447   0.62 13.62 ?  17  TYR   A C    1 
ATOM   436  C  C    B TYR   A 1 17  ? 13.131 -11.477 9.031   0.38 12.63 ?  17  TYR   A C    1 
ATOM   437  O  O    A TYR   A 1 17  ? 14.056 -10.726 8.901   0.62 13.07 ?  17  TYR   A O    1 
ATOM   438  O  O    B TYR   A 1 17  ? 13.988 -10.954 8.313   0.38 11.50 ?  17  TYR   A O    1 
ATOM   439  C  CB   A TYR   A 1 17  ? 13.823 -12.390 11.611  0.62 13.94 ?  17  TYR   A CB   1 
ATOM   440  C  CB   B TYR   A 1 17  ? 13.761 -12.513 11.191  0.38 12.67 ?  17  TYR   A CB   1 
ATOM   441  C  CG   A TYR   A 1 17  ? 14.061 -13.665 12.400  0.62 14.91 ?  17  TYR   A CG   1 
ATOM   442  C  CG   B TYR   A 1 17  ? 13.920 -13.750 12.037  0.38 14.32 ?  17  TYR   A CG   1 
ATOM   443  C  CD1  A TYR   A 1 17  ? 15.256 -14.376 12.293  0.62 16.02 ?  17  TYR   A CD1  1 
ATOM   444  C  CD1  B TYR   A 1 17  ? 15.088 -14.503 11.998  0.38 15.35 ?  17  TYR   A CD1  1 
ATOM   445  C  CD2  A TYR   A 1 17  ? 13.076 -14.173 13.237  0.62 15.71 ?  17  TYR   A CD2  1 
ATOM   446  C  CD2  B TYR   A 1 17  ? 12.894 -14.177 12.871  0.38 14.92 ?  17  TYR   A CD2  1 
ATOM   447  C  CE1  A TYR   A 1 17  ? 15.461 -15.558 13.010  0.62 17.17 ?  17  TYR   A CE1  1 
ATOM   448  C  CE1  B TYR   A 1 17  ? 15.229 -15.647 12.768  0.38 15.71 ?  17  TYR   A CE1  1 
ATOM   449  C  CE2  A TYR   A 1 17  ? 13.271 -15.351 13.957  0.62 16.63 ?  17  TYR   A CE2  1 
ATOM   450  C  CE2  B TYR   A 1 17  ? 13.025 -15.318 13.644  0.38 15.67 ?  17  TYR   A CE2  1 
ATOM   451  C  CZ   A TYR   A 1 17  ? 14.464 -16.038 13.842  0.62 17.23 ?  17  TYR   A CZ   1 
ATOM   452  C  CZ   B TYR   A 1 17  ? 14.195 -16.047 13.592  0.38 15.94 ?  17  TYR   A CZ   1 
ATOM   453  O  OH   A TYR   A 1 17  ? 14.654 -17.200 14.559  0.62 18.46 ?  17  TYR   A OH   1 
ATOM   454  O  OH   B TYR   A 1 17  ? 14.325 -17.180 14.361  0.38 16.37 ?  17  TYR   A OH   1 
ATOM   455  H  H    A TYR   A 1 17  ? 15.153 -12.790 9.318   0.62 15.80 ?  17  TYR   A H    1 
ATOM   456  H  H    B TYR   A 1 17  ? 15.215 -13.024 9.025   0.38 13.91 ?  17  TYR   A H    1 
ATOM   457  H  HA   A TYR   A 1 17  ? 12.598 -13.188 10.142  0.62 15.91 ?  17  TYR   A HA   1 
ATOM   458  H  HA   B TYR   A 1 17  ? 12.603 -13.363 9.707   0.38 14.44 ?  17  TYR   A HA   1 
ATOM   459  H  HB2  A TYR   A 1 17  ? 14.649 -11.879 11.610  0.62 16.75 ?  17  TYR   A HB2  1 
ATOM   460  H  HB2  B TYR   A 1 17  ? 14.601 -12.031 11.214  0.38 15.23 ?  17  TYR   A HB2  1 
ATOM   461  H  HB3  A TYR   A 1 17  ? 13.128 -11.887 12.059  0.62 16.75 ?  17  TYR   A HB3  1 
ATOM   462  H  HB3  B TYR   A 1 17  ? 13.058 -11.977 11.578  0.38 15.23 ?  17  TYR   A HB3  1 
ATOM   463  H  HD1  A TYR   A 1 17  ? 15.929 -14.062 11.732  0.62 19.24 ?  17  TYR   A HD1  1 
ATOM   464  H  HD1  B TYR   A 1 17  ? 15.786 -14.236 11.446  0.38 18.44 ?  17  TYR   A HD1  1 
ATOM   465  H  HD2  A TYR   A 1 17  ? 12.270 -13.716 13.317  0.62 18.88 ?  17  TYR   A HD2  1 
ATOM   466  H  HD2  B TYR   A 1 17  ? 12.102 -13.692 12.911  0.38 17.92 ?  17  TYR   A HD2  1 
ATOM   467  H  HE1  A TYR   A 1 17  ? 16.266 -16.024 12.930  0.62 20.62 ?  17  TYR   A HE1  1 
ATOM   468  H  HE1  B TYR   A 1 17  ? 16.022 -16.139 12.734  0.38 18.87 ?  17  TYR   A HE1  1 
ATOM   469  H  HE2  A TYR   A 1 17  ? 12.598 -15.667 14.512  0.62 19.97 ?  17  TYR   A HE2  1 
ATOM   470  H  HE2  B TYR   A 1 17  ? 12.330 -15.589 14.200  0.38 18.82 ?  17  TYR   A HE2  1 
ATOM   471  H  HH   A TYR   A 1 17  ? 15.417 -17.511 14.404  0.62 22.17 ?  17  TYR   A HH   1 
ATOM   472  H  HH   B TYR   A 1 17  ? 13.589 -17.380 14.705  0.38 19.66 ?  17  TYR   A HH   1 
ATOM   473  N  N    A ILE   A 1 18  ? 11.870 -10.877 9.431   0.62 14.18 ?  18  ILE   A N    1 
ATOM   474  N  N    B ILE   A 1 18  ? 11.946 -10.900 9.278   0.38 13.70 ?  18  ILE   A N    1 
ATOM   475  C  CA   A ILE   A 1 18  ? 11.500 -9.702  8.641   0.62 14.36 ?  18  ILE   A CA   1 
ATOM   476  C  CA   B ILE   A 1 18  ? 11.520 -9.683  8.584   0.38 14.22 ?  18  ILE   A CA   1 
ATOM   477  C  C    A ILE   A 1 18  ? 10.519 -8.827  9.417   0.62 15.16 ?  18  ILE   A C    1 
ATOM   478  C  C    B ILE   A 1 18  ? 10.625 -8.827  9.478   0.38 14.88 ?  18  ILE   A C    1 
ATOM   479  O  O    A ILE   A 1 18  ? 9.632  -9.334  10.113  0.62 15.11 ?  18  ILE   A O    1 
ATOM   480  O  O    B ILE   A 1 18  ? 9.935  -9.331  10.370  0.38 14.98 ?  18  ILE   A O    1 
ATOM   481  C  CB   A ILE   A 1 18  ? 10.988 -10.111 7.239   0.62 14.19 ?  18  ILE   A CB   1 
ATOM   482  C  CB   B ILE   A 1 18  ? 10.805 -10.024 7.256   0.38 14.62 ?  18  ILE   A CB   1 
ATOM   483  C  CG1  A ILE   A 1 18  ? 10.894 -8.903  6.310   0.62 15.12 ?  18  ILE   A CG1  1 
ATOM   484  C  CG1  B ILE   A 1 18  ? 10.811 -8.817  6.318   0.38 15.41 ?  18  ILE   A CG1  1 
ATOM   485  C  CG2  A ILE   A 1 18  ? 9.661  -10.883 7.319   0.62 14.02 ?  18  ILE   A CG2  1 
ATOM   486  C  CG2  B ILE   A 1 18  ? 9.380  -10.510 7.525   0.38 15.04 ?  18  ILE   A CG2  1 
ATOM   487  C  CD1  A ILE   A 1 18  ? 10.709 -9.285  4.864   0.62 16.47 ?  18  ILE   A CD1  1 
ATOM   488  C  CD1  B ILE   A 1 18  ? 10.370 -9.141  4.911   0.38 16.61 ?  18  ILE   A CD1  1 
ATOM   489  H  H    A ILE   A 1 18  ? 11.215 -11.239 9.859   0.62 17.03 ?  18  ILE   A H    1 
ATOM   490  H  H    B ILE   A 1 18  ? 11.383 -11.207 9.847   0.38 16.46 ?  18  ILE   A H    1 
ATOM   491  H  HA   A ILE   A 1 18  ? 12.299 -9.175  8.496   0.62 17.26 ?  18  ILE   A HA   1 
ATOM   492  H  HA   B ILE   A 1 18  ? 12.316 -9.172  8.368   0.38 17.09 ?  18  ILE   A HA   1 
ATOM   493  H  HB   A ILE   A 1 18  ? 11.643 -10.716 6.855   0.62 17.05 ?  18  ILE   A HB   1 
ATOM   494  H  HB   B ILE   A 1 18  ? 11.288 -10.743 6.828   0.38 17.56 ?  18  ILE   A HB   1 
ATOM   495  H  HG12 A ILE   A 1 18  ? 10.139 -8.359  6.571   0.62 18.17 ?  18  ILE   A HG12 1 
ATOM   496  H  HG12 B ILE   A 1 18  ? 10.211 -8.142  6.666   0.38 18.52 ?  18  ILE   A HG12 1 
ATOM   497  H  HG13 A ILE   A 1 18  ? 11.715 -8.393  6.374   0.62 18.17 ?  18  ILE   A HG13 1 
ATOM   498  H  HG13 B ILE   A 1 18  ? 11.714 -8.464  6.269   0.38 18.52 ?  18  ILE   A HG13 1 
ATOM   499  H  HG21 A ILE   A 1 18  ? 9.441  -11.228 6.435   0.62 16.84 ?  18  ILE   A HG21 1 
ATOM   500  H  HG21 B ILE   A 1 18  ? 9.028  -10.910 6.715   0.38 18.07 ?  18  ILE   A HG21 1 
ATOM   501  H  HG22 A ILE   A 1 18  ? 9.765  -11.622 7.939   0.62 16.84 ?  18  ILE   A HG22 1 
ATOM   502  H  HG22 B ILE   A 1 18  ? 9.399  -11.166 8.238   0.38 18.07 ?  18  ILE   A HG22 1 
ATOM   503  H  HG23 A ILE   A 1 18  ? 8.964  -10.287 7.623   0.62 16.84 ?  18  ILE   A HG23 1 
ATOM   504  H  HG23 B ILE   A 1 18  ? 8.827  -9.756  7.786   0.38 18.07 ?  18  ILE   A HG23 1 
ATOM   505  H  HD11 A ILE   A 1 18  ? 10.741 -8.481  4.320   0.62 19.78 ?  18  ILE   A HD11 1 
ATOM   506  H  HD11 B ILE   A 1 18  ? 10.439 -8.341  4.367   0.38 19.96 ?  18  ILE   A HD11 1 
ATOM   507  H  HD12 A ILE   A 1 18  ? 11.417 -9.891  4.601   0.62 19.78 ?  18  ILE   A HD12 1 
ATOM   508  H  HD12 B ILE   A 1 18  ? 10.946 -9.835  4.552   0.38 19.96 ?  18  ILE   A HD12 1 
ATOM   509  H  HD13 A ILE   A 1 18  ? 9.845  -9.717  4.759   0.62 19.78 ?  18  ILE   A HD13 1 
ATOM   510  H  HD13 B ILE   A 1 18  ? 9.452  -9.450  4.931   0.38 19.96 ?  18  ILE   A HD13 1 
ATOM   511  N  N    A LYS   A 1 19  ? 10.694 -7.506  9.305   0.62 15.49 ?  19  LYS   A N    1 
ATOM   512  N  N    B LYS   A 1 19  ? 10.609 -7.520  9.191   0.38 15.42 ?  19  LYS   A N    1 
ATOM   513  C  CA   A LYS   A 1 19  ? 9.888  -6.545  10.047  0.62 16.75 ?  19  LYS   A CA   1 
ATOM   514  C  CA   B LYS   A 1 19  ? 9.796  -6.543  9.908   0.38 16.13 ?  19  LYS   A CA   1 
ATOM   515  C  C    A LYS   A 1 19  ? 9.682  -5.300  9.199   0.62 16.59 ?  19  LYS   A C    1 
ATOM   516  C  C    B LYS   A 1 19  ? 9.616  -5.307  9.030   0.38 15.86 ?  19  LYS   A C    1 
ATOM   517  O  O    A LYS   A 1 19  ? 10.581 -4.888  8.463   0.62 16.60 ?  19  LYS   A O    1 
ATOM   518  O  O    B LYS   A 1 19  ? 10.522 -4.931  8.280   0.38 15.90 ?  19  LYS   A O    1 
ATOM   519  C  CB   A LYS   A 1 19  ? 10.619 -6.144  11.333  0.62 17.35 ?  19  LYS   A CB   1 
ATOM   520  C  CB   B LYS   A 1 19  ? 10.470 -6.147  11.229  0.38 16.92 ?  19  LYS   A CB   1 
ATOM   521  C  CG   A LYS   A 1 19  ? 9.880  -5.207  12.275  0.62 18.51 ?  19  LYS   A CG   1 
ATOM   522  C  CG   B LYS   A 1 19  ? 9.682  -5.154  12.076  0.38 17.70 ?  19  LYS   A CG   1 
ATOM   523  C  CD   A LYS   A 1 19  ? 10.783 -4.922  13.470  0.62 19.79 ?  19  LYS   A CD   1 
ATOM   524  C  CD   B LYS   A 1 19  ? 10.421 -4.849  13.368  0.38 18.43 ?  19  LYS   A CD   1 
ATOM   525  C  CE   A LYS   A 1 19  ? 10.143 -4.032  14.517  0.62 20.39 ?  19  LYS   A CE   1 
ATOM   526  C  CE   B LYS   A 1 19  ? 9.690  -3.826  14.220  0.38 18.62 ?  19  LYS   A CE   1 
ATOM   527  N  NZ   A LYS   A 1 19  ? 11.058 -3.875  15.685  0.62 20.74 ?  19  LYS   A NZ   1 
ATOM   528  N  NZ   B LYS   A 1 19  ? 10.497 -3.454  15.415  0.38 18.27 ?  19  LYS   A NZ   1 
ATOM   529  H  H    A LYS   A 1 19  ? 11.295 -7.140  8.797   0.62 18.61 ?  19  LYS   A H    1 
ATOM   530  H  H    B LYS   A 1 19  ? 11.074 -7.173  8.559   0.38 18.52 ?  19  LYS   A H    1 
ATOM   531  H  HA   A LYS   A 1 19  ? 9.029  -6.935  10.266  0.62 20.12 ?  19  LYS   A HA   1 
ATOM   532  H  HA   B LYS   A 1 19  ? 8.926  -6.927  10.105  0.38 19.38 ?  19  LYS   A HA   1 
ATOM   533  H  HB2  A LYS   A 1 19  ? 10.804 -6.950  11.832  0.62 20.85 ?  19  LYS   A HB2  1 
ATOM   534  H  HB2  B LYS   A 1 19  ? 10.602 -6.947  11.765  0.38 20.33 ?  19  LYS   A HB2  1 
ATOM   535  H  HB3  A LYS   A 1 19  ? 11.450 -5.712  11.088  0.62 20.85 ?  19  LYS   A HB3  1 
ATOM   536  H  HB3  B LYS   A 1 19  ? 11.329 -5.746  11.030  0.38 20.33 ?  19  LYS   A HB3  1 
ATOM   537  H  HG2  A LYS   A 1 19  ? 9.681  -4.370  11.825  0.62 22.23 ?  19  LYS   A HG2  1 
ATOM   538  H  HG2  B LYS   A 1 19  ? 9.572  -4.324  11.586  0.38 21.26 ?  19  LYS   A HG2  1 
ATOM   539  H  HG3  A LYS   A 1 19  ? 9.064  -5.629  12.591  0.62 22.23 ?  19  LYS   A HG3  1 
ATOM   540  H  HG3  B LYS   A 1 19  ? 8.817  -5.532  12.300  0.38 21.26 ?  19  LYS   A HG3  1 
ATOM   541  H  HD2  A LYS   A 1 19  ? 11.003 -5.763  13.896  0.62 23.77 ?  19  LYS   A HD2  1 
ATOM   542  H  HD2  B LYS   A 1 19  ? 10.508 -5.665  13.886  0.38 22.14 ?  19  LYS   A HD2  1 
ATOM   543  H  HD3  A LYS   A 1 19  ? 11.590 -4.486  13.157  0.62 23.77 ?  19  LYS   A HD3  1 
ATOM   544  H  HD3  B LYS   A 1 19  ? 11.299 -4.494  13.157  0.38 22.14 ?  19  LYS   A HD3  1 
ATOM   545  H  HE2  A LYS   A 1 19  ? 9.974  -3.155  14.137  0.62 24.49 ?  19  LYS   A HE2  1 
ATOM   546  H  HE2  B LYS   A 1 19  ? 9.534  -3.024  13.697  0.38 22.37 ?  19  LYS   A HE2  1 
ATOM   547  H  HE3  A LYS   A 1 19  ? 9.316  -4.435  14.824  0.62 24.49 ?  19  LYS   A HE3  1 
ATOM   548  H  HE3  B LYS   A 1 19  ? 8.850  -4.201  14.525  0.38 22.37 ?  19  LYS   A HE3  1 
ATOM   549  H  HZ1  A LYS   A 1 19  ? 10.667 -3.381  16.312  0.62 24.91 ?  19  LYS   A HZ1  1 
ATOM   550  H  HZ1  B LYS   A 1 19  ? 10.057 -2.859  15.908  0.38 21.95 ?  19  LYS   A HZ1  1 
ATOM   551  H  HZ2  A LYS   A 1 19  ? 11.255 -4.673  16.025  0.62 24.91 ?  19  LYS   A HZ2  1 
ATOM   552  H  HZ2  B LYS   A 1 19  ? 10.660 -4.176  15.911  0.38 21.95 ?  19  LYS   A HZ2  1 
ATOM   553  H  HZ3  A LYS   A 1 19  ? 11.810 -3.475  15.429  0.62 24.91 ?  19  LYS   A HZ3  1 
ATOM   554  H  HZ3  B LYS   A 1 19  ? 11.274 -3.100  15.161  0.38 21.95 ?  19  LYS   A HZ3  1 
ATOM   555  N  N    A ASN   A 1 20  ? 8.498  -4.700  9.311   0.62 17.34 ?  20  ASN   A N    1 
ATOM   556  N  N    B ASN   A 1 20  ? 8.437  -4.683  9.123   0.38 15.91 ?  20  ASN   A N    1 
ATOM   557  C  CA   A ASN   A 1 20  ? 8.267  -3.368  8.762   0.62 17.98 ?  20  ASN   A CA   1 
ATOM   558  C  CA   B ASN   A 1 20  ? 8.163  -3.404  8.459   0.38 16.18 ?  20  ASN   A CA   1 
ATOM   559  C  C    A ASN   A 1 20  ? 8.905  -2.375  9.722   0.62 17.78 ?  20  ASN   A C    1 
ATOM   560  C  C    B ASN   A 1 20  ? 8.709  -2.282  9.335   0.38 16.02 ?  20  ASN   A C    1 
ATOM   561  O  O    A ASN   A 1 20  ? 8.416  -2.178  10.839  0.62 17.86 ?  20  ASN   A O    1 
ATOM   562  O  O    B ASN   A 1 20  ? 8.057  -1.850  10.290  0.38 16.47 ?  20  ASN   A O    1 
ATOM   563  C  CB   A ASN   A 1 20  ? 6.772  -3.107  8.596   0.62 19.03 ?  20  ASN   A CB   1 
ATOM   564  C  CB   B ASN   A 1 20  ? 6.662  -3.239  8.222   0.38 16.39 ?  20  ASN   A CB   1 
ATOM   565  C  CG   A ASN   A 1 20  ? 6.459  -1.665  8.215   0.62 20.27 ?  20  ASN   A CG   1 
ATOM   566  C  CG   B ASN   A 1 20  ? 6.277  -1.843  7.716   0.38 16.69 ?  20  ASN   A CG   1 
ATOM   567  O  OD1  A ASN   A 1 20  ? 5.598  -1.026  8.824   0.62 21.61 ?  20  ASN   A OD1  1 
ATOM   568  O  OD1  B ASN   A 1 20  ? 5.143  -1.396  7.922   0.38 16.84 ?  20  ASN   A OD1  1 
ATOM   569  N  ND2  A ASN   A 1 20  ? 7.153  -1.150  7.204   0.62 21.23 ?  20  ASN   A ND2  1 
ATOM   570  N  ND2  B ASN   A 1 20  ? 7.204  -1.163  7.047   0.38 17.61 ?  20  ASN   A ND2  1 
ATOM   571  H  H    A ASN   A 1 20  ? 7.817  -5.046  9.703   0.62 20.83 ?  20  ASN   A H    1 
ATOM   572  H  H    B ASN   A 1 20  ? 7.759  -4.999  9.554   0.38 19.11 ?  20  ASN   A H    1 
ATOM   573  H  HA   A ASN   A 1 20  ? 8.695  -3.289  7.897   0.62 21.60 ?  20  ASN   A HA   1 
ATOM   574  H  HA   B ASN   A 1 20  ? 8.615  -3.378  7.603   0.38 19.44 ?  20  ASN   A HA   1 
ATOM   575  H  HB2  A ASN   A 1 20  ? 6.428  -3.684  7.895   0.62 22.85 ?  20  ASN   A HB2  1 
ATOM   576  H  HB2  B ASN   A 1 20  ? 6.369  -3.883  7.560   0.38 19.69 ?  20  ASN   A HB2  1 
ATOM   577  H  HB3  A ASN   A 1 20  ? 6.323  -3.300  9.433   0.62 22.85 ?  20  ASN   A HB3  1 
ATOM   578  H  HB3  B ASN   A 1 20  ? 6.189  -3.392  9.056   0.38 19.69 ?  20  ASN   A HB3  1 
ATOM   579  H  HD21 A ASN   A 1 20  ? 7.009  -0.340  6.952   0.62 25.50 ?  20  ASN   A HD21 1 
ATOM   580  H  HD21 B ASN   A 1 20  ? 7.023  -0.378  6.747   0.38 21.16 ?  20  ASN   A HD21 1 
ATOM   581  H  HD22 A ASN   A 1 20  ? 7.747  -1.625  6.801   0.62 25.50 ?  20  ASN   A HD22 1 
ATOM   582  H  HD22 B ASN   A 1 20  ? 7.982  -1.501  6.918   0.38 21.16 ?  20  ASN   A HD22 1 
ATOM   583  N  N    A ALA   A 1 21  ? 10.024 -1.784  9.315   0.62 18.21 ?  21  ALA   A N    1 
ATOM   584  N  N    B ALA   A 1 21  ? 9.904  -1.793  9.003   0.38 16.35 ?  21  ALA   A N    1 
ATOM   585  C  CA   A ALA   A 1 21  ? 10.746 -0.909  10.221  0.62 18.15 ?  21  ALA   A CA   1 
ATOM   586  C  CA   B ALA   A 1 21  ? 10.543 -0.772  9.822   0.38 16.28 ?  21  ALA   A CA   1 
ATOM   587  C  C    A ALA   A 1 21  ? 11.697 -0.026  9.437   0.62 17.81 ?  21  ALA   A C    1 
ATOM   588  C  C    B ALA   A 1 21  ? 11.606 -0.045  9.015   0.38 15.11 ?  21  ALA   A C    1 
ATOM   589  O  O    A ALA   A 1 21  ? 12.156 -0.388  8.350   0.62 18.16 ?  21  ALA   A O    1 
ATOM   590  O  O    B ALA   A 1 21  ? 12.085 -0.538  7.989   0.38 14.69 ?  21  ALA   A O    1 
ATOM   591  C  CB   A ALA   A 1 21  ? 11.526 -1.718  11.258  0.62 18.92 ?  21  ALA   A CB   1 
ATOM   592  C  CB   B ALA   A 1 21  ? 11.171 -1.371  11.084  0.38 17.29 ?  21  ALA   A CB   1 
ATOM   593  H  H    A ALA   A 1 21  ? 10.380 -1.883  8.539   0.62 21.87 ?  21  ALA   A H    1 
ATOM   594  H  H    B ALA   A 1 21  ? 10.354 -2.037  8.313   0.38 19.63 ?  21  ALA   A H    1 
ATOM   595  H  HA   A ALA   A 1 21  ? 10.111 -0.342  10.687  0.62 21.80 ?  21  ALA   A HA   1 
ATOM   596  H  HA   B ALA   A 1 21  ? 9.870  -0.131  10.097  0.38 19.56 ?  21  ALA   A HA   1 
ATOM   597  H  HB1  A ALA   A 1 21  ? 11.888 -1.105  11.910  0.62 22.73 ?  21  ALA   A HB1  1 
ATOM   598  H  HB1  B ALA   A 1 21  ? 11.583 -0.659  11.598  0.38 20.77 ?  21  ALA   A HB1  1 
ATOM   599  H  HB2  A ALA   A 1 21  ? 10.916 -2.340  11.689  0.62 22.73 ?  21  ALA   A HB2  1 
ATOM   600  H  HB2  B ALA   A 1 21  ? 10.478 -1.801  11.611  0.38 20.77 ?  21  ALA   A HB2  1 
ATOM   601  H  HB3  A ALA   A 1 21  ? 12.233 -2.203  10.812  0.62 22.73 ?  21  ALA   A HB3  1 
ATOM   602  H  HB3  B ALA   A 1 21  ? 11.841 -2.024  10.826  0.38 20.77 ?  21  ALA   A HB3  1 
ATOM   603  N  N    A ASP   A 1 22  ? 11.975 1.139   10.013  0.62 17.84 ?  22  ASP   A N    1 
ATOM   604  N  N    B ASP   A 1 22  ? 11.951 1.147   9.497   0.38 15.37 ?  22  ASP   A N    1 
ATOM   605  C  CA   A ASP   A 1 22  ? 13.011 2.039   9.523   0.62 17.59 ?  22  ASP   A CA   1 
ATOM   606  C  CA   B ASP   A 1 22  ? 13.103 1.898   9.009   0.38 15.40 ?  22  ASP   A CA   1 
ATOM   607  C  C    A ASP   A 1 22  ? 14.343 1.553   10.079  0.62 16.47 ?  22  ASP   A C    1 
ATOM   608  C  C    B ASP   A 1 22  ? 14.361 1.336   9.668   0.38 14.38 ?  22  ASP   A C    1 
ATOM   609  O  O    A ASP   A 1 22  ? 14.559 1.577   11.295  0.62 17.33 ?  22  ASP   A O    1 
ATOM   610  O  O    B ASP   A 1 22  ? 14.456 1.300   10.899  0.38 14.42 ?  22  ASP   A O    1 
ATOM   611  C  CB   A ASP   A 1 22  ? 12.705 3.451   10.013  0.62 19.02 ?  22  ASP   A CB   1 
ATOM   612  C  CB   B ASP   A 1 22  ? 12.920 3.375   9.370   0.38 16.70 ?  22  ASP   A CB   1 
ATOM   613  C  CG   A ASP   A 1 22  ? 13.689 4.487   9.499   0.62 20.30 ?  22  ASP   A CG   1 
ATOM   614  C  CG   B ASP   A 1 22  ? 14.063 4.261   8.888   0.38 17.45 ?  22  ASP   A CG   1 
ATOM   615  O  OD1  A ASP   A 1 22  ? 14.806 4.124   9.081   0.62 20.29 ?  22  ASP   A OD1  1 
ATOM   616  O  OD1  B ASP   A 1 22  ? 15.071 3.736   8.372   0.38 17.40 ?  22  ASP   A OD1  1 
ATOM   617  O  OD2  A ASP   A 1 22  ? 13.336 5.685   9.527   0.62 21.32 -1 22  ASP   A OD2  1 
ATOM   618  O  OD2  B ASP   A 1 22  ? 13.950 5.500   9.031   0.38 18.80 -1 22  ASP   A OD2  1 
ATOM   619  H  H    A ASP   A 1 22  ? 11.559 1.438   10.705  0.62 21.43 ?  22  ASP   A H    1 
ATOM   620  H  H    B ASP   A 1 22  ? 11.511 1.553   10.119  0.38 18.46 ?  22  ASP   A H    1 
ATOM   621  H  HA   A ASP   A 1 22  ? 13.037 2.025   8.552   0.62 21.13 ?  22  ASP   A HA   1 
ATOM   622  H  HA   B ASP   A 1 22  ? 13.170 1.807   8.044   0.38 18.50 ?  22  ASP   A HA   1 
ATOM   623  H  HB2  A ASP   A 1 22  ? 11.818 3.702   9.714   0.62 22.84 ?  22  ASP   A HB2  1 
ATOM   624  H  HB2  B ASP   A 1 22  ? 12.099 3.698   8.968   0.38 20.06 ?  22  ASP   A HB2  1 
ATOM   625  H  HB3  A ASP   A 1 22  ? 12.739 3.455   10.984  0.62 22.84 ?  22  ASP   A HB3  1 
ATOM   626  H  HB3  B ASP   A 1 22  ? 12.872 3.456   10.334  0.38 20.06 ?  22  ASP   A HB3  1 
ATOM   627  N  N    A ILE   A 1 23  ? 15.234 1.103   9.191   0.62 15.56 ?  23  ILE   A N    1 
ATOM   628  N  N    B ILE   A 1 23  ? 15.316 0.877   8.850   0.38 14.19 ?  23  ILE   A N    1 
ATOM   629  C  CA   A ILE   A 1 23  ? 16.497 0.509   9.626   0.62 15.16 ?  23  ILE   A CA   1 
ATOM   630  C  CA   B ILE   A 1 23  ? 16.547 0.279   9.371   0.38 14.01 ?  23  ILE   A CA   1 
ATOM   631  C  C    A ILE   A 1 23  ? 17.295 1.476   10.489  0.62 15.24 ?  23  ILE   A C    1 
ATOM   632  C  C    B ILE   A 1 23  ? 17.283 1.242   10.291  0.38 14.38 ?  23  ILE   A C    1 
ATOM   633  O  O    A ILE   A 1 23  ? 18.024 1.051   11.396  0.62 15.66 ?  23  ILE   A O    1 
ATOM   634  O  O    B ILE   A 1 23  ? 17.970 0.814   11.228  0.38 14.23 ?  23  ILE   A O    1 
ATOM   635  C  CB   A ILE   A 1 23  ? 17.294 -0.004  8.408   0.62 14.83 ?  23  ILE   A CB   1 
ATOM   636  C  CB   B ILE   A 1 23  ? 17.452 -0.241  8.228   0.38 13.56 ?  23  ILE   A CB   1 
ATOM   637  C  CG1  A ILE   A 1 23  ? 18.467 -0.878  8.862   0.62 14.87 ?  23  ILE   A CG1  1 
ATOM   638  C  CG1  B ILE   A 1 23  ? 18.504 -1.212  8.776   0.38 13.62 ?  23  ILE   A CG1  1 
ATOM   639  C  CG2  A ILE   A 1 23  ? 17.740 1.160   7.521   0.62 15.07 ?  23  ILE   A CG2  1 
ATOM   640  C  CG2  B ILE   A 1 23  ? 18.140 0.908   7.496   0.38 13.27 ?  23  ILE   A CG2  1 
ATOM   641  C  CD1  A ILE   A 1 23  ? 19.125 -1.649  7.737   0.62 15.33 ?  23  ILE   A CD1  1 
ATOM   642  C  CD1  B ILE   A 1 23  ? 19.425 -1.794  7.712   0.38 13.77 ?  23  ILE   A CD1  1 
ATOM   643  H  H    A ILE   A 1 23  ? 15.128 1.126   8.341   0.62 18.69 ?  23  ILE   A H    1 
ATOM   644  H  H    B ILE   A 1 23  ? 15.271 0.888   8.003   0.38 17.05 ?  23  ILE   A H    1 
ATOM   645  H  HA   A ILE   A 1 23  ? 16.298 -0.266  10.175  0.62 18.22 ?  23  ILE   A HA   1 
ATOM   646  H  HA   B ILE   A 1 23  ? 16.299 -0.493  9.899   0.38 16.83 ?  23  ILE   A HA   1 
ATOM   647  H  HB   A ILE   A 1 23  ? 16.702 -0.559  7.880   0.62 17.81 ?  23  ILE   A HB   1 
ATOM   648  H  HB   B ILE   A 1 23  ? 16.901 -0.721  7.589   0.38 16.29 ?  23  ILE   A HB   1 
ATOM   649  H  HG12 A ILE   A 1 23  ? 19.141 -0.315  9.267   0.62 17.86 ?  23  ILE   A HG12 1 
ATOM   650  H  HG12 B ILE   A 1 23  ? 19.059 -0.746  9.420   0.38 16.37 ?  23  ILE   A HG12 1 
ATOM   651  H  HG13 A ILE   A 1 23  ? 18.140 -1.523  9.509   0.62 17.86 ?  23  ILE   A HG13 1 
ATOM   652  H  HG13 B ILE   A 1 23  ? 18.051 -1.954  9.210   0.38 16.37 ?  23  ILE   A HG13 1 
ATOM   653  H  HG21 A ILE   A 1 23  ? 18.123 0.807   6.702   0.62 18.10 ?  23  ILE   A HG21 1 
ATOM   654  H  HG21 B ILE   A 1 23  ? 18.500 0.579   6.654   0.38 15.94 ?  23  ILE   A HG21 1 
ATOM   655  H  HG22 A ILE   A 1 23  ? 16.967 1.711   7.310   0.62 18.10 ?  23  ILE   A HG22 1 
ATOM   656  H  HG22 B ILE   A 1 23  ? 17.492 1.606   7.326   0.38 15.94 ?  23  ILE   A HG22 1 
ATOM   657  H  HG23 A ILE   A 1 23  ? 18.400 1.689   7.994   0.62 18.10 ?  23  ILE   A HG23 1 
ATOM   658  H  HG23 B ILE   A 1 23  ? 18.861 1.251   8.048   0.38 15.94 ?  23  ILE   A HG23 1 
ATOM   659  H  HD11 A ILE   A 1 23  ? 19.826 -2.208  8.108   0.62 18.41 ?  23  ILE   A HD11 1 
ATOM   660  H  HD11 B ILE   A 1 23  ? 19.960 -2.499  8.110   0.38 16.54 ?  23  ILE   A HD11 1 
ATOM   661  H  HD12 A ILE   A 1 23  ? 18.457 -2.203  7.302   0.62 18.41 ?  23  ILE   A HD12 1 
ATOM   662  H  HD12 B ILE   A 1 23  ? 18.883 -2.157  6.993   0.38 16.54 ?  23  ILE   A HD12 1 
ATOM   663  H  HD13 A ILE   A 1 23  ? 19.500 -1.022  7.102   0.62 18.41 ?  23  ILE   A HD13 1 
ATOM   664  H  HD13 B ILE   A 1 23  ? 20.000 -1.092  7.373   0.38 16.54 ?  23  ILE   A HD13 1 
ATOM   665  N  N    A VAL   A 1 24  ? 17.166 2.781   10.239  0.62 15.73 ?  24  VAL   A N    1 
ATOM   666  N  N    B VAL   A 1 24  ? 17.153 2.548   10.049  0.38 15.32 ?  24  VAL   A N    1 
ATOM   667  C  CA   A VAL   A 1 24  ? 17.832 3.766   11.086  0.62 16.74 ?  24  VAL   A CA   1 
ATOM   668  C  CA   B VAL   A 1 24  ? 17.820 3.533   10.894  0.38 16.47 ?  24  VAL   A CA   1 
ATOM   669  C  C    A VAL   A 1 24  ? 17.291 3.691   12.506  0.62 17.10 ?  24  VAL   A C    1 
ATOM   670  C  C    B VAL   A 1 24  ? 17.250 3.503   12.306  0.38 17.45 ?  24  VAL   A C    1 
ATOM   671  O  O    A VAL   A 1 24  ? 18.049 3.607   13.480  0.62 17.81 ?  24  VAL   A O    1 
ATOM   672  O  O    B VAL   A 1 24  ? 17.996 3.528   13.292  0.38 18.12 ?  24  VAL   A O    1 
ATOM   673  C  CB   A VAL   A 1 24  ? 17.668 5.179   10.499  0.62 17.47 ?  24  VAL   A CB   1 
ATOM   674  C  CB   B VAL   A 1 24  ? 17.708 4.930   10.260  0.38 17.26 ?  24  VAL   A CB   1 
ATOM   675  C  CG1  A VAL   A 1 24  ? 18.127 6.233   11.502  0.62 18.06 ?  24  VAL   A CG1  1 
ATOM   676  C  CG1  B VAL   A 1 24  ? 18.367 5.972   11.143  0.38 18.27 ?  24  VAL   A CG1  1 
ATOM   677  C  CG2  A VAL   A 1 24  ? 18.425 5.306   9.188   0.62 17.99 ?  24  VAL   A CG2  1 
ATOM   678  C  CG2  B VAL   A 1 24  ? 18.314 4.927   8.867   0.38 17.48 ?  24  VAL   A CG2  1 
ATOM   679  H  H    A VAL   A 1 24  ? 16.697 3.112   9.601   0.62 18.90 ?  24  VAL   A H    1 
ATOM   680  H  H    B VAL   A 1 24  ? 16.686 2.882   9.412   0.38 18.40 ?  24  VAL   A H    1 
ATOM   681  H  HA   A VAL   A 1 24  ? 18.778 3.566   11.118  0.62 20.11 ?  24  VAL   A HA   1 
ATOM   682  H  HA   B VAL   A 1 24  ? 18.760 3.309   10.954  0.38 19.78 ?  24  VAL   A HA   1 
ATOM   683  H  HB   A VAL   A 1 24  ? 16.729 5.335   10.310  0.62 20.98 ?  24  VAL   A HB   1 
ATOM   684  H  HB   B VAL   A 1 24  ? 16.771 5.162   10.175  0.38 20.73 ?  24  VAL   A HB   1 
ATOM   685  H  HG11 A VAL   A 1 24  ? 18.293 7.063   11.030  0.62 21.69 ?  24  VAL   A HG11 1 
ATOM   686  H  HG11 B VAL   A 1 24  ? 18.457 6.796   10.640  0.38 21.94 ?  24  VAL   A HG11 1 
ATOM   687  H  HG12 A VAL   A 1 24  ? 17.432 6.364   12.165  0.62 21.69 ?  24  VAL   A HG12 1 
ATOM   688  H  HG12 B VAL   A 1 24  ? 17.811 6.121   11.923  0.38 21.94 ?  24  VAL   A HG12 1 
ATOM   689  H  HG13 A VAL   A 1 24  ? 18.943 5.927   11.928  0.62 21.69 ?  24  VAL   A HG13 1 
ATOM   690  H  HG13 B VAL   A 1 24  ? 19.240 5.650   11.411  0.38 21.94 ?  24  VAL   A HG13 1 
ATOM   691  H  HG21 A VAL   A 1 24  ? 18.188 6.146   8.765   0.62 21.61 ?  24  VAL   A HG21 1 
ATOM   692  H  HG21 B VAL   A 1 24  ? 18.392 5.841   8.556   0.38 21.00 ?  24  VAL   A HG21 1 
ATOM   693  H  HG22 A VAL   A 1 24  ? 19.378 5.286   9.370   0.62 21.61 ?  24  VAL   A HG22 1 
ATOM   694  H  HG22 B VAL   A 1 24  ? 19.191 4.514   8.907   0.38 21.00 ?  24  VAL   A HG22 1 
ATOM   695  H  HG23 A VAL   A 1 24  ? 18.184 4.565   8.607   0.62 21.61 ?  24  VAL   A HG23 1 
ATOM   696  H  HG23 B VAL   A 1 24  ? 17.738 4.420   8.274   0.38 21.00 ?  24  VAL   A HG23 1 
ATOM   697  N  N    A GLU   A 1 25  ? 15.964 3.733   12.645  0.62 17.91 ?  25  GLU   A N    1 
ATOM   698  N  N    B GLU   A 1 25  ? 15.922 3.449   12.429  0.38 18.45 ?  25  GLU   A N    1 
ATOM   699  C  CA   A GLU   A 1 25  ? 15.362 3.658   13.971  0.62 19.47 ?  25  GLU   A CA   1 
ATOM   700  C  CA   B GLU   A 1 25  ? 15.312 3.410   13.754  0.38 19.82 ?  25  GLU   A CA   1 
ATOM   701  C  C    A GLU   A 1 25  ? 15.605 2.297   14.612  0.62 18.38 ?  25  GLU   A C    1 
ATOM   702  C  C    B GLU   A 1 25  ? 15.553 2.072   14.440  0.38 19.69 ?  25  GLU   A C    1 
ATOM   703  O  O    A GLU   A 1 25  ? 15.850 2.213   15.822  0.62 18.86 ?  25  GLU   A O    1 
ATOM   704  O  O    B GLU   A 1 25  ? 15.705 2.025   15.666  0.38 20.49 ?  25  GLU   A O    1 
ATOM   705  C  CB   A GLU   A 1 25  ? 13.870 3.995   13.893  0.62 22.49 ?  25  GLU   A CB   1 
ATOM   706  C  CB   B GLU   A 1 25  ? 13.817 3.715   13.657  0.38 21.93 ?  25  GLU   A CB   1 
ATOM   707  C  CG   A GLU   A 1 25  ? 13.601 5.457   13.545  0.62 25.98 ?  25  GLU   A CG   1 
ATOM   708  C  CG   B GLU   A 1 25  ? 13.525 5.113   13.133  0.38 24.66 ?  25  GLU   A CG   1 
ATOM   709  C  CD   A GLU   A 1 25  ? 14.353 6.425   14.446  0.62 29.17 ?  25  GLU   A CD   1 
ATOM   710  C  CD   B GLU   A 1 25  ? 14.254 6.196   13.901  0.38 27.18 ?  25  GLU   A CD   1 
ATOM   711  O  OE1  A GLU   A 1 25  ? 14.376 6.202   15.677  0.62 30.26 ?  25  GLU   A OE1  1 
ATOM   712  O  OE1  B GLU   A 1 25  ? 14.388 6.067   15.136  0.38 28.53 ?  25  GLU   A OE1  1 
ATOM   713  O  OE2  A GLU   A 1 25  ? 14.939 7.393   13.922  0.62 30.26 -1 25  GLU   A OE2  1 
ATOM   714  O  OE2  B GLU   A 1 25  ? 14.708 7.170   13.264  0.38 28.03 -1 25  GLU   A OE2  1 
ATOM   715  H  H    A GLU   A 1 25  ? 15.401 3.810   11.998  0.62 21.51 ?  25  GLU   A H    1 
ATOM   716  H  H    B GLU   A 1 25  ? 15.364 3.433   11.773  0.38 22.16 ?  25  GLU   A H    1 
ATOM   717  H  HA   A GLU   A 1 25  ? 15.782 4.317   14.542  0.62 23.39 ?  25  GLU   A HA   1 
ATOM   718  H  HA   B GLU   A 1 25  ? 15.722 4.095   14.301  0.38 23.81 ?  25  GLU   A HA   1 
ATOM   719  H  HB2  A GLU   A 1 25  ? 13.452 3.450   13.206  0.62 27.01 ?  25  GLU   A HB2  1 
ATOM   720  H  HB2  B GLU   A 1 25  ? 13.402 3.079   13.051  0.38 26.34 ?  25  GLU   A HB2  1 
ATOM   721  H  HB3  A GLU   A 1 25  ? 13.453 3.818   14.751  0.62 27.01 ?  25  GLU   A HB3  1 
ATOM   722  H  HB3  B GLU   A 1 25  ? 13.420 3.636   14.540  0.38 26.34 ?  25  GLU   A HB3  1 
ATOM   723  H  HG2  A GLU   A 1 25  ? 13.879 5.618   12.631  0.62 31.20 ?  25  GLU   A HG2  1 
ATOM   724  H  HG2  B GLU   A 1 25  ? 13.813 5.171   12.212  0.38 29.61 ?  25  GLU   A HG2  1 
ATOM   725  H  HG3  A GLU   A 1 25  ? 12.651 5.635   13.640  0.62 31.20 ?  25  GLU   A HG3  1 
ATOM   726  H  HG3  B GLU   A 1 25  ? 12.576 5.286   13.203  0.38 29.61 ?  25  GLU   A HG3  1 
ATOM   727  N  N    A GLU   A 1 26  ? 15.556 1.222   13.819  0.62 17.58 ?  26  GLU   A N    1 
ATOM   728  N  N    B GLU   A 1 26  ? 15.599 0.982   13.674  0.38 19.15 ?  26  GLU   A N    1 
ATOM   729  C  CA   A GLU   A 1 26  ? 15.870 -0.104  14.349  0.62 17.68 ?  26  GLU   A CA   1 
ATOM   730  C  CA   B GLU   A 1 26  ? 15.913 -0.315  14.261  0.38 18.63 ?  26  GLU   A CA   1 
ATOM   731  C  C    A GLU   A 1 26  ? 17.288 -0.139  14.903  0.62 16.59 ?  26  GLU   A C    1 
ATOM   732  C  C    B GLU   A 1 26  ? 17.338 -0.354  14.786  0.38 17.30 ?  26  GLU   A C    1 
ATOM   733  O  O    A GLU   A 1 26  ? 17.521 -0.598  16.028  0.62 16.65 ?  26  GLU   A O    1 
ATOM   734  O  O    B GLU   A 1 26  ? 17.611 -1.005  15.801  0.38 17.30 ?  26  GLU   A O    1 
ATOM   735  C  CB   A GLU   A 1 26  ? 15.721 -1.167  13.257  0.62 19.51 ?  26  GLU   A CB   1 
ATOM   736  C  CB   B GLU   A 1 26  ? 15.707 -1.422  13.228  0.38 19.51 ?  26  GLU   A CB   1 
ATOM   737  C  CG   A GLU   A 1 26  ? 14.351 -1.803  13.121  0.62 22.42 ?  26  GLU   A CG   1 
ATOM   738  C  CG   B GLU   A 1 26  ? 14.260 -1.729  12.957  0.38 20.95 ?  26  GLU   A CG   1 
ATOM   739  C  CD   A GLU   A 1 26  ? 13.941 -2.631  14.335  0.62 23.38 ?  26  GLU   A CD   1 
ATOM   740  C  CD   B GLU   A 1 26  ? 13.558 -2.278  14.171  0.38 21.17 ?  26  GLU   A CD   1 
ATOM   741  O  OE1  A GLU   A 1 26  ? 14.329 -3.816  14.466  0.62 23.78 ?  26  GLU   A OE1  1 
ATOM   742  O  OE1  B GLU   A 1 26  ? 14.157 -3.112  14.881  0.38 21.44 ?  26  GLU   A OE1  1 
ATOM   743  O  OE2  A GLU   A 1 26  ? 13.213 -2.083  15.172  0.62 23.76 -1 26  GLU   A OE2  1 
ATOM   744  O  OE2  B GLU   A 1 26  ? 12.416 -1.856  14.423  0.38 20.58 -1 26  GLU   A OE2  1 
ATOM   745  H  H    A GLU   A 1 26  ? 15.344 1.242   12.983  0.62 21.12 ?  26  GLU   A H    1 
ATOM   746  H  H    B GLU   A 1 26  ? 15.459 0.969   12.826  0.38 23.00 ?  26  GLU   A H    1 
ATOM   747  H  HA   A GLU   A 1 26  ? 15.255 -0.310  15.066  0.62 21.23 ?  26  GLU   A HA   1 
ATOM   748  H  HA   B GLU   A 1 26  ? 15.316 -0.476  15.004  0.38 22.37 ?  26  GLU   A HA   1 
ATOM   749  H  HB2  A GLU   A 1 26  ? 15.940 -0.756  12.403  0.62 23.43 ?  26  GLU   A HB2  1 
ATOM   750  H  HB2  B GLU   A 1 26  ? 16.114 -1.152  12.389  0.38 23.43 ?  26  GLU   A HB2  1 
ATOM   751  H  HB3  A GLU   A 1 26  ? 16.357 -1.874  13.443  0.62 23.43 ?  26  GLU   A HB3  1 
ATOM   752  H  HB3  B GLU   A 1 26  ? 16.131 -2.236  13.549  0.38 23.43 ?  26  GLU   A HB3  1 
ATOM   753  H  HG2  A GLU   A 1 26  ? 13.703 -1.092  12.998  0.62 26.93 ?  26  GLU   A HG2  1 
ATOM   754  H  HG2  B GLU   A 1 26  ? 13.806 -0.913  12.699  0.38 25.16 ?  26  GLU   A HG2  1 
ATOM   755  H  HG3  A GLU   A 1 26  ? 14.352 -2.389  12.351  0.62 26.93 ?  26  GLU   A HG3  1 
ATOM   756  H  HG3  B GLU   A 1 26  ? 14.197 -2.388  12.253  0.38 25.16 ?  26  GLU   A HG3  1 
ATOM   757  N  N    . ALA   A 1 27  ? 18.257 0.337   14.115  1.00 16.13 ?  27  ALA   A N    1 
ATOM   758  C  CA   . ALA   A 1 27  ? 19.644 0.339   14.566  1.00 16.54 ?  27  ALA   A CA   1 
ATOM   759  C  C    . ALA   A 1 27  ? 19.808 1.158   15.841  1.00 18.75 ?  27  ALA   A C    1 
ATOM   760  O  O    . ALA   A 1 27  ? 20.484 0.726   16.781  1.00 18.58 ?  27  ALA   A O    1 
ATOM   761  C  CB   . ALA   A 1 27  ? 20.568 0.849   13.455  1.00 15.92 ?  27  ALA   A CB   1 
ATOM   762  H  H    A ALA   A 1 27  ? 18.135 0.664   13.326  0.62 19.37 ?  27  ALA   A H    1 
ATOM   763  H  H    B ALA   A 1 27  ? 18.104 0.802   13.403  0.38 19.37 ?  27  ALA   A H    1 
ATOM   764  H  HA   . ALA   A 1 27  ? 19.903 -0.569  14.764  1.00 19.87 ?  27  ALA   A HA   1 
ATOM   765  H  HB1  . ALA   A 1 27  ? 21.486 0.839   13.774  1.00 19.13 ?  27  ALA   A HB1  1 
ATOM   766  H  HB2  . ALA   A 1 27  ? 20.485 0.268   12.679  1.00 19.13 ?  27  ALA   A HB2  1 
ATOM   767  H  HB3  . ALA   A 1 27  ? 20.314 1.755   13.214  1.00 19.13 ?  27  ALA   A HB3  1 
ATOM   768  N  N    A LYS   A 1 28  ? 19.182 2.335   15.911  0.62 21.02 ?  28  LYS   A N    1 
ATOM   769  N  N    B LYS   A 1 28  ? 19.191 2.343   15.893  0.38 20.92 ?  28  LYS   A N    1 
ATOM   770  C  CA   A LYS   A 1 28  ? 19.339 3.159   17.106  0.62 24.01 ?  28  LYS   A CA   1 
ATOM   771  C  CA   B LYS   A 1 28  ? 19.296 3.183   17.082  0.38 23.54 ?  28  LYS   A CA   1 
ATOM   772  C  C    A LYS   A 1 28  ? 18.772 2.482   18.347  0.62 25.18 ?  28  LYS   A C    1 
ATOM   773  C  C    B LYS   A 1 28  ? 18.705 2.490   18.304  0.38 24.58 ?  28  LYS   A C    1 
ATOM   774  O  O    A LYS   A 1 28  ? 19.230 2.755   19.462  0.62 26.40 ?  28  LYS   A O    1 
ATOM   775  O  O    B LYS   A 1 28  ? 19.251 2.593   19.408  0.38 25.32 ?  28  LYS   A O    1 
ATOM   776  C  CB   A LYS   A 1 28  ? 18.721 4.542   16.897  0.62 26.87 ?  28  LYS   A CB   1 
ATOM   777  C  CB   B LYS   A 1 28  ? 18.619 4.534   16.837  0.38 25.70 ?  28  LYS   A CB   1 
ATOM   778  C  CG   A LYS   A 1 28  ? 19.592 5.446   16.046  0.62 29.20 ?  28  LYS   A CG   1 
ATOM   779  C  CG   B LYS   A 1 28  ? 19.393 5.442   15.896  0.38 27.54 ?  28  LYS   A CG   1 
ATOM   780  C  CD   A LYS   A 1 28  ? 19.128 6.886   16.077  0.62 31.85 ?  28  LYS   A CD   1 
ATOM   781  C  CD   B LYS   A 1 28  ? 18.901 6.881   15.949  0.38 29.77 ?  28  LYS   A CD   1 
ATOM   782  C  CE   A LYS   A 1 28  ? 17.815 7.051   15.347  0.62 33.48 ?  28  LYS   A CE   1 
ATOM   783  C  CE   B LYS   A 1 28  ? 17.688 7.097   15.064  0.38 31.26 ?  28  LYS   A CE   1 
ATOM   784  N  NZ   A LYS   A 1 28  ? 17.452 8.486   15.213  0.62 34.69 ?  28  LYS   A NZ   1 
ATOM   785  N  NZ   B LYS   A 1 28  ? 17.394 8.548   14.886  0.38 32.27 ?  28  LYS   A NZ   1 
ATOM   786  H  H    A LYS   A 1 28  ? 18.684 2.672   15.298  0.62 25.24 ?  28  LYS   A H    1 
ATOM   787  H  H    B LYS   A 1 28  ? 18.718 2.678   15.260  0.38 25.12 ?  28  LYS   A H    1 
ATOM   788  H  HA   A LYS   A 1 28  ? 20.285 3.291   17.264  0.62 28.83 ?  28  LYS   A HA   1 
ATOM   789  H  HA   B LYS   A 1 28  ? 20.230 3.352   17.270  0.38 28.26 ?  28  LYS   A HA   1 
ATOM   790  H  HB2  A LYS   A 1 28  ? 17.866 4.445   16.453  0.62 32.27 ?  28  LYS   A HB2  1 
ATOM   791  H  HB2  B LYS   A 1 28  ? 17.746 4.386   16.445  0.38 30.86 ?  28  LYS   A HB2  1 
ATOM   792  H  HB3  A LYS   A 1 28  ? 18.601 4.970   17.761  0.62 32.27 ?  28  LYS   A HB3  1 
ATOM   793  H  HB3  B LYS   A 1 28  ? 18.527 5.000   17.682  0.38 30.86 ?  28  LYS   A HB3  1 
ATOM   794  H  HG2  A LYS   A 1 28  ? 20.503 5.416   16.380  0.62 35.06 ?  28  LYS   A HG2  1 
ATOM   795  H  HG2  B LYS   A 1 28  ? 20.329 5.436   16.147  0.38 33.07 ?  28  LYS   A HG2  1 
ATOM   796  H  HG3  A LYS   A 1 28  ? 19.563 5.139   15.127  0.62 35.06 ?  28  LYS   A HG3  1 
ATOM   797  H  HG3  B LYS   A 1 28  ? 19.288 5.122   14.987  0.38 33.07 ?  28  LYS   A HG3  1 
ATOM   798  H  HD2  A LYS   A 1 28  ? 19.003 7.165   16.998  0.62 38.25 ?  28  LYS   A HD2  1 
ATOM   799  H  HD2  B LYS   A 1 28  ? 18.654 7.103   16.861  0.38 35.75 ?  28  LYS   A HD2  1 
ATOM   800  H  HD3  A LYS   A 1 28  ? 19.791 7.446   15.643  0.62 38.25 ?  28  LYS   A HD3  1 
ATOM   801  H  HD3  B LYS   A 1 28  ? 19.608 7.471   15.643  0.38 35.75 ?  28  LYS   A HD3  1 
ATOM   802  H  HE2  A LYS   A 1 28  ? 17.893 6.669   14.458  0.62 40.20 ?  28  LYS   A HE2  1 
ATOM   803  H  HE2  B LYS   A 1 28  ? 17.856 6.712   14.190  0.38 37.53 ?  28  LYS   A HE2  1 
ATOM   804  H  HE3  A LYS   A 1 28  ? 17.113 6.602   15.845  0.62 40.20 ?  28  LYS   A HE3  1 
ATOM   805  H  HE3  B LYS   A 1 28  ? 16.914 6.678   15.473  0.38 37.53 ?  28  LYS   A HE3  1 
ATOM   806  H  HZ1  A LYS   A 1 28  ? 16.679 8.565   14.782  0.62 41.65 ?  28  LYS   A HZ1  1 
ATOM   807  H  HZ1  B LYS   A 1 28  ? 16.682 8.653   14.364  0.38 38.74 ?  28  LYS   A HZ1  1 
ATOM   808  H  HZ2  A LYS   A 1 28  ? 17.374 8.856   16.019  0.62 41.65 ?  28  LYS   A HZ2  1 
ATOM   809  H  HZ2  B LYS   A 1 28  ? 17.233 8.926   15.676  0.38 38.74 ?  28  LYS   A HZ2  1 
ATOM   810  H  HZ3  A LYS   A 1 28  ? 18.084 8.918   14.757  0.62 41.65 ?  28  LYS   A HZ3  1 
ATOM   811  H  HZ3  B LYS   A 1 28  ? 18.091 8.956   14.509  0.38 38.74 ?  28  LYS   A HZ3  1 
ATOM   812  N  N    A LYS   A 1 29  ? 17.792 1.591   18.180  0.62 25.56 ?  29  LYS   A N    1 
ATOM   813  N  N    B LYS   A 1 29  ? 17.598 1.769   18.124  0.38 25.09 ?  29  LYS   A N    1 
ATOM   814  C  CA   A LYS   A 1 29  ? 17.209 0.891   19.321  0.62 27.18 ?  29  LYS   A CA   1 
ATOM   815  C  CA   B LYS   A 1 29  ? 16.948 1.102   19.248  0.38 26.13 ?  29  LYS   A CA   1 
ATOM   816  C  C    A LYS   A 1 29  ? 18.039 -0.326  19.717  0.62 26.63 ?  29  LYS   A C    1 
ATOM   817  C  C    B LYS   A 1 29  ? 17.713 -0.144  19.673  0.38 24.83 ?  29  LYS   A C    1 
ATOM   818  O  O    A LYS   A 1 29  ? 18.378 -0.501  20.893  0.62 27.93 ?  29  LYS   A O    1 
ATOM   819  O  O    B LYS   A 1 29  ? 17.924 -0.375  20.869  0.38 25.07 ?  29  LYS   A O    1 
ATOM   820  C  CB   A LYS   A 1 29  ? 15.777 0.465   18.989  0.62 29.98 ?  29  LYS   A CB   1 
ATOM   821  C  CB   B LYS   A 1 29  ? 15.516 0.725   18.868  0.38 28.56 ?  29  LYS   A CB   1 
ATOM   822  C  CG   A LYS   A 1 29  ? 15.057 -0.260  20.121  0.62 33.27 ?  29  LYS   A CG   1 
ATOM   823  C  CG   B LYS   A 1 29  ? 14.727 0.060   19.987  0.38 31.17 ?  29  LYS   A CG   1 
ATOM   824  C  CD   A LYS   A 1 29  ? 14.723 0.688   21.261  0.62 36.19 ?  29  LYS   A CD   1 
ATOM   825  C  CD   B LYS   A 1 29  ? 14.506 1.015   21.146  0.38 33.39 ?  29  LYS   A CD   1 
ATOM   826  C  CE   A LYS   A 1 29  ? 13.859 0.011   22.313  0.62 38.12 ?  29  LYS   A CE   1 
ATOM   827  C  CE   B LYS   A 1 29  ? 13.628 0.391   22.216  0.38 34.93 ?  29  LYS   A CE   1 
ATOM   828  N  NZ   A LYS   A 1 29  ? 13.431 0.966   23.372  0.62 39.35 ?  29  LYS   A NZ   1 
ATOM   829  N  NZ   B LYS   A 1 29  ? 13.411 1.323   23.354  0.38 35.87 ?  29  LYS   A NZ   1 
ATOM   830  H  H    A LYS   A 1 29  ? 17.446 1.383   17.422  0.62 30.69 ?  29  LYS   A H    1 
ATOM   831  H  H    B LYS   A 1 29  ? 17.207 1.649   17.368  0.38 30.13 ?  29  LYS   A H    1 
ATOM   832  H  HA   A LYS   A 1 29  ? 17.175 1.490   20.081  0.62 32.64 ?  29  LYS   A HA   1 
ATOM   833  H  HA   B LYS   A 1 29  ? 16.916 1.709   20.003  0.38 31.37 ?  29  LYS   A HA   1 
ATOM   834  H  HB2  A LYS   A 1 29  ? 15.259 1.256   18.774  0.62 36.00 ?  29  LYS   A HB2  1 
ATOM   835  H  HB2  B LYS   A 1 29  ? 15.042 1.529   18.613  0.38 34.29 ?  29  LYS   A HB2  1 
ATOM   836  H  HB3  A LYS   A 1 29  ? 15.798 -0.132  18.226  0.62 36.00 ?  29  LYS   A HB3  1 
ATOM   837  H  HB3  B LYS   A 1 29  ? 15.545 0.107   18.122  0.38 34.29 ?  29  LYS   A HB3  1 
ATOM   838  H  HG2  A LYS   A 1 29  ? 14.227 -0.630  19.784  0.62 39.94 ?  29  LYS   A HG2  1 
ATOM   839  H  HG2  B LYS   A 1 29  ? 13.860 -0.210  19.647  0.38 37.42 ?  29  LYS   A HG2  1 
ATOM   840  H  HG3  A LYS   A 1 29  ? 15.620 -0.970  20.470  0.62 39.94 ?  29  LYS   A HG3  1 
ATOM   841  H  HG3  B LYS   A 1 29  ? 15.213 -0.714  20.316  0.38 37.42 ?  29  LYS   A HG3  1 
ATOM   842  H  HD2  A LYS   A 1 29  ? 15.544 0.983   21.686  0.62 43.45 ?  29  LYS   A HD2  1 
ATOM   843  H  HD2  B LYS   A 1 29  ? 15.361 1.237   21.547  0.38 40.09 ?  29  LYS   A HD2  1 
ATOM   844  H  HD3  A LYS   A 1 29  ? 14.235 1.450   20.910  0.62 43.45 ?  29  LYS   A HD3  1 
ATOM   845  H  HD3  B LYS   A 1 29  ? 14.068 1.817   20.820  0.38 40.09 ?  29  LYS   A HD3  1 
ATOM   846  H  HE2  A LYS   A 1 29  ? 13.063 -0.350  21.890  0.62 45.77 ?  29  LYS   A HE2  1 
ATOM   847  H  HE2  B LYS   A 1 29  ? 12.765 0.170   21.832  0.38 41.93 ?  29  LYS   A HE2  1 
ATOM   848  H  HE3  A LYS   A 1 29  ? 14.366 -0.702  22.734  0.62 45.77 ?  29  LYS   A HE3  1 
ATOM   849  H  HE3  B LYS   A 1 29  ? 14.059 -0.410  22.555  0.38 41.93 ?  29  LYS   A HE3  1 
ATOM   850  H  HZ1  A LYS   A 1 29  ? 12.926 0.547   23.974  0.62 47.24 ?  29  LYS   A HZ1  1 
ATOM   851  H  HZ1  B LYS   A 1 29  ? 12.895 0.937   23.968  0.38 43.06 ?  29  LYS   A HZ1  1 
ATOM   852  H  HZ2  A LYS   A 1 29  ? 14.144 1.308   23.779  0.62 47.24 ?  29  LYS   A HZ2  1 
ATOM   853  H  HZ2  B LYS   A 1 29  ? 14.191 1.537   23.725  0.38 43.06 ?  29  LYS   A HZ2  1 
ATOM   854  H  HZ3  A LYS   A 1 29  ? 12.958 1.628   23.011  0.62 47.24 ?  29  LYS   A HZ3  1 
ATOM   855  H  HZ3  B LYS   A 1 29  ? 13.013 2.066   23.067  0.38 43.06 ?  29  LYS   A HZ3  1 
ATOM   856  N  N    A VAL   A 1 30  ? 18.360 -1.185  18.748  0.62 24.84 ?  30  VAL   A N    1 
ATOM   857  N  N    B VAL   A 1 30  ? 18.115 -0.969  18.705  0.38 23.53 ?  30  VAL   A N    1 
ATOM   858  C  CA   A VAL   A 1 30  ? 19.011 -2.456  19.049  0.62 23.90 ?  30  VAL   A CA   1 
ATOM   859  C  CA   B VAL   A 1 30  ? 18.762 -2.235  19.027  0.38 22.66 ?  30  VAL   A CA   1 
ATOM   860  C  C    A VAL   A 1 30  ? 20.509 -2.283  19.279  0.62 22.44 ?  30  VAL   A C    1 
ATOM   861  C  C    B VAL   A 1 30  ? 20.255 -2.054  19.266  0.38 21.77 ?  30  VAL   A C    1 
ATOM   862  O  O    A VAL   A 1 30  ? 21.100 -2.993  20.098  0.62 22.87 ?  30  VAL   A O    1 
ATOM   863  O  O    B VAL   A 1 30  ? 20.840 -2.748  20.104  0.38 21.71 ?  30  VAL   A O    1 
ATOM   864  C  CB   A VAL   A 1 30  ? 18.731 -3.464  17.919  0.62 24.51 ?  30  VAL   A CB   1 
ATOM   865  C  CB   B VAL   A 1 30  ? 18.491 -3.260  17.911  0.38 22.64 ?  30  VAL   A CB   1 
ATOM   866  C  CG1  A VAL   A 1 30  ? 19.507 -4.761  18.138  0.62 25.11 ?  30  VAL   A CG1  1 
ATOM   867  C  CG1  B VAL   A 1 30  ? 19.238 -4.559  18.178  0.38 22.96 ?  30  VAL   A CG1  1 
ATOM   868  C  CG2  A VAL   A 1 30  ? 17.238 -3.744  17.808  0.62 25.31 ?  30  VAL   A CG2  1 
ATOM   869  C  CG2  B VAL   A 1 30  ? 16.997 -3.518  17.775  0.38 22.82 ?  30  VAL   A CG2  1 
ATOM   870  H  H    A VAL   A 1 30  ? 18.210 -1.057  17.912  0.62 29.83 ?  30  VAL   A H    1 
ATOM   871  H  H    B VAL   A 1 30  ? 18.018 -0.823  17.863  0.38 28.26 ?  30  VAL   A H    1 
ATOM   872  H  HA   A VAL   A 1 30  ? 18.623 -2.818  19.861  0.62 28.70 ?  30  VAL   A HA   1 
ATOM   873  H  HA   B VAL   A 1 30  ? 18.369 -2.584  19.841  0.38 27.21 ?  30  VAL   A HA   1 
ATOM   874  H  HB   A VAL   A 1 30  ? 19.028 -3.085  17.077  0.62 29.44 ?  30  VAL   A HB   1 
ATOM   875  H  HB   B VAL   A 1 30  ? 18.813 -2.903  17.068  0.38 27.18 ?  30  VAL   A HB   1 
ATOM   876  H  HG11 A VAL   A 1 30  ? 19.151 -5.446  17.549  0.62 30.15 ?  30  VAL   A HG11 1 
ATOM   877  H  HG11 B VAL   A 1 30  ? 18.874 -5.255  17.608  0.38 27.58 ?  30  VAL   A HG11 1 
ATOM   878  H  HG12 A VAL   A 1 30  ? 20.445 -4.612  17.938  0.62 30.15 ?  30  VAL   A HG12 1 
ATOM   879  H  HG12 B VAL   A 1 30  ? 20.180 -4.433  17.983  0.38 27.58 ?  30  VAL   A HG12 1 
ATOM   880  H  HG13 A VAL   A 1 30  ? 19.405 -5.039  19.062  0.62 30.15 ?  30  VAL   A HG13 1 
ATOM   881  H  HG13 B VAL   A 1 30  ? 19.121 -4.802  19.109  0.38 27.58 ?  30  VAL   A HG13 1 
ATOM   882  H  HG21 A VAL   A 1 30  ? 17.092 -4.409  17.118  0.62 30.39 ?  30  VAL   A HG21 1 
ATOM   883  H  HG21 B VAL   A 1 30  ? 16.856 -4.199  17.098  0.38 27.40 ?  30  VAL   A HG21 1 
ATOM   884  H  HG22 A VAL   A 1 30  ? 16.917 -4.074  18.661  0.62 30.39 ?  30  VAL   A HG22 1 
ATOM   885  H  HG22 B VAL   A 1 30  ? 16.653 -3.824  18.629  0.38 27.40 ?  30  VAL   A HG22 1 
ATOM   886  H  HG23 A VAL   A 1 30  ? 16.782 -2.921  17.577  0.62 30.39 ?  30  VAL   A HG23 1 
ATOM   887  H  HG23 B VAL   A 1 30  ? 16.558 -2.695  17.514  0.38 27.40 ?  30  VAL   A HG23 1 
ATOM   888  N  N    A LYS   A 1 31  ? 21.145 -1.355  18.574  0.62 21.09 ?  31  LYS   A N    1 
ATOM   889  N  N    B LYS   A 1 31  ? 20.890 -1.130  18.553  0.38 21.55 ?  31  LYS   A N    1 
ATOM   890  C  CA   A LYS   A 1 31  ? 22.599 -1.248  18.531  0.62 21.59 ?  31  LYS   A CA   1 
ATOM   891  C  CA   B LYS   A 1 31  ? 22.343 -1.015  18.517  0.38 22.06 ?  31  LYS   A CA   1 
ATOM   892  C  C    A LYS   A 1 31  ? 23.218 -2.609  18.201  0.62 19.20 ?  31  LYS   A C    1 
ATOM   893  C  C    B LYS   A 1 31  ? 22.973 -2.384  18.251  0.38 20.23 ?  31  LYS   A C    1 
ATOM   894  O  O    A LYS   A 1 31  ? 23.990 -3.158  18.995  0.62 20.18 ?  31  LYS   A O    1 
ATOM   895  O  O    B LYS   A 1 31  ? 23.726 -2.901  19.081  0.38 20.99 ?  31  LYS   A O    1 
ATOM   896  C  CB   A LYS   A 1 31  ? 23.173 -0.687  19.824  0.62 26.20 ?  31  LYS   A CB   1 
ATOM   897  C  CB   B LYS   A 1 31  ? 22.900 -0.397  19.792  0.38 25.12 ?  31  LYS   A CB   1 
ATOM   898  C  CG   A LYS   A 1 31  ? 22.482 0.569   20.319  0.62 31.02 ?  31  LYS   A CG   1 
ATOM   899  C  CG   B LYS   A 1 31  ? 22.231 0.901   20.189  0.38 28.64 ?  31  LYS   A CG   1 
ATOM   900  C  CD   A LYS   A 1 31  ? 23.488 1.614   20.778  0.62 34.73 ?  31  LYS   A CD   1 
ATOM   901  C  CD   B LYS   A 1 31  ? 23.229 1.865   20.799  0.38 31.46 ?  31  LYS   A CD   1 
ATOM   902  C  CE   A LYS   A 1 31  ? 22.831 2.664   21.661  0.62 37.04 ?  31  LYS   A CE   1 
ATOM   903  C  CE   B LYS   A 1 31  ? 22.536 2.909   21.653  0.38 33.36 ?  31  LYS   A CE   1 
ATOM   904  N  NZ   A LYS   A 1 31  ? 21.641 3.288   21.021  0.62 38.30 ?  31  LYS   A NZ   1 
ATOM   905  N  NZ   B LYS   A 1 31  ? 21.346 3.494   20.978  0.38 34.50 ?  31  LYS   A NZ   1 
ATOM   906  H  H    A LYS   A 1 31  ? 20.742 -0.765  18.101  0.62 25.32 ?  31  LYS   A H    1 
ATOM   907  H  H    B LYS   A 1 31  ? 20.489 -0.546  18.072  0.38 25.87 ?  31  LYS   A H    1 
ATOM   908  H  HA   A LYS   A 1 31  ? 22.832 -0.638  17.820  0.62 25.93 ?  31  LYS   A HA   1 
ATOM   909  H  HA   B LYS   A 1 31  ? 22.581 -0.433  17.785  0.38 26.49 ?  31  LYS   A HA   1 
ATOM   910  H  HB2  A LYS   A 1 31  ? 23.099 -1.363  20.512  0.62 31.46 ?  31  LYS   A HB2  1 
ATOM   911  H  HB2  B LYS   A 1 31  ? 22.776 -1.024  20.517  0.38 30.16 ?  31  LYS   A HB2  1 
ATOM   912  H  HB3  A LYS   A 1 31  ? 24.109 -0.471  19.676  0.62 31.46 ?  31  LYS   A HB3  1 
ATOM   913  H  HB3  B LYS   A 1 31  ? 23.849 -0.220  19.667  0.38 30.16 ?  31  LYS   A HB3  1 
ATOM   914  H  HG2  A LYS   A 1 31  ? 21.954 0.950   19.600  0.62 37.25 ?  31  LYS   A HG2  1 
ATOM   915  H  HG2  B LYS   A 1 31  ? 21.845 1.317   19.403  0.38 34.39 ?  31  LYS   A HG2  1 
ATOM   916  H  HG3  A LYS   A 1 31  ? 21.912 0.345   21.071  0.62 37.25 ?  31  LYS   A HG3  1 
ATOM   917  H  HG3  B LYS   A 1 31  ? 21.542 0.718   20.847  0.38 34.39 ?  31  LYS   A HG3  1 
ATOM   918  H  HD2  A LYS   A 1 31  ? 24.191 1.183   21.289  0.62 41.69 ?  31  LYS   A HD2  1 
ATOM   919  H  HD2  B LYS   A 1 31  ? 23.849 1.371   21.361  0.38 37.78 ?  31  LYS   A HD2  1 
ATOM   920  H  HD3  A LYS   A 1 31  ? 23.864 2.061   20.001  0.62 41.69 ?  31  LYS   A HD3  1 
ATOM   921  H  HD3  B LYS   A 1 31  ? 23.710 2.319   20.089  0.38 37.78 ?  31  LYS   A HD3  1 
ATOM   922  H  HE2  A LYS   A 1 31  ? 22.543 2.246   22.488  0.62 44.47 ?  31  LYS   A HE2  1 
ATOM   923  H  HE2  B LYS   A 1 31  ? 22.245 2.495   22.479  0.38 40.05 ?  31  LYS   A HE2  1 
ATOM   924  H  HE3  A LYS   A 1 31  ? 23.473 3.366   21.850  0.62 44.47 ?  31  LYS   A HE3  1 
ATOM   925  H  HE3  B LYS   A 1 31  ? 23.159 3.626   21.842  0.38 40.05 ?  31  LYS   A HE3  1 
ATOM   926  H  HZ1  A LYS   A 1 31  ? 21.303 3.916   21.554  0.62 45.98 ?  31  LYS   A HZ1  1 
ATOM   927  H  HZ1  B LYS   A 1 31  ? 21.016 4.159   21.468  0.38 41.42 ?  31  LYS   A HZ1  1 
ATOM   928  H  HZ2  A LYS   A 1 31  ? 21.871 3.660   20.246  0.62 45.98 ?  31  LYS   A HZ2  1 
ATOM   929  H  HZ2  B LYS   A 1 31  ? 21.575 3.809   20.178  0.38 41.42 ?  31  LYS   A HZ2  1 
ATOM   930  H  HZ3  A LYS   A 1 31  ? 21.017 2.671   20.871  0.62 45.98 ?  31  LYS   A HZ3  1 
ATOM   931  H  HZ3  B LYS   A 1 31  ? 20.717 2.872   20.874  0.38 41.42 ?  31  LYS   A HZ3  1 
ATOM   932  N  N    A PRO   A 1 32  ? 22.902 -3.173  17.039  0.62 17.32 ?  32  PRO   A N    1 
ATOM   933  N  N    B PRO   A 1 32  ? 22.688 -2.988  17.100  0.38 18.24 ?  32  PRO   A N    1 
ATOM   934  C  CA   A PRO   A 1 32  ? 23.379 -4.518  16.715  0.62 17.78 ?  32  PRO   A CA   1 
ATOM   935  C  CA   B PRO   A 1 32  ? 23.174 -4.343  16.834  0.38 17.60 ?  32  PRO   A CA   1 
ATOM   936  C  C    A PRO   A 1 32  ? 24.880 -4.541  16.500  0.62 17.62 ?  32  PRO   A C    1 
ATOM   937  C  C    B PRO   A 1 32  ? 24.681 -4.352  16.641  0.38 17.14 ?  32  PRO   A C    1 
ATOM   938  O  O    A PRO   A 1 32  ? 25.522 -3.521  16.239  0.62 16.84 ?  32  PRO   A O    1 
ATOM   939  O  O    B PRO   A 1 32  ? 25.340 -3.315  16.554  0.38 17.20 ?  32  PRO   A O    1 
ATOM   940  C  CB   A PRO   A 1 32  ? 22.654 -4.835  15.403  0.62 18.15 ?  32  PRO   A CB   1 
ATOM   941  C  CB   B PRO   A 1 32  ? 22.453 -4.712  15.536  0.38 17.75 ?  32  PRO   A CB   1 
ATOM   942  C  CG   A PRO   A 1 32  ? 22.471 -3.495  14.769  0.62 16.81 ?  32  PRO   A CG   1 
ATOM   943  C  CG   B PRO   A 1 32  ? 22.310 -3.406  14.831  0.38 17.23 ?  32  PRO   A CG   1 
ATOM   944  C  CD   A PRO   A 1 32  ? 22.170 -2.569  15.914  0.62 17.10 ?  32  PRO   A CD   1 
ATOM   945  C  CD   B PRO   A 1 32  ? 22.018 -2.408  15.923  0.38 17.61 ?  32  PRO   A CD   1 
ATOM   946  H  HA   A PRO   A 1 32  ? 23.121 -5.157  17.401  0.62 21.35 ?  32  PRO   A HA   1 
ATOM   947  H  HA   B PRO   A 1 32  ? 22.920 -4.955  17.542  0.38 21.14 ?  32  PRO   A HA   1 
ATOM   948  H  HB2  A PRO   A 1 32  ? 23.210 -5.413  14.850  0.62 21.80 ?  32  PRO   A HB2  1 
ATOM   949  H  HB2  B PRO   A 1 32  ? 22.991 -5.331  15.018  0.38 21.33 ?  32  PRO   A HB2  1 
ATOM   950  H  HB3  A PRO   A 1 32  ? 21.799 -5.257  15.587  0.62 21.80 ?  32  PRO   A HB3  1 
ATOM   951  H  HB3  B PRO   A 1 32  ? 21.581 -5.094  15.735  0.38 21.33 ?  32  PRO   A HB3  1 
ATOM   952  H  HG2  A PRO   A 1 32  ? 23.288 -3.239  14.315  0.62 20.19 ?  32  PRO   A HG2  1 
ATOM   953  H  HG2  B PRO   A 1 32  ? 23.141 -3.191  14.378  0.38 20.70 ?  32  PRO   A HG2  1 
ATOM   954  H  HG3  A PRO   A 1 32  ? 21.728 -3.535  14.144  0.62 20.19 ?  32  PRO   A HG3  1 
ATOM   955  H  HG3  B PRO   A 1 32  ? 21.576 -3.455  14.198  0.38 20.70 ?  32  PRO   A HG3  1 
ATOM   956  H  HD2  A PRO   A 1 32  ? 22.511 -1.684  15.716  0.62 20.54 ?  32  PRO   A HD2  1 
ATOM   957  H  HD2  B PRO   A 1 32  ? 22.403 -1.548  15.698  0.38 21.15 ?  32  PRO   A HD2  1 
ATOM   958  H  HD3  A PRO   A 1 32  ? 21.217 -2.557  16.088  0.62 20.54 ?  32  PRO   A HD3  1 
ATOM   959  H  HD3  B PRO   A 1 32  ? 21.062 -2.346  16.070  0.38 21.15 ?  32  PRO   A HD3  1 
ATOM   960  N  N    A THR   A 1 33  ? 25.437 -5.748  16.586  0.62 17.55 ?  33  THR   A N    1 
ATOM   961  N  N    B THR   A 1 33  ? 25.227 -5.566  16.569  0.38 16.88 ?  33  THR   A N    1 
ATOM   962  C  CA   A THR   A 1 33  ? 26.846 -5.924  16.263  0.62 17.89 ?  33  THR   A CA   1 
ATOM   963  C  CA   B THR   A 1 33  ? 26.652 -5.719  16.303  0.38 16.71 ?  33  THR   A CA   1 
ATOM   964  C  C    A THR   A 1 33  ? 27.138 -5.472  14.835  0.62 16.41 ?  33  THR   A C    1 
ATOM   965  C  C    B THR   A 1 33  ? 26.995 -5.275  14.885  0.38 15.67 ?  33  THR   A C    1 
ATOM   966  O  O    A THR   A 1 33  ? 28.196 -4.886  14.569  0.62 16.32 ?  33  THR   A O    1 
ATOM   967  O  O    B THR   A 1 33  ? 27.969 -4.545  14.668  0.38 15.40 ?  33  THR   A O    1 
ATOM   968  C  CB   A THR   A 1 33  ? 27.248 -7.385  16.471  0.62 19.85 ?  33  THR   A CB   1 
ATOM   969  C  CB   B THR   A 1 33  ? 27.062 -7.173  16.525  0.38 17.78 ?  33  THR   A CB   1 
ATOM   970  O  OG1  A THR   A 1 33  ? 26.977 -7.770  17.824  0.62 21.58 ?  33  THR   A OG1  1 
ATOM   971  O  OG1  B THR   A 1 33  ? 26.714 -7.563  17.858  0.38 18.85 ?  33  THR   A OG1  1 
ATOM   972  C  CG2  A THR   A 1 33  ? 28.725 -7.579  16.200  0.62 20.37 ?  33  THR   A CG2  1 
ATOM   973  C  CG2  B THR   A 1 33  ? 28.562 -7.343  16.322  0.38 18.21 ?  33  THR   A CG2  1 
ATOM   974  H  H    A THR   A 1 33  ? 25.026 -6.466  16.820  0.62 21.08 ?  33  THR   A H    1 
ATOM   975  H  H    B THR   A 1 33  ? 24.799 -6.305  16.677  0.38 20.27 ?  33  THR   A H    1 
ATOM   976  H  HA   A THR   A 1 33  ? 27.378 -5.380  16.866  0.62 21.49 ?  33  THR   A HA   1 
ATOM   977  H  HA   B THR   A 1 33  ? 27.151 -5.169  16.929  0.38 20.08 ?  33  THR   A HA   1 
ATOM   978  H  HB   A THR   A 1 33  ? 26.738 -7.950  15.868  0.62 23.84 ?  33  THR   A HB   1 
ATOM   979  H  HB   B THR   A 1 33  ? 26.595 -7.745  15.891  0.38 21.36 ?  33  THR   A HB   1 
ATOM   980  H  HG1  A THR   A 1 33  ? 27.403 -7.279  18.357  0.62 25.91 ?  33  THR   A HG1  1 
ATOM   981  H  HG1  B THR   A 1 33  ? 27.119 -7.080  18.415  0.38 22.64 ?  33  THR   A HG1  1 
ATOM   982  H  HG21 A THR   A 1 33  ? 28.999 -8.461  16.495  0.62 24.46 ?  33  THR   A HG21 1 
ATOM   983  H  HG21 B THR   A 1 33  ? 28.841 -8.221  16.627  0.38 21.88 ?  33  THR   A HG21 1 
ATOM   984  H  HG22 A THR   A 1 33  ? 28.903 -7.493  15.253  0.62 24.46 ?  33  THR   A HG22 1 
ATOM   985  H  HG22 B THR   A 1 33  ? 28.784 -7.252  15.382  0.38 21.88 ?  33  THR   A HG22 1 
ATOM   986  H  HG23 A THR   A 1 33  ? 29.238 -6.913  16.683  0.62 24.46 ?  33  THR   A HG23 1 
ATOM   987  H  HG23 B THR   A 1 33  ? 29.041 -6.668  16.828  0.38 21.88 ?  33  THR   A HG23 1 
ATOM   988  N  N    . VAL   A 1 34  ? 26.207 -5.717  13.909  1.00 15.13 ?  34  VAL   A N    1 
ATOM   989  C  CA   . VAL   A 1 34  ? 26.407 -5.393  12.499  1.00 13.79 ?  34  VAL   A CA   1 
ATOM   990  C  C    . VAL   A 1 34  ? 25.110 -4.844  11.926  1.00 13.09 ?  34  VAL   A C    1 
ATOM   991  O  O    . VAL   A 1 34  ? 24.073 -5.521  11.967  1.00 14.14 ?  34  VAL   A O    1 
ATOM   992  C  CB   . VAL   A 1 34  ? 26.864 -6.610  11.672  1.00 14.24 ?  34  VAL   A CB   1 
ATOM   993  C  CG1  . VAL   A 1 34  ? 27.032 -6.217  10.205  1.00 14.85 ?  34  VAL   A CG1  1 
ATOM   994  C  CG2  . VAL   A 1 34  ? 28.147 -7.211  12.225  1.00 15.62 ?  34  VAL   A CG2  1 
ATOM   995  H  H    A VAL   A 1 34  ? 25.440 -6.070  14.083  0.62 18.17 ?  34  VAL   A H    1 
ATOM   996  H  H    B VAL   A 1 34  ? 25.525 -6.224  14.049  0.38 18.17 ?  34  VAL   A H    1 
ATOM   997  H  HA   . VAL   A 1 34  ? 27.084 -4.701  12.424  1.00 16.57 ?  34  VAL   A HA   1 
ATOM   998  H  HB   . VAL   A 1 34  ? 26.175 -7.288  11.720  1.00 17.11 ?  34  VAL   A HB   1 
ATOM   999  H  HG11 . VAL   A 1 34  ? 27.535 -6.910  9.751   1.00 17.84 ?  34  VAL   A HG11 1 
ATOM   1000 H  HG12 . VAL   A 1 34  ? 26.157 -6.124  9.797   1.00 17.84 ?  34  VAL   A HG12 1 
ATOM   1001 H  HG13 . VAL   A 1 34  ? 27.512 -5.375  10.155  1.00 17.84 ?  34  VAL   A HG13 1 
ATOM   1002 H  HG21 . VAL   A 1 34  ? 28.424 -7.943  11.649  1.00 18.77 ?  34  VAL   A HG21 1 
ATOM   1003 H  HG22 . VAL   A 1 34  ? 28.835 -6.529  12.247  1.00 18.77 ?  34  VAL   A HG22 1 
ATOM   1004 H  HG23 . VAL   A 1 34  ? 27.980 -7.544  13.121  1.00 18.77 ?  34  VAL   A HG23 1 
ATOM   1005 N  N    . VAL   A 1 35  ? 25.175 -3.641  11.358  1.00 12.38 ?  35  VAL   A N    1 
ATOM   1006 C  CA   . VAL   A 1 35  ? 24.147 -3.130  10.461  1.00 12.28 ?  35  VAL   A CA   1 
ATOM   1007 C  C    . VAL   A 1 35  ? 24.708 -3.139  9.047   1.00 11.48 ?  35  VAL   A C    1 
ATOM   1008 O  O    . VAL   A 1 35  ? 25.857 -2.739  8.820   1.00 12.38 ?  35  VAL   A O    1 
ATOM   1009 C  CB   . VAL   A 1 35  ? 23.629 -1.728  10.857  1.00 12.78 ?  35  VAL   A CB   1 
ATOM   1010 C  CG1  . VAL   A 1 35  ? 24.699 -0.642  10.730  1.00 13.47 ?  35  VAL   A CG1  1 
ATOM   1011 C  CG2  . VAL   A 1 35  ? 22.392 -1.373  10.028  1.00 13.47 ?  35  VAL   A CG2  1 
ATOM   1012 H  H    . VAL   A 1 35  ? 25.823 -3.086  11.475  1.00 14.88 ?  35  VAL   A H    1 
ATOM   1013 H  HA   . VAL   A 1 35  ? 23.389 -3.735  10.477  1.00 14.75 ?  35  VAL   A HA   1 
ATOM   1014 H  HB   . VAL   A 1 35  ? 23.345 -1.755  11.781  1.00 15.36 ?  35  VAL   A HB   1 
ATOM   1015 H  HG11 . VAL   A 1 35  ? 24.351 0.188   11.092  1.00 16.18 ?  35  VAL   A HG11 1 
ATOM   1016 H  HG12 . VAL   A 1 35  ? 25.483 -0.919  11.224  1.00 16.18 ?  35  VAL   A HG12 1 
ATOM   1017 H  HG13 . VAL   A 1 35  ? 24.922 -0.524  9.791   1.00 16.18 ?  35  VAL   A HG13 1 
ATOM   1018 H  HG21 . VAL   A 1 35  ? 22.039 -0.524  10.329  1.00 16.19 ?  35  VAL   A HG21 1 
ATOM   1019 H  HG22 . VAL   A 1 35  ? 22.645 -1.309  9.089   1.00 16.19 ?  35  VAL   A HG22 1 
ATOM   1020 H  HG23 . VAL   A 1 35  ? 21.724 -2.069  10.138  1.00 16.19 ?  35  VAL   A HG23 1 
ATOM   1021 N  N    . VAL   A 1 36  ? 23.905 -3.601  8.097   1.00 10.99 ?  36  VAL   A N    1 
ATOM   1022 C  CA   . VAL   A 1 36  ? 24.287 -3.611  6.691   1.00 10.96 ?  36  VAL   A CA   1 
ATOM   1023 C  C    . VAL   A 1 36  ? 23.834 -2.320  6.026   1.00 10.99 ?  36  VAL   A C    1 
ATOM   1024 O  O    . VAL   A 1 36  ? 22.669 -1.918  6.154   1.00 11.70 ?  36  VAL   A O    1 
ATOM   1025 C  CB   . VAL   A 1 36  ? 23.687 -4.828  5.970   1.00 10.96 ?  36  VAL   A CB   1 
ATOM   1026 C  CG1  . VAL   A 1 36  ? 23.954 -4.771  4.490   1.00 11.55 ?  36  VAL   A CG1  1 
ATOM   1027 C  CG2  . VAL   A 1 36  ? 24.231 -6.116  6.558   1.00 11.93 ?  36  VAL   A CG2  1 
ATOM   1028 H  H    . VAL   A 1 36  ? 23.107 -3.913  8.236   1.00 13.21 ?  36  VAL   A H    1 
ATOM   1029 H  HA   . VAL   A 1 36  ? 25.253 -3.670  6.623   1.00 13.17 ?  36  VAL   A HA   1 
ATOM   1030 H  HB   . VAL   A 1 36  ? 22.725 -4.826  6.095   1.00 13.17 ?  36  VAL   A HB   1 
ATOM   1031 H  HG11 . VAL   A 1 36  ? 23.806 -5.650  4.107   1.00 13.88 ?  36  VAL   A HG11 1 
ATOM   1032 H  HG12 . VAL   A 1 36  ? 23.353 -4.129  4.080   1.00 13.88 ?  36  VAL   A HG12 1 
ATOM   1033 H  HG13 . VAL   A 1 36  ? 24.876 -4.502  4.345   1.00 13.88 ?  36  VAL   A HG13 1 
ATOM   1034 H  HG21 . VAL   A 1 36  ? 23.846 -6.876  6.085   1.00 14.34 ?  36  VAL   A HG21 1 
ATOM   1035 H  HG22 . VAL   A 1 36  ? 25.196 -6.131  6.470   1.00 14.34 ?  36  VAL   A HG22 1 
ATOM   1036 H  HG23 . VAL   A 1 36  ? 23.986 -6.168  7.500   1.00 14.34 ?  36  VAL   A HG23 1 
ATOM   1037 N  N    . ASN   A 1 37  ? 24.756 -1.691  5.292   1.00 10.35 ?  37  ASN   A N    1 
ATOM   1038 C  CA   . ASN   A 1 37  ? 24.435 -0.576  4.419   1.00 10.45 ?  37  ASN   A CA   1 
ATOM   1039 C  C    . ASN   A 1 37  ? 24.306 -1.052  2.983   1.00 10.13 ?  37  ASN   A C    1 
ATOM   1040 O  O    . ASN   A 1 37  ? 25.100 -1.876  2.510   1.00 10.88 ?  37  ASN   A O    1 
ATOM   1041 C  CB   . ASN   A 1 37  ? 25.512 0.504   4.502   1.00 10.92 ?  37  ASN   A CB   1 
ATOM   1042 C  CG   . ASN   A 1 37  ? 25.198 1.695   3.644   1.00 10.81 ?  37  ASN   A CG   1 
ATOM   1043 O  OD1  . ASN   A 1 37  ? 24.023 2.029   3.448   1.00 11.56 ?  37  ASN   A OD1  1 
ATOM   1044 N  ND2  . ASN   A 1 37  ? 26.230 2.350   3.125   1.00 11.28 ?  37  ASN   A ND2  1 
ATOM   1045 H  H    . ASN   A 1 37  ? 25.595 -1.893  5.300   1.00 12.44 ?  37  ASN   A H    1 
ATOM   1046 H  HA   . ASN   A 1 37  ? 23.595 -0.182  4.694   1.00 12.56 ?  37  ASN   A HA   1 
ATOM   1047 H  HB2  . ASN   A 1 37  ? 25.591 0.811   5.419   1.00 13.12 ?  37  ASN   A HB2  1 
ATOM   1048 H  HB3  . ASN   A 1 37  ? 26.361 0.136   4.203   1.00 13.12 ?  37  ASN   A HB3  1 
ATOM   1049 H  HD21 . ASN   A 1 37  ? 26.094 3.037   2.622   1.00 13.55 ?  37  ASN   A HD21 1 
ATOM   1050 H  HD22 . ASN   A 1 37  ? 27.026 2.090   3.280   1.00 13.55 ?  37  ASN   A HD22 1 
ATOM   1051 N  N    A ALA   A 1 38  ? 23.292 -0.508  2.298   0.62 10.67 ?  38  ALA   A N    1 
ATOM   1052 N  N    B ALA   A 1 38  ? 23.299 -0.535  2.277   0.38 10.68 ?  38  ALA   A N    1 
ATOM   1053 C  CA   A ALA   A 1 38  ? 23.112 -0.639  0.853   0.62 10.71 ?  38  ALA   A CA   1 
ATOM   1054 C  CA   B ALA   A 1 38  ? 23.159 -0.799  0.843   0.38 11.14 ?  38  ALA   A CA   1 
ATOM   1055 C  C    A ALA   A 1 38  ? 24.051 0.346   0.159   0.62 10.73 ?  38  ALA   A C    1 
ATOM   1056 C  C    B ALA   A 1 38  ? 23.969 0.246   0.075   0.38 10.91 ?  38  ALA   A C    1 
ATOM   1057 O  O    A ALA   A 1 38  ? 23.665 1.443   -0.254  0.62 10.62 ?  38  ALA   A O    1 
ATOM   1058 O  O    B ALA   A 1 38  ? 23.460 1.271   -0.386  0.38 11.08 ?  38  ALA   A O    1 
ATOM   1059 C  CB   A ALA   A 1 38  ? 21.661 -0.366  0.477   0.62 11.37 ?  38  ALA   A CB   1 
ATOM   1060 C  CB   B ALA   A 1 38  ? 21.692 -0.800  0.437   0.38 11.94 ?  38  ALA   A CB   1 
ATOM   1061 H  H    A ALA   A 1 38  ? 22.682 -0.023  2.666   0.62 12.82 ?  38  ALA   A H    1 
ATOM   1062 H  H    B ALA   A 1 38  ? 22.682 -0.029  2.608   0.38 12.84 ?  38  ALA   A H    1 
ATOM   1063 H  HA   A ALA   A 1 38  ? 23.343 -1.535  0.575   0.62 12.87 ?  38  ALA   A HA   1 
ATOM   1064 H  HA   B ALA   A 1 38  ? 23.529 -1.678  0.648   0.38 13.38 ?  38  ALA   A HA   1 
ATOM   1065 H  HB1  A ALA   A 1 38  ? 21.559 -0.463  -0.485  0.62 13.66 ?  38  ALA   A HB1  1 
ATOM   1066 H  HB1  B ALA   A 1 38  ? 21.640 -0.899  -0.526  0.38 14.35 ?  38  ALA   A HB1  1 
ATOM   1067 H  HB2  A ALA   A 1 38  ? 21.093 -1.005  0.934   0.62 13.66 ?  38  ALA   A HB2  1 
ATOM   1068 H  HB2  B ALA   A 1 38  ? 21.238 -1.539  0.872   0.38 14.35 ?  38  ALA   A HB2  1 
ATOM   1069 H  HB3  A ALA   A 1 38  ? 21.427 0.537   0.743   0.62 13.66 ?  38  ALA   A HB3  1 
ATOM   1070 H  HB3  B ALA   A 1 38  ? 21.293 0.041   0.702   0.38 14.35 ?  38  ALA   A HB3  1 
ATOM   1071 N  N    A ALA   A 1 39  ? 25.315 -0.052  0.048   0.62 11.05 ?  39  ALA   A N    1 
ATOM   1072 N  N    B ALA   A 1 39  ? 25.262 -0.035  -0.070  0.38 11.07 ?  39  ALA   A N    1 
ATOM   1073 C  CA   A ALA   A 1 39  ? 26.375 0.807   -0.447  0.62 10.43 ?  39  ALA   A CA   1 
ATOM   1074 C  CA   B ALA   A 1 39  ? 26.223 0.933   -0.567  0.38 11.23 ?  39  ALA   A CA   1 
ATOM   1075 C  C    A ALA   A 1 39  ? 26.471 0.758   -1.968  0.62 10.61 ?  39  ALA   A C    1 
ATOM   1076 C  C    B ALA   A 1 39  ? 26.426 0.793   -2.071  0.38 11.33 ?  39  ALA   A C    1 
ATOM   1077 O  O    A ALA   A 1 39  ? 25.969 -0.161  -2.628  0.62 11.11 ?  39  ALA   A O    1 
ATOM   1078 O  O    B ALA   A 1 39  ? 26.033 -0.194  -2.702  0.38 11.24 ?  39  ALA   A O    1 
ATOM   1079 C  CB   A ALA   A 1 39  ? 27.706 0.382   0.173   0.62 11.04 ?  39  ALA   A CB   1 
ATOM   1080 C  CB   B ALA   A 1 39  ? 27.562 0.754   0.151   0.38 11.91 ?  39  ALA   A CB   1 
ATOM   1081 H  H    A ALA   A 1 39  ? 25.589 -0.841  0.272   0.62 13.28 ?  39  ALA   A H    1 
ATOM   1082 H  H    B ALA   A 1 39  ? 25.605 -0.802  0.118   0.38 13.31 ?  39  ALA   A H    1 
ATOM   1083 H  HA   A ALA   A 1 39  ? 26.195 1.723   -0.180  0.62 12.54 ?  39  ALA   A HA   1 
ATOM   1084 H  HA   B ALA   A 1 39  ? 25.896 1.828   -0.378  0.38 13.50 ?  39  ALA   A HA   1 
ATOM   1085 H  HB1  A ALA   A 1 39  ? 28.410 0.964   -0.161  0.62 13.27 ?  39  ALA   A HB1  1 
ATOM   1086 H  HB1  B ALA   A 1 39  ? 28.192 1.407   -0.195  0.38 14.31 ?  39  ALA   A HB1  1 
ATOM   1087 H  HB2  A ALA   A 1 39  ? 27.648 0.465   1.141   0.62 13.27 ?  39  ALA   A HB2  1 
ATOM   1088 H  HB2  B ALA   A 1 39  ? 27.436 0.891   1.104   0.38 14.31 ?  39  ALA   A HB2  1 
ATOM   1089 H  HB3  A ALA   A 1 39  ? 27.893 -0.535  -0.069  0.62 13.27 ?  39  ALA   A HB3  1 
ATOM   1090 H  HB3  B ALA   A 1 39  ? 27.892 -0.143  -0.013  0.38 14.31 ?  39  ALA   A HB3  1 
ATOM   1091 N  N    A ASN   A 1 40  ? 27.145 1.767   -2.520  0.62 10.92 ?  40  ASN   A N    1 
ATOM   1092 N  N    B ASN   A 1 40  ? 27.057 1.812   -2.642  0.38 11.58 ?  40  ASN   A N    1 
ATOM   1093 C  CA   A ASN   A 1 40  ? 27.663 1.723   -3.881  0.62 11.43 ?  40  ASN   A CA   1 
ATOM   1094 C  CA   B ASN   A 1 40  ? 27.637 1.729   -3.972  0.38 11.78 ?  40  ASN   A CA   1 
ATOM   1095 C  C    A ASN   A 1 40  ? 29.188 1.612   -3.839  0.62 11.12 ?  40  ASN   A C    1 
ATOM   1096 C  C    B ASN   A 1 40  ? 29.155 1.594   -3.857  0.38 11.38 ?  40  ASN   A C    1 
ATOM   1097 O  O    A ASN   A 1 40  ? 29.805 1.725   -2.779  0.62 11.34 ?  40  ASN   A O    1 
ATOM   1098 O  O    B ASN   A 1 40  ? 29.734 1.689   -2.773  0.38 11.42 ?  40  ASN   A O    1 
ATOM   1099 C  CB   A ASN   A 1 40  ? 27.169 2.906   -4.732  0.62 12.37 ?  40  ASN   A CB   1 
ATOM   1100 C  CB   B ASN   A 1 40  ? 27.238 2.931   -4.838  0.38 12.19 ?  40  ASN   A CB   1 
ATOM   1101 C  CG   A ASN   A 1 40  ? 27.562 4.256   -4.167  0.62 13.07 ?  40  ASN   A CG   1 
ATOM   1102 C  CG   B ASN   A 1 40  ? 27.569 4.259   -4.191  0.38 12.55 ?  40  ASN   A CG   1 
ATOM   1103 O  OD1  A ASN   A 1 40  ? 28.730 4.499   -3.857  0.62 13.74 ?  40  ASN   A OD1  1 
ATOM   1104 O  OD1  B ASN   A 1 40  ? 28.736 4.574   -3.959  0.38 12.49 ?  40  ASN   A OD1  1 
ATOM   1105 N  ND2  A ASN   A 1 40  ? 26.578 5.146   -4.034  0.62 13.98 ?  40  ASN   A ND2  1 
ATOM   1106 N  ND2  B ASN   A 1 40  ? 26.538 5.052   -3.909  0.38 13.51 ?  40  ASN   A ND2  1 
ATOM   1107 H  H    A ASN   A 1 40  ? 27.323 2.505   -2.115  0.62 13.12 ?  40  ASN   A H    1 
ATOM   1108 H  H    B ASN   A 1 40  ? 27.167 2.573   -2.264  0.38 13.92 ?  40  ASN   A H    1 
ATOM   1109 H  HA   A ASN   A 1 40  ? 27.330 0.911   -4.300  0.62 13.73 ?  40  ASN   A HA   1 
ATOM   1110 H  HA   B ASN   A 1 40  ? 27.297 0.925   -4.406  0.38 14.15 ?  40  ASN   A HA   1 
ATOM   1111 H  HB2  A ASN   A 1 40  ? 27.548 2.826   -5.625  0.62 14.86 ?  40  ASN   A HB2  1 
ATOM   1112 H  HB2  B ASN   A 1 40  ? 27.714 2.878   -5.679  0.38 14.65 ?  40  ASN   A HB2  1 
ATOM   1113 H  HB3  A ASN   A 1 40  ? 26.202 2.870   -4.784  0.62 14.86 ?  40  ASN   A HB3  1 
ATOM   1114 H  HB3  B ASN   A 1 40  ? 26.281 2.900   -4.994  0.38 14.65 ?  40  ASN   A HB3  1 
ATOM   1115 H  HD21 A ASN   A 1 40  ? 26.744 5.929   -3.722  0.62 16.79 ?  40  ASN   A HD21 1 
ATOM   1116 H  HD21 B ASN   A 1 40  ? 26.674 5.817   -3.542  0.38 16.24 ?  40  ASN   A HD21 1 
ATOM   1117 H  HD22 A ASN   A 1 40  ? 25.773 4.931   -4.251  0.62 16.79 ?  40  ASN   A HD22 1 
ATOM   1118 H  HD22 B ASN   A 1 40  ? 25.736 4.800   -4.093  0.38 16.24 ?  40  ASN   A HD22 1 
ATOM   1119 N  N    . VAL   A 1 41  ? 29.796 1.347   -5.000  1.00 11.42 ?  41  VAL   A N    1 
ATOM   1120 C  CA   . VAL   A 1 41  ? 31.228 1.037   -5.022  1.00 12.26 ?  41  VAL   A CA   1 
ATOM   1121 C  C    . VAL   A 1 41  ? 32.089 2.184   -4.536  1.00 11.99 ?  41  VAL   A C    1 
ATOM   1122 O  O    . VAL   A 1 41  ? 33.232 1.963   -4.126  1.00 12.66 ?  41  VAL   A O    1 
ATOM   1123 C  CB   . VAL   A 1 41  ? 31.720 0.561   -6.407  1.00 13.40 ?  41  VAL   A CB   1 
ATOM   1124 C  CG1  . VAL   A 1 41  ? 31.040 -0.736  -6.820  1.00 14.34 ?  41  VAL   A CG1  1 
ATOM   1125 C  CG2  . VAL   A 1 41  ? 31.559 1.641   -7.469  1.00 14.20 ?  41  VAL   A CG2  1 
ATOM   1126 H  H    A VAL   A 1 41  ? 29.409 1.326   -5.766  0.62 13.72 ?  41  VAL   A H    1 
ATOM   1127 H  H    B VAL   A 1 41  ? 29.422 1.333   -5.773  0.38 13.72 ?  41  VAL   A H    1 
ATOM   1128 H  HA   . VAL   A 1 41  ? 31.383 0.296   -4.410  1.00 14.73 ?  41  VAL   A HA   1 
ATOM   1129 H  HB   . VAL   A 1 41  ? 32.669 0.367   -6.342  1.00 16.10 ?  41  VAL   A HB   1 
ATOM   1130 H  HG11 . VAL   A 1 41  ? 31.381 -1.012  -7.690  1.00 17.23 ?  41  VAL   A HG11 1 
ATOM   1131 H  HG12 . VAL   A 1 41  ? 31.233 -1.421  -6.162  1.00 17.23 ?  41  VAL   A HG12 1 
ATOM   1132 H  HG13 . VAL   A 1 41  ? 30.083 -0.590  -6.877  1.00 17.23 ?  41  VAL   A HG13 1 
ATOM   1133 H  HG21 . VAL   A 1 41  ? 31.792 1.270   -8.338  1.00 17.06 ?  41  VAL   A HG21 1 
ATOM   1134 H  HG22 . VAL   A 1 41  ? 30.643 1.948   -7.476  1.00 17.06 ?  41  VAL   A HG22 1 
ATOM   1135 H  HG23 . VAL   A 1 41  ? 32.156 2.380   -7.262  1.00 17.06 ?  41  VAL   A HG23 1 
ATOM   1136 N  N    . TYR   A 1 42  ? 31.583 3.413   -4.599  1.00 11.74 ?  42  TYR   A N    1 
ATOM   1137 C  CA   . TYR   A 1 42  ? 32.324 4.602   -4.195  1.00 11.86 ?  42  TYR   A CA   1 
ATOM   1138 C  C    . TYR   A 1 42  ? 32.071 4.976   -2.747  1.00 11.34 ?  42  TYR   A C    1 
ATOM   1139 O  O    . TYR   A 1 42  ? 32.626 5.975   -2.269  1.00 12.20 ?  42  TYR   A O    1 
ATOM   1140 C  CB   . TYR   A 1 42  ? 31.967 5.788   -5.109  1.00 12.52 ?  42  TYR   A CB   1 
ATOM   1141 C  CG   . TYR   A 1 42  ? 32.149 5.474   -6.577  1.00 13.16 ?  42  TYR   A CG   1 
ATOM   1142 C  CD1  . TYR   A 1 42  ? 33.412 5.283   -7.112  1.00 13.84 ?  42  TYR   A CD1  1 
ATOM   1143 C  CD2  . TYR   A 1 42  ? 31.058 5.338   -7.423  1.00 14.82 ?  42  TYR   A CD2  1 
ATOM   1144 C  CE1  . TYR   A 1 42  ? 33.580 4.971   -8.450  1.00 14.76 ?  42  TYR   A CE1  1 
ATOM   1145 C  CE2  . TYR   A 1 42  ? 31.223 5.048   -8.765  1.00 16.06 ?  42  TYR   A CE2  1 
ATOM   1146 C  CZ   . TYR   A 1 42  ? 32.487 4.855   -9.272  1.00 15.46 ?  42  TYR   A CZ   1 
ATOM   1147 O  OH   . TYR   A 1 42  ? 32.653 4.558   -10.600 1.00 17.03 ?  42  TYR   A OH   1 
ATOM   1148 H  H    . TYR   A 1 42  ? 30.790 3.585   -4.885  1.00 14.11 ?  42  TYR   A H    1 
ATOM   1149 H  HA   . TYR   A 1 42  ? 33.272 4.433   -4.293  1.00 14.25 ?  42  TYR   A HA   1 
ATOM   1150 H  HB2  . TYR   A 1 42  ? 31.034 6.026   -4.969  1.00 15.05 ?  42  TYR   A HB2  1 
ATOM   1151 H  HB3  . TYR   A 1 42  ? 32.536 6.540   -4.891  1.00 15.05 ?  42  TYR   A HB3  1 
ATOM   1152 H  HD1  . TYR   A 1 42  ? 34.160 5.354   -6.560  1.00 16.63 ?  42  TYR   A HD1  1 
ATOM   1153 H  HD2  . TYR   A 1 42  ? 30.202 5.468   -7.082  1.00 17.81 ?  42  TYR   A HD2  1 
ATOM   1154 H  HE1  . TYR   A 1 42  ? 34.435 4.848   -8.797  1.00 17.73 ?  42  TYR   A HE1  1 
ATOM   1155 H  HE2  . TYR   A 1 42  ? 30.480 4.964   -9.318  1.00 19.30 ?  42  TYR   A HE2  1 
ATOM   1156 H  HH   . TYR   A 1 42  ? 33.476 4.465   -10.770 1.00 20.45 ?  42  TYR   A HH   1 
ATOM   1157 N  N    . LEU   A 1 43  ? 31.212 4.227   -2.060  1.00 10.95 ?  43  LEU   A N    1 
ATOM   1158 C  CA   . LEU   A 1 43  ? 30.763 4.570   -0.712  1.00 10.75 ?  43  LEU   A CA   1 
ATOM   1159 C  C    . LEU   A 1 43  ? 30.278 6.017   -0.622  1.00 11.33 ?  43  LEU   A C    1 
ATOM   1160 O  O    . LEU   A 1 43  ? 30.527 6.718   0.362   1.00 12.32 ?  43  LEU   A O    1 
ATOM   1161 C  CB   . LEU   A 1 43  ? 31.803 4.262   0.362   1.00 11.68 ?  43  LEU   A CB   1 
ATOM   1162 C  CG   . LEU   A 1 43  ? 32.298 2.813   0.453   1.00 11.93 ?  43  LEU   A CG   1 
ATOM   1163 C  CD1  . LEU   A 1 43  ? 33.338 2.706   1.563   1.00 12.83 ?  43  LEU   A CD1  1 
ATOM   1164 C  CD2  . LEU   A 1 43  ? 31.154 1.831   0.671   1.00 12.19 ?  43  LEU   A CD2  1 
ATOM   1165 H  H    . LEU   A 1 43  ? 30.864 3.491   -2.354  1.00 13.16 ?  43  LEU   A H    1 
ATOM   1166 H  HA   . LEU   A 1 43  ? 29.990 4.013   -0.508  1.00 12.92 ?  43  LEU   A HA   1 
ATOM   1167 H  HB2  . LEU   A 1 43  ? 32.575 4.825   0.210   1.00 14.03 ?  43  LEU   A HB2  1 
ATOM   1168 H  HB3  . LEU   A 1 43  ? 31.416 4.481   1.231   1.00 14.03 ?  43  LEU   A HB3  1 
ATOM   1169 H  HG   . LEU   A 1 43  ? 32.734 2.583   -0.384  1.00 14.34 ?  43  LEU   A HG   1 
ATOM   1170 H  HD11 . LEU   A 1 43  ? 33.653 1.791   1.615   1.00 15.42 ?  43  LEU   A HD11 1 
ATOM   1171 H  HD12 . LEU   A 1 43  ? 34.079 3.300   1.362   1.00 15.42 ?  43  LEU   A HD12 1 
ATOM   1172 H  HD13 . LEU   A 1 43  ? 32.929 2.964   2.405   1.00 15.42 ?  43  LEU   A HD13 1 
ATOM   1173 H  HD21 . LEU   A 1 43  ? 31.525 0.949   0.818   1.00 14.65 ?  43  LEU   A HD21 1 
ATOM   1174 H  HD22 . LEU   A 1 43  ? 30.644 2.114   1.443   1.00 14.65 ?  43  LEU   A HD22 1 
ATOM   1175 H  HD23 . LEU   A 1 43  ? 30.591 1.829   -0.119  1.00 14.65 ?  43  LEU   A HD23 1 
ATOM   1176 N  N    A LYS   A 1 44  ? 29.570 6.456   -1.663  0.62 11.14 ?  44  LYS   A N    1 
ATOM   1177 N  N    B LYS   A 1 44  ? 29.539 6.453   -1.641  0.38 12.06 ?  44  LYS   A N    1 
ATOM   1178 C  CA   A LYS   A 1 44  ? 28.930 7.771   -1.685  0.62 11.35 ?  44  LYS   A CA   1 
ATOM   1179 C  CA   B LYS   A 1 44  ? 28.892 7.764   -1.631  0.38 13.09 ?  44  LYS   A CA   1 
ATOM   1180 C  C    A LYS   A 1 44  ? 27.499 7.591   -1.203  0.62 10.34 ?  44  LYS   A C    1 
ATOM   1181 C  C    B LYS   A 1 44  ? 27.470 7.581   -1.115  0.38 12.12 ?  44  LYS   A C    1 
ATOM   1182 O  O    A LYS   A 1 44  ? 26.644 7.074   -1.928  0.62 11.78 ?  44  LYS   A O    1 
ATOM   1183 O  O    B LYS   A 1 44  ? 26.599 7.065   -1.820  0.38 12.58 ?  44  LYS   A O    1 
ATOM   1184 C  CB   A LYS   A 1 44  ? 28.988 8.373   -3.081  0.62 13.55 ?  44  LYS   A CB   1 
ATOM   1185 C  CB   B LYS   A 1 44  ? 28.937 8.394   -3.019  0.38 15.45 ?  44  LYS   A CB   1 
ATOM   1186 C  CG   A LYS   A 1 44  ? 30.371 8.834   -3.503  0.62 16.86 ?  44  LYS   A CG   1 
ATOM   1187 C  CG   B LYS   A 1 44  ? 30.307 8.938   -3.411  0.38 18.09 ?  44  LYS   A CG   1 
ATOM   1188 C  CD   A LYS   A 1 44  ? 31.006 9.785   -2.493  0.62 21.80 ?  44  LYS   A CD   1 
ATOM   1189 C  CD   B LYS   A 1 44  ? 30.873 9.879   -2.347  0.38 21.52 ?  44  LYS   A CD   1 
ATOM   1190 C  CE   A LYS   A 1 44  ? 32.337 10.312  -2.993  0.62 25.10 ?  44  LYS   A CE   1 
ATOM   1191 C  CE   B LYS   A 1 44  ? 32.226 10.428  -2.745  0.38 23.83 ?  44  LYS   A CE   1 
ATOM   1192 N  NZ   A LYS   A 1 44  ? 33.113 10.968  -1.909  0.62 26.94 ?  44  LYS   A NZ   1 
ATOM   1193 N  NZ   B LYS   A 1 44  ? 32.992 10.910  -1.563  0.38 25.09 ?  44  LYS   A NZ   1 
ATOM   1194 H  H    A LYS   A 1 44  ? 29.445 5.999   -2.383  0.62 13.39 ?  44  LYS   A H    1 
ATOM   1195 H  H    B LYS   A 1 44  ? 29.396 6.003   -2.359  0.38 14.49 ?  44  LYS   A H    1 
ATOM   1196 H  HA   A LYS   A 1 44  ? 29.377 8.357   -1.056  0.62 13.65 ?  44  LYS   A HA   1 
ATOM   1197 H  HA   B LYS   A 1 44  ? 29.347 8.340   -1.000  0.38 15.73 ?  44  LYS   A HA   1 
ATOM   1198 H  HB2  A LYS   A 1 44  ? 28.689 7.710   -3.721  0.62 16.28 ?  44  LYS   A HB2  1 
ATOM   1199 H  HB2  B LYS   A 1 44  ? 28.690 7.726   -3.680  0.38 18.56 ?  44  LYS   A HB2  1 
ATOM   1200 H  HB3  A LYS   A 1 44  ? 28.399 9.145   -3.110  0.62 16.28 ?  44  LYS   A HB3  1 
ATOM   1201 H  HB3  B LYS   A 1 44  ? 28.312 9.135   -3.054  0.38 18.56 ?  44  LYS   A HB3  1 
ATOM   1202 H  HG2  A LYS   A 1 44  ? 30.951 8.063   -3.597  0.62 20.25 ?  44  LYS   A HG2  1 
ATOM   1203 H  HG2  B LYS   A 1 44  ? 30.924 8.197   -3.524  0.38 21.73 ?  44  LYS   A HG2  1 
ATOM   1204 H  HG3  A LYS   A 1 44  ? 30.305 9.304   -4.353  0.62 20.25 ?  44  LYS   A HG3  1 
ATOM   1205 H  HG3  B LYS   A 1 44  ? 30.229 9.435   -4.244  0.38 21.73 ?  44  LYS   A HG3  1 
ATOM   1206 H  HD2  A LYS   A 1 44  ? 30.407 10.533  -2.339  0.62 26.19 ?  44  LYS   A HD2  1 
ATOM   1207 H  HD2  B LYS   A 1 44  ? 30.255 10.616  -2.214  0.38 25.84 ?  44  LYS   A HD2  1 
ATOM   1208 H  HD3  A LYS   A 1 44  ? 31.168 9.306   -1.663  0.62 26.19 ?  44  LYS   A HD3  1 
ATOM   1209 H  HD3  B LYS   A 1 44  ? 30.997 9.391   -1.517  0.38 25.84 ?  44  LYS   A HD3  1 
ATOM   1210 H  HE2  A LYS   A 1 44  ? 32.862 9.572   -3.337  0.62 30.14 ?  44  LYS   A HE2  1 
ATOM   1211 H  HE2  B LYS   A 1 44  ? 32.741 9.725   -3.173  0.38 28.62 ?  44  LYS   A HE2  1 
ATOM   1212 H  HE3  A LYS   A 1 44  ? 32.177 10.964  -3.691  0.62 30.14 ?  44  LYS   A HE3  1 
ATOM   1213 H  HE3  B LYS   A 1 44  ? 32.101 11.171  -3.351  0.38 28.62 ?  44  LYS   A HE3  1 
ATOM   1214 H  HZ1  A LYS   A 1 44  ? 33.886 11.267  -2.229  0.62 32.35 ?  44  LYS   A HZ1  1 
ATOM   1215 H  HZ1  B LYS   A 1 44  ? 33.782 11.227  -1.822  0.38 30.13 ?  44  LYS   A HZ1  1 
ATOM   1216 H  HZ2  A LYS   A 1 44  ? 32.650 11.654  -1.579  0.62 32.35 ?  44  LYS   A HZ2  1 
ATOM   1217 H  HZ2  B LYS   A 1 44  ? 32.541 11.558  -1.152  0.38 30.13 ?  44  LYS   A HZ2  1 
ATOM   1218 H  HZ3  A LYS   A 1 44  ? 33.273 10.387  -1.255  0.62 32.35 ?  44  LYS   A HZ3  1 
ATOM   1219 H  HZ3  B LYS   A 1 44  ? 33.123 10.241  -0.989  0.38 30.13 ?  44  LYS   A HZ3  1 
ATOM   1220 N  N    A HIS   A 1 45  ? 27.254 7.979   0.044   0.62 10.22 ?  45  HIS   A N    1 
ATOM   1221 N  N    B HIS   A 1 45  ? 27.241 7.988   0.132   0.38 12.19 ?  45  HIS   A N    1 
ATOM   1222 C  CA   A HIS   A 1 45  ? 26.018 7.635   0.746   0.62 10.25 ?  45  HIS   A CA   1 
ATOM   1223 C  CA   B HIS   A 1 45  ? 25.985 7.706   0.826   0.38 12.21 ?  45  HIS   A CA   1 
ATOM   1224 C  C    A HIS   A 1 45  ? 24.992 8.760   0.588   0.62 11.01 ?  45  HIS   A C    1 
ATOM   1225 C  C    B HIS   A 1 45  ? 25.029 8.869   0.608   0.38 12.95 ?  45  HIS   A C    1 
ATOM   1226 O  O    A HIS   A 1 45  ? 24.618 9.456   1.535   0.62 11.70 ?  45  HIS   A O    1 
ATOM   1227 O  O    B HIS   A 1 45  ? 24.950 9.796   1.415   0.38 13.79 ?  45  HIS   A O    1 
ATOM   1228 C  CB   A HIS   A 1 45  ? 26.320 7.359   2.208   0.62 10.39 ?  45  HIS   A CB   1 
ATOM   1229 C  CB   B HIS   A 1 45  ? 26.243 7.480   2.307   0.38 11.86 ?  45  HIS   A CB   1 
ATOM   1230 C  CG   A HIS   A 1 45  ? 27.424 6.374   2.415   0.62 10.06 ?  45  HIS   A CG   1 
ATOM   1231 C  CG   B HIS   A 1 45  ? 27.369 6.537   2.578   0.38 11.21 ?  45  HIS   A CG   1 
ATOM   1232 N  ND1  A HIS   A 1 45  ? 27.402 5.099   1.885   0.62 9.94  ?  45  HIS   A ND1  1 
ATOM   1233 N  ND1  B HIS   A 1 45  ? 27.389 5.246   2.098   0.38 11.52 ?  45  HIS   A ND1  1 
ATOM   1234 C  CD2  A HIS   A 1 45  ? 28.594 6.490   3.085   0.62 10.64 ?  45  HIS   A CD2  1 
ATOM   1235 C  CD2  B HIS   A 1 45  ? 28.522 6.706   3.266   0.38 10.58 ?  45  HIS   A CD2  1 
ATOM   1236 C  CE1  A HIS   A 1 45  ? 28.512 4.471   2.239   0.62 10.62 ?  45  HIS   A CE1  1 
ATOM   1237 C  CE1  B HIS   A 1 45  ? 28.506 4.657   2.487   0.38 10.07 ?  45  HIS   A CE1  1 
ATOM   1238 N  NE2  A HIS   A 1 45  ? 29.254 5.295   2.960   0.62 11.19 ?  45  HIS   A NE2  1 
ATOM   1239 N  NE2  B HIS   A 1 45  ? 29.211 5.522   3.196   0.38 9.78  ?  45  HIS   A NE2  1 
ATOM   1240 H  H    A HIS   A 1 45  ? 27.794 8.452   0.516   0.62 12.29 ?  45  HIS   A H    1 
ATOM   1241 H  H    B HIS   A 1 45  ? 27.806 8.439   0.602   0.38 14.65 ?  45  HIS   A H    1 
ATOM   1242 H  HA   A HIS   A 1 45  ? 25.644 6.826   0.360   0.62 12.31 ?  45  HIS   A HA   1 
ATOM   1243 H  HA   B HIS   A 1 45  ? 25.585 6.908   0.451   0.38 14.68 ?  45  HIS   A HA   1 
ATOM   1244 H  HB2  A HIS   A 1 45  ? 26.574 8.183   2.642   0.62 12.49 ?  45  HIS   A HB2  1 
ATOM   1245 H  HB2  B HIS   A 1 45  ? 26.455 8.329   2.720   0.38 14.25 ?  45  HIS   A HB2  1 
ATOM   1246 H  HB3  A HIS   A 1 45  ? 25.520 6.996   2.632   0.62 12.49 ?  45  HIS   A HB3  1 
ATOM   1247 H  HB3  B HIS   A 1 45  ? 25.439 7.109   2.705   0.38 14.25 ?  45  HIS   A HB3  1 
ATOM   1248 H  HD2  A HIS   A 1 45  ? 28.897 7.242   3.540   0.62 12.79 ?  45  HIS   A HD2  1 
ATOM   1249 H  HD2  B HIS   A 1 45  ? 28.794 7.482   3.701   0.38 12.72 ?  45  HIS   A HD2  1 
ATOM   1250 H  HE1  A HIS   A 1 45  ? 28.742 3.591   2.021   0.62 12.76 ?  45  HIS   A HE1  1 
ATOM   1251 H  HE1  B HIS   A 1 45  ? 28.754 3.784   2.294   0.38 12.10 ?  45  HIS   A HE1  1 
ATOM   1252 H  HE2  A HIS   A 1 45  ? 30.027 5.110   3.302   0.62 13.45 ?  45  HIS   A HE2  1 
ATOM   1253 H  HE2  B HIS   A 1 45  ? 29.977 5.369   3.554   0.38 11.75 ?  45  HIS   A HE2  1 
ATOM   1254 N  N    A GLY   A 1 46  ? 24.522 8.917   -0.647  0.62 12.21 ?  46  GLY   A N    1 
ATOM   1255 N  N    B GLY   A 1 46  ? 24.279 8.811   -0.486  0.38 12.99 ?  46  GLY   A N    1 
ATOM   1256 C  CA   A GLY   A 1 46  ? 23.722 10.077  -0.995  0.62 13.31 ?  46  GLY   A CA   1 
ATOM   1257 C  CA   B GLY   A 1 46  ? 23.432 9.928   -0.850  0.38 12.75 ?  46  GLY   A CA   1 
ATOM   1258 C  C    A GLY   A 1 46  ? 22.231 9.942   -0.762  0.62 13.26 ?  46  GLY   A C    1 
ATOM   1259 C  C    B GLY   A 1 46  ? 21.972 9.781   -0.475  0.38 11.72 ?  46  GLY   A C    1 
ATOM   1260 O  O    A GLY   A 1 46  ? 21.551 10.933  -0.473  0.62 13.99 ?  46  GLY   A O    1 
ATOM   1261 O  O    B GLY   A 1 46  ? 21.344 10.742  -0.015  0.38 12.32 ?  46  GLY   A O    1 
ATOM   1262 H  H    A GLY   A 1 46  ? 24.649 8.359   -1.289  0.62 14.68 ?  46  GLY   A H    1 
ATOM   1263 H  H    B GLY   A 1 46  ? 24.252 8.138   -1.028  0.38 15.61 ?  46  GLY   A H    1 
ATOM   1264 H  HA2  A GLY   A 1 46  ? 24.046 10.836  -0.480  0.62 15.99 ?  46  GLY   A HA2  1 
ATOM   1265 H  HA2  B GLY   A 1 46  ? 23.765 10.729  -0.418  0.38 15.32 ?  46  GLY   A HA2  1 
ATOM   1266 H  HA3  A GLY   A 1 46  ? 23.857 10.272  -1.931  0.62 15.99 ?  46  GLY   A HA3  1 
ATOM   1267 H  HA3  B GLY   A 1 46  ? 23.483 10.058  -1.805  0.38 15.32 ?  46  GLY   A HA3  1 
ATOM   1268 N  N    A GLY   A 1 47  ? 21.707 8.730   -0.906  0.62 12.81 ?  47  GLY   A N    1 
ATOM   1269 N  N    B GLY   A 1 47  ? 21.419 8.584   -0.661  0.38 11.75 ?  47  GLY   A N    1 
ATOM   1270 C  CA   A GLY   A 1 47  ? 20.274 8.521   -0.873  0.62 13.01 ?  47  GLY   A CA   1 
ATOM   1271 C  CA   B GLY   A 1 47  ? 19.992 8.377   -0.530  0.38 12.01 ?  47  GLY   A CA   1 
ATOM   1272 C  C    A GLY   A 1 47  ? 19.959 7.086   -0.511  0.62 12.54 ?  47  GLY   A C    1 
ATOM   1273 C  C    B GLY   A 1 47  ? 19.662 6.951   -0.146  0.38 10.81 ?  47  GLY   A C    1 
ATOM   1274 O  O    A GLY   A 1 47  ? 20.852 6.274   -0.253  0.62 12.92 ?  47  GLY   A O    1 
ATOM   1275 O  O    B GLY   A 1 47  ? 20.544 6.103   0.014   0.38 10.48 ?  47  GLY   A O    1 
ATOM   1276 H  H    A GLY   A 1 47  ? 22.163 8.018   -1.013  0.62 15.39 ?  47  GLY   A H    1 
ATOM   1277 H  H    B GLY   A 1 47  ? 21.863 7.871   -0.853  0.38 14.12 ?  47  GLY   A H    1 
ATOM   1278 H  HA2  A GLY   A 1 47  ? 19.859 9.118   -0.226  0.62 15.63 ?  47  GLY   A HA2  1 
ATOM   1279 H  HA2  B GLY   A 1 47  ? 19.640 8.960   0.156   0.38 14.43 ?  47  GLY   A HA2  1 
ATOM   1280 H  HA3  A GLY   A 1 47  ? 19.901 8.703   -1.749  0.62 15.63 ?  47  GLY   A HA3  1 
ATOM   1281 H  HA3  B GLY   A 1 47  ? 19.558 8.590   -1.372  0.38 14.43 ?  47  GLY   A HA3  1 
ATOM   1282 N  N    A GLY   A 1 48  ? 18.668 6.772   -0.513  0.62 11.91 ?  48  GLY   A N    1 
ATOM   1283 N  N    B GLY   A 1 48  ? 18.363 6.694   0.003   0.38 10.85 ?  48  GLY   A N    1 
ATOM   1284 C  CA   A GLY   A 1 48  ? 18.261 5.437   -0.135  0.62 11.90 ?  48  GLY   A CA   1 
ATOM   1285 C  CA   B GLY   A 1 48  ? 17.920 5.383   0.443   0.38 10.64 ?  48  GLY   A CA   1 
ATOM   1286 C  C    A GLY   A 1 48  ? 18.651 5.126   1.296   0.62 11.42 ?  48  GLY   A C    1 
ATOM   1287 C  C    B GLY   A 1 48  ? 18.523 5.025   1.786   0.38 11.06 ?  48  GLY   A C    1 
ATOM   1288 O  O    A GLY   A 1 48  ? 18.796 6.017   2.143   0.62 11.78 ?  48  GLY   A O    1 
ATOM   1289 O  O    B GLY   A 1 48  ? 18.702 5.875   2.669   0.38 11.27 ?  48  GLY   A O    1 
ATOM   1290 H  H    A GLY   A 1 48  ? 18.026 7.297   -0.730  0.62 14.31 ?  48  GLY   A H    1 
ATOM   1291 H  H    B GLY   A 1 48  ? 17.722 7.257   -0.138  0.38 13.04 ?  48  GLY   A H    1 
ATOM   1292 H  HA2  A GLY   A 1 48  ? 17.305 5.344   -0.220  0.62 14.30 ?  48  GLY   A HA2  1 
ATOM   1293 H  HA2  B GLY   A 1 48  ? 16.950 5.367   0.521   0.38 12.78 ?  48  GLY   A HA2  1 
ATOM   1294 H  HA3  A GLY   A 1 48  ? 18.695 4.786   -0.708  0.62 14.30 ?  48  GLY   A HA3  1 
ATOM   1295 H  HA3  B GLY   A 1 48  ? 18.184 4.709   -0.207  0.38 12.78 ?  48  GLY   A HA3  1 
ATOM   1296 N  N    A VAL   A 1 49  ? 18.826 3.831   1.571   0.62 11.81 ?  49  VAL   A N    1 
ATOM   1297 N  N    B VAL   A 1 49  ? 18.835 3.738   1.946   0.38 10.96 ?  49  VAL   A N    1 
ATOM   1298 C  CA   A VAL   A 1 49  ? 19.261 3.401   2.897   0.62 12.36 ?  49  VAL   A CA   1 
ATOM   1299 C  CA   B VAL   A 1 49  ? 19.456 3.255   3.176   0.38 11.06 ?  49  VAL   A CA   1 
ATOM   1300 C  C    A VAL   A 1 49  ? 20.582 4.058   3.272   0.62 11.21 ?  49  VAL   A C    1 
ATOM   1301 C  C    B VAL   A 1 49  ? 20.724 4.040   3.493   0.38 10.29 ?  49  VAL   A C    1 
ATOM   1302 O  O    A VAL   A 1 49  ? 20.775 4.465   4.421   0.62 11.43 ?  49  VAL   A O    1 
ATOM   1303 O  O    B VAL   A 1 49  ? 20.933 4.479   4.630   0.38 10.34 ?  49  VAL   A O    1 
ATOM   1304 C  CB   A VAL   A 1 49  ? 19.360 1.864   2.947   0.62 13.65 ?  49  VAL   A CB   1 
ATOM   1305 C  CB   B VAL   A 1 49  ? 19.747 1.749   3.057   0.38 11.56 ?  49  VAL   A CB   1 
ATOM   1306 C  CG1  A VAL   A 1 49  ? 20.102 1.400   4.205   0.62 14.28 ?  49  VAL   A CG1  1 
ATOM   1307 C  CG1  B VAL   A 1 49  ? 20.621 1.292   4.204   0.38 11.41 ?  49  VAL   A CG1  1 
ATOM   1308 C  CG2  A VAL   A 1 49  ? 17.969 1.241   2.883   0.62 15.20 ?  49  VAL   A CG2  1 
ATOM   1309 C  CG2  B VAL   A 1 49  ? 18.451 0.949   3.010   0.38 12.59 ?  49  VAL   A CG2  1 
ATOM   1310 H  H    A VAL   A 1 49  ? 18.709 3.187   1.013   0.62 14.19 ?  49  VAL   A H    1 
ATOM   1311 H  H    B VAL   A 1 49  ? 18.690 3.124   1.359   0.38 13.18 ?  49  VAL   A H    1 
ATOM   1312 H  HA   A VAL   A 1 49  ? 18.600 3.667   3.552   0.62 14.85 ?  49  VAL   A HA   1 
ATOM   1313 H  HA   B VAL   A 1 49  ? 18.841 3.379   3.911   0.38 13.30 ?  49  VAL   A HA   1 
ATOM   1314 H  HB   A VAL   A 1 49  ? 19.865 1.550   2.177   0.62 16.40 ?  49  VAL   A HB   1 
ATOM   1315 H  HB   B VAL   A 1 49  ? 20.230 1.582   2.230   0.38 13.89 ?  49  VAL   A HB   1 
ATOM   1316 H  HG11 A VAL   A 1 49  ? 19.911 0.460   4.354   0.62 17.16 ?  49  VAL   A HG11 1 
ATOM   1317 H  HG11 B VAL   A 1 49  ? 20.549 0.329   4.291   0.38 13.72 ?  49  VAL   A HG11 1 
ATOM   1318 H  HG12 A VAL   A 1 49  ? 21.054 1.528   4.082   0.62 17.16 ?  49  VAL   A HG12 1 
ATOM   1319 H  HG12 B VAL   A 1 49  ? 21.544 1.536   4.021   0.38 13.72 ?  49  VAL   A HG12 1 
ATOM   1320 H  HG13 A VAL   A 1 49  ? 19.788 1.922   4.962   0.62 17.16 ?  49  VAL   A HG13 1 
ATOM   1321 H  HG13 B VAL   A 1 49  ? 20.320 1.719   5.020   0.38 13.72 ?  49  VAL   A HG13 1 
ATOM   1322 H  HG21 A VAL   A 1 49  ? 18.053 0.275   2.912   0.62 18.26 ?  49  VAL   A HG21 1 
ATOM   1323 H  HG21 B VAL   A 1 49  ? 18.661 0.006   2.933   0.38 15.13 ?  49  VAL   A HG21 1 
ATOM   1324 H  HG22 A VAL   A 1 49  ? 17.453 1.551   3.643   0.62 18.26 ?  49  VAL   A HG22 1 
ATOM   1325 H  HG22 B VAL   A 1 49  ? 17.952 1.110   3.828   0.38 15.13 ?  49  VAL   A HG22 1 
ATOM   1326 H  HG23 A VAL   A 1 49  ? 17.543 1.513   2.057   0.62 18.26 ?  49  VAL   A HG23 1 
ATOM   1327 H  HG23 B VAL   A 1 49  ? 17.929 1.236   2.244   0.38 15.13 ?  49  VAL   A HG23 1 
ATOM   1328 N  N    A ALA   A 1 50  ? 21.521 4.130   2.326   0.62 10.49 ?  50  ALA   A N    1 
ATOM   1329 N  N    B ALA   A 1 50  ? 21.602 4.197   2.499   0.38 10.37 ?  50  ALA   A N    1 
ATOM   1330 C  CA   A ALA   A 1 50  ? 22.842 4.676   2.624   0.62 10.50 ?  50  ALA   A CA   1 
ATOM   1331 C  CA   B ALA   A 1 50  ? 22.913 4.782   2.761   0.38 10.19 ?  50  ALA   A CA   1 
ATOM   1332 C  C    A ALA   A 1 50  ? 22.758 6.142   3.021   0.62 10.60 ?  50  ALA   A C    1 
ATOM   1333 C  C    B ALA   A 1 50  ? 22.788 6.224   3.233   0.38 9.92  ?  50  ALA   A C    1 
ATOM   1334 O  O    A ALA   A 1 50  ? 23.398 6.571   3.987   0.62 11.16 ?  50  ALA   A O    1 
ATOM   1335 O  O    B ALA   A 1 50  ? 23.387 6.614   4.244   0.38 9.90  ?  50  ALA   A O    1 
ATOM   1336 C  CB   A ALA   A 1 50  ? 23.753 4.510   1.412   0.62 10.99 ?  50  ALA   A CB   1 
ATOM   1337 C  CB   B ALA   A 1 50  ? 23.786 4.688   1.509   0.38 10.12 ?  50  ALA   A CB   1 
ATOM   1338 H  H    A ALA   A 1 50  ? 21.414 3.872   1.517   0.62 12.61 ?  50  ALA   A H    1 
ATOM   1339 H  H    B ALA   A 1 50  ? 21.460 3.987   1.671   0.38 12.47 ?  50  ALA   A H    1 
ATOM   1340 H  HA   A ALA   A 1 50  ? 23.226 4.190   3.370   0.62 12.62 ?  50  ALA   A HA   1 
ATOM   1341 H  HA   B ALA   A 1 50  ? 23.343 4.280   3.465   0.38 12.24 ?  50  ALA   A HA   1 
ATOM   1342 H  HB1  A ALA   A 1 50  ? 24.623 4.880   1.626   0.62 13.21 ?  50  ALA   A HB1  1 
ATOM   1343 H  HB1  B ALA   A 1 50  ? 24.653 5.077   1.700   0.38 12.17 ?  50  ALA   A HB1  1 
ATOM   1344 H  HB2  A ALA   A 1 50  ? 23.830 3.569   1.206   0.62 13.21 ?  50  ALA   A HB2  1 
ATOM   1345 H  HB2  B ALA   A 1 50  ? 23.889 3.753   1.265   0.38 12.17 ?  50  ALA   A HB2  1 
ATOM   1346 H  HB3  A ALA   A 1 50  ? 23.363 4.988   0.664   0.62 13.21 ?  50  ALA   A HB3  1 
ATOM   1347 H  HB3  B ALA   A 1 50  ? 23.357 5.172   0.786   0.38 12.17 ?  50  ALA   A HB3  1 
ATOM   1348 N  N    A GLY   A 1 51  ? 21.998 6.933   2.269   0.62 10.62 ?  51  GLY   A N    1 
ATOM   1349 N  N    B GLY   A 1 51  ? 22.006 7.030   2.515   0.38 10.34 ?  51  GLY   A N    1 
ATOM   1350 C  CA   A GLY   A 1 51  ? 21.837 8.328   2.633   0.62 11.22 ?  51  GLY   A CA   1 
ATOM   1351 C  CA   B GLY   A 1 51  ? 21.835 8.413   2.921   0.38 10.50 ?  51  GLY   A CA   1 
ATOM   1352 C  C    A GLY   A 1 51  ? 21.225 8.492   4.008   0.62 10.81 ?  51  GLY   A C    1 
ATOM   1353 C  C    B GLY   A 1 51  ? 21.206 8.529   4.295   0.38 10.57 ?  51  GLY   A C    1 
ATOM   1354 O  O    A GLY   A 1 51  ? 21.606 9.391   4.762   0.62 11.40 ?  51  GLY   A O    1 
ATOM   1355 O  O    B GLY   A 1 51  ? 21.572 9.404   5.086   0.38 10.58 ?  51  GLY   A O    1 
ATOM   1356 H  H    A GLY   A 1 51  ? 21.585 6.695   1.558   0.62 12.76 ?  51  GLY   A H    1 
ATOM   1357 H  H    B GLY   A 1 51  ? 21.569 6.802   1.806   0.38 12.43 ?  51  GLY   A H    1 
ATOM   1358 H  HA2  A GLY   A 1 51  ? 22.697 8.773   2.635   0.62 13.48 ?  51  GLY   A HA2  1 
ATOM   1359 H  HA2  B GLY   A 1 51  ? 22.698 8.855   2.936   0.38 12.62 ?  51  GLY   A HA2  1 
ATOM   1360 H  HA3  A GLY   A 1 51  ? 21.260 8.773   1.993   0.62 13.48 ?  51  GLY   A HA3  1 
ATOM   1361 H  HA3  B GLY   A 1 51  ? 21.270 8.873   2.272   0.38 12.62 ?  51  GLY   A HA3  1 
ATOM   1362 N  N    A ALA   A 1 52  ? 20.257 7.634   4.347   0.62 11.26 ?  52  ALA   A N    1 
ATOM   1363 N  N    B ALA   A 1 52  ? 20.251 7.645   4.597   0.38 10.23 ?  52  ALA   A N    1 
ATOM   1364 C  CA   A ALA   A 1 52  ? 19.598 7.717   5.646   0.62 11.89 ?  52  ALA   A CA   1 
ATOM   1365 C  CA   B ALA   A 1 52  ? 19.576 7.691   5.889   0.38 11.29 ?  52  ALA   A CA   1 
ATOM   1366 C  C    A ALA   A 1 52  ? 20.534 7.303   6.780   0.62 11.47 ?  52  ALA   A C    1 
ATOM   1367 C  C    B ALA   A 1 52  ? 20.510 7.259   7.017   0.38 10.77 ?  52  ALA   A C    1 
ATOM   1368 O  O    A ALA   A 1 52  ? 20.612 7.985   7.806   0.62 12.06 ?  52  ALA   A O    1 
ATOM   1369 O  O    B ALA   A 1 52  ? 20.562 7.901   8.073   0.38 11.31 ?  52  ALA   A O    1 
ATOM   1370 C  CB   A ALA   A 1 52  ? 18.324 6.871   5.638   0.62 13.15 ?  52  ALA   A CB   1 
ATOM   1371 C  CB   B ALA   A 1 52  ? 18.318 6.824   5.846   0.38 12.68 ?  52  ALA   A CB   1 
ATOM   1372 H  H    A ALA   A 1 52  ? 19.973 7.000   3.847   0.62 13.53 ?  52  ALA   A H    1 
ATOM   1373 H  H    B ALA   A 1 52  ? 19.986 7.014   4.070   0.38 12.29 ?  52  ALA   A H    1 
ATOM   1374 H  HA   A ALA   A 1 52  ? 19.338 8.633   5.809   0.62 14.28 ?  52  ALA   A HA   1 
ATOM   1375 H  HA   B ALA   A 1 52  ? 19.303 8.604   6.055   0.38 13.56 ?  52  ALA   A HA   1 
ATOM   1376 H  HB1  A ALA   A 1 52  ? 17.895 6.933   6.508   0.62 15.80 ?  52  ALA   A HB1  1 
ATOM   1377 H  HB1  B ALA   A 1 52  ? 17.847 6.918   6.687   0.38 15.24 ?  52  ALA   A HB1  1 
ATOM   1378 H  HB2  A ALA   A 1 52  ? 17.727 7.209   4.952   0.62 15.80 ?  52  ALA   A HB2  1 
ATOM   1379 H  HB2  B ALA   A 1 52  ? 17.754 7.124   5.115   0.38 15.24 ?  52  ALA   A HB2  1 
ATOM   1380 H  HB3  A ALA   A 1 52  ? 18.555 5.947   5.450   0.62 15.80 ?  52  ALA   A HB3  1 
ATOM   1381 H  HB3  B ALA   A 1 52  ? 18.575 5.900   5.706   0.38 15.24 ?  52  ALA   A HB3  1 
ATOM   1382 N  N    A LEU   A 1 53  ? 21.262 6.193   6.620   0.62 10.98 ?  53  LEU   A N    1 
ATOM   1383 N  N    B LEU   A 1 53  ? 21.257 6.169   6.818   0.38 10.36 ?  53  LEU   A N    1 
ATOM   1384 C  CA   A LEU   A 1 53  ? 22.189 5.782   7.673   0.62 12.10 ?  53  LEU   A CA   1 
ATOM   1385 C  CA   B LEU   A 1 53  ? 22.262 5.788   7.807   0.38 10.68 ?  53  LEU   A CA   1 
ATOM   1386 C  C    A LEU   A 1 53  ? 23.265 6.835   7.882   0.62 11.52 ?  53  LEU   A C    1 
ATOM   1387 C  C    B LEU   A 1 53  ? 23.275 6.909   7.994   0.38 10.13 ?  53  LEU   A C    1 
ATOM   1388 O  O    A LEU   A 1 53  ? 23.643 7.137   9.018   0.62 12.52 ?  53  LEU   A O    1 
ATOM   1389 O  O    B LEU   A 1 53  ? 23.526 7.358   9.118   0.38 10.37 ?  53  LEU   A O    1 
ATOM   1390 C  CB   A LEU   A 1 53  ? 22.834 4.435   7.338   0.62 12.87 ?  53  LEU   A CB   1 
ATOM   1391 C  CB   B LEU   A 1 53  ? 22.971 4.494   7.393   0.38 10.43 ?  53  LEU   A CB   1 
ATOM   1392 C  CG   A LEU   A 1 53  ? 21.923 3.201   7.349   0.62 12.94 ?  53  LEU   A CG   1 
ATOM   1393 C  CG   B LEU   A 1 53  ? 22.221 3.159   7.487   0.38 10.69 ?  53  LEU   A CG   1 
ATOM   1394 C  CD1  A LEU   A 1 53  ? 22.662 2.001   6.785   0.62 12.68 ?  53  LEU   A CD1  1 
ATOM   1395 C  CD1  B LEU   A 1 53  ? 23.058 2.045   6.875   0.38 11.44 ?  53  LEU   A CD1  1 
ATOM   1396 C  CD2  A LEU   A 1 53  ? 21.407 2.894   8.750   0.62 13.69 ?  53  LEU   A CD2  1 
ATOM   1397 C  CD2  B LEU   A 1 53  ? 21.868 2.810   8.921   0.38 10.60 ?  53  LEU   A CD2  1 
ATOM   1398 H  H    A LEU   A 1 53  ? 21.245 5.676   5.935   0.62 13.20 ?  53  LEU   A H    1 
ATOM   1399 H  H    B LEU   A 1 53  ? 21.197 5.643   6.137   0.38 12.45 ?  53  LEU   A H    1 
ATOM   1400 H  HA   A LEU   A 1 53  ? 21.705 5.679   8.507   0.62 14.54 ?  53  LEU   A HA   1 
ATOM   1401 H  HA   B LEU   A 1 53  ? 21.823 5.634   8.655   0.38 12.84 ?  53  LEU   A HA   1 
ATOM   1402 H  HB2  A LEU   A 1 53  ? 23.220 4.496   6.451   0.62 15.46 ?  53  LEU   A HB2  1 
ATOM   1403 H  HB2  B LEU   A 1 53  ? 23.244 4.590   6.469   0.38 12.54 ?  53  LEU   A HB2  1 
ATOM   1404 H  HB3  A LEU   A 1 53  ? 23.544 4.268   7.981   0.62 15.46 ?  53  LEU   A HB3  1 
ATOM   1405 H  HB3  B LEU   A 1 53  ? 23.760 4.403   7.947   0.38 12.54 ?  53  LEU   A HB3  1 
ATOM   1406 H  HG   A LEU   A 1 53  ? 21.159 3.371   6.778   0.62 15.55 ?  53  LEU   A HG   1 
ATOM   1407 H  HG   B LEU   A 1 53  ? 21.398 3.217   6.979   0.38 12.84 ?  53  LEU   A HG   1 
ATOM   1408 H  HD11 A LEU   A 1 53  ? 22.071 1.231   6.802   0.62 15.24 ?  53  LEU   A HD11 1 
ATOM   1409 H  HD11 B LEU   A 1 53  ? 22.572 1.206   6.944   0.38 13.74 ?  53  LEU   A HD11 1 
ATOM   1410 H  HD12 A LEU   A 1 53  ? 22.930 2.193   5.874   0.62 15.24 ?  53  LEU   A HD12 1 
ATOM   1411 H  HD12 B LEU   A 1 53  ? 23.231 2.250   5.944   0.38 13.74 ?  53  LEU   A HD12 1 
ATOM   1412 H  HD13 A LEU   A 1 53  ? 23.445 1.827   7.332   0.62 15.24 ?  53  LEU   A HD13 1 
ATOM   1413 H  HD13 B LEU   A 1 53  ? 23.898 1.977   7.360   0.38 13.74 ?  53  LEU   A HD13 1 
ATOM   1414 H  HD21 A LEU   A 1 53  ? 20.865 2.089   8.717   0.62 16.45 ?  53  LEU   A HD21 1 
ATOM   1415 H  HD21 B LEU   A 1 53  ? 21.430 1.943   8.939   0.38 12.74 ?  53  LEU   A HD21 1 
ATOM   1416 H  HD22 A LEU   A 1 53  ? 22.162 2.759   9.343   0.62 16.45 ?  53  LEU   A HD22 1 
ATOM   1417 H  HD22 B LEU   A 1 53  ? 22.680 2.780   9.449   0.38 12.74 ?  53  LEU   A HD22 1 
ATOM   1418 H  HD23 A LEU   A 1 53  ? 20.870 3.639   9.060   0.62 16.45 ?  53  LEU   A HD23 1 
ATOM   1419 H  HD23 B LEU   A 1 53  ? 21.270 3.489   9.270   0.38 12.74 ?  53  LEU   A HD23 1 
ATOM   1420 N  N    A ASN   A 1 54  ? 23.780 7.401   6.796   0.62 11.01 ?  54  ASN   A N    1 
ATOM   1421 N  N    B ASN   A 1 54  ? 23.856 7.389   6.895   0.38 10.54 ?  54  ASN   A N    1 
ATOM   1422 C  CA   A ASN   A 1 54  ? 24.843 8.383   6.948   0.62 11.15 ?  54  ASN   A CA   1 
ATOM   1423 C  CA   B ASN   A 1 54  ? 24.886 8.411   7.020   0.38 10.71 ?  54  ASN   A CA   1 
ATOM   1424 C  C    A ASN   A 1 54  ? 24.347 9.630   7.680   0.62 11.44 ?  54  ASN   A C    1 
ATOM   1425 C  C    B ASN   A 1 54  ? 24.347 9.657   7.713   0.38 11.04 ?  54  ASN   A C    1 
ATOM   1426 O  O    A ASN   A 1 54  ? 25.052 10.180  8.536   0.62 12.17 ?  54  ASN   A O    1 
ATOM   1427 O  O    B ASN   A 1 54  ? 25.018 10.231  8.581   0.38 11.25 ?  54  ASN   A O    1 
ATOM   1428 C  CB   A ASN   A 1 54  ? 25.415 8.741   5.587   0.62 11.32 ?  54  ASN   A CB   1 
ATOM   1429 C  CB   B ASN   A 1 54  ? 25.466 8.768   5.658   0.38 10.65 ?  54  ASN   A CB   1 
ATOM   1430 C  CG   A ASN   A 1 54  ? 26.472 9.801   5.691   0.62 11.89 ?  54  ASN   A CG   1 
ATOM   1431 C  CG   B ASN   A 1 54  ? 26.436 9.921   5.748   0.38 10.41 ?  54  ASN   A CG   1 
ATOM   1432 O  OD1  A ASN   A 1 54  ? 27.469 9.626   6.397   0.62 12.47 ?  54  ASN   A OD1  1 
ATOM   1433 O  OD1  B ASN   A 1 54  ? 27.463 9.822   6.424   0.38 9.99  ?  54  ASN   A OD1  1 
ATOM   1434 N  ND2  A ASN   A 1 54  ? 26.261 10.920  5.018   0.62 12.49 ?  54  ASN   A ND2  1 
ATOM   1435 N  ND2  B ASN   A 1 54  ? 26.107 11.033  5.105   0.38 10.93 ?  54  ASN   A ND2  1 
ATOM   1436 H  H    A ASN   A 1 54  ? 23.535 7.241   5.990   0.62 13.24 ?  54  ASN   A H    1 
ATOM   1437 H  H    B ASN   A 1 54  ? 23.669 7.154   6.091   0.38 12.67 ?  54  ASN   A H    1 
ATOM   1438 H  HA   A ASN   A 1 54  ? 25.549 7.993   7.481   0.62 13.40 ?  54  ASN   A HA   1 
ATOM   1439 H  HA   B ASN   A 1 54  ? 25.602 8.064   7.567   0.38 12.87 ?  54  ASN   A HA   1 
ATOM   1440 H  HB2  A ASN   A 1 54  ? 25.816 7.947   5.197   0.62 13.61 ?  54  ASN   A HB2  1 
ATOM   1441 H  HB2  B ASN   A 1 54  ? 25.944 7.998   5.308   0.38 12.80 ?  54  ASN   A HB2  1 
ATOM   1442 H  HB3  A ASN   A 1 54  ? 24.707 9.074   5.019   0.62 13.61 ?  54  ASN   A HB3  1 
ATOM   1443 H  HB3  B ASN   A 1 54  ? 24.749 9.019   5.059   0.38 12.80 ?  54  ASN   A HB3  1 
ATOM   1444 H  HD21 A ASN   A 1 54  ? 26.836 11.558  5.055   0.62 15.00 ?  54  ASN   A HD21 1 
ATOM   1445 H  HD21 B ASN   A 1 54  ? 26.625 11.721  5.139   0.38 13.14 ?  54  ASN   A HD21 1 
ATOM   1446 H  HD22 A ASN   A 1 54  ? 25.549 11.006  4.547   0.62 15.00 ?  54  ASN   A HD22 1 
ATOM   1447 H  HD22 B ASN   A 1 54  ? 25.378 11.067  4.651   0.38 13.14 ?  54  ASN   A HD22 1 
ATOM   1448 N  N    . LYS   A 1 55  ? 23.137 10.097  7.348   1.00 11.32 ?  55  LYS   A N    1 
ATOM   1449 C  CA   . LYS   A 1 55  ? 22.563 11.265  8.007   1.00 12.45 ?  55  LYS   A CA   1 
ATOM   1450 C  C    . LYS   A 1 55  ? 22.459 11.038  9.508   1.00 12.19 ?  55  LYS   A C    1 
ATOM   1451 O  O    . LYS   A 1 55  ? 22.742 11.940  10.308  1.00 12.92 ?  55  LYS   A O    1 
ATOM   1452 C  CB   . LYS   A 1 55  ? 21.192 11.562  7.398   1.00 12.87 ?  55  LYS   A CB   1 
ATOM   1453 C  CG   . LYS   A 1 55  ? 20.437 12.706  8.058   1.00 14.59 ?  55  LYS   A CG   1 
ATOM   1454 C  CD   . LYS   A 1 55  ? 19.118 12.948  7.330   1.00 17.24 ?  55  LYS   A CD   1 
ATOM   1455 C  CE   . LYS   A 1 55  ? 18.288 14.052  7.965   1.00 19.71 ?  55  LYS   A CE   1 
ATOM   1456 N  NZ   . LYS   A 1 55  ? 16.947 14.184  7.315   1.00 20.91 ?  55  LYS   A NZ   1 
ATOM   1457 H  H    A LYS   A 1 55  ? 22.626 9.751   6.746   0.62 13.61 ?  55  LYS   A H    1 
ATOM   1458 H  H    B LYS   A 1 55  ? 22.632 9.736   6.750   0.38 13.61 ?  55  LYS   A H    1 
ATOM   1459 H  HA   . LYS   A 1 55  ? 23.137 12.033  7.855   1.00 14.95 ?  55  LYS   A HA   1 
ATOM   1460 H  HB2  . LYS   A 1 55  ? 21.311 11.795  6.466   1.00 15.46 ?  55  LYS   A HB2  1 
ATOM   1461 H  HB3  . LYS   A 1 55  ? 20.641 10.769  7.473   1.00 15.46 ?  55  LYS   A HB3  1 
ATOM   1462 H  HG2  . LYS   A 1 55  ? 20.236 12.478  8.982   1.00 17.53 ?  55  LYS   A HG2  1 
ATOM   1463 H  HG3  . LYS   A 1 55  ? 20.965 13.517  8.016   1.00 17.53 ?  55  LYS   A HG3  1 
ATOM   1464 H  HD2  . LYS   A 1 55  ? 19.311 13.198  6.413   1.00 20.71 ?  55  LYS   A HD2  1 
ATOM   1465 H  HD3  . LYS   A 1 55  ? 18.597 12.128  7.347   1.00 20.71 ?  55  LYS   A HD3  1 
ATOM   1466 H  HE2  . LYS   A 1 55  ? 18.152 13.850  8.903   1.00 23.67 ?  55  LYS   A HE2  1 
ATOM   1467 H  HE3  . LYS   A 1 55  ? 18.757 14.896  7.868   1.00 23.67 ?  55  LYS   A HE3  1 
ATOM   1468 H  HZ1  . LYS   A 1 55  ? 16.425 14.723  7.799   1.00 25.11 ?  55  LYS   A HZ1  1 
ATOM   1469 H  HZ2  . LYS   A 1 55  ? 17.033 14.532  6.499   1.00 25.11 ?  55  LYS   A HZ2  1 
ATOM   1470 H  HZ3  . LYS   A 1 55  ? 16.555 13.389  7.251   1.00 25.11 ?  55  LYS   A HZ3  1 
ATOM   1471 N  N    . ALA   A 1 56  ? 22.068 9.827   9.909   1.00 12.41 ?  56  ALA   A N    1 
ATOM   1472 C  CA   . ALA   A 1 56  ? 21.936 9.507   11.321  1.00 12.97 ?  56  ALA   A CA   1 
ATOM   1473 C  C    . ALA   A 1 56  ? 23.273 9.529   12.049  1.00 12.74 ?  56  ALA   A C    1 
ATOM   1474 O  O    . ALA   A 1 56  ? 23.287 9.718   13.266  1.00 14.08 ?  56  ALA   A O    1 
ATOM   1475 C  CB   . ALA   A 1 56  ? 21.231 8.160   11.500  1.00 14.36 ?  56  ALA   A CB   1 
ATOM   1476 H  H    . ALA   A 1 56  ? 21.881 9.182   9.380   1.00 14.91 ?  56  ALA   A H    1 
ATOM   1477 H  HA   . ALA   A 1 56  ? 21.386 10.176  11.741  1.00 15.58 ?  56  ALA   A HA   1 
ATOM   1478 H  HB1  . ALA   A 1 56  ? 21.156 7.963   12.450  1.00 17.25 ?  56  ALA   A HB1  1 
ATOM   1479 H  HB2  . ALA   A 1 56  ? 20.345 8.216   11.108  1.00 17.25 ?  56  ALA   A HB2  1 
ATOM   1480 H  HB3  . ALA   A 1 56  ? 21.744 7.465   11.061  1.00 17.25 ?  56  ALA   A HB3  1 
ATOM   1481 N  N    . THR   A 1 57  ? 24.391 9.351   11.334  1.00 12.22 ?  57  THR   A N    1 
ATOM   1482 C  CA   . THR   A 1 57  ? 25.728 9.472   11.918  1.00 12.21 ?  57  THR   A CA   1 
ATOM   1483 C  C    . THR   A 1 57  ? 26.285 10.887  11.843  1.00 12.65 ?  57  THR   A C    1 
ATOM   1484 O  O    . THR   A 1 57  ? 27.468 11.090  12.137  1.00 13.34 ?  57  THR   A O    1 
ATOM   1485 C  CB   . THR   A 1 57  ? 26.740 8.520   11.254  1.00 12.05 ?  57  THR   A CB   1 
ATOM   1486 O  OG1  . THR   A 1 57  ? 27.125 9.007   9.955   1.00 11.79 ?  57  THR   A OG1  1 
ATOM   1487 C  CG2  . THR   A 1 57  ? 26.218 7.090   11.166  1.00 12.20 ?  57  THR   A CG2  1 
ATOM   1488 H  H    . THR   A 1 57  ? 24.403 9.140   10.498  1.00 14.69 ?  57  THR   A H    1 
ATOM   1489 H  HA   . THR   A 1 57  ? 25.675 9.219   12.857  1.00 14.67 ?  57  THR   A HA   1 
ATOM   1490 H  HB   . THR   A 1 57  ? 27.539 8.491   11.812  1.00 14.48 ?  57  THR   A HB   1 
ATOM   1491 H  HG1  . THR   A 1 57  ? 26.446 9.070   9.465   1.00 14.17 ?  57  THR   A HG1  1 
ATOM   1492 H  HG21 . THR   A 1 57  ? 26.893 6.507   10.780  1.00 14.66 ?  57  THR   A HG21 1 
ATOM   1493 H  HG22 . THR   A 1 57  ? 25.990 6.759   12.050  1.00 14.66 ?  57  THR   A HG22 1 
ATOM   1494 H  HG23 . THR   A 1 57  ? 25.424 7.057   10.608  1.00 14.66 ?  57  THR   A HG23 1 
ATOM   1495 N  N    . ASN   A 1 58  ? 25.478 11.864  11.438  1.00 13.22 ?  58  ASN   A N    1 
ATOM   1496 C  CA   . ASN   A 1 58  ? 25.953 13.241  11.350  1.00 13.81 ?  58  ASN   A CA   1 
ATOM   1497 C  C    . ASN   A 1 58  ? 27.087 13.364  10.327  1.00 12.85 ?  58  ASN   A C    1 
ATOM   1498 O  O    . ASN   A 1 58  ? 27.979 14.200  10.477  1.00 13.59 ?  58  ASN   A O    1 
ATOM   1499 C  CB   . ASN   A 1 58  ? 26.366 13.754  12.747  1.00 16.27 ?  58  ASN   A CB   1 
ATOM   1500 C  CG   . ASN   A 1 58  ? 26.785 15.214  12.767  1.00 19.44 ?  58  ASN   A CG   1 
ATOM   1501 O  OD1  . ASN   A 1 58  ? 26.148 16.053  12.143  1.00 20.97 ?  58  ASN   A OD1  1 
ATOM   1502 N  ND2  . ASN   A 1 58  ? 27.847 15.527  13.522  1.00 20.36 ?  58  ASN   A ND2  1 
ATOM   1503 H  H    . ASN   A 1 58  ? 24.657 11.749  11.203  1.00 15.88 ?  58  ASN   A H    1 
ATOM   1504 H  HA   . ASN   A 1 58  ? 25.221 13.789  11.044  1.00 16.59 ?  58  ASN   A HA   1 
ATOM   1505 H  HB2  . ASN   A 1 58  ? 25.610 13.653  13.356  1.00 19.54 ?  58  ASN   A HB2  1 
ATOM   1506 H  HB3  . ASN   A 1 58  ? 27.113 13.233  13.077  1.00 19.54 ?  58  ASN   A HB3  1 
ATOM   1507 H  HD21 . ASN   A 1 58  ? 28.119 16.343  13.573  1.00 24.45 ?  58  ASN   A HD21 1 
ATOM   1508 H  HD22 . ASN   A 1 58  ? 28.264 14.910  13.952  1.00 24.45 ?  58  ASN   A HD22 1 
ATOM   1509 N  N    . ASN   A 1 59  ? 27.068 12.533  9.278   1.00 11.99 ?  59  ASN   A N    1 
ATOM   1510 C  CA   . ASN   A 1 59  ? 28.057 12.501  8.188   1.00 11.69 ?  59  ASN   A CA   1 
ATOM   1511 C  C    . ASN   A 1 59  ? 29.373 11.825  8.589   1.00 11.25 ?  59  ASN   A C    1 
ATOM   1512 O  O    . ASN   A 1 59  ? 30.295 11.775  7.768   1.00 11.92 ?  59  ASN   A O    1 
ATOM   1513 C  CB   . ASN   A 1 59  ? 28.345 13.883  7.572   1.00 11.95 ?  59  ASN   A CB   1 
ATOM   1514 C  CG   . ASN   A 1 59  ? 28.709 13.806  6.108   1.00 12.18 ?  59  ASN   A CG   1 
ATOM   1515 O  OD1  . ASN   A 1 59  ? 27.996 13.188  5.310   1.00 12.36 ?  59  ASN   A OD1  1 
ATOM   1516 N  ND2  . ASN   A 1 59  ? 29.810 14.461  5.731   1.00 12.98 ?  59  ASN   A ND2  1 
ATOM   1517 H  H    . ASN   A 1 59  ? 26.451 11.942  9.163   1.00 14.41 ?  59  ASN   A H    1 
ATOM   1518 H  HA   . ASN   A 1 59  ? 27.681 11.969  7.478   1.00 14.05 ?  59  ASN   A HA   1 
ATOM   1519 H  HB2  . ASN   A 1 59  ? 27.557 14.444  7.648   1.00 14.36 ?  59  ASN   A HB2  1 
ATOM   1520 H  HB3  . ASN   A 1 59  ? 29.090 14.297  8.040   1.00 14.36 ?  59  ASN   A HB3  1 
ATOM   1521 H  HD21 . ASN   A 1 59  ? 30.066 14.454  4.906   1.00 15.60 ?  59  ASN   A HD21 1 
ATOM   1522 H  HD22 . ASN   A 1 59  ? 30.284 14.890  6.313   1.00 15.60 ?  59  ASN   A HD22 1 
ATOM   1523 N  N    . ALA   A 1 60  ? 29.485 11.281  9.799   1.00 11.44 ?  60  ALA   A N    1 
ATOM   1524 C  CA   . ALA   A 1 60  ? 30.723 10.604  10.168  1.00 11.87 ?  60  ALA   A CA   1 
ATOM   1525 C  C    . ALA   A 1 60  ? 30.954 9.362   9.315   1.00 11.76 ?  60  ALA   A C    1 
ATOM   1526 O  O    . ALA   A 1 60  ? 32.103 9.035   8.993   1.00 12.13 ?  60  ALA   A O    1 
ATOM   1527 C  CB   . ALA   A 1 60  ? 30.709 10.249  11.647  1.00 12.38 ?  60  ALA   A CB   1 
ATOM   1528 H  H    . ALA   A 1 60  ? 28.881 11.289  10.410  1.00 13.74 ?  60  ALA   A H    1 
ATOM   1529 H  HA   . ALA   A 1 60  ? 31.470 11.213  10.018  1.00 14.26 ?  60  ALA   A HA   1 
ATOM   1530 H  HB1  . ALA   A 1 60  ? 31.536 9.807   11.879  1.00 14.88 ?  60  ALA   A HB1  1 
ATOM   1531 H  HB2  . ALA   A 1 60  ? 30.615 11.069  12.168  1.00 14.88 ?  60  ALA   A HB2  1 
ATOM   1532 H  HB3  . ALA   A 1 60  ? 29.954 9.666   11.823  1.00 14.88 ?  60  ALA   A HB3  1 
ATOM   1533 N  N    . MET   A 1 61  ? 29.884 8.665   8.928   1.00 10.93 ?  61  MET   A N    1 
ATOM   1534 C  CA   . MET   A 1 61  ? 30.027 7.523   8.030   1.00 11.14 ?  61  MET   A CA   1 
ATOM   1535 C  C    . MET   A 1 61  ? 30.662 7.940   6.707   1.00 11.06 ?  61  MET   A C    1 
ATOM   1536 O  O    . MET   A 1 61  ? 31.565 7.266   6.202   1.00 11.49 ?  61  MET   A O    1 
ATOM   1537 C  CB   . MET   A 1 61  ? 28.663 6.866   7.814   1.00 11.07 ?  61  MET   A CB   1 
ATOM   1538 C  CG   . MET   A 1 61  ? 28.677 5.698   6.843   1.00 11.82 ?  61  MET   A CG   1 
ATOM   1539 S  SD   . MET   A 1 61  ? 27.049 4.958   6.617   1.00 12.97 ?  61  MET   A SD   1 
ATOM   1540 C  CE   . MET   A 1 61  ? 26.890 4.078   8.179   1.00 14.59 ?  61  MET   A CE   1 
ATOM   1541 H  H    . MET   A 1 61  ? 29.077 8.835   9.167   1.00 13.14 ?  61  MET   A H    1 
ATOM   1542 H  HA   . MET   A 1 61  ? 30.603 6.866   8.454   1.00 13.39 ?  61  MET   A HA   1 
ATOM   1543 H  HB2  . MET   A 1 61  ? 28.339 6.539   8.665   1.00 13.31 ?  61  MET   A HB2  1 
ATOM   1544 H  HB3  . MET   A 1 61  ? 28.051 7.531   7.463   1.00 13.31 ?  61  MET   A HB3  1 
ATOM   1545 H  HG2  . MET   A 1 61  ? 28.979 6.002   5.976   1.00 14.21 ?  61  MET   A HG2  1 
ATOM   1546 H  HG3  . MET   A 1 61  ? 29.271 5.011   7.183   1.00 14.21 ?  61  MET   A HG3  1 
ATOM   1547 H  HE1  . MET   A 1 61  ? 26.044 3.601   8.188   1.00 17.53 ?  61  MET   A HE1  1 
ATOM   1548 H  HE2  . MET   A 1 61  ? 27.624 3.455   8.268   1.00 17.53 ?  61  MET   A HE2  1 
ATOM   1549 H  HE3  . MET   A 1 61  ? 26.911 4.721   8.910   1.00 17.53 ?  61  MET   A HE3  1 
ATOM   1550 N  N    . GLN   A 1 62  ? 30.224 9.067   6.142   1.00 11.17 ?  62  GLN   A N    1 
ATOM   1551 C  CA   . GLN   A 1 62  ? 30.795 9.533   4.882   1.00 11.33 ?  62  GLN   A CA   1 
ATOM   1552 C  C    . GLN   A 1 62  ? 32.265 9.909   5.033   1.00 11.24 ?  62  GLN   A C    1 
ATOM   1553 O  O    . GLN   A 1 62  ? 33.079 9.593   4.160   1.00 11.60 ?  62  GLN   A O    1 
ATOM   1554 C  CB   . GLN   A 1 62  ? 30.000 10.719  4.339   1.00 11.34 ?  62  GLN   A CB   1 
ATOM   1555 C  CG   . GLN   A 1 62  ? 30.392 11.079  2.913   1.00 11.57 ?  62  GLN   A CG   1 
ATOM   1556 C  CD   . GLN   A 1 62  ? 30.058 9.955   1.967   1.00 11.69 ?  62  GLN   A CD   1 
ATOM   1557 O  OE1  . GLN   A 1 62  ? 28.880 9.658   1.743   1.00 12.43 ?  62  GLN   A OE1  1 
ATOM   1558 N  NE2  . GLN   A 1 62  ? 31.085 9.272   1.457   1.00 12.24 ?  62  GLN   A NE2  1 
ATOM   1559 H  H    . GLN   A 1 62  ? 29.605 9.567   6.466   1.00 13.42 ?  62  GLN   A H    1 
ATOM   1560 H  HA   . GLN   A 1 62  ? 30.742 8.812   4.238   1.00 13.61 ?  62  GLN   A HA   1 
ATOM   1561 H  HB2  . GLN   A 1 62  ? 29.057 10.500  4.350   1.00 13.63 ?  62  GLN   A HB2  1 
ATOM   1562 H  HB3  . GLN   A 1 62  ? 30.169 11.495  4.899   1.00 13.63 ?  62  GLN   A HB3  1 
ATOM   1563 H  HG2  . GLN   A 1 62  ? 29.892 11.857  2.631   1.00 13.91 ?  62  GLN   A HG2  1 
ATOM   1564 H  HG3  . GLN   A 1 62  ? 31.343 11.247  2.869   1.00 13.91 ?  62  GLN   A HG3  1 
ATOM   1565 H  HE21 . GLN   A 1 62  ? 31.895 9.500   1.653   1.00 14.71 ?  62  GLN   A HE21 1 
ATOM   1566 H  HE22 . GLN   A 1 62  ? 30.946 8.615   0.921   1.00 14.71 ?  62  GLN   A HE22 1 
ATOM   1567 N  N    . VAL   A 1 63  ? 32.621 10.590  6.126   1.00 11.84 ?  63  VAL   A N    1 
ATOM   1568 C  CA   . VAL   A 1 63  ? 34.014 10.978  6.344   1.00 12.76 ?  63  VAL   A CA   1 
ATOM   1569 C  C    . VAL   A 1 63  ? 34.905 9.742   6.419   1.00 12.00 ?  63  VAL   A C    1 
ATOM   1570 O  O    . VAL   A 1 63  ? 35.965 9.670   5.779   1.00 12.51 ?  63  VAL   A O    1 
ATOM   1571 C  CB   . VAL   A 1 63  ? 34.123 11.861  7.601   1.00 14.58 ?  63  VAL   A CB   1 
ATOM   1572 C  CG1  . VAL   A 1 63  ? 35.573 12.091  7.978   1.00 16.81 ?  63  VAL   A CG1  1 
ATOM   1573 C  CG2  . VAL   A 1 63  ? 33.407 13.193  7.372   1.00 14.68 ?  63  VAL   A CG2  1 
ATOM   1574 H  H    . VAL   A 1 63  ? 32.078 10.839  6.746   1.00 14.23 ?  63  VAL   A H    1 
ATOM   1575 H  HA   . VAL   A 1 63  ? 34.308 11.508  5.589   1.00 15.33 ?  63  VAL   A HA   1 
ATOM   1576 H  HB   . VAL   A 1 63  ? 33.690 11.418  8.343   1.00 17.51 ?  63  VAL   A HB   1 
ATOM   1577 H  HG11 . VAL   A 1 63  ? 35.617 12.832  8.606   1.00 20.19 ?  63  VAL   A HG11 1 
ATOM   1578 H  HG12 . VAL   A 1 63  ? 35.922 11.290  8.388   1.00 20.19 ?  63  VAL   A HG12 1 
ATOM   1579 H  HG13 . VAL   A 1 63  ? 36.073 12.311  7.178   1.00 20.19 ?  63  VAL   A HG13 1 
ATOM   1580 H  HG21 . VAL   A 1 63  ? 33.497 13.744  8.168   1.00 17.64 ?  63  VAL   A HG21 1 
ATOM   1581 H  HG22 . VAL   A 1 63  ? 33.810 13.646  6.614   1.00 17.64 ?  63  VAL   A HG22 1 
ATOM   1582 H  HG23 . VAL   A 1 63  ? 32.469 13.022  7.195   1.00 17.64 ?  63  VAL   A HG23 1 
ATOM   1583 N  N    . GLU   A 1 64  ? 34.474 8.739   7.187   1.00 11.75 ?  64  GLU   A N    1 
ATOM   1584 C  CA   . GLU   A 1 64  ? 35.241 7.505   7.291   1.00 11.97 ?  64  GLU   A CA   1 
ATOM   1585 C  C    . GLU   A 1 64  ? 35.340 6.812   5.941   1.00 11.58 ?  64  GLU   A C    1 
ATOM   1586 O  O    . GLU   A 1 64  ? 36.396 6.268   5.572   1.00 12.19 ?  64  GLU   A O    1 
ATOM   1587 C  CB   . GLU   A 1 64  ? 34.552 6.596   8.314   1.00 12.73 ?  64  GLU   A CB   1 
ATOM   1588 C  CG   . GLU   A 1 64  ? 35.201 5.244   8.461   1.00 13.45 ?  64  GLU   A CG   1 
ATOM   1589 C  CD   . GLU   A 1 64  ? 34.329 4.251   9.202   1.00 13.96 ?  64  GLU   A CD   1 
ATOM   1590 O  OE1  . GLU   A 1 64  ? 33.091 4.359   9.088   1.00 14.88 ?  64  GLU   A OE1  1 
ATOM   1591 O  OE2  . GLU   A 1 64  ? 34.894 3.361   9.883   1.00 14.31 -1 64  GLU   A OE2  1 
ATOM   1592 H  H    . GLU   A 1 64  ? 33.739 8.744   7.638   1.00 14.12 ?  64  GLU   A H    1 
ATOM   1593 H  HA   . GLU   A 1 64  ? 36.135 7.707   7.614   1.00 14.38 ?  64  GLU   A HA   1 
ATOM   1594 H  HB2  . GLU   A 1 64  ? 34.577 7.033   9.187   1.00 15.30 ?  64  GLU   A HB2  1 
ATOM   1595 H  HB3  . GLU   A 1 64  ? 33.630 6.470   8.044   1.00 15.30 ?  64  GLU   A HB3  1 
ATOM   1596 H  HG2  . GLU   A 1 64  ? 35.383 4.881   7.577   1.00 16.17 ?  64  GLU   A HG2  1 
ATOM   1597 H  HG3  . GLU   A 1 64  ? 36.022 5.346   8.952   1.00 16.17 ?  64  GLU   A HG3  1 
ATOM   1598 N  N    . SER   A 1 65  ? 34.228 6.807   5.201   1.00 11.31 ?  65  SER   A N    1 
ATOM   1599 C  CA   . SER   A 1 65  ? 34.176 6.142   3.904   1.00 11.40 ?  65  SER   A CA   1 
ATOM   1600 C  C    . SER   A 1 65  ? 35.102 6.801   2.893   1.00 11.54 ?  65  SER   A C    1 
ATOM   1601 O  O    . SER   A 1 65  ? 35.743 6.112   2.094   1.00 12.52 ?  65  SER   A O    1 
ATOM   1602 C  CB   . SER   A 1 65  ? 32.746 6.157   3.369   1.00 11.63 ?  65  SER   A CB   1 
ATOM   1603 O  OG   . SER   A 1 65  ? 31.886 5.341   4.165   1.00 11.85 ?  65  SER   A OG   1 
ATOM   1604 H  H    . SER   A 1 65  ? 33.490 7.185   5.431   1.00 13.59 ?  65  SER   A H    1 
ATOM   1605 H  HA   . SER   A 1 65  ? 34.456 5.220   4.007   1.00 13.71 ?  65  SER   A HA   1 
ATOM   1606 H  HB2  . SER   A 1 65  ? 32.414 7.064   3.374   1.00 13.97 ?  65  SER   A HB2  1 
ATOM   1607 H  HB3  . SER   A 1 65  ? 32.751 5.811   2.460   1.00 13.97 ?  65  SER   A HB3  1 
ATOM   1608 H  HG   . SER   A 1 65  ? 31.871 5.627   4.955   1.00 14.24 ?  65  SER   A HG   1 
ATOM   1609 N  N    . ASP   A 1 66  ? 35.172 8.137   2.893   1.00 11.88 ?  66  ASP   A N    1 
ATOM   1610 C  CA   . ASP   A 1 66  ? 36.049 8.823   1.950   1.00 12.63 ?  66  ASP   A CA   1 
ATOM   1611 C  C    . ASP   A 1 66  ? 37.511 8.473   2.209   1.00 12.51 ?  66  ASP   A C    1 
ATOM   1612 O  O    . ASP   A 1 66  ? 38.295 8.305   1.268   1.00 13.24 ?  66  ASP   A O    1 
ATOM   1613 C  CB   . ASP   A 1 66  ? 35.827 10.333  2.018   1.00 14.04 ?  66  ASP   A CB   1 
ATOM   1614 C  CG   . ASP   A 1 66  ? 34.491 10.778  1.408   1.00 16.00 ?  66  ASP   A CG   1 
ATOM   1615 O  OD1  . ASP   A 1 66  ? 33.795 9.978   0.744   1.00 16.32 ?  66  ASP   A OD1  1 
ATOM   1616 O  OD2  . ASP   A 1 66  ? 34.166 11.972  1.566   1.00 19.14 -1 66  ASP   A OD2  1 
ATOM   1617 H  H    . ASP   A 1 66  ? 34.719 8.661   3.411   1.00 14.28 ?  66  ASP   A H    1 
ATOM   1618 H  HA   . ASP   A 1 66  ? 35.828 8.534   1.051   1.00 15.17 ?  66  ASP   A HA   1 
ATOM   1619 H  HB2  . ASP   A 1 66  ? 35.838 10.611  2.947   1.00 16.86 ?  66  ASP   A HB2  1 
ATOM   1620 H  HB3  . ASP   A 1 66  ? 36.542 10.777  1.532   1.00 16.86 ?  66  ASP   A HB3  1 
ATOM   1621 N  N    . ASP   A 1 67  ? 37.895 8.360   3.481   1.00 12.51 ?  67  ASP   A N    1 
ATOM   1622 C  CA   . ASP   A 1 67  ? 39.250 7.917   3.800   1.00 13.31 ?  67  ASP   A CA   1 
ATOM   1623 C  C    . ASP   A 1 67  ? 39.481 6.484   3.333   1.00 13.45 ?  67  ASP   A C    1 
ATOM   1624 O  O    . ASP   A 1 67  ? 40.546 6.166   2.792   1.00 14.13 ?  67  ASP   A O    1 
ATOM   1625 C  CB   . ASP   A 1 67  ? 39.506 8.055   5.299   1.00 14.41 ?  67  ASP   A CB   1 
ATOM   1626 C  CG   . ASP   A 1 67  ? 40.803 7.409   5.725   1.00 16.02 ?  67  ASP   A CG   1 
ATOM   1627 O  OD1  . ASP   A 1 67  ? 41.868 8.061   5.620   1.00 19.03 ?  67  ASP   A OD1  1 
ATOM   1628 O  OD2  . ASP   A 1 67  ? 40.752 6.239   6.157   1.00 16.00 -1 67  ASP   A OD2  1 
ATOM   1629 H  H    . ASP   A 1 67  ? 37.403 8.544   4.161   1.00 15.04 ?  67  ASP   A H    1 
ATOM   1630 H  HA   . ASP   A 1 67  ? 39.885 8.486   3.340   1.00 15.99 ?  67  ASP   A HA   1 
ATOM   1631 H  HB2  . ASP   A 1 67  ? 39.548 8.995   5.527   1.00 17.31 ?  67  ASP   A HB2  1 
ATOM   1632 H  HB3  . ASP   A 1 67  ? 38.779 7.628   5.784   1.00 17.31 ?  67  ASP   A HB3  1 
ATOM   1633 N  N    . TYR   A 1 68  ? 38.484 5.606   3.513   1.00 13.06 ?  68  TYR   A N    1 
ATOM   1634 C  CA   . TYR   A 1 68  ? 38.613 4.226   3.041   1.00 13.06 ?  68  TYR   A CA   1 
ATOM   1635 C  C    . TYR   A 1 68  ? 38.855 4.173   1.531   1.00 12.78 ?  68  TYR   A C    1 
ATOM   1636 O  O    . TYR   A 1 68  ? 39.738 3.444   1.055   1.00 13.64 ?  68  TYR   A O    1 
ATOM   1637 C  CB   . TYR   A 1 68  ? 37.372 3.392   3.429   1.00 13.45 ?  68  TYR   A CB   1 
ATOM   1638 C  CG   . TYR   A 1 68  ? 37.403 2.006   2.800   1.00 15.04 ?  68  TYR   A CG   1 
ATOM   1639 C  CD1  . TYR   A 1 68  ? 36.941 1.811   1.503   1.00 16.79 ?  68  TYR   A CD1  1 
ATOM   1640 C  CD2  . TYR   A 1 68  ? 37.943 0.922   3.470   1.00 17.49 ?  68  TYR   A CD2  1 
ATOM   1641 C  CE1  . TYR   A 1 68  ? 37.013 0.601   0.886   1.00 18.25 ?  68  TYR   A CE1  1 
ATOM   1642 C  CE2  . TYR   A 1 68  ? 38.007 -0.333  2.854   1.00 18.65 ?  68  TYR   A CE2  1 
ATOM   1643 C  CZ   . TYR   A 1 68  ? 37.543 -0.470  1.561   1.00 18.80 ?  68  TYR   A CZ   1 
ATOM   1644 O  OH   . TYR   A 1 68  ? 37.628 -1.684  0.925   1.00 20.79 ?  68  TYR   A OH   1 
ATOM   1645 H  H    . TYR   A 1 68  ? 37.735 5.781   3.908   1.00 15.69 ?  68  TYR   A H    1 
ATOM   1646 H  HA   . TYR   A 1 68  ? 39.377 3.823   3.478   1.00 15.69 ?  68  TYR   A HA   1 
ATOM   1647 H  HB2  . TYR   A 1 68  ? 37.346 3.286   4.395   1.00 16.16 ?  68  TYR   A HB2  1 
ATOM   1648 H  HB3  . TYR   A 1 68  ? 36.571 3.848   3.123   1.00 16.16 ?  68  TYR   A HB3  1 
ATOM   1649 H  HD1  . TYR   A 1 68  ? 36.595 2.539   1.035   1.00 20.16 ?  68  TYR   A HD1  1 
ATOM   1650 H  HD2  . TYR   A 1 68  ? 38.274 1.027   4.330   1.00 21.01 ?  68  TYR   A HD2  1 
ATOM   1651 H  HE1  . TYR   A 1 68  ? 36.694 0.500   0.018   1.00 21.92 ?  68  TYR   A HE1  1 
ATOM   1652 H  HE2  . TYR   A 1 68  ? 38.377 -1.065  3.293   1.00 22.40 ?  68  TYR   A HE2  1 
ATOM   1653 H  HH   . TYR   A 1 68  ? 37.960 -2.255  1.439   1.00 24.97 ?  68  TYR   A HH   1 
ATOM   1654 N  N    . ILE   A 1 69  ? 38.068 4.928   0.757   1.00 12.48 ?  69  ILE   A N    1 
ATOM   1655 C  CA   . ILE   A 1 69  ? 38.208 4.916   -0.699  1.00 12.45 ?  69  ILE   A CA   1 
ATOM   1656 C  C    . ILE   A 1 69  ? 39.542 5.527   -1.123  1.00 12.59 ?  69  ILE   A C    1 
ATOM   1657 O  O    . ILE   A 1 69  ? 40.195 5.044   -2.054  1.00 12.96 ?  69  ILE   A O    1 
ATOM   1658 C  CB   . ILE   A 1 69  ? 37.013 5.620   -1.368  1.00 13.37 ?  69  ILE   A CB   1 
ATOM   1659 C  CG1  . ILE   A 1 69  ? 35.701 4.883   -1.089  1.00 14.07 ?  69  ILE   A CG1  1 
ATOM   1660 C  CG2  . ILE   A 1 69  ? 37.257 5.788   -2.868  1.00 15.08 ?  69  ILE   A CG2  1 
ATOM   1661 C  CD1  . ILE   A 1 69  ? 35.547 3.586   -1.843  1.00 14.96 ?  69  ILE   A CD1  1 
ATOM   1662 H  H    . ILE   A 1 69  ? 37.449 5.453   1.049   1.00 15.00 ?  69  ILE   A H    1 
ATOM   1663 H  HA   . ILE   A 1 69  ? 38.208 3.992   -0.997  1.00 14.96 ?  69  ILE   A HA   1 
ATOM   1664 H  HB   . ILE   A 1 69  ? 36.942 6.503   -0.987  1.00 16.06 ?  69  ILE   A HB   1 
ATOM   1665 H  HG12 . ILE   A 1 69  ? 35.654 4.685   -0.140  1.00 16.91 ?  69  ILE   A HG12 1 
ATOM   1666 H  HG13 . ILE   A 1 69  ? 34.963 5.463   -1.338  1.00 16.91 ?  69  ILE   A HG13 1 
ATOM   1667 H  HG21 . ILE   A 1 69  ? 36.414 5.981   -3.308  1.00 18.11 ?  69  ILE   A HG21 1 
ATOM   1668 H  HG22 . ILE   A 1 69  ? 37.874 6.528   -3.011  1.00 18.11 ?  69  ILE   A HG22 1 
ATOM   1669 H  HG23 . ILE   A 1 69  ? 37.636 4.971   -3.227  1.00 18.11 ?  69  ILE   A HG23 1 
ATOM   1670 H  HD11 . ILE   A 1 69  ? 34.750 3.136   -1.527  1.00 17.97 ?  69  ILE   A HD11 1 
ATOM   1671 H  HD12 . ILE   A 1 69  ? 35.463 3.780   -2.790  1.00 17.97 ?  69  ILE   A HD12 1 
ATOM   1672 H  HD13 . ILE   A 1 69  ? 36.325 3.033   -1.684  1.00 17.97 ?  69  ILE   A HD13 1 
ATOM   1673 N  N    . ALA   A 1 70  ? 39.957 6.602   -0.463  1.00 13.15 ?  70  ALA   A N    1 
ATOM   1674 C  CA   . ALA   A 1 70  ? 41.231 7.226   -0.806  1.00 14.20 ?  70  ALA   A CA   1 
ATOM   1675 C  C    . ALA   A 1 70  ? 42.393 6.259   -0.624  1.00 14.63 ?  70  ALA   A C    1 
ATOM   1676 O  O    . ALA   A 1 70  ? 43.388 6.335   -1.351  1.00 16.48 ?  70  ALA   A O    1 
ATOM   1677 C  CB   . ALA   A 1 70  ? 41.441 8.482   0.041   1.00 14.34 ?  70  ALA   A CB   1 
ATOM   1678 H  H    . ALA   A 1 70  ? 39.522 6.991   0.168   1.00 15.80 ?  70  ALA   A H    1 
ATOM   1679 H  HA   . ALA   A 1 70  ? 41.207 7.502   -1.740  1.00 17.05 ?  70  ALA   A HA   1 
ATOM   1680 H  HB1  . ALA   A 1 70  ? 42.296 8.882   -0.198  1.00 17.22 ?  70  ALA   A HB1  1 
ATOM   1681 H  HB2  . ALA   A 1 70  ? 40.725 9.108   -0.131  1.00 17.22 ?  70  ALA   A HB2  1 
ATOM   1682 H  HB3  . ALA   A 1 70  ? 41.448 8.230   0.978   1.00 17.22 ?  70  ALA   A HB3  1 
ATOM   1683 N  N    . THR   A 1 71  ? 42.278 5.335   0.323   1.00 14.28 ?  71  THR   A N    1 
ATOM   1684 C  CA   . THR   A 1 71  ? 43.329 4.361   0.592   1.00 15.90 ?  71  THR   A CA   1 
ATOM   1685 C  C    . THR   A 1 71  ? 43.223 3.123   -0.288  1.00 16.25 ?  71  THR   A C    1 
ATOM   1686 O  O    . THR   A 1 71  ? 44.243 2.612   -0.772  1.00 18.25 ?  71  THR   A O    1 
ATOM   1687 C  CB   . THR   A 1 71  ? 43.247 3.927   2.054   1.00 18.57 ?  71  THR   A CB   1 
ATOM   1688 O  OG1  . THR   A 1 71  ? 43.467 5.062   2.895   1.00 20.39 ?  71  THR   A OG1  1 
ATOM   1689 C  CG2  . THR   A 1 71  ? 44.268 2.835   2.372   1.00 19.99 ?  71  THR   A CG2  1 
ATOM   1690 H  H    . THR   A 1 71  ? 41.583 5.243   0.821   1.00 17.16 ?  71  THR   A H    1 
ATOM   1691 H  HA   . THR   A 1 71  ? 44.191 4.771   0.435   1.00 19.10 ?  71  THR   A HA   1 
ATOM   1692 H  HB   . THR   A 1 71  ? 42.360 3.568   2.224   1.00 22.30 ?  71  THR   A HB   1 
ATOM   1693 H  HG1  . THR   A 1 71  ? 42.879 5.640   2.750   1.00 24.49 ?  71  THR   A HG1  1 
ATOM   1694 H  HG21 . THR   A 1 71  ? 44.384 2.761   3.332   1.00 24.01 ?  71  THR   A HG21 1 
ATOM   1695 H  HG22 . THR   A 1 71  ? 43.968 1.978   2.026   1.00 24.01 ?  71  THR   A HG22 1 
ATOM   1696 H  HG23 . THR   A 1 71  ? 45.125 3.053   1.970   1.00 24.01 ?  71  THR   A HG23 1 
ATOM   1697 N  N    . ASN   A 1 72  ? 42.003 2.620   -0.498  1.00 15.05 ?  72  ASN   A N    1 
ATOM   1698 C  CA   . ASN   A 1 72  ? 41.792 1.295   -1.063  1.00 15.45 ?  72  ASN   A CA   1 
ATOM   1699 C  C    . ASN   A 1 72  ? 41.179 1.290   -2.452  1.00 15.36 ?  72  ASN   A C    1 
ATOM   1700 O  O    . ASN   A 1 72  ? 41.178 0.238   -3.102  1.00 16.71 ?  72  ASN   A O    1 
ATOM   1701 C  CB   . ASN   A 1 72  ? 40.899 0.475   -0.124  1.00 16.17 ?  72  ASN   A CB   1 
ATOM   1702 C  CG   . ASN   A 1 72  ? 41.510 0.326   1.243   1.00 17.49 ?  72  ASN   A CG   1 
ATOM   1703 O  OD1  . ASN   A 1 72  ? 41.055 0.923   2.215   1.00 19.08 ?  72  ASN   A OD1  1 
ATOM   1704 N  ND2  . ASN   A 1 72  ? 42.569 -0.447  1.321   1.00 18.39 ?  72  ASN   A ND2  1 
ATOM   1705 H  H    . ASN   A 1 72  ? 41.270 3.040   -0.318  1.00 18.08 ?  72  ASN   A H    1 
ATOM   1706 H  HA   . ASN   A 1 72  ? 42.646 0.848   -1.127  1.00 18.56 ?  72  ASN   A HA   1 
ATOM   1707 H  HB2  . ASN   A 1 72  ? 40.042 0.918   -0.031  1.00 19.42 ?  72  ASN   A HB2  1 
ATOM   1708 H  HB3  . ASN   A 1 72  ? 40.779 -0.412  -0.498  1.00 19.42 ?  72  ASN   A HB3  1 
ATOM   1709 H  HD21 . ASN   A 1 72  ? 42.962 -0.558  2.080   1.00 22.09 ?  72  ASN   A HD21 1 
ATOM   1710 H  HD22 . ASN   A 1 72  ? 42.867 -0.842  0.621   1.00 22.09 ?  72  ASN   A HD22 1 
ATOM   1711 N  N    . GLY   A 1 73  ? 40.634 2.407   -2.912  1.00 14.56 ?  73  GLY   A N    1 
ATOM   1712 C  CA   . GLY   A 1 73  ? 39.895 2.417   -4.149  1.00 14.47 ?  73  GLY   A CA   1 
ATOM   1713 C  C    . GLY   A 1 73  ? 38.507 1.832   -3.978  1.00 13.94 ?  73  GLY   A C    1 
ATOM   1714 O  O    . GLY   A 1 73  ? 38.114 1.394   -2.891  1.00 14.19 ?  73  GLY   A O    1 
ATOM   1715 H  H    . GLY   A 1 73  ? 40.684 3.184   -2.527  1.00 17.49 ?  73  GLY   A H    1 
ATOM   1716 H  HA2  . GLY   A 1 73  ? 39.815 3.334   -4.470  1.00 17.39 ?  73  GLY   A HA2  1 
ATOM   1717 H  HA3  . GLY   A 1 73  ? 40.370 1.899   -4.816  1.00 17.39 ?  73  GLY   A HA3  1 
ATOM   1718 N  N    . PRO   A 1 74  ? 37.732 1.837   -5.057  1.00 14.08 ?  74  PRO   A N    1 
ATOM   1719 C  CA   . PRO   A 1 74  ? 36.331 1.415   -4.976  1.00 14.33 ?  74  PRO   A CA   1 
ATOM   1720 C  C    . PRO   A 1 74  ? 36.178 -0.067  -4.660  1.00 13.77 ?  74  PRO   A C    1 
ATOM   1721 O  O    . PRO   A 1 74  ? 37.047 -0.899  -4.935  1.00 14.79 ?  74  PRO   A O    1 
ATOM   1722 C  CB   . PRO   A 1 74  ? 35.791 1.714   -6.378  1.00 15.94 ?  74  PRO   A CB   1 
ATOM   1723 C  CG   . PRO   A 1 74  ? 36.741 2.702   -6.971  1.00 18.91 ?  74  PRO   A CG   1 
ATOM   1724 C  CD   . PRO   A 1 74  ? 38.074 2.368   -6.386  1.00 16.28 ?  74  PRO   A CD   1 
ATOM   1725 H  HA   . PRO   A 1 74  ? 35.850 1.942   -4.314  1.00 17.22 ?  74  PRO   A HA   1 
ATOM   1726 H  HB2  . PRO   A 1 74  ? 35.775 0.895   -6.895  1.00 19.14 ?  74  PRO   A HB2  1 
ATOM   1727 H  HB3  . PRO   A 1 74  ? 34.902 2.093   -6.304  1.00 19.14 ?  74  PRO   A HB3  1 
ATOM   1728 H  HG2  . PRO   A 1 74  ? 36.759 2.600   -7.933  1.00 22.71 ?  74  PRO   A HG2  1 
ATOM   1729 H  HG3  . PRO   A 1 74  ? 36.477 3.599   -6.721  1.00 22.71 ?  74  PRO   A HG3  1 
ATOM   1730 H  HD2  . PRO   A 1 74  ? 38.522 1.688   -6.915  1.00 19.56 ?  74  PRO   A HD2  1 
ATOM   1731 H  HD3  . PRO   A 1 74  ? 38.617 3.171   -6.314  1.00 19.56 ?  74  PRO   A HD3  1 
ATOM   1732 N  N    . LEU   A 1 75  ? 35.021 -0.387  -4.089  1.00 12.85 ?  75  LEU   A N    1 
ATOM   1733 C  CA   . LEU   A 1 75  ? 34.621 -1.776  -3.942  1.00 12.17 ?  75  LEU   A CA   1 
ATOM   1734 C  C    . LEU   A 1 75  ? 34.242 -2.347  -5.306  1.00 12.47 ?  75  LEU   A C    1 
ATOM   1735 O  O    . LEU   A 1 75  ? 34.119 -1.630  -6.302  1.00 14.13 ?  75  LEU   A O    1 
ATOM   1736 C  CB   . LEU   A 1 75  ? 33.431 -1.896  -2.993  1.00 12.58 ?  75  LEU   A CB   1 
ATOM   1737 C  CG   . LEU   A 1 75  ? 33.638 -1.490  -1.538  1.00 14.25 ?  75  LEU   A CG   1 
ATOM   1738 C  CD1  . LEU   A 1 75  ? 32.356 -1.718  -0.745  1.00 16.38 ?  75  LEU   A CD1  1 
ATOM   1739 C  CD2  . LEU   A 1 75  ? 34.786 -2.206  -0.892  1.00 17.84 ?  75  LEU   A CD2  1 
ATOM   1740 H  H    . LEU   A 1 75  ? 34.448 0.180   -3.790  1.00 15.45 ?  75  LEU   A H    1 
ATOM   1741 H  HA   . LEU   A 1 75  ? 35.364 -2.289  -3.592  1.00 14.63 ?  75  LEU   A HA   1 
ATOM   1742 H  HB2  . LEU   A 1 75  ? 32.713 -1.356  -3.345  1.00 15.12 ?  75  LEU   A HB2  1 
ATOM   1743 H  HB3  . LEU   A 1 75  ? 33.155 -2.832  -2.991  1.00 15.12 ?  75  LEU   A HB3  1 
ATOM   1744 H  HG   . LEU   A 1 75  ? 33.839 -0.541  -1.513  1.00 17.13 ?  75  LEU   A HG   1 
ATOM   1745 H  HD11 . LEU   A 1 75  ? 32.504 -1.449  0.175   1.00 19.68 ?  75  LEU   A HD11 1 
ATOM   1746 H  HD12 . LEU   A 1 75  ? 31.648 -1.184  -1.137  1.00 19.68 ?  75  LEU   A HD12 1 
ATOM   1747 H  HD13 . LEU   A 1 75  ? 32.125 -2.658  -0.784  1.00 19.68 ?  75  LEU   A HD13 1 
ATOM   1748 H  HD21 . LEU   A 1 75  ? 34.829 -1.958  0.045   1.00 21.43 ?  75  LEU   A HD21 1 
ATOM   1749 H  HD22 . LEU   A 1 75  ? 34.653 -3.162  -0.976  1.00 21.43 ?  75  LEU   A HD22 1 
ATOM   1750 H  HD23 . LEU   A 1 75  ? 35.614 -1.949  -1.336  1.00 21.43 ?  75  LEU   A HD23 1 
ATOM   1751 N  N    . LYS   A 1 76  ? 34.064 -3.668  -5.330  1.00 13.01 ?  76  LYS   A N    1 
ATOM   1752 C  CA   . LYS   A 1 76  ? 33.475 -4.389  -6.449  1.00 13.58 ?  76  LYS   A CA   1 
ATOM   1753 C  C    . LYS   A 1 76  ? 31.964 -4.461  -6.264  1.00 12.11 ?  76  LYS   A C    1 
ATOM   1754 O  O    . LYS   A 1 76  ? 31.475 -4.575  -5.142  1.00 12.43 ?  76  LYS   A O    1 
ATOM   1755 C  CB   . LYS   A 1 76  ? 34.014 -5.830  -6.487  1.00 14.87 ?  76  LYS   A CB   1 
ATOM   1756 C  CG   . LYS   A 1 76  ? 35.517 -5.929  -6.729  1.00 16.31 ?  76  LYS   A CG   1 
ATOM   1757 C  CD   . LYS   A 1 76  ? 36.047 -7.330  -6.483  1.00 17.74 ?  76  LYS   A CD   1 
ATOM   1758 C  CE   . LYS   A 1 76  ? 37.544 -7.397  -6.694  1.00 20.00 ?  76  LYS   A CE   1 
ATOM   1759 N  NZ   . LYS   A 1 76  ? 38.089 -8.738  -6.424  1.00 21.26 ?  76  LYS   A NZ   1 
ATOM   1760 H  H    . LYS   A 1 76  ? 34.294 -4.189  -4.678  1.00 15.63 ?  76  LYS   A H    1 
ATOM   1761 H  HA   . LYS   A 1 76  ? 33.684 -3.947  -7.287  1.00 16.31 ?  76  LYS   A HA   1 
ATOM   1762 H  HB2  . LYS   A 1 76  ? 33.826 -6.256  -5.635  1.00 17.87 ?  76  LYS   A HB2  1 
ATOM   1763 H  HB3  . LYS   A 1 76  ? 33.568 -6.312  -7.200  1.00 17.87 ?  76  LYS   A HB3  1 
ATOM   1764 H  HG2  . LYS   A 1 76  ? 35.707 -5.693  -7.652  1.00 19.59 ?  76  LYS   A HG2  1 
ATOM   1765 H  HG3  . LYS   A 1 76  ? 35.979 -5.323  -6.129  1.00 19.59 ?  76  LYS   A HG3  1 
ATOM   1766 H  HD2  . LYS   A 1 76  ? 35.854 -7.588  -5.568  1.00 21.31 ?  76  LYS   A HD2  1 
ATOM   1767 H  HD3  . LYS   A 1 76  ? 35.622 -7.946  -7.102  1.00 21.31 ?  76  LYS   A HD3  1 
ATOM   1768 H  HE2  . LYS   A 1 76  ? 37.741 -7.170  -7.614  1.00 24.02 ?  76  LYS   A HE2  1 
ATOM   1769 H  HE3  . LYS   A 1 76  ? 37.973 -6.773  -6.092  1.00 24.02 ?  76  LYS   A HE3  1 
ATOM   1770 H  HZ1  . LYS   A 1 76  ? 38.970 -8.747  -6.559  1.00 25.53 ?  76  LYS   A HZ1  1 
ATOM   1771 H  HZ2  . LYS   A 1 76  ? 37.925 -8.979  -5.582  1.00 25.53 ?  76  LYS   A HZ2  1 
ATOM   1772 H  HZ3  . LYS   A 1 76  ? 37.714 -9.342  -6.969  1.00 25.53 ?  76  LYS   A HZ3  1 
ATOM   1773 N  N    . VAL   A 1 77  ? 31.224 -4.442  -7.377  1.00 12.72 ?  77  VAL   A N    1 
ATOM   1774 C  CA   . VAL   A 1 77  ? 29.814 -4.821  -7.296  1.00 12.54 ?  77  VAL   A CA   1 
ATOM   1775 C  C    . VAL   A 1 77  ? 29.744 -6.275  -6.850  1.00 12.26 ?  77  VAL   A C    1 
ATOM   1776 O  O    . VAL   A 1 77  ? 30.398 -7.148  -7.432  1.00 13.00 ?  77  VAL   A O    1 
ATOM   1777 C  CB   . VAL   A 1 77  ? 29.097 -4.616  -8.638  1.00 13.65 ?  77  VAL   A CB   1 
ATOM   1778 C  CG1  . VAL   A 1 77  ? 27.631 -5.026  -8.526  1.00 14.61 ?  77  VAL   A CG1  1 
ATOM   1779 C  CG2  . VAL   A 1 77  ? 29.216 -3.171  -9.095  1.00 14.85 ?  77  VAL   A CG2  1 
ATOM   1780 H  H    . VAL   A 1 77  ? 31.503 -4.215  -8.157  1.00 15.29 ?  77  VAL   A H    1 
ATOM   1781 H  HA   . VAL   A 1 77  ? 29.371 -4.275  -6.628  1.00 15.06 ?  77  VAL   A HA   1 
ATOM   1782 H  HB   . VAL   A 1 77  ? 29.516 -5.176  -9.310  1.00 16.40 ?  77  VAL   A HB   1 
ATOM   1783 H  HG11 . VAL   A 1 77  ? 27.161 -4.722  -9.317  1.00 17.55 ?  77  VAL   A HG11 1 
ATOM   1784 H  HG12 . VAL   A 1 77  ? 27.577 -5.989  -8.455  1.00 17.55 ?  77  VAL   A HG12 1 
ATOM   1785 H  HG13 . VAL   A 1 77  ? 27.252 -4.609  -7.735  1.00 17.55 ?  77  VAL   A HG13 1 
ATOM   1786 H  HG21 . VAL   A 1 77  ? 28.702 -3.055  -9.907  1.00 17.84 ?  77  VAL   A HG21 1 
ATOM   1787 H  HG22 . VAL   A 1 77  ? 28.872 -2.592  -8.397  1.00 17.84 ?  77  VAL   A HG22 1 
ATOM   1788 H  HG23 . VAL   A 1 77  ? 30.150 -2.969  -9.262  1.00 17.84 ?  77  VAL   A HG23 1 
ATOM   1789 N  N    . GLY   A 1 78  ? 28.970 -6.538  -5.798  1.00 11.88 ?  78  GLY   A N    1 
ATOM   1790 C  CA   . GLY   A 1 78  ? 28.945 -7.827  -5.139  1.00 12.62 ?  78  GLY   A CA   1 
ATOM   1791 C  C    . GLY   A 1 78  ? 29.850 -7.913  -3.929  1.00 12.09 ?  78  GLY   A C    1 
ATOM   1792 O  O    . GLY   A 1 78  ? 29.780 -8.912  -3.195  1.00 12.70 ?  78  GLY   A O    1 
ATOM   1793 H  H    . GLY   A 1 78  ? 28.434 -5.959  -5.445  1.00 14.27 ?  78  GLY   A H    1 
ATOM   1794 H  HA2  . GLY   A 1 78  ? 28.039 -8.017  -4.856  1.00 15.16 ?  78  GLY   A HA2  1 
ATOM   1795 H  HA3  . GLY   A 1 78  ? 29.218 -8.507  -5.771  1.00 15.16 ?  78  GLY   A HA3  1 
ATOM   1796 N  N    . GLY   A 1 79  ? 30.704 -6.905  -3.710  1.00 11.90 ?  79  GLY   A N    1 
ATOM   1797 C  CA   . GLY   A 1 79  ? 31.661 -6.914  -2.631  1.00 12.17 ?  79  GLY   A CA   1 
ATOM   1798 C  C    . GLY   A 1 79  ? 31.200 -6.121  -1.419  1.00 11.58 ?  79  GLY   A C    1 
ATOM   1799 O  O    . GLY   A 1 79  ? 30.080 -5.613  -1.345  1.00 12.24 ?  79  GLY   A O    1 
ATOM   1800 H  H    . GLY   A 1 79  ? 30.747 -6.191  -4.196  1.00 14.30 ?  79  GLY   A H    1 
ATOM   1801 H  HA2  . GLY   A 1 79  ? 31.822 -7.834  -2.356  1.00 14.63 ?  79  GLY   A HA2  1 
ATOM   1802 H  HA3  . GLY   A 1 79  ? 32.502 -6.543  -2.941  1.00 14.63 ?  79  GLY   A HA3  1 
ATOM   1803 N  N    . SER   A 1 80  ? 32.105 -6.027  -0.445  1.00 12.54 ?  80  SER   A N    1 
ATOM   1804 C  CA   . SER   A 1 80  ? 31.775 -5.399  0.826   1.00 11.97 ?  80  SER   A CA   1 
ATOM   1805 C  C    . SER   A 1 80  ? 33.040 -4.947  1.536   1.00 11.90 ?  80  SER   A C    1 
ATOM   1806 O  O    . SER   A 1 80  ? 34.154 -5.378  1.220   1.00 13.54 ?  80  SER   A O    1 
ATOM   1807 C  CB   . SER   A 1 80  ? 31.001 -6.358  1.737   1.00 12.94 ?  80  SER   A CB   1 
ATOM   1808 O  OG   . SER   A 1 80  ? 31.831 -7.402  2.228   1.00 14.65 ?  80  SER   A OG   1 
ATOM   1809 H  H    . SER   A 1 80  ? 32.917 -6.305  -0.499  1.00 15.06 ?  80  SER   A H    1 
ATOM   1810 H  HA   . SER   A 1 80  ? 31.222 -4.620  0.650   1.00 14.39 ?  80  SER   A HA   1 
ATOM   1811 H  HB2  . SER   A 1 80  ? 30.647 -5.862  2.491   1.00 15.55 ?  80  SER   A HB2  1 
ATOM   1812 H  HB3  . SER   A 1 80  ? 30.270 -6.751  1.232   1.00 15.55 ?  80  SER   A HB3  1 
ATOM   1813 H  HG   . SER   A 1 80  ? 32.141 -7.849  1.586   1.00 17.60 ?  80  SER   A HG   1 
ATOM   1814 N  N    . CYS   A 1 81  ? 32.843 -4.098  2.538   1.00 11.64 ?  81  CYS   A N    1 
ATOM   1815 C  CA   . CYS   A 1 81  ? 33.887 -3.807  3.508   1.00 11.85 ?  81  CYS   A CA   1 
ATOM   1816 C  C    . CYS   A 1 81  ? 33.238 -3.569  4.863   1.00 11.45 ?  81  CYS   A C    1 
ATOM   1817 O  O    . CYS   A 1 81  ? 32.071 -3.165  4.944   1.00 12.73 ?  81  CYS   A O    1 
ATOM   1818 C  CB   . CYS   A 1 81  ? 34.757 -2.616  3.100   1.00 12.51 ?  81  CYS   A CB   1 
ATOM   1819 S  SG   . CYS   A 1 81  ? 33.862 -1.042  3.091   1.00 12.55 ?  81  CYS   A SG   1 
ATOM   1820 H  H    . CYS   A 1 81  ? 32.106 -3.677  2.684   1.00 13.99 ?  81  CYS   A H    1 
ATOM   1821 H  HA   . CYS   A 1 81  ? 34.469 -4.578  3.585   1.00 14.24 ?  81  CYS   A HA   1 
ATOM   1822 H  HB2  . CYS   A 1 81  ? 35.502 -2.538  3.723   1.00 15.03 ?  81  CYS   A HB2  1 
ATOM   1823 H  HB3  . CYS   A 1 81  ? 35.105 -2.768  2.203   1.00 15.03 ?  81  CYS   A HB3  1 
ATOM   1824 H  HG   . CYS   A 1 81  ? 34.617 -0.166  2.766   1.00 15.08 ?  81  CYS   A HG   1 
ATOM   1825 N  N    . VAL   A 1 82  ? 33.998 -3.834  5.923   1.00 12.06 ?  82  VAL   A N    1 
ATOM   1826 C  CA   . VAL   A 1 82  ? 33.566 -3.593  7.293   1.00 12.25 ?  82  VAL   A CA   1 
ATOM   1827 C  C    . VAL   A 1 82  ? 34.166 -2.280  7.767   1.00 12.54 ?  82  VAL   A C    1 
ATOM   1828 O  O    . VAL   A 1 82  ? 35.392 -2.116  7.761   1.00 13.30 ?  82  VAL   A O    1 
ATOM   1829 C  CB   . VAL   A 1 82  ? 33.988 -4.738  8.226   1.00 13.86 ?  82  VAL   A CB   1 
ATOM   1830 C  CG1  . VAL   A 1 82  ? 33.560 -4.451  9.660   1.00 15.38 ?  82  VAL   A CG1  1 
ATOM   1831 C  CG2  . VAL   A 1 82  ? 33.422 -6.058  7.752   1.00 14.99 ?  82  VAL   A CG2  1 
ATOM   1832 H  H    . VAL   A 1 82  ? 34.792 -4.182  5.870   1.00 14.50 ?  82  VAL   A H    1 
ATOM   1833 H  HA   . VAL   A 1 82  ? 32.600 -3.514  7.314   1.00 14.72 ?  82  VAL   A HA   1 
ATOM   1834 H  HB   . VAL   A 1 82  ? 34.954 -4.805  8.216   1.00 16.65 ?  82  VAL   A HB   1 
ATOM   1835 H  HG11 . VAL   A 1 82  ? 33.662 -5.257  10.187  1.00 18.48 ?  82  VAL   A HG11 1 
ATOM   1836 H  HG12 . VAL   A 1 82  ? 34.118 -3.745  10.028  1.00 18.48 ?  82  VAL   A HG12 1 
ATOM   1837 H  HG13 . VAL   A 1 82  ? 32.630 -4.169  9.664   1.00 18.48 ?  82  VAL   A HG13 1 
ATOM   1838 H  HG21 . VAL   A 1 82  ? 33.662 -6.749  8.387   1.00 18.01 ?  82  VAL   A HG21 1 
ATOM   1839 H  HG22 . VAL   A 1 82  ? 32.456 -5.984  7.693   1.00 18.01 ?  82  VAL   A HG22 1 
ATOM   1840 H  HG23 . VAL   A 1 82  ? 33.791 -6.265  6.880   1.00 18.01 ?  82  VAL   A HG23 1 
ATOM   1841 N  N    . LEU   A 1 83  ? 33.310 -1.350  8.182   1.00 12.35 ?  83  LEU   A N    1 
ATOM   1842 C  CA   . LEU   A 1 83  ? 33.727 -0.085  8.763   1.00 12.12 ?  83  LEU   A CA   1 
ATOM   1843 C  C    . LEU   A 1 83  ? 33.006 0.100   10.094  1.00 12.26 ?  83  LEU   A C    1 
ATOM   1844 O  O    . LEU   A 1 83  ? 32.271 -0.779  10.556  1.00 12.98 ?  83  LEU   A O    1 
ATOM   1845 C  CB   . LEU   A 1 83  ? 33.485 1.074   7.785   1.00 12.72 ?  83  LEU   A CB   1 
ATOM   1846 C  CG   . LEU   A 1 83  ? 34.382 1.061   6.537   1.00 13.54 ?  83  LEU   A CG   1 
ATOM   1847 C  CD1  . LEU   A 1 83  ? 33.950 2.123   5.544   1.00 14.24 ?  83  LEU   A CD1  1 
ATOM   1848 C  CD2  . LEU   A 1 83  ? 35.856 1.252   6.910   1.00 14.31 ?  83  LEU   A CD2  1 
ATOM   1849 H  H    . LEU   A 1 83  ? 32.458 -1.430  8.131   1.00 14.84 ?  83  LEU   A H    1 
ATOM   1850 H  HA   . LEU   A 1 83  ? 34.682 -0.110  8.940   1.00 14.57 ?  83  LEU   A HA   1 
ATOM   1851 H  HB2  . LEU   A 1 83  ? 32.563 1.044   7.479   1.00 15.28 ?  83  LEU   A HB2  1 
ATOM   1852 H  HB3  . LEU   A 1 83  ? 33.640 1.918   8.242   1.00 15.28 ?  83  LEU   A HB3  1 
ATOM   1853 H  HG   . LEU   A 1 83  ? 34.293 0.202   6.100   1.00 16.26 ?  83  LEU   A HG   1 
ATOM   1854 H  HD11 . LEU   A 1 83  ? 34.530 2.086   4.766   1.00 17.11 ?  83  LEU   A HD11 1 
ATOM   1855 H  HD12 . LEU   A 1 83  ? 33.031 1.955   5.278   1.00 17.11 ?  83  LEU   A HD12 1 
ATOM   1856 H  HD13 . LEU   A 1 83  ? 34.017 2.996   5.962   1.00 17.11 ?  83  LEU   A HD13 1 
ATOM   1857 H  HD21 . LEU   A 1 83  ? 36.372 1.404   6.100   1.00 17.19 ?  83  LEU   A HD21 1 
ATOM   1858 H  HD22 . LEU   A 1 83  ? 35.938 2.020   7.498   1.00 17.19 ?  83  LEU   A HD22 1 
ATOM   1859 H  HD23 . LEU   A 1 83  ? 36.175 0.456   7.360   1.00 17.19 ?  83  LEU   A HD23 1 
ATOM   1860 N  N    . SER   A 1 84  ? 33.221 1.252   10.721  1.00 13.17 ?  84  SER   A N    1 
ATOM   1861 C  CA   . SER   A 1 84  ? 32.569 1.515   11.993  1.00 13.22 ?  84  SER   A CA   1 
ATOM   1862 C  C    . SER   A 1 84  ? 31.051 1.604   11.829  1.00 13.05 ?  84  SER   A C    1 
ATOM   1863 O  O    . SER   A 1 84  ? 30.537 2.055   10.806  1.00 13.38 ?  84  SER   A O    1 
ATOM   1864 C  CB   . SER   A 1 84  ? 33.074 2.832   12.568  1.00 14.56 ?  84  SER   A CB   1 
ATOM   1865 O  OG   . SER   A 1 84  ? 32.435 3.132   13.790  1.00 15.42 ?  84  SER   A OG   1 
ATOM   1866 H  H    . SER   A 1 84  ? 33.728 1.891   10.433  1.00 15.83 ?  84  SER   A H    1 
ATOM   1867 H  HA   . SER   A 1 84  ? 32.779 0.798   12.613  1.00 15.88 ?  84  SER   A HA   1 
ATOM   1868 H  HB2  . SER   A 1 84  ? 34.033 2.767   12.706  1.00 17.49 ?  84  SER   A HB2  1 
ATOM   1869 H  HB3  . SER   A 1 84  ? 32.880 3.543   11.938  1.00 17.49 ?  84  SER   A HB3  1 
ATOM   1870 H  HG   . SER   A 1 84  ? 32.737 3.852   14.104  1.00 18.52 ?  84  SER   A HG   1 
ATOM   1871 N  N    . GLY   A 1 85  ? 30.329 1.199   12.873  1.00 14.07 ?  85  GLY   A N    1 
ATOM   1872 C  CA   . GLY   A 1 85  ? 28.904 1.433   12.947  1.00 14.64 ?  85  GLY   A CA   1 
ATOM   1873 C  C    . GLY   A 1 85  ? 28.528 2.752   13.585  1.00 14.43 ?  85  GLY   A C    1 
ATOM   1874 O  O    . GLY   A 1 85  ? 27.336 3.068   13.681  1.00 15.16 ?  85  GLY   A O    1 
ATOM   1875 H  H    . GLY   A 1 85  ? 30.650 0.778   13.554  1.00 16.90 ?  85  GLY   A H    1 
ATOM   1876 H  HA2  . GLY   A 1 85  ? 28.536 1.421   12.048  1.00 17.59 ?  85  GLY   A HA2  1 
ATOM   1877 H  HA3  . GLY   A 1 85  ? 28.489 0.722   13.452  1.00 17.59 ?  85  GLY   A HA3  1 
ATOM   1878 N  N    . HIS   A 1 86  ? 29.510 3.530   14.034  1.00 13.90 ?  86  HIS   A N    1 
ATOM   1879 C  CA   . HIS   A 1 86  ? 29.281 4.870   14.590  1.00 14.47 ?  86  HIS   A CA   1 
ATOM   1880 C  C    . HIS   A 1 86  ? 28.287 4.754   15.738  1.00 14.83 ?  86  HIS   A C    1 
ATOM   1881 O  O    . HIS   A 1 86  ? 28.472 3.893   16.611  1.00 16.47 ?  86  HIS   A O    1 
ATOM   1882 C  CB   . HIS   A 1 86  ? 28.912 5.833   13.471  1.00 14.77 ?  86  HIS   A CB   1 
ATOM   1883 C  CG   . HIS   A 1 86  ? 29.980 5.931   12.443  1.00 14.46 ?  86  HIS   A CG   1 
ATOM   1884 N  ND1  . HIS   A 1 86  ? 31.065 6.770   12.584  1.00 16.19 ?  86  HIS   A ND1  1 
ATOM   1885 C  CD2  . HIS   A 1 86  ? 30.183 5.234   11.302  1.00 14.17 ?  86  HIS   A CD2  1 
ATOM   1886 C  CE1  . HIS   A 1 86  ? 31.879 6.598   11.559  1.00 16.04 ?  86  HIS   A CE1  1 
ATOM   1887 N  NE2  . HIS   A 1 86  ? 31.371 5.668   10.772  1.00 15.09 ?  86  HIS   A NE2  1 
ATOM   1888 H  H    . HIS   A 1 86  ? 30.337 3.305   14.028  1.00 16.71 ?  86  HIS   A H    1 
ATOM   1889 H  HA   . HIS   A 1 86  ? 30.113 5.185   14.964  1.00 17.38 ?  86  HIS   A HA   1 
ATOM   1890 H  HB2  . HIS   A 1 86  ? 28.098 5.530   13.034  1.00 17.75 ?  86  HIS   A HB2  1 
ATOM   1891 H  HB3  . HIS   A 1 86  ? 28.773 6.722   13.841  1.00 17.75 ?  86  HIS   A HB3  1 
ATOM   1892 H  HD2  . HIS   A 1 86  ? 29.627 4.576   10.941  1.00 17.02 ?  86  HIS   A HD2  1 
ATOM   1893 H  HE1  . HIS   A 1 86  ? 32.673 7.057   11.406  1.00 19.26 ?  86  HIS   A HE1  1 
ATOM   1894 H  HE2  . HIS   A 1 86  ? 31.719 5.394   10.026  1.00 18.12 ?  86  HIS   A HE2  1 
ATOM   1895 N  N    . ASN   A 1 87  ? 27.260 5.591   15.785  1.00 16.02 ?  87  ASN   A N    1 
ATOM   1896 C  CA   . ASN   A 1 87  ? 26.271 5.585   16.846  1.00 16.93 ?  87  ASN   A CA   1 
ATOM   1897 C  C    . ASN   A 1 87  ? 25.143 4.593   16.598  1.00 17.96 ?  87  ASN   A C    1 
ATOM   1898 O  O    . ASN   A 1 87  ? 24.208 4.531   17.399  1.00 20.54 ?  87  ASN   A O    1 
ATOM   1899 C  CB   . ASN   A 1 87  ? 25.683 6.995   17.003  1.00 17.87 ?  87  ASN   A CB   1 
ATOM   1900 C  CG   . ASN   A 1 87  ? 25.164 7.564   15.689  1.00 18.39 ?  87  ASN   A CG   1 
ATOM   1901 O  OD1  . ASN   A 1 87  ? 25.811 7.454   14.650  1.00 18.94 ?  87  ASN   A OD1  1 
ATOM   1902 N  ND2  . ASN   A 1 87  ? 23.992 8.175   15.734  1.00 19.54 ?  87  ASN   A ND2  1 
ATOM   1903 H  H    . ASN   A 1 87  ? 27.108 6.191   15.190  1.00 19.25 ?  87  ASN   A H    1 
ATOM   1904 H  HA   . ASN   A 1 87  ? 26.701 5.342   17.686  1.00 20.34 ?  87  ASN   A HA   1 
ATOM   1905 H  HB2  . ASN   A 1 87  ? 24.943 6.958   17.633  1.00 21.46 ?  87  ASN   A HB2  1 
ATOM   1906 H  HB3  . ASN   A 1 87  ? 26.373 7.587   17.337  1.00 21.46 ?  87  ASN   A HB3  1 
ATOM   1907 H  HD21 . ASN   A 1 87  ? 23.657 8.510   15.019  1.00 23.47 ?  87  ASN   A HD21 1 
ATOM   1908 H  HD22 . ASN   A 1 87  ? 23.572 8.243   16.482  1.00 23.47 ?  87  ASN   A HD22 1 
ATOM   1909 N  N    A LEU   A 1 88  ? 25.214 3.814   15.522  0.62 16.61 ?  88  LEU   A N    1 
ATOM   1910 N  N    B LEU   A 1 88  ? 25.211 3.806   15.524  0.38 17.25 ?  88  LEU   A N    1 
ATOM   1911 C  CA   A LEU   A 1 88  ? 24.113 2.945   15.119  0.62 16.42 ?  88  LEU   A CA   1 
ATOM   1912 C  CA   B LEU   A 1 88  ? 24.103 2.948   15.127  0.38 17.20 ?  88  LEU   A CA   1 
ATOM   1913 C  C    A LEU   A 1 88  ? 24.337 1.474   15.441  0.62 16.25 ?  88  LEU   A C    1 
ATOM   1914 C  C    B LEU   A 1 88  ? 24.337 1.464   15.376  0.38 16.69 ?  88  LEU   A C    1 
ATOM   1915 O  O    A LEU   A 1 88  ? 23.362 0.742   15.646  0.62 17.26 ?  88  LEU   A O    1 
ATOM   1916 O  O    B LEU   A 1 88  ? 23.362 0.709   15.456  0.38 16.99 ?  88  LEU   A O    1 
ATOM   1917 C  CB   A LEU   A 1 88  ? 23.878 3.082   13.613  0.62 16.76 ?  88  LEU   A CB   1 
ATOM   1918 C  CB   B LEU   A 1 88  ? 23.802 3.143   13.635  0.38 17.81 ?  88  LEU   A CB   1 
ATOM   1919 C  CG   A LEU   A 1 88  ? 23.581 4.493   13.103  0.62 18.01 ?  88  LEU   A CG   1 
ATOM   1920 C  CG   B LEU   A 1 88  ? 23.527 4.587   13.202  0.38 18.53 ?  88  LEU   A CG   1 
ATOM   1921 C  CD1  A LEU   A 1 88  ? 23.467 4.478   11.589  0.62 18.24 ?  88  LEU   A CD1  1 
ATOM   1922 C  CD1  B LEU   A 1 88  ? 23.370 4.691   11.691  0.38 18.77 ?  88  LEU   A CD1  1 
ATOM   1923 C  CD2  A LEU   A 1 88  ? 22.313 5.053   13.741  0.62 19.41 ?  88  LEU   A CD2  1 
ATOM   1924 C  CD2  B LEU   A 1 88  ? 22.297 5.136   13.908  0.38 19.01 ?  88  LEU   A CD2  1 
ATOM   1925 H  H    A LEU   A 1 88  ? 25.903 3.767   15.011  0.62 19.96 ?  88  LEU   A H    1 
ATOM   1926 H  H    B LEU   A 1 88  ? 25.898 3.750   15.014  0.38 20.72 ?  88  LEU   A H    1 
ATOM   1927 H  HA   A LEU   A 1 88  ? 23.307 3.229   15.574  0.62 19.73 ?  88  LEU   A HA   1 
ATOM   1928 H  HA   B LEU   A 1 88  ? 23.313 3.213   15.626  0.38 20.66 ?  88  LEU   A HA   1 
ATOM   1929 H  HB2  A LEU   A 1 88  ? 24.667 2.774   13.147  0.62 20.14 ?  88  LEU   A HB2  1 
ATOM   1930 H  HB2  B LEU   A 1 88  ? 24.562 2.826   13.126  0.38 21.40 ?  88  LEU   A HB2  1 
ATOM   1931 H  HB3  A LEU   A 1 88  ? 23.119 2.530   13.371  0.62 20.14 ?  88  LEU   A HB3  1 
ATOM   1932 H  HB3  B LEU   A 1 88  ? 23.018 2.618   13.412  0.38 21.40 ?  88  LEU   A HB3  1 
ATOM   1933 H  HG   A LEU   A 1 88  ? 24.316 5.079   13.339  0.62 21.63 ?  88  LEU   A HG   1 
ATOM   1934 H  HG   B LEU   A 1 88  ? 24.282 5.138   13.457  0.38 22.25 ?  88  LEU   A HG   1 
ATOM   1935 H  HD11 A LEU   A 1 88  ? 23.282 5.377   11.275  0.62 21.91 ?  88  LEU   A HD11 1 
ATOM   1936 H  HD11 B LEU   A 1 88  ? 23.204 5.618   11.453  0.38 22.54 ?  88  LEU   A HD11 1 
ATOM   1937 H  HD12 A LEU   A 1 88  ? 24.303 4.162   11.213  0.62 21.91 ?  88  LEU   A HD12 1 
ATOM   1938 H  HD12 B LEU   A 1 88  ? 24.186 4.383   11.266  0.38 22.54 ?  88  LEU   A HD12 1 
ATOM   1939 H  HD13 A LEU   A 1 88  ? 22.743 3.884   11.333  0.62 21.91 ?  88  LEU   A HD13 1 
ATOM   1940 H  HD13 B LEU   A 1 88  ? 22.623 4.140   11.410  0.38 22.54 ?  88  LEU   A HD13 1 
ATOM   1941 H  HD21 A LEU   A 1 88  ? 22.100 5.904   13.326  0.62 23.31 ?  88  LEU   A HD21 1 
ATOM   1942 H  HD21 B LEU   A 1 88  ? 22.087 6.007   13.538  0.38 22.84 ?  88  LEU   A HD21 1 
ATOM   1943 H  HD22 A LEU   A 1 88  ? 21.588 4.425   13.601  0.62 23.31 ?  88  LEU   A HD22 1 
ATOM   1944 H  HD22 B LEU   A 1 88  ? 21.557 4.527   13.765  0.38 22.84 ?  88  LEU   A HD22 1 
ATOM   1945 H  HD23 A LEU   A 1 88  ? 22.467 5.177   14.690  0.62 23.31 ?  88  LEU   A HD23 1 
ATOM   1946 H  HD23 B LEU   A 1 88  ? 22.487 5.213   14.854  0.38 22.84 ?  88  LEU   A HD23 1 
ATOM   1947 N  N    . ALA   A 1 89  ? 25.588 1.031   15.487  1.00 16.00 ?  89  ALA   A N    1 
ATOM   1948 C  CA   . ALA   A 1 89  ? 25.927 -0.381  15.594  1.00 15.47 ?  89  ALA   A CA   1 
ATOM   1949 C  C    . ALA   A 1 89  ? 27.407 -0.450  15.928  1.00 15.78 ?  89  ALA   A C    1 
ATOM   1950 O  O    . ALA   A 1 89  ? 28.124 0.546   15.819  1.00 16.50 ?  89  ALA   A O    1 
ATOM   1951 C  CB   . ALA   A 1 89  ? 25.678 -1.094  14.266  1.00 14.83 ?  89  ALA   A CB   1 
ATOM   1952 H  H    A ALA   A 1 89  ? 26.275 1.548   15.465  0.62 19.22 ?  89  ALA   A H    1 
ATOM   1953 H  H    B ALA   A 1 89  ? 26.273 1.551   15.489  0.38 19.22 ?  89  ALA   A H    1 
ATOM   1954 H  HA   . ALA   A 1 89  ? 25.407 -0.803  16.298  1.00 18.59 ?  89  ALA   A HA   1 
ATOM   1955 H  HB1  . ALA   A 1 89  ? 25.925 -2.026  14.356  1.00 17.82 ?  89  ALA   A HB1  1 
ATOM   1956 H  HB2  . ALA   A 1 89  ? 24.738 -1.020  14.033  1.00 17.82 ?  89  ALA   A HB2  1 
ATOM   1957 H  HB3  . ALA   A 1 89  ? 26.221 -0.674  13.577  1.00 17.82 ?  89  ALA   A HB3  1 
ATOM   1958 N  N    . LYS   A 1 90  ? 27.878 -1.628  16.328  1.00 16.01 ?  90  LYS   A N    1 
ATOM   1959 C  CA   . LYS   A 1 90  ? 29.323 -1.779  16.482  1.00 17.05 ?  90  LYS   A CA   1 
ATOM   1960 C  C    . LYS   A 1 90  ? 30.028 -1.590  15.142  1.00 15.92 ?  90  LYS   A C    1 
ATOM   1961 O  O    . LYS   A 1 90  ? 30.962 -0.779  15.021  1.00 17.06 ?  90  LYS   A O    1 
ATOM   1962 C  CB   . LYS   A 1 90  ? 29.668 -3.136  17.092  1.00 20.13 ?  90  LYS   A CB   1 
ATOM   1963 C  CG   . LYS   A 1 90  ? 31.150 -3.274  17.425  1.00 26.12 ?  90  LYS   A CG   1 
ATOM   1964 C  CD   . LYS   A 1 90  ? 31.405 -4.470  18.331  1.00 32.95 ?  90  LYS   A CD   1 
ATOM   1965 C  CE   . LYS   A 1 90  ? 32.826 -4.472  18.883  1.00 38.41 ?  90  LYS   A CE   1 
ATOM   1966 N  NZ   . LYS   A 1 90  ? 33.822 -4.979  17.899  1.00 41.44 ?  90  LYS   A NZ   1 
ATOM   1967 H  H    . LYS   A 1 90  ? 27.401 -2.315  16.523  1.00 19.24 ?  90  LYS   A H    1 
ATOM   1968 H  HA   . LYS   A 1 90  ? 29.645 -1.091  17.082  1.00 20.48 ?  90  LYS   A HA   1 
ATOM   1969 H  HB2  . LYS   A 1 90  ? 29.162 -3.250  17.915  1.00 24.17 ?  90  LYS   A HB2  1 
ATOM   1970 H  HB3  . LYS   A 1 90  ? 29.434 -3.836  16.463  1.00 24.17 ?  90  LYS   A HB3  1 
ATOM   1971 H  HG2  . LYS   A 1 90  ? 31.654 -3.398  16.605  1.00 31.37 ?  90  LYS   A HG2  1 
ATOM   1972 H  HG3  . LYS   A 1 90  ? 31.451 -2.473  17.885  1.00 31.37 ?  90  LYS   A HG3  1 
ATOM   1973 H  HD2  . LYS   A 1 90  ? 30.789 -4.440  19.080  1.00 39.56 ?  90  LYS   A HD2  1 
ATOM   1974 H  HD3  . LYS   A 1 90  ? 31.276 -5.287  17.824  1.00 39.56 ?  90  LYS   A HD3  1 
ATOM   1975 H  HE2  . LYS   A 1 90  ? 33.075 -3.564  19.121  1.00 46.11 ?  90  LYS   A HE2  1 
ATOM   1976 H  HE3  . LYS   A 1 90  ? 32.860 -5.041  19.667  1.00 46.11 ?  90  LYS   A HE3  1 
ATOM   1977 H  HZ1  . LYS   A 1 90  ? 33.600 -5.802  17.640  1.00 49.74 ?  90  LYS   A HZ1  1 
ATOM   1978 H  HZ2  . LYS   A 1 90  ? 33.845 -4.447  17.187  1.00 49.74 ?  90  LYS   A HZ2  1 
ATOM   1979 H  HZ3  . LYS   A 1 90  ? 34.631 -5.002  18.271  1.00 49.74 ?  90  LYS   A HZ3  1 
ATOM   1980 N  N    . HIS   A 1 91  ? 29.571 -2.315  14.121  1.00 14.04 ?  91  HIS   A N    1 
ATOM   1981 C  CA   . HIS   A 1 91  ? 30.155 -2.304  12.797  1.00 13.61 ?  91  HIS   A CA   1 
ATOM   1982 C  C    . HIS   A 1 91  ? 29.075 -2.034  11.768  1.00 12.10 ?  91  HIS   A C    1 
ATOM   1983 O  O    . HIS   A 1 91  ? 27.905 -2.387  11.954  1.00 13.38 ?  91  HIS   A O    1 
ATOM   1984 C  CB   . HIS   A 1 91  ? 30.761 -3.665  12.440  1.00 16.27 ?  91  HIS   A CB   1 
ATOM   1985 C  CG   . HIS   A 1 91  ? 31.747 -4.172  13.440  1.00 20.40 ?  91  HIS   A CG   1 
ATOM   1986 N  ND1  . HIS   A 1 91  ? 33.032 -3.683  13.530  1.00 22.53 ?  91  HIS   A ND1  1 
ATOM   1987 C  CD2  . HIS   A 1 91  ? 31.643 -5.133  14.388  1.00 22.52 ?  91  HIS   A CD2  1 
ATOM   1988 C  CE1  . HIS   A 1 91  ? 33.678 -4.320  14.492  1.00 23.62 ?  91  HIS   A CE1  1 
ATOM   1989 N  NE2  . HIS   A 1 91  ? 32.857 -5.205  15.028  1.00 23.91 ?  91  HIS   A NE2  1 
ATOM   1990 H  H    . HIS   A 1 91  ? 28.892 -2.858  14.186  1.00 16.87 ?  91  HIS   A H    1 
ATOM   1991 H  HA   . HIS   A 1 91  ? 30.840 -1.627  12.735  1.00 16.35 ?  91  HIS   A HA   1 
ATOM   1992 H  HB2  . HIS   A 1 91  ? 30.048 -4.321  12.375  1.00 19.55 ?  91  HIS   A HB2  1 
ATOM   1993 H  HB3  . HIS   A 1 91  ? 31.216 -3.592  11.586  1.00 19.55 ?  91  HIS   A HB3  1 
ATOM   1994 H  HD1  . HIS   A 1 91  ? 33.366 -3.062  13.032  1.00 27.06 ?  91  HIS   A HD1  1 
ATOM   1995 H  HD2  . HIS   A 1 91  ? 30.895 -5.646  14.573  1.00 27.04 ?  91  HIS   A HD2  1 
ATOM   1996 H  HE1  . HIS   A 1 91  ? 34.563 -4.165  14.745  1.00 28.36 ?  91  HIS   A HE1  1 
ATOM   1997 N  N    . CYS   A 1 92  ? 29.492 -1.435  10.659  1.00 11.94 ?  92  CYS   A N    1 
ATOM   1998 C  CA   . CYS   A 1 92  ? 28.671 -1.358  9.461   1.00 12.25 ?  92  CYS   A CA   1 
ATOM   1999 C  C    . CYS   A 1 92  ? 29.324 -2.186  8.359   1.00 11.53 ?  92  CYS   A C    1 
ATOM   2000 O  O    . CYS   A 1 92  ? 30.480 -1.937  7.987   1.00 12.61 ?  92  CYS   A O    1 
ATOM   2001 C  CB   . CYS   A 1 92  ? 28.463 0.087   9.001   1.00 12.59 ?  92  CYS   A CB   1 
ATOM   2002 S  SG   . CYS   A 1 92  ? 27.459 0.187   7.478   1.00 12.09 ?  92  CYS   A SG   1 
ATOM   2003 H  H    . CYS   A 1 92  ? 30.263 -1.054  10.571  1.00 14.34 ?  92  CYS   A H    1 
ATOM   2004 H  HA   . CYS   A 1 92  ? 27.801 -1.736  9.647   1.00 14.71 ?  92  CYS   A HA   1 
ATOM   2005 H  HB2  . CYS   A 1 92  ? 28.000 0.585   9.694   1.00 15.13 ?  92  CYS   A HB2  1 
ATOM   2006 H  HB3  . CYS   A 1 92  ? 29.323 0.497   8.816   1.00 15.13 ?  92  CYS   A HB3  1 
ATOM   2007 H  HG   . CYS   A 1 92  ? 27.322 1.341   7.180   1.00 14.53 ?  92  CYS   A HG   1 
ATOM   2008 N  N    . LEU   A 1 93  ? 28.586 -3.171  7.857   1.00 11.23 ?  93  LEU   A N    1 
ATOM   2009 C  CA   . LEU   A 1 93  ? 28.995 -3.932  6.683   1.00 11.27 ?  93  LEU   A CA   1 
ATOM   2010 C  C    . LEU   A 1 93  ? 28.408 -3.242  5.457   1.00 10.77 ?  93  LEU   A C    1 
ATOM   2011 O  O    . LEU   A 1 93  ? 27.195 -3.306  5.219   1.00 11.08 ?  93  LEU   A O    1 
ATOM   2012 C  CB   . LEU   A 1 93  ? 28.522 -5.380  6.794   1.00 11.52 ?  93  LEU   A CB   1 
ATOM   2013 C  CG   . LEU   A 1 93  ? 28.907 -6.267  5.614   1.00 11.83 ?  93  LEU   A CG   1 
ATOM   2014 C  CD1  . LEU   A 1 93  ? 30.405 -6.546  5.593   1.00 12.77 ?  93  LEU   A CD1  1 
ATOM   2015 C  CD2  . LEU   A 1 93  ? 28.119 -7.577  5.669   1.00 12.69 ?  93  LEU   A CD2  1 
ATOM   2016 H  H    . LEU   A 1 93  ? 27.832 -3.421  8.194   1.00 13.49 ?  93  LEU   A H    1 
ATOM   2017 H  HA   . LEU   A 1 93  ? 29.957 -3.919  6.616   1.00 13.54 ?  93  LEU   A HA   1 
ATOM   2018 H  HB2  . LEU   A 1 93  ? 28.914 -5.769  7.596   1.00 13.84 ?  93  LEU   A HB2  1 
ATOM   2019 H  HB3  . LEU   A 1 93  ? 27.558 -5.389  6.869   1.00 13.84 ?  93  LEU   A HB3  1 
ATOM   2020 H  HG   . LEU   A 1 93  ? 28.682 -5.814  4.791   1.00 14.22 ?  93  LEU   A HG   1 
ATOM   2021 H  HD11 . LEU   A 1 93  ? 30.608 -7.142  4.857   1.00 15.34 ?  93  LEU   A HD11 1 
ATOM   2022 H  HD12 . LEU   A 1 93  ? 30.886 -5.710  5.486   1.00 15.34 ?  93  LEU   A HD12 1 
ATOM   2023 H  HD13 . LEU   A 1 93  ? 30.663 -6.965  6.435   1.00 15.34 ?  93  LEU   A HD13 1 
ATOM   2024 H  HD21 . LEU   A 1 93  ? 28.377 -8.129  4.915   1.00 15.24 ?  93  LEU   A HD21 1 
ATOM   2025 H  HD22 . LEU   A 1 93  ? 28.317 -8.032  6.500   1.00 15.24 ?  93  LEU   A HD22 1 
ATOM   2026 H  HD23 . LEU   A 1 93  ? 27.171 -7.372  5.620   1.00 15.24 ?  93  LEU   A HD23 1 
ATOM   2027 N  N    . HIS   A 1 94  ? 29.261 -2.554  4.695   1.00 10.85 ?  94  HIS   A N    1 
ATOM   2028 C  CA   . HIS   A 1 94  ? 28.844 -1.881  3.467   1.00 10.88 ?  94  HIS   A CA   1 
ATOM   2029 C  C    . HIS   A 1 94  ? 28.860 -2.919  2.359   1.00 10.55 ?  94  HIS   A C    1 
ATOM   2030 O  O    . HIS   A 1 94  ? 29.928 -3.432  2.015   1.00 12.35 ?  94  HIS   A O    1 
ATOM   2031 C  CB   . HIS   A 1 94  ? 29.809 -0.741  3.140   1.00 10.92 ?  94  HIS   A CB   1 
ATOM   2032 C  CG   . HIS   A 1 94  ? 29.795 0.359   4.150   1.00 10.86 ?  94  HIS   A CG   1 
ATOM   2033 N  ND1  . HIS   A 1 94  ? 28.917 1.424   4.088   1.00 11.12 ?  94  HIS   A ND1  1 
ATOM   2034 C  CD2  . HIS   A 1 94  ? 30.526 0.530   5.272   1.00 11.78 ?  94  HIS   A CD2  1 
ATOM   2035 C  CE1  . HIS   A 1 94  ? 29.131 2.210   5.129   1.00 11.41 ?  94  HIS   A CE1  1 
ATOM   2036 N  NE2  . HIS   A 1 94  ? 30.098 1.686   5.863   1.00 11.56 ?  94  HIS   A NE2  1 
ATOM   2037 H  H    . HIS   A 1 94  ? 30.097 -2.454  4.876   1.00 13.04 ?  94  HIS   A H    1 
ATOM   2038 H  HA   . HIS   A 1 94  ? 27.941 -1.524  3.564   1.00 13.07 ?  94  HIS   A HA   1 
ATOM   2039 H  HB2  . HIS   A 1 94  ? 30.704 -1.093  3.099   1.00 13.12 ?  94  HIS   A HB2  1 
ATOM   2040 H  HB3  . HIS   A 1 94  ? 29.557 -0.356  2.284   1.00 13.12 ?  94  HIS   A HB3  1 
ATOM   2041 H  HD2  . HIS   A 1 94  ? 31.195 -0.025  5.587   1.00 14.15 ?  94  HIS   A HD2  1 
ATOM   2042 H  HE1  . HIS   A 1 94  ? 28.666 3.000   5.310   1.00 13.71 ?  94  HIS   A HE1  1 
ATOM   2043 H  HE2  . HIS   A 1 94  ? 30.408 2.035   6.584   1.00 13.89 ?  94  HIS   A HE2  1 
ATOM   2044 N  N    . VAL   A 1 95  ? 27.695 -3.241  1.802   1.00 10.25 ?  95  VAL   A N    1 
ATOM   2045 C  CA   . VAL   A 1 95  ? 27.560 -4.282  0.786   1.00 10.48 ?  95  VAL   A CA   1 
ATOM   2046 C  C    . VAL   A 1 95  ? 27.023 -3.650  -0.482  1.00 10.43 ?  95  VAL   A C    1 
ATOM   2047 O  O    . VAL   A 1 95  ? 26.022 -2.924  -0.435  1.00 11.25 ?  95  VAL   A O    1 
ATOM   2048 C  CB   . VAL   A 1 95  ? 26.628 -5.424  1.235   1.00 11.09 ?  95  VAL   A CB   1 
ATOM   2049 C  CG1  . VAL   A 1 95  ? 26.520 -6.472  0.129   1.00 12.13 ?  95  VAL   A CG1  1 
ATOM   2050 C  CG2  . VAL   A 1 95  ? 27.114 -6.031  2.532   1.00 11.56 ?  95  VAL   A CG2  1 
ATOM   2051 H  H    . VAL   A 1 95  ? 26.947 -2.866  2.006   1.00 12.32 ?  95  VAL   A H    1 
ATOM   2052 H  HA   . VAL   A 1 95  ? 28.431 -4.658  0.590   1.00 12.60 ?  95  VAL   A HA   1 
ATOM   2053 H  HB   . VAL   A 1 95  ? 25.745 -5.067  1.388   1.00 13.33 ?  95  VAL   A HB   1 
ATOM   2054 H  HG11 . VAL   A 1 95  ? 26.134 -7.283  0.494   1.00 14.58 ?  95  VAL   A HG11 1 
ATOM   2055 H  HG12 . VAL   A 1 95  ? 25.951 -6.130  -0.582  1.00 14.58 ?  95  VAL   A HG12 1 
ATOM   2056 H  HG13 . VAL   A 1 95  ? 27.406 -6.661  -0.224  1.00 14.58 ?  95  VAL   A HG13 1 
ATOM   2057 H  HG21 . VAL   A 1 95  ? 26.550 -6.791  2.751   1.00 13.90 ?  95  VAL   A HG21 1 
ATOM   2058 H  HG22 . VAL   A 1 95  ? 28.031 -6.316  2.425   1.00 13.90 ?  95  VAL   A HG22 1 
ATOM   2059 H  HG23 . VAL   A 1 95  ? 27.049 -5.361  3.230   1.00 13.90 ?  95  VAL   A HG23 1 
ATOM   2060 N  N    . VAL   A 1 96  ? 27.654 -3.950  -1.617  1.00 10.08 ?  96  VAL   A N    1 
ATOM   2061 C  CA   . VAL   A 1 96  ? 27.249 -3.402  -2.906  1.00 10.75 ?  96  VAL   A CA   1 
ATOM   2062 C  C    . VAL   A 1 96  ? 26.452 -4.457  -3.664  1.00 11.30 ?  96  VAL   A C    1 
ATOM   2063 O  O    . VAL   A 1 96  ? 27.015 -5.400  -4.225  1.00 12.19 ?  96  VAL   A O    1 
ATOM   2064 C  CB   . VAL   A 1 96  ? 28.445 -2.930  -3.730  1.00 11.37 ?  96  VAL   A CB   1 
ATOM   2065 C  CG1  . VAL   A 1 96  ? 27.937 -2.295  -5.008  1.00 11.70 ?  96  VAL   A CG1  1 
ATOM   2066 C  CG2  . VAL   A 1 96  ? 29.297 -1.955  -2.943  1.00 11.87 ?  96  VAL   A CG2  1 
ATOM   2067 H  H    . VAL   A 1 96  ? 28.343 -4.468  -1.663  1.00 12.11 ?  96  VAL   A H    1 
ATOM   2068 H  HA   . VAL   A 1 96  ? 26.673 -2.639  -2.756  1.00 12.92 ?  96  VAL   A HA   1 
ATOM   2069 H  HB   . VAL   A 1 96  ? 28.994 -3.687  -3.970  1.00 13.66 ?  96  VAL   A HB   1 
ATOM   2070 H  HG11 . VAL   A 1 96  ? 28.664 -1.811  -5.429  1.00 14.06 ?  96  VAL   A HG11 1 
ATOM   2071 H  HG12 . VAL   A 1 96  ? 27.613 -2.988  -5.600  1.00 14.06 ?  96  VAL   A HG12 1 
ATOM   2072 H  HG13 . VAL   A 1 96  ? 27.217 -1.679  -4.790  1.00 14.06 ?  96  VAL   A HG13 1 
ATOM   2073 H  HG21 . VAL   A 1 96  ? 30.000 -1.610  -3.514  1.00 14.26 ?  96  VAL   A HG21 1 
ATOM   2074 H  HG22 . VAL   A 1 96  ? 28.738 -1.224  -2.629  1.00 14.26 ?  96  VAL   A HG22 1 
ATOM   2075 H  HG23 . VAL   A 1 96  ? 29.686 -2.418  -2.183  1.00 14.26 ?  96  VAL   A HG23 1 
ATOM   2076 N  N    . GLY   A 1 97  ? 25.135 -4.302  -3.698  1.00 11.07 ?  97  GLY   A N    1 
ATOM   2077 C  CA   . GLY   A 1 97  ? 24.322 -5.062  -4.609  1.00 11.61 ?  97  GLY   A CA   1 
ATOM   2078 C  C    . GLY   A 1 97  ? 24.344 -4.425  -5.982  1.00 11.79 ?  97  GLY   A C    1 
ATOM   2079 O  O    . GLY   A 1 97  ? 24.631 -3.231  -6.131  1.00 12.89 ?  97  GLY   A O    1 
ATOM   2080 H  H    . GLY   A 1 97  ? 24.692 -3.753  -3.197  1.00 13.30 ?  97  GLY   A H    1 
ATOM   2081 H  HA2  . GLY   A 1 97  ? 24.670 -5.965  -4.654  1.00 13.95 ?  97  GLY   A HA2  1 
ATOM   2082 H  HA3  . GLY   A 1 97  ? 23.406 -5.095  -4.284  1.00 13.95 ?  97  GLY   A HA3  1 
ATOM   2083 N  N    A PRO   A 1 98  ? 23.973 -5.168  -7.020  0.62 11.99 ?  98  PRO   A N    1 
ATOM   2084 N  N    B PRO   A 1 98  ? 24.096 -5.241  -7.007  0.38 12.37 ?  98  PRO   A N    1 
ATOM   2085 C  CA   A PRO   A 1 98  ? 23.863 -4.545  -8.346  0.62 12.84 ?  98  PRO   A CA   1 
ATOM   2086 C  CA   B PRO   A 1 98  ? 24.079 -4.730  -8.379  0.38 13.07 ?  98  PRO   A CA   1 
ATOM   2087 C  C    A PRO   A 1 98  ? 22.759 -3.491  -8.376  0.62 12.86 ?  98  PRO   A C    1 
ATOM   2088 C  C    B PRO   A 1 98  ? 22.939 -3.748  -8.577  0.38 13.07 ?  98  PRO   A C    1 
ATOM   2089 O  O    A PRO   A 1 98  ? 21.687 -3.667  -7.794  0.62 12.02 ?  98  PRO   A O    1 
ATOM   2090 O  O    B PRO   A 1 98  ? 21.830 -3.931  -8.068  0.38 13.76 ?  98  PRO   A O    1 
ATOM   2091 C  CB   A PRO   A 1 98  ? 23.545 -5.727  -9.269  0.62 13.07 ?  98  PRO   A CB   1 
ATOM   2092 C  CB   B PRO   A 1 98  ? 23.882 -5.995  -9.226  0.38 13.37 ?  98  PRO   A CB   1 
ATOM   2093 C  CG   A PRO   A 1 98  ? 22.911 -6.751  -8.375  0.62 12.42 ?  98  PRO   A CG   1 
ATOM   2094 C  CG   B PRO   A 1 98  ? 23.233 -6.980  -8.295  0.38 13.57 ?  98  PRO   A CG   1 
ATOM   2095 C  CD   A PRO   A 1 98  ? 23.627 -6.601  -7.046  0.62 12.11 ?  98  PRO   A CD   1 
ATOM   2096 C  CD   B PRO   A 1 98  ? 23.846 -6.694  -6.954  0.38 12.41 ?  98  PRO   A CD   1 
ATOM   2097 H  HA   A PRO   A 1 98  ? 24.710 -4.152  -8.602  0.62 15.43 ?  98  PRO   A HA   1 
ATOM   2098 H  HA   B PRO   A 1 98  ? 24.925 -4.314  -8.602  0.38 15.70 ?  98  PRO   A HA   1 
ATOM   2099 H  HB2  A PRO   A 1 98  ? 22.926 -5.447  -9.958  0.62 15.71 ?  98  PRO   A HB2  1 
ATOM   2100 H  HB2  B PRO   A 1 98  ? 23.303 -5.800  -9.978  0.38 16.06 ?  98  PRO   A HB2  1 
ATOM   2101 H  HB3  A PRO   A 1 98  ? 24.364 -6.074  -9.659  0.62 15.71 ?  98  PRO   A HB3  1 
ATOM   2102 H  HB3  B PRO   A 1 98  ? 24.742 -6.328  -9.529  0.38 16.06 ?  98  PRO   A HB3  1 
ATOM   2103 H  HG2  A PRO   A 1 98  ? 21.966 -6.564  -8.280  0.62 14.92 ?  98  PRO   A HG2  1 
ATOM   2104 H  HG2  B PRO   A 1 98  ? 22.273 -6.831  -8.275  0.38 16.30 ?  98  PRO   A HG2  1 
ATOM   2105 H  HG3  A PRO   A 1 98  ? 23.052 -7.640  -8.743  0.62 14.92 ?  98  PRO   A HG3  1 
ATOM   2106 H  HG3  B PRO   A 1 98  ? 23.432 -7.887  -8.581  0.38 16.30 ?  98  PRO   A HG3  1 
ATOM   2107 H  HD2  A PRO   A 1 98  ? 23.027 -6.826  -6.311  0.62 14.55 ?  98  PRO   A HD2  1 
ATOM   2108 H  HD2  B PRO   A 1 98  ? 23.220 -6.911  -6.243  0.38 14.91 ?  98  PRO   A HD2  1 
ATOM   2109 H  HD3  A PRO   A 1 98  ? 24.428 -7.152  -7.024  0.62 14.55 ?  98  PRO   A HD3  1 
ATOM   2110 H  HD3  B PRO   A 1 98  ? 24.680 -7.182  -6.851  0.38 14.91 ?  98  PRO   A HD3  1 
ATOM   2111 N  N    A ASN   A 1 99  ? 23.043 -2.374  -9.044  0.62 13.90 ?  99  ASN   A N    1 
ATOM   2112 N  N    B ASN   A 1 99  ? 23.226 -2.690  -9.314  0.38 12.69 ?  99  ASN   A N    1 
ATOM   2113 C  CA   A ASN   A 1 99  ? 22.068 -1.301  -9.253  0.62 14.58 ?  99  ASN   A CA   1 
ATOM   2114 C  CA   B ASN   A 1 99  ? 22.232 -1.677  -9.635  0.38 13.56 ?  99  ASN   A CA   1 
ATOM   2115 C  C    A ASN   A 1 99  ? 21.492 -1.468  -10.657 0.62 15.51 ?  99  ASN   A C    1 
ATOM   2116 C  C    B ASN   A 1 99  ? 21.725 -1.953  -11.045 0.38 14.08 ?  99  ASN   A C    1 
ATOM   2117 O  O    A ASN   A 1 99  ? 22.156 -1.166  -11.653 0.62 16.85 ?  99  ASN   A O    1 
ATOM   2118 O  O    B ASN   A 1 99  ? 22.450 -1.766  -12.029 0.38 13.71 ?  99  ASN   A O    1 
ATOM   2119 C  CB   A ASN   A 1 99  ? 22.718 0.069   -9.068  0.62 14.99 ?  99  ASN   A CB   1 
ATOM   2120 C  CB   B ASN   A 1 99  ? 22.820 -0.277  -9.514  0.38 14.96 ?  99  ASN   A CB   1 
ATOM   2121 C  CG   A ASN   A 1 99  ? 21.702 1.218   -9.071  0.62 16.12 ?  99  ASN   A CG   1 
ATOM   2122 C  CG   B ASN   A 1 99  ? 21.765 0.791   -9.634  0.38 16.20 ?  99  ASN   A CG   1 
ATOM   2123 O  OD1  A ASN   A 1 99  ? 20.685 1.164   -9.761  0.62 15.74 ?  99  ASN   A OD1  1 
ATOM   2124 O  OD1  B ASN   A 1 99  ? 20.966 0.766   -10.560 0.38 15.44 ?  99  ASN   A OD1  1 
ATOM   2125 N  ND2  A ASN   A 1 99  ? 21.992 2.269   -8.305  0.62 16.42 ?  99  ASN   A ND2  1 
ATOM   2126 N  ND2  B ASN   A 1 99  ? 21.728 1.711   -8.675  0.38 16.70 ?  99  ASN   A ND2  1 
ATOM   2127 H  H    A ASN   A 1 99  ? 23.819 -2.207  -9.370  0.62 16.70 ?  99  ASN   A H    1 
ATOM   2128 H  H    B ASN   A 1 99  ? 24.007 -2.528  -9.634  0.38 15.25 ?  99  ASN   A H    1 
ATOM   2129 H  HA   A ASN   A 1 99  ? 21.348 -1.400  -8.604  0.62 17.52 ?  99  ASN   A HA   1 
ATOM   2130 H  HA   B ASN   A 1 99  ? 21.486 -1.753  -9.015  0.38 16.29 ?  99  ASN   A HA   1 
ATOM   2131 H  HB2  A ASN   A 1 99  ? 23.192 0.080   -8.223  0.62 18.01 ?  99  ASN   A HB2  1 
ATOM   2132 H  HB2  B ASN   A 1 99  ? 23.253 -0.183  -8.651  0.38 17.97 ?  99  ASN   A HB2  1 
ATOM   2133 H  HB3  A ASN   A 1 99  ? 23.339 0.213   -9.799  0.62 18.01 ?  99  ASN   A HB3  1 
ATOM   2134 H  HB3  B ASN   A 1 99  ? 23.460 -0.151  -10.228 0.38 17.97 ?  99  ASN   A HB3  1 
ATOM   2135 H  HD21 A ASN   A 1 99  ? 21.454 2.936   -8.269  0.62 19.72 ?  99  ASN   A HD21 1 
ATOM   2136 H  HD21 B ASN   A 1 99  ? 21.136 2.334   -8.692  0.38 20.07 ?  99  ASN   A HD21 1 
ATOM   2137 H  HD22 A ASN   A 1 99  ? 22.718 2.273   -7.842  0.62 19.72 ?  99  ASN   A HD22 1 
ATOM   2138 H  HD22 B ASN   A 1 99  ? 22.301 1.682   -8.031  0.38 20.07 ?  99  ASN   A HD22 1 
ATOM   2139 N  N    A VAL   A 1 100 ? 20.249 -1.960  -10.726 0.62 16.42 ?  100 VAL   A N    1 
ATOM   2140 N  N    B VAL   A 1 100 ? 20.481 -2.424  -11.133 0.38 15.66 ?  100 VAL   A N    1 
ATOM   2141 C  CA   A VAL   A 1 100 ? 19.598 -2.209  -12.012 0.62 18.21 ?  100 VAL   A CA   1 
ATOM   2142 C  CA   B VAL   A 1 100 ? 19.917 -2.798  -12.424 0.38 17.81 ?  100 VAL   A CA   1 
ATOM   2143 C  C    A VAL   A 1 100 ? 19.494 -0.923  -12.821 0.62 19.18 ?  100 VAL   A C    1 
ATOM   2144 C  C    B VAL   A 1 100 ? 19.717 -1.578  -13.311 0.38 18.28 ?  100 VAL   A C    1 
ATOM   2145 O  O    A VAL   A 1 100 ? 19.600 -0.942  -14.052 0.62 19.56 ?  100 VAL   A O    1 
ATOM   2146 O  O    B VAL   A 1 100 ? 19.719 -1.695  -14.543 0.38 19.20 ?  100 VAL   A O    1 
ATOM   2147 C  CB   A VAL   A 1 100 ? 18.226 -2.892  -11.800 0.62 19.17 ?  100 VAL   A CB   1 
ATOM   2148 C  CB   B VAL   A 1 100 ? 18.619 -3.596  -12.211 0.38 20.27 ?  100 VAL   A CB   1 
ATOM   2149 C  CG1  A VAL   A 1 100 ? 17.480 -3.058  -13.113 0.62 20.20 ?  100 VAL   A CG1  1 
ATOM   2150 C  CG1  B VAL   A 1 100 ? 17.730 -3.536  -13.445 0.38 21.01 ?  100 VAL   A CG1  1 
ATOM   2151 C  CG2  A VAL   A 1 100 ? 18.411 -4.250  -11.130 0.62 19.16 ?  100 VAL   A CG2  1 
ATOM   2152 C  CG2  B VAL   A 1 100 ? 18.951 -5.034  -11.855 0.38 21.26 ?  100 VAL   A CG2  1 
ATOM   2153 H  H    A VAL   A 1 100 ? 19.758 -2.156  -10.039 0.62 19.72 ?  100 VAL   A H    1 
ATOM   2154 H  H    B VAL   A 1 100 ? 19.957 -2.553  -10.459 0.38 18.81 ?  100 VAL   A H    1 
ATOM   2155 H  HA   A VAL   A 1 100 ? 20.145 -2.829  -12.517 0.62 21.88 ?  100 VAL   A HA   1 
ATOM   2156 H  HA   B VAL   A 1 100 ? 20.547 -3.385  -12.869 0.38 21.40 ?  100 VAL   A HA   1 
ATOM   2157 H  HB   A VAL   A 1 100 ? 17.682 -2.346  -11.215 0.62 23.02 ?  100 VAL   A HB   1 
ATOM   2158 H  HB   B VAL   A 1 100 ? 18.130 -3.206  -11.470 0.38 24.35 ?  100 VAL   A HB   1 
ATOM   2159 H  HG11 A VAL   A 1 100 ? 16.728 -3.659  -12.976 0.62 24.26 ?  100 VAL   A HG11 1 
ATOM   2160 H  HG11 B VAL   A 1 100 ? 17.048 -4.220  -13.371 0.38 25.23 ?  100 VAL   A HG11 1 
ATOM   2161 H  HG12 A VAL   A 1 100 ? 17.159 -2.193  -13.407 0.62 24.26 ?  100 VAL   A HG12 1 
ATOM   2162 H  HG12 B VAL   A 1 100 ? 17.312 -2.660  -13.496 0.38 25.23 ?  100 VAL   A HG12 1 
ATOM   2163 H  HG13 A VAL   A 1 100 ? 18.083 -3.434  -13.774 0.62 24.26 ?  100 VAL   A HG13 1 
ATOM   2164 H  HG13 B VAL   A 1 100 ? 18.271 -3.693  -14.234 0.38 25.23 ?  100 VAL   A HG13 1 
ATOM   2165 H  HG21 A VAL   A 1 100 ? 17.543 -4.680  -11.035 0.62 23.01 ?  100 VAL   A HG21 1 
ATOM   2166 H  HG21 B VAL   A 1 100 ? 18.126 -5.515  -11.694 0.38 25.53 ?  100 VAL   A HG21 1 
ATOM   2167 H  HG22 A VAL   A 1 100 ? 18.990 -4.801  -11.680 0.62 23.01 ?  100 VAL   A HG22 1 
ATOM   2168 H  HG22 B VAL   A 1 100 ? 19.433 -5.438  -12.595 0.38 25.53 ?  100 VAL   A HG22 1 
ATOM   2169 H  HG23 A VAL   A 1 100 ? 18.809 -4.121  -10.255 0.62 23.01 ?  100 VAL   A HG23 1 
ATOM   2170 H  HG23 B VAL   A 1 100 ? 19.502 -5.042  -11.057 0.38 25.53 ?  100 VAL   A HG23 1 
ATOM   2171 N  N    A ASN   A 1 101 ? 19.290 0.211   -12.154 0.62 20.29 ?  101 ASN   A N    1 
ATOM   2172 N  N    B ASN   A 1 101 ? 19.527 -0.395  -12.714 0.38 18.49 ?  101 ASN   A N    1 
ATOM   2173 C  CA   A ASN   A 1 101 ? 19.217 1.485   -12.859 0.62 21.66 ?  101 ASN   A CA   1 
ATOM   2174 C  CA   B ASN   A 1 101 ? 19.433 0.829   -13.502 0.38 19.55 ?  101 ASN   A CA   1 
ATOM   2175 C  C    A ASN   A 1 101 ? 20.568 1.929   -13.424 0.62 23.99 ?  101 ASN   A C    1 
ATOM   2176 C  C    B ASN   A 1 101 ? 20.749 1.172   -14.183 0.38 20.61 ?  101 ASN   A C    1 
ATOM   2177 O  O    A ASN   A 1 101 ? 20.625 2.967   -14.097 0.62 25.57 ?  101 ASN   A O    1 
ATOM   2178 O  O    B ASN   A 1 101 ? 20.742 1.905   -15.180 0.38 20.79 ?  101 ASN   A O    1 
ATOM   2179 C  CB   A ASN   A 1 101 ? 18.600 2.544   -11.941 0.62 20.08 ?  101 ASN   A CB   1 
ATOM   2180 C  CB   B ASN   A 1 101 ? 18.995 2.000   -12.619 0.38 19.36 ?  101 ASN   A CB   1 
ATOM   2181 C  CG   A ASN   A 1 101 ? 17.224 2.132   -11.421 0.62 19.34 ?  101 ASN   A CG   1 
ATOM   2182 C  CG   B ASN   A 1 101 ? 17.717 1.711   -11.855 0.38 19.78 ?  101 ASN   A CG   1 
ATOM   2183 O  OD1  A ASN   A 1 101 ? 16.381 1.637   -12.175 0.62 19.90 ?  101 ASN   A OD1  1 
ATOM   2184 O  OD1  B ASN   A 1 101 ? 16.775 1.121   -12.388 0.38 20.64 ?  101 ASN   A OD1  1 
ATOM   2185 N  ND2  A ASN   A 1 101 ? 16.998 2.323   -10.125 0.62 19.58 ?  101 ASN   A ND2  1 
ATOM   2186 N  ND2  B ASN   A 1 101 ? 17.684 2.116   -10.592 0.38 19.87 ?  101 ASN   A ND2  1 
ATOM   2187 H  H    A ASN   A 1 101 ? 19.183 0.265   -11.304 0.62 24.37 ?  101 ASN   A H    1 
ATOM   2188 H  H    B ASN   A 1 101 ? 19.442 -0.282  -11.862 0.38 22.20 ?  101 ASN   A H    1 
ATOM   2189 H  HA   A ASN   A 1 101 ? 18.618 1.376   -13.612 0.62 26.01 ?  101 ASN   A HA   1 
ATOM   2190 H  HA   B ASN   A 1 101 ? 18.767 0.708   -14.190 0.38 23.48 ?  101 ASN   A HA   1 
ATOM   2191 H  HB2  A ASN   A 1 101 ? 19.182 2.684   -11.179 0.62 24.11 ?  101 ASN   A HB2  1 
ATOM   2192 H  HB2  B ASN   A 1 101 ? 19.692 2.198   -11.973 0.38 23.25 ?  101 ASN   A HB2  1 
ATOM   2193 H  HB3  A ASN   A 1 101 ? 18.497 3.371   -12.439 0.62 24.11 ?  101 ASN   A HB3  1 
ATOM   2194 H  HB3  B ASN   A 1 101 ? 18.838 2.776   -13.180 0.38 23.25 ?  101 ASN   A HB3  1 
ATOM   2195 H  HD21 A ASN   A 1 101 ? 16.240 2.104   -9.783  0.62 23.52 ?  101 ASN   A HD21 1 
ATOM   2196 H  HD21 B ASN   A 1 101 ? 16.982 1.976   -10.116 0.38 23.87 ?  101 ASN   A HD21 1 
ATOM   2197 H  HD22 A ASN   A 1 101 ? 17.609 2.669   -9.626  0.62 23.52 ?  101 ASN   A HD22 1 
ATOM   2198 H  HD22 B ASN   A 1 101 ? 18.362 2.520   -10.250 0.38 23.87 ?  101 ASN   A HD22 1 
ATOM   2199 N  N    A LYS   A 1 102 ? 21.641 1.168   -13.181 0.62 25.64 ?  102 LYS   A N    1 
ATOM   2200 N  N    B LYS   A 1 102 ? 21.868 0.667   -13.664 0.38 22.32 ?  102 LYS   A N    1 
ATOM   2201 C  CA   A LYS   A 1 102 ? 22.929 1.361   -13.838 0.62 27.37 ?  102 LYS   A CA   1 
ATOM   2202 C  CA   B LYS   A 1 102 ? 23.187 0.885   -14.243 0.38 23.87 ?  102 LYS   A CA   1 
ATOM   2203 C  C    A LYS   A 1 102 ? 23.241 0.265   -14.850 0.62 27.69 ?  102 LYS   A C    1 
ATOM   2204 C  C    B LYS   A 1 102 ? 23.633 -0.279  -15.124 0.38 23.81 ?  102 LYS   A C    1 
ATOM   2205 O  O    A LYS   A 1 102 ? 24.294 0.321   -15.496 0.62 28.08 ?  102 LYS   A O    1 
ATOM   2206 O  O    B LYS   A 1 102 ? 24.816 -0.370  -15.465 0.38 23.93 ?  102 LYS   A O    1 
ATOM   2207 C  CB   A LYS   A 1 102 ? 24.060 1.407   -12.802 0.62 29.36 ?  102 LYS   A CB   1 
ATOM   2208 C  CB   B LYS   A 1 102 ? 24.215 1.131   -13.132 0.38 26.22 ?  102 LYS   A CB   1 
ATOM   2209 C  CG   A LYS   A 1 102 ? 23.986 2.550   -11.813 0.62 31.07 ?  102 LYS   A CG   1 
ATOM   2210 C  CG   B LYS   A 1 102 ? 24.064 2.484   -12.445 0.38 28.21 ?  102 LYS   A CG   1 
ATOM   2211 C  CD   A LYS   A 1 102 ? 25.192 2.523   -10.880 0.62 32.90 ?  102 LYS   A CD   1 
ATOM   2212 C  CD   B LYS   A 1 102 ? 24.648 2.495   -11.036 0.38 30.19 ?  102 LYS   A CD   1 
ATOM   2213 C  CE   A LYS   A 1 102 ? 25.134 3.638   -9.851  0.62 34.31 ?  102 LYS   A CE   1 
ATOM   2214 C  CE   B LYS   A 1 102 ? 24.472 3.862   -10.383 0.38 31.60 ?  102 LYS   A CE   1 
ATOM   2215 N  NZ   A LYS   A 1 102 ? 26.226 3.521   -8.841  0.62 34.99 ?  102 LYS   A NZ   1 
ATOM   2216 N  NZ   B LYS   A 1 102 ? 24.746 3.850   -8.916  0.38 32.39 ?  102 LYS   A NZ   1 
ATOM   2217 H  H    A LYS   A 1 102 ? 21.646 0.509   -12.625 0.62 30.78 ?  102 LYS   A H    1 
ATOM   2218 H  H    B LYS   A 1 102 ? 21.887 0.181   -12.951 0.38 26.80 ?  102 LYS   A H    1 
ATOM   2219 H  HA   A LYS   A 1 102 ? 22.921 2.206   -14.308 0.62 32.86 ?  102 LYS   A HA   1 
ATOM   2220 H  HA   B LYS   A 1 102 ? 23.152 1.691   -14.783 0.38 28.67 ?  102 LYS   A HA   1 
ATOM   2221 H  HB2  A LYS   A 1 102 ? 24.046 0.582   -12.292 0.62 35.25 ?  102 LYS   A HB2  1 
ATOM   2222 H  HB2  B LYS   A 1 102 ? 24.119 0.443   -12.455 0.38 31.49 ?  102 LYS   A HB2  1 
ATOM   2223 H  HB3  A LYS   A 1 102 ? 24.905 1.484   -13.271 0.62 35.25 ?  102 LYS   A HB3  1 
ATOM   2224 H  HB3  B LYS   A 1 102 ? 25.107 1.092   -13.515 0.38 31.49 ?  102 LYS   A HB3  1 
ATOM   2225 H  HG2  A LYS   A 1 102 ? 23.986 3.393   -12.292 0.62 37.30 ?  102 LYS   A HG2  1 
ATOM   2226 H  HG2  B LYS   A 1 102 ? 24.531 3.159   -12.965 0.38 33.87 ?  102 LYS   A HG2  1 
ATOM   2227 H  HG3  A LYS   A 1 102 ? 23.182 2.464   -11.278 0.62 37.30 ?  102 LYS   A HG3  1 
ATOM   2228 H  HG3  B LYS   A 1 102 ? 23.123 2.706   -12.381 0.38 33.87 ?  102 LYS   A HG3  1 
ATOM   2229 H  HD2  A LYS   A 1 102 ? 25.212 1.675   -10.409 0.62 39.50 ?  102 LYS   A HD2  1 
ATOM   2230 H  HD2  B LYS   A 1 102 ? 24.188 1.841   -10.489 0.38 36.25 ?  102 LYS   A HD2  1 
ATOM   2231 H  HD3  A LYS   A 1 102 ? 26.003 2.633   -11.403 0.62 39.50 ?  102 LYS   A HD3  1 
ATOM   2232 H  HD3  B LYS   A 1 102 ? 25.596 2.293   -11.075 0.38 36.25 ?  102 LYS   A HD3  1 
ATOM   2233 H  HE2  A LYS   A 1 102 ? 25.229 4.492   -10.303 0.62 41.19 ?  102 LYS   A HE2  1 
ATOM   2234 H  HE2  B LYS   A 1 102 ? 25.086 4.489   -10.795 0.38 37.94 ?  102 LYS   A HE2  1 
ATOM   2235 H  HE3  A LYS   A 1 102 ? 24.284 3.598   -9.387  0.62 41.19 ?  102 LYS   A HE3  1 
ATOM   2236 H  HE3  B LYS   A 1 102 ? 23.558 4.158   -10.513 0.38 37.94 ?  102 LYS   A HE3  1 
ATOM   2237 H  HZ1  A LYS   A 1 102 ? 26.167 4.186   -8.252  0.62 42.00 ?  102 LYS   A HZ1  1 
ATOM   2238 H  HZ1  B LYS   A 1 102 ? 24.631 4.666   -8.578  0.38 38.89 ?  102 LYS   A HZ1  1 
ATOM   2239 H  HZ2  A LYS   A 1 102 ? 26.158 2.746   -8.409  0.62 42.00 ?  102 LYS   A HZ2  1 
ATOM   2240 H  HZ2  B LYS   A 1 102 ? 24.189 3.288   -8.507  0.38 38.89 ?  102 LYS   A HZ2  1 
ATOM   2241 H  HZ3  A LYS   A 1 102 ? 27.019 3.560   -9.244  0.62 42.00 ?  102 LYS   A HZ3  1 
ATOM   2242 H  HZ3  B LYS   A 1 102 ? 25.582 3.589   -8.764  0.38 38.89 ?  102 LYS   A HZ3  1 
ATOM   2243 N  N    A GLY   A 1 103 ? 22.368 -0.731  -14.997 0.62 28.39 ?  103 GLY   A N    1 
ATOM   2244 N  N    B GLY   A 1 103 ? 22.716 -1.171  -15.492 0.38 23.57 ?  103 GLY   A N    1 
ATOM   2245 C  CA   A GLY   A 1 103 ? 22.600 -1.836  -15.909 0.62 28.36 ?  103 GLY   A CA   1 
ATOM   2246 C  CA   B GLY   A 1 103 ? 23.062 -2.288  -16.351 0.38 23.55 ?  103 GLY   A CA   1 
ATOM   2247 C  C    A GLY   A 1 103 ? 23.445 -2.967  -15.365 0.62 28.14 ?  103 GLY   A C    1 
ATOM   2248 C  C    B GLY   A 1 103 ? 23.883 -3.375  -15.691 0.38 22.92 ?  103 GLY   A C    1 
ATOM   2249 O  O    A GLY   A 1 103 ? 23.919 -3.798  -16.145 0.62 29.34 ?  103 GLY   A O    1 
ATOM   2250 O  O    B GLY   A 1 103 ? 24.532 -4.160  -16.388 0.38 23.60 ?  103 GLY   A O    1 
ATOM   2251 H  H    A GLY   A 1 103 ? 21.622 -0.779  -14.584 0.62 34.09 ?  103 GLY   A H    1 
ATOM   2252 H  H    B GLY   A 1 103 ? 21.888 -1.139  -15.258 0.38 28.30 ?  103 GLY   A H    1 
ATOM   2253 H  HA2  A GLY   A 1 103 ? 21.743 -2.208  -16.177 0.62 34.05 ?  103 GLY   A HA2  1 
ATOM   2254 H  HA2  B GLY   A 1 103 ? 22.242 -2.682  -16.690 0.38 28.28 ?  103 GLY   A HA2  1 
ATOM   2255 H  HA3  A GLY   A 1 103 ? 23.037 -1.496  -16.705 0.62 34.05 ?  103 GLY   A HA3  1 
ATOM   2256 H  HA3  B GLY   A 1 103 ? 23.564 -1.944  -17.110 0.38 28.28 ?  103 GLY   A HA3  1 
ATOM   2257 N  N    A GLU   A 1 104 ? 23.639 -3.041  -14.052 0.62 25.96 ?  104 GLU   A N    1 
ATOM   2258 N  N    B GLU   A 1 104 ? 23.865 -3.456  -14.366 0.38 20.77 ?  104 GLU   A N    1 
ATOM   2259 C  CA   A GLU   A 1 104 ? 24.531 -4.035  -13.470 0.62 24.09 ?  104 GLU   A CA   1 
ATOM   2260 C  CA   B GLU   A 1 104 ? 24.704 -4.407  -13.652 0.38 19.30 ?  104 GLU   A CA   1 
ATOM   2261 C  C    A GLU   A 1 104 ? 23.856 -5.401  -13.369 0.62 24.24 ?  104 GLU   A C    1 
ATOM   2262 C  C    B GLU   A 1 104 ? 24.005 -5.759  -13.507 0.38 18.67 ?  104 GLU   A C    1 
ATOM   2263 O  O    A GLU   A 1 104 ? 22.646 -5.511  -13.150 0.62 24.27 ?  104 GLU   A O    1 
ATOM   2264 O  O    B GLU   A 1 104 ? 22.780 -5.868  -13.576 0.38 18.85 ?  104 GLU   A O    1 
ATOM   2265 C  CB   A GLU   A 1 104 ? 25.032 -3.549  -12.107 0.62 22.24 ?  104 GLU   A CB   1 
ATOM   2266 C  CB   B GLU   A 1 104 ? 25.121 -3.837  -12.296 0.38 19.45 ?  104 GLU   A CB   1 
ATOM   2267 C  CG   A GLU   A 1 104 ? 25.923 -2.316  -12.267 0.62 21.72 ?  104 GLU   A CG   1 
ATOM   2268 C  CG   B GLU   A 1 104 ? 25.987 -2.587  -12.437 0.38 20.21 ?  104 GLU   A CG   1 
ATOM   2269 C  CD   A GLU   A 1 104 ? 26.290 -1.602  -10.975 0.62 20.69 ?  104 GLU   A CD   1 
ATOM   2270 C  CD   B GLU   A 1 104 ? 26.224 -1.844  -11.134 0.38 20.59 ?  104 GLU   A CD   1 
ATOM   2271 O  OE1  A GLU   A 1 104 ? 25.674 -1.847  -9.920  0.62 18.74 ?  104 GLU   A OE1  1 
ATOM   2272 O  OE1  B GLU   A 1 104 ? 25.732 -2.286  -10.076 0.38 21.12 ?  104 GLU   A OE1  1 
ATOM   2273 O  OE2  A GLU   A 1 104 ? 27.214 -0.759  -11.038 0.62 21.66 -1 104 GLU   A OE2  1 
ATOM   2274 O  OE2  B GLU   A 1 104 ? 26.904 -0.796  -11.179 0.38 21.02 -1 104 GLU   A OE2  1 
ATOM   2275 H  H    A GLU   A 1 104 ? 23.265 -2.524  -13.479 0.62 31.17 ?  104 GLU   A H    1 
ATOM   2276 H  H    B GLU   A 1 104 ? 23.368 -2.965  -13.863 0.38 24.95 ?  104 GLU   A H    1 
ATOM   2277 H  HA   A GLU   A 1 104 ? 25.301 -4.132  -14.050 0.62 28.92 ?  104 GLU   A HA   1 
ATOM   2278 H  HA   B GLU   A 1 104 ? 25.507 -4.545  -14.174 0.38 23.18 ?  104 GLU   A HA   1 
ATOM   2279 H  HB2  A GLU   A 1 104 ? 24.272 -3.314  -11.552 0.62 26.70 ?  104 GLU   A HB2  1 
ATOM   2280 H  HB2  B GLU   A 1 104 ? 24.328 -3.602  -11.793 0.38 23.36 ?  104 GLU   A HB2  1 
ATOM   2281 H  HB3  A GLU   A 1 104 ? 25.551 -4.254  -11.689 0.62 26.70 ?  104 GLU   A HB3  1 
ATOM   2282 H  HB3  B GLU   A 1 104 ? 25.635 -4.509  -11.823 0.38 23.36 ?  104 GLU   A HB3  1 
ATOM   2283 H  HG2  A GLU   A 1 104 ? 26.750 -2.590  -12.690 0.62 26.08 ?  104 GLU   A HG2  1 
ATOM   2284 H  HG2  B GLU   A 1 104 ? 26.848 -2.843  -12.803 0.38 24.27 ?  104 GLU   A HG2  1 
ATOM   2285 H  HG3  A GLU   A 1 104 ? 25.464 -1.678  -12.836 0.62 26.08 ?  104 GLU   A HG3  1 
ATOM   2286 H  HG3  B GLU   A 1 104 ? 25.546 -1.967  -13.041 0.38 24.27 ?  104 GLU   A HG3  1 
ATOM   2287 N  N    A ASP   A 1 105 ? 24.665 -6.447  -13.530 0.62 24.25 ?  105 ASP   A N    1 
ATOM   2288 N  N    B ASP   A 1 105 ? 24.817 -6.790  -13.290 0.38 18.54 ?  105 ASP   A N    1 
ATOM   2289 C  CA   A ASP   A 1 105 ? 24.161 -7.811  -13.651 0.62 25.09 ?  105 ASP   A CA   1 
ATOM   2290 C  CA   B ASP   A 1 105 ? 24.390 -8.180  -13.412 0.38 18.26 ?  105 ASP   A CA   1 
ATOM   2291 C  C    A ASP   A 1 105 ? 23.485 -8.247  -12.355 0.62 23.48 ?  105 ASP   A C    1 
ATOM   2292 C  C    B ASP   A 1 105 ? 23.626 -8.611  -12.162 0.38 17.02 ?  105 ASP   A C    1 
ATOM   2293 O  O    A ASP   A 1 105 ? 24.127 -8.313  -11.304 0.62 22.33 ?  105 ASP   A O    1 
ATOM   2294 O  O    B ASP   A 1 105 ? 24.189 -8.646  -11.065 0.38 15.39 ?  105 ASP   A O    1 
ATOM   2295 C  CB   A ASP   A 1 105 ? 25.323 -8.743  -13.985 0.62 27.70 ?  105 ASP   A CB   1 
ATOM   2296 C  CB   B ASP   A 1 105 ? 25.639 -9.040  -13.606 0.38 19.64 ?  105 ASP   A CB   1 
ATOM   2297 C  CG   A ASP   A 1 105 ? 24.881 -10.174 -14.177 0.62 30.15 ?  105 ASP   A CG   1 
ATOM   2298 C  CG   B ASP   A 1 105 ? 25.327 -10.498 -13.880 0.38 20.75 ?  105 ASP   A CG   1 
ATOM   2299 O  OD1  A ASP   A 1 105 ? 23.656 -10.409 -14.243 0.62 30.81 ?  105 ASP   A OD1  1 
ATOM   2300 O  OD1  B ASP   A 1 105 ? 24.138 -10.873 -13.931 0.38 20.80 ?  105 ASP   A OD1  1 
ATOM   2301 O  OD2  A ASP   A 1 105 ? 25.756 -11.062 -14.258 0.62 31.71 -1 105 ASP   A OD2  1 
ATOM   2302 O  OD2  B ASP   A 1 105 ? 26.294 -11.275 -14.037 0.38 21.63 -1 105 ASP   A OD2  1 
ATOM   2303 H  H    A ASP   A 1 105 ? 25.521 -6.393  -13.565 0.62 29.12 ?  105 ASP   A H    1 
ATOM   2304 H  H    B ASP   A 1 105 ? 25.635 -6.700  -13.053 0.38 22.27 ?  105 ASP   A H    1 
ATOM   2305 H  HA   A ASP   A 1 105 ? 23.512 -7.865  -14.369 0.62 30.12 ?  105 ASP   A HA   1 
ATOM   2306 H  HA   B ASP   A 1 105 ? 23.811 -8.282  -14.184 0.38 21.94 ?  105 ASP   A HA   1 
ATOM   2307 H  HB2  A ASP   A 1 105 ? 25.747 -8.444  -14.808 0.62 33.26 ?  105 ASP   A HB2  1 
ATOM   2308 H  HB2  B ASP   A 1 105 ? 26.155 -8.675  -14.346 0.38 23.59 ?  105 ASP   A HB2  1 
ATOM   2309 H  HB3  A ASP   A 1 105 ? 25.969 -8.723  -13.260 0.62 33.26 ?  105 ASP   A HB3  1 
ATOM   2310 H  HB3  B ASP   A 1 105 ? 26.165 -9.016  -12.796 0.38 23.59 ?  105 ASP   A HB3  1 
ATOM   2311 N  N    A ILE   A 1 106 ? 22.191 -8.571  -12.436 0.62 22.81 ?  106 ILE   A N    1 
ATOM   2312 N  N    B ILE   A 1 106 ? 22.344 -8.950  -12.329 0.38 17.71 ?  106 ILE   A N    1 
ATOM   2313 C  CA   A ILE   A 1 106 ? 21.433 -8.973  -11.256 0.62 21.92 ?  106 ILE   A CA   1 
ATOM   2314 C  CA   B ILE   A 1 106 ? 21.531 -9.378  -11.192 0.38 18.23 ?  106 ILE   A CA   1 
ATOM   2315 C  C    A ILE   A 1 106 ? 21.950 -10.274 -10.661 0.62 20.38 ?  106 ILE   A C    1 
ATOM   2316 C  C    B ILE   A 1 106 ? 22.115 -10.624 -10.545 0.38 18.82 ?  106 ILE   A C    1 
ATOM   2317 O  O    A ILE   A 1 106 ? 21.712 -10.547 -9.480  0.62 19.00 ?  106 ILE   A O    1 
ATOM   2318 O  O    B ILE   A 1 106 ? 21.919 -10.857 -9.347  0.38 18.60 ?  106 ILE   A O    1 
ATOM   2319 C  CB   A ILE   A 1 106 ? 19.925 -9.055  -11.588 0.62 23.24 ?  106 ILE   A CB   1 
ATOM   2320 C  CB   B ILE   A 1 106 ? 20.064 -9.582  -11.621 0.38 19.33 ?  106 ILE   A CB   1 
ATOM   2321 C  CG1  A ILE   A 1 106 ? 19.082 -9.093  -10.312 0.62 23.53 ?  106 ILE   A CG1  1 
ATOM   2322 C  CG1  B ILE   A 1 106 ? 19.145 -9.703  -10.401 0.38 19.58 ?  106 ILE   A CG1  1 
ATOM   2323 C  CG2  A ILE   A 1 106 ? 19.630 -10.290 -12.415 0.62 24.05 ?  106 ILE   A CG2  1 
ATOM   2324 C  CG2  B ILE   A 1 106 ? 19.926 -10.836 -12.447 0.38 19.75 ?  106 ILE   A CG2  1 
ATOM   2325 C  CD1  A ILE   A 1 106 ? 19.279 -7.903  -9.404  0.62 23.60 ?  106 ILE   A CD1  1 
ATOM   2326 C  CD1  B ILE   A 1 106 ? 18.921 -8.404  -9.662  0.38 19.63 ?  106 ILE   A CD1  1 
ATOM   2327 H  H    A ILE   A 1 106 ? 21.737 -8.559  -13.160 0.62 27.39 ?  106 ILE   A H    1 
ATOM   2328 H  H    B ILE   A 1 106 ? 21.930 -8.942  -13.078 0.38 21.27 ?  106 ILE   A H    1 
ATOM   2329 H  HA   A ILE   A 1 106 ? 21.552 -8.289  -10.584 0.62 26.33 ?  106 ILE   A HA   1 
ATOM   2330 H  HA   B ILE   A 1 106 ? 21.550 -8.686  -10.520 0.38 21.90 ?  106 ILE   A HA   1 
ATOM   2331 H  HB   A ILE   A 1 106 ? 19.678 -8.271  -12.102 0.62 27.91 ?  106 ILE   A HB   1 
ATOM   2332 H  HB   B ILE   A 1 106 ? 19.784 -8.818  -12.151 0.38 23.21 ?  106 ILE   A HB   1 
ATOM   2333 H  HG12 A ILE   A 1 106 ? 18.144 -9.120  -10.561 0.62 28.25 ?  106 ILE   A HG12 1 
ATOM   2334 H  HG12 B ILE   A 1 106 ? 18.280 -10.028 -10.696 0.38 23.51 ?  106 ILE   A HG12 1 
ATOM   2335 H  HG13 A ILE   A 1 106 ? 19.310 -9.890  -9.810  0.62 28.25 ?  106 ILE   A HG13 1 
ATOM   2336 H  HG13 B ILE   A 1 106 ? 19.532 -10.335 -9.775  0.38 23.51 ?  106 ILE   A HG13 1 
ATOM   2337 H  HG21 A ILE   A 1 106 ? 18.751 -10.198 -12.810 0.62 28.88 ?  106 ILE   A HG21 1 
ATOM   2338 H  HG21 B ILE   A 1 106 ? 19.059 -10.828 -12.875 0.38 23.72 ?  106 ILE   A HG21 1 
ATOM   2339 H  HG22 A ILE   A 1 106 ? 20.302 -10.369 -13.108 0.62 28.88 ?  106 ILE   A HG22 1 
ATOM   2340 H  HG22 B ILE   A 1 106 ? 20.631 -10.850 -13.109 0.38 23.72 ?  106 ILE   A HG22 1 
ATOM   2341 H  HG23 A ILE   A 1 106 ? 19.655 -11.069 -11.837 0.62 28.88 ?  106 ILE   A HG23 1 
ATOM   2342 H  HG23 B ILE   A 1 106 ? 20.000 -11.606 -11.862 0.38 23.72 ?  106 ILE   A HG23 1 
ATOM   2343 H  HD11 A ILE   A 1 106 ? 18.533 -7.849  -8.790  0.62 28.34 ?  106 ILE   A HD11 1 
ATOM   2344 H  HD11 B ILE   A 1 106 ? 18.259 -8.550  -8.966  0.38 23.58 ?  106 ILE   A HD11 1 
ATOM   2345 H  HD12 A ILE   A 1 106 ? 20.107 -8.016  -8.910  0.62 28.34 ?  106 ILE   A HD12 1 
ATOM   2346 H  HD12 B ILE   A 1 106 ? 19.756 -8.114  -9.268  0.38 23.58 ?  106 ILE   A HD12 1 
ATOM   2347 H  HD13 A ILE   A 1 106 ? 19.322 -7.098  -9.944  0.62 28.34 ?  106 ILE   A HD13 1 
ATOM   2348 H  HD13 B ILE   A 1 106 ? 18.597 -7.738  -10.289 0.38 23.58 ?  106 ILE   A HD13 1 
ATOM   2349 N  N    A GLN   A 1 107 ? 22.663 -11.086 -11.448 0.62 21.52 ?  107 GLN   A N    1 
ATOM   2350 N  N    B GLN   A 1 107 ? 22.840 -11.443 -11.317 0.38 20.16 ?  107 GLN   A N    1 
ATOM   2351 C  CA   A GLN   A 1 107 ? 23.266 -12.304 -10.917 0.62 23.51 ?  107 GLN   A CA   1 
ATOM   2352 C  CA   B GLN   A 1 107 ? 23.509 -12.607 -10.745 0.38 22.44 ?  107 GLN   A CA   1 
ATOM   2353 C  C    A GLN   A 1 107 ? 24.250 -12.009 -9.790  0.62 20.94 ?  107 GLN   A C    1 
ATOM   2354 C  C    B GLN   A 1 107 ? 24.457 -12.206 -9.622  0.38 20.34 ?  107 GLN   A C    1 
ATOM   2355 O  O    A GLN   A 1 107 ? 24.496 -12.879 -8.947  0.62 22.51 ?  107 GLN   A O    1 
ATOM   2356 O  O    B GLN   A 1 107 ? 24.727 -13.006 -8.718  0.38 20.63 ?  107 GLN   A O    1 
ATOM   2357 C  CB   A GLN   A 1 107 ? 23.951 -13.081 -12.048 0.62 28.18 ?  107 GLN   A CB   1 
ATOM   2358 C  CB   B GLN   A 1 107 ? 24.252 -13.373 -11.844 0.38 26.40 ?  107 GLN   A CB   1 
ATOM   2359 C  CG   A GLN   A 1 107 ? 23.054 -13.339 -13.258 0.62 33.39 ?  107 GLN   A CG   1 
ATOM   2360 C  CG   B GLN   A 1 107 ? 23.341 -13.919 -12.938 0.38 30.32 ?  107 GLN   A CG   1 
ATOM   2361 C  CD   A GLN   A 1 107 ? 21.778 -14.077 -12.896 0.62 37.85 ?  107 GLN   A CD   1 
ATOM   2362 C  CD   B GLN   A 1 107 ? 22.348 -14.938 -12.411 0.38 33.79 ?  107 GLN   A CD   1 
ATOM   2363 O  OE1  A GLN   A 1 107 ? 21.808 -15.083 -12.186 0.62 39.48 ?  107 GLN   A OE1  1 
ATOM   2364 O  OE1  B GLN   A 1 107 ? 22.683 -15.766 -11.563 0.38 34.55 ?  107 GLN   A OE1  1 
ATOM   2365 N  NE2  A GLN   A 1 107 ? 20.647 -13.576 -13.382 0.62 39.16 ?  107 GLN   A NE2  1 
ATOM   2366 N  NE2  B GLN   A 1 107 ? 21.117 -14.877 -12.907 0.38 34.75 ?  107 GLN   A NE2  1 
ATOM   2367 H  H    A GLN   A 1 107 ? 22.815 -10.948 -12.282 0.62 25.85 ?  107 GLN   A H    1 
ATOM   2368 H  H    B GLN   A 1 107 ? 22.962 -11.347 -12.164 0.38 24.22 ?  107 GLN   A H    1 
ATOM   2369 H  HA   A GLN   A 1 107 ? 22.569 -12.870 -10.558 0.62 28.23 ?  107 GLN   A HA   1 
ATOM   2370 H  HA   B GLN   A 1 107 ? 22.846 -13.204 -10.369 0.38 26.95 ?  107 GLN   A HA   1 
ATOM   2371 H  HB2  A GLN   A 1 107 ? 24.721 -12.579 -12.359 0.62 33.83 ?  107 GLN   A HB2  1 
ATOM   2372 H  HB2  B GLN   A 1 107 ? 24.893 -12.781 -12.269 0.38 31.70 ?  107 GLN   A HB2  1 
ATOM   2373 H  HB3  A GLN   A 1 107 ? 24.238 -13.945 -11.712 0.62 33.83 ?  107 GLN   A HB3  1 
ATOM   2374 H  HB3  B GLN   A 1 107 ? 24.716 -14.129 -11.450 0.38 31.70 ?  107 GLN   A HB3  1 
ATOM   2375 H  HG2  A GLN   A 1 107 ? 22.803 -12.492 -13.658 0.62 40.08 ?  107 GLN   A HG2  1 
ATOM   2376 H  HG2  B GLN   A 1 107 ? 22.839 -13.186 -13.330 0.38 36.40 ?  107 GLN   A HG2  1 
ATOM   2377 H  HG3  A GLN   A 1 107 ? 23.539 -13.876 -13.905 0.62 40.08 ?  107 GLN   A HG3  1 
ATOM   2378 H  HG3  B GLN   A 1 107 ? 23.881 -14.351 -13.620 0.38 36.40 ?  107 GLN   A HG3  1 
ATOM   2379 H  HE21 A GLN   A 1 107 ? 20.664 -12.870 -13.874 0.62 47.01 ?  107 GLN   A HE21 1 
ATOM   2380 H  HE21 B GLN   A 1 107 ? 20.919 -14.283 -13.496 0.38 41.72 ?  107 GLN   A HE21 1 
ATOM   2381 H  HE22 A GLN   A 1 107 ? 19.898 -13.959 -13.206 0.62 47.01 ?  107 GLN   A HE22 1 
ATOM   2382 H  HE22 B GLN   A 1 107 ? 20.518 -15.433 -12.638 0.38 41.72 ?  107 GLN   A HE22 1 
ATOM   2383 N  N    A LEU   A 1 108 ? 24.799 -10.793 -9.736  0.62 17.11 ?  108 LEU   A N    1 
ATOM   2384 N  N    B LEU   A 1 108 ? 24.958 -10.970 -9.649  0.38 18.18 ?  108 LEU   A N    1 
ATOM   2385 C  CA   A LEU   A 1 108 ? 25.728 -10.420 -8.675  0.62 15.33 ?  108 LEU   A CA   1 
ATOM   2386 C  CA   B LEU   A 1 108 ? 25.809 -10.485 -8.573  0.38 16.66 ?  108 LEU   A CA   1 
ATOM   2387 C  C    A LEU   A 1 108 ? 25.035 -10.256 -7.329  0.62 14.29 ?  108 LEU   A C    1 
ATOM   2388 C  C    B LEU   A 1 108 ? 25.040 -10.249 -7.280  0.38 15.13 ?  108 LEU   A C    1 
ATOM   2389 O  O    A LEU   A 1 108 ? 25.716 -10.107 -6.311  0.62 14.56 ?  108 LEU   A O    1 
ATOM   2390 O  O    B LEU   A 1 108 ? 25.672 -10.024 -6.243  0.38 15.29 ?  108 LEU   A O    1 
ATOM   2391 C  CB   A LEU   A 1 108 ? 26.475 -9.139  -9.062  0.62 15.29 ?  108 LEU   A CB   1 
ATOM   2392 C  CB   B LEU   A 1 108 ? 26.540 -9.209  -9.001  0.38 16.84 ?  108 LEU   A CB   1 
ATOM   2393 C  CG   A LEU   A 1 108 ? 27.451 -9.334  -10.225 0.62 16.74 ?  108 LEU   A CG   1 
ATOM   2394 C  CG   B LEU   A 1 108 ? 27.531 -9.404  -10.152 0.38 17.77 ?  108 LEU   A CG   1 
ATOM   2395 C  CD1  A LEU   A 1 108 ? 27.912 -8.000  -10.794 0.62 17.90 ?  108 LEU   A CD1  1 
ATOM   2396 C  CD1  B LEU   A 1 108 ? 28.083 -8.072  -10.640 0.38 18.39 ?  108 LEU   A CD1  1 
ATOM   2397 C  CD2  A LEU   A 1 108 ? 28.652 -10.161 -9.789  0.62 18.47 ?  108 LEU   A CD2  1 
ATOM   2398 C  CD2  B LEU   A 1 108 ? 28.666 -10.329 -9.737  0.38 18.87 ?  108 LEU   A CD2  1 
ATOM   2399 H  H    A LEU   A 1 108 ? 24.645 -10.173 -10.304 0.62 20.56 ?  108 LEU   A H    1 
ATOM   2400 H  H    B LEU   A 1 108 ? 24.820 -10.403 -10.274 0.38 21.84 ?  108 LEU   A H    1 
ATOM   2401 H  HA   A LEU   A 1 108 ? 26.383 -11.127 -8.576  0.62 18.42 ?  108 LEU   A HA   1 
ATOM   2402 H  HA   B LEU   A 1 108 ? 26.480 -11.158 -8.384  0.38 20.01 ?  108 LEU   A HA   1 
ATOM   2403 H  HB2  A LEU   A 1 108 ? 25.827 -8.468  -9.329  0.62 18.37 ?  108 LEU   A HB2  1 
ATOM   2404 H  HB2  B LEU   A 1 108 ? 25.885 -8.554  -9.285  0.38 20.23 ?  108 LEU   A HB2  1 
ATOM   2405 H  HB3  A LEU   A 1 108 ? 26.980 -8.829  -8.297  0.62 18.37 ?  108 LEU   A HB3  1 
ATOM   2406 H  HB3  B LEU   A 1 108 ? 27.037 -8.867  -8.242  0.38 20.23 ?  108 LEU   A HB3  1 
ATOM   2407 H  HG   A LEU   A 1 108 ? 27.003 -9.818  -10.936 0.62 20.11 ?  108 LEU   A HG   1 
ATOM   2408 H  HG   B LEU   A 1 108 ? 27.069 -9.821  -10.894 0.38 21.34 ?  108 LEU   A HG   1 
ATOM   2409 H  HD11 A LEU   A 1 108 ? 28.522 -8.164  -11.534 0.62 21.50 ?  108 LEU   A HD11 1 
ATOM   2410 H  HD11 B LEU   A 1 108 ? 28.699 -8.234  -11.373 0.38 22.08 ?  108 LEU   A HD11 1 
ATOM   2411 H  HD12 A LEU   A 1 108 ? 27.141 -7.504  -11.106 0.62 21.50 ?  108 LEU   A HD12 1 
ATOM   2412 H  HD12 B LEU   A 1 108 ? 27.347 -7.518  -10.945 0.38 22.08 ?  108 LEU   A HD12 1 
ATOM   2413 H  HD13 A LEU   A 1 108 ? 28.369 -7.500  -10.098 0.62 21.50 ?  108 LEU   A HD13 1 
ATOM   2414 H  HD13 B LEU   A 1 108 ? 28.546 -7.634  -9.909  0.38 22.08 ?  108 LEU   A HD13 1 
ATOM   2415 H  HD21 A LEU   A 1 108 ? 29.317 -10.148 -10.494 0.62 22.18 ?  108 LEU   A HD21 1 
ATOM   2416 H  HD21 B LEU   A 1 108 ? 29.365 -10.290 -10.407 0.38 22.66 ?  108 LEU   A HD21 1 
ATOM   2417 H  HD22 A LEU   A 1 108 ? 29.020 -9.777  -8.978  0.62 22.18 ?  108 LEU   A HD22 1 
ATOM   2418 H  HD22 B LEU   A 1 108 ? 29.012 -10.036 -8.879  0.38 22.66 ?  108 LEU   A HD22 1 
ATOM   2419 H  HD23 A LEU   A 1 108 ? 28.364 -11.072 -9.622  0.62 22.18 ?  108 LEU   A HD23 1 
ATOM   2420 H  HD23 B LEU   A 1 108 ? 28.324 -11.233 -9.664  0.38 22.66 ?  108 LEU   A HD23 1 
ATOM   2421 N  N    . LEU   A 1 109 ? 23.703 -10.311 -7.297  1.00 14.09 ?  109 LEU   A N    1 
ATOM   2422 C  CA   . LEU   A 1 109 ? 22.981 -10.181 -6.039  1.00 13.47 ?  109 LEU   A CA   1 
ATOM   2423 C  C    . LEU   A 1 109 ? 23.315 -11.331 -5.093  1.00 12.80 ?  109 LEU   A C    1 
ATOM   2424 O  O    . LEU   A 1 109 ? 23.444 -11.133 -3.882  1.00 13.32 ?  109 LEU   A O    1 
ATOM   2425 C  CB   . LEU   A 1 109 ? 21.482 -10.103 -6.314  1.00 14.21 ?  109 LEU   A CB   1 
ATOM   2426 C  CG   . LEU   A 1 109 ? 20.568 -9.822  -5.121  1.00 14.65 ?  109 LEU   A CG   1 
ATOM   2427 C  CD1  . LEU   A 1 109 ? 21.018 -8.571  -4.384  1.00 14.53 ?  109 LEU   A CD1  1 
ATOM   2428 C  CD2  . LEU   A 1 109 ? 19.127 -9.682  -5.587  1.00 15.46 ?  109 LEU   A CD2  1 
ATOM   2429 H  H    A LEU   A 1 109 ? 23.198 -10.425 -7.984  0.62 16.93 ?  109 LEU   A H    1 
ATOM   2430 H  H    B LEU   A 1 109 ? 23.212 -10.427 -7.994  0.38 16.93 ?  109 LEU   A H    1 
ATOM   2431 H  HA   . LEU   A 1 109 ? 23.252 -9.351  -5.612  1.00 16.19 ?  109 LEU   A HA   1 
ATOM   2432 H  HB2  . LEU   A 1 109 ? 21.330 -9.396  -6.960  1.00 17.07 ?  109 LEU   A HB2  1 
ATOM   2433 H  HB3  . LEU   A 1 109 ? 21.201 -10.948 -6.691  1.00 17.07 ?  109 LEU   A HB3  1 
ATOM   2434 H  HG   . LEU   A 1 109 ? 20.612 -10.564 -4.501  1.00 17.60 ?  109 LEU   A HG   1 
ATOM   2435 H  HD11 . LEU   A 1 109 ? 20.324 -8.292  -3.773  1.00 17.45 ?  109 LEU   A HD11 1 
ATOM   2436 H  HD12 . LEU   A 1 109 ? 21.835 -8.767  -3.896  1.00 17.45 ?  109 LEU   A HD12 1 
ATOM   2437 H  HD13 . LEU   A 1 109 ? 21.188 -7.866  -5.035  1.00 17.45 ?  109 LEU   A HD13 1 
ATOM   2438 H  HD21 . LEU   A 1 109 ? 18.572 -9.410  -4.835  1.00 18.57 ?  109 LEU   A HD21 1 
ATOM   2439 H  HD22 . LEU   A 1 109 ? 19.079 -9.010  -6.287  1.00 18.57 ?  109 LEU   A HD22 1 
ATOM   2440 H  HD23 . LEU   A 1 109 ? 18.817 -10.536 -5.930  1.00 18.57 ?  109 LEU   A HD23 1 
ATOM   2441 N  N    . LYS   A 1 110 ? 23.447 -12.547 -5.622  1.00 12.83 ?  110 LYS   A N    1 
ATOM   2442 C  CA   . LYS   A 1 110 ? 23.817 -13.668 -4.763  1.00 12.96 ?  110 LYS   A CA   1 
ATOM   2443 C  C    . LYS   A 1 110 ? 25.194 -13.445 -4.147  1.00 12.20 ?  110 LYS   A C    1 
ATOM   2444 O  O    . LYS   A 1 110 ? 25.385 -13.644 -2.944  1.00 12.50 ?  110 LYS   A O    1 
ATOM   2445 C  CB   . LYS   A 1 110 ? 23.757 -14.988 -5.533  1.00 13.65 ?  110 LYS   A CB   1 
ATOM   2446 C  CG   . LYS   A 1 110 ? 23.925 -16.199 -4.624  1.00 14.19 ?  110 LYS   A CG   1 
ATOM   2447 C  CD   . LYS   A 1 110 ? 23.693 -17.515 -5.341  1.00 14.93 ?  110 LYS   A CD   1 
ATOM   2448 C  CE   . LYS   A 1 110 ? 23.813 -18.697 -4.392  1.00 15.81 ?  110 LYS   A CE   1 
ATOM   2449 N  NZ   . LYS   A 1 110 ? 22.640 -18.836 -3.495  1.00 16.06 ?  110 LYS   A NZ   1 
ATOM   2450 H  H    . LYS   A 1 110 ? 23.324 -12.743 -6.446  1.00 15.42 ?  110 LYS   A H    1 
ATOM   2451 H  HA   . LYS   A 1 110 ? 23.174 -13.725 -4.035  1.00 15.57 ?  110 LYS   A HA   1 
ATOM   2452 H  HB2  . LYS   A 1 110 ? 22.896 -15.059 -5.974  1.00 16.40 ?  110 LYS   A HB2  1 
ATOM   2453 H  HB3  . LYS   A 1 110 ? 24.471 -15.004 -6.187  1.00 16.40 ?  110 LYS   A HB3  1 
ATOM   2454 H  HG2  . LYS   A 1 110 ? 24.823 -16.205 -4.266  1.00 17.05 ?  110 LYS   A HG2  1 
ATOM   2455 H  HG3  . LYS   A 1 110 ? 23.279 -16.138 -3.899  1.00 17.05 ?  110 LYS   A HG3  1 
ATOM   2456 H  HD2  . LYS   A 1 110 ? 22.803 -17.524 -5.719  1.00 17.94 ?  110 LYS   A HD2  1 
ATOM   2457 H  HD3  . LYS   A 1 110 ? 24.359 -17.618 -6.039  1.00 17.94 ?  110 LYS   A HD3  1 
ATOM   2458 H  HE2  . LYS   A 1 110 ? 23.899 -19.513 -4.908  1.00 18.99 ?  110 LYS   A HE2  1 
ATOM   2459 H  HE3  . LYS   A 1 110 ? 24.605 -18.576 -3.835  1.00 18.99 ?  110 LYS   A HE3  1 
ATOM   2460 H  HZ1  . LYS   A 1 110 ? 22.745 -19.532 -2.955  1.00 19.29 ?  110 LYS   A HZ1  1 
ATOM   2461 H  HZ2  . LYS   A 1 110 ? 22.544 -18.098 -3.002  1.00 19.29 ?  110 LYS   A HZ2  1 
ATOM   2462 H  HZ3  . LYS   A 1 110 ? 21.901 -18.952 -3.980  1.00 19.29 ?  110 LYS   A HZ3  1 
ATOM   2463 N  N    . SER   A 1 111 ? 26.156 -12.992 -4.954  1.00 12.16 ?  111 SER   A N    1 
ATOM   2464 C  CA   . SER   A 1 111 ? 27.486 -12.698 -4.432  1.00 12.47 ?  111 SER   A CA   1 
ATOM   2465 C  C    . SER   A 1 111 ? 27.421 -11.647 -3.328  1.00 12.15 ?  111 SER   A C    1 
ATOM   2466 O  O    . SER   A 1 111 ? 28.120 -11.747 -2.315  1.00 12.94 ?  111 SER   A O    1 
ATOM   2467 C  CB   . SER   A 1 111 ? 28.383 -12.212 -5.571  1.00 14.05 ?  111 SER   A CB   1 
ATOM   2468 O  OG   . SER   A 1 111 ? 28.435 -13.186 -6.603  1.00 16.07 ?  111 SER   A OG   1 
ATOM   2469 H  H    . SER   A 1 111 ? 26.059 -12.850 -5.794  1.00 14.62 ?  111 SER   A H    1 
ATOM   2470 H  HA   . SER   A 1 111 ? 27.874 -13.511 -4.065  1.00 14.99 ?  111 SER   A HA   1 
ATOM   2471 H  HB2  . SER   A 1 111 ? 28.016 -11.393 -5.936  1.00 16.88 ?  111 SER   A HB2  1 
ATOM   2472 H  HB3  . SER   A 1 111 ? 29.276 -12.056 -5.228  1.00 16.88 ?  111 SER   A HB3  1 
ATOM   2473 H  HG   . SER   A 1 111 ? 28.941 -12.912 -7.227  1.00 19.30 ?  111 SER   A HG   1 
ATOM   2474 N  N    . ALA   A 1 112 ? 26.587 -10.621 -3.515  1.00 12.02 ?  112 ALA   A N    1 
ATOM   2475 C  CA   . ALA   A 1 112 ? 26.435 -9.583  -2.498  1.00 11.85 ?  112 ALA   A CA   1 
ATOM   2476 C  C    . ALA   A 1 112 ? 25.942 -10.177 -1.180  1.00 11.73 ?  112 ALA   A C    1 
ATOM   2477 O  O    . ALA   A 1 112 ? 26.479 -9.881  -0.107  1.00 11.97 ?  112 ALA   A O    1 
ATOM   2478 C  CB   . ALA   A 1 112 ? 25.474 -8.499  -3.000  1.00 12.50 ?  112 ALA   A CB   1 
ATOM   2479 H  H    . ALA   A 1 112 ? 26.105 -10.504 -4.218  1.00 14.45 ?  112 ALA   A H    1 
ATOM   2480 H  HA   . ALA   A 1 112 ? 27.295 -9.163  -2.341  1.00 14.24 ?  112 ALA   A HA   1 
ATOM   2481 H  HB1  . ALA   A 1 112 ? 25.414 -7.793  -2.333  1.00 15.02 ?  112 ALA   A HB1  1 
ATOM   2482 H  HB2  . ALA   A 1 112 ? 25.810 -8.133  -3.833  1.00 15.02 ?  112 ALA   A HB2  1 
ATOM   2483 H  HB3  . ALA   A 1 112 ? 24.597 -8.890  -3.143  1.00 15.02 ?  112 ALA   A HB3  1 
ATOM   2484 N  N    . TYR   A 1 113 ? 24.907 -11.021 -1.240  1.00 12.08 ?  113 TYR   A N    1 
ATOM   2485 C  CA   . TYR   A 1 113 ? 24.383 -11.633 -0.022  1.00 11.85 ?  113 TYR   A CA   1 
ATOM   2486 C  C    . TYR   A 1 113 ? 25.385 -12.577 0.640   1.00 11.02 ?  113 TYR   A C    1 
ATOM   2487 O  O    . TYR   A 1 113 ? 25.337 -12.754 1.863   1.00 12.07 ?  113 TYR   A O    1 
ATOM   2488 C  CB   . TYR   A 1 113 ? 23.075 -12.373 -0.315  1.00 12.13 ?  113 TYR   A CB   1 
ATOM   2489 C  CG   . TYR   A 1 113 ? 21.855 -11.487 -0.237  1.00 12.22 ?  113 TYR   A CG   1 
ATOM   2490 C  CD1  . TYR   A 1 113 ? 21.483 -10.891 0.962   1.00 12.78 ?  113 TYR   A CD1  1 
ATOM   2491 C  CD2  . TYR   A 1 113 ? 21.054 -11.266 -1.352  1.00 12.60 ?  113 TYR   A CD2  1 
ATOM   2492 C  CE1  . TYR   A 1 113 ? 20.347 -10.100 1.051   1.00 13.07 ?  113 TYR   A CE1  1 
ATOM   2493 C  CE2  . TYR   A 1 113 ? 19.904 -10.469 -1.272  1.00 12.94 ?  113 TYR   A CE2  1 
ATOM   2494 C  CZ   . TYR   A 1 113 ? 19.564 -9.894  -0.064  1.00 12.92 ?  113 TYR   A CZ   1 
ATOM   2495 O  OH   . TYR   A 1 113 ? 18.437 -9.103  0.048   1.00 13.62 ?  113 TYR   A OH   1 
ATOM   2496 H  H    . TYR   A 1 113 ? 24.508 -11.250 -1.965  1.00 14.51 ?  113 TYR   A H    1 
ATOM   2497 H  HA   . TYR   A 1 113 ? 24.196 -10.935 0.612   1.00 14.24 ?  113 TYR   A HA   1 
ATOM   2498 H  HB2  . TYR   A 1 113 ? 23.114 -12.741 -1.211  1.00 14.58 ?  113 TYR   A HB2  1 
ATOM   2499 H  HB3  . TYR   A 1 113 ? 22.968 -13.086 0.332   1.00 14.58 ?  113 TYR   A HB3  1 
ATOM   2500 H  HD1  . TYR   A 1 113 ? 22.003 -11.036 1.722   1.00 15.36 ?  113 TYR   A HD1  1 
ATOM   2501 H  HD2  . TYR   A 1 113 ? 21.276 -11.662 -2.160  1.00 15.14 ?  113 TYR   A HD2  1 
ATOM   2502 H  HE1  . TYR   A 1 113 ? 20.116 -9.712  1.864   1.00 15.70 ?  113 TYR   A HE1  1 
ATOM   2503 H  HE2  . TYR   A 1 113 ? 19.370 -10.326 -2.019  1.00 15.54 ?  113 TYR   A HE2  1 
ATOM   2504 H  HH   . TYR   A 1 113 ? 18.045 -9.059  -0.694  1.00 16.37 ?  113 TYR   A HH   1 
ATOM   2505 N  N    . GLU   A 1 114 ? 26.292 -13.194 -0.135  1.00 11.48 ?  114 GLU   A N    1 
ATOM   2506 C  CA   . GLU   A 1 114 ? 27.284 -14.088 0.472   1.00 12.16 ?  114 GLU   A CA   1 
ATOM   2507 C  C    . GLU   A 1 114 ? 28.127 -13.368 1.522   1.00 11.82 ?  114 GLU   A C    1 
ATOM   2508 O  O    . GLU   A 1 114 ? 28.602 -13.998 2.477   1.00 12.57 ?  114 GLU   A O    1 
ATOM   2509 C  CB   . GLU   A 1 114 ? 28.167 -14.735 -0.607  1.00 12.32 ?  114 GLU   A CB   1 
ATOM   2510 C  CG   . GLU   A 1 114 ? 27.413 -15.788 -1.388  1.00 13.05 ?  114 GLU   A CG   1 
ATOM   2511 C  CD   . GLU   A 1 114 ? 28.136 -16.315 -2.622  1.00 13.11 ?  114 GLU   A CD   1 
ATOM   2512 O  OE1  . GLU   A 1 114 ? 29.080 -15.674 -3.128  1.00 13.77 ?  114 GLU   A OE1  1 
ATOM   2513 O  OE2  . GLU   A 1 114 ? 27.698 -17.374 -3.120  1.00 14.50 -1 114 GLU   A OE2  1 
ATOM   2514 H  H    . GLU   A 1 114 ? 26.355 -13.113 -0.997  1.00 13.80 ?  114 GLU   A H    1 
ATOM   2515 H  HA   . GLU   A 1 114 ? 26.813 -14.803 0.920   1.00 14.61 ?  114 GLU   A HA   1 
ATOM   2516 H  HB2  . GLU   A 1 114 ? 28.465 -14.051 -1.232  1.00 14.80 ?  114 GLU   A HB2  1 
ATOM   2517 H  HB3  . GLU   A 1 114 ? 28.930 -15.158 -0.188  1.00 14.80 ?  114 GLU   A HB3  1 
ATOM   2518 H  HG2  . GLU   A 1 114 ? 27.251 -16.548 -0.811  1.00 15.68 ?  114 GLU   A HG2  1 
ATOM   2519 H  HG3  . GLU   A 1 114 ? 26.565 -15.414 -1.679  1.00 15.68 ?  114 GLU   A HG3  1 
ATOM   2520 N  N    . ASN   A 1 115 ? 28.310 -12.052 1.379   1.00 12.02 ?  115 ASN   A N    1 
ATOM   2521 C  CA   . ASN   A 1 115 ? 29.069 -11.321 2.389   1.00 12.32 ?  115 ASN   A CA   1 
ATOM   2522 C  C    . ASN   A 1 115 ? 28.443 -11.446 3.773   1.00 12.23 ?  115 ASN   A C    1 
ATOM   2523 O  O    . ASN   A 1 115 ? 29.149 -11.373 4.784   1.00 12.41 ?  115 ASN   A O    1 
ATOM   2524 C  CB   . ASN   A 1 115 ? 29.179 -9.846  2.002   1.00 12.60 ?  115 ASN   A CB   1 
ATOM   2525 C  CG   . ASN   A 1 115 ? 29.978 -9.637  0.739   1.00 13.27 ?  115 ASN   A CG   1 
ATOM   2526 O  OD1  . ASN   A 1 115 ? 31.196 -9.751  0.760   1.00 16.27 ?  115 ASN   A OD1  1 
ATOM   2527 N  ND2  . ASN   A 1 115 ? 29.309 -9.324  -0.359  1.00 12.80 ?  115 ASN   A ND2  1 
ATOM   2528 H  H    . ASN   A 1 115 ? 28.007 -11.571 0.734   1.00 14.44 ?  115 ASN   A H    1 
ATOM   2529 H  HA   . ASN   A 1 115 ? 29.962 -11.687 2.435   1.00 14.80 ?  115 ASN   A HA   1 
ATOM   2530 H  HB2  . ASN   A 1 115 ? 28.288 -9.488  1.867   1.00 15.14 ?  115 ASN   A HB2  1 
ATOM   2531 H  HB3  . ASN   A 1 115 ? 29.622 -9.367  2.722   1.00 15.14 ?  115 ASN   A HB3  1 
ATOM   2532 H  HD21 . ASN   A 1 115 ? 29.726 -9.201  -1.102  1.00 15.37 ?  115 ASN   A HD21 1 
ATOM   2533 H  HD22 . ASN   A 1 115 ? 28.449 -9.272  -0.337  1.00 15.37 ?  115 ASN   A HD22 1 
ATOM   2534 N  N    . PHE   A 1 116 ? 27.116 -11.613 3.844   1.00 12.12 ?  116 PHE   A N    1 
ATOM   2535 C  CA   . PHE   A 1 116 ? 26.453 -11.711 5.143   1.00 11.77 ?  116 PHE   A CA   1 
ATOM   2536 C  C    . PHE   A 1 116 ? 26.930 -12.936 5.923   1.00 12.31 ?  116 PHE   A C    1 
ATOM   2537 O  O    . PHE   A 1 116 ? 26.857 -12.953 7.156   1.00 12.94 ?  116 PHE   A O    1 
ATOM   2538 C  CB   . PHE   A 1 116 ? 24.928 -11.840 4.998   1.00 12.27 ?  116 PHE   A CB   1 
ATOM   2539 C  CG   . PHE   A 1 116 ? 24.180 -10.594 4.528   1.00 11.84 ?  116 PHE   A CG   1 
ATOM   2540 C  CD1  . PHE   A 1 116 ? 24.758 -9.564  3.789   1.00 11.76 ?  116 PHE   A CD1  1 
ATOM   2541 C  CD2  . PHE   A 1 116 ? 22.826 -10.500 4.837   1.00 12.71 ?  116 PHE   A CD2  1 
ATOM   2542 C  CE1  . PHE   A 1 116 ? 23.987 -8.489  3.360   1.00 12.38 ?  116 PHE   A CE1  1 
ATOM   2543 C  CE2  . PHE   A 1 116 ? 22.059 -9.425  4.425   1.00 12.70 ?  116 PHE   A CE2  1 
ATOM   2544 C  CZ   . PHE   A 1 116 ? 22.638 -8.416  3.688   1.00 12.23 ?  116 PHE   A CZ   1 
ATOM   2545 H  H    . PHE   A 1 116 ? 26.585 -11.661 3.167   1.00 14.56 ?  116 PHE   A H    1 
ATOM   2546 H  HA   . PHE   A 1 116 ? 26.643 -10.918 5.666   1.00 14.15 ?  116 PHE   A HA   1 
ATOM   2547 H  HB2  . PHE   A 1 116 ? 24.741 -12.549 4.361   1.00 14.74 ?  116 PHE   A HB2  1 
ATOM   2548 H  HB3  . PHE   A 1 116 ? 24.561 -12.090 5.864   1.00 14.74 ?  116 PHE   A HB3  1 
ATOM   2549 H  HD1  . PHE   A 1 116 ? 25.652 -9.623  3.558   1.00 14.13 ?  116 PHE   A HD1  1 
ATOM   2550 H  HD2  . PHE   A 1 116 ? 22.423 -11.187 5.331   1.00 15.27 ?  116 PHE   A HD2  1 
ATOM   2551 H  HE1  . PHE   A 1 116 ? 24.387 -7.809  2.870   1.00 14.87 ?  116 PHE   A HE1  1 
ATOM   2552 H  HE2  . PHE   A 1 116 ? 21.153 -9.384  4.652   1.00 15.26 ?  116 PHE   A HE2  1 
ATOM   2553 H  HZ   . PHE   A 1 116 ? 22.128 -7.685  3.417   1.00 14.69 ?  116 PHE   A HZ   1 
ATOM   2554 N  N    . ASN   A 1 117 ? 27.381 -13.986 5.227   1.00 12.36 ?  117 ASN   A N    1 
ATOM   2555 C  CA   . ASN   A 1 117 ? 27.740 -15.226 5.907   1.00 12.78 ?  117 ASN   A CA   1 
ATOM   2556 C  C    . ASN   A 1 117 ? 28.999 -15.108 6.743   1.00 13.39 ?  117 ASN   A C    1 
ATOM   2557 O  O    . ASN   A 1 117 ? 29.292 -16.029 7.515   1.00 13.99 ?  117 ASN   A O    1 
ATOM   2558 C  CB   . ASN   A 1 117 ? 27.864 -16.357 4.897   1.00 12.82 ?  117 ASN   A CB   1 
ATOM   2559 C  CG   . ASN   A 1 117 ? 26.525 -16.742 4.343   1.00 13.12 ?  117 ASN   A CG   1 
ATOM   2560 O  OD1  . ASN   A 1 117 ? 25.538 -16.759 5.073   1.00 13.90 ?  117 ASN   A OD1  1 
ATOM   2561 N  ND2  . ASN   A 1 117 ? 26.463 -17.003 3.053   1.00 12.74 ?  117 ASN   A ND2  1 
ATOM   2562 H  H    . ASN   A 1 117 ? 27.465 -14.009 4.370   1.00 14.85 ?  117 ASN   A H    1 
ATOM   2563 H  HA   . ASN   A 1 117 ? 27.016 -15.458 6.513   1.00 15.35 ?  117 ASN   A HA   1 
ATOM   2564 H  HB2  . ASN   A 1 117 ? 28.431 -16.066 4.165   1.00 15.41 ?  117 ASN   A HB2  1 
ATOM   2565 H  HB3  . ASN   A 1 117 ? 28.250 -17.130 5.336   1.00 15.41 ?  117 ASN   A HB3  1 
ATOM   2566 H  HD21 . ASN   A 1 117 ? 25.718 -17.222 2.703   1.00 15.31 ?  117 ASN   A HD21 1 
ATOM   2567 H  HD22 . ASN   A 1 117 ? 27.181 -16.969 2.581   1.00 15.31 ?  117 ASN   A HD22 1 
ATOM   2568 N  N    . GLN   A 1 118 ? 29.730 -14.003 6.623   1.00 13.12 ?  118 GLN   A N    1 
ATOM   2569 C  CA   . GLN   A 1 118 ? 30.896 -13.771 7.460   1.00 13.75 ?  118 GLN   A CA   1 
ATOM   2570 C  C    . GLN   A 1 118 ? 30.543 -13.198 8.827   1.00 13.98 ?  118 GLN   A C    1 
ATOM   2571 O  O    . GLN   A 1 118 ? 31.459 -12.920 9.609   1.00 15.33 ?  118 GLN   A O    1 
ATOM   2572 C  CB   . GLN   A 1 118 ? 31.896 -12.865 6.734   1.00 14.28 ?  118 GLN   A CB   1 
ATOM   2573 C  CG   . GLN   A 1 118 ? 32.370 -13.436 5.408   1.00 14.34 ?  118 GLN   A CG   1 
ATOM   2574 C  CD   . GLN   A 1 118 ? 33.222 -14.685 5.579   1.00 14.53 ?  118 GLN   A CD   1 
ATOM   2575 O  OE1  . GLN   A 1 118 ? 34.089 -14.743 6.459   1.00 15.13 ?  118 GLN   A OE1  1 
ATOM   2576 N  NE2  . GLN   A 1 118 ? 32.982 -15.688 4.736   1.00 14.83 ?  118 GLN   A NE2  1 
ATOM   2577 H  H    . GLN   A 1 118 ? 29.560 -13.356 6.070   1.00 15.76 ?  118 GLN   A H    1 
ATOM   2578 H  HA   . GLN   A 1 118 ? 31.327 -14.625 7.608   1.00 16.52 ?  118 GLN   A HA   1 
ATOM   2579 H  HB2  . GLN   A 1 118 ? 31.480 -12.010 6.560   1.00 17.16 ?  118 GLN   A HB2  1 
ATOM   2580 H  HB3  . GLN   A 1 118 ? 32.676 -12.747 7.301   1.00 17.16 ?  118 GLN   A HB3  1 
ATOM   2581 H  HG2  . GLN   A 1 118 ? 31.601 -13.669 4.865   1.00 17.22 ?  118 GLN   A HG2  1 
ATOM   2582 H  HG3  . GLN   A 1 118 ? 32.907 -12.769 4.949   1.00 17.22 ?  118 GLN   A HG3  1 
ATOM   2583 H  HE21 . GLN   A 1 118 ? 32.360 -15.606 4.139   1.00 17.81 ?  118 GLN   A HE21 1 
ATOM   2584 H  HE22 . GLN   A 1 118 ? 33.428 -16.415 4.790   1.00 17.81 ?  118 GLN   A HE22 1 
ATOM   2585 N  N    . HIS   A 1 119 ? 29.254 -13.031 9.133   1.00 13.18 ?  119 HIS   A N    1 
ATOM   2586 C  CA   . HIS   A 1 119 ? 28.794 -12.409 10.370  1.00 13.75 ?  119 HIS   A CA   1 
ATOM   2587 C  C    . HIS   A 1 119 ? 27.651 -13.225 10.946  1.00 14.26 ?  119 HIS   A C    1 
ATOM   2588 O  O    . HIS   A 1 119 ? 26.709 -13.573 10.228  1.00 14.45 ?  119 HIS   A O    1 
ATOM   2589 C  CB   . HIS   A 1 119 ? 28.338 -10.981 10.079  1.00 14.04 ?  119 HIS   A CB   1 
ATOM   2590 C  CG   . HIS   A 1 119 ? 29.417 -10.182 9.445   1.00 15.36 ?  119 HIS   A CG   1 
ATOM   2591 N  ND1  . HIS   A 1 119 ? 30.400 -9.558  10.180  1.00 17.89 ?  119 HIS   A ND1  1 
ATOM   2592 C  CD2  . HIS   A 1 119 ? 29.742 -10.009 8.144   1.00 16.14 ?  119 HIS   A CD2  1 
ATOM   2593 C  CE1  . HIS   A 1 119 ? 31.255 -8.985  9.354   1.00 17.77 ?  119 HIS   A CE1  1 
ATOM   2594 N  NE2  . HIS   A 1 119 ? 30.891 -9.259  8.114   1.00 17.64 ?  119 HIS   A NE2  1 
ATOM   2595 H  H    . HIS   A 1 119 ? 28.603 -13.288 8.624   1.00 15.84 ?  119 HIS   A H    1 
ATOM   2596 H  HA   . HIS   A 1 119 ? 29.519 -12.384 11.011  1.00 16.52 ?  119 HIS   A HA   1 
ATOM   2597 H  HB2  . HIS   A 1 119 ? 27.577 -11.009 9.475   1.00 16.87 ?  119 HIS   A HB2  1 
ATOM   2598 H  HB3  . HIS   A 1 119 ? 28.087 -10.555 10.913  1.00 16.87 ?  119 HIS   A HB3  1 
ATOM   2599 H  HD2  . HIS   A 1 119 ? 29.280 -10.343 7.407   1.00 19.39 ?  119 HIS   A HD2  1 
ATOM   2600 H  HE1  . HIS   A 1 119 ? 31.991 -8.477  9.604   1.00 21.34 ?  119 HIS   A HE1  1 
ATOM   2601 H  HE2  . HIS   A 1 119 ? 31.289 -8.981  7.404   1.00 21.19 ?  119 HIS   A HE2  1 
ATOM   2602 N  N    A GLU   A 1 120 ? 27.741 -13.545 12.236  0.62 14.80 ?  120 GLU   A N    1 
ATOM   2603 N  N    B GLU   A 1 120 ? 27.718 -13.482 12.254  0.38 16.28 ?  120 GLU   A N    1 
ATOM   2604 C  CA   A GLU   A 1 120 ? 26.776 -14.472 12.823  0.62 16.62 ?  120 GLU   A CA   1 
ATOM   2605 C  CA   B GLU   A 1 120 ? 26.751 -14.377 12.886  0.38 18.84 ?  120 GLU   A CA   1 
ATOM   2606 C  C    A GLU   A 1 120 ? 25.361 -13.904 12.863  0.62 15.05 ?  120 GLU   A C    1 
ATOM   2607 C  C    B GLU   A 1 120 ? 25.344 -13.786 12.909  0.38 17.73 ?  120 GLU   A C    1 
ATOM   2608 O  O    A GLU   A 1 120 ? 24.390 -14.667 12.759  0.62 15.05 ?  120 GLU   A O    1 
ATOM   2609 O  O    B GLU   A 1 120 ? 24.362 -14.516 12.729  0.38 18.05 ?  120 GLU   A O    1 
ATOM   2610 C  CB   A GLU   A 1 120 ? 27.227 -14.881 14.226  0.62 20.53 ?  120 GLU   A CB   1 
ATOM   2611 C  CB   B GLU   A 1 120 ? 27.215 -14.743 14.297  0.38 22.70 ?  120 GLU   A CB   1 
ATOM   2612 C  CG   A GLU   A 1 120 ? 28.421 -15.819 14.233  0.62 26.52 ?  120 GLU   A CG   1 
ATOM   2613 C  CG   B GLU   A 1 120 ? 28.412 -15.678 14.328  0.38 27.19 ?  120 GLU   A CG   1 
ATOM   2614 C  CD   A GLU   A 1 120 ? 28.581 -16.552 15.549  0.62 31.80 ?  120 GLU   A CD   1 
ATOM   2615 C  CD   B GLU   A 1 120 ? 28.515 -16.447 15.631  0.38 31.24 ?  120 GLU   A CD   1 
ATOM   2616 O  OE1  A GLU   A 1 120 ? 28.183 -15.994 16.594  0.62 33.33 ?  120 GLU   A OE1  1 
ATOM   2617 O  OE1  B GLU   A 1 120 ? 28.084 -15.910 16.674  0.38 32.22 ?  120 GLU   A OE1  1 
ATOM   2618 O  OE2  A GLU   A 1 120 ? 29.099 -17.690 15.538  0.62 33.77 -1 120 GLU   A OE2  1 
ATOM   2619 O  OE2  B GLU   A 1 120 ? 29.018 -17.590 15.610  0.38 32.70 -1 120 GLU   A OE2  1 
ATOM   2620 H  H    A GLU   A 1 120 ? 28.349 -13.257 12.777  0.62 17.78 ?  120 GLU   A H    1 
ATOM   2621 H  H    B GLU   A 1 120 ? 28.314 -13.159 12.788  0.38 19.56 ?  120 GLU   A H    1 
ATOM   2622 H  HA   A GLU   A 1 120 ? 26.762 -15.279 12.286  0.62 19.97 ?  120 GLU   A HA   1 
ATOM   2623 H  HA   B GLU   A 1 120 ? 26.715 -15.197 12.375  0.38 22.63 ?  120 GLU   A HA   1 
ATOM   2624 H  HB2  A GLU   A 1 120 ? 27.476 -14.090 14.728  0.62 24.66 ?  120 GLU   A HB2  1 
ATOM   2625 H  HB2  B GLU   A 1 120 ? 27.465 -13.935 14.771  0.38 27.27 ?  120 GLU   A HB2  1 
ATOM   2626 H  HB3  A GLU   A 1 120 ? 26.496 -15.337 14.675  0.62 24.66 ?  120 GLU   A HB3  1 
ATOM   2627 H  HB3  B GLU   A 1 120 ? 26.487 -15.185 14.762  0.38 27.27 ?  120 GLU   A HB3  1 
ATOM   2628 H  HG2  A GLU   A 1 120 ? 28.314 -16.477 13.528  0.62 31.84 ?  120 GLU   A HG2  1 
ATOM   2629 H  HG2  B GLU   A 1 120 ? 28.340 -16.314 13.598  0.38 32.64 ?  120 GLU   A HG2  1 
ATOM   2630 H  HG3  A GLU   A 1 120 ? 29.231 -15.307 14.090  0.62 31.84 ?  120 GLU   A HG3  1 
ATOM   2631 H  HG3  B GLU   A 1 120 ? 29.226 -15.159 14.236  0.38 32.64 ?  120 GLU   A HG3  1 
ATOM   2632 N  N    A VAL   A 1 121 ? 25.223 -12.592 13.054  0.62 14.35 ?  121 VAL   A N    1 
ATOM   2633 N  N    B VAL   A 1 121 ? 25.217 -12.480 13.141  0.38 16.64 ?  121 VAL   A N    1 
ATOM   2634 C  CA   A VAL   A 1 121 ? 23.929 -11.920 13.144  0.62 14.69 ?  121 VAL   A CA   1 
ATOM   2635 C  CA   B VAL   A 1 121 ? 23.911 -11.831 13.255  0.38 16.19 ?  121 VAL   A CA   1 
ATOM   2636 C  C    A VAL   A 1 121 ? 24.057 -10.550 12.486  0.62 13.68 ?  121 VAL   A C    1 
ATOM   2637 C  C    B VAL   A 1 121 ? 23.990 -10.455 12.610  0.38 14.47 ?  121 VAL   A C    1 
ATOM   2638 O  O    A VAL   A 1 121 ? 25.057 -9.852  12.685  0.62 14.30 ?  121 VAL   A O    1 
ATOM   2639 O  O    B VAL   A 1 121 ? 24.894 -9.674  12.923  0.38 14.08 ?  121 VAL   A O    1 
ATOM   2640 C  CB   A VAL   A 1 121 ? 23.477 -11.747 14.613  0.62 17.98 ?  121 VAL   A CB   1 
ATOM   2641 C  CB   B VAL   A 1 121 ? 23.444 -11.696 14.720  0.38 18.45 ?  121 VAL   A CB   1 
ATOM   2642 C  CG1  A VAL   A 1 121 ? 22.083 -11.139 14.679  0.62 18.41 ?  121 VAL   A CG1  1 
ATOM   2643 C  CG1  B VAL   A 1 121 ? 22.083 -11.019 14.775  0.38 18.87 ?  121 VAL   A CG1  1 
ATOM   2644 C  CG2  A VAL   A 1 121 ? 23.507 -13.059 15.375  0.62 20.23 ?  121 VAL   A CG2  1 
ATOM   2645 C  CG2  B VAL   A 1 121 ? 23.382 -13.047 15.407  0.38 19.85 ?  121 VAL   A CG2  1 
ATOM   2646 H  H    A VAL   A 1 121 ? 25.888 -12.062 13.148  0.62 17.24 ?  121 VAL   A H    1 
ATOM   2647 H  H    B VAL   A 1 121 ? 25.882 -11.938 13.227  0.38 19.98 ?  121 VAL   A H    1 
ATOM   2648 H  HA   A VAL   A 1 121 ? 23.260 -12.448 12.674  0.62 17.65 ?  121 VAL   A HA   1 
ATOM   2649 H  HA   B VAL   A 1 121 ? 23.254 -12.352 12.776  0.38 19.45 ?  121 VAL   A HA   1 
ATOM   2650 H  HB   A VAL   A 1 121 ? 24.087 -11.138 15.055  0.62 21.60 ?  121 VAL   A HB   1 
ATOM   2651 H  HB   B VAL   A 1 121 ? 24.074 -11.142 15.206  0.38 22.16 ?  121 VAL   A HB   1 
ATOM   2652 H  HG11 A VAL   A 1 121 ? 21.776 -11.149 15.601  0.62 22.11 ?  121 VAL   A HG11 1 
ATOM   2653 H  HG11 B VAL   A 1 121 ? 21.705 -11.142 15.659  0.38 22.66 ?  121 VAL   A HG11 1 
ATOM   2654 H  HG12 A VAL   A 1 121 ? 22.118 -10.226 14.354  0.62 22.11 ?  121 VAL   A HG12 1 
ATOM   2655 H  HG12 B VAL   A 1 121 ? 22.188 -10.074 14.589  0.38 22.66 ?  121 VAL   A HG12 1 
ATOM   2656 H  HG13 A VAL   A 1 121 ? 21.481 -11.664 14.128  0.62 22.11 ?  121 VAL   A HG13 1 
ATOM   2657 H  HG13 B VAL   A 1 121 ? 21.502 -11.426 14.111  0.38 22.66 ?  121 VAL   A HG13 1 
ATOM   2658 H  HG21 A VAL   A 1 121 ? 23.148 -12.911 16.269  0.62 24.30 ?  121 VAL   A HG21 1 
ATOM   2659 H  HG21 B VAL   A 1 121 ? 23.032 -12.928 16.307  0.38 23.84 ?  121 VAL   A HG21 1 
ATOM   2660 H  HG22 A VAL   A 1 121 ? 22.961 -13.710 14.908  0.62 24.30 ?  121 VAL   A HG22 1 
ATOM   2661 H  HG22 B VAL   A 1 121 ? 22.795 -13.632 14.903  0.38 23.84 ?  121 VAL   A HG22 1 
ATOM   2662 H  HG23 A VAL   A 1 121 ? 24.420 -13.371 15.437  0.62 24.30 ?  121 VAL   A HG23 1 
ATOM   2663 H  HG23 B VAL   A 1 121 ? 24.273 -13.424 15.448  0.38 23.84 ?  121 VAL   A HG23 1 
ATOM   2664 N  N    . LEU   A 1 122 ? 23.032 -10.145 11.735  1.00 13.51 ?  122 LEU   A N    1 
ATOM   2665 C  CA   . LEU   A 1 122 ? 23.026 -8.856  11.046  1.00 13.33 ?  122 LEU   A CA   1 
ATOM   2666 C  C    . LEU   A 1 122 ? 21.630 -8.261  11.018  1.00 13.28 ?  122 LEU   A C    1 
ATOM   2667 O  O    . LEU   A 1 122 ? 20.645 -8.986  10.871  1.00 13.93 ?  122 LEU   A O    1 
ATOM   2668 C  CB   . LEU   A 1 122 ? 23.449 -8.978  9.578   1.00 14.51 ?  122 LEU   A CB   1 
ATOM   2669 C  CG   . LEU   A 1 122 ? 24.677 -9.807  9.237   1.00 14.55 ?  122 LEU   A CG   1 
ATOM   2670 C  CD1  . LEU   A 1 122 ? 24.286 -11.266 9.017   1.00 14.90 ?  122 LEU   A CD1  1 
ATOM   2671 C  CD2  . LEU   A 1 122 ? 25.388 -9.241  8.013   1.00 13.86 ?  122 LEU   A CD2  1 
ATOM   2672 H  H    A LEU   A 1 122 ? 22.311 -10.602 11.615  0.62 16.23 ?  122 LEU   A H    1 
ATOM   2673 H  H    B LEU   A 1 122 ? 22.378 -10.665 11.522  0.38 16.23 ?  122 LEU   A H    1 
ATOM   2674 H  HA   . LEU   A 1 122 ? 23.627 -8.237  11.492  1.00 16.02 ?  122 LEU   A HA   1 
ATOM   2675 H  HB2  . LEU   A 1 122 ? 22.718 -9.372  9.086   1.00 17.43 ?  122 LEU   A HB2  1 
ATOM   2676 H  HB3  . LEU   A 1 122 ? 23.624 -8.091  9.239   1.00 17.43 ?  122 LEU   A HB3  1 
ATOM   2677 H  HG   . LEU   A 1 122 ? 25.313 -9.781  9.970   1.00 17.48 ?  122 LEU   A HG   1 
ATOM   2678 H  HD11 . LEU   A 1 122 ? 25.074 -11.783 8.780   1.00 17.90 ?  122 LEU   A HD11 1 
ATOM   2679 H  HD12 . LEU   A 1 122 ? 23.899 -11.614 9.834   1.00 17.90 ?  122 LEU   A HD12 1 
ATOM   2680 H  HD13 . LEU   A 1 122 ? 23.636 -11.315 8.297   1.00 17.90 ?  122 LEU   A HD13 1 
ATOM   2681 H  HD21 . LEU   A 1 122 ? 26.153 -9.803  7.787   1.00 16.65 ?  122 LEU   A HD21 1 
ATOM   2682 H  HD22 . LEU   A 1 122 ? 24.770 -9.223  7.263   1.00 16.65 ?  122 LEU   A HD22 1 
ATOM   2683 H  HD23 . LEU   A 1 122 ? 25.694 -8.341  8.208   1.00 16.65 ?  122 LEU   A HD23 1 
ATOM   2684 N  N    . LEU   A 1 123 ? 21.567 -6.935  11.123  1.00 12.75 ?  123 LEU   A N    1 
ATOM   2685 C  CA   . LEU   A 1 123 ? 20.395 -6.140  10.758  1.00 12.34 ?  123 LEU   A CA   1 
ATOM   2686 C  C    . LEU   A 1 123 ? 20.632 -5.609  9.349   1.00 12.29 ?  123 LEU   A C    1 
ATOM   2687 O  O    . LEU   A 1 123 ? 21.685 -5.017  9.095   1.00 13.02 ?  123 LEU   A O    1 
ATOM   2688 C  CB   . LEU   A 1 123 ? 20.257 -4.965  11.727  1.00 13.21 ?  123 LEU   A CB   1 
ATOM   2689 C  CG   . LEU   A 1 123 ? 19.216 -3.909  11.360  1.00 14.00 ?  123 LEU   A CG   1 
ATOM   2690 C  CD1  . LEU   A 1 123 ? 17.800 -4.499  11.328  1.00 15.08 ?  123 LEU   A CD1  1 
ATOM   2691 C  CD2  . LEU   A 1 123 ? 19.310 -2.732  12.329  1.00 15.10 ?  123 LEU   A CD2  1 
ATOM   2692 H  H    . LEU   A 1 123 ? 22.223 -6.456  11.413  1.00 15.32 ?  123 LEU   A H    1 
ATOM   2693 H  HA   . LEU   A 1 123 ? 19.593 -6.687  10.783  1.00 14.83 ?  123 LEU   A HA   1 
ATOM   2694 H  HB2  . LEU   A 1 123 ? 20.011 -5.314  12.603  1.00 15.87 ?  123 LEU   A HB2  1 
ATOM   2695 H  HB3  . LEU   A 1 123 ? 21.112 -4.516  11.792  1.00 15.87 ?  123 LEU   A HB3  1 
ATOM   2696 H  HG   . LEU   A 1 123 ? 19.410 -3.565  10.474  1.00 16.82 ?  123 LEU   A HG   1 
ATOM   2697 H  HD11 . LEU   A 1 123 ? 17.164 -3.797  11.126  1.00 18.11 ?  123 LEU   A HD11 1 
ATOM   2698 H  HD12 . LEU   A 1 123 ? 17.759 -5.188  10.641  1.00 18.11 ?  123 LEU   A HD12 1 
ATOM   2699 H  HD13 . LEU   A 1 123 ? 17.599 -4.890  12.194  1.00 18.11 ?  123 LEU   A HD13 1 
ATOM   2700 H  HD21 . LEU   A 1 123 ? 18.645 -2.070  12.087  1.00 18.14 ?  123 LEU   A HD21 1 
ATOM   2701 H  HD22 . LEU   A 1 123 ? 19.142 -3.056  13.230  1.00 18.14 ?  123 LEU   A HD22 1 
ATOM   2702 H  HD23 . LEU   A 1 123 ? 20.198 -2.351  12.275  1.00 18.14 ?  123 LEU   A HD23 1 
ATOM   2703 N  N    . ALA   A 1 124 ? 19.682 -5.807  8.433   1.00 11.89 ?  124 ALA   A N    1 
ATOM   2704 C  CA   . ALA   A 1 124 ? 19.983 -5.537  7.037   1.00 11.78 ?  124 ALA   A CA   1 
ATOM   2705 C  C    . ALA   A 1 124 ? 18.747 -5.093  6.272   1.00 12.03 ?  124 ALA   A C    1 
ATOM   2706 O  O    . ALA   A 1 124 ? 17.615 -5.441  6.642   1.00 12.41 ?  124 ALA   A O    1 
ATOM   2707 C  CB   . ALA   A 1 124 ? 20.570 -6.770  6.348   1.00 12.45 ?  124 ALA   A CB   1 
ATOM   2708 H  H    . ALA   A 1 124 ? 18.881 -6.088  8.594   1.00 14.28 ?  124 ALA   A H    1 
ATOM   2709 H  HA   . ALA   A 1 124 ? 20.652 -4.833  7.012   1.00 14.16 ?  124 ALA   A HA   1 
ATOM   2710 H  HB1  . ALA   A 1 124 ? 20.772 -6.555  5.426   1.00 14.95 ?  124 ALA   A HB1  1 
ATOM   2711 H  HB2  . ALA   A 1 124 ? 21.394 -7.030  6.808   1.00 14.95 ?  124 ALA   A HB2  1 
ATOM   2712 H  HB3  . ALA   A 1 124 ? 19.932 -7.494  6.394   1.00 14.95 ?  124 ALA   A HB3  1 
ATOM   2713 N  N    A PRO   A 1 125 ? 18.936 -4.315  5.216   0.62 11.61 ?  125 PRO   A N    1 
ATOM   2714 N  N    B PRO   A 1 125 ? 18.941 -4.385  5.147   0.38 12.11 ?  125 PRO   A N    1 
ATOM   2715 C  CA   A PRO   A 1 125 ? 17.894 -4.097  4.218   0.62 12.03 ?  125 PRO   A CA   1 
ATOM   2716 C  CA   B PRO   A 1 125 ? 17.848 -4.111  4.214   0.38 12.60 ?  125 PRO   A CA   1 
ATOM   2717 C  C    A PRO   A 1 125 ? 17.962 -5.192  3.158   0.62 11.32 ?  125 PRO   A C    1 
ATOM   2718 C  C    B PRO   A 1 125 ? 17.857 -5.119  3.075   0.38 12.64 ?  125 PRO   A C    1 
ATOM   2719 O  O    A PRO   A 1 125 ? 18.951 -5.923  3.044   0.62 12.05 ?  125 PRO   A O    1 
ATOM   2720 O  O    B PRO   A 1 125 ? 18.753 -5.968  3.005   0.38 13.47 ?  125 PRO   A O    1 
ATOM   2721 C  CB   A PRO   A 1 125 ? 18.335 -2.767  3.596   0.62 12.42 ?  125 PRO   A CB   1 
ATOM   2722 C  CB   B PRO   A 1 125 ? 18.224 -2.725  3.688   0.38 12.47 ?  125 PRO   A CB   1 
ATOM   2723 C  CG   A PRO   A 1 125 ? 19.839 -2.916  3.543   0.62 12.27 ?  125 PRO   A CG   1 
ATOM   2724 C  CG   B PRO   A 1 125 ? 19.740 -2.841  3.543   0.38 12.26 ?  125 PRO   A CG   1 
ATOM   2725 C  CD   A PRO   A 1 125 ? 20.189 -3.630  4.846   0.62 12.21 ?  125 PRO   A CD   1 
ATOM   2726 C  CD   B PRO   A 1 125 ? 20.201 -3.785  4.667   0.38 12.01 ?  125 PRO   A CD   1 
ATOM   2727 H  HA   A PRO   A 1 125 ? 17.007 -4.035  4.611   0.62 14.46 ?  125 PRO   A HA   1 
ATOM   2728 H  HA   B PRO   A 1 125 ? 16.987 -4.096  4.658   0.38 15.14 ?  125 PRO   A HA   1 
ATOM   2729 H  HB2  A PRO   A 1 125 ? 17.957 -2.673  2.706   0.62 14.93 ?  125 PRO   A HB2  1 
ATOM   2730 H  HB2  B PRO   A 1 125 ? 17.799 -2.563  2.829   0.38 14.98 ?  125 PRO   A HB2  1 
ATOM   2731 H  HB3  A PRO   A 1 125 ? 18.074 -2.031  4.169   0.62 14.93 ?  125 PRO   A HB3  1 
ATOM   2732 H  HB3  B PRO   A 1 125 ? 17.982 -2.043  4.334   0.38 14.98 ?  125 PRO   A HB3  1 
ATOM   2733 H  HG2  A PRO   A 1 125 ? 20.095 -3.453  2.772   0.62 14.75 ?  125 PRO   A HG2  1 
ATOM   2734 H  HG2  B PRO   A 1 125 ? 19.957 -3.215  2.672   0.38 14.74 ?  125 PRO   A HG2  1 
ATOM   2735 H  HG3  A PRO   A 1 125 ? 20.257 -2.039  3.500   0.62 14.75 ?  125 PRO   A HG3  1 
ATOM   2736 H  HG3  B PRO   A 1 125 ? 20.145 -1.965  3.643   0.38 14.74 ?  125 PRO   A HG3  1 
ATOM   2737 H  HD2  A PRO   A 1 125 ? 20.905 -4.267  4.701   0.62 14.67 ?  125 PRO   A HD2  1 
ATOM   2738 H  HD2  B PRO   A 1 125 ? 20.802 -4.462  4.310   0.38 14.43 ?  125 PRO   A HD2  1 
ATOM   2739 H  HD3  A PRO   A 1 125 ? 20.426 -2.981  5.530   0.62 14.67 ?  125 PRO   A HD3  1 
ATOM   2740 H  HD3  B PRO   A 1 125 ? 20.629 -3.275  5.375   0.38 14.43 ?  125 PRO   A HD3  1 
ATOM   2741 N  N    A LEU   A 1 126 ? 16.902 -5.271  2.358   0.62 11.77 ?  126 LEU   A N    1 
ATOM   2742 N  N    B LEU   A 1 126 ? 16.892 -5.022  2.161   0.38 12.82 ?  126 LEU   A N    1 
ATOM   2743 C  CA   A LEU   A 1 126 ? 16.952 -6.103  1.165   0.62 12.33 ?  126 LEU   A CA   1 
ATOM   2744 C  CA   B LEU   A 1 126 ? 16.866 -5.880  0.980   0.38 12.71 ?  126 LEU   A CA   1 
ATOM   2745 C  C    A LEU   A 1 126 ? 17.903 -5.475  0.158   0.62 12.77 ?  126 LEU   A C    1 
ATOM   2746 C  C    B LEU   A 1 126 ? 17.813 -5.315  -0.072  0.38 11.93 ?  126 LEU   A C    1 
ATOM   2747 O  O    A LEU   A 1 126 ? 17.739 -4.316  -0.229  0.62 14.18 ?  126 LEU   A O    1 
ATOM   2748 O  O    B LEU   A 1 126 ? 17.566 -4.241  -0.629  0.38 11.93 ?  126 LEU   A O    1 
ATOM   2749 C  CB   A LEU   A 1 126 ? 15.564 -6.268  0.564   0.62 13.38 ?  126 LEU   A CB   1 
ATOM   2750 C  CB   B LEU   A 1 126 ? 15.452 -5.961  0.422   0.38 13.37 ?  126 LEU   A CB   1 
ATOM   2751 C  CG   A LEU   A 1 126 ? 14.665 -7.248  1.319   0.62 14.16 ?  126 LEU   A CG   1 
ATOM   2752 C  CG   B LEU   A 1 126 ? 14.466 -6.841  1.182   0.38 13.61 ?  126 LEU   A CG   1 
ATOM   2753 C  CD1  A LEU   A 1 126 ? 13.234 -7.131  0.843   0.62 15.51 ?  126 LEU   A CD1  1 
ATOM   2754 C  CD1  B LEU   A 1 126 ? 13.103 -6.689  0.546   0.38 13.82 ?  126 LEU   A CD1  1 
ATOM   2755 C  CD2  A LEU   A 1 126 ? 15.166 -8.685  1.161   0.62 14.32 ?  126 LEU   A CD2  1 
ATOM   2756 C  CD2  B LEU   A 1 126 ? 14.896 -8.301  1.183   0.38 13.83 ?  126 LEU   A CD2  1 
ATOM   2757 H  H    A LEU   A 1 126 ? 16.158 -4.851  2.470   0.62 14.14 ?  126 LEU   A H    1 
ATOM   2758 H  H    B LEU   A 1 126 ? 16.232 -4.469  2.207   0.38 15.41 ?  126 LEU   A H    1 
ATOM   2759 H  HA   A LEU   A 1 126 ? 17.292 -6.975  1.393   0.62 14.81 ?  126 LEU   A HA   1 
ATOM   2760 H  HA   B LEU   A 1 126 ? 17.159 -6.773  1.221   0.38 15.27 ?  126 LEU   A HA   1 
ATOM   2761 H  HB2  A LEU   A 1 126 ? 15.116 -5.406  0.561   0.62 16.08 ?  126 LEU   A HB2  1 
ATOM   2762 H  HB2  B LEU   A 1 126 ? 15.079 -5.066  0.407   0.38 16.07 ?  126 LEU   A HB2  1 
ATOM   2763 H  HB3  A LEU   A 1 126 ? 15.650 -6.591  -0.348  0.62 16.08 ?  126 LEU   A HB3  1 
ATOM   2764 H  HB3  B LEU   A 1 126 ? 15.500 -6.306  -0.481  0.38 16.07 ?  126 LEU   A HB3  1 
ATOM   2765 H  HG   A LEU   A 1 126 ? 14.684 -7.030  2.262   0.62 17.01 ?  126 LEU   A HG   1 
ATOM   2766 H  HG   B LEU   A 1 126 ? 14.403 -6.538  2.102   0.38 16.35 ?  126 LEU   A HG   1 
ATOM   2767 H  HD11 A LEU   A 1 126 ? 12.686 -7.764  1.335   0.62 18.63 ?  126 LEU   A HD11 1 
ATOM   2768 H  HD11 B LEU   A 1 126 ? 12.470 -7.253  1.017   0.38 16.60 ?  126 LEU   A HD11 1 
ATOM   2769 H  HD12 A LEU   A 1 126 ? 12.923 -6.228  1.002   0.62 18.63 ?  126 LEU   A HD12 1 
ATOM   2770 H  HD12 B LEU   A 1 126 ? 12.828 -5.762  0.603   0.38 16.60 ?  126 LEU   A HD12 1 
ATOM   2771 H  HD13 A LEU   A 1 126 ? 13.200 -7.333  -0.106  0.62 18.63 ?  126 LEU   A HD13 1 
ATOM   2772 H  HD13 B LEU   A 1 126 ? 13.159 -6.962  -0.384  0.38 16.60 ?  126 LEU   A HD13 1 
ATOM   2773 H  HD21 A LEU   A 1 126 ? 14.501 -9.293  1.517   0.62 17.20 ?  126 LEU   A HD21 1 
ATOM   2774 H  HD21 B LEU   A 1 126 ? 14.176 -8.842  1.537   0.38 16.62 ?  126 LEU   A HD21 1 
ATOM   2775 H  HD22 A LEU   A 1 126 ? 15.312 -8.867  0.219   0.62 17.20 ?  126 LEU   A HD22 1 
ATOM   2776 H  HD22 B LEU   A 1 126 ? 15.098 -8.568  0.273   0.38 16.62 ?  126 LEU   A HD22 1 
ATOM   2777 H  HD23 A LEU   A 1 126 ? 16.000 -8.785  1.649   0.62 17.20 ?  126 LEU   A HD23 1 
ATOM   2778 H  HD23 B LEU   A 1 126 ? 15.686 -8.394  1.738   0.38 16.62 ?  126 LEU   A HD23 1 
ATOM   2779 N  N    A LEU   A 1 127 ? 18.912 -6.236  -0.249  0.62 12.99 ?  127 LEU   A N    1 
ATOM   2780 N  N    B LEU   A 1 127 ? 18.878 -6.052  -0.374  0.38 11.36 ?  127 LEU   A N    1 
ATOM   2781 C  CA   A LEU   A 1 127 ? 19.900 -5.731  -1.188  0.62 12.57 ?  127 LEU   A CA   1 
ATOM   2782 C  CA   B LEU   A 1 127 ? 19.880 -5.556  -1.307  0.38 11.47 ?  127 LEU   A CA   1 
ATOM   2783 C  C    A LEU   A 1 127 ? 19.269 -5.485  -2.549  0.62 11.80 ?  127 LEU   A C    1 
ATOM   2784 C  C    B LEU   A 1 127 ? 19.343 -5.516  -2.738  0.38 11.58 ?  127 LEU   A C    1 
ATOM   2785 O  O    A LEU   A 1 127 ? 18.401 -6.237  -3.008  0.62 12.40 ?  127 LEU   A O    1 
ATOM   2786 O  O    B LEU   A 1 127 ? 18.555 -6.368  -3.161  0.38 11.31 ?  127 LEU   A O    1 
ATOM   2787 C  CB   A LEU   A 1 127 ? 21.053 -6.725  -1.336  0.62 12.62 ?  127 LEU   A CB   1 
ATOM   2788 C  CB   B LEU   A 1 127 ? 21.149 -6.409  -1.222  0.38 12.18 ?  127 LEU   A CB   1 
ATOM   2789 C  CG   A LEU   A 1 127 ? 21.881 -6.983  -0.075  0.62 12.51 ?  127 LEU   A CG   1 
ATOM   2790 C  CG   B LEU   A 1 127 ? 21.904 -6.394  0.112   0.38 12.85 ?  127 LEU   A CG   1 
ATOM   2791 C  CD1  A LEU   A 1 127 ? 22.976 -7.991  -0.372  0.62 12.29 ?  127 LEU   A CD1  1 
ATOM   2792 C  CD1  B LEU   A 1 127 ? 23.039 -7.398  0.068   0.38 13.46 ?  127 LEU   A CD1  1 
ATOM   2793 C  CD2  A LEU   A 1 127 ? 22.485 -5.700  0.486   0.62 13.36 ?  127 LEU   A CD2  1 
ATOM   2794 C  CD2  B LEU   A 1 127 ? 22.444 -5.005  0.426   0.38 13.40 ?  127 LEU   A CD2  1 
ATOM   2795 H  H    A LEU   A 1 127 ? 19.042 -7.047  0.002   0.62 15.61 ?  127 LEU   A H    1 
ATOM   2796 H  H    B LEU   A 1 127 ? 19.044 -6.837  -0.047  0.38 13.65 ?  127 LEU   A H    1 
ATOM   2797 H  HA   A LEU   A 1 127 ? 20.254 -4.893  -0.858  0.62 15.11 ?  127 LEU   A HA   1 
ATOM   2798 H  HA   B LEU   A 1 127 ? 20.111 -4.654  -1.059  0.38 13.79 ?  127 LEU   A HA   1 
ATOM   2799 H  HB2  A LEU   A 1 127 ? 20.683 -7.573  -1.627  0.62 15.17 ?  127 LEU   A HB2  1 
ATOM   2800 H  HB2  B LEU   A 1 127 ? 20.917 -7.330  -1.399  0.38 14.64 ?  127 LEU   A HB2  1 
ATOM   2801 H  HB3  A LEU   A 1 127 ? 21.653 -6.385  -2.020  0.62 15.17 ?  127 LEU   A HB3  1 
ATOM   2802 H  HB3  B LEU   A 1 127 ? 21.771 -6.094  -1.895  0.38 14.64 ?  127 LEU   A HB3  1 
ATOM   2803 H  HG   A LEU   A 1 127 ? 21.304 -7.367  0.599   0.62 15.03 ?  127 LEU   A HG   1 
ATOM   2804 H  HG   B LEU   A 1 127 ? 21.302 -6.649  0.830   0.38 15.44 ?  127 LEU   A HG   1 
ATOM   2805 H  HD11 A LEU   A 1 127 ? 23.448 -8.198  0.452   0.62 14.77 ?  127 LEU   A HD11 1 
ATOM   2806 H  HD11 B LEU   A 1 127 ? 23.578 -7.302  0.869   0.38 16.17 ?  127 LEU   A HD11 1 
ATOM   2807 H  HD12 A LEU   A 1 127 ? 22.575 -8.804  -0.729  0.62 14.77 ?  127 LEU   A HD12 1 
ATOM   2808 H  HD12 B LEU   A 1 127 ? 22.666 -8.291  0.024   0.38 16.17 ?  127 LEU   A HD12 1 
ATOM   2809 H  HD13 A LEU   A 1 127 ? 23.590 -7.617  -1.020  0.62 14.77 ?  127 LEU   A HD13 1 
ATOM   2810 H  HD13 B LEU   A 1 127 ? 23.581 -7.224  -0.716  0.38 16.17 ?  127 LEU   A HD13 1 
ATOM   2811 H  HD21 A LEU   A 1 127 ? 23.099 -5.934  1.202   0.62 16.05 ?  127 LEU   A HD21 1 
ATOM   2812 H  HD21 B LEU   A 1 127 ? 22.985 -5.046  1.232   0.38 16.10 ?  127 LEU   A HD21 1 
ATOM   2813 H  HD22 A LEU   A 1 127 ? 22.966 -5.243  -0.223  0.62 16.05 ?  127 LEU   A HD22 1 
ATOM   2814 H  HD22 B LEU   A 1 127 ? 22.989 -4.703  -0.320  0.38 16.10 ?  127 LEU   A HD22 1 
ATOM   2815 H  HD23 A LEU   A 1 127 ? 21.775 -5.140  0.823   0.62 16.05 ?  127 LEU   A HD23 1 
ATOM   2816 H  HD23 B LEU   A 1 127 ? 21.701 -4.397  0.558   0.38 16.10 ?  127 LEU   A HD23 1 
ATOM   2817 N  N    A SER   A 1 128 ? 19.723 -4.421  -3.198  0.62 11.75 ?  128 SER   A N    1 
ATOM   2818 N  N    B SER   A 1 128 ? 19.781 -4.501  -3.478  0.38 11.80 ?  128 SER   A N    1 
ATOM   2819 C  CA   A SER   A 1 128 ? 19.317 -4.022  -4.537  0.62 11.64 ?  128 SER   A CA   1 
ATOM   2820 C  CA   B SER   A 1 128 ? 19.439 -4.212  -4.868  0.38 11.51 ?  128 SER   A CA   1 
ATOM   2821 C  C    A SER   A 1 128 ? 17.858 -3.588  -4.625  0.62 11.65 ?  128 SER   A C    1 
ATOM   2822 C  C    B SER   A 1 128 ? 18.005 -3.724  -5.056  0.38 11.61 ?  128 SER   A C    1 
ATOM   2823 O  O    A SER   A 1 128 ? 17.376 -3.316  -5.723  0.62 12.63 ?  128 SER   A O    1 
ATOM   2824 O  O    B SER   A 1 128 ? 17.642 -3.349  -6.178  0.38 12.04 ?  128 SER   A O    1 
ATOM   2825 C  CB   A SER   A 1 128 ? 19.661 -5.069  -5.604  0.62 11.85 ?  128 SER   A CB   1 
ATOM   2826 C  CB   B SER   A 1 128 ? 19.770 -5.356  -5.843  0.38 11.91 ?  128 SER   A CB   1 
ATOM   2827 O  OG   A SER   A 1 128 ? 21.070 -5.268  -5.664  0.62 11.97 ?  128 SER   A OG   1 
ATOM   2828 O  OG   B SER   A 1 128 ? 21.172 -5.580  -5.910  0.38 12.14 ?  128 SER   A OG   1 
ATOM   2829 H  H    A SER   A 1 128 ? 20.319 -3.894  -2.869  0.62 14.12 ?  128 SER   A H    1 
ATOM   2830 H  H    B SER   A 1 128 ? 20.332 -3.928  -3.159  0.38 14.18 ?  128 SER   A H    1 
ATOM   2831 H  HA   A SER   A 1 128 ? 19.838 -3.245  -4.762  0.62 13.99 ?  128 SER   A HA   1 
ATOM   2832 H  HA   B SER   A 1 128 ? 19.999 -3.478  -5.133  0.38 13.83 ?  128 SER   A HA   1 
ATOM   2833 H  HB2  A SER   A 1 128 ? 19.226 -5.907  -5.381  0.62 14.23 ?  128 SER   A HB2  1 
ATOM   2834 H  HB2  B SER   A 1 128 ? 19.332 -6.169  -5.552  0.38 14.31 ?  128 SER   A HB2  1 
ATOM   2835 H  HB3  A SER   A 1 128 ? 19.348 -4.753  -6.469  0.62 14.23 ?  128 SER   A HB3  1 
ATOM   2836 H  HB3  B SER   A 1 128 ? 19.464 -5.109  -6.730  0.38 14.31 ?  128 SER   A HB3  1 
ATOM   2837 H  HG   A SER   A 1 128 ? 21.449 -4.542  -5.847  0.62 14.39 ?  128 SER   A HG   1 
ATOM   2838 H  HG   B SER   A 1 128 ? 21.564 -4.873  -6.133  0.38 14.58 ?  128 SER   A HG   1 
ATOM   2839 N  N    A ALA   A 1 129 ? 17.152 -3.496  -3.498  0.62 11.96 ?  129 ALA   A N    1 
ATOM   2840 N  N    B ALA   A 1 129 ? 17.187 -3.700  -4.004  0.38 11.98 ?  129 ALA   A N    1 
ATOM   2841 C  CA   A ALA   A 1 129 ? 15.786 -2.997  -3.487  0.62 12.10 ?  129 ALA   A CA   1 
ATOM   2842 C  CA   B ALA   A 1 129 ? 15.817 -3.215  -4.087  0.38 12.34 ?  129 ALA   A CA   1 
ATOM   2843 C  C    A ALA   A 1 129 ? 15.795 -1.468  -3.495  0.62 12.05 ?  129 ALA   A C    1 
ATOM   2844 C  C    B ALA   A 1 129 ? 15.793 -1.693  -3.911  0.38 13.18 ?  129 ALA   A C    1 
ATOM   2845 O  O    A ALA   A 1 129 ? 16.846 -0.822  -3.556  0.62 12.02 ?  129 ALA   A O    1 
ATOM   2846 O  O    B ALA   A 1 129 ? 16.826 -1.019  -3.964  0.38 13.40 ?  129 ALA   A O    1 
ATOM   2847 C  CB   A ALA   A 1 129 ? 15.018 -3.567  -2.294  0.62 12.99 ?  129 ALA   A CB   1 
ATOM   2848 C  CB   B ALA   A 1 129 ? 14.943 -3.952  -3.070  0.38 12.28 ?  129 ALA   A CB   1 
ATOM   2849 H  H    A ALA   A 1 129 ? 17.450 -3.713  -2.720  0.62 14.38 ?  129 ALA   A H    1 
ATOM   2850 H  H    B ALA   A 1 129 ? 17.406 -3.980  -3.216  0.38 14.39 ?  129 ALA   A H    1 
ATOM   2851 H  HA   A ALA   A 1 129 ? 15.339 -3.281  -4.290  0.62 14.55 ?  129 ALA   A HA   1 
ATOM   2852 H  HA   B ALA   A 1 129 ? 15.470 -3.413  -4.968  0.38 14.82 ?  129 ALA   A HA   1 
ATOM   2853 H  HB1  A ALA   A 1 129 ? 14.109 -3.225  -2.305  0.62 15.60 ?  129 ALA   A HB1  1 
ATOM   2854 H  HB1  B ALA   A 1 129 ? 14.029 -3.638  -3.151  0.38 14.75 ?  129 ALA   A HB1  1 
ATOM   2855 H  HB2  A ALA   A 1 129 ? 15.005 -4.535  -2.361  0.62 15.60 ?  129 ALA   A HB2  1 
ATOM   2856 H  HB2  B ALA   A 1 129 ? 14.978 -4.906  -3.254  0.38 14.75 ?  129 ALA   A HB2  1 
ATOM   2857 H  HB3  A ALA   A 1 129 ? 15.458 -3.301  -1.469  0.62 15.60 ?  129 ALA   A HB3  1 
ATOM   2858 H  HB3  B ALA   A 1 129 ? 15.276 -3.777  -2.177  0.38 14.75 ?  129 ALA   A HB3  1 
ATOM   2859 N  N    A GLY   A 1 130 ? 14.606 -0.874  -3.444  0.62 13.82 ?  130 GLY   A N    1 
ATOM   2860 N  N    B GLY   A 1 130 ? 14.599 -1.137  -3.715  0.38 13.71 ?  130 GLY   A N    1 
ATOM   2861 C  CA   A GLY   A 1 130 ? 14.531 0.579   -3.468  0.62 14.74 ?  130 GLY   A CA   1 
ATOM   2862 C  CA   B GLY   A 1 130 ? 14.472 0.298   -3.519  0.38 14.00 ?  130 GLY   A CA   1 
ATOM   2863 C  C    A GLY   A 1 130 ? 15.174 1.151   -4.719  0.62 14.74 ?  130 GLY   A C    1 
ATOM   2864 C  C    B GLY   A 1 130 ? 15.043 1.062   -4.695  0.38 14.14 ?  130 GLY   A C    1 
ATOM   2865 O  O    A GLY   A 1 130 ? 14.929 0.686   -5.837  0.62 15.16 ?  130 GLY   A O    1 
ATOM   2866 O  O    B GLY   A 1 130 ? 14.833 0.704   -5.859  0.38 14.08 ?  130 GLY   A O    1 
ATOM   2867 H  H    A GLY   A 1 130 ? 13.843 -1.278  -3.390  0.62 16.60 ?  130 GLY   A H    1 
ATOM   2868 H  H    B GLY   A 1 130 ? 13.856 -1.565  -3.696  0.38 16.47 ?  130 GLY   A H    1 
ATOM   2869 H  HA2  A GLY   A 1 130 ? 13.598 0.857   -3.441  0.62 17.71 ?  130 GLY   A HA2  1 
ATOM   2870 H  HA2  B GLY   A 1 130 ? 13.530 0.529   -3.406  0.38 16.82 ?  130 GLY   A HA2  1 
ATOM   2871 H  HA3  A GLY   A 1 130 ? 14.981 0.944   -2.692  0.62 17.71 ?  130 GLY   A HA3  1 
ATOM   2872 H  HA3  B GLY   A 1 130 ? 14.951 0.566   -2.723  0.38 16.82 ?  130 GLY   A HA3  1 
ATOM   2873 N  N    A ILE   A 1 131 ? 16.018 2.175   -4.531  0.62 14.36 ?  131 ILE   A N    1 
ATOM   2874 N  N    B ILE   A 1 131 ? 15.790 2.129   -4.392  0.38 14.76 ?  131 ILE   A N    1 
ATOM   2875 C  CA   A ILE   A 1 131 ? 16.583 2.922   -5.655  0.62 13.99 ?  131 ILE   A CA   1 
ATOM   2876 C  CA   B ILE   A 1 131 ? 16.383 2.962   -5.432  0.38 14.75 ?  131 ILE   A CA   1 
ATOM   2877 C  C    A ILE   A 1 131 ? 17.606 2.138   -6.461  0.62 13.54 ?  131 ILE   A C    1 
ATOM   2878 C  C    B ILE   A 1 131 ? 17.393 2.211   -6.294  0.38 14.06 ?  131 ILE   A C    1 
ATOM   2879 O  O    A ILE   A 1 131 ? 18.020 2.615   -7.525  0.62 14.35 ?  131 ILE   A O    1 
ATOM   2880 O  O    B ILE   A 1 131 ? 17.841 2.752   -7.309  0.38 14.24 ?  131 ILE   A O    1 
ATOM   2881 C  CB   A ILE   A 1 131 ? 17.147 4.295   -5.230  0.62 15.19 ?  131 ILE   A CB   1 
ATOM   2882 C  CB   B ILE   A 1 131 ? 17.017 4.243   -4.839  0.38 15.68 ?  131 ILE   A CB   1 
ATOM   2883 C  CG1  A ILE   A 1 131 ? 18.391 4.144   -4.347  0.62 15.81 ?  131 ILE   A CG1  1 
ATOM   2884 C  CG1  B ILE   A 1 131 ? 18.221 3.898   -3.954  0.38 16.32 ?  131 ILE   A CG1  1 
ATOM   2885 C  CG2  A ILE   A 1 131 ? 16.071 5.108   -4.524  0.62 15.54 ?  131 ILE   A CG2  1 
ATOM   2886 C  CG2  B ILE   A 1 131 ? 15.978 5.047   -4.061  0.38 16.37 ?  131 ILE   A CG2  1 
ATOM   2887 C  CD1  A ILE   A 1 131 ? 19.017 5.487   -3.938  0.62 16.57 ?  131 ILE   A CD1  1 
ATOM   2888 C  CD1  B ILE   A 1 131 ? 18.910 5.115   -3.347  0.38 17.14 ?  131 ILE   A CD1  1 
ATOM   2889 H  H    A ILE   A 1 131 ? 16.268 2.456   -3.761  0.62 17.25 ?  131 ILE   A H    1 
ATOM   2890 H  H    B ILE   A 1 131 ? 15.951 2.396   -3.588  0.38 17.74 ?  131 ILE   A H    1 
ATOM   2891 H  HA   A ILE   A 1 131 ? 15.860 3.103   -6.268  0.62 16.80 ?  131 ILE   A HA   1 
ATOM   2892 H  HA   B ILE   A 1 131 ? 15.669 3.255   -6.020  0.38 17.72 ?  131 ILE   A HA   1 
ATOM   2893 H  HB   A ILE   A 1 131 ? 17.403 4.772   -6.034  0.62 18.25 ?  131 ILE   A HB   1 
ATOM   2894 H  HB   B ILE   A 1 131 ? 17.328 4.792   -5.576  0.38 18.83 ?  131 ILE   A HB   1 
ATOM   2895 H  HG12 A ILE   A 1 131 ? 18.148 3.669   -3.539  0.62 19.00 ?  131 ILE   A HG12 1 
ATOM   2896 H  HG12 B ILE   A 1 131 ? 17.920 3.335   -3.226  0.38 19.61 ?  131 ILE   A HG12 1 
ATOM   2897 H  HG13 A ILE   A 1 131 ? 19.067 3.643   -4.833  0.62 19.00 ?  131 ILE   A HG13 1 
ATOM   2898 H  HG13 B ILE   A 1 131 ? 18.878 3.428   -4.487  0.38 19.61 ?  131 ILE   A HG13 1 
ATOM   2899 H  HG21 A ILE   A 1 131 ? 16.376 6.021   -4.426  0.62 18.67 ?  131 ILE   A HG21 1 
ATOM   2900 H  HG21 B ILE   A 1 131 ? 16.343 5.922   -3.854  0.38 19.67 ?  131 ILE   A HG21 1 
ATOM   2901 H  HG22 A ILE   A 1 131 ? 15.259 5.084   -5.056  0.62 18.67 ?  131 ILE   A HG22 1 
ATOM   2902 H  HG22 B ILE   A 1 131 ? 15.181 5.144   -4.606  0.38 19.67 ?  131 ILE   A HG22 1 
ATOM   2903 H  HG23 A ILE   A 1 131 ? 15.902 4.716   -3.652  0.62 18.67 ?  131 ILE   A HG23 1 
ATOM   2904 H  HG23 B ILE   A 1 131 ? 15.762 4.575   -3.242  0.38 19.67 ?  131 ILE   A HG23 1 
ATOM   2905 H  HD11 A ILE   A 1 131 ? 19.864 5.320   -3.494  0.62 19.90 ?  131 ILE   A HD11 1 
ATOM   2906 H  HD11 B ILE   A 1 131 ? 19.730 4.829   -2.915  0.38 20.59 ?  131 ILE   A HD11 1 
ATOM   2907 H  HD12 A ILE   A 1 131 ? 19.162 6.025   -4.733  0.62 19.90 ?  131 ILE   A HD12 1 
ATOM   2908 H  HD12 B ILE   A 1 131 ? 19.112 5.749   -4.053  0.38 20.59 ?  131 ILE   A HD12 1 
ATOM   2909 H  HD13 A ILE   A 1 131 ? 18.414 5.949   -3.334  0.62 19.90 ?  131 ILE   A HD13 1 
ATOM   2910 H  HD13 B ILE   A 1 131 ? 18.318 5.524   -2.696  0.38 20.59 ?  131 ILE   A HD13 1 
ATOM   2911 N  N    A PHE   A 1 132 ? 18.027 0.953   -5.997  0.62 12.73 ?  132 PHE   A N    1 
ATOM   2912 N  N    B PHE   A 1 132 ? 17.763 0.979   -5.924  0.38 13.68 ?  132 PHE   A N    1 
ATOM   2913 C  CA   A PHE   A 1 132 ? 18.857 0.084   -6.828  0.62 13.35 ?  132 PHE   A CA   1 
ATOM   2914 C  CA   B PHE   A 1 132 ? 18.731 0.219   -6.709  0.38 13.87 ?  132 PHE   A CA   1 
ATOM   2915 C  C    A PHE   A 1 132 ? 18.044 -0.678  -7.877  0.62 14.08 ?  132 PHE   A C    1 
ATOM   2916 C  C    B PHE   A 1 132 ? 18.117 -0.492  -7.914  0.38 14.78 ?  132 PHE   A C    1 
ATOM   2917 O  O    A PHE   A 1 132 ? 18.634 -1.337  -8.740  0.62 14.42 ?  132 PHE   A O    1 
ATOM   2918 O  O    B PHE   A 1 132 ? 18.866 -0.954  -8.782  0.38 15.23 ?  132 PHE   A O    1 
ATOM   2919 C  CB   A PHE   A 1 132 ? 19.679 -0.892  -5.971  0.62 13.04 ?  132 PHE   A CB   1 
ATOM   2920 C  CB   B PHE   A 1 132 ? 19.489 -0.784  -5.830  0.38 13.23 ?  132 PHE   A CB   1 
ATOM   2921 C  CG   A PHE   A 1 132 ? 20.889 -0.274  -5.292  0.62 12.95 ?  132 PHE   A CG   1 
ATOM   2922 C  CG   B PHE   A 1 132 ? 20.687 -0.201  -5.112  0.38 12.87 ?  132 PHE   A CG   1 
ATOM   2923 C  CD1  A PHE   A 1 132 ? 20.757 0.773   -4.395  0.62 13.41 ?  132 PHE   A CD1  1 
ATOM   2924 C  CD1  B PHE   A 1 132 ? 20.524 0.697   -4.071  0.38 13.16 ?  132 PHE   A CD1  1 
ATOM   2925 C  CD2  A PHE   A 1 132 ? 22.159 -0.794  -5.520  0.62 13.72 ?  132 PHE   A CD2  1 
ATOM   2926 C  CD2  B PHE   A 1 132 ? 21.974 -0.589  -5.460  0.38 13.71 ?  132 PHE   A CD2  1 
ATOM   2927 C  CE1  A PHE   A 1 132 ? 21.878 1.317   -3.768  0.62 13.60 ?  132 PHE   A CE1  1 
ATOM   2928 C  CE1  B PHE   A 1 132 ? 21.622 1.217   -3.407  0.38 13.72 ?  132 PHE   A CE1  1 
ATOM   2929 C  CE2  A PHE   A 1 132 ? 23.272 -0.262  -4.894  0.62 13.97 ?  132 PHE   A CE2  1 
ATOM   2930 C  CE2  B PHE   A 1 132 ? 23.077 -0.074  -4.797  0.38 14.17 ?  132 PHE   A CE2  1 
ATOM   2931 C  CZ   A PHE   A 1 132 ? 23.130 0.795   -4.018  0.62 13.60 ?  132 PHE   A CZ   1 
ATOM   2932 C  CZ   B PHE   A 1 132 ? 22.897 0.832   -3.768  0.38 13.75 ?  132 PHE   A CZ   1 
ATOM   2933 H  H    A PHE   A 1 132 ? 17.863 0.639   -5.205  0.62 15.30 ?  132 PHE   A H    1 
ATOM   2934 H  H    B PHE   A 1 132 ? 17.473 0.571   -5.221  0.38 16.43 ?  132 PHE   A H    1 
ATOM   2935 H  HA   A PHE   A 1 132 ? 19.493 0.638   -7.299  0.62 16.04 ?  132 PHE   A HA   1 
ATOM   2936 H  HA   B PHE   A 1 132 ? 19.382 0.843   -7.056  0.38 16.67 ?  132 PHE   A HA   1 
ATOM   2937 H  HB2  A PHE   A 1 132 ? 19.116 -1.251  -5.272  0.62 15.67 ?  132 PHE   A HB2  1 
ATOM   2938 H  HB2  B PHE   A 1 132 ? 18.889 -1.131  -5.156  0.38 15.89 ?  132 PHE   A HB2  1 
ATOM   2939 H  HB3  A PHE   A 1 132 ? 20.005 -1.617  -6.535  0.62 15.67 ?  132 PHE   A HB3  1 
ATOM   2940 H  HB3  B PHE   A 1 132 ? 19.809 -1.507  -6.391  0.38 15.89 ?  132 PHE   A HB3  1 
ATOM   2941 H  HD1  A PHE   A 1 132 ? 19.921 1.128   -4.221  0.62 16.12 ?  132 PHE   A HD1  1 
ATOM   2942 H  HD1  B PHE   A 1 132 ? 19.669 0.962   -3.823  0.38 15.81 ?  132 PHE   A HD1  1 
ATOM   2943 H  HD2  A PHE   A 1 132 ? 22.269 -1.505  -6.110  0.62 16.49 ?  132 PHE   A HD2  1 
ATOM   2944 H  HD2  B PHE   A 1 132 ? 22.102 -1.197  -6.155  0.38 16.47 ?  132 PHE   A HD2  1 
ATOM   2945 H  HE1  A PHE   A 1 132 ? 21.781 2.027   -3.172  0.62 16.34 ?  132 PHE   A HE1  1 
ATOM   2946 H  HE1  B PHE   A 1 132 ? 21.501 1.823   -2.714  0.38 16.48 ?  132 PHE   A HE1  1 
ATOM   2947 H  HE2  A PHE   A 1 132 ? 24.121 -0.612  -5.067  0.62 16.78 ?  132 PHE   A HE2  1 
ATOM   2948 H  HE2  B PHE   A 1 132 ? 23.937 -0.335  -5.045  0.38 17.03 ?  132 PHE   A HE2  1 
ATOM   2949 H  HZ   A PHE   A 1 132 ? 23.881 1.160   -3.596  0.62 16.33 ?  132 PHE   A HZ   1 
ATOM   2950 H  HZ   B PHE   A 1 132 ? 23.633 1.181   -3.319  0.38 16.53 ?  132 PHE   A HZ   1 
ATOM   2951 N  N    A GLY   A 1 133 ? 16.712 -0.609  -7.825  0.62 14.45 ?  133 GLY   A N    1 
ATOM   2952 N  N    B GLY   A 1 133 ? 16.788 -0.604  -8.001  0.38 14.92 ?  133 GLY   A N    1 
ATOM   2953 C  CA   A GLY   A 1 133 ? 15.879 -0.984  -8.954  0.62 14.93 ?  133 GLY   A CA   1 
ATOM   2954 C  CA   B GLY   A 1 133 ? 16.123 -0.957  -9.240  0.38 14.97 ?  133 GLY   A CA   1 
ATOM   2955 C  C    A GLY   A 1 133 ? 15.616 -2.461  -9.181  0.62 15.09 ?  133 GLY   A C    1 
ATOM   2956 C  C    B GLY   A 1 133 ? 15.546 -2.358  -9.318  0.38 15.11 ?  133 GLY   A C    1 
ATOM   2957 O  O    A GLY   A 1 133 ? 15.044 -2.804  -10.223 0.62 15.92 ?  133 GLY   A O    1 
ATOM   2958 O  O    B GLY   A 1 133 ? 14.648 -2.587  -10.141 0.38 14.98 ?  133 GLY   A O    1 
ATOM   2959 H  H    A GLY   A 1 133 ? 16.263 -0.343  -7.138  0.62 17.36 ?  133 GLY   A H    1 
ATOM   2960 H  H    B GLY   A 1 133 ? 16.244 -0.477  -7.343  0.38 17.92 ?  133 GLY   A H    1 
ATOM   2961 H  HA2  A GLY   A 1 133 ? 15.015 -0.549  -8.856  0.62 17.94 ?  133 GLY   A HA2  1 
ATOM   2962 H  HA2  B GLY   A 1 133 ? 15.386 -0.350  -9.383  0.38 17.98 ?  133 GLY   A HA2  1 
ATOM   2963 H  HA3  A GLY   A 1 133 ? 16.286 -0.644  -9.764  0.62 17.94 ?  133 GLY   A HA3  1 
ATOM   2964 H  HA3  B GLY   A 1 133 ? 16.749 -0.845  -9.972  0.38 17.98 ?  133 GLY   A HA3  1 
ATOM   2965 N  N    A ALA   A 1 134 ? 15.999 -3.347  -8.263  0.62 14.39 ?  134 ALA   A N    1 
ATOM   2966 N  N    B ALA   A 1 134 ? 16.015 -3.301  -8.505  0.38 14.88 ?  134 ALA   A N    1 
ATOM   2967 C  CA   A ALA   A 1 134 ? 15.665 -4.757  -8.409  0.62 14.76 ?  134 ALA   A CA   1 
ATOM   2968 C  CA   B ALA   A 1 134 ? 15.600 -4.688  -8.662  0.38 14.99 ?  134 ALA   A CA   1 
ATOM   2969 C  C    A ALA   A 1 134 ? 14.288 -5.050  -7.813  0.62 14.95 ?  134 ALA   A C    1 
ATOM   2970 C  C    B ALA   A 1 134 ? 14.304 -4.972  -7.903  0.38 15.03 ?  134 ALA   A C    1 
ATOM   2971 O  O    A ALA   A 1 134 ? 13.715 -4.255  -7.064  0.62 16.34 ?  134 ALA   A O    1 
ATOM   2972 O  O    B ALA   A 1 134 ? 13.887 -4.219  -7.019  0.38 15.92 ?  134 ALA   A O    1 
ATOM   2973 C  CB   A ALA   A 1 134 ? 16.728 -5.637  -7.748  0.62 14.89 ?  134 ALA   A CB   1 
ATOM   2974 C  CB   B ALA   A 1 134 ? 16.698 -5.642  -8.191  0.38 15.69 ?  134 ALA   A CB   1 
ATOM   2975 H  H    A ALA   A 1 134 ? 16.458 -3.157  -7.560  0.62 17.29 ?  134 ALA   A H    1 
ATOM   2976 H  H    B ALA   A 1 134 ? 16.565 -3.160  -7.856  0.38 17.87 ?  134 ALA   A H    1 
ATOM   2977 H  HA   A ALA   A 1 134 ? 15.642 -4.980  -9.354  0.62 17.74 ?  134 ALA   A HA   1 
ATOM   2978 H  HA   B ALA   A 1 134 ? 15.440 -4.861  -9.602  0.38 18.01 ?  134 ALA   A HA   1 
ATOM   2979 H  HB1  A ALA   A 1 134 ? 16.495 -6.569  -7.884  0.62 17.89 ?  134 ALA   A HB1  1 
ATOM   2980 H  HB1  B ALA   A 1 134 ? 16.393 -6.555  -8.314  0.38 18.85 ?  134 ALA   A HB1  1 
ATOM   2981 H  HB2  A ALA   A 1 134 ? 17.591 -5.450  -8.154  0.62 17.89 ?  134 ALA   A HB2  1 
ATOM   2982 H  HB2  B ALA   A 1 134 ? 17.496 -5.486  -8.720  0.38 18.85 ?  134 ALA   A HB2  1 
ATOM   2983 H  HB3  A ALA   A 1 134 ? 16.760 -5.437  -6.801  0.62 17.89 ?  134 ALA   A HB3  1 
ATOM   2984 H  HB3  B ALA   A 1 134 ? 16.881 -5.476  -7.255  0.38 18.85 ?  134 ALA   A HB3  1 
ATOM   2985 N  N    A ASP   A 1 135 ? 13.762 -6.218  -8.162  0.62 15.64 ?  135 ASP   A N    1 
ATOM   2986 N  N    B ASP   A 1 135 ? 13.678 -6.087  -8.263  0.38 15.50 ?  135 ASP   A N    1 
ATOM   2987 C  CA   A ASP   A 1 135 ? 12.500 -6.699  -7.609  0.62 16.65 ?  135 ASP   A CA   1 
ATOM   2988 C  CA   B ASP   A 1 135 ? 12.415 -6.496  -7.664  0.38 16.20 ?  135 ASP   A CA   1 
ATOM   2989 C  C    A ASP   A 1 135 ? 12.723 -7.126  -6.164  0.62 16.04 ?  135 ASP   A C    1 
ATOM   2990 C  C    B ASP   A 1 135 ? 12.658 -6.992  -6.245  0.38 15.67 ?  135 ASP   A C    1 
ATOM   2991 O  O    A ASP   A 1 135 ? 13.494 -8.063  -5.921  0.62 15.65 ?  135 ASP   A O    1 
ATOM   2992 O  O    B ASP   A 1 135 ? 13.429 -7.943  -6.055  0.38 15.51 ?  135 ASP   A O    1 
ATOM   2993 C  CB   A ASP   A 1 135 ? 12.035 -7.890  -8.449  0.62 18.64 ?  135 ASP   A CB   1 
ATOM   2994 C  CB   B ASP   A 1 135 ? 11.803 -7.613  -8.504  0.38 17.59 ?  135 ASP   A CB   1 
ATOM   2995 C  CG   A ASP   A 1 135 ? 10.802 -8.594  -7.881  0.62 20.77 ?  135 ASP   A CG   1 
ATOM   2996 C  CG   B ASP   A 1 135 ? 10.417 -8.019  -8.024  0.38 19.22 ?  135 ASP   A CG   1 
ATOM   2997 O  OD1  A ASP   A 1 135 ? 10.198 -8.110  -6.900  0.62 20.75 ?  135 ASP   A OD1  1 
ATOM   2998 O  OD1  B ASP   A 1 135 ? 9.975  -7.525  -6.964  0.38 19.96 ?  135 ASP   A OD1  1 
ATOM   2999 O  OD2  A ASP   A 1 135 ? 10.437 -9.652  -8.436  0.62 23.16 -1 135 ASP   A OD2  1 
ATOM   3000 O  OD2  B ASP   A 1 135 ? 9.770  -8.835  -8.714  0.38 20.34 -1 135 ASP   A OD2  1 
ATOM   3001 H  H    A ASP   A 1 135 ? 14.119 -6.759  -8.727  0.62 18.79 ?  135 ASP   A H    1 
ATOM   3002 H  H    B ASP   A 1 135 ? 13.965 -6.633  -8.857  0.38 18.62 ?  135 ASP   A H    1 
ATOM   3003 H  HA   A ASP   A 1 135 ? 11.830 -5.999  -7.654  0.62 20.00 ?  135 ASP   A HA   1 
ATOM   3004 H  HA   B ASP   A 1 135 ? 11.797 -5.748  -7.656  0.38 19.46 ?  135 ASP   A HA   1 
ATOM   3005 H  HB2  A ASP   A 1 135 ? 11.819 -7.577  -9.341  0.62 22.39 ?  135 ASP   A HB2  1 
ATOM   3006 H  HB2  B ASP   A 1 135 ? 11.737 -7.314  -9.426  0.38 21.13 ?  135 ASP   A HB2  1 
ATOM   3007 H  HB3  A ASP   A 1 135 ? 12.751 -8.541  -8.491  0.62 22.39 ?  135 ASP   A HB3  1 
ATOM   3008 H  HB3  B ASP   A 1 135 ? 12.373 -8.397  -8.453  0.38 21.13 ?  135 ASP   A HB3  1 
ATOM   3009 N  N    A PRO   A 1 136 ? 12.093 -6.477  -5.181  0.62 16.26 ?  136 PRO   A N    1 
ATOM   3010 N  N    B PRO   A 1 136 ? 12.036 -6.393  -5.229  0.38 15.89 ?  136 PRO   A N    1 
ATOM   3011 C  CA   A PRO   A 1 136 ? 12.333 -6.867  -3.780  0.62 16.36 ?  136 PRO   A CA   1 
ATOM   3012 C  CA   B PRO   A 1 136 ? 12.257 -6.867  -3.852  0.38 16.00 ?  136 PRO   A CA   1 
ATOM   3013 C  C    A PRO   A 1 136 ? 11.889 -8.281  -3.444  0.62 14.88 ?  136 PRO   A C    1 
ATOM   3014 C  C    B PRO   A 1 136 ? 11.869 -8.318  -3.623  0.38 15.39 ?  136 PRO   A C    1 
ATOM   3015 O  O    A PRO   A 1 136 ? 12.461 -8.891  -2.533  0.62 14.21 ?  136 PRO   A O    1 
ATOM   3016 O  O    B PRO   A 1 136 ? 12.522 -8.996  -2.821  0.38 15.27 ?  136 PRO   A O    1 
ATOM   3017 C  CB   A PRO   A 1 136 ? 11.556 -5.812  -2.980  0.62 17.51 ?  136 PRO   A CB   1 
ATOM   3018 C  CB   B PRO   A 1 136 ? 11.412 -5.901  -3.009  0.38 16.73 ?  136 PRO   A CB   1 
ATOM   3019 C  CG   A PRO   A 1 136 ? 10.509 -5.320  -3.929  0.62 18.89 ?  136 PRO   A CG   1 
ATOM   3020 C  CG   B PRO   A 1 136 ? 10.418 -5.325  -3.976  0.38 17.54 ?  136 PRO   A CG   1 
ATOM   3021 C  CD   A PRO   A 1 136 ? 11.134 -5.365  -5.289  0.62 17.89 ?  136 PRO   A CD   1 
ATOM   3022 C  CD   B PRO   A 1 136 ? 11.135 -5.230  -5.272  0.38 16.88 ?  136 PRO   A CD   1 
ATOM   3023 H  HA   A PRO   A 1 136 ? 13.278 -6.785  -3.565  0.62 19.65 ?  136 PRO   A HA   1 
ATOM   3024 H  HA   B PRO   A 1 136 ? 13.191 -6.760  -3.608  0.38 19.22 ?  136 PRO   A HA   1 
ATOM   3025 H  HB2  A PRO   A 1 136 ? 11.150 -6.223  -2.199  0.62 21.03 ?  136 PRO   A HB2  1 
ATOM   3026 H  HB2  B PRO   A 1 136 ? 10.964 -6.388  -2.301  0.38 20.09 ?  136 PRO   A HB2  1 
ATOM   3027 H  HB3  A PRO   A 1 136 ? 12.154 -5.093  -2.718  0.62 21.03 ?  136 PRO   A HB3  1 
ATOM   3028 H  HB3  B PRO   A 1 136 ? 11.982 -5.206  -2.643  0.38 20.09 ?  136 PRO   A HB3  1 
ATOM   3029 H  HG2  A PRO   A 1 136 ? 9.738  -5.904  -3.892  0.62 22.69 ?  136 PRO   A HG2  1 
ATOM   3030 H  HG2  B PRO   A 1 136 ? 9.660  -5.922  -4.058  0.38 21.07 ?  136 PRO   A HG2  1 
ATOM   3031 H  HG3  A PRO   A 1 136 ? 10.266 -4.411  -3.701  0.62 22.69 ?  136 PRO   A HG3  1 
ATOM   3032 H  HG3  B PRO   A 1 136 ? 10.140 -4.448  -3.678  0.38 21.07 ?  136 PRO   A HG3  1 
ATOM   3033 H  HD2  A PRO   A 1 136 ? 10.467 -5.568  -5.964  0.62 21.49 ?  136 PRO   A HD2  1 
ATOM   3034 H  HD2  B PRO   A 1 136 ? 10.510 -5.315  -6.009  0.38 20.27 ?  136 PRO   A HD2  1 
ATOM   3035 H  HD3  A PRO   A 1 136 ? 11.600 -4.537  -5.484  0.62 21.49 ?  136 PRO   A HD3  1 
ATOM   3036 H  HD3  B PRO   A 1 136 ? 11.647 -4.408  -5.328  0.38 20.27 ?  136 PRO   A HD3  1 
ATOM   3037 N  N    A ILE   A 1 137 ? 10.870 -8.810  -4.126  0.62 15.22 ?  137 ILE   A N    1 
ATOM   3038 N  N    B ILE   A 1 137 ? 10.820 -8.815  -4.284  0.38 15.80 ?  137 ILE   A N    1 
ATOM   3039 C  CA   A ILE   A 1 137 ? 10.489 -10.207 -3.925  0.62 15.59 ?  137 ILE   A CA   1 
ATOM   3040 C  CA   B ILE   A 1 137 ? 10.446 -10.219 -4.123  0.38 16.46 ?  137 ILE   A CA   1 
ATOM   3041 C  C    A ILE   A 1 137 ? 11.644 -11.124 -4.317  0.62 14.97 ?  137 ILE   A C    1 
ATOM   3042 C  C    B ILE   A 1 137 ? 11.611 -11.122 -4.503  0.38 16.15 ?  137 ILE   A C    1 
ATOM   3043 O  O    A ILE   A 1 137 ? 11.980 -12.079 -3.603  0.62 14.74 ?  137 ILE   A O    1 
ATOM   3044 O  O    B ILE   A 1 137 ? 11.882 -12.133 -3.842  0.38 16.46 ?  137 ILE   A O    1 
ATOM   3045 C  CB   A ILE   A 1 137 ? 9.202  -10.531 -4.706  0.62 17.60 ?  137 ILE   A CB   1 
ATOM   3046 C  CB   B ILE   A 1 137 ? 9.180  -10.535 -4.943  0.38 17.91 ?  137 ILE   A CB   1 
ATOM   3047 C  CG1  A ILE   A 1 137 ? 8.010  -9.725  -4.169  0.62 19.54 ?  137 ILE   A CG1  1 
ATOM   3048 C  CG1  B ILE   A 1 137 ? 8.038  -9.591  -4.555  0.38 19.16 ?  137 ILE   A CG1  1 
ATOM   3049 C  CG2  A ILE   A 1 137 ? 8.895  -12.022 -4.644  0.62 18.30 ?  137 ILE   A CG2  1 
ATOM   3050 C  CG2  B ILE   A 1 137 ? 8.762  -11.982 -4.732  0.38 18.45 ?  137 ILE   A CG2  1 
ATOM   3051 C  CD1  A ILE   A 1 137 ? 6.725  -9.919  -4.960  0.62 20.89 ?  137 ILE   A CD1  1 
ATOM   3052 C  CD1  B ILE   A 1 137 ? 6.754  -9.825  -5.326  0.38 19.86 ?  137 ILE   A CD1  1 
ATOM   3053 H  H    A ILE   A 1 137 ? 10.389 -8.382  -4.695  0.62 18.29 ?  137 ILE   A H    1 
ATOM   3054 H  H    B ILE   A 1 137 ? 10.319 -8.367  -4.820  0.38 18.98 ?  137 ILE   A H    1 
ATOM   3055 H  HA   A ILE   A 1 137 ? 10.308 -10.348 -2.985  0.62 18.72 ?  137 ILE   A HA   1 
ATOM   3056 H  HA   B ILE   A 1 137 ? 10.241 -10.385 -3.192  0.38 19.78 ?  137 ILE   A HA   1 
ATOM   3057 H  HB   A ILE   A 1 137 ? 9.333  -10.283 -5.631  0.62 21.14 ?  137 ILE   A HB   1 
ATOM   3058 H  HB   B ILE   A 1 137 ? 9.379  -10.407 -5.882  0.38 21.51 ?  137 ILE   A HB   1 
ATOM   3059 H  HG12 A ILE   A 1 137 ? 7.837  -9.985  -3.252  0.62 23.46 ?  137 ILE   A HG12 1 
ATOM   3060 H  HG12 B ILE   A 1 137 ? 7.847  -9.706  -3.611  0.38 23.02 ?  137 ILE   A HG12 1 
ATOM   3061 H  HG13 A ILE   A 1 137 ? 8.233  -8.776  -4.200  0.62 23.46 ?  137 ILE   A HG13 1 
ATOM   3062 H  HG13 B ILE   A 1 137 ? 8.315  -8.676  -4.722  0.38 23.02 ?  137 ILE   A HG13 1 
ATOM   3063 H  HG21 A ILE   A 1 137 ? 8.149  -12.220 -5.229  0.62 21.98 ?  137 ILE   A HG21 1 
ATOM   3064 H  HG21 B ILE   A 1 137 ? 7.966  -12.165 -5.254  0.38 22.15 ?  137 ILE   A HG21 1 
ATOM   3065 H  HG22 A ILE   A 1 137 ? 9.664  -12.523 -4.937  0.62 21.98 ?  137 ILE   A HG22 1 
ATOM   3066 H  HG22 B ILE   A 1 137 ? 9.480  -12.566 -5.019  0.38 22.15 ?  137 ILE   A HG22 1 
ATOM   3067 H  HG23 A ILE   A 1 137 ? 8.670  -12.255 -3.731  0.62 21.98 ?  137 ILE   A HG23 1 
ATOM   3068 H  HG23 B ILE   A 1 137 ? 8.579  -12.120 -3.790  0.38 22.15 ?  137 ILE   A HG23 1 
ATOM   3069 H  HD11 A ILE   A 1 137 ? 5.985  -9.671  -4.393  0.62 25.08 ?  137 ILE   A HD11 1 
ATOM   3070 H  HD11 B ILE   A 1 137 ? 6.385  -8.971  -5.592  0.38 23.86 ?  137 ILE   A HD11 1 
ATOM   3071 H  HD12 A ILE   A 1 137 ? 6.750  -9.354  -5.749  0.62 25.08 ?  137 ILE   A HD12 1 
ATOM   3072 H  HD12 B ILE   A 1 137 ? 6.952  -10.358 -6.111  0.38 23.86 ?  137 ILE   A HD12 1 
ATOM   3073 H  HD13 A ILE   A 1 137 ? 6.628  -10.846 -5.223  0.62 25.08 ?  137 ILE   A HD13 1 
ATOM   3074 H  HD13 B ILE   A 1 137 ? 6.127  -10.298 -4.755  0.38 23.86 ?  137 ILE   A HD13 1 
ATOM   3075 N  N    A HIS   A 1 138 ? 12.268 -10.842 -5.465  0.62 15.22 ?  138 HIS   A N    1 
ATOM   3076 N  N    B HIS   A 1 138 ? 12.320 -10.769 -5.575  0.38 15.91 ?  138 HIS   A N    1 
ATOM   3077 C  CA   A HIS   A 1 138 ? 13.444 -11.603 -5.873  0.62 15.54 ?  138 HIS   A CA   1 
ATOM   3078 C  CA   B HIS   A 1 138 ? 13.491 -11.536 -5.978  0.38 15.77 ?  138 HIS   A CA   1 
ATOM   3079 C  C    A HIS   A 1 138 ? 14.585 -11.440 -4.875  0.62 14.69 ?  138 HIS   A C    1 
ATOM   3080 C  C    B HIS   A 1 138 ? 14.618 -11.415 -4.955  0.38 14.80 ?  138 HIS   A C    1 
ATOM   3081 O  O    A HIS   A 1 138 ? 15.240 -12.421 -4.504  0.62 15.26 ?  138 HIS   A O    1 
ATOM   3082 O  O    B HIS   A 1 138 ? 15.287 -12.406 -4.639  0.38 15.12 ?  138 HIS   A O    1 
ATOM   3083 C  CB   A HIS   A 1 138 ? 13.877 -11.182 -7.276  0.62 16.70 ?  138 HIS   A CB   1 
ATOM   3084 C  CB   B HIS   A 1 138 ? 13.946 -11.065 -7.356  0.38 16.75 ?  138 HIS   A CB   1 
ATOM   3085 C  CG   A HIS   A 1 138 ? 15.142 -11.837 -7.733  0.62 17.66 ?  138 HIS   A CG   1 
ATOM   3086 C  CG   B HIS   A 1 138 ? 15.223 -11.691 -7.812  0.38 17.42 ?  138 HIS   A CG   1 
ATOM   3087 N  ND1  A HIS   A 1 138 ? 15.238 -13.193 -7.964  0.62 18.51 ?  138 HIS   A ND1  1 
ATOM   3088 N  ND1  B HIS   A 1 138 ? 15.349 -13.045 -8.037  0.38 18.00 ?  138 HIS   A ND1  1 
ATOM   3089 C  CD2  A HIS   A 1 138 ? 16.368 -11.324 -7.987  0.62 17.64 ?  138 HIS   A CD2  1 
ATOM   3090 C  CD2  B HIS   A 1 138 ? 16.434 -11.150 -8.075  0.38 17.72 ?  138 HIS   A CD2  1 
ATOM   3091 C  CE1  A HIS   A 1 138 ? 16.468 -13.484 -8.349  0.62 18.94 ?  138 HIS   A CE1  1 
ATOM   3092 C  CE1  B HIS   A 1 138 ? 16.584 -13.309 -8.424  0.38 18.12 ?  138 HIS   A CE1  1 
ATOM   3093 N  NE2  A HIS   A 1 138 ? 17.174 -12.369 -8.368  0.62 18.15 ?  138 HIS   A NE2  1 
ATOM   3094 N  NE2  B HIS   A 1 138 ? 17.263 -12.176 -8.454  0.38 18.02 ?  138 HIS   A NE2  1 
ATOM   3095 H  H    A HIS   A 1 138 ? 12.031 -10.222 -6.018  0.62 18.28 ?  138 HIS   A H    1 
ATOM   3096 H  H    B HIS   A 1 138 ? 12.139 -10.098 -6.084  0.38 19.12 ?  138 HIS   A H    1 
ATOM   3097 H  HA   A HIS   A 1 138 ? 13.208 -12.540 -5.910  0.62 18.67 ?  138 HIS   A HA   1 
ATOM   3098 H  HA   B HIS   A 1 138 ? 13.245 -12.470 -6.048  0.38 18.95 ?  138 HIS   A HA   1 
ATOM   3099 H  HB2  A HIS   A 1 138 ? 13.176 -11.419 -7.909  0.62 20.07 ?  138 HIS   A HB2  1 
ATOM   3100 H  HB2  B HIS   A 1 138 ? 13.257 -11.286 -8.005  0.38 20.13 ?  138 HIS   A HB2  1 
ATOM   3101 H  HB3  A HIS   A 1 138 ? 14.018 -10.222 -7.293  0.62 20.07 ?  138 HIS   A HB3  1 
ATOM   3102 H  HB3  B HIS   A 1 138 ? 14.077 -10.104 -7.333  0.38 20.13 ?  138 HIS   A HB3  1 
ATOM   3103 H  HD1  A HIS   A 1 138 ? 14.599 -13.760 -7.878  0.62 22.24 ?  138 HIS   A HD1  1 
ATOM   3104 H  HD2  A HIS   A 1 138 ? 16.617 -10.430 -7.920  0.62 21.19 ?  138 HIS   A HD2  1 
ATOM   3105 H  HD2  B HIS   A 1 138 ? 16.659 -10.250 -8.012  0.38 21.28 ?  138 HIS   A HD2  1 
ATOM   3106 H  HE1  A HIS   A 1 138 ? 16.788 -14.331 -8.565  0.62 22.75 ?  138 HIS   A HE1  1 
ATOM   3107 H  HE1  B HIS   A 1 138 ? 16.917 -14.150 -8.636  0.38 21.76 ?  138 HIS   A HE1  1 
ATOM   3108 H  HE2  B HIS   A 1 138 ? 18.087 -12.094 -8.676  0.38 21.64 ?  138 HIS   A HE2  1 
ATOM   3109 N  N    . SER   A 1 139 ? 14.839 -10.212 -4.424  1.00 13.80 ?  139 SER   A N    1 
ATOM   3110 C  CA   . SER   A 1 139 ? 15.905 -10.015 -3.453  1.00 13.92 ?  139 SER   A CA   1 
ATOM   3111 C  C    . SER   A 1 139 ? 15.678 -10.850 -2.198  1.00 13.89 ?  139 SER   A C    1 
ATOM   3112 O  O    . SER   A 1 139 ? 16.623 -11.445 -1.664  1.00 13.73 ?  139 SER   A O    1 
ATOM   3113 C  CB   . SER   A 1 139 ? 16.036 -8.531  -3.112  1.00 13.67 ?  139 SER   A CB   1 
ATOM   3114 O  OG   . SER   A 1 139 ? 17.103 -8.358  -2.201  1.00 14.29 ?  139 SER   A OG   1 
ATOM   3115 H  H    A SER   A 1 139 ? 14.418 -9.501  -4.651  0.62 16.58 ?  139 SER   A H    1 
ATOM   3116 H  H    B SER   A 1 139 ? 14.389 -9.506  -4.607  0.38 16.58 ?  139 SER   A H    1 
ATOM   3117 H  HA   . SER   A 1 139 ? 16.746 -10.299 -3.845  1.00 16.72 ?  139 SER   A HA   1 
ATOM   3118 H  HB2  . SER   A 1 139 ? 16.221 -8.027  -3.921  1.00 16.43 ?  139 SER   A HB2  1 
ATOM   3119 H  HB3  . SER   A 1 139 ? 15.210 -8.218  -2.706  1.00 16.43 ?  139 SER   A HB3  1 
ATOM   3120 H  HG   . SER   A 1 139 ? 17.185 -7.539  -1.999  1.00 17.17 ?  139 SER   A HG   1 
ATOM   3121 N  N    . LEU   A 1 140 ? 14.436 -10.912 -1.716  1.00 13.62 ?  140 LEU   A N    1 
ATOM   3122 C  CA   . LEU   A 1 140 ? 14.152 -11.725 -0.537  1.00 13.44 ?  140 LEU   A CA   1 
ATOM   3123 C  C    . LEU   A 1 140 ? 14.419 -13.201 -0.811  1.00 13.57 ?  140 LEU   A C    1 
ATOM   3124 O  O    . LEU   A 1 140 ? 14.955 -13.916 0.046   1.00 13.95 ?  140 LEU   A O    1 
ATOM   3125 C  CB   . LEU   A 1 140 ? 12.708 -11.500 -0.089  1.00 13.85 ?  140 LEU   A CB   1 
ATOM   3126 C  CG   . LEU   A 1 140 ? 12.233 -12.353 1.090   1.00 14.56 ?  140 LEU   A CG   1 
ATOM   3127 C  CD1  . LEU   A 1 140 ? 13.132 -12.181 2.311   1.00 15.43 ?  140 LEU   A CD1  1 
ATOM   3128 C  CD2  . LEU   A 1 140 ? 10.766 -12.028 1.434   1.00 15.22 ?  140 LEU   A CD2  1 
ATOM   3129 H  H    . LEU   A 1 140 ? 13.756 -10.492 -2.041  1.00 16.36 ?  140 LEU   A H    1 
ATOM   3130 H  HA   . LEU   A 1 140 ? 14.730 -11.447 0.186   1.00 16.14 ?  140 LEU   A HA   1 
ATOM   3131 H  HB2  . LEU   A 1 140 ? 12.606 -10.575 0.169   1.00 16.64 ?  140 LEU   A HB2  1 
ATOM   3132 H  HB3  . LEU   A 1 140 ? 12.121 -11.695 -0.838  1.00 16.64 ?  140 LEU   A HB3  1 
ATOM   3133 H  HG   . LEU   A 1 140 ? 12.258 -13.290 0.830   1.00 17.49 ?  140 LEU   A HG   1 
ATOM   3134 H  HD11 . LEU   A 1 140 ? 12.742 -12.671 3.057   1.00 18.54 ?  140 LEU   A HD11 1 
ATOM   3135 H  HD12 . LEU   A 1 140 ? 14.007 -12.545 2.105   1.00 18.54 ?  140 LEU   A HD12 1 
ATOM   3136 H  HD13 . LEU   A 1 140 ? 13.196 -11.245 2.525   1.00 18.54 ?  140 LEU   A HD13 1 
ATOM   3137 H  HD21 . LEU   A 1 140 ? 10.483 -12.581 2.183   1.00 18.28 ?  140 LEU   A HD21 1 
ATOM   3138 H  HD22 . LEU   A 1 140 ? 10.696 -11.091 1.673   1.00 18.28 ?  140 LEU   A HD22 1 
ATOM   3139 H  HD23 . LEU   A 1 140 ? 10.207 -12.214 0.662   1.00 18.28 ?  140 LEU   A HD23 1 
ATOM   3140 N  N    . ARG   A 1 141 ? 14.050 -13.673 -2.003  1.00 13.96 ?  141 ARG   A N    1 
ATOM   3141 C  CA   . ARG   A 1 141 ? 14.292 -15.068 -2.354  1.00 15.51 ?  141 ARG   A CA   1 
ATOM   3142 C  C    . ARG   A 1 141 ? 15.786 -15.373 -2.360  1.00 14.47 ?  141 ARG   A C    1 
ATOM   3143 O  O    . ARG   A 1 141 ? 16.230 -16.390 -1.812  1.00 14.96 ?  141 ARG   A O    1 
ATOM   3144 C  CB   . ARG   A 1 141 ? 13.676 -15.354 -3.724  1.00 17.46 ?  141 ARG   A CB   1 
ATOM   3145 C  CG   . ARG   A 1 141 ? 13.690 -16.809 -4.142  1.00 20.87 ?  141 ARG   A CG   1 
ATOM   3146 C  CD   . ARG   A 1 141 ? 12.641 -17.575 -3.395  1.00 24.28 ?  141 ARG   A CD   1 
ATOM   3147 N  NE   . ARG   A 1 141 ? 13.234 -18.401 -2.357  1.00 25.28 ?  141 ARG   A NE   1 
ATOM   3148 C  CZ   . ARG   A 1 141 ? 12.549 -18.952 -1.364  1.00 26.07 ?  141 ARG   A CZ   1 
ATOM   3149 N  NH1  . ARG   A 1 141 ? 11.269 -18.678 -1.169  1.00 25.46 ?  141 ARG   A NH1  1 
ATOM   3150 N  NH2  . ARG   A 1 141 ? 13.167 -19.790 -0.536  1.00 27.00 ?  141 ARG   A NH2  1 
ATOM   3151 H  H    . ARG   A 1 141 ? 13.661 -13.213 -2.620  1.00 16.77 ?  141 ARG   A H    1 
ATOM   3152 H  HA   . ARG   A 1 141 ? 13.870 -15.644 -1.702  1.00 18.63 ?  141 ARG   A HA   1 
ATOM   3153 H  HB2  . ARG   A 1 141 ? 12.750 -15.058 -3.716  1.00 20.98 ?  141 ARG   A HB2  1 
ATOM   3154 H  HB3  . ARG   A 1 141 ? 14.166 -14.858 -4.394  1.00 20.98 ?  141 ARG   A HB3  1 
ATOM   3155 H  HG2  . ARG   A 1 141 ? 13.501 -16.877 -5.093  1.00 25.06 ?  141 ARG   A HG2  1 
ATOM   3156 H  HG3  . ARG   A 1 141 ? 14.557 -17.201 -3.944  1.00 25.06 ?  141 ARG   A HG3  1 
ATOM   3157 H  HD2  . ARG   A 1 141 ? 12.029 -16.956 -2.964  1.00 29.16 ?  141 ARG   A HD2  1 
ATOM   3158 H  HD3  . ARG   A 1 141 ? 12.153 -18.145 -4.014  1.00 29.16 ?  141 ARG   A HD3  1 
ATOM   3159 H  HE   . ARG   A 1 141 ? 14.049 -18.649 -2.461  1.00 30.35 ?  141 ARG   A HE   1 
ATOM   3160 H  HH11 . ARG   A 1 141 ? 10.852 -18.147 -1.702  1.00 30.57 ?  141 ARG   A HH11 1 
ATOM   3161 H  HH12 . ARG   A 1 141 ? 10.845 -19.041 -0.512  1.00 30.57 ?  141 ARG   A HH12 1 
ATOM   3162 H  HH21 . ARG   A 1 141 ? 13.997 -19.976 -0.655  1.00 32.42 ?  141 ARG   A HH21 1 
ATOM   3163 H  HH22 . ARG   A 1 141 ? 12.736 -20.144 0.120   1.00 32.42 ?  141 ARG   A HH22 1 
ATOM   3164 N  N    . VAL   A 1 142 ? 16.583 -14.503 -2.983  1.00 13.78 ?  142 VAL   A N    1 
ATOM   3165 C  CA   . VAL   A 1 142 ? 18.030 -14.711 -2.996  1.00 13.85 ?  142 VAL   A CA   1 
ATOM   3166 C  C    . VAL   A 1 142 ? 18.582 -14.692 -1.578  1.00 13.08 ?  142 VAL   A C    1 
ATOM   3167 O  O    . VAL   A 1 142 ? 19.450 -15.496 -1.219  1.00 13.49 ?  142 VAL   A O    1 
ATOM   3168 C  CB   . VAL   A 1 142 ? 18.733 -13.688 -3.906  1.00 14.09 ?  142 VAL   A CB   1 
ATOM   3169 C  CG1  . VAL   A 1 142 ? 20.250 -13.903 -3.866  1.00 14.09 ?  142 VAL   A CG1  1 
ATOM   3170 C  CG2  . VAL   A 1 142 ? 18.239 -13.804 -5.333  1.00 15.42 ?  142 VAL   A CG2  1 
ATOM   3171 H  H    . VAL   A 1 142 ? 16.319 -13.791 -3.399  1.00 16.56 ?  142 VAL   A H    1 
ATOM   3172 H  HA   . VAL   A 1 142 ? 18.211 -15.583 -3.363  1.00 16.64 ?  142 VAL   A HA   1 
ATOM   3173 H  HB   . VAL   A 1 142 ? 18.555 -12.784 -3.592  1.00 16.93 ?  142 VAL   A HB   1 
ATOM   3174 H  HG11 . VAL   A 1 142 ? 20.664 -13.396 -4.584  1.00 16.93 ?  142 VAL   A HG11 1 
ATOM   3175 H  HG12 . VAL   A 1 142 ? 20.596 -13.592 -3.010  1.00 16.93 ?  142 VAL   A HG12 1 
ATOM   3176 H  HG13 . VAL   A 1 142 ? 20.439 -14.846 -3.976  1.00 16.93 ?  142 VAL   A HG13 1 
ATOM   3177 H  HG21 . VAL   A 1 142 ? 18.716 -13.160 -5.884  1.00 18.52 ?  142 VAL   A HG21 1 
ATOM   3178 H  HG22 . VAL   A 1 142 ? 18.416 -14.702 -5.649  1.00 18.52 ?  142 VAL   A HG22 1 
ATOM   3179 H  HG23 . VAL   A 1 142 ? 17.293 -13.620 -5.349  1.00 18.52 ?  142 VAL   A HG23 1 
ATOM   3180 N  N    . CYS   A 1 143 ? 18.100 -13.766 -0.751  1.00 13.03 ?  143 CYS   A N    1 
ATOM   3181 C  CA   . CYS   A 1 143 ? 18.550 -13.706 0.634   1.00 13.36 ?  143 CYS   A CA   1 
ATOM   3182 C  C    . CYS   A 1 143 ? 18.327 -15.045 1.329   1.00 13.50 ?  143 CYS   A C    1 
ATOM   3183 O  O    . CYS   A 1 143 ? 19.246 -15.626 1.915   1.00 13.63 ?  143 CYS   A O    1 
ATOM   3184 C  CB   . CYS   A 1 143 ? 17.799 -12.598 1.366   1.00 14.01 ?  143 CYS   A CB   1 
ATOM   3185 S  SG   . CYS   A 1 143 ? 18.281 -12.407 3.091   1.00 14.20 ?  143 CYS   A SG   1 
ATOM   3186 H  H    . CYS   A 1 143 ? 17.517 -13.166 -0.965  1.00 15.65 ?  143 CYS   A H    1 
ATOM   3187 H  HA   . CYS   A 1 143 ? 19.496 -13.505 0.658   1.00 16.05 ?  143 CYS   A HA   1 
ATOM   3188 H  HB2  . CYS   A 1 143 ? 17.957 -11.756 0.913   1.00 16.83 ?  143 CYS   A HB2  1 
ATOM   3189 H  HB3  . CYS   A 1 143 ? 16.849 -12.801 1.346   1.00 16.83 ?  143 CYS   A HB3  1 
ATOM   3190 H  HG   . CYS   A 1 143 ? 17.681 -11.481 3.559   1.00 17.06 ?  143 CYS   A HG   1 
ATOM   3191 N  N    . VAL   A 1 144 ? 17.096 -15.553 1.267   1.00 14.07 ?  144 VAL   A N    1 
ATOM   3192 C  CA   . VAL   A 1 144 ? 16.752 -16.788 1.963   1.00 15.59 ?  144 VAL   A CA   1 
ATOM   3193 C  C    . VAL   A 1 144 ? 17.578 -17.956 1.446   1.00 15.32 ?  144 VAL   A C    1 
ATOM   3194 O  O    . VAL   A 1 144 ? 17.930 -18.867 2.206   1.00 15.83 ?  144 VAL   A O    1 
ATOM   3195 C  CB   . VAL   A 1 144 ? 15.239 -17.033 1.819   1.00 18.51 ?  144 VAL   A CB   1 
ATOM   3196 C  CG1  . VAL   A 1 144 ? 14.882 -18.488 2.072   1.00 20.45 ?  144 VAL   A CG1  1 
ATOM   3197 C  CG2  . VAL   A 1 144 ? 14.482 -16.061 2.735   1.00 18.31 ?  144 VAL   A CG2  1 
ATOM   3198 H  H    . VAL   A 1 144 ? 16.438 -15.200 0.827   1.00 16.90 ?  144 VAL   A H    1 
ATOM   3199 H  HA   . VAL   A 1 144 ? 16.942 -16.680 2.903   1.00 18.73 ?  144 VAL   A HA   1 
ATOM   3200 H  HB   . VAL   A 1 144 ? 14.976 -16.823 0.905   1.00 22.23 ?  144 VAL   A HB   1 
ATOM   3201 H  HG11 . VAL   A 1 144 ? 13.922 -18.555 2.206   1.00 24.56 ?  144 VAL   A HG11 1 
ATOM   3202 H  HG12 . VAL   A 1 144 ? 15.140 -19.018 1.301   1.00 24.56 ?  144 VAL   A HG12 1 
ATOM   3203 H  HG13 . VAL   A 1 144 ? 15.349 -18.794 2.862   1.00 24.56 ?  144 VAL   A HG13 1 
ATOM   3204 H  HG21 . VAL   A 1 144 ? 13.524 -16.219 2.651   1.00 22.00 ?  144 VAL   A HG21 1 
ATOM   3205 H  HG22 . VAL   A 1 144 ? 14.756 -16.206 3.653   1.00 22.00 ?  144 VAL   A HG22 1 
ATOM   3206 H  HG23 . VAL   A 1 144 ? 14.682 -15.146 2.472   1.00 22.00 ?  144 VAL   A HG23 1 
ATOM   3207 N  N    . ASP   A 1 145 ? 17.849 -17.980 0.147   1.00 15.56 ?  145 ASP   A N    1 
ATOM   3208 C  CA   . ASP   A 1 145 ? 18.572 -19.085 -0.475  1.00 16.02 ?  145 ASP   A CA   1 
ATOM   3209 C  C    . ASP   A 1 145 ? 20.093 -18.941 -0.403  1.00 15.83 ?  145 ASP   A C    1 
ATOM   3210 O  O    . ASP   A 1 145 ? 20.804 -19.840 -0.865  1.00 18.13 ?  145 ASP   A O    1 
ATOM   3211 C  CB   . ASP   A 1 145 ? 18.149 -19.223 -1.941  1.00 17.65 ?  145 ASP   A CB   1 
ATOM   3212 C  CG   . ASP   A 1 145 ? 16.715 -19.705 -2.103  1.00 20.05 ?  145 ASP   A CG   1 
ATOM   3213 O  OD1  . ASP   A 1 145 ? 16.123 -20.228 -1.132  1.00 20.87 ?  145 ASP   A OD1  1 
ATOM   3214 O  OD2  . ASP   A 1 145 ? 16.183 -19.548 -3.219  1.00 21.78 -1 145 ASP   A OD2  1 
ATOM   3215 H  H    . ASP   A 1 145 ? 17.605 -17.369 -0.408  1.00 18.69 ?  145 ASP   A H    1 
ATOM   3216 H  HA   . ASP   A 1 145 ? 18.328 -19.907 -0.023  1.00 19.24 ?  145 ASP   A HA   1 
ATOM   3217 H  HB2  . ASP   A 1 145 ? 18.225 -18.358 -2.374  1.00 21.20 ?  145 ASP   A HB2  1 
ATOM   3218 H  HB3  . ASP   A 1 145 ? 18.733 -19.864 -2.375  1.00 21.20 ?  145 ASP   A HB3  1 
ATOM   3219 N  N    . THR   A 1 146 ? 20.608 -17.838 0.136   1.00 14.21 ?  146 THR   A N    1 
ATOM   3220 C  CA   . THR   A 1 146 ? 22.047 -17.583 0.167   1.00 13.58 ?  146 THR   A CA   1 
ATOM   3221 C  C    . THR   A 1 146 ? 22.591 -17.392 1.569   1.00 13.65 ?  146 THR   A C    1 
ATOM   3222 O  O    . THR   A 1 146 ? 23.661 -17.928 1.896   1.00 14.54 ?  146 THR   A O    1 
ATOM   3223 C  CB   . THR   A 1 146 ? 22.373 -16.336 -0.672  1.00 13.56 ?  146 THR   A CB   1 
ATOM   3224 O  OG1  . THR   A 1 146 ? 21.856 -16.503 -1.994  1.00 13.97 ?  146 THR   A OG1  1 
ATOM   3225 C  CG2  . THR   A 1 146 ? 23.871 -16.094 -0.743  1.00 14.05 ?  146 THR   A CG2  1 
ATOM   3226 H  H    . THR   A 1 146 ? 20.135 -17.202 0.483   1.00 17.07 ?  146 THR   A H    1 
ATOM   3227 H  HA   . THR   A 1 146 ? 22.509 -18.333 -0.225  1.00 16.31 ?  146 THR   A HA   1 
ATOM   3228 H  HB   . THR   A 1 146 ? 21.963 -15.557 -0.262  1.00 16.30 ?  146 THR   A HB   1 
ATOM   3229 H  HG1  . THR   A 1 146 ? 21.022 -16.579 -1.963  1.00 16.79 ?  146 THR   A HG1  1 
ATOM   3230 H  HG21 . THR   A 1 146 ? 24.062 -15.428 -1.419  1.00 16.88 ?  146 THR   A HG21 1 
ATOM   3231 H  HG22 . THR   A 1 146 ? 24.196 -15.774 0.115   1.00 16.88 ?  146 THR   A HG22 1 
ATOM   3232 H  HG23 . THR   A 1 146 ? 24.327 -16.917 -0.968  1.00 16.88 ?  146 THR   A HG23 1 
ATOM   3233 N  N    . VAL   A 1 147 ? 21.905 -16.613 2.393   1.00 13.34 ?  147 VAL   A N    1 
ATOM   3234 C  CA   . VAL   A 1 147 ? 22.391 -16.308 3.729   1.00 13.75 ?  147 VAL   A CA   1 
ATOM   3235 C  C    . VAL   A 1 147 ? 22.072 -17.474 4.652   1.00 13.95 ?  147 VAL   A C    1 
ATOM   3236 O  O    . VAL   A 1 147 ? 20.933 -17.963 4.693   1.00 14.67 ?  147 VAL   A O    1 
ATOM   3237 C  CB   . VAL   A 1 147 ? 21.771 -14.999 4.241   1.00 13.88 ?  147 VAL   A CB   1 
ATOM   3238 C  CG1  . VAL   A 1 147 ? 22.316 -14.662 5.607   1.00 14.98 ?  147 VAL   A CG1  1 
ATOM   3239 C  CG2  . VAL   A 1 147 ? 22.016 -13.853 3.251   1.00 14.44 ?  147 VAL   A CG2  1 
ATOM   3240 H  H    . VAL   A 1 147 ? 21.146 -16.250 2.208   1.00 16.03 ?  147 VAL   A H    1 
ATOM   3241 H  HA   . VAL   A 1 147 ? 23.351 -16.198 3.703   1.00 16.52 ?  147 VAL   A HA   1 
ATOM   3242 H  HB   . VAL   A 1 147 ? 20.814 -15.117 4.327   1.00 16.67 ?  147 VAL   A HB   1 
ATOM   3243 H  HG11 . VAL   A 1 147 ? 22.053 -13.758 5.836   1.00 17.99 ?  147 VAL   A HG11 1 
ATOM   3244 H  HG12 . VAL   A 1 147 ? 21.951 -15.286 6.255   1.00 17.99 ?  147 VAL   A HG12 1 
ATOM   3245 H  HG13 . VAL   A 1 147 ? 23.282 -14.731 5.587   1.00 17.99 ?  147 VAL   A HG13 1 
ATOM   3246 H  HG21 . VAL   A 1 147 ? 21.685 -13.026 3.638   1.00 17.35 ?  147 VAL   A HG21 1 
ATOM   3247 H  HG22 . VAL   A 1 147 ? 22.963 -13.782 3.074   1.00 17.35 ?  147 VAL   A HG22 1 
ATOM   3248 H  HG23 . VAL   A 1 147 ? 21.536 -14.043 2.426   1.00 17.35 ?  147 VAL   A HG23 1 
ATOM   3249 N  N    . ARG   A 1 148 ? 23.087 -17.917 5.394   1.00 13.91 ?  148 ARG   A N    1 
ATOM   3250 C  CA   . ARG   A 1 148 ? 22.970 -18.989 6.368   1.00 14.36 ?  148 ARG   A CA   1 
ATOM   3251 C  C    . ARG   A 1 148 ? 23.076 -18.506 7.802   1.00 14.55 ?  148 ARG   A C    1 
ATOM   3252 O  O    . ARG   A 1 148 ? 22.669 -19.231 8.718   1.00 16.14 ?  148 ARG   A O    1 
ATOM   3253 C  CB   . ARG   A 1 148 ? 24.036 -20.064 6.116   1.00 15.14 ?  148 ARG   A CB   1 
ATOM   3254 C  CG   . ARG   A 1 148 ? 23.903 -20.722 4.764   1.00 16.76 ?  148 ARG   A CG   1 
ATOM   3255 C  CD   . ARG   A 1 148 ? 25.017 -21.741 4.522   1.00 17.56 ?  148 ARG   A CD   1 
ATOM   3256 N  NE   . ARG   A 1 148 ? 26.351 -21.150 4.560   1.00 17.36 ?  148 ARG   A NE   1 
ATOM   3257 C  CZ   . ARG   A 1 148 ? 26.873 -20.431 3.576   1.00 16.23 ?  148 ARG   A CZ   1 
ATOM   3258 N  NH1  . ARG   A 1 148 ? 26.212 -20.232 2.445   1.00 16.45 ?  148 ARG   A NH1  1 
ATOM   3259 N  NH2  . ARG   A 1 148 ? 28.082 -19.892 3.733   1.00 16.46 ?  148 ARG   A NH2  1 
ATOM   3260 H  H    . ARG   A 1 148 ? 23.886 -17.595 5.338   1.00 16.71 ?  148 ARG   A H    1 
ATOM   3261 H  HA   . ARG   A 1 148 ? 22.107 -19.407 6.269   1.00 17.25 ?  148 ARG   A HA   1 
ATOM   3262 H  HB2  . ARG   A 1 148 ? 24.918 -19.668 6.169   1.00 18.18 ?  148 ARG   A HB2  1 
ATOM   3263 H  HB3  . ARG   A 1 148 ? 23.948 -20.764 6.789   1.00 18.18 ?  148 ARG   A HB3  1 
ATOM   3264 H  HG2  . ARG   A 1 148 ? 23.047 -21.171 4.718   1.00 20.13 ?  148 ARG   A HG2  1 
ATOM   3265 H  HG3  . ARG   A 1 148 ? 23.958 -20.032 4.081   1.00 20.13 ?  148 ARG   A HG3  1 
ATOM   3266 H  HD2  . ARG   A 1 148 ? 24.967 -22.419 5.211   1.00 21.10 ?  148 ARG   A HD2  1 
ATOM   3267 H  HD3  . ARG   A 1 148 ? 24.882 -22.139 3.650   1.00 21.10 ?  148 ARG   A HD3  1 
ATOM   3268 H  HE   . ARG   A 1 148 ? 26.823 -21.275 5.263   1.00 20.86 ?  148 ARG   A HE   1 
ATOM   3269 H  HH11 . ARG   A 1 148 ? 25.431 -20.563 2.334   1.00 19.76 ?  148 ARG   A HH11 1 
ATOM   3270 H  HH12 . ARG   A 1 148 ? 26.570 -19.753 1.822   1.00 19.76 ?  148 ARG   A HH12 1 
ATOM   3271 H  HH21 . ARG   A 1 148 ? 28.514 -20.012 4.467   1.00 19.77 ?  148 ARG   A HH21 1 
ATOM   3272 H  HH22 . ARG   A 1 148 ? 28.429 -19.418 3.103   1.00 19.77 ?  148 ARG   A HH22 1 
ATOM   3273 N  N    . THR   A 1 149 ? 23.616 -17.310 8.011   1.00 14.66 ?  149 THR   A N    1 
ATOM   3274 C  CA   . THR   A 1 149 ? 23.680 -16.695 9.323   1.00 14.78 ?  149 THR   A CA   1 
ATOM   3275 C  C    . THR   A 1 149 ? 22.352 -15.995 9.614   1.00 14.11 ?  149 THR   A C    1 
ATOM   3276 O  O    . THR   A 1 149 ? 21.431 -15.986 8.787   1.00 14.92 ?  149 THR   A O    1 
ATOM   3277 C  CB   . THR   A 1 149 ? 24.880 -15.758 9.379   1.00 15.08 ?  149 THR   A CB   1 
ATOM   3278 O  OG1  . THR   A 1 149 ? 24.755 -14.832 8.297   1.00 14.98 ?  149 THR   A OG1  1 
ATOM   3279 C  CG2  . THR   A 1 149 ? 26.191 -16.554 9.270   1.00 15.34 ?  149 THR   A CG2  1 
ATOM   3280 H  H    . THR   A 1 149 ? 23.967 -16.821 7.390   1.00 17.62 ?  149 THR   A H    1 
ATOM   3281 H  HA   . THR   A 1 149 ? 23.807 -17.391 9.987   1.00 17.76 ?  149 THR   A HA   1 
ATOM   3282 H  HB   . THR   A 1 149 ? 24.873 -15.281 10.218  1.00 18.11 ?  149 THR   A HB   1 
ATOM   3283 H  HG1  . THR   A 1 149 ? 25.404 -14.298 8.294   1.00 17.99 ?  149 THR   A HG1  1 
ATOM   3284 H  HG21 . THR   A 1 149 ? 26.952 -15.952 9.324   1.00 18.42 ?  149 THR   A HG21 1 
ATOM   3285 H  HG22 . THR   A 1 149 ? 26.253 -17.201 9.992   1.00 18.42 ?  149 THR   A HG22 1 
ATOM   3286 H  HG23 . THR   A 1 149 ? 26.230 -17.029 8.422   1.00 18.42 ?  149 THR   A HG23 1 
ATOM   3287 N  N    . ASN   A 1 150 ? 22.219 -15.454 10.818  1.00 14.55 ?  150 ASN   A N    1 
ATOM   3288 C  CA   . ASN   A 1 150 ? 20.933 -14.932 11.275  1.00 15.16 ?  150 ASN   A CA   1 
ATOM   3289 C  C    . ASN   A 1 150 ? 20.760 -13.496 10.801  1.00 14.33 ?  150 ASN   A C    1 
ATOM   3290 O  O    . ASN   A 1 150 ? 21.524 -12.605 11.192  1.00 15.76 ?  150 ASN   A O    1 
ATOM   3291 C  CB   . ASN   A 1 150 ? 20.837 -15.028 12.793  1.00 17.79 ?  150 ASN   A CB   1 
ATOM   3292 C  CG   . ASN   A 1 150 ? 20.749 -16.458 13.265  1.00 21.62 ?  150 ASN   A CG   1 
ATOM   3293 O  OD1  . ASN   A 1 150 ? 20.160 -17.298 12.589  1.00 22.71 ?  150 ASN   A OD1  1 
ATOM   3294 N  ND2  . ASN   A 1 150 ? 21.349 -16.751 14.415  1.00 23.96 ?  150 ASN   A ND2  1 
ATOM   3295 H  H    . ASN   A 1 150 ? 22.854 -15.383 11.394  1.00 17.49 ?  150 ASN   A H    1 
ATOM   3296 H  HA   . ASN   A 1 150 ? 20.219 -15.470 10.894  1.00 18.21 ?  150 ASN   A HA   1 
ATOM   3297 H  HB2  . ASN   A 1 150 ? 21.624 -14.631 13.190  1.00 21.37 ?  150 ASN   A HB2  1 
ATOM   3298 H  HB3  . ASN   A 1 150 ? 20.037 -14.569 13.093  1.00 21.37 ?  150 ASN   A HB3  1 
ATOM   3299 H  HD21 . ASN   A 1 150 ? 21.334 -17.556 14.728  1.00 28.78 ?  150 ASN   A HD21 1 
ATOM   3300 H  HD22 . ASN   A 1 150 ? 21.759 -16.135 14.857  1.00 28.78 ?  150 ASN   A HD22 1 
ATOM   3301 N  N    . VAL   A 1 151 ? 19.762 -13.270 9.955   1.00 13.81 ?  151 VAL   A N    1 
ATOM   3302 C  CA   . VAL   A 1 151 ? 19.553 -11.967 9.342   1.00 14.19 ?  151 VAL   A CA   1 
ATOM   3303 C  C    . VAL   A 1 151 ? 18.163 -11.451 9.693   1.00 14.01 ?  151 VAL   A C    1 
ATOM   3304 O  O    . VAL   A 1 151 ? 17.152 -12.159 9.541   1.00 15.44 ?  151 VAL   A O    1 
ATOM   3305 C  CB   . VAL   A 1 151 ? 19.846 -11.974 7.826   1.00 15.89 ?  151 VAL   A CB   1 
ATOM   3306 C  CG1  . VAL   A 1 151 ? 19.026 -13.006 7.088   1.00 17.28 ?  151 VAL   A CG1  1 
ATOM   3307 C  CG2  . VAL   A 1 151 ? 19.650 -10.575 7.241   1.00 15.87 ?  151 VAL   A CG2  1 
ATOM   3308 H  H    . VAL   A 1 151 ? 19.190 -13.864 9.718   1.00 16.59 ?  151 VAL   A H    1 
ATOM   3309 H  HA   . VAL   A 1 151 ? 20.195 -11.350 9.736   1.00 17.05 ?  151 VAL   A HA   1 
ATOM   3310 H  HB   . VAL   A 1 151 ? 20.786 -12.207 7.697   1.00 19.08 ?  151 VAL   A HB   1 
ATOM   3311 H  HG11 . VAL   A 1 151 ? 19.202 -12.936 6.137   1.00 20.75 ?  151 VAL   A HG11 1 
ATOM   3312 H  HG12 . VAL   A 1 151 ? 19.277 -13.892 7.403   1.00 20.75 ?  151 VAL   A HG12 1 
ATOM   3313 H  HG13 . VAL   A 1 151 ? 18.086 -12.849 7.264   1.00 20.75 ?  151 VAL   A HG13 1 
ATOM   3314 H  HG21 . VAL   A 1 151 ? 19.983 -10.565 6.326   1.00 19.06 ?  151 VAL   A HG21 1 
ATOM   3315 H  HG22 . VAL   A 1 151 ? 18.708 -10.356 7.249   1.00 19.06 ?  151 VAL   A HG22 1 
ATOM   3316 H  HG23 . VAL   A 1 151 ? 20.148 -9.933  7.773   1.00 19.06 ?  151 VAL   A HG23 1 
ATOM   3317 N  N    . TYR   A 1 152 ? 18.143 -10.207 10.168  1.00 14.03 ?  152 TYR   A N    1 
ATOM   3318 C  CA   . TYR   A 1 152 ? 16.946 -9.478  10.552  1.00 14.07 ?  152 TYR   A CA   1 
ATOM   3319 C  C    . TYR   A 1 152 ? 16.748 -8.378  9.519   1.00 13.17 ?  152 TYR   A C    1 
ATOM   3320 O  O    . TYR   A 1 152 ? 17.525 -7.415  9.472   1.00 13.66 ?  152 TYR   A O    1 
ATOM   3321 C  CB   . TYR   A 1 152 ? 17.125 -8.929  11.963  1.00 15.19 ?  152 TYR   A CB   1 
ATOM   3322 C  CG   . TYR   A 1 152 ? 17.082 -10.036 12.972  1.00 15.87 ?  152 TYR   A CG   1 
ATOM   3323 C  CD1  . TYR   A 1 152 ? 18.211 -10.795 13.262  1.00 17.66 ?  152 TYR   A CD1  1 
ATOM   3324 C  CD2  . TYR   A 1 152 ? 15.895 -10.360 13.611  1.00 16.29 ?  152 TYR   A CD2  1 
ATOM   3325 C  CE1  . TYR   A 1 152 ? 18.165 -11.834 14.168  1.00 19.34 ?  152 TYR   A CE1  1 
ATOM   3326 C  CE2  . TYR   A 1 152 ? 15.838 -11.406 14.527  1.00 18.06 ?  152 TYR   A CE2  1 
ATOM   3327 C  CZ   . TYR   A 1 152 ? 16.981 -12.138 14.803  1.00 19.45 ?  152 TYR   A CZ   1 
ATOM   3328 O  OH   . TYR   A 1 152 ? 16.940 -13.182 15.707  1.00 22.63 ?  152 TYR   A OH   1 
ATOM   3329 H  H    . TYR   A 1 152 ? 18.865 -9.729  10.265  1.00 16.86 ?  152 TYR   A H    1 
ATOM   3330 H  HA   . TYR   A 1 152 ? 16.187 -10.075 10.539  1.00 16.91 ?  152 TYR   A HA   1 
ATOM   3331 H  HB2  . TYR   A 1 152 ? 17.994 -8.496  12.031  1.00 18.25 ?  152 TYR   A HB2  1 
ATOM   3332 H  HB3  . TYR   A 1 152 ? 16.422 -8.302  12.162  1.00 18.25 ?  152 TYR   A HB3  1 
ATOM   3333 H  HD1  . TYR   A 1 152 ? 19.015 -10.598 12.833  1.00 21.21 ?  152 TYR   A HD1  1 
ATOM   3334 H  HD2  . TYR   A 1 152 ? 15.124 -9.864  13.424  1.00 19.57 ?  152 TYR   A HD2  1 
ATOM   3335 H  HE1  . TYR   A 1 152 ? 18.927 -12.327 14.354  1.00 23.23 ?  152 TYR   A HE1  1 
ATOM   3336 H  HE2  . TYR   A 1 152 ? 15.037 -11.604 14.954  1.00 21.69 ?  152 TYR   A HE2  1 
ATOM   3337 H  HH   . TYR   A 1 152 ? 16.166 -13.242 16.019  1.00 27.18 ?  152 TYR   A HH   1 
ATOM   3338 N  N    . LEU   A 1 153 ? 15.738 -8.542  8.669   1.00 13.37 ?  153 LEU   A N    1 
ATOM   3339 C  CA   . LEU   A 1 153 ? 15.495 -7.653  7.543   1.00 13.39 ?  153 LEU   A CA   1 
ATOM   3340 C  C    . LEU   A 1 153 ? 14.496 -6.576  7.928   1.00 14.08 ?  153 LEU   A C    1 
ATOM   3341 O  O    . LEU   A 1 153 ? 13.404 -6.883  8.420   1.00 15.35 ?  153 LEU   A O    1 
ATOM   3342 C  CB   . LEU   A 1 153 ? 14.922 -8.439  6.363   1.00 13.56 ?  153 LEU   A CB   1 
ATOM   3343 C  CG   . LEU   A 1 153 ? 15.860 -9.450  5.705   1.00 13.79 ?  153 LEU   A CG   1 
ATOM   3344 C  CD1  . LEU   A 1 153 ? 15.078 -10.330 4.737   1.00 14.02 ?  153 LEU   A CD1  1 
ATOM   3345 C  CD2  . LEU   A 1 153 ? 16.998 -8.733  4.978   1.00 14.46 ?  153 LEU   A CD2  1 
ATOM   3346 H  H    . LEU   A 1 153 ? 15.157 -9.182  8.736   1.00 16.06 ?  153 LEU   A H    1 
ATOM   3347 H  HA   . LEU   A 1 153 ? 16.328 -7.238  7.282   1.00 16.09 ?  153 LEU   A HA   1 
ATOM   3348 H  HB2  . LEU   A 1 153 ? 14.144 -8.924  6.674   1.00 16.29 ?  153 LEU   A HB2  1 
ATOM   3349 H  HB3  . LEU   A 1 153 ? 14.659 -7.802  5.683   1.00 16.29 ?  153 LEU   A HB3  1 
ATOM   3350 H  HG   . LEU   A 1 153 ? 16.252 -10.019 6.391   1.00 16.57 ?  153 LEU   A HG   1 
ATOM   3351 H  HD11 . LEU   A 1 153 ? 15.662 -11.020 4.395   1.00 16.84 ?  153 LEU   A HD11 1 
ATOM   3352 H  HD12 . LEU   A 1 153 ? 14.329 -10.722 5.205   1.00 16.84 ?  153 LEU   A HD12 1 
ATOM   3353 H  HD13 . LEU   A 1 153 ? 14.757 -9.773  4.005   1.00 16.84 ?  153 LEU   A HD13 1 
ATOM   3354 H  HD21 . LEU   A 1 153 ? 17.543 -9.388  4.523   1.00 17.37 ?  153 LEU   A HD21 1 
ATOM   3355 H  HD22 . LEU   A 1 153 ? 16.614 -8.114  4.336   1.00 17.37 ?  153 LEU   A HD22 1 
ATOM   3356 H  HD23 . LEU   A 1 153 ? 17.531 -8.246  5.627   1.00 17.37 ?  153 LEU   A HD23 1 
ATOM   3357 N  N    A ALA   A 1 154 ? 14.894 -5.322  7.743   0.62 13.98 ?  154 ALA   A N    1 
ATOM   3358 N  N    B ALA   A 1 154 ? 14.840 -5.322  7.649   0.38 14.09 ?  154 ALA   A N    1 
ATOM   3359 C  CA   A ALA   A 1 154 ? 14.034 -4.171  7.960   0.62 14.58 ?  154 ALA   A CA   1 
ATOM   3360 C  CA   B ALA   A 1 154 ? 13.961 -4.182  7.887   0.38 14.46 ?  154 ALA   A CA   1 
ATOM   3361 C  C    A ALA   A 1 154 ? 13.541 -3.688  6.604   0.62 14.80 ?  154 ALA   A C    1 
ATOM   3362 C  C    B ALA   A 1 154 ? 13.521 -3.610  6.543   0.38 14.69 ?  154 ALA   A C    1 
ATOM   3363 O  O    A ALA   A 1 154 ? 14.347 -3.367  5.721   0.62 15.70 ?  154 ALA   A O    1 
ATOM   3364 O  O    B ALA   A 1 154 ? 14.356 -3.133  5.765   0.38 15.20 ?  154 ALA   A O    1 
ATOM   3365 C  CB   A ALA   A 1 154 ? 14.799 -3.058  8.675   0.62 15.05 ?  154 ALA   A CB   1 
ATOM   3366 C  CB   B ALA   A 1 154 ? 14.683 -3.114  8.708   0.38 14.75 ?  154 ALA   A CB   1 
ATOM   3367 H  H    A ALA   A 1 154 ? 15.690 -5.108  7.482   0.62 16.79 ?  154 ALA   A H    1 
ATOM   3368 H  H    B ALA   A 1 154 ? 15.600 -5.103  7.311   0.38 16.93 ?  154 ALA   A H    1 
ATOM   3369 H  HA   A ALA   A 1 154 ? 13.273 -4.427  8.500   0.62 17.51 ?  154 ALA   A HA   1 
ATOM   3370 H  HA   B ALA   A 1 154 ? 13.175 -4.472  8.378   0.38 17.38 ?  154 ALA   A HA   1 
ATOM   3371 H  HB1  A ALA   A 1 154 ? 14.201 -2.303  8.805   0.62 18.08 ?  154 ALA   A HB1  1 
ATOM   3372 H  HB1  B ALA   A 1 154 ? 14.080 -2.368  8.853   0.38 17.72 ?  154 ALA   A HB1  1 
ATOM   3373 H  HB2  A ALA   A 1 154 ? 15.106 -3.386  9.533   0.62 18.08 ?  154 ALA   A HB2  1 
ATOM   3374 H  HB2  B ALA   A 1 154 ? 14.949 -3.494  9.561   0.38 17.72 ?  154 ALA   A HB2  1 
ATOM   3375 H  HB3  A ALA   A 1 154 ? 15.554 -2.791  8.130   0.62 18.08 ?  154 ALA   A HB3  1 
ATOM   3376 H  HB3  B ALA   A 1 154 ? 15.466 -2.817  8.220   0.38 17.72 ?  154 ALA   A HB3  1 
ATOM   3377 N  N    A VAL   A 1 155 ? 12.222 -3.650  6.443   0.62 15.11 ?  155 VAL   A N    1 
ATOM   3378 N  N    B VAL   A 1 155 ? 12.214 -3.641  6.284   0.38 14.93 ?  155 VAL   A N    1 
ATOM   3379 C  CA   A VAL   A 1 155 ? 11.568 -3.173  5.231   0.62 15.69 ?  155 VAL   A CA   1 
ATOM   3380 C  CA   B VAL   A 1 155 ? 11.629 -3.195  5.022   0.38 15.69 ?  155 VAL   A CA   1 
ATOM   3381 C  C    A VAL   A 1 155 ? 10.842 -1.888  5.594   0.62 16.28 ?  155 VAL   A C    1 
ATOM   3382 C  C    B VAL   A 1 155 ? 10.811 -1.939  5.307   0.38 16.51 ?  155 VAL   A C    1 
ATOM   3383 O  O    A VAL   A 1 155 ? 9.923  -1.902  6.419   0.62 16.51 ?  155 VAL   A O    1 
ATOM   3384 O  O    B VAL   A 1 155 ? 9.795  -1.997  6.009   0.38 16.43 ?  155 VAL   A O    1 
ATOM   3385 C  CB   A VAL   A 1 155 ? 10.604 -4.224  4.661   0.62 15.72 ?  155 VAL   A CB   1 
ATOM   3386 C  CB   B VAL   A 1 155 ? 10.772 -4.295  4.379   0.38 15.59 ?  155 VAL   A CB   1 
ATOM   3387 C  CG1  A VAL   A 1 155 ? 9.884  -3.680  3.441   0.62 16.40 ?  155 VAL   A CG1  1 
ATOM   3388 C  CG1  B VAL   A 1 155 ? 10.153 -3.804  3.082   0.38 15.76 ?  155 VAL   A CG1  1 
ATOM   3389 C  CG2  A VAL   A 1 155 ? 11.367 -5.498  4.309   0.62 16.15 ?  155 VAL   A CG2  1 
ATOM   3390 C  CG2  B VAL   A 1 155 ? 11.618 -5.541  4.133   0.38 15.86 ?  155 VAL   A CG2  1 
ATOM   3391 H  H    A VAL   A 1 155 ? 11.669 -3.906  7.049   0.62 18.16 ?  155 VAL   A H    1 
ATOM   3392 H  H    B VAL   A 1 155 ? 11.628 -3.930  6.846   0.38 17.93 ?  155 VAL   A H    1 
ATOM   3393 H  HA   A VAL   A 1 155 ? 12.235 -2.966  4.562   0.62 18.85 ?  155 VAL   A HA   1 
ATOM   3394 H  HA   B VAL   A 1 155 ? 12.339 -2.961  4.405   0.38 18.85 ?  155 VAL   A HA   1 
ATOM   3395 H  HB   A VAL   A 1 155 ? 9.938  -4.439  5.336   0.62 18.88 ?  155 VAL   A HB   1 
ATOM   3396 H  HB   B VAL   A 1 155 ? 10.055 -4.534  4.986   0.38 18.72 ?  155 VAL   A HB   1 
ATOM   3397 H  HG11 A VAL   A 1 155 ? 9.413  -4.408  3.005   0.62 19.70 ?  155 VAL   A HG11 1 
ATOM   3398 H  HG11 B VAL   A 1 155 ? 9.767  -4.560  2.611   0.38 18.94 ?  155 VAL   A HG11 1 
ATOM   3399 H  HG12 A VAL   A 1 155 ? 9.249  -2.998  3.717   0.62 19.70 ?  155 VAL   A HG12 1 
ATOM   3400 H  HG12 B VAL   A 1 155 ? 9.458  -3.157  3.286   0.38 18.94 ?  155 VAL   A HG12 1 
ATOM   3401 H  HG13 A VAL   A 1 155 ? 10.535 -3.298  2.832   0.62 19.70 ?  155 VAL   A HG13 1 
ATOM   3402 H  HG13 B VAL   A 1 155 ? 10.841 -3.392  2.538   0.38 18.94 ?  155 VAL   A HG13 1 
ATOM   3403 H  HG21 A VAL   A 1 155 ? 10.752 -6.133  3.912   0.62 19.40 ?  155 VAL   A HG21 1 
ATOM   3404 H  HG21 B VAL   A 1 155 ? 11.081 -6.200  3.666   0.38 19.05 ?  155 VAL   A HG21 1 
ATOM   3405 H  HG22 A VAL   A 1 155 ? 12.071 -5.278  3.677   0.62 19.40 ?  155 VAL   A HG22 1 
ATOM   3406 H  HG22 B VAL   A 1 155 ? 12.388 -5.300  3.596   0.38 19.05 ?  155 VAL   A HG22 1 
ATOM   3407 H  HG23 A VAL   A 1 155 ? 11.754 -5.870  5.117   0.62 19.40 ?  155 VAL   A HG23 1 
ATOM   3408 H  HG23 B VAL   A 1 155 ? 11.910 -5.899  4.987   0.38 19.05 ?  155 VAL   A HG23 1 
ATOM   3409 N  N    A PHE   A 1 156 ? 11.269 -0.772  5.000   0.62 16.65 ?  156 PHE   A N    1 
ATOM   3410 N  N    B PHE   A 1 156 ? 11.243 -0.806  4.756   0.38 18.11 ?  156 PHE   A N    1 
ATOM   3411 C  CA   A PHE   A 1 156 ? 10.715 0.531   5.364   0.62 17.49 ?  156 PHE   A CA   1 
ATOM   3412 C  CA   B PHE   A 1 156 ? 10.678 0.518   5.053   0.38 19.36 ?  156 PHE   A CA   1 
ATOM   3413 C  C    A PHE   A 1 156 ? 9.258  0.669   4.940   0.62 17.88 ?  156 PHE   A C    1 
ATOM   3414 C  C    B PHE   A 1 156 ? 9.487  0.862   4.157   0.38 20.41 ?  156 PHE   A C    1 
ATOM   3415 O  O    A PHE   A 1 156 ? 8.433  1.200   5.692   0.62 18.21 ?  156 PHE   A O    1 
ATOM   3416 O  O    B PHE   A 1 156 ? 9.426  1.936   3.557   0.38 21.49 ?  156 PHE   A O    1 
ATOM   3417 C  CB   A PHE   A 1 156 ? 11.557 1.626   4.710   0.62 18.27 ?  156 PHE   A CB   1 
ATOM   3418 C  CB   B PHE   A 1 156 ? 11.781 1.565   4.918   0.38 19.98 ?  156 PHE   A CB   1 
ATOM   3419 C  CG   A PHE   A 1 156 ? 11.087 3.015   5.017   0.62 19.75 ?  156 PHE   A CG   1 
ATOM   3420 C  CG   B PHE   A 1 156 ? 11.412 2.941   5.423   0.38 20.52 ?  156 PHE   A CG   1 
ATOM   3421 C  CD1  A PHE   A 1 156 ? 11.079 3.474   6.323   0.62 21.21 ?  156 PHE   A CD1  1 
ATOM   3422 C  CD1  B PHE   A 1 156 ? 10.450 3.122   6.403   0.38 20.67 ?  156 PHE   A CD1  1 
ATOM   3423 C  CD2  A PHE   A 1 156 ? 10.665 3.864   4.005   0.62 20.66 ?  156 PHE   A CD2  1 
ATOM   3424 C  CD2  B PHE   A 1 156 ? 12.053 4.059   4.912   0.38 20.79 ?  156 PHE   A CD2  1 
ATOM   3425 C  CE1  A PHE   A 1 156 ? 10.649 4.749   6.619   0.62 22.14 ?  156 PHE   A CE1  1 
ATOM   3426 C  CE1  B PHE   A 1 156 ? 10.131 4.396   6.858   0.38 21.05 ?  156 PHE   A CE1  1 
ATOM   3427 C  CE2  A PHE   A 1 156 ? 10.234 5.146   4.294   0.62 21.68 ?  156 PHE   A CE2  1 
ATOM   3428 C  CE2  B PHE   A 1 156 ? 11.741 5.330   5.362   0.38 20.84 ?  156 PHE   A CE2  1 
ATOM   3429 C  CZ   A PHE   A 1 156 ? 10.235 5.591   5.602   0.62 22.30 ?  156 PHE   A CZ   1 
ATOM   3430 C  CZ   B PHE   A 1 156 ? 10.779 5.501   6.334   0.38 21.08 ?  156 PHE   A CZ   1 
ATOM   3431 H  H    A PHE   A 1 156 ? 11.886 -0.743  4.397   0.62 20.00 ?  156 PHE   A H    1 
ATOM   3432 H  H    B PHE   A 1 156 ? 11.896 -0.776  4.199   0.38 21.75 ?  156 PHE   A H    1 
ATOM   3433 H  HA   A PHE   A 1 156 ? 10.774 0.649   6.327   0.62 21.01 ?  156 PHE   A HA   1 
ATOM   3434 H  HA   B PHE   A 1 156 ? 10.373 0.516   5.972   0.38 23.26 ?  156 PHE   A HA   1 
ATOM   3435 H  HB2  A PHE   A 1 156 ? 12.477 1.550   5.020   0.62 21.94 ?  156 PHE   A HB2  1 
ATOM   3436 H  HB2  B PHE   A 1 156 ? 12.546 1.273   5.433   0.38 24.00 ?  156 PHE   A HB2  1 
ATOM   3437 H  HB3  A PHE   A 1 156 ? 11.529 1.509   3.747   0.62 21.94 ?  156 PHE   A HB3  1 
ATOM   3438 H  HB3  B PHE   A 1 156 ? 12.028 1.650   3.982   0.38 24.00 ?  156 PHE   A HB3  1 
ATOM   3439 H  HD1  A PHE   A 1 156 ? 11.364 2.909   7.008   0.62 25.48 ?  156 PHE   A HD1  1 
ATOM   3440 H  HD1  B PHE   A 1 156 ? 10.013 2.383   6.761   0.38 24.83 ?  156 PHE   A HD1  1 
ATOM   3441 H  HD2  A PHE   A 1 156 ? 10.669 3.564   3.122   0.62 24.81 ?  156 PHE   A HD2  1 
ATOM   3442 H  HD2  B PHE   A 1 156 ? 12.703 3.955   4.255   0.38 24.97 ?  156 PHE   A HD2  1 
ATOM   3443 H  HE1  A PHE   A 1 156 ? 10.649 5.045   7.501   0.62 26.59 ?  156 PHE   A HE1  1 
ATOM   3444 H  HE1  B PHE   A 1 156 ? 9.482  4.504   7.517   0.38 25.28 ?  156 PHE   A HE1  1 
ATOM   3445 H  HE2  A PHE   A 1 156 ? 9.952  5.706   3.611   0.62 26.03 ?  156 PHE   A HE2  1 
ATOM   3446 H  HE2  B PHE   A 1 156 ? 12.177 6.072   5.006   0.38 25.03 ?  156 PHE   A HE2  1 
ATOM   3447 H  HZ   A PHE   A 1 156 ? 9.941  6.447   5.802   0.62 26.78 ?  156 PHE   A HZ   1 
ATOM   3448 H  HZ   B PHE   A 1 156 ? 10.566 6.353   6.637   0.38 25.32 ?  156 PHE   A HZ   1 
ATOM   3449 N  N    A ASP   A 1 157 ? 8.935  0.240   3.726   0.62 18.43 ?  157 ASP   A N    1 
ATOM   3450 N  N    B ASP   A 1 157 ? 8.515  -0.043  4.072   0.38 20.47 ?  157 ASP   A N    1 
ATOM   3451 C  CA   A ASP   A 1 157 ? 7.616  0.480   3.156   0.62 20.26 ?  157 ASP   A CA   1 
ATOM   3452 C  CA   B ASP   A 1 157 ? 7.344  0.173   3.232   0.38 20.55 ?  157 ASP   A CA   1 
ATOM   3453 C  C    A ASP   A 1 157 ? 6.635  -0.564  3.684   0.62 20.09 ?  157 ASP   A C    1 
ATOM   3454 C  C    B ASP   A 1 157 ? 6.285  -0.874  3.552   0.38 20.49 ?  157 ASP   A C    1 
ATOM   3455 O  O    A ASP   A 1 157 ? 6.811  -1.766  3.445   0.62 19.47 ?  157 ASP   A O    1 
ATOM   3456 O  O    B ASP   A 1 157 ? 6.488  -2.067  3.306   0.38 20.36 ?  157 ASP   A O    1 
ATOM   3457 C  CB   A ASP   A 1 157 ? 7.716  0.400   1.637   0.62 22.27 ?  157 ASP   A CB   1 
ATOM   3458 C  CB   B ASP   A 1 157 ? 7.740  0.118   1.755   0.38 20.54 ?  157 ASP   A CB   1 
ATOM   3459 C  CG   A ASP   A 1 157 ? 6.467  0.896   0.942   0.62 24.48 ?  157 ASP   A CG   1 
ATOM   3460 C  CG   B ASP   A 1 157 ? 6.670  0.685   0.843   0.38 20.99 ?  157 ASP   A CG   1 
ATOM   3461 O  OD1  A ASP   A 1 157 ? 6.204  2.115   0.980   0.62 26.00 ?  157 ASP   A OD1  1 
ATOM   3462 O  OD1  B ASP   A 1 157 ? 5.567  0.108   0.800   0.38 21.04 ?  157 ASP   A OD1  1 
ATOM   3463 O  OD2  A ASP   A 1 157 ? 5.746  0.063   0.354   0.62 24.36 -1 157 ASP   A OD2  1 
ATOM   3464 O  OD2  B ASP   A 1 157 ? 6.920  1.722   0.187   0.38 20.51 -1 157 ASP   A OD2  1 
ATOM   3465 H  H    A ASP   A 1 157 ? 9.480  -0.176  3.203   0.62 22.13 ?  157 ASP   A H    1 
ATOM   3466 H  H    B ASP   A 1 157 ? 8.508  -0.792  4.494   0.38 24.58 ?  157 ASP   A H    1 
ATOM   3467 H  HA   A ASP   A 1 157 ? 7.311  1.370   3.407   0.62 24.33 ?  157 ASP   A HA   1 
ATOM   3468 H  HA   B ASP   A 1 157 ? 6.974  1.053   3.410   0.38 24.68 ?  157 ASP   A HA   1 
ATOM   3469 H  HB2  A ASP   A 1 157 ? 8.490  0.914   1.343   0.62 26.74 ?  157 ASP   A HB2  1 
ATOM   3470 H  HB2  B ASP   A 1 157 ? 8.531  0.654   1.638   0.38 24.67 ?  157 ASP   A HB2  1 
ATOM   3471 H  HB3  A ASP   A 1 157 ? 7.824  -0.524  1.381   0.62 26.74 ?  157 ASP   A HB3  1 
ATOM   3472 H  HB3  B ASP   A 1 157 ? 7.921  -0.805  1.496   0.38 24.67 ?  157 ASP   A HB3  1 
ATOM   3473 N  N    A LYS   A 1 158 ? 5.603  -0.109  4.403   0.62 21.38 ?  158 LYS   A N    1 
ATOM   3474 N  N    B LYS   A 1 158 ? 5.152  -0.429  4.103   0.38 20.77 ?  158 LYS   A N    1 
ATOM   3475 C  CA   A LYS   A 1 158 ? 4.643  -1.049  4.975   0.62 22.08 ?  158 LYS   A CA   1 
ATOM   3476 C  CA   B LYS   A 1 158 ? 4.145  -1.357  4.613   0.38 21.26 ?  158 LYS   A CA   1 
ATOM   3477 C  C    A LYS   A 1 158 ? 3.902  -1.808  3.883   0.62 21.65 ?  158 LYS   A C    1 
ATOM   3478 C  C    B LYS   A 1 158 ? 3.597  -2.251  3.505   0.38 20.39 ?  158 LYS   A C    1 
ATOM   3479 O  O    A LYS   A 1 158 ? 3.682  -3.018  4.000   0.62 21.52 ?  158 LYS   A O    1 
ATOM   3480 O  O    B LYS   A 1 158 ? 3.548  -3.479  3.646   0.38 20.11 ?  158 LYS   A O    1 
ATOM   3481 C  CB   A LYS   A 1 158 ? 3.667  -0.321  5.904   0.62 23.51 ?  158 LYS   A CB   1 
ATOM   3482 C  CB   B LYS   A 1 158 ? 3.020  -0.570  5.298   0.38 22.72 ?  158 LYS   A CB   1 
ATOM   3483 C  CG   A LYS   A 1 158 ? 2.432  -1.138  6.312   0.62 24.77 ?  158 LYS   A CG   1 
ATOM   3484 C  CG   B LYS   A 1 158 ? 1.729  -1.355  5.501   0.38 24.43 ?  158 LYS   A CG   1 
ATOM   3485 C  CD   A LYS   A 1 158 ? 2.774  -2.425  7.079   0.62 25.59 ?  158 LYS   A CD   1 
ATOM   3486 C  CD   B LYS   A 1 158 ? 0.781  -0.679  6.492   0.38 25.85 ?  158 LYS   A CD   1 
ATOM   3487 C  CE   A LYS   A 1 158 ? 1.500  -3.113  7.588   0.62 25.54 ?  158 LYS   A CE   1 
ATOM   3488 C  CE   B LYS   A 1 158 ? 0.237  0.647   5.975   0.38 26.87 ?  158 LYS   A CE   1 
ATOM   3489 N  NZ   A LYS   A 1 158 ? 1.738  -4.458  8.197   0.62 25.51 ?  158 LYS   A NZ   1 
ATOM   3490 N  NZ   B LYS   A 1 158 ? -0.898 1.138   6.813   0.38 27.43 ?  158 LYS   A NZ   1 
ATOM   3491 H  H    A LYS   A 1 158 ? 5.449  0.720   4.569   0.62 25.67 ?  158 LYS   A H    1 
ATOM   3492 H  H    B LYS   A 1 158 ? 4.948  0.399   4.194   0.38 24.94 ?  158 LYS   A H    1 
ATOM   3493 H  HA   A LYS   A 1 158 ? 5.128  -1.697  5.510   0.62 26.52 ?  158 LYS   A HA   1 
ATOM   3494 H  HA   B LYS   A 1 158 ? 4.554  -1.929  5.280   0.38 25.53 ?  158 LYS   A HA   1 
ATOM   3495 H  HB2  A LYS   A 1 158 ? 4.140  -0.077  6.718   0.62 28.24 ?  158 LYS   A HB2  1 
ATOM   3496 H  HB2  B LYS   A 1 158 ? 3.330  -0.285  6.174   0.38 27.29 ?  158 LYS   A HB2  1 
ATOM   3497 H  HB3  A LYS   A 1 158 ? 3.357  0.482   5.458   0.62 28.24 ?  158 LYS   A HB3  1 
ATOM   3498 H  HB3  B LYS   A 1 158 ? 2.811  0.207   4.759   0.38 27.29 ?  158 LYS   A HB3  1 
ATOM   3499 H  HG2  A LYS   A 1 158 ? 1.879  -0.591  6.889   0.62 29.74 ?  158 LYS   A HG2  1 
ATOM   3500 H  HG2  B LYS   A 1 158 ? 1.266  -1.429  4.652   0.38 29.33 ?  158 LYS   A HG2  1 
ATOM   3501 H  HG3  A LYS   A 1 158 ? 1.930  -1.383  5.518   0.62 29.74 ?  158 LYS   A HG3  1 
ATOM   3502 H  HG3  B LYS   A 1 158 ? 1.942  -2.236  5.843   0.38 29.33 ?  158 LYS   A HG3  1 
ATOM   3503 H  HD2  A LYS   A 1 158 ? 3.239  -3.039  6.489   0.62 30.73 ?  158 LYS   A HD2  1 
ATOM   3504 H  HD2  B LYS   A 1 158 ? 0.027  -1.265  6.662   0.38 31.04 ?  158 LYS   A HD2  1 
ATOM   3505 H  HD3  A LYS   A 1 158 ? 3.331  -2.204  7.843   0.62 30.73 ?  158 LYS   A HD3  1 
ATOM   3506 H  HD3  B LYS   A 1 158 ? 1.258  -0.504  7.319   0.38 31.04 ?  158 LYS   A HD3  1 
ATOM   3507 H  HE2  A LYS   A 1 158 ? 1.085  -2.550  8.260   0.62 30.67 ?  158 LYS   A HE2  1 
ATOM   3508 H  HE2  B LYS   A 1 158 ? 0.941  1.316   6.000   0.38 32.26 ?  158 LYS   A HE2  1 
ATOM   3509 H  HE3  A LYS   A 1 158 ? 0.894  -3.230  6.843   0.62 30.67 ?  158 LYS   A HE3  1 
ATOM   3510 H  HE3  B LYS   A 1 158 ? -0.085 0.533   5.068   0.38 32.26 ?  158 LYS   A HE3  1 
ATOM   3511 H  HZ1  A LYS   A 1 158 ? 0.967  -4.808  8.474   0.62 30.64 ?  158 LYS   A HZ1  1 
ATOM   3512 H  HZ1  B LYS   A 1 158 ? -1.202 1.913   6.496   0.38 32.93 ?  158 LYS   A HZ1  1 
ATOM   3513 H  HZ2  A LYS   A 1 158 ? 2.102  -5.005  7.595   0.62 30.64 ?  158 LYS   A HZ2  1 
ATOM   3514 H  HZ2  B LYS   A 1 158 ? -1.562 0.545   6.806   0.38 32.93 ?  158 LYS   A HZ2  1 
ATOM   3515 H  HZ3  A LYS   A 1 158 ? 2.289  -4.388  8.892   0.62 30.64 ?  158 LYS   A HZ3  1 
ATOM   3516 H  HZ3  B LYS   A 1 158 ? -0.629 1.258   7.654   0.38 32.93 ?  158 LYS   A HZ3  1 
ATOM   3517 N  N    A ASN   A 1 159 ? 3.518  -1.122  2.805   0.62 21.70 ?  159 ASN   A N    1 
ATOM   3518 N  N    B ASN   A 1 159 ? 3.178  -1.652  2.389   0.38 20.50 ?  159 ASN   A N    1 
ATOM   3519 C  CA   A ASN   A 1 159 ? 2.858  -1.820  1.707   0.62 21.75 ?  159 ASN   A CA   1 
ATOM   3520 C  CA   B ASN   A 1 159 ? 2.552  -2.435  1.329   0.38 20.56 ?  159 ASN   A CA   1 
ATOM   3521 C  C    A ASN   A 1 159 ? 3.765  -2.898  1.117   0.62 20.71 ?  159 ASN   A C    1 
ATOM   3522 C  C    B ASN   A 1 159 ? 3.535  -3.427  0.710   0.38 18.66 ?  159 ASN   A C    1 
ATOM   3523 O  O    A ASN   A 1 159 ? 3.315  -4.016  0.842   0.62 19.77 ?  159 ASN   A O    1 
ATOM   3524 O  O    B ASN   A 1 159 ? 3.162  -4.563  0.394   0.38 18.49 ?  159 ASN   A O    1 
ATOM   3525 C  CB   A ASN   A 1 159 ? 2.397  -0.817  0.646   0.62 23.65 ?  159 ASN   A CB   1 
ATOM   3526 C  CB   B ASN   A 1 159 ? 1.934  -1.497  0.289   0.38 23.34 ?  159 ASN   A CB   1 
ATOM   3527 C  CG   A ASN   A 1 159 ? 1.157  -0.037  1.074   0.62 26.58 ?  159 ASN   A CG   1 
ATOM   3528 C  CG   B ASN   A 1 159 ? 0.925  -0.537  0.903   0.38 26.21 ?  159 ASN   A CG   1 
ATOM   3529 O  OD1  A ASN   A 1 159 ? 0.301  -0.557  1.788   0.62 28.27 ?  159 ASN   A OD1  1 
ATOM   3530 O  OD1  B ASN   A 1 159 ? 0.119  -0.930  1.747   0.38 27.34 ?  159 ASN   A OD1  1 
ATOM   3531 N  ND2  A ASN   A 1 159 ? 1.053  1.209   0.633   0.62 27.77 ?  159 ASN   A ND2  1 
ATOM   3532 N  ND2  B ASN   A 1 159 ? 0.977  0.730   0.492   0.38 27.32 ?  159 ASN   A ND2  1 
ATOM   3533 H  H    A ASN   A 1 159 ? 3.630  -0.276  2.690   0.62 26.07 ?  159 ASN   A H    1 
ATOM   3534 H  H    B ASN   A 1 159 ? 3.245  -0.812  2.228   0.38 24.62 ?  159 ASN   A H    1 
ATOM   3535 H  HA   A ASN   A 1 159 ? 2.068  -2.258  2.058   0.62 26.12 ?  159 ASN   A HA   1 
ATOM   3536 H  HA   B ASN   A 1 159 ? 1.830  -2.950  1.714   0.38 24.70 ?  159 ASN   A HA   1 
ATOM   3537 H  HB2  A ASN   A 1 159 ? 3.102  -0.177  0.482   0.62 28.40 ?  159 ASN   A HB2  1 
ATOM   3538 H  HB2  B ASN   A 1 159 ? 2.632  -0.969  -0.125  0.38 28.02 ?  159 ASN   A HB2  1 
ATOM   3539 H  HB3  A ASN   A 1 159 ? 2.185  -1.299  -0.170  0.62 28.40 ?  159 ASN   A HB3  1 
ATOM   3540 H  HB3  B ASN   A 1 159 ? 1.467  -2.021  -0.378  0.38 28.02 ?  159 ASN   A HB3  1 
ATOM   3541 H  HD21 A ASN   A 1 159 ? 0.367  1.678   0.846   0.62 33.35 ?  159 ASN   A HD21 1 
ATOM   3542 H  HD21 B ASN   A 1 159 ? 0.432  1.318   0.815   0.38 32.81 ?  159 ASN   A HD21 1 
ATOM   3543 H  HD22 A ASN   A 1 159 ? 1.669  1.540   0.140   0.62 33.35 ?  159 ASN   A HD22 1 
ATOM   3544 H  HD22 B ASN   A 1 159 ? 1.556  0.967   -0.098  0.38 32.81 ?  159 ASN   A HD22 1 
ATOM   3545 N  N    A LEU   A 1 160 ? 5.052  -2.597  0.944   0.62 19.90 ?  160 LEU   A N    1 
ATOM   3546 N  N    B LEU   A 1 160 ? 4.800  -3.031  0.555   0.38 17.59 ?  160 LEU   A N    1 
ATOM   3547 C  CA   A LEU   A 1 160 ? 5.965  -3.615  0.433   0.62 19.27 ?  160 LEU   A CA   1 
ATOM   3548 C  CA   B LEU   A 1 160 ? 5.801  -3.966  0.054   0.38 16.77 ?  160 LEU   A CA   1 
ATOM   3549 C  C    A LEU   A 1 160 ? 6.128  -4.756  1.428   0.62 18.60 ?  160 LEU   A C    1 
ATOM   3550 C  C    B LEU   A 1 160 ? 6.055  -5.084  1.060   0.38 16.39 ?  160 LEU   A C    1 
ATOM   3551 O  O    A LEU   A 1 160 ? 6.156  -5.929  1.038   0.62 19.08 ?  160 LEU   A O    1 
ATOM   3552 O  O    B LEU   A 1 160 ? 6.105  -6.266  0.696   0.38 16.64 ?  160 LEU   A O    1 
ATOM   3553 C  CB   A LEU   A 1 160 ? 7.320  -2.999  0.101   0.62 19.31 ?  160 LEU   A CB   1 
ATOM   3554 C  CB   B LEU   A 1 160 ? 7.094  -3.217  -0.250  0.38 16.85 ?  160 LEU   A CB   1 
ATOM   3555 C  CG   A LEU   A 1 160 ? 8.376  -4.034  -0.290  0.62 19.95 ?  160 LEU   A CG   1 
ATOM   3556 C  CG   B LEU   A 1 160 ? 8.234  -4.103  -0.729  0.38 17.96 ?  160 LEU   A CG   1 
ATOM   3557 C  CD1  A LEU   A 1 160 ? 7.946  -4.785  -1.532  0.62 20.72 ?  160 LEU   A CD1  1 
ATOM   3558 C  CD1  B LEU   A 1 160 ? 7.757  -4.928  -1.903  0.38 18.91 ?  160 LEU   A CD1  1 
ATOM   3559 C  CD2  A LEU   A 1 160 ? 9.717  -3.371  -0.505  0.62 19.33 ?  160 LEU   A CD2  1 
ATOM   3560 C  CD2  B LEU   A 1 160 ? 9.419  -3.238  -1.107  0.38 17.88 ?  160 LEU   A CD2  1 
ATOM   3561 H  H    A LEU   A 1 160 ? 5.409  -1.834  1.118   0.62 23.90 ?  160 LEU   A H    1 
ATOM   3562 H  H    B LEU   A 1 160 ? 5.100  -2.245  0.729   0.38 21.13 ?  160 LEU   A H    1 
ATOM   3563 H  HA   A LEU   A 1 160 ? 5.593  -3.976  -0.383  0.62 23.14 ?  160 LEU   A HA   1 
ATOM   3564 H  HA   B LEU   A 1 160 ? 5.471  -4.359  -0.770  0.38 20.14 ?  160 LEU   A HA   1 
ATOM   3565 H  HB2  A LEU   A 1 160 ? 7.217  -2.373  -0.639  0.62 23.20 ?  160 LEU   A HB2  1 
ATOM   3566 H  HB2  B LEU   A 1 160 ? 6.922  -2.560  -0.945  0.38 20.24 ?  160 LEU   A HB2  1 
ATOM   3567 H  HB3  A LEU   A 1 160 ? 7.648  -2.533  0.884   0.62 23.20 ?  160 LEU   A HB3  1 
ATOM   3568 H  HB3  B LEU   A 1 160 ? 7.391  -2.768  0.557   0.38 20.24 ?  160 LEU   A HB3  1 
ATOM   3569 H  HG   A LEU   A 1 160 ? 8.482  -4.676  0.428   0.62 23.96 ?  160 LEU   A HG   1 
ATOM   3570 H  HG   B LEU   A 1 160 ? 8.507  -4.703  -0.015  0.38 21.57 ?  160 LEU   A HG   1 
ATOM   3571 H  HD11 A LEU   A 1 160 ? 8.680  -5.340  -1.832  0.62 24.89 ?  160 LEU   A HD11 1 
ATOM   3572 H  HD11 B LEU   A 1 160 ? 8.505  -5.416  -2.259  0.38 22.71 ?  160 LEU   A HD11 1 
ATOM   3573 H  HD12 A LEU   A 1 160 ? 7.177  -5.339  -1.320  0.62 24.89 ?  160 LEU   A HD12 1 
ATOM   3574 H  HD12 B LEU   A 1 160 ? 7.079  -5.553  -1.602  0.38 22.71 ?  160 LEU   A HD12 1 
ATOM   3575 H  HD13 A LEU   A 1 160 ? 7.711  -4.144  -2.222  0.62 24.89 ?  160 LEU   A HD13 1 
ATOM   3576 H  HD13 B LEU   A 1 160 ? 7.387  -4.333  -2.575  0.38 22.71 ?  160 LEU   A HD13 1 
ATOM   3577 H  HD21 A LEU   A 1 160 ? 10.367 -4.050  -0.748  0.62 23.22 ?  160 LEU   A HD21 1 
ATOM   3578 H  HD21 B LEU   A 1 160 ? 10.147 -3.806  -1.398  0.38 21.48 ?  160 LEU   A HD21 1 
ATOM   3579 H  HD22 A LEU   A 1 160 ? 9.637  -2.721  -1.221  0.62 23.22 ?  160 LEU   A HD22 1 
ATOM   3580 H  HD22 B LEU   A 1 160 ? 9.156  -2.640  -1.825  0.38 21.48 ?  160 LEU   A HD22 1 
ATOM   3581 H  HD23 A LEU   A 1 160 ? 9.988  -2.931  0.315   0.62 23.22 ?  160 LEU   A HD23 1 
ATOM   3582 H  HD23 B LEU   A 1 160 ? 9.693  -2.720  -0.332  0.38 21.48 ?  160 LEU   A HD23 1 
ATOM   3583 N  N    A TYR   A 1 161 ? 6.239  -4.432  2.717   0.62 18.18 ?  161 TYR   A N    1 
ATOM   3584 N  N    B TYR   A 1 161 ? 6.228  -4.721  2.332   0.38 16.30 ?  161 TYR   A N    1 
ATOM   3585 C  CA   A TYR   A 1 161 ? 6.365  -5.473  3.730   0.62 17.84 ?  161 TYR   A CA   1 
ATOM   3586 C  CA   B TYR   A 1 161 ? 6.359  -5.714  3.392   0.38 16.69 ?  161 TYR   A CA   1 
ATOM   3587 C  C    A TYR   A 1 161 ? 5.232  -6.490  3.628   0.62 18.61 ?  161 TYR   A C    1 
ATOM   3588 C  C    B TYR   A 1 161 ? 5.194  -6.696  3.366   0.38 17.17 ?  161 TYR   A C    1 
ATOM   3589 O  O    A TYR   A 1 161 ? 5.460  -7.704  3.676   0.62 18.05 ?  161 TYR   A O    1 
ATOM   3590 O  O    B TYR   A 1 161 ? 5.392  -7.914  3.319   0.38 16.30 ?  161 TYR   A O    1 
ATOM   3591 C  CB   A TYR   A 1 161 ? 6.411  -4.857  5.129   0.62 18.27 ?  161 TYR   A CB   1 
ATOM   3592 C  CB   B TYR   A 1 161 ? 6.442  -5.007  4.748   0.38 16.88 ?  161 TYR   A CB   1 
ATOM   3593 C  CG   A TYR   A 1 161 ? 6.320  -5.907  6.205   0.62 18.16 ?  161 TYR   A CG   1 
ATOM   3594 C  CG   B TYR   A 1 161 ? 6.319  -5.932  5.940   0.38 17.63 ?  161 TYR   A CG   1 
ATOM   3595 C  CD1  A TYR   A 1 161 ? 7.448  -6.594  6.624   0.62 17.72 ?  161 TYR   A CD1  1 
ATOM   3596 C  CD1  B TYR   A 1 161 ? 7.431  -6.582  6.456   0.38 17.89 ?  161 TYR   A CD1  1 
ATOM   3597 C  CD2  A TYR   A 1 161 ? 5.100  -6.234  6.782   0.62 18.39 ?  161 TYR   A CD2  1 
ATOM   3598 C  CD2  B TYR   A 1 161 ? 5.092  -6.144  6.561   0.38 18.22 ?  161 TYR   A CD2  1 
ATOM   3599 C  CE1  A TYR   A 1 161 ? 7.367  -7.574  7.591   0.62 18.12 ?  161 TYR   A CE1  1 
ATOM   3600 C  CE1  B TYR   A 1 161 ? 7.326  -7.428  7.544   0.38 18.38 ?  161 TYR   A CE1  1 
ATOM   3601 C  CE2  A TYR   A 1 161 ? 5.008  -7.212  7.752   0.62 18.27 ?  161 TYR   A CE2  1 
ATOM   3602 C  CE2  B TYR   A 1 161 ? 4.977  -6.991  7.654   0.38 18.54 ?  161 TYR   A CE2  1 
ATOM   3603 C  CZ   A TYR   A 1 161 ? 6.145  -7.878  8.154   0.62 18.22 ?  161 TYR   A CZ   1 
ATOM   3604 C  CZ   B TYR   A 1 161 ? 6.099  -7.629  8.140   0.38 18.92 ?  161 TYR   A CZ   1 
ATOM   3605 O  OH   A TYR   A 1 161 ? 6.066  -8.853  9.121   0.62 18.33 ?  161 TYR   A OH   1 
ATOM   3606 O  OH   B TYR   A 1 161 ? 6.003  -8.472  9.225   0.38 19.93 ?  161 TYR   A OH   1 
ATOM   3607 H  H    A TYR   A 1 161 ? 6.236  -3.628  3.025   0.62 21.84 ?  161 TYR   A H    1 
ATOM   3608 H  H    B TYR   A 1 161 ? 6.266  -3.913  2.602   0.38 19.58 ?  161 TYR   A H    1 
ATOM   3609 H  HA   A TYR   A 1 161 ? 7.191  -5.948  3.588   0.62 21.43 ?  161 TYR   A HA   1 
ATOM   3610 H  HA   B TYR   A 1 161 ? 7.176  -6.219  3.263   0.38 20.04 ?  161 TYR   A HA   1 
ATOM   3611 H  HB2  A TYR   A 1 161 ? 7.246  -4.379  5.238   0.62 21.94 ?  161 TYR   A HB2  1 
ATOM   3612 H  HB2  B TYR   A 1 161 ? 7.298  -4.556  4.810   0.38 20.28 ?  161 TYR   A HB2  1 
ATOM   3613 H  HB3  A TYR   A 1 161 ? 5.661  -4.246  5.236   0.62 21.94 ?  161 TYR   A HB3  1 
ATOM   3614 H  HB3  B TYR   A 1 161 ? 5.724  -4.355  4.804   0.38 20.28 ?  161 TYR   A HB3  1 
ATOM   3615 H  HD1  A TYR   A 1 161 ? 8.273  -6.393  6.245   0.62 21.28 ?  161 TYR   A HD1  1 
ATOM   3616 H  HD1  B TYR   A 1 161 ? 8.260  -6.451  6.059   0.38 21.49 ?  161 TYR   A HD1  1 
ATOM   3617 H  HD2  A TYR   A 1 161 ? 4.327  -5.789  6.512   0.62 22.09 ?  161 TYR   A HD2  1 
ATOM   3618 H  HD2  B TYR   A 1 161 ? 4.332  -5.716  6.237   0.38 21.88 ?  161 TYR   A HD2  1 
ATOM   3619 H  HE1  A TYR   A 1 161 ? 8.132  -8.024  7.866   0.62 21.76 ?  161 TYR   A HE1  1 
ATOM   3620 H  HE1  B TYR   A 1 161 ? 8.079  -7.859  7.878   0.38 22.07 ?  161 TYR   A HE1  1 
ATOM   3621 H  HE2  A TYR   A 1 161 ? 4.181  -7.418  8.131   0.62 21.95 ?  161 TYR   A HE2  1 
ATOM   3622 H  HE2  B TYR   A 1 161 ? 4.146  -7.125  8.057   0.38 22.27 ?  161 TYR   A HE2  1 
ATOM   3623 H  HH   A TYR   A 1 161 ? 5.263  -8.938  9.373   0.62 22.01 ?  161 TYR   A HH   1 
ATOM   3624 H  HH   B TYR   A 1 161 ? 6.755  -8.793  9.416   0.38 23.93 ?  161 TYR   A HH   1 
ATOM   3625 N  N    A ASP   A 1 162 ? 3.992  -6.012  3.490   0.62 19.75 ?  162 ASP   A N    1 
ATOM   3626 N  N    B ASP   A 1 162 ? 3.962  -6.177  3.391   0.38 18.63 ?  162 ASP   A N    1 
ATOM   3627 C  CA   A ASP   A 1 162 ? 2.855  -6.930  3.451   0.62 20.64 ?  162 ASP   A CA   1 
ATOM   3628 C  CA   B ASP   A 1 162 ? 2.788  -7.044  3.327   0.38 20.24 ?  162 ASP   A CA   1 
ATOM   3629 C  C    A ASP   A 1 162 ? 2.907  -7.818  2.213   0.62 20.35 ?  162 ASP   A C    1 
ATOM   3630 C  C    B ASP   A 1 162 ? 2.814  -7.911  2.076   0.38 20.72 ?  162 ASP   A C    1 
ATOM   3631 O  O    A ASP   A 1 162 ? 2.558  -9.004  2.277   0.62 21.22 ?  162 ASP   A O    1 
ATOM   3632 O  O    B ASP   A 1 162 ? 2.437  -9.088  2.117   0.38 21.11 ?  162 ASP   A O    1 
ATOM   3633 C  CB   A ASP   A 1 162 ? 1.532  -6.158  3.502   0.62 21.98 ?  162 ASP   A CB   1 
ATOM   3634 C  CB   B ASP   A 1 162 ? 1.507  -6.207  3.365   0.38 21.57 ?  162 ASP   A CB   1 
ATOM   3635 C  CG   A ASP   A 1 162 ? 1.220  -5.589  4.876   0.62 23.40 ?  162 ASP   A CG   1 
ATOM   3636 C  CG   B ASP   A 1 162 ? 1.264  -5.562  4.718   0.38 22.81 ?  162 ASP   A CG   1 
ATOM   3637 O  OD1  A ASP   A 1 162 ? 1.942  -5.889  5.846   0.62 24.34 ?  162 ASP   A OD1  1 
ATOM   3638 O  OD1  B ASP   A 1 162 ? 1.710  -6.126  5.739   0.38 23.02 ?  162 ASP   A OD1  1 
ATOM   3639 O  OD2  A ASP   A 1 162 ? 0.222  -4.841  4.981   0.62 23.62 -1 162 ASP   A OD2  1 
ATOM   3640 O  OD2  B ASP   A 1 162 ? 0.610  -4.497  4.758   0.38 23.52 -1 162 ASP   A OD2  1 
ATOM   3641 H  H    A ASP   A 1 162 ? 3.780  -5.177  3.413   0.62 23.72 ?  162 ASP   A H    1 
ATOM   3642 H  H    B ASP   A 1 162 ? 3.782  -5.338  3.446   0.38 22.38 ?  162 ASP   A H    1 
ATOM   3643 H  HA   A ASP   A 1 162 ? 2.887  -7.506  4.226   0.62 24.79 ?  162 ASP   A HA   1 
ATOM   3644 H  HA   B ASP   A 1 162 ? 2.781  -7.630  4.097   0.38 24.31 ?  162 ASP   A HA   1 
ATOM   3645 H  HB2  A ASP   A 1 162 ? 1.559  -5.422  2.876   0.62 26.40 ?  162 ASP   A HB2  1 
ATOM   3646 H  HB2  B ASP   A 1 162 ? 1.563  -5.501  2.702   0.38 25.90 ?  162 ASP   A HB2  1 
ATOM   3647 H  HB3  A ASP   A 1 162 ? 0.799  -6.756  3.287   0.62 26.40 ?  162 ASP   A HB3  1 
ATOM   3648 H  HB3  B ASP   A 1 162 ? 0.744  -6.778  3.176   0.38 25.90 ?  162 ASP   A HB3  1 
ATOM   3649 N  N    A LYS   A 1 163 ? 3.338  -7.266  1.077   0.62 21.01 ?  163 LYS   A N    1 
ATOM   3650 N  N    B LYS   A 1 163 ? 3.250  -7.344  0.950   0.38 21.48 ?  163 LYS   A N    1 
ATOM   3651 C  CA   A LYS   A 1 163 ? 3.421  -8.059  -0.145  0.62 21.57 ?  163 LYS   A CA   1 
ATOM   3652 C  CA   B LYS   A 1 163 ? 3.358  -8.131  -0.272  0.38 22.37 ?  163 LYS   A CA   1 
ATOM   3653 C  C    A LYS   A 1 163 ? 4.523  -9.109  -0.054  0.62 20.86 ?  163 LYS   A C    1 
ATOM   3654 C  C    B LYS   A 1 163 ? 4.442  -9.195  -0.144  0.38 21.14 ?  163 LYS   A C    1 
ATOM   3655 O  O    A LYS   A 1 163 ? 4.378  -10.216 -0.585  0.62 21.54 ?  163 LYS   A O    1 
ATOM   3656 O  O    B LYS   A 1 163 ? 4.233  -10.351 -0.531  0.38 21.76 ?  163 LYS   A O    1 
ATOM   3657 C  CB   A LYS   A 1 163 ? 3.645  -7.138  -1.344  0.62 24.11 ?  163 LYS   A CB   1 
ATOM   3658 C  CB   B LYS   A 1 163 ? 3.623  -7.208  -1.463  0.38 24.82 ?  163 LYS   A CB   1 
ATOM   3659 C  CG   A LYS   A 1 163 ? 3.706  -7.855  -2.680  0.62 27.05 ?  163 LYS   A CG   1 
ATOM   3660 C  CG   B LYS   A 1 163 ? 3.916  -7.944  -2.761  0.38 27.28 ?  163 LYS   A CG   1 
ATOM   3661 C  CD   A LYS   A 1 163 ? 4.052  -6.891  -3.802  0.62 30.21 ?  163 LYS   A CD   1 
ATOM   3662 C  CD   B LYS   A 1 163 ? 4.781  -7.118  -3.693  0.38 29.74 ?  163 LYS   A CD   1 
ATOM   3663 C  CE   A LYS   A 1 163 ? 4.005  -7.579  -5.157  0.62 32.82 ?  163 LYS   A CE   1 
ATOM   3664 C  CE   B LYS   A 1 163 ? 3.966  -6.475  -4.798  0.38 31.58 ?  163 LYS   A CE   1 
ATOM   3665 N  NZ   A LYS   A 1 163 ? 4.658  -6.768  -6.221  0.62 34.17 ?  163 LYS   A NZ   1 
ATOM   3666 N  NZ   B LYS   A 1 163 ? 4.846  -5.921  -5.862  0.38 32.59 ?  163 LYS   A NZ   1 
ATOM   3667 H  H    A LYS   A 1 163 ? 3.585  -6.444  0.991   0.62 25.23 ?  163 LYS   A H    1 
ATOM   3668 H  H    B LYS   A 1 163 ? 3.489  -6.522  0.870   0.38 25.79 ?  163 LYS   A H    1 
ATOM   3669 H  HA   A LYS   A 1 163 ? 2.579  -8.518  -0.275  0.62 25.90 ?  163 LYS   A HA   1 
ATOM   3670 H  HA   B LYS   A 1 163 ? 2.518  -8.583  -0.433  0.38 26.87 ?  163 LYS   A HA   1 
ATOM   3671 H  HB2  A LYS   A 1 163 ? 2.913  -6.500  -1.386  0.62 28.95 ?  163 LYS   A HB2  1 
ATOM   3672 H  HB2  B LYS   A 1 163 ? 2.833  -6.654  -1.614  0.38 29.81 ?  163 LYS   A HB2  1 
ATOM   3673 H  HB3  A LYS   A 1 163 ? 4.482  -6.667  -1.224  0.62 28.95 ?  163 LYS   A HB3  1 
ATOM   3674 H  HB3  B LYS   A 1 163 ? 4.379  -6.640  -1.256  0.38 29.81 ?  163 LYS   A HB3  1 
ATOM   3675 H  HG2  A LYS   A 1 163 ? 4.390  -8.541  -2.650  0.62 32.48 ?  163 LYS   A HG2  1 
ATOM   3676 H  HG2  B LYS   A 1 163 ? 4.383  -8.774  -2.585  0.38 32.76 ?  163 LYS   A HG2  1 
ATOM   3677 H  HG3  A LYS   A 1 163 ? 2.840  -8.250  -2.872  0.62 32.48 ?  163 LYS   A HG3  1 
ATOM   3678 H  HG3  B LYS   A 1 163 ? 3.076  -8.128  -3.207  0.38 32.76 ?  163 LYS   A HG3  1 
ATOM   3679 H  HD2  A LYS   A 1 163 ? 3.409  -6.163  -3.808  0.62 36.27 ?  163 LYS   A HD2  1 
ATOM   3680 H  HD2  B LYS   A 1 163 ? 5.221  -6.413  -3.191  0.38 35.71 ?  163 LYS   A HD2  1 
ATOM   3681 H  HD3  A LYS   A 1 163 ? 4.947  -6.546  -3.663  0.62 36.27 ?  163 LYS   A HD3  1 
ATOM   3682 H  HD3  B LYS   A 1 163 ? 5.443  -7.697  -4.097  0.38 35.71 ?  163 LYS   A HD3  1 
ATOM   3683 H  HE2  A LYS   A 1 163 ? 4.460  -8.432  -5.101  0.62 39.40 ?  163 LYS   A HE2  1 
ATOM   3684 H  HE2  B LYS   A 1 163 ? 3.386  -7.143  -5.198  0.38 37.92 ?  163 LYS   A HE2  1 
ATOM   3685 H  HE3  A LYS   A 1 163 ? 3.080  -7.715  -5.408  0.62 39.40 ?  163 LYS   A HE3  1 
ATOM   3686 H  HE3  B LYS   A 1 163 ? 3.438  -5.751  -4.427  0.38 37.92 ?  163 LYS   A HE3  1 
ATOM   3687 H  HZ1  A LYS   A 1 163 ? 4.616  -7.198  -6.999  0.62 41.03 ?  163 LYS   A HZ1  1 
ATOM   3688 H  HZ1  B LYS   A 1 163 ? 4.352  -5.550  -6.502  0.38 39.13 ?  163 LYS   A HZ1  1 
ATOM   3689 H  HZ2  A LYS   A 1 163 ? 4.245  -5.984  -6.301  0.62 41.03 ?  163 LYS   A HZ2  1 
ATOM   3690 H  HZ2  B LYS   A 1 163 ? 5.387  -5.304  -5.518  0.38 39.13 ?  163 LYS   A HZ2  1 
ATOM   3691 H  HZ3  A LYS   A 1 163 ? 5.512  -6.625  -6.015  0.62 41.03 ?  163 LYS   A HZ3  1 
ATOM   3692 H  HZ3  B LYS   A 1 163 ? 5.339  -6.572  -6.218  0.38 39.13 ?  163 LYS   A HZ3  1 
ATOM   3693 N  N    A LEU   A 1 164 ? 5.636  -8.775  0.603   0.62 19.29 ?  164 LEU   A N    1 
ATOM   3694 N  N    B LEU   A 1 164 ? 5.605  -8.826  0.398   0.38 19.40 ?  164 LEU   A N    1 
ATOM   3695 C  CA   A LEU   A 1 164 ? 6.735  -9.728  0.751   0.62 18.37 ?  164 LEU   A CA   1 
ATOM   3696 C  CA   B LEU   A 1 164 ? 6.676  -9.802  0.576   0.38 18.48 ?  164 LEU   A CA   1 
ATOM   3697 C  C    A LEU   A 1 164 ? 6.304  -10.941 1.566   0.62 18.80 ?  164 LEU   A C    1 
ATOM   3698 C  C    B LEU   A 1 164 ? 6.244  -10.916 1.519   0.38 18.62 ?  164 LEU   A C    1 
ATOM   3699 O  O    A LEU   A 1 164 ? 6.615  -12.084 1.209   0.62 19.43 ?  164 LEU   A O    1 
ATOM   3700 O  O    B LEU   A 1 164 ? 6.539  -12.093 1.281   0.38 18.90 ?  164 LEU   A O    1 
ATOM   3701 C  CB   A LEU   A 1 164 ? 7.926  -9.037  1.416   0.62 17.77 ?  164 LEU   A CB   1 
ATOM   3702 C  CB   B LEU   A 1 164 ? 7.927  -9.110  1.115   0.38 17.71 ?  164 LEU   A CB   1 
ATOM   3703 C  CG   A LEU   A 1 164 ? 8.706  -8.041  0.556   0.62 17.59 ?  164 LEU   A CG   1 
ATOM   3704 C  CG   B LEU   A 1 164 ? 8.639  -8.155  0.159   0.38 16.96 ?  164 LEU   A CG   1 
ATOM   3705 C  CD1  A LEU   A 1 164 ? 9.631  -7.182  1.412   0.62 17.28 ?  164 LEU   A CD1  1 
ATOM   3706 C  CD1  B LEU   A 1 164 ? 9.563  -7.227  0.931   0.38 16.35 ?  164 LEU   A CD1  1 
ATOM   3707 C  CD2  A LEU   A 1 164 ? 9.502  -8.784  -0.504  0.62 17.85 ?  164 LEU   A CD2  1 
ATOM   3708 C  CD2  B LEU   A 1 164 ? 9.417  -8.937  -0.882  0.38 17.65 ?  164 LEU   A CD2  1 
ATOM   3709 H  H    A LEU   A 1 164 ? 5.782  -8.008  0.967   0.62 23.17 ?  164 LEU   A H    1 
ATOM   3710 H  H    B LEU   A 1 164 ? 5.792  -8.032  0.678   0.38 23.30 ?  164 LEU   A H    1 
ATOM   3711 H  HA   A LEU   A 1 164 ? 7.012  -10.038 -0.122  0.62 22.06 ?  164 LEU   A HA   1 
ATOM   3712 H  HA   B LEU   A 1 164 ? 6.896  -10.196 -0.282  0.38 22.20 ?  164 LEU   A HA   1 
ATOM   3713 H  HB2  A LEU   A 1 164 ? 7.605  -8.554  2.192   0.62 21.34 ?  164 LEU   A HB2  1 
ATOM   3714 H  HB2  B LEU   A 1 164 ? 7.679  -8.599  1.900   0.38 21.27 ?  164 LEU   A HB2  1 
ATOM   3715 H  HB3  A LEU   A 1 164 ? 8.556  -9.719  1.701   0.62 21.34 ?  164 LEU   A HB3  1 
ATOM   3716 H  HB3  B LEU   A 1 164 ? 8.569  -9.794  1.366   0.38 21.27 ?  164 LEU   A HB3  1 
ATOM   3717 H  HG   A LEU   A 1 164 ? 8.082  -7.449  0.109   0.62 21.13 ?  164 LEU   A HG   1 
ATOM   3718 H  HG   B LEU   A 1 164 ? 7.981  -7.612  -0.299  0.38 20.38 ?  164 LEU   A HG   1 
ATOM   3719 H  HD11 A LEU   A 1 164 ? 10.110 -6.562  0.840   0.62 20.75 ?  164 LEU   A HD11 1 
ATOM   3720 H  HD11 B LEU   A 1 164 ? 10.022 -6.645  0.305   0.38 19.64 ?  164 LEU   A HD11 1 
ATOM   3721 H  HD12 A LEU   A 1 164 ? 9.099  -6.689  2.058   0.62 20.75 ?  164 LEU   A HD12 1 
ATOM   3722 H  HD12 B LEU   A 1 164 ? 9.033  -6.696  1.548   0.38 19.64 ?  164 LEU   A HD12 1 
ATOM   3723 H  HD13 A LEU   A 1 164 ? 10.261 -7.757  1.875   0.62 20.75 ?  164 LEU   A HD13 1 
ATOM   3724 H  HD13 B LEU   A 1 164 ? 10.208 -7.759  1.423   0.38 19.64 ?  164 LEU   A HD13 1 
ATOM   3725 H  HD21 A LEU   A 1 164 ? 10.047 -8.146  -0.994  0.62 21.44 ?  164 LEU   A HD21 1 
ATOM   3726 H  HD21 B LEU   A 1 164 ? 9.873  -8.313  -1.468  0.38 21.19 ?  164 LEU   A HD21 1 
ATOM   3727 H  HD22 A LEU   A 1 164 ? 10.069 -9.439  -0.072  0.62 21.44 ?  164 LEU   A HD22 1 
ATOM   3728 H  HD22 B LEU   A 1 164 ? 10.064 -9.502  -0.432  0.38 21.19 ?  164 LEU   A HD22 1 
ATOM   3729 H  HD23 A LEU   A 1 164 ? 8.886  -9.223  -1.110  0.62 21.44 ?  164 LEU   A HD23 1 
ATOM   3730 H  HD23 B LEU   A 1 164 ? 8.799  -9.481  -1.393  0.38 21.19 ?  164 LEU   A HD23 1 
ATOM   3731 N  N    A VAL   A 1 165 ? 5.595  -10.708 2.668   0.62 18.10 ?  165 VAL   A N    1 
ATOM   3732 N  N    B VAL   A 1 165 ? 5.545  -10.562 2.598   0.38 18.17 ?  165 VAL   A N    1 
ATOM   3733 C  CA   A VAL   A 1 165 ? 5.132  -11.801 3.517   0.62 18.01 ?  165 VAL   A CA   1 
ATOM   3734 C  CA   B VAL   A 1 165 ? 5.059  -11.572 3.533   0.38 18.10 ?  165 VAL   A CA   1 
ATOM   3735 C  C    A VAL   A 1 165 ? 4.093  -12.641 2.785   0.62 18.54 ?  165 VAL   A C    1 
ATOM   3736 C  C    B VAL   A 1 165 ? 4.031  -12.470 2.861   0.38 18.45 ?  165 VAL   A C    1 
ATOM   3737 O  O    A VAL   A 1 165 ? 4.180  -13.874 2.739   0.62 18.72 ?  165 VAL   A O    1 
ATOM   3738 O  O    B VAL   A 1 165 ? 4.137  -13.701 2.900   0.38 18.66 ?  165 VAL   A O    1 
ATOM   3739 C  CB   A VAL   A 1 165 ? 4.570  -11.231 4.832   0.62 18.33 ?  165 VAL   A CB   1 
ATOM   3740 C  CB   B VAL   A 1 165 ? 4.489  -10.906 4.799   0.38 18.36 ?  165 VAL   A CB   1 
ATOM   3741 C  CG1  A VAL   A 1 165 ? 3.867  -12.318 5.639   0.62 18.67 ?  165 VAL   A CG1  1 
ATOM   3742 C  CG1  B VAL   A 1 165 ? 3.706  -11.919 5.632   0.38 18.39 ?  165 VAL   A CG1  1 
ATOM   3743 C  CG2  A VAL   A 1 165 ? 5.675  -10.564 5.641   0.62 18.68 ?  165 VAL   A CG2  1 
ATOM   3744 C  CG2  B VAL   A 1 165 ? 5.607  -10.283 5.615   0.38 18.70 ?  165 VAL   A CG2  1 
ATOM   3745 H  H    A VAL   A 1 165 ? 5.365  -9.930  2.946   0.62 21.73 ?  165 VAL   A H    1 
ATOM   3746 H  H    B VAL   A 1 165 ? 5.341  -9.753  2.807   0.38 21.82 ?  165 VAL   A H    1 
ATOM   3747 H  HA   A VAL   A 1 165 ? 5.881  -12.378 3.736   0.62 21.63 ?  165 VAL   A HA   1 
ATOM   3748 H  HA   B VAL   A 1 165 ? 5.802  -12.128 3.802   0.38 21.73 ?  165 VAL   A HA   1 
ATOM   3749 H  HB   A VAL   A 1 165 ? 3.912  -10.554 4.618   0.62 22.02 ?  165 VAL   A HB   1 
ATOM   3750 H  HB   B VAL   A 1 165 ? 3.877  -10.200 4.537   0.38 22.05 ?  165 VAL   A HB   1 
ATOM   3751 H  HG11 A VAL   A 1 165 ? 3.764  -12.012 6.553   0.62 22.43 ?  165 VAL   A HG11 1 
ATOM   3752 H  HG11 B VAL   A 1 165 ? 3.602  -11.572 6.532   0.38 22.09 ?  165 VAL   A HG11 1 
ATOM   3753 H  HG12 A VAL   A 1 165 ? 2.992  -12.486 5.250   0.62 22.43 ?  165 VAL   A HG12 1 
ATOM   3754 H  HG12 B VAL   A 1 165 ? 2.833  -12.058 5.232   0.38 22.09 ?  165 VAL   A HG12 1 
ATOM   3755 H  HG13 A VAL   A 1 165 ? 4.402  -13.125 5.617   0.62 22.43 ?  165 VAL   A HG13 1 
ATOM   3756 H  HG13 B VAL   A 1 165 ? 4.197  -12.755 5.658   0.38 22.09 ?  165 VAL   A HG13 1 
ATOM   3757 H  HG21 A VAL   A 1 165 ? 5.301  -10.226 6.471   0.62 22.44 ?  165 VAL   A HG21 1 
ATOM   3758 H  HG21 B VAL   A 1 165 ? 5.226  -9.855  6.397   0.38 22.46 ?  165 VAL   A HG21 1 
ATOM   3759 H  HG22 A VAL   A 1 165 ? 6.368  -11.215 5.832   0.62 22.44 ?  165 VAL   A HG22 1 
ATOM   3760 H  HG22 B VAL   A 1 165 ? 6.225  -10.980 5.886   0.38 22.46 ?  165 VAL   A HG22 1 
ATOM   3761 H  HG23 A VAL   A 1 165 ? 6.045  -9.829  5.125   0.62 22.44 ?  165 VAL   A HG23 1 
ATOM   3762 H  HG23 B VAL   A 1 165 ? 6.067  -9.626  5.068   0.38 22.46 ?  165 VAL   A HG23 1 
ATOM   3763 N  N    A SER   A 1 166 ? 3.087  -11.983 2.207   0.62 19.13 ?  166 SER   A N    1 
ATOM   3764 N  N    B SER   A 1 166 ? 3.021  -11.870 2.231   0.38 18.74 ?  166 SER   A N    1 
ATOM   3765 C  CA   A SER   A 1 166 ? 1.957  -12.691 1.616   0.62 20.55 ?  166 SER   A CA   1 
ATOM   3766 C  CA   B SER   A 1 166 ? 1.905  -12.664 1.728   0.38 19.39 ?  166 SER   A CA   1 
ATOM   3767 C  C    A SER   A 1 166 ? 2.341  -13.478 0.377   0.62 21.07 ?  166 SER   A C    1 
ATOM   3768 C  C    B SER   A 1 166 ? 2.345  -13.587 0.600   0.38 20.01 ?  166 SER   A C    1 
ATOM   3769 O  O    A SER   A 1 166 ? 1.590  -14.373 -0.029  0.62 21.96 ?  166 SER   A O    1 
ATOM   3770 O  O    B SER   A 1 166 ? 1.903  -14.741 0.528   0.38 20.02 ?  166 SER   A O    1 
ATOM   3771 C  CB   A SER   A 1 166 ? 0.858  -11.700 1.229   0.62 21.75 ?  166 SER   A CB   1 
ATOM   3772 C  CB   B SER   A 1 166 ? 0.757  -11.749 1.292   0.38 19.48 ?  166 SER   A CB   1 
ATOM   3773 O  OG   A SER   A 1 166 ? 0.263  -11.109 2.371   0.62 23.09 ?  166 SER   A OG   1 
ATOM   3774 O  OG   B SER   A 1 166 ? 1.125  -10.925 0.204   0.38 19.28 ?  166 SER   A OG   1 
ATOM   3775 H  H    A SER   A 1 166 ? 3.029  -11.133 2.151   0.62 22.98 ?  166 SER   A H    1 
ATOM   3776 H  H    B SER   A 1 166 ? 2.959  -11.028 2.078   0.38 22.50 ?  166 SER   A H    1 
ATOM   3777 H  HA   A SER   A 1 166 ? 1.582  -13.312 2.262   0.62 24.68 ?  166 SER   A HA   1 
ATOM   3778 H  HA   B SER   A 1 166 ? 1.569  -13.223 2.441   0.38 23.29 ?  166 SER   A HA   1 
ATOM   3779 H  HB2  A SER   A 1 166 ? 1.243  -11.012 0.663   0.62 26.12 ?  166 SER   A HB2  1 
ATOM   3780 H  HB2  B SER   A 1 166 ? -0.004 -12.292 1.025   0.38 23.39 ?  166 SER   A HB2  1 
ATOM   3781 H  HB3  A SER   A 1 166 ? 0.160  -12.170 0.745   0.62 26.12 ?  166 SER   A HB3  1 
ATOM   3782 H  HB3  B SER   A 1 166 ? 0.503  -11.181 2.040   0.38 23.39 ?  166 SER   A HB3  1 
ATOM   3783 H  HG   A SER   A 1 166 ? -0.310 -10.542 2.141   0.62 27.73 ?  166 SER   A HG   1 
ATOM   3784 H  HG   B SER   A 1 166 ? 1.782  -10.443 0.415   0.38 23.16 ?  166 SER   A HG   1 
ATOM   3785 N  N    A SER   A 1 167 ? 3.472  -13.153 -0.243  0.62 20.42 ?  167 SER   A N    1 
ATOM   3786 N  N    B SER   A 1 167 ? 3.233  -13.111 -0.270  0.38 20.63 ?  167 SER   A N    1 
ATOM   3787 C  CA   A SER   A 1 167 ? 3.941  -13.858 -1.423  0.62 21.39 ?  167 SER   A CA   1 
ATOM   3788 C  CA   B SER   A 1 167 ? 3.672  -13.874 -1.430  0.38 21.50 ?  167 SER   A CA   1 
ATOM   3789 C  C    A SER   A 1 167 ? 5.096  -14.801 -1.128  0.62 21.37 ?  167 SER   A C    1 
ATOM   3790 C  C    B SER   A 1 167 ? 4.836  -14.806 -1.120  0.38 22.20 ?  167 SER   A C    1 
ATOM   3791 O  O    A SER   A 1 167 ? 5.641  -15.394 -2.063  0.62 21.78 ?  167 SER   A O    1 
ATOM   3792 O  O    B SER   A 1 167 ? 5.243  -15.575 -1.997  0.38 22.39 ?  167 SER   A O    1 
ATOM   3793 C  CB   A SER   A 1 167 ? 4.356  -12.858 -2.511  0.62 22.11 ?  167 SER   A CB   1 
ATOM   3794 C  CB   B SER   A 1 167 ? 4.067  -12.929 -2.571  0.38 21.62 ?  167 SER   A CB   1 
ATOM   3795 O  OG   A SER   A 1 167 ? 5.321  -11.939 -2.021  0.62 22.66 ?  167 SER   A OG   1 
ATOM   3796 O  OG   B SER   A 1 167 ? 5.362  -12.392 -2.362  0.38 21.56 ?  167 SER   A OG   1 
ATOM   3797 H  H    A SER   A 1 167 ? 3.988  -12.507 0.003   0.62 24.52 ?  167 SER   A H    1 
ATOM   3798 H  H    B SER   A 1 167 ? 3.605  -12.338 -0.203  0.38 24.77 ?  167 SER   A H    1 
ATOM   3799 H  HA   A SER   A 1 167 ? 3.218  -14.389 -1.777  0.62 25.69 ?  167 SER   A HA   1 
ATOM   3800 H  HA   B SER   A 1 167 ? 2.934  -14.415 -1.744  0.38 25.82 ?  167 SER   A HA   1 
ATOM   3801 H  HB2  A SER   A 1 167 ? 4.739  -13.345 -3.258  0.62 26.55 ?  167 SER   A HB2  1 
ATOM   3802 H  HB2  B SER   A 1 167 ? 4.063  -13.423 -3.408  0.38 25.97 ?  167 SER   A HB2  1 
ATOM   3803 H  HB3  A SER   A 1 167 ? 3.563  -12.378 -2.809  0.62 26.55 ?  167 SER   A HB3  1 
ATOM   3804 H  HB3  B SER   A 1 167 ? 3.426  -12.200 -2.618  0.38 25.97 ?  167 SER   A HB3  1 
ATOM   3805 H  HG   A SER   A 1 167 ? 5.002  -11.515 -1.369  0.62 27.21 ?  167 SER   A HG   1 
ATOM   3806 H  HG   B SER   A 1 167 ? 5.379  -11.955 -1.645  0.38 25.89 ?  167 SER   A HG   1 
ATOM   3807 N  N    A PHE   A 1 168 ? 5.485  -14.955 0.136   0.62 21.21 ?  168 PHE   A N    1 
ATOM   3808 N  N    B PHE   A 1 168 ? 5.380  -14.761 0.094   0.38 23.07 ?  168 PHE   A N    1 
ATOM   3809 C  CA   A PHE   A 1 168 ? 6.676  -15.732 0.451   0.62 21.54 ?  168 PHE   A CA   1 
ATOM   3810 C  CA   B PHE   A 1 168 ? 6.523  -15.599 0.425   0.38 24.38 ?  168 PHE   A CA   1 
ATOM   3811 C  C    A PHE   A 1 168 ? 6.393  -17.220 0.323   0.62 24.12 ?  168 PHE   A C    1 
ATOM   3812 C  C    B PHE   A 1 168 ? 6.139  -17.068 0.348   0.38 27.29 ?  168 PHE   A C    1 
ATOM   3813 O  O    A PHE   A 1 168 ? 5.436  -17.739 0.911   0.62 24.45 ?  168 PHE   A O    1 
ATOM   3814 O  O    B PHE   A 1 168 ? 4.992  -17.449 0.602   0.38 27.89 ?  168 PHE   A O    1 
ATOM   3815 C  CB   A PHE   A 1 168 ? 7.189  -15.438 1.859   0.62 20.16 ?  168 PHE   A CB   1 
ATOM   3816 C  CB   B PHE   A 1 168 ? 7.024  -15.287 1.835   0.38 22.95 ?  168 PHE   A CB   1 
ATOM   3817 C  CG   A PHE   A 1 168 ? 8.460  -16.174 2.185   0.62 18.91 ?  168 PHE   A CG   1 
ATOM   3818 C  CG   B PHE   A 1 168 ? 8.316  -15.976 2.184   0.38 21.75 ?  168 PHE   A CG   1 
ATOM   3819 C  CD1  A PHE   A 1 168 ? 9.637  -15.835 1.546   0.62 18.85 ?  168 PHE   A CD1  1 
ATOM   3820 C  CD1  B PHE   A 1 168 ? 9.521  -15.482 1.719   0.38 21.19 ?  168 PHE   A CD1  1 
ATOM   3821 C  CD2  A PHE   A 1 168 ? 8.482  -17.221 3.098   0.62 17.94 ?  168 PHE   A CD2  1 
ATOM   3822 C  CD2  B PHE   A 1 168 ? 8.326  -17.114 2.975   0.38 21.42 ?  168 PHE   A CD2  1 
ATOM   3823 C  CE1  A PHE   A 1 168 ? 10.814 -16.506 1.818   0.62 18.24 ?  168 PHE   A CE1  1 
ATOM   3824 C  CE1  B PHE   A 1 168 ? 10.715 -16.108 2.035   0.38 21.01 ?  168 PHE   A CE1  1 
ATOM   3825 C  CE2  A PHE   A 1 168 ? 9.668  -17.898 3.377   0.62 18.30 ?  168 PHE   A CE2  1 
ATOM   3826 C  CE2  B PHE   A 1 168 ? 9.518  -17.744 3.296   0.38 21.52 ?  168 PHE   A CE2  1 
ATOM   3827 C  CZ   A PHE   A 1 168 ? 10.831 -17.538 2.733   0.62 18.56 ?  168 PHE   A CZ   1 
ATOM   3828 C  CZ   B PHE   A 1 168 ? 10.712 -17.240 2.824   0.38 21.26 ?  168 PHE   A CZ   1 
ATOM   3829 H  H    A PHE   A 1 168 ? 5.094  -14.617 0.822   0.62 25.47 ?  168 PHE   A H    1 
ATOM   3830 H  H    B PHE   A 1 168 ? 5.108  -14.259 0.735   0.38 27.71 ?  168 PHE   A H    1 
ATOM   3831 H  HA   A PHE   A 1 168 ? 7.386  -15.504 -0.177  0.62 25.86 ?  168 PHE   A HA   1 
ATOM   3832 H  HA   B PHE   A 1 168 ? 7.240  -15.438 -0.205  0.38 29.27 ?  168 PHE   A HA   1 
ATOM   3833 H  HB2  A PHE   A 1 168 ? 7.372  -14.487 1.939   0.62 24.21 ?  168 PHE   A HB2  1 
ATOM   3834 H  HB2  B PHE   A 1 168 ? 7.168  -14.333 1.908   0.38 27.56 ?  168 PHE   A HB2  1 
ATOM   3835 H  HB3  A PHE   A 1 168 ? 6.521  -15.705 2.504   0.62 24.21 ?  168 PHE   A HB3  1 
ATOM   3836 H  HB3  B PHE   A 1 168 ? 6.353  -15.570 2.475   0.38 27.56 ?  168 PHE   A HB3  1 
ATOM   3837 H  HD1  A PHE   A 1 168 ? 9.650  -15.143 0.928   0.62 22.64 ?  168 PHE   A HD1  1 
ATOM   3838 H  HD1  B PHE   A 1 168 ? 9.531  -14.720 1.186   0.38 25.45 ?  168 PHE   A HD1  1 
ATOM   3839 H  HD2  A PHE   A 1 168 ? 7.703  -17.467 3.535   0.62 21.55 ?  168 PHE   A HD2  1 
ATOM   3840 H  HD2  B PHE   A 1 168 ? 7.525  -17.459 3.296   0.38 25.73 ?  168 PHE   A HD2  1 
ATOM   3841 H  HE1  A PHE   A 1 168 ? 11.607 -16.265 1.384   0.62 21.90 ?  168 PHE   A HE1  1 
ATOM   3842 H  HE1  B PHE   A 1 168 ? 11.521 -15.767 1.716   0.38 25.23 ?  168 PHE   A HE1  1 
ATOM   3843 H  HE2  A PHE   A 1 168 ? 9.674  -18.597 3.993   0.62 21.98 ?  168 PHE   A HE2  1 
ATOM   3844 H  HE2  B PHE   A 1 168 ? 9.513  -18.507 3.828   0.38 25.85 ?  168 PHE   A HE2  1 
ATOM   3845 H  HZ   A PHE   A 1 168 ? 11.629 -17.990 2.914   0.62 22.29 ?  168 PHE   A HZ   1 
ATOM   3846 H  HZ   B PHE   A 1 168 ? 11.515 -17.661 3.037   0.38 25.54 ?  168 PHE   A HZ   1 
ATOM   3847 N  N    A LEU   A 1 169 ? 7.250  -17.910 -0.425  0.62 27.87 ?  169 LEU   A N    1 
ATOM   3848 N  N    B LEU   A 1 169 ? 7.113  -17.897 -0.008  0.38 29.89 ?  169 LEU   A N    1 
ATOM   3849 C  CA   A LEU   A 1 169 ? 7.115  -19.347 -0.584  0.62 33.15 ?  169 LEU   A CA   1 
ATOM   3850 C  CA   B LEU   A 1 169 ? 6.880  -19.323 -0.093  0.38 32.77 ?  169 LEU   A CA   1 
ATOM   3851 C  C    A LEU   A 1 169 ? 8.060  -20.058 0.372   0.62 35.72 ?  169 LEU   A C    1 
ATOM   3852 C  C    B LEU   A 1 169 ? 7.660  -20.050 0.995   0.38 34.07 ?  169 LEU   A C    1 
ATOM   3853 O  O    A LEU   A 1 169 ? 7.639  -20.593 1.399   0.62 36.69 ?  169 LEU   A O    1 
ATOM   3854 O  O    B LEU   A 1 169 ? 7.071  -20.639 1.901   0.38 34.43 ?  169 LEU   A O    1 
ATOM   3855 C  CB   A LEU   A 1 169 ? 7.414  -19.763 -2.024  0.62 34.92 ?  169 LEU   A CB   1 
ATOM   3856 C  CB   B LEU   A 1 169 ? 7.287  -19.850 -1.478  0.38 33.92 ?  169 LEU   A CB   1 
ATOM   3857 C  CG   A LEU   A 1 169 ? 7.097  -21.221 -2.368  0.62 36.41 ?  169 LEU   A CG   1 
ATOM   3858 C  CG   B LEU   A 1 169 ? 6.301  -20.756 -2.228  0.38 34.78 ?  169 LEU   A CG   1 
ATOM   3859 C  CD1  A LEU   A 1 169 ? 5.684  -21.581 -1.933  0.62 36.89 ?  169 LEU   A CD1  1 
ATOM   3860 C  CD1  B LEU   A 1 169 ? 5.011  -20.987 -1.447  0.38 34.93 ?  169 LEU   A CD1  1 
ATOM   3861 C  CD2  A LEU   A 1 169 ? 7.273  -21.461 -3.857  0.62 36.71 ?  169 LEU   A CD2  1 
ATOM   3862 C  CD2  B LEU   A 1 169 ? 5.994  -20.168 -3.598  0.38 34.95 ?  169 LEU   A CD2  1 
ATOM   3863 O  OXT  A LEU   A 1 169 ? 9.267  -20.103 0.142   0.62 35.94 -1 169 LEU   A OXT  1 
ATOM   3864 O  OXT  B LEU   A 1 169 ? 8.894  -20.058 0.995   0.38 34.32 -1 169 LEU   A OXT  1 
ATOM   3865 H  H    A LEU   A 1 169 ? 7.922  -17.570 -0.855  0.62 33.46 ?  169 LEU   A H    1 
ATOM   3866 H  H    B LEU   A 1 169 ? 7.911  -17.660 -0.207  0.38 35.89 ?  169 LEU   A H    1 
ATOM   3867 H  HA   A LEU   A 1 169 ? 6.205  -19.595 -0.368  0.62 39.80 ?  169 LEU   A HA   1 
ATOM   3868 H  HA   B LEU   A 1 169 ? 5.935  -19.462 0.066   0.38 39.35 ?  169 LEU   A HA   1 
ATOM   3869 H  HB2  A LEU   A 1 169 ? 6.892  -19.206 -2.619  0.62 41.92 ?  169 LEU   A HB2  1 
ATOM   3870 H  HB2  B LEU   A 1 169 ? 7.463  -19.087 -2.053  0.38 40.73 ?  169 LEU   A HB2  1 
ATOM   3871 H  HB3  A LEU   A 1 169 ? 8.359  -19.626 -2.193  0.62 41.92 ?  169 LEU   A HB3  1 
ATOM   3872 H  HB3  B LEU   A 1 169 ? 8.110  -20.358 -1.374  0.38 40.73 ?  169 LEU   A HB3  1 
ATOM   3873 H  HG   A LEU   A 1 169 ? 7.714  -21.802 -1.895  0.62 43.71 ?  169 LEU   A HG   1 
ATOM   3874 H  HG   B LEU   A 1 169 ? 6.718  -21.621 -2.371  0.38 41.76 ?  169 LEU   A HG   1 
ATOM   3875 H  HD11 A LEU   A 1 169 ? 5.419  -22.401 -2.373  0.62 44.29 ?  169 LEU   A HD11 1 
ATOM   3876 H  HD11 B LEU   A 1 169 ? 4.458  -21.598 -1.938  0.38 41.94 ?  169 LEU   A HD11 1 
ATOM   3877 H  HD12 A LEU   A 1 169 ? 5.671  -21.702 -0.970  0.62 44.29 ?  169 LEU   A HD12 1 
ATOM   3878 H  HD12 B LEU   A 1 169 ? 5.229  -21.365 -0.576  0.38 41.94 ?  169 LEU   A HD12 1 
ATOM   3879 H  HD13 A LEU   A 1 169 ? 5.085  -20.860 -2.185  0.62 44.29 ?  169 LEU   A HD13 1 
ATOM   3880 H  HD13 B LEU   A 1 169 ? 4.548  -20.137 -1.338  0.38 41.94 ?  169 LEU   A HD13 1 
ATOM   3881 H  HD21 A LEU   A 1 169 ? 7.076  -22.391 -4.052  0.62 44.07 ?  169 LEU   A HD21 1 
ATOM   3882 H  HD21 B LEU   A 1 169 ? 5.374  -20.754 -4.060  0.38 41.96 ?  169 LEU   A HD21 1 
ATOM   3883 H  HD22 A LEU   A 1 169 ? 6.662  -20.884 -4.343  0.62 44.07 ?  169 LEU   A HD22 1 
ATOM   3884 H  HD22 B LEU   A 1 169 ? 5.597  -19.291 -3.482  0.38 41.96 ?  169 LEU   A HD22 1 
ATOM   3885 H  HD23 A LEU   A 1 169 ? 8.188  -21.257 -4.104  0.62 44.07 ?  169 LEU   A HD23 1 
ATOM   3886 H  HD23 B LEU   A 1 169 ? 6.819  -20.094 -4.103  0.38 41.96 ?  169 LEU   A HD23 1 
ATOM   3887 N  N    A SER   B 1 1   ? 50.837 -9.254  -23.724 0.62 26.72 ?  1   SER   B N    1 
ATOM   3888 N  N    B SER   B 1 1   ? 50.733 -9.252  -23.685 0.38 26.25 ?  1   SER   B N    1 
ATOM   3889 C  CA   A SER   B 1 1   ? 51.321 -10.295 -22.795 0.62 27.22 ?  1   SER   B CA   1 
ATOM   3890 C  CA   B SER   B 1 1   ? 51.237 -10.237 -22.704 0.38 26.38 ?  1   SER   B CA   1 
ATOM   3891 C  C    A SER   B 1 1   ? 50.250 -11.354 -22.546 0.62 26.35 ?  1   SER   B C    1 
ATOM   3892 C  C    B SER   B 1 1   ? 50.211 -11.336 -22.478 0.38 25.67 ?  1   SER   B C    1 
ATOM   3893 O  O    A SER   B 1 1   ? 49.054 -11.150 -22.807 0.62 26.37 ?  1   SER   B O    1 
ATOM   3894 O  O    B SER   B 1 1   ? 49.007 -11.147 -22.687 0.38 25.60 ?  1   SER   B O    1 
ATOM   3895 C  CB   A SER   B 1 1   ? 51.764 -9.674  -21.471 0.62 28.06 ?  1   SER   B CB   1 
ATOM   3896 C  CB   B SER   B 1 1   ? 51.563 -9.558  -21.377 0.38 26.75 ?  1   SER   B CB   1 
ATOM   3897 O  OG   A SER   B 1 1   ? 50.651 -9.388  -20.645 0.62 30.29 ?  1   SER   B OG   1 
ATOM   3898 O  OG   B SER   B 1 1   ? 50.433 -9.551  -20.523 0.38 27.98 ?  1   SER   B OG   1 
ATOM   3899 H  H1   A SER   B 1 1   ? 50.753 -9.606  -24.535 0.62 32.08 ?  1   SER   B H1   1 
ATOM   3900 H  H1   B SER   B 1 1   ? 50.636 -9.652  -24.472 0.38 31.52 ?  1   SER   B H1   1 
ATOM   3901 H  H2   A SER   B 1 1   ? 50.053 -8.956  -23.440 0.62 32.08 ?  1   SER   B H2   1 
ATOM   3902 H  H2   B SER   B 1 1   ? 49.953 -8.939  -23.405 0.38 31.52 ?  1   SER   B H2   1 
ATOM   3903 H  H3   A SER   B 1 1   ? 51.425 -8.588  -23.745 0.62 32.08 ?  1   SER   B H3   1 
ATOM   3904 H  H3   B SER   B 1 1   ? 51.320 -8.589  -23.753 0.38 31.52 ?  1   SER   B H3   1 
ATOM   3905 H  HA   A SER   B 1 1   ? 52.091 -10.720 -23.200 0.62 32.68 ?  1   SER   B HA   1 
ATOM   3906 H  HA   B SER   B 1 1   ? 52.045 -10.631 -23.058 0.38 31.68 ?  1   SER   B HA   1 
ATOM   3907 H  HB2  A SER   B 1 1   ? 52.342 -10.302 -21.014 0.62 33.69 ?  1   SER   B HB2  1 
ATOM   3908 H  HB2  B SER   B 1 1   ? 52.281 -10.047 -20.950 0.38 32.12 ?  1   SER   B HB2  1 
ATOM   3909 H  HB3  A SER   B 1 1   ? 52.247 -8.850  -21.651 0.62 33.69 ?  1   SER   B HB3  1 
ATOM   3910 H  HB3  B SER   B 1 1   ? 51.838 -8.643  -21.548 0.38 32.12 ?  1   SER   B HB3  1 
ATOM   3911 H  HG   A SER   B 1 1   ? 50.911 -9.004  -19.942 0.62 36.36 ?  1   SER   B HG   1 
ATOM   3912 H  HG   B SER   B 1 1   ? 50.611 -9.120  -19.824 0.38 33.59 ?  1   SER   B HG   1 
ATOM   3913 N  N    A MET   B 1 2   ? 50.704 -12.492 -22.038 0.62 25.64 ?  2   MET   B N    1 
ATOM   3914 N  N    B MET   B 1 2   ? 50.704 -12.489 -22.045 0.38 25.05 ?  2   MET   B N    1 
ATOM   3915 C  CA   A MET   B 1 2   ? 49.879 -13.679 -21.866 0.62 26.00 ?  2   MET   B CA   1 
ATOM   3916 C  CA   B MET   B 1 2   ? 49.881 -13.672 -21.852 0.38 24.85 ?  2   MET   B CA   1 
ATOM   3917 C  C    A MET   B 1 2   ? 49.615 -13.875 -20.379 0.62 24.21 ?  2   MET   B C    1 
ATOM   3918 C  C    B MET   B 1 2   ? 49.619 -13.852 -20.366 0.38 23.65 ?  2   MET   B C    1 
ATOM   3919 O  O    A MET   B 1 2   ? 50.541 -14.140 -19.610 0.62 24.43 ?  2   MET   B O    1 
ATOM   3920 O  O    B MET   B 1 2   ? 50.551 -14.077 -19.589 0.38 23.89 ?  2   MET   B O    1 
ATOM   3921 C  CB   A MET   B 1 2   ? 50.610 -14.879 -22.454 0.62 29.85 ?  2   MET   B CB   1 
ATOM   3922 C  CB   B MET   B 1 2   ? 50.601 -14.884 -22.421 0.38 26.84 ?  2   MET   B CB   1 
ATOM   3923 C  CG   A MET   B 1 2   ? 49.776 -16.142 -22.561 0.62 33.44 ?  2   MET   B CG   1 
ATOM   3924 C  CG   B MET   B 1 2   ? 49.698 -16.060 -22.765 0.38 28.40 ?  2   MET   B CG   1 
ATOM   3925 S  SD   A MET   B 1 2   ? 50.613 -17.382 -23.566 0.62 37.18 ?  2   MET   B SD   1 
ATOM   3926 S  SD   B MET   B 1 2   ? 50.517 -17.252 -23.837 0.38 29.81 ?  2   MET   B SD   1 
ATOM   3927 C  CE   A MET   B 1 2   ? 51.130 -16.352 -24.931 0.62 37.42 ?  2   MET   B CE   1 
ATOM   3928 C  CE   B MET   B 1 2   ? 51.811 -16.227 -24.514 0.38 30.25 ?  2   MET   B CE   1 
ATOM   3929 H  H    A MET   B 1 2   ? 51.522 -12.608 -21.786 0.62 30.79 ?  2   MET   B H    1 
ATOM   3930 H  H    B MET   B 1 2   ? 51.537 -12.618 -21.858 0.38 30.08 ?  2   MET   B H    1 
ATOM   3931 H  HA   A MET   B 1 2   ? 49.045 -13.571 -22.343 0.62 31.22 ?  2   MET   B HA   1 
ATOM   3932 H  HA   B MET   B 1 2   ? 49.048 -13.581 -22.336 0.38 29.84 ?  2   MET   B HA   1 
ATOM   3933 H  HB2  A MET   B 1 2   ? 50.906 -14.609 -23.334 0.62 35.84 ?  2   MET   B HB2  1 
ATOM   3934 H  HB2  B MET   B 1 2   ? 50.995 -14.531 -23.225 0.38 32.23 ?  2   MET   B HB2  1 
ATOM   3935 H  HB3  A MET   B 1 2   ? 51.378 -15.094 -21.907 0.62 35.84 ?  2   MET   B HB3  1 
ATOM   3936 H  HB3  B MET   B 1 2   ? 51.292 -15.208 -21.818 0.38 32.23 ?  2   MET   B HB3  1 
ATOM   3937 H  HG2  A MET   B 1 2   ? 49.633 -16.509 -21.671 0.62 40.15 ?  2   MET   B HG2  1 
ATOM   3938 H  HG2  B MET   B 1 2   ? 49.424 -16.508 -21.944 0.38 34.09 ?  2   MET   B HG2  1 
ATOM   3939 H  HG3  A MET   B 1 2   ? 48.925 -15.936 -22.980 0.62 40.15 ?  2   MET   B HG3  1 
ATOM   3940 H  HG3  B MET   B 1 2   ? 48.922 -15.744 -23.244 0.38 34.09 ?  2   MET   B HG3  1 
ATOM   3941 H  HE1  A MET   B 1 2   ? 51.286 -16.909 -25.694 0.62 44.92 ?  2   MET   B HE1  1 
ATOM   3942 H  HE1  B MET   B 1 2   ? 52.284 -16.752 -25.139 0.38 36.31 ?  2   MET   B HE1  1 
ATOM   3943 H  HE2  A MET   B 1 2   ? 50.423 -15.709 -25.123 0.62 44.92 ?  2   MET   B HE2  1 
ATOM   3944 H  HE2  B MET   B 1 2   ? 51.396 -15.465 -24.960 0.38 36.31 ?  2   MET   B HE2  1 
ATOM   3945 H  HE3  A MET   B 1 2   ? 51.945 -15.878 -24.686 0.62 44.92 ?  2   MET   B HE3  1 
ATOM   3946 H  HE3  B MET   B 1 2   ? 52.427 -15.924 -23.815 0.38 36.31 ?  2   MET   B HE3  1 
ATOM   3947 N  N    . VAL   B 1 3   ? 48.356 -13.734 -19.976 1.00 22.06 ?  3   VAL   B N    1 
ATOM   3948 C  CA   . VAL   B 1 3   ? 47.943 -13.955 -18.599 1.00 20.96 ?  3   VAL   B CA   1 
ATOM   3949 C  C    . VAL   B 1 3   ? 46.707 -14.841 -18.608 1.00 19.32 ?  3   VAL   B C    1 
ATOM   3950 O  O    . VAL   B 1 3   ? 45.985 -14.930 -19.603 1.00 19.90 ?  3   VAL   B O    1 
ATOM   3951 C  CB   . VAL   B 1 3   ? 47.659 -12.641 -17.845 1.00 22.56 ?  3   VAL   B CB   1 
ATOM   3952 C  CG1  . VAL   B 1 3   ? 48.925 -11.779 -17.748 1.00 23.28 ?  3   VAL   B CG1  1 
ATOM   3953 C  CG2  . VAL   B 1 3   ? 46.520 -11.885 -18.519 1.00 22.85 ?  3   VAL   B CG2  1 
ATOM   3954 H  H    A VAL   B 1 3   ? 47.712 -13.516 -20.504 0.62 26.50 ?  3   VAL   B H    1 
ATOM   3955 H  H    B VAL   B 1 3   ? 47.711 -13.528 -20.508 0.38 26.50 ?  3   VAL   B H    1 
ATOM   3956 H  HA   . VAL   B 1 3   ? 48.647 -14.430 -18.130 1.00 25.18 ?  3   VAL   B HA   1 
ATOM   3957 H  HB   . VAL   B 1 3   ? 47.377 -12.865 -16.945 1.00 27.09 ?  3   VAL   B HB   1 
ATOM   3958 H  HG11 . VAL   B 1 3   ? 48.710 -10.971 -17.261 1.00 27.96 ?  3   VAL   B HG11 1 
ATOM   3959 H  HG12 . VAL   B 1 3   ? 49.607 -12.281 -17.276 1.00 27.96 ?  3   VAL   B HG12 1 
ATOM   3960 H  HG13 . VAL   B 1 3   ? 49.225 -11.564 -18.642 1.00 27.96 ?  3   VAL   B HG13 1 
ATOM   3961 H  HG21 . VAL   B 1 3   ? 46.464 -11.000 -18.138 1.00 27.43 ?  3   VAL   B HG21 1 
ATOM   3962 H  HG22 . VAL   B 1 3   ? 46.693 -11.831 -19.471 1.00 27.43 ?  3   VAL   B HG22 1 
ATOM   3963 H  HG23 . VAL   B 1 3   ? 45.685 -12.364 -18.365 1.00 27.43 ?  3   VAL   B HG23 1 
ATOM   3964 N  N    . ASN   B 1 4   ? 46.471 -15.504 -17.479 1.00 17.48 ?  4   ASN   B N    1 
ATOM   3965 C  CA   . ASN   B 1 4   ? 45.329 -16.409 -17.345 1.00 16.09 ?  4   ASN   B CA   1 
ATOM   3966 C  C    . ASN   B 1 4   ? 45.262 -17.379 -18.519 1.00 16.35 ?  4   ASN   B C    1 
ATOM   3967 O  O    . ASN   B 1 4   ? 44.199 -17.628 -19.081 1.00 16.89 ?  4   ASN   B O    1 
ATOM   3968 C  CB   . ASN   B 1 4   ? 44.018 -15.632 -17.190 1.00 15.79 ?  4   ASN   B CB   1 
ATOM   3969 C  CG   . ASN   B 1 4   ? 43.971 -14.823 -15.906 1.00 15.32 ?  4   ASN   B CG   1 
ATOM   3970 O  OD1  . ASN   B 1 4   ? 44.258 -15.337 -14.829 1.00 15.04 ?  4   ASN   B OD1  1 
ATOM   3971 N  ND2  . ASN   B 1 4   ? 43.635 -13.540 -16.020 1.00 16.67 ?  4   ASN   B ND2  1 
ATOM   3972 H  H    . ASN   B 1 4   ? 46.965 -15.455 -16.783 1.00 20.99 ?  4   ASN   B H    1 
ATOM   3973 H  HA   . ASN   B 1 4   ? 45.456 -16.940 -16.544 1.00 19.33 ?  4   ASN   B HA   1 
ATOM   3974 H  HB2  . ASN   B 1 4   ? 43.921 -15.021 -17.935 1.00 18.97 ?  4   ASN   B HB2  1 
ATOM   3975 H  HB3  . ASN   B 1 4   ? 43.278 -16.261 -17.176 1.00 18.97 ?  4   ASN   B HB3  1 
ATOM   3976 H  HD21 . ASN   B 1 4   ? 43.595 -13.038 -15.318 1.00 20.03 ?  4   ASN   B HD21 1 
ATOM   3977 H  HD22 . ASN   B 1 4   ? 43.448 -13.209 -16.790 1.00 20.03 ?  4   ASN   B HD22 1 
ATOM   3978 N  N    . SER   B 1 5   ? 46.417 -17.926 -18.895 1.00 17.48 ?  5   SER   B N    1 
ATOM   3979 C  CA   . SER   B 1 5   ? 46.515 -18.830 -20.039 1.00 19.05 ?  5   SER   B CA   1 
ATOM   3980 C  C    . SER   B 1 5   ? 46.457 -20.269 -19.541 1.00 20.85 ?  5   SER   B C    1 
ATOM   3981 O  O    . SER   B 1 5   ? 47.430 -21.012 -19.562 1.00 24.42 ?  5   SER   B O    1 
ATOM   3982 C  CB   . SER   B 1 5   ? 47.793 -18.553 -20.830 1.00 20.56 ?  5   SER   B CB   1 
ATOM   3983 O  OG   . SER   B 1 5   ? 48.955 -18.711 -20.030 1.00 23.52 ?  5   SER   B OG   1 
ATOM   3984 H  H    . SER   B 1 5   ? 47.166 -17.797 -18.497 1.00 21.00 ?  5   SER   B H    1 
ATOM   3985 H  HA   . SER   B 1 5   ? 45.761 -18.688 -20.631 1.00 22.88 ?  5   SER   B HA   1 
ATOM   3986 H  HB2  . SER   B 1 5   ? 47.840 -19.173 -21.578 1.00 24.69 ?  5   SER   B HB2  1 
ATOM   3987 H  HB3  . SER   B 1 5   ? 47.750 -17.643 -21.162 1.00 24.69 ?  5   SER   B HB3  1 
ATOM   3988 H  HG   . SER   B 1 5   ? 48.990 -19.497 -19.738 1.00 28.25 ?  5   SER   B HG   1 
ATOM   3989 N  N    A PHE   B 1 6   ? 45.271 -20.668 -19.099 0.62 21.37 ?  6   PHE   B N    1 
ATOM   3990 N  N    B PHE   B 1 6   ? 45.276 -20.607 -19.030 0.38 20.17 ?  6   PHE   B N    1 
ATOM   3991 C  CA   A PHE   B 1 6   ? 45.075 -22.020 -18.593 0.62 21.47 ?  6   PHE   B CA   1 
ATOM   3992 C  CA   B PHE   B 1 6   ? 44.977 -21.959 -18.588 0.38 19.32 ?  6   PHE   B CA   1 
ATOM   3993 C  C    A PHE   B 1 6   ? 44.998 -23.008 -19.750 0.62 25.25 ?  6   PHE   B C    1 
ATOM   3994 C  C    B PHE   B 1 6   ? 44.780 -22.840 -19.809 0.38 20.34 ?  6   PHE   B C    1 
ATOM   3995 O  O    A PHE   B 1 6   ? 44.325 -22.757 -20.753 0.62 27.44 ?  6   PHE   B O    1 
ATOM   3996 O  O    B PHE   B 1 6   ? 44.079 -22.458 -20.751 0.38 21.55 ?  6   PHE   B O    1 
ATOM   3997 C  CB   A PHE   B 1 6   ? 43.798 -22.089 -17.757 0.62 19.88 ?  6   PHE   B CB   1 
ATOM   3998 C  CB   B PHE   B 1 6   ? 43.692 -21.949 -17.759 0.38 18.62 ?  6   PHE   B CB   1 
ATOM   3999 C  CG   A PHE   B 1 6   ? 43.838 -21.233 -16.524 0.62 18.27 ?  6   PHE   B CG   1 
ATOM   4000 C  CG   B PHE   B 1 6   ? 43.767 -21.098 -16.520 0.38 17.78 ?  6   PHE   B CG   1 
ATOM   4001 C  CD1  A PHE   B 1 6   ? 44.349 -21.728 -15.339 0.62 17.16 ?  6   PHE   B CD1  1 
ATOM   4002 C  CD1  B PHE   B 1 6   ? 44.260 -21.622 -15.339 0.38 17.26 ?  6   PHE   B CD1  1 
ATOM   4003 C  CD2  A PHE   B 1 6   ? 43.370 -19.930 -16.555 0.62 17.94 ?  6   PHE   B CD2  1 
ATOM   4004 C  CD2  B PHE   B 1 6   ? 43.333 -19.779 -16.533 0.38 17.46 ?  6   PHE   B CD2  1 
ATOM   4005 C  CE1  A PHE   B 1 6   ? 44.385 -20.937 -14.200 0.62 16.95 ?  6   PHE   B CE1  1 
ATOM   4006 C  CE1  B PHE   B 1 6   ? 44.327 -20.848 -14.193 0.38 17.06 ?  6   PHE   B CE1  1 
ATOM   4007 C  CE2  A PHE   B 1 6   ? 43.405 -19.135 -15.429 0.62 18.57 ?  6   PHE   B CE2  1 
ATOM   4008 C  CE2  B PHE   B 1 6   ? 43.399 -18.999 -15.391 0.38 17.83 ?  6   PHE   B CE2  1 
ATOM   4009 C  CZ   A PHE   B 1 6   ? 43.916 -19.632 -14.250 0.62 17.50 ?  6   PHE   B CZ   1 
ATOM   4010 C  CZ   B PHE   B 1 6   ? 43.897 -19.532 -14.221 0.38 17.22 ?  6   PHE   B CZ   1 
ATOM   4011 H  H    A PHE   B 1 6   ? 44.565 -20.180 -19.084 0.62 25.67 ?  6   PHE   B H    1 
ATOM   4012 H  H    B PHE   B 1 6   ? 44.622 -20.067 -18.937 0.38 24.23 ?  6   PHE   B H    1 
ATOM   4013 H  HA   A PHE   B 1 6   ? 45.821 -22.268 -18.028 0.62 25.78 ?  6   PHE   B HA   1 
ATOM   4014 H  HA   B PHE   B 1 6   ? 45.702 -22.314 -18.051 0.38 23.20 ?  6   PHE   B HA   1 
ATOM   4015 H  HB2  A PHE   B 1 6   ? 43.049 -21.793 -18.298 0.62 23.87 ?  6   PHE   B HB2  1 
ATOM   4016 H  HB2  B PHE   B 1 6   ? 42.969 -21.605 -18.309 0.38 22.37 ?  6   PHE   B HB2  1 
ATOM   4017 H  HB3  A PHE   B 1 6   ? 43.654 -23.007 -17.474 0.62 23.87 ?  6   PHE   B HB3  1 
ATOM   4018 H  HB3  B PHE   B 1 6   ? 43.484 -22.856 -17.483 0.38 22.37 ?  6   PHE   B HB3  1 
ATOM   4019 H  HD1  A PHE   B 1 6   ? 44.670 -22.601 -15.303 0.62 20.61 ?  6   PHE   B HD1  1 
ATOM   4020 H  HD1  B PHE   B 1 6   ? 44.555 -22.503 -15.317 0.38 20.73 ?  6   PHE   B HD1  1 
ATOM   4021 H  HD2  A PHE   B 1 6   ? 43.025 -19.590 -17.347 0.62 21.55 ?  6   PHE   B HD2  1 
ATOM   4022 H  HD2  B PHE   B 1 6   ? 42.994 -19.415 -17.319 0.38 20.97 ?  6   PHE   B HD2  1 
ATOM   4023 H  HE1  A PHE   B 1 6   ? 44.737 -21.277 -13.407 0.62 20.36 ?  6   PHE   B HE1  1 
ATOM   4024 H  HE1  B PHE   B 1 6   ? 44.668 -21.208 -13.406 0.38 20.49 ?  6   PHE   B HE1  1 
ATOM   4025 H  HE2  A PHE   B 1 6   ? 43.085 -18.263 -15.467 0.62 22.30 ?  6   PHE   B HE2  1 
ATOM   4026 H  HE2  B PHE   B 1 6   ? 43.105 -18.116 -15.413 0.38 21.41 ?  6   PHE   B HE2  1 
ATOM   4027 H  HZ   A PHE   B 1 6   ? 43.941 -19.101 -13.488 0.62 21.03 ?  6   PHE   B HZ   1 
ATOM   4028 H  HZ   B PHE   B 1 6   ? 43.943 -19.010 -13.451 0.38 20.68 ?  6   PHE   B HZ   1 
ATOM   4029 N  N    A SER   B 1 7   ? 45.701 -24.134 -19.607 0.62 26.81 ?  7   SER   B N    1 
ATOM   4030 N  N    B SER   B 1 7   ? 45.405 -24.016 -19.797 0.38 20.33 ?  7   SER   B N    1 
ATOM   4031 C  CA   A SER   B 1 7   ? 45.805 -25.124 -20.670 0.62 29.44 ?  7   SER   B CA   1 
ATOM   4032 C  CA   B SER   B 1 7   ? 45.355 -24.931 -20.926 0.38 21.63 ?  7   SER   B CA   1 
ATOM   4033 C  C    A SER   B 1 7   ? 45.762 -26.526 -20.085 0.62 29.02 ?  7   SER   B C    1 
ATOM   4034 C  C    B SER   B 1 7   ? 45.305 -26.362 -20.414 0.38 21.10 ?  7   SER   B C    1 
ATOM   4035 O  O    A SER   B 1 7   ? 46.387 -26.801 -19.057 0.62 29.79 ?  7   SER   B O    1 
ATOM   4036 O  O    B SER   B 1 7   ? 45.940 -26.695 -19.412 0.38 21.65 ?  7   SER   B O    1 
ATOM   4037 C  CB   A SER   B 1 7   ? 47.110 -24.954 -21.457 0.62 31.52 ?  7   SER   B CB   1 
ATOM   4038 C  CB   B SER   B 1 7   ? 46.578 -24.736 -21.838 0.38 23.05 ?  7   SER   B CB   1 
ATOM   4039 O  OG   A SER   B 1 7   ? 47.216 -25.925 -22.484 0.62 33.05 ?  7   SER   B OG   1 
ATOM   4040 O  OG   B SER   B 1 7   ? 46.430 -25.445 -23.057 0.38 23.92 ?  7   SER   B OG   1 
ATOM   4041 H  H    A SER   B 1 7   ? 46.135 -24.347 -18.893 0.62 32.19 ?  7   SER   B H    1 
ATOM   4042 H  H    B SER   B 1 7   ? 45.881 -24.309 -19.138 0.38 24.42 ?  7   SER   B H    1 
ATOM   4043 H  HA   A SER   B 1 7   ? 45.061 -25.027 -21.281 0.62 35.35 ?  7   SER   B HA   1 
ATOM   4044 H  HA   B SER   B 1 7   ? 44.562 -24.766 -21.450 0.38 25.98 ?  7   SER   B HA   1 
ATOM   4045 H  HB2  A SER   B 1 7   ? 47.123 -24.071 -21.855 0.62 37.85 ?  7   SER   B HB2  1 
ATOM   4046 H  HB2  B SER   B 1 7   ? 46.673 -23.792 -22.052 0.38 27.68 ?  7   SER   B HB2  1 
ATOM   4047 H  HB3  A SER   B 1 7   ? 47.861 -25.058 -20.853 0.62 37.85 ?  7   SER   B HB3  1 
ATOM   4048 H  HB3  B SER   B 1 7   ? 47.378 -25.045 -21.376 0.38 27.68 ?  7   SER   B HB3  1 
ATOM   4049 H  HG   A SER   B 1 7   ? 47.931 -25.818 -22.910 0.62 39.68 ?  7   SER   B HG   1 
ATOM   4050 H  HG   B SER   B 1 7   ? 47.120 -25.348 -23.534 0.38 28.73 ?  7   SER   B HG   1 
ATOM   4051 N  N    A GLY   B 1 8   ? 45.029 -27.410 -20.759 0.62 28.56 ?  8   GLY   B N    1 
ATOM   4052 N  N    B GLY   B 1 8   ? 44.537 -27.202 -21.103 0.38 20.34 ?  8   GLY   B N    1 
ATOM   4053 C  CA   A GLY   B 1 8   ? 44.991 -28.802 -20.371 0.62 27.28 ?  8   GLY   B CA   1 
ATOM   4054 C  CA   B GLY   B 1 8   ? 44.492 -28.610 -20.773 0.38 19.71 ?  8   GLY   B CA   1 
ATOM   4055 C  C    A GLY   B 1 8   ? 44.064 -29.117 -19.227 0.62 25.46 ?  8   GLY   B C    1 
ATOM   4056 C  C    B GLY   B 1 8   ? 43.623 -28.973 -19.596 0.38 18.94 ?  8   GLY   B C    1 
ATOM   4057 O  O    A GLY   B 1 8   ? 44.258 -30.140 -18.559 0.62 26.61 ?  8   GLY   B O    1 
ATOM   4058 O  O    B GLY   B 1 8   ? 43.757 -30.082 -19.066 0.38 19.70 ?  8   GLY   B O    1 
ATOM   4059 H  H    A GLY   B 1 8   ? 44.545 -27.223 -21.445 0.62 34.29 ?  8   GLY   B H    1 
ATOM   4060 H  H    B GLY   B 1 8   ? 44.047 -26.975 -21.765 0.38 24.42 ?  8   GLY   B H    1 
ATOM   4061 H  HA2  A GLY   B 1 8   ? 44.730 -29.338 -21.138 0.62 32.75 ?  8   GLY   B HA2  1 
ATOM   4062 H  HA2  B GLY   B 1 8   ? 44.136 -29.097 -21.522 0.38 23.68 ?  8   GLY   B HA2  1 
ATOM   4063 H  HA3  A GLY   B 1 8   ? 45.872 -29.080 -20.093 0.62 32.75 ?  8   GLY   B HA3  1 
ATOM   4064 H  HA3  B GLY   B 1 8   ? 45.393 -28.926 -20.600 0.38 23.68 ?  8   GLY   B HA3  1 
ATOM   4065 N  N    A TYR   B 1 9   ? 43.060 -28.280 -18.977 0.62 23.60 ?  9   TYR   B N    1 
ATOM   4066 N  N    B TYR   B 1 9   ? 42.706 -28.097 -19.193 0.38 17.82 ?  9   TYR   B N    1 
ATOM   4067 C  CA   A TYR   B 1 9   ? 42.104 -28.545 -17.914 0.62 21.43 ?  9   TYR   B CA   1 
ATOM   4068 C  CA   B TYR   B 1 9   ? 41.827 -28.394 -18.072 0.38 16.85 ?  9   TYR   B CA   1 
ATOM   4069 C  C    A TYR   B 1 9   ? 40.919 -29.341 -18.430 0.62 20.60 ?  9   TYR   B C    1 
ATOM   4070 C  C    B TYR   B 1 9   ? 40.621 -29.197 -18.529 0.38 17.21 ?  9   TYR   B C    1 
ATOM   4071 O  O    A TYR   B 1 9   ? 40.543 -29.252 -19.603 0.62 21.86 ?  9   TYR   B O    1 
ATOM   4072 O  O    B TYR   B 1 9   ? 40.105 -29.018 -19.637 0.38 18.52 ?  9   TYR   B O    1 
ATOM   4073 C  CB   A TYR   B 1 9   ? 41.619 -27.250 -17.264 0.62 21.03 ?  9   TYR   B CB   1 
ATOM   4074 C  CB   B TYR   B 1 9   ? 41.330 -27.114 -17.397 0.38 16.01 ?  9   TYR   B CB   1 
ATOM   4075 C  CG   A TYR   B 1 9   ? 42.665 -26.661 -16.348 0.62 20.25 ?  9   TYR   B CG   1 
ATOM   4076 C  CG   B TYR   B 1 9   ? 42.365 -26.471 -16.510 0.38 15.08 ?  9   TYR   B CG   1 
ATOM   4077 C  CD1  A TYR   B 1 9   ? 43.802 -26.053 -16.865 0.62 20.42 ?  9   TYR   B CD1  1 
ATOM   4078 C  CD1  B TYR   B 1 9   ? 43.397 -25.725 -17.056 0.38 14.89 ?  9   TYR   B CD1  1 
ATOM   4079 C  CD2  A TYR   B 1 9   ? 42.535 -26.740 -14.970 0.62 19.67 ?  9   TYR   B CD2  1 
ATOM   4080 C  CD2  B TYR   B 1 9   ? 42.322 -26.617 -15.131 0.38 14.77 ?  9   TYR   B CD2  1 
ATOM   4081 C  CE1  A TYR   B 1 9   ? 44.776 -25.524 -16.033 0.62 20.36 ?  9   TYR   B CE1  1 
ATOM   4082 C  CE1  B TYR   B 1 9   ? 44.360 -25.136 -16.257 0.38 14.90 ?  9   TYR   B CE1  1 
ATOM   4083 C  CE2  A TYR   B 1 9   ? 43.506 -26.216 -14.129 0.62 19.94 ?  9   TYR   B CE2  1 
ATOM   4084 C  CE2  B TYR   B 1 9   ? 43.285 -26.034 -14.320 0.38 14.93 ?  9   TYR   B CE2  1 
ATOM   4085 C  CZ   A TYR   B 1 9   ? 44.626 -25.606 -14.666 0.62 20.32 ?  9   TYR   B CZ   1 
ATOM   4086 C  CZ   B TYR   B 1 9   ? 44.301 -25.289 -14.892 0.38 15.12 ?  9   TYR   B CZ   1 
ATOM   4087 O  OH   A TYR   B 1 9   ? 45.595 -25.090 -13.836 0.62 20.52 ?  9   TYR   B OH   1 
ATOM   4088 O  OH   B TYR   B 1 9   ? 45.260 -24.704 -14.099 0.38 16.06 ?  9   TYR   B OH   1 
ATOM   4089 H  H    A TYR   B 1 9   ? 42.904 -27.550 -19.411 0.62 28.34 ?  9   TYR   B H    1 
ATOM   4090 H  H    B TYR   B 1 9   ? 42.554 -27.336 -19.562 0.38 21.40 ?  9   TYR   B H    1 
ATOM   4091 H  HA   A TYR   B 1 9   ? 42.528 -29.075 -17.232 0.62 25.74 ?  9   TYR   B HA   1 
ATOM   4092 H  HA   B TYR   B 1 9   ? 42.298 -28.910 -17.405 0.38 20.24 ?  9   TYR   B HA   1 
ATOM   4093 H  HB2  A TYR   B 1 9   ? 41.408 -26.598 -17.954 0.62 25.25 ?  9   TYR   B HB2  1 
ATOM   4094 H  HB2  B TYR   B 1 9   ? 41.060 -26.463 -18.065 0.38 19.23 ?  9   TYR   B HB2  1 
ATOM   4095 H  HB3  A TYR   B 1 9   ? 40.822 -27.440 -16.737 0.62 25.25 ?  9   TYR   B HB3  1 
ATOM   4096 H  HB3  B TYR   B 1 9   ? 40.578 -27.350 -16.838 0.38 19.23 ?  9   TYR   B HB3  1 
ATOM   4097 H  HD1  A TYR   B 1 9   ? 43.902 -26.001 -17.792 0.62 24.52 ?  9   TYR   B HD1  1 
ATOM   4098 H  HD1  B TYR   B 1 9   ? 43.439 -25.619 -17.976 0.38 17.89 ?  9   TYR   B HD1  1 
ATOM   4099 H  HD2  A TYR   B 1 9   ? 41.775 -27.152 -14.607 0.62 23.63 ?  9   TYR   B HD2  1 
ATOM   4100 H  HD2  B TYR   B 1 9   ? 41.631 -27.114 -14.740 0.38 17.75 ?  9   TYR   B HD2  1 
ATOM   4101 H  HE1  A TYR   B 1 9   ? 45.521 -25.128 -16.402 0.62 24.45 ?  9   TYR   B HE1  1 
ATOM   4102 H  HE1  B TYR   B 1 9   ? 45.042 -24.642 -16.639 0.38 17.90 ?  9   TYR   B HE1  1 
ATOM   4103 H  HE2  A TYR   B 1 9   ? 43.396 -26.278 -13.208 0.62 23.94 ?  9   TYR   B HE2  1 
ATOM   4104 H  HE2  B TYR   B 1 9   ? 43.234 -26.138 -13.394 0.38 17.93 ?  9   TYR   B HE2  1 
ATOM   4105 H  HH   A TYR   B 1 9   ? 46.207 -24.761 -14.301 0.62 24.65 ?  9   TYR   B HH   1 
ATOM   4106 H  HH   B TYR   B 1 9   ? 45.808 -24.296 -14.584 0.38 19.29 ?  9   TYR   B HH   1 
ATOM   4107 N  N    A LEU   B 1 10  ? 40.354 -30.148 -17.536 0.62 19.43 ?  10  LEU   B N    1 
ATOM   4108 N  N    B LEU   B 1 10  ? 40.171 -30.087 -17.650 0.38 16.94 ?  10  LEU   B N    1 
ATOM   4109 C  CA   A LEU   B 1 10  ? 39.158 -30.931 -17.801 0.62 19.25 ?  10  LEU   B CA   1 
ATOM   4110 C  CA   B LEU   B 1 10  ? 38.942 -30.837 -17.851 0.38 17.90 ?  10  LEU   B CA   1 
ATOM   4111 C  C    A LEU   B 1 10  ? 37.962 -30.182 -17.234 0.62 19.18 ?  10  LEU   B C    1 
ATOM   4112 C  C    B LEU   B 1 10  ? 37.777 -30.025 -17.306 0.38 18.11 ?  10  LEU   B C    1 
ATOM   4113 O  O    A LEU   B 1 10  ? 37.972 -29.779 -16.066 0.62 18.98 ?  10  LEU   B O    1 
ATOM   4114 O  O    B LEU   B 1 10  ? 37.833 -29.529 -16.176 0.38 17.33 ?  10  LEU   B O    1 
ATOM   4115 C  CB   A LEU   B 1 10  ? 39.274 -32.304 -17.135 0.62 19.96 ?  10  LEU   B CB   1 
ATOM   4116 C  CB   B LEU   B 1 10  ? 39.024 -32.175 -17.118 0.38 19.63 ?  10  LEU   B CB   1 
ATOM   4117 C  CG   A LEU   B 1 10  ? 38.141 -33.286 -17.432 0.62 21.71 ?  10  LEU   B CG   1 
ATOM   4118 C  CG   B LEU   B 1 10  ? 37.923 -33.183 -17.442 0.38 21.53 ?  10  LEU   B CG   1 
ATOM   4119 C  CD1  A LEU   B 1 10  ? 38.219 -33.770 -18.870 0.62 23.19 ?  10  LEU   B CD1  1 
ATOM   4120 C  CD1  B LEU   B 1 10  ? 38.155 -33.789 -18.818 0.38 22.65 ?  10  LEU   B CD1  1 
ATOM   4121 C  CD2  A LEU   B 1 10  ? 38.170 -34.457 -16.464 0.62 22.39 ?  10  LEU   B CD2  1 
ATOM   4122 C  CD2  B LEU   B 1 10  ? 37.842 -34.266 -16.377 0.38 21.79 ?  10  LEU   B CD2  1 
ATOM   4123 H  H    A LEU   B 1 10  ? 40.653 -30.265 -16.735 0.62 23.33 ?  10  LEU   B H    1 
ATOM   4124 H  H    B LEU   B 1 10  ? 40.566 -30.272 -16.907 0.38 20.35 ?  10  LEU   B H    1 
ATOM   4125 H  HA   A LEU   B 1 10  ? 39.034 -31.054 -18.754 0.62 23.12 ?  10  LEU   B HA   1 
ATOM   4126 H  HA   B LEU   B 1 10  ? 38.799 -30.997 -18.794 0.38 21.50 ?  10  LEU   B HA   1 
ATOM   4127 H  HB2  A LEU   B 1 10  ? 40.100 -32.721 -17.429 0.62 23.97 ?  10  LEU   B HB2  1 
ATOM   4128 H  HB2  B LEU   B 1 10  ? 39.871 -32.590 -17.340 0.38 23.57 ?  10  LEU   B HB2  1 
ATOM   4129 H  HB3  A LEU   B 1 10  ? 39.303 -32.180 -16.172 0.62 23.97 ?  10  LEU   B HB3  1 
ATOM   4130 H  HB3  B LEU   B 1 10  ? 38.988 -32.005 -16.164 0.38 23.57 ?  10  LEU   B HB3  1 
ATOM   4131 H  HG   A LEU   B 1 10  ? 37.291 -32.832 -17.318 0.62 26.08 ?  10  LEU   B HG   1 
ATOM   4132 H  HG   B LEU   B 1 10  ? 37.069 -32.724 -17.461 0.38 25.85 ?  10  LEU   B HG   1 
ATOM   4133 H  HD11 A LEU   B 1 10  ? 37.527 -34.432 -19.018 0.62 27.84 ?  10  LEU   B HD11 1 
ATOM   4134 H  HD11 B LEU   B 1 10  ? 37.465 -34.446 -18.994 0.38 27.19 ?  10  LEU   B HD11 1 
ATOM   4135 H  HD12 A LEU   B 1 10  ? 38.086 -33.014 -19.463 0.62 27.84 ?  10  LEU   B HD12 1 
ATOM   4136 H  HD12 B LEU   B 1 10  ? 38.117 -33.083 -19.483 0.38 27.19 ?  10  LEU   B HD12 1 
ATOM   4137 H  HD13 A LEU   B 1 10  ? 39.092 -34.162 -19.022 0.62 27.84 ?  10  LEU   B HD13 1 
ATOM   4138 H  HD13 B LEU   B 1 10  ? 39.028 -34.211 -18.833 0.38 27.19 ?  10  LEU   B HD13 1 
ATOM   4139 H  HD21 A LEU   B 1 10  ? 37.442 -35.060 -16.680 0.62 26.89 ?  10  LEU   B HD21 1 
ATOM   4140 H  HD21 B LEU   B 1 10  ? 37.140 -34.891 -16.615 0.38 26.17 ?  10  LEU   B HD21 1 
ATOM   4141 H  HD22 A LEU   B 1 10  ? 39.019 -34.914 -16.551 0.62 26.89 ?  10  LEU   B HD22 1 
ATOM   4142 H  HD22 B LEU   B 1 10  ? 38.694 -34.727 -16.331 0.38 26.17 ?  10  LEU   B HD22 1 
ATOM   4143 H  HD23 A LEU   B 1 10  ? 38.064 -34.119 -15.561 0.62 26.89 ?  10  LEU   B HD23 1 
ATOM   4144 H  HD23 B LEU   B 1 10  ? 37.642 -33.853 -15.522 0.38 26.17 ?  10  LEU   B HD23 1 
ATOM   4145 N  N    A LYS   B 1 11  ? 36.940 -29.997 -18.062 0.62 19.95 ?  11  LYS   B N    1 
ATOM   4146 N  N    B LYS   B 1 11  ? 36.729 -29.883 -18.114 0.38 19.22 ?  11  LYS   B N    1 
ATOM   4147 C  CA   A LYS   B 1 11  ? 35.731 -29.314 -17.635 0.62 21.73 ?  11  LYS   B CA   1 
ATOM   4148 C  CA   B LYS   B 1 11  ? 35.529 -29.157 -17.717 0.38 21.24 ?  11  LYS   B CA   1 
ATOM   4149 C  C    A LYS   B 1 11  ? 34.917 -30.234 -16.732 0.62 20.29 ?  11  LYS   B C    1 
ATOM   4150 C  C    B LYS   B 1 11  ? 34.658 -30.064 -16.855 0.38 20.09 ?  11  LYS   B C    1 
ATOM   4151 O  O    A LYS   B 1 11  ? 34.683 -31.403 -17.064 0.62 21.15 ?  11  LYS   B O    1 
ATOM   4152 O  O    B LYS   B 1 11  ? 34.127 -31.068 -17.342 0.38 19.96 ?  11  LYS   B O    1 
ATOM   4153 C  CB   A LYS   B 1 11  ? 34.917 -28.928 -18.873 0.62 25.74 ?  11  LYS   B CB   1 
ATOM   4154 C  CB   B LYS   B 1 11  ? 34.770 -28.731 -18.970 0.38 24.55 ?  11  LYS   B CB   1 
ATOM   4155 C  CG   A LYS   B 1 11  ? 33.889 -27.822 -18.669 0.62 29.28 ?  11  LYS   B CG   1 
ATOM   4156 C  CG   B LYS   B 1 11  ? 33.676 -27.711 -18.733 0.38 27.55 ?  11  LYS   B CG   1 
ATOM   4157 C  CD   A LYS   B 1 11  ? 33.173 -27.506 -19.982 0.62 31.94 ?  11  LYS   B CD   1 
ATOM   4158 C  CD   B LYS   B 1 11  ? 32.951 -27.391 -20.031 0.38 29.83 ?  11  LYS   B CD   1 
ATOM   4159 C  CE   A LYS   B 1 11  ? 32.150 -26.390 -19.826 0.62 33.84 ?  11  LYS   B CE   1 
ATOM   4160 C  CE   B LYS   B 1 11  ? 31.955 -26.262 -19.846 0.38 31.42 ?  11  LYS   B CE   1 
ATOM   4161 N  NZ   A LYS   B 1 11  ? 32.787 -25.070 -19.570 0.62 34.89 ?  11  LYS   B NZ   1 
ATOM   4162 N  NZ   B LYS   B 1 11  ? 32.632 -24.983 -19.496 0.38 32.30 ?  11  LYS   B NZ   1 
ATOM   4163 H  H    A LYS   B 1 11  ? 36.916 -30.270 -18.875 0.62 23.96 ?  11  LYS   B H    1 
ATOM   4164 H  H    B LYS   B 1 11  ? 36.690 -30.195 -18.918 0.38 23.08 ?  11  LYS   B H    1 
ATOM   4165 H  HA   A LYS   B 1 11  ? 35.956 -28.508 -17.145 0.62 26.10 ?  11  LYS   B HA   1 
ATOM   4166 H  HA   B LYS   B 1 11  ? 35.771 -28.367 -17.208 0.38 25.51 ?  11  LYS   B HA   1 
ATOM   4167 H  HB2  A LYS   B 1 11  ? 35.531 -28.623 -19.562 0.62 30.91 ?  11  LYS   B HB2  1 
ATOM   4168 H  HB2  B LYS   B 1 11  ? 35.399 -28.348 -19.598 0.38 29.49 ?  11  LYS   B HB2  1 
ATOM   4169 H  HB3  A LYS   B 1 11  ? 34.439 -29.709 -19.190 0.62 30.91 ?  11  LYS   B HB3  1 
ATOM   4170 H  HB3  B LYS   B 1 11  ? 34.357 -29.518 -19.362 0.38 29.49 ?  11  LYS   B HB3  1 
ATOM   4171 H  HG2  A LYS   B 1 11  ? 33.226 -28.110 -18.023 0.62 35.15 ?  11  LYS   B HG2  1 
ATOM   4172 H  HG2  B LYS   B 1 11  ? 33.031 -28.069 -18.104 0.38 33.09 ?  11  LYS   B HG2  1 
ATOM   4173 H  HG3  A LYS   B 1 11  ? 34.333 -27.015 -18.364 0.62 35.15 ?  11  LYS   B HG3  1 
ATOM   4174 H  HG3  B LYS   B 1 11  ? 34.069 -26.894 -18.390 0.38 33.09 ?  11  LYS   B HG3  1 
ATOM   4175 H  HD2  A LYS   B 1 11  ? 33.827 -27.225 -20.643 0.62 38.35 ?  11  LYS   B HD2  1 
ATOM   4176 H  HD2  B LYS   B 1 11  ? 33.600 -27.119 -20.700 0.38 35.82 ?  11  LYS   B HD2  1 
ATOM   4177 H  HD3  A LYS   B 1 11  ? 32.709 -28.300 -20.292 0.62 38.35 ?  11  LYS   B HD3  1 
ATOM   4178 H  HD3  B LYS   B 1 11  ? 32.470 -28.178 -20.331 0.38 35.82 ?  11  LYS   B HD3  1 
ATOM   4179 H  HE2  A LYS   B 1 11  ? 31.628 -26.320 -20.642 0.62 40.62 ?  11  LYS   B HE2  1 
ATOM   4180 H  HE2  B LYS   B 1 11  ? 31.465 -26.129 -20.672 0.38 37.72 ?  11  LYS   B HE2  1 
ATOM   4181 H  HE3  A LYS   B 1 11  ? 31.569 -26.596 -19.078 0.62 40.62 ?  11  LYS   B HE3  1 
ATOM   4182 H  HE3  B LYS   B 1 11  ? 31.345 -26.492 -19.127 0.38 37.72 ?  11  LYS   B HE3  1 
ATOM   4183 H  HZ1  A LYS   B 1 11  ? 32.162 -24.441 -19.488 0.62 41.88 ?  11  LYS   B HZ1  1 
ATOM   4184 H  HZ1  B LYS   B 1 11  ? 32.036 -24.325 -19.455 0.38 38.78 ?  11  LYS   B HZ1  1 
ATOM   4185 H  HZ2  A LYS   B 1 11  ? 33.265 -25.103 -18.821 0.62 41.88 ?  11  LYS   B HZ2  1 
ATOM   4186 H  HZ2  B LYS   B 1 11  ? 33.036 -25.059 -18.706 0.38 38.78 ?  11  LYS   B HZ2  1 
ATOM   4187 H  HZ3  A LYS   B 1 11  ? 33.324 -24.855 -20.247 0.62 41.88 ?  11  LYS   B HZ3  1 
ATOM   4188 H  HZ3  B LYS   B 1 11  ? 33.241 -24.784 -20.114 0.38 38.78 ?  11  LYS   B HZ3  1 
ATOM   4189 N  N    . LEU   B 1 12  ? 34.499 -29.712 -15.578 1.00 18.88 ?  12  LEU   B N    1 
ATOM   4190 C  CA   . LEU   B 1 12  ? 33.552 -30.410 -14.712 1.00 18.31 ?  12  LEU   B CA   1 
ATOM   4191 C  C    . LEU   B 1 12  ? 32.172 -29.786 -14.793 1.00 18.23 ?  12  LEU   B C    1 
ATOM   4192 O  O    . LEU   B 1 12  ? 31.177 -30.492 -14.967 1.00 19.20 ?  12  LEU   B O    1 
ATOM   4193 C  CB   . LEU   B 1 12  ? 34.029 -30.430 -13.257 1.00 17.58 ?  12  LEU   B CB   1 
ATOM   4194 C  CG   . LEU   B 1 12  ? 35.365 -31.118 -13.010 1.00 17.52 ?  12  LEU   B CG   1 
ATOM   4195 C  CD1  . LEU   B 1 12  ? 35.754 -31.052 -11.539 1.00 17.71 ?  12  LEU   B CD1  1 
ATOM   4196 C  CD2  . LEU   B 1 12  ? 35.346 -32.556 -13.503 1.00 18.12 ?  12  LEU   B CD2  1 
ATOM   4197 H  H    A LEU   B 1 12  ? 34.753 -28.944 -15.272 0.62 22.68 ?  12  LEU   B H    1 
ATOM   4198 H  H    B LEU   B 1 12  ? 34.922 -29.066 -15.194 0.38 22.68 ?  12  LEU   B H    1 
ATOM   4199 H  HA   . LEU   B 1 12  ? 33.468 -31.323 -15.011 1.00 21.99 ?  12  LEU   B HA   1 
ATOM   4200 H  HB2  . LEU   B 1 12  ? 34.104 -29.519 -12.943 1.00 21.12 ?  12  LEU   B HB2  1 
ATOM   4201 H  HB3  . LEU   B 1 12  ? 33.360 -30.900 -12.727 1.00 21.12 ?  12  LEU   B HB3  1 
ATOM   4202 H  HG   . LEU   B 1 12  ? 36.048 -30.645 -13.509 1.00 21.05 ?  12  LEU   B HG   1 
ATOM   4203 H  HD11 . LEU   B 1 12  ? 36.613 -31.493 -11.417 1.00 21.27 ?  12  LEU   B HD11 1 
ATOM   4204 H  HD12 . LEU   B 1 12  ? 35.823 -30.122 -11.267 1.00 21.27 ?  12  LEU   B HD12 1 
ATOM   4205 H  HD13 . LEU   B 1 12  ? 35.078 -31.501 -11.008 1.00 21.27 ?  12  LEU   B HD13 1 
ATOM   4206 H  HD21 . LEU   B 1 12  ? 36.149 -33.005 -13.201 1.00 21.76 ?  12  LEU   B HD21 1 
ATOM   4207 H  HD22 . LEU   B 1 12  ? 34.562 -33.001 -13.146 1.00 21.76 ?  12  LEU   B HD22 1 
ATOM   4208 H  HD23 . LEU   B 1 12  ? 35.312 -32.554 -14.473 1.00 21.76 ?  12  LEU   B HD23 1 
ATOM   4209 N  N    A THR   B 1 13  ? 32.096 -28.469 -14.653 0.62 18.10 ?  13  THR   B N    1 
ATOM   4210 N  N    B THR   B 1 13  ? 32.096 -28.461 -14.673 0.38 18.48 ?  13  THR   B N    1 
ATOM   4211 C  CA   A THR   B 1 13  ? 30.879 -27.710 -14.865 0.62 18.07 ?  13  THR   B CA   1 
ATOM   4212 C  CA   B THR   B 1 13  ? 30.870 -27.703 -14.884 0.38 18.83 ?  13  THR   B CA   1 
ATOM   4213 C  C    A THR   B 1 13  ? 31.232 -26.542 -15.773 0.62 20.26 ?  13  THR   B C    1 
ATOM   4214 C  C    B THR   B 1 13  ? 31.197 -26.523 -15.794 0.38 20.53 ?  13  THR   B C    1 
ATOM   4215 O  O    A THR   B 1 13  ? 32.387 -26.367 -16.175 0.62 21.53 ?  13  THR   B O    1 
ATOM   4216 O  O    B THR   B 1 13  ? 32.334 -26.358 -16.247 0.38 21.31 ?  13  THR   B O    1 
ATOM   4217 C  CB   A THR   B 1 13  ? 30.284 -27.201 -13.548 0.62 17.40 ?  13  THR   B CB   1 
ATOM   4218 C  CB   B THR   B 1 13  ? 30.276 -27.206 -13.558 0.38 18.35 ?  13  THR   B CB   1 
ATOM   4219 O  OG1  A THR   B 1 13  ? 31.141 -26.186 -13.010 0.62 16.94 ?  13  THR   B OG1  1 
ATOM   4220 O  OG1  B THR   B 1 13  ? 31.128 -26.195 -13.008 0.38 18.04 ?  13  THR   B OG1  1 
ATOM   4221 C  CG2  A THR   B 1 13  ? 30.139 -28.332 -12.549 0.62 17.55 ?  13  THR   B CG2  1 
ATOM   4222 C  CG2  B THR   B 1 13  ? 30.140 -28.344 -12.553 0.38 18.39 ?  13  THR   B CG2  1 
ATOM   4223 H  H    A THR   B 1 13  ? 32.769 -27.973 -14.438 0.62 21.74 ?  13  THR   B H    1 
ATOM   4224 H  H    B THR   B 1 13  ? 32.768 -27.960 -14.464 0.38 22.19 ?  13  THR   B H    1 
ATOM   4225 H  HA   A THR   B 1 13  ? 30.223 -28.265 -15.302 0.62 21.71 ?  13  THR   B HA   1 
ATOM   4226 H  HA   B THR   B 1 13  ? 30.212 -28.263 -15.324 0.38 22.62 ?  13  THR   B HA   1 
ATOM   4227 H  HB   A THR   B 1 13  ? 29.401 -26.825 -13.712 0.62 20.90 ?  13  THR   B HB   1 
ATOM   4228 H  HB   B THR   B 1 13  ? 29.394 -26.829 -13.720 0.38 22.04 ?  13  THR   B HB   1 
ATOM   4229 H  HG1  A THR   B 1 13  ? 30.934 -25.430 -13.332 0.62 20.35 ?  13  THR   B HG1  1 
ATOM   4230 H  HG1  B THR   B 1 13  ? 30.888 -25.436 -13.283 0.38 21.67 ?  13  THR   B HG1  1 
ATOM   4231 H  HG21 A THR   B 1 13  ? 29.664 -28.021 -11.763 0.62 21.08 ?  13  THR   B HG21 1 
ATOM   4232 H  HG21 B THR   B 1 13  ? 29.675 -28.032 -11.759 0.38 22.09 ?  13  THR   B HG21 1 
ATOM   4233 H  HG22 A THR   B 1 13  ? 29.639 -29.059 -12.952 0.62 21.08 ?  13  THR   B HG22 1 
ATOM   4234 H  HG22 B THR   B 1 13  ? 29.636 -29.073 -12.945 0.38 22.09 ?  13  THR   B HG22 1 
ATOM   4235 H  HG23 A THR   B 1 13  ? 31.012 -28.654 -12.287 0.62 21.08 ?  13  THR   B HG23 1 
ATOM   4236 H  HG23 B THR   B 1 13  ? 31.017 -28.667 -12.297 0.38 22.09 ?  13  THR   B HG23 1 
ATOM   4237 N  N    A ASP   B 1 14  ? 30.233 -25.719 -16.082 0.62 21.55 ?  14  ASP   B N    1 
ATOM   4238 N  N    B ASP   B 1 14  ? 30.196 -25.682 -16.055 0.38 21.64 ?  14  ASP   B N    1 
ATOM   4239 C  CA   A ASP   B 1 14  ? 30.488 -24.575 -16.947 0.62 23.24 ?  14  ASP   B CA   1 
ATOM   4240 C  CA   B ASP   B 1 14  ? 30.411 -24.531 -16.926 0.38 22.88 ?  14  ASP   B CA   1 
ATOM   4241 C  C    A ASP   B 1 14  ? 31.600 -23.688 -16.399 0.62 21.13 ?  14  ASP   B C    1 
ATOM   4242 C  C    B ASP   B 1 14  ? 31.406 -23.528 -16.360 0.38 20.67 ?  14  ASP   B C    1 
ATOM   4243 O  O    A ASP   B 1 14  ? 32.345 -23.081 -17.180 0.62 22.02 ?  14  ASP   B O    1 
ATOM   4244 O  O    B ASP   B 1 14  ? 31.830 -22.633 -17.099 0.38 20.69 ?  14  ASP   B O    1 
ATOM   4245 C  CB   A ASP   B 1 14  ? 29.201 -23.781 -17.174 0.62 27.18 ?  14  ASP   B CB   1 
ATOM   4246 C  CB   B ASP   B 1 14  ? 29.097 -23.800 -17.191 0.38 26.31 ?  14  ASP   B CB   1 
ATOM   4247 C  CG   A ASP   B 1 14  ? 28.200 -24.525 -18.029 0.62 30.89 ?  14  ASP   B CG   1 
ATOM   4248 C  CG   B ASP   B 1 14  ? 28.213 -24.532 -18.179 0.38 29.41 ?  14  ASP   B CG   1 
ATOM   4249 O  OD1  A ASP   B 1 14  ? 28.595 -25.467 -18.753 0.62 31.96 ?  14  ASP   B OD1  1 
ATOM   4250 O  OD1  B ASP   B 1 14  ? 28.754 -25.252 -19.046 0.38 30.42 ?  14  ASP   B OD1  1 
ATOM   4251 O  OD2  A ASP   B 1 14  ? 27.008 -24.164 -17.971 0.62 32.47 -1 14  ASP   B OD2  1 
ATOM   4252 O  OD2  B ASP   B 1 14  ? 26.976 -24.389 -18.091 0.38 30.60 -1 14  ASP   B OD2  1 
ATOM   4253 H  H    A ASP   B 1 14  ? 29.431 -25.788 -15.793 0.62 25.88 ?  14  ASP   B H    1 
ATOM   4254 H  H    B ASP   B 1 14  ? 29.399 -25.750 -15.746 0.38 25.99 ?  14  ASP   B H    1 
ATOM   4255 H  HA   A ASP   B 1 14  ? 30.786 -24.892 -17.808 0.62 27.90 ?  14  ASP   B HA   1 
ATOM   4256 H  HA   B ASP   B 1 14  ? 30.751 -24.849 -17.777 0.38 27.47 ?  14  ASP   B HA   1 
ATOM   4257 H  HB2  A ASP   B 1 14  ? 28.760 -23.620 -16.329 0.62 32.64 ?  14  ASP   B HB2  1 
ATOM   4258 H  HB2  B ASP   B 1 14  ? 28.614 -23.713 -16.356 0.38 31.59 ?  14  ASP   B HB2  1 
ATOM   4259 H  HB3  A ASP   B 1 14  ? 29.407 -22.940 -17.612 0.62 32.64 ?  14  ASP   B HB3  1 
ATOM   4260 H  HB3  B ASP   B 1 14  ? 29.298 -22.917 -17.550 0.38 31.59 ?  14  ASP   B HB3  1 
ATOM   4261 N  N    . ASN   B 1 15  ? 31.757 -23.623 -15.073 1.00 18.97 ?  15  ASN   B N    1 
ATOM   4262 C  CA   . ASN   B 1 15  ? 32.726 -22.712 -14.464 1.00 16.77 ?  15  ASN   B CA   1 
ATOM   4263 C  C    . ASN   B 1 15  ? 33.820 -23.373 -13.633 1.00 15.35 ?  15  ASN   B C    1 
ATOM   4264 O  O    . ASN   B 1 15  ? 34.704 -22.656 -13.145 1.00 15.53 ?  15  ASN   B O    1 
ATOM   4265 C  CB   . ASN   B 1 15  ? 32.026 -21.658 -13.592 1.00 17.06 ?  15  ASN   B CB   1 
ATOM   4266 C  CG   . ASN   B 1 15  ? 31.411 -22.258 -12.343 1.00 16.94 ?  15  ASN   B CG   1 
ATOM   4267 O  OD1  . ASN   B 1 15  ? 30.454 -23.032 -12.423 1.00 18.87 ?  15  ASN   B OD1  1 
ATOM   4268 N  ND2  . ASN   B 1 15  ? 31.955 -21.926 -11.191 1.00 15.93 ?  15  ASN   B ND2  1 
ATOM   4269 H  H    A ASN   B 1 15  ? 31.312 -24.095 -14.510 0.62 22.78 ?  15  ASN   B H    1 
ATOM   4270 H  H    B ASN   B 1 15  ? 31.403 -24.176 -14.522 0.38 22.78 ?  15  ASN   B H    1 
ATOM   4271 H  HA   . ASN   B 1 15  ? 33.171 -22.224 -15.166 1.00 20.15 ?  15  ASN   B HA   1 
ATOM   4272 H  HB2  . ASN   B 1 15  ? 32.676 -20.985 -13.317 1.00 20.49 ?  15  ASN   B HB2  1 
ATOM   4273 H  HB3  . ASN   B 1 15  ? 31.317 -21.229 -14.104 1.00 20.49 ?  15  ASN   B HB3  1 
ATOM   4274 H  HD21 . ASN   B 1 15  ? 31.640 -22.238 -10.454 1.00 19.14 ?  15  ASN   B HD21 1 
ATOM   4275 H  HD22 . ASN   B 1 15  ? 32.633 -21.387 -11.167 1.00 19.14 ?  15  ASN   B HD22 1 
ATOM   4276 N  N    . VAL   B 1 16  ? 33.792 -24.691 -13.437 1.00 15.33 ?  16  VAL   B N    1 
ATOM   4277 C  CA   . VAL   B 1 16  ? 34.802 -25.388 -12.645 1.00 14.77 ?  16  VAL   B CA   1 
ATOM   4278 C  C    . VAL   B 1 16  ? 35.582 -26.325 -13.551 1.00 14.98 ?  16  VAL   B C    1 
ATOM   4279 O  O    . VAL   B 1 16  ? 35.000 -27.203 -14.208 1.00 15.67 ?  16  VAL   B O    1 
ATOM   4280 C  CB   . VAL   B 1 16  ? 34.189 -26.162 -11.466 1.00 14.77 ?  16  VAL   B CB   1 
ATOM   4281 C  CG1  . VAL   B 1 16  ? 35.280 -26.919 -10.700 1.00 15.07 ?  16  VAL   B CG1  1 
ATOM   4282 C  CG2  . VAL   B 1 16  ? 33.401 -25.221 -10.552 1.00 15.77 ?  16  VAL   B CG2  1 
ATOM   4283 H  H    . VAL   B 1 16  ? 33.172 -25.213 -13.749 1.00 18.41 ?  16  VAL   B H    1 
ATOM   4284 H  HA   . VAL   B 1 16  ? 35.414 -24.736 -12.280 1.00 17.75 ?  16  VAL   B HA   1 
ATOM   4285 H  HB   . VAL   B 1 16  ? 33.565 -26.821 -11.815 1.00 17.75 ?  16  VAL   B HB   1 
ATOM   4286 H  HG11 . VAL   B 1 16  ? 34.916 -27.219 -9.851  1.00 18.11 ?  16  VAL   B HG11 1 
ATOM   4287 H  HG12 . VAL   B 1 16  ? 35.564 -27.683 -11.223 1.00 18.11 ?  16  VAL   B HG12 1 
ATOM   4288 H  HG13 . VAL   B 1 16  ? 36.026 -26.321 -10.545 1.00 18.11 ?  16  VAL   B HG13 1 
ATOM   4289 H  HG21 . VAL   B 1 16  ? 33.069 -25.728 -9.789  1.00 18.95 ?  16  VAL   B HG21 1 
ATOM   4290 H  HG22 . VAL   B 1 16  ? 33.982 -24.512 -10.248 1.00 18.95 ?  16  VAL   B HG22 1 
ATOM   4291 H  HG23 . VAL   B 1 16  ? 32.652 -24.851 -11.047 1.00 18.95 ?  16  VAL   B HG23 1 
ATOM   4292 N  N    . TYR   B 1 17  ? 36.899 -26.165 -13.534 1.00 15.11 ?  17  TYR   B N    1 
ATOM   4293 C  CA   . TYR   B 1 17  ? 37.836 -26.906 -14.358 1.00 15.55 ?  17  TYR   B CA   1 
ATOM   4294 C  C    . TYR   B 1 17  ? 38.895 -27.528 -13.458 1.00 14.67 ?  17  TYR   B C    1 
ATOM   4295 O  O    . TYR   B 1 17  ? 39.201 -26.998 -12.386 1.00 14.80 ?  17  TYR   B O    1 
ATOM   4296 C  CB   . TYR   B 1 17  ? 38.534 -25.963 -15.350 1.00 19.54 ?  17  TYR   B CB   1 
ATOM   4297 C  CG   . TYR   B 1 17  ? 37.611 -25.192 -16.265 1.00 23.58 ?  17  TYR   B CG   1 
ATOM   4298 C  CD1  . TYR   B 1 17  ? 37.058 -23.979 -15.876 1.00 26.05 ?  17  TYR   B CD1  1 
ATOM   4299 C  CD2  . TYR   B 1 17  ? 37.301 -25.679 -17.528 1.00 26.23 ?  17  TYR   B CD2  1 
ATOM   4300 C  CE1  . TYR   B 1 17  ? 36.214 -23.272 -16.718 1.00 28.23 ?  17  TYR   B CE1  1 
ATOM   4301 C  CE2  . TYR   B 1 17  ? 36.462 -24.982 -18.377 1.00 28.30 ?  17  TYR   B CE2  1 
ATOM   4302 C  CZ   . TYR   B 1 17  ? 35.918 -23.779 -17.967 1.00 29.68 ?  17  TYR   B CZ   1 
ATOM   4303 O  OH   . TYR   B 1 17  ? 35.083 -23.080 -18.808 1.00 31.03 ?  17  TYR   B OH   1 
ATOM   4304 H  H    . TYR   B 1 17  ? 37.300 -25.591 -13.024 1.00 18.15 ?  17  TYR   B H    1 
ATOM   4305 H  HA   . TYR   B 1 17  ? 37.368 -27.601 -14.852 1.00 18.68 ?  17  TYR   B HA   1 
ATOM   4306 H  HB2  . TYR   B 1 17  ? 39.071 -25.325 -14.858 1.00 23.46 ?  17  TYR   B HB2  1 
ATOM   4307 H  HB3  . TYR   B 1 17  ? 39.097 -26.498 -15.917 1.00 23.46 ?  17  TYR   B HB3  1 
ATOM   4308 H  HD1  . TYR   B 1 17  ? 37.256 -23.635 -15.037 1.00 31.29 ?  17  TYR   B HD1  1 
ATOM   4309 H  HD2  . TYR   B 1 17  ? 37.660 -26.489 -17.809 1.00 31.50 ?  17  TYR   B HD2  1 
ATOM   4310 H  HE1  . TYR   B 1 17  ? 35.851 -22.460 -16.445 1.00 33.89 ?  17  TYR   B HE1  1 
ATOM   4311 H  HE2  . TYR   B 1 17  ? 36.257 -25.322 -19.221 1.00 33.98 ?  17  TYR   B HE2  1 
ATOM   4312 H  HH   . TYR   B 1 17  ? 34.832 -22.370 -18.435 1.00 37.26 ?  17  TYR   B HH   1 
ATOM   4313 N  N    . ILE   B 1 18  ? 39.486 -28.637 -13.901 1.00 14.89 ?  18  ILE   B N    1 
ATOM   4314 C  CA   . ILE   B 1 18  ? 40.419 -29.372 -13.054 1.00 14.98 ?  18  ILE   B CA   1 
ATOM   4315 C  C    . ILE   B 1 18  ? 41.567 -29.922 -13.888 1.00 15.50 ?  18  ILE   B C    1 
ATOM   4316 O  O    . ILE   B 1 18  ? 41.396 -30.298 -15.052 1.00 16.52 ?  18  ILE   B O    1 
ATOM   4317 C  CB   . ILE   B 1 18  ? 39.683 -30.480 -12.253 1.00 15.39 ?  18  ILE   B CB   1 
ATOM   4318 C  CG1  . ILE   B 1 18  ? 40.549 -31.026 -11.112 1.00 15.84 ?  18  ILE   B CG1  1 
ATOM   4319 C  CG2  . ILE   B 1 18  ? 39.178 -31.597 -13.179 1.00 15.46 ?  18  ILE   B CG2  1 
ATOM   4320 C  CD1  . ILE   B 1 18  ? 39.761 -31.847 -10.096 1.00 17.33 ?  18  ILE   B CD1  1 
ATOM   4321 H  H    . ILE   B 1 18  ? 39.368 -28.973 -14.681 1.00 17.88 ?  18  ILE   B H    1 
ATOM   4322 H  HA   . ILE   B 1 18  ? 40.792 -28.756 -12.403 1.00 18.00 ?  18  ILE   B HA   1 
ATOM   4323 H  HB   . ILE   B 1 18  ? 38.900 -30.079 -11.846 1.00 18.49 ?  18  ILE   B HB   1 
ATOM   4324 H  HG12 . ILE   B 1 18  ? 41.239 -31.593 -11.480 1.00 19.03 ?  18  ILE   B HG12 1 
ATOM   4325 H  HG13 . ILE   B 1 18  ? 40.948 -30.278 -10.639 1.00 19.03 ?  18  ILE   B HG13 1 
ATOM   4326 H  HG21 . ILE   B 1 18  ? 38.598 -32.190 -12.674 1.00 18.57 ?  18  ILE   B HG21 1 
ATOM   4327 H  HG22 . ILE   B 1 18  ? 38.680 -31.194 -13.910 1.00 18.57 ?  18  ILE   B HG22 1 
ATOM   4328 H  HG23 . ILE   B 1 18  ? 39.935 -32.089 -13.527 1.00 18.57 ?  18  ILE   B HG23 1 
ATOM   4329 H  HD11 . ILE   B 1 18  ? 40.359 -32.124 -9.383  1.00 20.82 ?  18  ILE   B HD11 1 
ATOM   4330 H  HD12 . ILE   B 1 18  ? 39.046 -31.301 -9.733  1.00 20.82 ?  18  ILE   B HD12 1 
ATOM   4331 H  HD13 . ILE   B 1 18  ? 39.391 -32.626 -10.539 1.00 20.82 ?  18  ILE   B HD13 1 
ATOM   4332 N  N    A LYS   B 1 19  ? 42.751 -29.976 -13.271 0.62 15.66 ?  19  LYS   B N    1 
ATOM   4333 N  N    B LYS   B 1 19  ? 42.748 -29.964 -13.282 0.38 16.05 ?  19  LYS   B N    1 
ATOM   4334 C  CA   A LYS   B 1 19  ? 43.959 -30.460 -13.927 0.62 16.78 ?  19  LYS   B CA   1 
ATOM   4335 C  CA   B LYS   B 1 19  ? 43.937 -30.423 -13.978 0.38 17.10 ?  19  LYS   B CA   1 
ATOM   4336 C  C    A LYS   B 1 19  ? 44.857 -31.141 -12.901 0.62 16.47 ?  19  LYS   B C    1 
ATOM   4337 C  C    B LYS   B 1 19  ? 44.866 -31.083 -12.974 0.38 16.57 ?  19  LYS   B C    1 
ATOM   4338 O  O    A LYS   B 1 19  ? 44.918 -30.738 -11.737 0.62 15.95 ?  19  LYS   B O    1 
ATOM   4339 O  O    B LYS   B 1 19  ? 45.009 -30.611 -11.843 0.38 15.88 ?  19  LYS   B O    1 
ATOM   4340 C  CB   A LYS   B 1 19  ? 44.726 -29.308 -14.591 0.62 18.65 ?  19  LYS   B CB   1 
ATOM   4341 C  CB   B LYS   B 1 19  ? 44.662 -29.249 -14.644 0.38 18.83 ?  19  LYS   B CB   1 
ATOM   4342 C  CG   A LYS   B 1 19  ? 45.930 -29.732 -15.415 0.62 20.98 ?  19  LYS   B CG   1 
ATOM   4343 C  CG   B LYS   B 1 19  ? 45.841 -29.650 -15.511 0.38 20.81 ?  19  LYS   B CG   1 
ATOM   4344 C  CD   A LYS   B 1 19  ? 46.694 -28.516 -15.923 0.62 23.28 ?  19  LYS   B CD   1 
ATOM   4345 C  CD   B LYS   B 1 19  ? 46.531 -28.425 -16.085 0.38 22.61 ?  19  LYS   B CD   1 
ATOM   4346 C  CE   A LYS   B 1 19  ? 47.894 -28.908 -16.767 0.62 25.44 ?  19  LYS   B CE   1 
ATOM   4347 C  CE   B LYS   B 1 19  ? 47.750 -28.802 -16.906 0.38 24.20 ?  19  LYS   B CE   1 
ATOM   4348 N  NZ   A LYS   B 1 19  ? 48.634 -27.717 -17.262 0.62 26.63 ?  19  LYS   B NZ   1 
ATOM   4349 N  NZ   B LYS   B 1 19  ? 48.434 -27.601 -17.455 0.38 25.12 ?  19  LYS   B NZ   1 
ATOM   4350 H  H    A LYS   B 1 19  ? 42.866 -29.735 -12.454 0.62 18.81 ?  19  LYS   B H    1 
ATOM   4351 H  H    B LYS   B 1 19  ? 42.876 -29.733 -12.464 0.38 19.28 ?  19  LYS   B H    1 
ATOM   4352 H  HA   A LYS   B 1 19  ? 43.710 -31.109 -14.606 0.62 20.15 ?  19  LYS   B HA   1 
ATOM   4353 H  HA   B LYS   B 1 19  ? 43.684 -31.073 -14.657 0.38 20.53 ?  19  LYS   B HA   1 
ATOM   4354 H  HB2  A LYS   B 1 19  ? 44.116 -28.847 -15.186 0.62 22.40 ?  19  LYS   B HB2  1 
ATOM   4355 H  HB2  B LYS   B 1 19  ? 44.028 -28.776 -15.203 0.38 22.62 ?  19  LYS   B HB2  1 
ATOM   4356 H  HB3  A LYS   B 1 19  ? 45.029 -28.704 -13.897 0.62 22.40 ?  19  LYS   B HB3  1 
ATOM   4357 H  HB3  B LYS   B 1 19  ? 44.989 -28.660 -13.947 0.38 22.62 ?  19  LYS   B HB3  1 
ATOM   4358 H  HG2  A LYS   B 1 19  ? 46.521 -30.263 -14.863 0.62 25.19 ?  19  LYS   B HG2  1 
ATOM   4359 H  HG2  B LYS   B 1 19  ? 46.480 -30.142 -14.975 0.38 25.00 ?  19  LYS   B HG2  1 
ATOM   4360 H  HG3  A LYS   B 1 19  ? 45.623 -30.248 -16.178 0.62 25.19 ?  19  LYS   B HG3  1 
ATOM   4361 H  HG3  B LYS   B 1 19  ? 45.522 -30.198 -16.246 0.38 25.00 ?  19  LYS   B HG3  1 
ATOM   4362 H  HD2  A LYS   B 1 19  ? 46.102 -27.975 -16.469 0.62 27.95 ?  19  LYS   B HD2  1 
ATOM   4363 H  HD2  B LYS   B 1 19  ? 45.912 -27.948 -16.660 0.38 27.15 ?  19  LYS   B HD2  1 
ATOM   4364 H  HD3  A LYS   B 1 19  ? 47.010 -28.001 -15.163 0.62 27.95 ?  19  LYS   B HD3  1 
ATOM   4365 H  HD3  B LYS   B 1 19  ? 46.820 -27.851 -15.357 0.38 27.15 ?  19  LYS   B HD3  1 
ATOM   4366 H  HE2  A LYS   B 1 19  ? 48.499 -29.443 -16.229 0.62 30.55 ?  19  LYS   B HE2  1 
ATOM   4367 H  HE2  B LYS   B 1 19  ? 48.379 -29.283 -16.343 0.38 29.06 ?  19  LYS   B HE2  1 
ATOM   4368 H  HE3  A LYS   B 1 19  ? 47.589 -29.419 -17.534 0.62 30.55 ?  19  LYS   B HE3  1 
ATOM   4369 H  HE3  B LYS   B 1 19  ? 47.474 -29.363 -17.649 0.38 29.06 ?  19  LYS   B HE3  1 
ATOM   4370 H  HZ1  A LYS   B 1 19  ? 49.280 -27.970 -17.819 0.62 31.98 ?  19  LYS   B HZ1  1 
ATOM   4371 H  HZ1  B LYS   B 1 19  ? 49.142 -27.848 -17.936 0.38 30.17 ?  19  LYS   B HZ1  1 
ATOM   4372 H  HZ2  A LYS   B 1 19  ? 48.078 -27.170 -17.693 0.62 31.98 ?  19  LYS   B HZ2  1 
ATOM   4373 H  HZ2  B LYS   B 1 19  ? 47.876 -27.145 -17.975 0.38 30.17 ?  19  LYS   B HZ2  1 
ATOM   4374 H  HZ3  A LYS   B 1 19  ? 48.997 -27.278 -16.578 0.62 31.98 ?  19  LYS   B HZ3  1 
ATOM   4375 H  HZ3  B LYS   B 1 19  ? 48.706 -27.076 -16.790 0.38 30.17 ?  19  LYS   B HZ3  1 
ATOM   4376 N  N    A ASN   B 1 20  ? 45.562 -32.178 -13.345 0.62 17.92 ?  20  ASN   B N    1 
ATOM   4377 N  N    B ASN   B 1 20  ? 45.503 -32.167 -13.398 0.38 17.14 ?  20  ASN   B N    1 
ATOM   4378 C  CA   A ASN   B 1 20  ? 46.571 -32.846 -12.521 0.62 19.20 ?  20  ASN   B CA   1 
ATOM   4379 C  CA   B ASN   B 1 20  ? 46.566 -32.778 -12.613 0.38 17.50 ?  20  ASN   B CA   1 
ATOM   4380 C  C    A ASN   B 1 20  ? 47.890 -32.094 -12.678 0.62 20.06 ?  20  ASN   B C    1 
ATOM   4381 C  C    B ASN   B 1 20  ? 47.805 -31.914 -12.817 0.38 16.91 ?  20  ASN   B C    1 
ATOM   4382 O  O    A ASN   B 1 20  ? 48.640 -32.328 -13.631 0.62 21.63 ?  20  ASN   B O    1 
ATOM   4383 O  O    B ASN   B 1 20  ? 48.342 -31.843 -13.928 0.38 16.45 ?  20  ASN   B O    1 
ATOM   4384 C  CB   A ASN   B 1 20  ? 46.702 -34.306 -12.947 0.62 21.08 ?  20  ASN   B CB   1 
ATOM   4385 C  CB   B ASN   B 1 20  ? 46.772 -34.220 -13.078 0.38 19.42 ?  20  ASN   B CB   1 
ATOM   4386 C  CG   A ASN   B 1 20  ? 47.852 -35.032 -12.261 0.62 22.69 ?  20  ASN   B CG   1 
ATOM   4387 C  CG   B ASN   B 1 20  ? 47.944 -34.910 -12.391 0.38 21.14 ?  20  ASN   B CG   1 
ATOM   4388 O  OD1  A ASN   B 1 20  ? 48.495 -35.896 -12.866 0.62 24.43 ?  20  ASN   B OD1  1 
ATOM   4389 O  OD1  B ASN   B 1 20  ? 48.645 -35.718 -13.006 0.38 22.67 ?  20  ASN   B OD1  1 
ATOM   4390 N  ND2  A ASN   B 1 20  ? 48.110 -34.700 -11.001 0.62 22.77 ?  20  ASN   B ND2  1 
ATOM   4391 N  ND2  B ASN   B 1 20  ? 48.159 -34.603 -11.118 0.38 21.22 ?  20  ASN   B ND2  1 
ATOM   4392 H  H    A ASN   B 1 20  ? 45.451 -32.528 -14.122 0.62 21.53 ?  20  ASN   B H    1 
ATOM   4393 H  H    B ASN   B 1 20  ? 45.354 -32.554 -14.148 0.38 20.59 ?  20  ASN   B H    1 
ATOM   4394 H  HA   A ASN   B 1 20  ? 46.294 -32.805 -11.592 0.62 23.06 ?  20  ASN   B HA   1 
ATOM   4395 H  HA   B ASN   B 1 20  ? 46.322 -32.783 -11.673 0.38 21.02 ?  20  ASN   B HA   1 
ATOM   4396 H  HB2  A ASN   B 1 20  ? 45.883 -34.767 -12.727 0.62 25.31 ?  20  ASN   B HB2  1 
ATOM   4397 H  HB2  B ASN   B 1 20  ? 45.959 -34.728 -12.888 0.38 23.32 ?  20  ASN   B HB2  1 
ATOM   4398 H  HB3  A ASN   B 1 20  ? 46.854 -34.331 -13.904 0.62 25.31 ?  20  ASN   B HB3  1 
ATOM   4399 H  HB3  B ASN   B 1 20  ? 46.940 -34.223 -14.030 0.38 23.32 ?  20  ASN   B HB3  1 
ATOM   4400 H  HD21 A ASN   B 1 20  ? 48.752 -35.077 -10.578 0.62 27.34 ?  20  ASN   B HD21 1 
ATOM   4401 H  HD21 B ASN   B 1 20  ? 48.801 -34.977 -10.689 0.38 25.48 ?  20  ASN   B HD21 1 
ATOM   4402 H  HD22 A ASN   B 1 20  ? 47.635 -34.093 -10.603 0.62 27.34 ?  20  ASN   B HD22 1 
ATOM   4403 H  HD22 B ASN   B 1 20  ? 47.656 -34.028 -10.718 0.38 25.48 ?  20  ASN   B HD22 1 
ATOM   4404 N  N    A ALA   B 1 21  ? 48.197 -31.209 -11.726 0.62 19.72 ?  21  ALA   B N    1 
ATOM   4405 N  N    B ALA   B 1 21  ? 48.225 -31.200 -11.772 0.38 17.30 ?  21  ALA   B N    1 
ATOM   4406 C  CA   A ALA   B 1 21  ? 49.324 -30.302 -11.896 0.62 20.23 ?  21  ALA   B CA   1 
ATOM   4407 C  CA   B ALA   B 1 21  ? 49.334 -30.269 -11.925 0.38 18.27 ?  21  ALA   B CA   1 
ATOM   4408 C  C    A ALA   B 1 21  ? 49.806 -29.797 -10.542 0.62 18.93 ?  21  ALA   B C    1 
ATOM   4409 C  C    B ALA   B 1 21  ? 49.800 -29.775 -10.562 0.38 17.93 ?  21  ALA   B C    1 
ATOM   4410 O  O    A ALA   B 1 21  ? 49.075 -29.820 -9.547  0.62 18.66 ?  21  ALA   B O    1 
ATOM   4411 O  O    B ALA   B 1 21  ? 49.052 -29.784 -9.580  0.38 17.64 ?  21  ALA   B O    1 
ATOM   4412 C  CB   A ALA   B 1 21  ? 48.948 -29.133 -12.807 0.62 21.56 ?  21  ALA   B CB   1 
ATOM   4413 C  CB   B ALA   B 1 21  ? 48.931 -29.087 -12.806 0.38 19.28 ?  21  ALA   B CB   1 
ATOM   4414 H  H    A ALA   B 1 21  ? 47.785 -31.135 -10.972 0.62 23.68 ?  21  ALA   B H    1 
ATOM   4415 H  H    B ALA   B 1 21  ? 47.878 -31.228 -10.986 0.38 20.78 ?  21  ALA   B H    1 
ATOM   4416 H  HA   A ALA   B 1 21  ? 50.053 -30.788 -12.311 0.62 24.30 ?  21  ALA   B HA   1 
ATOM   4417 H  HA   B ALA   B 1 21  ? 50.076 -30.728 -12.352 0.38 21.94 ?  21  ALA   B HA   1 
ATOM   4418 H  HB1  A ALA   B 1 21  ? 49.744 -28.613 -12.984 0.62 25.89 ?  21  ALA   B HB1  1 
ATOM   4419 H  HB1  B ALA   B 1 21  ? 49.713 -28.543 -12.958 0.38 23.15 ?  21  ALA   B HB1  1 
ATOM   4420 H  HB2  A ALA   B 1 21  ? 48.595 -29.490 -13.638 0.62 25.89 ?  21  ALA   B HB2  1 
ATOM   4421 H  HB2  B ALA   B 1 21  ? 48.593 -29.429 -13.649 0.38 23.15 ?  21  ALA   B HB2  1 
ATOM   4422 H  HB3  A ALA   B 1 21  ? 48.278 -28.592 -12.367 0.62 25.89 ?  21  ALA   B HB3  1 
ATOM   4423 H  HB3  B ALA   B 1 21  ? 48.242 -28.581 -12.353 0.38 23.15 ?  21  ALA   B HB3  1 
ATOM   4424 N  N    . ASP   B 1 22  ? 51.063 -29.345 -10.532 1.00 17.73 ?  22  ASP   B N    1 
ATOM   4425 C  CA   . ASP   B 1 22  ? 51.675 -28.684 -9.380  1.00 17.06 ?  22  ASP   B CA   1 
ATOM   4426 C  C    . ASP   B 1 22  ? 51.287 -27.205 -9.434  1.00 15.23 ?  22  ASP   B C    1 
ATOM   4427 O  O    . ASP   B 1 22  ? 51.593 -26.524 -10.417 1.00 15.71 ?  22  ASP   B O    1 
ATOM   4428 C  CB   . ASP   B 1 22  ? 53.194 -28.873 -9.534  1.00 18.40 ?  22  ASP   B CB   1 
ATOM   4429 C  CG   . ASP   B 1 22  ? 54.034 -28.107 -8.519  1.00 19.85 ?  22  ASP   B CG   1 
ATOM   4430 O  OD1  . ASP   B 1 22  ? 53.668 -26.994 -8.105  1.00 19.94 ?  22  ASP   B OD1  1 
ATOM   4431 O  OD2  . ASP   B 1 22  ? 55.125 -28.620 -8.176  1.00 22.57 -1 22  ASP   B OD2  1 
ATOM   4432 H  H    A ASP   B 1 22  ? 51.596 -29.411 -11.206 0.62 21.30 ?  22  ASP   B H    1 
ATOM   4433 H  H    B ASP   B 1 22  ? 51.606 -29.433 -11.195 0.38 21.30 ?  22  ASP   B H    1 
ATOM   4434 H  HA   . ASP   B 1 22  ? 51.372 -29.084 -8.547  1.00 20.49 ?  22  ASP   B HA   1 
ATOM   4435 H  HB2  . ASP   B 1 22  ? 53.407 -29.810 -9.440  1.00 22.10 ?  22  ASP   B HB2  1 
ATOM   4436 H  HB3  . ASP   B 1 22  ? 53.457 -28.559 -10.413 1.00 22.10 ?  22  ASP   B HB3  1 
ATOM   4437 N  N    . ILE   B 1 23  ? 50.582 -26.717 -8.404  1.00 14.49 ?  23  ILE   B N    1 
ATOM   4438 C  CA   . ILE   B 1 23  ? 50.006 -25.368 -8.459  1.00 13.78 ?  23  ILE   B CA   1 
ATOM   4439 C  C    . ILE   B 1 23  ? 51.074 -24.289 -8.593  1.00 13.43 ?  23  ILE   B C    1 
ATOM   4440 O  O    . ILE   B 1 23  ? 50.822 -23.241 -9.196  1.00 12.96 ?  23  ILE   B O    1 
ATOM   4441 C  CB   . ILE   B 1 23  ? 49.077 -25.116 -7.256  1.00 14.16 ?  23  ILE   B CB   1 
ATOM   4442 C  CG1  . ILE   B 1 23  ? 48.263 -23.833 -7.450  1.00 14.68 ?  23  ILE   B CG1  1 
ATOM   4443 C  CG2  . ILE   B 1 23  ? 49.852 -25.112 -5.948  1.00 14.52 ?  23  ILE   B CG2  1 
ATOM   4444 C  CD1  . ILE   B 1 23  ? 47.144 -23.667 -6.429  1.00 15.11 ?  23  ILE   B CD1  1 
ATOM   4445 H  H    . ILE   B 1 23  ? 50.413 -27.147 -7.680  1.00 17.41 ?  23  ILE   B H    1 
ATOM   4446 H  HA   . ILE   B 1 23  ? 49.455 -25.311 -9.253  1.00 16.55 ?  23  ILE   B HA   1 
ATOM   4447 H  HB   . ILE   B 1 23  ? 48.449 -25.854 -7.219  1.00 17.01 ?  23  ILE   B HB   1 
ATOM   4448 H  HG12 . ILE   B 1 23  ? 48.860 -23.070 -7.366  1.00 17.64 ?  23  ILE   B HG12 1 
ATOM   4449 H  HG13 . ILE   B 1 23  ? 47.867 -23.844 -8.335  1.00 17.64 ?  23  ILE   B HG13 1 
ATOM   4450 H  HG21 . ILE   B 1 23  ? 49.223 -25.098 -5.211  1.00 17.45 ?  23  ILE   B HG21 1 
ATOM   4451 H  HG22 . ILE   B 1 23  ? 50.396 -25.914 -5.903  1.00 17.45 ?  23  ILE   B HG22 1 
ATOM   4452 H  HG23 . ILE   B 1 23  ? 50.417 -24.326 -5.920  1.00 17.45 ?  23  ILE   B HG23 1 
ATOM   4453 H  HD11 . ILE   B 1 23  ? 46.629 -22.879 -6.656  1.00 18.15 ?  23  ILE   B HD11 1 
ATOM   4454 H  HD12 . ILE   B 1 23  ? 46.578 -24.455 -6.459  1.00 18.15 ?  23  ILE   B HD12 1 
ATOM   4455 H  HD13 . ILE   B 1 23  ? 47.534 -23.571 -5.548  1.00 18.15 ?  23  ILE   B HD13 1 
ATOM   4456 N  N    . VAL   B 1 24  ? 52.262 -24.502 -8.024  1.00 13.73 ?  24  VAL   B N    1 
ATOM   4457 C  CA   . VAL   B 1 24  ? 53.346 -23.528 -8.179  1.00 14.27 ?  24  VAL   B CA   1 
ATOM   4458 C  C    . VAL   B 1 24  ? 53.803 -23.473 -9.629  1.00 14.54 ?  24  VAL   B C    1 
ATOM   4459 O  O    . VAL   B 1 24  ? 53.940 -22.393 -10.217 1.00 15.06 ?  24  VAL   B O    1 
ATOM   4460 C  CB   . VAL   B 1 24  ? 54.519 -23.860 -7.235  1.00 15.21 ?  24  VAL   B CB   1 
ATOM   4461 C  CG1  . VAL   B 1 24  ? 55.738 -22.988 -7.553  1.00 16.21 ?  24  VAL   B CG1  1 
ATOM   4462 C  CG2  . VAL   B 1 24  ? 54.104 -23.681 -5.789  1.00 16.28 ?  24  VAL   B CG2  1 
ATOM   4463 H  H    . VAL   B 1 24  ? 52.467 -25.187 -7.551  1.00 16.50 ?  24  VAL   B H    1 
ATOM   4464 H  HA   . VAL   B 1 24  ? 53.015 -22.647 -7.938  1.00 17.15 ?  24  VAL   B HA   1 
ATOM   4465 H  HB   . VAL   B 1 24  ? 54.772 -24.787 -7.356  1.00 18.27 ?  24  VAL   B HB   1 
ATOM   4466 H  HG11 . VAL   B 1 24  ? 56.338 -22.995 -6.790  1.00 19.47 ?  24  VAL   B HG11 1 
ATOM   4467 H  HG12 . VAL   B 1 24  ? 56.190 -23.349 -8.330  1.00 19.47 ?  24  VAL   B HG12 1 
ATOM   4468 H  HG13 . VAL   B 1 24  ? 55.441 -22.082 -7.729  1.00 19.47 ?  24  VAL   B HG13 1 
ATOM   4469 H  HG21 . VAL   B 1 24  ? 54.823 -23.978 -5.212  1.00 19.55 ?  24  VAL   B HG21 1 
ATOM   4470 H  HG22 . VAL   B 1 24  ? 53.919 -22.740 -5.629  1.00 19.55 ?  24  VAL   B HG22 1 
ATOM   4471 H  HG23 . VAL   B 1 24  ? 53.305 -24.206 -5.620  1.00 19.55 ?  24  VAL   B HG23 1 
ATOM   4472 N  N    . GLU   B 1 25  ? 54.075 -24.639 -10.222 1.00 15.49 ?  25  GLU   B N    1 
ATOM   4473 C  CA   . GLU   B 1 25  ? 54.470 -24.669 -11.624 1.00 17.28 ?  25  GLU   B CA   1 
ATOM   4474 C  C    . GLU   B 1 25  ? 53.359 -24.135 -12.515 1.00 16.03 ?  25  GLU   B C    1 
ATOM   4475 O  O    . GLU   B 1 25  ? 53.625 -23.421 -13.491 1.00 17.13 ?  25  GLU   B O    1 
ATOM   4476 C  CB   . GLU   B 1 25  ? 54.876 -26.086 -12.021 1.00 21.75 ?  25  GLU   B CB   1 
ATOM   4477 C  CG   . GLU   B 1 25  ? 56.166 -26.541 -11.345 1.00 27.06 ?  25  GLU   B CG   1 
ATOM   4478 C  CD   . GLU   B 1 25  ? 57.293 -25.524 -11.460 1.00 32.15 ?  25  GLU   B CD   1 
ATOM   4479 O  OE1  . GLU   B 1 25  ? 57.693 -25.203 -12.600 1.00 34.10 ?  25  GLU   B OE1  1 
ATOM   4480 O  OE2  . GLU   B 1 25  ? 57.770 -25.027 -10.412 1.00 33.85 -1 25  GLU   B OE2  1 
ATOM   4481 H  H    . GLU   B 1 25  ? 54.039 -25.407 -9.837  1.00 18.61 ?  25  GLU   B H    1 
ATOM   4482 H  HA   . GLU   B 1 25  ? 55.230 -24.083 -11.745 1.00 20.76 ?  25  GLU   B HA   1 
ATOM   4483 H  HB2  . GLU   B 1 25  ? 54.173 -26.704 -11.761 1.00 26.12 ?  25  GLU   B HB2  1 
ATOM   4484 H  HB3  . GLU   B 1 25  ? 55.009 -26.122 -12.981 1.00 26.12 ?  25  GLU   B HB3  1 
ATOM   4485 H  HG2  . GLU   B 1 25  ? 56.003 -26.674 -10.405 1.00 32.49 ?  25  GLU   B HG2  1 
ATOM   4486 H  HG3  . GLU   B 1 25  ? 56.466 -27.365 -11.760 1.00 32.49 ?  25  GLU   B HG3  1 
ATOM   4487 N  N    A GLU   B 1 26  ? 52.105 -24.462 -12.191 0.62 15.22 ?  26  GLU   B N    1 
ATOM   4488 N  N    B GLU   B 1 26  ? 52.104 -24.460 -12.191 0.38 15.45 ?  26  GLU   B N    1 
ATOM   4489 C  CA   A GLU   B 1 26  ? 50.979 -23.940 -12.958 0.62 16.00 ?  26  GLU   B CA   1 
ATOM   4490 C  CA   B GLU   B 1 26  ? 50.980 -23.939 -12.962 0.38 15.83 ?  26  GLU   B CA   1 
ATOM   4491 C  C    A GLU   B 1 26  ? 50.919 -22.422 -12.881 0.62 14.91 ?  26  GLU   B C    1 
ATOM   4492 C  C    B GLU   B 1 26  ? 50.918 -22.421 -12.883 0.38 14.83 ?  26  GLU   B C    1 
ATOM   4493 O  O    A GLU   B 1 26  ? 50.719 -21.747 -13.897 0.62 16.07 ?  26  GLU   B O    1 
ATOM   4494 O  O    B GLU   B 1 26  ? 50.720 -21.744 -13.897 0.38 15.61 ?  26  GLU   B O    1 
ATOM   4495 C  CB   A GLU   B 1 26  ? 49.671 -24.531 -12.439 0.62 18.15 ?  26  GLU   B CB   1 
ATOM   4496 C  CB   B GLU   B 1 26  ? 49.668 -24.540 -12.458 0.38 17.30 ?  26  GLU   B CB   1 
ATOM   4497 C  CG   A GLU   B 1 26  ? 49.287 -25.846 -13.070 0.62 21.61 ?  26  GLU   B CG   1 
ATOM   4498 C  CG   B GLU   B 1 26  ? 49.206 -25.764 -13.216 0.38 19.79 ?  26  GLU   B CG   1 
ATOM   4499 C  CD   A GLU   B 1 26  ? 49.066 -25.758 -14.576 0.62 22.89 ?  26  GLU   B CD   1 
ATOM   4500 C  CD   B GLU   B 1 26  ? 48.849 -25.462 -14.674 0.38 20.13 ?  26  GLU   B CD   1 
ATOM   4501 O  OE1  A GLU   B 1 26  ? 48.252 -24.922 -15.028 0.62 22.46 ?  26  GLU   B OE1  1 
ATOM   4502 O  OE1  B GLU   B 1 26  ? 47.722 -24.986 -14.947 0.38 20.73 ?  26  GLU   B OE1  1 
ATOM   4503 O  OE2  A GLU   B 1 26  ? 49.706 -26.537 -15.303 0.62 24.21 -1 26  GLU   B OE2  1 
ATOM   4504 O  OE2  B GLU   B 1 26  ? 49.701 -25.699 -15.545 0.38 20.19 -1 26  GLU   B OE2  1 
ATOM   4505 H  H    A GLU   B 1 26  ? 51.884 -24.983 -11.539 0.62 18.28 ?  26  GLU   B H    1 
ATOM   4506 H  H    B GLU   B 1 26  ? 51.884 -24.977 -11.537 0.38 18.56 ?  26  GLU   B H    1 
ATOM   4507 H  HA   A GLU   B 1 26  ? 51.087 -24.191 -13.886 0.62 19.22 ?  26  GLU   B HA   1 
ATOM   4508 H  HA   B GLU   B 1 26  ? 51.096 -24.186 -13.891 0.38 19.01 ?  26  GLU   B HA   1 
ATOM   4509 H  HB2  A GLU   B 1 26  ? 49.755 -24.674 -11.479 0.62 21.80 ?  26  GLU   B HB2  1 
ATOM   4510 H  HB2  B GLU   B 1 26  ? 49.779 -24.788 -11.526 0.38 20.78 ?  26  GLU   B HB2  1 
ATOM   4511 H  HB3  A GLU   B 1 26  ? 48.957 -23.895 -12.607 0.62 21.80 ?  26  GLU   B HB3  1 
ATOM   4512 H  HB3  B GLU   B 1 26  ? 48.973 -23.867 -12.535 0.38 20.78 ?  26  GLU   B HB3  1 
ATOM   4513 H  HG2  A GLU   B 1 26  ? 50.005 -26.468 -12.916 0.62 25.96 ?  26  GLU   B HG2  1 
ATOM   4514 H  HG2  B GLU   B 1 26  ? 49.915 -26.426 -13.164 0.38 23.77 ?  26  GLU   B HG2  1 
ATOM   4515 H  HG3  A GLU   B 1 26  ? 48.468 -26.154 -12.659 0.62 25.96 ?  26  GLU   B HG3  1 
ATOM   4516 H  HG3  B GLU   B 1 26  ? 48.402 -26.100 -12.804 0.38 23.77 ?  26  GLU   B HG3  1 
ATOM   4517 N  N    . ALA   B 1 27  ? 51.071 -21.867 -11.678 1.00 13.83 ?  27  ALA   B N    1 
ATOM   4518 C  CA   . ALA   B 1 27  ? 51.036 -20.417 -11.532 1.00 14.06 ?  27  ALA   B CA   1 
ATOM   4519 C  C    . ALA   B 1 27  ? 52.109 -19.756 -12.391 1.00 14.77 ?  27  ALA   B C    1 
ATOM   4520 O  O    . ALA   B 1 27  ? 51.849 -18.759 -13.079 1.00 15.94 ?  27  ALA   B O    1 
ATOM   4521 C  CB   . ALA   B 1 27  ? 51.188 -20.035 -10.059 1.00 13.60 ?  27  ALA   B CB   1 
ATOM   4522 H  H    A ALA   B 1 27  ? 51.190 -22.301 -10.943 0.62 16.62 ?  27  ALA   B H    1 
ATOM   4523 H  H    B ALA   B 1 27  ? 51.194 -22.302 -10.944 0.38 16.62 ?  27  ALA   B H    1 
ATOM   4524 H  HA   . ALA   B 1 27  ? 50.180 -20.091 -11.834 1.00 16.89 ?  27  ALA   B HA   1 
ATOM   4525 H  HB1  . ALA   B 1 27  ? 51.155 -19.068 -9.977  1.00 16.34 ?  27  ALA   B HB1  1 
ATOM   4526 H  HB2  . ALA   B 1 27  ? 50.457 -20.431 -9.555  1.00 16.34 ?  27  ALA   B HB2  1 
ATOM   4527 H  HB3  . ALA   B 1 27  ? 52.035 -20.367 -9.727  1.00 16.34 ?  27  ALA   B HB3  1 
ATOM   4528 N  N    . LYS   B 1 28  ? 53.325 -20.304 -12.376 1.00 16.36 ?  28  LYS   B N    1 
ATOM   4529 C  CA   . LYS   B 1 28  ? 54.397 -19.689 -13.148 1.00 18.79 ?  28  LYS   B CA   1 
ATOM   4530 C  C    . LYS   B 1 28  ? 54.144 -19.782 -14.645 1.00 19.13 ?  28  LYS   B C    1 
ATOM   4531 O  O    . LYS   B 1 28  ? 54.568 -18.895 -15.396 1.00 20.29 ?  28  LYS   B O    1 
ATOM   4532 C  CB   . LYS   B 1 28  ? 55.755 -20.276 -12.751 1.00 22.08 ?  28  LYS   B CB   1 
ATOM   4533 C  CG   . LYS   B 1 28  ? 56.139 -19.933 -11.317 1.00 25.37 ?  28  LYS   B CG   1 
ATOM   4534 C  CD   . LYS   B 1 28  ? 57.568 -20.322 -10.962 1.00 30.14 ?  28  LYS   B CD   1 
ATOM   4535 C  CE   . LYS   B 1 28  ? 57.685 -21.797 -10.662 1.00 34.02 ?  28  LYS   B CE   1 
ATOM   4536 N  NZ   . LYS   B 1 28  ? 59.047 -22.147 -10.161 1.00 35.76 ?  28  LYS   B NZ   1 
ATOM   4537 H  H    . LYS   B 1 28  ? 53.554 -21.010 -11.937 1.00 19.65 ?  28  LYS   B H    1 
ATOM   4538 H  HA   . LYS   B 1 28  ? 54.427 -18.749 -12.936 1.00 22.56 ?  28  LYS   B HA   1 
ATOM   4539 H  HB2  . LYS   B 1 28  ? 55.729 -21.241 -12.830 1.00 26.51 ?  28  LYS   B HB2  1 
ATOM   4540 H  HB3  . LYS   B 1 28  ? 56.446 -19.916 -13.337 1.00 26.51 ?  28  LYS   B HB3  1 
ATOM   4541 H  HG2  . LYS   B 1 28  ? 56.046 -18.974 -11.194 1.00 30.46 ?  28  LYS   B HG2  1 
ATOM   4542 H  HG3  . LYS   B 1 28  ? 55.539 -20.401 -10.718 1.00 30.46 ?  28  LYS   B HG3  1 
ATOM   4543 H  HD2  . LYS   B 1 28  ? 58.149 -20.113 -11.710 1.00 36.18 ?  28  LYS   B HD2  1 
ATOM   4544 H  HD3  . LYS   B 1 28  ? 57.842 -19.824 -10.175 1.00 36.18 ?  28  LYS   B HD3  1 
ATOM   4545 H  HE2  . LYS   B 1 28  ? 57.039 -22.036 -9.978  1.00 40.84 ?  28  LYS   B HE2  1 
ATOM   4546 H  HE3  . LYS   B 1 28  ? 57.518 -22.303 -11.472 1.00 40.84 ?  28  LYS   B HE3  1 
ATOM   4547 H  HZ1  . LYS   B 1 28  ? 59.093 -23.019 -9.990  1.00 42.93 ?  28  LYS   B HZ1  1 
ATOM   4548 H  HZ2  . LYS   B 1 28  ? 59.658 -21.939 -10.774 1.00 42.93 ?  28  LYS   B HZ2  1 
ATOM   4549 H  HZ3  . LYS   B 1 28  ? 59.222 -21.696 -9.414  1.00 42.93 ?  28  LYS   B HZ3  1 
ATOM   4550 N  N    . LYS   B 1 29  ? 53.427 -20.814 -15.095 1.00 20.51 ?  29  LYS   B N    1 
ATOM   4551 C  CA   . LYS   B 1 29  ? 53.156 -20.977 -16.520 1.00 23.49 ?  29  LYS   B CA   1 
ATOM   4552 C  C    . LYS   B 1 29  ? 51.909 -20.221 -16.977 1.00 22.15 ?  29  LYS   B C    1 
ATOM   4553 O  O    . LYS   B 1 29  ? 51.917 -19.609 -18.051 1.00 23.85 ?  29  LYS   B O    1 
ATOM   4554 C  CB   . LYS   B 1 29  ? 53.027 -22.465 -16.863 1.00 28.69 ?  29  LYS   B CB   1 
ATOM   4555 C  CG   . LYS   B 1 29  ? 52.860 -22.751 -18.344 1.00 33.84 ?  29  LYS   B CG   1 
ATOM   4556 C  CD   . LYS   B 1 29  ? 53.033 -24.237 -18.638 1.00 38.16 ?  29  LYS   B CD   1 
ATOM   4557 C  CE   . LYS   B 1 29  ? 51.875 -25.066 -18.099 1.00 41.40 ?  29  LYS   B CE   1 
ATOM   4558 N  NZ   . LYS   B 1 29  ? 52.055 -26.522 -18.382 1.00 42.98 ?  29  LYS   B NZ   1 
ATOM   4559 H  H    . LYS   B 1 29  ? 53.079 -21.434 -14.593 1.00 24.64 ?  29  LYS   B H    1 
ATOM   4560 H  HA   . LYS   B 1 29  ? 53.908 -20.630 -17.015 1.00 28.21 ?  29  LYS   B HA   1 
ATOM   4561 H  HB2  . LYS   B 1 29  ? 53.833 -22.924 -16.571 1.00 34.45 ?  29  LYS   B HB2  1 
ATOM   4562 H  HB3  . LYS   B 1 29  ? 52.258 -22.832 -16.407 1.00 34.45 ?  29  LYS   B HB3  1 
ATOM   4563 H  HG2  . LYS   B 1 29  ? 51.969 -22.485 -18.623 1.00 40.63 ?  29  LYS   B HG2  1 
ATOM   4564 H  HG3  . LYS   B 1 29  ? 53.530 -22.258 -18.846 1.00 40.63 ?  29  LYS   B HG3  1 
ATOM   4565 H  HD2  . LYS   B 1 29  ? 53.081 -24.369 -19.596 1.00 45.81 ?  29  LYS   B HD2  1 
ATOM   4566 H  HD3  . LYS   B 1 29  ? 53.850 -24.550 -18.216 1.00 45.81 ?  29  LYS   B HD3  1 
ATOM   4567 H  HE2  . LYS   B 1 29  ? 51.815 -24.951 -17.138 1.00 49.70 ?  29  LYS   B HE2  1 
ATOM   4568 H  HE3  . LYS   B 1 29  ? 51.051 -24.775 -18.522 1.00 49.70 ?  29  LYS   B HE3  1 
ATOM   4569 H  HZ1  . LYS   B 1 29  ? 51.365 -26.983 -18.059 1.00 51.59 ?  29  LYS   B HZ1  1 
ATOM   4570 H  HZ2  . LYS   B 1 29  ? 52.107 -26.658 -19.260 1.00 51.59 ?  29  LYS   B HZ2  1 
ATOM   4571 H  HZ3  . LYS   B 1 29  ? 52.803 -26.816 -18.000 1.00 51.59 ?  29  LYS   B HZ3  1 
ATOM   4572 N  N    . VAL   B 1 30  ? 50.838 -20.260 -16.179 1.00 20.24 ?  30  VAL   B N    1 
ATOM   4573 C  CA   . VAL   B 1 30  ? 49.555 -19.661 -16.552 1.00 20.22 ?  30  VAL   B CA   1 
ATOM   4574 C  C    . VAL   B 1 30  ? 49.566 -18.150 -16.399 1.00 18.30 ?  30  VAL   B C    1 
ATOM   4575 O  O    . VAL   B 1 30  ? 48.808 -17.442 -17.082 1.00 19.10 ?  30  VAL   B O    1 
ATOM   4576 C  CB   . VAL   B 1 30  ? 48.449 -20.268 -15.666 1.00 22.18 ?  30  VAL   B CB   1 
ATOM   4577 C  CG1  . VAL   B 1 30  ? 47.161 -19.467 -15.764 1.00 23.21 ?  30  VAL   B CG1  1 
ATOM   4578 C  CG2  . VAL   B 1 30  ? 48.223 -21.728 -16.025 1.00 23.17 ?  30  VAL   B CG2  1 
ATOM   4579 H  H    . VAL   B 1 30  ? 50.819 -20.663 -15.410 1.00 24.31 ?  30  VAL   B H    1 
ATOM   4580 H  HA   . VAL   B 1 30  ? 49.352 -19.888 -17.474 1.00 24.29 ?  30  VAL   B HA   1 
ATOM   4581 H  HB   . VAL   B 1 30  ? 48.737 -20.243 -14.740 1.00 26.64 ?  30  VAL   B HB   1 
ATOM   4582 H  HG11 . VAL   B 1 30  ? 46.420 -20.072 -15.621 1.00 27.88 ?  30  VAL   B HG11 1 
ATOM   4583 H  HG12 . VAL   B 1 30  ? 47.160 -18.779 -15.083 1.00 27.88 ?  30  VAL   B HG12 1 
ATOM   4584 H  HG13 . VAL   B 1 30  ? 47.090 -19.083 -16.644 1.00 27.88 ?  30  VAL   B HG13 1 
ATOM   4585 H  HG21 . VAL   B 1 30  ? 47.532 -22.099 -15.448 1.00 27.82 ?  30  VAL   B HG21 1 
ATOM   4586 H  HG22 . VAL   B 1 30  ? 47.936 -21.787 -16.952 1.00 27.82 ?  30  VAL   B HG22 1 
ATOM   4587 H  HG23 . VAL   B 1 30  ? 49.049 -22.219 -15.903 1.00 27.82 ?  30  VAL   B HG23 1 
ATOM   4588 N  N    . LYS   B 1 31  ? 50.378 -17.647 -15.480 1.00 17.65 ?  31  LYS   B N    1 
ATOM   4589 C  CA   . LYS   B 1 31  ? 50.390 -16.239 -15.106 1.00 18.42 ?  31  LYS   B CA   1 
ATOM   4590 C  C    . LYS   B 1 31  ? 48.992 -15.742 -14.719 1.00 16.58 ?  31  LYS   B C    1 
ATOM   4591 O  O    . LYS   B 1 31  ? 48.452 -14.829 -15.350 1.00 16.88 ?  31  LYS   B O    1 
ATOM   4592 C  CB   . LYS   B 1 31  ? 51.014 -15.388 -16.204 1.00 21.86 ?  31  LYS   B CB   1 
ATOM   4593 C  CG   . LYS   B 1 31  ? 52.449 -15.829 -16.524 1.00 25.61 ?  31  LYS   B CG   1 
ATOM   4594 C  CD   . LYS   B 1 31  ? 53.045 -15.058 -17.679 1.00 30.08 ?  31  LYS   B CD   1 
ATOM   4595 C  CE   . LYS   B 1 31  ? 54.541 -15.275 -17.770 1.00 33.37 ?  31  LYS   B CE   1 
ATOM   4596 N  NZ   . LYS   B 1 31  ? 55.242 -14.784 -16.547 1.00 35.18 ?  31  LYS   B NZ   1 
ATOM   4597 H  H    . LYS   B 1 31  ? 50.970 -18.123 -15.073 1.00 21.20 ?  31  LYS   B H    1 
ATOM   4598 H  HA   . LYS   B 1 31  ? 50.951 -16.157 -14.329 1.00 22.13 ?  31  LYS   B HA   1 
ATOM   4599 H  HB2  . LYS   B 1 31  ? 50.492 -15.469 -17.016 1.00 26.26 ?  31  LYS   B HB2  1 
ATOM   4600 H  HB3  . LYS   B 1 31  ? 51.045 -14.468 -15.910 1.00 26.26 ?  31  LYS   B HB3  1 
ATOM   4601 H  HG2  . LYS   B 1 31  ? 53.003 -15.687 -15.740 1.00 30.75 ?  31  LYS   B HG2  1 
ATOM   4602 H  HG3  . LYS   B 1 31  ? 52.449 -16.774 -16.759 1.00 30.75 ?  31  LYS   B HG3  1 
ATOM   4603 H  HD2  . LYS   B 1 31  ? 52.638 -15.368 -18.503 1.00 36.12 ?  31  LYS   B HD2  1 
ATOM   4604 H  HD3  . LYS   B 1 31  ? 52.875 -14.117 -17.547 1.00 36.12 ?  31  LYS   B HD3  1 
ATOM   4605 H  HE2  . LYS   B 1 31  ? 54.725 -16.224 -17.865 1.00 40.06 ?  31  LYS   B HE2  1 
ATOM   4606 H  HE3  . LYS   B 1 31  ? 54.886 -14.788 -18.534 1.00 40.06 ?  31  LYS   B HE3  1 
ATOM   4607 H  HZ1  . LYS   B 1 31  ? 56.122 -14.797 -16.674 1.00 42.23 ?  31  LYS   B HZ1  1 
ATOM   4608 H  HZ2  . LYS   B 1 31  ? 54.988 -13.950 -16.366 1.00 42.23 ?  31  LYS   B HZ2  1 
ATOM   4609 H  HZ3  . LYS   B 1 31  ? 55.042 -15.303 -15.851 1.00 42.23 ?  31  LYS   B HZ3  1 
ATOM   4610 N  N    . PRO   B 1 32  ? 48.387 -16.321 -13.677 1.00 14.69 ?  32  PRO   B N    1 
ATOM   4611 C  CA   . PRO   B 1 32  ? 47.015 -15.955 -13.311 1.00 14.27 ?  32  PRO   B CA   1 
ATOM   4612 C  C    . PRO   B 1 32  ? 46.954 -14.608 -12.608 1.00 14.35 ?  32  PRO   B C    1 
ATOM   4613 O  O    . PRO   B 1 32  ? 47.890 -14.192 -11.916 1.00 15.21 ?  32  PRO   B O    1 
ATOM   4614 C  CB   . PRO   B 1 32  ? 46.619 -17.066 -12.332 1.00 14.56 ?  32  PRO   B CB   1 
ATOM   4615 C  CG   . PRO   B 1 32  ? 47.929 -17.416 -11.667 1.00 14.32 ?  32  PRO   B CG   1 
ATOM   4616 C  CD   . PRO   B 1 32  ? 48.975 -17.294 -12.737 1.00 14.69 ?  32  PRO   B CD   1 
ATOM   4617 H  HA   . PRO   B 1 32  ? 46.426 -15.970 -14.092 1.00 17.14 ?  32  PRO   B HA   1 
ATOM   4618 H  HB2  . PRO   B 1 32  ? 45.984 -16.722 -11.686 1.00 17.49 ?  32  PRO   B HB2  1 
ATOM   4619 H  HB3  . PRO   B 1 32  ? 46.260 -17.826 -12.811 1.00 17.49 ?  32  PRO   B HB3  1 
ATOM   4620 H  HG2  . PRO   B 1 32  ? 48.116 -16.789 -10.946 1.00 17.20 ?  32  PRO   B HG2  1 
ATOM   4621 H  HG3  . PRO   B 1 32  ? 47.900 -18.323 -11.327 1.00 17.20 ?  32  PRO   B HG3  1 
ATOM   4622 H  HD2  . PRO   B 1 32  ? 49.801 -16.946 -12.375 1.00 17.65 ?  32  PRO   B HD2  1 
ATOM   4623 H  HD3  . PRO   B 1 32  ? 49.110 -18.151 -13.175 1.00 17.65 ?  32  PRO   B HD3  1 
ATOM   4624 N  N    . THR   B 1 33  ? 45.803 -13.945 -12.763 1.00 13.95 ?  33  THR   B N    1 
ATOM   4625 C  CA   . THR   B 1 33  ? 45.523 -12.765 -11.954 1.00 13.83 ?  33  THR   B CA   1 
ATOM   4626 C  C    . THR   B 1 33  ? 45.479 -13.116 -10.471 1.00 13.60 ?  33  THR   B C    1 
ATOM   4627 O  O    . THR   B 1 33  ? 45.966 -12.341 -9.632  1.00 14.44 ?  33  THR   B O    1 
ATOM   4628 C  CB   . THR   B 1 33  ? 44.206 -12.118 -12.389 1.00 14.82 ?  33  THR   B CB   1 
ATOM   4629 O  OG1  . THR   B 1 33  ? 44.223 -11.876 -13.797 1.00 15.20 ?  33  THR   B OG1  1 
ATOM   4630 C  CG2  . THR   B 1 33  ? 43.995 -10.819 -11.656 1.00 16.05 ?  33  THR   B CG2  1 
ATOM   4631 H  H    . THR   B 1 33  ? 45.176 -14.168 -13.318 1.00 16.76 ?  33  THR   B H    1 
ATOM   4632 H  HA   . THR   B 1 33  ? 46.233 -12.124 -12.098 1.00 16.62 ?  33  THR   B HA   1 
ATOM   4633 H  HB   . THR   B 1 33  ? 43.469 -12.718 -12.182 1.00 17.80 ?  33  THR   B HB   1 
ATOM   4634 H  HG1  . THR   B 1 33  ? 43.506 -11.497 -14.039 1.00 18.26 ?  33  THR   B HG1  1 
ATOM   4635 H  HG21 . THR   B 1 33  ? 43.251 -10.339 -12.040 1.00 19.28 ?  33  THR   B HG21 1 
ATOM   4636 H  HG22 . THR   B 1 33  ? 43.815 -10.993 -10.719 1.00 19.28 ?  33  THR   B HG22 1 
ATOM   4637 H  HG23 . THR   B 1 33  ? 44.796 -10.271 -11.724 1.00 19.28 ?  33  THR   B HG23 1 
ATOM   4638 N  N    . VAL   B 1 34  ? 44.912 -14.281 -10.127 1.00 12.82 ?  34  VAL   B N    1 
ATOM   4639 C  CA   . VAL   B 1 34  ? 44.709 -14.667 -8.735  1.00 12.41 ?  34  VAL   B CA   1 
ATOM   4640 C  C    . VAL   B 1 34  ? 45.124 -16.118 -8.560  1.00 11.55 ?  34  VAL   B C    1 
ATOM   4641 O  O    . VAL   B 1 34  ? 44.595 -17.003 -9.246  1.00 12.40 ?  34  VAL   B O    1 
ATOM   4642 C  CB   . VAL   B 1 34  ? 43.240 -14.506 -8.293  1.00 13.64 ?  34  VAL   B CB   1 
ATOM   4643 C  CG1  . VAL   B 1 34  ? 43.060 -14.954 -6.852  1.00 13.67 ?  34  VAL   B CG1  1 
ATOM   4644 C  CG2  . VAL   B 1 34  ? 42.754 -13.077 -8.499  1.00 14.30 ?  34  VAL   B CG2  1 
ATOM   4645 H  H    . VAL   B 1 34  ? 44.651 -14.877 -10.694 1.00 15.40 ?  34  VAL   B H    1 
ATOM   4646 H  HA   . VAL   B 1 34  ? 45.265 -14.118 -8.162  1.00 14.91 ?  34  VAL   B HA   1 
ATOM   4647 H  HB   . VAL   B 1 34  ? 42.690 -15.077 -8.851  1.00 16.39 ?  34  VAL   B HB   1 
ATOM   4648 H  HG11 . VAL   B 1 34  ? 42.209 -14.622 -6.525  1.00 16.42 ?  34  VAL   B HG11 1 
ATOM   4649 H  HG12 . VAL   B 1 34  ? 43.072 -15.922 -6.818  1.00 16.42 ?  34  VAL   B HG12 1 
ATOM   4650 H  HG13 . VAL   B 1 34  ? 43.783 -14.591 -6.317  1.00 16.42 ?  34  VAL   B HG13 1 
ATOM   4651 H  HG21 . VAL   B 1 34  ? 41.833 -13.010 -8.197  1.00 17.18 ?  34  VAL   B HG21 1 
ATOM   4652 H  HG22 . VAL   B 1 34  ? 43.314 -12.473 -7.995  1.00 17.18 ?  34  VAL   B HG22 1 
ATOM   4653 H  HG23 . VAL   B 1 34  ? 42.801 -12.858 -9.448  1.00 17.18 ?  34  VAL   B HG23 1 
ATOM   4654 N  N    . VAL   B 1 35  ? 46.030 -16.375 -7.618  1.00 10.80 ?  35  VAL   B N    1 
ATOM   4655 C  CA   . VAL   B 1 35  ? 46.251 -17.721 -7.104  1.00 11.03 ?  35  VAL   B CA   1 
ATOM   4656 C  C    . VAL   B 1 35  ? 45.707 -17.770 -5.689  1.00 10.43 ?  35  VAL   B C    1 
ATOM   4657 O  O    . VAL   B 1 35  ? 45.928 -16.852 -4.894  1.00 10.79 ?  35  VAL   B O    1 
ATOM   4658 C  CB   . VAL   B 1 35  ? 47.732 -18.160 -7.178  1.00 11.70 ?  35  VAL   B CB   1 
ATOM   4659 C  CG1  . VAL   B 1 35  ? 48.633 -17.324 -6.260  1.00 12.62 ?  35  VAL   B CG1  1 
ATOM   4660 C  CG2  . VAL   B 1 35  ? 47.868 -19.654 -6.857  1.00 12.38 ?  35  VAL   B CG2  1 
ATOM   4661 H  H    . VAL   B 1 35  ? 46.530 -15.772 -7.255  1.00 12.98 ?  35  VAL   B H    1 
ATOM   4662 H  HA   . VAL   B 1 35  ? 45.738 -18.343 -7.631  1.00 13.26 ?  35  VAL   B HA   1 
ATOM   4663 H  HB   . VAL   B 1 35  ? 48.046 -18.030 -8.087  1.00 14.07 ?  35  VAL   B HB   1 
ATOM   4664 H  HG11 . VAL   B 1 35  ? 49.558 -17.555 -6.434  1.00 15.16 ?  35  VAL   B HG11 1 
ATOM   4665 H  HG12 . VAL   B 1 35  ? 48.480 -16.388 -6.437  1.00 15.16 ?  35  VAL   B HG12 1 
ATOM   4666 H  HG13 . VAL   B 1 35  ? 48.412 -17.529 -5.335  1.00 15.16 ?  35  VAL   B HG13 1 
ATOM   4667 H  HG21 . VAL   B 1 35  ? 48.792 -19.927 -6.955  1.00 14.88 ?  35  VAL   B HG21 1 
ATOM   4668 H  HG22 . VAL   B 1 35  ? 47.574 -19.816 -5.941  1.00 14.88 ?  35  VAL   B HG22 1 
ATOM   4669 H  HG23 . VAL   B 1 35  ? 47.308 -20.168 -7.468  1.00 14.88 ?  35  VAL   B HG23 1 
ATOM   4670 N  N    . VAL   B 1 36  ? 44.996 -18.853 -5.372  1.00 10.47 ?  36  VAL   B N    1 
ATOM   4671 C  CA   . VAL   B 1 36  ? 44.450 -19.048 -4.042  1.00 10.11 ?  36  VAL   B CA   1 
ATOM   4672 C  C    . VAL   B 1 36  ? 45.455 -19.806 -3.186  1.00 9.77  ?  36  VAL   B C    1 
ATOM   4673 O  O    . VAL   B 1 36  ? 45.991 -20.842 -3.602  1.00 11.24 ?  36  VAL   B O    1 
ATOM   4674 C  CB   . VAL   B 1 36  ? 43.110 -19.803 -4.112  1.00 10.64 ?  36  VAL   B CB   1 
ATOM   4675 C  CG1  . VAL   B 1 36  ? 42.604 -20.159 -2.717  1.00 11.38 ?  36  VAL   B CG1  1 
ATOM   4676 C  CG2  . VAL   B 1 36  ? 42.086 -18.980 -4.867  1.00 11.26 ?  36  VAL   B CG2  1 
ATOM   4677 H  H    . VAL   B 1 36  ? 44.833 -19.500 -5.916  1.00 12.58 ?  36  VAL   B H    1 
ATOM   4678 H  HA   . VAL   B 1 36  ? 44.287 -18.187 -3.630  1.00 12.15 ?  36  VAL   B HA   1 
ATOM   4679 H  HB   . VAL   B 1 36  ? 43.242 -20.633 -4.600  1.00 12.79 ?  36  VAL   B HB   1 
ATOM   4680 H  HG11 . VAL   B 1 36  ? 41.668 -20.393 -2.772  1.00 13.67 ?  36  VAL   B HG11 1 
ATOM   4681 H  HG12 . VAL   B 1 36  ? 43.117 -20.907 -2.375  1.00 13.67 ?  36  VAL   B HG12 1 
ATOM   4682 H  HG13 . VAL   B 1 36  ? 42.719 -19.386 -2.138  1.00 13.67 ?  36  VAL   B HG13 1 
ATOM   4683 H  HG21 . VAL   B 1 36  ? 41.243 -19.460 -4.886  1.00 13.53 ?  36  VAL   B HG21 1 
ATOM   4684 H  HG22 . VAL   B 1 36  ? 41.974 -18.127 -4.423  1.00 13.53 ?  36  VAL   B HG22 1 
ATOM   4685 H  HG23 . VAL   B 1 36  ? 42.402 -18.839 -5.777  1.00 13.53 ?  36  VAL   B HG23 1 
ATOM   4686 N  N    . ASN   B 1 37  ? 45.670 -19.314 -1.974  1.00 10.23 ?  37  ASN   B N    1 
ATOM   4687 C  CA   . ASN   B 1 37  ? 46.418 -20.036 -0.958  1.00 10.67 ?  37  ASN   B CA   1 
ATOM   4688 C  C    . ASN   B 1 37  ? 45.465 -20.705 0.025   1.00 10.90 ?  37  ASN   B C    1 
ATOM   4689 O  O    . ASN   B 1 37  ? 44.456 -20.121 0.436   1.00 11.29 ?  37  ASN   B O    1 
ATOM   4690 C  CB   . ASN   B 1 37  ? 47.346 -19.088 -0.196  1.00 10.44 ?  37  ASN   B CB   1 
ATOM   4691 C  CG   . ASN   B 1 37  ? 48.198 -19.804 0.821   1.00 10.92 ?  37  ASN   B CG   1 
ATOM   4692 O  OD1  . ASN   B 1 37  ? 48.531 -20.983 0.647   1.00 11.99 ?  37  ASN   B OD1  1 
ATOM   4693 N  ND2  . ASN   B 1 37  ? 48.544 -19.109 1.892   1.00 11.07 ?  37  ASN   B ND2  1 
ATOM   4694 H  H    . ASN   B 1 37  ? 45.386 -18.545 -1.704  1.00 12.29 ?  37  ASN   B H    1 
ATOM   4695 H  HA   . ASN   B 1 37  ? 46.956 -20.726 -1.370  1.00 12.82 ?  37  ASN   B HA   1 
ATOM   4696 H  HB2  . ASN   B 1 37  ? 47.942 -18.659 -0.828  1.00 12.55 ?  37  ASN   B HB2  1 
ATOM   4697 H  HB3  . ASN   B 1 37  ? 46.817 -18.427 0.272   1.00 12.55 ?  37  ASN   B HB3  1 
ATOM   4698 H  HD21 . ASN   B 1 37  ? 49.037 -19.471 2.501   1.00 13.30 ?  37  ASN   B HD21 1 
ATOM   4699 H  HD22 . ASN   B 1 37  ? 48.299 -18.294 1.979   1.00 13.30 ?  37  ASN   B HD22 1 
ATOM   4700 N  N    . ALA   B 1 38  ? 45.808 -21.935 0.411   1.00 11.24 ?  38  ALA   B N    1 
ATOM   4701 C  CA   . ALA   B 1 38  ? 45.153 -22.670 1.496   1.00 11.57 ?  38  ALA   B CA   1 
ATOM   4702 C  C    . ALA   B 1 38  ? 45.753 -22.186 2.816   1.00 11.26 ?  38  ALA   B C    1 
ATOM   4703 O  O    . ALA   B 1 38  ? 46.654 -22.798 3.399   1.00 12.40 ?  38  ALA   B O    1 
ATOM   4704 C  CB   . ALA   B 1 38  ? 45.367 -24.167 1.312   1.00 13.27 ?  38  ALA   B CB   1 
ATOM   4705 H  H    . ALA   B 1 38  ? 46.454 -22.377 0.054   1.00 13.51 ?  38  ALA   B H    1 
ATOM   4706 H  HA   . ALA   B 1 38  ? 44.204 -22.480 1.494   1.00 13.91 ?  38  ALA   B HA   1 
ATOM   4707 H  HB1  . ALA   B 1 38  ? 44.924 -24.638 2.042   1.00 15.94 ?  38  ALA   B HB1  1 
ATOM   4708 H  HB2  . ALA   B 1 38  ? 44.980 -24.438 0.467   1.00 15.94 ?  38  ALA   B HB2  1 
ATOM   4709 H  HB3  . ALA   B 1 38  ? 46.314 -24.358 1.326   1.00 15.94 ?  38  ALA   B HB3  1 
ATOM   4710 N  N    . ALA   B 1 39  ? 45.240 -21.047 3.285   1.00 11.07 ?  39  ALA   B N    1 
ATOM   4711 C  CA   . ALA   B 1 39  ? 45.794 -20.313 4.412   1.00 11.53 ?  39  ALA   B CA   1 
ATOM   4712 C  C    . ALA   B 1 39  ? 45.179 -20.759 5.735   1.00 11.36 ?  39  ALA   B C    1 
ATOM   4713 O  O    . ALA   B 1 39  ? 44.144 -21.424 5.783   1.00 12.43 ?  39  ALA   B O    1 
ATOM   4714 C  CB   . ALA   B 1 39  ? 45.549 -18.810 4.223   1.00 11.92 ?  39  ALA   B CB   1 
ATOM   4715 H  H    . ALA   B 1 39  ? 44.540 -20.673 2.948   1.00 13.30 ?  39  ALA   B H    1 
ATOM   4716 H  HA   . ALA   B 1 39  ? 46.749 -20.459 4.452   1.00 13.86 ?  39  ALA   B HA   1 
ATOM   4717 H  HB1  . ALA   B 1 39  ? 45.924 -18.328 4.979   1.00 14.32 ?  39  ALA   B HB1  1 
ATOM   4718 H  HB2  . ALA   B 1 39  ? 45.979 -18.516 3.402   1.00 14.32 ?  39  ALA   B HB2  1 
ATOM   4719 H  HB3  . ALA   B 1 39  ? 44.594 -18.644 4.169   1.00 14.32 ?  39  ALA   B HB3  1 
ATOM   4720 N  N    . ASN   B 1 40  ? 45.831 -20.361 6.821   1.00 11.97 ?  40  ASN   B N    1 
ATOM   4721 C  CA   . ASN   B 1 40  ? 45.264 -20.396 8.159   1.00 12.88 ?  40  ASN   B CA   1 
ATOM   4722 C  C    . ASN   B 1 40  ? 45.066 -18.965 8.665   1.00 12.47 ?  40  ASN   B C    1 
ATOM   4723 O  O    . ASN   B 1 40  ? 45.475 -17.992 8.029   1.00 12.28 ?  40  ASN   B O    1 
ATOM   4724 C  CB   . ASN   B 1 40  ? 46.115 -21.256 9.107   1.00 13.37 ?  40  ASN   B CB   1 
ATOM   4725 C  CG   . ASN   B 1 40  ? 47.557 -20.828 9.150   1.00 14.60 ?  40  ASN   B CG   1 
ATOM   4726 O  OD1  . ASN   B 1 40  ? 47.857 -19.642 9.275   1.00 16.71 ?  40  ASN   B OD1  1 
ATOM   4727 N  ND2  . ASN   B 1 40  ? 48.464 -21.786 9.052   1.00 15.11 ?  40  ASN   B ND2  1 
ATOM   4728 H  H    . ASN   B 1 40  ? 46.637 -20.057 6.804   1.00 14.39 ?  40  ASN   B H    1 
ATOM   4729 H  HA   . ASN   B 1 40  ? 44.384 -20.796 8.110   1.00 15.48 ?  40  ASN   B HA   1 
ATOM   4730 H  HB2  . ASN   B 1 40  ? 45.751 -21.190 10.002  1.00 16.06 ?  40  ASN   B HB2  1 
ATOM   4731 H  HB3  . ASN   B 1 40  ? 46.080 -22.178 8.801   1.00 16.06 ?  40  ASN   B HB3  1 
ATOM   4732 H  HD21 . ASN   B 1 40  ? 49.300 -21.590 9.076   1.00 18.15 ?  40  ASN   B HD21 1 
ATOM   4733 H  HD22 . ASN   B 1 40  ? 48.215 -22.605 8.965   1.00 18.15 ?  40  ASN   B HD22 1 
ATOM   4734 N  N    . VAL   B 1 41  ? 44.410 -18.828 9.817   1.00 12.86 ?  41  VAL   B N    1 
ATOM   4735 C  CA   . VAL   B 1 41  ? 43.950 -17.505 10.255  1.00 13.81 ?  41  VAL   B CA   1 
ATOM   4736 C  C    . VAL   B 1 41  ? 45.101 -16.546 10.540  1.00 13.30 ?  41  VAL   B C    1 
ATOM   4737 O  O    . VAL   B 1 41  ? 44.918 -15.325 10.465  1.00 13.49 ?  41  VAL   B O    1 
ATOM   4738 C  CB   . VAL   B 1 41  ? 42.991 -17.586 11.462  1.00 15.34 ?  41  VAL   B CB   1 
ATOM   4739 C  CG1  . VAL   B 1 41  ? 41.688 -18.280 11.080  1.00 16.00 ?  41  VAL   B CG1  1 
ATOM   4740 C  CG2  . VAL   B 1 41  ? 43.670 -18.258 12.650  1.00 16.31 ?  41  VAL   B CG2  1 
ATOM   4741 H  H    . VAL   B 1 41  ? 44.216 -19.471 10.345  1.00 15.46 ?  41  VAL   B H    1 
ATOM   4742 H  HA   . VAL   B 1 41  ? 43.438 -17.118 9.527   1.00 16.59 ?  41  VAL   B HA   1 
ATOM   4743 H  HB   . VAL   B 1 41  ? 42.763 -16.684 11.732  1.00 18.43 ?  41  VAL   B HB   1 
ATOM   4744 H  HG11 . VAL   B 1 41  ? 41.096 -18.289 11.850  1.00 19.22 ?  41  VAL   B HG11 1 
ATOM   4745 H  HG12 . VAL   B 1 41  ? 41.273 -17.801 10.348  1.00 19.22 ?  41  VAL   B HG12 1 
ATOM   4746 H  HG13 . VAL   B 1 41  ? 41.884 -19.194 10.809  1.00 19.22 ?  41  VAL   B HG13 1 
ATOM   4747 H  HG21 . VAL   B 1 41  ? 43.046 -18.303 13.387  1.00 19.59 ?  41  VAL   B HG21 1 
ATOM   4748 H  HG22 . VAL   B 1 41  ? 43.944 -19.154 12.392  1.00 19.59 ?  41  VAL   B HG22 1 
ATOM   4749 H  HG23 . VAL   B 1 41  ? 44.448 -17.737 12.903  1.00 19.59 ?  41  VAL   B HG23 1 
ATOM   4750 N  N    . TYR   B 1 42  ? 46.274 -17.061 10.913  1.00 13.74 ?  42  TYR   B N    1 
ATOM   4751 C  CA   . TYR   B 1 42  ? 47.428 -16.216 11.185  1.00 13.91 ?  42  TYR   B CA   1 
ATOM   4752 C  C    . TYR   B 1 42  ? 48.394 -16.143 10.004  1.00 13.34 ?  42  TYR   B C    1 
ATOM   4753 O  O    . TYR   B 1 42  ? 49.486 -15.573 10.139  1.00 14.40 ?  42  TYR   B O    1 
ATOM   4754 C  CB   . TYR   B 1 42  ? 48.116 -16.634 12.491  1.00 16.15 ?  42  TYR   B CB   1 
ATOM   4755 C  CG   . TYR   B 1 42  ? 47.533 -15.921 13.714  1.00 16.17 ?  42  TYR   B CG   1 
ATOM   4756 C  CD1  . TYR   B 1 42  ? 47.753 -14.562 13.907  1.00 15.31 ?  42  TYR   B CD1  1 
ATOM   4757 C  CD2  . TYR   B 1 42  ? 46.766 -16.592 14.658  1.00 17.77 ?  42  TYR   B CD2  1 
ATOM   4758 C  CE1  . TYR   B 1 42  ? 47.240 -13.891 14.998  1.00 16.28 ?  42  TYR   B CE1  1 
ATOM   4759 C  CE2  . TYR   B 1 42  ? 46.246 -15.921 15.772  1.00 17.73 ?  42  TYR   B CE2  1 
ATOM   4760 C  CZ   . TYR   B 1 42  ? 46.489 -14.563 15.929  1.00 17.91 ?  42  TYR   B CZ   1 
ATOM   4761 O  OH   . TYR   B 1 42  ? 46.002 -13.860 17.019  1.00 20.29 ?  42  TYR   B OH   1 
ATOM   4762 H  H    . TYR   B 1 42  ? 46.422 -17.910 11.000  1.00 16.51 ?  42  TYR   B H    1 
ATOM   4763 H  HA   . TYR   B 1 42  ? 47.095 -15.319 11.321  1.00 16.71 ?  42  TYR   B HA   1 
ATOM   4764 H  HB2  . TYR   B 1 42  ? 48.004 -17.588 12.618  1.00 19.40 ?  42  TYR   B HB2  1 
ATOM   4765 H  HB3  . TYR   B 1 42  ? 49.058 -16.413 12.430  1.00 19.40 ?  42  TYR   B HB3  1 
ATOM   4766 H  HD1  . TYR   B 1 42  ? 48.266 -14.089 13.281  1.00 18.39 ?  42  TYR   B HD1  1 
ATOM   4767 H  HD2  . TYR   B 1 42  ? 46.602 -17.503 14.551  1.00 21.34 ?  42  TYR   B HD2  1 
ATOM   4768 H  HE1  . TYR   B 1 42  ? 47.409 -12.982 15.101  1.00 19.56 ?  42  TYR   B HE1  1 
ATOM   4769 H  HE2  . TYR   B 1 42  ? 45.733 -16.381 16.397  1.00 21.30 ?  42  TYR   B HE2  1 
ATOM   4770 H  HH   . TYR   B 1 42  ? 46.237 -13.053 16.962  1.00 24.37 ?  42  TYR   B HH   1 
ATOM   4771 N  N    . LEU   B 1 43  ? 47.994 -16.662 8.845   1.00 11.98 ?  43  LEU   B N    1 
ATOM   4772 C  CA   . LEU   B 1 43  ? 48.812 -16.596 7.637   1.00 11.99 ?  43  LEU   B CA   1 
ATOM   4773 C  C    . LEU   B 1 43  ? 50.226 -17.103 7.898   1.00 12.33 ?  43  LEU   B C    1 
ATOM   4774 O  O    . LEU   B 1 43  ? 51.210 -16.510 7.450   1.00 13.45 ?  43  LEU   B O    1 
ATOM   4775 C  CB   . LEU   B 1 43  ? 48.832 -15.193 7.025   1.00 12.29 ?  43  LEU   B CB   1 
ATOM   4776 C  CG   . LEU   B 1 43  ? 47.475 -14.572 6.668   1.00 12.65 ?  43  LEU   B CG   1 
ATOM   4777 C  CD1  . LEU   B 1 43  ? 47.679 -13.173 6.080   1.00 13.94 ?  43  LEU   B CD1  1 
ATOM   4778 C  CD2  . LEU   B 1 43  ? 46.693 -15.459 5.711   1.00 12.85 ?  43  LEU   B CD2  1 
ATOM   4779 H  H    . LEU   B 1 43  ? 47.248 -17.081 8.733   1.00 14.39 ?  43  LEU   B H    1 
ATOM   4780 H  HA   . LEU   B 1 43  ? 48.414 -17.188 6.975   1.00 14.40 ?  43  LEU   B HA   1 
ATOM   4781 H  HB2  . LEU   B 1 43  ? 49.266 -14.596 7.650   1.00 14.77 ?  43  LEU   B HB2  1 
ATOM   4782 H  HB3  . LEU   B 1 43  ? 49.350 -15.232 6.204   1.00 14.77 ?  43  LEU   B HB3  1 
ATOM   4783 H  HG   . LEU   B 1 43  ? 46.951 -14.478 7.477   1.00 15.20 ?  43  LEU   B HG   1 
ATOM   4784 H  HD11 . LEU   B 1 43  ? 46.813 -12.791 5.863   1.00 16.75 ?  43  LEU   B HD11 1 
ATOM   4785 H  HD12 . LEU   B 1 43  ? 48.126 -12.617 6.739   1.00 16.75 ?  43  LEU   B HD12 1 
ATOM   4786 H  HD13 . LEU   B 1 43  ? 48.221 -13.240 5.280   1.00 16.75 ?  43  LEU   B HD13 1 
ATOM   4787 H  HD21 . LEU   B 1 43  ? 45.889 -14.994 5.429   1.00 15.44 ?  43  LEU   B HD21 1 
ATOM   4788 H  HD22 . LEU   B 1 43  ? 47.246 -15.659 4.938   1.00 15.44 ?  43  LEU   B HD22 1 
ATOM   4789 H  HD23 . LEU   B 1 43  ? 46.455 -16.283 6.165   1.00 15.44 ?  43  LEU   B HD23 1 
ATOM   4790 N  N    . LYS   B 1 44  ? 50.324 -18.221 8.619   1.00 12.48 ?  44  LYS   B N    1 
ATOM   4791 C  CA   . LYS   B 1 44  ? 51.591 -18.897 8.875   1.00 13.35 ?  44  LYS   B CA   1 
ATOM   4792 C  C    . LYS   B 1 44  ? 51.710 -20.015 7.852   1.00 12.78 ?  44  LYS   B C    1 
ATOM   4793 O  O    . LYS   B 1 44  ? 51.020 -21.033 7.941   1.00 14.02 ?  44  LYS   B O    1 
ATOM   4794 C  CB   . LYS   B 1 44  ? 51.620 -19.407 10.311  1.00 15.02 ?  44  LYS   B CB   1 
ATOM   4795 C  CG   . LYS   B 1 44  ? 51.837 -18.297 11.328  1.00 17.68 ?  44  LYS   B CG   1 
ATOM   4796 C  CD   . LYS   B 1 44  ? 53.047 -17.450 10.904  1.00 21.32 ?  44  LYS   B CD   1 
ATOM   4797 C  CE   . LYS   B 1 44  ? 53.562 -16.529 11.974  1.00 24.46 ?  44  LYS   B CE   1 
ATOM   4798 N  NZ   . LYS   B 1 44  ? 54.770 -15.771 11.550  1.00 25.64 ?  44  LYS   B NZ   1 
ATOM   4799 H  H    . LYS   B 1 44  ? 49.649 -18.610 8.987   1.00 15.00 ?  44  LYS   B H    1 
ATOM   4800 H  HA   . LYS   B 1 44  ? 52.322 -18.287 8.710   1.00 16.04 ?  44  LYS   B HA   1 
ATOM   4801 H  HB2  . LYS   B 1 44  ? 50.762 -19.829 10.516  1.00 18.04 ?  44  LYS   B HB2  1 
ATOM   4802 H  HB3  . LYS   B 1 44  ? 52.333 -20.049 10.411  1.00 18.04 ?  44  LYS   B HB3  1 
ATOM   4803 H  HG2  . LYS   B 1 44  ? 51.053 -17.729 11.369  1.00 21.23 ?  44  LYS   B HG2  1 
ATOM   4804 H  HG3  . LYS   B 1 44  ? 52.021 -18.689 12.201  1.00 21.23 ?  44  LYS   B HG3  1 
ATOM   4805 H  HD2  . LYS   B 1 44  ? 53.763 -18.057 10.628  1.00 25.60 ?  44  LYS   B HD2  1 
ATOM   4806 H  HD3  . LYS   B 1 44  ? 52.782 -16.898 10.151  1.00 25.60 ?  44  LYS   B HD3  1 
ATOM   4807 H  HE2  . LYS   B 1 44  ? 52.868 -15.895 12.194  1.00 29.38 ?  44  LYS   B HE2  1 
ATOM   4808 H  HE3  . LYS   B 1 44  ? 53.805 -17.060 12.739  1.00 29.38 ?  44  LYS   B HE3  1 
ATOM   4809 H  HZ1  . LYS   B 1 44  ? 55.034 -15.233 12.207  1.00 30.79 ?  44  LYS   B HZ1  1 
ATOM   4810 H  HZ2  . LYS   B 1 44  ? 55.432 -16.332 11.351  1.00 30.79 ?  44  LYS   B HZ2  1 
ATOM   4811 H  HZ3  . LYS   B 1 44  ? 54.587 -15.277 10.829  1.00 30.79 ?  44  LYS   B HZ3  1 
ATOM   4812 N  N    . HIS   B 1 45  ? 52.558 -19.801 6.850   1.00 12.51 ?  45  HIS   B N    1 
ATOM   4813 C  CA   . HIS   B 1 45  ? 52.578 -20.634 5.646   1.00 12.62 ?  45  HIS   B CA   1 
ATOM   4814 C  C    . HIS   B 1 45  ? 53.603 -21.750 5.799   1.00 14.62 ?  45  HIS   B C    1 
ATOM   4815 O  O    . HIS   B 1 45  ? 54.662 -21.758 5.180   1.00 17.22 ?  45  HIS   B O    1 
ATOM   4816 C  CB   . HIS   B 1 45  ? 52.894 -19.783 4.429   1.00 12.77 ?  45  HIS   B CB   1 
ATOM   4817 C  CG   . HIS   B 1 45  ? 52.025 -18.583 4.318   1.00 12.82 ?  45  HIS   B CG   1 
ATOM   4818 N  ND1  . HIS   B 1 45  ? 50.648 -18.663 4.291   1.00 12.72 ?  45  HIS   B ND1  1 
ATOM   4819 C  CD2  . HIS   B 1 45  ? 52.342 -17.270 4.246   1.00 13.38 ?  45  HIS   B CD2  1 
ATOM   4820 C  CE1  . HIS   B 1 45  ? 50.161 -17.440 4.192   1.00 12.38 ?  45  HIS   B CE1  1 
ATOM   4821 N  NE2  . HIS   B 1 45  ? 51.164 -16.578 4.156   1.00 13.13 ?  45  HIS   B NE2  1 
ATOM   4822 H  H    . HIS   B 1 45  ? 53.126 -19.159 6.837   1.00 15.03 ?  45  HIS   B H    1 
ATOM   4823 H  HA   . HIS   B 1 45  ? 51.699 -21.035 5.515   1.00 15.17 ?  45  HIS   B HA   1 
ATOM   4824 H  HB2  . HIS   B 1 45  ? 53.813 -19.486 4.481   1.00 15.35 ?  45  HIS   B HB2  1 
ATOM   4825 H  HB3  . HIS   B 1 45  ? 52.767 -20.324 3.626   1.00 15.35 ?  45  HIS   B HB3  1 
ATOM   4826 H  HD2  . HIS   B 1 45  ? 53.197 -16.905 4.250   1.00 16.07 ?  45  HIS   B HD2  1 
ATOM   4827 H  HE1  . HIS   B 1 45  ? 49.256 -17.221 4.140   1.00 14.88 ?  45  HIS   B HE1  1 
ATOM   4828 H  HE2  . HIS   B 1 45  ? 51.085 -15.723 4.107   1.00 15.77 ?  45  HIS   B HE2  1 
ATOM   4829 N  N    A GLY   B 1 46  ? 53.238 -22.732 6.615   0.62 15.67 ?  46  GLY   B N    1 
ATOM   4830 N  N    B GLY   B 1 46  ? 53.252 -22.715 6.636   0.38 15.50 ?  46  GLY   B N    1 
ATOM   4831 C  CA   A GLY   B 1 46  ? 54.173 -23.774 6.997   0.62 17.39 ?  46  GLY   B CA   1 
ATOM   4832 C  CA   B GLY   B 1 46  ? 54.181 -23.775 6.961   0.38 16.72 ?  46  GLY   B CA   1 
ATOM   4833 C  C    A GLY   B 1 46  ? 54.202 -25.027 6.144   0.62 19.01 ?  46  GLY   B C    1 
ATOM   4834 C  C    B GLY   B 1 46  ? 54.182 -24.928 5.978   0.38 18.07 ?  46  GLY   B C    1 
ATOM   4835 O  O    A GLY   B 1 46  ? 55.282 -25.513 5.794   0.62 21.37 ?  46  GLY   B O    1 
ATOM   4836 O  O    B GLY   B 1 46  ? 55.198 -25.212 5.336   0.38 18.73 ?  46  GLY   B O    1 
ATOM   4837 H  H    A GLY   B 1 46  ? 52.457 -22.802 6.974   0.62 18.83 ?  46  GLY   B H    1 
ATOM   4838 H  H    B GLY   B 1 46  ? 52.484 -22.769 7.027   0.38 18.62 ?  46  GLY   B H    1 
ATOM   4839 H  HA2  A GLY   B 1 46  ? 55.065 -23.397 7.003   0.62 20.89 ?  46  GLY   B HA2  1 
ATOM   4840 H  HA2  B GLY   B 1 46  ? 55.076 -23.404 6.992   0.38 20.09 ?  46  GLY   B HA2  1 
ATOM   4841 H  HA3  A GLY   B 1 46  ? 53.963 -24.059 7.896   0.62 20.89 ?  46  GLY   B HA3  1 
ATOM   4842 H  HA3  B GLY   B 1 46  ? 53.965 -24.115 7.842   0.38 20.09 ?  46  GLY   B HA3  1 
ATOM   4843 N  N    . GLY   B 1 47  ? 53.036 -25.590 5.830   1.00 19.03 ?  47  GLY   B N    1 
ATOM   4844 C  CA   . GLY   B 1 47  ? 52.963 -26.865 5.148   1.00 17.12 ?  47  GLY   B CA   1 
ATOM   4845 C  C    . GLY   B 1 47  ? 52.052 -26.841 3.938   1.00 14.95 ?  47  GLY   B C    1 
ATOM   4846 O  O    . GLY   B 1 47  ? 51.399 -25.838 3.648   1.00 14.97 ?  47  GLY   B O    1 
ATOM   4847 H  H    A GLY   B 1 47  ? 52.265 -25.256 6.030   0.62 22.86 ?  47  GLY   B H    1 
ATOM   4848 H  H    B GLY   B 1 47  ? 52.272 -25.304 6.115   0.38 22.86 ?  47  GLY   B H    1 
ATOM   4849 H  HA2  . GLY   B 1 47  ? 53.846 -27.128 4.848   1.00 20.56 ?  47  GLY   B HA2  1 
ATOM   4850 H  HA3  . GLY   B 1 47  ? 52.636 -27.537 5.764   1.00 20.56 ?  47  GLY   B HA3  1 
ATOM   4851 N  N    . GLY   B 1 48  ? 51.995 -27.986 3.256   1.00 13.77 ?  48  GLY   B N    1 
ATOM   4852 C  CA   . GLY   B 1 48  ? 51.080 -28.129 2.142   1.00 13.58 ?  48  GLY   B CA   1 
ATOM   4853 C  C    . GLY   B 1 48  ? 51.222 -27.016 1.131   1.00 12.85 ?  48  GLY   B C    1 
ATOM   4854 O  O    . GLY   B 1 48  ? 52.325 -26.549 0.823   1.00 13.27 ?  48  GLY   B O    1 
ATOM   4855 H  H    . GLY   B 1 48  ? 52.475 -28.676 3.421   1.00 16.54 ?  48  GLY   B H    1 
ATOM   4856 H  HA2  . GLY   B 1 48  ? 51.247 -28.979 1.696   1.00 16.32 ?  48  GLY   B HA2  1 
ATOM   4857 H  HA3  . GLY   B 1 48  ? 50.166 -28.133 2.467   1.00 16.32 ?  48  GLY   B HA3  1 
ATOM   4858 N  N    . VAL   B 1 49  ? 50.080 -26.590 0.593   1.00 12.59 ?  49  VAL   B N    1 
ATOM   4859 C  CA   . VAL   B 1 49  ? 50.073 -25.567 -0.451  1.00 12.44 ?  49  VAL   B CA   1 
ATOM   4860 C  C    . VAL   B 1 49  ? 50.732 -24.281 0.040   1.00 11.82 ?  49  VAL   B C    1 
ATOM   4861 O  O    . VAL   B 1 49  ? 51.530 -23.666 -0.677  1.00 12.45 ?  49  VAL   B O    1 
ATOM   4862 C  CB   . VAL   B 1 49  ? 48.634 -25.312 -0.944  1.00 13.90 ?  49  VAL   B CB   1 
ATOM   4863 C  CG1  . VAL   B 1 49  ? 48.565 -24.062 -1.821  1.00 14.04 ?  49  VAL   B CG1  1 
ATOM   4864 C  CG2  . VAL   B 1 49  ? 48.103 -26.532 -1.688  1.00 15.69 ?  49  VAL   B CG2  1 
ATOM   4865 H  H    . VAL   B 1 49  ? 49.295 -26.878 0.805   1.00 15.13 ?  49  VAL   B H    1 
ATOM   4866 H  HA   . VAL   B 1 49  ? 50.585 -25.888 -1.208  1.00 14.95 ?  49  VAL   B HA   1 
ATOM   4867 H  HB   . VAL   B 1 49  ? 48.062 -25.163 -0.178  1.00 16.70 ?  49  VAL   B HB   1 
ATOM   4868 H  HG11 . VAL   B 1 49  ? 47.733 -24.072 -2.323  1.00 16.86 ?  49  VAL   B HG11 1 
ATOM   4869 H  HG12 . VAL   B 1 49  ? 48.592 -23.271 -1.255  1.00 16.86 ?  49  VAL   B HG12 1 
ATOM   4870 H  HG13 . VAL   B 1 49  ? 49.316 -24.057 -2.433  1.00 16.86 ?  49  VAL   B HG13 1 
ATOM   4871 H  HG21 . VAL   B 1 49  ? 47.200 -26.350 -1.994  1.00 18.85 ?  49  VAL   B HG21 1 
ATOM   4872 H  HG22 . VAL   B 1 49  ? 48.678 -26.715 -2.448  1.00 18.85 ?  49  VAL   B HG22 1 
ATOM   4873 H  HG23 . VAL   B 1 49  ? 48.101 -27.292 -1.085  1.00 18.85 ?  49  VAL   B HG23 1 
ATOM   4874 N  N    . ALA   B 1 50  ? 50.384 -23.835 1.249   1.00 11.61 ?  50  ALA   B N    1 
ATOM   4875 C  CA   . ALA   B 1 50  ? 50.908 -22.561 1.731   1.00 11.44 ?  50  ALA   B CA   1 
ATOM   4876 C  C    . ALA   B 1 50  ? 52.426 -22.597 1.836   1.00 11.79 ?  50  ALA   B C    1 
ATOM   4877 O  O    . ALA   B 1 50  ? 53.108 -21.633 1.467   1.00 11.86 ?  50  ALA   B O    1 
ATOM   4878 C  CB   . ALA   B 1 50  ? 50.282 -22.210 3.076   1.00 12.11 ?  50  ALA   B CB   1 
ATOM   4879 H  H    . ALA   B 1 50  ? 49.856 -24.240 1.796   1.00 13.95 ?  50  ALA   B H    1 
ATOM   4880 H  HA   . ALA   B 1 50  ? 50.679 -21.866 1.102   1.00 13.75 ?  50  ALA   B HA   1 
ATOM   4881 H  HB1  . ALA   B 1 50  ? 50.643 -21.362 3.381   1.00 14.56 ?  50  ALA   B HB1  1 
ATOM   4882 H  HB2  . ALA   B 1 50  ? 49.321 -22.138 2.966   1.00 14.56 ?  50  ALA   B HB2  1 
ATOM   4883 H  HB3  . ALA   B 1 50  ? 50.491 -22.907 3.717   1.00 14.56 ?  50  ALA   B HB3  1 
ATOM   4884 N  N    . GLY   B 1 51  ? 52.975 -23.690 2.355   1.00 12.37 ?  51  GLY   B N    1 
ATOM   4885 C  CA   . GLY   B 1 51  ? 54.419 -23.796 2.424   1.00 13.22 ?  51  GLY   B CA   1 
ATOM   4886 C  C    . GLY   B 1 51  ? 55.066 -23.745 1.054   1.00 13.10 ?  51  GLY   B C    1 
ATOM   4887 O  O    . GLY   B 1 51  ? 56.114 -23.117 0.874   1.00 13.52 ?  51  GLY   B O    1 
ATOM   4888 H  H    . GLY   B 1 51  ? 52.551 -24.375 2.659   1.00 14.87 ?  51  GLY   B H    1 
ATOM   4889 H  HA2  . GLY   B 1 51  ? 54.777 -23.064 2.954   1.00 15.88 ?  51  GLY   B HA2  1 
ATOM   4890 H  HA3  . GLY   B 1 51  ? 54.674 -24.632 2.849   1.00 15.88 ?  51  GLY   B HA3  1 
ATOM   4891 N  N    . ALA   B 1 52  ? 54.464 -24.415 0.074   1.00 12.45 ?  52  ALA   B N    1 
ATOM   4892 C  CA   . ALA   B 1 52  ? 55.025 -24.430 -1.271  1.00 12.97 ?  52  ALA   B CA   1 
ATOM   4893 C  C    . ALA   B 1 52  ? 54.945 -23.055 -1.925  1.00 12.27 ?  52  ALA   B C    1 
ATOM   4894 O  O    . ALA   B 1 52  ? 55.916 -22.605 -2.552  1.00 13.12 ?  52  ALA   B O    1 
ATOM   4895 C  CB   . ALA   B 1 52  ? 54.310 -25.475 -2.120  1.00 13.32 ?  52  ALA   B CB   1 
ATOM   4896 H  H    . ALA   B 1 52  ? 53.735 -24.862 0.162   1.00 14.96 ?  52  ALA   B H    1 
ATOM   4897 H  HA   . ALA   B 1 52  ? 55.958 -24.678 -1.217  1.00 15.59 ?  52  ALA   B HA   1 
ATOM   4898 H  HB1  . ALA   B 1 52  ? 54.695 -25.471 -3.011  1.00 16.01 ?  52  ALA   B HB1  1 
ATOM   4899 H  HB2  . ALA   B 1 52  ? 54.430 -26.346 -1.712  1.00 16.01 ?  52  ALA   B HB2  1 
ATOM   4900 H  HB3  . ALA   B 1 52  ? 53.367 -25.255 -2.165  1.00 16.01 ?  52  ALA   B HB3  1 
ATOM   4901 N  N    . LEU   B 1 53  ? 53.800 -22.371 -1.808  1.00 11.98 ?  53  LEU   B N    1 
ATOM   4902 C  CA   . LEU   B 1 53  ? 53.697 -21.030 -2.380  1.00 11.91 ?  53  LEU   B CA   1 
ATOM   4903 C  C    . LEU   B 1 53  ? 54.709 -20.091 -1.734  1.00 11.93 ?  53  LEU   B C    1 
ATOM   4904 O  O    . LEU   B 1 53  ? 55.416 -19.342 -2.422  1.00 12.68 ?  53  LEU   B O    1 
ATOM   4905 C  CB   . LEU   B 1 53  ? 52.273 -20.477 -2.216  1.00 12.67 ?  53  LEU   B CB   1 
ATOM   4906 C  CG   . LEU   B 1 53  ? 51.136 -21.217 -2.929  1.00 12.98 ?  53  LEU   B CG   1 
ATOM   4907 C  CD1  . LEU   B 1 53  ? 49.804 -20.586 -2.601  1.00 14.67 ?  53  LEU   B CD1  1 
ATOM   4908 C  CD2  . LEU   B 1 53  ? 51.350 -21.252 -4.437  1.00 14.93 ?  53  LEU   B CD2  1 
ATOM   4909 H  H    . LEU   B 1 53  ? 53.093 -22.648 -1.405  1.00 14.39 ?  53  LEU   B H    1 
ATOM   4910 H  HA   . LEU   B 1 53  ? 53.897 -21.079 -3.332  1.00 14.31 ?  53  LEU   B HA   1 
ATOM   4911 H  HB2  . LEU   B 1 53  ? 52.064 -20.473 -1.274  1.00 15.22 ?  53  LEU   B HB2  1 
ATOM   4912 H  HB3  . LEU   B 1 53  ? 52.269 -19.567 -2.552  1.00 15.22 ?  53  LEU   B HB3  1 
ATOM   4913 H  HG   . LEU   B 1 53  ? 51.109 -22.131 -2.608  1.00 15.60 ?  53  LEU   B HG   1 
ATOM   4914 H  HD11 . LEU   B 1 53  ? 49.099 -21.077 -3.059  1.00 17.63 ?  53  LEU   B HD11 1 
ATOM   4915 H  HD12 . LEU   B 1 53  ? 49.659 -20.630 -1.640  1.00 17.63 ?  53  LEU   B HD12 1 
ATOM   4916 H  HD13 . LEU   B 1 53  ? 49.807 -19.663 -2.892  1.00 17.63 ?  53  LEU   B HD13 1 
ATOM   4917 H  HD21 . LEU   B 1 53  ? 50.615 -21.737 -4.849  1.00 17.94 ?  53  LEU   B HD21 1 
ATOM   4918 H  HD22 . LEU   B 1 53  ? 51.380 -20.348 -4.776  1.00 17.94 ?  53  LEU   B HD22 1 
ATOM   4919 H  HD23 . LEU   B 1 53  ? 52.186 -21.709 -4.626  1.00 17.94 ?  53  LEU   B HD23 1 
ATOM   4920 N  N    . ASN   B 1 54  ? 54.796 -20.114 -0.409  1.00 11.58 ?  54  ASN   B N    1 
ATOM   4921 C  CA   . ASN   B 1 54  ? 55.714 -19.208 0.264   1.00 12.04 ?  54  ASN   B CA   1 
ATOM   4922 C  C    . ASN   B 1 54  ? 57.157 -19.493 -0.136  1.00 12.77 ?  54  ASN   B C    1 
ATOM   4923 O  O    . ASN   B 1 54  ? 57.934 -18.558 -0.377  1.00 13.21 ?  54  ASN   B O    1 
ATOM   4924 C  CB   . ASN   B 1 54  ? 55.561 -19.281 1.775   1.00 13.35 ?  54  ASN   B CB   1 
ATOM   4925 C  CG   . ASN   B 1 54  ? 56.538 -18.360 2.474   1.00 13.25 ?  54  ASN   B CG   1 
ATOM   4926 O  OD1  . ASN   B 1 54  ? 56.548 -17.155 2.222   1.00 13.57 ?  54  ASN   B OD1  1 
ATOM   4927 N  ND2  . ASN   B 1 54  ? 57.381 -18.916 3.332   1.00 14.71 ?  54  ASN   B ND2  1 
ATOM   4928 H  H    . ASN   B 1 54  ? 54.347 -20.636 0.107   1.00 13.92 ?  54  ASN   B H    1 
ATOM   4929 H  HA   . ASN   B 1 54  ? 55.507 -18.304 -0.012  1.00 14.47 ?  54  ASN   B HA   1 
ATOM   4930 H  HB2  . ASN   B 1 54  ? 54.662 -19.006 2.018   1.00 16.03 ?  54  ASN   B HB2  1 
ATOM   4931 H  HB3  . ASN   B 1 54  ? 55.731 -20.185 2.074   1.00 16.03 ?  54  ASN   B HB3  1 
ATOM   4932 H  HD21 . ASN   B 1 54  ? 57.960 -18.428 3.747   1.00 17.68 ?  54  ASN   B HD21 1 
ATOM   4933 H  HD22 . ASN   B 1 54  ? 57.355 -19.762 3.476   1.00 17.68 ?  54  ASN   B HD22 1 
ATOM   4934 N  N    . LYS   B 1 55  ? 57.543 -20.771 -0.192  1.00 13.40 ?  55  LYS   B N    1 
ATOM   4935 C  CA   . LYS   B 1 55  ? 58.896 -21.118 -0.616  1.00 14.15 ?  55  LYS   B CA   1 
ATOM   4936 C  C    . LYS   B 1 55  ? 59.186 -20.579 -2.010  1.00 14.25 ?  55  LYS   B C    1 
ATOM   4937 O  O    . LYS   B 1 55  ? 60.285 -20.077 -2.272  1.00 15.05 ?  55  LYS   B O    1 
ATOM   4938 C  CB   . LYS   B 1 55  ? 59.072 -22.636 -0.574  1.00 16.34 ?  55  LYS   B CB   1 
ATOM   4939 C  CG   . LYS   B 1 55  ? 60.444 -23.109 -1.024  1.00 20.80 ?  55  LYS   B CG   1 
ATOM   4940 C  CD   . LYS   B 1 55  ? 60.605 -24.613 -0.842  1.00 24.47 ?  55  LYS   B CD   1 
ATOM   4941 C  CE   . LYS   B 1 55  ? 60.630 -25.005 0.635   1.00 27.27 ?  55  LYS   B CE   1 
ATOM   4942 N  NZ   . LYS   B 1 55  ? 60.995 -26.427 0.836   1.00 28.63 ?  55  LYS   B NZ   1 
ATOM   4943 H  H    . LYS   B 1 55  ? 57.041 -21.443 -0.004  1.00 16.09 ?  55  LYS   B H    1 
ATOM   4944 H  HA   . LYS   B 1 55  ? 59.530 -20.725 -0.003  1.00 17.00 ?  55  LYS   B HA   1 
ATOM   4945 H  HB2  . LYS   B 1 55  ? 58.935 -22.935 0.338   1.00 19.63 ?  55  LYS   B HB2  1 
ATOM   4946 H  HB3  . LYS   B 1 55  ? 58.414 -23.049 -1.156  1.00 19.63 ?  55  LYS   B HB3  1 
ATOM   4947 H  HG2  . LYS   B 1 55  ? 60.566 -22.907 -1.966  1.00 24.98 ?  55  LYS   B HG2  1 
ATOM   4948 H  HG3  . LYS   B 1 55  ? 61.128 -22.666 -0.496  1.00 24.98 ?  55  LYS   B HG3  1 
ATOM   4949 H  HD2  . LYS   B 1 55  ? 59.858 -25.070 -1.263  1.00 29.38 ?  55  LYS   B HD2  1 
ATOM   4950 H  HD3  . LYS   B 1 55  ? 61.441 -24.902 -1.243  1.00 29.38 ?  55  LYS   B HD3  1 
ATOM   4951 H  HE2  . LYS   B 1 55  ? 61.280 -24.448 1.096   1.00 32.74 ?  55  LYS   B HE2  1 
ATOM   4952 H  HE3  . LYS   B 1 55  ? 59.746 -24.860 1.014   1.00 32.74 ?  55  LYS   B HE3  1 
ATOM   4953 H  HZ1  . LYS   B 1 55  ? 60.978 -26.622 1.704   1.00 34.38 ?  55  LYS   B HZ1  1 
ATOM   4954 H  HZ2  . LYS   B 1 55  ? 60.415 -26.949 0.409   1.00 34.38 ?  55  LYS   B HZ2  1 
ATOM   4955 H  HZ3  . LYS   B 1 55  ? 61.810 -26.576 0.519   1.00 34.38 ?  55  LYS   B HZ3  1 
ATOM   4956 N  N    . ALA   B 1 56  ? 58.212 -20.667 -2.919  1.00 13.76 ?  56  ALA   B N    1 
ATOM   4957 C  CA   . ALA   B 1 56  ? 58.432 -20.174 -4.275  1.00 14.52 ?  56  ALA   B CA   1 
ATOM   4958 C  C    . ALA   B 1 56  ? 58.718 -18.679 -4.279  1.00 14.49 ?  56  ALA   B C    1 
ATOM   4959 O  O    . ALA   B 1 56  ? 59.459 -18.190 -5.142  1.00 15.32 ?  56  ALA   B O    1 
ATOM   4960 C  CB   . ALA   B 1 56  ? 57.232 -20.499 -5.164  1.00 15.24 ?  56  ALA   B CB   1 
ATOM   4961 H  H    . ALA   B 1 56  ? 57.424 -20.984 -2.774  1.00 16.53 ?  56  ALA   B H    1 
ATOM   4962 H  HA   . ALA   B 1 56  ? 59.204 -20.620 -4.646  1.00 17.45 ?  56  ALA   B HA   1 
ATOM   4963 H  HB1  . ALA   B 1 56  ? 57.403 -20.169 -6.063  1.00 18.31 ?  56  ALA   B HB1  1 
ATOM   4964 H  HB2  . ALA   B 1 56  ? 57.108 -21.463 -5.189  1.00 18.31 ?  56  ALA   B HB2  1 
ATOM   4965 H  HB3  . ALA   B 1 56  ? 56.439 -20.075 -4.803  1.00 18.31 ?  56  ALA   B HB3  1 
ATOM   4966 N  N    . THR   B 1 57  ? 58.138 -17.937 -3.331  1.00 13.86 ?  57  THR   B N    1 
ATOM   4967 C  CA   . THR   B 1 57  ? 58.388 -16.502 -3.209  1.00 14.06 ?  57  THR   B CA   1 
ATOM   4968 C  C    . THR   B 1 57  ? 59.642 -16.173 -2.398  1.00 14.60 ?  57  THR   B C    1 
ATOM   4969 O  O    . THR   B 1 57  ? 59.877 -14.995 -2.104  1.00 15.10 ?  57  THR   B O    1 
ATOM   4970 C  CB   . THR   B 1 57  ? 57.188 -15.771 -2.576  1.00 13.09 ?  57  THR   B CB   1 
ATOM   4971 O  OG1  . THR   B 1 57  ? 57.167 -15.980 -1.158  1.00 13.72 ?  57  THR   B OG1  1 
ATOM   4972 C  CG2  . THR   B 1 57  ? 55.867 -16.203 -3.215  1.00 13.43 ?  57  THR   B CG2  1 
ATOM   4973 H  H    . THR   B 1 57  ? 57.580 -18.241 -2.749  1.00 16.65 ?  57  THR   B H    1 
ATOM   4974 H  HA   . THR   B 1 57  ? 58.507 -16.135 -4.099  1.00 16.89 ?  57  THR   B HA   1 
ATOM   4975 H  HB   . THR   B 1 57  ? 57.284 -14.818 -2.746  1.00 15.72 ?  57  THR   B HB   1 
ATOM   4976 H  HG1  . THR   B 1 57  ? 57.096 -16.801 -0.995  1.00 16.48 ?  57  THR   B HG1  1 
ATOM   4977 H  HG21 . THR   B 1 57  ? 55.148 -15.624 -2.928  1.00 16.14 ?  57  THR   B HG21 1 
ATOM   4978 H  HG22 . THR   B 1 57  ? 55.936 -16.167 -4.184  1.00 16.14 ?  57  THR   B HG22 1 
ATOM   4979 H  HG23 . THR   B 1 57  ? 55.657 -17.116 -2.955  1.00 16.14 ?  57  THR   B HG23 1 
ATOM   4980 N  N    . ASN   B 1 58  ? 60.441 -17.171 -2.031  1.00 15.67 ?  58  ASN   B N    1 
ATOM   4981 C  CA   . ASN   B 1 58  ? 61.642 -16.953 -1.226  1.00 18.46 ?  58  ASN   B CA   1 
ATOM   4982 C  C    . ASN   B 1 58  ? 61.309 -16.233 0.080   1.00 16.49 ?  58  ASN   B C    1 
ATOM   4983 O  O    . ASN   B 1 58  ? 62.047 -15.355 0.538   1.00 17.28 ?  58  ASN   B O    1 
ATOM   4984 C  CB   . ASN   B 1 58  ? 62.731 -16.209 -2.007  1.00 26.19 ?  58  ASN   B CB   1 
ATOM   4985 C  CG   . ASN   B 1 58  ? 64.108 -16.381 -1.394  1.00 36.07 ?  58  ASN   B CG   1 
ATOM   4986 O  OD1  . ASN   B 1 58  ? 64.414 -17.420 -0.810  1.00 38.51 ?  58  ASN   B OD1  1 
ATOM   4987 N  ND2  . ASN   B 1 58  ? 64.946 -15.360 -1.524  1.00 42.61 ?  58  ASN   B ND2  1 
ATOM   4988 H  H    . ASN   B 1 58  ? 60.307 -17.998 -2.234  1.00 18.83 ?  58  ASN   B H    1 
ATOM   4989 H  HA   . ASN   B 1 58  ? 62.006 -17.823 -0.998  1.00 22.17 ?  58  ASN   B HA   1 
ATOM   4990 H  HB2  . ASN   B 1 58  ? 62.763 -16.551 -2.916  1.00 31.45 ?  58  ASN   B HB2  1 
ATOM   4991 H  HB3  . ASN   B 1 58  ? 62.527 -15.262 -2.015  1.00 31.45 ?  58  ASN   B HB3  1 
ATOM   4992 H  HD21 . ASN   B 1 58  ? 65.739 -15.411 -1.195  1.00 51.15 ?  58  ASN   B HD21 1 
ATOM   4993 H  HD22 . ASN   B 1 58  ? 64.695 -14.650 -1.936  1.00 51.15 ?  58  ASN   B HD22 1 
ATOM   4994 N  N    . ASN   B 1 59  ? 60.184 -16.615 0.684   1.00 15.27 ?  59  ASN   B N    1 
ATOM   4995 C  CA   . ASN   B 1 59  ? 59.712 -16.147 1.986   1.00 15.26 ?  59  ASN   B CA   1 
ATOM   4996 C  C    . ASN   B 1 59  ? 59.107 -14.745 1.927   1.00 14.39 ?  59  ASN   B C    1 
ATOM   4997 O  O    . ASN   B 1 59  ? 58.684 -14.233 2.969   1.00 14.67 ?  59  ASN   B O    1 
ATOM   4998 C  CB   . ASN   B 1 59  ? 60.788 -16.199 3.086   1.00 16.16 ?  59  ASN   B CB   1 
ATOM   4999 C  CG   . ASN   B 1 59  ? 60.197 -16.358 4.470   1.00 16.90 ?  59  ASN   B CG   1 
ATOM   5000 O  OD1  . ASN   B 1 59  ? 59.363 -17.240 4.708   1.00 17.10 ?  59  ASN   B OD1  1 
ATOM   5001 N  ND2  . ASN   B 1 59  ? 60.620 -15.505 5.394   1.00 17.82 ?  59  ASN   B ND2  1 
ATOM   5002 H  H    . ASN   B 1 59  ? 59.638 -17.192 0.337   1.00 18.34 ?  59  ASN   B H    1 
ATOM   5003 H  HA   . ASN   B 1 59  ? 59.008 -16.748 2.276   1.00 18.33 ?  59  ASN   B HA   1 
ATOM   5004 H  HB2  . ASN   B 1 59  ? 61.378 -16.957 2.929   1.00 19.41 ?  59  ASN   B HB2  1 
ATOM   5005 H  HB3  . ASN   B 1 59  ? 61.300 -15.376 3.077   1.00 19.41 ?  59  ASN   B HB3  1 
ATOM   5006 H  HD21 . ASN   B 1 59  ? 60.317 -15.555 6.198   1.00 21.40 ?  59  ASN   B HD21 1 
ATOM   5007 H  HD22 . ASN   B 1 59  ? 61.203 -14.903 5.194   1.00 21.40 ?  59  ASN   B HD22 1 
ATOM   5008 N  N    . ALA   B 1 60  ? 59.035 -14.110 0.754   1.00 14.37 ?  60  ALA   B N    1 
ATOM   5009 C  CA   . ALA   B 1 60  ? 58.447 -12.775 0.689   1.00 14.41 ?  60  ALA   B CA   1 
ATOM   5010 C  C    . ALA   B 1 60  ? 56.976 -12.795 1.084   1.00 13.35 ?  60  ALA   B C    1 
ATOM   5011 O  O    . ALA   B 1 60  ? 56.472 -11.838 1.686   1.00 14.06 ?  60  ALA   B O    1 
ATOM   5012 C  CB   . ALA   B 1 60  ? 58.609 -12.189 -0.709  1.00 15.43 ?  60  ALA   B CB   1 
ATOM   5013 H  H    . ALA   B 1 60  ? 59.323 -14.428 0.010   1.00 17.27 ?  60  ALA   B H    1 
ATOM   5014 H  HA   . ALA   B 1 60  ? 58.913 -12.204 1.318   1.00 17.31 ?  60  ALA   B HA   1 
ATOM   5015 H  HB1  . ALA   B 1 60  ? 58.211 -11.310 -0.723  1.00 18.54 ?  60  ALA   B HB1  1 
ATOM   5016 H  HB2  . ALA   B 1 60  ? 59.556 -12.134 -0.917  1.00 18.54 ?  60  ALA   B HB2  1 
ATOM   5017 H  HB3  . ALA   B 1 60  ? 58.165 -12.771 -1.345  1.00 18.54 ?  60  ALA   B HB3  1 
ATOM   5018 N  N    . MET   B 1 61  ? 56.264 -13.869 0.734   1.00 13.10 ?  61  MET   B N    1 
ATOM   5019 C  CA   . MET   B 1 61  ? 54.868 -13.990 1.123   1.00 12.42 ?  61  MET   B CA   1 
ATOM   5020 C  C    . MET   B 1 61  ? 54.730 -13.982 2.642   1.00 12.34 ?  61  MET   B C    1 
ATOM   5021 O  O    . MET   B 1 61  ? 53.824 -13.330 3.184   1.00 12.43 ?  61  MET   B O    1 
ATOM   5022 C  CB   . MET   B 1 61  ? 54.294 -15.270 0.503   1.00 12.29 ?  61  MET   B CB   1 
ATOM   5023 C  CG   . MET   B 1 61  ? 52.857 -15.567 0.907   1.00 12.59 ?  61  MET   B CG   1 
ATOM   5024 S  SD   . MET   B 1 61  ? 52.207 -17.062 0.149   1.00 13.07 ?  61  MET   B SD   1 
ATOM   5025 C  CE   . MET   B 1 61  ? 51.957 -16.483 -1.524  1.00 14.54 ?  61  MET   B CE   1 
ATOM   5026 H  H    . MET   B 1 61  ? 56.569 -14.543 0.276   1.00 15.74 ?  61  MET   B H    1 
ATOM   5027 H  HA   . MET   B 1 61  ? 54.377 -13.245 0.748   1.00 14.92 ?  61  MET   B HA   1 
ATOM   5028 H  HB2  . MET   B 1 61  ? 54.318 -15.193 -0.467  1.00 14.77 ?  61  MET   B HB2  1 
ATOM   5029 H  HB3  . MET   B 1 61  ? 54.840 -16.027 0.777   1.00 14.77 ?  61  MET   B HB3  1 
ATOM   5030 H  HG2  . MET   B 1 61  ? 52.815 -15.683 1.869   1.00 15.13 ?  61  MET   B HG2  1 
ATOM   5031 H  HG3  . MET   B 1 61  ? 52.295 -14.825 0.637   1.00 15.13 ?  61  MET   B HG3  1 
ATOM   5032 H  HE1  . MET   B 1 61  ? 51.569 -17.198 -2.052  1.00 17.47 ?  61  MET   B HE1  1 
ATOM   5033 H  HE2  . MET   B 1 61  ? 51.358 -15.720 -1.512  1.00 17.47 ?  61  MET   B HE2  1 
ATOM   5034 H  HE3  . MET   B 1 61  ? 52.814 -16.223 -1.900  1.00 17.47 ?  61  MET   B HE3  1 
ATOM   5035 N  N    . GLN   B 1 62  ? 55.607 -14.701 3.349   1.00 12.38 ?  62  GLN   B N    1 
ATOM   5036 C  CA   . GLN   B 1 62  ? 55.503 -14.748 4.804   1.00 12.85 ?  62  GLN   B CA   1 
ATOM   5037 C  C    . GLN   B 1 62  ? 55.783 -13.387 5.425   1.00 12.94 ?  62  GLN   B C    1 
ATOM   5038 O  O    . GLN   B 1 62  ? 55.098 -12.977 6.369   1.00 13.52 ?  62  GLN   B O    1 
ATOM   5039 C  CB   . GLN   B 1 62  ? 56.461 -15.791 5.379   1.00 13.18 ?  62  GLN   B CB   1 
ATOM   5040 C  CG   . GLN   B 1 62  ? 56.229 -16.058 6.861   1.00 13.49 ?  62  GLN   B CG   1 
ATOM   5041 C  CD   . GLN   B 1 62  ? 54.851 -16.653 7.102   1.00 13.07 ?  62  GLN   B CD   1 
ATOM   5042 O  OE1  . GLN   B 1 62  ? 54.593 -17.803 6.742   1.00 14.04 ?  62  GLN   B OE1  1 
ATOM   5043 N  NE2  . GLN   B 1 62  ? 53.940 -15.858 7.660   1.00 13.26 ?  62  GLN   B NE2  1 
ATOM   5044 H  H    . GLN   B 1 62  ? 56.251 -15.158 3.012   1.00 14.87 ?  62  GLN   B H    1 
ATOM   5045 H  HA   . GLN   B 1 62  ? 54.599 -15.005 5.042   1.00 15.44 ?  62  GLN   B HA   1 
ATOM   5046 H  HB2  . GLN   B 1 62  ? 56.344 -16.628 4.901   1.00 15.84 ?  62  GLN   B HB2  1 
ATOM   5047 H  HB3  . GLN   B 1 62  ? 57.373 -15.475 5.270   1.00 15.84 ?  62  GLN   B HB3  1 
ATOM   5048 H  HG2  . GLN   B 1 62  ? 56.895 -16.690 7.175   1.00 16.21 ?  62  GLN   B HG2  1 
ATOM   5049 H  HG3  . GLN   B 1 62  ? 56.296 -15.226 7.350   1.00 16.21 ?  62  GLN   B HG3  1 
ATOM   5050 H  HE21 . GLN   B 1 62  ? 54.146 -15.058 7.884   1.00 15.93 ?  62  GLN   B HE21 1 
ATOM   5051 H  HE22 . GLN   B 1 62  ? 53.145 -16.157 7.803   1.00 15.93 ?  62  GLN   B HE22 1 
ATOM   5052 N  N    . VAL   B 1 63  ? 56.789 -12.672 4.919   1.00 13.44 ?  63  VAL   B N    1 
ATOM   5053 C  CA   . VAL   B 1 63  ? 57.096 -11.356 5.472   1.00 14.59 ?  63  VAL   B CA   1 
ATOM   5054 C  C    . VAL   B 1 63  ? 55.908 -10.422 5.287   1.00 13.63 ?  63  VAL   B C    1 
ATOM   5055 O  O    . VAL   B 1 63  ? 55.496 -9.711  6.213   1.00 14.12 ?  63  VAL   B O    1 
ATOM   5056 C  CB   . VAL   B 1 63  ? 58.388 -10.797 4.851   1.00 15.67 ?  63  VAL   B CB   1 
ATOM   5057 C  CG1  . VAL   B 1 63  ? 58.606 -9.356  5.299   1.00 16.23 ?  63  VAL   B CG1  1 
ATOM   5058 C  CG2  . VAL   B 1 63  ? 59.570 -11.663 5.258   1.00 16.37 ?  63  VAL   B CG2  1 
ATOM   5059 H  H    . VAL   B 1 63  ? 57.293 -12.922 4.264   1.00 16.15 ?  63  VAL   B H    1 
ATOM   5060 H  HA   . VAL   B 1 63  ? 57.248 -11.453 6.421   1.00 17.53 ?  63  VAL   B HA   1 
ATOM   5061 H  HB   . VAL   B 1 63  ? 58.323 -10.818 3.883   1.00 18.82 ?  63  VAL   B HB   1 
ATOM   5062 H  HG11 . VAL   B 1 63  ? 59.526 -9.113  5.133   1.00 19.49 ?  63  VAL   B HG11 1 
ATOM   5063 H  HG12 . VAL   B 1 63  ? 58.010 -8.782  4.798   1.00 19.49 ?  63  VAL   B HG12 1 
ATOM   5064 H  HG13 . VAL   B 1 63  ? 58.410 -9.296  6.248   1.00 19.49 ?  63  VAL   B HG13 1 
ATOM   5065 H  HG21 . VAL   B 1 63  ? 60.383 -11.293 4.877   1.00 19.66 ?  63  VAL   B HG21 1 
ATOM   5066 H  HG22 . VAL   B 1 63  ? 59.638 -11.669 6.229   1.00 19.66 ?  63  VAL   B HG22 1 
ATOM   5067 H  HG23 . VAL   B 1 63  ? 59.435 -12.567 4.934   1.00 19.66 ?  63  VAL   B HG23 1 
ATOM   5068 N  N    . GLU   B 1 64  ? 55.336 -10.419 4.085   1.00 13.32 ?  64  GLU   B N    1 
ATOM   5069 C  CA   . GLU   B 1 64  ? 54.175 -9.582  3.809   1.00 13.04 ?  64  GLU   B CA   1 
ATOM   5070 C  C    . GLU   B 1 64  ? 52.989 -9.982  4.679   1.00 12.63 ?  64  GLU   B C    1 
ATOM   5071 O  O    . GLU   B 1 64  ? 52.237 -9.124  5.173   1.00 12.83 ?  64  GLU   B O    1 
ATOM   5072 C  CB   . GLU   B 1 64  ? 53.819 -9.728  2.329   1.00 13.38 ?  64  GLU   B CB   1 
ATOM   5073 C  CG   . GLU   B 1 64  ? 52.555 -8.994  1.895   1.00 13.73 ?  64  GLU   B CG   1 
ATOM   5074 C  CD   . GLU   B 1 64  ? 52.025 -9.475  0.551   1.00 14.53 ?  64  GLU   B CD   1 
ATOM   5075 O  OE1  . GLU   B 1 64  ? 52.200 -10.681 0.234   1.00 15.45 ?  64  GLU   B OE1  1 
ATOM   5076 O  OE2  . GLU   B 1 64  ? 51.412 -8.650  -0.173  1.00 15.29 -1 64  GLU   B OE2  1 
ATOM   5077 H  H    . GLU   B 1 64  ? 55.601 -10.895 3.410   1.00 16.00 ?  64  GLU   B H    1 
ATOM   5078 H  HA   . GLU   B 1 64  ? 54.389 -8.658  3.982   1.00 15.67 ?  64  GLU   B HA   1 
ATOM   5079 H  HB2  . GLU   B 1 64  ? 54.549 -9.370  1.792   1.00 16.07 ?  64  GLU   B HB2  1 
ATOM   5080 H  HB3  . GLU   B 1 64  ? 53.695 -10.664 2.122   1.00 16.07 ?  64  GLU   B HB3  1 
ATOM   5081 H  HG2  . GLU   B 1 64  ? 51.853 -9.133  2.554   1.00 16.50 ?  64  GLU   B HG2  1 
ATOM   5082 H  HG3  . GLU   B 1 64  ? 52.748 -8.046  1.821   1.00 16.50 ?  64  GLU   B HG3  1 
ATOM   5083 N  N    . SER   B 1 65  ? 52.809 -11.289 4.872   1.00 12.33 ?  65  SER   B N    1 
ATOM   5084 C  CA   . SER   B 1 65  ? 51.696 -11.790 5.667   1.00 12.32 ?  65  SER   B CA   1 
ATOM   5085 C  C    . SER   B 1 65  ? 51.826 -11.385 7.127   1.00 12.41 ?  65  SER   B C    1 
ATOM   5086 O  O    . SER   B 1 65  ? 50.827 -11.015 7.761   1.00 13.11 ?  65  SER   B O    1 
ATOM   5087 C  CB   . SER   B 1 65  ? 51.610 -13.313 5.543   1.00 12.72 ?  65  SER   B CB   1 
ATOM   5088 O  OG   . SER   B 1 65  ? 51.257 -13.726 4.229   1.00 13.05 ?  65  SER   B OG   1 
ATOM   5089 H  H    . SER   B 1 65  ? 53.325 -11.914 4.564   1.00 14.82 ?  65  SER   B H    1 
ATOM   5090 H  HA   . SER   B 1 65  ? 50.869 -11.412 5.326   1.00 14.80 ?  65  SER   B HA   1 
ATOM   5091 H  HB2  . SER   B 1 65  ? 52.468 -13.692 5.769   1.00 15.28 ?  65  SER   B HB2  1 
ATOM   5092 H  HB3  . SER   B 1 65  ? 50.932 -13.633 6.164   1.00 15.28 ?  65  SER   B HB3  1 
ATOM   5093 H  HG   . SER   B 1 65  ? 51.827 -13.437 3.676   1.00 15.68 ?  65  SER   B HG   1 
ATOM   5094 N  N    . ASP   B 1 66  ? 53.033 -11.482 7.696   1.00 12.75 ?  66  ASP   B N    1 
ATOM   5095 C  CA   . ASP   B 1 66  ? 53.207 -11.087 9.090   1.00 13.45 ?  66  ASP   B CA   1 
ATOM   5096 C  C    . ASP   B 1 66  ? 52.895 -9.607  9.283   1.00 13.52 ?  66  ASP   B C    1 
ATOM   5097 O  O    . ASP   B 1 66  ? 52.322 -9.208  10.304  1.00 14.07 ?  66  ASP   B O    1 
ATOM   5098 C  CB   . ASP   B 1 66  ? 54.632 -11.389 9.558   1.00 14.56 ?  66  ASP   B CB   1 
ATOM   5099 C  CG   . ASP   B 1 66  ? 54.908 -12.883 9.710   1.00 16.39 ?  66  ASP   B CG   1 
ATOM   5100 O  OD1  . ASP   B 1 66  ? 53.959 -13.699 9.652   1.00 17.25 ?  66  ASP   B OD1  1 
ATOM   5101 O  OD2  . ASP   B 1 66  ? 56.092 -13.246 9.905   1.00 19.61 -1 66  ASP   B OD2  1 
ATOM   5102 H  H    . ASP   B 1 66  ? 53.738 -11.784 7.316   1.00 15.31 ?  66  ASP   B H    1 
ATOM   5103 H  HA   . ASP   B 1 66  ? 52.598 -11.591 9.654   1.00 16.16 ?  66  ASP   B HA   1 
ATOM   5104 H  HB2  . ASP   B 1 66  ? 55.260 -11.029 8.914   1.00 17.49 ?  66  ASP   B HB2  1 
ATOM   5105 H  HB3  . ASP   B 1 66  ? 54.777 -10.969 10.427  1.00 17.49 ?  66  ASP   B HB3  1 
ATOM   5106 N  N    . ASP   B 1 67  ? 53.270 -8.770  8.314   1.00 13.13 ?  67  ASP   B N    1 
ATOM   5107 C  CA   . ASP   B 1 67  ? 52.922 -7.359  8.393   1.00 13.86 ?  67  ASP   B CA   1 
ATOM   5108 C  C    . ASP   B 1 67  ? 51.413 -7.153  8.315   1.00 13.88 ?  67  ASP   B C    1 
ATOM   5109 O  O    . ASP   B 1 67  ? 50.855 -6.337  9.061   1.00 14.35 ?  67  ASP   B O    1 
ATOM   5110 C  CB   . ASP   B 1 67  ? 53.635 -6.599  7.283   1.00 15.16 ?  67  ASP   B CB   1 
ATOM   5111 C  CG   . ASP   B 1 67  ? 53.208 -5.156  7.226   1.00 16.77 ?  67  ASP   B CG   1 
ATOM   5112 O  OD1  . ASP   B 1 67  ? 53.699 -4.327  8.031   1.00 17.94 ?  67  ASP   B OD1  1 
ATOM   5113 O  OD2  . ASP   B 1 67  ? 52.337 -4.867  6.394   1.00 18.15 -1 67  ASP   B OD2  1 
ATOM   5114 H  H    . ASP   B 1 67  ? 53.718 -8.995  7.613   1.00 15.77 ?  67  ASP   B H    1 
ATOM   5115 H  HA   . ASP   B 1 67  ? 53.229 -7.002  9.238   1.00 16.65 ?  67  ASP   B HA   1 
ATOM   5116 H  HB2  . ASP   B 1 67  ? 54.594 -6.629  7.436   1.00 18.21 ?  67  ASP   B HB2  1 
ATOM   5117 H  HB3  . ASP   B 1 67  ? 53.430 -7.017  6.425   1.00 18.21 ?  67  ASP   B HB3  1 
ATOM   5118 N  N    . TYR   B 1 68  ? 50.734 -7.888  7.422   1.00 13.56 ?  68  TYR   B N    1 
ATOM   5119 C  CA   . TYR   B 1 68  ? 49.276 -7.815  7.347   1.00 14.35 ?  68  TYR   B CA   1 
ATOM   5120 C  C    . TYR   B 1 68  ? 48.643 -8.160  8.692   1.00 13.95 ?  68  TYR   B C    1 
ATOM   5121 O  O    . TYR   B 1 68  ? 47.706 -7.483  9.138   1.00 14.63 ?  68  TYR   B O    1 
ATOM   5122 C  CB   . TYR   B 1 68  ? 48.742 -8.744  6.246   1.00 15.20 ?  68  TYR   B CB   1 
ATOM   5123 C  CG   . TYR   B 1 68  ? 47.238 -8.892  6.302   1.00 16.26 ?  68  TYR   B CG   1 
ATOM   5124 C  CD1  . TYR   B 1 68  ? 46.653 -9.843  7.129   1.00 17.11 ?  68  TYR   B CD1  1 
ATOM   5125 C  CD2  . TYR   B 1 68  ? 46.406 -8.051  5.579   1.00 17.52 ?  68  TYR   B CD2  1 
ATOM   5126 C  CE1  . TYR   B 1 68  ? 45.292 -9.963  7.227   1.00 18.15 ?  68  TYR   B CE1  1 
ATOM   5127 C  CE2  . TYR   B 1 68  ? 45.025 -8.176  5.662   1.00 18.00 ?  68  TYR   B CE2  1 
ATOM   5128 C  CZ   . TYR   B 1 68  ? 44.490 -9.135  6.490   1.00 18.22 ?  68  TYR   B CZ   1 
ATOM   5129 O  OH   . TYR   B 1 68  ? 43.123 -9.249  6.597   1.00 19.41 ?  68  TYR   B OH   1 
ATOM   5130 H  H    . TYR   B 1 68  ? 51.093 -8.443  6.859   1.00 16.29 ?  68  TYR   B H    1 
ATOM   5131 H  HA   . TYR   B 1 68  ? 49.026 -6.909  7.125   1.00 17.24 ?  68  TYR   B HA   1 
ATOM   5132 H  HB2  . TYR   B 1 68  ? 48.969 -8.373  5.380   1.00 18.26 ?  68  TYR   B HB2  1 
ATOM   5133 H  HB3  . TYR   B 1 68  ? 49.131 -9.623  6.350   1.00 18.26 ?  68  TYR   B HB3  1 
ATOM   5134 H  HD1  . TYR   B 1 68  ? 47.196 -10.413 7.628   1.00 20.55 ?  68  TYR   B HD1  1 
ATOM   5135 H  HD2  . TYR   B 1 68  ? 46.774 -7.394  5.038   1.00 21.04 ?  68  TYR   B HD2  1 
ATOM   5136 H  HE1  . TYR   B 1 68  ? 44.915 -10.622 7.770   1.00 21.80 ?  68  TYR   B HE1  1 
ATOM   5137 H  HE2  . TYR   B 1 68  ? 44.464 -7.608  5.183   1.00 21.62 ?  68  TYR   B HE2  1 
ATOM   5138 H  HH   . TYR   B 1 68  ? 42.733 -8.699  6.090   1.00 23.32 ?  68  TYR   B HH   1 
ATOM   5139 N  N    . ILE   B 1 69  ? 49.130 -9.225  9.340   1.00 13.60 ?  69  ILE   B N    1 
ATOM   5140 C  CA   . ILE   B 1 69  ? 48.577 -9.647  10.627  1.00 14.13 ?  69  ILE   B CA   1 
ATOM   5141 C  C    . ILE   B 1 69  ? 48.825 -8.591  11.696  1.00 14.04 ?  69  ILE   B C    1 
ATOM   5142 O  O    . ILE   B 1 69  ? 47.959 -8.319  12.534  1.00 14.18 ?  69  ILE   B O    1 
ATOM   5143 C  CB   . ILE   B 1 69  ? 49.156 -11.016 11.036  1.00 14.80 ?  69  ILE   B CB   1 
ATOM   5144 C  CG1  . ILE   B 1 69  ? 48.632 -12.135 10.126  1.00 15.27 ?  69  ILE   B CG1  1 
ATOM   5145 C  CG2  . ILE   B 1 69  ? 48.872 -11.318 12.507  1.00 15.96 ?  69  ILE   B CG2  1 
ATOM   5146 C  CD1  . ILE   B 1 69  ? 47.148 -12.443 10.269  1.00 16.02 ?  69  ILE   B CD1  1 
ATOM   5147 H  H    . ILE   B 1 69  ? 49.778 -9.719  9.056   1.00 16.34 ?  69  ILE   B H    1 
ATOM   5148 H  HA   . ILE   B 1 69  ? 47.622 -9.747  10.534  1.00 16.98 ?  69  ILE   B HA   1 
ATOM   5149 H  HB   . ILE   B 1 69  ? 50.118 -10.980 10.928  1.00 17.78 ?  69  ILE   B HB   1 
ATOM   5150 H  HG12 . ILE   B 1 69  ? 48.790 -11.881 9.204   1.00 18.34 ?  69  ILE   B HG12 1 
ATOM   5151 H  HG13 . ILE   B 1 69  ? 49.121 -12.951 10.325  1.00 18.34 ?  69  ILE   B HG13 1 
ATOM   5152 H  HG21 . ILE   B 1 69  ? 49.019 -12.265 12.669  1.00 19.17 ?  69  ILE   B HG21 1 
ATOM   5153 H  HG22 . ILE   B 1 69  ? 49.472 -10.797 13.063  1.00 19.17 ?  69  ILE   B HG22 1 
ATOM   5154 H  HG23 . ILE   B 1 69  ? 47.950 -11.091 12.707  1.00 19.17 ?  69  ILE   B HG23 1 
ATOM   5155 H  HD11 . ILE   B 1 69  ? 46.924 -13.178 9.677   1.00 19.25 ?  69  ILE   B HD11 1 
ATOM   5156 H  HD12 . ILE   B 1 69  ? 46.964 -12.696 11.188  1.00 19.25 ?  69  ILE   B HD12 1 
ATOM   5157 H  HD13 . ILE   B 1 69  ? 46.636 -11.658 10.031  1.00 19.25 ?  69  ILE   B HD13 1 
ATOM   5158 N  N    . ALA   B 1 70  ? 50.021 -8.000  11.716  1.00 14.06 ?  70  ALA   B N    1 
ATOM   5159 C  CA   . ALA   B 1 70  ? 50.297 -6.959  12.701  1.00 13.85 ?  70  ALA   B CA   1 
ATOM   5160 C  C    . ALA   B 1 70  ? 49.288 -5.825  12.591  1.00 14.37 ?  70  ALA   B C    1 
ATOM   5161 O  O    . ALA   B 1 70  ? 48.834 -5.287  13.605  1.00 15.01 ?  70  ALA   B O    1 
ATOM   5162 C  CB   . ALA   B 1 70  ? 51.719 -6.429  12.521  1.00 14.69 ?  70  ALA   B CB   1 
ATOM   5163 H  H    . ALA   B 1 70  ? 50.669 -8.176  11.184  1.00 16.89 ?  70  ALA   B H    1 
ATOM   5164 H  HA   . ALA   B 1 70  ? 50.233 -7.336  13.592  1.00 16.64 ?  70  ALA   B HA   1 
ATOM   5165 H  HB1  . ALA   B 1 70  ? 51.911 -5.784  13.223  1.00 17.64 ?  70  ALA   B HB1  1 
ATOM   5166 H  HB2  . ALA   B 1 70  ? 52.346 -7.168  12.577  1.00 17.64 ?  70  ALA   B HB2  1 
ATOM   5167 H  HB3  . ALA   B 1 70  ? 51.793 -6.001  11.652  1.00 17.64 ?  70  ALA   B HB3  1 
ATOM   5168 N  N    . THR   B 1 71  ? 48.919 -5.461  11.368  1.00 14.89 ?  71  THR   B N    1 
ATOM   5169 C  CA   . THR   B 1 71  ? 48.020 -4.331  11.155  1.00 16.03 ?  71  THR   B CA   1 
ATOM   5170 C  C    . THR   B 1 71  ? 46.553 -4.702  11.361  1.00 16.37 ?  71  THR   B C    1 
ATOM   5171 O  O    . THR   B 1 71  ? 45.769 -3.889  11.874  1.00 18.06 ?  71  THR   B O    1 
ATOM   5172 C  CB   . THR   B 1 71  ? 48.233 -3.775  9.745   1.00 18.19 ?  71  THR   B CB   1 
ATOM   5173 O  OG1  . THR   B 1 71  ? 49.558 -3.240  9.638   1.00 20.20 ?  71  THR   B OG1  1 
ATOM   5174 C  CG2  . THR   B 1 71  ? 47.212 -2.697  9.418   1.00 19.30 ?  71  THR   B CG2  1 
ATOM   5175 H  H    . THR   B 1 71  ? 49.170 -5.859  10.648  1.00 17.89 ?  71  THR   B H    1 
ATOM   5176 H  HA   . THR   B 1 71  ? 48.243 -3.633  11.788  1.00 19.25 ?  71  THR   B HA   1 
ATOM   5177 H  HB   . THR   B 1 71  ? 48.144 -4.490  9.098   1.00 21.84 ?  71  THR   B HB   1 
ATOM   5178 H  HG1  . THR   B 1 71  ? 49.685 -2.912  8.869   1.00 24.26 ?  71  THR   B HG1  1 
ATOM   5179 H  HG21 . THR   B 1 71  ? 47.517 -2.171  8.661   1.00 23.18 ?  71  THR   B HG21 1 
ATOM   5180 H  HG22 . THR   B 1 71  ? 46.362 -3.102  9.196   1.00 23.18 ?  71  THR   B HG22 1 
ATOM   5181 H  HG23 . THR   B 1 71  ? 47.097 -2.108  10.181  1.00 23.18 ?  71  THR   B HG23 1 
ATOM   5182 N  N    . ASN   B 1 72  ? 46.160 -5.916  10.971  1.00 15.71 ?  72  ASN   B N    1 
ATOM   5183 C  CA   . ASN   B 1 72  ? 44.755 -6.272  10.857  1.00 16.43 ?  72  ASN   B CA   1 
ATOM   5184 C  C    . ASN   B 1 72  ? 44.292 -7.361  11.812  1.00 16.95 ?  72  ASN   B C    1 
ATOM   5185 O  O    . ASN   B 1 72  ? 43.078 -7.520  11.990  1.00 17.94 ?  72  ASN   B O    1 
ATOM   5186 C  CB   . ASN   B 1 72  ? 44.443 -6.712  9.420   1.00 17.31 ?  72  ASN   B CB   1 
ATOM   5187 C  CG   . ASN   B 1 72  ? 44.715 -5.620  8.416   1.00 18.28 ?  72  ASN   B CG   1 
ATOM   5188 O  OD1  . ASN   B 1 72  ? 45.739 -5.627  7.726   1.00 19.20 ?  72  ASN   B OD1  1 
ATOM   5189 N  ND2  . ASN   B 1 72  ? 43.827 -4.649  8.358   1.00 20.12 ?  72  ASN   B ND2  1 
ATOM   5190 H  H    . ASN   B 1 72  ? 46.702 -6.564  10.776  1.00 18.87 ?  72  ASN   B H    1 
ATOM   5191 H  HA   . ASN   B 1 72  ? 44.227 -5.482  11.039  1.00 19.74 ?  72  ASN   B HA   1 
ATOM   5192 H  HB2  . ASN   B 1 72  ? 45.003 -7.474  9.192   1.00 20.79 ?  72  ASN   B HB2  1 
ATOM   5193 H  HB3  . ASN   B 1 72  ? 43.509 -6.953  9.357   1.00 20.79 ?  72  ASN   B HB3  1 
ATOM   5194 H  HD21 . ASN   B 1 72  ? 43.930 -4.001  7.801   1.00 24.17 ?  72  ASN   B HD21 1 
ATOM   5195 H  HD22 . ASN   B 1 72  ? 43.123 -4.677  8.855   1.00 24.17 ?  72  ASN   B HD22 1 
ATOM   5196 N  N    . GLY   B 1 73  ? 45.201 -8.107  12.433  1.00 16.30 ?  73  GLY   B N    1 
ATOM   5197 C  CA   . GLY   B 1 73  ? 44.811 -9.246  13.226  1.00 16.12 ?  73  GLY   B CA   1 
ATOM   5198 C  C    . GLY   B 1 73  ? 44.462 -10.439 12.361  1.00 14.75 ?  73  GLY   B C    1 
ATOM   5199 O  O    . GLY   B 1 73  ? 44.451 -10.366 11.132  1.00 14.42 ?  73  GLY   B O    1 
ATOM   5200 H  H    . GLY   B 1 73  ? 46.052 -7.969  12.409  1.00 19.58 ?  73  GLY   B H    1 
ATOM   5201 H  HA2  . GLY   B 1 73  ? 45.537 -9.492  13.824  1.00 19.37 ?  73  GLY   B HA2  1 
ATOM   5202 H  HA3  . GLY   B 1 73  ? 44.036 -9.017  13.768  1.00 19.37 ?  73  GLY   B HA3  1 
ATOM   5203 N  N    . PRO   B 1 74  ? 44.159 -11.559 13.009  1.00 14.49 ?  74  PRO   B N    1 
ATOM   5204 C  CA   . PRO   B 1 74  ? 43.902 -12.800 12.276  1.00 13.96 ?  74  PRO   B CA   1 
ATOM   5205 C  C    . PRO   B 1 74  ? 42.610 -12.745 11.477  1.00 13.14 ?  74  PRO   B C    1 
ATOM   5206 O  O    . PRO   B 1 74  ? 41.673 -12.005 11.796  1.00 15.06 ?  74  PRO   B O    1 
ATOM   5207 C  CB   . PRO   B 1 74  ? 43.811 -13.846 13.394  1.00 15.34 ?  74  PRO   B CB   1 
ATOM   5208 C  CG   . PRO   B 1 74  ? 43.377 -13.062 14.596  1.00 16.93 ?  74  PRO   B CG   1 
ATOM   5209 C  CD   . PRO   B 1 74  ? 44.066 -11.742 14.465  1.00 16.21 ?  74  PRO   B CD   1 
ATOM   5210 H  HA   . PRO   B 1 74  ? 44.648 -13.008 11.689  1.00 16.78 ?  74  PRO   B HA   1 
ATOM   5211 H  HB2  . PRO   B 1 74  ? 43.149 -14.515 13.158  1.00 18.42 ?  74  PRO   B HB2  1 
ATOM   5212 H  HB3  . PRO   B 1 74  ? 44.679 -14.249 13.538  1.00 18.42 ?  74  PRO   B HB3  1 
ATOM   5213 H  HG2  . PRO   B 1 74  ? 42.411 -12.944 14.583  1.00 20.34 ?  74  PRO   B HG2  1 
ATOM   5214 H  HG3  . PRO   B 1 74  ? 43.654 -13.516 15.405  1.00 20.34 ?  74  PRO   B HG3  1 
ATOM   5215 H  HD2  . PRO   B 1 74  ? 43.528 -11.037 14.870  1.00 19.47 ?  74  PRO   B HD2  1 
ATOM   5216 H  HD3  . PRO   B 1 74  ? 44.951 -11.780 14.863  1.00 19.47 ?  74  PRO   B HD3  1 
ATOM   5217 N  N    . LEU   B 1 75  ? 42.576 -13.549 10.422  1.00 12.88 ?  75  LEU   B N    1 
ATOM   5218 C  CA   . LEU   B 1 75  ? 41.364 -13.756 9.654   1.00 12.98 ?  75  LEU   B CA   1 
ATOM   5219 C  C    . LEU   B 1 75  ? 40.380 -14.598 10.457  1.00 13.49 ?  75  LEU   B C    1 
ATOM   5220 O  O    . LEU   B 1 75  ? 40.726 -15.203 11.474  1.00 14.80 ?  75  LEU   B O    1 
ATOM   5221 C  CB   . LEU   B 1 75  ? 41.687 -14.483 8.351   1.00 12.82 ?  75  LEU   B CB   1 
ATOM   5222 C  CG   . LEU   B 1 75  ? 42.510 -13.719 7.310   1.00 15.02 ?  75  LEU   B CG   1 
ATOM   5223 C  CD1  . LEU   B 1 75  ? 42.721 -14.557 6.049   1.00 16.52 ?  75  LEU   B CD1  1 
ATOM   5224 C  CD2  . LEU   B 1 75  ? 41.890 -12.394 6.971   1.00 19.01 ?  75  LEU   B CD2  1 
ATOM   5225 H  H    . LEU   B 1 75  ? 43.251 -14.001 10.133  1.00 15.47 ?  75  LEU   B H    1 
ATOM   5226 H  HA   . LEU   B 1 75  ? 40.953 -12.904 9.445   1.00 15.60 ?  75  LEU   B HA   1 
ATOM   5227 H  HB2  . LEU   B 1 75  ? 42.183 -15.294 8.567   1.00 15.41 ?  75  LEU   B HB2  1 
ATOM   5228 H  HB3  . LEU   B 1 75  ? 40.850 -14.736 7.923   1.00 15.41 ?  75  LEU   B HB3  1 
ATOM   5229 H  HG   . LEU   B 1 75  ? 43.385 -13.543 7.687   1.00 18.04 ?  75  LEU   B HG   1 
ATOM   5230 H  HD11 . LEU   B 1 75  ? 43.253 -14.044 5.416   1.00 19.84 ?  75  LEU   B HD11 1 
ATOM   5231 H  HD12 . LEU   B 1 75  ? 43.191 -15.373 6.285   1.00 19.84 ?  75  LEU   B HD12 1 
ATOM   5232 H  HD13 . LEU   B 1 75  ? 41.861 -14.769 5.659   1.00 19.84 ?  75  LEU   B HD13 1 
ATOM   5233 H  HD21 . LEU   B 1 75  ? 42.362 -12.009 6.219   1.00 22.83 ?  75  LEU   B HD21 1 
ATOM   5234 H  HD22 . LEU   B 1 75  ? 40.958 -12.531 6.748   1.00 22.83 ?  75  LEU   B HD22 1 
ATOM   5235 H  HD23 . LEU   B 1 75  ? 41.963 -11.807 7.743   1.00 22.83 ?  75  LEU   B HD23 1 
ATOM   5236 N  N    . LYS   B 1 76  ? 39.138 -14.641 9.974   1.00 14.55 ?  76  LYS   B N    1 
ATOM   5237 C  CA   . LYS   B 1 76  ? 38.144 -15.600 10.439  1.00 15.56 ?  76  LYS   B CA   1 
ATOM   5238 C  C    . LYS   B 1 76  ? 38.266 -16.893 9.637   1.00 14.48 ?  76  LYS   B C    1 
ATOM   5239 O  O    . LYS   B 1 76  ? 38.566 -16.867 8.446   1.00 14.41 ?  76  LYS   B O    1 
ATOM   5240 C  CB   . LYS   B 1 76  ? 36.731 -15.049 10.207  1.00 17.51 ?  76  LYS   B CB   1 
ATOM   5241 C  CG   . LYS   B 1 76  ? 36.425 -13.687 10.842  1.00 18.72 ?  76  LYS   B CG   1 
ATOM   5242 C  CD   . LYS   B 1 76  ? 35.031 -13.163 10.455  1.00 19.72 ?  76  LYS   B CD   1 
ATOM   5243 C  CE   . LYS   B 1 76  ? 34.767 -11.790 11.055  1.00 21.56 ?  76  LYS   B CE   1 
ATOM   5244 N  NZ   . LYS   B 1 76  ? 33.495 -11.194 10.584  1.00 22.48 ?  76  LYS   B NZ   1 
ATOM   5245 H  H    . LYS   B 1 76  ? 38.847 -14.120 9.352   1.00 17.48 ?  76  LYS   B H    1 
ATOM   5246 H  HA   . LYS   B 1 76  ? 38.271 -15.792 11.382  1.00 18.69 ?  76  LYS   B HA   1 
ATOM   5247 H  HB2  . LYS   B 1 76  ? 36.593 -14.959 9.251   1.00 21.03 ?  76  LYS   B HB2  1 
ATOM   5248 H  HB3  . LYS   B 1 76  ? 36.093 -15.683 10.567  1.00 21.03 ?  76  LYS   B HB3  1 
ATOM   5249 H  HG2  . LYS   B 1 76  ? 36.460 -13.770 11.808  1.00 22.48 ?  76  LYS   B HG2  1 
ATOM   5250 H  HG3  . LYS   B 1 76  ? 37.085 -13.039 10.541  1.00 22.48 ?  76  LYS   B HG3  1 
ATOM   5251 H  HD2  . LYS   B 1 76  ? 34.973 -13.090 9.488   1.00 23.69 ?  76  LYS   B HD2  1 
ATOM   5252 H  HD3  . LYS   B 1 76  ? 34.356 -13.775 10.787  1.00 23.69 ?  76  LYS   B HD3  1 
ATOM   5253 H  HE2  . LYS   B 1 76  ? 34.723 -11.870 12.019  1.00 25.89 ?  76  LYS   B HE2  1 
ATOM   5254 H  HE3  . LYS   B 1 76  ? 35.490 -11.192 10.802  1.00 25.89 ?  76  LYS   B HE3  1 
ATOM   5255 H  HZ1  . LYS   B 1 76  ? 33.376 -10.392 10.954  1.00 27.00 ?  76  LYS   B HZ1  1 
ATOM   5256 H  HZ2  . LYS   B 1 76  ? 33.508 -11.100 9.697   1.00 27.00 ?  76  LYS   B HZ2  1 
ATOM   5257 H  HZ3  . LYS   B 1 76  ? 32.809 -11.717 10.806  1.00 27.00 ?  76  LYS   B HZ3  1 
ATOM   5258 N  N    . VAL   B 1 77  ? 38.020 -18.033 10.291  1.00 15.06 ?  77  VAL   B N    1 
ATOM   5259 C  CA   . VAL   B 1 77  ? 37.819 -19.262 9.528   1.00 15.34 ?  77  VAL   B CA   1 
ATOM   5260 C  C    . VAL   B 1 77  ? 36.634 -19.048 8.596   1.00 13.98 ?  77  VAL   B C    1 
ATOM   5261 O  O    . VAL   B 1 77  ? 35.564 -18.610 9.032   1.00 14.35 ?  77  VAL   B O    1 
ATOM   5262 C  CB   . VAL   B 1 77  ? 37.608 -20.466 10.458  1.00 16.78 ?  77  VAL   B CB   1 
ATOM   5263 C  CG1  . VAL   B 1 77  ? 37.352 -21.718 9.624   1.00 17.34 ?  77  VAL   B CG1  1 
ATOM   5264 C  CG2  . VAL   B 1 77  ? 38.814 -20.660 11.382  1.00 17.75 ?  77  VAL   B CG2  1 
ATOM   5265 H  H    . VAL   B 1 77  ? 37.974 -18.116 11.141  1.00 18.09 ?  77  VAL   B H    1 
ATOM   5266 H  HA   . VAL   B 1 77  ? 38.601 -19.431 8.982   1.00 18.43 ?  77  VAL   B HA   1 
ATOM   5267 H  HB   . VAL   B 1 77  ? 36.823 -20.306 11.009  1.00 20.16 ?  77  VAL   B HB   1 
ATOM   5268 H  HG11 . VAL   B 1 77  ? 37.390 -22.492 10.203  1.00 20.83 ?  77  VAL   B HG11 1 
ATOM   5269 H  HG12 . VAL   B 1 77  ? 36.476 -21.654 9.212   1.00 20.83 ?  77  VAL   B HG12 1 
ATOM   5270 H  HG13 . VAL   B 1 77  ? 38.036 -21.781 8.939   1.00 20.83 ?  77  VAL   B HG13 1 
ATOM   5271 H  HG21 . VAL   B 1 77  ? 38.670 -21.454 11.918  1.00 21.32 ?  77  VAL   B HG21 1 
ATOM   5272 H  HG22 . VAL   B 1 77  ? 39.609 -20.762 10.840  1.00 21.32 ?  77  VAL   B HG22 1 
ATOM   5273 H  HG23 . VAL   B 1 77  ? 38.897 -19.882 11.956  1.00 21.32 ?  77  VAL   B HG23 1 
ATOM   5274 N  N    . GLY   B 1 78  ? 36.825 -19.327 7.309   1.00 13.48 ?  78  GLY   B N    1 
ATOM   5275 C  CA   . GLY   B 1 78  ? 35.855 -19.013 6.285   1.00 13.31 ?  78  GLY   B CA   1 
ATOM   5276 C  C    . GLY   B 1 78  ? 36.100 -17.702 5.571   1.00 13.00 ?  78  GLY   B C    1 
ATOM   5277 O  O    . GLY   B 1 78  ? 35.406 -17.420 4.587   1.00 13.44 ?  78  GLY   B O    1 
ATOM   5278 H  H    . GLY   B 1 78  ? 37.532 -19.714 7.003   1.00 16.20 ?  78  GLY   B H    1 
ATOM   5279 H  HA2  . GLY   B 1 78  ? 35.854 -19.711 5.625   1.00 15.99 ?  78  GLY   B HA2  1 
ATOM   5280 H  HA3  . GLY   B 1 78  ? 34.975 -18.970 6.693   1.00 15.99 ?  78  GLY   B HA3  1 
ATOM   5281 N  N    . GLY   B 1 79  ? 37.034 -16.881 6.062   1.00 12.82 ?  79  GLY   B N    1 
ATOM   5282 C  CA   . GLY   B 1 79  ? 37.332 -15.593 5.470   1.00 12.47 ?  79  GLY   B CA   1 
ATOM   5283 C  C    . GLY   B 1 79  ? 38.565 -15.627 4.577   1.00 12.15 ?  79  GLY   B C    1 
ATOM   5284 O  O    . GLY   B 1 79  ? 39.175 -16.667 4.335   1.00 12.71 ?  79  GLY   B O    1 
ATOM   5285 H  H    . GLY   B 1 79  ? 37.517 -17.053 6.754   1.00 15.40 ?  79  GLY   B H    1 
ATOM   5286 H  HA2  . GLY   B 1 79  ? 36.579 -15.298 4.933   1.00 14.99 ?  79  GLY   B HA2  1 
ATOM   5287 H  HA3  . GLY   B 1 79  ? 37.482 -14.937 6.171   1.00 14.99 ?  79  GLY   B HA3  1 
ATOM   5288 N  N    . SER   B 1 80  ? 38.940 -14.441 4.096   1.00 11.97 ?  80  SER   B N    1 
ATOM   5289 C  CA   . SER   B 1 80  ? 40.048 -14.317 3.159   1.00 11.67 ?  80  SER   B CA   1 
ATOM   5290 C  C    . SER   B 1 80  ? 40.629 -12.911 3.205   1.00 11.56 ?  80  SER   B C    1 
ATOM   5291 O  O    . SER   B 1 80  ? 40.012 -11.973 3.717   1.00 12.79 ?  80  SER   B O    1 
ATOM   5292 C  CB   . SER   B 1 80  ? 39.611 -14.620 1.725   1.00 12.15 ?  80  SER   B CB   1 
ATOM   5293 O  OG   . SER   B 1 80  ? 38.769 -13.602 1.210   1.00 13.43 ?  80  SER   B OG   1 
ATOM   5294 H  H    . SER   B 1 80  ? 38.576 -13.694 4.305   1.00 14.39 ?  80  SER   B H    1 
ATOM   5295 H  HA   . SER   B 1 80  ? 40.742 -14.947 3.408   1.00 14.02 ?  80  SER   B HA   1 
ATOM   5296 H  HB2  . SER   B 1 80  ? 40.394 -14.686 1.157   1.00 14.60 ?  80  SER   B HB2  1 
ATOM   5297 H  HB3  . SER   B 1 80  ? 39.125 -15.462 1.712   1.00 14.60 ?  80  SER   B HB3  1 
ATOM   5298 H  HG   . SER   B 1 80  ? 38.073 -13.531 1.691   1.00 16.14 ?  80  SER   B HG   1 
ATOM   5299 N  N    . CYS   B 1 81  ? 41.815 -12.772 2.612   1.00 11.71 ?  81  CYS   B N    1 
ATOM   5300 C  CA   . CYS   B 1 81  ? 42.372 -11.463 2.303   1.00 11.81 ?  81  CYS   B CA   1 
ATOM   5301 C  C    . CYS   B 1 81  ? 43.133 -11.549 0.988   1.00 11.15 ?  81  CYS   B C    1 
ATOM   5302 O  O    . CYS   B 1 81  ? 43.626 -12.616 0.604   1.00 12.13 ?  81  CYS   B O    1 
ATOM   5303 C  CB   . CYS   B 1 81  ? 43.270 -10.917 3.425   1.00 12.32 ?  81  CYS   B CB   1 
ATOM   5304 S  SG   . CYS   B 1 81  ? 44.780 -11.865 3.660   1.00 12.90 ?  81  CYS   B SG   1 
ATOM   5305 H  H    . CYS   B 1 81  ? 42.324 -13.429 2.377   1.00 14.07 ?  81  CYS   B H    1 
ATOM   5306 H  HA   . CYS   B 1 81  ? 41.643 -10.836 2.179   1.00 14.19 ?  81  CYS   B HA   1 
ATOM   5307 H  HB2  . CYS   B 1 81  ? 43.519 -10.003 3.214   1.00 14.81 ?  81  CYS   B HB2  1 
ATOM   5308 H  HB3  . CYS   B 1 81  ? 42.769 -10.932 4.260   1.00 14.81 ?  81  CYS   B HB3  1 
ATOM   5309 H  HG   . CYS   B 1 81  ? 45.412 -11.371 4.556   1.00 15.49 ?  81  CYS   B HG   1 
ATOM   5310 N  N    . VAL   B 1 82  ? 43.248 -10.407 0.316   1.00 11.51 ?  82  VAL   B N    1 
ATOM   5311 C  CA   . VAL   B 1 82  ? 44.006 -10.285 -0.925  1.00 11.72 ?  82  VAL   B CA   1 
ATOM   5312 C  C    . VAL   B 1 82  ? 45.351 -9.642  -0.616  1.00 12.02 ?  82  VAL   B C    1 
ATOM   5313 O  O    . VAL   B 1 82  ? 45.408 -8.521  -0.089  1.00 13.23 ?  82  VAL   B O    1 
ATOM   5314 C  CB   . VAL   B 1 82  ? 43.254 -9.452  -1.974  1.00 13.09 ?  82  VAL   B CB   1 
ATOM   5315 C  CG1  . VAL   B 1 82  ? 44.091 -9.330  -3.247  1.00 14.48 ?  82  VAL   B CG1  1 
ATOM   5316 C  CG2  . VAL   B 1 82  ? 41.884 -10.045 -2.271  1.00 14.34 ?  82  VAL   B CG2  1 
ATOM   5317 H  H    . VAL   B 1 82  ? 42.879 -9.661  0.562   1.00 13.84 ?  82  VAL   B H    1 
ATOM   5318 H  HA   . VAL   B 1 82  ? 44.164 -11.165 -1.293  1.00 14.08 ?  82  VAL   B HA   1 
ATOM   5319 H  HB   . VAL   B 1 82  ? 43.120 -8.557  -1.630  1.00 15.73 ?  82  VAL   B HB   1 
ATOM   5320 H  HG11 . VAL   B 1 82  ? 43.530 -9.006  -3.970  1.00 17.39 ?  82  VAL   B HG11 1 
ATOM   5321 H  HG12 . VAL   B 1 82  ? 44.820 -8.704  -3.096  1.00 17.39 ?  82  VAL   B HG12 1 
ATOM   5322 H  HG13 . VAL   B 1 82  ? 44.451 -10.202 -3.479  1.00 17.39 ?  82  VAL   B HG13 1 
ATOM   5323 H  HG21 . VAL   B 1 82  ? 41.453 -9.521  -2.968  1.00 17.23 ?  82  VAL   B HG21 1 
ATOM   5324 H  HG22 . VAL   B 1 82  ? 41.992 -10.962 -2.573  1.00 17.23 ?  82  VAL   B HG22 1 
ATOM   5325 H  HG23 . VAL   B 1 82  ? 41.348 -10.024 -1.464  1.00 17.23 ?  82  VAL   B HG23 1 
ATOM   5326 N  N    . LEU   B 1 83  ? 46.426 -10.333 -0.982  1.00 11.62 ?  83  LEU   B N    1 
ATOM   5327 C  CA   . LEU   B 1 83  ? 47.785 -9.821  -0.865  1.00 11.67 ?  83  LEU   B CA   1 
ATOM   5328 C  C    . LEU   B 1 83  ? 48.480 -9.969  -2.218  1.00 11.62 ?  83  LEU   B C    1 
ATOM   5329 O  O    . LEU   B 1 83  ? 47.875 -10.400 -3.200  1.00 11.56 ?  83  LEU   B O    1 
ATOM   5330 C  CB   . LEU   B 1 83  ? 48.533 -10.502 0.288   1.00 12.09 ?  83  LEU   B CB   1 
ATOM   5331 C  CG   . LEU   B 1 83  ? 48.040 -10.149 1.697   1.00 13.23 ?  83  LEU   B CG   1 
ATOM   5332 C  CD1  . LEU   B 1 83  ? 48.678 -11.023 2.752   1.00 13.71 ?  83  LEU   B CD1  1 
ATOM   5333 C  CD2  . LEU   B 1 83  ? 48.275 -8.676  2.014   1.00 14.48 ?  83  LEU   B CD2  1 
ATOM   5334 H  H    . LEU   B 1 83  ? 46.388 -11.130 -1.311  1.00 13.97 ?  83  LEU   B H    1 
ATOM   5335 H  HA   . LEU   B 1 83  ? 47.737 -8.875  -0.673  1.00 14.02 ?  83  LEU   B HA   1 
ATOM   5336 H  HB2  . LEU   B 1 83  ? 48.455 -11.458 0.184   1.00 14.53 ?  83  LEU   B HB2  1 
ATOM   5337 H  HB3  . LEU   B 1 83  ? 49.467 -10.243 0.236   1.00 14.53 ?  83  LEU   B HB3  1 
ATOM   5338 H  HG   . LEU   B 1 83  ? 47.086 -10.302 1.734   1.00 15.90 ?  83  LEU   B HG   1 
ATOM   5339 H  HD11 . LEU   B 1 83  ? 48.330 -10.774 3.627   1.00 16.47 ?  83  LEU   B HD11 1 
ATOM   5340 H  HD12 . LEU   B 1 83  ? 48.456 -11.954 2.571   1.00 16.47 ?  83  LEU   B HD12 1 
ATOM   5341 H  HD13 . LEU   B 1 83  ? 49.638 -10.905 2.735   1.00 16.47 ?  83  LEU   B HD13 1 
ATOM   5342 H  HD21 . LEU   B 1 83  ? 48.079 -8.522  2.951   1.00 17.39 ?  83  LEU   B HD21 1 
ATOM   5343 H  HD22 . LEU   B 1 83  ? 49.202 -8.459  1.829   1.00 17.39 ?  83  LEU   B HD22 1 
ATOM   5344 H  HD23 . LEU   B 1 83  ? 47.690 -8.139  1.459   1.00 17.39 ?  83  LEU   B HD23 1 
ATOM   5345 N  N    . SER   B 1 84  ? 49.758 -9.596  -2.281  1.00 12.84 ?  84  SER   B N    1 
ATOM   5346 C  CA   . SER   B 1 84  ? 50.494 -9.742  -3.529  1.00 13.06 ?  84  SER   B CA   1 
ATOM   5347 C  C    . SER   B 1 84  ? 50.654 -11.209 -3.910  1.00 11.81 ?  84  SER   B C    1 
ATOM   5348 O  O    . SER   B 1 84  ? 50.768 -12.088 -3.056  1.00 12.03 ?  84  SER   B O    1 
ATOM   5349 C  CB   . SER   B 1 84  ? 51.892 -9.129  -3.397  1.00 14.87 ?  84  SER   B CB   1 
ATOM   5350 O  OG   . SER   B 1 84  ? 52.633 -9.359  -4.583  1.00 15.88 ?  84  SER   B OG   1 
ATOM   5351 H  H    . SER   B 1 84  ? 50.202 -9.245  -1.632  1.00 15.43 ?  84  SER   B H    1 
ATOM   5352 H  HA   . SER   B 1 84  ? 50.025 -9.286  -4.243  1.00 15.69 ?  84  SER   B HA   1 
ATOM   5353 H  HB2  . SER   B 1 84  ? 51.810 -8.173  -3.246  1.00 17.86 ?  84  SER   B HB2  1 
ATOM   5354 H  HB3  . SER   B 1 84  ? 52.353 -9.542  -2.646  1.00 17.86 ?  84  SER   B HB3  1 
ATOM   5355 H  HG   . SER   B 1 84  ? 53.408 -9.015  -4.507  1.00 19.08 ?  84  SER   B HG   1 
ATOM   5356 N  N    . GLY   B 1 85  ? 50.718 -11.455 -5.212  1.00 12.72 ?  85  GLY   B N    1 
ATOM   5357 C  CA   . GLY   B 1 85  ? 51.069 -12.759 -5.722  1.00 13.89 ?  85  GLY   B CA   1 
ATOM   5358 C  C    . GLY   B 1 85  ? 52.537 -12.946 -6.031  1.00 12.78 ?  85  GLY   B C    1 
ATOM   5359 O  O    . GLY   B 1 85  ? 52.915 -14.027 -6.484  1.00 13.24 ?  85  GLY   B O    1 
ATOM   5360 H  H    . GLY   B 1 85  ? 50.565 -10.880 -5.829  1.00 15.29 ?  85  GLY   B H    1 
ATOM   5361 H  HA2  . GLY   B 1 85  ? 50.816 -13.438 -5.073  1.00 16.68 ?  85  GLY   B HA2  1 
ATOM   5362 H  HA3  . GLY   B 1 85  ? 50.575 -12.933 -6.537  1.00 16.68 ?  85  GLY   B HA3  1 
ATOM   5363 N  N    . HIS   B 1 86  ? 53.385 -11.941 -5.824  1.00 12.69 ?  86  HIS   B N    1 
ATOM   5364 C  CA   . HIS   B 1 86  ? 54.845 -12.105 -5.923  1.00 13.42 ?  86  HIS   B CA   1 
ATOM   5365 C  C    . HIS   B 1 86  ? 55.215 -12.630 -7.309  1.00 13.28 ?  86  HIS   B C    1 
ATOM   5366 O  O    . HIS   B 1 86  ? 54.817 -12.026 -8.320  1.00 14.08 ?  86  HIS   B O    1 
ATOM   5367 C  CB   . HIS   B 1 86  ? 55.352 -12.929 -4.738  1.00 13.99 ?  86  HIS   B CB   1 
ATOM   5368 C  CG   . HIS   B 1 86  ? 55.034 -12.310 -3.420  1.00 13.96 ?  86  HIS   B CG   1 
ATOM   5369 N  ND1  . HIS   B 1 86  ? 55.862 -11.398 -2.806  1.00 15.81 ?  86  HIS   B ND1  1 
ATOM   5370 C  CD2  . HIS   B 1 86  ? 53.951 -12.436 -2.617  1.00 14.32 ?  86  HIS   B CD2  1 
ATOM   5371 C  CE1  . HIS   B 1 86  ? 55.305 -10.993 -1.678  1.00 15.89 ?  86  HIS   B CE1  1 
ATOM   5372 N  NE2  . HIS   B 1 86  ? 54.143 -11.604 -1.541  1.00 15.02 ?  86  HIS   B NE2  1 
ATOM   5373 H  H    . HIS   B 1 86  ? 53.143 -11.145 -5.623  1.00 15.25 ?  86  HIS   B H    1 
ATOM   5374 H  HA   . HIS   B 1 86  ? 55.252 -11.234 -5.839  1.00 16.12 ?  86  HIS   B HA   1 
ATOM   5375 H  HB2  . HIS   B 1 86  ? 54.945 -13.812 -4.763  1.00 16.81 ?  86  HIS   B HB2  1 
ATOM   5376 H  HB3  . HIS   B 1 86  ? 56.319 -13.016 -4.800  1.00 16.81 ?  86  HIS   B HB3  1 
ATOM   5377 H  HD2  . HIS   B 1 86  ? 53.205 -12.973 -2.775  1.00 17.20 ?  86  HIS   B HD2  1 
ATOM   5378 H  HE1  . HIS   B 1 86  ? 55.677 -10.393 -1.076  1.00 19.08 ?  86  HIS   B HE1  1 
ATOM   5379 H  HE2  . HIS   B 1 86  ? 53.600 -11.510 -0.882  1.00 18.05 ?  86  HIS   B HE2  1 
ATOM   5380 N  N    . ASN   B 1 87  ? 55.987 -13.716 -7.410  1.00 13.63 ?  87  ASN   B N    1 
ATOM   5381 C  CA   . ASN   B 1 87  ? 56.378 -14.308 -8.682  1.00 14.50 ?  87  ASN   B CA   1 
ATOM   5382 C  C    . ASN   B 1 87  ? 55.385 -15.341 -9.185  1.00 13.83 ?  87  ASN   B C    1 
ATOM   5383 O  O    . ASN   B 1 87  ? 55.680 -16.028 -10.167 1.00 16.06 ?  87  ASN   B O    1 
ATOM   5384 C  CB   . ASN   B 1 87  ? 57.766 -14.952 -8.566  1.00 16.83 ?  87  ASN   B CB   1 
ATOM   5385 C  CG   . ASN   B 1 87  ? 57.814 -16.061 -7.525  1.00 17.40 ?  87  ASN   B CG   1 
ATOM   5386 O  OD1  . ASN   B 1 87  ? 57.179 -15.969 -6.467  1.00 16.19 ?  87  ASN   B OD1  1 
ATOM   5387 N  ND2  . ASN   B 1 87  ? 58.574 -17.122 -7.824  1.00 19.73 ?  87  ASN   B ND2  1 
ATOM   5388 H  H    . ASN   B 1 87  ? 56.298 -14.148 -6.732  1.00 16.37 ?  87  ASN   B H    1 
ATOM   5389 H  HA   . ASN   B 1 87  ? 56.432 -13.611 -9.347  1.00 17.43 ?  87  ASN   B HA   1 
ATOM   5390 H  HB2  . ASN   B 1 87  ? 58.016 -15.333 -9.427  1.00 20.22 ?  87  ASN   B HB2  1 
ATOM   5391 H  HB3  . ASN   B 1 87  ? 58.409 -14.272 -8.312  1.00 20.22 ?  87  ASN   B HB3  1 
ATOM   5392 H  HD21 . ASN   B 1 87  ? 58.643 -17.776 -7.270  1.00 23.69 ?  87  ASN   B HD21 1 
ATOM   5393 H  HD22 . ASN   B 1 87  ? 59.008 -17.151 -8.572  1.00 23.69 ?  87  ASN   B HD22 1 
ATOM   5394 N  N    . LEU   B 1 88  ? 54.214 -15.447 -8.554  1.00 12.92 ?  88  LEU   B N    1 
ATOM   5395 C  CA   . LEU   B 1 88  ? 53.224 -16.468 -8.875  1.00 13.48 ?  88  LEU   B CA   1 
ATOM   5396 C  C    . LEU   B 1 88  ? 51.997 -15.940 -9.598  1.00 13.32 ?  88  LEU   B C    1 
ATOM   5397 O  O    . LEU   B 1 88  ? 51.393 -16.679 -10.384 1.00 15.04 ?  88  LEU   B O    1 
ATOM   5398 C  CB   . LEU   B 1 88  ? 52.750 -17.141 -7.586  1.00 14.63 ?  88  LEU   B CB   1 
ATOM   5399 C  CG   . LEU   B 1 88  ? 53.871 -17.814 -6.814  1.00 16.90 ?  88  LEU   B CG   1 
ATOM   5400 C  CD1  . LEU   B 1 88  ? 53.395 -18.162 -5.419  1.00 18.64 ?  88  LEU   B CD1  1 
ATOM   5401 C  CD2  . LEU   B 1 88  ? 54.296 -19.052 -7.567  1.00 20.24 ?  88  LEU   B CD2  1 
ATOM   5402 H  H    . LEU   B 1 88  ? 53.968 -14.923 -7.913  1.00 15.53 ?  88  LEU   B H    1 
ATOM   5403 H  HA   . LEU   B 1 88  ? 53.630 -17.138 -9.435  1.00 16.20 ?  88  LEU   B HA   1 
ATOM   5404 H  HB2  . LEU   B 1 88  ? 52.346 -16.474 -7.007  1.00 17.57 ?  88  LEU   B HB2  1 
ATOM   5405 H  HB3  . LEU   B 1 88  ? 52.090 -17.820 -7.810  1.00 17.57 ?  88  LEU   B HB3  1 
ATOM   5406 H  HG   . LEU   B 1 88  ? 54.629 -17.211 -6.747  1.00 20.30 ?  88  LEU   B HG   1 
ATOM   5407 H  HD11 . LEU   B 1 88  ? 54.050 -18.740 -5.001  1.00 22.39 ?  88  LEU   B HD11 1 
ATOM   5408 H  HD12 . LEU   B 1 88  ? 53.294 -17.345 -4.908  1.00 22.39 ?  88  LEU   B HD12 1 
ATOM   5409 H  HD13 . LEU   B 1 88  ? 52.543 -18.619 -5.488  1.00 22.39 ?  88  LEU   B HD13 1 
ATOM   5410 H  HD21 . LEU   B 1 88  ? 54.923 -19.549 -7.022  1.00 24.31 ?  88  LEU   B HD21 1 
ATOM   5411 H  HD22 . LEU   B 1 88  ? 53.513 -19.593 -7.751  1.00 24.31 ?  88  LEU   B HD22 1 
ATOM   5412 H  HD23 . LEU   B 1 88  ? 54.718 -18.788 -8.400  1.00 24.31 ?  88  LEU   B HD23 1 
ATOM   5413 N  N    . ALA   B 1 89  ? 51.593 -14.705 -9.320  1.00 12.65 ?  89  ALA   B N    1 
ATOM   5414 C  CA   . ALA   B 1 89  ? 50.309 -14.192 -9.771  1.00 12.16 ?  89  ALA   B CA   1 
ATOM   5415 C  C    . ALA   B 1 89  ? 50.304 -12.701 -9.481  1.00 12.57 ?  89  ALA   B C    1 
ATOM   5416 O  O    . ALA   B 1 89  ? 51.126 -12.206 -8.710  1.00 13.23 ?  89  ALA   B O    1 
ATOM   5417 C  CB   . ALA   B 1 89  ? 49.164 -14.858 -9.018  1.00 12.51 ?  89  ALA   B CB   1 
ATOM   5418 H  H    . ALA   B 1 89  ? 52.052 -14.129 -8.874  1.00 15.20 ?  89  ALA   B H    1 
ATOM   5419 H  HA   . ALA   B 1 89  ? 50.197 -14.337 -10.732 1.00 14.61 ?  89  ALA   B HA   1 
ATOM   5420 H  HB1  . ALA   B 1 89  ? 48.321 -14.515 -9.356  1.00 15.03 ?  89  ALA   B HB1  1 
ATOM   5421 H  HB2  . ALA   B 1 89  ? 49.210 -15.818 -9.168  1.00 15.03 ?  89  ALA   B HB2  1 
ATOM   5422 H  HB3  . ALA   B 1 89  ? 49.255 -14.663 -8.079  1.00 15.03 ?  89  ALA   B HB3  1 
ATOM   5423 N  N    . LYS   B 1 90  ? 49.346 -11.988 -10.069 1.00 13.19 ?  90  LYS   B N    1 
ATOM   5424 C  CA   . LYS   B 1 90  ? 49.166 -10.599 -9.660  1.00 13.12 ?  90  LYS   B CA   1 
ATOM   5425 C  C    . LYS   B 1 90  ? 48.836 -10.522 -8.172  1.00 12.58 ?  90  LYS   B C    1 
ATOM   5426 O  O    . LYS   B 1 90  ? 49.479 -9.780  -7.416  1.00 13.34 ?  90  LYS   B O    1 
ATOM   5427 C  CB   . LYS   B 1 90  ? 48.097 -9.931  -10.521 1.00 14.53 ?  90  LYS   B CB   1 
ATOM   5428 C  CG   . LYS   B 1 90  ? 47.764 -8.506  -10.109 1.00 15.05 ?  90  LYS   B CG   1 
ATOM   5429 C  CD   . LYS   B 1 90  ? 48.950 -7.576  -10.174 1.00 17.25 ?  90  LYS   B CD   1 
ATOM   5430 C  CE   . LYS   B 1 90  ? 48.471 -6.187  -9.835  1.00 18.93 ?  90  LYS   B CE   1 
ATOM   5431 N  NZ   . LYS   B 1 90  ? 49.576 -5.206  -9.794  1.00 18.05 ?  90  LYS   B NZ   1 
ATOM   5432 H  H    . LYS   B 1 90  ? 48.809 -12.273 -10.681 1.00 15.85 ?  90  LYS   B H    1 
ATOM   5433 H  HA   . LYS   B 1 90  ? 49.998 -10.125 -9.806  1.00 15.76 ?  90  LYS   B HA   1 
ATOM   5434 H  HB2  . LYS   B 1 90  ? 48.405 -9.906  -11.445 1.00 17.45 ?  90  LYS   B HB2  1 
ATOM   5435 H  HB3  . LYS   B 1 90  ? 47.280 -10.454 -10.471 1.00 17.45 ?  90  LYS   B HB3  1 
ATOM   5436 H  HG2  . LYS   B 1 90  ? 47.080 -8.157  -10.708 1.00 18.09 ?  90  LYS   B HG2  1 
ATOM   5437 H  HG3  . LYS   B 1 90  ? 47.426 -8.503  -9.199  1.00 18.09 ?  90  LYS   B HG3  1 
ATOM   5438 H  HD2  . LYS   B 1 90  ? 49.619 -7.842  -9.525  1.00 20.72 ?  90  LYS   B HD2  1 
ATOM   5439 H  HD3  . LYS   B 1 90  ? 49.320 -7.569  -11.072 1.00 20.72 ?  90  LYS   B HD3  1 
ATOM   5440 H  HE2  . LYS   B 1 90  ? 47.835 -5.890  -10.508 1.00 22.74 ?  90  LYS   B HE2  1 
ATOM   5441 H  HE3  . LYS   B 1 90  ? 48.049 -6.193  -8.962  1.00 22.74 ?  90  LYS   B HE3  1 
ATOM   5442 H  HZ1  . LYS   B 1 90  ? 49.263 -4.394  -9.594  1.00 21.68 ?  90  LYS   B HZ1  1 
ATOM   5443 H  HZ2  . LYS   B 1 90  ? 50.174 -5.442  -9.181  1.00 21.68 ?  90  LYS   B HZ2  1 
ATOM   5444 H  HZ3  . LYS   B 1 90  ? 49.980 -5.166  -10.589 1.00 21.68 ?  90  LYS   B HZ3  1 
ATOM   5445 N  N    . HIS   B 1 91  ? 47.861 -11.329 -7.734  1.00 11.66 ?  91  HIS   B N    1 
ATOM   5446 C  CA   . HIS   B 1 91  ? 47.381 -11.354 -6.366  1.00 11.63 ?  91  HIS   B CA   1 
ATOM   5447 C  C    . HIS   B 1 91  ? 47.370 -12.779 -5.840  1.00 10.82 ?  91  HIS   B C    1 
ATOM   5448 O  O    . HIS   B 1 91  ? 47.135 -13.729 -6.594  1.00 11.49 ?  91  HIS   B O    1 
ATOM   5449 C  CB   . HIS   B 1 91  ? 45.929 -10.860 -6.261  1.00 13.10 ?  91  HIS   B CB   1 
ATOM   5450 C  CG   . HIS   B 1 91  ? 45.737 -9.440  -6.670  1.00 16.42 ?  91  HIS   B CG   1 
ATOM   5451 N  ND1  . HIS   B 1 91  ? 46.365 -8.385  -6.041  1.00 18.96 ?  91  HIS   B ND1  1 
ATOM   5452 C  CD2  . HIS   B 1 91  ? 44.953 -8.894  -7.627  1.00 19.28 ?  91  HIS   B CD2  1 
ATOM   5453 C  CE1  . HIS   B 1 91  ? 45.994 -7.251  -6.609  1.00 20.02 ?  91  HIS   B CE1  1 
ATOM   5454 N  NE2  . HIS   B 1 91  ? 45.133 -7.532  -7.571  1.00 20.61 ?  91  HIS   B NE2  1 
ATOM   5455 H  H    . HIS   B 1 91  ? 47.452 -11.895 -8.242  1.00 14.02 ?  91  HIS   B H    1 
ATOM   5456 H  HA   . HIS   B 1 91  ? 47.950 -10.802 -5.802  1.00 13.98 ?  91  HIS   B HA   1 
ATOM   5457 H  HB2  . HIS   B 1 91  ? 45.367 -11.406 -6.832  1.00 15.73 ?  91  HIS   B HB2  1 
ATOM   5458 H  HB3  . HIS   B 1 91  ? 45.634 -10.939 -5.340  1.00 15.73 ?  91  HIS   B HB3  1 
ATOM   5459 H  HD2  . HIS   B 1 91  ? 44.402 -9.347  -8.223  1.00 23.16 ?  91  HIS   B HD2  1 
ATOM   5460 H  HE1  . HIS   B 1 91  ? 46.281 -6.398  -6.363  1.00 24.05 ?  91  HIS   B HE1  1 
ATOM   5461 H  HE2  . HIS   B 1 91  ? 44.755 -6.949  -8.084  1.00 24.75 ?  91  HIS   B HE2  1 
ATOM   5462 N  N    . CYS   B 1 92  ? 47.553 -12.911 -4.535  1.00 10.66 ?  92  CYS   B N    1 
ATOM   5463 C  CA   . CYS   B 1 92  ? 47.243 -14.145 -3.826  1.00 10.86 ?  92  CYS   B CA   1 
ATOM   5464 C  C    . CYS   B 1 92  ? 46.021 -13.904 -2.949  1.00 10.58 ?  92  CYS   B C    1 
ATOM   5465 O  O    . CYS   B 1 92  ? 46.021 -12.995 -2.109  1.00 11.27 ?  92  CYS   B O    1 
ATOM   5466 C  CB   . CYS   B 1 92  ? 48.422 -14.616 -2.980  1.00 11.21 ?  92  CYS   B CB   1 
ATOM   5467 S  SG   . CYS   B 1 92  ? 48.052 -16.141 -2.061  1.00 11.59 ?  92  CYS   B SG   1 
ATOM   5468 H  H    . CYS   B 1 92  ? 47.873 -12.289 -4.029  1.00 12.82 ?  92  CYS   B H    1 
ATOM   5469 H  HA   . CYS   B 1 92  ? 47.033 -14.839 -4.470  1.00 13.05 ?  92  CYS   B HA   1 
ATOM   5470 H  HB2  . CYS   B 1 92  ? 49.177 -14.790 -3.557  1.00 13.47 ?  92  CYS   B HB2  1 
ATOM   5471 H  HB3  . CYS   B 1 92  ? 48.641 -13.926 -2.335  1.00 13.47 ?  92  CYS   B HB3  1 
ATOM   5472 H  HG   . CYS   B 1 92  ? 49.025 -16.462 -1.446  1.00 13.93 ?  92  CYS   B HG   1 
ATOM   5473 N  N    . LEU   B 1 93  ? 44.982 -14.712 -3.157  1.00 10.50 ?  93  LEU   B N    1 
ATOM   5474 C  CA   . LEU   B 1 93  ? 43.805 -14.717 -2.299  1.00 10.38 ?  93  LEU   B CA   1 
ATOM   5475 C  C    . LEU   B 1 93  ? 44.034 -15.778 -1.228  1.00 10.19 ?  93  LEU   B C    1 
ATOM   5476 O  O    . LEU   B 1 93  ? 43.987 -16.979 -1.518  1.00 10.91 ?  93  LEU   B O    1 
ATOM   5477 C  CB   . LEU   B 1 93  ? 42.546 -15.005 -3.114  1.00 10.73 ?  93  LEU   B CB   1 
ATOM   5478 C  CG   . LEU   B 1 93  ? 41.251 -15.018 -2.298  1.00 11.62 ?  93  LEU   B CG   1 
ATOM   5479 C  CD1  . LEU   B 1 93  ? 40.888 -13.630 -1.797  1.00 12.44 ?  93  LEU   B CD1  1 
ATOM   5480 C  CD2  . LEU   B 1 93  ? 40.120 -15.623 -3.112  1.00 11.96 ?  93  LEU   B CD2  1 
ATOM   5481 H  H    . LEU   B 1 93  ? 44.940 -15.287 -3.802  1.00 12.62 ?  93  LEU   B H    1 
ATOM   5482 H  HA   . LEU   B 1 93  ? 43.709 -13.854 -1.872  1.00 12.48 ?  93  LEU   B HA   1 
ATOM   5483 H  HB2  . LEU   B 1 93  ? 42.457 -14.316 -3.796  1.00 12.90 ?  93  LEU   B HB2  1 
ATOM   5484 H  HB3  . LEU   B 1 93  ? 42.638 -15.870 -3.536  1.00 12.90 ?  93  LEU   B HB3  1 
ATOM   5485 H  HG   . LEU   B 1 93  ? 41.382 -15.577 -1.521  1.00 13.96 ?  93  LEU   B HG   1 
ATOM   5486 H  HD11 . LEU   B 1 93  ? 40.038 -13.676 -1.337  1.00 14.94 ?  93  LEU   B HD11 1 
ATOM   5487 H  HD12 . LEU   B 1 93  ? 41.580 -13.321 -1.193  1.00 14.94 ?  93  LEU   B HD12 1 
ATOM   5488 H  HD13 . LEU   B 1 93  ? 40.821 -13.029 -2.558  1.00 14.94 ?  93  LEU   B HD13 1 
ATOM   5489 H  HD21 . LEU   B 1 93  ? 39.306 -15.613 -2.581  1.00 14.37 ?  93  LEU   B HD21 1 
ATOM   5490 H  HD22 . LEU   B 1 93  ? 39.991 -15.102 -3.920  1.00 14.37 ?  93  LEU   B HD22 1 
ATOM   5491 H  HD23 . LEU   B 1 93  ? 40.349 -16.538 -3.343  1.00 14.37 ?  93  LEU   B HD23 1 
ATOM   5492 N  N    . HIS   B 1 94  ? 44.314 -15.340 -0.008  1.00 10.31 ?  94  HIS   B N    1 
ATOM   5493 C  CA   . HIS   B 1 94  ? 44.528 -16.244 1.114   1.00 10.41 ?  94  HIS   B CA   1 
ATOM   5494 C  C    . HIS   B 1 94  ? 43.166 -16.594 1.695   1.00 10.68 ?  94  HIS   B C    1 
ATOM   5495 O  O    . HIS   B 1 94  ? 42.494 -15.718 2.240   1.00 12.31 ?  94  HIS   B O    1 
ATOM   5496 C  CB   . HIS   B 1 94  ? 45.401 -15.573 2.173   1.00 11.11 ?  94  HIS   B CB   1 
ATOM   5497 C  CG   . HIS   B 1 94  ? 46.781 -15.271 1.699   1.00 11.05 ?  94  HIS   B CG   1 
ATOM   5498 N  ND1  . HIS   B 1 94  ? 47.808 -16.185 1.782   1.00 11.12 ?  94  HIS   B ND1  1 
ATOM   5499 C  CD2  . HIS   B 1 94  ? 47.288 -14.164 1.101   1.00 11.39 ?  94  HIS   B CD2  1 
ATOM   5500 C  CE1  . HIS   B 1 94  ? 48.897 -15.635 1.270   1.00 11.44 ?  94  HIS   B CE1  1 
ATOM   5501 N  NE2  . HIS   B 1 94  ? 48.610 -14.414 0.848   1.00 11.52 ?  94  HIS   B NE2  1 
ATOM   5502 H  H    . HIS   B 1 94  ? 44.398 -14.502 0.193   1.00 12.40 ?  94  HIS   B H    1 
ATOM   5503 H  HA   . HIS   B 1 94  ? 44.965 -17.050 0.806   1.00 12.51 ?  94  HIS   B HA   1 
ATOM   5504 H  HB2  . HIS   B 1 94  ? 44.989 -14.738 2.435   1.00 13.36 ?  94  HIS   B HB2  1 
ATOM   5505 H  HB3  . HIS   B 1 94  ? 45.475 -16.166 2.932   1.00 13.36 ?  94  HIS   B HB3  1 
ATOM   5506 H  HD2  . HIS   B 1 94  ? 46.827 -13.381 0.902   1.00 13.68 ?  94  HIS   B HD2  1 
ATOM   5507 H  HE1  . HIS   B 1 94  ? 49.726 -16.052 1.207   1.00 13.74 ?  94  HIS   B HE1  1 
ATOM   5508 H  HE2  . HIS   B 1 94  ? 49.164 -13.873 0.477   1.00 13.85 ?  94  HIS   B HE2  1 
ATOM   5509 N  N    . VAL   B 1 95  ? 42.729 -17.847 1.553   1.00 10.57 ?  95  VAL   B N    1 
ATOM   5510 C  CA   . VAL   B 1 95  ? 41.400 -18.279 1.986   1.00 10.62 ?  95  VAL   B CA   1 
ATOM   5511 C  C    . VAL   B 1 95  ? 41.562 -19.311 3.086   1.00 10.76 ?  95  VAL   B C    1 
ATOM   5512 O  O    . VAL   B 1 95  ? 42.336 -20.265 2.934   1.00 11.73 ?  95  VAL   B O    1 
ATOM   5513 C  CB   . VAL   B 1 95  ? 40.587 -18.887 0.828   1.00 11.06 ?  95  VAL   B CB   1 
ATOM   5514 C  CG1  . VAL   B 1 95  ? 39.216 -19.333 1.315   1.00 12.59 ?  95  VAL   B CG1  1 
ATOM   5515 C  CG2  . VAL   B 1 95  ? 40.445 -17.900 -0.305  1.00 11.30 ?  95  VAL   B CG2  1 
ATOM   5516 H  H    . VAL   B 1 95  ? 43.198 -18.480 1.197   1.00 12.71 ?  95  VAL   B H    1 
ATOM   5517 H  HA   . VAL   B 1 95  ? 40.910 -17.522 2.338   1.00 12.77 ?  95  VAL   B HA   1 
ATOM   5518 H  HB   . VAL   B 1 95  ? 41.052 -19.664 0.486   1.00 13.29 ?  95  VAL   B HB   1 
ATOM   5519 H  HG11 . VAL   B 1 95  ? 38.650 -19.513 0.544   1.00 15.13 ?  95  VAL   B HG11 1 
ATOM   5520 H  HG12 . VAL   B 1 95  ? 39.312 -20.140 1.843   1.00 15.13 ?  95  VAL   B HG12 1 
ATOM   5521 H  HG13 . VAL   B 1 95  ? 38.823 -18.627 1.851   1.00 15.13 ?  95  VAL   B HG13 1 
ATOM   5522 H  HG21 . VAL   B 1 95  ? 39.877 -18.287 -0.989  1.00 13.58 ?  95  VAL   B HG21 1 
ATOM   5523 H  HG22 . VAL   B 1 95  ? 40.039 -17.086 0.039   1.00 13.58 ?  95  VAL   B HG22 1 
ATOM   5524 H  HG23 . VAL   B 1 95  ? 41.320 -17.708 -0.665  1.00 13.58 ?  95  VAL   B HG23 1 
ATOM   5525 N  N    . VAL   B 1 96  ? 40.837 -19.128 4.181   1.00 11.39 ?  96  VAL   B N    1 
ATOM   5526 C  CA   . VAL   B 1 96  ? 40.917 -20.031 5.328   1.00 11.97 ?  96  VAL   B CA   1 
ATOM   5527 C  C    . VAL   B 1 96  ? 39.732 -20.995 5.286   1.00 12.69 ?  96  VAL   B C    1 
ATOM   5528 O  O    . VAL   B 1 96  ? 38.613 -20.645 5.668   1.00 13.18 ?  96  VAL   B O    1 
ATOM   5529 C  CB   . VAL   B 1 96  ? 40.964 -19.277 6.660   1.00 12.56 ?  96  VAL   B CB   1 
ATOM   5530 C  CG1  . VAL   B 1 96  ? 41.121 -20.273 7.807   1.00 13.64 ?  96  VAL   B CG1  1 
ATOM   5531 C  CG2  . VAL   B 1 96  ? 42.088 -18.248 6.675   1.00 13.22 ?  96  VAL   B CG2  1 
ATOM   5532 H  H    . VAL   B 1 96  ? 40.284 -18.478 4.294   1.00 13.68 ?  96  VAL   B H    1 
ATOM   5533 H  HA   . VAL   B 1 96  ? 41.734 -20.556 5.263   1.00 14.39 ?  96  VAL   B HA   1 
ATOM   5534 H  HB   . VAL   B 1 96  ? 40.127 -18.810 6.791   1.00 15.10 ?  96  VAL   B HB   1 
ATOM   5535 H  HG11 . VAL   B 1 96  ? 41.331 -19.789 8.625   1.00 16.39 ?  96  VAL   B HG11 1 
ATOM   5536 H  HG12 . VAL   B 1 96  ? 40.293 -20.766 7.924   1.00 16.39 ?  96  VAL   B HG12 1 
ATOM   5537 H  HG13 . VAL   B 1 96  ? 41.845 -20.889 7.601   1.00 16.39 ?  96  VAL   B HG13 1 
ATOM   5538 H  HG21 . VAL   B 1 96  ? 42.127 -17.828 7.552   1.00 15.89 ?  96  VAL   B HG21 1 
ATOM   5539 H  HG22 . VAL   B 1 96  ? 42.930 -18.687 6.483   1.00 15.89 ?  96  VAL   B HG22 1 
ATOM   5540 H  HG23 . VAL   B 1 96  ? 41.906 -17.572 6.000   1.00 15.89 ?  96  VAL   B HG23 1 
ATOM   5541 N  N    . GLY   B 1 97  ? 39.967 -22.220 4.831   1.00 12.43 ?  97  GLY   B N    1 
ATOM   5542 C  CA   . GLY   B 1 97  ? 39.006 -23.283 5.016   1.00 13.49 ?  97  GLY   B CA   1 
ATOM   5543 C  C    . GLY   B 1 97  ? 39.167 -23.886 6.395   1.00 15.04 ?  97  GLY   B C    1 
ATOM   5544 O  O    . GLY   B 1 97  ? 40.220 -23.758 7.028   1.00 15.58 ?  97  GLY   B O    1 
ATOM   5545 H  H    . GLY   B 1 97  ? 40.683 -22.450 4.402   1.00 14.94 ?  97  GLY   B H    1 
ATOM   5546 H  HA2  . GLY   B 1 97  ? 38.110 -22.922 4.912   1.00 16.21 ?  97  GLY   B HA2  1 
ATOM   5547 H  HA3  . GLY   B 1 97  ? 39.147 -23.968 4.344   1.00 16.21 ?  97  GLY   B HA3  1 
ATOM   5548 N  N    . PRO   B 1 98  ? 38.124 -24.549 6.894   1.00 16.19 ?  98  PRO   B N    1 
ATOM   5549 C  CA   . PRO   B 1 98  ? 38.242 -25.224 8.191   1.00 17.83 ?  98  PRO   B CA   1 
ATOM   5550 C  C    . PRO   B 1 98  ? 39.252 -26.361 8.142   1.00 17.09 ?  98  PRO   B C    1 
ATOM   5551 O  O    . PRO   B 1 98  ? 39.330 -27.111 7.169   1.00 16.97 ?  98  PRO   B O    1 
ATOM   5552 C  CB   . PRO   B 1 98  ? 36.822 -25.745 8.448   1.00 18.95 ?  98  PRO   B CB   1 
ATOM   5553 C  CG   . PRO   B 1 98  ? 36.222 -25.894 7.102   1.00 18.18 ?  98  PRO   B CG   1 
ATOM   5554 C  CD   . PRO   B 1 98  ? 36.789 -24.743 6.296   1.00 17.03 ?  98  PRO   B CD   1 
ATOM   5555 H  HA   . PRO   B 1 98  ? 38.493 -24.593 8.880   1.00 21.41 ?  98  PRO   B HA   1 
ATOM   5556 H  HB2  . PRO   B 1 98  ? 36.866 -26.602 8.903   1.00 22.76 ?  98  PRO   B HB2  1 
ATOM   5557 H  HB3  . PRO   B 1 98  ? 36.328 -25.100 8.975   1.00 22.76 ?  98  PRO   B HB3  1 
ATOM   5558 H  HG2  . PRO   B 1 98  ? 36.489 -26.747 6.721   1.00 21.83 ?  98  PRO   B HG2  1 
ATOM   5559 H  HG3  . PRO   B 1 98  ? 35.259 -25.832 7.167   1.00 21.83 ?  98  PRO   B HG3  1 
ATOM   5560 H  HD2  . PRO   B 1 98  ? 36.862 -24.993 5.358   1.00 20.45 ?  98  PRO   B HD2  1 
ATOM   5561 H  HD3  . PRO   B 1 98  ? 36.247 -23.949 6.411   1.00 20.45 ?  98  PRO   B HD3  1 
ATOM   5562 N  N    . ASN   B 1 99  ? 40.024 -26.487 9.217   1.00 18.48 ?  99  ASN   B N    1 
ATOM   5563 C  CA   . ASN   B 1 99  ? 41.008 -27.557 9.372   1.00 19.55 ?  99  ASN   B CA   1 
ATOM   5564 C  C    . ASN   B 1 99  ? 40.401 -28.621 10.282  1.00 21.78 ?  99  ASN   B C    1 
ATOM   5565 O  O    . ASN   B 1 99  ? 40.383 -28.464 11.504  1.00 23.48 ?  99  ASN   B O    1 
ATOM   5566 C  CB   . ASN   B 1 99  ? 42.295 -26.993 9.962   1.00 19.94 ?  99  ASN   B CB   1 
ATOM   5567 C  CG   . ASN   B 1 99  ? 43.427 -28.000 9.973   1.00 20.41 ?  99  ASN   B CG   1 
ATOM   5568 O  OD1  . ASN   B 1 99  ? 43.216 -29.180 10.212  1.00 21.02 ?  99  ASN   B OD1  1 
ATOM   5569 N  ND2  . ASN   B 1 99  ? 44.631 -27.534 9.702   1.00 20.65 ?  99  ASN   B ND2  1 
ATOM   5570 H  H    . ASN   B 1 99  ? 39.997 -25.949 9.881   1.00 22.19 ?  99  ASN   B H    1 
ATOM   5571 H  HA   . ASN   B 1 99  ? 41.200 -27.962 8.510   1.00 23.48 ?  99  ASN   B HA   1 
ATOM   5572 H  HB2  . ASN   B 1 99  ? 42.565 -26.231 9.440   1.00 23.95 ?  99  ASN   B HB2  1 
ATOM   5573 H  HB3  . ASN   B 1 99  ? 42.121 -26.733 10.881  1.00 23.95 ?  99  ASN   B HB3  1 
ATOM   5574 H  HD21 . ASN   B 1 99  ? 45.303 -28.061 9.686   1.00 24.79 ?  99  ASN   B HD21 1 
ATOM   5575 H  HD22 . ASN   B 1 99  ? 44.731 -26.693 9.542   1.00 24.79 ?  99  ASN   B HD22 1 
ATOM   5576 N  N    . VAL   B 1 100 ? 39.887 -29.696 9.673   1.00 24.32 ?  100 VAL   B N    1 
ATOM   5577 C  CA   . VAL   B 1 100 ? 39.278 -30.784 10.439  1.00 27.66 ?  100 VAL   B CA   1 
ATOM   5578 C  C    . VAL   B 1 100 ? 40.303 -31.464 11.340  1.00 28.28 ?  100 VAL   B C    1 
ATOM   5579 O  O    . VAL   B 1 100 ? 39.958 -31.961 12.419  1.00 29.83 ?  100 VAL   B O    1 
ATOM   5580 C  CB   . VAL   B 1 100 ? 38.580 -31.780 9.488   1.00 30.20 ?  100 VAL   B CB   1 
ATOM   5581 C  CG1  . VAL   B 1 100 ? 38.090 -33.001 10.247  1.00 31.34 ?  100 VAL   B CG1  1 
ATOM   5582 C  CG2  . VAL   B 1 100 ? 37.419 -31.097 8.778   1.00 30.95 ?  100 VAL   B CG2  1 
ATOM   5583 H  H    . VAL   B 1 100 ? 39.859 -29.809 8.814   1.00 29.21 ?  100 VAL   B H    1 
ATOM   5584 H  HA   . VAL   B 1 100 ? 38.587 -30.413 11.006  1.00 33.21 ?  100 VAL   B HA   1 
ATOM   5585 H  HB   . VAL   B 1 100 ? 39.211 -32.080 8.814   1.00 36.26 ?  100 VAL   B HB   1 
ATOM   5586 H  HG11 . VAL   B 1 100 ? 37.468 -33.493 9.685   1.00 37.63 ?  100 VAL   B HG11 1 
ATOM   5587 H  HG12 . VAL   B 1 100 ? 38.846 -33.565 10.469  1.00 37.63 ?  100 VAL   B HG12 1 
ATOM   5588 H  HG13 . VAL   B 1 100 ? 37.640 -32.710 11.055  1.00 37.63 ?  100 VAL   B HG13 1 
ATOM   5589 H  HG21 . VAL   B 1 100 ? 36.974 -31.742 8.205   1.00 37.16 ?  100 VAL   B HG21 1 
ATOM   5590 H  HG22 . VAL   B 1 100 ? 36.796 -30.762 9.443   1.00 37.16 ?  100 VAL   B HG22 1 
ATOM   5591 H  HG23 . VAL   B 1 100 ? 37.762 -30.364 8.246   1.00 37.16 ?  100 VAL   B HG23 1 
ATOM   5592 N  N    . ASN   B 1 101 ? 41.568 -31.520 10.915  1.00 29.22 ?  101 ASN   B N    1 
ATOM   5593 C  CA   . ASN   B 1 101 ? 42.612 -32.059 11.784  1.00 30.70 ?  101 ASN   B CA   1 
ATOM   5594 C  C    . ASN   B 1 101 ? 42.792 -31.224 13.046  1.00 34.64 ?  101 ASN   B C    1 
ATOM   5595 O  O    . ASN   B 1 101 ? 43.385 -31.709 14.019  1.00 35.19 ?  101 ASN   B O    1 
ATOM   5596 C  CB   . ASN   B 1 101 ? 43.930 -32.198 11.019  1.00 29.96 ?  101 ASN   B CB   1 
ATOM   5597 C  CG   . ASN   B 1 101 ? 43.910 -33.358 10.038  1.00 28.92 ?  101 ASN   B CG   1 
ATOM   5598 O  OD1  . ASN   B 1 101 ? 43.214 -34.348 10.250  1.00 29.56 ?  101 ASN   B OD1  1 
ATOM   5599 N  ND2  . ASN   B 1 101 ? 44.665 -33.234 8.953   1.00 28.39 ?  101 ASN   B ND2  1 
ATOM   5600 H  H    . ASN   B 1 101 ? 41.835 -31.277 10.135  1.00 35.08 ?  101 ASN   B H    1 
ATOM   5601 H  HA   . ASN   B 1 101 ? 42.347 -32.946 12.065  1.00 36.86 ?  101 ASN   B HA   1 
ATOM   5602 H  HB2  . ASN   B 1 101 ? 44.101 -31.386 10.519  1.00 35.97 ?  101 ASN   B HB2  1 
ATOM   5603 H  HB3  . ASN   B 1 101 ? 44.648 -32.355 11.652  1.00 35.97 ?  101 ASN   B HB3  1 
ATOM   5604 H  HD21 . ASN   B 1 101 ? 44.683 -33.865 8.370   1.00 34.09 ?  101 ASN   B HD21 1 
ATOM   5605 H  HD22 . ASN   B 1 101 ? 45.137 -32.524 8.835   1.00 34.09 ?  101 ASN   B HD22 1 
ATOM   5606 N  N    A LYS   B 1 102 ? 42.301 -29.984 13.048  0.62 37.17 ?  102 LYS   B N    1 
ATOM   5607 N  N    B LYS   B 1 102 ? 42.298 -29.986 13.053  0.38 37.06 ?  102 LYS   B N    1 
ATOM   5608 C  CA   A LYS   B 1 102 ? 42.252 -29.146 14.238  0.62 39.73 ?  102 LYS   B CA   1 
ATOM   5609 C  CA   B LYS   B 1 102 ? 42.255 -29.160 14.251  0.38 39.42 ?  102 LYS   B CA   1 
ATOM   5610 C  C    A LYS   B 1 102 ? 40.871 -29.132 14.882  0.62 39.51 ?  102 LYS   B C    1 
ATOM   5611 C  C    B LYS   B 1 102 ? 40.867 -29.126 14.878  0.38 39.47 ?  102 LYS   B C    1 
ATOM   5612 O  O    A LYS   B 1 102 ? 40.634 -28.340 15.800  0.62 39.98 ?  102 LYS   B O    1 
ATOM   5613 O  O    B LYS   B 1 102 ? 40.625 -28.320 15.783  0.38 39.84 ?  102 LYS   B O    1 
ATOM   5614 C  CB   A LYS   B 1 102 ? 42.657 -27.711 13.897  0.62 42.56 ?  102 LYS   B CB   1 
ATOM   5615 C  CB   B LYS   B 1 102 ? 42.713 -27.735 13.935  0.38 41.73 ?  102 LYS   B CB   1 
ATOM   5616 C  CG   A LYS   B 1 102 ? 44.109 -27.518 13.504  0.62 45.00 ?  102 LYS   B CG   1 
ATOM   5617 C  CG   B LYS   B 1 102 ? 44.182 -27.612 13.563  0.38 43.66 ?  102 LYS   B CG   1 
ATOM   5618 C  CD   A LYS   B 1 102 ? 44.350 -26.065 13.125  0.62 47.47 ?  102 LYS   B CD   1 
ATOM   5619 C  CD   B LYS   B 1 102 ? 44.525 -26.178 13.189  0.38 45.65 ?  102 LYS   B CD   1 
ATOM   5620 C  CE   A LYS   B 1 102 ? 45.809 -25.787 12.822  0.62 49.05 ?  102 LYS   B CE   1 
ATOM   5621 C  CE   B LYS   B 1 102 ? 46.007 -26.005 12.903  0.38 46.88 ?  102 LYS   B CE   1 
ATOM   5622 N  NZ   A LYS   B 1 102 ? 46.022 -24.359 12.446  0.62 50.06 ?  102 LYS   B NZ   1 
ATOM   5623 N  NZ   B LYS   B 1 102 ? 46.330 -24.602 12.509  0.38 47.74 ?  102 LYS   B NZ   1 
ATOM   5624 H  H    A LYS   B 1 102 ? 41.981 -29.596 12.348  0.62 44.62 ?  102 LYS   B H    1 
ATOM   5625 H  H    B LYS   B 1 102 ? 41.970 -29.596 12.359  0.38 44.50 ?  102 LYS   B H    1 
ATOM   5626 H  HA   A LYS   B 1 102 ? 42.887 -29.487 14.886  0.62 47.70 ?  102 LYS   B HA   1 
ATOM   5627 H  HA   B LYS   B 1 102 ? 42.869 -29.527 14.905  0.38 47.33 ?  102 LYS   B HA   1 
ATOM   5628 H  HB2  A LYS   B 1 102 ? 42.114 -27.405 13.155  0.62 51.09 ?  102 LYS   B HB2  1 
ATOM   5629 H  HB2  B LYS   B 1 102 ? 42.191 -27.399 13.190  0.38 50.10 ?  102 LYS   B HB2  1 
ATOM   5630 H  HB3  A LYS   B 1 102 ? 42.492 -27.153 14.673  0.62 51.09 ?  102 LYS   B HB3  1 
ATOM   5631 H  HB3  B LYS   B 1 102 ? 42.561 -27.180 14.717  0.38 50.10 ?  102 LYS   B HB3  1 
ATOM   5632 H  HG2  A LYS   B 1 102 ? 44.684 -27.741 14.254  0.62 54.02 ?  102 LYS   B HG2  1 
ATOM   5633 H  HG2  B LYS   B 1 102 ? 44.730 -27.871 14.321  0.38 52.41 ?  102 LYS   B HG2  1 
ATOM   5634 H  HG3  A LYS   B 1 102 ? 44.318 -28.076 12.738  0.62 54.02 ?  102 LYS   B HG3  1 
ATOM   5635 H  HG3  B LYS   B 1 102 ? 44.370 -28.182 12.800  0.38 52.41 ?  102 LYS   B HG3  1 
ATOM   5636 H  HD2  A LYS   B 1 102 ? 43.830 -25.852 12.333  0.62 56.98 ?  102 LYS   B HD2  1 
ATOM   5637 H  HD2  B LYS   B 1 102 ? 44.031 -25.929 12.391  0.38 54.80 ?  102 LYS   B HD2  1 
ATOM   5638 H  HD3  A LYS   B 1 102 ? 44.080 -25.495 13.863  0.62 56.98 ?  102 LYS   B HD3  1 
ATOM   5639 H  HD3  B LYS   B 1 102 ? 44.287 -25.591 13.925  0.38 54.80 ?  102 LYS   B HD3  1 
ATOM   5640 H  HE2  A LYS   B 1 102 ? 46.342 -25.977 13.610  0.62 58.87 ?  102 LYS   B HE2  1 
ATOM   5641 H  HE2  B LYS   B 1 102 ? 46.515 -26.220 13.701  0.38 56.27 ?  102 LYS   B HE2  1 
ATOM   5642 H  HE3  A LYS   B 1 102 ? 46.094 -26.343 12.080  0.62 58.87 ?  102 LYS   B HE3  1 
ATOM   5643 H  HE3  B LYS   B 1 102 ? 46.264 -26.592 12.174  0.38 56.27 ?  102 LYS   B HE3  1 
ATOM   5644 H  HZ1  A LYS   B 1 102 ? 46.882 -24.215 12.272  0.62 60.09 ?  102 LYS   B HZ1  1 
ATOM   5645 H  HZ1  B LYS   B 1 102 ? 47.201 -24.524 12.347  0.38 57.31 ?  102 LYS   B HZ1  1 
ATOM   5646 H  HZ2  A LYS   B 1 102 ? 45.543 -24.161 11.722  0.62 60.09 ?  102 LYS   B HZ2  1 
ATOM   5647 H  HZ2  B LYS   B 1 102 ? 45.877 -24.381 11.775  0.38 57.31 ?  102 LYS   B HZ2  1 
ATOM   5648 H  HZ3  A LYS   B 1 102 ? 45.768 -23.828 13.114  0.62 60.09 ?  102 LYS   B HZ3  1 
ATOM   5649 H  HZ3  B LYS   B 1 102 ? 46.106 -24.043 13.165  0.38 57.31 ?  102 LYS   B HZ3  1 
ATOM   5650 N  N    . GLY   B 1 103 ? 39.950 -29.970 14.412  1.00 39.52 ?  103 GLY   B N    1 
ATOM   5651 C  CA   . GLY   B 1 103 ? 38.619 -30.043 14.980  1.00 39.90 ?  103 GLY   B CA   1 
ATOM   5652 C  C    . GLY   B 1 103 ? 37.653 -28.976 14.516  1.00 39.78 ?  103 GLY   B C    1 
ATOM   5653 O  O    . GLY   B 1 103 ? 36.537 -28.908 15.044  1.00 40.28 ?  103 GLY   B O    1 
ATOM   5654 H  H    A GLY   B 1 103 ? 40.076 -30.509 13.756  0.62 47.44 ?  103 GLY   B H    1 
ATOM   5655 H  H    B GLY   B 1 103 ? 40.079 -30.513 13.760  0.38 47.44 ?  103 GLY   B H    1 
ATOM   5656 H  HA2  . GLY   B 1 103 ? 38.238 -30.911 14.768  1.00 47.90 ?  103 GLY   B HA2  1 
ATOM   5657 H  HA3  . GLY   B 1 103 ? 38.684 -29.974 15.943  1.00 47.90 ?  103 GLY   B HA3  1 
ATOM   5658 N  N    . GLU   B 1 104 ? 38.038 -28.142 13.554  1.00 38.25 ?  104 GLU   B N    1 
ATOM   5659 C  CA   . GLU   B 1 104 ? 37.170 -27.066 13.099  1.00 36.71 ?  104 GLU   B CA   1 
ATOM   5660 C  C    . GLU   B 1 104 ? 35.989 -27.616 12.299  1.00 37.08 ?  104 GLU   B C    1 
ATOM   5661 O  O    . GLU   B 1 104 ? 36.030 -28.722 11.752  1.00 38.06 ?  104 GLU   B O    1 
ATOM   5662 C  CB   . GLU   B 1 104 ? 37.968 -26.061 12.268  1.00 35.80 ?  104 GLU   B CB   1 
ATOM   5663 C  CG   . GLU   B 1 104 ? 39.088 -25.418 13.070  1.00 34.78 ?  104 GLU   B CG   1 
ATOM   5664 C  CD   . GLU   B 1 104 ? 39.993 -24.506 12.259  1.00 33.70 ?  104 GLU   B CD   1 
ATOM   5665 O  OE1  . GLU   B 1 104 ? 39.996 -24.588 11.013  1.00 31.61 ?  104 GLU   B OE1  1 
ATOM   5666 O  OE2  . GLU   B 1 104 ? 40.716 -23.701 12.880  1.00 33.89 -1 104 GLU   B OE2  1 
ATOM   5667 H  H    . GLU   B 1 104 ? 38.800 -28.169 13.159  1.00 45.92 ?  104 GLU   B H    1 
ATOM   5668 H  HA   . GLU   B 1 104 ? 36.819 -26.601 13.874  1.00 44.07 ?  104 GLU   B HA   1 
ATOM   5669 H  HB2  . GLU   B 1 104 ? 38.358 -26.520 11.509  1.00 42.98 ?  104 GLU   B HB2  1 
ATOM   5670 H  HB3  . GLU   B 1 104 ? 37.368 -25.360 11.963  1.00 42.98 ?  104 GLU   B HB3  1 
ATOM   5671 H  HG2  . GLU   B 1 104 ? 38.694 -24.895 13.786  1.00 41.76 ?  104 GLU   B HG2  1 
ATOM   5672 H  HG3  . GLU   B 1 104 ? 39.645 -26.118 13.442  1.00 41.76 ?  104 GLU   B HG3  1 
ATOM   5673 N  N    . ASP   B 1 105 ? 34.925 -26.815 12.237  1.00 35.75 ?  105 ASP   B N    1 
ATOM   5674 C  CA   . ASP   B 1 105 ? 33.651 -27.262 11.688  1.00 35.64 ?  105 ASP   B CA   1 
ATOM   5675 C  C    . ASP   B 1 105 ? 33.718 -27.301 10.167  1.00 32.79 ?  105 ASP   B C    1 
ATOM   5676 O  O    . ASP   B 1 105 ? 33.894 -26.262 9.520   1.00 32.01 ?  105 ASP   B O    1 
ATOM   5677 C  CB   . ASP   B 1 105 ? 32.533 -26.321 12.132  1.00 38.98 ?  105 ASP   B CB   1 
ATOM   5678 C  CG   . ASP   B 1 105 ? 31.164 -26.801 11.704  1.00 41.90 ?  105 ASP   B CG   1 
ATOM   5679 O  OD1  . ASP   B 1 105 ? 31.073 -27.907 11.133  1.00 42.12 ?  105 ASP   B OD1  1 
ATOM   5680 O  OD2  . ASP   B 1 105 ? 30.175 -26.073 11.939  1.00 43.65 -1 105 ASP   B OD2  1 
ATOM   5681 H  H    . ASP   B 1 105 ? 34.917 -25.999 12.507  1.00 42.92 ?  105 ASP   B H    1 
ATOM   5682 H  HA   . ASP   B 1 105 ? 33.449 -28.156 12.011  1.00 42.79 ?  105 ASP   B HA   1 
ATOM   5683 H  HB2  . ASP   B 1 105 ? 32.545 -26.246 13.098  1.00 46.80 ?  105 ASP   B HB2  1 
ATOM   5684 H  HB3  . ASP   B 1 105 ? 32.671 -25.451 11.727  1.00 46.80 ?  105 ASP   B HB3  1 
ATOM   5685 N  N    A ILE   B 1 106 ? 33.550 -28.498 9.599   0.62 32.03 ?  106 ILE   B N    1 
ATOM   5686 N  N    B ILE   B 1 106 ? 33.558 -28.498 9.598   0.38 32.62 ?  106 ILE   B N    1 
ATOM   5687 C  CA   A ILE   B 1 106 ? 33.534 -28.666 8.151   0.62 30.83 ?  106 ILE   B CA   1 
ATOM   5688 C  CA   B ILE   B 1 106 ? 33.583 -28.658 8.150   0.38 32.21 ?  106 ILE   B CA   1 
ATOM   5689 C  C    A ILE   B 1 106 ? 32.451 -27.820 7.492   0.62 28.95 ?  106 ILE   B C    1 
ATOM   5690 C  C    B ILE   B 1 106 ? 32.484 -27.847 7.477   0.38 31.16 ?  106 ILE   B C    1 
ATOM   5691 O  O    A ILE   B 1 106 ? 32.552 -27.502 6.304   0.62 27.86 ?  106 ILE   B O    1 
ATOM   5692 O  O    B ILE   B 1 106 ? 32.558 -27.581 6.273   0.38 31.01 ?  106 ILE   B O    1 
ATOM   5693 C  CB   A ILE   B 1 106 ? 33.391 -30.169 7.809   0.62 31.43 ?  106 ILE   B CB   1 
ATOM   5694 C  CB   B ILE   B 1 106 ? 33.500 -30.161 7.793   0.38 32.72 ?  106 ILE   B CB   1 
ATOM   5695 C  CG1  A ILE   B 1 106 ? 33.600 -30.420 6.313   0.62 31.57 ?  106 ILE   B CG1  1 
ATOM   5696 C  CG1  B ILE   B 1 106 ? 33.766 -30.387 6.303   0.38 32.73 ?  106 ILE   B CG1  1 
ATOM   5697 C  CG2  A ILE   B 1 106 ? 32.028 -30.692 8.251   0.62 32.24 ?  106 ILE   B CG2  1 
ATOM   5698 C  CG2  B ILE   B 1 106 ? 32.142 -30.730 8.184   0.38 33.28 ?  106 ILE   B CG2  1 
ATOM   5699 C  CD1  A ILE   B 1 106 ? 34.956 -29.994 5.814   0.62 31.39 ?  106 ILE   B CD1  1 
ATOM   5700 C  CD1  B ILE   B 1 106 ? 35.100 -29.851 5.837   0.38 32.64 ?  106 ILE   B CD1  1 
ATOM   5701 H  H    A ILE   B 1 106 ? 33.445 -29.231 10.035  0.62 38.46 ?  106 ILE   B H    1 
ATOM   5702 H  H    B ILE   B 1 106 ? 33.433 -29.230 10.029  0.38 39.16 ?  106 ILE   B H    1 
ATOM   5703 H  HA   A ILE   B 1 106 ? 34.383 -28.366 7.800   0.62 37.02 ?  106 ILE   B HA   1 
ATOM   5704 H  HA   B ILE   B 1 106 ? 34.429 -28.322 7.827   0.38 38.67 ?  106 ILE   B HA   1 
ATOM   5705 H  HB   A ILE   B 1 106 ? 34.071 -30.661 8.295   0.62 37.73 ?  106 ILE   B HB   1 
ATOM   5706 H  HB   B ILE   B 1 106 ? 34.180 -30.632 8.296   0.38 39.28 ?  106 ILE   B HB   1 
ATOM   5707 H  HG12 A ILE   B 1 106 ? 33.510 -31.372 6.138   0.62 37.90 ?  106 ILE   B HG12 1 
ATOM   5708 H  HG12 B ILE   B 1 106 ? 33.756 -31.343 6.125   0.38 39.30 ?  106 ILE   B HG12 1 
ATOM   5709 H  HG13 A ILE   B 1 106 ? 32.931 -29.932 5.811   0.62 37.90 ?  106 ILE   B HG13 1 
ATOM   5710 H  HG13 B ILE   B 1 106 ? 33.072 -29.951 5.787   0.38 39.30 ?  106 ILE   B HG13 1 
ATOM   5711 H  HG21 A ILE   B 1 106 ? 32.011 -31.657 8.151   0.62 38.70 ?  106 ILE   B HG21 1 
ATOM   5712 H  HG21 B ILE   B 1 106 ? 32.161 -31.694 8.076   0.38 39.96 ?  106 ILE   B HG21 1 
ATOM   5713 H  HG22 A ILE   B 1 106 ? 31.886 -30.455 9.181   0.62 38.70 ?  106 ILE   B HG22 1 
ATOM   5714 H  HG22 B ILE   B 1 106 ? 31.962 -30.506 9.111   0.38 39.96 ?  106 ILE   B HG22 1 
ATOM   5715 H  HG23 A ILE   B 1 106 ? 31.339 -30.291 7.698   0.62 38.70 ?  106 ILE   B HG23 1 
ATOM   5716 H  HG23 B ILE   B 1 106 ? 31.459 -30.346 7.613   0.38 39.96 ?  106 ILE   B HG23 1 
ATOM   5717 H  HD11 A ILE   B 1 106 ? 35.111 -30.392 4.944   0.62 37.69 ?  106 ILE   B HD11 1 
ATOM   5718 H  HD11 B ILE   B 1 106 ? 35.318 -30.250 4.983   0.38 39.18 ?  106 ILE   B HD11 1 
ATOM   5719 H  HD12 A ILE   B 1 106 ? 34.977 -29.026 5.743   0.62 37.69 ?  106 ILE   B HD12 1 
ATOM   5720 H  HD12 B ILE   B 1 106 ? 35.037 -28.887 5.746   0.38 39.18 ?  106 ILE   B HD12 1 
ATOM   5721 H  HD13 A ILE   B 1 106 ? 35.632 -30.295 6.441   0.62 37.69 ?  106 ILE   B HD13 1 
ATOM   5722 H  HD13 B ILE   B 1 106 ? 35.777 -30.079 6.493   0.38 39.18 ?  106 ILE   B HD13 1 
ATOM   5723 N  N    A GLN   B 1 107 ? 31.414 -27.433 8.239   0.62 28.76 ?  107 GLN   B N    1 
ATOM   5724 N  N    B GLN   B 1 107 ? 31.461 -27.437 8.231   0.38 30.60 ?  107 GLN   B N    1 
ATOM   5725 C  CA   A GLN   B 1 107 ? 30.338 -26.634 7.659   0.62 28.60 ?  107 GLN   B CA   1 
ATOM   5726 C  CA   B GLN   B 1 107 ? 30.369 -26.657 7.660   0.38 29.79 ?  107 GLN   B CA   1 
ATOM   5727 C  C    A GLN   B 1 107 ? 30.823 -25.278 7.165   0.62 26.03 ?  107 GLN   B C    1 
ATOM   5728 C  C    B GLN   B 1 107 ? 30.824 -25.285 7.176   0.38 26.74 ?  107 GLN   B C    1 
ATOM   5729 O  O    A GLN   B 1 107 ? 30.172 -24.687 6.300   0.62 26.34 ?  107 GLN   B O    1 
ATOM   5730 O  O    B GLN   B 1 107 ? 30.146 -24.689 6.335   0.38 26.89 ?  107 GLN   B O    1 
ATOM   5731 C  CB   A GLN   B 1 107 ? 29.211 -26.443 8.678   0.62 32.41 ?  107 GLN   B CB   1 
ATOM   5732 C  CB   B GLN   B 1 107 ? 29.246 -26.510 8.691   0.38 32.54 ?  107 GLN   B CB   1 
ATOM   5733 C  CG   A GLN   B 1 107 ? 27.876 -25.993 8.081   0.62 35.76 ?  107 GLN   B CG   1 
ATOM   5734 C  CG   B GLN   B 1 107 ? 27.907 -26.052 8.122   0.38 34.95 ?  107 GLN   B CG   1 
ATOM   5735 C  CD   A GLN   B 1 107 ? 27.761 -24.483 7.953   0.62 38.28 ?  107 GLN   B CD   1 
ATOM   5736 C  CD   B GLN   B 1 107 ? 27.763 -24.541 8.094   0.38 36.81 ?  107 GLN   B CD   1 
ATOM   5737 O  OE1  A GLN   B 1 107 ? 28.568 -23.736 8.507   0.62 39.22 ?  107 GLN   B OE1  1 
ATOM   5738 O  OE1  B GLN   B 1 107 ? 28.565 -23.816 8.683   0.38 37.42 ?  107 GLN   B OE1  1 
ATOM   5739 N  NE2  A GLN   B 1 107 ? 26.747 -24.026 7.221   0.62 39.10 ?  107 GLN   B NE2  1 
ATOM   5740 N  NE2  B GLN   B 1 107 ? 26.731 -24.059 7.409   0.38 37.44 ?  107 GLN   B NE2  1 
ATOM   5741 H  H    A GLN   B 1 107 ? 31.311 -27.614 9.065   0.62 34.53 ?  107 GLN   B H    1 
ATOM   5742 H  H    B GLN   B 1 107 ? 31.375 -27.599 9.069   0.38 36.74 ?  107 GLN   B H    1 
ATOM   5743 H  HA   A GLN   B 1 107 ? 29.970 -27.108 6.896   0.62 34.34 ?  107 GLN   B HA   1 
ATOM   5744 H  HA   B GLN   B 1 107 ? 30.010 -27.136 6.898   0.38 35.77 ?  107 GLN   B HA   1 
ATOM   5745 H  HB2  A GLN   B 1 107 ? 29.059 -27.286 9.124   0.62 38.91 ?  107 GLN   B HB2  1 
ATOM   5746 H  HB2  B GLN   B 1 107 ? 29.104 -27.370 9.109   0.38 39.07 ?  107 GLN   B HB2  1 
ATOM   5747 H  HB3  A GLN   B 1 107 ? 29.486 -25.774 9.324   0.62 38.91 ?  107 GLN   B HB3  1 
ATOM   5748 H  HB3  B GLN   B 1 107 ? 29.521 -25.864 9.360   0.38 39.07 ?  107 GLN   B HB3  1 
ATOM   5749 H  HG2  A GLN   B 1 107 ? 27.778 -26.373 7.194   0.62 42.93 ?  107 GLN   B HG2  1 
ATOM   5750 H  HG2  B GLN   B 1 107 ? 27.819 -26.376 7.213   0.38 41.96 ?  107 GLN   B HG2  1 
ATOM   5751 H  HG3  A GLN   B 1 107 ? 27.154 -26.303 8.653   0.62 42.93 ?  107 GLN   B HG3  1 
ATOM   5752 H  HG3  B GLN   B 1 107 ? 27.191 -26.413 8.672   0.38 41.96 ?  107 GLN   B HG3  1 
ATOM   5753 H  HE21 A GLN   B 1 107 ? 26.201 -24.576 6.846   0.62 46.94 ?  107 GLN   B HE21 1 
ATOM   5754 H  HE21 B GLN   B 1 107 ? 26.191 -24.597 7.009   0.38 44.95 ?  107 GLN   B HE21 1 
ATOM   5755 H  HE22 A GLN   B 1 107 ? 26.636 -23.178 7.121   0.62 46.94 ?  107 GLN   B HE22 1 
ATOM   5756 H  HE22 B GLN   B 1 107 ? 26.604 -23.210 7.366   0.38 44.95 ?  107 GLN   B HE22 1 
ATOM   5757 N  N    . LEU   B 1 108 ? 31.953 -24.776 7.678   1.00 23.76 ?  108 LEU   B N    1 
ATOM   5758 C  CA   . LEU   B 1 108 ? 32.484 -23.477 7.253   1.00 20.14 ?  108 LEU   B CA   1 
ATOM   5759 C  C    . LEU   B 1 108 ? 33.128 -23.514 5.875   1.00 17.50 ?  108 LEU   B C    1 
ATOM   5760 O  O    . LEU   B 1 108 ? 33.554 -22.466 5.374   1.00 16.30 ?  108 LEU   B O    1 
ATOM   5761 C  CB   . LEU   B 1 108 ? 33.471 -22.943 8.291   1.00 21.00 ?  108 LEU   B CB   1 
ATOM   5762 C  CG   . LEU   B 1 108 ? 32.842 -22.383 9.569   1.00 22.68 ?  108 LEU   B CG   1 
ATOM   5763 C  CD1  . LEU   B 1 108 ? 33.837 -22.411 10.712  1.00 23.45 ?  108 LEU   B CD1  1 
ATOM   5764 C  CD2  . LEU   B 1 108 ? 32.362 -20.959 9.333   1.00 23.42 ?  108 LEU   B CD2  1 
ATOM   5765 H  H    A LEU   B 1 108 ? 32.420 -25.167 8.282   0.62 28.53 ?  108 LEU   B H    1 
ATOM   5766 H  H    B LEU   B 1 108 ? 32.424 -25.164 8.280   0.38 28.53 ?  108 LEU   B H    1 
ATOM   5767 H  HA   . LEU   B 1 108 ? 31.748 -22.853 7.208   1.00 24.19 ?  108 LEU   B HA   1 
ATOM   5768 H  HB2  . LEU   B 1 108 ? 34.061 -23.663 8.557   1.00 25.22 ?  108 LEU   B HB2  1 
ATOM   5769 H  HB3  . LEU   B 1 108 ? 33.984 -22.229 7.889   1.00 25.22 ?  108 LEU   B HB3  1 
ATOM   5770 H  HG   . LEU   B 1 108 ? 32.075 -22.923 9.820   1.00 27.24 ?  108 LEU   B HG   1 
ATOM   5771 H  HD11 . LEU   B 1 108 ? 33.405 -22.080 11.516  1.00 28.16 ?  108 LEU   B HD11 1 
ATOM   5772 H  HD12 . LEU   B 1 108 ? 34.133 -23.324 10.849  1.00 28.16 ?  108 LEU   B HD12 1 
ATOM   5773 H  HD13 . LEU   B 1 108 ? 34.592 -21.847 10.487  1.00 28.16 ?  108 LEU   B HD13 1 
ATOM   5774 H  HD21 . LEU   B 1 108 ? 31.957 -20.621 10.147  1.00 28.13 ?  108 LEU   B HD21 1 
ATOM   5775 H  HD22 . LEU   B 1 108 ? 33.122 -20.407 9.088   1.00 28.13 ?  108 LEU   B HD22 1 
ATOM   5776 H  HD23 . LEU   B 1 108 ? 31.709 -20.961 8.616   1.00 28.13 ?  108 LEU   B HD23 1 
ATOM   5777 N  N    . LEU   B 1 109 ? 33.187 -24.685 5.250   1.00 15.95 ?  109 LEU   B N    1 
ATOM   5778 C  CA   . LEU   B 1 109 ? 33.811 -24.802 3.938   1.00 15.11 ?  109 LEU   B CA   1 
ATOM   5779 C  C    . LEU   B 1 109 ? 33.035 -24.033 2.874   1.00 14.50 ?  109 LEU   B C    1 
ATOM   5780 O  O    . LEU   B 1 109 ? 33.643 -23.449 1.966   1.00 14.17 ?  109 LEU   B O    1 
ATOM   5781 C  CB   . LEU   B 1 109 ? 33.935 -26.282 3.579   1.00 15.67 ?  109 LEU   B CB   1 
ATOM   5782 C  CG   . LEU   B 1 109 ? 34.697 -26.638 2.307   1.00 14.96 ?  109 LEU   B CG   1 
ATOM   5783 C  CD1  . LEU   B 1 109 ? 36.071 -25.982 2.299   1.00 14.61 ?  109 LEU   B CD1  1 
ATOM   5784 C  CD2  . LEU   B 1 109 ? 34.828 -28.158 2.162   1.00 15.59 ?  109 LEU   B CD2  1 
ATOM   5785 H  H    . LEU   B 1 109 ? 32.896 -25.426 5.565   1.00 19.16 ?  109 LEU   B H    1 
ATOM   5786 H  HA   . LEU   B 1 109 ? 34.710 -24.434 3.979   1.00 18.15 ?  109 LEU   B HA   1 
ATOM   5787 H  HB2  . LEU   B 1 109 ? 34.387 -26.740 4.307   1.00 18.83 ?  109 LEU   B HB2  1 
ATOM   5788 H  HB3  . LEU   B 1 109 ? 33.043 -26.650 3.483   1.00 18.83 ?  109 LEU   B HB3  1 
ATOM   5789 H  HG   . LEU   B 1 109 ? 34.202 -26.323 1.534   1.00 17.97 ?  109 LEU   B HG   1 
ATOM   5790 H  HD11 . LEU   B 1 109 ? 36.599 -26.359 1.577   1.00 17.55 ?  109 LEU   B HD11 1 
ATOM   5791 H  HD12 . LEU   B 1 109 ? 35.960 -25.033 2.171   1.00 17.55 ?  109 LEU   B HD12 1 
ATOM   5792 H  HD13 . LEU   B 1 109 ? 36.505 -26.161 3.150   1.00 17.55 ?  109 LEU   B HD13 1 
ATOM   5793 H  HD21 . LEU   B 1 109 ? 35.394 -28.360 1.395   1.00 18.73 ?  109 LEU   B HD21 1 
ATOM   5794 H  HD22 . LEU   B 1 109 ? 35.228 -28.522 2.966   1.00 18.73 ?  109 LEU   B HD22 1 
ATOM   5795 H  HD23 . LEU   B 1 109 ? 33.948 -28.548 2.026   1.00 18.73 ?  109 LEU   B HD23 1 
ATOM   5796 N  N    . LYS   B 1 110 ? 31.701 -24.006 2.964   1.00 14.23 ?  110 LYS   B N    1 
ATOM   5797 C  CA   . LYS   B 1 110 ? 30.939 -23.251 1.975   1.00 13.99 ?  110 LYS   B CA   1 
ATOM   5798 C  C    . LYS   B 1 110 ? 31.276 -21.764 2.055   1.00 13.83 ?  110 LYS   B C    1 
ATOM   5799 O  O    . LYS   B 1 110 ? 31.526 -21.116 1.032   1.00 13.75 ?  110 LYS   B O    1 
ATOM   5800 C  CB   . LYS   B 1 110 ? 29.435 -23.497 2.136   1.00 14.62 ?  110 LYS   B CB   1 
ATOM   5801 C  CG   . LYS   B 1 110 ? 28.621 -22.871 0.998   1.00 15.04 ?  110 LYS   B CG   1 
ATOM   5802 C  CD   . LYS   B 1 110 ? 27.158 -23.313 1.014   1.00 15.53 ?  110 LYS   B CD   1 
ATOM   5803 C  CE   . LYS   B 1 110 ? 26.399 -22.778 -0.197  1.00 16.38 ?  110 LYS   B CE   1 
ATOM   5804 N  NZ   . LYS   B 1 110 ? 26.709 -23.512 -1.453  1.00 16.92 ?  110 LYS   B NZ   1 
ATOM   5805 H  H    . LYS   B 1 110 ? 31.236 -24.403 3.571   1.00 17.09 ?  110 LYS   B H    1 
ATOM   5806 H  HA   . LYS   B 1 110 ? 31.194 -23.560 1.095   1.00 16.81 ?  110 LYS   B HA   1 
ATOM   5807 H  HB2  . LYS   B 1 110 ? 29.270 -24.454 2.139   1.00 17.57 ?  110 LYS   B HB2  1 
ATOM   5808 H  HB3  . LYS   B 1 110 ? 29.137 -23.107 2.974   1.00 17.57 ?  110 LYS   B HB3  1 
ATOM   5809 H  HG2  . LYS   B 1 110 ? 28.640 -21.907 1.087   1.00 18.06 ?  110 LYS   B HG2  1 
ATOM   5810 H  HG3  . LYS   B 1 110 ? 29.004 -23.139 0.151   1.00 18.06 ?  110 LYS   B HG3  1 
ATOM   5811 H  HD2  . LYS   B 1 110 ? 27.118 -24.286 0.998   1.00 18.66 ?  110 LYS   B HD2  1 
ATOM   5812 H  HD3  . LYS   B 1 110 ? 26.730 -22.978 1.819   1.00 18.66 ?  110 LYS   B HD3  1 
ATOM   5813 H  HE2  . LYS   B 1 110 ? 25.449 -22.854 -0.033  1.00 19.67 ?  110 LYS   B HE2  1 
ATOM   5814 H  HE3  . LYS   B 1 110 ? 26.641 -21.847 -0.330  1.00 19.67 ?  110 LYS   B HE3  1 
ATOM   5815 H  HZ1  . LYS   B 1 110 ? 26.251 -23.167 -2.130  1.00 20.33 ?  110 LYS   B HZ1  1 
ATOM   5816 H  HZ2  . LYS   B 1 110 ? 27.581 -23.454 -1.633  1.00 20.33 ?  110 LYS   B HZ2  1 
ATOM   5817 H  HZ3  . LYS   B 1 110 ? 26.494 -24.372 -1.363  1.00 20.33 ?  110 LYS   B HZ3  1 
ATOM   5818 N  N    . SER   B 1 111 ? 31.294 -21.208 3.271   1.00 14.14 ?  111 SER   B N    1 
ATOM   5819 C  CA   . SER   B 1 111 ? 31.687 -19.809 3.435   1.00 13.92 ?  111 SER   B CA   1 
ATOM   5820 C  C    . SER   B 1 111 ? 33.062 -19.556 2.831   1.00 13.49 ?  111 SER   B C    1 
ATOM   5821 O  O    . SER   B 1 111 ? 33.286 -18.528 2.174   1.00 13.65 ?  111 SER   B O    1 
ATOM   5822 C  CB   . SER   B 1 111 ? 31.704 -19.443 4.916   1.00 14.83 ?  111 SER   B CB   1 
ATOM   5823 O  OG   . SER   B 1 111 ? 30.410 -19.446 5.470   1.00 16.18 ?  111 SER   B OG   1 
ATOM   5824 H  H    . SER   B 1 111 ? 31.101 -21.618 4.005   1.00 16.99 ?  111 SER   B H    1 
ATOM   5825 H  HA   . SER   B 1 111 ? 31.047 -19.243 2.984   1.00 16.73 ?  111 SER   B HA   1 
ATOM   5826 H  HB2  . SER   B 1 111 ? 32.241 -20.092 5.397   1.00 17.81 ?  111 SER   B HB2  1 
ATOM   5827 H  HB3  . SER   B 1 111 ? 32.084 -18.559 5.017   1.00 17.81 ?  111 SER   B HB3  1 
ATOM   5828 H  HG   . SER   B 1 111 ? 30.441 -19.233 6.292   1.00 19.43 ?  111 SER   B HG   1 
ATOM   5829 N  N    . ALA   B 1 112 ? 34.004 -20.474 3.057   1.00 13.38 ?  112 ALA   B N    1 
ATOM   5830 C  CA   . ALA   B 1 112 ? 35.345 -20.302 2.512   1.00 13.14 ?  112 ALA   B CA   1 
ATOM   5831 C  C    . ALA   B 1 112 ? 35.314 -20.213 0.987   1.00 12.68 ?  112 ALA   B C    1 
ATOM   5832 O  O    . ALA   B 1 112 ? 35.934 -19.322 0.390   1.00 13.23 ?  112 ALA   B O    1 
ATOM   5833 C  CB   . ALA   B 1 112 ? 36.251 -21.438 2.999   1.00 13.56 ?  112 ALA   B CB   1 
ATOM   5834 H  H    . ALA   B 1 112 ? 33.890 -21.196 3.523   1.00 16.08 ?  112 ALA   B H    1 
ATOM   5835 H  HA   . ALA   B 1 112 ? 35.708 -19.471 2.852   1.00 15.79 ?  112 ALA   B HA   1 
ATOM   5836 H  HB1  . ALA   B 1 112 ? 37.143 -21.303 2.635   1.00 16.30 ?  112 ALA   B HB1  1 
ATOM   5837 H  HB2  . ALA   B 1 112 ? 36.293 -21.414 3.973   1.00 16.30 ?  112 ALA   B HB2  1 
ATOM   5838 H  HB3  . ALA   B 1 112 ? 35.893 -22.283 2.704   1.00 16.30 ?  112 ALA   B HB3  1 
ATOM   5839 N  N    . TYR   B 1 113 ? 34.574 -21.115 0.334   1.00 12.46 ?  113 TYR   B N    1 
ATOM   5840 C  CA   . TYR   B 1 113 ? 34.503 -21.073 -1.120  1.00 12.47 ?  113 TYR   B CA   1 
ATOM   5841 C  C    . TYR   B 1 113 ? 33.795 -19.825 -1.641  1.00 12.11 ?  113 TYR   B C    1 
ATOM   5842 O  O    . TYR   B 1 113 ? 34.066 -19.400 -2.769  1.00 12.13 ?  113 TYR   B O    1 
ATOM   5843 C  CB   . TYR   B 1 113 ? 33.833 -22.334 -1.660  1.00 12.45 ?  113 TYR   B CB   1 
ATOM   5844 C  CG   . TYR   B 1 113 ? 34.789 -23.483 -1.905  1.00 12.88 ?  113 TYR   B CG   1 
ATOM   5845 C  CD1  . TYR   B 1 113 ? 35.780 -23.392 -2.876  1.00 13.44 ?  113 TYR   B CD1  1 
ATOM   5846 C  CD2  . TYR   B 1 113 ? 34.694 -24.660 -1.182  1.00 13.27 ?  113 TYR   B CD2  1 
ATOM   5847 C  CE1  . TYR   B 1 113 ? 36.660 -24.428 -3.117  1.00 13.56 ?  113 TYR   B CE1  1 
ATOM   5848 C  CE2  . TYR   B 1 113 ? 35.573 -25.718 -1.416  1.00 13.63 ?  113 TYR   B CE2  1 
ATOM   5849 C  CZ   . TYR   B 1 113 ? 36.545 -25.594 -2.391  1.00 13.17 ?  113 TYR   B CZ   1 
ATOM   5850 O  OH   . TYR   B 1 113 ? 37.431 -26.609 -2.664  1.00 14.33 ?  113 TYR   B OH   1 
ATOM   5851 H  H    . TYR   B 1 113 ? 34.102 -21.738 0.712   1.00 14.97 ?  113 TYR   B H    1 
ATOM   5852 H  HA   . TYR   B 1 113 ? 35.407 -21.055 -1.454  1.00 14.98 ?  113 TYR   B HA   1 
ATOM   5853 H  HB2  . TYR   B 1 113 ? 33.171 -22.643 -1.021  1.00 14.96 ?  113 TYR   B HB2  1 
ATOM   5854 H  HB3  . TYR   B 1 113 ? 33.405 -22.124 -2.502  1.00 14.96 ?  113 TYR   B HB3  1 
ATOM   5855 H  HD1  . TYR   B 1 113 ? 35.860 -22.609 -3.373  1.00 16.15 ?  113 TYR   B HD1  1 
ATOM   5856 H  HD2  . TYR   B 1 113 ? 34.036 -24.741 -0.535  1.00 15.95 ?  113 TYR   B HD2  1 
ATOM   5857 H  HE1  . TYR   B 1 113 ? 37.317 -24.350 -3.773  1.00 16.29 ?  113 TYR   B HE1  1 
ATOM   5858 H  HE2  . TYR   B 1 113 ? 35.497 -26.506 -0.928  1.00 16.38 ?  113 TYR   B HE2  1 
ATOM   5859 H  HH   . TYR   B 1 113 ? 37.269 -27.269 -2.172  1.00 17.21 ?  113 TYR   B HH   1 
ATOM   5860 N  N    . GLU   B 1 114 ? 32.868 -19.253 -0.864  1.00 12.47 ?  114 GLU   B N    1 
ATOM   5861 C  CA   . GLU   B 1 114 ? 32.182 -18.043 -1.317  1.00 12.42 ?  114 GLU   B CA   1 
ATOM   5862 C  C    . GLU   B 1 114 ? 33.167 -16.922 -1.622  1.00 12.15 ?  114 GLU   B C    1 
ATOM   5863 O  O    . GLU   B 1 114 ? 32.891 -16.068 -2.468  1.00 12.55 ?  114 GLU   B O    1 
ATOM   5864 C  CB   . GLU   B 1 114 ? 31.125 -17.611 -0.294  1.00 12.63 ?  114 GLU   B CB   1 
ATOM   5865 C  CG   . GLU   B 1 114 ? 29.907 -18.537 -0.357  1.00 13.14 ?  114 GLU   B CG   1 
ATOM   5866 C  CD   . GLU   B 1 114 ? 28.883 -18.346 0.748   1.00 13.56 ?  114 GLU   B CD   1 
ATOM   5867 O  OE1  . GLU   B 1 114 ? 29.177 -17.735 1.792   1.00 13.53 ?  114 GLU   B OE1  1 
ATOM   5868 O  OE2  . GLU   B 1 114 ? 27.761 -18.881 0.578   1.00 14.75 -1 114 GLU   B OE2  1 
ATOM   5869 H  H    . GLU   B 1 114 ? 32.612 -19.553 -0.090  1.00 14.98 ?  114 GLU   B H    1 
ATOM   5870 H  HA   . GLU   B 1 114 ? 31.713 -18.253 -2.135  1.00 14.92 ?  114 GLU   B HA   1 
ATOM   5871 H  HB2  . GLU   B 1 114 ? 31.497 -17.660 0.604   1.00 15.18 ?  114 GLU   B HB2  1 
ATOM   5872 H  HB3  . GLU   B 1 114 ? 30.833 -16.710 -0.490  1.00 15.18 ?  114 GLU   B HB3  1 
ATOM   5873 H  HG2  . GLU   B 1 114 ? 29.459 -18.390 -1.200  1.00 15.79 ?  114 GLU   B HG2  1 
ATOM   5874 H  HG3  . GLU   B 1 114 ? 30.220 -19.454 -0.306  1.00 15.79 ?  114 GLU   B HG3  1 
ATOM   5875 N  N    . ASN   B 1 115 ? 34.336 -16.918 -0.978  1.00 12.09 ?  115 ASN   B N    1 
ATOM   5876 C  CA   . ASN   B 1 115 ? 35.327 -15.883 -1.279  1.00 11.69 ?  115 ASN   B CA   1 
ATOM   5877 C  C    . ASN   B 1 115 ? 35.744 -15.910 -2.744  1.00 11.75 ?  115 ASN   B C    1 
ATOM   5878 O  O    . ASN   B 1 115 ? 36.124 -14.870 -3.306  1.00 12.21 ?  115 ASN   B O    1 
ATOM   5879 C  CB   . ASN   B 1 115 ? 36.566 -16.051 -0.391  1.00 12.72 ?  115 ASN   B CB   1 
ATOM   5880 C  CG   . ASN   B 1 115 ? 36.293 -15.782 1.070   1.00 12.78 ?  115 ASN   B CG   1 
ATOM   5881 O  OD1  . ASN   B 1 115 ? 36.277 -14.631 1.506   1.00 14.87 ?  115 ASN   B OD1  1 
ATOM   5882 N  ND2  . ASN   B 1 115 ? 36.126 -16.848 1.853   1.00 12.93 ?  115 ASN   B ND2  1 
ATOM   5883 H  H    . ASN   B 1 115 ? 34.576 -17.483 -0.370  1.00 14.53 ?  115 ASN   B H    1 
ATOM   5884 H  HA   . ASN   B 1 115 ? 34.939 -15.014 -1.091  1.00 14.05 ?  115 ASN   B HA   1 
ATOM   5885 H  HB2  . ASN   B 1 115 ? 36.894 -16.957 -0.478  1.00 15.28 ?  115 ASN   B HB2  1 
ATOM   5886 H  HB3  . ASN   B 1 115 ? 37.245 -15.423 -0.684  1.00 15.28 ?  115 ASN   B HB3  1 
ATOM   5887 H  HD21 . ASN   B 1 115 ? 35.986 -16.746 2.696   1.00 15.54 ?  115 ASN   B HD21 1 
ATOM   5888 H  HD22 . ASN   B 1 115 ? 36.162 -17.639 1.518   1.00 15.54 ?  115 ASN   B HD22 1 
ATOM   5889 N  N    . PHE   B 1 116 ? 35.709 -17.086 -3.375  1.00 11.58 ?  116 PHE   B N    1 
ATOM   5890 C  CA   . PHE   B 1 116 ? 36.137 -17.179 -4.765  1.00 11.80 ?  116 PHE   B CA   1 
ATOM   5891 C  C    . PHE   B 1 116 ? 35.236 -16.358 -5.678  1.00 11.50 ?  116 PHE   B C    1 
ATOM   5892 O  O    . PHE   B 1 116 ? 35.667 -15.928 -6.755  1.00 12.39 ?  116 PHE   B O    1 
ATOM   5893 C  CB   . PHE   B 1 116 ? 36.098 -18.625 -5.284  1.00 11.52 ?  116 PHE   B CB   1 
ATOM   5894 C  CG   . PHE   B 1 116 ? 37.168 -19.587 -4.731  1.00 11.42 ?  116 PHE   B CG   1 
ATOM   5895 C  CD1  . PHE   B 1 116 ? 37.813 -19.400 -3.518  1.00 12.17 ?  116 PHE   B CD1  1 
ATOM   5896 C  CD2  . PHE   B 1 116 ? 37.474 -20.727 -5.464  1.00 11.82 ?  116 PHE   B CD2  1 
ATOM   5897 C  CE1  . PHE   B 1 116 ? 38.739 -20.337 -3.059  1.00 12.29 ?  116 PHE   B CE1  1 
ATOM   5898 C  CE2  . PHE   B 1 116 ? 38.401 -21.655 -5.013  1.00 12.00 ?  116 PHE   B CE2  1 
ATOM   5899 C  CZ   . PHE   B 1 116 ? 39.022 -21.467 -3.811  1.00 11.85 ?  116 PHE   B CZ   1 
ATOM   5900 H  H    . PHE   B 1 116 ? 35.441 -17.830 -3.029  1.00 13.92 ?  116 PHE   B H    1 
ATOM   5901 H  HA   . PHE   B 1 116 ? 37.043 -16.851 -4.846  1.00 14.18 ?  116 PHE   B HA   1 
ATOM   5902 H  HB2  . PHE   B 1 116 ? 35.222 -18.999 -5.064  1.00 13.84 ?  116 PHE   B HB2  1 
ATOM   5903 H  HB3  . PHE   B 1 116 ? 36.196 -18.604 -6.247  1.00 13.84 ?  116 PHE   B HB3  1 
ATOM   5904 H  HD1  . PHE   B 1 116 ? 37.607 -18.656 -2.997  1.00 14.62 ?  116 PHE   B HD1  1 
ATOM   5905 H  HD2  . PHE   B 1 116 ? 37.037 -20.871 -6.277  1.00 14.20 ?  116 PHE   B HD2  1 
ATOM   5906 H  HE1  . PHE   B 1 116 ? 39.167 -20.204 -2.245  1.00 14.77 ?  116 PHE   B HE1  1 
ATOM   5907 H  HE2  . PHE   B 1 116 ? 38.590 -22.403 -5.523  1.00 14.42 ?  116 PHE   B HE2  1 
ATOM   5908 H  HZ   . PHE   B 1 116 ? 39.656 -22.076 -3.510  1.00 14.25 ?  116 PHE   B HZ   1 
ATOM   5909 N  N    . ASN   B 1 117 ? 33.969 -16.154 -5.291  1.00 12.13 ?  117 ASN   B N    1 
ATOM   5910 C  CA   . ASN   B 1 117 ? 33.021 -15.445 -6.148  1.00 12.50 ?  117 ASN   B CA   1 
ATOM   5911 C  C    . ASN   B 1 117 ? 33.339 -13.967 -6.295  1.00 12.89 ?  117 ASN   B C    1 
ATOM   5912 O  O    . ASN   B 1 117 ? 32.729 -13.304 -7.137  1.00 13.95 ?  117 ASN   B O    1 
ATOM   5913 C  CB   . ASN   B 1 117 ? 31.598 -15.668 -5.649  1.00 12.75 ?  117 ASN   B CB   1 
ATOM   5914 C  CG   . ASN   B 1 117 ? 31.147 -17.080 -5.899  1.00 13.11 ?  117 ASN   B CG   1 
ATOM   5915 O  OD1  . ASN   B 1 117 ? 31.494 -17.664 -6.923  1.00 13.97 ?  117 ASN   B OD1  1 
ATOM   5916 N  ND2  . ASN   B 1 117 ? 30.406 -17.656 -4.962  1.00 13.02 ?  117 ASN   B ND2  1 
ATOM   5917 H  H    . ASN   B 1 117 ? 33.645 -16.408 -4.533  1.00 14.58 ?  117 ASN   B H    1 
ATOM   5918 H  HA   . ASN   B 1 117 ? 33.074 -15.839 -7.026  1.00 15.02 ?  117 ASN   B HA   1 
ATOM   5919 H  HB2  . ASN   B 1 117 ? 31.554 -15.501 -4.691  1.00 15.32 ?  117 ASN   B HB2  1 
ATOM   5920 H  HB3  . ASN   B 1 117 ? 30.994 -15.065 -6.116  1.00 15.32 ?  117 ASN   B HB3  1 
ATOM   5921 H  HD21 . ASN   B 1 117 ? 30.128 -18.464 -5.068  1.00 15.65 ?  117 ASN   B HD21 1 
ATOM   5922 H  HD22 . ASN   B 1 117 ? 30.185 -17.218 -4.253  1.00 15.65 ?  117 ASN   B HD22 1 
ATOM   5923 N  N    . GLN   B 1 118 ? 34.281 -13.448 -5.523  1.00 12.45 ?  118 GLN   B N    1 
ATOM   5924 C  CA   . GLN   B 1 118 ? 34.708 -12.062 -5.657  1.00 13.47 ?  118 GLN   B CA   1 
ATOM   5925 C  C    . GLN   B 1 118 ? 35.772 -11.864 -6.731  1.00 13.45 ?  118 GLN   B C    1 
ATOM   5926 O  O    . GLN   B 1 118 ? 36.251 -10.737 -6.901  1.00 14.94 ?  118 GLN   B O    1 
ATOM   5927 C  CB   . GLN   B 1 118 ? 35.179 -11.532 -4.298  1.00 13.94 ?  118 GLN   B CB   1 
ATOM   5928 C  CG   . GLN   B 1 118 ? 34.088 -11.566 -3.235  1.00 14.32 ?  118 GLN   B CG   1 
ATOM   5929 C  CD   . GLN   B 1 118 ? 32.919 -10.659 -3.575  1.00 14.12 ?  118 GLN   B CD   1 
ATOM   5930 O  OE1  . GLN   B 1 118 ? 33.107 -9.524  -4.011  1.00 14.85 ?  118 GLN   B OE1  1 
ATOM   5931 N  NE2  . GLN   B 1 118 ? 31.708 -11.160 -3.390  1.00 14.40 ?  118 GLN   B NE2  1 
ATOM   5932 H  H    . GLN   B 1 118 ? 34.708 -13.882 -4.911  1.00 14.96 ?  118 GLN   B H    1 
ATOM   5933 H  HA   . GLN   B 1 118 ? 33.945 -11.535 -5.928  1.00 16.18 ?  118 GLN   B HA   1 
ATOM   5934 H  HB2  . GLN   B 1 118 ? 35.921 -12.065 -3.984  1.00 16.74 ?  118 GLN   B HB2  1 
ATOM   5935 H  HB3  . GLN   B 1 118 ? 35.456 -10.604 -4.397  1.00 16.74 ?  118 GLN   B HB3  1 
ATOM   5936 H  HG2  . GLN   B 1 118 ? 33.754 -12.480 -3.158  1.00 17.20 ?  118 GLN   B HG2  1 
ATOM   5937 H  HG3  . GLN   B 1 118 ? 34.459 -11.283 -2.386  1.00 17.20 ?  118 GLN   B HG3  1 
ATOM   5938 H  HE21 . GLN   B 1 118 ? 31.617 -11.962 -3.082  1.00 17.30 ?  118 GLN   B HE21 1 
ATOM   5939 H  HE22 . GLN   B 1 118 ? 31.021 -10.688 -3.570  1.00 17.30 ?  118 GLN   B HE22 1 
ATOM   5940 N  N    . HIS   B 1 119 ? 36.124 -12.918 -7.473  1.00 12.64 ?  119 HIS   B N    1 
ATOM   5941 C  CA   . HIS   B 1 119 ? 37.172 -12.869 -8.485  1.00 12.89 ?  119 HIS   B CA   1 
ATOM   5942 C  C    . HIS   B 1 119 ? 36.694 -13.590 -9.731  1.00 12.97 ?  119 HIS   B C    1 
ATOM   5943 O  O    . HIS   B 1 119 ? 36.185 -14.707 -9.641  1.00 13.80 ?  119 HIS   B O    1 
ATOM   5944 C  CB   . HIS   B 1 119 ? 38.446 -13.511 -7.943  1.00 13.36 ?  119 HIS   B CB   1 
ATOM   5945 C  CG   . HIS   B 1 119 ? 38.915 -12.834 -6.705  1.00 14.24 ?  119 HIS   B CG   1 
ATOM   5946 N  ND1  . HIS   B 1 119 ? 39.711 -11.709 -6.732  1.00 15.96 ?  119 HIS   B ND1  1 
ATOM   5947 C  CD2  . HIS   B 1 119 ? 38.608 -13.051 -5.406  1.00 15.33 ?  119 HIS   B CD2  1 
ATOM   5948 C  CE1  . HIS   B 1 119 ? 39.909 -11.292 -5.494  1.00 17.14 ?  119 HIS   B CE1  1 
ATOM   5949 N  NE2  . HIS   B 1 119 ? 39.242 -12.080 -4.672  1.00 16.86 ?  119 HIS   B NE2  1 
ATOM   5950 H  H    . HIS   B 1 119 ? 35.755 -13.696 -7.407  1.00 15.19 ?  119 HIS   B H    1 
ATOM   5951 H  HA   . HIS   B 1 119 ? 37.356 -11.942 -8.715  1.00 15.49 ?  119 HIS   B HA   1 
ATOM   5952 H  HB2  . HIS   B 1 119 ? 38.272 -14.438 -7.743  1.00 16.05 ?  119 HIS   B HB2  1 
ATOM   5953 H  HB3  . HIS   B 1 119 ? 39.144 -13.435 -8.617  1.00 16.05 ?  119 HIS   B HB3  1 
ATOM   5954 H  HD2  . HIS   B 1 119 ? 38.071 -13.736 -5.076  1.00 18.41 ?  119 HIS   B HD2  1 
ATOM   5955 H  HE1  . HIS   B 1 119 ? 40.440 -10.573 -5.239  1.00 20.59 ?  119 HIS   B HE1  1 
ATOM   5956 H  HE2  . HIS   B 1 119 ? 39.239 -12.026 -3.813  1.00 20.25 ?  119 HIS   B HE2  1 
ATOM   5957 N  N    A GLU   B 1 120 ? 36.854 -12.959 -10.893 0.62 13.38 ?  120 GLU   B N    1 
ATOM   5958 N  N    B GLU   B 1 120 ? 36.859 -12.952 -10.892 0.38 14.25 ?  120 GLU   B N    1 
ATOM   5959 C  CA   A GLU   B 1 120 ? 36.269 -13.528 -12.102 0.62 15.00 ?  120 GLU   B CA   1 
ATOM   5960 C  CA   B GLU   B 1 120 ? 36.288 -13.507 -12.115 0.38 16.09 ?  120 GLU   B CA   1 
ATOM   5961 C  C    A GLU   B 1 120 ? 36.938 -14.833 -12.514 0.62 13.80 ?  120 GLU   B C    1 
ATOM   5962 C  C    B GLU   B 1 120 ? 36.937 -14.829 -12.505 0.38 14.59 ?  120 GLU   B C    1 
ATOM   5963 O  O    A GLU   B 1 120 ? 36.276 -15.699 -13.098 0.62 14.14 ?  120 GLU   B O    1 
ATOM   5964 O  O    B GLU   B 1 120 ? 36.262 -15.705 -13.057 0.38 14.73 ?  120 GLU   B O    1 
ATOM   5965 C  CB   A GLU   B 1 120 ? 36.304 -12.511 -13.241 0.62 19.62 ?  120 GLU   B CB   1 
ATOM   5966 C  CB   B GLU   B 1 120 ? 36.393 -12.495 -13.255 0.38 20.13 ?  120 GLU   B CB   1 
ATOM   5967 C  CG   A GLU   B 1 120 ? 35.280 -11.398 -13.083 0.62 25.58 ?  120 GLU   B CG   1 
ATOM   5968 C  CG   B GLU   B 1 120 ? 35.507 -11.274 -13.072 0.38 24.68 ?  120 GLU   B CG   1 
ATOM   5969 C  CD   A GLU   B 1 120 ? 35.144 -10.541 -14.322 0.62 30.63 ?  120 GLU   B CD   1 
ATOM   5970 C  CD   B GLU   B 1 120 ? 35.468 -10.397 -14.310 0.38 28.82 ?  120 GLU   B CD   1 
ATOM   5971 O  OE1  A GLU   B 1 120 ? 36.166 -10.305 -15.003 0.62 32.43 ?  120 GLU   B OE1  1 
ATOM   5972 O  OE1  B GLU   B 1 120 ? 36.434 -10.451 -15.103 0.38 30.12 ?  120 GLU   B OE1  1 
ATOM   5973 O  OE2  A GLU   B 1 120 ? 34.010 -10.109 -14.618 0.62 32.84 -1 120 GLU   B OE2  1 
ATOM   5974 O  OE2  B GLU   B 1 120 ? 34.482 -9.653  -14.488 0.38 30.21 -1 120 GLU   B OE2  1 
ATOM   5975 H  H    A GLU   B 1 120 ? 37.285 -12.219 -11.009 0.62 16.08 ?  120 GLU   B H    1 
ATOM   5976 H  H    B GLU   B 1 120 ? 37.292 -12.213 -10.998 0.38 17.11 ?  120 GLU   B H    1 
ATOM   5977 H  HA   A GLU   B 1 120 ? 35.341 -13.727 -11.926 0.62 18.02 ?  120 GLU   B HA   1 
ATOM   5978 H  HA   B GLU   B 1 120 ? 35.350 -13.679 -11.965 0.38 19.33 ?  120 GLU   B HA   1 
ATOM   5979 H  HB2  A GLU   B 1 120 ? 37.180 -12.097 -13.278 0.62 23.57 ?  120 GLU   B HB2  1 
ATOM   5980 H  HB2  B GLU   B 1 120 ? 37.308 -12.182 -13.322 0.38 24.18 ?  120 GLU   B HB2  1 
ATOM   5981 H  HB3  A GLU   B 1 120 ? 36.117 -12.963 -14.080 0.62 23.57 ?  120 GLU   B HB3  1 
ATOM   5982 H  HB3  B GLU   B 1 120 ? 36.131 -12.926 -14.086 0.38 24.18 ?  120 GLU   B HB3  1 
ATOM   5983 H  HG2  A GLU   B 1 120 ? 34.409 -11.789 -12.905 0.62 30.71 ?  120 GLU   B HG2  1 
ATOM   5984 H  HG2  B GLU   B 1 120 ? 34.604 -11.568 -12.848 0.38 29.64 ?  120 GLU   B HG2  1 
ATOM   5985 H  HG3  A GLU   B 1 120 ? 35.542 -10.824 -12.348 0.62 30.71 ?  120 GLU   B HG3  1 
ATOM   5986 H  HG3  B GLU   B 1 120 ? 35.860 -10.726 -12.357 0.38 29.64 ?  120 GLU   B HG3  1 
ATOM   5987 N  N    . VAL   B 1 121 ? 38.230 -14.991 -12.234 1.00 13.52 ?  121 VAL   B N    1 
ATOM   5988 C  CA   . VAL   B 1 121 ? 38.968 -16.199 -12.592 1.00 13.38 ?  121 VAL   B CA   1 
ATOM   5989 C  C    . VAL   B 1 121 ? 40.085 -16.415 -11.580 1.00 13.06 ?  121 VAL   B C    1 
ATOM   5990 O  O    . VAL   B 1 121 ? 40.772 -15.466 -11.184 1.00 13.33 ?  121 VAL   B O    1 
ATOM   5991 C  CB   . VAL   B 1 121 ? 39.488 -16.136 -14.047 1.00 15.77 ?  121 VAL   B CB   1 
ATOM   5992 C  CG1  . VAL   B 1 121 ? 40.351 -14.900 -14.276 1.00 17.22 ?  121 VAL   B CG1  1 
ATOM   5993 C  CG2  . VAL   B 1 121 ? 40.241 -17.409 -14.416 1.00 16.93 ?  121 VAL   B CG2  1 
ATOM   5994 H  H    A VAL   B 1 121 ? 38.714 -14.398 -11.837 0.62 16.24 ?  121 VAL   B H    1 
ATOM   5995 H  H    B VAL   B 1 121 ? 38.717 -14.398 -11.840 0.38 16.24 ?  121 VAL   B H    1 
ATOM   5996 H  HA   . VAL   B 1 121 ? 38.358 -16.951 -12.537 1.00 16.07 ?  121 VAL   B HA   1 
ATOM   5997 H  HB   . VAL   B 1 121 ? 38.723 -16.069 -14.645 1.00 18.95 ?  121 VAL   B HB   1 
ATOM   5998 H  HG11 . VAL   B 1 121 ? 40.665 -14.898 -15.194 1.00 20.69 ?  121 VAL   B HG11 1 
ATOM   5999 H  HG12 . VAL   B 1 121 ? 39.819 -14.104 -14.110 1.00 20.69 ?  121 VAL   B HG12 1 
ATOM   6000 H  HG13 . VAL   B 1 121 ? 41.106 -14.924 -13.668 1.00 20.69 ?  121 VAL   B HG13 1 
ATOM   6001 H  HG21 . VAL   B 1 121 ? 40.435 -17.397 -15.368 1.00 20.33 ?  121 VAL   B HG21 1 
ATOM   6002 H  HG22 . VAL   B 1 121 ? 41.071 -17.443 -13.914 1.00 20.33 ?  121 VAL   B HG22 1 
ATOM   6003 H  HG23 . VAL   B 1 121 ? 39.691 -18.177 -14.201 1.00 20.33 ?  121 VAL   B HG23 1 
ATOM   6004 N  N    . LEU   B 1 122 ? 40.259 -17.669 -11.155 1.00 12.31 ?  122 LEU   B N    1 
ATOM   6005 C  CA   . LEU   B 1 122 ? 41.237 -18.032 -10.135 1.00 11.82 ?  122 LEU   B CA   1 
ATOM   6006 C  C    . LEU   B 1 122 ? 41.888 -19.367 -10.463 1.00 11.38 ?  122 LEU   B C    1 
ATOM   6007 O  O    . LEU   B 1 122 ? 41.221 -20.287 -10.961 1.00 13.03 ?  122 LEU   B O    1 
ATOM   6008 C  CB   . LEU   B 1 122 ? 40.592 -18.260 -8.753  1.00 13.81 ?  122 LEU   B CB   1 
ATOM   6009 C  CG   . LEU   B 1 122 ? 39.551 -17.252 -8.269  1.00 14.00 ?  122 LEU   B CG   1 
ATOM   6010 C  CD1  . LEU   B 1 122 ? 38.156 -17.616 -8.748  1.00 14.68 ?  122 LEU   B CD1  1 
ATOM   6011 C  CD2  . LEU   B 1 122 ? 39.588 -17.158 -6.764  1.00 13.24 ?  122 LEU   B CD2  1 
ATOM   6012 H  H    . LEU   B 1 122 ? 39.806 -18.347 -11.445 1.00 14.79 ?  122 LEU   B H    1 
ATOM   6013 H  HA   . LEU   B 1 122 ? 41.917 -17.344 -10.059 1.00 14.20 ?  122 LEU   B HA   1 
ATOM   6014 H  HB2  . LEU   B 1 122 ? 40.158 -19.124 -8.762  1.00 16.59 ?  122 LEU   B HB2  1 
ATOM   6015 H  HB3  . LEU   B 1 122 ? 41.298 -18.264 -8.088  1.00 16.59 ?  122 LEU   B HB3  1 
ATOM   6016 H  HG   . LEU   B 1 122 ? 39.765 -16.375 -8.627  1.00 16.82 ?  122 LEU   B HG   1 
ATOM   6017 H  HD11 . LEU   B 1 122 ? 37.517 -16.981 -8.384  1.00 17.64 ?  122 LEU   B HD11 1 
ATOM   6018 H  HD12 . LEU   B 1 122 ? 38.132 -17.577 -9.721  1.00 17.64 ?  122 LEU   B HD12 1 
ATOM   6019 H  HD13 . LEU   B 1 122 ? 37.939 -18.510 -8.450  1.00 17.64 ?  122 LEU   B HD13 1 
ATOM   6020 H  HD21 . LEU   B 1 122 ? 38.893 -16.550 -6.464  1.00 15.91 ?  122 LEU   B HD21 1 
ATOM   6021 H  HD22 . LEU   B 1 122 ? 39.442 -18.039 -6.387  1.00 15.91 ?  122 LEU   B HD22 1 
ATOM   6022 H  HD23 . LEU   B 1 122 ? 40.458 -16.822 -6.491  1.00 15.91 ?  122 LEU   B HD23 1 
ATOM   6023 N  N    . LEU   B 1 123 ? 43.172 -19.482 -10.100 1.00 11.27 ?  123 LEU   B N    1 
ATOM   6024 C  CA   . LEU   B 1 123 ? 43.875 -20.757 -9.983  1.00 11.53 ?  123 LEU   B CA   1 
ATOM   6025 C  C    . LEU   B 1 123 ? 43.848 -21.152 -8.513  1.00 11.07 ?  123 LEU   B C    1 
ATOM   6026 O  O    . LEU   B 1 123 ? 44.201 -20.331 -7.659  1.00 11.50 ?  123 LEU   B O    1 
ATOM   6027 C  CB   . LEU   B 1 123 ? 45.325 -20.588 -10.451 1.00 12.01 ?  123 LEU   B CB   1 
ATOM   6028 C  CG   . LEU   B 1 123 ? 46.262 -21.772 -10.206 1.00 12.48 ?  123 LEU   B CG   1 
ATOM   6029 C  CD1  . LEU   B 1 123 ? 45.839 -23.020 -10.974 1.00 13.45 ?  123 LEU   B CD1  1 
ATOM   6030 C  CD2  . LEU   B 1 123 ? 47.677 -21.379 -10.582 1.00 13.66 ?  123 LEU   B CD2  1 
ATOM   6031 H  H    . LEU   B 1 123 ? 43.669 -18.804 -9.894  1.00 13.54 ?  123 LEU   B H    1 
ATOM   6032 H  HA   . LEU   B 1 123 ? 43.429 -21.436 -10.514 1.00 13.86 ?  123 LEU   B HA   1 
ATOM   6033 H  HB2  . LEU   B 1 123 ? 45.308 -20.422 -11.411 1.00 14.43 ?  123 LEU   B HB2  1 
ATOM   6034 H  HB3  . LEU   B 1 123 ? 45.698 -19.818 -10.001 1.00 14.43 ?  123 LEU   B HB3  1 
ATOM   6035 H  HG   . LEU   B 1 123 ? 46.252 -21.986 -9.261  1.00 15.00 ?  123 LEU   B HG   1 
ATOM   6036 H  HD11 . LEU   B 1 123 ? 46.471 -23.730 -10.784 1.00 16.16 ?  123 LEU   B HD11 1 
ATOM   6037 H  HD12 . LEU   B 1 123 ? 44.949 -23.283 -10.686 1.00 16.16 ?  123 LEU   B HD12 1 
ATOM   6038 H  HD13 . LEU   B 1 123 ? 45.836 -22.820 -11.921 1.00 16.16 ?  123 LEU   B HD13 1 
ATOM   6039 H  HD21 . LEU   B 1 123 ? 48.262 -22.132 -10.425 1.00 16.41 ?  123 LEU   B HD21 1 
ATOM   6040 H  HD22 . LEU   B 1 123 ? 47.695 -21.131 -11.521 1.00 16.41 ?  123 LEU   B HD22 1 
ATOM   6041 H  HD23 . LEU   B 1 123 ? 47.948 -20.623 -10.037 1.00 16.41 ?  123 LEU   B HD23 1 
ATOM   6042 N  N    . ALA   B 1 124 ? 43.409 -22.381 -8.205  1.00 11.15 ?  124 ALA   B N    1 
ATOM   6043 C  CA   . ALA   B 1 124 ? 43.160 -22.699 -6.808  1.00 11.46 ?  124 ALA   B CA   1 
ATOM   6044 C  C    . ALA   B 1 124 ? 43.430 -24.159 -6.478  1.00 10.92 ?  124 ALA   B C    1 
ATOM   6045 O  O    . ALA   B 1 124 ? 43.295 -25.032 -7.344  1.00 11.68 ?  124 ALA   B O    1 
ATOM   6046 C  CB   . ALA   B 1 124 ? 41.705 -22.393 -6.425  1.00 11.93 ?  124 ALA   B CB   1 
ATOM   6047 H  H    . ALA   B 1 124 ? 43.237 -23.016 -8.769  1.00 13.40 ?  124 ALA   B H    1 
ATOM   6048 H  HA   . ALA   B 1 124 ? 43.736 -22.146 -6.266  1.00 13.77 ?  124 ALA   B HA   1 
ATOM   6049 H  HB1  . ALA   B 1 124 ? 41.567 -22.607 -5.492  1.00 14.34 ?  124 ALA   B HB1  1 
ATOM   6050 H  HB2  . ALA   B 1 124 ? 41.537 -21.441 -6.572  1.00 14.34 ?  124 ALA   B HB2  1 
ATOM   6051 H  HB3  . ALA   B 1 124 ? 41.110 -22.916 -6.982  1.00 14.34 ?  124 ALA   B HB3  1 
ATOM   6052 N  N    . PRO   B 1 125 ? 43.738 -24.451 -5.219  1.00 11.32 ?  125 PRO   B N    1 
ATOM   6053 C  CA   . PRO   B 1 125 ? 43.675 -25.815 -4.696  1.00 12.03 ?  125 PRO   B CA   1 
ATOM   6054 C  C    . PRO   B 1 125 ? 42.275 -26.087 -4.145  1.00 12.30 ?  125 PRO   B C    1 
ATOM   6055 O  O    . PRO   B 1 125 ? 41.476 -25.173 -3.949  1.00 12.54 ?  125 PRO   B O    1 
ATOM   6056 C  CB   . PRO   B 1 125 ? 44.666 -25.742 -3.531  1.00 13.26 ?  125 PRO   B CB   1 
ATOM   6057 C  CG   . PRO   B 1 125 ? 44.420 -24.353 -2.959  1.00 12.99 ?  125 PRO   B CG   1 
ATOM   6058 C  CD   . PRO   B 1 125 ? 44.076 -23.481 -4.162  1.00 12.30 ?  125 PRO   B CD   1 
ATOM   6059 H  HA   . PRO   B 1 125 ? 43.948 -26.483 -5.348  1.00 14.45 ?  125 PRO   B HA   1 
ATOM   6060 H  HB2  . PRO   B 1 125 ? 44.465 -26.427 -2.874  1.00 15.93 ?  125 PRO   B HB2  1 
ATOM   6061 H  HB3  . PRO   B 1 125 ? 45.577 -25.825 -3.856  1.00 15.93 ?  125 PRO   B HB3  1 
ATOM   6062 H  HG2  . PRO   B 1 125 ? 43.674 -24.380 -2.337  1.00 15.61 ?  125 PRO   B HG2  1 
ATOM   6063 H  HG3  . PRO   B 1 125 ? 45.221 -24.029 -2.516  1.00 15.61 ?  125 PRO   B HG3  1 
ATOM   6064 H  HD2  . PRO   B 1 125 ? 43.316 -22.916 -3.971  1.00 14.77 ?  125 PRO   B HD2  1 
ATOM   6065 H  HD3  . PRO   B 1 125 ? 44.853 -22.951 -4.424  1.00 14.77 ?  125 PRO   B HD3  1 
ATOM   6066 N  N    . LEU   B 1 126 ? 42.011 -27.360 -3.836  1.00 12.73 ?  126 LEU   B N    1 
ATOM   6067 C  CA   . LEU   B 1 126 ? 40.794 -27.718 -3.111  1.00 13.31 ?  126 LEU   B CA   1 
ATOM   6068 C  C    . LEU   B 1 126 ? 40.923 -27.320 -1.645  1.00 13.39 ?  126 LEU   B C    1 
ATOM   6069 O  O    . LEU   B 1 126 ? 41.821 -27.781 -0.937  1.00 15.89 ?  126 LEU   B O    1 
ATOM   6070 C  CB   . LEU   B 1 126 ? 40.541 -29.214 -3.220  1.00 14.72 ?  126 LEU   B CB   1 
ATOM   6071 C  CG   . LEU   B 1 126 ? 40.016 -29.709 -4.569  1.00 15.83 ?  126 LEU   B CG   1 
ATOM   6072 C  CD1  . LEU   B 1 126 ? 40.066 -31.217 -4.626  1.00 18.02 ?  126 LEU   B CD1  1 
ATOM   6073 C  CD2  . LEU   B 1 126 ? 38.605 -29.212 -4.832  1.00 16.09 ?  126 LEU   B CD2  1 
ATOM   6074 H  H    . LEU   B 1 126 ? 42.526 -28.028 -4.019  1.00 15.29 ?  126 LEU   B H    1 
ATOM   6075 H  HA   . LEU   B 1 126 ? 40.044 -27.239 -3.495  1.00 15.99 ?  126 LEU   B HA   1 
ATOM   6076 H  HB2  . LEU   B 1 126 ? 41.374 -29.673 -3.045  1.00 17.68 ?  126 LEU   B HB2  1 
ATOM   6077 H  HB3  . LEU   B 1 126 ? 39.886 -29.455 -2.549  1.00 17.68 ?  126 LEU   B HB3  1 
ATOM   6078 H  HG   . LEU   B 1 126 ? 40.591 -29.355 -5.272  1.00 19.02 ?  126 LEU   B HG   1 
ATOM   6079 H  HD11 . LEU   B 1 126 ? 39.730 -31.508 -5.487  1.00 21.64 ?  126 LEU   B HD11 1 
ATOM   6080 H  HD12 . LEU   B 1 126 ? 40.985 -31.506 -4.513  1.00 21.64 ?  126 LEU   B HD12 1 
ATOM   6081 H  HD13 . LEU   B 1 126 ? 39.515 -31.575 -3.914  1.00 21.64 ?  126 LEU   B HD13 1 
ATOM   6082 H  HD21 . LEU   B 1 126 ? 38.275 -29.622 -5.649  1.00 19.32 ?  126 LEU   B HD21 1 
ATOM   6083 H  HD22 . LEU   B 1 126 ? 38.037 -29.462 -4.087  1.00 19.32 ?  126 LEU   B HD22 1 
ATOM   6084 H  HD23 . LEU   B 1 126 ? 38.612 -28.246 -4.931  1.00 19.32 ?  126 LEU   B HD23 1 
ATOM   6085 N  N    . LEU   B 1 127 ? 39.997 -26.494 -1.173  1.00 13.21 ?  127 LEU   B N    1 
ATOM   6086 C  CA   . LEU   B 1 127 ? 40.061 -26.002 0.192   1.00 13.88 ?  127 LEU   B CA   1 
ATOM   6087 C  C    . LEU   B 1 127 ? 39.767 -27.118 1.188   1.00 13.70 ?  127 LEU   B C    1 
ATOM   6088 O  O    . LEU   B 1 127 ? 38.943 -28.011 0.951   1.00 13.95 ?  127 LEU   B O    1 
ATOM   6089 C  CB   . LEU   B 1 127 ? 39.052 -24.876 0.399   1.00 14.51 ?  127 LEU   B CB   1 
ATOM   6090 C  CG   . LEU   B 1 127 ? 39.236 -23.614 -0.442  1.00 15.14 ?  127 LEU   B CG   1 
ATOM   6091 C  CD1  . LEU   B 1 127 ? 38.114 -22.636 -0.127  1.00 15.70 ?  127 LEU   B CD1  1 
ATOM   6092 C  CD2  . LEU   B 1 127 ? 40.595 -22.982 -0.207  1.00 16.22 ?  127 LEU   B CD2  1 
ATOM   6093 H  H    . LEU   B 1 127 ? 39.320 -26.197 -1.624  1.00 15.87 ?  127 LEU   B H    1 
ATOM   6094 H  HA   . LEU   B 1 127 ? 40.953 -25.650 0.365   1.00 16.67 ?  127 LEU   B HA   1 
ATOM   6095 H  HB2  . LEU   B 1 127 ? 38.170 -25.228 0.198   1.00 17.43 ?  127 LEU   B HB2  1 
ATOM   6096 H  HB3  . LEU   B 1 127 ? 39.086 -24.611 1.330   1.00 17.43 ?  127 LEU   B HB3  1 
ATOM   6097 H  HG   . LEU   B 1 127 ? 39.166 -23.844 -1.375  1.00 18.18 ?  127 LEU   B HG   1 
ATOM   6098 H  HD11 . LEU   B 1 127 ? 38.242 -21.826 -0.653  1.00 18.86 ?  127 LEU   B HD11 1 
ATOM   6099 H  HD12 . LEU   B 1 127 ? 37.262 -23.038 -0.346  1.00 18.86 ?  127 LEU   B HD12 1 
ATOM   6100 H  HD13 . LEU   B 1 127 ? 38.140 -22.411 0.821   1.00 18.86 ?  127 LEU   B HD13 1 
ATOM   6101 H  HD21 . LEU   B 1 127 ? 40.633 -22.130 -0.664  1.00 19.49 ?  127 LEU   B HD21 1 
ATOM   6102 H  HD22 . LEU   B 1 127 ? 40.726 -22.853 0.747   1.00 19.49 ?  127 LEU   B HD22 1 
ATOM   6103 H  HD23 . LEU   B 1 127 ? 41.280 -23.577 -0.554  1.00 19.49 ?  127 LEU   B HD23 1 
ATOM   6104 N  N    . SER   B 1 128 ? 40.442 -27.038 2.329   1.00 13.85 ?  128 SER   B N    1 
ATOM   6105 C  CA   . SER   B 1 128 ? 40.306 -27.937 3.467   1.00 14.39 ?  128 SER   B CA   1 
ATOM   6106 C  C    . SER   B 1 128 ? 40.786 -29.352 3.167   1.00 15.85 ?  128 SER   B C    1 
ATOM   6107 O  O    . SER   B 1 128 ? 40.672 -30.219 4.031   1.00 17.38 ?  128 SER   B O    1 
ATOM   6108 C  CB   . SER   B 1 128 ? 38.896 -27.913 4.083   1.00 14.55 ?  128 SER   B CB   1 
ATOM   6109 O  OG   . SER   B 1 128 ? 38.612 -26.631 4.642   1.00 15.00 ?  128 SER   B OG   1 
ATOM   6110 H  H    . SER   B 1 128 ? 41.021 -26.416 2.476   1.00 16.64 ?  128 SER   B H    1 
ATOM   6111 H  HA   . SER   B 1 128 ? 40.898 -27.599 4.153   1.00 17.29 ?  128 SER   B HA   1 
ATOM   6112 H  HB2  . SER   B 1 128 ? 38.240 -28.120 3.402   1.00 17.48 ?  128 SER   B HB2  1 
ATOM   6113 H  HB3  . SER   B 1 128 ? 38.854 -28.586 4.794   1.00 17.48 ?  128 SER   B HB3  1 
ATOM   6114 H  HG   . SER   B 1 128 ? 39.185 -26.450 5.235   1.00 18.02 ?  128 SER   B HG   1 
ATOM   6115 N  N    . ALA   B 1 129 ? 41.368 -29.592 1.989   1.00 17.54 ?  129 ALA   B N    1 
ATOM   6116 C  CA   . ALA   B 1 129 ? 41.906 -30.895 1.635   1.00 18.26 ?  129 ALA   B CA   1 
ATOM   6117 C  C    . ALA   B 1 129 ? 43.314 -31.057 2.196   1.00 17.24 ?  129 ALA   B C    1 
ATOM   6118 O  O    . ALA   B 1 129 ? 43.871 -30.163 2.847   1.00 16.77 ?  129 ALA   B O    1 
ATOM   6119 C  CB   . ALA   B 1 129 ? 41.929 -31.059 0.116   1.00 20.77 ?  129 ALA   B CB   1 
ATOM   6120 H  H    . ALA   B 1 129 ? 41.463 -29.001 1.363   1.00 21.07 ?  129 ALA   B H    1 
ATOM   6121 H  HA   . ALA   B 1 129 ? 41.341 -31.585 2.006   1.00 21.93 ?  129 ALA   B HA   1 
ATOM   6122 H  HB1  . ALA   B 1 129 ? 42.272 -31.940 -0.102  1.00 24.94 ?  129 ALA   B HB1  1 
ATOM   6123 H  HB2  . ALA   B 1 129 ? 41.027 -30.962 -0.226  1.00 24.94 ?  129 ALA   B HB2  1 
ATOM   6124 H  HB3  . ALA   B 1 129 ? 42.503 -30.377 -0.269  1.00 24.94 ?  129 ALA   B HB3  1 
ATOM   6125 N  N    . GLY   B 1 130 ? 43.902 -32.216 1.914   1.00 17.04 ?  130 GLY   B N    1 
ATOM   6126 C  CA   . GLY   B 1 130 ? 45.291 -32.441 2.263   1.00 17.31 ?  130 GLY   B CA   1 
ATOM   6127 C  C    . GLY   B 1 130 ? 45.503 -32.353 3.754   1.00 17.00 ?  130 GLY   B C    1 
ATOM   6128 O  O    . GLY   B 1 130 ? 44.803 -32.999 4.548   1.00 17.89 ?  130 GLY   B O    1 
ATOM   6129 H  H    . GLY   B 1 130 ? 43.527 -32.877 1.507   1.00 20.47 ?  130 GLY   B H    1 
ATOM   6130 H  HA2  . GLY   B 1 130 ? 45.566 -33.325 1.961   1.00 20.79 ?  130 GLY   B HA2  1 
ATOM   6131 H  HA3  . GLY   B 1 130 ? 45.852 -31.781 1.829   1.00 20.79 ?  130 GLY   B HA3  1 
ATOM   6132 N  N    . ILE   B 1 131 ? 46.481 -31.528 4.147   1.00 17.61 ?  131 ILE   B N    1 
ATOM   6133 C  CA   . ILE   B 1 131 ? 46.857 -31.420 5.548   1.00 18.43 ?  131 ILE   B CA   1 
ATOM   6134 C  C    . ILE   B 1 131 ? 45.755 -30.821 6.401   1.00 17.44 ?  131 ILE   B C    1 
ATOM   6135 O  O    . ILE   B 1 131 ? 45.843 -30.892 7.629   1.00 18.96 ?  131 ILE   B O    1 
ATOM   6136 C  CB   . ILE   B 1 131 ? 48.183 -30.648 5.742   1.00 20.27 ?  131 ILE   B CB   1 
ATOM   6137 C  CG1  . ILE   B 1 131 ? 48.013 -29.159 5.411   1.00 21.29 ?  131 ILE   B CG1  1 
ATOM   6138 C  CG2  . ILE   B 1 131 ? 49.292 -31.265 4.892   1.00 21.52 ?  131 ILE   B CG2  1 
ATOM   6139 C  CD1  . ILE   B 1 131 ? 49.233 -28.313 5.725   1.00 22.41 ?  131 ILE   B CD1  1 
ATOM   6140 H  H    . ILE   B 1 131 ? 46.937 -31.022 3.620   1.00 21.15 ?  131 ILE   B H    1 
ATOM   6141 H  HA   . ILE   B 1 131 ? 47.006 -32.318 5.883   1.00 22.14 ?  131 ILE   B HA   1 
ATOM   6142 H  HB   . ILE   B 1 131 ? 48.440 -30.722 6.675   1.00 24.35 ?  131 ILE   B HB   1 
ATOM   6143 H  HG12 . ILE   B 1 131 ? 47.823 -29.073 4.464   1.00 25.57 ?  131 ILE   B HG12 1 
ATOM   6144 H  HG13 . ILE   B 1 131 ? 47.271 -28.800 5.926   1.00 25.57 ?  131 ILE   B HG13 1 
ATOM   6145 H  HG21 . ILE   B 1 131 ? 50.138 -30.867 5.143   1.00 25.85 ?  131 ILE   B HG21 1 
ATOM   6146 H  HG22 . ILE   B 1 131 ? 49.311 -32.219 5.046   1.00 25.85 ?  131 ILE   B HG22 1 
ATOM   6147 H  HG23 . ILE   B 1 131 ? 49.104 -31.084 3.956   1.00 25.85 ?  131 ILE   B HG23 1 
ATOM   6148 H  HD11 . ILE   B 1 131 ? 49.012 -27.379 5.588   1.00 26.91 ?  131 ILE   B HD11 1 
ATOM   6149 H  HD12 . ILE   B 1 131 ? 49.489 -28.459 6.650   1.00 26.91 ?  131 ILE   B HD12 1 
ATOM   6150 H  HD13 . ILE   B 1 131 ? 49.958 -28.572 5.137   1.00 26.91 ?  131 ILE   B HD13 1 
ATOM   6151 N  N    . PHE   B 1 132 ? 44.720 -30.238 5.787   1.00 16.54 ?  132 PHE   B N    1 
ATOM   6152 C  CA   . PHE   B 1 132 ? 43.575 -29.733 6.534   1.00 17.08 ?  132 PHE   B CA   1 
ATOM   6153 C  C    . PHE   B 1 132 ? 42.560 -30.821 6.879   1.00 18.81 ?  132 PHE   B C    1 
ATOM   6154 O  O    . PHE   B 1 132 ? 41.680 -30.571 7.710   1.00 20.71 ?  132 PHE   B O    1 
ATOM   6155 C  CB   . PHE   B 1 132 ? 42.875 -28.615 5.751   1.00 16.10 ?  132 PHE   B CB   1 
ATOM   6156 C  CG   . PHE   B 1 132 ? 43.571 -27.269 5.820   1.00 15.77 ?  132 PHE   B CG   1 
ATOM   6157 C  CD1  . PHE   B 1 132 ? 44.855 -27.095 5.322   1.00 17.48 ?  132 PHE   B CD1  1 
ATOM   6158 C  CD2  . PHE   B 1 132 ? 42.904 -26.162 6.334   1.00 15.39 ?  132 PHE   B CD2  1 
ATOM   6159 C  CE1  . PHE   B 1 132 ? 45.475 -25.854 5.380   1.00 17.42 ?  132 PHE   B CE1  1 
ATOM   6160 C  CE2  . PHE   B 1 132 ? 43.512 -24.915 6.379   1.00 16.15 ?  132 PHE   B CE2  1 
ATOM   6161 C  CZ   . PHE   B 1 132 ? 44.798 -24.764 5.906   1.00 16.78 ?  132 PHE   B CZ   1 
ATOM   6162 H  H    . PHE   B 1 132 ? 44.659 -30.133 4.933   1.00 19.87 ?  132 PHE   B H    1 
ATOM   6163 H  HA   . PHE   B 1 132 ? 43.896 -29.357 7.366   1.00 20.52 ?  132 PHE   B HA   1 
ATOM   6164 H  HB2  . PHE   B 1 132 ? 42.836 -28.876 4.819   1.00 19.34 ?  132 PHE   B HB2  1 
ATOM   6165 H  HB3  . PHE   B 1 132 ? 41.980 -28.505 6.102   1.00 19.34 ?  132 PHE   B HB3  1 
ATOM   6166 H  HD1  . PHE   B 1 132 ? 45.318 -27.828 4.974   1.00 21.00 ?  132 PHE   B HD1  1 
ATOM   6167 H  HD2  . PHE   B 1 132 ? 42.039 -26.264 6.659   1.00 18.49 ?  132 PHE   B HD2  1 
ATOM   6168 H  HE1  . PHE   B 1 132 ? 46.343 -25.753 5.055   1.00 20.93 ?  132 PHE   B HE1  1 
ATOM   6169 H  HE2  . PHE   B 1 132 ? 43.058 -24.187 6.742   1.00 19.40 ?  132 PHE   B HE2  1 
ATOM   6170 H  HZ   . PHE   B 1 132 ? 45.213 -23.929 5.942   1.00 20.15 ?  132 PHE   B HZ   1 
ATOM   6171 N  N    . GLY   B 1 133 ? 42.636 -32.005 6.252   1.00 18.04 ?  133 GLY   B N    1 
ATOM   6172 C  CA   . GLY   B 1 133 ? 41.937 -33.181 6.744   1.00 19.28 ?  133 GLY   B CA   1 
ATOM   6173 C  C    . GLY   B 1 133 ? 40.538 -33.452 6.218   1.00 20.08 ?  133 GLY   B C    1 
ATOM   6174 O  O    . GLY   B 1 133 ? 39.970 -34.489 6.572   1.00 22.10 ?  133 GLY   B O    1 
ATOM   6175 H  H    . GLY   B 1 133 ? 43.096 -32.144 5.532   1.00 21.67 ?  133 GLY   B H    1 
ATOM   6176 H  HA2  . GLY   B 1 133 ? 42.480 -33.963 6.546   1.00 23.16 ?  133 GLY   B HA2  1 
ATOM   6177 H  HA3  . GLY   B 1 133 ? 41.867 -33.111 7.706   1.00 23.16 ?  133 GLY   B HA3  1 
ATOM   6178 N  N    . ALA   B 1 134 ? 39.954 -32.574 5.411   1.00 19.03 ?  134 ALA   B N    1 
ATOM   6179 C  CA   . ALA   B 1 134 ? 38.636 -32.866 4.867   1.00 19.07 ?  134 ALA   B CA   1 
ATOM   6180 C  C    . ALA   B 1 134 ? 38.747 -33.829 3.693   1.00 18.89 ?  134 ALA   B C    1 
ATOM   6181 O  O    . ALA   B 1 134 ? 39.812 -34.003 3.096   1.00 19.83 ?  134 ALA   B O    1 
ATOM   6182 C  CB   . ALA   B 1 134 ? 37.934 -31.585 4.422   1.00 19.01 ?  134 ALA   B CB   1 
ATOM   6183 H  H    . ALA   B 1 134 ? 40.285 -31.813 5.179   1.00 22.85 ?  134 ALA   B H    1 
ATOM   6184 H  HA   . ALA   B 1 134 ? 38.095 -33.287 5.551   1.00 22.90 ?  134 ALA   B HA   1 
ATOM   6185 H  HB1  . ALA   B 1 134 ? 37.048 -31.811 4.095   1.00 22.83 ?  134 ALA   B HB1  1 
ATOM   6186 H  HB2  . ALA   B 1 134 ? 37.863 -30.986 5.181   1.00 22.83 ?  134 ALA   B HB2  1 
ATOM   6187 H  HB3  . ALA   B 1 134 ? 38.451 -31.169 3.716   1.00 22.83 ?  134 ALA   B HB3  1 
ATOM   6188 N  N    . ASP   B 1 135 ? 37.626 -34.468 3.381   1.00 19.73 ?  135 ASP   B N    1 
ATOM   6189 C  CA   . ASP   B 1 135 ? 37.555 -35.356 2.232   1.00 20.52 ?  135 ASP   B CA   1 
ATOM   6190 C  C    . ASP   B 1 135 ? 37.630 -34.512 0.966   1.00 18.84 ?  135 ASP   B C    1 
ATOM   6191 O  O    . ASP   B 1 135 ? 36.770 -33.640 0.760   1.00 18.70 ?  135 ASP   B O    1 
ATOM   6192 C  CB   . ASP   B 1 135 ? 36.233 -36.117 2.286   1.00 22.74 ?  135 ASP   B CB   1 
ATOM   6193 C  CG   . ASP   B 1 135 ? 36.082 -37.127 1.164   1.00 24.49 ?  135 ASP   B CG   1 
ATOM   6194 O  OD1  . ASP   B 1 135 ? 36.936 -37.154 0.255   1.00 24.07 ?  135 ASP   B OD1  1 
ATOM   6195 O  OD2  . ASP   B 1 135 ? 35.106 -37.910 1.202   1.00 27.82 -1 135 ASP   B OD2  1 
ATOM   6196 H  H    . ASP   B 1 135 ? 36.890 -34.402 3.818   1.00 23.69 ?  135 ASP   B H    1 
ATOM   6197 H  HA   . ASP   B 1 135 ? 38.289 -35.993 2.261   1.00 24.65 ?  135 ASP   B HA   1 
ATOM   6198 H  HB2  . ASP   B 1 135 ? 36.184 -36.596 3.127   1.00 27.31 ?  135 ASP   B HB2  1 
ATOM   6199 H  HB3  . ASP   B 1 135 ? 35.506 -35.484 2.218   1.00 27.31 ?  135 ASP   B HB3  1 
ATOM   6200 N  N    . PRO   B 1 136 ? 38.629 -34.710 0.105   1.00 18.63 ?  136 PRO   B N    1 
ATOM   6201 C  CA   . PRO   B 1 136 ? 38.704 -33.888 -1.114  1.00 17.66 ?  136 PRO   B CA   1 
ATOM   6202 C  C    . PRO   B 1 136 ? 37.501 -34.052 -2.021  1.00 16.88 ?  136 PRO   B C    1 
ATOM   6203 O  O    . PRO   B 1 136 ? 37.158 -33.113 -2.747  1.00 16.26 ?  136 PRO   B O    1 
ATOM   6204 C  CB   . PRO   B 1 136 ? 40.013 -34.348 -1.776  1.00 18.92 ?  136 PRO   B CB   1 
ATOM   6205 C  CG   . PRO   B 1 136 ? 40.257 -35.727 -1.215  1.00 20.42 ?  136 PRO   B CG   1 
ATOM   6206 C  CD   . PRO   B 1 136 ? 39.735 -35.680 0.188   1.00 20.10 ?  136 PRO   B CD   1 
ATOM   6207 H  HA   . PRO   B 1 136 ? 38.787 -32.954 -0.884  1.00 21.22 ?  136 PRO   B HA   1 
ATOM   6208 H  HB2  . PRO   B 1 136 ? 39.906 -34.386 -2.741  1.00 22.73 ?  136 PRO   B HB2  1 
ATOM   6209 H  HB3  . PRO   B 1 136 ? 40.733 -33.748 -1.533  1.00 22.73 ?  136 PRO   B HB3  1 
ATOM   6210 H  HG2  . PRO   B 1 136 ? 39.769 -36.387 -1.737  1.00 24.53 ?  136 PRO   B HG2  1 
ATOM   6211 H  HG3  . PRO   B 1 136 ? 41.207 -35.924 -1.219  1.00 24.53 ?  136 PRO   B HG3  1 
ATOM   6212 H  HD2  . PRO   B 1 136 ? 39.403 -36.551 0.455   1.00 24.14 ?  136 PRO   B HD2  1 
ATOM   6213 H  HD3  . PRO   B 1 136 ? 40.420 -35.357 0.796   1.00 24.14 ?  136 PRO   B HD3  1 
ATOM   6214 N  N    . ILE   B 1 137 ? 36.851 -35.220 -2.010  1.00 17.21 ?  137 ILE   B N    1 
ATOM   6215 C  CA   . ILE   B 1 137 ? 35.624 -35.394 -2.785  1.00 17.57 ?  137 ILE   B CA   1 
ATOM   6216 C  C    . ILE   B 1 137 ? 34.550 -34.426 -2.302  1.00 17.19 ?  137 ILE   B C    1 
ATOM   6217 O  O    . ILE   B 1 137 ? 33.819 -33.822 -3.100  1.00 16.71 ?  137 ILE   B O    1 
ATOM   6218 C  CB   . ILE   B 1 137 ? 35.149 -36.863 -2.715  1.00 19.71 ?  137 ILE   B CB   1 
ATOM   6219 C  CG1  . ILE   B 1 137 ? 36.157 -37.769 -3.420  1.00 21.69 ?  137 ILE   B CG1  1 
ATOM   6220 C  CG2  . ILE   B 1 137 ? 33.759 -37.013 -3.326  1.00 20.26 ?  137 ILE   B CG2  1 
ATOM   6221 C  CD1  . ILE   B 1 137 ? 35.866 -39.257 -3.265  1.00 24.26 ?  137 ILE   B CD1  1 
ATOM   6222 H  H    . ILE   B 1 137 ? 37.098 -35.919 -1.572  1.00 20.67 ?  137 ILE   B H    1 
ATOM   6223 H  HA   . ILE   B 1 137 ? 35.807 -35.193 -3.716  1.00 21.10 ?  137 ILE   B HA   1 
ATOM   6224 H  HB   . ILE   B 1 137 ? 35.100 -37.126 -1.787  1.00 23.67 ?  137 ILE   B HB   1 
ATOM   6225 H  HG12 . ILE   B 1 137 ? 36.155 -37.577 -4.369  1.00 26.05 ?  137 ILE   B HG12 1 
ATOM   6226 H  HG13 . ILE   B 1 137 ? 37.038 -37.613 -3.051  1.00 26.05 ?  137 ILE   B HG13 1 
ATOM   6227 H  HG21 . ILE   B 1 137 ? 33.499 -37.951 -3.323  1.00 24.33 ?  137 ILE   B HG21 1 
ATOM   6228 H  HG22 . ILE   B 1 137 ? 33.119 -36.513 -2.800  1.00 24.33 ?  137 ILE   B HG22 1 
ATOM   6229 H  HG23 . ILE   B 1 137 ? 33.773 -36.683 -4.236  1.00 24.33 ?  137 ILE   B HG23 1 
ATOM   6230 H  HD11 . ILE   B 1 137 ? 36.425 -39.745 -3.888  1.00 29.13 ?  137 ILE   B HD11 1 
ATOM   6231 H  HD12 . ILE   B 1 137 ? 36.068 -39.531 -2.355  1.00 29.13 ?  137 ILE   B HD12 1 
ATOM   6232 H  HD13 . ILE   B 1 137 ? 34.935 -39.441 -3.464  1.00 29.13 ?  137 ILE   B HD13 1 
ATOM   6233 N  N    . HIS   B 1 138 ? 34.433 -34.273 -0.986  1.00 17.45 ?  138 HIS   B N    1 
ATOM   6234 C  CA   . HIS   B 1 138 ? 33.485 -33.309 -0.444  1.00 17.91 ?  138 HIS   B CA   1 
ATOM   6235 C  C    . HIS   B 1 138 ? 33.891 -31.880 -0.779  1.00 16.74 ?  138 HIS   B C    1 
ATOM   6236 O  O    . HIS   B 1 138 ? 33.038 -31.040 -1.090  1.00 17.63 ?  138 HIS   B O    1 
ATOM   6237 C  CB   . HIS   B 1 138 ? 33.388 -33.489 1.064   1.00 19.45 ?  138 HIS   B CB   1 
ATOM   6238 C  CG   . HIS   B 1 138 ? 32.479 -32.503 1.719   1.00 21.21 ?  138 HIS   B CG   1 
ATOM   6239 N  ND1  . HIS   B 1 138 ? 31.138 -32.417 1.413   1.00 23.25 ?  138 HIS   B ND1  1 
ATOM   6240 C  CD2  . HIS   B 1 138 ? 32.721 -31.539 2.638   1.00 22.03 ?  138 HIS   B CD2  1 
ATOM   6241 C  CE1  . HIS   B 1 138 ? 30.588 -31.451 2.128   1.00 23.53 ?  138 HIS   B CE1  1 
ATOM   6242 N  NE2  . HIS   B 1 138 ? 31.526 -30.904 2.882   1.00 22.58 ?  138 HIS   B NE2  1 
ATOM   6243 H  H    . HIS   B 1 138 ? 34.890 -34.706 -0.398  1.00 20.96 ?  138 HIS   B H    1 
ATOM   6244 H  HA   . HIS   B 1 138 ? 32.612 -33.478 -0.828  1.00 21.51 ?  138 HIS   B HA   1 
ATOM   6245 H  HB2  . HIS   B 1 138 ? 33.048 -34.380 1.252   1.00 23.36 ?  138 HIS   B HB2  1 
ATOM   6246 H  HB3  . HIS   B 1 138 ? 34.271 -33.386 1.451   1.00 23.36 ?  138 HIS   B HB3  1 
ATOM   6247 H  HD1  . HIS   B 1 138 ? 30.725 -32.918 0.845   1.00 27.92 ?  138 HIS   B HD1  1 
ATOM   6248 H  HD2  . HIS   B 1 138 ? 33.532 -31.355 3.046   1.00 26.46 ?  138 HIS   B HD2  1 
ATOM   6249 H  HE1  . HIS   B 1 138 ? 29.689 -31.210 2.107   1.00 28.26 ?  138 HIS   B HE1  1 
ATOM   6250 N  N    . SER   B 1 139 ? 35.185 -31.579 -0.713  1.00 16.10 ?  139 SER   B N    1 
ATOM   6251 C  CA   . SER   B 1 139 ? 35.625 -30.233 -1.045  1.00 15.51 ?  139 SER   B CA   1 
ATOM   6252 C  C    . SER   B 1 139 ? 35.277 -29.889 -2.483  1.00 14.69 ?  139 SER   B C    1 
ATOM   6253 O  O    . SER   B 1 139 ? 34.827 -28.774 -2.764  1.00 14.72 ?  139 SER   B O    1 
ATOM   6254 C  CB   . SER   B 1 139 ? 37.122 -30.100 -0.792  1.00 15.83 ?  139 SER   B CB   1 
ATOM   6255 O  OG   . SER   B 1 139 ? 37.531 -28.765 -1.027  1.00 15.96 ?  139 SER   B OG   1 
ATOM   6256 H  H    . SER   B 1 139 ? 35.814 -32.124 -0.495  1.00 19.35 ?  139 SER   B H    1 
ATOM   6257 H  HA   . SER   B 1 139 ? 35.163 -29.604 -0.476  1.00 18.63 ?  139 SER   B HA   1 
ATOM   6258 H  HB2  . SER   B 1 139 ? 37.307 -30.342 0.131   1.00 19.01 ?  139 SER   B HB2  1 
ATOM   6259 H  HB3  . SER   B 1 139 ? 37.603 -30.686 -1.394  1.00 19.01 ?  139 SER   B HB3  1 
ATOM   6260 H  HG   . SER   B 1 139 ? 38.357 -28.689 -0.868  1.00 19.17 ?  139 SER   B HG   1 
ATOM   6261 N  N    . LEU   B 1 140 ? 35.459 -30.838 -3.406  1.00 14.61 ?  140 LEU   B N    1 
ATOM   6262 C  CA   . LEU   B 1 140 ? 35.085 -30.588 -4.793  1.00 14.24 ?  140 LEU   B CA   1 
ATOM   6263 C  C    . LEU   B 1 140 ? 33.581 -30.357 -4.913  1.00 14.65 ?  140 LEU   B C    1 
ATOM   6264 O  O    . LEU   B 1 140 ? 33.137 -29.475 -5.655  1.00 14.64 ?  140 LEU   B O    1 
ATOM   6265 C  CB   . LEU   B 1 140 ? 35.554 -31.746 -5.672  1.00 14.47 ?  140 LEU   B CB   1 
ATOM   6266 C  CG   . LEU   B 1 140 ? 35.181 -31.638 -7.142  1.00 14.89 ?  140 LEU   B CG   1 
ATOM   6267 C  CD1  . LEU   B 1 140 ? 35.749 -30.366 -7.749  1.00 16.11 ?  140 LEU   B CD1  1 
ATOM   6268 C  CD2  . LEU   B 1 140 ? 35.665 -32.873 -7.880  1.00 16.27 ?  140 LEU   B CD2  1 
ATOM   6269 H  H    . LEU   B 1 140 ? 35.786 -31.618 -3.260  1.00 17.55 ?  140 LEU   B H    1 
ATOM   6270 H  HA   . LEU   B 1 140 ? 35.537 -29.786 -5.099  1.00 17.10 ?  140 LEU   B HA   1 
ATOM   6271 H  HB2  . LEU   B 1 140 ? 36.521 -31.807 -5.622  1.00 17.38 ?  140 LEU   B HB2  1 
ATOM   6272 H  HB3  . LEU   B 1 140 ? 35.160 -32.569 -5.340  1.00 17.38 ?  140 LEU   B HB3  1 
ATOM   6273 H  HG   . LEU   B 1 140 ? 34.219 -31.594 -7.222  1.00 17.89 ?  140 LEU   B HG   1 
ATOM   6274 H  HD11 . LEU   B 1 140 ? 35.621 -30.392 -8.709  1.00 19.35 ?  140 LEU   B HD11 1 
ATOM   6275 H  HD12 . LEU   B 1 140 ? 35.284 -29.599 -7.375  1.00 19.35 ?  140 LEU   B HD12 1 
ATOM   6276 H  HD13 . LEU   B 1 140 ? 36.696 -30.310 -7.543  1.00 19.35 ?  140 LEU   B HD13 1 
ATOM   6277 H  HD21 . LEU   B 1 140 ? 35.422 -32.793 -8.816  1.00 19.55 ?  140 LEU   B HD21 1 
ATOM   6278 H  HD22 . LEU   B 1 140 ? 36.623 -32.946 -7.787  1.00 19.55 ?  140 LEU   B HD22 1 
ATOM   6279 H  HD23 . LEU   B 1 140 ? 35.231 -33.653 -7.493  1.00 19.55 ?  140 LEU   B HD23 1 
ATOM   6280 N  N    A ARG   B 1 141 ? 32.786 -31.154 -4.192  0.62 15.06 ?  141 ARG   B N    1 
ATOM   6281 N  N    B ARG   B 1 141 ? 32.783 -31.132 -4.178  0.38 14.81 ?  141 ARG   B N    1 
ATOM   6282 C  CA   A ARG   B 1 141 ? 31.338 -30.979 -4.146  0.62 16.08 ?  141 ARG   B CA   1 
ATOM   6283 C  CA   B ARG   B 1 141 ? 31.335 -30.955 -4.197  0.38 15.39 ?  141 ARG   B CA   1 
ATOM   6284 C  C    A ARG   B 1 141 ? 30.968 -29.558 -3.747  0.62 15.66 ?  141 ARG   B C    1 
ATOM   6285 C  C    B ARG   B 1 141 ? 30.948 -29.552 -3.743  0.38 15.19 ?  141 ARG   B C    1 
ATOM   6286 O  O    A ARG   B 1 141 ? 30.178 -28.885 -4.425  0.62 16.11 ?  141 ARG   B O    1 
ATOM   6287 O  O    B ARG   B 1 141 ? 30.126 -28.881 -4.383  0.38 15.24 ?  141 ARG   B O    1 
ATOM   6288 C  CB   A ARG   B 1 141 ? 30.773 -31.972 -3.124  0.62 17.48 ?  141 ARG   B CB   1 
ATOM   6289 C  CB   B ARG   B 1 141 ? 30.700 -32.023 -3.304  0.38 16.22 ?  141 ARG   B CB   1 
ATOM   6290 C  CG   A ARG   B 1 141 ? 29.277 -31.929 -2.927  0.62 19.10 ?  141 ARG   B CG   1 
ATOM   6291 C  CG   B ARG   B 1 141 ? 29.272 -31.758 -2.859  0.38 17.61 ?  141 ARG   B CG   1 
ATOM   6292 C  CD   A ARG   B 1 141 ? 28.600 -32.589 -4.078  0.62 20.73 ?  141 ARG   B CD   1 
ATOM   6293 C  CD   B ARG   B 1 141 ? 28.271 -32.395 -3.784  0.38 18.04 ?  141 ARG   B CD   1 
ATOM   6294 N  NE   A ARG   B 1 141 ? 28.265 -31.644 -5.133  0.62 20.82 ?  141 ARG   B NE   1 
ATOM   6295 N  NE   B ARG   B 1 141 ? 27.986 -31.577 -4.955  0.38 19.30 ?  141 ARG   B NE   1 
ATOM   6296 C  CZ   A ARG   B 1 141 ? 28.175 -31.957 -6.419  0.62 20.51 ?  141 ARG   B CZ   1 
ATOM   6297 C  CZ   B ARG   B 1 141 ? 28.266 -31.914 -6.208  0.38 19.37 ?  141 ARG   B CZ   1 
ATOM   6298 N  NH1  A ARG   B 1 141 ? 28.535 -33.150 -6.868  0.62 19.93 ?  141 ARG   B NH1  1 
ATOM   6299 N  NH1  B ARG   B 1 141 ? 28.910 -33.035 -6.501  0.38 18.91 ?  141 ARG   B NH1  1 
ATOM   6300 N  NH2  A ARG   B 1 141 ? 27.712 -31.053 -7.276  0.62 21.40 ?  141 ARG   B NH2  1 
ATOM   6301 N  NH2  B ARG   B 1 141 ? 27.876 -31.112 -7.195  0.38 20.21 ?  141 ARG   B NH2  1 
ATOM   6302 H  H    A ARG   B 1 141 ? 33.074 -31.803 -3.711  0.62 18.10 ?  141 ARG   B H    1 
ATOM   6303 H  H    B ARG   B 1 141 ? 33.059 -31.756 -3.658  0.38 17.79 ?  141 ARG   B H    1 
ATOM   6304 H  HA   A ARG   B 1 141 ? 30.956 -31.165 -5.012  0.62 19.32 ?  141 ARG   B HA   1 
ATOM   6305 H  HA   B ARG   B 1 141 ? 31.007 -31.076 -5.097  0.38 18.48 ?  141 ARG   B HA   1 
ATOM   6306 H  HB2  A ARG   B 1 141 ? 31.015 -32.866 -3.402  0.62 20.99 ?  141 ARG   B HB2  1 
ATOM   6307 H  HB2  B ARG   B 1 141 ? 30.707 -32.864 -3.788  0.38 19.49 ?  141 ARG   B HB2  1 
ATOM   6308 H  HB3  A ARG   B 1 141 ? 31.178 -31.785 -2.263  0.62 20.99 ?  141 ARG   B HB3  1 
ATOM   6309 H  HB3  B ARG   B 1 141 ? 31.239 -32.112 -2.502  0.38 19.49 ?  141 ARG   B HB3  1 
ATOM   6310 H  HG2  A ARG   B 1 141 ? 29.047 -32.403 -2.114  0.62 22.93 ?  141 ARG   B HG2  1 
ATOM   6311 H  HG2  B ARG   B 1 141 ? 29.151 -32.140 -1.981  0.38 21.15 ?  141 ARG   B HG2  1 
ATOM   6312 H  HG3  A ARG   B 1 141 ? 28.973 -31.005 -2.873  0.62 22.93 ?  141 ARG   B HG3  1 
ATOM   6313 H  HG3  B ARG   B 1 141 ? 29.081 -30.806 -2.824  0.38 21.15 ?  141 ARG   B HG3  1 
ATOM   6314 H  HD2  A ARG   B 1 141 ? 29.194 -33.260 -4.447  0.62 24.90 ?  141 ARG   B HD2  1 
ATOM   6315 H  HD2  B ARG   B 1 141 ? 28.606 -33.261 -4.069  0.38 21.67 ?  141 ARG   B HD2  1 
ATOM   6316 H  HD3  A ARG   B 1 141 ? 27.784 -33.005 -3.765  0.62 24.90 ?  141 ARG   B HD3  1 
ATOM   6317 H  HD3  B ARG   B 1 141 ? 27.444 -32.513 -3.303  0.38 21.67 ?  141 ARG   B HD3  1 
ATOM   6318 H  HE   A ARG   B 1 141 ? 28.082 -30.835 -4.902  0.62 25.01 ?  141 ARG   B HE   1 
ATOM   6319 H  HE   B ARG   B 1 141 ? 27.555 -30.842 -4.829  0.38 23.18 ?  141 ARG   B HE   1 
ATOM   6320 H  HH11 A ARG   B 1 141 ? 28.825 -33.750 -6.326  0.62 23.94 ?  141 ARG   B HH11 1 
ATOM   6321 H  HH11 B ARG   B 1 141 ? 29.166 -33.568 -5.877  0.38 22.71 ?  141 ARG   B HH11 1 
ATOM   6322 H  HH12 A ARG   B 1 141 ? 28.474 -33.326 -7.707  0.62 23.94 ?  141 ARG   B HH12 1 
ATOM   6323 H  HH12 B ARG   B 1 141 ? 29.079 -33.227 -7.320  0.38 22.71 ?  141 ARG   B HH12 1 
ATOM   6324 H  HH21 A ARG   B 1 141 ? 27.484 -30.271 -6.997  0.62 25.71 ?  141 ARG   B HH21 1 
ATOM   6325 H  HH21 B ARG   B 1 141 ? 27.460 -30.380 -7.017  0.38 24.28 ?  141 ARG   B HH21 1 
ATOM   6326 H  HH22 A ARG   B 1 141 ? 27.668 -31.238 -8.115  0.62 25.71 ?  141 ARG   B HH22 1 
ATOM   6327 H  HH22 B ARG   B 1 141 ? 28.056 -31.315 -8.011  0.38 24.28 ?  141 ARG   B HH22 1 
ATOM   6328 N  N    . VAL   B 1 142 ? 31.511 -29.099 -2.622  1.00 15.49 ?  142 VAL   B N    1 
ATOM   6329 C  CA   . VAL   B 1 142 ? 31.186 -27.765 -2.136  1.00 15.01 ?  142 VAL   B CA   1 
ATOM   6330 C  C    . VAL   B 1 142 ? 31.658 -26.713 -3.131  1.00 14.39 ?  142 VAL   B C    1 
ATOM   6331 O  O    . VAL   B 1 142 ? 30.956 -25.731 -3.394  1.00 14.91 ?  142 VAL   B O    1 
ATOM   6332 C  CB   . VAL   B 1 142 ? 31.747 -27.536 -0.720  1.00 15.55 ?  142 VAL   B CB   1 
ATOM   6333 C  CG1  . VAL   B 1 142 ? 31.425 -26.117 -0.248  1.00 15.52 ?  142 VAL   B CG1  1 
ATOM   6334 C  CG2  . VAL   B 1 142 ? 31.185 -28.567 0.246   1.00 16.39 ?  142 VAL   B CG2  1 
ATOM   6335 H  H    A VAL   B 1 142 ? 32.063 -29.532 -2.122  0.62 18.61 ?  142 VAL   B H    1 
ATOM   6336 H  H    B VAL   B 1 142 ? 32.077 -29.529 -2.135  0.38 18.61 ?  142 VAL   B H    1 
ATOM   6337 H  HA   . VAL   B 1 142 ? 30.226 -27.684 -2.072  1.00 18.03 ?  142 VAL   B HA   1 
ATOM   6338 H  HB   . VAL   B 1 142 ? 32.715 -27.635 -0.737  1.00 18.68 ?  142 VAL   B HB   1 
ATOM   6339 H  HG11 . VAL   B 1 142 ? 31.614 -26.048 0.701   1.00 18.64 ?  142 VAL   B HG11 1 
ATOM   6340 H  HG12 . VAL   B 1 142 ? 31.984 -25.485 -0.737  1.00 18.64 ?  142 VAL   B HG12 1 
ATOM   6341 H  HG13 . VAL   B 1 142 ? 30.492 -25.931 -0.416  1.00 18.64 ?  142 VAL   B HG13 1 
ATOM   6342 H  HG21 . VAL   B 1 142 ? 31.508 -28.368 1.139   1.00 19.69 ?  142 VAL   B HG21 1 
ATOM   6343 H  HG22 . VAL   B 1 142 ? 30.219 -28.519 0.223   1.00 19.69 ?  142 VAL   B HG22 1 
ATOM   6344 H  HG23 . VAL   B 1 142 ? 31.485 -29.447 -0.026  1.00 19.69 ?  142 VAL   B HG23 1 
ATOM   6345 N  N    . CYS   B 1 143 ? 32.838 -26.915 -3.723  1.00 13.87 ?  143 CYS   B N    1 
ATOM   6346 C  CA   . CYS   B 1 143 ? 33.325 -25.982 -4.734  1.00 14.04 ?  143 CYS   B CA   1 
ATOM   6347 C  C    . CYS   B 1 143 ? 32.318 -25.842 -5.869  1.00 14.18 ?  143 CYS   B C    1 
ATOM   6348 O  O    . CYS   B 1 143 ? 31.917 -24.730 -6.232  1.00 14.44 ?  143 CYS   B O    1 
ATOM   6349 C  CB   . CYS   B 1 143 ? 34.679 -26.466 -5.263  1.00 14.03 ?  143 CYS   B CB   1 
ATOM   6350 S  SG   . CYS   B 1 143 ? 35.430 -25.369 -6.498  1.00 14.54 ?  143 CYS   B SG   1 
ATOM   6351 H  H    . CYS   B 1 143 ? 33.369 -27.568 -3.554  1.00 16.67 ?  143 CYS   B H    1 
ATOM   6352 H  HA   . CYS   B 1 143 ? 33.455 -25.105 -4.332  1.00 16.86 ?  143 CYS   B HA   1 
ATOM   6353 H  HB2  . CYS   B 1 143 ? 35.303 -26.540 -4.521  1.00 16.86 ?  143 CYS   B HB2  1 
ATOM   6354 H  HB3  . CYS   B 1 143 ? 34.561 -27.333 -5.673  1.00 16.86 ?  143 CYS   B HB3  1 
ATOM   6355 H  HG   . CYS   B 1 143 ? 36.505 -25.799 -6.825  1.00 17.47 ?  143 CYS   B HG   1 
ATOM   6356 N  N    . VAL   B 1 144 ? 31.914 -26.964 -6.457  1.00 14.76 ?  144 VAL   B N    1 
ATOM   6357 C  CA   . VAL   B 1 144 ? 31.003 -26.907 -7.593  1.00 15.71 ?  144 VAL   B CA   1 
ATOM   6358 C  C    . VAL   B 1 144 ? 29.661 -26.292 -7.219  1.00 15.66 ?  144 VAL   B C    1 
ATOM   6359 O  O    . VAL   B 1 144 ? 29.046 -25.587 -8.030  1.00 16.93 ?  144 VAL   B O    1 
ATOM   6360 C  CB   . VAL   B 1 144 ? 30.833 -28.326 -8.143  1.00 18.25 ?  144 VAL   B CB   1 
ATOM   6361 C  CG1  . VAL   B 1 144 ? 29.531 -28.471 -8.932  1.00 20.88 ?  144 VAL   B CG1  1 
ATOM   6362 C  CG2  . VAL   B 1 144 ? 32.056 -28.737 -8.952  1.00 18.31 ?  144 VAL   B CG2  1 
ATOM   6363 H  H    . VAL   B 1 144 ? 32.155 -27.754 -6.224  1.00 17.74 ?  144 VAL   B H    1 
ATOM   6364 H  HA   . VAL   B 1 144 ? 31.391 -26.360 -8.290  1.00 18.87 ?  144 VAL   B HA   1 
ATOM   6365 H  HB   . VAL   B 1 144 ? 30.776 -28.933 -7.389  1.00 21.92 ?  144 VAL   B HB   1 
ATOM   6366 H  HG11 . VAL   B 1 144 ? 29.596 -29.267 -9.486  1.00 25.08 ?  144 VAL   B HG11 1 
ATOM   6367 H  HG12 . VAL   B 1 144 ? 28.793 -28.566 -8.312  1.00 25.08 ?  144 VAL   B HG12 1 
ATOM   6368 H  HG13 . VAL   B 1 144 ? 29.409 -27.692 -9.491  1.00 25.08 ?  144 VAL   B HG13 1 
ATOM   6369 H  HG21 . VAL   B 1 144 ? 31.923 -29.640 -9.286  1.00 21.99 ?  144 VAL   B HG21 1 
ATOM   6370 H  HG22 . VAL   B 1 144 ? 32.162 -28.124 -9.697  1.00 21.99 ?  144 VAL   B HG22 1 
ATOM   6371 H  HG23 . VAL   B 1 144 ? 32.838 -28.706 -8.383  1.00 21.99 ?  144 VAL   B HG23 1 
ATOM   6372 N  N    . ASP   B 1 145 ? 29.190 -26.535 -6.002  1.00 15.90 ?  145 ASP   B N    1 
ATOM   6373 C  CA   . ASP   B 1 145 ? 27.889 -26.055 -5.570  1.00 16.77 ?  145 ASP   B CA   1 
ATOM   6374 C  C    . ASP   B 1 145 ? 27.926 -24.632 -5.038  1.00 16.53 ?  145 ASP   B C    1 
ATOM   6375 O  O    . ASP   B 1 145 ? 26.869 -24.086 -4.699  1.00 17.97 ?  145 ASP   B O    1 
ATOM   6376 C  CB   . ASP   B 1 145 ? 27.315 -26.957 -4.471  1.00 18.48 ?  145 ASP   B CB   1 
ATOM   6377 C  CG   . ASP   B 1 145 ? 26.938 -28.335 -4.967  1.00 20.53 ?  145 ASP   B CG   1 
ATOM   6378 O  OD1  . ASP   B 1 145 ? 26.812 -28.535 -6.193  1.00 20.67 ?  145 ASP   B OD1  1 
ATOM   6379 O  OD2  . ASP   B 1 145 ? 26.762 -29.223 -4.109  1.00 22.58 -1 145 ASP   B OD2  1 
ATOM   6380 H  H    . ASP   B 1 145 ? 29.623 -26.961 -5.391  1.00 19.10 ?  145 ASP   B H    1 
ATOM   6381 H  HA   . ASP   B 1 145 ? 27.284 -26.057 -6.322  1.00 20.15 ?  145 ASP   B HA   1 
ATOM   6382 H  HB2  . ASP   B 1 145 ? 27.976 -27.070 -3.778  1.00 22.20 ?  145 ASP   B HB2  1 
ATOM   6383 H  HB3  . ASP   B 1 145 ? 26.517 -26.535 -4.108  1.00 22.20 ?  145 ASP   B HB3  1 
ATOM   6384 N  N    . THR   B 1 146 ? 29.104 -24.024 -4.945  1.00 14.63 ?  146 THR   B N    1 
ATOM   6385 C  CA   . THR   B 1 146 ? 29.247 -22.699 -4.348  1.00 14.31 ?  146 THR   B CA   1 
ATOM   6386 C  C    . THR   B 1 146 ? 29.869 -21.672 -5.280  1.00 14.04 ?  146 THR   B C    1 
ATOM   6387 O  O    . THR   B 1 146 ? 29.420 -20.508 -5.324  1.00 14.09 ?  146 THR   B O    1 
ATOM   6388 C  CB   . THR   B 1 146 ? 30.084 -22.798 -3.066  1.00 14.59 ?  146 THR   B CB   1 
ATOM   6389 O  OG1  . THR   B 1 146 ? 29.509 -23.781 -2.195  1.00 14.91 ?  146 THR   B OG1  1 
ATOM   6390 C  CG2  . THR   B 1 146 ? 30.168 -21.463 -2.359  1.00 14.94 ?  146 THR   B CG2  1 
ATOM   6391 H  H    . THR   B 1 146 ? 29.853 -24.353 -5.226  1.00 17.58 ?  146 THR   B H    1 
ATOM   6392 H  HA   . THR   B 1 146 ? 28.377 -22.369 -4.098  1.00 17.19 ?  146 THR   B HA   1 
ATOM   6393 H  HB   . THR   B 1 146 ? 30.992 -23.064 -3.293  1.00 17.53 ?  146 THR   B HB   1 
ATOM   6394 H  HG1  . THR   B 1 146 ? 29.542 -24.543 -2.564  1.00 17.91 ?  146 THR   B HG1  1 
ATOM   6395 H  HG21 . THR   B 1 146 ? 30.515 -21.576 -1.463  1.00 17.95 ?  146 THR   B HG21 1 
ATOM   6396 H  HG22 . THR   B 1 146 ? 30.763 -20.863 -2.848  1.00 17.95 ?  146 THR   B HG22 1 
ATOM   6397 H  HG23 . THR   B 1 146 ? 29.289 -21.057 -2.311  1.00 17.95 ?  146 THR   B HG23 1 
ATOM   6398 N  N    . VAL   B 1 147 ? 30.933 -22.047 -5.982  1.00 13.67 ?  147 VAL   B N    1 
ATOM   6399 C  CA   . VAL   B 1 147 ? 31.660 -21.107 -6.823  1.00 13.48 ?  147 VAL   B CA   1 
ATOM   6400 C  C    . VAL   B 1 147 ? 30.923 -20.969 -8.142  1.00 13.91 ?  147 VAL   B C    1 
ATOM   6401 O  O    . VAL   B 1 147 ? 30.554 -21.969 -8.775  1.00 14.73 ?  147 VAL   B O    1 
ATOM   6402 C  CB   . VAL   B 1 147 ? 33.112 -21.563 -7.031  1.00 13.61 ?  147 VAL   B CB   1 
ATOM   6403 C  CG1  . VAL   B 1 147 ? 33.868 -20.524 -7.835  1.00 13.75 ?  147 VAL   B CG1  1 
ATOM   6404 C  CG2  . VAL   B 1 147 ? 33.793 -21.775 -5.691  1.00 13.82 ?  147 VAL   B CG2  1 
ATOM   6405 H  H    . VAL   B 1 147 ? 31.254 -22.850 -5.994  1.00 16.42 ?  147 VAL   B H    1 
ATOM   6406 H  HA   . VAL   B 1 147 ? 31.676 -20.241 -6.390  1.00 16.20 ?  147 VAL   B HA   1 
ATOM   6407 H  HB   . VAL   B 1 147 ? 33.126 -22.400 -7.526  1.00 16.35 ?  147 VAL   B HB   1 
ATOM   6408 H  HG11 . VAL   B 1 147 ? 34.811 -20.741 -7.833  1.00 16.53 ?  147 VAL   B HG11 1 
ATOM   6409 H  HG12 . VAL   B 1 147 ? 33.532 -20.512 -8.746  1.00 16.53 ?  147 VAL   B HG12 1 
ATOM   6410 H  HG13 . VAL   B 1 147 ? 33.732 -19.649 -7.426  1.00 16.53 ?  147 VAL   B HG13 1 
ATOM   6411 H  HG21 . VAL   B 1 147 ? 34.731 -21.965 -5.840  1.00 16.61 ?  147 VAL   B HG21 1 
ATOM   6412 H  HG22 . VAL   B 1 147 ? 33.695 -20.971 -5.160  1.00 16.61 ?  147 VAL   B HG22 1 
ATOM   6413 H  HG23 . VAL   B 1 147 ? 33.370 -22.524 -5.239  1.00 16.61 ?  147 VAL   B HG23 1 
ATOM   6414 N  N    . ARG   B 1 148 ? 30.714 -19.719 -8.556  1.00 13.96 ?  148 ARG   B N    1 
ATOM   6415 C  CA   . ARG   B 1 148 ? 30.090 -19.395 -9.828  1.00 14.00 ?  148 ARG   B CA   1 
ATOM   6416 C  C    . ARG   B 1 148 ? 31.041 -18.705 -10.796 1.00 14.06 ?  148 ARG   B C    1 
ATOM   6417 O  O    . ARG   B 1 148 ? 30.748 -18.668 -11.994 1.00 15.28 ?  148 ARG   B O    1 
ATOM   6418 C  CB   . ARG   B 1 148 ? 28.845 -18.521 -9.604  1.00 14.34 ?  148 ARG   B CB   1 
ATOM   6419 C  CG   . ARG   B 1 148 ? 27.796 -19.241 -8.774  1.00 15.24 ?  148 ARG   B CG   1 
ATOM   6420 C  CD   . ARG   B 1 148 ? 26.567 -18.382 -8.479  1.00 16.37 ?  148 ARG   B CD   1 
ATOM   6421 N  NE   . ARG   B 1 148 ? 26.925 -17.176 -7.745  1.00 16.25 ?  148 ARG   B NE   1 
ATOM   6422 C  CZ   . ARG   B 1 148 ? 27.241 -17.143 -6.457  1.00 15.39 ?  148 ARG   B CZ   1 
ATOM   6423 N  NH1  . ARG   B 1 148 ? 27.202 -18.234 -5.706  1.00 15.34 ?  148 ARG   B NH1  1 
ATOM   6424 N  NH2  . ARG   B 1 148 ? 27.620 -15.990 -5.912  1.00 15.28 ?  148 ARG   B NH2  1 
ATOM   6425 H  H    . ARG   B 1 148 ? 30.935 -19.019 -8.095  1.00 16.78 ?  148 ARG   B H    1 
ATOM   6426 H  HA   . ARG   B 1 148 ? 29.794 -20.216 -10.242 1.00 16.82 ?  148 ARG   B HA   1 
ATOM   6427 H  HB2  . ARG   B 1 148 ? 29.098 -17.712 -9.132  1.00 17.22 ?  148 ARG   B HB2  1 
ATOM   6428 H  HB3  . ARG   B 1 148 ? 28.450 -18.300 -10.461 1.00 17.22 ?  148 ARG   B HB3  1 
ATOM   6429 H  HG2  . ARG   B 1 148 ? 27.497 -20.030 -9.256  1.00 18.31 ?  148 ARG   B HG2  1 
ATOM   6430 H  HG3  . ARG   B 1 148 ? 28.185 -19.502 -7.925  1.00 18.31 ?  148 ARG   B HG3  1 
ATOM   6431 H  HD2  . ARG   B 1 148 ? 26.153 -18.119 -9.315  1.00 19.66 ?  148 ARG   B HD2  1 
ATOM   6432 H  HD3  . ARG   B 1 148 ? 25.941 -18.892 -7.940  1.00 19.66 ?  148 ARG   B HD3  1 
ATOM   6433 H  HE   . ARG   B 1 148 ? 26.951 -16.436 -8.182  1.00 19.52 ?  148 ARG   B HE   1 
ATOM   6434 H  HH11 . ARG   B 1 148 ? 26.957 -18.987 -6.045  1.00 18.43 ?  148 ARG   B HH11 1 
ATOM   6435 H  HH12 . ARG   B 1 148 ? 27.405 -18.190 -4.870  1.00 18.43 ?  148 ARG   B HH12 1 
ATOM   6436 H  HH21 . ARG   B 1 148 ? 27.657 -15.281 -6.394  1.00 18.36 ?  148 ARG   B HH21 1 
ATOM   6437 H  HH22 . ARG   B 1 148 ? 27.828 -15.957 -5.079  1.00 18.36 ?  148 ARG   B HH22 1 
ATOM   6438 N  N    . THR   B 1 149 ? 32.156 -18.161 -10.308 1.00 13.91 ?  149 THR   B N    1 
ATOM   6439 C  CA   . THR   B 1 149 ? 33.194 -17.594 -11.156 1.00 13.90 ?  149 THR   B CA   1 
ATOM   6440 C  C    . THR   B 1 149 ? 34.072 -18.730 -11.683 1.00 13.47 ?  149 THR   B C    1 
ATOM   6441 O  O    . THR   B 1 149 ? 33.876 -19.904 -11.353 1.00 13.97 ?  149 THR   B O    1 
ATOM   6442 C  CB   . THR   B 1 149 ? 33.968 -16.550 -10.367 1.00 14.03 ?  149 THR   B CB   1 
ATOM   6443 O  OG1  . THR   B 1 149 ? 34.430 -17.161 -9.163  1.00 13.80 ?  149 THR   B OG1  1 
ATOM   6444 C  CG2  . THR   B 1 149 ? 33.086 -15.336 -10.058 1.00 14.67 ?  149 THR   B CG2  1 
ATOM   6445 H  H    . THR   B 1 149 ? 32.329 -18.112 -9.464  1.00 16.71 ?  149 THR   B H    1 
ATOM   6446 H  HA   . THR   B 1 149 ? 32.776 -17.154 -11.910 1.00 16.70 ?  149 THR   B HA   1 
ATOM   6447 H  HB   . THR   B 1 149 ? 34.729 -16.260 -10.881 1.00 16.85 ?  149 THR   B HB   1 
ATOM   6448 H  HG1  . THR   B 1 149 ? 34.847 -16.599 -8.692  1.00 16.58 ?  149 THR   B HG1  1 
ATOM   6449 H  HG21 . THR   B 1 149 ? 33.597 -14.676 -9.563  1.00 17.63 ?  149 THR   B HG21 1 
ATOM   6450 H  HG22 . THR   B 1 149 ? 32.775 -14.938 -10.886 1.00 17.63 ?  149 THR   B HG22 1 
ATOM   6451 H  HG23 . THR   B 1 149 ? 32.320 -15.604 -9.528  1.00 17.63 ?  149 THR   B HG23 1 
ATOM   6452 N  N    . ASN   B 1 150 ? 35.027 -18.401 -12.539 1.00 13.45 ?  150 ASN   B N    1 
ATOM   6453 C  CA   . ASN   B 1 150 ? 35.793 -19.423 -13.241 1.00 14.22 ?  150 ASN   B CA   1 
ATOM   6454 C  C    . ASN   B 1 150 ? 36.958 -19.879 -12.373 1.00 13.28 ?  150 ASN   B C    1 
ATOM   6455 O  O    . ASN   B 1 150 ? 37.895 -19.117 -12.127 1.00 14.14 ?  150 ASN   B O    1 
ATOM   6456 C  CB   . ASN   B 1 150 ? 36.262 -18.896 -14.589 1.00 16.30 ?  150 ASN   B CB   1 
ATOM   6457 C  CG   . ASN   B 1 150 ? 35.115 -18.676 -15.538 1.00 19.31 ?  150 ASN   B CG   1 
ATOM   6458 O  OD1  . ASN   B 1 150 ? 34.188 -19.479 -15.593 1.00 20.48 ?  150 ASN   B OD1  1 
ATOM   6459 N  ND2  . ASN   B 1 150 ? 35.149 -17.576 -16.268 1.00 21.33 ?  150 ASN   B ND2  1 
ATOM   6460 H  H    . ASN   B 1 150 ? 35.253 -17.592 -12.725 1.00 16.16 ?  150 ASN   B H    1 
ATOM   6461 H  HA   . ASN   B 1 150 ? 35.213 -20.189 -13.400 1.00 17.08 ?  150 ASN   B HA   1 
ATOM   6462 H  HB2  . ASN   B 1 150 ? 36.711 -18.046 -14.453 1.00 19.58 ?  150 ASN   B HB2  1 
ATOM   6463 H  HB3  . ASN   B 1 150 ? 36.866 -19.537 -14.984 1.00 19.58 ?  150 ASN   B HB3  1 
ATOM   6464 H  HD21 . ASN   B 1 150 ? 34.515 -17.405 -16.825 1.00 25.62 ?  150 ASN   B HD21 1 
ATOM   6465 H  HD22 . ASN   B 1 150 ? 35.812 -17.030 -16.197 1.00 25.62 ?  150 ASN   B HD22 1 
ATOM   6466 N  N    . VAL   B 1 151 ? 36.905 -21.120 -11.904 1.00 12.98 ?  151 VAL   B N    1 
ATOM   6467 C  CA   . VAL   B 1 151 ? 37.926 -21.658 -11.016 1.00 13.25 ?  151 VAL   B CA   1 
ATOM   6468 C  C    . VAL   B 1 151 ? 38.617 -22.835 -11.693 1.00 13.06 ?  151 VAL   B C    1 
ATOM   6469 O  O    . VAL   B 1 151 ? 37.962 -23.762 -12.196 1.00 14.25 ?  151 VAL   B O    1 
ATOM   6470 C  CB   . VAL   B 1 151 ? 37.370 -22.000 -9.618  1.00 14.21 ?  151 VAL   B CB   1 
ATOM   6471 C  CG1  . VAL   B 1 151 ? 36.197 -22.983 -9.692  1.00 15.70 ?  151 VAL   B CG1  1 
ATOM   6472 C  CG2  . VAL   B 1 151 ? 38.482 -22.514 -8.710  1.00 14.93 ?  151 VAL   B CG2  1 
ATOM   6473 H  H    . VAL   B 1 151 ? 36.273 -21.680 -12.092 1.00 15.60 ?  151 VAL   B H    1 
ATOM   6474 H  HA   . VAL   B 1 151 ? 38.595 -20.966 -10.884 1.00 15.92 ?  151 VAL   B HA   1 
ATOM   6475 H  HB   . VAL   B 1 151 ? 37.031 -21.182 -9.217  1.00 17.07 ?  151 VAL   B HB   1 
ATOM   6476 H  HG11 . VAL   B 1 151 ? 35.882 -23.172 -8.791  1.00 18.87 ?  151 VAL   B HG11 1 
ATOM   6477 H  HG12 . VAL   B 1 151 ? 35.477 -22.584 -10.211 1.00 18.87 ?  151 VAL   B HG12 1 
ATOM   6478 H  HG13 . VAL   B 1 151 ? 36.492 -23.803 -10.115 1.00 18.87 ?  151 VAL   B HG13 1 
ATOM   6479 H  HG21 . VAL   B 1 151 ? 38.138 -22.588 -7.804  1.00 17.94 ?  151 VAL   B HG21 1 
ATOM   6480 H  HG22 . VAL   B 1 151 ? 38.771 -23.384 -9.023  1.00 17.94 ?  151 VAL   B HG22 1 
ATOM   6481 H  HG23 . VAL   B 1 151 ? 39.222 -21.888 -8.730  1.00 17.94 ?  151 VAL   B HG23 1 
ATOM   6482 N  N    . TYR   B 1 152 ? 39.948 -22.761 -11.712 1.00 12.68 ?  152 TYR   B N    1 
ATOM   6483 C  CA   . TYR   B 1 152 ? 40.841 -23.749 -12.298 1.00 13.00 ?  152 TYR   B CA   1 
ATOM   6484 C  C    . TYR   B 1 152 ? 41.560 -24.434 -11.140 1.00 12.33 ?  152 TYR   B C    1 
ATOM   6485 O  O    . TYR   B 1 152 ? 42.414 -23.826 -10.488 1.00 12.78 ?  152 TYR   B O    1 
ATOM   6486 C  CB   . TYR   B 1 152 ? 41.810 -23.042 -13.249 1.00 14.03 ?  152 TYR   B CB   1 
ATOM   6487 C  CG   . TYR   B 1 152 ? 41.126 -22.561 -14.506 1.00 14.57 ?  152 TYR   B CG   1 
ATOM   6488 C  CD1  . TYR   B 1 152 ? 40.492 -21.320 -14.559 1.00 14.94 ?  152 TYR   B CD1  1 
ATOM   6489 C  CD2  . TYR   B 1 152 ? 41.093 -23.361 -15.632 1.00 15.76 ?  152 TYR   B CD2  1 
ATOM   6490 C  CE1  . TYR   B 1 152 ? 39.851 -20.898 -15.711 1.00 16.95 ?  152 TYR   B CE1  1 
ATOM   6491 C  CE2  . TYR   B 1 152 ? 40.457 -22.953 -16.779 1.00 16.78 ?  152 TYR   B CE2  1 
ATOM   6492 C  CZ   . TYR   B 1 152 ? 39.843 -21.717 -16.821 1.00 17.59 ?  152 TYR   B CZ   1 
ATOM   6493 O  OH   . TYR   B 1 152 ? 39.213 -21.321 -17.978 1.00 19.88 ?  152 TYR   B OH   1 
ATOM   6494 H  H    . TYR   B 1 152 ? 40.385 -22.093 -11.367 1.00 15.24 ?  152 TYR   B H    1 
ATOM   6495 H  HA   . TYR   B 1 152 ? 40.329 -24.404 -12.791 1.00 15.62 ?  152 TYR   B HA   1 
ATOM   6496 H  HB2  . TYR   B 1 152 ? 42.187 -22.268 -12.793 1.00 16.86 ?  152 TYR   B HB2  1 
ATOM   6497 H  HB3  . TYR   B 1 152 ? 42.519 -23.650 -13.496 1.00 16.86 ?  152 TYR   B HB3  1 
ATOM   6498 H  HD1  . TYR   B 1 152 ? 40.500 -20.767 -13.805 1.00 17.95 ?  152 TYR   B HD1  1 
ATOM   6499 H  HD2  . TYR   B 1 152 ? 41.506 -24.195 -15.607 1.00 18.93 ?  152 TYR   B HD2  1 
ATOM   6500 H  HE1  . TYR   B 1 152 ? 39.435 -20.065 -15.740 1.00 20.36 ?  152 TYR   B HE1  1 
ATOM   6501 H  HE2  . TYR   B 1 152 ? 40.453 -23.505 -17.528 1.00 20.15 ?  152 TYR   B HE2  1 
ATOM   6502 H  HH   . TYR   B 1 152 ? 38.879 -20.558 -17.869 1.00 23.87 ?  152 TYR   B HH   1 
ATOM   6503 N  N    . LEU   B 1 153 ? 41.195 -25.688 -10.873 1.00 12.41 ?  153 LEU   B N    1 
ATOM   6504 C  CA   . LEU   B 1 153 ? 41.707 -26.436 -9.735  1.00 12.18 ?  153 LEU   B CA   1 
ATOM   6505 C  C    . LEU   B 1 153 ? 42.931 -27.240 -10.140 1.00 12.34 ?  153 LEU   B C    1 
ATOM   6506 O  O    . LEU   B 1 153 ? 42.901 -27.968 -11.132 1.00 13.83 ?  153 LEU   B O    1 
ATOM   6507 C  CB   . LEU   B 1 153 ? 40.630 -27.392 -9.222  1.00 12.70 ?  153 LEU   B CB   1 
ATOM   6508 C  CG   . LEU   B 1 153 ? 39.380 -26.734 -8.642  1.00 13.32 ?  153 LEU   B CG   1 
ATOM   6509 C  CD1  . LEU   B 1 153 ? 38.289 -27.773 -8.469  1.00 14.34 ?  153 LEU   B CD1  1 
ATOM   6510 C  CD2  . LEU   B 1 153 ? 39.684 -26.068 -7.308  1.00 13.79 ?  153 LEU   B CD2  1 
ATOM   6511 H  H    . LEU   B 1 153 ? 40.627 -26.130 -11.350 1.00 14.91 ?  153 LEU   B H    1 
ATOM   6512 H  HA   . LEU   B 1 153 ? 41.941 -25.822 -9.026  1.00 14.64 ?  153 LEU   B HA   1 
ATOM   6513 H  HB2  . LEU   B 1 153 ? 40.342 -27.959 -9.952  1.00 15.26 ?  153 LEU   B HB2  1 
ATOM   6514 H  HB3  . LEU   B 1 153 ? 41.014 -27.938 -8.518  1.00 15.26 ?  153 LEU   B HB3  1 
ATOM   6515 H  HG   . LEU   B 1 153 ? 39.050 -26.051 -9.254  1.00 16.01 ?  153 LEU   B HG   1 
ATOM   6516 H  HD11 . LEU   B 1 153 ? 37.483 -27.338 -8.142  1.00 17.22 ?  153 LEU   B HD11 1 
ATOM   6517 H  HD12 . LEU   B 1 153 ? 38.115 -28.190 -9.324  1.00 17.22 ?  153 LEU   B HD12 1 
ATOM   6518 H  HD13 . LEU   B 1 153 ? 38.588 -28.435 -7.827  1.00 17.22 ?  153 LEU   B HD13 1 
ATOM   6519 H  HD21 . LEU   B 1 153 ? 38.869 -25.696 -6.939  1.00 16.57 ?  153 LEU   B HD21 1 
ATOM   6520 H  HD22 . LEU   B 1 153 ? 40.050 -26.732 -6.702  1.00 16.57 ?  153 LEU   B HD22 1 
ATOM   6521 H  HD23 . LEU   B 1 153 ? 40.335 -25.360 -7.451  1.00 16.57 ?  153 LEU   B HD23 1 
ATOM   6522 N  N    . ALA   B 1 154 ? 43.990 -27.130 -9.348  1.00 12.81 ?  154 ALA   B N    1 
ATOM   6523 C  CA   . ALA   B 1 154 ? 45.218 -27.885 -9.547  1.00 14.09 ?  154 ALA   B CA   1 
ATOM   6524 C  C    . ALA   B 1 154 ? 45.296 -28.964 -8.475  1.00 15.01 ?  154 ALA   B C    1 
ATOM   6525 O  O    . ALA   B 1 154 ? 45.263 -28.663 -7.272  1.00 16.92 ?  154 ALA   B O    1 
ATOM   6526 C  CB   . ALA   B 1 154 ? 46.437 -26.962 -9.505  1.00 15.17 ?  154 ALA   B CB   1 
ATOM   6527 H  H    . ALA   B 1 154 ? 44.013 -26.603 -8.664  1.00 15.39 ?  154 ALA   B H    1 
ATOM   6528 H  HA   . ALA   B 1 154 ? 45.189 -28.311 -10.417 1.00 16.93 ?  154 ALA   B HA   1 
ATOM   6529 H  HB1  . ALA   B 1 154 ? 47.236 -27.491 -9.645  1.00 18.23 ?  154 ALA   B HB1  1 
ATOM   6530 H  HB2  . ALA   B 1 154 ? 46.356 -26.296 -10.211 1.00 18.23 ?  154 ALA   B HB2  1 
ATOM   6531 H  HB3  . ALA   B 1 154 ? 46.474 -26.522 -8.643  1.00 18.23 ?  154 ALA   B HB3  1 
ATOM   6532 N  N    . VAL   B 1 155 ? 45.371 -30.215 -8.910  1.00 14.25 ?  155 VAL   B N    1 
ATOM   6533 C  CA   . VAL   B 1 155 ? 45.480 -31.362 -8.019  1.00 14.53 ?  155 VAL   B CA   1 
ATOM   6534 C  C    . VAL   B 1 155 ? 46.813 -32.039 -8.313  1.00 14.37 ?  155 VAL   B C    1 
ATOM   6535 O  O    . VAL   B 1 155 ? 47.035 -32.532 -9.427  1.00 16.45 ?  155 VAL   B O    1 
ATOM   6536 C  CB   . VAL   B 1 155 ? 44.314 -32.346 -8.203  1.00 16.08 ?  155 VAL   B CB   1 
ATOM   6537 C  CG1  . VAL   B 1 155 ? 44.494 -33.539 -7.278  1.00 16.12 ?  155 VAL   B CG1  1 
ATOM   6538 C  CG2  . VAL   B 1 155 ? 42.988 -31.636 -7.943  1.00 17.40 ?  155 VAL   B CG2  1 
ATOM   6539 H  H    . VAL   B 1 155 ? 45.364 -30.431 -9.745  1.00 17.12 ?  155 VAL   B H    1 
ATOM   6540 H  HA   . VAL   B 1 155 ? 45.480 -31.061 -7.097  1.00 17.45 ?  155 VAL   B HA   1 
ATOM   6541 H  HB   . VAL   B 1 155 ? 44.308 -32.669 -9.120  1.00 19.31 ?  155 VAL   B HB   1 
ATOM   6542 H  HG11 . VAL   B 1 155 ? 43.663 -34.042 -7.244  1.00 19.36 ?  155 VAL   B HG11 1 
ATOM   6543 H  HG12 . VAL   B 1 155 ? 45.204 -34.105 -7.619  1.00 19.36 ?  155 VAL   B HG12 1 
ATOM   6544 H  HG13 . VAL   B 1 155 ? 44.720 -33.220 -6.390  1.00 19.36 ?  155 VAL   B HG13 1 
ATOM   6545 H  HG21 . VAL   B 1 155 ? 42.264 -32.285 -8.007  1.00 20.89 ?  155 VAL   B HG21 1 
ATOM   6546 H  HG22 . VAL   B 1 155 ? 43.003 -31.251 -7.054  1.00 20.89 ?  155 VAL   B HG22 1 
ATOM   6547 H  HG23 . VAL   B 1 155 ? 42.862 -30.940 -8.605  1.00 20.89 ?  155 VAL   B HG23 1 
ATOM   6548 N  N    A PHE   B 1 156 ? 47.676 -32.111 -7.295  0.62 14.71 ?  156 PHE   B N    1 
ATOM   6549 N  N    B PHE   B 1 156 ? 47.704 -32.048 -7.322  0.38 15.01 ?  156 PHE   B N    1 
ATOM   6550 C  CA   A PHE   B 1 156 ? 49.053 -32.574 -7.491  0.62 15.32 ?  156 PHE   B CA   1 
ATOM   6551 C  CA   B PHE   B 1 156 ? 49.080 -32.477 -7.565  0.38 16.00 ?  156 PHE   B CA   1 
ATOM   6552 C  C    A PHE   B 1 156 ? 49.139 -34.080 -7.724  0.62 16.92 ?  156 PHE   B C    1 
ATOM   6553 C  C    B PHE   B 1 156 ? 49.161 -33.961 -7.901  0.38 17.18 ?  156 PHE   B C    1 
ATOM   6554 O  O    A PHE   B 1 156 ? 49.842 -34.540 -8.634  0.62 18.91 ?  156 PHE   B O    1 
ATOM   6555 O  O    B PHE   B 1 156 ? 49.828 -34.355 -8.867  0.38 18.13 ?  156 PHE   B O    1 
ATOM   6556 C  CB   A PHE   B 1 156 ? 49.886 -32.183 -6.273  0.62 14.98 ?  156 PHE   B CB   1 
ATOM   6557 C  CB   B PHE   B 1 156 ? 49.937 -32.152 -6.343  0.38 15.90 ?  156 PHE   B CB   1 
ATOM   6558 C  CG   A PHE   B 1 156 ? 51.312 -32.640 -6.331  0.62 15.65 ?  156 PHE   B CG   1 
ATOM   6559 C  CG   B PHE   B 1 156 ? 51.350 -32.638 -6.445  0.38 16.38 ?  156 PHE   B CG   1 
ATOM   6560 C  CD1  A PHE   B 1 156 ? 52.188 -32.115 -7.265  0.62 17.25 ?  156 PHE   B CD1  1 
ATOM   6561 C  CD1  B PHE   B 1 156 ? 52.194 -32.155 -7.429  0.38 17.56 ?  156 PHE   B CD1  1 
ATOM   6562 C  CD2  A PHE   B 1 156 ? 51.789 -33.569 -5.425  0.62 16.16 ?  156 PHE   B CD2  1 
ATOM   6563 C  CD2  B PHE   B 1 156 ? 51.841 -33.566 -5.546  0.38 16.57 ?  156 PHE   B CD2  1 
ATOM   6564 C  CE1  A PHE   B 1 156 ? 53.507 -32.524 -7.306  0.62 17.87 ?  156 PHE   B CE1  1 
ATOM   6565 C  CE1  B PHE   B 1 156 ? 53.499 -32.596 -7.520  0.38 18.03 ?  156 PHE   B CE1  1 
ATOM   6566 C  CE2  A PHE   B 1 156 ? 53.108 -33.977 -5.462  0.62 17.41 ?  156 PHE   B CE2  1 
ATOM   6567 C  CE2  B PHE   B 1 156 ? 53.147 -34.009 -5.631  0.38 17.42 ?  156 PHE   B CE2  1 
ATOM   6568 C  CZ   A PHE   B 1 156 ? 53.962 -33.456 -6.407  0.62 17.63 ?  156 PHE   B CZ   1 
ATOM   6569 C  CZ   B PHE   B 1 156 ? 53.975 -33.523 -6.622  0.38 17.73 ?  156 PHE   B CZ   1 
ATOM   6570 H  H    A PHE   B 1 156 ? 47.488 -31.900 -6.482  0.62 17.67 ?  156 PHE   B H    1 
ATOM   6571 H  H    B PHE   B 1 156 ? 47.538 -31.820 -6.510  0.38 18.03 ?  156 PHE   B H    1 
ATOM   6572 H  HA   A PHE   B 1 156 ? 49.424 -32.130 -8.265  0.62 18.41 ?  156 PHE   B HA   1 
ATOM   6573 H  HA   B PHE   B 1 156 ? 49.433 -31.984 -8.317  0.38 19.22 ?  156 PHE   B HA   1 
ATOM   6574 H  HB2  A PHE   B 1 156 ? 49.887 -31.217 -6.198  0.62 17.99 ?  156 PHE   B HB2  1 
ATOM   6575 H  HB2  B PHE   B 1 156 ? 49.962 -31.188 -6.233  0.38 19.10 ?  156 PHE   B HB2  1 
ATOM   6576 H  HB3  A PHE   B 1 156 ? 49.483 -32.573 -5.481  0.62 17.99 ?  156 PHE   B HB3  1 
ATOM   6577 H  HB3  B PHE   B 1 156 ? 49.537 -32.561 -5.560  0.38 19.10 ?  156 PHE   B HB3  1 
ATOM   6578 H  HD1  A PHE   B 1 156 ? 51.883 -31.483 -7.879  0.62 20.72 ?  156 PHE   B HD1  1 
ATOM   6579 H  HD1  B PHE   B 1 156 ? 51.876 -31.526 -8.039  0.38 21.09 ?  156 PHE   B HD1  1 
ATOM   6580 H  HD2  A PHE   B 1 156 ? 51.212 -33.928 -4.788  0.62 19.41 ?  156 PHE   B HD2  1 
ATOM   6581 H  HD2  B PHE   B 1 156 ? 51.284 -33.898 -4.877  0.38 19.91 ?  156 PHE   B HD2  1 
ATOM   6582 H  HE1  A PHE   B 1 156 ? 54.085 -32.169 -7.944  0.62 21.47 ?  156 PHE   B HE1  1 
ATOM   6583 H  HE1  B PHE   B 1 156 ? 54.056 -32.265 -8.187  0.38 21.65 ?  156 PHE   B HE1  1 
ATOM   6584 H  HE2  A PHE   B 1 156 ? 53.417 -34.613 -4.855  0.62 20.91 ?  156 PHE   B HE2  1 
ATOM   6585 H  HE2  B PHE   B 1 156 ? 53.465 -34.638 -5.024  0.38 20.92 ?  156 PHE   B HE2  1 
ATOM   6586 H  HZ   A PHE   B 1 156 ? 54.849 -33.733 -6.434  0.62 21.17 ?  156 PHE   B HZ   1 
ATOM   6587 H  HZ   B PHE   B 1 156 ? 54.854 -33.821 -6.682  0.38 21.29 ?  156 PHE   B HZ   1 
ATOM   6588 N  N    A ASP   B 1 157 ? 48.471 -34.869 -6.892  0.62 17.11 ?  157 ASP   B N    1 
ATOM   6589 N  N    B ASP   B 1 157 ? 48.497 -34.798 -7.114  0.38 17.68 ?  157 ASP   B N    1 
ATOM   6590 C  CA   A ASP   B 1 157 ? 48.614 -36.320 -6.944  0.62 18.62 ?  157 ASP   B CA   1 
ATOM   6591 C  CA   B ASP   B 1 157 ? 48.621 -36.243 -7.241  0.38 18.25 ?  157 ASP   B CA   1 
ATOM   6592 C  C    A ASP   B 1 157 ? 47.693 -36.889 -8.018  0.62 18.50 ?  157 ASP   B C    1 
ATOM   6593 C  C    B ASP   B 1 157 ? 47.734 -36.741 -8.376  0.38 18.52 ?  157 ASP   B C    1 
ATOM   6594 O  O    A ASP   B 1 157 ? 46.469 -36.777 -7.911  0.62 17.32 ?  157 ASP   B O    1 
ATOM   6595 O  O    B ASP   B 1 157 ? 46.523 -36.499 -8.376  0.38 18.41 ?  157 ASP   B O    1 
ATOM   6596 C  CB   A ASP   B 1 157 ? 48.275 -36.899 -5.574  0.62 20.27 ?  157 ASP   B CB   1 
ATOM   6597 C  CB   B ASP   B 1 157 ? 48.209 -36.890 -5.922  0.38 18.44 ?  157 ASP   B CB   1 
ATOM   6598 C  CG   A ASP   B 1 157 ? 48.392 -38.408 -5.524  0.62 22.76 ?  157 ASP   B CG   1 
ATOM   6599 C  CG   B ASP   B 1 157 ? 48.435 -38.392 -5.914  0.38 19.02 ?  157 ASP   B CG   1 
ATOM   6600 O  OD1  A ASP   B 1 157 ? 48.892 -39.016 -6.495  0.62 23.46 ?  157 ASP   B OD1  1 
ATOM   6601 O  OD1  B ASP   B 1 157 ? 48.689 -38.981 -6.991  0.38 18.71 ?  157 ASP   B OD1  1 
ATOM   6602 O  OD2  A ASP   B 1 157 ? 47.973 -38.989 -4.502  0.62 24.81 -1 157 ASP   B OD2  1 
ATOM   6603 O  OD2  B ASP   B 1 157 ? 48.375 -38.988 -4.820  0.38 19.98 -1 157 ASP   B OD2  1 
ATOM   6604 H  H    A ASP   B 1 157 ? 47.918 -34.595 -6.298  0.62 20.55 ?  157 ASP   B H    1 
ATOM   6605 H  H    B ASP   B 1 157 ? 47.960 -34.551 -6.493  0.38 21.24 ?  157 ASP   B H    1 
ATOM   6606 H  HA   A ASP   B 1 157 ? 49.529 -36.555 -7.165  0.62 22.36 ?  157 ASP   B HA   1 
ATOM   6607 H  HA   B ASP   B 1 157 ? 49.541 -36.486 -7.431  0.38 21.92 ?  157 ASP   B HA   1 
ATOM   6608 H  HB2  A ASP   B 1 157 ? 48.867 -36.507 -4.912  0.62 24.34 ?  157 ASP   B HB2  1 
ATOM   6609 H  HB2  B ASP   B 1 157 ? 48.727 -36.491 -5.199  0.38 22.15 ?  157 ASP   B HB2  1 
ATOM   6610 H  HB3  A ASP   B 1 157 ? 47.359 -36.689 -5.360  0.62 24.34 ?  157 ASP   B HB3  1 
ATOM   6611 H  HB3  B ASP   B 1 157 ? 47.262 -36.715 -5.767  0.38 22.15 ?  157 ASP   B HB3  1 
ATOM   6612 N  N    A LYS   B 1 158 ? 48.287 -37.510 -9.045  0.62 20.16 ?  158 LYS   B N    1 
ATOM   6613 N  N    B LYS   B 1 158 ? 48.331 -37.457 -9.333  0.38 19.40 ?  158 LYS   B N    1 
ATOM   6614 C  CA   A LYS   B 1 158 ? 47.522 -38.114 -10.138 0.62 21.42 ?  158 LYS   B CA   1 
ATOM   6615 C  CA   B LYS   B 1 158 ? 47.547 -38.025 -10.426 0.38 20.89 ?  158 LYS   B CA   1 
ATOM   6616 C  C    A LYS   B 1 158 ? 46.455 -39.076 -9.627  0.62 21.11 ?  158 LYS   B C    1 
ATOM   6617 C  C    B LYS   B 1 158 ? 46.481 -38.982 -9.906  0.38 20.87 ?  158 LYS   B C    1 
ATOM   6618 O  O    A LYS   B 1 158 ? 45.344 -39.131 -10.169 0.62 21.33 ?  158 LYS   B O    1 
ATOM   6619 O  O    B LYS   B 1 158 ? 45.395 -39.080 -10.490 0.38 20.85 ?  158 LYS   B O    1 
ATOM   6620 C  CB   A LYS   B 1 158 ? 48.482 -38.837 -11.092 0.62 23.28 ?  158 LYS   B CB   1 
ATOM   6621 C  CB   B LYS   B 1 158 ? 48.478 -38.743 -11.407 0.38 22.73 ?  158 LYS   B CB   1 
ATOM   6622 C  CG   A LYS   B 1 158 ? 47.826 -39.754 -12.121 0.62 25.64 ?  158 LYS   B CG   1 
ATOM   6623 C  CG   B LYS   B 1 158 ? 47.776 -39.656 -12.401 0.38 24.64 ?  158 LYS   B CG   1 
ATOM   6624 C  CD   A LYS   B 1 158 ? 46.973 -38.988 -13.117 0.62 27.44 ?  158 LYS   B CD   1 
ATOM   6625 C  CD   B LYS   B 1 158 ? 46.867 -38.884 -13.334 0.38 26.26 ?  158 LYS   B CD   1 
ATOM   6626 C  CE   A LYS   B 1 158 ? 46.373 -39.925 -14.157 0.62 29.17 ?  158 LYS   B CE   1 
ATOM   6627 C  CE   B LYS   B 1 158 ? 46.264 -39.801 -14.385 0.38 27.57 ?  158 LYS   B CE   1 
ATOM   6628 N  NZ   A LYS   B 1 158 ? 45.316 -39.264 -14.977 0.62 29.68 ?  158 LYS   B NZ   1 
ATOM   6629 N  NZ   B LYS   B 1 158 ? 45.204 -39.115 -15.173 0.38 27.97 ?  158 LYS   B NZ   1 
ATOM   6630 H  H    A LYS   B 1 158 ? 49.135 -37.592 -9.127  0.62 24.22 ?  158 LYS   B H    1 
ATOM   6631 H  H    B LYS   B 1 158 ? 49.174 -37.638 -9.363  0.38 23.30 ?  158 LYS   B H    1 
ATOM   6632 H  HA   A LYS   B 1 158 ? 47.078 -37.416 -10.638 0.62 25.73 ?  158 LYS   B HA   1 
ATOM   6633 H  HA   B LYS   B 1 158 ? 47.108 -37.305 -10.903 0.38 25.09 ?  158 LYS   B HA   1 
ATOM   6634 H  HB2  A LYS   B 1 158 ? 48.988 -38.168 -11.585 0.62 27.96 ?  158 LYS   B HB2  1 
ATOM   6635 H  HB2  B LYS   B 1 158 ? 48.964 -38.074 -11.918 0.38 27.30 ?  158 LYS   B HB2  1 
ATOM   6636 H  HB3  A LYS   B 1 158 ? 49.093 -39.378 -10.568 0.62 27.96 ?  158 LYS   B HB3  1 
ATOM   6637 H  HB3  B LYS   B 1 158 ? 49.105 -39.284 -10.902 0.38 27.30 ?  158 LYS   B HB3  1 
ATOM   6638 H  HG2  A LYS   B 1 158 ? 48.524 -40.209 -12.619 0.62 30.79 ?  158 LYS   B HG2  1 
ATOM   6639 H  HG2  B LYS   B 1 158 ? 48.446 -40.101 -12.941 0.38 29.59 ?  158 LYS   B HG2  1 
ATOM   6640 H  HG3  A LYS   B 1 158 ? 47.267 -40.410 -11.676 0.62 30.79 ?  158 LYS   B HG3  1 
ATOM   6641 H  HG3  B LYS   B 1 158 ? 47.245 -40.317 -11.929 0.38 29.59 ?  158 LYS   B HG3  1 
ATOM   6642 H  HD2  A LYS   B 1 158 ? 46.248 -38.546 -12.650 0.62 32.95 ?  158 LYS   B HD2  1 
ATOM   6643 H  HD2  B LYS   B 1 158 ? 46.145 -38.485 -12.824 0.38 31.53 ?  158 LYS   B HD2  1 
ATOM   6644 H  HD3  A LYS   B 1 158 ? 47.524 -38.336 -13.579 0.62 32.95 ?  158 LYS   B HD3  1 
ATOM   6645 H  HD3  B LYS   B 1 158 ? 47.381 -38.195 -13.785 0.38 31.53 ?  158 LYS   B HD3  1 
ATOM   6646 H  HE2  A LYS   B 1 158 ? 47.072 -40.224 -14.758 0.62 35.02 ?  158 LYS   B HE2  1 
ATOM   6647 H  HE2  B LYS   B 1 158 ? 46.962 -40.086 -14.997 0.38 33.10 ?  158 LYS   B HE2  1 
ATOM   6648 H  HE3  A LYS   B 1 158 ? 45.974 -40.687 -13.709 0.62 35.02 ?  158 LYS   B HE3  1 
ATOM   6649 H  HE3  B LYS   B 1 158 ? 45.870 -40.572 -13.947 0.38 33.10 ?  158 LYS   B HE3  1 
ATOM   6650 H  HZ1  A LYS   B 1 158 ? 44.986 -39.838 -15.572 0.62 35.63 ?  158 LYS   B HZ1  1 
ATOM   6651 H  HZ1  B LYS   B 1 158 ? 44.868 -39.672 -15.779 0.38 33.58 ?  158 LYS   B HZ1  1 
ATOM   6652 H  HZ2  A LYS   B 1 158 ? 44.655 -38.981 -14.451 0.62 35.63 ?  158 LYS   B HZ2  1 
ATOM   6653 H  HZ2  B LYS   B 1 158 ? 44.550 -38.847 -14.631 0.38 33.58 ?  158 LYS   B HZ2  1 
ATOM   6654 H  HZ3  A LYS   B 1 158 ? 45.659 -38.565 -15.409 0.62 35.63 ?  158 LYS   B HZ3  1 
ATOM   6655 H  HZ3  B LYS   B 1 158 ? 45.545 -38.405 -15.587 0.38 33.58 ?  158 LYS   B HZ3  1 
ATOM   6656 N  N    A ASN   B 1 159 ? 46.780 -39.871 -8.609  0.62 21.22 ?  159 ASN   B N    1 
ATOM   6657 N  N    B ASN   B 1 159 ? 46.776 -39.704 -8.823  0.38 20.89 ?  159 ASN   B N    1 
ATOM   6658 C  CA   A ASN   B 1 159 ? 45.807 -40.836 -8.108  0.62 21.54 ?  159 ASN   B CA   1 
ATOM   6659 C  CA   B ASN   B 1 159 ? 45.831 -40.690 -8.305  0.38 20.93 ?  159 ASN   B CA   1 
ATOM   6660 C  C    A ASN   B 1 159 ? 44.632 -40.141 -7.429  0.62 20.48 ?  159 ASN   B C    1 
ATOM   6661 C  C    B ASN   B 1 159 ? 44.631 -40.024 -7.630  0.38 20.18 ?  159 ASN   B C    1 
ATOM   6662 O  O    A ASN   B 1 159 ? 43.507 -40.656 -7.449  0.62 20.74 ?  159 ASN   B O    1 
ATOM   6663 O  O    B ASN   B 1 159 ? 43.487 -40.451 -7.830  0.38 20.17 ?  159 ASN   B O    1 
ATOM   6664 C  CB   A ASN   B 1 159 ? 46.491 -41.820 -7.162  0.62 23.12 ?  159 ASN   B CB   1 
ATOM   6665 C  CB   B ASN   B 1 159 ? 46.555 -41.657 -7.364  0.38 21.61 ?  159 ASN   B CB   1 
ATOM   6666 C  CG   A ASN   B 1 159 ? 47.534 -42.667 -7.861  0.62 25.10 ?  159 ASN   B CG   1 
ATOM   6667 C  CG   B ASN   B 1 159 ? 47.537 -42.558 -8.098  0.38 22.72 ?  159 ASN   B CG   1 
ATOM   6668 O  OD1  A ASN   B 1 159 ? 47.304 -43.168 -8.966  0.62 25.80 ?  159 ASN   B OD1  1 
ATOM   6669 O  OD1  B ASN   B 1 159 ? 47.266 -43.015 -9.212  0.38 23.11 ?  159 ASN   B OD1  1 
ATOM   6670 N  ND2  A ASN   B 1 159 ? 48.692 -42.831 -7.222  0.62 25.92 ?  159 ASN   B ND2  1 
ATOM   6671 N  ND2  B ASN   B 1 159 ? 48.686 -42.818 -7.476  0.38 23.16 ?  159 ASN   B ND2  1 
ATOM   6672 H  H    A ASN   B 1 159 ? 47.536 -39.871 -8.205  0.62 25.49 ?  159 ASN   B H    1 
ATOM   6673 H  H    B ASN   B 1 159 ? 47.515 -39.649 -8.390  0.38 25.08 ?  159 ASN   B H    1 
ATOM   6674 H  HA   A ASN   B 1 159 ? 45.461 -41.345 -8.863  0.62 25.87 ?  159 ASN   B HA   1 
ATOM   6675 H  HA   B ASN   B 1 159 ? 45.498 -41.213 -9.052  0.38 25.14 ?  159 ASN   B HA   1 
ATOM   6676 H  HB2  A ASN   B 1 159 ? 46.928 -41.326 -6.453  0.62 27.76 ?  159 ASN   B HB2  1 
ATOM   6677 H  HB2  B ASN   B 1 159 ? 47.055 -41.152 -6.706  0.38 25.95 ?  159 ASN   B HB2  1 
ATOM   6678 H  HB3  A ASN   B 1 159 ? 45.822 -42.417 -6.793  0.62 27.76 ?  159 ASN   B HB3  1 
ATOM   6679 H  HB3  B ASN   B 1 159 ? 45.903 -42.225 -6.925  0.38 25.95 ?  159 ASN   B HB3  1 
ATOM   6680 H  HD21 A ASN   B 1 159 ? 49.318 -43.306 -7.574  0.62 31.12 ?  159 ASN   B HD21 1 
ATOM   6681 H  HD21 B ASN   B 1 159 ? 49.274 -43.326 -7.848  0.38 27.81 ?  159 ASN   B HD21 1 
ATOM   6682 H  HD22 A ASN   B 1 159 ? 48.812 -42.475 -6.447  0.62 31.12 ?  159 ASN   B HD22 1 
ATOM   6683 H  HD22 B ASN   B 1 159 ? 48.841 -42.486 -6.697  0.38 27.81 ?  159 ASN   B HD22 1 
ATOM   6684 N  N    . LEU   B 1 160 ? 44.861 -38.972 -6.834  1.00 20.12 ?  160 LEU   B N    1 
ATOM   6685 C  CA   . LEU   B 1 160 ? 43.742 -38.229 -6.268  1.00 19.35 ?  160 LEU   B CA   1 
ATOM   6686 C  C    . LEU   B 1 160 ? 42.941 -37.558 -7.370  1.00 18.49 ?  160 LEU   B C    1 
ATOM   6687 O  O    . LEU   B 1 160 ? 41.704 -37.554 -7.328  1.00 18.44 ?  160 LEU   B O    1 
ATOM   6688 C  CB   . LEU   B 1 160 ? 44.225 -37.199 -5.248  1.00 18.81 ?  160 LEU   B CB   1 
ATOM   6689 C  CG   . LEU   B 1 160 ? 43.097 -36.295 -4.728  1.00 18.50 ?  160 LEU   B CG   1 
ATOM   6690 C  CD1  . LEU   B 1 160 ? 41.976 -37.106 -4.096  1.00 19.51 ?  160 LEU   B CD1  1 
ATOM   6691 C  CD2  . LEU   B 1 160 ? 43.639 -35.264 -3.744  1.00 18.71 ?  160 LEU   B CD2  1 
ATOM   6692 H  H    A LEU   B 1 160 ? 45.631 -38.605 -6.749  0.62 24.16 ?  160 LEU   B H    1 
ATOM   6693 H  H    B LEU   B 1 160 ? 45.638 -38.673 -6.631  0.38 24.16 ?  160 LEU   B H    1 
ATOM   6694 H  HA   . LEU   B 1 160 ? 43.155 -38.851 -5.814  1.00 23.24 ?  160 LEU   B HA   1 
ATOM   6695 H  HB2  . LEU   B 1 160 ? 44.612 -37.671 -4.491  1.00 22.60 ?  160 LEU   B HB2  1 
ATOM   6696 H  HB3  . LEU   B 1 160 ? 44.900 -36.639 -5.665  1.00 22.60 ?  160 LEU   B HB3  1 
ATOM   6697 H  HG   . LEU   B 1 160 ? 42.722 -35.810 -5.478  1.00 22.22 ?  160 LEU   B HG   1 
ATOM   6698 H  HD11 . LEU   B 1 160 ? 41.360 -36.501 -3.663  1.00 23.43 ?  160 LEU   B HD11 1 
ATOM   6699 H  HD12 . LEU   B 1 160 ? 41.515 -37.610 -4.788  1.00 23.43 ?  160 LEU   B HD12 1 
ATOM   6700 H  HD13 . LEU   B 1 160 ? 42.356 -37.718 -3.444  1.00 23.43 ?  160 LEU   B HD13 1 
ATOM   6701 H  HD21 . LEU   B 1 160 ? 42.910 -34.691 -3.465  1.00 22.48 ?  160 LEU   B HD21 1 
ATOM   6702 H  HD22 . LEU   B 1 160 ? 44.015 -35.725 -2.980  1.00 22.48 ?  160 LEU   B HD22 1 
ATOM   6703 H  HD23 . LEU   B 1 160 ? 44.325 -34.738 -4.186  1.00 22.48 ?  160 LEU   B HD23 1 
ATOM   6704 N  N    A TYR   B 1 161 ? 43.631 -36.994 -8.365  0.62 18.61 ?  161 TYR   B N    1 
ATOM   6705 N  N    B TYR   B 1 161 ? 43.625 -37.002 -8.377  0.38 18.52 ?  161 TYR   B N    1 
ATOM   6706 C  CA   A TYR   B 1 161 ? 42.952 -36.436 -9.528  0.62 18.26 ?  161 TYR   B CA   1 
ATOM   6707 C  CA   B TYR   B 1 161 ? 42.930 -36.431 -9.527  0.38 18.28 ?  161 TYR   B CA   1 
ATOM   6708 C  C    A TYR   B 1 161 ? 41.996 -37.458 -10.125 0.62 18.02 ?  161 TYR   B C    1 
ATOM   6709 C  C    B TYR   B 1 161 ? 41.993 -37.455 -10.148 0.38 18.18 ?  161 TYR   B C    1 
ATOM   6710 O  O    A TYR   B 1 161 ? 40.819 -37.163 -10.355 0.62 17.93 ?  161 TYR   B O    1 
ATOM   6711 O  O    B TYR   B 1 161 ? 40.827 -37.157 -10.431 0.38 18.15 ?  161 TYR   B O    1 
ATOM   6712 C  CB   A TYR   B 1 161 ? 43.990 -35.983 -10.563 0.62 18.37 ?  161 TYR   B CB   1 
ATOM   6713 C  CB   B TYR   B 1 161 ? 43.941 -35.921 -10.563 0.38 18.35 ?  161 TYR   B CB   1 
ATOM   6714 C  CG   A TYR   B 1 161 ? 43.411 -35.505 -11.874 0.62 18.83 ?  161 TYR   B CG   1 
ATOM   6715 C  CG   B TYR   B 1 161 ? 43.323 -35.450 -11.869 0.38 18.90 ?  161 TYR   B CG   1 
ATOM   6716 C  CD1  A TYR   B 1 161 ? 43.036 -34.177 -12.043 0.62 18.71 ?  161 TYR   B CD1  1 
ATOM   6717 C  CD1  B TYR   B 1 161 ? 42.919 -34.129 -12.032 0.38 18.97 ?  161 TYR   B CD1  1 
ATOM   6718 C  CD2  A TYR   B 1 161 ? 43.236 -36.377 -12.944 0.62 19.38 ?  161 TYR   B CD2  1 
ATOM   6719 C  CD2  B TYR   B 1 161 ? 43.144 -36.325 -12.937 0.38 19.17 ?  161 TYR   B CD2  1 
ATOM   6720 C  CE1  A TYR   B 1 161 ? 42.506 -33.733 -13.234 0.62 19.79 ?  161 TYR   B CE1  1 
ATOM   6721 C  CE1  B TYR   B 1 161 ? 42.352 -33.693 -13.217 0.38 19.66 ?  161 TYR   B CE1  1 
ATOM   6722 C  CE2  A TYR   B 1 161 ? 42.704 -35.941 -14.140 0.62 20.66 ?  161 TYR   B CE2  1 
ATOM   6723 C  CE2  B TYR   B 1 161 ? 42.576 -35.897 -14.126 0.38 20.05 ?  161 TYR   B CE2  1 
ATOM   6724 C  CZ   A TYR   B 1 161 ? 42.341 -34.619 -14.280 0.62 20.67 ?  161 TYR   B CZ   1 
ATOM   6725 C  CZ   B TYR   B 1 161 ? 42.185 -34.581 -14.261 0.38 20.18 ?  161 TYR   B CZ   1 
ATOM   6726 O  OH   A TYR   B 1 161 ? 41.810 -34.177 -15.468 0.62 22.72 ?  161 TYR   B OH   1 
ATOM   6727 O  OH   B TYR   B 1 161 ? 41.618 -34.150 -15.440 0.38 21.45 ?  161 TYR   B OH   1 
ATOM   6728 H  H    A TYR   B 1 161 ? 44.486 -36.939 -8.397  0.62 22.35 ?  161 TYR   B H    1 
ATOM   6729 H  H    B TYR   B 1 161 ? 44.482 -36.955 -8.420  0.38 22.24 ?  161 TYR   B H    1 
ATOM   6730 H  HA   A TYR   B 1 161 ? 42.436 -35.664 -9.259  0.62 21.93 ?  161 TYR   B HA   1 
ATOM   6731 H  HA   B TYR   B 1 161 ? 42.396 -35.678 -9.234  0.38 21.96 ?  161 TYR   B HA   1 
ATOM   6732 H  HB2  A TYR   B 1 161 ? 44.503 -35.252 -10.186 0.62 22.06 ?  161 TYR   B HB2  1 
ATOM   6733 H  HB2  B TYR   B 1 161 ? 44.424 -35.171 -10.182 0.38 22.04 ?  161 TYR   B HB2  1 
ATOM   6734 H  HB3  A TYR   B 1 161 ? 44.580 -36.728 -10.760 0.62 22.06 ?  161 TYR   B HB3  1 
ATOM   6735 H  HB3  B TYR   B 1 161 ? 44.561 -36.636 -10.774 0.38 22.04 ?  161 TYR   B HB3  1 
ATOM   6736 H  HD1  A TYR   B 1 161 ? 43.146 -33.576 -11.341 0.62 22.47 ?  161 TYR   B HD1  1 
ATOM   6737 H  HD1  B TYR   B 1 161 ? 43.028 -33.526 -11.334 0.38 22.78 ?  161 TYR   B HD1  1 
ATOM   6738 H  HD2  A TYR   B 1 161 ? 43.477 -37.271 -12.856 0.62 23.27 ?  161 TYR   B HD2  1 
ATOM   6739 H  HD2  B TYR   B 1 161 ? 43.405 -37.213 -12.854 0.38 23.02 ?  161 TYR   B HD2  1 
ATOM   6740 H  HE1  A TYR   B 1 161 ? 42.261 -32.838 -13.329 0.62 23.77 ?  161 TYR   B HE1  1 
ATOM   6741 H  HE1  B TYR   B 1 161 ? 42.087 -32.804 -13.310 0.38 23.62 ?  161 TYR   B HE1  1 
ATOM   6742 H  HE2  A TYR   B 1 161 ? 42.589 -36.530 -14.848 0.62 24.81 ?  161 TYR   B HE2  1 
ATOM   6743 H  HE2  B TYR   B 1 161 ? 42.463 -36.492 -14.832 0.38 24.08 ?  161 TYR   B HE2  1 
ATOM   6744 H  HH   A TYR   B 1 161 ? 41.634 -33.354 -15.418 0.62 27.29 ?  161 TYR   B HH   1 
ATOM   6745 H  HH   B TYR   B 1 161 ? 41.577 -34.784 -15.989 0.38 25.75 ?  161 TYR   B HH   1 
ATOM   6746 N  N    . ASP   B 1 162 ? 42.486 -38.679 -10.357 1.00 18.71 ?  162 ASP   B N    1 
ATOM   6747 C  CA   . ASP   B 1 162 ? 41.647 -39.716 -10.948 1.00 19.19 ?  162 ASP   B CA   1 
ATOM   6748 C  C    . ASP   B 1 162 ? 40.451 -40.039 -10.060 1.00 18.94 ?  162 ASP   B C    1 
ATOM   6749 O  O    . ASP   B 1 162 ? 39.338 -40.238 -10.560 1.00 19.48 ?  162 ASP   B O    1 
ATOM   6750 C  CB   . ASP   B 1 162 ? 42.468 -40.982 -11.201 1.00 20.65 ?  162 ASP   B CB   1 
ATOM   6751 C  CG   . ASP   B 1 162 ? 43.485 -40.821 -12.313 1.00 22.49 ?  162 ASP   B CG   1 
ATOM   6752 O  OD1  . ASP   B 1 162 ? 43.371 -39.876 -13.114 1.00 23.10 ?  162 ASP   B OD1  1 
ATOM   6753 O  OD2  . ASP   B 1 162 ? 44.380 -41.688 -12.413 1.00 24.32 -1 162 ASP   B OD2  1 
ATOM   6754 H  H    A ASP   B 1 162 ? 43.288 -38.928 -10.184 0.62 22.47 ?  162 ASP   B H    1 
ATOM   6755 H  H    B ASP   B 1 162 ? 43.284 -38.929 -10.170 0.38 22.47 ?  162 ASP   B H    1 
ATOM   6756 H  HA   . ASP   B 1 162 ? 41.303 -39.405 -11.797 1.00 23.05 ?  162 ASP   B HA   1 
ATOM   6757 H  HB2  . ASP   B 1 162 ? 42.951 -41.216 -10.398 1.00 24.81 ?  162 ASP   B HB2  1 
ATOM   6758 H  HB3  . ASP   B 1 162 ? 41.870 -41.703 -11.456 1.00 24.81 ?  162 ASP   B HB3  1 
ATOM   6759 N  N    . LYS   B 1 163 ? 40.660 -40.117 -8.743  1.00 18.35 ?  163 LYS   B N    1 
ATOM   6760 C  CA   . LYS   B 1 163 ? 39.544 -40.387 -7.841  1.00 19.07 ?  163 LYS   B CA   1 
ATOM   6761 C  C    . LYS   B 1 163 ? 38.509 -39.266 -7.895  1.00 17.60 ?  163 LYS   B C    1 
ATOM   6762 O  O    . LYS   B 1 163 ? 37.295 -39.524 -7.887  1.00 18.61 ?  163 LYS   B O    1 
ATOM   6763 C  CB   . LYS   B 1 163 ? 40.057 -40.571 -6.414  1.00 22.28 ?  163 LYS   B CB   1 
ATOM   6764 C  CG   . LYS   B 1 163 ? 38.986 -41.009 -5.437  1.00 28.26 ?  163 LYS   B CG   1 
ATOM   6765 C  CD   . LYS   B 1 163 ? 39.529 -41.180 -4.030  1.00 34.30 ?  163 LYS   B CD   1 
ATOM   6766 C  CE   . LYS   B 1 163 ? 38.475 -41.798 -3.120  1.00 38.80 ?  163 LYS   B CE   1 
ATOM   6767 N  NZ   . LYS   B 1 163 ? 38.806 -41.656 -1.675  1.00 41.37 ?  163 LYS   B NZ   1 
ATOM   6768 H  H    . LYS   B 1 163 ? 41.425 -40.021 -8.357  1.00 22.03 ?  163 LYS   B H    1 
ATOM   6769 H  HA   . LYS   B 1 163 ? 39.112 -41.208 -8.110  1.00 22.91 ?  163 LYS   B HA   1 
ATOM   6770 H  HB2  . LYS   B 1 163 ? 40.751 -41.252 -6.414  1.00 26.76 ?  163 LYS   B HB2  1 
ATOM   6771 H  HB3  . LYS   B 1 163 ? 40.422 -39.732 -6.096  1.00 26.76 ?  163 LYS   B HB3  1 
ATOM   6772 H  HG2  . LYS   B 1 163 ? 38.287 -40.339 -5.410  1.00 33.93 ?  163 LYS   B HG2  1 
ATOM   6773 H  HG3  . LYS   B 1 163 ? 38.622 -41.861 -5.727  1.00 33.93 ?  163 LYS   B HG3  1 
ATOM   6774 H  HD2  . LYS   B 1 163 ? 40.299 -41.771 -4.052  1.00 41.18 ?  163 LYS   B HD2  1 
ATOM   6775 H  HD3  . LYS   B 1 163 ? 39.775 -40.314 -3.673  1.00 41.18 ?  163 LYS   B HD3  1 
ATOM   6776 H  HE2  . LYS   B 1 163 ? 37.622 -41.367 -3.280  1.00 46.58 ?  163 LYS   B HE2  1 
ATOM   6777 H  HE3  . LYS   B 1 163 ? 38.406 -42.744 -3.321  1.00 46.58 ?  163 LYS   B HE3  1 
ATOM   6778 H  HZ1  . LYS   B 1 163 ? 38.166 -42.028 -1.180  1.00 49.67 ?  163 LYS   B HZ1  1 
ATOM   6779 H  HZ2  . LYS   B 1 163 ? 39.579 -42.060 -1.499  1.00 49.67 ?  163 LYS   B HZ2  1 
ATOM   6780 H  HZ3  . LYS   B 1 163 ? 38.873 -40.795 -1.461  1.00 49.67 ?  163 LYS   B HZ3  1 
ATOM   6781 N  N    . LEU   B 1 164 ? 38.972 -38.016 -7.953  1.00 16.31 ?  164 LEU   B N    1 
ATOM   6782 C  CA   . LEU   B 1 164 ? 38.065 -36.873 -8.005  1.00 16.02 ?  164 LEU   B CA   1 
ATOM   6783 C  C    . LEU   B 1 164 ? 37.263 -36.854 -9.301  1.00 16.68 ?  164 LEU   B C    1 
ATOM   6784 O  O    . LEU   B 1 164 ? 36.043 -36.640 -9.286  1.00 17.66 ?  164 LEU   B O    1 
ATOM   6785 C  CB   . LEU   B 1 164 ? 38.867 -35.581 -7.854  1.00 15.40 ?  164 LEU   B CB   1 
ATOM   6786 C  CG   . LEU   B 1 164 ? 39.430 -35.314 -6.463  1.00 16.01 ?  164 LEU   B CG   1 
ATOM   6787 C  CD1  . LEU   B 1 164 ? 40.494 -34.230 -6.538  1.00 16.18 ?  164 LEU   B CD1  1 
ATOM   6788 C  CD2  . LEU   B 1 164 ? 38.329 -34.902 -5.505  1.00 17.69 ?  164 LEU   B CD2  1 
ATOM   6789 H  H    . LEU   B 1 164 ? 39.811 -37.802 -7.965  1.00 19.60 ?  164 LEU   B H    1 
ATOM   6790 H  HA   . LEU   B 1 164 ? 37.444 -36.931 -7.269  1.00 19.25 ?  164 LEU   B HA   1 
ATOM   6791 H  HB2  . LEU   B 1 164 ? 39.618 -35.608 -8.472  1.00 18.50 ?  164 LEU   B HB2  1 
ATOM   6792 H  HB3  . LEU   B 1 164 ? 38.292 -34.834 -8.081  1.00 18.50 ?  164 LEU   B HB3  1 
ATOM   6793 H  HG   . LEU   B 1 164 ? 39.848 -36.123 -6.126  1.00 19.23 ?  164 LEU   B HG   1 
ATOM   6794 H  HD11 . LEU   B 1 164 ? 40.840 -34.062 -5.646  1.00 19.43 ?  164 LEU   B HD11 1 
ATOM   6795 H  HD12 . LEU   B 1 164 ? 41.216 -34.529 -7.117  1.00 19.43 ?  164 LEU   B HD12 1 
ATOM   6796 H  HD13 . LEU   B 1 164 ? 40.099 -33.421 -6.896  1.00 19.43 ?  164 LEU   B HD13 1 
ATOM   6797 H  HD21 . LEU   B 1 164 ? 38.721 -34.678 -4.649  1.00 21.25 ?  164 LEU   B HD21 1 
ATOM   6798 H  HD22 . LEU   B 1 164 ? 37.865 -34.134 -5.870  1.00 21.25 ?  164 LEU   B HD22 1 
ATOM   6799 H  HD23 . LEU   B 1 164 ? 37.709 -35.644 -5.402  1.00 21.25 ?  164 LEU   B HD23 1 
ATOM   6800 N  N    . VAL   B 1 165 ? 37.936 -37.035 -10.438 1.00 18.10 ?  165 VAL   B N    1 
ATOM   6801 C  CA   . VAL   B 1 165 ? 37.254 -36.965 -11.726 1.00 19.70 ?  165 VAL   B CA   1 
ATOM   6802 C  C    . VAL   B 1 165 ? 36.314 -38.150 -11.890 1.00 22.18 ?  165 VAL   B C    1 
ATOM   6803 O  O    . VAL   B 1 165 ? 35.144 -37.997 -12.264 1.00 23.64 ?  165 VAL   B O    1 
ATOM   6804 C  CB   . VAL   B 1 165 ? 38.274 -36.908 -12.877 1.00 20.97 ?  165 VAL   B CB   1 
ATOM   6805 C  CG1  . VAL   B 1 165 ? 37.568 -37.037 -14.202 1.00 22.44 ?  165 VAL   B CG1  1 
ATOM   6806 C  CG2  . VAL   B 1 165 ? 39.080 -35.623 -12.823 1.00 20.73 ?  165 VAL   B CG2  1 
ATOM   6807 H  H    . VAL   B 1 165 ? 38.786 -37.185 -10.491 1.00 21.74 ?  165 VAL   B H    1 
ATOM   6808 H  HA   . VAL   B 1 165 ? 36.726 -36.153 -11.761 1.00 23.66 ?  165 VAL   B HA   1 
ATOM   6809 H  HB   . VAL   B 1 165 ? 38.896 -37.649 -12.789 1.00 25.19 ?  165 VAL   B HB   1 
ATOM   6810 H  HG11 . VAL   B 1 165 ? 38.149 -36.723 -14.906 1.00 26.95 ?  165 VAL   B HG11 1 
ATOM   6811 H  HG12 . VAL   B 1 165 ? 37.358 -37.974 -14.349 1.00 26.95 ?  165 VAL   B HG12 1 
ATOM   6812 H  HG13 . VAL   B 1 165 ? 36.752 -36.518 -14.179 1.00 26.95 ?  165 VAL   B HG13 1 
ATOM   6813 H  HG21 . VAL   B 1 165 ? 39.687 -35.598 -13.582 1.00 24.90 ?  165 VAL   B HG21 1 
ATOM   6814 H  HG22 . VAL   B 1 165 ? 38.472 -34.867 -12.866 1.00 24.90 ?  165 VAL   B HG22 1 
ATOM   6815 H  HG23 . VAL   B 1 165 ? 39.584 -35.596 -11.996 1.00 24.90 ?  165 VAL   B HG23 1 
ATOM   6816 N  N    . SER   B 1 166 ? 36.829 -39.357 -11.623 1.00 23.30 ?  166 SER   B N    1 
ATOM   6817 C  CA   . SER   B 1 166 ? 36.074 -40.570 -11.907 1.00 25.01 ?  166 SER   B CA   1 
ATOM   6818 C  C    . SER   B 1 166 ? 34.821 -40.655 -11.053 1.00 25.37 ?  166 SER   B C    1 
ATOM   6819 O  O    . SER   B 1 166 ? 33.845 -41.274 -11.469 1.00 27.09 ?  166 SER   B O    1 
ATOM   6820 C  CB   . SER   B 1 166 ? 36.946 -41.826 -11.742 1.00 25.77 ?  166 SER   B CB   1 
ATOM   6821 O  OG   . SER   B 1 166 ? 37.343 -42.036 -10.398 1.00 26.09 ?  166 SER   B OG   1 
ATOM   6822 H  H    . SER   B 1 166 ? 37.611 -39.496 -11.295 1.00 27.98 ?  166 SER   B H    1 
ATOM   6823 H  HA   . SER   B 1 166 ? 35.790 -40.547 -12.834 1.00 30.03 ?  166 SER   B HA   1 
ATOM   6824 H  HB2  . SER   B 1 166 ? 36.441 -42.598 -12.039 1.00 30.95 ?  166 SER   B HB2  1 
ATOM   6825 H  HB3  . SER   B 1 166 ? 37.742 -41.727 -12.291 1.00 30.95 ?  166 SER   B HB3  1 
ATOM   6826 H  HG   . SER   B 1 166 ? 37.792 -41.375 -10.130 1.00 31.33 ?  166 SER   B HG   1 
ATOM   6827 N  N    . SER   B 1 167 ? 34.813 -40.038 -9.877  1.00 23.46 ?  167 SER   B N    1 
ATOM   6828 C  CA   . SER   B 1 167 ? 33.667 -40.086 -8.977  1.00 23.30 ?  167 SER   B CA   1 
ATOM   6829 C  C    . SER   B 1 167 ? 32.761 -38.857 -9.061  1.00 22.61 ?  167 SER   B C    1 
ATOM   6830 O  O    . SER   B 1 167 ? 31.684 -38.861 -8.456  1.00 23.20 ?  167 SER   B O    1 
ATOM   6831 C  CB   . SER   B 1 167 ? 34.134 -40.274 -7.526  1.00 23.30 ?  167 SER   B CB   1 
ATOM   6832 O  OG   . SER   B 1 167 ? 34.802 -39.112 -7.041  1.00 23.24 ?  167 SER   B OG   1 
ATOM   6833 H  H    . SER   B 1 167 ? 35.464 -39.582 -9.579  1.00 28.17 ?  167 SER   B H    1 
ATOM   6834 H  HA   . SER   B 1 167 ? 33.123 -40.861 -9.212  1.00 27.98 ?  167 SER   B HA   1 
ATOM   6835 H  HB2  . SER   B 1 167 ? 33.354 -40.461 -6.974  1.00 27.97 ?  167 SER   B HB2  1 
ATOM   6836 H  HB3  . SER   B 1 167 ? 34.740 -41.036 -7.495  1.00 27.97 ?  167 SER   B HB3  1 
ATOM   6837 H  HG   . SER   B 1 167 ? 35.467 -38.960 -7.514  1.00 27.91 ?  167 SER   B HG   1 
ATOM   6838 N  N    . PHE   B 1 168 ? 33.155 -37.804 -9.783  1.00 22.17 ?  168 PHE   B N    1 
ATOM   6839 C  CA   . PHE   B 1 168 ? 32.314 -36.606 -9.856  1.00 20.35 ?  168 PHE   B CA   1 
ATOM   6840 C  C    . PHE   B 1 168 ? 31.025 -36.877 -10.630 1.00 17.20 ?  168 PHE   B C    1 
ATOM   6841 O  O    . PHE   B 1 168 ? 29.953 -36.324 -10.305 1.00 17.35 ?  168 PHE   B O    1 
ATOM   6842 C  CB   . PHE   B 1 168 ? 33.087 -35.465 -10.513 1.00 21.11 ?  168 PHE   B CB   1 
ATOM   6843 C  CG   . PHE   B 1 168 ? 32.275 -34.232 -10.690 1.00 21.23 ?  168 PHE   B CG   1 
ATOM   6844 C  CD1  . PHE   B 1 168 ? 31.916 -33.477 -9.585  1.00 22.05 ?  168 PHE   B CD1  1 
ATOM   6845 C  CD2  . PHE   B 1 168 ? 31.849 -33.833 -11.941 1.00 20.61 ?  168 PHE   B CD2  1 
ATOM   6846 C  CE1  . PHE   B 1 168 ? 31.146 -32.346 -9.720  1.00 22.01 ?  168 PHE   B CE1  1 
ATOM   6847 C  CE2  . PHE   B 1 168 ? 31.091 -32.680 -12.090 1.00 21.68 ?  168 PHE   B CE2  1 
ATOM   6848 C  CZ   . PHE   B 1 168 ? 30.731 -31.937 -10.973 1.00 21.43 ?  168 PHE   B CZ   1 
ATOM   6849 H  H    . PHE   B 1 168 ? 33.886 -37.759 -10.230 1.00 26.62 ?  168 PHE   B H    1 
ATOM   6850 H  HA   . PHE   B 1 168 ? 32.072 -36.333 -8.959  1.00 24.44 ?  168 PHE   B HA   1 
ATOM   6851 H  HB2  . PHE   B 1 168 ? 33.849 -35.243 -9.957  1.00 25.35 ?  168 PHE   B HB2  1 
ATOM   6852 H  HB3  . PHE   B 1 168 ? 33.386 -35.750 -11.390 1.00 25.35 ?  168 PHE   B HB3  1 
ATOM   6853 H  HD1  . PHE   B 1 168 ? 32.187 -33.754 -8.740  1.00 26.47 ?  168 PHE   B HD1  1 
ATOM   6854 H  HD2  . PHE   B 1 168 ? 32.086 -34.325 -12.689 1.00 24.75 ?  168 PHE   B HD2  1 
ATOM   6855 H  HE1  . PHE   B 1 168 ? 30.914 -31.854 -8.967  1.00 26.43 ?  168 PHE   B HE1  1 
ATOM   6856 H  HE2  . PHE   B 1 168 ? 30.804 -32.414 -12.935 1.00 26.04 ?  168 PHE   B HE2  1 
ATOM   6857 H  HZ   . PHE   B 1 168 ? 30.214 -31.170 -11.068 1.00 25.73 ?  168 PHE   B HZ   1 
ATOM   6858 N  N    . LEU   B 1 169 ? 31.110 -37.732 -11.645 1.00 18.04 ?  169 LEU   B N    1 
ATOM   6859 C  CA   . LEU   B 1 169 ? 29.959 -38.089 -12.468 1.00 20.85 ?  169 LEU   B CA   1 
ATOM   6860 C  C    . LEU   B 1 169 ? 29.943 -39.537 -12.933 1.00 24.10 ?  169 LEU   B C    1 
ATOM   6861 O  O    . LEU   B 1 169 ? 29.030 -39.962 -13.645 1.00 26.35 ?  169 LEU   B O    1 
ATOM   6862 C  CB   . LEU   B 1 169 ? 29.904 -37.192 -13.699 1.00 23.01 ?  169 LEU   B CB   1 
ATOM   6863 C  CG   . LEU   B 1 169 ? 28.672 -36.297 -13.794 1.00 25.92 ?  169 LEU   B CG   1 
ATOM   6864 C  CD1  . LEU   B 1 169 ? 28.602 -35.691 -15.174 1.00 26.83 ?  169 LEU   B CD1  1 
ATOM   6865 C  CD2  . LEU   B 1 169 ? 27.389 -37.059 -13.468 1.00 26.22 ?  169 LEU   B CD2  1 
ATOM   6866 O  OXT  . LEU   B 1 169 ? 30.837 -40.308 -12.620 1.00 25.20 -1 169 LEU   B OXT  1 
ATOM   6867 H  H    . LEU   B 1 169 ? 31.839 -38.119 -11.886 1.00 21.66 ?  169 LEU   B H    1 
ATOM   6868 H  HA   . LEU   B 1 169 ? 29.165 -37.947 -11.939 1.00 25.04 ?  169 LEU   B HA   1 
ATOM   6869 H  HB2  . LEU   B 1 169 ? 30.684 -36.614 -13.704 1.00 27.63 ?  169 LEU   B HB2  1 
ATOM   6870 H  HB3  . LEU   B 1 169 ? 29.911 -37.752 -14.492 1.00 27.63 ?  169 LEU   B HB3  1 
ATOM   6871 H  HG   . LEU   B 1 169 ? 28.757 -35.572 -13.153 1.00 31.13 ?  169 LEU   B HG   1 
ATOM   6872 H  HD11 . LEU   B 1 169 ? 27.836 -35.099 -15.219 1.00 32.21 ?  169 LEU   B HD11 1 
ATOM   6873 H  HD12 . LEU   B 1 169 ? 29.417 -35.194 -15.338 1.00 32.21 ?  169 LEU   B HD12 1 
ATOM   6874 H  HD13 . LEU   B 1 169 ? 28.510 -36.404 -15.824 1.00 32.21 ?  169 LEU   B HD13 1 
ATOM   6875 H  HD21 . LEU   B 1 169 ? 26.647 -36.645 -13.930 1.00 31.48 ?  169 LEU   B HD21 1 
ATOM   6876 H  HD22 . LEU   B 1 169 ? 27.490 -37.981 -13.761 1.00 31.48 ?  169 LEU   B HD22 1 
ATOM   6877 H  HD23 . LEU   B 1 169 ? 27.241 -37.035 -12.509 1.00 31.48 ?  169 LEU   B HD23 1 
HETATM 6878 N  N2   B A1BBK C 2 .   ? 15.566 3.630   5.911   0.38 15.10 ?  201 A1BBK A N2   1 
HETATM 6879 C  C3   B A1BBK C 2 .   ? 15.112 1.265   3.171   0.38 15.45 ?  201 A1BBK A C3   1 
HETATM 6880 C  C6   B A1BBK C 2 .   ? 15.730 4.526   4.825   0.38 14.47 ?  201 A1BBK A C6   1 
HETATM 6881 C  C9   B A1BBK C 2 .   ? 13.004 -1.431  -0.320  0.38 19.12 ?  201 A1BBK A C9   1 
HETATM 6882 C  C12  B A1BBK C 2 .   ? 12.478 0.732   0.908   0.38 19.63 ?  201 A1BBK A C12  1 
HETATM 6883 C  C1   B A1BBK C 2 .   ? 13.349 -0.539  0.958   0.38 18.30 ?  201 A1BBK A C1   1 
HETATM 6884 C  C10  B A1BBK C 2 .   ? 11.398 0.266   -0.891  0.38 20.26 ?  201 A1BBK A C10  1 
HETATM 6885 C  C11  B A1BBK C 2 .   ? 11.048 0.218   0.621   0.38 20.08 ?  201 A1BBK A C11  1 
HETATM 6886 C  C13  B A1BBK C 2 .   ? 12.558 1.284   -0.564  0.38 20.14 ?  201 A1BBK A C13  1 
HETATM 6887 C  C2   B A1BBK C 2 .   ? 14.841 -0.022  1.009   0.38 17.06 ?  201 A1BBK A C2   1 
HETATM 6888 C  C4   B A1BBK C 2 .   ? 15.346 2.489   3.890   0.38 15.01 ?  201 A1BBK A C4   1 
HETATM 6889 C  C5   B A1BBK C 2 .   ? 15.611 3.861   3.615   0.38 15.01 ?  201 A1BBK A C5   1 
HETATM 6890 C  C7   B A1BBK C 2 .   ? 15.325 2.386   5.302   0.38 14.91 ?  201 A1BBK A C7   1 
HETATM 6891 C  C8   B A1BBK C 2 .   ? 14.911 0.184   5.240   0.38 15.84 ?  201 A1BBK A C8   1 
HETATM 6892 N  N1   B A1BBK C 2 .   ? 15.100 1.205   1.774   0.38 15.95 ?  201 A1BBK A N1   1 
HETATM 6893 N  N3   B A1BBK C 2 .   ? 15.103 1.250   6.024   0.38 15.56 ?  201 A1BBK A N3   1 
HETATM 6894 N  N4   B A1BBK C 2 .   ? 14.894 0.119   3.869   0.38 15.79 ?  201 A1BBK A N4   1 
HETATM 6895 O  O1   B A1BBK C 2 .   ? 13.056 -1.202  2.180   0.38 17.83 ?  201 A1BBK A O1   1 
HETATM 6896 O  O2   B A1BBK C 2 .   ? 11.999 -0.954  -1.202  0.38 20.31 ?  201 A1BBK A O2   1 
HETATM 6897 H  H7   B A1BBK C 2 .   ? 15.598 3.842   6.862   0.38 18.14 ?  201 A1BBK A H7   1 
HETATM 6898 H  H6   B A1BBK C 2 .   ? 15.924 5.558   5.072   0.38 17.39 ?  201 A1BBK A H6   1 
HETATM 6899 H  H10  B A1BBK C 2 .   ? 13.864 -1.599  -0.978  0.38 22.97 ?  201 A1BBK A H10  1 
HETATM 6900 H  H9   B A1BBK C 2 .   ? 12.701 -2.456  -0.021  0.38 22.97 ?  201 A1BBK A H9   1 
HETATM 6901 H  H14  B A1BBK C 2 .   ? 12.528 1.415   1.741   0.38 23.57 ?  201 A1BBK A H14  1 
HETATM 6902 H  H11  B A1BBK C 2 .   ? 10.550 0.578   -1.504  0.38 24.33 ?  201 A1BBK A H11  1 
HETATM 6903 H  H13  B A1BBK C 2 .   ? 10.806 -0.796  0.975   0.38 24.12 ?  201 A1BBK A H13  1 
HETATM 6904 H  H12  B A1BBK C 2 .   ? 10.313 0.915   0.937   0.38 24.12 ?  201 A1BBK A H12  1 
HETATM 6905 H  H15  B A1BBK C 2 .   ? 12.330 2.348   -0.691  0.38 24.19 ?  201 A1BBK A H15  1 
HETATM 6906 H  H16  B A1BBK C 2 .   ? 13.479 1.134   -1.140  0.38 24.19 ?  201 A1BBK A H16  1 
HETATM 6907 H  H2   B A1BBK C 2 .   ? 15.200 0.062   -0.039  0.38 20.50 ?  201 A1BBK A H2   1 
HETATM 6908 H  H3   B A1BBK C 2 .   ? 15.415 -0.879  1.441   0.38 20.50 ?  201 A1BBK A H3   1 
HETATM 6909 H  H5   B A1BBK C 2 .   ? 15.687 4.320   2.648   0.38 18.04 ?  201 A1BBK A H5   1 
HETATM 6910 H  H8   B A1BBK C 2 .   ? 14.721 -0.761  5.823   0.38 19.03 ?  201 A1BBK A H8   1 
HETATM 6911 H  H4   B A1BBK C 2 .   ? 15.272 2.045   1.245   0.38 19.16 ?  201 A1BBK A H4   1 
HETATM 6912 H  H1   B A1BBK C 2 .   ? 13.543 -2.027  2.237   0.38 21.41 ?  201 A1BBK A H1   1 
HETATM 6913 CL CL   B CL    D 3 .   ? 15.970 2.699   -1.111  0.38 15.25 ?  202 CL    A CL   1 
HETATM 6914 O  O    A HOH   E 4 .   ? 14.719 -4.560  20.345  0.62 37.15 ?  301 HOH   A O    1 
HETATM 6915 O  O    . HOH   E 4 .   ? 4.659  3.753   0.516   1.00 30.43 ?  302 HOH   A O    1 
HETATM 6916 O  O    . HOH   E 4 .   ? 18.572 -2.420  -16.460 1.00 46.97 ?  303 HOH   A O    1 
HETATM 6917 O  O    . HOH   E 4 .   ? 15.166 -12.240 18.605  1.00 51.45 ?  304 HOH   A O    1 
HETATM 6918 O  O    . HOH   E 4 .   ? 11.671 -10.790 -10.096 1.00 53.70 ?  305 HOH   A O    1 
HETATM 6919 O  O    . HOH   E 4 .   ? 34.286 -1.861  12.484  1.00 38.78 ?  306 HOH   A O    1 
HETATM 6920 O  O    . HOH   E 4 .   ? 9.088  -10.074 19.192  1.00 45.87 ?  307 HOH   A O    1 
HETATM 6921 O  O    . HOH   E 4 .   ? 28.928 0.509   -9.745  1.00 23.24 ?  308 HOH   A O    1 
HETATM 6922 O  O    . HOH   E 4 .   ? -0.424 -3.061  2.988   1.00 42.85 ?  309 HOH   A O    1 
HETATM 6923 O  O    . HOH   E 4 .   ? 8.131  -21.562 3.984   1.00 54.58 ?  310 HOH   A O    1 
HETATM 6924 O  O    . HOH   E 4 .   ? 17.029 -17.897 14.994  1.00 31.29 ?  311 HOH   A O    1 
HETATM 6925 O  O    . HOH   E 4 .   ? 18.929 -21.947 6.986   1.00 35.91 ?  312 HOH   A O    1 
HETATM 6926 O  O    . HOH   E 4 .   ? 26.861 11.462  1.601   1.00 18.09 ?  313 HOH   A O    1 
HETATM 6927 O  O    . HOH   E 4 .   ? 30.205 -13.273 -8.429  1.00 26.36 ?  314 HOH   A O    1 
HETATM 6928 O  O    . HOH   E 4 .   ? 0.635  -4.649  0.022   1.00 33.55 ?  315 HOH   A O    1 
HETATM 6929 O  O    . HOH   E 4 .   ? 14.663 -13.849 16.685  1.00 34.17 ?  316 HOH   A O    1 
HETATM 6930 O  O    . HOH   E 4 .   ? 16.987 -19.241 4.888   1.00 16.82 ?  317 HOH   A O    1 
HETATM 6931 O  O    . HOH   E 4 .   ? 24.115 -7.683  14.372  1.00 18.02 ?  318 HOH   A O    1 
HETATM 6932 O  O    . HOH   E 4 .   ? 28.148 -6.228  19.544  1.00 45.03 ?  319 HOH   A O    1 
HETATM 6933 O  O    A HOH   E 4 .   ? 12.233 0.281   14.778  0.62 26.70 ?  320 HOH   A O    1 
HETATM 6934 O  O    . HOH   E 4 .   ? 14.070 -22.992 7.355   1.00 20.77 ?  321 HOH   A O    1 
HETATM 6935 O  O    . HOH   E 4 .   ? 38.150 10.252  7.067   1.00 52.33 ?  322 HOH   A O    1 
HETATM 6936 O  O    . HOH   E 4 .   ? 42.322 10.543  4.957   1.00 20.71 ?  323 HOH   A O    1 
HETATM 6937 O  O    . HOH   E 4 .   ? 7.911  -12.649 -1.002  1.00 22.92 ?  324 HOH   A O    1 
HETATM 6938 O  O    . HOH   E 4 .   ? 6.799  -8.071  11.695  1.00 22.73 ?  325 HOH   A O    1 
HETATM 6939 O  O    . HOH   E 4 .   ? 17.544 -1.757  0.357   1.00 24.15 ?  326 HOH   A O    1 
HETATM 6940 O  O    . HOH   E 4 .   ? 37.445 2.810   10.247  1.00 25.73 ?  327 HOH   A O    1 
HETATM 6941 O  O    . HOH   E 4 .   ? 36.141 -5.098  -0.495  1.00 31.88 ?  328 HOH   A O    1 
HETATM 6942 O  O    . HOH   E 4 .   ? 23.785 -15.753 -9.161  1.00 39.31 ?  329 HOH   A O    1 
HETATM 6943 O  O    . HOH   E 4 .   ? 22.243 5.359   18.987  1.00 44.32 ?  330 HOH   A O    1 
HETATM 6944 O  O    . HOH   E 4 .   ? 26.506 -19.320 -1.752  1.00 15.93 ?  331 HOH   A O    1 
HETATM 6945 O  O    . HOH   E 4 .   ? 9.904  -21.370 5.613   1.00 21.09 ?  332 HOH   A O    1 
HETATM 6946 O  O    . HOH   E 4 .   ? 24.537 1.979   -7.024  1.00 21.75 ?  333 HOH   A O    1 
HETATM 6947 O  O    . HOH   E 4 .   ? 19.960 -12.605 -8.824  1.00 27.83 ?  334 HOH   A O    1 
HETATM 6948 O  O    . HOH   E 4 .   ? 19.045 -11.070 24.054  1.00 87.01 ?  335 HOH   A O    1 
HETATM 6949 O  O    . HOH   E 4 .   ? 18.681 -19.339 13.504  1.00 34.31 ?  336 HOH   A O    1 
HETATM 6950 O  O    . HOH   E 4 .   ? 14.929 4.055   17.540  1.00 42.95 ?  337 HOH   A O    1 
HETATM 6951 O  O    . HOH   E 4 .   ? 21.265 -2.418  -2.294  1.00 17.14 ?  338 HOH   A O    1 
HETATM 6952 O  O    . HOH   E 4 .   ? 13.540 -15.256 -7.687  1.00 29.26 ?  339 HOH   A O    1 
HETATM 6953 O  O    . HOH   E 4 .   ? 7.562  -6.383  -6.664  1.00 41.00 ?  340 HOH   A O    1 
HETATM 6954 O  O    . HOH   E 4 .   ? 43.322 7.736   2.674   1.00 43.75 ?  341 HOH   A O    1 
HETATM 6955 O  O    . HOH   E 4 .   ? 28.323 -0.140  -13.408 1.00 37.08 ?  342 HOH   A O    1 
HETATM 6956 O  O    . HOH   E 4 .   ? 44.290 7.213   6.439   1.00 28.23 ?  343 HOH   A O    1 
HETATM 6957 O  O    . HOH   E 4 .   ? 42.563 4.339   5.548   1.00 36.47 ?  344 HOH   A O    1 
HETATM 6958 O  O    . HOH   E 4 .   ? 31.605 8.242   14.779  1.00 28.61 ?  345 HOH   A O    1 
HETATM 6959 O  O    . HOH   E 4 .   ? -0.626 -8.579  2.066   1.00 46.47 ?  346 HOH   A O    1 
HETATM 6960 O  O    . HOH   E 4 .   ? 10.904 1.694   12.428  1.00 26.48 ?  347 HOH   A O    1 
HETATM 6961 O  O    . HOH   E 4 .   ? 34.044 -1.185  -8.964  1.00 28.77 ?  348 HOH   A O    1 
HETATM 6962 O  O    . HOH   E 4 .   ? 3.482  -9.225  9.834   1.00 35.08 ?  349 HOH   A O    1 
HETATM 6963 O  O    . HOH   E 4 .   ? 31.042 -18.077 7.788   1.00 18.97 ?  350 HOH   A O    1 
HETATM 6964 O  O    . HOH   E 4 .   ? 22.502 -11.932 21.831  1.00 59.16 ?  351 HOH   A O    1 
HETATM 6965 O  O    . HOH   E 4 .   ? 38.503 4.972   7.013   1.00 15.73 ?  352 HOH   A O    1 
HETATM 6966 O  O    A HOH   E 4 .   ? 14.232 0.589   6.714   0.62 20.31 ?  353 HOH   A O    1 
HETATM 6967 O  O    . HOH   E 4 .   ? 22.708 12.523  1.535   1.00 16.07 ?  354 HOH   A O    1 
HETATM 6968 O  O    . HOH   E 4 .   ? 14.117 -4.691  -11.963 1.00 33.32 ?  355 HOH   A O    1 
HETATM 6969 O  O    . HOH   E 4 .   ? 27.393 13.819  2.724   1.00 31.34 ?  356 HOH   A O    1 
HETATM 6970 O  O    . HOH   E 4 .   ? 14.377 -21.308 -4.270  1.00 29.97 ?  357 HOH   A O    1 
HETATM 6971 O  O    . HOH   E 4 .   ? 39.767 -1.033  -5.158  1.00 21.69 ?  358 HOH   A O    1 
HETATM 6972 O  O    . HOH   E 4 .   ? 37.161 -2.782  9.745   1.00 46.13 ?  359 HOH   A O    1 
HETATM 6973 O  O    . HOH   E 4 .   ? 13.841 -4.872  17.395  1.00 30.34 ?  360 HOH   A O    1 
HETATM 6974 O  O    . HOH   E 4 .   ? 20.640 -19.792 -5.108  1.00 30.15 ?  361 HOH   A O    1 
HETATM 6975 O  O    . HOH   E 4 .   ? 24.022 -2.120  -2.135  1.00 11.75 ?  362 HOH   A O    1 
HETATM 6976 O  O    . HOH   E 4 .   ? 22.026 -19.247 11.389  1.00 38.72 ?  363 HOH   A O    1 
HETATM 6977 O  O    . HOH   E 4 .   ? 35.750 -12.591 6.873   1.00 16.20 ?  364 HOH   A O    1 
HETATM 6978 O  O    . HOH   E 4 .   ? 25.715 -0.816  -7.364  1.00 16.95 ?  365 HOH   A O    1 
HETATM 6979 O  O    . HOH   E 4 .   ? 31.103 -13.931 -2.432  1.00 15.04 ?  366 HOH   A O    1 
HETATM 6980 O  O    . HOH   E 4 .   ? 17.144 -17.821 -5.145  1.00 29.04 ?  367 HOH   A O    1 
HETATM 6981 O  O    . HOH   E 4 .   ? 27.348 -10.511 14.076  1.00 18.48 ?  368 HOH   A O    1 
HETATM 6982 O  O    . HOH   E 4 .   ? 18.487 9.485   8.986   1.00 24.31 ?  369 HOH   A O    1 
HETATM 6983 O  O    . HOH   E 4 .   ? 30.736 3.121   8.261   1.00 13.33 ?  370 HOH   A O    1 
HETATM 6984 O  O    . HOH   E 4 .   ? 24.401 3.579   -1.853  1.00 17.04 ?  371 HOH   A O    1 
HETATM 6985 O  O    . HOH   E 4 .   ? 33.622 -7.138  4.331   1.00 17.46 ?  372 HOH   A O    1 
HETATM 6986 O  O    . HOH   E 4 .   ? 10.336 -22.197 -1.336  1.00 51.30 ?  373 HOH   A O    1 
HETATM 6987 O  O    . HOH   E 4 .   ? 31.846 -9.398  -6.688  1.00 25.55 ?  374 HOH   A O    1 
HETATM 6988 O  O    . HOH   E 4 .   ? 21.802 -21.866 8.445   1.00 30.52 ?  375 HOH   A O    1 
HETATM 6989 O  O    . HOH   E 4 .   ? 16.515 -22.082 0.913   1.00 31.41 ?  376 HOH   A O    1 
HETATM 6990 O  O    . HOH   E 4 .   ? 6.622  -3.220  12.709  1.00 32.72 ?  377 HOH   A O    1 
HETATM 6991 O  O    . HOH   E 4 .   ? 26.913 4.183   -0.708  1.00 13.53 ?  378 HOH   A O    1 
HETATM 6992 O  O    . HOH   E 4 .   ? 21.327 3.076   -0.327  1.00 14.15 ?  379 HOH   A O    1 
HETATM 6993 O  O    . HOH   E 4 .   ? 13.361 -1.483  -6.797  1.00 18.18 ?  380 HOH   A O    1 
HETATM 6994 O  O    . HOH   E 4 .   ? 37.212 12.004  4.869   1.00 27.81 ?  381 HOH   A O    1 
HETATM 6995 O  O    A HOH   E 4 .   ? 18.934 -0.666  -1.699  0.62 13.14 ?  382 HOH   A O    1 
HETATM 6996 O  O    . HOH   E 4 .   ? 24.584 -17.459 12.739  1.00 25.39 ?  383 HOH   A O    1 
HETATM 6997 O  O    . HOH   E 4 .   ? 21.111 10.342  14.915  1.00 36.77 ?  384 HOH   A O    1 
HETATM 6998 O  O    . HOH   E 4 .   ? 14.564 -3.666  2.930   1.00 18.95 ?  385 HOH   A O    1 
HETATM 6999 O  O    . HOH   E 4 .   ? 15.822 2.199   24.512  1.00 46.52 ?  386 HOH   A O    1 
HETATM 7000 O  O    . HOH   E 4 .   ? 20.093 4.516   -7.643  1.00 22.88 ?  387 HOH   A O    1 
HETATM 7001 O  O    . HOH   E 4 .   ? 23.431 11.408  4.022   1.00 12.97 ?  388 HOH   A O    1 
HETATM 7002 O  O    . HOH   E 4 .   ? 44.018 8.611   -2.896  1.00 29.06 ?  389 HOH   A O    1 
HETATM 7003 O  O    . HOH   E 4 .   ? 31.879 -7.238  -9.841  1.00 22.92 ?  390 HOH   A O    1 
HETATM 7004 O  O    . HOH   E 4 .   ? 20.499 -20.023 2.801   1.00 21.65 ?  391 HOH   A O    1 
HETATM 7005 O  O    . HOH   E 4 .   ? 37.557 -2.060  5.933   1.00 29.10 ?  392 HOH   A O    1 
HETATM 7006 O  O    . HOH   E 4 .   ? 16.209 16.657  8.504   1.00 44.25 ?  393 HOH   A O    1 
HETATM 7007 O  O    . HOH   E 4 .   ? 14.573 -0.670  -12.244 1.00 25.73 ?  394 HOH   A O    1 
HETATM 7008 O  O    . HOH   E 4 .   ? 6.356  -5.535  10.983  1.00 21.57 ?  395 HOH   A O    1 
HETATM 7009 O  O    B HOH   E 4 .   ? 11.992 -2.480  -3.601  0.38 18.21 ?  396 HOH   A O    1 
HETATM 7010 O  O    . HOH   E 4 .   ? 15.159 -21.421 14.176  1.00 19.81 ?  397 HOH   A O    1 
HETATM 7011 O  O    A HOH   E 4 .   ? 28.558 -10.660 -13.954 0.62 33.31 ?  398 HOH   A O    1 
HETATM 7012 O  O    . HOH   E 4 .   ? 30.549 1.947   16.680  1.00 22.18 ?  399 HOH   A O    1 
HETATM 7013 O  O    . HOH   E 4 .   ? 32.719 -9.265  5.910   1.00 20.37 ?  400 HOH   A O    1 
HETATM 7014 O  O    A HOH   E 4 .   ? 15.761 -0.931  5.191   0.62 24.30 ?  401 HOH   A O    1 
HETATM 7015 O  O    . HOH   E 4 .   ? 15.426 11.810  7.841   1.00 50.97 ?  402 HOH   A O    1 
HETATM 7016 O  O    . HOH   E 4 .   ? 14.460 -24.603 11.488  1.00 40.41 ?  403 HOH   A O    1 
HETATM 7017 O  O    . HOH   E 4 .   ? 11.586 -10.740 16.840  1.00 32.41 ?  404 HOH   A O    1 
HETATM 7018 O  O    A HOH   E 4 .   ? 11.035 -0.374  1.843   0.62 21.94 ?  405 HOH   A O    1 
HETATM 7019 O  O    . HOH   E 4 .   ? 16.003 6.895   2.781   1.00 19.83 ?  406 HOH   A O    1 
HETATM 7020 O  O    . HOH   E 4 .   ? 30.902 6.172   -12.239 1.00 30.28 ?  407 HOH   A O    1 
HETATM 7021 O  O    . HOH   E 4 .   ? 38.115 -1.351  -1.906  1.00 20.10 ?  408 HOH   A O    1 
HETATM 7022 O  O    . HOH   E 4 .   ? 27.532 -6.025  -13.941 1.00 39.75 ?  409 HOH   A O    1 
HETATM 7023 O  O    . HOH   E 4 .   ? 8.955  -12.028 17.157  1.00 40.45 ?  410 HOH   A O    1 
HETATM 7024 O  O    . HOH   E 4 .   ? 5.156  2.708   4.928   1.00 33.05 ?  411 HOH   A O    1 
HETATM 7025 O  O    . HOH   E 4 .   ? 23.955 -20.280 -1.351  1.00 19.60 ?  412 HOH   A O    1 
HETATM 7026 O  O    . HOH   E 4 .   ? 30.219 -12.851 13.589  1.00 21.93 ?  413 HOH   A O    1 
HETATM 7027 O  O    . HOH   E 4 .   ? 21.854 -13.784 -8.148  1.00 42.53 ?  414 HOH   A O    1 
HETATM 7028 O  O    . HOH   E 4 .   ? 32.697 -4.311  -9.895  1.00 29.71 ?  415 HOH   A O    1 
HETATM 7029 O  O    . HOH   E 4 .   ? 29.959 -10.013 13.036  1.00 25.88 ?  416 HOH   A O    1 
HETATM 7030 O  O    . HOH   E 4 .   ? 40.953 -8.250  -6.780  1.00 35.92 ?  417 HOH   A O    1 
HETATM 7031 O  O    . HOH   E 4 .   ? 41.583 1.427   5.054   1.00 39.24 ?  418 HOH   A O    1 
HETATM 7032 O  O    . HOH   E 4 .   ? 36.655 -4.967  5.408   1.00 24.46 ?  419 HOH   A O    1 
HETATM 7033 O  O    . HOH   E 4 .   ? 27.154 2.347   18.728  1.00 39.26 ?  420 HOH   A O    1 
HETATM 7034 O  O    . HOH   E 4 .   ? 27.924 0.790   -7.191  1.00 15.34 ?  421 HOH   A O    1 
HETATM 7035 O  O    . HOH   E 4 .   ? 24.019 3.900   -4.885  1.00 21.62 ?  422 HOH   A O    1 
HETATM 7036 O  O    . HOH   E 4 .   ? 35.080 -5.229  -3.058  1.00 18.03 ?  423 HOH   A O    1 
HETATM 7037 O  O    . HOH   E 4 .   ? 10.375 -13.798 -1.834  1.00 18.54 ?  424 HOH   A O    1 
HETATM 7038 O  O    . HOH   E 4 .   ? 15.207 -8.066  -9.945  1.00 25.93 ?  425 HOH   A O    1 
HETATM 7039 O  O    . HOH   E 4 .   ? 22.530 8.246   18.302  1.00 43.43 ?  426 HOH   A O    1 
HETATM 7040 O  O    . HOH   E 4 .   ? 45.021 -0.574  2.970   1.00 45.23 ?  427 HOH   A O    1 
HETATM 7041 O  O    . HOH   E 4 .   ? 26.918 -3.117  19.458  1.00 40.03 ?  428 HOH   A O    1 
HETATM 7042 O  O    . HOH   E 4 .   ? 32.489 -10.624 3.288   1.00 31.45 ?  429 HOH   A O    1 
HETATM 7043 O  O    . HOH   E 4 .   ? 16.194 -14.213 20.070  1.00 61.97 ?  430 HOH   A O    1 
HETATM 7044 O  O    A HOH   E 4 .   ? 18.835 2.038   -0.829  0.62 12.53 ?  431 HOH   A O    1 
HETATM 7045 O  O    . HOH   E 4 .   ? 23.196 7.608   -3.279  1.00 35.63 ?  432 HOH   A O    1 
HETATM 7046 O  O    . HOH   E 4 .   ? 23.455 -20.899 1.335   1.00 21.92 ?  433 HOH   A O    1 
HETATM 7047 O  O    . HOH   E 4 .   ? 21.328 -9.030  21.295  1.00 57.02 ?  434 HOH   A O    1 
HETATM 7048 O  O    . HOH   E 4 .   ? 23.408 -7.967  17.042  1.00 23.28 ?  435 HOH   A O    1 
HETATM 7049 O  O    . HOH   E 4 .   ? -1.527 -4.893  7.493   1.00 47.98 ?  436 HOH   A O    1 
HETATM 7050 O  O    . HOH   E 4 .   ? 34.425 -8.026  -0.538  1.00 30.85 ?  437 HOH   A O    1 
HETATM 7051 O  O    . HOH   E 4 .   ? 37.726 -8.776  -3.368  1.00 23.11 ?  438 HOH   A O    1 
HETATM 7052 O  O    B HOH   E 4 .   ? 18.724 -1.498  -1.462  0.38 23.99 ?  439 HOH   A O    1 
HETATM 7053 O  O    . HOH   E 4 .   ? 21.383 -14.802 17.766  1.00 56.50 ?  440 HOH   A O    1 
HETATM 7054 O  O    A HOH   E 4 .   ? 16.231 2.950   -1.526  0.62 17.82 ?  441 HOH   A O    1 
HETATM 7055 O  O    . HOH   E 4 .   ? 31.328 -12.785 0.048   1.00 22.35 ?  442 HOH   A O    1 
HETATM 7056 O  O    . HOH   E 4 .   ? 30.502 14.736  2.674   1.00 21.15 ?  443 HOH   A O    1 
HETATM 7057 O  O    . HOH   E 4 .   ? 18.227 4.444   -15.512 1.00 57.27 ?  444 HOH   A O    1 
HETATM 7058 O  O    . HOH   E 4 .   ? 18.323 -15.970 16.212  1.00 46.90 ?  445 HOH   A O    1 
HETATM 7059 O  O    . HOH   E 4 .   ? 20.557 -17.642 24.819  1.00 58.04 ?  446 HOH   A O    1 
HETATM 7060 O  O    B HOH   E 4 .   ? 18.746 1.582   -0.386  0.38 15.70 ?  447 HOH   A O    1 
HETATM 7061 O  O    . HOH   E 4 .   ? 9.410  -16.261 -2.095  1.00 39.82 ?  448 HOH   A O    1 
HETATM 7062 O  O    A HOH   E 4 .   ? 13.992 -0.329  3.377   0.62 19.23 ?  449 HOH   A O    1 
HETATM 7063 O  O    . HOH   E 4 .   ? 29.838 -1.915  -12.736 1.00 50.39 ?  450 HOH   A O    1 
HETATM 7064 O  O    . HOH   E 4 .   ? 32.409 -15.865 10.890  1.00 29.96 ?  451 HOH   A O    1 
HETATM 7065 O  O    . HOH   E 4 .   ? 25.329 8.277   -4.798  1.00 33.24 ?  452 HOH   A O    1 
HETATM 7066 O  O    . HOH   E 4 .   ? 29.826 -16.130 10.856  1.00 36.75 ?  453 HOH   A O    1 
HETATM 7067 O  O    . HOH   E 4 .   ? 27.750 7.000   -6.715  1.00 41.98 ?  454 HOH   A O    1 
HETATM 7068 O  O    . HOH   E 4 .   ? 24.671 5.675   20.648  1.00 53.76 ?  455 HOH   A O    1 
HETATM 7069 O  O    . HOH   E 4 .   ? 19.860 -17.368 -5.132  1.00 24.90 ?  456 HOH   A O    1 
HETATM 7070 O  O    . HOH   E 4 .   ? 23.209 -22.367 -3.283  1.00 40.70 ?  457 HOH   A O    1 
HETATM 7071 O  O    . HOH   E 4 .   ? 21.968 5.192   -6.104  1.00 34.78 ?  458 HOH   A O    1 
HETATM 7072 O  O    . HOH   E 4 .   ? 24.567 14.737  7.735   1.00 40.17 ?  459 HOH   A O    1 
HETATM 7073 O  O    . HOH   E 4 .   ? 15.746 -21.515 3.673   1.00 26.17 ?  460 HOH   A O    1 
HETATM 7074 O  O    . HOH   E 4 .   ? 18.771 11.000  11.210  1.00 34.31 ?  461 HOH   A O    1 
HETATM 7075 O  O    . HOH   E 4 .   ? 26.903 11.715  -1.423  1.00 36.41 ?  462 HOH   A O    1 
HETATM 7076 O  O    . HOH   E 4 .   ? 39.628 -7.003  -3.443  1.00 44.82 ?  463 HOH   A O    1 
HETATM 7077 O  O    . HOH   E 4 .   ? 10.986 -15.000 -6.145  1.00 37.79 ?  464 HOH   A O    1 
HETATM 7078 O  O    . HOH   E 4 .   ? 25.843 10.788  -3.705  1.00 28.37 ?  465 HOH   A O    1 
HETATM 7079 O  O    . HOH   E 4 .   ? 23.369 13.697  5.493   1.00 18.92 ?  466 HOH   A O    1 
HETATM 7080 O  O    . HOH   E 4 .   ? 27.487 -11.358 16.548  1.00 40.23 ?  467 HOH   A O    1 
HETATM 7081 O  O    . HOH   E 4 .   ? 12.155 1.623   17.148  1.00 41.94 ?  468 HOH   A O    1 
HETATM 7082 O  O    . HOH   E 4 .   ? 12.011 -13.321 16.333  1.00 54.89 ?  469 HOH   A O    1 
HETATM 7083 O  O    . HOH   E 4 .   ? 18.207 -16.185 -8.964  1.00 42.38 ?  470 HOH   A O    1 
HETATM 7084 O  O    . HOH   E 4 .   ? 23.143 11.866  -4.068  1.00 22.55 ?  471 HOH   A O    1 
HETATM 7085 O  O    . HOH   E 4 .   ? 28.684 8.998   17.443  1.00 37.25 ?  472 HOH   A O    1 
HETATM 7086 O  O    . HOH   E 4 .   ? 16.831 -20.399 16.044  1.00 32.40 ?  473 HOH   A O    1 
HETATM 7087 O  O    . HOH   E 4 .   ? 35.116 7.514   12.169  1.00 56.23 ?  474 HOH   A O    1 
HETATM 7088 O  O    . HOH   E 4 .   ? 15.731 -17.219 -7.063  1.00 33.87 ?  475 HOH   A O    1 
HETATM 7089 O  O    . HOH   E 4 .   ? 40.995 -3.902  -0.452  1.00 41.75 ?  476 HOH   A O    1 
HETATM 7090 O  O    . HOH   E 4 .   ? 16.165 -23.364 5.734   1.00 33.75 ?  477 HOH   A O    1 
HETATM 7091 O  O    . HOH   E 4 .   ? 13.905 -25.082 8.901   1.00 38.03 ?  478 HOH   A O    1 
HETATM 7092 O  O    . HOH   E 4 .   ? 30.765 0.699   19.154  1.00 42.21 ?  479 HOH   A O    1 
HETATM 7093 O  O    . HOH   E 4 .   ? 44.474 10.445  -1.624  1.00 33.71 ?  480 HOH   A O    1 
HETATM 7094 O  O    . HOH   E 4 .   ? 20.119 -22.284 4.272   1.00 34.24 ?  481 HOH   A O    1 
HETATM 7095 O  O    . HOH   E 4 .   ? 8.096  -3.151  -5.813  1.00 57.79 ?  482 HOH   A O    1 
HETATM 7096 O  O    . HOH   E 4 .   ? 17.390 -18.760 19.609  1.00 58.37 ?  483 HOH   A O    1 
HETATM 7097 O  O    . HOH   E 4 .   ? 23.055 -12.875 19.240  1.00 61.37 ?  484 HOH   A O    1 
HETATM 7098 O  O    . HOH   E 4 .   ? 14.060 -10.272 -11.046 1.00 37.93 ?  485 HOH   A O    1 
HETATM 7099 O  O    . HOH   E 4 .   ? 39.216 2.388   7.298   1.00 30.71 ?  486 HOH   A O    1 
HETATM 7100 O  O    . HOH   E 4 .   ? 31.508 -0.547  -10.610 1.00 30.50 ?  487 HOH   A O    1 
HETATM 7101 O  O    . HOH   E 4 .   ? 28.800 -7.964  -15.238 1.00 51.33 ?  488 HOH   A O    1 
HETATM 7102 O  O    . HOH   E 4 .   ? 18.428 -23.172 1.899   1.00 52.37 ?  489 HOH   A O    1 
HETATM 7103 O  O    . HOH   E 4 .   ? 41.710 9.469   -3.909  1.00 31.67 ?  490 HOH   A O    1 
HETATM 7104 O  O    . HOH   E 4 .   ? 28.613 -4.703  -12.350 1.00 41.82 ?  491 HOH   A O    1 
HETATM 7105 O  O    . HOH   E 4 .   ? 25.751 -18.909 -11.871 1.00 39.84 ?  492 HOH   A O    1 
HETATM 7106 O  O    . HOH   E 4 .   ? 16.062 -6.897  -11.940 1.00 45.55 ?  493 HOH   A O    1 
HETATM 7107 O  O    . HOH   E 4 .   ? 40.588 -0.334  -7.775  1.00 34.04 ?  494 HOH   A O    1 
HETATM 7108 O  O    . HOH   E 4 .   ? 20.619 -16.116 -7.455  1.00 31.00 ?  495 HOH   A O    1 
HETATM 7109 O  O    . HOH   E 4 .   ? 37.363 -6.562  7.643   1.00 28.17 ?  496 HOH   A O    1 
HETATM 7110 O  O    . HOH   E 4 .   ? 39.470 -0.075  6.618   1.00 35.49 ?  497 HOH   A O    1 
HETATM 7111 O  O    . HOH   E 4 .   ? 30.705 -5.824  -11.935 1.00 53.83 ?  498 HOH   A O    1 
HETATM 7112 O  O    . HOH   E 4 .   ? 30.738 5.778   -14.761 1.00 37.11 ?  499 HOH   A O    1 
HETATM 7113 O  O    B HOH   E 4 .   ? 14.439 8.170   5.012   0.38 23.96 ?  500 HOH   A O    1 
HETATM 7114 O  O    . HOH   E 4 .   ? 28.940 14.480  0.812   1.00 54.58 ?  501 HOH   A O    1 
HETATM 7115 O  O    . HOH   E 4 .   ? 37.905 14.021  6.594   1.00 33.19 ?  502 HOH   A O    1 
HETATM 7116 O  O    . HOH   E 4 .   ? 36.458 -6.465  10.282  1.00 50.58 ?  503 HOH   A O    1 
HETATM 7117 O  O    . HOH   E 4 .   ? 22.056 -23.984 4.535   1.00 29.07 ?  504 HOH   A O    1 
HETATM 7118 O  O    A HOH   E 4 .   ? 14.807 8.663   4.790   0.62 31.20 ?  505 HOH   A O    1 
HETATM 7119 O  O    . HOH   E 4 .   ? 17.306 -6.768  -14.127 1.00 47.24 ?  506 HOH   A O    1 
HETATM 7120 O  O    . HOH   E 4 .   ? 24.074 9.101   -7.221  1.00 39.45 ?  507 HOH   A O    1 
HETATM 7121 O  O    . HOH   E 4 .   ? 15.689 -12.275 27.292  1.00 47.19 ?  508 HOH   A O    1 
HETATM 7122 O  O    . HOH   E 4 .   ? 16.250 -21.168 18.750  1.00 41.16 ?  509 HOH   A O    1 
HETATM 7123 O  O    . HOH   E 4 .   ? 14.699 -22.764 19.779  1.00 37.15 ?  510 HOH   A O    1 
HETATM 7124 O  O    . HOH   F 4 .   ? 29.872 -22.413 5.549   1.00 19.90 ?  201 HOH   B O    1 
HETATM 7125 O  O    . HOH   F 4 .   ? 27.659 -29.105 -1.823  1.00 39.76 ?  202 HOH   B O    1 
HETATM 7126 O  O    . HOH   F 4 .   ? 31.116 -28.682 4.599   1.00 30.79 ?  203 HOH   B O    1 
HETATM 7127 O  O    . HOH   F 4 .   ? 27.877 -41.693 -15.093 1.00 36.92 ?  204 HOH   B O    1 
HETATM 7128 O  O    . HOH   F 4 .   ? 38.093 -39.391 -0.117  1.00 41.78 ?  205 HOH   B O    1 
HETATM 7129 O  O    . HOH   F 4 .   ? 42.832 -20.225 -20.644 1.00 38.72 ?  206 HOH   B O    1 
HETATM 7130 O  O    . HOH   F 4 .   ? 48.014 -6.896  15.455  1.00 29.46 ?  207 HOH   B O    1 
HETATM 7131 O  O    . HOH   F 4 .   ? 41.566 -36.085 -17.198 1.00 36.78 ?  208 HOH   B O    1 
HETATM 7132 O  O    . HOH   F 4 .   ? 59.128 -18.651 6.875   1.00 36.24 ?  209 HOH   B O    1 
HETATM 7133 O  O    . HOH   F 4 .   ? 52.993 -13.454 -20.235 1.00 34.95 ?  210 HOH   B O    1 
HETATM 7134 O  O    . HOH   F 4 .   ? 30.191 -40.946 -7.970  1.00 18.44 ?  211 HOH   B O    1 
HETATM 7135 O  O    . HOH   F 4 .   ? 54.467 -9.454  -8.642  1.00 19.33 ?  212 HOH   B O    1 
HETATM 7136 O  O    . HOH   F 4 .   ? 30.022 -26.284 4.233   1.00 25.86 ?  213 HOH   B O    1 
HETATM 7137 O  O    . HOH   F 4 .   ? 48.587 -36.460 -15.515 1.00 47.43 ?  214 HOH   B O    1 
HETATM 7138 O  O    . HOH   F 4 .   ? 41.266 -7.796  5.456   1.00 41.03 ?  215 HOH   B O    1 
HETATM 7139 O  O    . HOH   F 4 .   ? 58.197 -12.931 8.352   1.00 29.99 ?  216 HOH   B O    1 
HETATM 7140 O  O    . HOH   F 4 .   ? 56.365 -19.734 7.080   1.00 30.67 ?  217 HOH   B O    1 
HETATM 7141 O  O    . HOH   F 4 .   ? 49.421 -22.735 -19.811 1.00 51.11 ?  218 HOH   B O    1 
HETATM 7142 O  O    . HOH   F 4 .   ? 50.083 -3.444  7.052   1.00 38.86 ?  219 HOH   B O    1 
HETATM 7143 O  O    . HOH   F 4 .   ? 34.512 -36.349 -7.108  1.00 20.86 ?  220 HOH   B O    1 
HETATM 7144 O  O    . HOH   F 4 .   ? 57.743 -24.403 5.077   1.00 41.32 ?  221 HOH   B O    1 
HETATM 7145 O  O    . HOH   F 4 .   ? 37.066 -19.722 -18.178 1.00 48.82 ?  222 HOH   B O    1 
HETATM 7146 O  O    . HOH   F 4 .   ? 57.128 -26.911 -7.627  1.00 37.96 ?  223 HOH   B O    1 
HETATM 7147 O  O    . HOH   F 4 .   ? 28.250 -34.287 -9.289  1.00 18.56 ?  224 HOH   B O    1 
HETATM 7148 O  O    . HOH   F 4 .   ? 50.890 -39.928 -8.219  1.00 36.96 ?  225 HOH   B O    1 
HETATM 7149 O  O    . HOH   F 4 .   ? 57.357 -16.300 -12.261 1.00 18.25 ?  226 HOH   B O    1 
HETATM 7150 O  O    . HOH   F 4 .   ? 25.436 -25.883 -1.222  1.00 34.74 ?  227 HOH   B O    1 
HETATM 7151 O  O    . HOH   F 4 .   ? 41.477 -39.184 -14.917 1.00 22.58 ?  228 HOH   B O    1 
HETATM 7152 O  O    . HOH   F 4 .   ? 56.639 -30.822 -7.734  1.00 29.24 ?  229 HOH   B O    1 
HETATM 7153 O  O    . HOH   F 4 .   ? 47.771 -24.492 -17.896 1.00 32.73 ?  230 HOH   B O    1 
HETATM 7154 O  O    . HOH   F 4 .   ? 50.759 -6.041  0.159   1.00 28.65 ?  231 HOH   B O    1 
HETATM 7155 O  O    . HOH   F 4 .   ? 32.688 -43.719 -11.286 1.00 26.26 ?  232 HOH   B O    1 
HETATM 7156 O  O    . HOH   F 4 .   ? 35.105 -8.012  -2.973  1.00 19.14 ?  233 HOH   B O    1 
HETATM 7157 O  O    . HOH   F 4 .   ? 44.410 -7.067  1.972   1.00 36.10 ?  234 HOH   B O    1 
HETATM 7158 O  O    . HOH   F 4 .   ? 51.631 -6.464  4.316   1.00 21.22 ?  235 HOH   B O    1 
HETATM 7159 O  O    . HOH   F 4 .   ? 40.515 -16.098 14.035  1.00 25.19 ?  236 HOH   B O    1 
HETATM 7160 O  O    . HOH   F 4 .   ? 41.382 -9.608  13.055  1.00 23.44 ?  237 HOH   B O    1 
HETATM 7161 O  O    . HOH   F 4 .   ? 34.933 -24.624 13.855  1.00 37.59 ?  238 HOH   B O    1 
HETATM 7162 O  O    . HOH   F 4 .   ? 39.315 -10.842 6.100   1.00 25.49 ?  239 HOH   B O    1 
HETATM 7163 O  O    . HOH   F 4 .   ? 55.270 -16.509 -14.266 1.00 32.17 ?  240 HOH   B O    1 
HETATM 7164 O  O    . HOH   F 4 .   ? 45.796 -40.348 -3.565  1.00 32.62 ?  241 HOH   B O    1 
HETATM 7165 O  O    . HOH   F 4 .   ? 44.541 -27.762 -0.681  1.00 22.70 ?  242 HOH   B O    1 
HETATM 7166 O  O    . HOH   F 4 .   ? 57.659 -24.317 -3.775  1.00 21.01 ?  243 HOH   B O    1 
HETATM 7167 O  O    . HOH   F 4 .   ? 42.945 -43.223 -8.199  1.00 30.17 ?  244 HOH   B O    1 
HETATM 7168 O  O    . HOH   F 4 .   ? 58.201 -10.696 -4.036  1.00 21.54 ?  245 HOH   B O    1 
HETATM 7169 O  O    . HOH   F 4 .   ? 47.417 -7.242  -3.789  1.00 42.75 ?  246 HOH   B O    1 
HETATM 7170 O  O    . HOH   F 4 .   ? 50.770 -12.976 -0.467  1.00 12.60 ?  247 HOH   B O    1 
HETATM 7171 O  O    . HOH   F 4 .   ? 46.401 -1.529  13.112  1.00 28.96 ?  248 HOH   B O    1 
HETATM 7172 O  O    . HOH   F 4 .   ? 42.652 -22.825 3.878   1.00 12.36 ?  249 HOH   B O    1 
HETATM 7173 O  O    . HOH   F 4 .   ? 38.483 -11.058 -2.236  1.00 20.59 ?  250 HOH   B O    1 
HETATM 7174 O  O    . HOH   F 4 .   ? 39.537 -11.111 0.337   1.00 17.48 ?  251 HOH   B O    1 
HETATM 7175 O  O    . HOH   F 4 .   ? 43.076 -32.359 -17.096 1.00 26.00 ?  252 HOH   B O    1 
HETATM 7176 O  O    . HOH   F 4 .   ? 44.882 -43.610 -10.470 1.00 28.51 ?  253 HOH   B O    1 
HETATM 7177 O  O    . HOH   F 4 .   ? 29.710 -25.153 -10.676 1.00 18.13 ?  254 HOH   B O    1 
HETATM 7178 O  O    . HOH   F 4 .   ? 42.589 -25.337 2.692   1.00 16.08 ?  255 HOH   B O    1 
HETATM 7179 O  O    . HOH   F 4 .   ? 28.411 -19.643 -13.102 1.00 26.99 ?  256 HOH   B O    1 
HETATM 7180 O  O    . HOH   F 4 .   ? 41.902 -23.504 9.318   1.00 20.73 ?  257 HOH   B O    1 
HETATM 7181 O  O    . HOH   F 4 .   ? 31.796 -17.821 -14.420 1.00 30.89 ?  258 HOH   B O    1 
HETATM 7182 O  O    . HOH   F 4 .   ? 34.340 -18.314 11.505  1.00 27.96 ?  259 HOH   B O    1 
HETATM 7183 O  O    . HOH   F 4 .   ? 45.175 -34.951 6.830   1.00 42.19 ?  260 HOH   B O    1 
HETATM 7184 O  O    . HOH   F 4 .   ? 40.360 -12.732 -11.479 1.00 15.95 ?  261 HOH   B O    1 
HETATM 7185 O  O    . HOH   F 4 .   ? 51.511 -13.791 10.978  1.00 27.20 ?  262 HOH   B O    1 
HETATM 7186 O  O    . HOH   F 4 .   ? 27.099 -31.774 -9.900  1.00 20.81 ?  263 HOH   B O    1 
HETATM 7187 O  O    . HOH   F 4 .   ? 42.419 -34.647 3.852   1.00 26.58 ?  264 HOH   B O    1 
HETATM 7188 O  O    . HOH   F 4 .   ? 47.061 -33.944 -4.666  1.00 19.95 ?  265 HOH   B O    1 
HETATM 7189 O  O    . HOH   F 4 .   ? 33.533 -16.913 8.135   1.00 19.73 ?  266 HOH   B O    1 
HETATM 7190 O  O    . HOH   F 4 .   ? 30.862 -15.702 2.720   1.00 14.75 ?  267 HOH   B O    1 
HETATM 7191 O  O    . HOH   F 4 .   ? 46.950 -29.531 9.815   1.00 32.00 ?  268 HOH   B O    1 
HETATM 7192 O  O    . HOH   F 4 .   ? 28.415 -30.932 -14.725 1.00 32.74 ?  269 HOH   B O    1 
HETATM 7193 O  O    . HOH   F 4 .   ? 57.496 -9.236  1.367   1.00 20.37 ?  270 HOH   B O    1 
HETATM 7194 O  O    . HOH   F 4 .   ? 38.916 -11.879 12.352  1.00 39.42 ?  271 HOH   B O    1 
HETATM 7195 O  O    . HOH   F 4 .   ? 56.157 -23.572 -14.721 1.00 28.07 ?  272 HOH   B O    1 
HETATM 7196 O  O    . HOH   F 4 .   ? 49.651 -0.476  10.190  1.00 31.75 ?  273 HOH   B O    1 
HETATM 7197 O  O    . HOH   F 4 .   ? 43.412 -15.799 -12.175 1.00 14.92 ?  274 HOH   B O    1 
HETATM 7198 O  O    . HOH   F 4 .   ? 48.612 -12.155 -14.457 1.00 26.50 ?  275 HOH   B O    1 
HETATM 7199 O  O    . HOH   F 4 .   ? 48.081 -22.742 5.838   1.00 19.26 ?  276 HOH   B O    1 
HETATM 7200 O  O    . HOH   F 4 .   ? 56.927 -8.599  8.384   1.00 19.10 ?  277 HOH   B O    1 
HETATM 7201 O  O    . HOH   F 4 .   ? 41.129 -5.526  11.508  1.00 47.57 ?  278 HOH   B O    1 
HETATM 7202 O  O    . HOH   F 4 .   ? 49.264 -28.727 -6.907  1.00 16.60 ?  279 HOH   B O    1 
HETATM 7203 O  O    . HOH   F 4 .   ? 38.391 -12.172 -16.211 1.00 48.34 ?  280 HOH   B O    1 
HETATM 7204 O  O    . HOH   F 4 .   ? 42.331 -9.893  9.309   1.00 21.56 ?  281 HOH   B O    1 
HETATM 7205 O  O    . HOH   F 4 .   ? 29.827 -34.160 -0.411  1.00 37.95 ?  282 HOH   B O    1 
HETATM 7206 O  O    . HOH   F 4 .   ? 30.362 -42.237 -10.586 1.00 33.03 ?  283 HOH   B O    1 
HETATM 7207 O  O    . HOH   F 4 .   ? 48.388 -25.034 3.117   1.00 14.78 ?  284 HOH   B O    1 
HETATM 7208 O  O    . HOH   F 4 .   ? 34.917 -33.293 -19.176 1.00 36.05 ?  285 HOH   B O    1 
HETATM 7209 O  O    . HOH   F 4 .   ? 45.227 -33.353 -15.978 1.00 24.84 ?  286 HOH   B O    1 
HETATM 7210 O  O    . HOH   F 4 .   ? 34.467 -12.771 2.712   1.00 24.75 ?  287 HOH   B O    1 
HETATM 7211 O  O    . HOH   F 4 .   ? 46.561 -31.216 -4.810  1.00 24.87 ?  288 HOH   B O    1 
HETATM 7212 O  O    . HOH   F 4 .   ? 51.172 -37.514 -9.731  1.00 28.98 ?  289 HOH   B O    1 
HETATM 7213 O  O    . HOH   F 4 .   ? 27.963 -22.870 -7.929  1.00 18.31 ?  290 HOH   B O    1 
HETATM 7214 O  O    . HOH   F 4 .   ? 27.519 -26.583 -15.525 1.00 34.42 ?  291 HOH   B O    1 
HETATM 7215 O  O    . HOH   F 4 .   ? 51.671 -6.028  -7.996  1.00 40.74 ?  292 HOH   B O    1 
HETATM 7216 O  O    . HOH   F 4 .   ? 36.814 -12.750 -1.480  1.00 28.60 ?  293 HOH   B O    1 
HETATM 7217 O  O    . HOH   F 4 .   ? 52.498 -10.335 12.955  1.00 23.25 ?  294 HOH   B O    1 
HETATM 7218 O  O    . HOH   F 4 .   ? 35.158 -33.696 4.672   1.00 34.71 ?  295 HOH   B O    1 
HETATM 7219 O  O    . HOH   F 4 .   ? 48.718 -20.003 5.976   1.00 14.81 ?  296 HOH   B O    1 
HETATM 7220 O  O    . HOH   F 4 .   ? 33.530 -15.250 -13.889 1.00 22.30 ?  297 HOH   B O    1 
HETATM 7221 O  O    . HOH   F 4 .   ? 57.080 -12.035 12.343  1.00 39.53 ?  298 HOH   B O    1 
HETATM 7222 O  O    . HOH   F 4 .   ? 36.015 -43.474 -8.257  1.00 42.64 ?  299 HOH   B O    1 
HETATM 7223 O  O    . HOH   F 4 .   ? 42.739 -12.187 -18.426 1.00 28.20 ?  300 HOH   B O    1 
HETATM 7224 O  O    . HOH   F 4 .   ? 59.798 -15.275 8.168   1.00 32.87 ?  301 HOH   B O    1 
HETATM 7225 O  O    . HOH   F 4 .   ? 51.369 -33.088 -10.976 1.00 45.37 ?  302 HOH   B O    1 
HETATM 7226 O  O    . HOH   F 4 .   ? 47.991 -32.694 -16.683 1.00 45.17 ?  303 HOH   B O    1 
HETATM 7227 O  O    . HOH   F 4 .   ? 52.435 -29.260 -13.092 1.00 25.58 ?  304 HOH   B O    1 
HETATM 7228 O  O    . HOH   F 4 .   ? 44.628 -27.464 2.054   1.00 16.87 ?  305 HOH   B O    1 
HETATM 7229 O  O    . HOH   F 4 .   ? 40.276 -10.839 -9.459  1.00 18.36 ?  306 HOH   B O    1 
HETATM 7230 O  O    . HOH   F 4 .   ? 53.618 -12.612 -22.149 1.00 36.44 ?  307 HOH   B O    1 
HETATM 7231 O  O    . HOH   F 4 .   ? 52.553 -35.605 -8.834  1.00 31.81 ?  308 HOH   B O    1 
HETATM 7232 O  O    . HOH   F 4 .   ? 49.931 -24.653 5.884   1.00 36.83 ?  309 HOH   B O    1 
HETATM 7233 O  O    . HOH   F 4 .   ? 38.432 -9.331  -13.282 1.00 32.84 ?  310 HOH   B O    1 
HETATM 7234 O  O    . HOH   F 4 .   ? 53.444 -30.192 4.533   1.00 19.18 ?  311 HOH   B O    1 
HETATM 7235 O  O    . HOH   F 4 .   ? 52.993 -15.987 -12.746 1.00 26.80 ?  312 HOH   B O    1 
HETATM 7236 O  O    . HOH   F 4 .   ? 37.355 -17.856 13.145  1.00 33.13 ?  313 HOH   B O    1 
HETATM 7237 O  O    . HOH   F 4 .   ? 25.946 -21.458 -3.408  1.00 18.21 ?  314 HOH   B O    1 
HETATM 7238 O  O    . HOH   F 4 .   ? 38.315 -12.648 7.979   1.00 17.96 ?  315 HOH   B O    1 
HETATM 7239 O  O    . HOH   F 4 .   ? 44.044 -29.354 -4.685  1.00 23.89 ?  316 HOH   B O    1 
HETATM 7240 O  O    . HOH   F 4 .   ? 43.205 -34.450 0.121   1.00 24.86 ?  317 HOH   B O    1 
HETATM 7241 O  O    . HOH   F 4 .   ? 36.975 -30.535 -20.980 1.00 32.07 ?  318 HOH   B O    1 
HETATM 7242 O  O    . HOH   F 4 .   ? 37.890 -10.190 -10.707 1.00 19.25 ?  319 HOH   B O    1 
HETATM 7243 O  O    . HOH   F 4 .   ? 32.842 -34.571 -5.791  1.00 18.33 ?  320 HOH   B O    1 
HETATM 7244 O  O    . HOH   F 4 .   ? 41.792 -8.061  1.386   1.00 24.10 ?  321 HOH   B O    1 
HETATM 7245 O  O    . HOH   F 4 .   ? 62.732 -13.549 4.696   1.00 28.30 ?  322 HOH   B O    1 
HETATM 7246 O  O    . HOH   F 4 .   ? 42.460 -9.731  -14.844 1.00 41.49 ?  323 HOH   B O    1 
HETATM 7247 O  O    . HOH   F 4 .   ? 43.226 -21.396 10.726  1.00 16.57 ?  324 HOH   B O    1 
HETATM 7248 O  O    . HOH   F 4 .   ? 26.346 -21.042 -6.190  1.00 18.13 ?  325 HOH   B O    1 
HETATM 7249 O  O    . HOH   F 4 .   ? 44.090 -1.783  7.597   1.00 49.24 ?  326 HOH   B O    1 
HETATM 7250 O  O    . HOH   F 4 .   ? 44.700 -24.556 9.585   1.00 22.16 ?  327 HOH   B O    1 
HETATM 7251 O  O    . HOH   F 4 .   ? 37.299 -35.629 7.263   1.00 34.61 ?  328 HOH   B O    1 
HETATM 7252 O  O    . HOH   F 4 .   ? 45.610 -36.295 -16.101 1.00 37.07 ?  329 HOH   B O    1 
HETATM 7253 O  O    . HOH   F 4 .   ? 33.718 -31.079 11.134  1.00 38.11 ?  330 HOH   B O    1 
HETATM 7254 O  O    . HOH   F 4 .   ? 59.907 -17.306 -10.526 1.00 35.84 ?  331 HOH   B O    1 
HETATM 7255 O  O    . HOH   F 4 .   ? 36.746 -12.369 4.302   1.00 18.42 ?  332 HOH   B O    1 
HETATM 7256 O  O    . HOH   F 4 .   ? 47.267 -24.421 8.162   1.00 22.09 ?  333 HOH   B O    1 
HETATM 7257 O  O    . HOH   F 4 .   ? 34.407 -10.355 7.814   1.00 22.71 ?  334 HOH   B O    1 
HETATM 7258 O  O    . HOH   F 4 .   ? 62.898 -20.173 -0.706  1.00 39.40 ?  335 HOH   B O    1 
HETATM 7259 O  O    . HOH   F 4 .   ? 57.586 -21.974 3.339   1.00 32.41 ?  336 HOH   B O    1 
HETATM 7260 O  O    . HOH   F 4 .   ? 47.467 -27.393 2.026   1.00 15.84 ?  337 HOH   B O    1 
HETATM 7261 O  O    . HOH   F 4 .   ? 27.539 -14.706 -9.497  1.00 40.97 ?  338 HOH   B O    1 
HETATM 7262 O  O    . HOH   F 4 .   ? 42.866 -43.593 -14.345 1.00 42.84 ?  339 HOH   B O    1 
HETATM 7263 O  O    . HOH   F 4 .   ? 43.516 -15.410 18.056  1.00 31.84 ?  340 HOH   B O    1 
HETATM 7264 O  O    . HOH   F 4 .   ? 37.068 -15.118 -16.578 1.00 43.20 ?  341 HOH   B O    1 
HETATM 7265 O  O    . HOH   F 4 .   ? 37.032 -45.087 -9.665  1.00 37.02 ?  342 HOH   B O    1 
HETATM 7266 O  O    . HOH   F 4 .   ? 41.349 -24.476 15.901  1.00 47.98 ?  343 HOH   B O    1 
HETATM 7267 O  O    . HOH   F 4 .   ? 28.891 -42.827 -12.248 1.00 52.16 ?  344 HOH   B O    1 
HETATM 7268 O  O    . HOH   F 4 .   ? 46.773 -19.908 12.313  1.00 32.42 ?  345 HOH   B O    1 
HETATM 7269 O  O    . HOH   F 4 .   ? 33.014 -14.659 1.071   1.00 22.07 ?  346 HOH   B O    1 
HETATM 7270 O  O    . HOH   F 4 .   ? 44.175 -37.415 -17.817 1.00 37.36 ?  347 HOH   B O    1 
HETATM 7271 O  O    . HOH   F 4 .   ? 39.795 -44.140 -11.189 1.00 45.14 ?  348 HOH   B O    1 
HETATM 7272 O  O    . HOH   F 4 .   ? 33.633 -9.833  -8.778  1.00 32.10 ?  349 HOH   B O    1 
HETATM 7273 O  O    . HOH   F 4 .   ? 38.571 -22.322 15.070  1.00 45.42 ?  350 HOH   B O    1 
HETATM 7274 O  O    . HOH   F 4 .   ? 40.308 -43.442 -9.109  1.00 28.88 ?  351 HOH   B O    1 
HETATM 7275 O  O    . HOH   F 4 .   ? 39.632 -23.667 -20.358 1.00 40.24 ?  352 HOH   B O    1 
HETATM 7276 O  O    . HOH   F 4 .   ? 62.477 -20.031 -4.853  1.00 46.59 ?  353 HOH   B O    1 
HETATM 7277 O  O    . HOH   F 4 .   ? 33.874 -7.948  11.483  1.00 40.07 ?  354 HOH   B O    1 
HETATM 7278 O  O    . HOH   F 4 .   ? 27.807 -26.587 -0.480  1.00 30.95 ?  355 HOH   B O    1 
HETATM 7279 O  O    . HOH   F 4 .   ? 55.702 -8.251  10.795  1.00 25.11 ?  356 HOH   B O    1 
HETATM 7280 O  O    . HOH   F 4 .   ? 23.208 -23.637 6.863   1.00 36.26 ?  357 HOH   B O    1 
HETATM 7281 O  O    . HOH   F 4 .   ? 56.623 -7.278  2.948   1.00 28.06 ?  358 HOH   B O    1 
HETATM 7282 O  O    . HOH   F 4 .   ? 36.146 -8.446  -9.739  1.00 37.24 ?  359 HOH   B O    1 
HETATM 7283 O  O    . HOH   F 4 .   ? 61.462 -19.866 1.798   1.00 38.90 ?  360 HOH   B O    1 
HETATM 7284 O  O    . HOH   F 4 .   ? 40.545 -11.264 -13.862 1.00 33.01 ?  361 HOH   B O    1 
HETATM 7285 O  O    . HOH   F 4 .   ? 56.872 -21.673 -16.443 1.00 40.59 ?  362 HOH   B O    1 
HETATM 7286 O  O    . HOH   F 4 .   ? 40.236 -8.836  9.903   1.00 38.61 ?  363 HOH   B O    1 
HETATM 7287 O  O    . HOH   F 4 .   ? 27.158 -25.886 -11.302 1.00 35.95 ?  364 HOH   B O    1 
HETATM 7288 O  O    . HOH   F 4 .   ? 48.230 -26.412 8.846   1.00 43.85 ?  365 HOH   B O    1 
HETATM 7289 O  O    . HOH   F 4 .   ? 43.206 -12.612 -21.138 1.00 42.18 ?  366 HOH   B O    1 
HETATM 7290 O  O    . HOH   F 4 .   ? 54.225 -5.720  2.966   1.00 38.22 ?  367 HOH   B O    1 
HETATM 7291 O  O    . HOH   F 4 .   ? 36.179 -8.658  8.968   1.00 31.37 ?  368 HOH   B O    1 
HETATM 7292 O  O    . HOH   F 4 .   ? 32.597 -23.490 14.033  1.00 41.28 ?  369 HOH   B O    1 
HETATM 7293 O  O    . HOH   F 4 .   ? 58.987 -10.404 9.118   1.00 40.20 ?  370 HOH   B O    1 
HETATM 7294 O  O    . HOH   F 4 .   ? 39.812 -7.046  7.792   1.00 42.40 ?  371 HOH   B O    1 
HETATM 7295 O  O    . HOH   F 4 .   ? 52.079 -12.900 13.281  1.00 29.48 ?  372 HOH   B O    1 
HETATM 7296 O  O    . HOH   F 4 .   ? 56.070 -7.812  -0.666  1.00 38.44 ?  373 HOH   B O    1 
HETATM 7297 O  O    . HOH   F 4 .   ? 63.054 -12.427 6.931   1.00 37.92 ?  374 HOH   B O    1 
HETATM 7298 O  O    . HOH   F 4 .   ? 41.894 -9.981  -17.472 1.00 59.98 ?  375 HOH   B O    1 
HETATM 7299 O  O    . HOH   F 4 .   ? 40.221 -7.748  3.118   1.00 45.85 ?  376 HOH   B O    1 
HETATM 7300 O  O    . HOH   F 4 .   ? 42.699 -17.102 -23.067 1.00 46.59 ?  377 HOH   B O    1 
HETATM 7301 O  O    . HOH   F 4 .   ? 37.956 -10.466 10.026  1.00 27.41 ?  378 HOH   B O    1 
HETATM 7302 O  O    . HOH   F 4 .   ? 36.438 -22.875 13.289  1.00 30.95 ?  379 HOH   B O    1 
HETATM 7303 O  O    . HOH   F 4 .   ? 41.804 -6.650  -4.866  1.00 49.50 ?  380 HOH   B O    1 
HETATM 7304 O  O    . HOH   F 4 .   ? 39.633 -14.011 15.594  1.00 54.39 ?  381 HOH   B O    1 
HETATM 7305 O  O    . HOH   F 4 .   ? 44.067 -5.568  -3.508  1.00 42.39 ?  382 HOH   B O    1 
HETATM 7306 O  O    . HOH   F 4 .   ? 52.865 -29.916 7.225   1.00 23.57 ?  383 HOH   B O    1 
HETATM 7307 O  O    . HOH   F 4 .   ? 46.767 -5.377  2.848   1.00 39.43 ?  384 HOH   B O    1 
HETATM 7308 O  O    . HOH   F 4 .   ? 60.479 -22.186 2.970   1.00 51.74 ?  385 HOH   B O    1 
HETATM 7309 O  O    . HOH   F 4 .   ? 41.053 -9.628  15.776  1.00 50.20 ?  386 HOH   B O    1 
HETATM 7310 O  O    . HOH   F 4 .   ? 35.492 -33.697 7.491   1.00 43.78 ?  387 HOH   B O    1 
HETATM 7311 O  O    . HOH   F 4 .   ? 23.914 -20.910 -7.599  1.00 30.44 ?  388 HOH   B O    1 
HETATM 7312 O  O    . HOH   F 4 .   ? 35.183 -20.371 13.333  1.00 37.22 ?  389 HOH   B O    1 
HETATM 7313 O  O    . HOH   F 4 .   ? 23.175 -23.728 1.595   1.00 37.15 ?  390 HOH   B O    1 
HETATM 7314 O  O    . HOH   F 4 .   ? 40.760 -6.581  -0.810  1.00 29.64 ?  391 HOH   B O    1 
HETATM 7315 O  O    . HOH   F 4 .   ? 44.177 -31.734 -3.808  1.00 45.81 ?  392 HOH   B O    1 
HETATM 7316 O  O    . HOH   F 4 .   ? 26.608 -27.846 -13.370 1.00 39.28 ?  393 HOH   B O    1 
HETATM 7317 O  O    . HOH   F 4 .   ? 28.017 -27.058 2.331   1.00 29.66 ?  394 HOH   B O    1 
HETATM 7318 O  O    . HOH   F 4 .   ? 26.842 -30.613 -12.627 1.00 27.87 ?  395 HOH   B O    1 
HETATM 7319 O  O    . HOH   F 4 .   ? 50.653 -30.863 8.737   1.00 31.96 ?  396 HOH   B O    1 
HETATM 7320 O  O    . HOH   F 4 .   ? 24.665 -20.592 -10.501 1.00 42.90 ?  397 HOH   B O    1 
HETATM 7321 O  O    . HOH   F 4 .   ? 34.371 -33.455 9.661   1.00 38.34 ?  398 HOH   B O    1 
HETATM 7322 O  O    . HOH   F 4 .   ? 45.675 -19.980 15.249  1.00 41.71 ?  399 HOH   B O    1 
HETATM 7323 O  O    . HOH   F 4 .   ? 57.700 -6.521  -2.314  1.00 35.47 ?  400 HOH   B O    1 
HETATM 7324 O  O    . HOH   F 4 .   ? 40.877 -11.765 -22.188 1.00 41.36 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   A VAL   A 3   ? 0.7940 0.7926 0.9179 0.0108  -0.0253 0.0662  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.7785 0.7744 0.8853 0.0007  -0.0192 0.0366  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.7894 0.7881 0.9070 0.0085  -0.0242 0.0661  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.7735 0.7691 0.8738 -0.0007 -0.0185 0.0369  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.7673 0.7678 0.8678 0.0002  -0.0237 0.0669  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.7515 0.7478 0.8315 -0.0060 -0.0189 0.0369  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.7703 0.7711 0.8880 0.0016  -0.0252 0.0681  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.7544 0.7507 0.8458 -0.0053 -0.0200 0.0371  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.8029 0.8002 0.9267 0.0127  -0.0236 0.0649  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.7864 0.7812 0.8962 0.0020  -0.0176 0.0365  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.8068 0.8036 0.9289 0.0146  -0.0236 0.0643  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.7899 0.7846 0.9005 0.0033  -0.0174 0.0362  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.8081 0.8050 0.9295 0.0137  -0.0233 0.0649  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.7915 0.7860 0.9010 0.0027  -0.0173 0.0367  3   VAL   A CG2 
31   N  N   A ASN   A 4   ? 0.7382 0.7402 0.7983 -0.0104 -0.0201 0.0657  4   ASN   A N   
32   N  N   B ASN   A 4   ? 0.7233 0.7200 0.7663 -0.0123 -0.0173 0.0363  4   ASN   A N   
33   C  CA  A ASN   A 4   ? 0.7040 0.7088 0.7186 -0.0213 -0.0147 0.0627  4   ASN   A CA  
34   C  CA  B ASN   A 4   ? 0.6910 0.6891 0.6938 -0.0189 -0.0150 0.0342  4   ASN   A CA  
35   C  C   A ASN   A 4   ? 0.6524 0.6676 0.6692 -0.0374 0.0004  0.0494  4   ASN   A C   
36   C  C   B ASN   A 4   ? 0.6461 0.6498 0.6478 -0.0278 -0.0046 0.0262  4   ASN   A C   
37   O  O   A ASN   A 4   ? 0.6541 0.6703 0.6683 -0.0377 -0.0011 0.0494  4   ASN   A O   
38   O  O   B ASN   A 4   ? 0.6476 0.6518 0.6475 -0.0281 -0.0051 0.0267  4   ASN   A O   
39   C  CB  A ASN   A 4   ? 0.7172 0.7159 0.6821 -0.0174 -0.0226 0.0728  4   ASN   A CB  
40   C  CB  B ASN   A 4   ? 0.7007 0.6954 0.6632 -0.0171 -0.0219 0.0400  4   ASN   A CB  
41   C  CG  A ASN   A 4   ? 0.7263 0.7203 0.6485 -0.0144 -0.0307 0.0815  4   ASN   A CG  
42   C  CG  B ASN   A 4   ? 0.7073 0.6994 0.6357 -0.0157 -0.0283 0.0448  4   ASN   A CG  
43   O  OD1 A ASN   A 4   ? 0.7304 0.7227 0.6376 -0.0138 -0.0359 0.0842  4   ASN   A OD1 
44   O  OD1 B ASN   A 4   ? 0.7101 0.7014 0.6263 -0.0155 -0.0320 0.0462  4   ASN   A OD1 
45   N  ND2 A ASN   A 4   ? 0.7282 0.7208 0.6379 -0.0127 -0.0314 0.0862  4   ASN   A ND2 
46   N  ND2 B ASN   A 4   ? 0.7088 0.6999 0.6272 -0.0148 -0.0293 0.0476  4   ASN   A ND2 
59   N  N   A SER   A 5   ? 0.5961 0.6209 0.6136 -0.0547 0.0176  0.0371  5   SER   A N   
60   N  N   B SER   A 5   ? 0.5978 0.6065 0.5972 -0.0369 0.0066  0.0181  5   SER   A N   
61   C  CA  A SER   A 5   ? 0.5368 0.5715 0.5543 -0.0732 0.0370  0.0260  5   SER   A CA  
62   C  CA  B SER   A 5   ? 0.5476 0.5614 0.5461 -0.0462 0.0192  0.0111  5   SER   A CA  
63   C  C   A SER   A 5   ? 0.4724 0.5123 0.4744 -0.0906 0.0583  0.0281  5   SER   A C   
64   C  C   B SER   A 5   ? 0.4942 0.5114 0.4788 -0.0533 0.0305  0.0099  5   SER   A C   
65   O  O   A SER   A 5   ? 0.4758 0.5133 0.4682 -0.0895 0.0613  0.0232  5   SER   A O   
66   O  O   B SER   A 5   ? 0.4956 0.5115 0.4727 -0.0538 0.0337  0.0073  5   SER   A O   
67   C  CB  A SER   A 5   ? 0.5413 0.5796 0.5799 -0.0747 0.0361  0.0165  5   SER   A CB  
68   C  CB  B SER   A 5   ? 0.5505 0.5655 0.5667 -0.0474 0.0206  0.0070  5   SER   A CB  
69   O  OG  A SER   A 5   ? 0.5435 0.5839 0.5920 -0.0761 0.0356  0.0112  5   SER   A OG  
70   O  OG  B SER   A 5   ? 0.5521 0.5677 0.5758 -0.0482 0.0211  0.0045  5   SER   A OG  
81   N  N   A PHE   A 6   ? 0.4035 0.4512 0.3933 -0.1089 0.0769  0.0394  6   PHE   A N   
82   N  N   B PHE   A 6   ? 0.4393 0.4610 0.4162 -0.0593 0.0373  0.0120  6   PHE   A N   
83   C  CA  A PHE   A 6   ? 0.3377 0.3887 0.3161 -0.1204 0.0844  0.0570  6   PHE   A CA  
84   C  CA  B PHE   A 6   ? 0.3865 0.4111 0.3617 -0.0628 0.0410  0.0167  6   PHE   A CA  
85   C  C   A PHE   A 6   ? 0.3211 0.3740 0.3059 -0.1218 0.0916  0.0504  6   PHE   A C   
86   C  C   B PHE   A 6   ? 0.3641 0.3953 0.3599 -0.0674 0.0466  0.0185  6   PHE   A C   
87   O  O   A PHE   A 6   ? 0.3242 0.3758 0.3376 -0.1223 0.0875  0.0610  6   PHE   A O   
88   O  O   B PHE   A 6   ? 0.3678 0.3981 0.3739 -0.0665 0.0441  0.0223  6   PHE   A O   
89   C  CB  A PHE   A 6   ? 0.2989 0.3447 0.2768 -0.1195 0.0662  0.0709  6   PHE   A CB  
90   C  CB  B PHE   A 6   ? 0.3601 0.3789 0.3234 -0.0599 0.0358  0.0140  6   PHE   A CB  
91   C  CG  A PHE   A 6   ? 0.2659 0.3100 0.2480 -0.1074 0.0394  0.0680  6   PHE   A CG  
92   C  CG  B PHE   A 6   ? 0.3369 0.3502 0.2929 -0.0578 0.0293  0.0100  6   PHE   A CG  
93   C  CD1 A PHE   A 6   ? 0.2473 0.2990 0.2502 -0.1000 0.0256  0.0609  6   PHE   A CD1 
94   C  CD1 B PHE   A 6   ? 0.3257 0.3387 0.2835 -0.0560 0.0245  0.0109  6   PHE   A CD1 
95   C  CD2 A PHE   A 6   ? 0.2653 0.2973 0.2545 -0.0892 0.0327  0.0708  6   PHE   A CD2 
96   C  CD2 B PHE   A 6   ? 0.3311 0.3384 0.2917 -0.0527 0.0295  0.0059  6   PHE   A CD2 
97   C  CE1 A PHE   A 6   ? 0.2407 0.2904 0.2481 -0.0930 0.0246  0.0643  6   PHE   A CE1 
98   C  CE1 B PHE   A 6   ? 0.3206 0.3313 0.2828 -0.0560 0.0280  0.0125  6   PHE   A CE1 
99   C  CE2 A PHE   A 6   ? 0.2579 0.2939 0.2648 -0.0798 0.0290  0.0629  6   PHE   A CE2 
100  C  CE2 B PHE   A 6   ? 0.3254 0.3315 0.2854 -0.0513 0.0304  0.0064  6   PHE   A CE2 
101  C  CZ  A PHE   A 6   ? 0.2501 0.2888 0.2536 -0.0828 0.0220  0.0595  6   PHE   A CZ  
102  C  CZ  B PHE   A 6   ? 0.3212 0.3289 0.2846 -0.0534 0.0297  0.0086  6   PHE   A CZ  
121  N  N   A SER   A 7   ? 0.3007 0.3555 0.2754 -0.1207 0.0988  0.0290  7   SER   A N   
122  N  N   B SER   A 7   ? 0.3380 0.3765 0.3447 -0.0723 0.0510  0.0133  7   SER   A N   
123  C  CA  A SER   A 7   ? 0.2942 0.3424 0.2727 -0.1062 0.0924  0.0043  7   SER   A CA  
124  C  CA  B SER   A 7   ? 0.3180 0.3585 0.3410 -0.0736 0.0539  0.0054  7   SER   A CA  
125  C  C   A SER   A 7   ? 0.2769 0.3136 0.2653 -0.1002 0.0963  -0.0033 7   SER   A C   
126  C  C   B SER   A 7   ? 0.3002 0.3362 0.3171 -0.0712 0.0561  0.0034  7   SER   A C   
127  O  O   A SER   A 7   ? 0.2846 0.3077 0.2606 -0.1084 0.0968  -0.0039 7   SER   A O   
128  O  O   B SER   A 7   ? 0.3025 0.3338 0.3127 -0.0747 0.0540  0.0012  7   SER   A O   
129  C  CB  A SER   A 7   ? 0.3118 0.3575 0.2871 -0.0967 0.0785  -0.0015 7   SER   A CB  
130  C  CB  B SER   A 7   ? 0.3209 0.3620 0.3643 -0.0715 0.0492  -0.0009 7   SER   A CB  
131  O  OG  A SER   A 7   ? 0.3284 0.3677 0.3119 -0.0870 0.0629  -0.0119 7   SER   A OG  
132  O  OG  B SER   A 7   ? 0.3249 0.3664 0.3902 -0.0686 0.0427  -0.0094 7   SER   A OG  
143  N  N   A GLY   A 8   ? 0.2520 0.2892 0.2711 -0.0874 0.0952  -0.0076 8   GLY   A N   
144  N  N   B GLY   A 8   ? 0.2811 0.3160 0.2968 -0.0652 0.0580  -0.0030 8   GLY   A N   
145  C  CA  A GLY   A 8   ? 0.2321 0.2647 0.2820 -0.0644 0.0919  -0.0057 8   GLY   A CA  
146  C  CA  B GLY   A 8   ? 0.2620 0.2956 0.2829 -0.0514 0.0607  -0.0018 8   GLY   A CA  
147  C  C   A GLY   A 8   ? 0.2040 0.2470 0.2801 -0.0442 0.0789  -0.0072 8   GLY   A C   
148  C  C   B GLY   A 8   ? 0.2409 0.2772 0.2717 -0.0415 0.0544  -0.0046 8   GLY   A C   
149  O  O   A GLY   A 8   ? 0.2037 0.2480 0.3164 -0.0241 0.0778  -0.0344 8   GLY   A O   
150  O  O   B GLY   A 8   ? 0.2408 0.2773 0.2848 -0.0351 0.0558  -0.0137 8   GLY   A O   
157  N  N   A TYR   A 9   ? 0.1831 0.2335 0.2636 -0.0334 0.0743  0.0201  9   TYR   A N   
158  N  N   B TYR   A 9   ? 0.2188 0.2602 0.2553 -0.0317 0.0469  0.0052  9   TYR   A N   
159  C  CA  A TYR   A 9   ? 0.1618 0.2187 0.2500 -0.0276 0.0595  0.0331  9   TYR   A CA  
160  C  CA  B TYR   A 9   ? 0.1978 0.2406 0.2369 -0.0234 0.0323  0.0152  9   TYR   A CA  
161  C  C   A TYR   A 9   ? 0.1597 0.2009 0.2560 -0.0195 0.0539  0.0459  9   TYR   A C   
162  C  C   B TYR   A 9   ? 0.1945 0.2264 0.2408 -0.0219 0.0332  0.0251  9   TYR   A C   
163  O  O   A TYR   A 9   ? 0.1770 0.2170 0.2707 -0.0204 0.0379  0.0414  9   TYR   A O   
164  O  O   B TYR   A 9   ? 0.2035 0.2344 0.2421 -0.0249 0.0321  0.0240  9   TYR   A O   
165  C  CB  A TYR   A 9   ? 0.1593 0.2342 0.2485 -0.0173 0.0494  0.0296  9   TYR   A CB  
166  C  CB  B TYR   A 9   ? 0.1829 0.2364 0.2255 -0.0113 0.0188  0.0132  9   TYR   A CB  
167  C  CG  A TYR   A 9   ? 0.1579 0.2433 0.2351 -0.0142 0.0439  0.0240  9   TYR   A CG  
168  C  CG  B TYR   A 9   ? 0.1672 0.2285 0.2034 -0.0010 0.0062  0.0135  9   TYR   A CG  
169  C  CD1 A TYR   A 9   ? 0.1637 0.2497 0.2302 -0.0178 0.0385  0.0217  9   TYR   A CD1 
170  C  CD1 B TYR   A 9   ? 0.1628 0.2251 0.1974 0.0002  -0.0003 0.0127  9   TYR   A CD1 
171  C  CD2 A TYR   A 9   ? 0.1505 0.2410 0.2262 -0.0094 0.0382  0.0258  9   TYR   A CD2 
172  C  CD2 B TYR   A 9   ? 0.1630 0.2227 0.1976 -0.0009 0.0020  0.0139  9   TYR   A CD2 
173  C  CE1 A TYR   A 9   ? 0.1667 0.2480 0.2328 -0.0164 0.0426  0.0176  9   TYR   A CE1 
174  C  CE1 B TYR   A 9   ? 0.1652 0.2248 0.2004 0.0009  -0.0041 0.0063  9   TYR   A CE1 
175  C  CE2 A TYR   A 9   ? 0.1546 0.2427 0.2241 -0.0111 0.0400  0.0204  9   TYR   A CE2 
176  C  CE2 B TYR   A 9   ? 0.1669 0.2229 0.1959 -0.0019 0.0038  0.0116  9   TYR   A CE2 
177  C  CZ  A TYR   A 9   ? 0.1517 0.2436 0.2337 -0.0218 0.0492  0.0212  9   TYR   A CZ  
178  C  CZ  B TYR   A 9   ? 0.1681 0.2242 0.2072 -0.0060 0.0024  0.0116  9   TYR   A CZ  
179  O  OH  A TYR   A 9   ? 0.1471 0.2496 0.2500 -0.0392 0.0372  0.0280  9   TYR   A OH  
180  O  OH  B TYR   A 9   ? 0.1811 0.2268 0.2195 -0.0107 0.0017  0.0179  9   TYR   A OH  
199  N  N   A LEU   A 10  ? 0.1581 0.1874 0.2562 -0.0210 0.0422  0.0426  10  LEU   A N   
200  N  N   B LEU   A 10  ? 0.1896 0.2111 0.2409 -0.0226 0.0250  0.0286  10  LEU   A N   
201  C  CA  A LEU   A 10  ? 0.1576 0.1777 0.2465 -0.0268 0.0229  0.0473  10  LEU   A CA  
202  C  CA  B LEU   A 10  ? 0.1838 0.2023 0.2384 -0.0248 0.0149  0.0327  10  LEU   A CA  
203  C  C   A LEU   A 10  ? 0.1534 0.1763 0.2058 -0.0327 0.0121  0.0434  10  LEU   A C   
204  C  C   B LEU   A 10  ? 0.1796 0.1907 0.2134 -0.0335 0.0143  0.0369  10  LEU   A C   
205  O  O   A LEU   A 10  ? 0.1549 0.1636 0.1806 -0.0324 0.0103  0.0338  10  LEU   A O   
206  O  O   B LEU   A 10  ? 0.1821 0.1877 0.1881 -0.0316 0.0122  0.0263  10  LEU   A O   
207  C  CB  A LEU   A 10  ? 0.1634 0.1771 0.2905 -0.0278 0.0132  0.0602  10  LEU   A CB  
208  C  CB  B LEU   A 10  ? 0.1826 0.2102 0.2607 -0.0158 0.0041  0.0372  10  LEU   A CB  
209  C  CG  A LEU   A 10  ? 0.1808 0.1790 0.3216 -0.0118 -0.0200 0.0660  10  LEU   A CG  
210  C  CG  B LEU   A 10  ? 0.1846 0.2212 0.2717 -0.0004 -0.0165 0.0490  10  LEU   A CG  
211  C  CD1 A LEU   A 10  ? 0.1971 0.1762 0.3437 -0.0142 -0.0148 0.0562  10  LEU   A CD1 
212  C  CD1 B LEU   A 10  ? 0.1942 0.2332 0.2988 -0.0055 -0.0062 0.0437  10  LEU   A CD1 
213  C  CD2 A LEU   A 10  ? 0.2004 0.1975 0.3509 -0.0032 -0.0042 0.0486  10  LEU   A CD2 
214  C  CD2 B LEU   A 10  ? 0.1958 0.2280 0.2931 0.0151  -0.0345 0.0558  10  LEU   A CD2 
237  N  N   A LYS   A 11  ? 0.1626 0.1849 0.2212 -0.0350 0.0185  0.0503  11  LYS   A N   
238  N  N   B LYS   A 11  ? 0.1769 0.1816 0.2214 -0.0392 0.0187  0.0481  11  LYS   A N   
239  C  CA  A LYS   A 11  ? 0.1709 0.1858 0.2142 -0.0383 0.0156  0.0432  11  LYS   A CA  
240  C  CA  B LYS   A 11  ? 0.1748 0.1693 0.2173 -0.0453 0.0166  0.0491  11  LYS   A CA  
241  C  C   A LYS   A 11  ? 0.1586 0.1923 0.2184 -0.0435 0.0077  0.0428  11  LYS   A C   
242  C  C   B LYS   A 11  ? 0.1657 0.1636 0.2172 -0.0409 0.0112  0.0486  11  LYS   A C   
243  O  O   A LYS   A 11  ? 0.1610 0.2059 0.2318 -0.0563 0.0041  0.0608  11  LYS   A O   
244  O  O   B LYS   A 11  ? 0.1628 0.1646 0.2268 -0.0306 -0.0062 0.0533  11  LYS   A O   
245  C  CB  A LYS   A 11  ? 0.1926 0.1767 0.1985 -0.0371 0.0102  0.0204  11  LYS   A CB  
246  C  CB  B LYS   A 11  ? 0.1841 0.1625 0.2063 -0.0524 0.0101  0.0392  11  LYS   A CB  
247  C  CG  A LYS   A 11  ? 0.2061 0.1725 0.1790 -0.0315 0.0050  0.0221  11  LYS   A CG  
248  C  CG  B LYS   A 11  ? 0.1919 0.1564 0.1931 -0.0536 0.0089  0.0389  11  LYS   A CG  
249  C  CD  A LYS   A 11  ? 0.2153 0.1670 0.1540 -0.0292 -0.0044 0.0163  11  LYS   A CD  
250  C  CD  B LYS   A 11  ? 0.2020 0.1637 0.1905 -0.0409 0.0070  0.0337  11  LYS   A CD  
251  C  CE  A LYS   A 11  ? 0.2245 0.1650 0.1512 -0.0201 0.0003  0.0222  11  LYS   A CE  
252  C  CE  B LYS   A 11  ? 0.2039 0.1673 0.2009 -0.0335 0.0011  0.0256  11  LYS   A CE  
253  N  NZ  A LYS   A 11  ? 0.2221 0.1640 0.1636 -0.0064 0.0041  0.0274  11  LYS   A NZ  
254  N  NZ  B LYS   A 11  ? 0.1984 0.1665 0.2072 -0.0266 -0.0045 0.0283  11  LYS   A NZ  
281  N  N   A LEU   A 12  ? 0.1548 0.1832 0.2109 -0.0350 0.0014  0.0315  12  LEU   A N   
282  N  N   B LEU   A 12  ? 0.1589 0.1600 0.2160 -0.0445 0.0122  0.0408  12  LEU   A N   
283  C  CA  A LEU   A 12  ? 0.1599 0.1961 0.2010 -0.0289 0.0011  0.0371  12  LEU   A CA  
284  C  CA  B LEU   A 12  ? 0.1626 0.1759 0.2017 -0.0377 0.0067  0.0378  12  LEU   A CA  
285  C  C   A LEU   A 12  ? 0.1640 0.1898 0.1773 -0.0321 0.0089  0.0305  12  LEU   A C   
286  C  C   B LEU   A 12  ? 0.1648 0.1751 0.1752 -0.0420 0.0116  0.0338  12  LEU   A C   
287  O  O   A LEU   A 12  ? 0.1663 0.1988 0.1829 -0.0272 0.0047  0.0135  12  LEU   A O   
288  O  O   B LEU   A 12  ? 0.1598 0.1794 0.1553 -0.0484 0.0170  0.0448  12  LEU   A O   
289  C  CB  A LEU   A 12  ? 0.1732 0.2043 0.2199 -0.0192 -0.0040 0.0544  12  LEU   A CB  
290  C  CB  B LEU   A 12  ? 0.1611 0.1821 0.2048 -0.0305 0.0024  0.0389  12  LEU   A CB  
291  C  CG  A LEU   A 12  ? 0.1774 0.2116 0.2558 -0.0176 0.0072  0.0583  12  LEU   A CG  
292  C  CG  B LEU   A 12  ? 0.1585 0.1898 0.2224 -0.0238 0.0089  0.0329  12  LEU   A CG  
293  C  CD1 A LEU   A 12  ? 0.1836 0.2185 0.2681 -0.0074 0.0175  0.0643  12  LEU   A CD1 
294  C  CD1 B LEU   A 12  ? 0.1572 0.1972 0.2329 -0.0140 0.0235  0.0363  12  LEU   A CD1 
295  C  CD2 A LEU   A 12  ? 0.1772 0.2110 0.2707 -0.0185 0.0083  0.0508  12  LEU   A CD2 
296  C  CD2 B LEU   A 12  ? 0.1575 0.1902 0.2231 -0.0226 0.0024  0.0166  12  LEU   A CD2 
319  N  N   A THR   A 13  ? 0.1596 0.1795 0.1628 -0.0302 0.0106  0.0136  13  THR   A N   
320  N  N   B THR   A 13  ? 0.1654 0.1723 0.1706 -0.0339 0.0184  0.0125  13  THR   A N   
321  C  CA  A THR   A 13  ? 0.1620 0.1694 0.1604 -0.0366 0.0160  0.0126  13  THR   A CA  
322  C  CA  B THR   A 13  ? 0.1680 0.1702 0.1651 -0.0278 0.0255  0.0040  13  THR   A CA  
323  C  C   A THR   A 13  ? 0.1614 0.1618 0.1599 -0.0333 0.0187  0.0221  13  THR   A C   
324  C  C   B THR   A 13  ? 0.1630 0.1645 0.1715 -0.0244 0.0260  0.0031  13  THR   A C   
325  O  O   A THR   A 13  ? 0.1696 0.1695 0.1697 -0.0288 0.0168  0.0180  13  THR   A O   
326  O  O   B THR   A 13  ? 0.1614 0.1639 0.1759 -0.0106 0.0321  0.0028  13  THR   A O   
327  C  CB  A THR   A 13  ? 0.1674 0.1873 0.1675 -0.0336 0.0119  0.0181  13  THR   A CB  
328  C  CB  B THR   A 13  ? 0.1708 0.1766 0.1606 -0.0248 0.0162  0.0115  13  THR   A CB  
329  O  OG1 A THR   A 13  ? 0.1589 0.1857 0.1556 -0.0429 0.0182  0.0179  13  THR   A OG1 
330  O  OG1 B THR   A 13  ? 0.1739 0.1674 0.1903 -0.0194 0.0169  -0.0053 13  THR   A OG1 
331  C  CG2 A THR   A 13  ? 0.1787 0.2007 0.1945 -0.0232 0.0074  0.0212  13  THR   A CG2 
332  C  CG2 B THR   A 13  ? 0.1738 0.1833 0.1541 -0.0280 0.0238  0.0254  13  THR   A CG2 
347  N  N   A ASP   A 14  ? 0.1705 0.1540 0.1731 -0.0353 0.0116  0.0290  14  ASP   A N   
348  N  N   B ASP   A 14  ? 0.1654 0.1714 0.1919 -0.0220 0.0253  0.0022  14  ASP   A N   
349  C  CA  A ASP   A 14  ? 0.1803 0.1624 0.1947 -0.0297 0.0036  0.0416  14  ASP   A CA  
350  C  CA  B ASP   A 14  ? 0.1722 0.1791 0.1914 -0.0200 0.0107  0.0133  14  ASP   A CA  
351  C  C   A ASP   A 14  ? 0.1787 0.1679 0.1728 -0.0289 -0.0065 0.0372  14  ASP   A C   
352  C  C   B ASP   A 14  ? 0.1585 0.1685 0.1448 -0.0185 0.0092  0.0203  14  ASP   A C   
353  O  O   A ASP   A 14  ? 0.1939 0.1791 0.1640 -0.0343 0.0063  0.0216  14  ASP   A O   
354  O  O   B ASP   A 14  ? 0.1660 0.1733 0.1381 -0.0173 0.0178  0.0227  14  ASP   A O   
355  C  CB  A ASP   A 14  ? 0.1975 0.1792 0.2660 -0.0316 0.0040  0.0482  14  ASP   A CB  
356  C  CB  B ASP   A 14  ? 0.1961 0.2089 0.2515 -0.0131 0.0004  0.0186  14  ASP   A CB  
357  C  CG  A ASP   A 14  ? 0.2156 0.2259 0.3482 -0.0279 0.0112  0.0427  14  ASP   A CG  
358  C  CG  B ASP   A 14  ? 0.2184 0.2436 0.3126 -0.0099 -0.0099 0.0149  14  ASP   A CG  
359  O  OD1 A ASP   A 14  ? 0.2152 0.2437 0.3710 -0.0288 0.0122  0.0715  14  ASP   A OD1 
360  O  OD1 B ASP   A 14  ? 0.2303 0.2544 0.3274 -0.0082 -0.0184 0.0314  14  ASP   A OD1 
361  O  OD2 A ASP   A 14  ? 0.2273 0.2460 0.3809 -0.0174 -0.0000 0.0099  14  ASP   A OD2 
362  O  OD2 B ASP   A 14  ? 0.2263 0.2609 0.3499 0.0010  -0.0176 -0.0021 14  ASP   A OD2 
371  N  N   A ASN   A 15  ? 0.1697 0.1639 0.1673 -0.0277 0.0017  0.0346  15  ASN   A N   
372  N  N   B ASN   A 15  ? 0.1432 0.1583 0.1319 -0.0234 0.0122  0.0233  15  ASN   A N   
373  C  CA  A ASN   A 15  ? 0.1625 0.1635 0.1742 -0.0258 -0.0000 0.0267  15  ASN   A CA  
374  C  CA  B ASN   A 15  ? 0.1389 0.1566 0.1498 -0.0245 0.0083  0.0107  15  ASN   A CA  
375  C  C   A ASN   A 15  ? 0.1590 0.1578 0.1789 -0.0216 0.0072  0.0268  15  ASN   A C   
376  C  C   B ASN   A 15  ? 0.1411 0.1522 0.1677 -0.0250 0.0055  0.0107  15  ASN   A C   
377  O  O   A ASN   A 15  ? 0.1644 0.1588 0.1867 -0.0245 -0.0030 0.0204  15  ASN   A O   
378  O  O   B ASN   A 15  ? 0.1433 0.1504 0.1789 -0.0213 -0.0026 0.0054  15  ASN   A O   
379  C  CB  A ASN   A 15  ? 0.1668 0.1696 0.1688 -0.0202 0.0067  0.0274  15  ASN   A CB  
380  C  CB  B ASN   A 15  ? 0.1320 0.1621 0.1484 -0.0220 0.0124  0.0134  15  ASN   A CB  
381  C  CG  A ASN   A 15  ? 0.1664 0.1766 0.1695 -0.0158 0.0186  0.0149  15  ASN   A CG  
382  C  CG  B ASN   A 15  ? 0.1288 0.1731 0.1614 -0.0168 0.0171  0.0073  15  ASN   A CG  
383  O  OD1 A ASN   A 15  ? 0.1723 0.1704 0.1826 -0.0224 0.0351  0.0111  15  ASN   A OD1 
384  O  OD1 B ASN   A 15  ? 0.1377 0.1719 0.1598 -0.0167 0.0273  0.0000  15  ASN   A OD1 
385  N  ND2 A ASN   A 15  ? 0.1689 0.1903 0.1750 -0.0188 0.0050  0.0353  15  ASN   A ND2 
386  N  ND2 B ASN   A 15  ? 0.1344 0.1830 0.1577 -0.0207 0.0061  0.0187  15  ASN   A ND2 
399  N  N   A VAL   A 16  ? 0.1583 0.1532 0.1907 -0.0269 0.0007  0.0289  16  VAL   A N   
400  N  N   B VAL   A 16  ? 0.1431 0.1518 0.1681 -0.0223 0.0011  0.0078  16  VAL   A N   
401  C  CA  A VAL   A 16  ? 0.1550 0.1588 0.1763 -0.0263 0.0041  0.0338  16  VAL   A CA  
402  C  CA  B VAL   A 16  ? 0.1428 0.1491 0.1603 -0.0225 0.0006  0.0053  16  VAL   A CA  
403  C  C   A VAL   A 16  ? 0.1511 0.1714 0.1833 -0.0285 0.0057  0.0251  16  VAL   A C   
404  C  C   B VAL   A 16  ? 0.1409 0.1435 0.1548 -0.0235 -0.0014 0.0109  16  VAL   A C   
405  O  O   A VAL   A 16  ? 0.1496 0.1746 0.1829 -0.0312 0.0187  0.0091  16  VAL   A O   
406  O  O   B VAL   A 16  ? 0.1384 0.1426 0.1426 -0.0307 0.0013  0.0201  16  VAL   A O   
407  C  CB  A VAL   A 16  ? 0.1665 0.1757 0.1593 -0.0058 0.0100  0.0294  16  VAL   A CB  
408  C  CB  B VAL   A 16  ? 0.1519 0.1618 0.1736 -0.0110 0.0130  0.0011  16  VAL   A CB  
409  C  CG1 A VAL   A 16  ? 0.1781 0.1834 0.1581 0.0007  0.0090  0.0262  16  VAL   A CG1 
410  C  CG1 B VAL   A 16  ? 0.1587 0.1731 0.1854 -0.0086 0.0148  -0.0019 16  VAL   A CG1 
411  C  CG2 A VAL   A 16  ? 0.1736 0.1905 0.1848 0.0031  0.0286  0.0228  16  VAL   A CG2 
412  C  CG2 B VAL   A 16  ? 0.1570 0.1654 0.1752 -0.0095 0.0286  0.0072  16  VAL   A CG2 
431  N  N   A TYR   A 17  ? 0.1533 0.1694 0.1768 -0.0284 0.0206  0.0279  17  TYR   A N   
432  N  N   B TYR   A 17  ? 0.1434 0.1353 0.1611 -0.0150 0.0149  0.0191  17  TYR   A N   
433  C  CA  A TYR   A 17  ? 0.1567 0.1679 0.1786 -0.0324 0.0210  0.0282  17  TYR   A CA  
434  C  CA  B TYR   A 17  ? 0.1532 0.1433 0.1599 -0.0226 0.0147  0.0243  17  TYR   A CA  
435  C  C   A TYR   A 17  ? 0.1514 0.1725 0.1936 -0.0255 0.0152  0.0341  17  TYR   A C   
436  C  C   B TYR   A 17  ? 0.1550 0.1494 0.1755 -0.0213 0.0080  0.0189  17  TYR   A C   
437  O  O   A TYR   A 17  ? 0.1424 0.1729 0.1812 -0.0257 0.0069  0.0368  17  TYR   A O   
438  O  O   B TYR   A 17  ? 0.1446 0.1435 0.1489 -0.0237 0.0026  0.0054  17  TYR   A O   
439  C  CB  A TYR   A 17  ? 0.1741 0.1684 0.1871 -0.0367 0.0014  0.0203  17  TYR   A CB  
440  C  CB  B TYR   A 17  ? 0.1693 0.1495 0.1627 -0.0272 -0.0036 0.0402  17  TYR   A CB  
441  C  CG  A TYR   A 17  ? 0.1964 0.1757 0.1945 -0.0406 -0.0110 0.0200  17  TYR   A CG  
442  C  CG  B TYR   A 17  ? 0.1893 0.1622 0.1924 -0.0362 -0.0196 0.0411  17  TYR   A CG  
443  C  CD1 A TYR   A 17  ? 0.2128 0.1857 0.2101 -0.0278 -0.0139 0.0310  17  TYR   A CD1 
444  C  CD1 B TYR   A 17  ? 0.1963 0.1701 0.2169 -0.0364 -0.0300 0.0326  17  TYR   A CD1 
445  C  CD2 A TYR   A 17  ? 0.2115 0.1875 0.1980 -0.0482 -0.0119 0.0236  17  TYR   A CD2 
446  C  CD2 B TYR   A 17  ? 0.1997 0.1702 0.1969 -0.0492 -0.0255 0.0432  17  TYR   A CD2 
447  C  CE1 A TYR   A 17  ? 0.2312 0.1942 0.2269 -0.0261 -0.0188 0.0438  17  TYR   A CE1 
448  C  CE1 B TYR   A 17  ? 0.2040 0.1726 0.2204 -0.0413 -0.0434 0.0294  17  TYR   A CE1 
449  C  CE2 A TYR   A 17  ? 0.2306 0.1919 0.2092 -0.0445 -0.0124 0.0303  17  TYR   A CE2 
450  C  CE2 B TYR   A 17  ? 0.2110 0.1703 0.2139 -0.0558 -0.0346 0.0278  17  TYR   A CE2 
451  C  CZ  A TYR   A 17  ? 0.2420 0.1934 0.2192 -0.0343 -0.0239 0.0477  17  TYR   A CZ  
452  C  CZ  B TYR   A 17  ? 0.2166 0.1688 0.2202 -0.0531 -0.0435 0.0280  17  TYR   A CZ  
453  O  OH  A TYR   A 17  ? 0.2576 0.1992 0.2445 -0.0258 -0.0233 0.0538  17  TYR   A OH  
454  O  OH  B TYR   A 17  ? 0.2301 0.1690 0.2229 -0.0548 -0.0454 0.0188  17  TYR   A OH  
473  N  N   A ILE   A 18  ? 0.1492 0.1705 0.2189 -0.0186 0.0257  0.0454  18  ILE   A N   
474  N  N   B ILE   A 18  ? 0.1607 0.1586 0.2013 -0.0200 0.0120  0.0338  18  ILE   A N   
475  C  CA  A ILE   A 18  ? 0.1493 0.1656 0.2308 -0.0193 0.0224  0.0393  18  ILE   A CA  
476  C  CA  B ILE   A 18  ? 0.1611 0.1660 0.2134 -0.0198 0.0171  0.0311  18  ILE   A CA  
477  C  C   A ILE   A 18  ? 0.1479 0.1748 0.2535 -0.0234 0.0302  0.0448  18  ILE   A C   
478  C  C   B ILE   A 18  ? 0.1589 0.1819 0.2247 -0.0248 0.0185  0.0388  18  ILE   A C   
479  O  O   A ILE   A 18  ? 0.1365 0.1828 0.2547 -0.0285 0.0222  0.0438  18  ILE   A O   
480  O  O   B ILE   A 18  ? 0.1533 0.1915 0.2245 -0.0253 0.0095  0.0370  18  ILE   A O   
481  C  CB  A ILE   A 18  ? 0.1614 0.1654 0.2125 -0.0104 0.0112  0.0503  18  ILE   A CB  
482  C  CB  B ILE   A 18  ? 0.1708 0.1687 0.2159 -0.0130 0.0252  0.0303  18  ILE   A CB  
483  C  CG1 A ILE   A 18  ? 0.1696 0.1775 0.2275 -0.0035 0.0017  0.0571  18  ILE   A CG1 
484  C  CG1 B ILE   A 18  ? 0.1813 0.1826 0.2217 -0.0209 0.0276  0.0271  18  ILE   A CG1 
485  C  CG2 A ILE   A 18  ? 0.1601 0.1562 0.2163 -0.0002 0.0147  0.0388  18  ILE   A CG2 
486  C  CG2 B ILE   A 18  ? 0.1735 0.1665 0.2316 -0.0124 0.0253  0.0369  18  ILE   A CG2 
487  C  CD1 A ILE   A 18  ? 0.1855 0.1923 0.2479 0.0086  -0.0022 0.0668  18  ILE   A CD1 
488  C  CD1 B ILE   A 18  ? 0.1928 0.2003 0.2382 -0.0164 0.0290  0.0242  18  ILE   A CD1 
511  N  N   A LYS   A 19  ? 0.1529 0.1740 0.2615 -0.0105 0.0426  0.0356  19  LYS   A N   
512  N  N   B LYS   A 19  ? 0.1608 0.1855 0.2394 -0.0228 0.0350  0.0385  19  LYS   A N   
513  C  CA  A LYS   A 19  ? 0.1769 0.1924 0.2671 -0.0026 0.0474  0.0285  19  LYS   A CA  
514  C  CA  B LYS   A 19  ? 0.1719 0.1977 0.2434 -0.0211 0.0376  0.0358  19  LYS   A CA  
515  C  C   A LYS   A 19  ? 0.1694 0.1868 0.2741 0.0102  0.0453  0.0172  19  LYS   A C   
516  C  C   B LYS   A 19  ? 0.1592 0.1920 0.2514 -0.0271 0.0411  0.0352  19  LYS   A C   
517  O  O   A LYS   A 19  ? 0.1654 0.1867 0.2785 0.0140  0.0376  0.0335  19  LYS   A O   
518  O  O   B LYS   A 19  ? 0.1540 0.1935 0.2566 -0.0293 0.0428  0.0409  19  LYS   A O   
519  C  CB  A LYS   A 19  ? 0.1885 0.2112 0.2598 -0.0051 0.0599  0.0274  19  LYS   A CB  
520  C  CB  B LYS   A 19  ? 0.1869 0.2131 0.2430 -0.0141 0.0406  0.0278  19  LYS   A CB  
521  C  CG  A LYS   A 19  ? 0.2189 0.2264 0.2580 -0.0066 0.0575  0.0242  19  LYS   A CG  
522  C  CG  B LYS   A 19  ? 0.2005 0.2248 0.2472 -0.0093 0.0362  0.0173  19  LYS   A CG  
523  C  CD  A LYS   A 19  ? 0.2418 0.2448 0.2653 -0.0060 0.0607  0.0271  19  LYS   A CD  
524  C  CD  B LYS   A 19  ? 0.2096 0.2390 0.2517 -0.0035 0.0368  0.0109  19  LYS   A CD  
525  C  CE  A LYS   A 19  ? 0.2549 0.2477 0.2721 -0.0079 0.0561  0.0259  19  LYS   A CE  
526  C  CE  B LYS   A 19  ? 0.2145 0.2427 0.2503 -0.0015 0.0426  0.0141  19  LYS   A CE  
527  N  NZ  A LYS   A 19  ? 0.2619 0.2497 0.2764 -0.0137 0.0638  0.0202  19  LYS   A NZ  
528  N  NZ  B LYS   A 19  ? 0.2135 0.2436 0.2372 0.0040  0.0420  0.0140  19  LYS   A NZ  
555  N  N   A ASN   A 20  ? 0.1745 0.1948 0.2895 0.0082  0.0399  0.0146  20  ASN   A N   
556  N  N   B ASN   A 20  ? 0.1532 0.1923 0.2591 -0.0324 0.0365  0.0428  20  ASN   A N   
557  C  CA  A ASN   A 20  ? 0.1833 0.2105 0.2894 0.0227  0.0337  0.0105  20  ASN   A CA  
558  C  CA  B ASN   A 20  ? 0.1546 0.2028 0.2575 -0.0114 0.0323  0.0422  20  ASN   A CA  
559  C  C   A ASN   A 20  ? 0.1937 0.2085 0.2734 0.0157  0.0421  0.0065  20  ASN   A C   
560  C  C   B ASN   A 20  ? 0.1608 0.2024 0.2456 -0.0020 0.0390  0.0350  20  ASN   A C   
561  O  O   A ASN   A 20  ? 0.2068 0.2155 0.2564 0.0054  0.0414  0.0120  20  ASN   A O   
562  O  O   B ASN   A 20  ? 0.1764 0.2021 0.2473 0.0124  0.0335  0.0342  20  ASN   A O   
563  C  CB  A ASN   A 20  ? 0.1962 0.2259 0.3008 0.0278  0.0338  0.0206  20  ASN   A CB  
564  C  CB  B ASN   A 20  ? 0.1541 0.2106 0.2581 -0.0095 0.0301  0.0508  20  ASN   A CB  
565  C  CG  A ASN   A 20  ? 0.2087 0.2379 0.3236 0.0389  0.0354  0.0231  20  ASN   A CG  
566  C  CG  B ASN   A 20  ? 0.1517 0.2140 0.2685 0.0057  0.0252  0.0617  20  ASN   A CG  
567  O  OD1 A ASN   A 20  ? 0.2233 0.2492 0.3485 0.0415  0.0301  0.0199  20  ASN   A OD1 
568  O  OD1 B ASN   A 20  ? 0.1474 0.2134 0.2790 0.0187  0.0206  0.0589  20  ASN   A OD1 
569  N  ND2 A ASN   A 20  ? 0.2221 0.2406 0.3440 0.0459  0.0334  0.0326  20  ASN   A ND2 
570  N  ND2 B ASN   A 20  ? 0.1674 0.2159 0.2860 0.0099  0.0191  0.0778  20  ASN   A ND2 
583  N  N   A ALA   A 21  ? 0.2003 0.2106 0.2808 0.0123  0.0322  -0.0035 21  ALA   A N   
584  N  N   B ALA   A 21  ? 0.1644 0.2046 0.2521 -0.0100 0.0413  0.0247  21  ALA   A N   
585  C  CA  A ALA   A 21  ? 0.2104 0.2102 0.2690 0.0109  0.0327  0.0148  21  ALA   A CA  
586  C  CA  B ALA   A 21  ? 0.1732 0.2013 0.2441 -0.0145 0.0379  0.0239  21  ALA   A CA  
587  C  C   A ALA   A 21  ? 0.2092 0.2077 0.2598 0.0124  0.0348  0.0125  21  ALA   A C   
588  C  C   B ALA   A 21  ? 0.1581 0.1882 0.2280 -0.0174 0.0342  0.0171  21  ALA   A C   
589  O  O   A ALA   A 21  ? 0.2117 0.2162 0.2621 0.0074  0.0331  0.0053  21  ALA   A O   
590  O  O   B ALA   A 21  ? 0.1473 0.1835 0.2274 -0.0289 0.0255  0.0008  21  ALA   A O   
591  C  CB  A ALA   A 21  ? 0.2199 0.2132 0.2859 0.0080  0.0246  0.0236  21  ALA   A CB  
592  C  CB  B ALA   A 21  ? 0.1845 0.2077 0.2648 -0.0114 0.0254  0.0154  21  ALA   A CB  
603  N  N   A ASP   A 22  ? 0.2106 0.1994 0.2680 0.0091  0.0363  0.0094  22  ASP   A N   
604  N  N   B ASP   A 22  ? 0.1614 0.1833 0.2393 -0.0151 0.0338  0.0116  22  ASP   A N   
605  C  CA  A ASP   A 22  ? 0.2142 0.1935 0.2607 0.0112  0.0309  0.0116  22  ASP   A CA  
606  C  CA  B ASP   A 22  ? 0.1668 0.1766 0.2418 -0.0118 0.0337  0.0162  22  ASP   A CA  
607  C  C   A ASP   A 22  ? 0.2044 0.1935 0.2278 0.0052  0.0337  0.0203  22  ASP   A C   
608  C  C   B ASP   A 22  ? 0.1518 0.1761 0.2185 -0.0264 0.0398  0.0093  22  ASP   A C   
609  O  O   A ASP   A 22  ? 0.2110 0.2043 0.2430 -0.0027 0.0373  0.0260  22  ASP   A O   
610  O  O   B ASP   A 22  ? 0.1481 0.1820 0.2180 -0.0379 0.0350  -0.0063 22  ASP   A O   
611  C  CB  A ASP   A 22  ? 0.2315 0.1941 0.2970 0.0115  0.0264  -0.0039 22  ASP   A CB  
612  C  CB  B ASP   A 22  ? 0.1837 0.1799 0.2708 0.0004  0.0413  0.0178  22  ASP   A CB  
613  C  CG  A ASP   A 22  ? 0.2372 0.1936 0.3404 0.0084  0.0121  0.0015  22  ASP   A CG  
614  C  CG  B ASP   A 22  ? 0.1926 0.1846 0.2858 0.0098  0.0493  0.0304  22  ASP   A CG  
615  O  OD1 A ASP   A 22  ? 0.2347 0.1858 0.3504 -0.0049 -0.0170 0.0142  22  ASP   A OD1 
616  O  OD1 B ASP   A 22  ? 0.1967 0.1811 0.2831 0.0098  0.0465  0.0358  22  ASP   A OD1 
617  O  OD2 A ASP   A 22  ? 0.2423 0.2002 0.3676 0.0210  0.0282  -0.0067 22  ASP   A OD2 
618  O  OD2 B ASP   A 22  ? 0.2005 0.1998 0.3139 0.0109  0.0499  0.0349  22  ASP   A OD2 
627  N  N   A ILE   A 23  ? 0.1976 0.1889 0.2045 0.0052  0.0307  0.0193  23  ILE   A N   
628  N  N   B ILE   A 23  ? 0.1504 0.1740 0.2149 -0.0221 0.0357  0.0103  23  ILE   A N   
629  C  CA  A ILE   A 23  ? 0.1916 0.1832 0.2013 0.0020  0.0276  0.0175  23  ILE   A CA  
630  C  CA  B ILE   A 23  ? 0.1518 0.1790 0.2015 -0.0220 0.0232  0.0146  23  ILE   A CA  
631  C  C   A ILE   A 23  ? 0.1854 0.1899 0.2037 0.0060  0.0396  0.0196  23  ILE   A C   
632  C  C   B ILE   A 23  ? 0.1599 0.1890 0.1975 -0.0278 0.0242  0.0063  23  ILE   A C   
633  O  O   A ILE   A 23  ? 0.1896 0.2024 0.2031 0.0030  0.0356  0.0173  23  ILE   A O   
634  O  O   B ILE   A 23  ? 0.1597 0.1869 0.1941 -0.0280 0.0258  0.0065  23  ILE   A O   
635  C  CB  A ILE   A 23  ? 0.2008 0.1789 0.1836 0.0032  0.0191  0.0125  23  ILE   A CB  
636  C  CB  B ILE   A 23  ? 0.1532 0.1754 0.1866 -0.0064 0.0163  0.0169  23  ILE   A CB  
637  C  CG1 A ILE   A 23  ? 0.2070 0.1739 0.1840 0.0028  0.0220  0.0084  23  ILE   A CG1 
638  C  CG1 B ILE   A 23  ? 0.1574 0.1753 0.1849 -0.0093 0.0129  0.0049  23  ILE   A CG1 
639  C  CG2 A ILE   A 23  ? 0.2023 0.1820 0.1883 0.0011  0.0241  0.0227  23  ILE   A CG2 
640  C  CG2 B ILE   A 23  ? 0.1553 0.1708 0.1781 0.0049  0.0196  0.0228  23  ILE   A CG2 
641  C  CD1 A ILE   A 23  ? 0.2138 0.1751 0.1935 0.0052  0.0076  0.0058  23  ILE   A CD1 
642  C  CD1 B ILE   A 23  ? 0.1593 0.1772 0.1866 -0.0112 0.0037  0.0006  23  ILE   A CD1 
665  N  N   A VAL   A 24  ? 0.1894 0.1920 0.2165 -0.0010 0.0343  0.0150  24  VAL   A N   
666  N  N   B VAL   A 24  ? 0.1727 0.2011 0.2083 -0.0372 0.0202  0.0055  24  VAL   A N   
667  C  CA  A VAL   A 24  ? 0.2023 0.2014 0.2325 -0.0122 0.0360  0.0107  24  VAL   A CA  
668  C  CA  B VAL   A 24  ? 0.1921 0.2113 0.2224 -0.0418 0.0245  0.0108  24  VAL   A CA  
669  C  C   A VAL   A 24  ? 0.2079 0.2130 0.2290 -0.0216 0.0411  0.0084  24  VAL   A C   
670  C  C   B VAL   A 24  ? 0.2053 0.2315 0.2261 -0.0380 0.0300  0.0069  24  VAL   A C   
671  O  O   A VAL   A 24  ? 0.2267 0.2184 0.2316 -0.0180 0.0423  -0.0007 24  VAL   A O   
672  O  O   B VAL   A 24  ? 0.2170 0.2361 0.2355 -0.0365 0.0284  0.0020  24  VAL   A O   
673  C  CB  A VAL   A 24  ? 0.2065 0.1999 0.2573 -0.0128 0.0410  0.0103  24  VAL   A CB  
674  C  CB  B VAL   A 24  ? 0.1966 0.2094 0.2498 -0.0497 0.0233  0.0255  24  VAL   A CB  
675  C  CG1 A VAL   A 24  ? 0.2122 0.2060 0.2679 -0.0079 0.0440  0.0002  24  VAL   A CG1 
676  C  CG1 B VAL   A 24  ? 0.2063 0.2151 0.2726 -0.0459 0.0152  0.0264  24  VAL   A CG1 
677  C  CG2 A VAL   A 24  ? 0.2153 0.2035 0.2649 -0.0113 0.0526  0.0211  24  VAL   A CG2 
678  C  CG2 B VAL   A 24  ? 0.2017 0.2096 0.2529 -0.0549 0.0252  0.0213  24  VAL   A CG2 
697  N  N   A GLU   A 25  ? 0.2099 0.2341 0.2364 -0.0266 0.0526  0.0054  25  GLU   A N   
698  N  N   B GLU   A 25  ? 0.2146 0.2515 0.2349 -0.0311 0.0442  0.0052  25  GLU   A N   
699  C  CA  A GLU   A 25  ? 0.2251 0.2621 0.2526 -0.0156 0.0648  0.0058  25  GLU   A CA  
700  C  CA  B GLU   A 25  ? 0.2309 0.2719 0.2504 -0.0226 0.0496  0.0044  25  GLU   A CA  
701  C  C   A GLU   A 25  ? 0.2129 0.2644 0.2210 -0.0298 0.0692  0.0041  25  GLU   A C   
702  C  C   B GLU   A 25  ? 0.2273 0.2783 0.2424 -0.0277 0.0479  0.0056  25  GLU   A C   
703  O  O   A GLU   A 25  ? 0.2148 0.2804 0.2213 -0.0341 0.0675  0.0017  25  GLU   A O   
704  O  O   B GLU   A 25  ? 0.2337 0.2874 0.2576 -0.0266 0.0483  0.0032  25  GLU   A O   
705  C  CB  A GLU   A 25  ? 0.2569 0.2949 0.3028 -0.0045 0.0722  0.0122  25  GLU   A CB  
706  C  CB  B GLU   A 25  ? 0.2557 0.2903 0.2873 -0.0128 0.0564  0.0051  25  GLU   A CB  
707  C  CG  A GLU   A 25  ? 0.2936 0.3252 0.3684 -0.0028 0.0590  0.0092  25  GLU   A CG  
708  C  CG  B GLU   A 25  ? 0.2869 0.3107 0.3395 -0.0079 0.0485  0.0040  25  GLU   A CG  
709  C  CD  A GLU   A 25  ? 0.3265 0.3539 0.4281 0.0021  0.0429  0.0045  25  GLU   A CD  
710  C  CD  B GLU   A 25  ? 0.3142 0.3309 0.3877 -0.0041 0.0365  0.0011  25  GLU   A CD  
711  O  OE1 A GLU   A 25  ? 0.3419 0.3671 0.4409 0.0060  0.0353  -0.0000 25  GLU   A OE1 
712  O  OE1 B GLU   A 25  ? 0.3287 0.3434 0.4118 -0.0009 0.0319  0.0031  25  GLU   A OE1 
713  O  OE2 A GLU   A 25  ? 0.3340 0.3633 0.4524 0.0005  0.0350  -0.0029 25  GLU   A OE2 
714  O  OE2 B GLU   A 25  ? 0.3221 0.3337 0.4091 -0.0052 0.0308  -0.0064 25  GLU   A OE2 
727  N  N   A GLU   A 26  ? 0.2008 0.2480 0.2194 -0.0408 0.0745  -0.0059 26  GLU   A N   
728  N  N   B GLU   A 26  ? 0.2199 0.2740 0.2337 -0.0336 0.0487  0.0054  26  GLU   A N   
729  C  CA  A GLU   A 26  ? 0.2179 0.2445 0.2092 -0.0507 0.0613  0.0011  26  GLU   A CA  
730  C  CA  B GLU   A 26  ? 0.2216 0.2704 0.2157 -0.0419 0.0450  0.0105  26  GLU   A CA  
731  C  C   A GLU   A 26  ? 0.2143 0.2361 0.1801 -0.0451 0.0498  0.0068  26  GLU   A C   
732  C  C   B GLU   A 26  ? 0.2140 0.2503 0.1931 -0.0416 0.0503  0.0094  26  GLU   A C   
733  O  O   A GLU   A 26  ? 0.2251 0.2296 0.1779 -0.0538 0.0408  0.0105  26  GLU   A O   
734  O  O   B GLU   A 26  ? 0.2182 0.2483 0.1909 -0.0464 0.0571  0.0083  26  GLU   A O   
735  C  CB  A GLU   A 26  ? 0.2434 0.2476 0.2502 -0.0651 0.0572  0.0076  26  GLU   A CB  
736  C  CB  B GLU   A 26  ? 0.2302 0.2855 0.2255 -0.0501 0.0276  0.0176  26  GLU   A CB  
737  C  CG  A GLU   A 26  ? 0.2647 0.2628 0.3246 -0.0735 0.0713  -0.0113 26  GLU   A CG  
738  C  CG  B GLU   A 26  ? 0.2394 0.3017 0.2549 -0.0519 0.0200  0.0150  26  GLU   A CG  
739  C  CD  A GLU   A 26  ? 0.2722 0.2669 0.3493 -0.0821 0.1073  -0.0280 26  GLU   A CD  
740  C  CD  B GLU   A 26  ? 0.2390 0.3100 0.2555 -0.0542 0.0216  0.0156  26  GLU   A CD  
741  O  OE1 A GLU   A 26  ? 0.2639 0.2773 0.3624 -0.0814 0.1244  -0.0692 26  GLU   A OE1 
742  O  OE1 B GLU   A 26  ? 0.2468 0.3164 0.2516 -0.0518 0.0291  0.0118  26  GLU   A OE1 
743  O  OE2 A GLU   A 26  ? 0.2868 0.2698 0.3461 -0.0781 0.1277  -0.0225 26  GLU   A OE2 
744  O  OE2 B GLU   A 26  ? 0.2282 0.3124 0.2413 -0.0587 0.0145  0.0148  26  GLU   A OE2 
757  N  N   . ALA   A 27  ? 0.1983 0.2322 0.1822 -0.0410 0.0455  0.0086  27  ALA   A N   
758  C  CA  . ALA   A 27  ? 0.2061 0.2503 0.1721 -0.0370 0.0403  0.0077  27  ALA   A CA  
759  C  C   . ALA   A 27  ? 0.2446 0.2830 0.1847 -0.0478 0.0532  -0.0109 27  ALA   A C   
760  O  O   . ALA   A 27  ? 0.2410 0.2753 0.1898 -0.0564 0.0439  -0.0021 27  ALA   A O   
761  C  CB  . ALA   A 27  ? 0.1888 0.2379 0.1782 -0.0369 0.0363  0.0087  27  ALA   A CB  
768  N  N   A LYS   A 28  ? 0.2829 0.3096 0.2059 -0.0458 0.0467  -0.0368 28  LYS   A N   
769  N  N   B LYS   A 28  ? 0.2771 0.3041 0.2136 -0.0371 0.0403  -0.0278 28  LYS   A N   
770  C  CA  A LYS   A 28  ? 0.3228 0.3492 0.2403 -0.0361 0.0492  -0.0571 28  LYS   A CA  
771  C  CA  B LYS   A 28  ? 0.3094 0.3329 0.2519 -0.0225 0.0319  -0.0421 28  LYS   A CA  
772  C  C   A LYS   A 28  ? 0.3470 0.3800 0.2296 -0.0433 0.0591  -0.0410 28  LYS   A C   
773  C  C   B LYS   A 28  ? 0.3287 0.3522 0.2530 -0.0186 0.0317  -0.0335 28  LYS   A C   
774  O  O   A LYS   A 28  ? 0.3590 0.3902 0.2541 -0.0412 0.0406  -0.0430 28  LYS   A O   
775  O  O   B LYS   A 28  ? 0.3380 0.3604 0.2636 -0.0175 0.0242  -0.0362 28  LYS   A O   
776  C  CB  A LYS   A 28  ? 0.3438 0.3643 0.3130 -0.0224 0.0390  -0.0730 28  LYS   A CB  
777  C  CB  B LYS   A 28  ? 0.3261 0.3459 0.3044 -0.0145 0.0223  -0.0537 28  LYS   A CB  
778  C  CG  A LYS   A 28  ? 0.3626 0.3772 0.3698 -0.0117 0.0366  -0.0776 28  LYS   A CG  
779  C  CG  B LYS   A 28  ? 0.3418 0.3573 0.3472 -0.0081 0.0182  -0.0587 28  LYS   A CG  
780  C  CD  A LYS   A 28  ? 0.3797 0.3940 0.4366 -0.0018 0.0277  -0.0734 28  LYS   A CD  
781  C  CD  B LYS   A 28  ? 0.3574 0.3715 0.4024 -0.0013 0.0118  -0.0577 28  LYS   A CD  
782  C  CE  A LYS   A 28  ? 0.3919 0.4049 0.4753 0.0054  0.0226  -0.0782 28  LYS   A CE  
783  C  CE  B LYS   A 28  ? 0.3695 0.3811 0.4371 0.0036  0.0081  -0.0617 28  LYS   A CE  
784  N  NZ  A LYS   A 28  ? 0.4007 0.4106 0.5068 0.0116  0.0219  -0.0873 28  LYS   A NZ  
785  N  NZ  B LYS   A 28  ? 0.3772 0.3860 0.4629 0.0075  0.0050  -0.0675 28  LYS   A NZ  
812  N  N   A LYS   A 29  ? 0.3559 0.3996 0.2156 -0.0546 0.0887  -0.0163 29  LYS   A N   
813  N  N   B LYS   A 29  ? 0.3361 0.3624 0.2548 -0.0165 0.0418  -0.0180 29  LYS   A N   
814  C  CA  A LYS   A 29  ? 0.3695 0.4205 0.2428 -0.0622 0.1075  0.0020  29  LYS   A CA  
815  C  CA  B LYS   A 29  ? 0.3448 0.3748 0.2730 -0.0154 0.0491  -0.0033 29  LYS   A CA  
816  C  C   A LYS   A 29  ? 0.3674 0.4129 0.2317 -0.0767 0.0958  0.0189  29  LYS   A C   
817  C  C   B LYS   A 29  ? 0.3363 0.3654 0.2417 -0.0198 0.0431  0.0115  29  LYS   A C   
818  O  O   A LYS   A 29  ? 0.3802 0.4274 0.2537 -0.0677 0.0845  0.0124  29  LYS   A O   
819  O  O   B LYS   A 29  ? 0.3392 0.3738 0.2396 -0.0133 0.0431  0.0133  29  LYS   A O   
820  C  CB  A LYS   A 29  ? 0.3854 0.4486 0.3052 -0.0514 0.1215  0.0019  29  LYS   A CB  
821  C  CB  B LYS   A 29  ? 0.3618 0.3960 0.3271 -0.0089 0.0560  -0.0034 29  LYS   A CB  
822  C  CG  A LYS   A 29  ? 0.4050 0.4739 0.3852 -0.0407 0.1186  0.0031  29  LYS   A CG  
823  C  CG  B LYS   A 29  ? 0.3797 0.4152 0.3893 -0.0029 0.0576  -0.0039 29  LYS   A CG  
824  C  CD  A LYS   A 29  ? 0.4217 0.4956 0.4578 -0.0320 0.1128  0.0008  29  LYS   A CD  
825  C  CD  B LYS   A 29  ? 0.3949 0.4310 0.4427 0.0021  0.0574  -0.0042 29  LYS   A CD  
826  C  CE  A LYS   A 29  ? 0.4343 0.5105 0.5037 -0.0268 0.1092  -0.0022 29  LYS   A CE  
827  C  CE  B LYS   A 29  ? 0.4050 0.4423 0.4798 0.0046  0.0575  -0.0062 29  LYS   A CE  
828  N  NZ  A LYS   A 29  ? 0.4403 0.5185 0.5364 -0.0225 0.1039  -0.0050 29  LYS   A NZ  
829  N  NZ  B LYS   A 29  ? 0.4108 0.4481 0.5039 0.0061  0.0538  -0.0060 29  LYS   A NZ  
856  N  N   A VAL   A 30  ? 0.3517 0.3900 0.2023 -0.0963 0.0915  0.0322  30  VAL   A N   
857  N  N   B VAL   A 30  ? 0.3239 0.3474 0.2228 -0.0307 0.0385  0.0227  30  VAL   A N   
858  C  CA  A VAL   A 30  ? 0.3449 0.3680 0.1952 -0.1121 0.0636  0.0434  30  VAL   A CA  
859  C  CA  B VAL   A 30  ? 0.3131 0.3295 0.2183 -0.0416 0.0204  0.0346  30  VAL   A CA  
860  C  C   A VAL   A 30  ? 0.3454 0.3498 0.1574 -0.1088 0.0449  0.0442  30  VAL   A C   
861  C  C   B VAL   A 30  ? 0.3097 0.3192 0.1983 -0.0393 0.0080  0.0359  30  VAL   A C   
862  O  O   A VAL   A 30  ? 0.3576 0.3495 0.1620 -0.1025 0.0430  0.0507  30  VAL   A O   
863  O  O   B VAL   A 30  ? 0.3139 0.3171 0.1939 -0.0378 0.0051  0.0422  30  VAL   A O   
864  C  CB  A VAL   A 30  ? 0.3392 0.3639 0.2282 -0.1271 0.0497  0.0476  30  VAL   A CB  
865  C  CB  B VAL   A 30  ? 0.3070 0.3211 0.2319 -0.0532 0.0147  0.0421  30  VAL   A CB  
866  C  CG1 A VAL   A 30  ? 0.3457 0.3629 0.2455 -0.1245 0.0384  0.0485  30  VAL   A CG1 
867  C  CG1 B VAL   A 30  ? 0.3091 0.3191 0.2442 -0.0533 0.0114  0.0428  30  VAL   A CG1 
868  C  CG2 A VAL   A 30  ? 0.3363 0.3661 0.2592 -0.1343 0.0492  0.0451  30  VAL   A CG2 
869  C  CG2 B VAL   A 30  ? 0.3049 0.3197 0.2425 -0.0579 0.0152  0.0490  30  VAL   A CG2 
888  N  N   A LYS   A 31  ? 0.3312 0.3321 0.1379 -0.1098 0.0205  0.0386  31  LYS   A N   
889  N  N   B LYS   A 31  ? 0.3046 0.3124 0.2017 -0.0366 -0.0061 0.0314  31  LYS   A N   
890  C  CA  A LYS   A 31  ? 0.3348 0.3278 0.1577 -0.0932 -0.0082 0.0343  31  LYS   A CA  
891  C  CA  B LYS   A 31  ? 0.3044 0.3106 0.2231 -0.0274 -0.0151 0.0284  31  LYS   A CA  
892  C  C   A LYS   A 31  ? 0.3091 0.3016 0.1189 -0.0787 -0.0118 0.0628  31  LYS   A C   
893  C  C   B LYS   A 31  ? 0.2799 0.2935 0.1952 -0.0173 -0.0072 0.0441  31  LYS   A C   
894  O  O   A LYS   A 31  ? 0.3172 0.3127 0.1370 -0.0683 -0.0230 0.0718  31  LYS   A O   
895  O  O   B LYS   A 31  ? 0.2865 0.2996 0.2114 -0.0113 -0.0137 0.0455  31  LYS   A O   
896  C  CB  A LYS   A 31  ? 0.3704 0.3563 0.2690 -0.0798 -0.0270 0.0118  31  LYS   A CB  
897  C  CB  B LYS   A 31  ? 0.3315 0.3304 0.2926 -0.0247 -0.0267 0.0122  31  LYS   A CB  
898  C  CG  A LYS   A 31  ? 0.4058 0.3811 0.3918 -0.0637 -0.0402 -0.0059 31  LYS   A CG  
899  C  CG  B LYS   A 31  ? 0.3580 0.3518 0.3785 -0.0218 -0.0353 -0.0016 31  LYS   A CG  
900  C  CD  A LYS   A 31  ? 0.4348 0.3992 0.4855 -0.0496 -0.0514 -0.0216 31  LYS   A CD  
901  C  CD  B LYS   A 31  ? 0.3785 0.3686 0.4483 -0.0186 -0.0438 -0.0149 31  LYS   A CD  
902  C  CE  A LYS   A 31  ? 0.4534 0.4123 0.5416 -0.0392 -0.0602 -0.0330 31  LYS   A CE  
903  C  CE  B LYS   A 31  ? 0.3925 0.3822 0.4928 -0.0177 -0.0491 -0.0239 31  LYS   A CE  
904  N  NZ  A LYS   A 31  ? 0.4632 0.4176 0.5744 -0.0320 -0.0670 -0.0380 31  LYS   A NZ  
905  N  NZ  B LYS   A 31  ? 0.4009 0.3894 0.5206 -0.0161 -0.0503 -0.0299 31  LYS   A NZ  
932  N  N   A PRO   A 32  ? 0.2760 0.2745 0.1076 -0.0812 -0.0098 0.0477  32  PRO   A N   
933  N  N   B PRO   A 32  ? 0.2508 0.2726 0.1696 -0.0150 0.0082  0.0397  32  PRO   A N   
934  C  CA  A PRO   A 32  ? 0.2681 0.2580 0.1493 -0.0725 -0.0157 0.0577  32  PRO   A CA  
935  C  CA  B PRO   A 32  ? 0.2382 0.2610 0.1695 -0.0094 0.0079  0.0467  32  PRO   A CA  
936  C  C   A PRO   A 32  ? 0.2608 0.2467 0.1619 -0.0622 -0.0231 0.0570  32  PRO   A C   
937  C  C   B PRO   A 32  ? 0.2309 0.2530 0.1671 -0.0044 -0.0070 0.0523  32  PRO   A C   
938  O  O   A PRO   A 32  ? 0.2516 0.2365 0.1517 -0.0676 -0.0272 0.0460  32  PRO   A O   
939  O  O   B PRO   A 32  ? 0.2272 0.2511 0.1752 0.0000  -0.0190 0.0515  32  PRO   A O   
940  C  CB  A PRO   A 32  ? 0.2630 0.2635 0.1632 -0.0751 -0.0179 0.0469  32  PRO   A CB  
941  C  CB  B PRO   A 32  ? 0.2346 0.2642 0.1758 -0.0095 0.0133  0.0326  32  PRO   A CB  
942  C  CG  A PRO   A 32  ? 0.2601 0.2708 0.1078 -0.0738 -0.0333 0.0372  32  PRO   A CG  
943  C  CG  B PRO   A 32  ? 0.2359 0.2689 0.1500 -0.0094 0.0139  0.0245  32  PRO   A CG  
944  C  CD  A PRO   A 32  ? 0.2634 0.2721 0.1142 -0.0796 -0.0234 0.0390  32  PRO   A CD  
945  C  CD  B PRO   A 32  ? 0.2407 0.2715 0.1570 -0.0128 0.0134  0.0275  32  PRO   A CD  
960  N  N   A THR   A 33  ? 0.2626 0.2447 0.1594 -0.0460 -0.0355 0.0605  33  THR   A N   
961  N  N   B THR   A 33  ? 0.2320 0.2461 0.1631 -0.0042 -0.0153 0.0535  33  THR   A N   
962  C  CA  A THR   A 33  ? 0.2627 0.2437 0.1734 -0.0316 -0.0426 0.0612  33  THR   A CA  
963  C  CA  B THR   A 33  ? 0.2336 0.2360 0.1655 -0.0036 -0.0233 0.0555  33  THR   A CA  
964  C  C   A THR   A 33  ? 0.2325 0.2249 0.1662 -0.0291 -0.0395 0.0535  33  THR   A C   
965  C  C   B THR   A 33  ? 0.2173 0.2145 0.1638 -0.0161 -0.0254 0.0487  33  THR   A C   
966  O  O   A THR   A 33  ? 0.2235 0.2169 0.1796 -0.0262 -0.0482 0.0553  33  THR   A O   
967  O  O   B THR   A 33  ? 0.2104 0.2001 0.1746 -0.0167 -0.0221 0.0434  33  THR   A O   
968  C  CB  A THR   A 33  ? 0.2886 0.2666 0.1989 -0.0211 -0.0489 0.0732  33  THR   A CB  
969  C  CB  B THR   A 33  ? 0.2530 0.2487 0.1738 0.0071  -0.0223 0.0703  33  THR   A CB  
970  O  OG1 A THR   A 33  ? 0.3096 0.2808 0.2296 -0.0107 -0.0432 0.0855  33  THR   A OG1 
971  O  OG1 B THR   A 33  ? 0.2676 0.2596 0.1889 0.0171  -0.0246 0.0879  33  THR   A OG1 
972  C  CG2 A THR   A 33  ? 0.2926 0.2746 0.2066 -0.0161 -0.0553 0.0728  33  THR   A CG2 
973  C  CG2 B THR   A 33  ? 0.2552 0.2515 0.1854 0.0094  -0.0212 0.0648  33  THR   A CG2 
988  N  N   . VAL   A 34  ? 0.2060 0.2141 0.1547 -0.0315 -0.0246 0.0481  34  VAL   A N   
989  C  CA  . VAL   A 34  ? 0.1912 0.1960 0.1369 -0.0261 -0.0195 0.0404  34  VAL   A CA  
990  C  C   . VAL   A 34  ? 0.1801 0.1826 0.1348 -0.0280 -0.0121 0.0428  34  VAL   A C   
991  O  O   . VAL   A 34  ? 0.1798 0.1840 0.1733 -0.0341 -0.0100 0.0414  34  VAL   A O   
992  C  CB  . VAL   A 34  ? 0.1929 0.1959 0.1522 -0.0261 -0.0138 0.0272  34  VAL   A CB  
993  C  CG1 . VAL   A 34  ? 0.2001 0.1967 0.1673 -0.0222 -0.0092 0.0181  34  VAL   A CG1 
994  C  CG2 . VAL   A 34  ? 0.1988 0.2126 0.1823 -0.0240 -0.0157 0.0259  34  VAL   A CG2 
1005 N  N   . VAL   A 35  ? 0.1666 0.1744 0.1295 -0.0284 -0.0142 0.0339  35  VAL   A N   
1006 C  CA  . VAL   A 35  ? 0.1586 0.1698 0.1381 -0.0225 -0.0059 0.0293  35  VAL   A CA  
1007 C  C   . VAL   A 35  ? 0.1521 0.1580 0.1261 -0.0144 -0.0027 0.0258  35  VAL   A C   
1008 O  O   . VAL   A 35  ? 0.1439 0.1730 0.1537 -0.0258 0.0111  0.0161  35  VAL   A O   
1009 C  CB  . VAL   A 35  ? 0.1601 0.1731 0.1524 -0.0121 0.0099  0.0143  35  VAL   A CB  
1010 C  CG1 . VAL   A 35  ? 0.1688 0.1761 0.1668 -0.0036 0.0031  0.0069  35  VAL   A CG1 
1011 C  CG2 . VAL   A 35  ? 0.1612 0.1734 0.1773 -0.0094 0.0132  0.0069  35  VAL   A CG2 
1021 N  N   . VAL   A 36  ? 0.1410 0.1557 0.1209 -0.0122 0.0040  0.0241  36  VAL   A N   
1022 C  CA  . VAL   A 36  ? 0.1367 0.1394 0.1402 -0.0107 0.0044  0.0086  36  VAL   A CA  
1023 C  C   . VAL   A 36  ? 0.1366 0.1400 0.1408 -0.0162 0.0065  0.0171  36  VAL   A C   
1024 O  O   . VAL   A 36  ? 0.1398 0.1435 0.1613 -0.0087 0.0172  0.0176  36  VAL   A O   
1025 C  CB  . VAL   A 36  ? 0.1368 0.1352 0.1445 -0.0074 0.0025  0.0186  36  VAL   A CB  
1026 C  CG1 . VAL   A 36  ? 0.1435 0.1395 0.1559 -0.0101 -0.0009 -0.0004 36  VAL   A CG1 
1027 C  CG2 . VAL   A 36  ? 0.1478 0.1447 0.1608 -0.0087 0.0014  0.0359  36  VAL   A CG2 
1037 N  N   . ASN   A 37  ? 0.1332 0.1283 0.1317 -0.0046 0.0015  0.0251  37  ASN   A N   
1038 C  CA  . ASN   A 37  ? 0.1290 0.1324 0.1355 0.0001  0.0007  0.0171  37  ASN   A CA  
1039 C  C   . ASN   A 37  ? 0.1266 0.1305 0.1276 -0.0045 0.0127  0.0251  37  ASN   A C   
1040 O  O   . ASN   A 37  ? 0.1418 0.1399 0.1316 0.0025  0.0087  0.0128  37  ASN   A O   
1041 C  CB  . ASN   A 37  ? 0.1362 0.1312 0.1474 -0.0006 0.0021  0.0176  37  ASN   A CB  
1042 C  CG  . ASN   A 37  ? 0.1327 0.1301 0.1479 0.0031  0.0016  0.0129  37  ASN   A CG  
1043 O  OD1 . ASN   A 37  ? 0.1337 0.1348 0.1706 -0.0031 0.0028  0.0180  37  ASN   A OD1 
1044 N  ND2 . ASN   A 37  ? 0.1382 0.1293 0.1610 -0.0035 -0.0004 0.0239  37  ASN   A ND2 
1051 N  N   A ALA   A 38  ? 0.1268 0.1396 0.1390 -0.0033 0.0087  0.0170  38  ALA   A N   
1052 N  N   B ALA   A 38  ? 0.1283 0.1406 0.1371 -0.0070 0.0036  0.0187  38  ALA   A N   
1053 C  CA  A ALA   A 38  ? 0.1322 0.1425 0.1321 -0.0027 -0.0017 0.0075  38  ALA   A CA  
1054 C  CA  B ALA   A 38  ? 0.1322 0.1487 0.1423 -0.0106 -0.0068 0.0145  38  ALA   A CA  
1055 C  C   A ALA   A 38  ? 0.1336 0.1410 0.1332 -0.0010 -0.0053 -0.0007 38  ALA   A C   
1056 C  C   B ALA   A 38  ? 0.1322 0.1454 0.1367 -0.0056 -0.0119 0.0119  38  ALA   A C   
1057 O  O   A ALA   A 38  ? 0.1339 0.1296 0.1401 -0.0043 -0.0081 -0.0014 38  ALA   A O   
1058 O  O   B ALA   A 38  ? 0.1268 0.1418 0.1526 0.0001  -0.0217 0.0120  38  ALA   A O   
1059 C  CB  A ALA   A 38  ? 0.1397 0.1580 0.1342 -0.0146 -0.0099 0.0044  38  ALA   A CB  
1060 C  CB  B ALA   A 38  ? 0.1372 0.1590 0.1575 -0.0169 -0.0104 0.0058  38  ALA   A CB  
1071 N  N   A ALA   A 39  ? 0.1298 0.1354 0.1548 0.0031  -0.0010 0.0106  39  ALA   A N   
1072 N  N   B ALA   A 39  ? 0.1356 0.1448 0.1403 -0.0087 0.0021  0.0337  39  ALA   A N   
1073 C  CA  A ALA   A 39  ? 0.1249 0.1281 0.1432 0.0080  0.0077  0.0089  39  ALA   A CA  
1074 C  CA  B ALA   A 39  ? 0.1403 0.1490 0.1374 -0.0077 -0.0002 0.0276  39  ALA   A CA  
1075 C  C   A ALA   A 39  ? 0.1343 0.1290 0.1399 0.0024  0.0010  0.0118  39  ALA   A C   
1076 C  C   B ALA   A 39  ? 0.1391 0.1410 0.1506 -0.0099 0.0014  0.0207  39  ALA   A C   
1077 O  O   A ALA   A 39  ? 0.1481 0.1350 0.1392 -0.0011 0.0009  0.0087  39  ALA   A O   
1078 O  O   B ALA   A 39  ? 0.1388 0.1412 0.1472 -0.0147 0.0112  0.0151  39  ALA   A O   
1079 C  CB  A ALA   A 39  ? 0.1239 0.1275 0.1680 0.0128  -0.0117 0.0013  39  ALA   A CB  
1080 C  CB  B ALA   A 39  ? 0.1506 0.1593 0.1427 0.0061  -0.0116 0.0166  39  ALA   A CB  
1091 N  N   A ASN   A 40  ? 0.1457 0.1356 0.1335 -0.0082 0.0219  0.0096  40  ASN   A N   
1092 N  N   B ASN   A 40  ? 0.1474 0.1408 0.1518 -0.0125 0.0158  0.0112  40  ASN   A N   
1093 C  CA  A ASN   A 40  ? 0.1565 0.1316 0.1460 -0.0046 0.0121  0.0054  40  ASN   A CA  
1094 C  CA  B ASN   A 40  ? 0.1542 0.1381 0.1551 -0.0049 0.0152  0.0059  40  ASN   A CA  
1095 C  C   A ASN   A 40  ? 0.1599 0.1220 0.1406 -0.0055 0.0260  0.0126  40  ASN   A C   
1096 C  C   B ASN   A 40  ? 0.1567 0.1294 0.1461 -0.0051 0.0226  0.0107  40  ASN   A C   
1097 O  O   A ASN   A 40  ? 0.1541 0.1288 0.1480 -0.0065 0.0213  0.0169  40  ASN   A O   
1098 O  O   B ASN   A 40  ? 0.1492 0.1335 0.1513 -0.0071 0.0174  0.0146  40  ASN   A O   
1099 C  CB  A ASN   A 40  ? 0.1665 0.1411 0.1623 -0.0010 -0.0013 0.0156  40  ASN   A CB  
1100 C  CB  B ASN   A 40  ? 0.1592 0.1461 0.1578 -0.0002 0.0192  0.0055  40  ASN   A CB  
1101 C  CG  A ASN   A 40  ? 0.1717 0.1442 0.1808 0.0039  -0.0106 0.0257  40  ASN   A CG  
1102 C  CG  B ASN   A 40  ? 0.1607 0.1490 0.1673 -0.0001 0.0267  0.0026  40  ASN   A CG  
1103 O  OD1 A ASN   A 40  ? 0.1797 0.1372 0.2050 -0.0051 -0.0126 0.0186  40  ASN   A OD1 
1104 O  OD1 B ASN   A 40  ? 0.1652 0.1436 0.1656 -0.0064 0.0413  -0.0030 40  ASN   A OD1 
1105 N  ND2 A ASN   A 40  ? 0.1751 0.1606 0.1954 0.0077  -0.0104 0.0146  40  ASN   A ND2 
1106 N  ND2 B ASN   A 40  ? 0.1613 0.1605 0.1916 0.0015  0.0214  -0.0147 40  ASN   A ND2 
1119 N  N   . VAL   A 41  ? 0.1607 0.1302 0.1429 -0.0035 0.0215  0.0132  41  VAL   A N   
1120 C  CA  . VAL   A 41  ? 0.1714 0.1352 0.1591 -0.0033 0.0373  0.0134  41  VAL   A CA  
1121 C  C   . VAL   A 41  ? 0.1643 0.1370 0.1541 -0.0008 0.0322  0.0184  41  VAL   A C   
1122 O  O   . VAL   A 41  ? 0.1640 0.1348 0.1822 0.0036  0.0268  0.0087  41  VAL   A O   
1123 C  CB  . VAL   A 41  ? 0.1882 0.1453 0.1757 -0.0071 0.0413  0.0060  41  VAL   A CB  
1124 C  CG1 . VAL   A 41  ? 0.1966 0.1510 0.1972 -0.0048 0.0379  -0.0040 41  VAL   A CG1 
1125 C  CG2 . VAL   A 41  ? 0.2130 0.1573 0.1691 -0.0178 0.0480  0.0028  41  VAL   A CG2 
1136 N  N   . TYR   A 42  ? 0.1488 0.1292 0.1679 -0.0017 0.0300  0.0232  42  TYR   A N   
1137 C  CA  . TYR   A 42  ? 0.1511 0.1303 0.1691 -0.0065 0.0257  0.0283  42  TYR   A CA  
1138 C  C   . TYR   A 42  ? 0.1408 0.1298 0.1605 -0.0019 0.0226  0.0270  42  TYR   A C   
1139 O  O   . TYR   A 42  ? 0.1431 0.1340 0.1866 -0.0131 0.0206  0.0074  42  TYR   A O   
1140 C  CB  . TYR   A 42  ? 0.1649 0.1422 0.1686 -0.0057 0.0304  0.0363  42  TYR   A CB  
1141 C  CG  . TYR   A 42  ? 0.1832 0.1518 0.1651 -0.0088 0.0205  0.0371  42  TYR   A CG  
1142 C  CD1 . TYR   A 42  ? 0.1916 0.1583 0.1762 -0.0162 0.0341  0.0336  42  TYR   A CD1 
1143 C  CD2 . TYR   A 42  ? 0.2008 0.1718 0.1906 -0.0084 0.0159  0.0275  42  TYR   A CD2 
1144 C  CE1 . TYR   A 42  ? 0.2095 0.1704 0.1810 -0.0176 0.0306  0.0252  42  TYR   A CE1 
1145 C  CE2 . TYR   A 42  ? 0.2202 0.1818 0.2083 -0.0198 0.0138  0.0285  42  TYR   A CE2 
1146 C  CZ  . TYR   A 42  ? 0.2327 0.1797 0.1750 -0.0273 0.0350  0.0245  42  TYR   A CZ  
1147 O  OH  . TYR   A 42  ? 0.2566 0.2015 0.1889 -0.0371 0.0382  0.0127  42  TYR   A OH  
1157 N  N   . LEU   A 43  ? 0.1421 0.1315 0.1426 -0.0040 0.0156  0.0142  43  LEU   A N   
1158 C  CA  . LEU   A 43  ? 0.1369 0.1293 0.1424 -0.0077 0.0079  0.0146  43  LEU   A CA  
1159 C  C   . LEU   A 43  ? 0.1382 0.1365 0.1560 -0.0068 0.0114  0.0093  43  LEU   A C   
1160 O  O   . LEU   A 43  ? 0.1530 0.1421 0.1730 0.0053  -0.0054 0.0022  43  LEU   A O   
1161 C  CB  . LEU   A 43  ? 0.1457 0.1243 0.1738 -0.0089 0.0027  0.0097  43  LEU   A CB  
1162 C  CG  . LEU   A 43  ? 0.1429 0.1328 0.1778 -0.0035 0.0019  0.0070  43  LEU   A CG  
1163 C  CD1 . LEU   A 43  ? 0.1541 0.1404 0.1930 -0.0019 0.0004  0.0112  43  LEU   A CD1 
1164 C  CD2 . LEU   A 43  ? 0.1543 0.1336 0.1753 -0.0057 0.0105  0.0315  43  LEU   A CD2 
1176 N  N   A LYS   A 44  ? 0.1422 0.1312 0.1499 0.0071  0.0073  0.0125  44  LYS   A N   
1177 N  N   B LYS   A 44  ? 0.1502 0.1515 0.1565 -0.0102 0.0071  0.0093  44  LYS   A N   
1178 C  CA  A LYS   A 44  ? 0.1574 0.1272 0.1468 0.0072  0.0161  0.0212  44  LYS   A CA  
1179 C  CA  B LYS   A 44  ? 0.1675 0.1674 0.1625 -0.0192 0.0119  0.0124  44  LYS   A CA  
1180 C  C   A LYS   A 44  ? 0.1390 0.1234 0.1306 0.0116  0.0069  0.0144  44  LYS   A C   
1181 C  C   B LYS   A 44  ? 0.1586 0.1635 0.1384 -0.0182 0.0120  0.0065  44  LYS   A C   
1182 O  O   A LYS   A 44  ? 0.1483 0.1469 0.1523 0.0066  -0.0032 -0.0007 44  LYS   A O   
1183 O  O   B LYS   A 44  ? 0.1623 0.1738 0.1419 -0.0223 0.0083  0.0016  44  LYS   A O   
1184 C  CB  A LYS   A 44  ? 0.1925 0.1371 0.1852 0.0110  0.0317  0.0275  44  LYS   A CB  
1185 C  CB  B LYS   A 44  ? 0.1942 0.1918 0.2010 -0.0235 0.0198  0.0161  44  LYS   A CB  
1186 C  CG  A LYS   A 44  ? 0.2265 0.1703 0.2439 0.0038  0.0525  0.0322  44  LYS   A CG  
1187 C  CG  B LYS   A 44  ? 0.2201 0.2178 0.2495 -0.0265 0.0271  0.0151  44  LYS   A CG  
1188 C  CD  A LYS   A 44  ? 0.2633 0.2232 0.3420 -0.0051 0.0530  0.0302  44  LYS   A CD  
1189 C  CD  B LYS   A 44  ? 0.2483 0.2499 0.3194 -0.0279 0.0241  0.0149  44  LYS   A CD  
1190 C  CE  A LYS   A 44  ? 0.2841 0.2571 0.4126 -0.0106 0.0502  0.0277  44  LYS   A CE  
1191 C  CE  B LYS   A 44  ? 0.2639 0.2726 0.3689 -0.0320 0.0204  0.0164  44  LYS   A CE  
1192 N  NZ  A LYS   A 44  ? 0.2950 0.2836 0.4451 -0.0170 0.0461  0.0285  44  LYS   A NZ  
1193 N  NZ  B LYS   A 44  ? 0.2734 0.2888 0.3911 -0.0380 0.0152  0.0238  44  LYS   A NZ  
1220 N  N   A HIS   A 45  ? 0.1275 0.1271 0.1338 0.0063  -0.0013 0.0126  45  HIS   A N   
1221 N  N   B HIS   A 45  ? 0.1541 0.1604 0.1486 -0.0144 0.0032  0.0084  45  HIS   A N   
1222 C  CA  A HIS   A 45  ? 0.1265 0.1230 0.1398 0.0052  0.0065  0.0096  45  HIS   A CA  
1223 C  CA  B HIS   A 45  ? 0.1535 0.1514 0.1592 -0.0100 -0.0059 0.0048  45  HIS   A CA  
1224 C  C   A HIS   A 45  ? 0.1269 0.1424 0.1491 0.0057  0.0119  0.0213  45  HIS   A C   
1225 C  C   B HIS   A 45  ? 0.1581 0.1581 0.1758 -0.0058 -0.0035 0.0076  45  HIS   A C   
1226 O  O   A HIS   A 45  ? 0.1330 0.1383 0.1732 0.0021  0.0172  0.0119  45  HIS   A O   
1227 O  O   B HIS   A 45  ? 0.1674 0.1606 0.1958 0.0007  -0.0024 -0.0019 45  HIS   A O   
1228 C  CB  A HIS   A 45  ? 0.1318 0.1244 0.1386 0.0032  0.0074  0.0030  45  HIS   A CB  
1229 C  CB  B HIS   A 45  ? 0.1477 0.1475 0.1555 -0.0042 -0.0111 -0.0022 45  HIS   A CB  
1230 C  CG  A HIS   A 45  ? 0.1311 0.1165 0.1347 -0.0059 0.0066  0.0069  45  HIS   A CG  
1231 C  CG  B HIS   A 45  ? 0.1369 0.1456 0.1436 -0.0003 -0.0057 -0.0003 45  HIS   A CG  
1232 N  ND1 A HIS   A 45  ? 0.1258 0.1231 0.1288 -0.0032 0.0039  0.0121  45  HIS   A ND1 
1233 N  ND1 B HIS   A 45  ? 0.1315 0.1481 0.1583 0.0027  -0.0076 0.0067  45  HIS   A ND1 
1234 C  CD2 A HIS   A 45  ? 0.1356 0.1219 0.1469 -0.0032 0.0045  0.0135  45  HIS   A CD2 
1235 C  CD2 B HIS   A 45  ? 0.1305 0.1372 0.1344 0.0061  -0.0078 0.0006  45  HIS   A CD2 
1236 C  CE1 A HIS   A 45  ? 0.1333 0.1313 0.1388 -0.0081 0.0092  0.0165  45  HIS   A CE1 
1237 C  CE1 B HIS   A 45  ? 0.1268 0.1370 0.1186 -0.0040 -0.0155 -0.0061 45  HIS   A CE1 
1238 N  NE2 A HIS   A 45  ? 0.1359 0.1375 0.1517 -0.0024 0.0147  0.0180  45  HIS   A NE2 
1239 N  NE2 B HIS   A 45  ? 0.1250 0.1352 0.1113 -0.0004 -0.0174 -0.0109 45  HIS   A NE2 
1254 N  N   A GLY   A 46  ? 0.1326 0.1606 0.1708 0.0159  -0.0021 0.0347  46  GLY   A N   
1255 N  N   B GLY   A 46  ? 0.1570 0.1576 0.1790 -0.0099 -0.0058 0.0189  46  GLY   A N   
1256 C  CA  A GLY   A 46  ? 0.1404 0.1673 0.1981 0.0124  -0.0003 0.0444  46  GLY   A CA  
1257 C  CA  B GLY   A 46  ? 0.1487 0.1604 0.1755 -0.0095 0.0007  0.0212  46  GLY   A CA  
1258 C  C   A GLY   A 46  ? 0.1464 0.1596 0.1978 0.0224  -0.0052 0.0618  46  GLY   A C   
1259 C  C   B GLY   A 46  ? 0.1491 0.1529 0.1433 0.0007  0.0165  0.0304  46  GLY   A C   
1260 O  O   A GLY   A 46  ? 0.1568 0.1567 0.2180 0.0147  -0.0096 0.0626  46  GLY   A O   
1261 O  O   B GLY   A 46  ? 0.1554 0.1628 0.1498 0.0087  0.0106  0.0257  46  GLY   A O   
1268 N  N   A GLY   A 47  ? 0.1446 0.1618 0.1801 0.0233  -0.0066 0.0478  47  GLY   A N   
1269 N  N   B GLY   A 47  ? 0.1516 0.1486 0.1461 -0.0019 0.0194  0.0165  47  GLY   A N   
1270 C  CA  A GLY   A 47  ? 0.1490 0.1718 0.1735 0.0223  -0.0096 0.0318  47  GLY   A CA  
1271 C  CA  B GLY   A 47  ? 0.1489 0.1540 0.1532 -0.0040 0.0119  0.0114  47  GLY   A CA  
1272 C  C   A GLY   A 47  ? 0.1436 0.1661 0.1670 0.0141  -0.0060 0.0223  47  GLY   A C   
1273 C  C   B GLY   A 47  ? 0.1406 0.1426 0.1277 0.0040  0.0193  0.0013  47  GLY   A C   
1274 O  O   A GLY   A 47  ? 0.1390 0.1560 0.1958 0.0198  -0.0047 0.0317  47  GLY   A O   
1275 O  O   B GLY   A 47  ? 0.1372 0.1346 0.1266 0.0137  0.0020  0.0116  47  GLY   A O   
1282 N  N   A GLY   A 48  ? 0.1385 0.1647 0.1493 0.0181  -0.0064 0.0209  48  GLY   A N   
1283 N  N   B GLY   A 48  ? 0.1372 0.1461 0.1291 0.0051  0.0276  0.0036  48  GLY   A N   
1284 C  CA  A GLY   A 48  ? 0.1356 0.1629 0.1535 0.0065  -0.0104 0.0048  48  GLY   A CA  
1285 C  CA  B GLY   A 48  ? 0.1402 0.1352 0.1287 0.0025  0.0212  0.0035  48  GLY   A CA  
1286 C  C   A GLY   A 48  ? 0.1353 0.1597 0.1391 -0.0011 -0.0004 0.0008  48  GLY   A C   
1287 C  C   B GLY   A 48  ? 0.1468 0.1357 0.1376 0.0004  0.0119  0.0086  48  GLY   A C   
1288 O  O   A GLY   A 48  ? 0.1518 0.1567 0.1390 0.0034  0.0035  0.0181  48  GLY   A O   
1289 O  O   B GLY   A 48  ? 0.1646 0.1358 0.1279 0.0055  0.0252  0.0026  48  GLY   A O   
1296 N  N   A VAL   A 49  ? 0.1389 0.1565 0.1534 -0.0081 -0.0069 0.0061  49  VAL   A N   
1297 N  N   B VAL   A 49  ? 0.1344 0.1328 0.1494 0.0018  0.0046  0.0023  49  VAL   A N   
1298 C  CA  A VAL   A 49  ? 0.1554 0.1420 0.1720 -0.0105 -0.0007 0.0144  49  VAL   A CA  
1299 C  CA  B VAL   A 49  ? 0.1302 0.1385 0.1516 0.0004  0.0021  0.0125  49  VAL   A CA  
1300 C  C   A VAL   A 49  ? 0.1532 0.1330 0.1398 -0.0085 0.0014  0.0235  49  VAL   A C   
1301 C  C   B VAL   A 49  ? 0.1363 0.1358 0.1188 0.0060  0.0009  -0.0095 49  VAL   A C   
1302 O  O   A VAL   A 49  ? 0.1558 0.1378 0.1409 -0.0147 0.0036  0.0114  49  VAL   A O   
1303 O  O   B VAL   A 49  ? 0.1416 0.1449 0.1065 0.0094  0.0065  -0.0055 49  VAL   A O   
1304 C  CB  A VAL   A 49  ? 0.1699 0.1449 0.2038 -0.0129 -0.0127 0.0103  49  VAL   A CB  
1305 C  CB  B VAL   A 49  ? 0.1260 0.1412 0.1720 0.0039  -0.0025 0.0214  49  VAL   A CB  
1306 C  CG1 A VAL   A 49  ? 0.1734 0.1417 0.2277 -0.0059 -0.0090 0.0100  49  VAL   A CG1 
1307 C  CG1 B VAL   A 49  ? 0.1183 0.1345 0.1809 0.0159  -0.0014 0.0292  49  VAL   A CG1 
1308 C  CG2 A VAL   A 49  ? 0.1840 0.1496 0.2440 -0.0309 -0.0174 0.0105  49  VAL   A CG2 
1309 C  CG2 B VAL   A 49  ? 0.1316 0.1475 0.1994 0.0025  -0.0065 0.0246  49  VAL   A CG2 
1328 N  N   A ALA   A 50  ? 0.1407 0.1283 0.1297 -0.0075 -0.0123 0.0177  50  ALA   A N   
1329 N  N   B ALA   A 50  ? 0.1383 0.1309 0.1249 0.0096  -0.0002 -0.0131 50  ALA   A N   
1330 C  CA  A ALA   A 50  ? 0.1307 0.1274 0.1408 -0.0116 -0.0129 0.0241  50  ALA   A CA  
1331 C  CA  B ALA   A 50  ? 0.1422 0.1289 0.1159 0.0057  -0.0000 -0.0099 50  ALA   A CA  
1332 C  C   A ALA   A 50  ? 0.1259 0.1309 0.1461 -0.0126 -0.0079 0.0184  50  ALA   A C   
1333 C  C   B ALA   A 50  ? 0.1496 0.1272 0.0999 0.0036  0.0026  -0.0127 50  ALA   A C   
1334 O  O   A ALA   A 50  ? 0.1248 0.1355 0.1638 -0.0048 -0.0124 0.0143  50  ALA   A O   
1335 O  O   B ALA   A 50  ? 0.1553 0.1268 0.0942 0.0055  0.0025  -0.0096 50  ALA   A O   
1336 C  CB  A ALA   A 50  ? 0.1307 0.1313 0.1556 -0.0065 -0.0139 0.0150  50  ALA   A CB  
1337 C  CB  B ALA   A 50  ? 0.1453 0.1309 0.1084 0.0080  0.0053  -0.0255 50  ALA   A CB  
1348 N  N   A GLY   A 51  ? 0.1300 0.1285 0.1450 0.0020  -0.0141 0.0121  51  GLY   A N   
1349 N  N   B GLY   A 51  ? 0.1540 0.1274 0.1114 0.0085  -0.0029 -0.0130 51  GLY   A N   
1350 C  CA  A GLY   A 51  ? 0.1400 0.1236 0.1626 0.0036  -0.0060 0.0104  51  GLY   A CA  
1351 C  CA  B GLY   A 51  ? 0.1620 0.1254 0.1115 0.0061  -0.0076 -0.0125 51  GLY   A CA  
1352 C  C   A GLY   A 51  ? 0.1214 0.1317 0.1577 0.0026  -0.0004 0.0035  51  GLY   A C   
1353 C  C   B GLY   A 51  ? 0.1536 0.1363 0.1118 0.0054  0.0037  -0.0143 51  GLY   A C   
1354 O  O   A GLY   A 51  ? 0.1275 0.1463 0.1594 0.0001  -0.0143 0.0022  51  GLY   A O   
1355 O  O   B GLY   A 51  ? 0.1569 0.1430 0.1022 0.0055  0.0099  -0.0156 51  GLY   A O   
1362 N  N   A ALA   A 52  ? 0.1221 0.1484 0.1573 0.0027  -0.0035 0.0139  52  ALA   A N   
1363 N  N   B ALA   A 52  ? 0.1503 0.1426 0.0955 0.0029  0.0062  -0.0256 52  ALA   A N   
1364 C  CA  A ALA   A 52  ? 0.1312 0.1561 0.1643 -0.0045 -0.0076 0.0094  52  ALA   A CA  
1365 C  CA  B ALA   A 52  ? 0.1494 0.1496 0.1298 -0.0045 0.0049  -0.0197 52  ALA   A CA  
1366 C  C   A ALA   A 52  ? 0.1313 0.1532 0.1512 -0.0082 -0.0015 0.0101  52  ALA   A C   
1367 C  C   B ALA   A 52  ? 0.1398 0.1469 0.1225 -0.0078 0.0209  -0.0180 52  ALA   A C   
1368 O  O   A ALA   A 52  ? 0.1403 0.1635 0.1542 -0.0017 -0.0039 0.0066  52  ALA   A O   
1369 O  O   B ALA   A 52  ? 0.1464 0.1534 0.1299 -0.0101 0.0276  -0.0148 52  ALA   A O   
1370 C  CB  A ALA   A 52  ? 0.1348 0.1750 0.1898 -0.0078 -0.0073 0.0183  52  ALA   A CB  
1371 C  CB  B ALA   A 52  ? 0.1546 0.1669 0.1604 -0.0070 -0.0032 -0.0081 52  ALA   A CB  
1382 N  N   A LEU   A 53  ? 0.1248 0.1473 0.1451 -0.0071 0.0002  0.0151  53  LEU   A N   
1383 N  N   B LEU   A 53  ? 0.1315 0.1424 0.1197 0.0016  0.0086  -0.0153 53  LEU   A N   
1384 C  CA  A LEU   A 53  ? 0.1427 0.1567 0.1604 -0.0133 -0.0033 0.0122  53  LEU   A CA  
1385 C  CA  B LEU   A 53  ? 0.1355 0.1474 0.1231 0.0039  -0.0047 -0.0029 53  LEU   A CA  
1386 C  C   A LEU   A 53  ? 0.1425 0.1560 0.1392 -0.0080 0.0039  0.0046  53  LEU   A C   
1387 C  C   B LEU   A 53  ? 0.1371 0.1487 0.0992 0.0152  0.0022  -0.0029 53  LEU   A C   
1388 O  O   A LEU   A 53  ? 0.1523 0.1525 0.1707 -0.0225 0.0015  -0.0045 53  LEU   A O   
1389 O  O   B LEU   A 53  ? 0.1434 0.1523 0.0985 0.0180  -0.0018 0.0032  53  LEU   A O   
1390 C  CB  A LEU   A 53  ? 0.1525 0.1555 0.1808 -0.0126 0.0056  0.0125  53  LEU   A CB  
1391 C  CB  B LEU   A 53  ? 0.1356 0.1455 0.1152 -0.0007 -0.0102 0.0020  53  LEU   A CB  
1392 C  CG  A LEU   A 53  ? 0.1560 0.1523 0.1835 -0.0138 -0.0031 0.0089  53  LEU   A CG  
1393 C  CG  B LEU   A 53  ? 0.1343 0.1470 0.1247 -0.0039 -0.0170 0.0070  53  LEU   A CG  
1394 C  CD1 A LEU   A 53  ? 0.1507 0.1549 0.1762 -0.0043 -0.0032 0.0095  53  LEU   A CD1 
1395 C  CD1 B LEU   A 53  ? 0.1376 0.1519 0.1450 -0.0075 -0.0132 -0.0006 53  LEU   A CD1 
1396 C  CD2 A LEU   A 53  ? 0.1648 0.1677 0.1878 -0.0142 -0.0103 0.0121  53  LEU   A CD2 
1397 C  CD2 B LEU   A 53  ? 0.1347 0.1509 0.1173 -0.0095 -0.0131 0.0124  53  LEU   A CD2 
1420 N  N   A ASN   A 54  ? 0.1329 0.1512 0.1345 -0.0104 -0.0111 0.0088  54  ASN   A N   
1421 N  N   B ASN   A 54  ? 0.1356 0.1482 0.1166 0.0099  0.0018  -0.0052 54  ASN   A N   
1422 C  CA  A ASN   A 54  ? 0.1249 0.1403 0.1583 -0.0089 -0.0028 0.0071  54  ASN   A CA  
1423 C  CA  B ASN   A 54  ? 0.1307 0.1446 0.1314 0.0087  0.0032  -0.0107 54  ASN   A CA  
1424 C  C   A ASN   A 54  ? 0.1371 0.1417 0.1560 -0.0139 -0.0005 0.0061  54  ASN   A C   
1425 C  C   B ASN   A 54  ? 0.1391 0.1455 0.1350 -0.0051 0.0013  -0.0061 54  ASN   A C   
1426 O  O   A ASN   A 54  ? 0.1416 0.1515 0.1692 -0.0093 -0.0074 -0.0003 54  ASN   A O   
1427 O  O   B ASN   A 54  ? 0.1426 0.1498 0.1352 -0.0072 -0.0013 -0.0114 54  ASN   A O   
1428 C  CB  A ASN   A 54  ? 0.1240 0.1396 0.1666 -0.0106 -0.0134 0.0133  54  ASN   A CB  
1429 C  CB  B ASN   A 54  ? 0.1314 0.1473 0.1261 0.0166  -0.0009 -0.0125 54  ASN   A CB  
1430 C  CG  A ASN   A 54  ? 0.1242 0.1426 0.1851 -0.0101 -0.0049 0.0195  54  ASN   A CG  
1431 C  CG  B ASN   A 54  ? 0.1290 0.1489 0.1177 0.0146  0.0024  -0.0182 54  ASN   A CG  
1432 O  OD1 A ASN   A 54  ? 0.1268 0.1384 0.2086 -0.0130 -0.0114 0.0281  54  ASN   A OD1 
1433 O  OD1 B ASN   A 54  ? 0.1269 0.1428 0.1098 0.0112  -0.0053 -0.0329 54  ASN   A OD1 
1434 N  ND2 A ASN   A 54  ? 0.1302 0.1467 0.1975 -0.0129 -0.0133 0.0288  54  ASN   A ND2 
1435 N  ND2 B ASN   A 54  ? 0.1358 0.1523 0.1273 0.0070  -0.0012 -0.0035 54  ASN   A ND2 
1448 N  N   . LYS   A 55  ? 0.1370 0.1437 0.1495 -0.0040 -0.0016 -0.0043 55  LYS   A N   
1449 C  CA  . LYS   A 55  ? 0.1469 0.1563 0.1697 0.0027  -0.0046 -0.0110 55  LYS   A CA  
1450 C  C   . LYS   A 55  ? 0.1395 0.1589 0.1646 0.0015  -0.0030 -0.0184 55  LYS   A C   
1451 O  O   . LYS   A 55  ? 0.1518 0.1740 0.1651 0.0059  -0.0102 -0.0216 55  LYS   A O   
1452 C  CB  . LYS   A 55  ? 0.1515 0.1626 0.1749 0.0136  0.0001  -0.0129 55  LYS   A CB  
1453 C  CG  . LYS   A 55  ? 0.1699 0.1970 0.1874 0.0283  -0.0151 -0.0199 55  LYS   A CG  
1454 C  CD  . LYS   A 55  ? 0.1931 0.2347 0.2273 0.0492  -0.0096 -0.0198 55  LYS   A CD  
1455 C  CE  . LYS   A 55  ? 0.2137 0.2788 0.2564 0.0644  -0.0179 -0.0252 55  LYS   A CE  
1456 N  NZ  . LYS   A 55  ? 0.2252 0.3062 0.2632 0.0714  -0.0280 -0.0178 55  LYS   A NZ  
1471 N  N   . ALA   A 56  ? 0.1469 0.1675 0.1572 -0.0072 -0.0045 -0.0119 56  ALA   A N   
1472 C  CA  . ALA   A 56  ? 0.1599 0.1791 0.1536 -0.0087 0.0132  -0.0074 56  ALA   A CA  
1473 C  C   . ALA   A 56  ? 0.1631 0.1920 0.1290 -0.0092 0.0082  -0.0149 56  ALA   A C   
1474 O  O   . ALA   A 56  ? 0.1664 0.2240 0.1445 0.0052  0.0158  -0.0137 56  ALA   A O   
1475 C  CB  . ALA   A 56  ? 0.1648 0.1947 0.1862 -0.0146 0.0060  0.0009  56  ALA   A CB  
1481 N  N   . THR   A 57  ? 0.1488 0.1823 0.1333 -0.0102 0.0116  -0.0078 57  THR   A N   
1482 C  CA  . THR   A 57  ? 0.1522 0.1761 0.1357 -0.0117 0.0049  -0.0026 57  THR   A CA  
1483 C  C   . THR   A 57  ? 0.1565 0.1785 0.1457 -0.0065 -0.0013 -0.0088 57  THR   A C   
1484 O  O   . THR   A 57  ? 0.1541 0.1806 0.1721 -0.0128 -0.0085 -0.0260 57  THR   A O   
1485 C  CB  . THR   A 57  ? 0.1474 0.1712 0.1392 -0.0082 0.0020  -0.0062 57  THR   A CB  
1486 O  OG1 . THR   A 57  ? 0.1378 0.1693 0.1408 -0.0056 0.0039  -0.0089 57  THR   A OG1 
1487 C  CG2 . THR   A 57  ? 0.1503 0.1754 0.1379 -0.0064 0.0025  0.0040  57  THR   A CG2 
1495 N  N   . ASN   A 58  ? 0.1564 0.1734 0.1724 -0.0063 0.0025  -0.0199 58  ASN   A N   
1496 C  CA  . ASN   A 58  ? 0.1718 0.1667 0.1861 -0.0125 0.0139  -0.0334 58  ASN   A CA  
1497 C  C   . ASN   A 58  ? 0.1531 0.1577 0.1776 0.0003  -0.0001 -0.0195 58  ASN   A C   
1498 O  O   . ASN   A 58  ? 0.1598 0.1660 0.1905 -0.0120 0.0007  -0.0251 58  ASN   A O   
1499 C  CB  . ASN   A 58  ? 0.2162 0.1842 0.2177 -0.0168 0.0325  -0.0451 58  ASN   A CB  
1500 C  CG  . ASN   A 58  ? 0.2517 0.2079 0.2790 -0.0123 0.0271  -0.0266 58  ASN   A CG  
1501 O  OD1 . ASN   A 58  ? 0.2708 0.2085 0.3176 0.0234  0.0538  -0.0156 58  ASN   A OD1 
1502 N  ND2 . ASN   A 58  ? 0.2608 0.2138 0.2988 -0.0126 0.0111  -0.0294 58  ASN   A ND2 
1509 N  N   . ASN   A 59  ? 0.1420 0.1457 0.1680 -0.0031 -0.0056 -0.0137 59  ASN   A N   
1510 C  CA  . ASN   A 59  ? 0.1445 0.1365 0.1631 -0.0012 -0.0071 -0.0143 59  ASN   A CA  
1511 C  C   . ASN   A 59  ? 0.1430 0.1409 0.1436 -0.0080 -0.0095 -0.0041 59  ASN   A C   
1512 O  O   . ASN   A 59  ? 0.1445 0.1447 0.1638 -0.0057 -0.0031 0.0058  59  ASN   A O   
1513 C  CB  . ASN   A 59  ? 0.1545 0.1369 0.1627 0.0062  -0.0135 -0.0094 59  ASN   A CB  
1514 C  CG  . ASN   A 59  ? 0.1552 0.1427 0.1649 0.0007  -0.0233 0.0036  59  ASN   A CG  
1515 O  OD1 . ASN   A 59  ? 0.1650 0.1475 0.1570 -0.0111 -0.0227 -0.0012 59  ASN   A OD1 
1516 N  ND2 . ASN   A 59  ? 0.1642 0.1540 0.1751 -0.0160 -0.0153 0.0076  59  ASN   A ND2 
1523 N  N   . ALA   A 60  ? 0.1332 0.1473 0.1539 -0.0048 -0.0006 0.0042  60  ALA   A N   
1524 C  CA  . ALA   A 60  ? 0.1415 0.1470 0.1624 -0.0026 -0.0128 0.0043  60  ALA   A CA  
1525 C  C   . ALA   A 60  ? 0.1391 0.1489 0.1588 -0.0012 -0.0082 0.0024  60  ALA   A C   
1526 O  O   . ALA   A 60  ? 0.1316 0.1445 0.1847 -0.0041 -0.0068 -0.0019 60  ALA   A O   
1527 C  CB  . ALA   A 60  ? 0.1462 0.1518 0.1724 0.0000  -0.0137 -0.0159 60  ALA   A CB  
1533 N  N   . MET   A 61  ? 0.1327 0.1392 0.1434 -0.0052 0.0053  -0.0044 61  MET   A N   
1534 C  CA  . MET   A 61  ? 0.1337 0.1383 0.1514 -0.0053 -0.0009 0.0062  61  MET   A CA  
1535 C  C   . MET   A 61  ? 0.1298 0.1379 0.1526 -0.0043 0.0006  -0.0082 61  MET   A C   
1536 O  O   . MET   A 61  ? 0.1363 0.1348 0.1654 -0.0027 0.0039  0.0017  61  MET   A O   
1537 C  CB  . MET   A 61  ? 0.1423 0.1383 0.1401 -0.0087 0.0106  -0.0030 61  MET   A CB  
1538 C  CG  . MET   A 61  ? 0.1426 0.1429 0.1638 -0.0060 -0.0069 0.0031  61  MET   A CG  
1539 S  SD  . MET   A 61  ? 0.1482 0.1507 0.1938 -0.0108 -0.0005 -0.0138 61  MET   A SD  
1540 C  CE  . MET   A 61  ? 0.1624 0.1623 0.2296 -0.0153 0.0141  -0.0068 61  MET   A CE  
1550 N  N   . GLN   A 62  ? 0.1323 0.1365 0.1555 -0.0067 -0.0021 -0.0003 62  GLN   A N   
1551 C  CA  . GLN   A 62  ? 0.1368 0.1313 0.1623 -0.0034 -0.0023 0.0070  62  GLN   A CA  
1552 C  C   . GLN   A 62  ? 0.1387 0.1209 0.1672 -0.0002 0.0085  0.0051  62  GLN   A C   
1553 O  O   . GLN   A 62  ? 0.1424 0.1362 0.1621 -0.0034 0.0079  0.0007  62  GLN   A O   
1554 C  CB  . GLN   A 62  ? 0.1380 0.1256 0.1674 -0.0032 0.0009  0.0017  62  GLN   A CB  
1555 C  CG  . GLN   A 62  ? 0.1388 0.1294 0.1715 -0.0027 0.0017  0.0125  62  GLN   A CG  
1556 C  CD  . GLN   A 62  ? 0.1454 0.1363 0.1625 -0.0001 0.0077  0.0118  62  GLN   A CD  
1557 O  OE1 . GLN   A 62  ? 0.1473 0.1497 0.1754 -0.0015 -0.0056 0.0029  62  GLN   A OE1 
1558 N  NE2 . GLN   A 62  ? 0.1565 0.1358 0.1728 0.0042  0.0082  -0.0056 62  GLN   A NE2 
1567 N  N   . VAL   A 63  ? 0.1343 0.1314 0.1843 -0.0038 0.0014  -0.0169 63  VAL   A N   
1568 C  CA  . VAL   A 63  ? 0.1378 0.1432 0.2037 -0.0091 -0.0014 -0.0061 63  VAL   A CA  
1569 C  C   . VAL   A 63  ? 0.1280 0.1440 0.1841 -0.0121 -0.0088 -0.0106 63  VAL   A C   
1570 O  O   . VAL   A 63  ? 0.1283 0.1436 0.2033 -0.0158 -0.0031 -0.0040 63  VAL   A O   
1571 C  CB  . VAL   A 63  ? 0.1548 0.1571 0.2420 -0.0113 -0.0096 -0.0356 63  VAL   A CB  
1572 C  CG1 . VAL   A 63  ? 0.1694 0.1794 0.2899 -0.0113 -0.0183 -0.0633 63  VAL   A CG1 
1573 C  CG2 . VAL   A 63  ? 0.1584 0.1559 0.2434 -0.0069 0.0020  -0.0284 63  VAL   A CG2 
1583 N  N   . GLU   A 64  ? 0.1294 0.1459 0.1711 -0.0057 -0.0071 -0.0077 64  GLU   A N   
1584 C  CA  . GLU   A 64  ? 0.1327 0.1477 0.1744 -0.0086 -0.0092 0.0076  64  GLU   A CA  
1585 C  C   . GLU   A 64  ? 0.1234 0.1460 0.1704 -0.0077 0.0028  0.0100  64  GLU   A C   
1586 O  O   . GLU   A 64  ? 0.1364 0.1459 0.1809 -0.0017 0.0044  0.0035  64  GLU   A O   
1587 C  CB  . GLU   A 64  ? 0.1385 0.1604 0.1848 -0.0057 -0.0003 0.0018  64  GLU   A CB  
1588 C  CG  . GLU   A 64  ? 0.1472 0.1608 0.2033 -0.0058 -0.0099 0.0042  64  GLU   A CG  
1589 C  CD  . GLU   A 64  ? 0.1616 0.1695 0.1991 -0.0127 -0.0052 0.0066  64  GLU   A CD  
1590 O  OE1 . GLU   A 64  ? 0.1646 0.1852 0.2157 -0.0200 0.0050  0.0091  64  GLU   A OE1 
1591 O  OE2 . GLU   A 64  ? 0.1854 0.1701 0.1881 -0.0195 -0.0061 0.0140  64  GLU   A OE2 
1598 N  N   . SER   A 65  ? 0.1233 0.1415 0.1648 0.0006  -0.0038 0.0072  65  SER   A N   
1599 C  CA  . SER   A 65  ? 0.1333 0.1392 0.1608 -0.0015 -0.0038 0.0031  65  SER   A CA  
1600 C  C   . SER   A 65  ? 0.1325 0.1435 0.1624 -0.0050 -0.0045 0.0048  65  SER   A C   
1601 O  O   . SER   A 65  ? 0.1427 0.1484 0.1846 0.0011  0.0148  0.0005  65  SER   A O   
1602 C  CB  . SER   A 65  ? 0.1389 0.1348 0.1681 -0.0037 0.0030  0.0075  65  SER   A CB  
1603 O  OG  . SER   A 65  ? 0.1326 0.1449 0.1729 -0.0074 0.0010  0.0164  65  SER   A OG  
1609 N  N   . ASP   A 66  ? 0.1323 0.1433 0.1759 -0.0024 0.0130  0.0072  66  ASP   A N   
1610 C  CA  . ASP   A 66  ? 0.1441 0.1539 0.1818 -0.0047 0.0119  0.0153  66  ASP   A CA  
1611 C  C   . ASP   A 66  ? 0.1434 0.1475 0.1846 -0.0068 0.0116  0.0161  66  ASP   A C   
1612 O  O   . ASP   A 66  ? 0.1477 0.1574 0.1979 -0.0047 0.0266  0.0210  66  ASP   A O   
1613 C  CB  . ASP   A 66  ? 0.1558 0.1584 0.2190 0.0104  0.0146  0.0324  66  ASP   A CB  
1614 C  CG  . ASP   A 66  ? 0.1829 0.1777 0.2475 0.0026  0.0056  0.0526  66  ASP   A CG  
1615 O  OD1 . ASP   A 66  ? 0.1776 0.2076 0.2350 -0.0071 -0.0040 0.0467  66  ASP   A OD1 
1616 O  OD2 . ASP   A 66  ? 0.2000 0.2033 0.3241 0.0216  -0.0111 0.0308  66  ASP   A OD2 
1621 N  N   . ASP   A 67  ? 0.1375 0.1478 0.1902 -0.0059 0.0088  0.0146  67  ASP   A N   
1622 C  CA  . ASP   A 67  ? 0.1359 0.1661 0.2037 -0.0038 0.0065  0.0254  67  ASP   A CA  
1623 C  C   . ASP   A 67  ? 0.1366 0.1683 0.2061 0.0057  0.0151  0.0278  67  ASP   A C   
1624 O  O   . ASP   A 67  ? 0.1324 0.1763 0.2281 0.0018  0.0221  0.0337  67  ASP   A O   
1625 C  CB  . ASP   A 67  ? 0.1470 0.1715 0.2288 -0.0037 -0.0058 0.0284  67  ASP   A CB  
1626 C  CG  . ASP   A 67  ? 0.1446 0.1879 0.2764 -0.0056 -0.0213 0.0469  67  ASP   A CG  
1627 O  OD1 . ASP   A 67  ? 0.1506 0.2125 0.3600 -0.0130 -0.0286 0.0569  67  ASP   A OD1 
1628 O  OD2 . ASP   A 67  ? 0.1472 0.1976 0.2630 0.0020  -0.0195 0.0389  67  ASP   A OD2 
1633 N  N   . TYR   A 68  ? 0.1402 0.1528 0.2031 0.0062  0.0185  0.0298  68  TYR   A N   
1634 C  CA  . TYR   A 68  ? 0.1524 0.1508 0.1929 0.0034  0.0186  0.0263  68  TYR   A CA  
1635 C  C   . TYR   A 68  ? 0.1411 0.1559 0.1886 -0.0006 0.0265  0.0230  68  TYR   A C   
1636 O  O   . TYR   A 68  ? 0.1484 0.1596 0.2102 0.0127  0.0302  0.0219  68  TYR   A O   
1637 C  CB  . TYR   A 68  ? 0.1576 0.1466 0.2069 0.0095  0.0407  0.0265  68  TYR   A CB  
1638 C  CG  . TYR   A 68  ? 0.1620 0.1620 0.2473 0.0091  0.0475  0.0319  68  TYR   A CG  
1639 C  CD1 . TYR   A 68  ? 0.1716 0.1743 0.2919 -0.0200 0.0465  -0.0089 68  TYR   A CD1 
1640 C  CD2 . TYR   A 68  ? 0.1826 0.1711 0.3107 0.0153  0.0605  0.0364  68  TYR   A CD2 
1641 C  CE1 . TYR   A 68  ? 0.1782 0.1878 0.3272 -0.0180 0.0627  -0.0177 68  TYR   A CE1 
1642 C  CE2 . TYR   A 68  ? 0.1851 0.1808 0.3425 0.0054  0.0726  0.0086  68  TYR   A CE2 
1643 C  CZ  . TYR   A 68  ? 0.1797 0.1789 0.3557 -0.0172 0.0603  -0.0230 68  TYR   A CZ  
1644 O  OH  . TYR   A 68  ? 0.2099 0.1858 0.3942 -0.0152 0.0425  -0.0532 68  TYR   A OH  
1654 N  N   . ILE   A 69  ? 0.1381 0.1435 0.1926 0.0010  0.0157  0.0202  69  ILE   A N   
1655 C  CA  . ILE   A 69  ? 0.1423 0.1493 0.1813 0.0078  0.0104  0.0069  69  ILE   A CA  
1656 C  C   . ILE   A 69  ? 0.1506 0.1496 0.1783 0.0103  0.0232  0.0136  69  ILE   A C   
1657 O  O   . ILE   A 69  ? 0.1532 0.1571 0.1823 0.0030  0.0251  0.0154  69  ILE   A O   
1658 C  CB  . ILE   A 69  ? 0.1502 0.1718 0.1860 0.0092  0.0110  -0.0031 69  ILE   A CB  
1659 C  CG1 . ILE   A 69  ? 0.1538 0.1802 0.2008 0.0085  0.0197  -0.0272 69  ILE   A CG1 
1660 C  CG2 . ILE   A 69  ? 0.1710 0.1935 0.2083 0.0221  0.0066  -0.0163 69  ILE   A CG2 
1661 C  CD1 . ILE   A 69  ? 0.1565 0.1895 0.2224 -0.0061 0.0196  -0.0240 69  ILE   A CD1 
1673 N  N   . ALA   A 70  ? 0.1527 0.1500 0.1969 -0.0029 0.0229  0.0145  70  ALA   A N   
1674 C  CA  . ALA   A 70  ? 0.1569 0.1667 0.2157 -0.0141 0.0311  0.0229  70  ALA   A CA  
1675 C  C   . ALA   A 70  ? 0.1518 0.1784 0.2256 -0.0136 0.0279  0.0228  70  ALA   A C   
1676 O  O   . ALA   A 70  ? 0.1671 0.2140 0.2449 0.0132  0.0418  0.0431  70  ALA   A O   
1677 C  CB  . ALA   A 70  ? 0.1550 0.1669 0.2228 -0.0139 0.0243  0.0192  70  ALA   A CB  
1683 N  N   . THR   A 71  ? 0.1437 0.1791 0.2198 -0.0022 0.0208  0.0296  71  THR   A N   
1684 C  CA  . THR   A 71  ? 0.1566 0.1995 0.2480 0.0149  0.0210  0.0375  71  THR   A CA  
1685 C  C   . THR   A 71  ? 0.1457 0.1908 0.2808 0.0232  0.0394  0.0298  71  THR   A C   
1686 O  O   . THR   A 71  ? 0.1530 0.2099 0.3305 0.0167  0.0515  0.0046  71  THR   A O   
1687 C  CB  . THR   A 71  ? 0.1977 0.2314 0.2765 0.0211  -0.0244 0.0494  71  THR   A CB  
1688 O  OG1 . THR   A 71  ? 0.2332 0.2498 0.2918 0.0045  -0.0425 0.0402  71  THR   A OG1 
1689 C  CG2 . THR   A 71  ? 0.2094 0.2533 0.2967 0.0317  -0.0278 0.0667  71  THR   A CG2 
1697 N  N   . ASN   A 72  ? 0.1540 0.1716 0.2461 0.0183  0.0357  0.0348  72  ASN   A N   
1698 C  CA  . ASN   A 72  ? 0.1660 0.1724 0.2486 0.0215  0.0407  0.0333  72  ASN   A CA  
1699 C  C   . ASN   A 72  ? 0.1748 0.1674 0.2417 0.0137  0.0548  0.0217  72  ASN   A C   
1700 O  O   . ASN   A 72  ? 0.1925 0.1629 0.2795 0.0164  0.0429  0.0107  72  ASN   A O   
1701 C  CB  . ASN   A 72  ? 0.1874 0.1829 0.2441 0.0225  0.0558  0.0406  72  ASN   A CB  
1702 C  CG  . ASN   A 72  ? 0.2103 0.1957 0.2587 0.0296  0.0458  0.0441  72  ASN   A CG  
1703 O  OD1 . ASN   A 72  ? 0.2259 0.2256 0.2735 0.0308  0.0491  0.0405  72  ASN   A OD1 
1704 N  ND2 . ASN   A 72  ? 0.2294 0.1948 0.2745 0.0568  0.0323  0.0392  72  ASN   A ND2 
1711 N  N   . GLY   A 73  ? 0.1769 0.1586 0.2177 0.0067  0.0502  0.0198  73  GLY   A N   
1712 C  CA  . GLY   A 73  ? 0.1806 0.1598 0.2094 -0.0009 0.0524  0.0139  73  GLY   A CA  
1713 C  C   . GLY   A 73  ? 0.1799 0.1529 0.1969 0.0063  0.0503  0.0286  73  GLY   A C   
1714 O  O   . GLY   A 73  ? 0.1786 0.1574 0.2032 0.0152  0.0406  0.0255  73  GLY   A O   
1718 N  N   . PRO   A 74  ? 0.1915 0.1556 0.1880 -0.0095 0.0537  0.0149  74  PRO   A N   
1719 C  CA  . PRO   A 74  ? 0.1884 0.1508 0.2054 0.0016  0.0481  0.0204  74  PRO   A CA  
1720 C  C   . PRO   A 74  ? 0.1831 0.1353 0.2049 -0.0023 0.0336  0.0109  74  PRO   A C   
1721 O  O   . PRO   A 74  ? 0.1844 0.1410 0.2366 0.0047  0.0364  0.0008  74  PRO   A O   
1722 C  CB  . PRO   A 74  ? 0.2039 0.1794 0.2222 0.0069  0.0594  0.0406  74  PRO   A CB  
1723 C  CG  . PRO   A 74  ? 0.2320 0.2203 0.2661 -0.0149 0.0413  0.0321  74  PRO   A CG  
1724 C  CD  . PRO   A 74  ? 0.2091 0.1930 0.2165 -0.0212 0.0426  0.0096  74  PRO   A CD  
1732 N  N   . LEU   A 75  ? 0.1755 0.1315 0.1814 -0.0018 0.0241  0.0074  75  LEU   A N   
1733 C  CA  . LEU   A 75  ? 0.1701 0.1325 0.1599 0.0002  0.0148  0.0134  75  LEU   A CA  
1734 C  C   . LEU   A 75  ? 0.1808 0.1429 0.1501 0.0067  0.0180  0.0151  75  LEU   A C   
1735 O  O   . LEU   A 75  ? 0.2240 0.1566 0.1562 0.0124  0.0113  0.0155  75  LEU   A O   
1736 C  CB  . LEU   A 75  ? 0.1748 0.1370 0.1664 0.0002  0.0156  0.0178  75  LEU   A CB  
1737 C  CG  . LEU   A 75  ? 0.1943 0.1777 0.1696 -0.0346 0.0133  0.0140  75  LEU   A CG  
1738 C  CD1 . LEU   A 75  ? 0.2058 0.2302 0.1866 -0.0393 0.0099  -0.0009 75  LEU   A CD1 
1739 C  CD2 . LEU   A 75  ? 0.2233 0.2210 0.2336 -0.0174 0.0116  0.0169  75  LEU   A CD2 
1751 N  N   . LYS   A 76  ? 0.1726 0.1428 0.1789 -0.0004 0.0109  0.0046  76  LYS   A N   
1752 C  CA  . LYS   A 76  ? 0.1697 0.1621 0.1842 -0.0034 0.0065  -0.0104 76  LYS   A CA  
1753 C  C   . LYS   A 76  ? 0.1708 0.1484 0.1409 0.0020  0.0034  0.0084  76  LYS   A C   
1754 O  O   . LYS   A 76  ? 0.1801 0.1403 0.1516 0.0023  0.0128  0.0199  76  LYS   A O   
1755 C  CB  . LYS   A 76  ? 0.1678 0.1830 0.2143 0.0088  0.0098  -0.0227 76  LYS   A CB  
1756 C  CG  . LYS   A 76  ? 0.1811 0.1794 0.2590 0.0128  -0.0050 -0.0165 76  LYS   A CG  
1757 C  CD  . LYS   A 76  ? 0.1902 0.1776 0.3062 0.0140  -0.0170 -0.0169 76  LYS   A CD  
1758 C  CE  . LYS   A 76  ? 0.2003 0.1911 0.3686 0.0002  -0.0064 -0.0227 76  LYS   A CE  
1759 N  NZ  . LYS   A 76  ? 0.2013 0.1801 0.4263 -0.0070 -0.0043 -0.0307 76  LYS   A NZ  
1773 N  N   . VAL   A 77  ? 0.1762 0.1515 0.1557 -0.0010 0.0120  0.0145  77  VAL   A N   
1774 C  CA  . VAL   A 77  ? 0.1720 0.1499 0.1545 0.0075  0.0016  0.0102  77  VAL   A CA  
1775 C  C   . VAL   A 77  ? 0.1710 0.1440 0.1509 0.0103  0.0131  0.0102  77  VAL   A C   
1776 O  O   . VAL   A 77  ? 0.1797 0.1513 0.1629 0.0119  0.0283  0.0016  77  VAL   A O   
1777 C  CB  . VAL   A 77  ? 0.1868 0.1673 0.1645 0.0024  0.0067  0.0179  77  VAL   A CB  
1778 C  CG1 . VAL   A 77  ? 0.1796 0.1804 0.1950 0.0084  -0.0006 0.0103  77  VAL   A CG1 
1779 C  CG2 . VAL   A 77  ? 0.2083 0.1813 0.1746 0.0066  -0.0045 0.0200  77  VAL   A CG2 
1789 N  N   . GLY   A 78  ? 0.1648 0.1429 0.1436 0.0067  0.0163  0.0074  78  GLY   A N   
1790 C  CA  . GLY   A 78  ? 0.1671 0.1453 0.1670 0.0068  0.0173  0.0068  78  GLY   A CA  
1791 C  C   . GLY   A 78  ? 0.1527 0.1385 0.1681 0.0087  0.0190  0.0187  78  GLY   A C   
1792 O  O   . GLY   A 78  ? 0.1522 0.1467 0.1835 0.0034  0.0175  0.0321  78  GLY   A O   
1796 N  N   . GLY   A 79  ? 0.1589 0.1334 0.1599 -0.0000 0.0090  0.0213  79  GLY   A N   
1797 C  CA  . GLY   A 79  ? 0.1569 0.1355 0.1701 0.0031  0.0126  0.0244  79  GLY   A CA  
1798 C  C   . GLY   A 79  ? 0.1431 0.1311 0.1657 -0.0024 0.0126  0.0094  79  GLY   A C   
1799 O  O   . GLY   A 79  ? 0.1473 0.1432 0.1745 0.0157  0.0112  0.0114  79  GLY   A O   
1803 N  N   . SER   A 80  ? 0.1423 0.1501 0.1840 -0.0021 0.0121  0.0047  80  SER   A N   
1804 C  CA  . SER   A 80  ? 0.1423 0.1414 0.1713 0.0039  0.0060  0.0066  80  SER   A CA  
1805 C  C   . SER   A 80  ? 0.1354 0.1449 0.1720 -0.0016 0.0055  0.0179  80  SER   A C   
1806 O  O   . SER   A 80  ? 0.1358 0.1692 0.2096 0.0069  0.0135  0.0003  80  SER   A O   
1807 C  CB  . SER   A 80  ? 0.1571 0.1418 0.1928 -0.0042 0.0137  0.0054  80  SER   A CB  
1808 O  OG  . SER   A 80  ? 0.1796 0.1422 0.2349 0.0028  0.0002  0.0212  80  SER   A OG  
1814 N  N   . CYS   A 81  ? 0.1374 0.1340 0.1710 0.0041  -0.0049 0.0161  81  CYS   A N   
1815 C  CA  . CYS   A 81  ? 0.1336 0.1484 0.1681 -0.0042 -0.0098 0.0199  81  CYS   A CA  
1816 C  C   . CYS   A 81  ? 0.1342 0.1476 0.1534 -0.0066 -0.0004 0.0323  81  CYS   A C   
1817 O  O   . CYS   A 81  ? 0.1313 0.1728 0.1797 0.0002  -0.0023 0.0332  81  CYS   A O   
1818 C  CB  . CYS   A 81  ? 0.1430 0.1548 0.1774 -0.0120 -0.0034 0.0282  81  CYS   A CB  
1819 S  SG  . CYS   A 81  ? 0.1564 0.1466 0.1740 -0.0133 0.0003  0.0159  81  CYS   A SG  
1825 N  N   . VAL   A 82  ? 0.1399 0.1528 0.1656 0.0002  -0.0129 0.0255  82  VAL   A N   
1826 C  CA  . VAL   A 82  ? 0.1551 0.1537 0.1565 0.0015  -0.0125 0.0265  82  VAL   A CA  
1827 C  C   . VAL   A 82  ? 0.1441 0.1627 0.1696 -0.0051 -0.0095 0.0250  82  VAL   A C   
1828 O  O   . VAL   A 82  ? 0.1390 0.1675 0.1990 -0.0047 -0.0055 0.0002  82  VAL   A O   
1829 C  CB  . VAL   A 82  ? 0.1835 0.1656 0.1776 -0.0020 -0.0128 0.0304  82  VAL   A CB  
1830 C  CG1 . VAL   A 82  ? 0.2087 0.1779 0.1978 0.0043  -0.0073 0.0299  82  VAL   A CG1 
1831 C  CG2 . VAL   A 82  ? 0.1937 0.1644 0.2115 -0.0068 -0.0115 0.0280  82  VAL   A CG2 
1841 N  N   . LEU   A 83  ? 0.1437 0.1556 0.1698 -0.0088 -0.0086 0.0088  83  LEU   A N   
1842 C  CA  . LEU   A 83  ? 0.1414 0.1584 0.1607 -0.0066 -0.0095 0.0148  83  LEU   A CA  
1843 C  C   . LEU   A 83  ? 0.1456 0.1636 0.1565 -0.0119 -0.0147 0.0107  83  LEU   A C   
1844 O  O   . LEU   A 83  ? 0.1549 0.1620 0.1761 -0.0208 -0.0086 0.0201  83  LEU   A O   
1845 C  CB  . LEU   A 83  ? 0.1472 0.1646 0.1714 -0.0105 -0.0124 0.0170  83  LEU   A CB  
1846 C  CG  . LEU   A 83  ? 0.1620 0.1754 0.1769 -0.0125 0.0039  0.0094  83  LEU   A CG  
1847 C  CD1 . LEU   A 83  ? 0.1754 0.1768 0.1889 -0.0215 0.0022  0.0209  83  LEU   A CD1 
1848 C  CD2 . LEU   A 83  ? 0.1585 0.1882 0.1969 -0.0093 0.0060  0.0201  83  LEU   A CD2 
1860 N  N   . SER   A 84  ? 0.1655 0.1659 0.1691 -0.0163 -0.0175 0.0220  84  SER   A N   
1861 C  CA  . SER   A 84  ? 0.1810 0.1704 0.1508 -0.0141 -0.0155 0.0245  84  SER   A CA  
1862 C  C   . SER   A 84  ? 0.1756 0.1681 0.1520 -0.0208 -0.0047 0.0147  84  SER   A C   
1863 O  O   . SER   A 84  ? 0.1687 0.1858 0.1539 -0.0092 -0.0126 0.0205  84  SER   A O   
1864 C  CB  . SER   A 84  ? 0.1924 0.1923 0.1684 -0.0096 -0.0145 0.0093  84  SER   A CB  
1865 O  OG  . SER   A 84  ? 0.1978 0.2205 0.1676 -0.0156 -0.0191 -0.0048 84  SER   A OG  
1871 N  N   . GLY   A 85  ? 0.1881 0.1865 0.1598 -0.0204 0.0101  0.0119  85  GLY   A N   
1872 C  CA  . GLY   A 85  ? 0.1904 0.1944 0.1715 -0.0253 0.0090  -0.0052 85  GLY   A CA  
1873 C  C   . GLY   A 85  ? 0.1835 0.2043 0.1606 -0.0229 -0.0090 0.0073  85  GLY   A C   
1874 O  O   . GLY   A 85  ? 0.1829 0.2248 0.1682 -0.0336 0.0056  -0.0080 85  GLY   A O   
1878 N  N   . HIS   A 86  ? 0.1847 0.1939 0.1497 -0.0127 -0.0134 0.0042  86  HIS   A N   
1879 C  CA  . HIS   A 86  ? 0.2031 0.1987 0.1479 -0.0137 -0.0085 0.0095  86  HIS   A CA  
1880 C  C   . HIS   A 86  ? 0.2243 0.2166 0.1227 -0.0146 -0.0185 0.0050  86  HIS   A C   
1881 O  O   . HIS   A 86  ? 0.2399 0.2469 0.1389 -0.0133 -0.0009 0.0085  86  HIS   A O   
1882 C  CB  . HIS   A 86  ? 0.2080 0.1948 0.1586 -0.0093 -0.0027 0.0151  86  HIS   A CB  
1883 C  CG  . HIS   A 86  ? 0.2013 0.1940 0.1541 0.0004  0.0027  0.0262  86  HIS   A CG  
1884 N  ND1 . HIS   A 86  ? 0.2109 0.1980 0.2064 -0.0095 -0.0024 0.0236  86  HIS   A ND1 
1885 C  CD2 . HIS   A 86  ? 0.2025 0.1941 0.1418 0.0194  0.0144  0.0206  86  HIS   A CD2 
1886 C  CE1 . HIS   A 86  ? 0.2102 0.1985 0.2006 -0.0021 0.0147  0.0249  86  HIS   A CE1 
1887 N  NE2 . HIS   A 86  ? 0.2075 0.1975 0.1682 0.0160  0.0196  0.0325  86  HIS   A NE2 
1895 N  N   . ASN   A 87  ? 0.2344 0.2251 0.1493 -0.0047 0.0054  -0.0087 87  ASN   A N   
1896 C  CA  . ASN   A 87  ? 0.2535 0.2394 0.1504 -0.0034 0.0241  -0.0041 87  ASN   A CA  
1897 C  C   . ASN   A 87  ? 0.2491 0.2504 0.1829 -0.0122 0.0460  0.0098  87  ASN   A C   
1898 O  O   . ASN   A 87  ? 0.2830 0.2799 0.2176 -0.0307 0.0860  -0.0063 87  ASN   A O   
1899 C  CB  . ASN   A 87  ? 0.2700 0.2419 0.1669 0.0041  0.0235  -0.0012 87  ASN   A CB  
1900 C  CG  . ASN   A 87  ? 0.2798 0.2502 0.1686 0.0096  0.0363  0.0101  87  ASN   A CG  
1901 O  OD1 . ASN   A 87  ? 0.2975 0.2475 0.1747 0.0282  0.0347  0.0179  87  ASN   A OD1 
1902 N  ND2 . ASN   A 87  ? 0.2817 0.2750 0.1858 0.0078  0.0287  0.0109  87  ASN   A ND2 
1909 N  N   A LEU   A 88  ? 0.2212 0.2352 0.1748 -0.0101 0.0279  0.0165  88  LEU   A N   
1910 N  N   B LEU   A 88  ? 0.2302 0.2429 0.1823 -0.0119 0.0337  0.0096  88  LEU   A N   
1911 C  CA  A LEU   A 88  ? 0.2046 0.2336 0.1858 -0.0199 0.0294  0.0347  88  LEU   A CA  
1912 C  CA  B LEU   A 88  ? 0.2173 0.2427 0.1934 -0.0184 0.0322  0.0171  88  LEU   A CA  
1913 C  C   A LEU   A 88  ? 0.2035 0.2382 0.1760 -0.0251 0.0287  0.0390  88  LEU   A C   
1914 C  C   B LEU   A 88  ? 0.2105 0.2418 0.1817 -0.0222 0.0260  0.0293  88  LEU   A C   
1915 O  O   A LEU   A 88  ? 0.2029 0.2386 0.2141 -0.0209 0.0326  0.0515  88  LEU   A O   
1916 O  O   B LEU   A 88  ? 0.2094 0.2420 0.1943 -0.0185 0.0287  0.0446  88  LEU   A O   
1917 C  CB  A LEU   A 88  ? 0.2056 0.2400 0.1914 -0.0264 -0.0058 0.0434  88  LEU   A CB  
1918 C  CB  B LEU   A 88  ? 0.2199 0.2498 0.2072 -0.0232 0.0174  0.0101  88  LEU   A CB  
1919 C  CG  A LEU   A 88  ? 0.2216 0.2506 0.2120 -0.0268 -0.0232 0.0550  88  LEU   A CG  
1920 C  CG  B LEU   A 88  ? 0.2271 0.2574 0.2194 -0.0239 0.0102  0.0050  88  LEU   A CG  
1921 C  CD1 A LEU   A 88  ? 0.2302 0.2574 0.2056 -0.0264 -0.0336 0.0500  88  LEU   A CD1 
1922 C  CD1 B LEU   A 88  ? 0.2306 0.2626 0.2199 -0.0242 0.0049  -0.0028 88  LEU   A CD1 
1923 C  CD2 A LEU   A 88  ? 0.2334 0.2578 0.2463 -0.0200 -0.0171 0.0540  88  LEU   A CD2 
1924 C  CD2 B LEU   A 88  ? 0.2328 0.2610 0.2286 -0.0193 0.0140  0.0025  88  LEU   A CD2 
1947 N  N   . ALA   A 89  ? 0.2051 0.2361 0.1668 -0.0240 0.0115  0.0183  89  ALA   A N   
1948 C  CA  . ALA   A 89  ? 0.2039 0.2313 0.1527 -0.0172 -0.0011 0.0246  89  ALA   A CA  
1949 C  C   . ALA   A 89  ? 0.2114 0.2317 0.1565 -0.0106 -0.0063 0.0231  89  ALA   A C   
1950 O  O   . ALA   A 89  ? 0.1981 0.2264 0.2025 -0.0205 -0.0059 -0.0066 89  ALA   A O   
1951 C  CB  . ALA   A 89  ? 0.1981 0.2258 0.1396 -0.0167 0.0043  0.0168  89  ALA   A CB  
1958 N  N   . LYS   A 90  ? 0.2200 0.2421 0.1464 -0.0216 -0.0157 0.0265  90  LYS   A N   
1959 C  CA  . LYS   A 90  ? 0.2386 0.2620 0.1471 -0.0128 -0.0278 0.0208  90  LYS   A CA  
1960 C  C   . LYS   A 90  ? 0.2112 0.2410 0.1527 -0.0176 -0.0311 0.0145  90  LYS   A C   
1961 O  O   . LYS   A 90  ? 0.2119 0.2541 0.1822 -0.0190 -0.0346 0.0086  90  LYS   A O   
1962 C  CB  . LYS   A 90  ? 0.2762 0.3101 0.1784 -0.0207 -0.0385 0.0458  90  LYS   A CB  
1963 C  CG  . LYS   A 90  ? 0.3371 0.3635 0.2920 -0.0242 -0.0339 0.0623  90  LYS   A CG  
1964 C  CD  . LYS   A 90  ? 0.4069 0.4246 0.4205 -0.0317 -0.0140 0.0608  90  LYS   A CD  
1965 C  CE  . LYS   A 90  ? 0.4682 0.4798 0.5113 -0.0385 0.0023  0.0528  90  LYS   A CE  
1966 N  NZ  . LYS   A 90  ? 0.4977 0.5044 0.5723 -0.0437 0.0097  0.0548  90  LYS   A NZ  
1980 N  N   . HIS   A 91  ? 0.2007 0.2087 0.1241 -0.0184 -0.0334 0.0285  91  HIS   A N   
1981 C  CA  . HIS   A 91  ? 0.1862 0.1924 0.1385 -0.0102 -0.0235 0.0205  91  HIS   A CA  
1982 C  C   . HIS   A 91  ? 0.1642 0.1773 0.1183 -0.0073 -0.0163 0.0170  91  HIS   A C   
1983 O  O   . HIS   A 91  ? 0.1589 0.1951 0.1545 -0.0162 -0.0072 0.0269  91  HIS   A O   
1984 C  CB  . HIS   A 91  ? 0.2029 0.2214 0.1940 0.0095  -0.0429 0.0221  91  HIS   A CB  
1985 C  CG  . HIS   A 91  ? 0.2445 0.2750 0.2557 0.0197  -0.0698 0.0070  91  HIS   A CG  
1986 N  ND1 . HIS   A 91  ? 0.2531 0.3067 0.2963 0.0251  -0.0883 -0.0114 91  HIS   A ND1 
1987 C  CD2 . HIS   A 91  ? 0.2728 0.2993 0.2834 0.0239  -0.0882 0.0102  91  HIS   A CD2 
1988 C  CE1 . HIS   A 91  ? 0.2701 0.3175 0.3098 0.0286  -0.0903 -0.0001 91  HIS   A CE1 
1989 N  NE2 . HIS   A 91  ? 0.2833 0.3172 0.3079 0.0304  -0.0982 0.0026  91  HIS   A NE2 
1997 N  N   . CYS   A 92  ? 0.1594 0.1689 0.1252 -0.0140 -0.0145 0.0190  92  CYS   A N   
1998 C  CA  . CYS   A 92  ? 0.1502 0.1634 0.1517 -0.0107 0.0019  0.0199  92  CYS   A CA  
1999 C  C   . CYS   A 92  ? 0.1435 0.1550 0.1395 -0.0123 0.0024  0.0230  92  CYS   A C   
2000 O  O   . CYS   A 92  ? 0.1481 0.1618 0.1694 -0.0166 0.0014  0.0136  92  CYS   A O   
2001 C  CB  . CYS   A 92  ? 0.1537 0.1624 0.1623 -0.0098 -0.0078 0.0106  92  CYS   A CB  
2002 S  SG  . CYS   A 92  ? 0.1545 0.1533 0.1514 -0.0112 -0.0072 0.0152  92  CYS   A SG  
2008 N  N   . LEU   A 93  ? 0.1418 0.1407 0.1440 -0.0120 0.0099  0.0190  93  LEU   A N   
2009 C  CA  . LEU   A 93  ? 0.1304 0.1452 0.1525 -0.0085 0.0075  0.0169  93  LEU   A CA  
2010 C  C   . LEU   A 93  ? 0.1348 0.1353 0.1391 -0.0036 0.0005  0.0210  93  LEU   A C   
2011 O  O   . LEU   A 93  ? 0.1267 0.1388 0.1553 -0.0045 -0.0019 0.0189  93  LEU   A O   
2012 C  CB  . LEU   A 93  ? 0.1400 0.1385 0.1592 -0.0047 -0.0023 0.0258  93  LEU   A CB  
2013 C  CG  . LEU   A 93  ? 0.1489 0.1418 0.1588 -0.0036 0.0101  0.0237  93  LEU   A CG  
2014 C  CD1 . LEU   A 93  ? 0.1521 0.1426 0.1904 -0.0019 0.0097  0.0176  93  LEU   A CD1 
2015 C  CD2 . LEU   A 93  ? 0.1695 0.1418 0.1707 -0.0053 0.0036  0.0224  93  LEU   A CD2 
2027 N  N   . HIS   A 94  ? 0.1329 0.1269 0.1524 -0.0054 0.0019  0.0211  94  HIS   A N   
2028 C  CA  . HIS   A 94  ? 0.1276 0.1294 0.1563 -0.0034 0.0009  0.0180  94  HIS   A CA  
2029 C  C   . HIS   A 94  ? 0.1254 0.1299 0.1454 -0.0031 0.0026  0.0185  94  HIS   A C   
2030 O  O   . HIS   A 94  ? 0.1278 0.1511 0.1903 -0.0009 0.0020  -0.0066 94  HIS   A O   
2031 C  CB  . HIS   A 94  ? 0.1246 0.1283 0.1618 -0.0094 -0.0062 0.0196  94  HIS   A CB  
2032 C  CG  . HIS   A 94  ? 0.1358 0.1251 0.1519 -0.0097 -0.0070 0.0172  94  HIS   A CG  
2033 N  ND1 . HIS   A 94  ? 0.1320 0.1292 0.1613 -0.0057 -0.0038 0.0184  94  HIS   A ND1 
2034 C  CD2 . HIS   A 94  ? 0.1416 0.1422 0.1636 -0.0089 -0.0111 0.0051  94  HIS   A CD2 
2035 C  CE1 . HIS   A 94  ? 0.1371 0.1374 0.1589 -0.0072 -0.0185 0.0056  94  HIS   A CE1 
2036 N  NE2 . HIS   A 94  ? 0.1475 0.1399 0.1518 -0.0103 -0.0138 0.0014  94  HIS   A NE2 
2044 N  N   . VAL   A 95  ? 0.1216 0.1231 0.1448 -0.0022 0.0054  0.0134  95  VAL   A N   
2045 C  CA  . VAL   A 95  ? 0.1322 0.1287 0.1374 -0.0043 0.0064  0.0192  95  VAL   A CA  
2046 C  C   . VAL   A 95  ? 0.1323 0.1270 0.1372 -0.0125 0.0065  0.0049  95  VAL   A C   
2047 O  O   . VAL   A 95  ? 0.1370 0.1374 0.1532 0.0115  0.0005  0.0089  95  VAL   A O   
2048 C  CB  . VAL   A 95  ? 0.1336 0.1284 0.1596 -0.0096 0.0026  0.0174  95  VAL   A CB  
2049 C  CG1 . VAL   A 95  ? 0.1506 0.1306 0.1798 -0.0122 0.0027  0.0025  95  VAL   A CG1 
2050 C  CG2 . VAL   A 95  ? 0.1375 0.1351 0.1668 -0.0082 0.0044  0.0298  95  VAL   A CG2 
2060 N  N   . VAL   A 96  ? 0.1363 0.1281 0.1185 -0.0012 0.0039  0.0136  96  VAL   A N   
2061 C  CA  . VAL   A 96  ? 0.1402 0.1294 0.1387 -0.0019 0.0056  0.0171  96  VAL   A CA  
2062 C  C   . VAL   A 96  ? 0.1467 0.1349 0.1478 0.0005  0.0051  0.0143  96  VAL   A C   
2063 O  O   . VAL   A 96  ? 0.1571 0.1359 0.1703 -0.0039 0.0138  -0.0008 96  VAL   A O   
2064 C  CB  . VAL   A 96  ? 0.1433 0.1365 0.1521 -0.0013 0.0109  0.0157  96  VAL   A CB  
2065 C  CG1 . VAL   A 96  ? 0.1546 0.1431 0.1469 -0.0021 0.0142  0.0103  96  VAL   A CG1 
2066 C  CG2 . VAL   A 96  ? 0.1483 0.1462 0.1564 -0.0107 0.0132  0.0062  96  VAL   A CG2 
2076 N  N   . GLY   A 97  ? 0.1430 0.1358 0.1418 -0.0054 0.0044  0.0108  97  GLY   A N   
2077 C  CA  . GLY   A 97  ? 0.1504 0.1497 0.1410 -0.0013 -0.0033 0.0127  97  GLY   A CA  
2078 C  C   . GLY   A 97  ? 0.1523 0.1590 0.1366 -0.0067 -0.0092 0.0116  97  GLY   A C   
2079 O  O   . GLY   A 97  ? 0.1655 0.1567 0.1677 -0.0123 -0.0026 0.0190  97  GLY   A O   
2083 N  N   A PRO   A 98  ? 0.1547 0.1650 0.1356 -0.0024 -0.0104 0.0116  98  PRO   A N   
2084 N  N   B PRO   A 98  ? 0.1639 0.1581 0.1480 0.0009  -0.0050 0.0263  98  PRO   A N   
2085 C  CA  A PRO   A 98  ? 0.1592 0.1819 0.1468 -0.0018 -0.0061 0.0047  98  PRO   A CA  
2086 C  CA  B PRO   A 98  ? 0.1722 0.1657 0.1586 0.0014  -0.0081 0.0204  98  PRO   A CA  
2087 C  C   A PRO   A 98  ? 0.1617 0.1844 0.1426 -0.0068 -0.0014 0.0123  98  PRO   A C   
2088 C  C   B PRO   A 98  ? 0.1849 0.1614 0.1505 -0.0004 -0.0015 0.0214  98  PRO   A C   
2089 O  O   A PRO   A 98  ? 0.1528 0.1639 0.1398 -0.0003 0.0072  0.0101  98  PRO   A O   
2090 O  O   B PRO   A 98  ? 0.1833 0.1604 0.1793 0.0061  0.0061  0.0087  98  PRO   A O   
2091 C  CB  A PRO   A 98  ? 0.1636 0.1909 0.1423 0.0099  -0.0121 -0.0113 98  PRO   A CB  
2092 C  CB  B PRO   A 98  ? 0.1729 0.1661 0.1690 0.0134  -0.0103 0.0243  98  PRO   A CB  
2093 C  CG  A PRO   A 98  ? 0.1607 0.1787 0.1325 0.0100  -0.0188 -0.0203 98  PRO   A CG  
2094 C  CG  B PRO   A 98  ? 0.1766 0.1640 0.1749 0.0123  -0.0090 0.0220  98  PRO   A CG  
2095 C  CD  A PRO   A 98  ? 0.1557 0.1654 0.1389 0.0029  -0.0124 -0.0104 98  PRO   A CD  
2096 C  CD  B PRO   A 98  ? 0.1644 0.1536 0.1535 0.0086  -0.0123 0.0344  98  PRO   A CD  
2111 N  N   A ASN   A 99  ? 0.1729 0.2088 0.1466 -0.0085 -0.0018 0.0247  99  ASN   A N   
2112 N  N   B ASN   A 99  ? 0.1998 0.1612 0.1211 0.0071  -0.0010 0.0365  99  ASN   A N   
2113 C  CA  A ASN   A 99  ? 0.1915 0.2202 0.1425 -0.0116 0.0026  0.0288  99  ASN   A CA  
2114 C  CA  B ASN   A 99  ? 0.2215 0.1656 0.1281 0.0106  -0.0049 0.0371  99  ASN   A CA  
2115 C  C   A ASN   A 99  ? 0.2160 0.2422 0.1310 -0.0160 0.0056  0.0316  99  ASN   A C   
2116 C  C   B ASN   A 99  ? 0.2327 0.1730 0.1292 0.0091  -0.0114 0.0466  99  ASN   A C   
2117 O  O   A ASN   A 99  ? 0.2222 0.2631 0.1547 -0.0066 0.0014  0.0250  99  ASN   A O   
2118 O  O   B ASN   A 99  ? 0.2291 0.1567 0.1352 0.0185  -0.0202 0.0267  99  ASN   A O   
2119 C  CB  A ASN   A 99  ? 0.1921 0.2154 0.1620 -0.0167 -0.0220 0.0294  99  ASN   A CB  
2120 C  CB  B ASN   A 99  ? 0.2300 0.1620 0.1764 0.0202  -0.0198 0.0321  99  ASN   A CB  
2121 C  CG  A ASN   A 99  ? 0.2002 0.2058 0.2064 -0.0133 -0.0289 0.0040  99  ASN   A CG  
2122 C  CG  B ASN   A 99  ? 0.2362 0.1725 0.2067 0.0233  -0.0300 0.0273  99  ASN   A CG  
2123 O  OD1 A ASN   A 99  ? 0.1997 0.2137 0.1845 0.0051  -0.0192 0.0013  99  ASN   A OD1 
2124 O  OD1 B ASN   A 99  ? 0.2362 0.1734 0.1771 0.0227  -0.0357 0.0570  99  ASN   A OD1 
2125 N  ND2 A ASN   A 99  ? 0.2058 0.1817 0.2364 -0.0211 -0.0466 0.0195  99  ASN   A ND2 
2126 N  ND2 B ASN   A 99  ? 0.2362 0.1805 0.2180 0.0335  -0.0374 0.0070  99  ASN   A ND2 
2139 N  N   A VAL   A 100 ? 0.2329 0.2475 0.1433 -0.0303 -0.0242 0.0210  100 VAL   A N   
2140 N  N   B VAL   A 100 ? 0.2463 0.1988 0.1499 0.0037  -0.0124 0.0578  100 VAL   A N   
2141 C  CA  A VAL   A 100 ? 0.2559 0.2711 0.1650 -0.0360 -0.0302 0.0235  100 VAL   A CA  
2142 C  CA  B VAL   A 100 ? 0.2659 0.2221 0.1889 -0.0028 -0.0256 0.0551  100 VAL   A CA  
2143 C  C   A VAL   A 100 ? 0.2694 0.2900 0.1695 -0.0399 -0.0294 0.0445  100 VAL   A C   
2144 C  C   B VAL   A 100 ? 0.2687 0.2310 0.1950 0.0037  -0.0413 0.0543  100 VAL   A C   
2145 O  O   A VAL   A 100 ? 0.2759 0.2954 0.1720 -0.0355 -0.0142 0.0487  100 VAL   A O   
2146 O  O   B VAL   A 100 ? 0.2723 0.2401 0.2172 0.0024  -0.0517 0.0330  100 VAL   A O   
2147 C  CB  A VAL   A 100 ? 0.2685 0.2751 0.1847 -0.0344 -0.0284 0.0080  100 VAL   A CB  
2148 C  CB  B VAL   A 100 ? 0.2826 0.2428 0.2449 -0.0108 -0.0222 0.0426  100 VAL   A CB  
2149 C  CG1 A VAL   A 100 ? 0.2731 0.2845 0.2100 -0.0344 -0.0124 -0.0013 100 VAL   A CG1 
2150 C  CG1 B VAL   A 100 ? 0.2853 0.2456 0.2674 -0.0119 -0.0194 0.0357  100 VAL   A CG1 
2151 C  CG2 A VAL   A 100 ? 0.2738 0.2748 0.1794 -0.0393 -0.0222 0.0102  100 VAL   A CG2 
2152 C  CG2 B VAL   A 100 ? 0.2882 0.2527 0.2669 -0.0098 -0.0229 0.0434  100 VAL   A CG2 
2171 N  N   A ASN   A 101 ? 0.2747 0.2963 0.1999 -0.0453 -0.0379 0.0746  101 ASN   A N   
2172 N  N   B ASN   A 101 ? 0.2734 0.2368 0.1922 0.0064  -0.0479 0.0609  101 ASN   A N   
2173 C  CA  A ASN   A 101 ? 0.2906 0.3105 0.2217 -0.0441 -0.0356 0.0946  101 ASN   A CA  
2174 C  CA  B ASN   A 101 ? 0.2840 0.2472 0.2117 0.0127  -0.0468 0.0688  101 ASN   A CA  
2175 C  C   A ASN   A 101 ? 0.3196 0.3495 0.2425 -0.0433 -0.0137 0.1270  101 ASN   A C   
2176 C  C   B ASN   A 101 ? 0.3036 0.2668 0.2127 0.0158  -0.0360 0.0883  101 ASN   A C   
2177 O  O   A ASN   A 101 ? 0.3332 0.3564 0.2821 -0.0399 -0.0104 0.1182  101 ASN   A O   
2178 O  O   B ASN   A 101 ? 0.3119 0.2737 0.2042 0.0127  -0.0387 0.0893  101 ASN   A O   
2179 C  CB  A ASN   A 101 ? 0.2778 0.2859 0.1992 -0.0398 -0.0614 0.0847  101 ASN   A CB  
2180 C  CB  B ASN   A 101 ? 0.2738 0.2384 0.2232 0.0130  -0.0483 0.0617  101 ASN   A CB  
2181 C  CG  A ASN   A 101 ? 0.2698 0.2664 0.1985 -0.0357 -0.0718 0.0564  101 ASN   A CG  
2182 C  CG  B ASN   A 101 ? 0.2670 0.2380 0.2466 0.0104  -0.0495 0.0472  101 ASN   A CG  
2183 O  OD1 A ASN   A 101 ? 0.2649 0.2663 0.2250 -0.0223 -0.0647 0.0299  101 ASN   A OD1 
2184 O  OD1 B ASN   A 101 ? 0.2705 0.2462 0.2675 0.0063  -0.0496 0.0460  101 ASN   A OD1 
2185 N  ND2 A ASN   A 101 ? 0.2717 0.2634 0.2089 -0.0389 -0.0745 0.0379  101 ASN   A ND2 
2186 N  ND2 B ASN   A 101 ? 0.2644 0.2300 0.2607 0.0108  -0.0389 0.0299  101 ASN   A ND2 
2199 N  N   A LYS   A 102 ? 0.3305 0.3829 0.2606 -0.0461 -0.0063 0.1421  102 LYS   A N   
2200 N  N   B LYS   A 102 ? 0.3149 0.2827 0.2505 0.0159  -0.0101 0.0958  102 LYS   A N   
2201 C  CA  A LYS   A 102 ? 0.3461 0.4147 0.2792 -0.0415 -0.0201 0.1371  102 LYS   A CA  
2202 C  CA  B LYS   A 102 ? 0.3306 0.3038 0.2727 0.0090  0.0101  0.0940  102 LYS   A CA  
2203 C  C   A LYS   A 102 ? 0.3548 0.4349 0.2624 -0.0279 -0.0249 0.1295  102 LYS   A C   
2204 C  C   B LYS   A 102 ? 0.3305 0.3068 0.2674 0.0178  0.0002  0.1076  102 LYS   A C   
2205 O  O   A LYS   A 102 ? 0.3584 0.4468 0.2615 -0.0196 -0.0360 0.1306  102 LYS   A O   
2206 O  O   B LYS   A 102 ? 0.3358 0.3043 0.2694 0.0198  0.0089  0.1276  102 LYS   A O   
2207 C  CB  A LYS   A 102 ? 0.3561 0.4263 0.3332 -0.0484 -0.0372 0.1216  102 LYS   A CB  
2208 C  CB  B LYS   A 102 ? 0.3473 0.3236 0.3254 -0.0031 0.0238  0.0696  102 LYS   A CB  
2209 C  CG  A LYS   A 102 ? 0.3649 0.4358 0.3797 -0.0548 -0.0539 0.0995  102 LYS   A CG  
2210 C  CG  B LYS   A 102 ? 0.3640 0.3412 0.3666 -0.0120 0.0332  0.0425  102 LYS   A CG  
2211 C  CD  A LYS   A 102 ? 0.3754 0.4454 0.4292 -0.0575 -0.0628 0.0745  102 LYS   A CD  
2212 C  CD  B LYS   A 102 ? 0.3806 0.3581 0.4083 -0.0185 0.0435  0.0219  102 LYS   A CD  
2213 C  CE  A LYS   A 102 ? 0.3843 0.4514 0.4680 -0.0577 -0.0692 0.0599  102 LYS   A CE  
2214 C  CE  B LYS   A 102 ? 0.3915 0.3712 0.4380 -0.0232 0.0497  0.0050  102 LYS   A CE  
2215 N  NZ  A LYS   A 102 ? 0.3878 0.4533 0.4882 -0.0612 -0.0760 0.0513  102 LYS   A NZ  
2216 N  NZ  B LYS   A 102 ? 0.3978 0.3788 0.4541 -0.0247 0.0544  -0.0029 102 LYS   A NZ  
2243 N  N   A GLY   A 103 ? 0.3572 0.4440 0.2776 -0.0187 -0.0235 0.1041  103 GLY   A N   
2244 N  N   B GLY   A 103 ? 0.3239 0.3141 0.2575 0.0294  -0.0191 0.0894  103 GLY   A N   
2245 C  CA  A GLY   A 103 ? 0.3583 0.4465 0.2728 -0.0112 -0.0203 0.0838  103 GLY   A CA  
2246 C  CA  B GLY   A 103 ? 0.3154 0.3189 0.2604 0.0367  -0.0283 0.0771  103 GLY   A CA  
2247 C  C   A GLY   A 103 ? 0.3523 0.4468 0.2701 -0.0084 -0.0125 0.0608  103 GLY   A C   
2248 C  C   B GLY   A 103 ? 0.3033 0.3189 0.2489 0.0432  -0.0351 0.0590  103 GLY   A C   
2249 O  O   A GLY   A 103 ? 0.3615 0.4572 0.2959 -0.0011 -0.0133 0.0486  103 GLY   A O   
2250 O  O   B GLY   A 103 ? 0.3081 0.3293 0.2596 0.0478  -0.0390 0.0544  103 GLY   A O   
2257 N  N   A GLU   A 104 ? 0.3321 0.4314 0.2228 -0.0177 0.0006  0.0490  104 GLU   A N   
2258 N  N   B GLU   A 104 ? 0.2807 0.3007 0.2079 0.0446  -0.0413 0.0642  104 GLU   A N   
2259 C  CA  A GLU   A 104 ? 0.3094 0.4135 0.1923 -0.0305 0.0144  0.0370  104 GLU   A CA  
2260 C  CA  B GLU   A 104 ? 0.2639 0.2861 0.1834 0.0393  -0.0340 0.0471  104 GLU   A CA  
2261 C  C   A GLU   A 104 ? 0.3159 0.4149 0.1902 -0.0271 0.0089  0.0094  104 GLU   A C   
2262 C  C   B GLU   A 104 ? 0.2521 0.2740 0.1832 0.0443  -0.0190 0.0162  104 GLU   A C   
2263 O  O   A GLU   A 104 ? 0.3141 0.4139 0.1942 -0.0325 0.0078  -0.0115 104 GLU   A O   
2264 O  O   B GLU   A 104 ? 0.2450 0.2722 0.1989 0.0438  -0.0187 0.0064  104 GLU   A O   
2265 C  CB  A GLU   A 104 ? 0.2766 0.3926 0.1757 -0.0483 0.0286  0.0562  104 GLU   A CB  
2266 C  CB  B GLU   A 104 ? 0.2629 0.2869 0.1894 0.0283  -0.0342 0.0549  104 GLU   A CB  
2267 C  CG  A GLU   A 104 ? 0.2544 0.3748 0.1959 -0.0590 0.0165  0.0668  104 GLU   A CG  
2268 C  CG  B GLU   A 104 ? 0.2652 0.2943 0.2085 0.0206  -0.0433 0.0600  104 GLU   A CG  
2269 C  CD  A GLU   A 104 ? 0.2331 0.3551 0.1980 -0.0651 0.0093  0.0809  104 GLU   A CD  
2270 C  CD  B GLU   A 104 ? 0.2669 0.3027 0.2127 0.0179  -0.0531 0.0647  104 GLU   A CD  
2271 O  OE1 A GLU   A 104 ? 0.2189 0.3357 0.1573 -0.0639 0.0021  0.0896  104 GLU   A OE1 
2272 O  OE1 B GLU   A 104 ? 0.2661 0.3074 0.2290 0.0225  -0.0484 0.0590  104 GLU   A OE1 
2273 O  OE2 A GLU   A 104 ? 0.2360 0.3562 0.2310 -0.0723 0.0071  0.0889  104 GLU   A OE2 
2274 O  OE2 B GLU   A 104 ? 0.2728 0.3092 0.2164 0.0096  -0.0629 0.0662  104 GLU   A OE2 
2287 N  N   A ASP   A 105 ? 0.3178 0.4148 0.1889 -0.0188 0.0035  0.0018  105 ASP   A N   
2288 N  N   B ASP   A 105 ? 0.2498 0.2646 0.1901 0.0471  -0.0156 0.0030  105 ASP   A N   
2289 C  CA  A ASP   A 105 ? 0.3175 0.4151 0.2206 -0.0056 0.0054  -0.0223 105 ASP   A CA  
2290 C  CA  B ASP   A 105 ? 0.2432 0.2521 0.1987 0.0553  -0.0018 -0.0242 105 ASP   A CA  
2291 C  C   A ASP   A 105 ? 0.2915 0.3960 0.2047 -0.0116 -0.0024 -0.0348 105 ASP   A C   
2292 C  C   B ASP   A 105 ? 0.2347 0.2296 0.1825 0.0485  -0.0029 -0.0205 105 ASP   A C   
2293 O  O   A ASP   A 105 ? 0.2825 0.3963 0.1695 -0.0110 -0.0057 -0.0468 105 ASP   A O   
2294 O  O   B ASP   A 105 ? 0.2239 0.2116 0.1491 0.0526  -0.0084 -0.0042 105 ASP   A O   
2295 C  CB  A ASP   A 105 ? 0.3393 0.4337 0.2794 0.0100  0.0166  -0.0335 105 ASP   A CB  
2296 C  CB  B ASP   A 105 ? 0.2443 0.2661 0.2357 0.0665  0.0030  -0.0453 105 ASP   A CB  
2297 C  CG  A ASP   A 105 ? 0.3567 0.4502 0.3388 0.0234  0.0223  -0.0430 105 ASP   A CG  
2298 C  CG  B ASP   A 105 ? 0.2466 0.2759 0.2658 0.0753  0.0044  -0.0648 105 ASP   A CG  
2299 O  OD1 A ASP   A 105 ? 0.3601 0.4564 0.3540 0.0277  0.0210  -0.0529 105 ASP   A OD1 
2300 O  OD1 B ASP   A 105 ? 0.2518 0.2767 0.2617 0.0693  -0.0068 -0.0716 105 ASP   A OD1 
2301 O  OD2 A ASP   A 105 ? 0.3686 0.4569 0.3795 0.0280  0.0287  -0.0397 105 ASP   A OD2 
2302 O  OD2 B ASP   A 105 ? 0.2442 0.2837 0.2938 0.0822  0.0136  -0.0590 105 ASP   A OD2 
2311 N  N   A ILE   A 106 ? 0.2718 0.3715 0.2234 -0.0193 -0.0223 -0.0429 106 ILE   A N   
2312 N  N   B ILE   A 106 ? 0.2372 0.2309 0.2047 0.0414  -0.0163 -0.0271 106 ILE   A N   
2313 C  CA  A ILE   A 106 ? 0.2493 0.3431 0.2406 -0.0292 -0.0336 -0.0552 106 ILE   A CA  
2314 C  CA  B ILE   A 106 ? 0.2405 0.2393 0.2130 0.0248  -0.0196 -0.0401 106 ILE   A CA  
2315 C  C   A ILE   A 106 ? 0.2244 0.3108 0.2392 -0.0417 -0.0270 -0.0698 106 ILE   A C   
2316 C  C   B ILE   A 106 ? 0.2515 0.2426 0.2209 0.0163  -0.0076 -0.0197 106 ILE   A C   
2317 O  O   A ILE   A 106 ? 0.1948 0.2888 0.2382 -0.0452 -0.0093 -0.0616 106 ILE   A O   
2318 O  O   B ILE   A 106 ? 0.2446 0.2405 0.2218 0.0102  0.0089  -0.0062 106 ILE   A O   
2319 C  CB  A ILE   A 106 ? 0.2542 0.3484 0.2803 -0.0221 -0.0520 -0.0372 106 ILE   A CB  
2320 C  CB  B ILE   A 106 ? 0.2410 0.2554 0.2379 0.0121  -0.0376 -0.0554 106 ILE   A CB  
2321 C  CG1 A ILE   A 106 ? 0.2471 0.3422 0.3046 -0.0136 -0.0571 -0.0257 106 ILE   A CG1 
2322 C  CG1 B ILE   A 106 ? 0.2363 0.2636 0.2440 0.0083  -0.0409 -0.0622 106 ILE   A CG1 
2323 C  CG2 A ILE   A 106 ? 0.2625 0.3550 0.2965 -0.0196 -0.0535 -0.0302 106 ILE   A CG2 
2324 C  CG2 B ILE   A 106 ? 0.2458 0.2604 0.2443 0.0090  -0.0431 -0.0620 106 ILE   A CG2 
2325 C  CD1 A ILE   A 106 ? 0.2431 0.3369 0.3166 -0.0107 -0.0618 -0.0166 106 ILE   A CD1 
2326 C  CD1 B ILE   A 106 ? 0.2304 0.2655 0.2500 0.0049  -0.0412 -0.0616 106 ILE   A CD1 
2349 N  N   A GLN   A 107 ? 0.2445 0.3039 0.2694 -0.0442 -0.0233 -0.0895 107 GLN   A N   
2350 N  N   B GLN   A 107 ? 0.2705 0.2483 0.2474 0.0151  -0.0084 -0.0133 107 GLN   A N   
2351 C  CA  A GLN   A 107 ? 0.2674 0.2941 0.3319 -0.0354 -0.0066 -0.0960 107 GLN   A CA  
2352 C  CA  B GLN   A 107 ? 0.2926 0.2616 0.2985 0.0112  -0.0087 -0.0048 107 GLN   A CA  
2353 C  C   A GLN   A 107 ? 0.2320 0.2487 0.3150 -0.0303 0.0177  -0.0713 107 GLN   A C   
2354 C  C   B GLN   A 107 ? 0.2683 0.2299 0.2744 0.0102  0.0007  0.0182  107 GLN   A C   
2355 O  O   A GLN   A 107 ? 0.2347 0.2479 0.3725 -0.0296 0.0312  -0.0679 107 GLN   A O   
2356 O  O   B GLN   A 107 ? 0.2691 0.2247 0.2902 0.0114  -0.0070 0.0272  107 GLN   A O   
2357 C  CB  A GLN   A 107 ? 0.3195 0.3303 0.4208 -0.0385 -0.0207 -0.1062 107 GLN   A CB  
2358 C  CB  B GLN   A 107 ? 0.3325 0.3064 0.3642 0.0032  -0.0228 -0.0129 107 GLN   A CB  
2359 C  CG  A GLN   A 107 ? 0.3740 0.3686 0.5260 -0.0347 -0.0283 -0.0976 107 GLN   A CG  
2360 C  CG  B GLN   A 107 ? 0.3690 0.3496 0.4333 -0.0023 -0.0378 -0.0114 107 GLN   A CG  
2361 C  CD  A GLN   A 107 ? 0.4211 0.3981 0.6190 -0.0322 -0.0321 -0.0840 107 GLN   A CD  
2362 C  CD  B GLN   A 107 ? 0.3986 0.3862 0.4990 -0.0050 -0.0483 -0.0070 107 GLN   A CD  
2363 O  OE1 A GLN   A 107 ? 0.4384 0.4079 0.6538 -0.0327 -0.0334 -0.0785 107 GLN   A OE1 
2364 O  OE1 B GLN   A 107 ? 0.4051 0.3918 0.5158 -0.0047 -0.0535 -0.0047 107 GLN   A OE1 
2365 N  NE2 A GLN   A 107 ? 0.4314 0.4067 0.6498 -0.0306 -0.0341 -0.0816 107 GLN   A NE2 
2366 N  NE2 B GLN   A 107 ? 0.4070 0.3968 0.5167 -0.0073 -0.0535 -0.0061 107 GLN   A NE2 
2383 N  N   A LEU   A 108 ? 0.1983 0.2089 0.2430 -0.0274 0.0284  -0.0608 108 LEU   A N   
2384 N  N   B LEU   A 108 ? 0.2428 0.2095 0.2385 0.0055  0.0133  0.0214  108 LEU   A N   
2385 C  CA  A LEU   A 108 ? 0.1832 0.1861 0.2132 -0.0108 0.0216  -0.0287 108 LEU   A CA  
2386 C  CA  B LEU   A 108 ? 0.2208 0.1941 0.2179 0.0055  0.0202  0.0160  108 LEU   A CA  
2387 C  C   A LEU   A 108 ? 0.1712 0.1597 0.2122 -0.0045 0.0190  -0.0058 108 LEU   A C   
2388 C  C   B LEU   A 108 ? 0.1936 0.1704 0.2111 0.0046  0.0224  0.0168  108 LEU   A C   
2389 O  O   A LEU   A 108 ? 0.1704 0.1579 0.2248 -0.0032 0.0217  0.0035  108 LEU   A O   
2390 O  O   B LEU   A 108 ? 0.1942 0.1706 0.2159 0.0059  0.0315  0.0238  108 LEU   A O   
2391 C  CB  A LEU   A 108 ? 0.1864 0.2008 0.1937 -0.0146 0.0235  -0.0247 108 LEU   A CB  
2392 C  CB  B LEU   A 108 ? 0.2287 0.2068 0.2045 0.0005  0.0223  0.0125  108 LEU   A CB  
2393 C  CG  A LEU   A 108 ? 0.1951 0.2258 0.2151 -0.0118 0.0320  -0.0145 108 LEU   A CG  
2394 C  CG  B LEU   A 108 ? 0.2371 0.2203 0.2176 0.0022  0.0269  0.0134  108 LEU   A CG  
2395 C  CD1 A LEU   A 108 ? 0.2114 0.2339 0.2347 -0.0196 0.0349  -0.0103 108 LEU   A CD1 
2396 C  CD1 B LEU   A 108 ? 0.2466 0.2248 0.2272 -0.0008 0.0321  0.0148  108 LEU   A CD1 
2397 C  CD2 A LEU   A 108 ? 0.1971 0.2453 0.2593 -0.0035 0.0305  -0.0075 108 LEU   A CD2 
2398 C  CD2 B LEU   A 108 ? 0.2393 0.2321 0.2454 0.0056  0.0249  0.0124  108 LEU   A CD2 
2421 N  N   . LEU   A 109 ? 0.1710 0.1586 0.2057 0.0069  0.0200  0.0140  109 LEU   A N   
2422 C  CA  . LEU   A 109 ? 0.1614 0.1525 0.1980 0.0105  0.0067  0.0171  109 LEU   A CA  
2423 C  C   . LEU   A 109 ? 0.1444 0.1447 0.1974 0.0024  0.0165  0.0102  109 LEU   A C   
2424 O  O   . LEU   A 109 ? 0.1548 0.1366 0.2146 -0.0034 0.0103  0.0094  109 LEU   A O   
2425 C  CB  . LEU   A 109 ? 0.1644 0.1581 0.2175 0.0140  0.0028  0.0261  109 LEU   A CB  
2426 C  CG  . LEU   A 109 ? 0.1650 0.1654 0.2263 0.0085  0.0070  0.0344  109 LEU   A CG  
2427 C  CD1 . LEU   A 109 ? 0.1661 0.1618 0.2240 0.0000  0.0138  0.0171  109 LEU   A CD1 
2428 C  CD2 . LEU   A 109 ? 0.1576 0.1880 0.2418 0.0123  0.0043  0.0332  109 LEU   A CD2 
2441 N  N   . LYS   A 110 ? 0.1518 0.1456 0.1901 0.0004  -0.0069 0.0040  110 LYS   A N   
2442 C  CA  . LYS   A 110 ? 0.1535 0.1369 0.2021 -0.0075 -0.0085 0.0133  110 LYS   A CA  
2443 C  C   . LYS   A 110 ? 0.1482 0.1345 0.1807 -0.0066 -0.0032 -0.0018 110 LYS   A C   
2444 O  O   . LYS   A 110 ? 0.1403 0.1345 0.2003 -0.0044 0.0014  -0.0023 110 LYS   A O   
2445 C  CB  . LYS   A 110 ? 0.1528 0.1453 0.2206 -0.0018 -0.0118 -0.0016 110 LYS   A CB  
2446 C  CG  . LYS   A 110 ? 0.1586 0.1449 0.2358 0.0013  -0.0153 -0.0043 110 LYS   A CG  
2447 C  CD  . LYS   A 110 ? 0.1628 0.1491 0.2553 -0.0039 -0.0060 -0.0105 110 LYS   A CD  
2448 C  CE  . LYS   A 110 ? 0.1739 0.1527 0.2739 -0.0061 0.0116  -0.0105 110 LYS   A CE  
2449 N  NZ  . LYS   A 110 ? 0.1732 0.1608 0.2762 -0.0138 0.0144  -0.0032 110 LYS   A NZ  
2463 N  N   . SER   A 111 ? 0.1490 0.1363 0.1768 0.0014  -0.0039 0.0011  111 SER   A N   
2464 C  CA  . SER   A 111 ? 0.1443 0.1404 0.1891 0.0004  0.0059  -0.0003 111 SER   A CA  
2465 C  C   . SER   A 111 ? 0.1378 0.1372 0.1866 -0.0023 0.0097  0.0144  111 SER   A C   
2466 O  O   . SER   A 111 ? 0.1516 0.1309 0.2092 -0.0035 0.0097  0.0114  111 SER   A O   
2467 C  CB  . SER   A 111 ? 0.1647 0.1677 0.2013 0.0014  0.0044  -0.0136 111 SER   A CB  
2468 O  OG  . SER   A 111 ? 0.2078 0.1861 0.2166 0.0057  0.0166  -0.0200 111 SER   A OG  
2474 N  N   . ALA   A 112 ? 0.1446 0.1325 0.1797 -0.0003 0.0061  0.0103  112 ALA   A N   
2475 C  CA  . ALA   A 112 ? 0.1486 0.1289 0.1727 -0.0041 0.0133  0.0041  112 ALA   A CA  
2476 C  C   . ALA   A 112 ? 0.1404 0.1259 0.1793 0.0001  0.0007  0.0065  112 ALA   A C   
2477 O  O   . ALA   A 112 ? 0.1442 0.1252 0.1855 -0.0085 0.0120  0.0157  112 ALA   A O   
2478 C  CB  . ALA   A 112 ? 0.1616 0.1306 0.1828 -0.0048 0.0090  0.0137  112 ALA   A CB  
2484 N  N   . TYR   A 113 ? 0.1299 0.1330 0.1959 -0.0030 0.0122  0.0172  113 TYR   A N   
2485 C  CA  . TYR   A 113 ? 0.1335 0.1298 0.1869 -0.0061 0.0104  0.0183  113 TYR   A CA  
2486 C  C   . TYR   A 113 ? 0.1289 0.1275 0.1625 -0.0119 0.0045  0.0077  113 TYR   A C   
2487 O  O   . TYR   A 113 ? 0.1330 0.1330 0.1925 -0.0027 0.0166  0.0107  113 TYR   A O   
2488 C  CB  . TYR   A 113 ? 0.1290 0.1337 0.1983 -0.0004 0.0007  0.0276  113 TYR   A CB  
2489 C  CG  . TYR   A 113 ? 0.1305 0.1440 0.1899 -0.0063 0.0144  0.0271  113 TYR   A CG  
2490 C  CD1 . TYR   A 113 ? 0.1352 0.1546 0.1958 -0.0032 0.0127  0.0284  113 TYR   A CD1 
2491 C  CD2 . TYR   A 113 ? 0.1406 0.1484 0.1898 -0.0080 0.0022  0.0203  113 TYR   A CD2 
2492 C  CE1 . TYR   A 113 ? 0.1390 0.1640 0.1936 -0.0038 0.0065  0.0223  113 TYR   A CE1 
2493 C  CE2 . TYR   A 113 ? 0.1419 0.1534 0.1963 -0.0103 0.0016  0.0360  113 TYR   A CE2 
2494 C  CZ  . TYR   A 113 ? 0.1379 0.1569 0.1960 0.0048  0.0119  0.0264  113 TYR   A CZ  
2495 O  OH  . TYR   A 113 ? 0.1376 0.1638 0.2162 0.0089  0.0140  0.0257  113 TYR   A OH  
2505 N  N   . GLU   A 114 ? 0.1303 0.1265 0.1795 -0.0043 0.0121  0.0162  114 GLU   A N   
2506 C  CA  . GLU   A 114 ? 0.1370 0.1266 0.1985 0.0045  0.0075  0.0192  114 GLU   A CA  
2507 C  C   . GLU   A 114 ? 0.1343 0.1294 0.1853 -0.0016 0.0027  0.0190  114 GLU   A C   
2508 O  O   . GLU   A 114 ? 0.1447 0.1296 0.2034 0.0013  0.0039  0.0210  114 GLU   A O   
2509 C  CB  . GLU   A 114 ? 0.1366 0.1305 0.2008 -0.0045 0.0032  0.0152  114 GLU   A CB  
2510 C  CG  . GLU   A 114 ? 0.1428 0.1365 0.2164 -0.0009 0.0067  0.0112  114 GLU   A CG  
2511 C  CD  . GLU   A 114 ? 0.1456 0.1316 0.2207 0.0001  -0.0030 0.0083  114 GLU   A CD  
2512 O  OE1 . GLU   A 114 ? 0.1520 0.1402 0.2311 -0.0109 0.0100  -0.0031 114 GLU   A OE1 
2513 O  OE2 . GLU   A 114 ? 0.1711 0.1453 0.2345 -0.0104 0.0039  -0.0136 114 GLU   A OE2 
2520 N  N   . ASN   A 115 ? 0.1363 0.1309 0.1894 -0.0045 0.0074  0.0109  115 ASN   A N   
2521 C  CA  . ASN   A 115 ? 0.1385 0.1375 0.1920 -0.0083 0.0123  0.0156  115 ASN   A CA  
2522 C  C   . ASN   A 115 ? 0.1420 0.1346 0.1880 -0.0097 0.0034  0.0137  115 ASN   A C   
2523 O  O   . ASN   A 115 ? 0.1436 0.1450 0.1831 -0.0093 0.0103  0.0167  115 ASN   A O   
2524 C  CB  . ASN   A 115 ? 0.1473 0.1453 0.1862 -0.0097 0.0129  0.0184  115 ASN   A CB  
2525 C  CG  . ASN   A 115 ? 0.1430 0.1614 0.1998 -0.0158 0.0153  0.0079  115 ASN   A CG  
2526 O  OD1 . ASN   A 115 ? 0.1475 0.2497 0.2211 -0.0160 0.0212  0.0279  115 ASN   A OD1 
2527 N  ND2 . ASN   A 115 ? 0.1471 0.1458 0.1933 -0.0144 0.0235  0.0150  115 ASN   A ND2 
2534 N  N   . PHE   A 116 ? 0.1315 0.1314 0.1975 0.0029  0.0135  0.0211  116 PHE   A N   
2535 C  CA  . PHE   A 116 ? 0.1330 0.1342 0.1800 0.0010  0.0151  0.0178  116 PHE   A CA  
2536 C  C   . PHE   A 116 ? 0.1340 0.1453 0.1885 -0.0077 0.0157  0.0297  116 PHE   A C   
2537 O  O   . PHE   A 116 ? 0.1365 0.1518 0.2031 0.0058  0.0186  0.0387  116 PHE   A O   
2538 C  CB  . PHE   A 116 ? 0.1352 0.1370 0.1940 -0.0043 0.0160  0.0151  116 PHE   A CB  
2539 C  CG  . PHE   A 116 ? 0.1377 0.1343 0.1778 -0.0052 0.0107  0.0178  116 PHE   A CG  
2540 C  CD1 . PHE   A 116 ? 0.1400 0.1314 0.1755 -0.0083 0.0083  0.0126  116 PHE   A CD1 
2541 C  CD2 . PHE   A 116 ? 0.1419 0.1442 0.1968 -0.0058 0.0110  0.0159  116 PHE   A CD2 
2542 C  CE1 . PHE   A 116 ? 0.1389 0.1339 0.1973 -0.0160 0.0079  0.0112  116 PHE   A CE1 
2543 C  CE2 . PHE   A 116 ? 0.1362 0.1383 0.2081 -0.0025 0.0147  0.0136  116 PHE   A CE2 
2544 C  CZ  . PHE   A 116 ? 0.1440 0.1241 0.1965 -0.0034 0.0008  0.0115  116 PHE   A CZ  
2554 N  N   . ASN   A 117 ? 0.1339 0.1381 0.1974 -0.0065 0.0084  0.0231  117 ASN   A N   
2555 C  CA  . ASN   A 117 ? 0.1435 0.1363 0.2056 -0.0004 0.0122  0.0296  117 ASN   A CA  
2556 C  C   . ASN   A 117 ? 0.1478 0.1414 0.2194 -0.0037 0.0154  0.0219  117 ASN   A C   
2557 O  O   . ASN   A 117 ? 0.1527 0.1485 0.2303 -0.0063 0.0010  0.0348  117 ASN   A O   
2558 C  CB  . ASN   A 117 ? 0.1386 0.1419 0.2066 -0.0064 0.0075  0.0301  117 ASN   A CB  
2559 C  CG  . ASN   A 117 ? 0.1403 0.1450 0.2133 -0.0053 0.0106  0.0314  117 ASN   A CG  
2560 O  OD1 . ASN   A 117 ? 0.1403 0.1655 0.2224 -0.0142 0.0147  0.0203  117 ASN   A OD1 
2561 N  ND2 . ASN   A 117 ? 0.1318 0.1406 0.2117 -0.0068 0.0107  0.0367  117 ASN   A ND2 
2568 N  N   . GLN   A 118 ? 0.1356 0.1477 0.2152 -0.0037 0.0037  0.0296  118 GLN   A N   
2569 C  CA  . GLN   A 118 ? 0.1449 0.1568 0.2208 -0.0078 0.0072  0.0248  118 GLN   A CA  
2570 C  C   . GLN   A 118 ? 0.1518 0.1693 0.2100 -0.0066 -0.0006 0.0337  118 GLN   A C   
2571 O  O   . GLN   A 118 ? 0.1484 0.1957 0.2384 0.0033  -0.0130 0.0143  118 GLN   A O   
2572 C  CB  . GLN   A 118 ? 0.1414 0.1542 0.2472 -0.0012 0.0147  0.0263  118 GLN   A CB  
2573 C  CG  . GLN   A 118 ? 0.1395 0.1603 0.2449 0.0022  0.0107  0.0373  118 GLN   A CG  
2574 C  CD  . GLN   A 118 ? 0.1415 0.1613 0.2491 0.0028  0.0095  0.0315  118 GLN   A CD  
2575 O  OE1 . GLN   A 118 ? 0.1434 0.1746 0.2571 0.0088  0.0073  0.0213  118 GLN   A OE1 
2576 N  NE2 . GLN   A 118 ? 0.1490 0.1618 0.2525 0.0049  0.0066  0.0359  118 GLN   A NE2 
2585 N  N   . HIS   A 119 ? 0.1504 0.1564 0.1942 0.0028  -0.0034 0.0355  119 HIS   A N   
2586 C  CA  . HIS   A 119 ? 0.1573 0.1686 0.1966 -0.0064 -0.0002 0.0374  119 HIS   A CA  
2587 C  C   . HIS   A 119 ? 0.1701 0.1819 0.1899 -0.0113 0.0111  0.0459  119 HIS   A C   
2588 O  O   . HIS   A 119 ? 0.1689 0.1850 0.1950 -0.0242 -0.0035 0.0380  119 HIS   A O   
2589 C  CB  . HIS   A 119 ? 0.1582 0.1614 0.2138 -0.0051 0.0217  0.0336  119 HIS   A CB  
2590 C  CG  . HIS   A 119 ? 0.1576 0.1677 0.2585 0.0023  0.0064  0.0443  119 HIS   A CG  
2591 N  ND1 . HIS   A 119 ? 0.1762 0.1819 0.3216 -0.0100 0.0072  0.0287  119 HIS   A ND1 
2592 C  CD2 . HIS   A 119 ? 0.1696 0.1775 0.2662 0.0096  0.0290  0.0601  119 HIS   A CD2 
2593 C  CE1 . HIS   A 119 ? 0.1728 0.1793 0.3232 -0.0108 0.0182  0.0494  119 HIS   A CE1 
2594 N  NE2 . HIS   A 119 ? 0.1829 0.1786 0.3087 0.0012  0.0412  0.0687  119 HIS   A NE2 
2602 N  N   A GLU   A 120 ? 0.1734 0.1966 0.1923 -0.0049 0.0036  0.0688  120 GLU   A N   
2603 N  N   B GLU   A 120 ? 0.1953 0.2098 0.2135 -0.0093 0.0070  0.0546  120 GLU   A N   
2604 C  CA  A GLU   A 120 ? 0.1910 0.2206 0.2199 -0.0007 0.0014  0.1036  120 GLU   A CA  
2605 C  CA  B GLU   A 120 ? 0.2251 0.2428 0.2480 -0.0053 0.0067  0.0690  120 GLU   A CA  
2606 C  C   A GLU   A 120 ? 0.1726 0.2076 0.1916 -0.0137 0.0031  0.0935  120 GLU   A C   
2607 C  C   B GLU   A 120 ? 0.2146 0.2407 0.2183 -0.0096 0.0068  0.0637  120 GLU   A C   
2608 O  O   A GLU   A 120 ? 0.1646 0.1976 0.2098 -0.0157 0.0039  0.0950  120 GLU   A O   
2609 O  O   B GLU   A 120 ? 0.2146 0.2445 0.2268 -0.0096 0.0016  0.0577  120 GLU   A O   
2610 C  CB  A GLU   A 120 ? 0.2414 0.2635 0.2753 0.0138  0.0010  0.1378  120 GLU   A CB  
2611 C  CB  B GLU   A 120 ? 0.2680 0.2801 0.3146 0.0016  0.0084  0.0808  120 GLU   A CB  
2612 C  CG  A GLU   A 120 ? 0.3066 0.3104 0.3906 0.0271  0.0006  0.1270  120 GLU   A CG  
2613 C  CG  B GLU   A 120 ? 0.3142 0.3180 0.4007 0.0099  0.0094  0.0763  120 GLU   A CG  
2614 C  CD  A GLU   A 120 ? 0.3658 0.3510 0.4915 0.0408  0.0057  0.1098  120 GLU   A CD  
2615 C  CD  B GLU   A 120 ? 0.3569 0.3524 0.4778 0.0183  0.0124  0.0679  120 GLU   A CD  
2616 O  OE1 A GLU   A 120 ? 0.3895 0.3648 0.5123 0.0413  0.0082  0.1040  120 GLU   A OE1 
2617 O  OE1 B GLU   A 120 ? 0.3699 0.3614 0.4931 0.0188  0.0146  0.0661  120 GLU   A OE1 
2618 O  OE2 A GLU   A 120 ? 0.3869 0.3648 0.5313 0.0434  0.0062  0.1005  120 GLU   A OE2 
2619 O  OE2 B GLU   A 120 ? 0.3704 0.3631 0.5088 0.0205  0.0120  0.0635  120 GLU   A OE2 
2632 N  N   A VAL   A 121 ? 0.1701 0.2083 0.1668 -0.0191 0.0090  0.0726  121 VAL   A N   
2633 N  N   B VAL   A 121 ? 0.2053 0.2333 0.1935 -0.0107 0.0105  0.0586  121 VAL   A N   
2634 C  CA  A VAL   A 121 ? 0.1807 0.2261 0.1514 -0.0172 0.0238  0.0695  121 VAL   A CA  
2635 C  CA  B VAL   A 121 ? 0.1999 0.2341 0.1813 -0.0078 0.0171  0.0550  121 VAL   A CA  
2636 C  C   A VAL   A 121 ? 0.1697 0.2072 0.1430 -0.0259 0.0128  0.0468  121 VAL   A C   
2637 C  C   B VAL   A 121 ? 0.1790 0.2085 0.1624 -0.0112 0.0109  0.0489  121 VAL   A C   
2638 O  O   A VAL   A 121 ? 0.1663 0.1998 0.1773 -0.0375 -0.0040 0.0235  121 VAL   A O   
2639 O  O   B VAL   A 121 ? 0.1730 0.2001 0.1618 -0.0037 0.0024  0.0424  121 VAL   A O   
2640 C  CB  A VAL   A 121 ? 0.2164 0.2666 0.2002 -0.0041 0.0346  0.0784  121 VAL   A CB  
2641 C  CB  B VAL   A 121 ? 0.2221 0.2614 0.2174 0.0005  0.0227  0.0540  121 VAL   A CB  
2642 C  CG1 A VAL   A 121 ? 0.2195 0.2793 0.2005 0.0016  0.0413  0.0798  121 VAL   A CG1 
2643 C  CG1 B VAL   A 121 ? 0.2243 0.2696 0.2230 0.0029  0.0240  0.0532  121 VAL   A CG1 
2644 C  CG2 A VAL   A 121 ? 0.2357 0.2844 0.2485 -0.0116 0.0356  0.0689  121 VAL   A CG2 
2645 C  CG2 B VAL   A 121 ? 0.2343 0.2734 0.2466 -0.0014 0.0246  0.0451  121 VAL   A CG2 
2664 N  N   . LEU   A 122 ? 0.1616 0.1850 0.1666 -0.0249 0.0097  0.0488  122 LEU   A N   
2665 C  CA  . LEU   A 122 ? 0.1686 0.1683 0.1696 -0.0204 0.0193  0.0450  122 LEU   A CA  
2666 C  C   . LEU   A 122 ? 0.1602 0.1662 0.1782 -0.0246 0.0052  0.0340  122 LEU   A C   
2667 O  O   . LEU   A 122 ? 0.1570 0.1689 0.2032 -0.0297 0.0107  0.0345  122 LEU   A O   
2668 C  CB  . LEU   A 122 ? 0.1803 0.1704 0.2005 -0.0138 0.0078  0.0569  122 LEU   A CB  
2669 C  CG  . LEU   A 122 ? 0.1741 0.1719 0.2069 -0.0057 0.0181  0.0350  122 LEU   A CG  
2670 C  CD1 . LEU   A 122 ? 0.1829 0.1709 0.2122 -0.0108 0.0224  0.0352  122 LEU   A CD1 
2671 C  CD2 . LEU   A 122 ? 0.1655 0.1657 0.1955 -0.0005 0.0250  0.0342  122 LEU   A CD2 
2684 N  N   . LEU   A 123 ? 0.1521 0.1625 0.1697 -0.0257 0.0028  0.0277  123 LEU   A N   
2685 C  CA  . LEU   A 123 ? 0.1468 0.1645 0.1577 -0.0228 0.0068  0.0235  123 LEU   A CA  
2686 C  C   . LEU   A 123 ? 0.1449 0.1629 0.1592 -0.0143 0.0083  0.0363  123 LEU   A C   
2687 O  O   . LEU   A 123 ? 0.1459 0.1755 0.1731 -0.0275 0.0031  0.0332  123 LEU   A O   
2688 C  CB  . LEU   A 123 ? 0.1617 0.1779 0.1621 -0.0235 0.0164  0.0273  123 LEU   A CB  
2689 C  CG  . LEU   A 123 ? 0.1612 0.1914 0.1793 -0.0140 0.0188  0.0114  123 LEU   A CG  
2690 C  CD1 . LEU   A 123 ? 0.1647 0.2083 0.1999 -0.0065 0.0174  0.0110  123 LEU   A CD1 
2691 C  CD2 . LEU   A 123 ? 0.1801 0.1974 0.1964 -0.0115 0.0096  0.0097  123 LEU   A CD2 
2703 N  N   . ALA   A 124 ? 0.1511 0.1507 0.1498 -0.0137 0.0075  0.0323  124 ALA   A N   
2704 C  CA  . ALA   A 124 ? 0.1423 0.1472 0.1581 -0.0114 -0.0009 0.0245  124 ALA   A CA  
2705 C  C   . ALA   A 124 ? 0.1392 0.1500 0.1680 -0.0168 0.0091  0.0281  124 ALA   A C   
2706 O  O   . ALA   A 124 ? 0.1410 0.1571 0.1733 -0.0108 0.0089  0.0366  124 ALA   A O   
2707 C  CB  . ALA   A 124 ? 0.1446 0.1462 0.1821 -0.0083 0.0053  0.0239  124 ALA   A CB  
2713 N  N   A PRO   A 125 ? 0.1310 0.1463 0.1640 -0.0108 0.0113  0.0353  125 PRO   A N   
2714 N  N   B PRO   A 125 ? 0.1442 0.1510 0.1648 -0.0143 -0.0003 0.0275  125 PRO   A N   
2715 C  CA  A PRO   A 125 ? 0.1366 0.1396 0.1810 -0.0064 0.0042  0.0305  125 PRO   A CA  
2716 C  CA  B PRO   A 125 ? 0.1534 0.1545 0.1707 -0.0063 -0.0055 0.0248  125 PRO   A CA  
2717 C  C   A PRO   A 125 ? 0.1196 0.1402 0.1703 -0.0118 0.0110  0.0321  125 PRO   A C   
2718 C  C   B PRO   A 125 ? 0.1489 0.1636 0.1676 -0.0056 -0.0094 0.0283  125 PRO   A C   
2719 O  O   A PRO   A 125 ? 0.1266 0.1394 0.1919 -0.0078 0.0011  0.0250  125 PRO   A O   
2720 O  O   B PRO   A 125 ? 0.1581 0.1710 0.1827 -0.0068 -0.0151 0.0189  125 PRO   A O   
2721 C  CB  A PRO   A 125 ? 0.1520 0.1398 0.1801 -0.0086 0.0096  0.0273  125 PRO   A CB  
2722 C  CB  B PRO   A 125 ? 0.1603 0.1493 0.1641 -0.0058 0.0037  0.0180  125 PRO   A CB  
2723 C  CG  A PRO   A 125 ? 0.1513 0.1430 0.1720 -0.0136 0.0070  0.0281  125 PRO   A CG  
2724 C  CG  B PRO   A 125 ? 0.1614 0.1455 0.1590 -0.0136 -0.0028 0.0224  125 PRO   A CG  
2725 C  CD  A PRO   A 125 ? 0.1376 0.1515 0.1749 -0.0162 0.0184  0.0294  125 PRO   A CD  
2726 C  CD  B PRO   A 125 ? 0.1504 0.1460 0.1599 -0.0214 0.0003  0.0239  125 PRO   A CD  
2741 N  N   A LEU   A 126 ? 0.1263 0.1537 0.1671 -0.0030 0.0179  0.0319  126 LEU   A N   
2742 N  N   B LEU   A 126 ? 0.1484 0.1683 0.1704 -0.0008 -0.0116 0.0344  126 LEU   A N   
2743 C  CA  A LEU   A 126 ? 0.1339 0.1581 0.1763 -0.0012 0.0029  0.0407  126 LEU   A CA  
2744 C  CA  B LEU   A 126 ? 0.1428 0.1607 0.1793 -0.0059 -0.0099 0.0329  126 LEU   A CA  
2745 C  C   A LEU   A 126 ? 0.1423 0.1615 0.1814 0.0059  -0.0014 0.0348  126 LEU   A C   
2746 C  C   B LEU   A 126 ? 0.1370 0.1538 0.1624 -0.0041 -0.0109 0.0241  126 LEU   A C   
2747 O  O   A LEU   A 126 ? 0.1560 0.1578 0.2248 0.0185  0.0166  0.0460  126 LEU   A O   
2748 O  O   B LEU   A 126 ? 0.1473 0.1498 0.1562 -0.0060 -0.0046 0.0299  126 LEU   A O   
2749 C  CB  A LEU   A 126 ? 0.1444 0.1636 0.2005 0.0012  -0.0068 0.0312  126 LEU   A CB  
2750 C  CB  B LEU   A 126 ? 0.1440 0.1650 0.1992 -0.0165 -0.0002 0.0175  126 LEU   A CB  
2751 C  CG  A LEU   A 126 ? 0.1452 0.1698 0.2231 0.0069  0.0003  0.0318  126 LEU   A CG  
2752 C  CG  B LEU   A 126 ? 0.1354 0.1624 0.2193 -0.0114 0.0036  0.0074  126 LEU   A CG  
2753 C  CD1 A LEU   A 126 ? 0.1492 0.1844 0.2558 0.0041  0.0082  0.0388  126 LEU   A CD1 
2754 C  CD1 B LEU   A 126 ? 0.1349 0.1624 0.2277 -0.0128 -0.0073 0.0071  126 LEU   A CD1 
2755 C  CD2 A LEU   A 126 ? 0.1587 0.1676 0.2178 0.0053  0.0014  0.0306  126 LEU   A CD2 
2756 C  CD2 B LEU   A 126 ? 0.1318 0.1611 0.2326 -0.0122 0.0004  0.0084  126 LEU   A CD2 
2779 N  N   A LEU   A 127 ? 0.1491 0.1678 0.1766 0.0034  0.0058  0.0241  127 LEU   A N   
2780 N  N   B LEU   A 127 ? 0.1337 0.1502 0.1476 -0.0026 -0.0033 0.0304  127 LEU   A N   
2781 C  CA  A LEU   A 127 ? 0.1504 0.1649 0.1624 -0.0026 0.0071  0.0210  127 LEU   A CA  
2782 C  CA  B LEU   A 127 ? 0.1337 0.1568 0.1454 -0.0070 -0.0078 0.0297  127 LEU   A CA  
2783 C  C   A LEU   A 127 ? 0.1496 0.1571 0.1416 -0.0020 0.0069  0.0202  127 LEU   A C   
2784 C  C   B LEU   A 127 ? 0.1341 0.1419 0.1640 -0.0088 -0.0127 0.0213  127 LEU   A C   
2785 O  O   A LEU   A 127 ? 0.1566 0.1547 0.1598 -0.0079 0.0093  0.0132  127 LEU   A O   
2786 O  O   B LEU   A 127 ? 0.1372 0.1267 0.1657 -0.0140 -0.0112 0.0235  127 LEU   A O   
2787 C  CB  A LEU   A 127 ? 0.1456 0.1559 0.1781 0.0042  0.0044  0.0155  127 LEU   A CB  
2788 C  CB  B LEU   A 127 ? 0.1331 0.1773 0.1524 0.0002  -0.0111 0.0235  127 LEU   A CB  
2789 C  CG  A LEU   A 127 ? 0.1526 0.1461 0.1767 -0.0008 -0.0016 0.0203  127 LEU   A CG  
2790 C  CG  B LEU   A 127 ? 0.1415 0.1880 0.1586 0.0053  -0.0081 0.0237  127 LEU   A CG  
2791 C  CD1 A LEU   A 127 ? 0.1536 0.1368 0.1767 -0.0032 -0.0060 0.0158  127 LEU   A CD1 
2792 C  CD1 B LEU   A 127 ? 0.1404 0.1920 0.1788 0.0150  -0.0039 0.0255  127 LEU   A CD1 
2793 C  CD2 A LEU   A 127 ? 0.1616 0.1478 0.1981 0.0063  -0.0160 0.0234  127 LEU   A CD2 
2794 C  CD2 B LEU   A 127 ? 0.1514 0.1945 0.1632 0.0008  -0.0185 0.0128  127 LEU   A CD2 
2817 N  N   A SER   A 128 ? 0.1559 0.1536 0.1369 -0.0020 0.0027  0.0233  128 SER   A N   
2818 N  N   B SER   A 128 ? 0.1424 0.1412 0.1646 -0.0095 -0.0104 0.0077  128 SER   A N   
2819 C  CA  A SER   A 128 ? 0.1585 0.1490 0.1346 0.0047  -0.0039 0.0192  128 SER   A CA  
2820 C  CA  B SER   A 128 ? 0.1436 0.1378 0.1560 -0.0011 0.0042  0.0080  128 SER   A CA  
2821 C  C   A SER   A 128 ? 0.1641 0.1529 0.1257 0.0043  -0.0003 0.0216  128 SER   A C   
2822 C  C   B SER   A 128 ? 0.1453 0.1448 0.1511 0.0004  -0.0099 0.0157  128 SER   A C   
2823 O  O   A SER   A 128 ? 0.1780 0.1706 0.1312 0.0114  0.0075  0.0141  128 SER   A O   
2824 O  O   B SER   A 128 ? 0.1482 0.1492 0.1600 -0.0006 -0.0109 0.0204  128 SER   A O   
2825 C  CB  A SER   A 128 ? 0.1567 0.1517 0.1416 0.0005  -0.0043 0.0113  128 SER   A CB  
2826 C  CB  B SER   A 128 ? 0.1490 0.1442 0.1593 -0.0035 0.0150  0.0072  128 SER   A CB  
2827 O  OG  A SER   A 128 ? 0.1554 0.1534 0.1462 -0.0050 -0.0034 0.0030  128 SER   A OG  
2828 O  OG  B SER   A 128 ? 0.1464 0.1491 0.1657 0.0004  0.0245  0.0077  128 SER   A OG  
2839 N  N   A ALA   A 129 ? 0.1618 0.1533 0.1395 -0.0062 -0.0039 0.0232  129 ALA   A N   
2840 N  N   B ALA   A 129 ? 0.1419 0.1482 0.1650 0.0033  -0.0101 0.0095  129 ALA   A N   
2841 C  CA  A ALA   A 129 ? 0.1548 0.1572 0.1480 -0.0029 0.0051  0.0150  129 ALA   A CA  
2842 C  CA  B ALA   A 129 ? 0.1441 0.1485 0.1761 0.0008  -0.0083 0.0066  129 ALA   A CA  
2843 C  C   A ALA   A 129 ? 0.1539 0.1506 0.1532 -0.0030 -0.0010 0.0028  129 ALA   A C   
2844 C  C   B ALA   A 129 ? 0.1562 0.1566 0.1881 0.0038  -0.0039 0.0048  129 ALA   A C   
2845 O  O   A ALA   A 129 ? 0.1595 0.1496 0.1475 -0.0084 0.0005  0.0141  129 ALA   A O   
2846 O  O   B ALA   A 129 ? 0.1630 0.1636 0.1826 0.0060  -0.0095 0.0009  129 ALA   A O   
2847 C  CB  A ALA   A 129 ? 0.1630 0.1670 0.1634 0.0030  0.0034  0.0169  129 ALA   A CB  
2848 C  CB  B ALA   A 129 ? 0.1455 0.1500 0.1710 0.0001  -0.0026 0.0092  129 ALA   A CB  
2859 N  N   A GLY   A 130 ? 0.1633 0.1498 0.2119 -0.0024 0.0021  0.0033  130 GLY   A N   
2860 N  N   B GLY   A 130 ? 0.1648 0.1578 0.1983 0.0004  0.0022  0.0168  130 GLY   A N   
2861 C  CA  A GLY   A 130 ? 0.1764 0.1502 0.2334 0.0025  -0.0031 0.0013  130 GLY   A CA  
2862 C  CA  B GLY   A 130 ? 0.1771 0.1607 0.1941 0.0032  0.0029  0.0149  130 GLY   A CA  
2863 C  C   A GLY   A 130 ? 0.1765 0.1514 0.2320 0.0040  -0.0205 0.0031  130 GLY   A C   
2864 C  C   B GLY   A 130 ? 0.1827 0.1638 0.1909 0.0030  -0.0006 0.0118  130 GLY   A C   
2865 O  O   A GLY   A 130 ? 0.1757 0.1524 0.2478 0.0029  -0.0287 0.0135  130 GLY   A O   
2866 O  O   B GLY   A 130 ? 0.1828 0.1641 0.1880 -0.0039 -0.0059 0.0164  130 GLY   A O   
2873 N  N   A ILE   A 131 ? 0.1827 0.1483 0.2145 -0.0062 -0.0206 0.0169  131 ILE   A N   
2874 N  N   B ILE   A 131 ? 0.1901 0.1668 0.2041 0.0040  0.0037  0.0128  131 ILE   A N   
2875 C  CA  A ILE   A 131 ? 0.2003 0.1480 0.1831 -0.0102 -0.0356 0.0206  131 ILE   A CA  
2876 C  CA  B ILE   A 131 ? 0.2032 0.1686 0.1884 0.0001  -0.0029 0.0115  131 ILE   A CA  
2877 C  C   A ILE   A 131 ? 0.1877 0.1502 0.1765 -0.0041 -0.0292 0.0321  131 ILE   A C   
2878 C  C   B ILE   A 131 ? 0.1950 0.1620 0.1771 -0.0016 0.0013  0.0084  131 ILE   A C   
2879 O  O   A ILE   A 131 ? 0.2005 0.1600 0.1849 0.0008  -0.0221 0.0324  131 ILE   A O   
2880 O  O   B ILE   A 131 ? 0.1963 0.1571 0.1878 0.0010  -0.0027 0.0109  131 ILE   A O   
2881 C  CB  A ILE   A 131 ? 0.2311 0.1627 0.1833 -0.0284 -0.0364 0.0111  131 ILE   A CB  
2882 C  CB  B ILE   A 131 ? 0.2203 0.1828 0.1924 -0.0073 0.0001  0.0198  131 ILE   A CB  
2883 C  CG1 A ILE   A 131 ? 0.2353 0.1875 0.1780 -0.0449 -0.0380 0.0124  131 ILE   A CG1 
2884 C  CG1 B ILE   A 131 ? 0.2258 0.1941 0.2002 -0.0199 -0.0055 0.0352  131 ILE   A CG1 
2885 C  CG2 A ILE   A 131 ? 0.2530 0.1494 0.1882 -0.0216 -0.0167 0.0134  131 ILE   A CG2 
2886 C  CG2 B ILE   A 131 ? 0.2313 0.1840 0.2068 -0.0012 0.0039  0.0107  131 ILE   A CG2 
2887 C  CD1 A ILE   A 131 ? 0.2443 0.1951 0.1900 -0.0506 -0.0436 0.0147  131 ILE   A CD1 
2888 C  CD1 B ILE   A 131 ? 0.2336 0.2028 0.2148 -0.0251 0.0017  0.0452  131 ILE   A CD1 
2911 N  N   A PHE   A 132 ? 0.1705 0.1452 0.1681 0.0018  -0.0341 0.0311  132 PHE   A N   
2912 N  N   B PHE   A 132 ? 0.1873 0.1617 0.1706 -0.0027 0.0058  0.0068  132 PHE   A N   
2913 C  CA  A PHE   A 132 ? 0.1763 0.1518 0.1793 -0.0059 -0.0215 0.0173  132 PHE   A CA  
2914 C  CA  B PHE   A 132 ? 0.1909 0.1686 0.1676 -0.0029 -0.0028 -0.0032 132 PHE   A CA  
2915 C  C   A PHE   A 132 ? 0.1836 0.1630 0.1883 -0.0099 -0.0286 0.0217  132 PHE   A C   
2916 C  C   B PHE   A 132 ? 0.1962 0.1770 0.1882 -0.0026 -0.0169 0.0068  132 PHE   A C   
2917 O  O   A PHE   A 132 ? 0.1898 0.1661 0.1918 -0.0201 -0.0250 0.0227  132 PHE   A O   
2918 O  O   B PHE   A 132 ? 0.2041 0.1860 0.1888 -0.0116 -0.0210 0.0031  132 PHE   A O   
2919 C  CB  A PHE   A 132 ? 0.1707 0.1524 0.1724 -0.0031 -0.0164 0.0265  132 PHE   A CB  
2920 C  CB  B PHE   A 132 ? 0.1863 0.1681 0.1482 0.0021  -0.0028 -0.0188 132 PHE   A CB  
2921 C  CG  A PHE   A 132 ? 0.1689 0.1552 0.1678 0.0023  -0.0123 0.0255  132 PHE   A CG  
2922 C  CG  B PHE   A 132 ? 0.1828 0.1702 0.1359 0.0049  -0.0051 -0.0147 132 PHE   A CG  
2923 C  CD1 A PHE   A 132 ? 0.1630 0.1695 0.1772 0.0094  -0.0027 0.0133  132 PHE   A CD1 
2924 C  CD1 B PHE   A 132 ? 0.1833 0.1788 0.1377 0.0052  -0.0026 -0.0143 132 PHE   A CD1 
2925 C  CD2 A PHE   A 132 ? 0.1691 0.1639 0.1884 0.0156  -0.0250 0.0155  132 PHE   A CD2 
2926 C  CD2 B PHE   A 132 ? 0.1821 0.1764 0.1624 0.0099  -0.0081 -0.0242 132 PHE   A CD2 
2927 C  CE1 A PHE   A 132 ? 0.1678 0.1712 0.1779 0.0045  -0.0091 0.0090  132 PHE   A CE1 
2928 C  CE1 B PHE   A 132 ? 0.1852 0.1857 0.1503 0.0068  -0.0041 -0.0135 132 PHE   A CE1 
2929 C  CE2 A PHE   A 132 ? 0.1618 0.1744 0.1945 0.0162  -0.0262 0.0120  132 PHE   A CE2 
2930 C  CE2 B PHE   A 132 ? 0.1773 0.1852 0.1759 0.0166  -0.0019 -0.0222 132 PHE   A CE2 
2931 C  CZ  A PHE   A 132 ? 0.1601 0.1708 0.1857 0.0024  -0.0313 0.0106  132 PHE   A CZ  
2932 C  CZ  B PHE   A 132 ? 0.1792 0.1847 0.1587 0.0076  -0.0035 -0.0149 132 PHE   A CZ  
2951 N  N   A GLY   A 133 ? 0.1843 0.1733 0.1914 -0.0082 -0.0389 0.0225  133 GLY   A N   
2952 N  N   B GLY   A 133 ? 0.1929 0.1738 0.2001 0.0039  -0.0262 0.0186  133 GLY   A N   
2953 C  CA  A GLY   A 133 ? 0.1907 0.1858 0.1908 -0.0097 -0.0393 0.0159  133 GLY   A CA  
2954 C  CA  B GLY   A 133 ? 0.1933 0.1731 0.2022 0.0035  -0.0265 0.0104  133 GLY   A CA  
2955 C  C   A GLY   A 133 ? 0.1857 0.1947 0.1930 -0.0099 -0.0517 0.0153  133 GLY   A C   
2956 C  C   B GLY   A 133 ? 0.1917 0.1793 0.2031 0.0009  -0.0363 -0.0025 133 GLY   A C   
2957 O  O   A GLY   A 133 ? 0.1896 0.2070 0.2084 -0.0060 -0.0516 0.0021  133 GLY   A O   
2958 O  O   B GLY   A 133 ? 0.1926 0.1805 0.1961 0.0041  -0.0419 -0.0200 133 GLY   A O   
2965 N  N   A ALA   A 134 ? 0.1851 0.1838 0.1780 -0.0120 -0.0310 0.0151  134 ALA   A N   
2966 N  N   B ALA   A 134 ? 0.1886 0.1776 0.1992 -0.0017 -0.0260 -0.0057 134 ALA   A N   
2967 C  CA  A ALA   A 134 ? 0.1824 0.1850 0.1936 -0.0099 -0.0264 0.0132  134 ALA   A CA  
2968 C  CA  B ALA   A 134 ? 0.1859 0.1802 0.2034 -0.0007 -0.0298 0.0007  134 ALA   A CA  
2969 C  C   A ALA   A 134 ? 0.1799 0.1892 0.1991 -0.0081 -0.0296 0.0140  134 ALA   A C   
2970 C  C   B ALA   A 134 ? 0.1860 0.1804 0.2047 -0.0011 -0.0266 0.0122  134 ALA   A C   
2971 O  O   A ALA   A 134 ? 0.1902 0.1973 0.2332 -0.0038 -0.0053 0.0122  134 ALA   A O   
2972 O  O   B ALA   A 134 ? 0.1886 0.1855 0.2308 0.0012  -0.0050 0.0180  134 ALA   A O   
2973 C  CB  A ALA   A 134 ? 0.1871 0.1796 0.1992 -0.0077 -0.0262 0.0065  134 ALA   A CB  
2974 C  CB  B ALA   A 134 ? 0.1889 0.1819 0.2254 0.0001  -0.0312 -0.0043 134 ALA   A CB  
2985 N  N   A ASP   A 135 ? 0.1841 0.1939 0.2164 -0.0141 -0.0328 0.0250  135 ASP   A N   
2986 N  N   B ASP   A 135 ? 0.1938 0.1836 0.2116 -0.0078 -0.0299 0.0202  135 ASP   A N   
2987 C  CA  A ASP   A 135 ? 0.1847 0.2083 0.2397 -0.0226 -0.0449 0.0339  135 ASP   A CA  
2988 C  CA  B ASP   A 135 ? 0.1946 0.1932 0.2276 -0.0120 -0.0373 0.0245  135 ASP   A CA  
2989 C  C   A ASP   A 135 ? 0.1718 0.2056 0.2320 -0.0190 -0.0265 0.0477  135 ASP   A C   
2990 C  C   B ASP   A 135 ? 0.1858 0.1877 0.2219 -0.0054 -0.0277 0.0398  135 ASP   A C   
2991 O  O   A ASP   A 135 ? 0.1683 0.2000 0.2262 -0.0229 -0.0230 0.0536  135 ASP   A O   
2992 O  O   B ASP   A 135 ? 0.1836 0.1804 0.2254 -0.0060 -0.0251 0.0467  135 ASP   A O   
2993 C  CB  A ASP   A 135 ? 0.2055 0.2302 0.2725 -0.0358 -0.0614 0.0328  135 ASP   A CB  
2994 C  CB  B ASP   A 135 ? 0.2039 0.2110 0.2534 -0.0207 -0.0478 0.0169  135 ASP   A CB  
2995 C  CG  A ASP   A 135 ? 0.2257 0.2473 0.3161 -0.0490 -0.0575 0.0298  135 ASP   A CG  
2996 C  CG  B ASP   A 135 ? 0.2134 0.2283 0.2885 -0.0227 -0.0505 0.0168  135 ASP   A CG  
2997 O  OD1 A ASP   A 135 ? 0.2195 0.2535 0.3153 -0.0607 -0.0592 0.0556  135 ASP   A OD1 
2998 O  OD1 B ASP   A 135 ? 0.2145 0.2306 0.3135 -0.0156 -0.0446 0.0255  135 ASP   A OD1 
2999 O  OD2 A ASP   A 135 ? 0.2534 0.2623 0.3642 -0.0435 -0.0323 0.0161  135 ASP   A OD2 
3000 O  OD2 B ASP   A 135 ? 0.2193 0.2402 0.3134 -0.0309 -0.0558 0.0146  135 ASP   A OD2 
3009 N  N   A PRO   A 136 ? 0.1656 0.2078 0.2445 -0.0017 -0.0113 0.0567  136 PRO   A N   
3010 N  N   B PRO   A 136 ? 0.1826 0.1894 0.2316 0.0019  -0.0136 0.0455  136 PRO   A N   
3011 C  CA  A PRO   A 136 ? 0.1642 0.2073 0.2499 -0.0036 -0.0005 0.0370  136 PRO   A CA  
3012 C  CA  B PRO   A 136 ? 0.1812 0.1914 0.2352 0.0007  -0.0097 0.0335  136 PRO   A CA  
3013 C  C   A PRO   A 136 ? 0.1403 0.1940 0.2310 -0.0033 0.0053  0.0324  136 PRO   A C   
3014 C  C   B PRO   A 136 ? 0.1712 0.1893 0.2242 0.0001  -0.0150 0.0273  136 PRO   A C   
3015 O  O   A PRO   A 136 ? 0.1358 0.1884 0.2156 -0.0024 0.0180  0.0358  136 PRO   A O   
3016 O  O   B PRO   A 136 ? 0.1688 0.1890 0.2222 -0.0042 -0.0154 0.0309  136 PRO   A O   
3017 C  CB  A PRO   A 136 ? 0.1796 0.2143 0.2714 0.0012  -0.0006 0.0419  136 PRO   A CB  
3018 C  CB  B PRO   A 136 ? 0.1903 0.1930 0.2522 0.0041  -0.0033 0.0408  136 PRO   A CB  
3019 C  CG  A PRO   A 136 ? 0.1944 0.2257 0.2977 0.0092  -0.0018 0.0443  136 PRO   A CG  
3020 C  CG  B PRO   A 136 ? 0.1975 0.1997 0.2692 0.0082  -0.0031 0.0400  136 PRO   A CG  
3021 C  CD  A PRO   A 136 ? 0.1844 0.2204 0.2750 0.0067  0.0023  0.0593  136 PRO   A CD  
3022 C  CD  B PRO   A 136 ? 0.1922 0.1956 0.2534 0.0071  -0.0022 0.0472  136 PRO   A CD  
3037 N  N   A ILE   A 137 ? 0.1424 0.1927 0.2433 -0.0116 -0.0094 0.0298  137 ILE   A N   
3038 N  N   B ILE   A 137 ? 0.1746 0.1955 0.2302 -0.0024 -0.0183 0.0234  137 ILE   A N   
3039 C  CA  A ILE   A 137 ? 0.1424 0.2040 0.2458 -0.0214 -0.0147 0.0335  137 ILE   A CA  
3040 C  CA  B ILE   A 137 ? 0.1802 0.2083 0.2370 -0.0050 -0.0186 0.0229  137 ILE   A CA  
3041 C  C   A ILE   A 137 ? 0.1440 0.1966 0.2280 -0.0202 -0.0146 0.0363  137 ILE   A C   
3042 C  C   B ILE   A 137 ? 0.1793 0.2031 0.2311 -0.0063 -0.0156 0.0220  137 ILE   A C   
3043 O  O   A ILE   A 137 ? 0.1483 0.1919 0.2199 -0.0246 -0.0148 0.0274  137 ILE   A O   
3044 O  O   B ILE   A 137 ? 0.1841 0.2007 0.2406 -0.0042 -0.0126 0.0204  137 ILE   A O   
3045 C  CB  A ILE   A 137 ? 0.1543 0.2340 0.2804 -0.0246 -0.0321 0.0263  137 ILE   A CB  
3046 C  CB  B ILE   A 137 ? 0.1912 0.2308 0.2586 -0.0043 -0.0251 0.0198  137 ILE   A CB  
3047 C  CG1 A ILE   A 137 ? 0.1706 0.2650 0.3067 -0.0166 -0.0325 0.0331  137 ILE   A CG1 
3048 C  CG1 B ILE   A 137 ? 0.2015 0.2510 0.2757 0.0056  -0.0301 0.0270  137 ILE   A CG1 
3049 C  CG2 A ILE   A 137 ? 0.1626 0.2383 0.2944 -0.0321 -0.0498 0.0225  137 ILE   A CG2 
3050 C  CG2 B ILE   A 137 ? 0.1964 0.2351 0.2693 -0.0114 -0.0268 0.0160  137 ILE   A CG2 
3051 C  CD1 A ILE   A 137 ? 0.1882 0.2826 0.3227 -0.0076 -0.0259 0.0365  137 ILE   A CD1 
3052 C  CD1 B ILE   A 137 ? 0.2090 0.2598 0.2860 0.0123  -0.0282 0.0331  137 ILE   A CD1 
3075 N  N   A HIS   A 138 ? 0.1495 0.2079 0.2209 -0.0125 -0.0075 0.0347  138 HIS   A N   
3076 N  N   B HIS   A 138 ? 0.1758 0.2066 0.2223 -0.0079 -0.0121 0.0173  138 HIS   A N   
3077 C  CA  A HIS   A 138 ? 0.1586 0.2155 0.2164 -0.0088 -0.0083 0.0280  138 HIS   A CA  
3078 C  CA  B HIS   A 138 ? 0.1724 0.2064 0.2205 -0.0106 -0.0103 0.0158  138 HIS   A CA  
3079 C  C   A HIS   A 138 ? 0.1507 0.1961 0.2114 -0.0076 -0.0086 0.0270  138 HIS   A C   
3080 C  C   B HIS   A 138 ? 0.1585 0.1931 0.2108 -0.0069 -0.0096 0.0253  138 HIS   A C   
3081 O  O   A HIS   A 138 ? 0.1665 0.1960 0.2174 -0.0032 -0.0016 0.0210  138 HIS   A O   
3082 O  O   B HIS   A 138 ? 0.1685 0.1943 0.2117 -0.0035 -0.0027 0.0295  138 HIS   A O   
3083 C  CB  A HIS   A 138 ? 0.1802 0.2399 0.2146 -0.0089 -0.0235 0.0239  138 HIS   A CB  
3084 C  CB  B HIS   A 138 ? 0.1879 0.2212 0.2275 -0.0164 -0.0197 0.0045  138 HIS   A CB  
3085 C  CG  A HIS   A 138 ? 0.1956 0.2528 0.2229 -0.0149 -0.0133 0.0213  138 HIS   A CG  
3086 C  CG  B HIS   A 138 ? 0.1968 0.2308 0.2342 -0.0243 -0.0104 -0.0048 138 HIS   A CG  
3087 N  ND1 A HIS   A 138 ? 0.2072 0.2620 0.2342 -0.0157 -0.0058 0.0046  138 HIS   A ND1 
3088 N  ND1 B HIS   A 138 ? 0.2037 0.2387 0.2415 -0.0231 -0.0028 -0.0157 138 HIS   A ND1 
3089 C  CD2 A HIS   A 138 ? 0.1961 0.2589 0.2153 -0.0111 -0.0173 0.0272  138 HIS   A CD2 
3090 C  CD2 B HIS   A 138 ? 0.1983 0.2375 0.2374 -0.0221 -0.0139 -0.0040 138 HIS   A CD2 
3091 C  CE1 A HIS   A 138 ? 0.2122 0.2681 0.2393 -0.0069 -0.0039 0.0115  138 HIS   A CE1 
3092 C  CE1 B HIS   A 138 ? 0.2053 0.2419 0.2412 -0.0199 -0.0012 -0.0092 138 HIS   A CE1 
3093 N  NE2 A HIS   A 138 ? 0.2047 0.2679 0.2170 -0.0082 -0.0086 0.0195  138 HIS   A NE2 
3094 N  NE2 B HIS   A 138 ? 0.2031 0.2434 0.2381 -0.0202 -0.0104 -0.0079 138 HIS   A NE2 
3109 N  N   . SER   A 139 ? 0.1436 0.1831 0.1977 -0.0003 -0.0089 0.0284  139 SER   A N   
3110 C  CA  . SER   A 139 ? 0.1427 0.1776 0.2085 -0.0072 0.0075  0.0370  139 SER   A CA  
3111 C  C   . SER   A 139 ? 0.1374 0.1714 0.2191 -0.0103 0.0036  0.0267  139 SER   A C   
3112 O  O   . SER   A 139 ? 0.1324 0.1653 0.2240 -0.0127 -0.0026 0.0271  139 SER   A O   
3113 C  CB  . SER   A 139 ? 0.1370 0.1774 0.2051 -0.0082 -0.0008 0.0357  139 SER   A CB  
3114 O  OG  . SER   A 139 ? 0.1452 0.1775 0.2202 -0.0201 -0.0072 0.0424  139 SER   A OG  
3121 N  N   . LEU   A 140 ? 0.1392 0.1766 0.2017 -0.0063 0.0014  0.0374  140 LEU   A N   
3122 C  CA  . LEU   A 140 ? 0.1367 0.1665 0.2073 -0.0071 0.0007  0.0276  140 LEU   A CA  
3123 C  C   . LEU   A 140 ? 0.1315 0.1743 0.2098 -0.0148 0.0016  0.0334  140 LEU   A C   
3124 O  O   . LEU   A 140 ? 0.1403 0.1731 0.2164 -0.0081 0.0004  0.0364  140 LEU   A O   
3125 C  CB  . LEU   A 140 ? 0.1418 0.1699 0.2147 -0.0094 0.0067  0.0313  140 LEU   A CB  
3126 C  CG  . LEU   A 140 ? 0.1383 0.1913 0.2237 -0.0195 0.0068  0.0458  140 LEU   A CG  
3127 C  CD1 . LEU   A 140 ? 0.1404 0.1958 0.2502 -0.0122 0.0030  0.0380  140 LEU   A CD1 
3128 C  CD2 . LEU   A 140 ? 0.1426 0.2048 0.2309 -0.0131 0.0095  0.0500  140 LEU   A CD2 
3140 N  N   . ARG   A 141 ? 0.1413 0.1744 0.2147 -0.0095 -0.0051 0.0215  141 ARG   A N   
3141 C  CA  . ARG   A 141 ? 0.1593 0.1888 0.2411 -0.0195 -0.0112 0.0063  141 ARG   A CA  
3142 C  C   . ARG   A 141 ? 0.1502 0.1750 0.2247 -0.0128 -0.0106 0.0052  141 ARG   A C   
3143 O  O   . ARG   A 141 ? 0.1491 0.1760 0.2432 -0.0173 0.0061  0.0140  141 ARG   A O   
3144 C  CB  . ARG   A 141 ? 0.1732 0.2210 0.2693 -0.0207 -0.0159 -0.0160 141 ARG   A CB  
3145 C  CG  . ARG   A 141 ? 0.2163 0.2630 0.3135 -0.0294 -0.0001 -0.0254 141 ARG   A CG  
3146 C  CD  . ARG   A 141 ? 0.2580 0.3014 0.3633 -0.0458 -0.0030 -0.0259 141 ARG   A CD  
3147 N  NE  . ARG   A 141 ? 0.2532 0.3352 0.3719 -0.0540 -0.0132 -0.0210 141 ARG   A NE  
3148 C  CZ  . ARG   A 141 ? 0.2565 0.3582 0.3757 -0.0809 -0.0043 -0.0162 141 ARG   A CZ  
3149 N  NH1 . ARG   A 141 ? 0.2399 0.3584 0.3690 -0.0961 0.0238  -0.0436 141 ARG   A NH1 
3150 N  NH2 . ARG   A 141 ? 0.2688 0.3725 0.3847 -0.0784 -0.0202 -0.0041 141 ARG   A NH2 
3164 N  N   . VAL   A 142 ? 0.1402 0.1677 0.2158 -0.0120 -0.0011 -0.0012 142 VAL   A N   
3165 C  CA  . VAL   A 142 ? 0.1434 0.1649 0.2178 -0.0094 0.0166  0.0077  142 VAL   A CA  
3166 C  C   . VAL   A 142 ? 0.1331 0.1600 0.2039 -0.0146 0.0019  0.0054  142 VAL   A C   
3167 O  O   . VAL   A 142 ? 0.1370 0.1632 0.2125 0.0003  0.0007  0.0152  142 VAL   A O   
3168 C  CB  . VAL   A 142 ? 0.1485 0.1740 0.2129 -0.0068 0.0115  0.0135  142 VAL   A CB  
3169 C  CG1 . VAL   A 142 ? 0.1508 0.1612 0.2234 -0.0115 0.0101  0.0103  142 VAL   A CG1 
3170 C  CG2 . VAL   A 142 ? 0.1586 0.1922 0.2351 0.0037  0.0139  0.0108  142 VAL   A CG2 
3180 N  N   . CYS   A 143 ? 0.1403 0.1598 0.1949 -0.0164 0.0081  0.0143  143 CYS   A N   
3181 C  CA  . CYS   A 143 ? 0.1392 0.1622 0.2062 -0.0148 0.0121  0.0214  143 CYS   A CA  
3182 C  C   . CYS   A 143 ? 0.1350 0.1596 0.2184 -0.0149 0.0080  0.0245  143 CYS   A C   
3183 O  O   . CYS   A 143 ? 0.1333 0.1608 0.2239 -0.0077 0.0021  0.0244  143 CYS   A O   
3184 C  CB  . CYS   A 143 ? 0.1492 0.1643 0.2188 -0.0010 0.0191  0.0251  143 CYS   A CB  
3185 S  SG  . CYS   A 143 ? 0.1669 0.1699 0.2025 0.0020  0.0123  0.0195  143 CYS   A SG  
3191 N  N   . VAL   A 144 ? 0.1329 0.1596 0.2421 -0.0100 0.0090  0.0364  144 VAL   A N   
3192 C  CA  . VAL   A 144 ? 0.1445 0.1732 0.2748 -0.0101 0.0181  0.0422  144 VAL   A CA  
3193 C  C   . VAL   A 144 ? 0.1472 0.1583 0.2765 -0.0155 -0.0071 0.0251  144 VAL   A C   
3194 O  O   . VAL   A 144 ? 0.1664 0.1615 0.2735 -0.0046 -0.0058 0.0380  144 VAL   A O   
3195 C  CB  . VAL   A 144 ? 0.1730 0.1954 0.3349 0.0003  0.0481  0.0454  144 VAL   A CB  
3196 C  CG1 . VAL   A 144 ? 0.1868 0.2199 0.3703 -0.0083 0.0370  0.0325  144 VAL   A CG1 
3197 C  CG2 . VAL   A 144 ? 0.1575 0.1979 0.3403 -0.0038 0.0490  0.0645  144 VAL   A CG2 
3207 N  N   . ASP   A 145 ? 0.1530 0.1529 0.2853 -0.0131 0.0025  0.0191  145 ASP   A N   
3208 C  CA  . ASP   A 145 ? 0.1670 0.1602 0.2812 -0.0154 0.0005  0.0081  145 ASP   A CA  
3209 C  C   . ASP   A 145 ? 0.1639 0.1562 0.2813 -0.0084 0.0022  0.0063  145 ASP   A C   
3210 O  O   . ASP   A 145 ? 0.1810 0.1656 0.3422 -0.0113 -0.0064 -0.0242 145 ASP   A O   
3211 C  CB  . ASP   A 145 ? 0.1783 0.1918 0.3005 -0.0257 -0.0150 0.0012  145 ASP   A CB  
3212 C  CG  . ASP   A 145 ? 0.2048 0.2305 0.3263 -0.0441 -0.0276 0.0068  145 ASP   A CG  
3213 O  OD1 . ASP   A 145 ? 0.2045 0.2469 0.3418 -0.0583 -0.0201 0.0127  145 ASP   A OD1 
3214 O  OD2 . ASP   A 145 ? 0.2285 0.2538 0.3453 -0.0535 -0.0515 -0.0067 145 ASP   A OD2 
3219 N  N   . THR   A 146 ? 0.1500 0.1481 0.2419 -0.0137 0.0068  0.0133  146 THR   A N   
3220 C  CA  . THR   A 146 ? 0.1414 0.1490 0.2255 -0.0020 0.0025  0.0126  146 THR   A CA  
3221 C  C   . THR   A 146 ? 0.1382 0.1466 0.2340 -0.0001 0.0094  0.0198  146 THR   A C   
3222 O  O   . THR   A 146 ? 0.1487 0.1538 0.2497 0.0021  -0.0012 0.0161  146 THR   A O   
3223 C  CB  . THR   A 146 ? 0.1461 0.1507 0.2186 -0.0010 0.0028  0.0225  146 THR   A CB  
3224 O  OG1 . THR   A 146 ? 0.1454 0.1643 0.2212 0.0008  0.0008  0.0156  146 THR   A OG1 
3225 C  CG2 . THR   A 146 ? 0.1411 0.1495 0.2430 -0.0044 0.0011  0.0213  146 THR   A CG2 
3233 N  N   . VAL   A 147 ? 0.1384 0.1452 0.2234 -0.0052 0.0115  0.0144  147 VAL   A N   
3234 C  CA  . VAL   A 147 ? 0.1409 0.1501 0.2315 -0.0157 0.0251  0.0262  147 VAL   A CA  
3235 C  C   . VAL   A 147 ? 0.1411 0.1502 0.2386 -0.0095 0.0187  0.0272  147 VAL   A C   
3236 O  O   . VAL   A 147 ? 0.1435 0.1562 0.2578 -0.0151 0.0078  0.0399  147 VAL   A O   
3237 C  CB  . VAL   A 147 ? 0.1477 0.1489 0.2307 -0.0169 0.0220  0.0269  147 VAL   A CB  
3238 C  CG1 . VAL   A 147 ? 0.1822 0.1598 0.2271 -0.0094 0.0134  0.0357  147 VAL   A CG1 
3239 C  CG2 . VAL   A 147 ? 0.1536 0.1502 0.2448 -0.0106 0.0103  0.0329  147 VAL   A CG2 
3249 N  N   . ARG   A 148 ? 0.1420 0.1523 0.2342 -0.0129 0.0201  0.0455  148 ARG   A N   
3250 C  CA  . ARG   A 148 ? 0.1498 0.1551 0.2406 -0.0152 0.0140  0.0480  148 ARG   A CA  
3251 C  C   . ARG   A 148 ? 0.1605 0.1528 0.2395 -0.0171 0.0152  0.0584  148 ARG   A C   
3252 O  O   . ARG   A 148 ? 0.1918 0.1645 0.2568 -0.0223 0.0200  0.0562  148 ARG   A O   
3253 C  CB  . ARG   A 148 ? 0.1585 0.1563 0.2604 -0.0095 0.0220  0.0413  148 ARG   A CB  
3254 C  CG  . ARG   A 148 ? 0.1691 0.1587 0.3089 -0.0100 0.0437  0.0280  148 ARG   A CG  
3255 C  CD  . ARG   A 148 ? 0.1883 0.1555 0.3235 -0.0071 0.0528  0.0513  148 ARG   A CD  
3256 N  NE  . ARG   A 148 ? 0.1870 0.1598 0.3129 0.0091  0.0454  0.0606  148 ARG   A NE  
3257 C  CZ  . ARG   A 148 ? 0.1855 0.1494 0.2817 0.0049  0.0418  0.0581  148 ARG   A CZ  
3258 N  NH1 . ARG   A 148 ? 0.1919 0.1435 0.2897 -0.0093 0.0482  0.0301  148 ARG   A NH1 
3259 N  NH2 . ARG   A 148 ? 0.1759 0.1644 0.2850 0.0093  0.0382  0.0547  148 ARG   A NH2 
3273 N  N   . THR   A 149 ? 0.1616 0.1613 0.2342 -0.0166 0.0038  0.0599  149 THR   A N   
3274 C  CA  . THR   A 149 ? 0.1622 0.1686 0.2309 -0.0150 0.0064  0.0490  149 THR   A CA  
3275 C  C   . THR   A 149 ? 0.1588 0.1718 0.2054 -0.0234 0.0101  0.0554  149 THR   A C   
3276 O  O   . THR   A 149 ? 0.1605 0.1810 0.2253 -0.0278 0.0027  0.0581  149 THR   A O   
3277 C  CB  . THR   A 149 ? 0.1624 0.1770 0.2334 -0.0187 0.0041  0.0420  149 THR   A CB  
3278 O  OG1 . THR   A 149 ? 0.1681 0.1656 0.2353 -0.0210 0.0110  0.0451  149 THR   A OG1 
3279 C  CG2 . THR   A 149 ? 0.1554 0.1919 0.2354 -0.0145 -0.0039 0.0254  149 THR   A CG2 
3287 N  N   . ASN   A 150 ? 0.1610 0.1769 0.2151 -0.0149 0.0057  0.0615  150 ASN   A N   
3288 C  CA  . ASN   A 150 ? 0.1767 0.1822 0.2170 -0.0221 0.0045  0.0582  150 ASN   A CA  
3289 C  C   . ASN   A 150 ? 0.1584 0.1713 0.2149 -0.0212 0.0052  0.0504  150 ASN   A C   
3290 O  O   . ASN   A 150 ? 0.1624 0.1826 0.2539 -0.0215 -0.0067 0.0497  150 ASN   A O   
3291 C  CB  . ASN   A 150 ? 0.2193 0.2059 0.2508 -0.0290 0.0152  0.0748  150 ASN   A CB  
3292 C  CG  . ASN   A 150 ? 0.2753 0.2391 0.3072 -0.0322 0.0091  0.0807  150 ASN   A CG  
3293 O  OD1 . ASN   A 150 ? 0.2927 0.2422 0.3278 -0.0364 0.0150  0.0953  150 ASN   A OD1 
3294 N  ND2 . ASN   A 150 ? 0.3073 0.2631 0.3401 -0.0270 -0.0003 0.0849  150 ASN   A ND2 
3301 N  N   . VAL   A 151 ? 0.1599 0.1590 0.2059 -0.0187 0.0031  0.0408  151 VAL   A N   
3302 C  CA  . VAL   A 151 ? 0.1721 0.1627 0.2045 -0.0203 0.0096  0.0456  151 VAL   A CA  
3303 C  C   . VAL   A 151 ? 0.1560 0.1602 0.2163 -0.0259 0.0130  0.0459  151 VAL   A C   
3304 O  O   . VAL   A 151 ? 0.1641 0.1653 0.2572 -0.0250 0.0125  0.0426  151 VAL   A O   
3305 C  CB  . VAL   A 151 ? 0.2013 0.1853 0.2170 -0.0122 0.0123  0.0428  151 VAL   A CB  
3306 C  CG1 . VAL   A 151 ? 0.1964 0.2139 0.2462 -0.0197 0.0120  0.0321  151 VAL   A CG1 
3307 C  CG2 . VAL   A 151 ? 0.2183 0.1801 0.2044 -0.0094 0.0230  0.0409  151 VAL   A CG2 
3317 N  N   . TYR   A 152 ? 0.1535 0.1658 0.2139 -0.0264 0.0043  0.0406  152 TYR   A N   
3318 C  CA  . TYR   A 152 ? 0.1587 0.1780 0.1981 -0.0272 0.0117  0.0396  152 TYR   A CA  
3319 C  C   . TYR   A 152 ? 0.1515 0.1651 0.1839 -0.0237 0.0195  0.0423  152 TYR   A C   
3320 O  O   . TYR   A 152 ? 0.1605 0.1592 0.1993 -0.0268 0.0209  0.0367  152 TYR   A O   
3321 C  CB  . TYR   A 152 ? 0.1779 0.1959 0.2032 -0.0276 0.0249  0.0557  152 TYR   A CB  
3322 C  CG  . TYR   A 152 ? 0.1856 0.2194 0.1980 -0.0268 0.0230  0.0611  152 TYR   A CG  
3323 C  CD1 . TYR   A 152 ? 0.2050 0.2465 0.2195 -0.0092 0.0256  0.0672  152 TYR   A CD1 
3324 C  CD2 . TYR   A 152 ? 0.1953 0.2283 0.1955 -0.0359 0.0147  0.0566  152 TYR   A CD2 
3325 C  CE1 . TYR   A 152 ? 0.2421 0.2577 0.2350 -0.0047 0.0186  0.0750  152 TYR   A CE1 
3326 C  CE2 . TYR   A 152 ? 0.2287 0.2467 0.2107 -0.0348 0.0178  0.0619  152 TYR   A CE2 
3327 C  CZ  . TYR   A 152 ? 0.2621 0.2494 0.2276 -0.0242 0.0173  0.0916  152 TYR   A CZ  
3328 O  OH  . TYR   A 152 ? 0.3060 0.2726 0.2813 -0.0201 0.0233  0.1139  152 TYR   A OH  
3338 N  N   . LEU   A 153 ? 0.1537 0.1665 0.1878 -0.0248 0.0195  0.0411  153 LEU   A N   
3339 C  CA  . LEU   A 153 ? 0.1461 0.1647 0.1981 -0.0213 0.0177  0.0368  153 LEU   A CA  
3340 C  C   . LEU   A 153 ? 0.1473 0.1704 0.2171 -0.0109 0.0264  0.0375  153 LEU   A C   
3341 O  O   . LEU   A 153 ? 0.1627 0.1766 0.2439 -0.0138 0.0439  0.0315  153 LEU   A O   
3342 C  CB  . LEU   A 153 ? 0.1436 0.1636 0.2080 -0.0140 0.0088  0.0327  153 LEU   A CB  
3343 C  CG  . LEU   A 153 ? 0.1485 0.1674 0.2081 -0.0158 0.0115  0.0339  153 LEU   A CG  
3344 C  CD1 . LEU   A 153 ? 0.1577 0.1710 0.2039 -0.0166 0.0053  0.0301  153 LEU   A CD1 
3345 C  CD2 . LEU   A 153 ? 0.1583 0.1709 0.2201 -0.0136 0.0176  0.0107  153 LEU   A CD2 
3357 N  N   A ALA   A 154 ? 0.1396 0.1651 0.2264 -0.0049 0.0268  0.0398  154 ALA   A N   
3358 N  N   B ALA   A 154 ? 0.1451 0.1686 0.2216 -0.0164 0.0287  0.0370  154 ALA   A N   
3359 C  CA  A ALA   A 154 ? 0.1512 0.1672 0.2353 -0.0013 0.0207  0.0332  154 ALA   A CA  
3360 C  CA  B ALA   A 154 ? 0.1554 0.1720 0.2221 -0.0179 0.0249  0.0297  154 ALA   A CA  
3361 C  C   A ALA   A 154 ? 0.1490 0.1681 0.2453 0.0053  0.0240  0.0439  154 ALA   A C   
3362 C  C   B ALA   A 154 ? 0.1586 0.1737 0.2257 -0.0139 0.0247  0.0375  154 ALA   A C   
3363 O  O   A ALA   A 154 ? 0.1590 0.1808 0.2566 0.0011  0.0249  0.0465  154 ALA   A O   
3364 O  O   B ALA   A 154 ? 0.1642 0.1796 0.2337 -0.0147 0.0228  0.0404  154 ALA   A O   
3365 C  CB  A ALA   A 154 ? 0.1601 0.1716 0.2402 0.0033  0.0179  0.0116  154 ALA   A CB  
3366 C  CB  B ALA   A 154 ? 0.1601 0.1757 0.2245 -0.0179 0.0281  0.0188  154 ALA   A CB  
3377 N  N   A VAL   A 155 ? 0.1539 0.1660 0.2543 0.0146  0.0185  0.0494  155 VAL   A N   
3378 N  N   B VAL   A 155 ? 0.1649 0.1729 0.2292 -0.0094 0.0266  0.0402  155 VAL   A N   
3379 C  CA  A VAL   A 155 ? 0.1635 0.1765 0.2561 0.0092  0.0204  0.0490  155 VAL   A CA  
3380 C  CA  B VAL   A 155 ? 0.1743 0.1811 0.2408 -0.0066 0.0251  0.0312  155 VAL   A CA  
3381 C  C   A VAL   A 155 ? 0.1713 0.1827 0.2644 0.0196  0.0161  0.0537  155 VAL   A C   
3382 C  C   B VAL   A 155 ? 0.1864 0.1938 0.2473 -0.0019 0.0295  0.0344  155 VAL   A C   
3383 O  O   A VAL   A 155 ? 0.1676 0.1948 0.2649 0.0288  0.0171  0.0372  155 VAL   A O   
3384 O  O   B VAL   A 155 ? 0.1816 0.1972 0.2457 0.0022  0.0392  0.0322  155 VAL   A O   
3385 C  CB  A VAL   A 155 ? 0.1693 0.1839 0.2441 0.0110  0.0218  0.0340  155 VAL   A CB  
3386 C  CB  B VAL   A 155 ? 0.1731 0.1795 0.2396 -0.0003 0.0199  0.0233  155 VAL   A CB  
3387 C  CG1 A VAL   A 155 ? 0.1872 0.1942 0.2417 0.0162  0.0271  0.0268  155 VAL   A CG1 
3388 C  CG1 B VAL   A 155 ? 0.1770 0.1835 0.2385 0.0096  0.0203  0.0200  155 VAL   A CG1 
3389 C  CG2 A VAL   A 155 ? 0.1793 0.1870 0.2472 0.0180  0.0071  0.0381  155 VAL   A CG2 
3390 C  CG2 B VAL   A 155 ? 0.1761 0.1797 0.2468 0.0052  0.0179  0.0228  155 VAL   A CG2 
3409 N  N   A PHE   A 156 ? 0.1784 0.1765 0.2777 0.0261  0.0310  0.0661  156 PHE   A N   
3410 N  N   B PHE   A 156 ? 0.2034 0.2062 0.2785 0.0009  0.0268  0.0353  156 PHE   A N   
3411 C  CA  A PHE   A 156 ? 0.1995 0.1712 0.2940 0.0317  0.0249  0.0658  156 PHE   A CA  
3412 C  CA  B PHE   A 156 ? 0.2240 0.2204 0.2913 0.0033  0.0162  0.0302  156 PHE   A CA  
3413 C  C   A PHE   A 156 ? 0.2030 0.1760 0.3004 0.0338  0.0239  0.0694  156 PHE   A C   
3414 C  C   B PHE   A 156 ? 0.2396 0.2333 0.3026 0.0069  0.0130  0.0295  156 PHE   A C   
3415 O  O   A PHE   A 156 ? 0.1934 0.1874 0.3112 0.0343  0.0339  0.0496  156 PHE   A O   
3416 O  O   B PHE   A 156 ? 0.2519 0.2462 0.3185 0.0091  0.0086  0.0279  156 PHE   A O   
3417 C  CB  A PHE   A 156 ? 0.2230 0.1756 0.2954 0.0315  0.0043  0.0776  156 PHE   A CB  
3418 C  CB  B PHE   A 156 ? 0.2319 0.2266 0.3008 -0.0005 0.0133  0.0255  156 PHE   A CB  
3419 C  CG  A PHE   A 156 ? 0.2541 0.1842 0.3120 0.0372  -0.0078 0.0708  156 PHE   A CG  
3420 C  CG  B PHE   A 156 ? 0.2373 0.2325 0.3099 -0.0042 0.0070  0.0106  156 PHE   A CG  
3421 C  CD1 A PHE   A 156 ? 0.2766 0.1941 0.3353 0.0364  -0.0128 0.0647  156 PHE   A CD1 
3422 C  CD1 B PHE   A 156 ? 0.2385 0.2347 0.3122 -0.0099 0.0055  0.0083  156 PHE   A CD1 
3423 C  CD2 A PHE   A 156 ? 0.2674 0.1920 0.3254 0.0483  -0.0126 0.0750  156 PHE   A CD2 
3424 C  CD2 B PHE   A 156 ? 0.2404 0.2349 0.3147 -0.0075 -0.0001 0.0064  156 PHE   A CD2 
3425 C  CE1 A PHE   A 156 ? 0.2909 0.1972 0.3532 0.0362  -0.0108 0.0649  156 PHE   A CE1 
3426 C  CE1 B PHE   A 156 ? 0.2399 0.2390 0.3210 -0.0117 -0.0022 0.0064  156 PHE   A CE1 
3427 C  CE2 A PHE   A 156 ? 0.2844 0.2003 0.3389 0.0537  -0.0128 0.0675  156 PHE   A CE2 
3428 C  CE2 B PHE   A 156 ? 0.2410 0.2350 0.3160 -0.0087 -0.0052 0.0035  156 PHE   A CE2 
3429 C  CZ  A PHE   A 156 ? 0.2936 0.2027 0.3511 0.0505  -0.0146 0.0593  156 PHE   A CZ  
3430 C  CZ  B PHE   A 156 ? 0.2402 0.2386 0.3221 -0.0075 -0.0098 0.0024  156 PHE   A CZ  
3449 N  N   A ASP   A 157 ? 0.2177 0.1804 0.3020 0.0313  0.0114  0.0944  157 ASP   A N   
3450 N  N   B ASP   A 157 ? 0.2410 0.2330 0.3037 0.0070  0.0081  0.0402  157 ASP   A N   
3451 C  CA  A ASP   A 157 ? 0.2403 0.2013 0.3282 0.0322  -0.0025 0.0916  157 ASP   A CA  
3452 C  CA  B ASP   A 157 ? 0.2416 0.2393 0.3000 0.0047  -0.0005 0.0447  157 ASP   A CA  
3453 C  C   A ASP   A 157 ? 0.2133 0.2165 0.3333 0.0447  0.0045  0.0958  157 ASP   A C   
3454 C  C   B ASP   A 157 ? 0.2394 0.2380 0.3010 -0.0007 -0.0117 0.0408  157 ASP   A C   
3455 O  O   A ASP   A 157 ? 0.2000 0.2135 0.3261 0.0450  0.0082  0.0943  157 ASP   A O   
3456 O  O   B ASP   A 157 ? 0.2357 0.2327 0.3053 -0.0018 -0.0159 0.0414  157 ASP   A O   
3457 C  CB  A ASP   A 157 ? 0.2767 0.2143 0.3551 0.0365  -0.0265 0.0870  157 ASP   A CB  
3458 C  CB  B ASP   A 157 ? 0.2349 0.2464 0.2991 0.0110  0.0066  0.0569  157 ASP   A CB  
3459 C  CG  A ASP   A 157 ? 0.3080 0.2287 0.3932 0.0431  -0.0493 0.0819  157 ASP   A CG  
3460 C  CG  B ASP   A 157 ? 0.2249 0.2555 0.3171 0.0222  0.0071  0.0604  157 ASP   A CG  
3461 O  OD1 A ASP   A 157 ? 0.3330 0.2373 0.4175 0.0469  -0.0704 0.0600  157 ASP   A OD1 
3462 O  OD1 B ASP   A 157 ? 0.2191 0.2541 0.3262 0.0273  0.0064  0.0714  157 ASP   A OD1 
3463 O  OD2 A ASP   A 157 ? 0.3003 0.2282 0.3972 0.0397  -0.0503 0.1034  157 ASP   A OD2 
3464 O  OD2 B ASP   A 157 ? 0.2076 0.2606 0.3110 0.0223  0.0118  0.0551  157 ASP   A OD2 
3473 N  N   A LYS   A 158 ? 0.2197 0.2421 0.3505 0.0512  0.0083  0.0858  158 LYS   A N   
3474 N  N   B LYS   A 158 ? 0.2411 0.2473 0.3007 -0.0053 -0.0191 0.0347  158 LYS   A N   
3475 C  CA  A LYS   A 158 ? 0.2201 0.2666 0.3522 0.0615  0.0184  0.0724  158 LYS   A CA  
3476 C  CA  B LYS   A 158 ? 0.2464 0.2594 0.3019 -0.0064 -0.0152 0.0248  158 LYS   A CA  
3477 C  C   A LYS   A 158 ? 0.2089 0.2696 0.3440 0.0601  0.0145  0.0801  158 LYS   A C   
3478 C  C   B LYS   A 158 ? 0.2314 0.2580 0.2853 -0.0110 -0.0139 0.0332  158 LYS   A C   
3479 O  O   A LYS   A 158 ? 0.2081 0.2697 0.3397 0.0566  0.0255  0.0874  158 LYS   A O   
3480 O  O   B LYS   A 158 ? 0.2261 0.2576 0.2806 -0.0186 -0.0087 0.0343  158 LYS   A O   
3481 C  CB  A LYS   A 158 ? 0.2391 0.2878 0.3665 0.0632  0.0452  0.0516  158 LYS   A CB  
3482 C  CB  B LYS   A 158 ? 0.2649 0.2793 0.3191 -0.0015 -0.0195 0.0089  158 LYS   A CB  
3483 C  CG  A LYS   A 158 ? 0.2562 0.3066 0.3784 0.0597  0.0644  0.0472  158 LYS   A CG  
3484 C  CG  B LYS   A 158 ? 0.2825 0.2987 0.3470 0.0033  -0.0246 -0.0016 158 LYS   A CG  
3485 C  CD  A LYS   A 158 ? 0.2652 0.3195 0.3876 0.0552  0.0941  0.0534  158 LYS   A CD  
3486 C  CD  B LYS   A 158 ? 0.2970 0.3132 0.3719 0.0083  -0.0310 -0.0099 158 LYS   A CD  
3487 C  CE  A LYS   A 158 ? 0.2684 0.3217 0.3802 0.0513  0.1171  0.0685  158 LYS   A CE  
3488 C  CE  B LYS   A 158 ? 0.3053 0.3234 0.3921 0.0096  -0.0362 -0.0137 158 LYS   A CE  
3489 N  NZ  A LYS   A 158 ? 0.2690 0.3210 0.3795 0.0458  0.1246  0.0811  158 LYS   A NZ  
3490 N  NZ  B LYS   A 158 ? 0.3096 0.3264 0.4062 0.0113  -0.0404 -0.0152 158 LYS   A NZ  
3517 N  N   A ASN   A 159 ? 0.1971 0.2679 0.3597 0.0566  0.0025  0.0749  159 ASN   A N   
3518 N  N   B ASN   A 159 ? 0.2272 0.2606 0.2911 -0.0048 -0.0125 0.0358  159 ASN   A N   
3519 C  CA  A ASN   A 159 ? 0.1928 0.2712 0.3625 0.0486  -0.0127 0.0892  159 ASN   A CA  
3520 C  CA  B ASN   A 159 ? 0.2213 0.2620 0.2980 -0.0027 -0.0134 0.0404  159 ASN   A CA  
3521 C  C   A ASN   A 159 ? 0.1766 0.2742 0.3362 0.0325  -0.0035 0.0703  159 ASN   A C   
3522 C  C   B ASN   A 159 ? 0.1999 0.2494 0.2599 -0.0123 -0.0218 0.0332  159 ASN   A C   
3523 O  O   A ASN   A 159 ? 0.1654 0.2718 0.3141 0.0321  -0.0098 0.0491  159 ASN   A O   
3524 O  O   B ASN   A 159 ? 0.1985 0.2553 0.2487 -0.0156 -0.0312 0.0315  159 ASN   A O   
3525 C  CB  A ASN   A 159 ? 0.2130 0.2757 0.4100 0.0480  -0.0186 0.1088  159 ASN   A CB  
3526 C  CB  B ASN   A 159 ? 0.2414 0.2830 0.3622 0.0045  -0.0053 0.0451  159 ASN   A CB  
3527 C  CG  A ASN   A 159 ? 0.2410 0.2895 0.4793 0.0432  -0.0141 0.1035  159 ASN   A CG  
3528 C  CG  B ASN   A 159 ? 0.2634 0.3075 0.4250 0.0051  0.0103  0.0452  159 ASN   A CG  
3529 O  OD1 A ASN   A 159 ? 0.2522 0.3067 0.5151 0.0375  -0.0010 0.0966  159 ASN   A OD1 
3530 O  OD1 B ASN   A 159 ? 0.2719 0.3165 0.4503 0.0040  0.0157  0.0458  159 ASN   A OD1 
3531 N  ND2 A ASN   A 159 ? 0.2497 0.2951 0.5105 0.0416  -0.0168 0.0936  159 ASN   A ND2 
3532 N  ND2 B ASN   A 159 ? 0.2726 0.3155 0.4501 0.0055  0.0119  0.0395  159 ASN   A ND2 
3545 N  N   A LEU   A 160 ? 0.1673 0.2696 0.3191 0.0236  -0.0079 0.0806  160 LEU   A N   
3546 N  N   B LEU   A 160 ? 0.1865 0.2334 0.2485 -0.0186 -0.0270 0.0389  160 LEU   A N   
3547 C  CA  A LEU   A 160 ? 0.1687 0.2662 0.2973 0.0133  0.0085  0.0874  160 LEU   A CA  
3548 C  CA  B LEU   A 160 ? 0.1825 0.2261 0.2285 -0.0174 -0.0189 0.0434  160 LEU   A CA  
3549 C  C   A LEU   A 160 ? 0.1581 0.2669 0.2819 0.0111  0.0204  0.0777  160 LEU   A C   
3550 C  C   B LEU   A 160 ? 0.1769 0.2194 0.2264 -0.0095 -0.0167 0.0390  160 LEU   A C   
3551 O  O   A LEU   A 160 ? 0.1560 0.2773 0.2916 0.0069  0.0176  0.0723  160 LEU   A O   
3552 O  O   B LEU   A 160 ? 0.1763 0.2122 0.2438 -0.0127 -0.0191 0.0253  160 LEU   A O   
3553 C  CB  A LEU   A 160 ? 0.1768 0.2683 0.2888 0.0058  0.0146  0.0917  160 LEU   A CB  
3554 C  CB  B LEU   A 160 ? 0.1872 0.2275 0.2253 -0.0210 -0.0106 0.0445  160 LEU   A CB  
3555 C  CG  A LEU   A 160 ? 0.1895 0.2752 0.2933 -0.0051 0.0137  0.0802  160 LEU   A CG  
3556 C  CG  B LEU   A 160 ? 0.2019 0.2379 0.2426 -0.0239 -0.0062 0.0370  160 LEU   A CG  
3557 C  CD1 A LEU   A 160 ? 0.1995 0.2847 0.3032 -0.0110 0.0133  0.0654  160 LEU   A CD1 
3558 C  CD1 B LEU   A 160 ? 0.2145 0.2482 0.2559 -0.0249 -0.0022 0.0380  160 LEU   A CD1 
3559 C  CD2 A LEU   A 160 ? 0.1928 0.2665 0.2752 -0.0064 0.0191  0.0873  160 LEU   A CD2 
3560 C  CD2 B LEU   A 160 ? 0.2028 0.2356 0.2410 -0.0207 -0.0079 0.0343  160 LEU   A CD2 
3583 N  N   A TYR   A 161 ? 0.1588 0.2558 0.2763 0.0140  0.0278  0.0724  161 TYR   A N   
3584 N  N   B TYR   A 161 ? 0.1795 0.2271 0.2127 -0.0029 -0.0028 0.0523  161 TYR   A N   
3585 C  CA  A TYR   A 161 ? 0.1549 0.2506 0.2723 0.0169  0.0367  0.0576  161 TYR   A CA  
3586 C  CA  B TYR   A 161 ? 0.1813 0.2349 0.2179 -0.0013 0.0071  0.0578  161 TYR   A CA  
3587 C  C   A TYR   A 161 ? 0.1467 0.2661 0.2943 0.0093  0.0280  0.0606  161 TYR   A C   
3588 C  C   B TYR   A 161 ? 0.1774 0.2438 0.2313 -0.0029 -0.0022 0.0534  161 TYR   A C   
3589 O  O   A TYR   A 161 ? 0.1430 0.2634 0.2793 -0.0038 0.0313  0.0558  161 TYR   A O   
3590 O  O   B TYR   A 161 ? 0.1697 0.2380 0.2115 -0.0117 -0.0126 0.0567  161 TYR   A O   
3591 C  CB  A TYR   A 161 ? 0.1692 0.2425 0.2825 0.0134  0.0317  0.0481  161 TYR   A CB  
3592 C  CB  B TYR   A 161 ? 0.1850 0.2347 0.2216 0.0044  0.0164  0.0632  161 TYR   A CB  
3593 C  CG  A TYR   A 161 ? 0.1711 0.2324 0.2866 0.0156  0.0230  0.0408  161 TYR   A CG  
3594 C  CG  B TYR   A 161 ? 0.1879 0.2370 0.2448 0.0082  0.0188  0.0586  161 TYR   A CG  
3595 C  CD1 A TYR   A 161 ? 0.1672 0.2186 0.2874 0.0038  0.0166  0.0330  161 TYR   A CD1 
3596 C  CD1 B TYR   A 161 ? 0.1872 0.2350 0.2577 0.0049  0.0145  0.0544  161 TYR   A CD1 
3597 C  CD2 A TYR   A 161 ? 0.1745 0.2326 0.2918 0.0227  0.0146  0.0440  161 TYR   A CD2 
3598 C  CD2 B TYR   A 161 ? 0.1921 0.2410 0.2591 0.0116  0.0222  0.0616  161 TYR   A CD2 
3599 C  CE1 A TYR   A 161 ? 0.1761 0.2152 0.2970 0.0010  0.0131  0.0431  161 TYR   A CE1 
3600 C  CE1 B TYR   A 161 ? 0.1931 0.2387 0.2665 0.0069  0.0159  0.0597  161 TYR   A CE1 
3601 C  CE2 A TYR   A 161 ? 0.1806 0.2212 0.2925 0.0161  0.0099  0.0522  161 TYR   A CE2 
3602 C  CE2 B TYR   A 161 ? 0.1971 0.2407 0.2668 0.0074  0.0199  0.0664  161 TYR   A CE2 
3603 C  CZ  A TYR   A 161 ? 0.1864 0.2090 0.2970 0.0044  0.0047  0.0551  161 TYR   A CZ  
3604 C  CZ  B TYR   A 161 ? 0.2034 0.2401 0.2753 0.0047  0.0169  0.0660  161 TYR   A CZ  
3605 O  OH  A TYR   A 161 ? 0.1937 0.1945 0.3081 0.0030  -0.0114 0.0631  161 TYR   A OH  
3606 O  OH  B TYR   A 161 ? 0.2152 0.2425 0.2994 0.0018  0.0151  0.0707  161 TYR   A OH  
3625 N  N   A ASP   A 162 ? 0.1407 0.2866 0.3230 0.0117  0.0357  0.0767  162 ASP   A N   
3626 N  N   B ASP   A 162 ? 0.1822 0.2587 0.2670 -0.0022 0.0066  0.0562  162 ASP   A N   
3627 C  CA  A ASP   A 162 ? 0.1378 0.3146 0.3318 0.0082  0.0372  0.0769  162 ASP   A CA  
3628 C  CA  B ASP   A 162 ? 0.1921 0.2835 0.2936 -0.0092 0.0117  0.0534  162 ASP   A CA  
3629 C  C   A ASP   A 162 ? 0.1192 0.3245 0.3296 -0.0000 0.0279  0.0806  162 ASP   A C   
3630 C  C   B ASP   A 162 ? 0.1984 0.2946 0.2943 -0.0164 0.0084  0.0606  162 ASP   A C   
3631 O  O   A ASP   A 162 ? 0.1232 0.3277 0.3554 -0.0069 0.0284  0.0726  162 ASP   A O   
3632 O  O   B ASP   A 162 ? 0.1995 0.2947 0.3080 -0.0205 0.0040  0.0642  162 ASP   A O   
3633 C  CB  A ASP   A 162 ? 0.1561 0.3337 0.3454 0.0188  0.0491  0.0702  162 ASP   A CB  
3634 C  CB  B ASP   A 162 ? 0.1986 0.2991 0.3218 -0.0037 0.0181  0.0421  162 ASP   A CB  
3635 C  CG  A ASP   A 162 ? 0.1724 0.3515 0.3650 0.0265  0.0569  0.0653  162 ASP   A CG  
3636 C  CG  B ASP   A 162 ? 0.2046 0.3143 0.3480 -0.0001 0.0236  0.0350  162 ASP   A CG  
3637 O  OD1 A ASP   A 162 ? 0.1801 0.3647 0.3801 0.0238  0.0521  0.0578  162 ASP   A OD1 
3638 O  OD1 B ASP   A 162 ? 0.2034 0.3189 0.3523 -0.0014 0.0230  0.0318  162 ASP   A OD1 
3639 O  OD2 A ASP   A 162 ? 0.1765 0.3522 0.3689 0.0315  0.0731  0.0634  162 ASP   A OD2 
3640 O  OD2 B ASP   A 162 ? 0.2071 0.3213 0.3653 0.0001  0.0357  0.0302  162 ASP   A OD2 
3649 N  N   A LYS   A 163 ? 0.1311 0.3348 0.3323 0.0048  -0.0022 0.0769  163 LYS   A N   
3650 N  N   B LYS   A 163 ? 0.2109 0.3056 0.2995 -0.0202 -0.0001 0.0551  163 LYS   A N   
3651 C  CA  A LYS   A 163 ? 0.1473 0.3452 0.3269 -0.0013 -0.0089 0.0691  163 LYS   A CA  
3652 C  CA  B LYS   A 163 ? 0.2259 0.3166 0.3077 -0.0239 -0.0012 0.0469  163 LYS   A CA  
3653 C  C   A LYS   A 163 ? 0.1419 0.3333 0.3175 -0.0096 0.0154  0.0644  163 LYS   A C   
3654 C  C   B LYS   A 163 ? 0.2131 0.3037 0.2863 -0.0298 0.0047  0.0429  163 LYS   A C   
3655 O  O   A LYS   A 163 ? 0.1382 0.3484 0.3318 -0.0138 0.0165  0.0574  163 LYS   A O   
3656 O  O   B LYS   A 163 ? 0.2179 0.3131 0.2959 -0.0270 -0.0003 0.0378  163 LYS   A O   
3657 C  CB  A LYS   A 163 ? 0.1888 0.3675 0.3596 0.0099  -0.0289 0.0665  163 LYS   A CB  
3658 C  CB  B LYS   A 163 ? 0.2580 0.3387 0.3465 -0.0199 -0.0085 0.0423  163 LYS   A CB  
3659 C  CG  A LYS   A 163 ? 0.2363 0.3867 0.4047 0.0145  -0.0298 0.0665  163 LYS   A CG  
3660 C  CG  B LYS   A 163 ? 0.2871 0.3577 0.3919 -0.0185 -0.0076 0.0406  163 LYS   A CG  
3661 C  CD  A LYS   A 163 ? 0.2905 0.4010 0.4561 0.0177  -0.0314 0.0641  163 LYS   A CD  
3662 C  CD  B LYS   A 163 ? 0.3153 0.3723 0.4424 -0.0183 -0.0077 0.0381  163 LYS   A CD  
3663 C  CE  A LYS   A 163 ? 0.3389 0.4109 0.4972 0.0188  -0.0252 0.0619  163 LYS   A CE  
3664 C  CE  B LYS   A 163 ? 0.3411 0.3823 0.4766 -0.0181 -0.0058 0.0371  163 LYS   A CE  
3665 N  NZ  A LYS   A 163 ? 0.3584 0.4162 0.5238 0.0178  -0.0199 0.0616  163 LYS   A NZ  
3666 N  NZ  B LYS   A 163 ? 0.3494 0.3873 0.5015 -0.0186 -0.0060 0.0361  163 LYS   A NZ  
3693 N  N   A LEU   A 164 ? 0.1339 0.3036 0.2955 -0.0189 0.0172  0.0615  164 LEU   A N   
3694 N  N   B LEU   A 164 ? 0.1950 0.2804 0.2616 -0.0365 0.0072  0.0430  164 LEU   A N   
3695 C  CA  A LEU   A 164 ? 0.1433 0.2797 0.2748 -0.0232 0.0293  0.0587  164 LEU   A CA  
3696 C  CA  B LEU   A 164 ? 0.1881 0.2629 0.2514 -0.0362 0.0199  0.0459  164 LEU   A CA  
3697 C  C   A LEU   A 164 ? 0.1540 0.2748 0.2854 -0.0233 0.0347  0.0472  164 LEU   A C   
3698 C  C   B LEU   A 164 ? 0.1894 0.2645 0.2533 -0.0289 0.0260  0.0447  164 LEU   A C   
3699 O  O   A LEU   A 164 ? 0.1634 0.2827 0.2921 -0.0258 0.0520  0.0355  164 LEU   A O   
3700 O  O   B LEU   A 164 ? 0.1935 0.2687 0.2558 -0.0295 0.0387  0.0387  164 LEU   A O   
3701 C  CB  A LEU   A 164 ? 0.1509 0.2692 0.2550 -0.0197 0.0304  0.0600  164 LEU   A CB  
3702 C  CB  B LEU   A 164 ? 0.1834 0.2497 0.2398 -0.0386 0.0193  0.0484  164 LEU   A CB  
3703 C  CG  A LEU   A 164 ? 0.1607 0.2644 0.2433 -0.0125 0.0273  0.0571  164 LEU   A CG  
3704 C  CG  B LEU   A 164 ? 0.1803 0.2403 0.2239 -0.0377 0.0122  0.0487  164 LEU   A CG  
3705 C  CD1 A LEU   A 164 ? 0.1587 0.2626 0.2352 -0.0064 0.0227  0.0535  164 LEU   A CD1 
3706 C  CD1 B LEU   A 164 ? 0.1746 0.2359 0.2108 -0.0352 -0.0011 0.0567  164 LEU   A CD1 
3707 C  CD2 A LEU   A 164 ? 0.1728 0.2668 0.2385 -0.0136 0.0293  0.0459  164 LEU   A CD2 
3708 C  CD2 B LEU   A 164 ? 0.1900 0.2419 0.2385 -0.0347 0.0110  0.0327  164 LEU   A CD2 
3731 N  N   A VAL   A 165 ? 0.1452 0.2630 0.2793 -0.0182 0.0266  0.0511  165 VAL   A N   
3732 N  N   B VAL   A 165 ? 0.1835 0.2629 0.2440 -0.0182 0.0233  0.0539  165 VAL   A N   
3733 C  CA  A VAL   A 165 ? 0.1569 0.2616 0.2656 -0.0250 0.0302  0.0610  165 VAL   A CA  
3734 C  CA  B VAL   A 165 ? 0.1882 0.2665 0.2327 -0.0138 0.0226  0.0635  165 VAL   A CA  
3735 C  C   A VAL   A 165 ? 0.1482 0.2808 0.2754 -0.0265 0.0283  0.0609  165 VAL   A C   
3736 C  C   B VAL   A 165 ? 0.1831 0.2798 0.2381 -0.0146 0.0219  0.0576  165 VAL   A C   
3737 O  O   A VAL   A 165 ? 0.1463 0.2869 0.2780 -0.0299 0.0354  0.0588  165 VAL   A O   
3738 O  O   B VAL   A 165 ? 0.1830 0.2840 0.2419 -0.0123 0.0226  0.0530  165 VAL   A O   
3739 C  CB  A VAL   A 165 ? 0.1758 0.2517 0.2691 -0.0237 0.0324  0.0529  165 VAL   A CB  
3740 C  CB  B VAL   A 165 ? 0.1977 0.2635 0.2364 -0.0071 0.0202  0.0652  165 VAL   A CB  
3741 C  CG1 A VAL   A 165 ? 0.1836 0.2542 0.2718 -0.0286 0.0407  0.0510  165 VAL   A CG1 
3742 C  CG1 B VAL   A 165 ? 0.1994 0.2638 0.2357 -0.0039 0.0222  0.0625  165 VAL   A CG1 
3743 C  CG2 A VAL   A 165 ? 0.1864 0.2494 0.2739 -0.0171 0.0306  0.0517  165 VAL   A CG2 
3744 C  CG2 B VAL   A 165 ? 0.2019 0.2653 0.2434 -0.0007 0.0124  0.0653  165 VAL   A CG2 
3763 N  N   A SER   A 166 ? 0.1446 0.2936 0.2888 -0.0220 0.0249  0.0582  166 SER   A N   
3764 N  N   B SER   A 166 ? 0.1781 0.2867 0.2471 -0.0162 0.0233  0.0519  166 SER   A N   
3765 C  CA  A SER   A 166 ? 0.1561 0.3171 0.3077 -0.0250 0.0149  0.0605  166 SER   A CA  
3766 C  CA  B SER   A 166 ? 0.1793 0.2992 0.2583 -0.0240 0.0214  0.0484  166 SER   A CA  
3767 C  C   A SER   A 166 ? 0.1462 0.3381 0.3162 -0.0233 -0.0079 0.0579  166 SER   A C   
3768 C  C   B SER   A 166 ? 0.1888 0.3190 0.2524 -0.0274 0.0200  0.0416  166 SER   A C   
3769 O  O   A SER   A 166 ? 0.1594 0.3429 0.3320 -0.0253 -0.0368 0.0546  166 SER   A O   
3770 O  O   B SER   A 166 ? 0.1878 0.3245 0.2483 -0.0287 0.0097  0.0330  166 SER   A O   
3771 C  CB  A SER   A 166 ? 0.1832 0.3272 0.3161 -0.0171 0.0214  0.0576  166 SER   A CB  
3772 C  CB  B SER   A 166 ? 0.1730 0.2947 0.2723 -0.0192 0.0162  0.0493  166 SER   A CB  
3773 O  OG  A SER   A 166 ? 0.2087 0.3347 0.3338 -0.0081 0.0239  0.0631  166 SER   A OG  
3774 O  OG  B SER   A 166 ? 0.1553 0.2896 0.2877 -0.0151 0.0118  0.0560  166 SER   A OG  
3785 N  N   A SER   A 167 ? 0.1371 0.3474 0.2913 -0.0093 -0.0072 0.0528  167 SER   A N   
3786 N  N   B SER   A 167 ? 0.2038 0.3288 0.2512 -0.0225 0.0269  0.0373  167 SER   A N   
3787 C  CA  A SER   A 167 ? 0.1723 0.3541 0.2863 -0.0024 -0.0155 0.0329  167 SER   A CA  
3788 C  CA  B SER   A 167 ? 0.2213 0.3390 0.2566 -0.0172 0.0264  0.0215  167 SER   A CA  
3789 C  C   A SER   A 167 ? 0.1782 0.3523 0.2816 0.0078  -0.0026 0.0211  167 SER   A C   
3790 C  C   B SER   A 167 ? 0.2252 0.3427 0.2757 -0.0153 0.0271  0.0189  167 SER   A C   
3791 O  O   A SER   A 167 ? 0.1873 0.3549 0.2855 0.0088  -0.0049 0.0170  167 SER   A O   
3792 O  O   B SER   A 167 ? 0.2219 0.3435 0.2855 -0.0203 0.0219  0.0127  167 SER   A O   
3793 C  CB  A SER   A 167 ? 0.1878 0.3601 0.2920 0.0018  -0.0123 0.0268  167 SER   A CB  
3794 C  CB  B SER   A 167 ? 0.2317 0.3443 0.2455 -0.0128 0.0312  0.0095  167 SER   A CB  
3795 O  OG  A SER   A 167 ? 0.2024 0.3622 0.2963 0.0021  -0.0026 0.0216  167 SER   A OG  
3796 O  OG  B SER   A 167 ? 0.2357 0.3486 0.2348 -0.0111 0.0416  -0.0008 167 SER   A OG  
3807 N  N   A PHE   A 168 ? 0.1766 0.3496 0.2797 0.0198  0.0080  0.0128  168 PHE   A N   
3808 N  N   B PHE   A 168 ? 0.2372 0.3468 0.2926 -0.0031 0.0237  0.0244  168 PHE   A N   
3809 C  CA  A PHE   A 168 ? 0.1735 0.3442 0.3005 0.0134  0.0191  0.0040  168 PHE   A CA  
3810 C  CA  B PHE   A 168 ? 0.2527 0.3517 0.3218 0.0026  0.0195  0.0273  168 PHE   A CA  
3811 C  C   A PHE   A 168 ? 0.1995 0.3713 0.3455 -0.0025 0.0465  0.0006  168 PHE   A C   
3812 C  C   B PHE   A 168 ? 0.2891 0.3759 0.3718 -0.0017 0.0131  0.0217  168 PHE   A C   
3813 O  O   A PHE   A 168 ? 0.1924 0.3734 0.3630 -0.0154 0.0531  0.0159  168 PHE   A O   
3814 O  O   B PHE   A 168 ? 0.2911 0.3785 0.3903 -0.0066 0.0148  0.0259  168 PHE   A O   
3815 C  CB  A PHE   A 168 ? 0.1645 0.3154 0.2861 0.0108  -0.0002 0.0026  168 PHE   A CB  
3816 C  CB  B PHE   A 168 ? 0.2374 0.3340 0.3007 0.0134  0.0204  0.0370  168 PHE   A CB  
3817 C  CG  A PHE   A 168 ? 0.1603 0.2887 0.2696 -0.0011 -0.0078 0.0060  168 PHE   A CG  
3818 C  CG  B PHE   A 168 ? 0.2263 0.3201 0.2800 0.0193  0.0206  0.0476  168 PHE   A CG  
3819 C  CD1 A PHE   A 168 ? 0.1636 0.2819 0.2705 -0.0073 -0.0073 0.0131  168 PHE   A CD1 
3820 C  CD1 B PHE   A 168 ? 0.2213 0.3150 0.2689 0.0215  0.0234  0.0567  168 PHE   A CD1 
3821 C  CD2 A PHE   A 168 ? 0.1512 0.2750 0.2553 -0.0086 0.0068  0.0013  168 PHE   A CD2 
3822 C  CD2 B PHE   A 168 ? 0.2246 0.3154 0.2739 0.0169  0.0234  0.0489  168 PHE   A CD2 
3823 C  CE1 A PHE   A 168 ? 0.1574 0.2735 0.2620 -0.0096 -0.0127 0.0124  168 PHE   A CE1 
3824 C  CE1 B PHE   A 168 ? 0.2193 0.3110 0.2678 0.0221  0.0195  0.0649  168 PHE   A CE1 
3825 C  CE2 A PHE   A 168 ? 0.1597 0.2697 0.2657 -0.0094 0.0005  0.0074  168 PHE   A CE2 
3826 C  CE2 B PHE   A 168 ? 0.2271 0.3123 0.2783 0.0168  0.0211  0.0536  168 PHE   A CE2 
3827 C  CZ  A PHE   A 168 ? 0.1638 0.2724 0.2689 -0.0104 -0.0024 0.0115  168 PHE   A CZ  
3828 C  CZ  B PHE   A 168 ? 0.2233 0.3115 0.2731 0.0190  0.0195  0.0607  168 PHE   A CZ  
3847 N  N   A LEU   A 169 ? 0.2610 0.3976 0.4002 -0.0119 0.0448  -0.0225 169 LEU   A N   
3848 N  N   B LEU   A 169 ? 0.3288 0.3985 0.4084 -0.0058 -0.0021 0.0099  169 LEU   A N   
3849 C  CA  A LEU   A 169 ? 0.3456 0.4291 0.4848 -0.0144 0.0185  -0.0318 169 LEU   A CA  
3850 C  CA  B LEU   A 169 ? 0.3676 0.4221 0.4555 -0.0037 -0.0163 0.0026  169 LEU   A CA  
3851 C  C   A LEU   A 169 ? 0.3795 0.4390 0.5387 -0.0198 0.0089  -0.0262 169 LEU   A C   
3852 C  C   B LEU   A 169 ? 0.3765 0.4291 0.4888 -0.0048 -0.0183 0.0015  169 LEU   A C   
3853 O  O   A LEU   A 169 ? 0.3922 0.4457 0.5560 -0.0232 0.0109  -0.0243 169 LEU   A O   
3854 O  O   B LEU   A 169 ? 0.3814 0.4317 0.4950 -0.0047 -0.0147 0.0033  169 LEU   A O   
3855 C  CB  A LEU   A 169 ? 0.3851 0.4479 0.4937 -0.0143 0.0077  -0.0455 169 LEU   A CB  
3856 C  CB  B LEU   A 169 ? 0.3905 0.4364 0.4620 -0.0034 -0.0274 -0.0007 169 LEU   A CB  
3857 C  CG  A LEU   A 169 ? 0.4143 0.4619 0.5070 -0.0152 0.0018  -0.0619 169 LEU   A CG  
3858 C  CG  B LEU   A 169 ? 0.4063 0.4465 0.4688 -0.0047 -0.0344 -0.0027 169 LEU   A CG  
3859 C  CD1 A LEU   A 169 ? 0.4229 0.4659 0.5128 -0.0153 0.0004  -0.0668 169 LEU   A CD1 
3860 C  CD1 B LEU   A 169 ? 0.4107 0.4491 0.4676 -0.0060 -0.0366 -0.0037 169 LEU   A CD1 
3861 C  CD2 A LEU   A 169 ? 0.4244 0.4671 0.5033 -0.0162 0.0012  -0.0681 169 LEU   A CD2 
3862 C  CD2 B LEU   A 169 ? 0.4127 0.4503 0.4648 -0.0043 -0.0369 -0.0028 169 LEU   A CD2 
3863 O  OXT A LEU   A 169 ? 0.3803 0.4385 0.5467 -0.0204 0.0122  -0.0267 169 LEU   A OXT 
3864 O  OXT B LEU   A 169 ? 0.3761 0.4323 0.4957 -0.0081 -0.0218 -0.0010 169 LEU   A OXT 
3887 N  N   A SER   B 1   ? 0.3618 0.3212 0.3322 -0.1001 -0.0796 0.0124  1   SER   B N   
3888 N  N   B SER   B 1   ? 0.3429 0.3150 0.3393 -0.0735 -0.0449 0.0025  1   SER   B N   
3889 C  CA  A SER   B 1   ? 0.3549 0.3297 0.3496 -0.1073 -0.0861 0.0079  1   SER   B CA  
3890 C  CA  B SER   B 1   ? 0.3369 0.3203 0.3452 -0.0776 -0.0465 0.0021  1   SER   B CA  
3891 C  C   A SER   B 1   ? 0.3291 0.3315 0.3406 -0.1128 -0.0957 0.0308  1   SER   B C   
3892 C  C   B SER   B 1   ? 0.3194 0.3226 0.3335 -0.0787 -0.0567 0.0251  1   SER   B C   
3893 O  O   A SER   B 1   ? 0.3419 0.3340 0.3261 -0.1015 -0.0893 0.0368  1   SER   B O   
3894 O  O   B SER   B 1   ? 0.3261 0.3239 0.3227 -0.0722 -0.0491 0.0233  1   SER   B O   
3895 C  CB  A SER   B 1   ? 0.3700 0.3316 0.3646 -0.1083 -0.0773 -0.0122 1   SER   B CB  
3896 C  CB  B SER   B 1   ? 0.3447 0.3197 0.3521 -0.0795 -0.0356 -0.0180 1   SER   B CB  
3897 O  OG  A SER   B 1   ? 0.3880 0.3444 0.4184 -0.1039 -0.0644 -0.0140 1   SER   B OG  
3898 O  OG  B SER   B 1   ? 0.3538 0.3252 0.3840 -0.0810 -0.0300 -0.0263 1   SER   B OG  
3913 N  N   A MET   B 2   ? 0.3015 0.3310 0.3419 -0.1208 -0.0950 0.0676  2   MET   B N   
3914 N  N   B MET   B 2   ? 0.3006 0.3235 0.3276 -0.0819 -0.0660 0.0635  2   MET   B N   
3915 C  CA  A MET   B 2   ? 0.2853 0.3407 0.3619 -0.1040 -0.0894 0.0905  2   MET   B CA  
3916 C  CA  B MET   B 2   ? 0.2852 0.3290 0.3300 -0.0731 -0.0751 0.0938  2   MET   B CA  
3917 C  C   A MET   B 2   ? 0.2521 0.3323 0.3357 -0.0868 -0.0967 0.1211  2   MET   B C   
3918 C  C   B MET   B 2   ? 0.2576 0.3222 0.3188 -0.0752 -0.0837 0.1206  2   MET   B C   
3919 O  O   A MET   B 2   ? 0.2417 0.3469 0.3395 -0.0763 -0.1154 0.1290  2   MET   B O   
3920 O  O   B MET   B 2   ? 0.2567 0.3307 0.3202 -0.0693 -0.0921 0.1254  2   MET   B O   
3921 C  CB  A MET   B 2   ? 0.3138 0.3718 0.4487 -0.0843 -0.0621 0.0660  2   MET   B CB  
3922 C  CB  B MET   B 2   ? 0.3026 0.3487 0.3684 -0.0511 -0.0692 0.0860  2   MET   B CB  
3923 C  CG  A MET   B 2   ? 0.3434 0.4005 0.5268 -0.0611 -0.0327 0.0485  2   MET   B CG  
3924 C  CG  B MET   B 2   ? 0.3195 0.3672 0.3922 -0.0273 -0.0645 0.0874  2   MET   B CG  
3925 S  SD  A MET   B 2   ? 0.3738 0.4307 0.6082 -0.0375 -0.0124 0.0337  2   MET   B SD  
3926 S  SD  B MET   B 2   ? 0.3361 0.3883 0.4083 -0.0024 -0.0704 0.0887  2   MET   B SD  
3927 C  CE  A MET   B 2   ? 0.3771 0.4351 0.6094 -0.0370 -0.0093 0.0310  2   MET   B CE  
3928 C  CE  B MET   B 2   ? 0.3402 0.3919 0.4171 -0.0027 -0.0657 0.0825  2   MET   B CE  
3947 N  N   . VAL   B 3   ? 0.2303 0.3014 0.3066 -0.0850 -0.0807 0.1435  3   VAL   B N   
3948 C  CA  . VAL   B 3   ? 0.2197 0.2678 0.3091 -0.0765 -0.0801 0.1330  3   VAL   B CA  
3949 C  C   . VAL   B 3   ? 0.2020 0.2620 0.2702 -0.0707 -0.0796 0.1150  3   VAL   B C   
3950 O  O   . VAL   B 3   ? 0.1973 0.2861 0.2726 -0.0735 -0.0733 0.1192  3   VAL   B O   
3951 C  CB  . VAL   B 3   ? 0.2345 0.2574 0.3653 -0.0751 -0.0714 0.1025  3   VAL   B CB  
3952 C  CG1 . VAL   B 3   ? 0.2460 0.2487 0.3898 -0.0781 -0.0686 0.1002  3   VAL   B CG1 
3953 C  CG2 . VAL   B 3   ? 0.2313 0.2567 0.3800 -0.0694 -0.0516 0.1088  3   VAL   B CG2 
3964 N  N   . ASN   B 4   ? 0.1958 0.2298 0.2384 -0.0639 -0.0654 0.0925  4   ASN   B N   
3965 C  CA  . ASN   B 4   ? 0.1926 0.2322 0.1865 -0.0628 -0.0537 0.0587  4   ASN   B CA  
3966 C  C   . ASN   B 4   ? 0.1979 0.2552 0.1681 -0.0618 -0.0392 0.0410  4   ASN   B C   
3967 O  O   . ASN   B 4   ? 0.2003 0.2639 0.1776 -0.0602 -0.0321 0.0211  4   ASN   B O   
3968 C  CB  . ASN   B 4   ? 0.1936 0.2268 0.1796 -0.0598 -0.0536 0.0473  4   ASN   B CB  
3969 C  CG  . ASN   B 4   ? 0.1989 0.2124 0.1708 -0.0540 -0.0544 0.0340  4   ASN   B CG  
3970 O  OD1 . ASN   B 4   ? 0.2050 0.1989 0.1677 -0.0523 -0.0519 0.0359  4   ASN   B OD1 
3971 N  ND2 . ASN   B 4   ? 0.2217 0.2189 0.1929 -0.0347 -0.0390 0.0363  4   ASN   B ND2 
3978 N  N   . SER   B 5   ? 0.1987 0.2727 0.1927 -0.0643 -0.0345 0.0314  5   SER   B N   
3979 C  CA  . SER   B 5   ? 0.2214 0.3068 0.1956 -0.0524 -0.0187 0.0343  5   SER   B CA  
3980 C  C   . SER   B 5   ? 0.2476 0.3093 0.2352 -0.0720 0.0131  0.0270  5   SER   B C   
3981 O  O   . SER   B 5   ? 0.2719 0.3081 0.3478 -0.0600 0.0670  0.0379  5   SER   B O   
3982 C  CB  . SER   B 5   ? 0.2314 0.3236 0.2260 -0.0383 -0.0098 0.0464  5   SER   B CB  
3983 O  OG  . SER   B 5   ? 0.2616 0.3490 0.2832 -0.0244 -0.0095 0.0530  5   SER   B OG  
3989 N  N   A PHE   B 6   ? 0.2708 0.3244 0.2169 -0.0805 0.0220  0.0276  6   PHE   B N   
3990 N  N   B PHE   B 6   ? 0.2505 0.3070 0.2089 -0.0732 0.0147  0.0188  6   PHE   B N   
3991 C  CA  A PHE   B 6   ? 0.2932 0.3289 0.1937 -0.0955 0.0226  0.0202  6   PHE   B CA  
3992 C  CA  B PHE   B 6   ? 0.2523 0.2961 0.1855 -0.0804 0.0085  0.0066  6   PHE   B CA  
3993 C  C   A PHE   B 6   ? 0.3431 0.3610 0.2555 -0.0978 0.0392  -0.0031 6   PHE   B C   
3994 C  C   B PHE   B 6   ? 0.2682 0.3002 0.2043 -0.0824 0.0144  -0.0099 6   PHE   B C   
3995 O  O   A PHE   B 6   ? 0.3591 0.3842 0.2993 -0.0913 0.0294  -0.0067 6   PHE   B O   
3996 O  O   B PHE   B 6   ? 0.2822 0.3110 0.2258 -0.0688 0.0102  -0.0080 6   PHE   B O   
3997 C  CB  A PHE   B 6   ? 0.2723 0.3067 0.1762 -0.0931 0.0051  0.0215  6   PHE   B CB  
3998 C  CB  B PHE   B 6   ? 0.2410 0.2837 0.1828 -0.0771 -0.0017 0.0050  6   PHE   B CB  
3999 C  CG  A PHE   B 6   ? 0.2474 0.2818 0.1649 -0.0911 -0.0110 0.0220  6   PHE   B CG  
4000 C  CG  B PHE   B 6   ? 0.2253 0.2697 0.1805 -0.0763 -0.0091 0.0055  6   PHE   B CG  
4001 C  CD1 A PHE   B 6   ? 0.2492 0.2571 0.1457 -0.0883 -0.0203 0.0241  6   PHE   B CD1 
4002 C  CD1 B PHE   B 6   ? 0.2273 0.2549 0.1734 -0.0735 -0.0144 0.0103  6   PHE   B CD1 
4003 C  CD2 A PHE   B 6   ? 0.2269 0.2780 0.1769 -0.0824 -0.0141 0.0520  6   PHE   B CD2 
4004 C  CD2 B PHE   B 6   ? 0.2122 0.2676 0.1836 -0.0714 -0.0097 0.0239  6   PHE   B CD2 
4005 C  CE1 A PHE   B 6   ? 0.2451 0.2388 0.1602 -0.0797 -0.0326 0.0238  6   PHE   B CE1 
4006 C  CE1 B PHE   B 6   ? 0.2246 0.2441 0.1793 -0.0694 -0.0202 0.0099  6   PHE   B CE1 
4007 C  CE2 A PHE   B 6   ? 0.2313 0.2656 0.2085 -0.0724 -0.0114 0.0500  6   PHE   B CE2 
4008 C  CE2 B PHE   B 6   ? 0.2150 0.2608 0.2015 -0.0649 -0.0045 0.0278  6   PHE   B CE2 
4009 C  CZ  A PHE   B 6   ? 0.2364 0.2467 0.1819 -0.0732 -0.0260 0.0371  6   PHE   B CZ  
4010 C  CZ  B PHE   B 6   ? 0.2180 0.2476 0.1885 -0.0662 -0.0138 0.0182  6   PHE   B CZ  
4029 N  N   A SER   B 7   ? 0.3753 0.3582 0.2851 -0.1109 0.0656  -0.0273 7   SER   B N   
4030 N  N   B SER   B 7   ? 0.2716 0.2855 0.2155 -0.0974 0.0368  -0.0252 7   SER   B N   
4031 C  CA  A SER   B 7   ? 0.4053 0.3701 0.3431 -0.1059 0.0815  -0.0358 7   SER   B CA  
4032 C  CA  B SER   B 7   ? 0.2767 0.2923 0.2530 -0.0927 0.0405  -0.0301 7   SER   B CA  
4033 C  C   A SER   B 7   ? 0.4108 0.3616 0.3301 -0.1092 0.0944  -0.0437 7   SER   B C   
4034 C  C   B SER   B 7   ? 0.2580 0.2887 0.2548 -0.0888 0.0631  -0.0376 7   SER   B C   
4035 O  O   A SER   B 7   ? 0.4172 0.3634 0.3512 -0.1146 0.0957  -0.0401 7   SER   B O   
4036 O  O   B SER   B 7   ? 0.2609 0.2914 0.2704 -0.0947 0.0568  -0.0411 7   SER   B O   
4037 C  CB  A SER   B 7   ? 0.4180 0.3845 0.3952 -0.1003 0.0879  -0.0300 7   SER   B CB  
4038 C  CB  B SER   B 7   ? 0.2915 0.2990 0.2854 -0.0918 0.0307  -0.0204 7   SER   B CB  
4039 O  OG  A SER   B 7   ? 0.4249 0.3953 0.4355 -0.0956 0.0898  -0.0204 7   SER   B OG  
4040 O  OG  B SER   B 7   ? 0.2994 0.3035 0.3061 -0.0892 0.0237  -0.0122 7   SER   B OG  
4051 N  N   A GLY   B 8   ? 0.4090 0.3497 0.3265 -0.1016 0.1017  -0.0553 8   GLY   B N   
4052 N  N   B GLY   B 8   ? 0.2451 0.2843 0.2433 -0.0709 0.0731  -0.0468 8   GLY   B N   
4053 C  CA  A GLY   B 8   ? 0.3956 0.3273 0.3135 -0.0996 0.1054  -0.0658 8   GLY   B CA  
4054 C  CA  B GLY   B 8   ? 0.2323 0.2768 0.2399 -0.0545 0.0818  -0.0469 8   GLY   B CA  
4055 C  C   A GLY   B 8   ? 0.3769 0.2945 0.2961 -0.1005 0.1014  -0.0693 8   GLY   B C   
4056 C  C   B GLY   B 8   ? 0.2195 0.2648 0.2354 -0.0413 0.0864  -0.0517 8   GLY   B C   
4057 O  O   A GLY   B 8   ? 0.3844 0.3072 0.3195 -0.0920 0.0990  -0.0785 8   GLY   B O   
4058 O  O   B GLY   B 8   ? 0.2235 0.2656 0.2595 -0.0361 0.0741  -0.0640 8   GLY   B O   
4065 N  N   A TYR   B 9   ? 0.3616 0.2583 0.2769 -0.0952 0.0810  -0.0765 9   TYR   B N   
4066 N  N   B TYR   B 9   ? 0.2014 0.2560 0.2197 -0.0357 0.0764  -0.0536 9   TYR   B N   
4067 C  CA  A TYR   B 9   ? 0.3464 0.2242 0.2436 -0.0841 0.0601  -0.0640 9   TYR   B CA  
4068 C  CA  B TYR   B 9   ? 0.1921 0.2515 0.1967 -0.0336 0.0600  -0.0545 9   TYR   B CA  
4069 C  C   A TYR   B 9   ? 0.3365 0.2140 0.2323 -0.0810 0.0417  -0.0514 9   TYR   B C   
4070 C  C   B TYR   B 9   ? 0.2035 0.2529 0.1976 -0.0330 0.0362  -0.0565 9   TYR   B C   
4071 O  O   A TYR   B 9   ? 0.3408 0.2268 0.2630 -0.0810 0.0505  -0.0356 9   TYR   B O   
4072 O  O   B TYR   B 9   ? 0.2170 0.2636 0.2229 -0.0364 0.0296  -0.0490 9   TYR   B O   
4073 C  CB  A TYR   B 9   ? 0.3476 0.1972 0.2541 -0.0776 0.0502  -0.0605 9   TYR   B CB  
4074 C  CB  B TYR   B 9   ? 0.1741 0.2421 0.1920 -0.0307 0.0533  -0.0501 9   TYR   B CB  
4075 C  CG  A TYR   B 9   ? 0.3447 0.1753 0.2493 -0.0814 0.0472  -0.0650 9   TYR   B CG  
4076 C  CG  B TYR   B 9   ? 0.1643 0.2332 0.1756 -0.0310 0.0379  -0.0422 9   TYR   B CG  
4077 C  CD1 A TYR   B 9   ? 0.3467 0.1719 0.2571 -0.0882 0.0544  -0.0590 9   TYR   B CD1 
4078 C  CD1 B TYR   B 9   ? 0.1622 0.2291 0.1746 -0.0331 0.0314  -0.0327 9   TYR   B CD1 
4079 C  CD2 A TYR   B 9   ? 0.3387 0.1697 0.2392 -0.0760 0.0416  -0.0689 9   TYR   B CD2 
4080 C  CD2 B TYR   B 9   ? 0.1652 0.2323 0.1637 -0.0328 0.0282  -0.0357 9   TYR   B CD2 
4081 C  CE1 A TYR   B 9   ? 0.3443 0.1793 0.2501 -0.0830 0.0630  -0.0644 9   TYR   B CE1 
4082 C  CE1 B TYR   B 9   ? 0.1646 0.2263 0.1754 -0.0348 0.0344  -0.0308 9   TYR   B CE1 
4083 C  CE2 A TYR   B 9   ? 0.3394 0.1687 0.2494 -0.0740 0.0435  -0.0592 9   TYR   B CE2 
4084 C  CE2 B TYR   B 9   ? 0.1683 0.2311 0.1678 -0.0328 0.0222  -0.0280 9   TYR   B CE2 
4085 C  CZ  A TYR   B 9   ? 0.3403 0.1766 0.2553 -0.0759 0.0497  -0.0758 9   TYR   B CZ  
4086 C  CZ  B TYR   B 9   ? 0.1724 0.2306 0.1715 -0.0360 0.0225  -0.0318 9   TYR   B CZ  
4087 O  OH  A TYR   B 9   ? 0.3381 0.1799 0.2619 -0.0703 0.0558  -0.0819 9   TYR   B OH  
4088 O  OH  B TYR   B 9   ? 0.1792 0.2375 0.1933 -0.0397 0.0214  -0.0295 9   TYR   B OH  
4107 N  N   A LEU   B 10  ? 0.3266 0.1927 0.2188 -0.0854 0.0244  -0.0396 10  LEU   B N   
4108 N  N   B LEU   B 10  ? 0.2020 0.2477 0.1940 -0.0354 0.0283  -0.0517 10  LEU   B N   
4109 C  CA  A LEU   B 10  ? 0.3258 0.1893 0.2164 -0.0966 -0.0150 -0.0302 10  LEU   B CA  
4110 C  CA  B LEU   B 10  ? 0.2206 0.2541 0.2055 -0.0510 0.0021  -0.0431 10  LEU   B CA  
4111 C  C   A LEU   B 10  ? 0.3136 0.1955 0.2196 -0.0893 -0.0317 -0.0147 10  LEU   B C   
4112 C  C   B LEU   B 10  ? 0.2127 0.2593 0.2162 -0.0522 -0.0101 -0.0388 10  LEU   B C   
4113 O  O   A LEU   B 10  ? 0.3069 0.1920 0.2224 -0.0732 -0.0329 -0.0020 10  LEU   B O   
4114 O  O   B LEU   B 10  ? 0.1917 0.2599 0.2068 -0.0487 -0.0059 -0.0438 10  LEU   B O   
4115 C  CB  A LEU   B 10  ? 0.3408 0.1842 0.2335 -0.1013 -0.0371 -0.0108 10  LEU   B CB  
4116 C  CB  B LEU   B 10  ? 0.2553 0.2604 0.2300 -0.0563 -0.0049 -0.0270 10  LEU   B CB  
4117 C  CG  A LEU   B 10  ? 0.3595 0.1965 0.2691 -0.0933 -0.0672 0.0027  10  LEU   B CG  
4118 C  CG  B LEU   B 10  ? 0.2875 0.2704 0.2600 -0.0613 -0.0144 -0.0103 10  LEU   B CG  
4119 C  CD1 A LEU   B 10  ? 0.3767 0.2091 0.2953 -0.0848 -0.0658 0.0024  10  LEU   B CD1 
4120 C  CD1 B LEU   B 10  ? 0.3060 0.2750 0.2795 -0.0587 -0.0141 -0.0099 10  LEU   B CD1 
4121 C  CD2 A LEU   B 10  ? 0.3629 0.1992 0.2886 -0.0895 -0.0658 0.0287  10  LEU   B CD2 
4122 C  CD2 B LEU   B 10  ? 0.2907 0.2746 0.2626 -0.0660 -0.0092 0.0009  10  LEU   B CD2 
4145 N  N   A LYS   B 11  ? 0.3184 0.2238 0.2159 -0.0836 -0.0395 -0.0098 11  LYS   B N   
4146 N  N   B LYS   B 11  ? 0.2339 0.2710 0.2252 -0.0502 -0.0208 -0.0302 11  LYS   B N   
4147 C  CA  A LYS   B 11  ? 0.3267 0.2495 0.2495 -0.0691 -0.0447 -0.0177 11  LYS   B CA  
4148 C  CA  B LYS   B 11  ? 0.2657 0.2816 0.2597 -0.0446 -0.0252 -0.0268 11  LYS   B CA  
4149 C  C   A LYS   B 11  ? 0.2961 0.2307 0.2441 -0.0786 -0.0405 -0.0284 11  LYS   B C   
4150 C  C   B LYS   B 11  ? 0.2594 0.2595 0.2444 -0.0586 -0.0326 -0.0321 11  LYS   B C   
4151 O  O   A LYS   B 11  ? 0.3066 0.2301 0.2671 -0.0902 -0.0473 -0.0420 11  LYS   B O   
4152 O  O   B LYS   B 11  ? 0.2563 0.2694 0.2327 -0.0596 -0.0435 -0.0414 11  LYS   B O   
4153 C  CB  A LYS   B 11  ? 0.3613 0.2961 0.3206 -0.0471 -0.0493 -0.0261 11  LYS   B CB  
4154 C  CB  B LYS   B 11  ? 0.3000 0.3110 0.3220 -0.0281 -0.0253 -0.0272 11  LYS   B CB  
4155 C  CG  A LYS   B 11  ? 0.3910 0.3276 0.3938 -0.0299 -0.0507 -0.0276 11  LYS   B CG  
4156 C  CG  B LYS   B 11  ? 0.3284 0.3311 0.3874 -0.0168 -0.0264 -0.0271 11  LYS   B CG  
4157 C  CD  A LYS   B 11  ? 0.4118 0.3478 0.4539 -0.0197 -0.0515 -0.0296 11  LYS   B CD  
4158 C  CD  B LYS   B 11  ? 0.3492 0.3425 0.4417 -0.0093 -0.0271 -0.0265 11  LYS   B CD  
4159 C  CE  A LYS   B 11  ? 0.4259 0.3620 0.4977 -0.0145 -0.0512 -0.0307 11  LYS   B CE  
4160 C  CE  B LYS   B 11  ? 0.3633 0.3515 0.4790 -0.0055 -0.0277 -0.0265 11  LYS   B CE  
4161 N  NZ  A LYS   B 11  ? 0.4340 0.3709 0.5206 -0.0131 -0.0519 -0.0290 11  LYS   B NZ  
4162 N  NZ  B LYS   B 11  ? 0.3705 0.3570 0.4998 -0.0040 -0.0283 -0.0247 11  LYS   B NZ  
4189 N  N   . LEU   B 12  ? 0.2512 0.2271 0.2392 -0.0677 -0.0399 -0.0382 12  LEU   B N   
4190 C  CA  . LEU   B 12  ? 0.2308 0.2020 0.2629 -0.0567 -0.0248 -0.0335 12  LEU   B CA  
4191 C  C   . LEU   B 12  ? 0.2204 0.1995 0.2726 -0.0577 -0.0345 -0.0337 12  LEU   B C   
4192 O  O   . LEU   B 12  ? 0.2192 0.2024 0.3079 -0.0581 -0.0617 -0.0250 12  LEU   B O   
4193 C  CB  . LEU   B 12  ? 0.2295 0.1779 0.2605 -0.0388 -0.0190 -0.0285 12  LEU   B CB  
4194 C  CG  . LEU   B 12  ? 0.2343 0.1719 0.2595 -0.0404 -0.0147 -0.0220 12  LEU   B CG  
4195 C  CD1 . LEU   B 12  ? 0.2475 0.1767 0.2486 -0.0267 -0.0164 -0.0090 12  LEU   B CD1 
4196 C  CD2 . LEU   B 12  ? 0.2417 0.1773 0.2693 -0.0422 -0.0077 -0.0329 12  LEU   B CD2 
4209 N  N   A THR   B 13  ? 0.2153 0.1996 0.2727 -0.0556 -0.0398 -0.0452 13  THR   B N   
4210 N  N   B THR   B 13  ? 0.2298 0.2049 0.2674 -0.0564 -0.0360 -0.0363 13  THR   B N   
4211 C  CA  A THR   B 13  ? 0.2142 0.2062 0.2664 -0.0605 -0.0626 -0.0299 13  THR   B CA  
4212 C  CA  B THR   B 13  ? 0.2404 0.2147 0.2605 -0.0575 -0.0478 -0.0236 13  THR   B CA  
4213 C  C   A THR   B 13  ? 0.2554 0.2256 0.2887 -0.0698 -0.0797 -0.0238 13  THR   B C   
4214 C  C   B THR   B 13  ? 0.2673 0.2312 0.2815 -0.0628 -0.0588 -0.0147 13  THR   B C   
4215 O  O   A THR   B 13  ? 0.2753 0.2347 0.3082 -0.0635 -0.0506 -0.0248 13  THR   B O   
4216 O  O   B THR   B 13  ? 0.2795 0.2381 0.2921 -0.0600 -0.0404 -0.0136 13  THR   B O   
4217 C  CB  A THR   B 13  ? 0.1926 0.2017 0.2667 -0.0514 -0.0468 -0.0180 13  THR   B CB  
4218 C  CB  B THR   B 13  ? 0.2331 0.2117 0.2524 -0.0520 -0.0398 -0.0197 13  THR   B CB  
4219 O  OG1 A THR   B 13  ? 0.1817 0.1951 0.2669 -0.0485 -0.0372 -0.0164 13  THR   B OG1 
4220 O  OG1 B THR   B 13  ? 0.2287 0.2073 0.2496 -0.0496 -0.0371 -0.0229 13  THR   B OG1 
4221 C  CG2 A THR   B 13  ? 0.1960 0.2058 0.2651 -0.0425 -0.0342 -0.0076 13  THR   B CG2 
4222 C  CG2 B THR   B 13  ? 0.2354 0.2141 0.2492 -0.0477 -0.0319 -0.0121 13  THR   B CG2 
4237 N  N   A ASP   B 14  ? 0.2784 0.2399 0.3004 -0.0804 -0.1102 -0.0036 14  ASP   B N   
4238 N  N   B ASP   B 14  ? 0.2818 0.2421 0.2985 -0.0679 -0.0806 0.0012  14  ASP   B N   
4239 C  CA  A ASP   B 14  ? 0.2980 0.2571 0.3278 -0.0804 -0.1221 0.0171  14  ASP   B CA  
4240 C  CA  B ASP   B 14  ? 0.2933 0.2532 0.3229 -0.0669 -0.0923 0.0137  14  ASP   B CA  
4241 C  C   A ASP   B 14  ? 0.2851 0.2362 0.2814 -0.0821 -0.1101 0.0201  14  ASP   B C   
4242 C  C   B ASP   B 14  ? 0.2751 0.2310 0.2792 -0.0693 -0.1022 0.0155  14  ASP   B C   
4243 O  O   A ASP   B 14  ? 0.3065 0.2461 0.2841 -0.0794 -0.0971 0.0301  14  ASP   B O   
4244 O  O   B ASP   B 14  ? 0.2841 0.2271 0.2747 -0.0637 -0.1058 0.0190  14  ASP   B O   
4245 C  CB  A ASP   B 14  ? 0.3248 0.3000 0.4081 -0.0737 -0.1365 0.0176  14  ASP   B CB  
4246 C  CB  B ASP   B 14  ? 0.3191 0.2891 0.3912 -0.0598 -0.0922 0.0164  14  ASP   B CB  
4247 C  CG  A ASP   B 14  ? 0.3507 0.3336 0.4895 -0.0672 -0.1308 0.0025  14  ASP   B CG  
4248 C  CG  B ASP   B 14  ? 0.3418 0.3184 0.4570 -0.0524 -0.0858 0.0078  14  ASP   B CG  
4249 O  OD1 A ASP   B 14  ? 0.3634 0.3425 0.5086 -0.0658 -0.1312 -0.0080 14  ASP   B OD1 
4250 O  OD1 B ASP   B 14  ? 0.3509 0.3303 0.4744 -0.0496 -0.0830 0.0025  14  ASP   B OD1 
4251 O  OD2 A ASP   B 14  ? 0.3562 0.3503 0.5271 -0.0672 -0.1249 0.0012  14  ASP   B OD2 
4252 O  OD2 B ASP   B 14  ? 0.3492 0.3302 0.4832 -0.0509 -0.0826 0.0071  14  ASP   B OD2 
4261 N  N   . ASN   B 15  ? 0.2519 0.2122 0.2565 -0.0659 -0.1007 0.0214  15  ASN   B N   
4262 C  CA  . ASN   B 15  ? 0.2094 0.1883 0.2397 -0.0442 -0.0730 0.0082  15  ASN   B CA  
4263 C  C   . ASN   B 15  ? 0.1876 0.1708 0.2250 -0.0258 -0.0503 -0.0025 15  ASN   B C   
4264 O  O   . ASN   B 15  ? 0.1836 0.1633 0.2431 -0.0261 -0.0572 -0.0105 15  ASN   B O   
4265 C  CB  . ASN   B 15  ? 0.2001 0.1854 0.2627 -0.0217 -0.0691 0.0169  15  ASN   B CB  
4266 C  CG  . ASN   B 15  ? 0.1771 0.1824 0.2843 -0.0288 -0.0398 0.0191  15  ASN   B CG  
4267 O  OD1 . ASN   B 15  ? 0.1841 0.2123 0.3204 -0.0481 -0.0419 0.0217  15  ASN   B OD1 
4268 N  ND2 . ASN   B 15  ? 0.1784 0.1549 0.2720 -0.0134 -0.0122 -0.0055 15  ASN   B ND2 
4276 N  N   . VAL   B 16  ? 0.1810 0.1618 0.2396 -0.0316 -0.0559 -0.0033 16  VAL   B N   
4277 C  CA  . VAL   B 16  ? 0.1815 0.1631 0.2168 -0.0312 -0.0434 -0.0257 16  VAL   B CA  
4278 C  C   . VAL   B 16  ? 0.1811 0.1796 0.2085 -0.0379 -0.0370 -0.0055 16  VAL   B C   
4279 O  O   . VAL   B 16  ? 0.1850 0.1874 0.2229 -0.0369 -0.0344 -0.0297 16  VAL   B O   
4280 C  CB  . VAL   B 16  ? 0.1833 0.1563 0.2217 -0.0174 -0.0297 -0.0217 16  VAL   B CB  
4281 C  CG1 . VAL   B 16  ? 0.1911 0.1628 0.2187 -0.0067 -0.0295 -0.0182 16  VAL   B CG1 
4282 C  CG2 . VAL   B 16  ? 0.1882 0.1624 0.2488 -0.0072 -0.0165 -0.0254 16  VAL   B CG2 
4292 N  N   . TYR   B 17  ? 0.1826 0.1867 0.2046 -0.0279 -0.0255 -0.0086 17  TYR   B N   
4293 C  CA  . TYR   B 17  ? 0.1883 0.2024 0.2003 -0.0350 -0.0342 0.0066  17  TYR   B CA  
4294 C  C   . TYR   B 17  ? 0.1855 0.1762 0.1956 -0.0356 -0.0198 -0.0150 17  TYR   B C   
4295 O  O   . TYR   B 17  ? 0.1878 0.1778 0.1965 -0.0325 -0.0255 -0.0383 17  TYR   B O   
4296 C  CB  . TYR   B 17  ? 0.2294 0.2635 0.2494 -0.0202 -0.0392 0.0368  17  TYR   B CB  
4297 C  CG  . TYR   B 17  ? 0.2656 0.3289 0.3013 -0.0101 -0.0658 0.0578  17  TYR   B CG  
4298 C  CD1 . TYR   B 17  ? 0.2902 0.3575 0.3422 -0.0105 -0.0766 0.0683  17  TYR   B CD1 
4299 C  CD2 . TYR   B 17  ? 0.2932 0.3629 0.3405 -0.0015 -0.0784 0.0627  17  TYR   B CD2 
4300 C  CE1 . TYR   B 17  ? 0.3150 0.3894 0.3681 0.0005  -0.0895 0.0702  17  TYR   B CE1 
4301 C  CE2 . TYR   B 17  ? 0.3157 0.3917 0.3678 0.0110  -0.0923 0.0725  17  TYR   B CE2 
4302 C  CZ  . TYR   B 17  ? 0.3295 0.4100 0.3881 0.0138  -0.0997 0.0733  17  TYR   B CZ  
4303 O  OH  . TYR   B 17  ? 0.3491 0.4291 0.4009 0.0199  -0.1087 0.0789  17  TYR   B OH  
4313 N  N   . ILE   B 18  ? 0.1906 0.1836 0.1914 -0.0320 -0.0103 -0.0192 18  ILE   B N   
4314 C  CA  . ILE   B 18  ? 0.1964 0.1721 0.2008 -0.0421 -0.0002 -0.0306 18  ILE   B CA  
4315 C  C   . ILE   B 18  ? 0.2052 0.1761 0.2078 -0.0507 -0.0041 -0.0421 18  ILE   B C   
4316 O  O   . ILE   B 18  ? 0.2200 0.1956 0.2122 -0.0468 0.0015  -0.0505 18  ILE   B O   
4317 C  CB  . ILE   B 18  ? 0.2040 0.1704 0.2105 -0.0431 -0.0039 -0.0252 18  ILE   B CB  
4318 C  CG1 . ILE   B 18  ? 0.2037 0.1755 0.2229 -0.0428 0.0039  -0.0272 18  ILE   B CG1 
4319 C  CG2 . ILE   B 18  ? 0.2083 0.1693 0.2099 -0.0464 -0.0198 -0.0241 18  ILE   B CG2 
4320 C  CD1 . ILE   B 18  ? 0.2201 0.1991 0.2394 -0.0385 -0.0149 0.0078  18  ILE   B CD1 
4332 N  N   A LYS   B 19  ? 0.2107 0.1690 0.2152 -0.0307 0.0264  -0.0466 19  LYS   B N   
4333 N  N   B LYS   B 19  ? 0.2097 0.1837 0.2164 -0.0336 0.0198  -0.0484 19  LYS   B N   
4334 C  CA  A LYS   B 19  ? 0.2174 0.1743 0.2457 -0.0356 0.0319  -0.0499 19  LYS   B CA  
4335 C  CA  B LYS   B 19  ? 0.2146 0.1971 0.2379 -0.0311 0.0290  -0.0559 19  LYS   B CA  
4336 C  C   A LYS   B 19  ? 0.2025 0.1690 0.2544 -0.0311 0.0396  -0.0626 19  LYS   B C   
4337 C  C   B LYS   B 19  ? 0.2020 0.1944 0.2331 -0.0264 0.0286  -0.0736 19  LYS   B C   
4338 O  O   A LYS   B 19  ? 0.1997 0.1680 0.2383 -0.0261 0.0363  -0.0501 19  LYS   B O   
4339 O  O   B LYS   B 19  ? 0.1973 0.1982 0.2079 -0.0266 0.0275  -0.0811 19  LYS   B O   
4340 C  CB  A LYS   B 19  ? 0.2470 0.2002 0.2615 -0.0423 0.0453  -0.0468 19  LYS   B CB  
4341 C  CB  B LYS   B 19  ? 0.2366 0.2190 0.2598 -0.0322 0.0452  -0.0488 19  LYS   B CB  
4342 C  CG  A LYS   B 19  ? 0.2791 0.2211 0.2969 -0.0570 0.0572  -0.0485 19  LYS   B CG  
4343 C  CG  B LYS   B 19  ? 0.2594 0.2382 0.2932 -0.0391 0.0585  -0.0438 19  LYS   B CG  
4344 C  CD  A LYS   B 19  ? 0.3156 0.2512 0.3176 -0.0608 0.0709  -0.0478 19  LYS   B CD  
4345 C  CD  B LYS   B 19  ? 0.2841 0.2592 0.3157 -0.0417 0.0733  -0.0398 19  LYS   B CD  
4346 C  CE  A LYS   B 19  ? 0.3454 0.2749 0.3463 -0.0601 0.0670  -0.0568 19  LYS   B CE  
4347 C  CE  B LYS   B 19  ? 0.3036 0.2754 0.3404 -0.0416 0.0759  -0.0435 19  LYS   B CE  
4348 N  NZ  A LYS   B 19  ? 0.3637 0.2899 0.3584 -0.0619 0.0665  -0.0543 19  LYS   B NZ  
4349 N  NZ  B LYS   B 19  ? 0.3148 0.2864 0.3534 -0.0440 0.0779  -0.0417 19  LYS   B NZ  
4376 N  N   A ASN   B 20  ? 0.2086 0.1868 0.2857 -0.0216 0.0472  -0.0711 20  ASN   B N   
4377 N  N   B ASN   B 20  ? 0.2027 0.1971 0.2516 -0.0165 0.0279  -0.0719 20  ASN   B N   
4378 C  CA  A ASN   B 20  ? 0.2154 0.2038 0.3104 -0.0125 0.0475  -0.0940 20  ASN   B CA  
4379 C  CA  B ASN   B 20  ? 0.2044 0.1980 0.2626 -0.0097 0.0267  -0.0792 20  ASN   B CA  
4380 C  C   A ASN   B 20  ? 0.2129 0.2287 0.3204 -0.0163 0.0604  -0.1031 20  ASN   B C   
4381 C  C   B ASN   B 20  ? 0.1964 0.1935 0.2527 -0.0048 0.0275  -0.0750 20  ASN   B C   
4382 O  O   A ASN   B 20  ? 0.2237 0.2552 0.3431 -0.0178 0.0653  -0.1043 20  ASN   B O   
4383 O  O   B ASN   B 20  ? 0.1952 0.1857 0.2440 0.0077  0.0194  -0.0577 20  ASN   B O   
4384 C  CB  A ASN   B 20  ? 0.2478 0.2067 0.3463 0.0177  0.0296  -0.0980 20  ASN   B CB  
4385 C  CB  B ASN   B 20  ? 0.2301 0.2116 0.2961 0.0015  0.0223  -0.0854 20  ASN   B CB  
4386 C  CG  A ASN   B 20  ? 0.2761 0.2153 0.3709 0.0492  0.0236  -0.1036 20  ASN   B CG  
4387 C  CG  B ASN   B 20  ? 0.2536 0.2276 0.3221 0.0157  0.0219  -0.0875 20  ASN   B CG  
4388 O  OD1 A ASN   B 20  ? 0.3038 0.2355 0.3891 0.0609  0.0220  -0.1040 20  ASN   B OD1 
4389 O  OD1 B ASN   B 20  ? 0.2735 0.2455 0.3422 0.0230  0.0218  -0.0814 20  ASN   B OD1 
4390 N  ND2 A ASN   B 20  ? 0.2727 0.2201 0.3723 0.0541  0.0077  -0.1007 20  ASN   B ND2 
4391 N  ND2 B ASN   B 20  ? 0.2511 0.2323 0.3228 0.0149  0.0101  -0.0898 20  ASN   B ND2 
4404 N  N   A ALA   B 21  ? 0.2130 0.2223 0.3139 -0.0241 0.0659  -0.0923 21  ALA   B N   
4405 N  N   B ALA   B 21  ? 0.2017 0.1940 0.2617 -0.0161 0.0398  -0.0751 21  ALA   B N   
4406 C  CA  A ALA   B 21  ? 0.2225 0.2265 0.3198 -0.0284 0.0521  -0.0748 21  ALA   B CA  
4407 C  CA  B ALA   B 21  ? 0.2122 0.2033 0.2785 -0.0224 0.0352  -0.0679 21  ALA   B CA  
4408 C  C   A ALA   B 21  ? 0.2198 0.2009 0.2987 -0.0264 0.0516  -0.0609 21  ALA   B C   
4409 C  C   B ALA   B 21  ? 0.2130 0.1911 0.2772 -0.0229 0.0413  -0.0599 21  ALA   B C   
4410 O  O   A ALA   B 21  ? 0.2277 0.1925 0.2887 -0.0361 0.0455  -0.0596 21  ALA   B O   
4411 O  O   B ALA   B 21  ? 0.2172 0.1858 0.2671 -0.0286 0.0383  -0.0611 21  ALA   B O   
4412 C  CB  A ALA   B 21  ? 0.2342 0.2516 0.3333 -0.0381 0.0519  -0.0589 21  ALA   B CB  
4413 C  CB  B ALA   B 21  ? 0.2217 0.2229 0.2878 -0.0285 0.0345  -0.0579 21  ALA   B CB  
4424 N  N   . ASP   B 22  ? 0.2090 0.1818 0.2829 -0.0266 0.0382  -0.0536 22  ASP   B N   
4425 C  CA  . ASP   B 22  ? 0.2041 0.1763 0.2678 -0.0164 0.0201  -0.0291 22  ASP   B CA  
4426 C  C   . ASP   B 22  ? 0.2005 0.1702 0.2079 -0.0217 0.0195  -0.0205 22  ASP   B C   
4427 O  O   . ASP   B 22  ? 0.2059 0.1753 0.2157 -0.0117 0.0117  -0.0158 22  ASP   B O   
4428 C  CB  . ASP   B 22  ? 0.2090 0.1824 0.3079 -0.0061 0.0221  -0.0181 22  ASP   B CB  
4429 C  CG  . ASP   B 22  ? 0.2059 0.2028 0.3456 0.0119  0.0069  -0.0095 22  ASP   B CG  
4430 O  OD1 . ASP   B 22  ? 0.2200 0.1919 0.3457 0.0062  -0.0115 -0.0095 22  ASP   B OD1 
4431 O  OD2 . ASP   B 22  ? 0.2122 0.2311 0.4141 0.0220  -0.0118 -0.0163 22  ASP   B OD2 
4437 N  N   . ILE   B 23  ? 0.1972 0.1580 0.1955 -0.0134 -0.0058 0.0126  23  ILE   B N   
4438 C  CA  . ILE   B 23  ? 0.1854 0.1566 0.1815 -0.0120 -0.0048 0.0094  23  ILE   B CA  
4439 C  C   . ILE   B 23  ? 0.1769 0.1604 0.1729 -0.0045 -0.0063 0.0046  23  ILE   B C   
4440 O  O   . ILE   B 23  ? 0.1666 0.1579 0.1679 -0.0077 -0.0048 0.0062  23  ILE   B O   
4441 C  CB  . ILE   B 23  ? 0.1792 0.1590 0.1998 -0.0200 -0.0039 0.0221  23  ILE   B CB  
4442 C  CG1 . ILE   B 23  ? 0.1778 0.1664 0.2135 -0.0114 0.0004  0.0287  23  ILE   B CG1 
4443 C  CG2 . ILE   B 23  ? 0.1883 0.1748 0.1887 -0.0129 0.0005  0.0039  23  ILE   B CG2 
4444 C  CD1 . ILE   B 23  ? 0.1832 0.1797 0.2112 -0.0099 -0.0043 0.0270  23  ILE   B CD1 
4456 N  N   . VAL   B 24  ? 0.1791 0.1535 0.1893 -0.0047 -0.0080 -0.0015 24  VAL   B N   
4457 C  CA  . VAL   B 24  ? 0.1705 0.1571 0.2148 -0.0060 -0.0181 0.0017  24  VAL   B CA  
4458 C  C   . VAL   B 24  ? 0.1744 0.1661 0.2122 -0.0026 -0.0108 0.0056  24  VAL   B C   
4459 O  O   . VAL   B 24  ? 0.1696 0.1753 0.2276 -0.0099 -0.0035 0.0061  24  VAL   B O   
4460 C  CB  . VAL   B 24  ? 0.1799 0.1732 0.2248 0.0021  -0.0180 0.0068  24  VAL   B CB  
4461 C  CG1 . VAL   B 24  ? 0.1779 0.1791 0.2588 -0.0081 -0.0209 -0.0028 24  VAL   B CG1 
4462 C  CG2 . VAL   B 24  ? 0.1901 0.2027 0.2257 0.0062  -0.0149 -0.0038 24  VAL   B CG2 
4472 N  N   . GLU   B 25  ? 0.1923 0.1765 0.2197 -0.0044 0.0069  0.0006  25  GLU   B N   
4473 C  CA  . GLU   B 25  ? 0.2065 0.2062 0.2440 0.0069  0.0159  -0.0092 25  GLU   B CA  
4474 C  C   . GLU   B 25  ? 0.2041 0.1974 0.2077 -0.0105 0.0208  -0.0010 25  GLU   B C   
4475 O  O   . GLU   B 25  ? 0.2138 0.2140 0.2230 -0.0141 0.0271  0.0014  25  GLU   B O   
4476 C  CB  . GLU   B 25  ? 0.2464 0.2570 0.3229 0.0378  0.0330  -0.0159 25  GLU   B CB  
4477 C  CG  . GLU   B 25  ? 0.2835 0.3163 0.4282 0.0436  0.0338  -0.0271 25  GLU   B CG  
4478 C  CD  . GLU   B 25  ? 0.3261 0.3760 0.5194 0.0345  0.0256  -0.0355 25  GLU   B CD  
4479 O  OE1 . GLU   B 25  ? 0.3498 0.4005 0.5452 0.0385  0.0327  -0.0358 25  GLU   B OE1 
4480 O  OE2 . GLU   B 25  ? 0.3458 0.3923 0.5482 0.0294  0.0122  -0.0447 25  GLU   B OE2 
4487 N  N   A GLU   B 26  ? 0.2017 0.1859 0.1906 -0.0218 0.0220  -0.0087 26  GLU   B N   
4488 N  N   B GLU   B 26  ? 0.1998 0.1883 0.1990 -0.0203 0.0151  0.0018  26  GLU   B N   
4489 C  CA  A GLU   B 26  ? 0.2075 0.2043 0.1960 -0.0335 0.0065  -0.0045 26  GLU   B CA  
4490 C  CA  B GLU   B 26  ? 0.1989 0.1965 0.2059 -0.0301 0.0007  0.0085  26  GLU   B CA  
4491 C  C   A GLU   B 26  ? 0.1880 0.2021 0.1765 -0.0267 0.0055  0.0114  26  GLU   B C   
4492 C  C   B GLU   B 26  ? 0.1847 0.1963 0.1823 -0.0254 0.0038  0.0161  26  GLU   B C   
4493 O  O   A GLU   B 26  ? 0.2036 0.2236 0.1835 -0.0241 0.0015  0.0175  26  GLU   B O   
4494 O  O   B GLU   B 26  ? 0.1955 0.2119 0.1857 -0.0235 0.0014  0.0194  26  GLU   B O   
4495 C  CB  A GLU   B 26  ? 0.2429 0.2246 0.2222 -0.0409 0.0198  0.0087  26  GLU   B CB  
4496 C  CB  B GLU   B 26  ? 0.2176 0.2041 0.2354 -0.0379 -0.0025 0.0212  26  GLU   B CB  
4497 C  CG  A GLU   B 26  ? 0.2830 0.2529 0.2853 -0.0410 0.0408  -0.0016 26  GLU   B CG  
4498 C  CG  B GLU   B 26  ? 0.2400 0.2181 0.2940 -0.0407 -0.0010 0.0119  26  GLU   B CG  
4499 C  CD  A GLU   B 26  ? 0.3062 0.2663 0.2973 -0.0580 0.0769  -0.0120 26  GLU   B CD  
4500 C  CD  B GLU   B 26  ? 0.2429 0.2157 0.3064 -0.0585 0.0005  -0.0058 26  GLU   B CD  
4501 O  OE1 A GLU   B 26  ? 0.3135 0.2536 0.2862 -0.0619 0.1284  -0.0078 26  GLU   B OE1 
4502 O  OE1 B GLU   B 26  ? 0.2347 0.2116 0.3414 -0.0759 0.0252  -0.0321 26  GLU   B OE1 
4503 O  OE2 A GLU   B 26  ? 0.3113 0.2843 0.3241 -0.0674 0.0830  0.0049  26  GLU   B OE2 
4504 O  OE2 B GLU   B 26  ? 0.2477 0.2131 0.3064 -0.0591 0.0011  0.0007  26  GLU   B OE2 
4517 N  N   . ALA   B 27  ? 0.1700 0.1845 0.1711 -0.0213 0.0094  0.0190  27  ALA   B N   
4518 C  CA  . ALA   B 27  ? 0.1632 0.1809 0.1901 -0.0158 -0.0040 0.0280  27  ALA   B CA  
4519 C  C   . ALA   B 27  ? 0.1668 0.1880 0.2063 -0.0187 0.0120  0.0374  27  ALA   B C   
4520 O  O   . ALA   B 27  ? 0.1824 0.2004 0.2228 -0.0070 0.0096  0.0482  27  ALA   B O   
4521 C  CB  . ALA   B 27  ? 0.1743 0.1613 0.1812 -0.0120 -0.0071 0.0289  27  ALA   B CB  
4528 N  N   . LYS   B 28  ? 0.1642 0.2124 0.2449 -0.0254 0.0168  0.0537  28  LYS   B N   
4529 C  CA  . LYS   B 28  ? 0.1844 0.2546 0.2747 -0.0156 0.0468  0.0822  28  LYS   B CA  
4530 C  C   . LYS   B 28  ? 0.2047 0.2726 0.2496 -0.0067 0.0620  0.0697  28  LYS   B C   
4531 O  O   . LYS   B 28  ? 0.2293 0.2852 0.2563 -0.0065 0.0648  0.0648  28  LYS   B O   
4532 C  CB  . LYS   B 28  ? 0.2053 0.2940 0.3395 -0.0005 0.0761  0.0969  28  LYS   B CB  
4533 C  CG  . LYS   B 28  ? 0.2333 0.3425 0.3880 0.0102  0.0881  0.1074  28  LYS   B CG  
4534 C  CD  . LYS   B 28  ? 0.2890 0.4020 0.4540 0.0189  0.0919  0.1091  28  LYS   B CD  
4535 C  CE  . LYS   B 28  ? 0.3352 0.4457 0.5116 0.0255  0.0919  0.1138  28  LYS   B CE  
4536 N  NZ  . LYS   B 28  ? 0.3587 0.4658 0.5341 0.0319  0.0875  0.1172  28  LYS   B NZ  
4550 N  N   . LYS   B 29  ? 0.2219 0.2945 0.2631 0.0089  0.0552  0.0543  29  LYS   B N   
4551 C  CA  . LYS   B 29  ? 0.2722 0.3324 0.2880 0.0099  0.0545  0.0499  29  LYS   B CA  
4552 C  C   . LYS   B 29  ? 0.2689 0.3266 0.2461 0.0058  0.0355  0.0589  29  LYS   B C   
4553 O  O   . LYS   B 29  ? 0.2946 0.3542 0.2572 0.0140  0.0386  0.0616  29  LYS   B O   
4554 C  CB  . LYS   B 29  ? 0.3314 0.3791 0.3797 0.0104  0.0566  0.0386  29  LYS   B CB  
4555 C  CG  . LYS   B 29  ? 0.3812 0.4181 0.4864 0.0091  0.0559  0.0328  29  LYS   B CG  
4556 C  CD  . LYS   B 29  ? 0.4279 0.4519 0.5699 0.0061  0.0625  0.0275  29  LYS   B CD  
4557 C  CE  . LYS   B 29  ? 0.4687 0.4815 0.6229 0.0026  0.0733  0.0254  29  LYS   B CE  
4558 N  NZ  . LYS   B 29  ? 0.4840 0.4896 0.6593 0.0004  0.0778  0.0248  29  LYS   B NZ  
4572 N  N   . VAL   B 30  ? 0.2337 0.2993 0.2361 -0.0122 0.0181  0.0577  30  VAL   B N   
4573 C  CA  . VAL   B 30  ? 0.2204 0.2819 0.2660 -0.0280 -0.0194 0.0646  30  VAL   B CA  
4574 C  C   . VAL   B 30  ? 0.1954 0.2691 0.2309 -0.0274 -0.0168 0.0743  30  VAL   B C   
4575 O  O   . VAL   B 30  ? 0.2046 0.2824 0.2388 -0.0226 -0.0183 0.0822  30  VAL   B O   
4576 C  CB  . VAL   B 30  ? 0.2307 0.2754 0.3366 -0.0508 -0.0407 0.0657  30  VAL   B CB  
4577 C  CG1 . VAL   B 30  ? 0.2469 0.2880 0.3472 -0.0433 -0.0250 0.0606  30  VAL   B CG1 
4578 C  CG2 . VAL   B 30  ? 0.2456 0.2773 0.3575 -0.0637 -0.0549 0.0452  30  VAL   B CG2 
4588 N  N   . LYS   B 31  ? 0.1915 0.2262 0.2530 -0.0403 -0.0169 0.0743  31  LYS   B N   
4589 C  CA  . LYS   B 31  ? 0.1780 0.2275 0.2944 -0.0396 -0.0191 0.0799  31  LYS   B CA  
4590 C  C   . LYS   B 31  ? 0.1728 0.1971 0.2599 -0.0402 -0.0310 0.0695  31  LYS   B C   
4591 O  O   . LYS   B 31  ? 0.1740 0.2084 0.2587 -0.0308 -0.0274 0.0759  31  LYS   B O   
4592 C  CB  . LYS   B 31  ? 0.1897 0.2815 0.3595 -0.0309 0.0178  0.1031  31  LYS   B CB  
4593 C  CG  . LYS   B 31  ? 0.2260 0.3284 0.4187 -0.0287 0.0385  0.1064  31  LYS   B CG  
4594 C  CD  . LYS   B 31  ? 0.2725 0.3854 0.4852 -0.0262 0.0443  0.0974  31  LYS   B CD  
4595 C  CE  . LYS   B 31  ? 0.3067 0.4221 0.5391 -0.0238 0.0414  0.0887  31  LYS   B CE  
4596 N  NZ  . LYS   B 31  ? 0.3371 0.4438 0.5557 -0.0171 0.0352  0.0804  31  LYS   B NZ  
4610 N  N   . PRO   B 32  ? 0.1900 0.1712 0.1968 -0.0391 -0.0419 0.0511  32  PRO   B N   
4611 C  CA  . PRO   B 32  ? 0.2007 0.1693 0.1720 -0.0408 -0.0442 0.0257  32  PRO   B CA  
4612 C  C   . PRO   B 32  ? 0.2072 0.1620 0.1761 -0.0445 -0.0545 0.0386  32  PRO   B C   
4613 O  O   . PRO   B 32  ? 0.2102 0.1589 0.2090 -0.0398 -0.0669 0.0328  32  PRO   B O   
4614 C  CB  . PRO   B 32  ? 0.2183 0.1639 0.1710 -0.0458 -0.0308 0.0172  32  PRO   B CB  
4615 C  CG  . PRO   B 32  ? 0.2287 0.1560 0.1594 -0.0334 -0.0478 0.0259  32  PRO   B CG  
4616 C  CD  . PRO   B 32  ? 0.2101 0.1599 0.1881 -0.0289 -0.0494 0.0301  32  PRO   B CD  
4624 N  N   . THR   B 33  ? 0.2091 0.1526 0.1683 -0.0406 -0.0456 0.0217  33  THR   B N   
4625 C  CA  . THR   B 33  ? 0.2099 0.1578 0.1578 -0.0410 -0.0495 0.0325  33  THR   B CA  
4626 C  C   . THR   B 33  ? 0.2081 0.1490 0.1597 -0.0396 -0.0462 0.0219  33  THR   B C   
4627 O  O   . THR   B 33  ? 0.2252 0.1517 0.1719 -0.0485 -0.0547 0.0277  33  THR   B O   
4628 C  CB  . THR   B 33  ? 0.2220 0.1702 0.1709 -0.0265 -0.0545 0.0325  33  THR   B CB  
4629 O  OG1 . THR   B 33  ? 0.2139 0.1781 0.1857 -0.0267 -0.0601 0.0306  33  THR   B OG1 
4630 C  CG2 . THR   B 33  ? 0.2466 0.1764 0.1868 -0.0178 -0.0507 0.0281  33  THR   B CG2 
4638 N  N   . VAL   B 34  ? 0.1923 0.1433 0.1513 -0.0386 -0.0464 0.0258  34  VAL   B N   
4639 C  CA  . VAL   B 34  ? 0.1799 0.1435 0.1479 -0.0320 -0.0384 0.0123  34  VAL   B CA  
4640 C  C   . VAL   B 34  ? 0.1683 0.1416 0.1290 -0.0312 -0.0260 0.0110  34  VAL   B C   
4641 O  O   . VAL   B 34  ? 0.1880 0.1461 0.1369 -0.0271 -0.0369 0.0075  34  VAL   B O   
4642 C  CB  . VAL   B 34  ? 0.1907 0.1574 0.1703 -0.0100 -0.0273 0.0067  34  VAL   B CB  
4643 C  CG1 . VAL   B 34  ? 0.1878 0.1715 0.1602 -0.0086 -0.0119 0.0016  34  VAL   B CG1 
4644 C  CG2 . VAL   B 34  ? 0.1887 0.1619 0.1928 -0.0122 -0.0251 0.0102  34  VAL   B CG2 
4654 N  N   . VAL   B 35  ? 0.1533 0.1354 0.1215 -0.0290 -0.0126 0.0046  35  VAL   B N   
4655 C  CA  . VAL   B 35  ? 0.1557 0.1363 0.1271 -0.0201 -0.0091 0.0120  35  VAL   B CA  
4656 C  C   . VAL   B 35  ? 0.1432 0.1259 0.1271 -0.0162 -0.0178 0.0015  35  VAL   B C   
4657 O  O   . VAL   B 35  ? 0.1454 0.1352 0.1295 -0.0203 -0.0035 -0.0020 35  VAL   B O   
4658 C  CB  . VAL   B 35  ? 0.1532 0.1528 0.1388 -0.0209 -0.0020 0.0023  35  VAL   B CB  
4659 C  CG1 . VAL   B 35  ? 0.1435 0.1689 0.1671 -0.0250 -0.0013 -0.0022 35  VAL   B CG1 
4660 C  CG2 . VAL   B 35  ? 0.1524 0.1495 0.1685 -0.0133 -0.0022 0.0087  35  VAL   B CG2 
4670 N  N   . VAL   B 36  ? 0.1433 0.1297 0.1247 -0.0153 -0.0158 0.0061  36  VAL   B N   
4671 C  CA  . VAL   B 36  ? 0.1393 0.1236 0.1211 -0.0113 -0.0069 -0.0004 36  VAL   B CA  
4672 C  C   . VAL   B 36  ? 0.1315 0.1302 0.1097 -0.0061 -0.0146 0.0060  36  VAL   B C   
4673 O  O   . VAL   B 36  ? 0.1447 0.1384 0.1438 -0.0109 -0.0067 -0.0033 36  VAL   B O   
4674 C  CB  . VAL   B 36  ? 0.1403 0.1367 0.1272 -0.0115 -0.0037 0.0029  36  VAL   B CB  
4675 C  CG1 . VAL   B 36  ? 0.1372 0.1455 0.1495 -0.0176 -0.0060 0.0044  36  VAL   B CG1 
4676 C  CG2 . VAL   B 36  ? 0.1483 0.1439 0.1357 -0.0133 -0.0190 0.0060  36  VAL   B CG2 
4686 N  N   . ASN   B 37  ? 0.1399 0.1324 0.1162 -0.0009 -0.0182 0.0098  37  ASN   B N   
4687 C  CA  . ASN   B 37  ? 0.1440 0.1389 0.1224 -0.0027 -0.0166 0.0058  37  ASN   B CA  
4688 C  C   . ASN   B 37  ? 0.1453 0.1414 0.1276 0.0034  -0.0140 0.0091  37  ASN   B C   
4689 O  O   . ASN   B 37  ? 0.1485 0.1426 0.1379 0.0015  0.0013  0.0100  37  ASN   B O   
4690 C  CB  . ASN   B 37  ? 0.1420 0.1365 0.1184 -0.0021 -0.0114 0.0008  37  ASN   B CB  
4691 C  CG  . ASN   B 37  ? 0.1472 0.1432 0.1245 0.0009  -0.0136 0.0003  37  ASN   B CG  
4692 O  OD1 . ASN   B 37  ? 0.1521 0.1460 0.1574 0.0137  -0.0193 0.0028  37  ASN   B OD1 
4693 N  ND2 . ASN   B 37  ? 0.1525 0.1415 0.1266 -0.0017 -0.0199 0.0062  37  ASN   B ND2 
4700 N  N   . ALA   B 38  ? 0.1560 0.1363 0.1347 0.0081  -0.0001 0.0056  38  ALA   B N   
4701 C  CA  . ALA   B 38  ? 0.1608 0.1437 0.1352 -0.0049 0.0018  0.0092  38  ALA   B CA  
4702 C  C   . ALA   B 38  ? 0.1545 0.1358 0.1374 0.0011  -0.0023 0.0177  38  ALA   B C   
4703 O  O   . ALA   B 38  ? 0.1672 0.1485 0.1553 0.0067  -0.0039 0.0131  38  ALA   B O   
4704 C  CB  . ALA   B 38  ? 0.1884 0.1510 0.1647 -0.0130 0.0085  0.0133  38  ALA   B CB  
4710 N  N   . ALA   B 39  ? 0.1566 0.1355 0.1283 0.0090  -0.0037 0.0076  39  ALA   B N   
4711 C  CA  . ALA   B 39  ? 0.1654 0.1407 0.1322 0.0043  -0.0096 -0.0036 39  ALA   B CA  
4712 C  C   . ALA   B 39  ? 0.1689 0.1458 0.1170 0.0102  -0.0088 0.0004  39  ALA   B C   
4713 O  O   . ALA   B 39  ? 0.1733 0.1533 0.1456 -0.0027 -0.0040 0.0058  39  ALA   B O   
4714 C  CB  . ALA   B 39  ? 0.1555 0.1447 0.1527 -0.0018 -0.0081 0.0066  39  ALA   B CB  
4720 N  N   . ASN   B 40  ? 0.1725 0.1650 0.1174 -0.0001 -0.0021 -0.0087 40  ASN   B N   
4721 C  CA  . ASN   B 40  ? 0.1732 0.1734 0.1428 0.0059  -0.0070 -0.0013 40  ASN   B CA  
4722 C  C   . ASN   B 40  ? 0.1803 0.1703 0.1232 0.0069  -0.0080 0.0065  40  ASN   B C   
4723 O  O   . ASN   B 40  ? 0.1774 0.1616 0.1276 0.0073  -0.0141 0.0010  40  ASN   B O   
4724 C  CB  . ASN   B 40  ? 0.1843 0.1691 0.1546 0.0118  -0.0157 0.0095  40  ASN   B CB  
4725 C  CG  . ASN   B 40  ? 0.1921 0.1766 0.1859 0.0073  -0.0229 0.0256  40  ASN   B CG  
4726 O  OD1 . ASN   B 40  ? 0.1913 0.1747 0.2690 0.0013  -0.0410 0.0291  40  ASN   B OD1 
4727 N  ND2 . ASN   B 40  ? 0.2041 0.1800 0.1900 0.0029  -0.0220 0.0189  40  ASN   B ND2 
4734 N  N   . VAL   B 41  ? 0.1892 0.1729 0.1266 0.0166  0.0012  0.0076  41  VAL   B N   
4735 C  CA  . VAL   B 41  ? 0.1922 0.1888 0.1436 0.0051  0.0039  -0.0030 41  VAL   B CA  
4736 C  C   . VAL   B 41  ? 0.1884 0.1903 0.1265 0.0140  -0.0041 -0.0054 41  VAL   B C   
4737 O  O   . VAL   B 41  ? 0.1843 0.1861 0.1424 0.0160  -0.0081 -0.0074 41  VAL   B O   
4738 C  CB  . VAL   B 41  ? 0.2083 0.2034 0.1712 -0.0045 0.0148  -0.0225 41  VAL   B CB  
4739 C  CG1 . VAL   B 41  ? 0.2016 0.2101 0.1961 -0.0044 0.0269  -0.0239 41  VAL   B CG1 
4740 C  CG2 . VAL   B 41  ? 0.2227 0.2228 0.1741 -0.0149 0.0184  -0.0072 41  VAL   B CG2 
4750 N  N   . TYR   B 42  ? 0.1996 0.1905 0.1319 0.0175  -0.0185 0.0018  42  TYR   B N   
4751 C  CA  . TYR   B 42  ? 0.2052 0.1915 0.1316 0.0182  -0.0300 -0.0119 42  TYR   B CA  
4752 C  C   . TYR   B 42  ? 0.1865 0.1734 0.1469 0.0195  -0.0271 -0.0057 42  TYR   B C   
4753 O  O   . TYR   B 42  ? 0.1771 0.1871 0.1830 0.0165  -0.0238 -0.0146 42  TYR   B O   
4754 C  CB  . TYR   B 42  ? 0.2252 0.2202 0.1682 0.0142  -0.0351 -0.0010 42  TYR   B CB  
4755 C  CG  . TYR   B 42  ? 0.2281 0.2323 0.1540 0.0018  -0.0353 0.0172  42  TYR   B CG  
4756 C  CD1 . TYR   B 42  ? 0.2213 0.2269 0.1336 -0.0061 -0.0144 0.0125  42  TYR   B CD1 
4757 C  CD2 . TYR   B 42  ? 0.2404 0.2380 0.1967 0.0039  -0.0209 0.0219  42  TYR   B CD2 
4758 C  CE1 . TYR   B 42  ? 0.2318 0.2425 0.1443 -0.0030 -0.0191 0.0155  42  TYR   B CE1 
4759 C  CE2 . TYR   B 42  ? 0.2382 0.2521 0.1835 0.0077  0.0075  0.0346  42  TYR   B CE2 
4760 C  CZ  . TYR   B 42  ? 0.2458 0.2617 0.1730 0.0139  0.0070  0.0184  42  TYR   B CZ  
4761 O  OH  . TYR   B 42  ? 0.2768 0.2891 0.2052 0.0263  0.0035  0.0276  42  TYR   B OH  
4771 N  N   . LEU   B 43  ? 0.1782 0.1575 0.1193 0.0042  -0.0202 -0.0137 43  LEU   B N   
4772 C  CA  . LEU   B 43  ? 0.1727 0.1595 0.1232 0.0037  -0.0235 -0.0077 43  LEU   B CA  
4773 C  C   . LEU   B 43  ? 0.1746 0.1601 0.1339 0.0017  -0.0206 -0.0052 43  LEU   B C   
4774 O  O   . LEU   B 43  ? 0.1731 0.1701 0.1679 0.0026  -0.0219 0.0075  43  LEU   B O   
4775 C  CB  . LEU   B 43  ? 0.1695 0.1538 0.1436 -0.0009 -0.0235 -0.0067 43  LEU   B CB  
4776 C  CG  . LEU   B 43  ? 0.1724 0.1474 0.1607 0.0024  -0.0210 -0.0073 43  LEU   B CG  
4777 C  CD1 . LEU   B 43  ? 0.1827 0.1568 0.1901 -0.0016 -0.0347 -0.0028 43  LEU   B CD1 
4778 C  CD2 . LEU   B 43  ? 0.1737 0.1510 0.1637 -0.0056 -0.0209 -0.0056 43  LEU   B CD2 
4790 N  N   . LYS   B 44  ? 0.1781 0.1601 0.1361 0.0081  -0.0179 0.0004  44  LYS   B N   
4791 C  CA  . LYS   B 44  ? 0.1948 0.1682 0.1444 0.0084  -0.0121 0.0050  44  LYS   B CA  
4792 C  C   . LYS   B 44  ? 0.1855 0.1582 0.1418 0.0160  -0.0210 -0.0061 44  LYS   B C   
4793 O  O   . LYS   B 44  ? 0.2009 0.1601 0.1716 0.0091  -0.0025 -0.0056 44  LYS   B O   
4794 C  CB  . LYS   B 44  ? 0.2199 0.1921 0.1586 0.0199  -0.0233 -0.0041 44  LYS   B CB  
4795 C  CG  . LYS   B 44  ? 0.2566 0.2191 0.1961 0.0130  -0.0474 0.0030  44  LYS   B CG  
4796 C  CD  . LYS   B 44  ? 0.2918 0.2394 0.2789 -0.0080 -0.0621 -0.0043 44  LYS   B CD  
4797 C  CE  . LYS   B 44  ? 0.3238 0.2622 0.3435 -0.0169 -0.0723 0.0113  44  LYS   B CE  
4798 N  NZ  . LYS   B 44  ? 0.3358 0.2698 0.3686 -0.0171 -0.0847 0.0283  44  LYS   B NZ  
4812 N  N   . HIS   B 45  ? 0.1735 0.1637 0.1379 0.0049  -0.0126 0.0085  45  HIS   B N   
4813 C  CA  . HIS   B 45  ? 0.1729 0.1633 0.1435 0.0052  -0.0179 -0.0004 45  HIS   B CA  
4814 C  C   . HIS   B 45  ? 0.1889 0.1817 0.1850 0.0174  -0.0261 -0.0026 45  HIS   B C   
4815 O  O   . HIS   B 45  ? 0.2024 0.2116 0.2404 0.0406  0.0036  -0.0040 45  HIS   B O   
4816 C  CB  . HIS   B 45  ? 0.1713 0.1636 0.1503 0.0030  -0.0077 -0.0115 45  HIS   B CB  
4817 C  CG  . HIS   B 45  ? 0.1693 0.1590 0.1586 -0.0018 -0.0164 -0.0060 45  HIS   B CG  
4818 N  ND1 . HIS   B 45  ? 0.1751 0.1492 0.1590 -0.0000 -0.0243 -0.0009 45  HIS   B ND1 
4819 C  CD2 . HIS   B 45  ? 0.1812 0.1621 0.1650 -0.0084 -0.0253 0.0017  45  HIS   B CD2 
4820 C  CE1 . HIS   B 45  ? 0.1824 0.1438 0.1441 -0.0010 -0.0309 -0.0023 45  HIS   B CE1 
4821 N  NE2 . HIS   B 45  ? 0.1876 0.1544 0.1568 -0.0004 -0.0263 -0.0058 45  HIS   B NE2 
4829 N  N   A GLY   B 46  ? 0.2004 0.1758 0.2193 0.0227  -0.0368 0.0103  46  GLY   B N   
4830 N  N   B GLY   B 46  ? 0.2010 0.1840 0.2040 0.0184  -0.0347 0.0128  46  GLY   B N   
4831 C  CA  A GLY   B 46  ? 0.2149 0.1859 0.2599 0.0146  -0.0398 0.0057  46  GLY   B CA  
4832 C  CA  B GLY   B 46  ? 0.2151 0.1943 0.2261 0.0121  -0.0380 0.0178  46  GLY   B CA  
4833 C  C   A GLY   B 46  ? 0.2163 0.1986 0.3075 0.0224  -0.0393 0.0137  46  GLY   B C   
4834 C  C   B GLY   B 46  ? 0.2225 0.2067 0.2573 0.0157  -0.0358 0.0310  46  GLY   B C   
4835 O  O   A GLY   B 46  ? 0.2164 0.2049 0.3907 0.0288  -0.0213 -0.0101 46  GLY   B O   
4836 O  O   B GLY   B 46  ? 0.2295 0.2139 0.2684 0.0181  -0.0235 0.0506  46  GLY   B O   
4843 N  N   . GLY   B 47  ? 0.2263 0.2141 0.2829 0.0029  -0.0265 0.0077  47  GLY   B N   
4844 C  CA  . GLY   B 47  ? 0.2210 0.1878 0.2417 -0.0026 -0.0257 0.0120  47  GLY   B CA  
4845 C  C   . GLY   B 47  ? 0.1974 0.1677 0.2028 -0.0031 -0.0124 0.0120  47  GLY   B C   
4846 O  O   . GLY   B 47  ? 0.2126 0.1537 0.2024 0.0021  -0.0117 0.0176  47  GLY   B O   
4851 N  N   . GLY   B 48  ? 0.1678 0.1552 0.2001 0.0035  -0.0132 0.0290  48  GLY   B N   
4852 C  CA  . GLY   B 48  ? 0.1650 0.1534 0.1977 -0.0029 -0.0133 0.0157  48  GLY   B CA  
4853 C  C   . GLY   B 48  ? 0.1575 0.1503 0.1804 0.0018  -0.0025 0.0054  48  GLY   B C   
4854 O  O   . GLY   B 48  ? 0.1496 0.1486 0.2060 0.0086  -0.0079 0.0123  48  GLY   B O   
4858 N  N   . VAL   B 49  ? 0.1532 0.1496 0.1756 0.0093  -0.0093 0.0045  49  VAL   B N   
4859 C  CA  . VAL   B 49  ? 0.1546 0.1591 0.1590 0.0125  -0.0114 -0.0131 49  VAL   B CA  
4860 C  C   . VAL   B 49  ? 0.1443 0.1520 0.1530 0.0112  -0.0106 -0.0052 49  VAL   B C   
4861 O  O   . VAL   B 49  ? 0.1567 0.1560 0.1602 0.0066  -0.0060 -0.0017 49  VAL   B O   
4862 C  CB  . VAL   B 49  ? 0.1613 0.1748 0.1922 0.0014  -0.0223 -0.0036 49  VAL   B CB  
4863 C  CG1 . VAL   B 49  ? 0.1610 0.1868 0.1856 0.0010  -0.0362 0.0033  49  VAL   B CG1 
4864 C  CG2 . VAL   B 49  ? 0.1811 0.1964 0.2188 -0.0053 -0.0411 -0.0139 49  VAL   B CG2 
4874 N  N   . ALA   B 50  ? 0.1477 0.1461 0.1473 0.0058  -0.0015 0.0032  50  ALA   B N   
4875 C  CA  . ALA   B 50  ? 0.1504 0.1379 0.1464 0.0108  -0.0132 0.0030  50  ALA   B CA  
4876 C  C   . ALA   B 50  ? 0.1590 0.1438 0.1449 -0.0005 -0.0091 0.0060  50  ALA   B C   
4877 O  O   . ALA   B 50  ? 0.1574 0.1458 0.1474 0.0040  -0.0037 0.0025  50  ALA   B O   
4878 C  CB  . ALA   B 50  ? 0.1631 0.1418 0.1554 -0.0016 -0.0086 0.0122  50  ALA   B CB  
4884 N  N   . GLY   B 51  ? 0.1592 0.1522 0.1588 0.0079  -0.0241 0.0110  51  GLY   B N   
4885 C  CA  . GLY   B 51  ? 0.1633 0.1579 0.1811 0.0156  -0.0203 0.0102  51  GLY   B CA  
4886 C  C   . GLY   B 51  ? 0.1604 0.1597 0.1776 0.0162  -0.0091 0.0036  51  GLY   B C   
4887 O  O   . GLY   B 51  ? 0.1528 0.1683 0.1928 0.0060  -0.0088 -0.0027 51  GLY   B O   
4891 N  N   . ALA   B 52  ? 0.1577 0.1477 0.1678 0.0130  -0.0049 -0.0006 52  ALA   B N   
4892 C  CA  . ALA   B 52  ? 0.1626 0.1559 0.1744 0.0176  -0.0019 -0.0094 52  ALA   B CA  
4893 C  C   . ALA   B 52  ? 0.1507 0.1512 0.1642 0.0092  -0.0075 -0.0074 52  ALA   B C   
4894 O  O   . ALA   B 52  ? 0.1475 0.1598 0.1912 0.0054  -0.0023 -0.0046 52  ALA   B O   
4895 C  CB  . ALA   B 52  ? 0.1746 0.1567 0.1749 0.0104  0.0040  -0.0108 52  ALA   B CB  
4901 N  N   . LEU   B 53  ? 0.1482 0.1496 0.1573 0.0160  -0.0090 0.0028  53  LEU   B N   
4902 C  CA  . LEU   B 53  ? 0.1496 0.1621 0.1407 0.0079  -0.0040 -0.0027 53  LEU   B CA  
4903 C  C   . LEU   B 53  ? 0.1519 0.1519 0.1497 0.0061  0.0014  0.0002  53  LEU   B C   
4904 O  O   . LEU   B 53  ? 0.1583 0.1613 0.1622 0.0005  0.0029  0.0087  53  LEU   B O   
4905 C  CB  . LEU   B 53  ? 0.1482 0.1640 0.1692 0.0087  -0.0014 0.0164  53  LEU   B CB  
4906 C  CG  . LEU   B 53  ? 0.1452 0.1726 0.1755 0.0056  -0.0080 0.0206  53  LEU   B CG  
4907 C  CD1 . LEU   B 53  ? 0.1559 0.1942 0.2074 0.0126  -0.0070 0.0072  53  LEU   B CD1 
4908 C  CD2 . LEU   B 53  ? 0.1667 0.2085 0.1921 -0.0038 -0.0090 -0.0160 53  LEU   B CD2 
4920 N  N   . ASN   B 54  ? 0.1548 0.1450 0.1401 0.0030  -0.0045 0.0034  54  ASN   B N   
4921 C  CA  . ASN   B 54  ? 0.1576 0.1570 0.1430 0.0030  -0.0044 -0.0072 54  ASN   B CA  
4922 C  C   . ASN   B 54  ? 0.1542 0.1604 0.1707 0.0029  0.0000  -0.0004 54  ASN   B C   
4923 O  O   . ASN   B 54  ? 0.1522 0.1642 0.1857 -0.0040 0.0027  -0.0016 54  ASN   B O   
4924 C  CB  . ASN   B 54  ? 0.1613 0.1759 0.1698 0.0069  -0.0004 -0.0068 54  ASN   B CB  
4925 C  CG  . ASN   B 54  ? 0.1577 0.1798 0.1659 0.0029  -0.0104 -0.0012 54  ASN   B CG  
4926 O  OD1 . ASN   B 54  ? 0.1527 0.1722 0.1908 0.0026  -0.0146 -0.0235 54  ASN   B OD1 
4927 N  ND2 . ASN   B 54  ? 0.1740 0.1885 0.1966 0.0031  -0.0286 0.0056  54  ASN   B ND2 
4934 N  N   . LYS   B 55  ? 0.1504 0.1616 0.1969 0.0074  -0.0076 -0.0007 55  LYS   B N   
4935 C  CA  . LYS   B 55  ? 0.1550 0.1775 0.2052 0.0158  -0.0076 -0.0097 55  LYS   B CA  
4936 C  C   . LYS   B 55  ? 0.1528 0.1754 0.2131 0.0130  0.0034  -0.0151 55  LYS   B C   
4937 O  O   . LYS   B 55  ? 0.1462 0.1946 0.2310 0.0129  0.0072  -0.0052 55  LYS   B O   
4938 C  CB  . LYS   B 55  ? 0.1693 0.1910 0.2605 0.0229  0.0077  -0.0092 55  LYS   B CB  
4939 C  CG  . LYS   B 55  ? 0.2147 0.2269 0.3487 0.0229  0.0142  0.0119  55  LYS   B CG  
4940 C  CD  . LYS   B 55  ? 0.2553 0.2536 0.4207 0.0352  0.0314  0.0311  55  LYS   B CD  
4941 C  CE  . LYS   B 55  ? 0.2763 0.2755 0.4842 0.0390  0.0482  0.0443  55  LYS   B CE  
4942 N  NZ  . LYS   B 55  ? 0.2787 0.2910 0.5182 0.0409  0.0306  0.0629  55  LYS   B NZ  
4956 N  N   . ALA   B 56  ? 0.1525 0.1758 0.1944 0.0112  -0.0003 -0.0131 56  ALA   B N   
4957 C  CA  . ALA   B 56  ? 0.1660 0.1946 0.1911 0.0061  0.0037  -0.0069 56  ALA   B CA  
4958 C  C   . ALA   B 56  ? 0.1699 0.1888 0.1918 0.0050  0.0128  -0.0021 56  ALA   B C   
4959 O  O   . ALA   B 56  ? 0.1817 0.1963 0.2039 0.0082  0.0319  -0.0024 56  ALA   B O   
4960 C  CB  . ALA   B 56  ? 0.1759 0.2086 0.1946 -0.0060 0.0001  -0.0106 56  ALA   B CB  
4966 N  N   . THR   B 57  ? 0.1560 0.1740 0.1965 0.0010  0.0197  -0.0013 57  THR   B N   
4967 C  CA  . THR   B 57  ? 0.1657 0.1751 0.1934 -0.0021 0.0232  -0.0059 57  THR   B CA  
4968 C  C   . THR   B 57  ? 0.1632 0.1881 0.2035 -0.0017 0.0224  -0.0057 57  THR   B C   
4969 O  O   . THR   B 57  ? 0.1688 0.1878 0.2171 -0.0154 0.0187  -0.0034 57  THR   B O   
4970 C  CB  . THR   B 57  ? 0.1766 0.1640 0.1567 -0.0027 0.0132  0.0072  57  THR   B CB  
4971 O  OG1 . THR   B 57  ? 0.1753 0.1592 0.1867 -0.0077 0.0103  0.0053  57  THR   B OG1 
4972 C  CG2 . THR   B 57  ? 0.1721 0.1727 0.1655 -0.0030 0.0151  0.0054  57  THR   B CG2 
4980 N  N   . ASN   B 58  ? 0.1513 0.2090 0.2352 -0.0110 0.0164  -0.0263 58  ASN   B N   
4981 C  CA  . ASN   B 58  ? 0.1680 0.2585 0.2749 -0.0258 0.0369  -0.0201 58  ASN   B CA  
4982 C  C   . ASN   B 58  ? 0.1514 0.2337 0.2414 -0.0184 0.0049  -0.0226 58  ASN   B C   
4983 O  O   . ASN   B 58  ? 0.1585 0.2419 0.2560 -0.0187 0.0015  -0.0289 58  ASN   B O   
4984 C  CB  . ASN   B 58  ? 0.2685 0.3464 0.3803 -0.0427 0.0767  -0.0071 58  ASN   B CB  
4985 C  CG  . ASN   B 58  ? 0.4020 0.4422 0.5262 -0.0444 0.1019  0.0168  58  ASN   B CG  
4986 O  OD1 . ASN   B 58  ? 0.4216 0.4616 0.5800 -0.0433 0.1049  0.0230  58  ASN   B OD1 
4987 N  ND2 . ASN   B 58  ? 0.5211 0.5211 0.5766 -0.0450 0.1129  0.0209  58  ASN   B ND2 
4994 N  N   . ASN   B 59  ? 0.1574 0.2161 0.2066 -0.0169 -0.0099 -0.0197 59  ASN   B N   
4995 C  CA  . ASN   B 59  ? 0.1585 0.2173 0.2038 -0.0107 -0.0200 -0.0090 59  ASN   B CA  
4996 C  C   . ASN   B 59  ? 0.1560 0.2037 0.1871 -0.0162 -0.0213 -0.0180 59  ASN   B C   
4997 O  O   . ASN   B 59  ? 0.1580 0.2030 0.1964 -0.0111 -0.0138 -0.0140 59  ASN   B O   
4998 C  CB  . ASN   B 59  ? 0.1672 0.2360 0.2109 -0.0046 -0.0295 -0.0045 59  ASN   B CB  
4999 C  CG  . ASN   B 59  ? 0.1796 0.2424 0.2202 0.0012  -0.0400 0.0026  59  ASN   B CG  
5000 O  OD1 . ASN   B 59  ? 0.1835 0.2445 0.2218 0.0003  -0.0279 0.0202  59  ASN   B OD1 
5001 N  ND2 . ASN   B 59  ? 0.1941 0.2497 0.2333 -0.0008 -0.0511 -0.0088 59  ASN   B ND2 
5008 N  N   . ALA   B 60  ? 0.1629 0.1905 0.1927 -0.0171 0.0017  -0.0185 60  ALA   B N   
5009 C  CA  . ALA   B 60  ? 0.1672 0.1839 0.1965 -0.0215 0.0047  -0.0029 60  ALA   B CA  
5010 C  C   . ALA   B 60  ? 0.1663 0.1691 0.1718 -0.0127 -0.0100 -0.0033 60  ALA   B C   
5011 O  O   . ALA   B 60  ? 0.1711 0.1664 0.1966 -0.0198 -0.0000 -0.0118 60  ALA   B O   
5012 C  CB  . ALA   B 60  ? 0.1817 0.1872 0.2175 -0.0174 0.0116  0.0013  60  ALA   B CB  
5018 N  N   . MET   B 61  ? 0.1582 0.1624 0.1771 -0.0092 -0.0028 -0.0031 61  MET   B N   
5019 C  CA  . MET   B 61  ? 0.1523 0.1559 0.1637 -0.0083 -0.0080 -0.0078 61  MET   B CA  
5020 C  C   . MET   B 61  ? 0.1567 0.1552 0.1569 -0.0108 -0.0115 -0.0003 61  MET   B C   
5021 O  O   . MET   B 61  ? 0.1629 0.1533 0.1560 -0.0046 -0.0049 -0.0154 61  MET   B O   
5022 C  CB  . MET   B 61  ? 0.1483 0.1578 0.1609 -0.0007 -0.0058 -0.0034 61  MET   B CB  
5023 C  CG  . MET   B 61  ? 0.1468 0.1608 0.1708 -0.0026 -0.0145 0.0025  61  MET   B CG  
5024 S  SD  . MET   B 61  ? 0.1528 0.1609 0.1829 -0.0033 -0.0096 -0.0123 61  MET   B SD  
5025 C  CE  . MET   B 61  ? 0.1611 0.1840 0.2073 -0.0010 -0.0092 -0.0236 61  MET   B CE  
5035 N  N   . GLN   B 62  ? 0.1556 0.1614 0.1534 -0.0044 -0.0250 -0.0015 62  GLN   B N   
5036 C  CA  . GLN   B 62  ? 0.1596 0.1667 0.1618 -0.0007 -0.0213 -0.0021 62  GLN   B CA  
5037 C  C   . GLN   B 62  ? 0.1609 0.1692 0.1616 -0.0005 -0.0278 -0.0137 62  GLN   B C   
5038 O  O   . GLN   B 62  ? 0.1724 0.1742 0.1671 -0.0042 -0.0240 -0.0193 62  GLN   B O   
5039 C  CB  . GLN   B 62  ? 0.1647 0.1697 0.1665 0.0027  -0.0170 0.0055  62  GLN   B CB  
5040 C  CG  . GLN   B 62  ? 0.1699 0.1749 0.1678 0.0014  -0.0230 -0.0069 62  GLN   B CG  
5041 C  CD  . GLN   B 62  ? 0.1672 0.1722 0.1574 0.0023  -0.0225 0.0025  62  GLN   B CD  
5042 O  OE1 . GLN   B 62  ? 0.1727 0.1650 0.1955 -0.0011 -0.0289 -0.0108 62  GLN   B OE1 
5043 N  NE2 . GLN   B 62  ? 0.1679 0.1756 0.1603 0.0081  -0.0245 -0.0122 62  GLN   B NE2 
5052 N  N   . VAL   B 63  ? 0.1601 0.1682 0.1824 -0.0088 -0.0276 -0.0164 63  VAL   B N   
5053 C  CA  . VAL   B 63  ? 0.1719 0.1737 0.2088 -0.0099 -0.0257 -0.0016 63  VAL   B CA  
5054 C  C   . VAL   B 63  ? 0.1756 0.1633 0.1789 -0.0223 -0.0283 -0.0240 63  VAL   B C   
5055 O  O   . VAL   B 63  ? 0.1888 0.1626 0.1850 -0.0135 -0.0380 -0.0263 63  VAL   B O   
5056 C  CB  . VAL   B 63  ? 0.1667 0.1856 0.2431 -0.0172 -0.0279 -0.0126 63  VAL   B CB  
5057 C  CG1 . VAL   B 63  ? 0.1750 0.1895 0.2520 -0.0250 -0.0206 -0.0115 63  VAL   B CG1 
5058 C  CG2 . VAL   B 63  ? 0.1619 0.2033 0.2567 -0.0112 -0.0327 -0.0133 63  VAL   B CG2 
5068 N  N   . GLU   B 64  ? 0.1711 0.1587 0.1761 -0.0124 -0.0216 -0.0212 64  GLU   B N   
5069 C  CA  . GLU   B 64  ? 0.1667 0.1514 0.1774 -0.0117 -0.0225 -0.0110 64  GLU   B CA  
5070 C  C   . GLU   B 64  ? 0.1582 0.1523 0.1693 -0.0031 -0.0325 -0.0187 64  GLU   B C   
5071 O  O   . GLU   B 64  ? 0.1709 0.1600 0.1566 -0.0044 -0.0216 -0.0176 64  GLU   B O   
5072 C  CB  . GLU   B 64  ? 0.1695 0.1599 0.1790 -0.0159 -0.0203 -0.0021 64  GLU   B CB  
5073 C  CG  . GLU   B 64  ? 0.1777 0.1612 0.1829 -0.0251 -0.0219 -0.0169 64  GLU   B CG  
5074 C  CD  . GLU   B 64  ? 0.1799 0.1794 0.1927 -0.0340 -0.0250 -0.0106 64  GLU   B CD  
5075 O  OE1 . GLU   B 64  ? 0.1808 0.2014 0.2047 -0.0358 -0.0109 -0.0346 64  GLU   B OE1 
5076 O  OE2 . GLU   B 64  ? 0.2012 0.1880 0.1915 -0.0342 -0.0272 -0.0069 64  GLU   B OE2 
5083 N  N   . SER   B 65  ? 0.1623 0.1500 0.1564 -0.0057 -0.0245 -0.0226 65  SER   B N   
5084 C  CA  . SER   B 65  ? 0.1594 0.1513 0.1574 -0.0006 -0.0249 -0.0169 65  SER   B CA  
5085 C  C   . SER   B 65  ? 0.1674 0.1528 0.1514 0.0014  -0.0267 -0.0116 65  SER   B C   
5086 O  O   . SER   B 65  ? 0.1774 0.1630 0.1576 -0.0005 -0.0234 -0.0186 65  SER   B O   
5087 C  CB  . SER   B 65  ? 0.1635 0.1541 0.1656 -0.0089 -0.0188 -0.0141 65  SER   B CB  
5088 O  OG  . SER   B 65  ? 0.1723 0.1608 0.1628 -0.0070 -0.0198 -0.0270 65  SER   B OG  
5094 N  N   . ASP   B 66  ? 0.1795 0.1552 0.1496 -0.0021 -0.0293 -0.0224 66  ASP   B N   
5095 C  CA  . ASP   B 66  ? 0.1883 0.1687 0.1540 0.0029  -0.0373 -0.0162 66  ASP   B CA  
5096 C  C   . ASP   B 66  ? 0.1939 0.1751 0.1447 -0.0056 -0.0270 -0.0245 66  ASP   B C   
5097 O  O   . ASP   B 66  ? 0.1961 0.1816 0.1571 0.0009  -0.0240 -0.0271 66  ASP   B O   
5098 C  CB  . ASP   B 66  ? 0.2029 0.1779 0.1725 0.0089  -0.0471 -0.0242 66  ASP   B CB  
5099 C  CG  . ASP   B 66  ? 0.2219 0.1945 0.2064 0.0209  -0.0584 -0.0089 66  ASP   B CG  
5100 O  OD1 . ASP   B 66  ? 0.2465 0.1883 0.2205 0.0128  -0.0472 0.0015  66  ASP   B OD1 
5101 O  OD2 . ASP   B 66  ? 0.2385 0.2245 0.2822 0.0469  -0.0509 -0.0083 66  ASP   B OD2 
5106 N  N   . ASP   B 67  ? 0.1852 0.1675 0.1461 -0.0093 -0.0242 -0.0225 67  ASP   B N   
5107 C  CA  . ASP   B 67  ? 0.1968 0.1598 0.1698 -0.0084 -0.0223 -0.0075 67  ASP   B CA  
5108 C  C   . ASP   B 67  ? 0.1947 0.1587 0.1739 0.0022  -0.0167 -0.0160 67  ASP   B C   
5109 O  O   . ASP   B 67  ? 0.1990 0.1693 0.1767 0.0017  -0.0145 -0.0312 67  ASP   B O   
5110 C  CB  . ASP   B 67  ? 0.2168 0.1688 0.1903 -0.0169 -0.0385 -0.0144 67  ASP   B CB  
5111 C  CG  . ASP   B 67  ? 0.2589 0.1755 0.2029 -0.0147 -0.0611 -0.0115 67  ASP   B CG  
5112 O  OD1 . ASP   B 67  ? 0.2794 0.1806 0.2216 -0.0118 -0.0665 -0.0023 67  ASP   B OD1 
5113 O  OD2 . ASP   B 67  ? 0.2752 0.1870 0.2275 0.0029  -0.0693 -0.0113 67  ASP   B OD2 
5118 N  N   . TYR   B 68  ? 0.1892 0.1606 0.1655 0.0032  -0.0323 -0.0270 68  TYR   B N   
5119 C  CA  . TYR   B 68  ? 0.1853 0.1754 0.1846 0.0153  -0.0327 -0.0344 68  TYR   B CA  
5120 C  C   . TYR   B 68  ? 0.1815 0.1694 0.1792 0.0083  -0.0271 -0.0357 68  TYR   B C   
5121 O  O   . TYR   B 68  ? 0.1885 0.1777 0.1897 0.0106  -0.0277 -0.0443 68  TYR   B O   
5122 C  CB  . TYR   B 68  ? 0.1871 0.1981 0.1922 0.0124  -0.0454 -0.0511 68  TYR   B CB  
5123 C  CG  . TYR   B 68  ? 0.2021 0.2165 0.1992 0.0194  -0.0339 -0.0686 68  TYR   B CG  
5124 C  CD1 . TYR   B 68  ? 0.2046 0.2253 0.2200 -0.0050 -0.0240 -0.0730 68  TYR   B CD1 
5125 C  CD2 . TYR   B 68  ? 0.2061 0.2413 0.2181 0.0290  -0.0542 -0.0548 68  TYR   B CD2 
5126 C  CE1 . TYR   B 68  ? 0.2070 0.2378 0.2448 -0.0009 -0.0241 -0.0736 68  TYR   B CE1 
5127 C  CE2 . TYR   B 68  ? 0.2070 0.2455 0.2316 0.0248  -0.0394 -0.0752 68  TYR   B CE2 
5128 C  CZ  . TYR   B 68  ? 0.2008 0.2469 0.2444 0.0057  -0.0357 -0.0804 68  TYR   B CZ  
5129 O  OH  . TYR   B 68  ? 0.1930 0.2673 0.2773 -0.0039 -0.0265 -0.0638 68  TYR   B OH  
5139 N  N   . ILE   B 69  ? 0.1831 0.1676 0.1660 0.0087  -0.0345 -0.0354 69  ILE   B N   
5140 C  CA  . ILE   B 69  ? 0.1898 0.1720 0.1751 -0.0024 -0.0259 -0.0349 69  ILE   B CA  
5141 C  C   . ILE   B 69  ? 0.1834 0.1708 0.1792 0.0091  -0.0259 -0.0257 69  ILE   B C   
5142 O  O   . ILE   B 69  ? 0.1902 0.1878 0.1609 0.0065  -0.0182 -0.0344 69  ILE   B O   
5143 C  CB  . ILE   B 69  ? 0.1960 0.1721 0.1941 -0.0004 0.0011  -0.0286 69  ILE   B CB  
5144 C  CG1 . ILE   B 69  ? 0.1947 0.1771 0.2083 -0.0038 0.0136  -0.0286 69  ILE   B CG1 
5145 C  CG2 . ILE   B 69  ? 0.2136 0.1846 0.2082 0.0046  0.0062  -0.0267 69  ILE   B CG2 
5146 C  CD1 . ILE   B 69  ? 0.1943 0.1892 0.2253 -0.0230 0.0142  -0.0358 69  ILE   B CD1 
5158 N  N   . ALA   B 70  ? 0.1819 0.1727 0.1794 0.0037  -0.0275 -0.0265 70  ALA   B N   
5159 C  CA  . ALA   B 70  ? 0.1849 0.1769 0.1646 0.0018  -0.0374 -0.0305 70  ALA   B CA  
5160 C  C   . ALA   B 70  ? 0.1988 0.1774 0.1695 -0.0026 -0.0327 -0.0400 70  ALA   B C   
5161 O  O   . ALA   B 70  ? 0.2135 0.1771 0.1797 0.0038  -0.0387 -0.0387 70  ALA   B O   
5162 C  CB  . ALA   B 70  ? 0.1879 0.1934 0.1768 0.0015  -0.0336 -0.0346 70  ALA   B CB  
5168 N  N   . THR   B 71  ? 0.2010 0.1792 0.1857 0.0021  -0.0461 -0.0328 71  THR   B N   
5169 C  CA  . THR   B 71  ? 0.2161 0.1766 0.2162 0.0070  -0.0598 -0.0324 71  THR   B CA  
5170 C  C   . THR   B 71  ? 0.2059 0.1733 0.2427 0.0299  -0.0564 -0.0501 71  THR   B C   
5171 O  O   . THR   B 71  ? 0.2184 0.1808 0.2871 0.0270  -0.0504 -0.0669 71  THR   B O   
5172 C  CB  . THR   B 71  ? 0.2453 0.1999 0.2458 -0.0029 -0.0675 -0.0078 71  THR   B CB  
5173 O  OG1 . THR   B 71  ? 0.2599 0.2290 0.2787 -0.0234 -0.0662 0.0178  71  THR   B OG1 
5174 C  CG2 . THR   B 71  ? 0.2612 0.1929 0.2792 0.0012  -0.0575 0.0027  71  THR   B CG2 
5182 N  N   . ASN   B 72  ? 0.1920 0.1775 0.2273 0.0191  -0.0633 -0.0638 72  ASN   B N   
5183 C  CA  . ASN   B 72  ? 0.1926 0.1904 0.2415 0.0192  -0.0450 -0.0719 72  ASN   B CA  
5184 C  C   . ASN   B 72  ? 0.1929 0.2048 0.2465 0.0010  -0.0235 -0.0655 72  ASN   B C   
5185 O  O   . ASN   B 72  ? 0.1889 0.2221 0.2708 0.0066  -0.0056 -0.0699 72  ASN   B O   
5186 C  CB  . ASN   B 72  ? 0.2012 0.2088 0.2477 0.0189  -0.0552 -0.0604 72  ASN   B CB  
5187 C  CG  . ASN   B 72  ? 0.2171 0.2248 0.2528 0.0264  -0.0628 -0.0359 72  ASN   B CG  
5188 O  OD1 . ASN   B 72  ? 0.2408 0.2408 0.2480 0.0137  -0.0517 -0.0398 72  ASN   B OD1 
5189 N  ND2 . ASN   B 72  ? 0.2247 0.2353 0.3045 0.0433  -0.0528 0.0027  72  ASN   B ND2 
5196 N  N   . GLY   B 73  ? 0.1981 0.2036 0.2176 0.0018  -0.0297 -0.0706 73  GLY   B N   
5197 C  CA  . GLY   B 73  ? 0.1931 0.2140 0.2055 0.0001  -0.0180 -0.0571 73  GLY   B CA  
5198 C  C   . GLY   B 73  ? 0.1859 0.2085 0.1659 0.0044  -0.0220 -0.0437 73  GLY   B C   
5199 O  O   . GLY   B 73  ? 0.1829 0.1961 0.1691 0.0067  -0.0187 -0.0369 73  GLY   B O   
5203 N  N   . PRO   B 74  ? 0.1861 0.2188 0.1458 0.0033  -0.0275 -0.0395 74  PRO   B N   
5204 C  CA  . PRO   B 74  ? 0.1818 0.2203 0.1284 0.0093  -0.0178 -0.0237 74  PRO   B CA  
5205 C  C   . PRO   B 74  ? 0.1688 0.2031 0.1273 0.0029  -0.0157 -0.0121 74  PRO   B C   
5206 O  O   . PRO   B 74  ? 0.1732 0.2076 0.1914 0.0044  -0.0117 -0.0238 74  PRO   B O   
5207 C  CB  . PRO   B 74  ? 0.2015 0.2407 0.1406 0.0017  -0.0241 -0.0159 74  PRO   B CB  
5208 C  CG  . PRO   B 74  ? 0.2242 0.2528 0.1663 0.0021  -0.0126 -0.0139 74  PRO   B CG  
5209 C  CD  . PRO   B 74  ? 0.2178 0.2400 0.1580 0.0057  -0.0147 -0.0227 74  PRO   B CD  
5217 N  N   . LEU   B 75  ? 0.1672 0.1923 0.1298 -0.0013 -0.0184 -0.0209 75  LEU   B N   
5218 C  CA  . LEU   B 75  ? 0.1727 0.1895 0.1310 -0.0032 -0.0176 -0.0010 75  LEU   B CA  
5219 C  C   . LEU   B 75  ? 0.1778 0.1973 0.1376 0.0058  -0.0005 0.0031  75  LEU   B C   
5220 O  O   . LEU   B 75  ? 0.1917 0.2136 0.1569 -0.0018 -0.0037 0.0105  75  LEU   B O   
5221 C  CB  . LEU   B 75  ? 0.1761 0.1919 0.1193 -0.0127 -0.0178 0.0055  75  LEU   B CB  
5222 C  CG  . LEU   B 75  ? 0.2098 0.2094 0.1515 -0.0361 -0.0107 0.0052  75  LEU   B CG  
5223 C  CD1 . LEU   B 75  ? 0.2488 0.2300 0.1488 -0.0467 0.0151  -0.0013 75  LEU   B CD1 
5224 C  CD2 . LEU   B 75  ? 0.2518 0.2312 0.2393 -0.0251 0.0105  0.0178  75  LEU   B CD2 
5236 N  N   . LYS   B 76  ? 0.1747 0.2087 0.1694 0.0021  0.0032  0.0131  76  LYS   B N   
5237 C  CA  . LYS   B 76  ? 0.1894 0.2152 0.1864 -0.0080 0.0199  0.0025  76  LYS   B CA  
5238 C  C   . LYS   B 76  ? 0.1838 0.2030 0.1634 -0.0078 0.0139  0.0241  76  LYS   B C   
5239 O  O   . LYS   B 76  ? 0.1948 0.1829 0.1699 -0.0081 0.0097  0.0229  76  LYS   B O   
5240 C  CB  . LYS   B 76  ? 0.2065 0.2201 0.2386 -0.0111 0.0293  -0.0211 76  LYS   B CB  
5241 C  CG  . LYS   B 76  ? 0.2123 0.2344 0.2646 -0.0051 0.0179  -0.0227 76  LYS   B CG  
5242 C  CD  . LYS   B 76  ? 0.2152 0.2368 0.2973 -0.0004 0.0130  -0.0338 76  LYS   B CD  
5243 C  CE  . LYS   B 76  ? 0.2181 0.2498 0.3513 0.0039  -0.0031 -0.0388 76  LYS   B CE  
5244 N  NZ  . LYS   B 76  ? 0.2200 0.2557 0.3785 -0.0012 -0.0248 -0.0537 76  LYS   B NZ  
5258 N  N   . VAL   B 77  ? 0.1892 0.2156 0.1673 -0.0037 0.0044  0.0294  77  VAL   B N   
5259 C  CA  . VAL   B 77  ? 0.1927 0.2076 0.1826 0.0020  0.0046  0.0526  77  VAL   B CA  
5260 C  C   . VAL   B 77  ? 0.1784 0.1843 0.1683 0.0034  0.0303  0.0317  77  VAL   B C   
5261 O  O   . VAL   B 77  ? 0.1813 0.1916 0.1724 0.0137  0.0335  0.0254  77  VAL   B O   
5262 C  CB  . VAL   B 77  ? 0.2080 0.2174 0.2124 -0.0010 0.0159  0.0661  77  VAL   B CB  
5263 C  CG1 . VAL   B 77  ? 0.2094 0.2101 0.2394 -0.0074 0.0157  0.0780  77  VAL   B CG1 
5264 C  CG2 . VAL   B 77  ? 0.2218 0.2323 0.2203 -0.0052 -0.0048 0.0672  77  VAL   B CG2 
5274 N  N   . GLY   B 78  ? 0.1685 0.1761 0.1677 0.0037  0.0208  0.0275  78  GLY   B N   
5275 C  CA  . GLY   B 78  ? 0.1746 0.1666 0.1645 0.0022  0.0235  0.0206  78  GLY   B CA  
5276 C  C   . GLY   B 78  ? 0.1699 0.1652 0.1588 0.0060  0.0171  0.0252  78  GLY   B C   
5277 O  O   . GLY   B 78  ? 0.1682 0.1651 0.1773 0.0119  0.0147  0.0239  78  GLY   B O   
5281 N  N   . GLY   B 79  ? 0.1558 0.1686 0.1627 0.0071  0.0114  0.0203  79  GLY   B N   
5282 C  CA  . GLY   B 79  ? 0.1609 0.1577 0.1554 0.0052  0.0160  0.0201  79  GLY   B CA  
5283 C  C   . GLY   B 79  ? 0.1524 0.1481 0.1612 0.0099  0.0074  0.0157  79  GLY   B C   
5284 O  O   . GLY   B 79  ? 0.1562 0.1535 0.1735 0.0073  0.0125  0.0189  79  GLY   B O   
5288 N  N   . SER   B 80  ? 0.1546 0.1464 0.1540 0.0049  0.0155  0.0105  80  SER   B N   
5289 C  CA  . SER   B 80  ? 0.1440 0.1468 0.1525 0.0025  0.0042  0.0079  80  SER   B CA  
5290 C  C   . SER   B 80  ? 0.1475 0.1405 0.1511 0.0053  -0.0001 0.0091  80  SER   B C   
5291 O  O   . SER   B 80  ? 0.1577 0.1476 0.1807 0.0070  0.0056  0.0005  80  SER   B O   
5292 C  CB  . SER   B 80  ? 0.1486 0.1503 0.1628 0.0026  0.0059  0.0060  80  SER   B CB  
5293 O  OG  . SER   B 80  ? 0.1563 0.1715 0.1826 -0.0073 -0.0078 0.0131  80  SER   B OG  
5299 N  N   . CYS   B 81  ? 0.1493 0.1360 0.1597 0.0034  0.0012  -0.0025 81  CYS   B N   
5300 C  CA  . CYS   B 81  ? 0.1538 0.1306 0.1642 0.0014  -0.0050 0.0018  81  CYS   B CA  
5301 C  C   . CYS   B 81  ? 0.1508 0.1337 0.1392 -0.0025 -0.0185 -0.0007 81  CYS   B C   
5302 O  O   . CYS   B 81  ? 0.1714 0.1318 0.1578 0.0057  -0.0039 -0.0017 81  CYS   B O   
5303 C  CB  . CYS   B 81  ? 0.1622 0.1487 0.1573 -0.0115 -0.0101 0.0030  81  CYS   B CB  
5304 S  SG  . CYS   B 81  ? 0.1678 0.1690 0.1532 -0.0056 -0.0239 -0.0073 81  CYS   B SG  
5310 N  N   . VAL   B 82  ? 0.1520 0.1323 0.1531 -0.0018 -0.0104 -0.0017 82  VAL   B N   
5311 C  CA  . VAL   B 82  ? 0.1650 0.1352 0.1449 -0.0050 -0.0107 0.0119  82  VAL   B CA  
5312 C  C   . VAL   B 82  ? 0.1717 0.1303 0.1547 -0.0070 -0.0052 0.0026  82  VAL   B C   
5313 O  O   . VAL   B 82  ? 0.1752 0.1283 0.1990 -0.0053 -0.0034 -0.0152 82  VAL   B O   
5314 C  CB  . VAL   B 82  ? 0.1670 0.1553 0.1752 -0.0052 -0.0171 0.0140  82  VAL   B CB  
5315 C  CG1 . VAL   B 82  ? 0.1878 0.1832 0.1790 -0.0019 -0.0169 0.0223  82  VAL   B CG1 
5316 C  CG2 . VAL   B 82  ? 0.1778 0.1701 0.1970 -0.0134 -0.0348 0.0224  82  VAL   B CG2 
5326 N  N   . LEU   B 83  ? 0.1569 0.1301 0.1546 -0.0155 -0.0192 -0.0026 83  LEU   B N   
5327 C  CA  . LEU   B 83  ? 0.1560 0.1386 0.1487 -0.0129 -0.0170 -0.0010 83  LEU   B CA  
5328 C  C   . LEU   B 83  ? 0.1554 0.1349 0.1511 -0.0166 -0.0244 0.0036  83  LEU   B C   
5329 O  O   . LEU   B 83  ? 0.1598 0.1463 0.1331 -0.0200 -0.0147 0.0019  83  LEU   B O   
5330 C  CB  . LEU   B 83  ? 0.1595 0.1496 0.1505 -0.0130 -0.0192 -0.0090 83  LEU   B CB  
5331 C  CG  . LEU   B 83  ? 0.1788 0.1683 0.1557 -0.0160 -0.0132 -0.0075 83  LEU   B CG  
5332 C  CD1 . LEU   B 83  ? 0.1913 0.1758 0.1538 -0.0120 -0.0234 -0.0003 83  LEU   B CD1 
5333 C  CD2 . LEU   B 83  ? 0.2017 0.1657 0.1826 -0.0081 -0.0225 -0.0228 83  LEU   B CD2 
5345 N  N   . SER   B 84  ? 0.1614 0.1491 0.1773 -0.0269 -0.0264 0.0071  84  SER   B N   
5346 C  CA  . SER   B 84  ? 0.1640 0.1721 0.1601 -0.0308 -0.0096 0.0180  84  SER   B CA  
5347 C  C   . SER   B 84  ? 0.1487 0.1852 0.1149 -0.0188 -0.0180 0.0200  84  SER   B C   
5348 O  O   . SER   B 84  ? 0.1627 0.1694 0.1250 -0.0193 -0.0118 0.0043  84  SER   B O   
5349 C  CB  . SER   B 84  ? 0.1822 0.1806 0.2020 -0.0291 0.0116  0.0142  84  SER   B CB  
5350 O  OG  . SER   B 84  ? 0.1765 0.1890 0.2380 -0.0367 0.0056  0.0199  84  SER   B OG  
5356 N  N   . GLY   B 85  ? 0.1547 0.2005 0.1282 -0.0227 -0.0144 0.0235  85  GLY   B N   
5357 C  CA  . GLY   B 85  ? 0.1606 0.2053 0.1618 -0.0337 -0.0011 -0.0146 85  GLY   B CA  
5358 C  C   . GLY   B 85  ? 0.1570 0.1909 0.1376 -0.0367 -0.0060 0.0083  85  GLY   B C   
5359 O  O   . GLY   B 85  ? 0.1698 0.1816 0.1518 -0.0487 0.0148  -0.0133 85  GLY   B O   
5363 N  N   . HIS   B 86  ? 0.1503 0.1705 0.1614 -0.0339 -0.0101 0.0107  86  HIS   B N   
5364 C  CA  . HIS   B 86  ? 0.1592 0.1746 0.1760 -0.0300 -0.0171 0.0078  86  HIS   B CA  
5365 C  C   . HIS   B 86  ? 0.1577 0.1887 0.1584 -0.0411 -0.0046 0.0227  86  HIS   B C   
5366 O  O   . HIS   B 86  ? 0.1694 0.1969 0.1685 -0.0301 0.0073  0.0247  86  HIS   B O   
5367 C  CB  . HIS   B 86  ? 0.1685 0.1856 0.1775 -0.0194 -0.0261 -0.0011 86  HIS   B CB  
5368 C  CG  . HIS   B 86  ? 0.1662 0.1968 0.1673 -0.0070 -0.0241 0.0026  86  HIS   B CG  
5369 N  ND1 . HIS   B 86  ? 0.1773 0.2221 0.2013 -0.0235 -0.0087 -0.0195 86  HIS   B ND1 
5370 C  CD2 . HIS   B 86  ? 0.1752 0.2024 0.1665 -0.0026 -0.0169 -0.0014 86  HIS   B CD2 
5371 C  CE1 . HIS   B 86  ? 0.1882 0.2183 0.1971 -0.0095 -0.0018 -0.0323 86  HIS   B CE1 
5372 N  NE2 . HIS   B 86  ? 0.1871 0.2087 0.1750 0.0077  -0.0099 -0.0069 86  HIS   B NE2 
5380 N  N   . ASN   B 87  ? 0.1569 0.1853 0.1755 -0.0303 0.0052  0.0108  87  ASN   B N   
5381 C  CA  . ASN   B 87  ? 0.1729 0.2060 0.1722 -0.0284 0.0368  0.0131  87  ASN   B CA  
5382 C  C   . ASN   B 87  ? 0.1880 0.1911 0.1466 -0.0255 0.0411  0.0108  87  ASN   B C   
5383 O  O   . ASN   B 87  ? 0.2183 0.2025 0.1896 -0.0178 0.0558  -0.0002 87  ASN   B O   
5384 C  CB  . ASN   B 87  ? 0.1758 0.2423 0.2214 -0.0201 0.0350  0.0144  87  ASN   B CB  
5385 C  CG  . ASN   B 87  ? 0.1819 0.2585 0.2206 0.0088  0.0328  0.0294  87  ASN   B CG  
5386 O  OD1 . ASN   B 87  ? 0.1708 0.2394 0.2051 0.0139  0.0480  0.0334  87  ASN   B OD1 
5387 N  ND2 . ASN   B 87  ? 0.2150 0.2738 0.2607 0.0173  0.0432  0.0290  87  ASN   B ND2 
5394 N  N   . LEU   B 88  ? 0.1805 0.1757 0.1348 -0.0285 0.0164  0.0099  88  LEU   B N   
5395 C  CA  . LEU   B 88  ? 0.1973 0.1699 0.1451 -0.0331 -0.0030 -0.0017 88  LEU   B CA  
5396 C  C   . LEU   B 88  ? 0.1903 0.1646 0.1511 -0.0384 -0.0091 -0.0032 88  LEU   B C   
5397 O  O   . LEU   B 88  ? 0.2150 0.1750 0.1815 -0.0252 -0.0356 -0.0118 88  LEU   B O   
5398 C  CB  . LEU   B 88  ? 0.2141 0.1808 0.1609 -0.0422 -0.0094 0.0138  88  LEU   B CB  
5399 C  CG  . LEU   B 88  ? 0.2471 0.2086 0.1865 -0.0377 -0.0287 0.0256  88  LEU   B CG  
5400 C  CD1 . LEU   B 88  ? 0.2583 0.2324 0.2175 -0.0495 -0.0221 0.0486  88  LEU   B CD1 
5401 C  CD2 . LEU   B 88  ? 0.2815 0.2341 0.2536 -0.0041 -0.0605 0.0007  88  LEU   B CD2 
5413 N  N   . ALA   B 89  ? 0.1705 0.1696 0.1404 -0.0434 0.0213  -0.0035 89  ALA   B N   
5414 C  CA  . ALA   B 89  ? 0.1725 0.1617 0.1279 -0.0384 0.0079  0.0083  89  ALA   B CA  
5415 C  C   . ALA   B 89  ? 0.1808 0.1621 0.1345 -0.0436 0.0131  0.0030  89  ALA   B C   
5416 O  O   . ALA   B 89  ? 0.1528 0.1709 0.1789 -0.0399 0.0108  -0.0257 89  ALA   B O   
5417 C  CB  . ALA   B 89  ? 0.1593 0.1619 0.1539 -0.0311 -0.0016 0.0168  89  ALA   B CB  
5423 N  N   . LYS   B 90  ? 0.2127 0.1519 0.1367 -0.0463 -0.0105 0.0093  90  LYS   B N   
5424 C  CA  . LYS   B 90  ? 0.2184 0.1488 0.1313 -0.0427 -0.0158 0.0102  90  LYS   B CA  
5425 C  C   . LYS   B 90  ? 0.1941 0.1392 0.1446 -0.0327 -0.0123 0.0011  90  LYS   B C   
5426 O  O   . LYS   B 90  ? 0.1937 0.1553 0.1580 -0.0427 -0.0027 0.0043  90  LYS   B O   
5427 C  CB  . LYS   B 90  ? 0.2294 0.1588 0.1638 -0.0341 -0.0115 0.0206  90  LYS   B CB  
5428 C  CG  . LYS   B 90  ? 0.2200 0.1783 0.1737 -0.0203 0.0084  0.0102  90  LYS   B CG  
5429 C  CD  . LYS   B 90  ? 0.2408 0.1933 0.2213 -0.0028 0.0180  0.0033  90  LYS   B CD  
5430 C  CE  . LYS   B 90  ? 0.2502 0.2041 0.2651 -0.0056 0.0191  0.0011  90  LYS   B CE  
5431 N  NZ  . LYS   B 90  ? 0.2535 0.1934 0.2389 -0.0140 0.0416  -0.0040 90  LYS   B NZ  
5445 N  N   . HIS   B 91  ? 0.1737 0.1348 0.1347 -0.0285 -0.0162 0.0140  91  HIS   B N   
5446 C  CA  . HIS   B 91  ? 0.1632 0.1341 0.1447 -0.0231 -0.0163 0.0055  91  HIS   B CA  
5447 C  C   . HIS   B 91  ? 0.1528 0.1373 0.1208 -0.0208 -0.0081 0.0112  91  HIS   B C   
5448 O  O   . HIS   B 91  ? 0.1667 0.1424 0.1275 -0.0246 -0.0213 -0.0020 91  HIS   B O   
5449 C  CB  . HIS   B 91  ? 0.1765 0.1381 0.1830 -0.0077 -0.0139 0.0137  91  HIS   B CB  
5450 C  CG  . HIS   B 91  ? 0.2177 0.1615 0.2448 0.0003  0.0186  0.0218  91  HIS   B CG  
5451 N  ND1 . HIS   B 91  ? 0.2484 0.1632 0.3087 0.0009  0.0251  0.0168  91  HIS   B ND1 
5452 C  CD2 . HIS   B 91  ? 0.2312 0.1907 0.3107 0.0141  0.0023  0.0558  91  HIS   B CD2 
5453 C  CE1 . HIS   B 91  ? 0.2512 0.1810 0.3286 0.0150  0.0241  0.0198  91  HIS   B CE1 
5454 N  NE2 . HIS   B 91  ? 0.2493 0.1957 0.3380 0.0235  0.0153  0.0647  91  HIS   B NE2 
5462 N  N   . CYS   B 92  ? 0.1489 0.1354 0.1208 -0.0237 -0.0109 0.0005  92  CYS   B N   
5463 C  CA  . CYS   B 92  ? 0.1462 0.1360 0.1304 -0.0161 -0.0045 0.0002  92  CYS   B CA  
5464 C  C   . CYS   B 92  ? 0.1460 0.1287 0.1274 -0.0142 -0.0086 0.0006  92  CYS   B C   
5465 O  O   . CYS   B 92  ? 0.1522 0.1356 0.1404 -0.0127 -0.0031 0.0019  92  CYS   B O   
5466 C  CB  . CYS   B 92  ? 0.1467 0.1416 0.1376 -0.0141 -0.0055 0.0028  92  CYS   B CB  
5467 S  SG  . CYS   B 92  ? 0.1498 0.1427 0.1479 -0.0114 -0.0109 0.0052  92  CYS   B SG  
5473 N  N   . LEU   B 93  ? 0.1398 0.1315 0.1277 -0.0182 -0.0068 -0.0032 93  LEU   B N   
5474 C  CA  . LEU   B 93  ? 0.1384 0.1303 0.1257 -0.0087 -0.0131 0.0049  93  LEU   B CA  
5475 C  C   . LEU   B 93  ? 0.1333 0.1316 0.1223 -0.0050 -0.0080 0.0118  93  LEU   B C   
5476 O  O   . LEU   B 93  ? 0.1442 0.1261 0.1441 -0.0052 -0.0098 0.0008  93  LEU   B O   
5477 C  CB  . LEU   B 93  ? 0.1441 0.1312 0.1324 -0.0015 -0.0083 0.0063  93  LEU   B CB  
5478 C  CG  . LEU   B 93  ? 0.1424 0.1437 0.1553 -0.0067 -0.0129 0.0183  93  LEU   B CG  
5479 C  CD1 . LEU   B 93  ? 0.1458 0.1536 0.1731 0.0027  -0.0026 0.0010  93  LEU   B CD1 
5480 C  CD2 . LEU   B 93  ? 0.1444 0.1422 0.1679 -0.0033 -0.0190 0.0033  93  LEU   B CD2 
5492 N  N   . HIS   B 94  ? 0.1418 0.1329 0.1172 -0.0058 -0.0137 0.0098  94  HIS   B N   
5493 C  CA  . HIS   B 94  ? 0.1447 0.1280 0.1228 -0.0006 -0.0056 0.0085  94  HIS   B CA  
5494 C  C   . HIS   B 94  ? 0.1452 0.1294 0.1312 0.0006  -0.0093 0.0103  94  HIS   B C   
5495 O  O   . HIS   B 94  ? 0.1423 0.1360 0.1892 -0.0049 0.0144  -0.0068 94  HIS   B O   
5496 C  CB  . HIS   B 94  ? 0.1426 0.1374 0.1423 -0.0024 -0.0164 -0.0037 94  HIS   B CB  
5497 C  CG  . HIS   B 94  ? 0.1398 0.1306 0.1493 -0.0072 -0.0266 0.0006  94  HIS   B CG  
5498 N  ND1 . HIS   B 94  ? 0.1493 0.1346 0.1387 -0.0038 -0.0193 -0.0010 94  HIS   B ND1 
5499 C  CD2 . HIS   B 94  ? 0.1416 0.1396 0.1514 -0.0048 -0.0163 -0.0002 94  HIS   B CD2 
5500 C  CE1 . HIS   B 94  ? 0.1518 0.1386 0.1441 -0.0067 -0.0200 0.0056  94  HIS   B CE1 
5501 N  NE2 . HIS   B 94  ? 0.1435 0.1431 0.1513 -0.0132 -0.0157 0.0043  94  HIS   B NE2 
5509 N  N   . VAL   B 95  ? 0.1374 0.1236 0.1407 0.0003  -0.0045 0.0089  95  VAL   B N   
5510 C  CA  . VAL   B 95  ? 0.1320 0.1386 0.1331 -0.0023 -0.0014 0.0146  95  VAL   B CA  
5511 C  C   . VAL   B 95  ? 0.1463 0.1364 0.1262 -0.0005 0.0089  0.0183  95  VAL   B C   
5512 O  O   . VAL   B 95  ? 0.1522 0.1326 0.1607 0.0083  0.0026  0.0242  95  VAL   B O   
5513 C  CB  . VAL   B 95  ? 0.1442 0.1340 0.1421 -0.0027 -0.0125 0.0067  95  VAL   B CB  
5514 C  CG1 . VAL   B 95  ? 0.1585 0.1544 0.1656 -0.0080 -0.0036 0.0127  95  VAL   B CG1 
5515 C  CG2 . VAL   B 95  ? 0.1504 0.1345 0.1444 0.0051  -0.0132 0.0060  95  VAL   B CG2 
5525 N  N   . VAL   B 96  ? 0.1571 0.1382 0.1374 0.0077  0.0075  0.0176  96  VAL   B N   
5526 C  CA  . VAL   B 96  ? 0.1627 0.1541 0.1381 0.0059  0.0054  0.0211  96  VAL   B CA  
5527 C  C   . VAL   B 96  ? 0.1685 0.1523 0.1614 0.0077  0.0095  0.0213  96  VAL   B C   
5528 O  O   . VAL   B 96  ? 0.1677 0.1593 0.1737 -0.0030 0.0195  0.0075  96  VAL   B O   
5529 C  CB  . VAL   B 96  ? 0.1663 0.1756 0.1355 0.0104  -0.0011 0.0124  96  VAL   B CB  
5530 C  CG1 . VAL   B 96  ? 0.1665 0.1959 0.1559 0.0136  0.0078  0.0108  96  VAL   B CG1 
5531 C  CG2 . VAL   B 96  ? 0.1766 0.1713 0.1545 0.0067  0.0173  0.0012  96  VAL   B CG2 
5541 N  N   . GLY   B 97  ? 0.1733 0.1545 0.1446 0.0008  0.0022  0.0338  97  GLY   B N   
5542 C  CA  . GLY   B 97  ? 0.2002 0.1615 0.1509 0.0030  0.0069  0.0248  97  GLY   B CA  
5543 C  C   . GLY   B 97  ? 0.2293 0.1684 0.1737 0.0094  0.0140  0.0301  97  GLY   B C   
5544 O  O   . GLY   B 97  ? 0.2459 0.1742 0.1720 0.0097  0.0026  0.0196  97  GLY   B O   
5548 N  N   . PRO   B 98  ? 0.2460 0.1749 0.1943 0.0174  0.0453  0.0428  98  PRO   B N   
5549 C  CA  . PRO   B 98  ? 0.2680 0.1987 0.2106 0.0347  0.0655  0.0462  98  PRO   B CA  
5550 C  C   . PRO   B 98  ? 0.2771 0.1968 0.1754 0.0545  0.0666  0.0605  98  PRO   B C   
5551 O  O   . PRO   B 98  ? 0.2602 0.1886 0.1961 0.0349  0.0595  0.0540  98  PRO   B O   
5552 C  CB  . PRO   B 98  ? 0.2657 0.2121 0.2423 0.0300  0.0826  0.0590  98  PRO   B CB  
5553 C  CG  . PRO   B 98  ? 0.2487 0.1959 0.2461 0.0196  0.0753  0.0700  98  PRO   B CG  
5554 C  CD  . PRO   B 98  ? 0.2363 0.1747 0.2360 0.0255  0.0626  0.0587  98  PRO   B CD  
5562 N  N   . ASN   B 99  ? 0.2952 0.2202 0.1867 0.0772  0.0691  0.0481  99  ASN   B N   
5563 C  CA  . ASN   B 99  ? 0.3158 0.2408 0.1862 0.0963  0.0661  0.0665  99  ASN   B CA  
5564 C  C   . ASN   B 99  ? 0.3390 0.2761 0.2124 0.1066  0.1030  0.0924  99  ASN   B C   
5565 O  O   . ASN   B 99  ? 0.3648 0.2934 0.2339 0.1062  0.0980  0.0944  99  ASN   B O   
5566 C  CB  . ASN   B 99  ? 0.3252 0.2406 0.1919 0.0883  0.0411  0.0565  99  ASN   B CB  
5567 C  CG  . ASN   B 99  ? 0.3269 0.2422 0.2065 0.0813  0.0374  0.0455  99  ASN   B CG  
5568 O  OD1 . ASN   B 99  ? 0.3223 0.2365 0.2399 0.0889  0.0471  0.0509  99  ASN   B OD1 
5569 N  ND2 . ASN   B 99  ? 0.3303 0.2464 0.2078 0.0760  0.0125  0.0326  99  ASN   B ND2 
5576 N  N   . VAL   B 100 ? 0.3543 0.2906 0.2793 0.0929  0.1129  0.1194  100 VAL   B N   
5577 C  CA  . VAL   B 100 ? 0.3829 0.3174 0.3506 0.0730  0.1030  0.1463  100 VAL   B CA  
5578 C  C   . VAL   B 100 ? 0.4137 0.3277 0.3331 0.0750  0.0982  0.1805  100 VAL   B C   
5579 O  O   . VAL   B 100 ? 0.4286 0.3469 0.3578 0.0728  0.1174  0.1708  100 VAL   B O   
5580 C  CB  . VAL   B 100 ? 0.3865 0.3304 0.4307 0.0407  0.0912  0.1565  100 VAL   B CB  
5581 C  CG1 . VAL   B 100 ? 0.3918 0.3373 0.4616 0.0386  0.0851  0.1573  100 VAL   B CG1 
5582 C  CG2 . VAL   B 100 ? 0.3845 0.3354 0.4560 0.0241  0.0867  0.1598  100 VAL   B CG2 
5592 N  N   . ASN   B 101 ? 0.4367 0.3372 0.3363 0.0782  0.0619  0.1793  101 ASN   B N   
5593 C  CA  . ASN   B 101 ? 0.4725 0.3578 0.3361 0.0681  0.0275  0.1787  101 ASN   B CA  
5594 C  C   . ASN   B 101 ? 0.5306 0.4199 0.3656 0.0561  0.0108  0.1657  101 ASN   B C   
5595 O  O   . ASN   B 101 ? 0.5317 0.4274 0.3779 0.0628  0.0110  0.1402  101 ASN   B O   
5596 C  CB  . ASN   B 101 ? 0.4554 0.3336 0.3492 0.0613  0.0202  0.1521  101 ASN   B CB  
5597 C  CG  . ASN   B 101 ? 0.4386 0.3083 0.3520 0.0574  0.0191  0.1474  101 ASN   B CG  
5598 O  OD1 . ASN   B 101 ? 0.4343 0.3039 0.3851 0.0488  0.0382  0.1337  101 ASN   B OD1 
5599 N  ND2 . ASN   B 101 ? 0.4316 0.3038 0.3434 0.0559  0.0154  0.1330  101 ASN   B ND2 
5606 N  N   A LYS   B 102 ? 0.5605 0.4512 0.4006 0.0443  0.0092  0.1553  102 LYS   B N   
5607 N  N   B LYS   B 102 ? 0.5561 0.4508 0.4014 0.0461  0.0073  0.1522  102 LYS   B N   
5608 C  CA  A LYS   B 102 ? 0.5870 0.4845 0.4382 0.0306  0.0108  0.1336  102 LYS   B CA  
5609 C  CA  B LYS   B 102 ? 0.5788 0.4818 0.4374 0.0354  0.0074  0.1315  102 LYS   B CA  
5610 C  C   A LYS   B 102 ? 0.5918 0.4917 0.4177 0.0344  0.0174  0.1475  102 LYS   B C   
5611 C  C   B LYS   B 102 ? 0.5862 0.4905 0.4231 0.0365  0.0174  0.1448  102 LYS   B C   
5612 O  O   A LYS   B 102 ? 0.5992 0.4947 0.4252 0.0338  0.0075  0.1481  102 LYS   B O   
5613 O  O   B LYS   B 102 ? 0.5911 0.4935 0.4291 0.0358  0.0102  0.1461  102 LYS   B O   
5614 C  CB  A LYS   B 102 ? 0.6047 0.5081 0.5042 0.0149  0.0152  0.0906  102 LYS   B CB  
5615 C  CB  B LYS   B 102 ? 0.5911 0.5015 0.4930 0.0253  0.0046  0.0927  102 LYS   B CB  
5616 C  CG  A LYS   B 102 ? 0.6197 0.5287 0.5613 0.0015  0.0208  0.0521  102 LYS   B CG  
5617 C  CG  B LYS   B 102 ? 0.6010 0.5183 0.5395 0.0171  0.0035  0.0581  102 LYS   B CG  
5618 C  CD  A LYS   B 102 ? 0.6337 0.5462 0.6237 -0.0089 0.0274  0.0218  102 LYS   B CD  
5619 C  CD  B LYS   B 102 ? 0.6100 0.5326 0.5921 0.0107  0.0044  0.0303  102 LYS   B CD  
5620 C  CE  A LYS   B 102 ? 0.6439 0.5581 0.6616 -0.0168 0.0322  -0.0017 102 LYS   B CE  
5621 C  CE  B LYS   B 102 ? 0.6162 0.5425 0.6224 0.0060  0.0049  0.0096  102 LYS   B CE  
5622 N  NZ  A LYS   B 102 ? 0.6501 0.5650 0.6870 -0.0204 0.0334  -0.0164 102 LYS   B NZ  
5623 N  NZ  B LYS   B 102 ? 0.6201 0.5485 0.6454 0.0036  0.0044  -0.0028 102 LYS   B NZ  
5650 N  N   . GLY   B 103 ? 0.5864 0.4940 0.4210 0.0392  0.0374  0.1484  103 GLY   B N   
5651 C  CA  . GLY   B 103 ? 0.5781 0.4982 0.4397 0.0501  0.0751  0.1381  103 GLY   B CA  
5652 C  C   . GLY   B 103 ? 0.5660 0.4974 0.4481 0.0598  0.1098  0.1291  103 GLY   B C   
5653 O  O   . GLY   B 103 ? 0.5708 0.5040 0.4557 0.0584  0.1202  0.1374  103 GLY   B O   
5658 N  N   . GLU   B 104 ? 0.5447 0.4850 0.4236 0.0714  0.1346  0.1074  104 GLU   B N   
5659 C  CA  . GLU   B 104 ? 0.5210 0.4712 0.4026 0.0858  0.1509  0.0819  104 GLU   B CA  
5660 C  C   . GLU   B 104 ? 0.5154 0.4707 0.4229 0.0642  0.1981  0.0895  104 GLU   B C   
5661 O  O   . GLU   B 104 ? 0.5191 0.4762 0.4508 0.0595  0.2038  0.0953  104 GLU   B O   
5662 C  CB  . GLU   B 104 ? 0.5102 0.4567 0.3933 0.1221  0.1062  0.0376  104 GLU   B CB  
5663 C  CG  . GLU   B 104 ? 0.5017 0.4479 0.3720 0.1566  0.0577  -0.0079 104 GLU   B CG  
5664 C  CD  . GLU   B 104 ? 0.4967 0.4425 0.3414 0.1850  0.0127  -0.0410 104 GLU   B CD  
5665 O  OE1 . GLU   B 104 ? 0.4915 0.4342 0.2754 0.1995  0.0184  -0.0564 104 GLU   B OE1 
5666 O  OE2 . GLU   B 104 ? 0.4961 0.4481 0.3435 0.1912  -0.0265 -0.0485 104 GLU   B OE2 
5673 N  N   . ASP   B 105 ? 0.5007 0.4613 0.3962 0.0490  0.2292  0.0891  105 ASP   B N   
5674 C  CA  . ASP   B 105 ? 0.4910 0.4537 0.4096 0.0307  0.2427  0.0694  105 ASP   B CA  
5675 C  C   . ASP   B 105 ? 0.4598 0.4117 0.3744 0.0031  0.2231  0.0547  105 ASP   B C   
5676 O  O   . ASP   B 105 ? 0.4442 0.4018 0.3704 0.0102  0.2346  0.0599  105 ASP   B O   
5677 C  CB  . ASP   B 105 ? 0.5092 0.4839 0.4880 0.0431  0.2582  0.0568  105 ASP   B CB  
5678 C  CG  . ASP   B 105 ? 0.5202 0.5096 0.5621 0.0489  0.2851  0.0503  105 ASP   B CG  
5679 O  OD1 . ASP   B 105 ? 0.5189 0.5167 0.5647 0.0456  0.3142  0.0634  105 ASP   B OD1 
5680 O  OD2 . ASP   B 105 ? 0.5257 0.5191 0.6138 0.0557  0.2727  0.0358  105 ASP   B OD2 
5685 N  N   A ILE   B 106 ? 0.4487 0.3859 0.3825 -0.0167 0.2048  0.0487  106 ILE   B N   
5686 N  N   B ILE   B 106 ? 0.4532 0.4019 0.3844 -0.0056 0.1807  0.0410  106 ILE   B N   
5687 C  CA  A ILE   B 106 ? 0.4256 0.3565 0.3893 -0.0413 0.2014  0.0380  106 ILE   B CA  
5688 C  CA  B ILE   B 106 ? 0.4389 0.3888 0.3962 -0.0164 0.1468  0.0239  106 ILE   B CA  
5689 C  C   A ILE   B 106 ? 0.3862 0.3395 0.3744 -0.0475 0.2079  0.0296  106 ILE   B C   
5690 C  C   B ILE   B 106 ? 0.4125 0.3768 0.3945 -0.0164 0.1337  0.0140  106 ILE   B C   
5691 O  O   A ILE   B 106 ? 0.3715 0.3200 0.3670 -0.0540 0.2047  0.0316  106 ILE   B O   
5692 O  O   B ILE   B 106 ? 0.4102 0.3698 0.3981 -0.0190 0.1306  0.0127  106 ILE   B O   
5693 C  CB  A ILE   B 106 ? 0.4414 0.3452 0.4075 -0.0583 0.1855  0.0350  106 ILE   B CB  
5694 C  CB  B ILE   B 106 ? 0.4487 0.3873 0.4071 -0.0261 0.1273  0.0161  106 ILE   B CB  
5695 C  CG1 A ILE   B 106 ? 0.4470 0.3402 0.4122 -0.0573 0.1699  0.0264  106 ILE   B CG1 
5696 C  CG1 B ILE   B 106 ? 0.4514 0.3848 0.4075 -0.0261 0.1136  0.0095  106 ILE   B CG1 
5697 C  CG2 A ILE   B 106 ? 0.4478 0.3471 0.4300 -0.0667 0.1815  0.0339  106 ILE   B CG2 
5698 C  CG2 B ILE   B 106 ? 0.4535 0.3906 0.4203 -0.0309 0.1226  0.0139  106 ILE   B CG2 
5699 C  CD1 A ILE   B 106 ? 0.4494 0.3385 0.4049 -0.0539 0.1629  0.0250  106 ILE   B CD1 
5700 C  CD1 B ILE   B 106 ? 0.4524 0.3835 0.4041 -0.0248 0.1058  0.0062  106 ILE   B CD1 
5723 N  N   A GLN   B 107 ? 0.3635 0.3433 0.3860 -0.0493 0.1983  0.0314  107 GLN   B N   
5724 N  N   B GLN   B 107 ? 0.3893 0.3718 0.4016 -0.0161 0.1239  0.0115  107 GLN   B N   
5725 C  CA  A GLN   B 107 ? 0.3419 0.3471 0.3978 -0.0445 0.1636  0.0238  107 GLN   B CA  
5726 C  CA  B GLN   B 107 ? 0.3655 0.3640 0.4023 -0.0148 0.1069  0.0106  107 GLN   B CA  
5727 C  C   A GLN   B 107 ? 0.3061 0.3206 0.3624 -0.0296 0.1338  0.0126  107 GLN   B C   
5728 C  C   B GLN   B 107 ? 0.3229 0.3322 0.3608 -0.0103 0.1083  0.0087  107 GLN   B C   
5729 O  O   A GLN   B 107 ? 0.2916 0.3215 0.3876 -0.0213 0.1040  -0.0143 107 GLN   B O   
5730 O  O   B GLN   B 107 ? 0.3174 0.3334 0.3711 -0.0057 0.0922  -0.0031 107 GLN   B O   
5731 C  CB  A GLN   B 107 ? 0.3749 0.3849 0.4716 -0.0407 0.1224  0.0181  107 GLN   B CB  
5732 C  CB  B GLN   B 107 ? 0.3888 0.3895 0.4581 -0.0142 0.0812  0.0097  107 GLN   B CB  
5733 C  CG  A GLN   B 107 ? 0.4070 0.4172 0.5347 -0.0350 0.0797  0.0137  107 GLN   B CG  
5734 C  CG  B GLN   B 107 ? 0.4096 0.4111 0.5072 -0.0123 0.0548  0.0091  107 GLN   B CG  
5735 C  CD  A GLN   B 107 ? 0.4300 0.4408 0.5837 -0.0334 0.0504  0.0138  107 GLN   B CD  
5736 C  CD  B GLN   B 107 ? 0.4249 0.4268 0.5467 -0.0123 0.0354  0.0098  107 GLN   B CD  
5737 O  OE1 A GLN   B 107 ? 0.4397 0.4505 0.6000 -0.0329 0.0456  0.0111  107 GLN   B OE1 
5738 O  OE1 B GLN   B 107 ? 0.4308 0.4330 0.5581 -0.0125 0.0321  0.0090  107 GLN   B OE1 
5739 N  NE2 A GLN   B 107 ? 0.4378 0.4474 0.6005 -0.0301 0.0370  0.0163  107 GLN   B NE2 
5740 N  NE2 B GLN   B 107 ? 0.4301 0.4315 0.5609 -0.0105 0.0269  0.0111  107 GLN   B NE2 
5757 N  N   . LEU   B 108 ? 0.2820 0.3007 0.3200 -0.0003 0.1214  0.0131  108 LEU   B N   
5758 C  CA  . LEU   B 108 ? 0.2482 0.2630 0.2540 0.0188  0.0906  0.0303  108 LEU   B CA  
5759 C  C   . LEU   B 108 ? 0.2015 0.2104 0.2531 0.0175  0.0471  0.0244  108 LEU   B C   
5760 O  O   . LEU   B 108 ? 0.1936 0.1960 0.2298 0.0167  0.0354  0.0261  108 LEU   B O   
5761 C  CB  . LEU   B 108 ? 0.2673 0.2854 0.2453 0.0230  0.0944  0.0544  108 LEU   B CB  
5762 C  CG  . LEU   B 108 ? 0.2862 0.3189 0.2566 0.0318  0.0780  0.0379  108 LEU   B CG  
5763 C  CD1 . LEU   B 108 ? 0.2994 0.3371 0.2544 0.0300  0.0771  0.0364  108 LEU   B CD1 
5764 C  CD2 . LEU   B 108 ? 0.2979 0.3308 0.2613 0.0357  0.0491  0.0155  108 LEU   B CD2 
5777 N  N   . LEU   B 109 ? 0.1824 0.1793 0.2443 0.0060  0.0328  0.0176  109 LEU   B N   
5778 C  CA  . LEU   B 109 ? 0.1618 0.1582 0.2540 0.0034  0.0361  0.0244  109 LEU   B CA  
5779 C  C   . LEU   B 109 ? 0.1571 0.1457 0.2481 -0.0009 0.0292  0.0177  109 LEU   B C   
5780 O  O   . LEU   B 109 ? 0.1578 0.1387 0.2420 0.0024  0.0345  0.0278  109 LEU   B O   
5781 C  CB  . LEU   B 109 ? 0.1755 0.1511 0.2690 0.0018  0.0159  0.0347  109 LEU   B CB  
5782 C  CG  . LEU   B 109 ? 0.1679 0.1463 0.2541 0.0011  0.0137  0.0159  109 LEU   B CG  
5783 C  CD1 . LEU   B 109 ? 0.1634 0.1559 0.2359 0.0049  0.0141  0.0145  109 LEU   B CD1 
5784 C  CD2 . LEU   B 109 ? 0.1799 0.1490 0.2635 0.0022  0.0086  0.0146  109 LEU   B CD2 
5796 N  N   . LYS   B 110 ? 0.1556 0.1451 0.2399 -0.0080 0.0264  0.0232  110 LYS   B N   
5797 C  CA  . LYS   B 110 ? 0.1485 0.1446 0.2385 -0.0056 0.0322  0.0173  110 LYS   B CA  
5798 C  C   . LYS   B 110 ? 0.1459 0.1491 0.2305 -0.0050 0.0279  0.0166  110 LYS   B C   
5799 O  O   . LYS   B 110 ? 0.1459 0.1494 0.2272 -0.0076 0.0254  0.0058  110 LYS   B O   
5800 C  CB  . LYS   B 110 ? 0.1537 0.1417 0.2602 -0.0031 0.0267  0.0212  110 LYS   B CB  
5801 C  CG  . LYS   B 110 ? 0.1514 0.1420 0.2779 -0.0067 0.0107  0.0298  110 LYS   B CG  
5802 C  CD  . LYS   B 110 ? 0.1562 0.1542 0.2797 -0.0051 0.0065  0.0235  110 LYS   B CD  
5803 C  CE  . LYS   B 110 ? 0.1570 0.1634 0.3019 -0.0037 0.0076  0.0026  110 LYS   B CE  
5804 N  NZ  . LYS   B 110 ? 0.1632 0.1822 0.2976 0.0005  -0.0032 0.0040  110 LYS   B NZ  
5818 N  N   . SER   B 111 ? 0.1511 0.1425 0.2438 -0.0028 0.0263  0.0114  111 SER   B N   
5819 C  CA  . SER   B 111 ? 0.1596 0.1438 0.2256 0.0025  0.0228  0.0116  111 SER   B CA  
5820 C  C   . SER   B 111 ? 0.1567 0.1370 0.2188 -0.0010 0.0178  0.0042  111 SER   B C   
5821 O  O   . SER   B 111 ? 0.1481 0.1508 0.2196 -0.0015 0.0085  0.0017  111 SER   B O   
5822 C  CB  . SER   B 111 ? 0.1693 0.1686 0.2253 0.0062  0.0415  0.0088  111 SER   B CB  
5823 O  OG  . SER   B 111 ? 0.1921 0.1972 0.2252 0.0030  0.0283  0.0204  111 SER   B OG  
5829 N  N   . ALA   B 112 ? 0.1433 0.1410 0.2242 0.0019  0.0228  0.0122  112 ALA   B N   
5830 C  CA  . ALA   B 112 ? 0.1413 0.1502 0.2079 0.0007  0.0107  0.0046  112 ALA   B CA  
5831 C  C   . ALA   B 112 ? 0.1362 0.1436 0.2019 -0.0018 0.0127  0.0105  112 ALA   B C   
5832 O  O   . ALA   B 112 ? 0.1395 0.1446 0.2184 -0.0046 0.0121  0.0037  112 ALA   B O   
5833 C  CB  . ALA   B 112 ? 0.1471 0.1486 0.2197 0.0006  0.0043  0.0113  112 ALA   B CB  
5839 N  N   . TYR   B 113 ? 0.1375 0.1314 0.2046 -0.0043 0.0049  0.0073  113 TYR   B N   
5840 C  CA  . TYR   B 113 ? 0.1338 0.1334 0.2066 -0.0031 0.0106  -0.0008 113 TYR   B CA  
5841 C  C   . TYR   B 113 ? 0.1320 0.1279 0.2002 -0.0080 0.0186  0.0036  113 TYR   B C   
5842 O  O   . TYR   B 113 ? 0.1365 0.1302 0.1942 -0.0045 0.0086  -0.0004 113 TYR   B O   
5843 C  CB  . TYR   B 113 ? 0.1416 0.1218 0.2098 -0.0029 0.0147  0.0111  113 TYR   B CB  
5844 C  CG  . TYR   B 113 ? 0.1411 0.1260 0.2223 -0.0087 0.0049  0.0106  113 TYR   B CG  
5845 C  CD1 . TYR   B 113 ? 0.1410 0.1353 0.2345 -0.0062 0.0038  0.0172  113 TYR   B CD1 
5846 C  CD2 . TYR   B 113 ? 0.1486 0.1359 0.2198 -0.0050 0.0012  0.0119  113 TYR   B CD2 
5847 C  CE1 . TYR   B 113 ? 0.1497 0.1379 0.2275 -0.0033 0.0050  0.0016  113 TYR   B CE1 
5848 C  CE2 . TYR   B 113 ? 0.1545 0.1324 0.2311 0.0011  0.0051  0.0145  113 TYR   B CE2 
5849 C  CZ  . TYR   B 113 ? 0.1400 0.1292 0.2310 0.0052  0.0029  0.0085  113 TYR   B CZ  
5850 O  OH  . TYR   B 113 ? 0.1519 0.1268 0.2657 0.0080  0.0114  0.0054  113 TYR   B OH  
5860 N  N   . GLU   B 114 ? 0.1311 0.1255 0.2171 -0.0064 0.0141  0.0090  114 GLU   B N   
5861 C  CA  . GLU   B 114 ? 0.1347 0.1244 0.2127 0.0016  0.0005  0.0084  114 GLU   B CA  
5862 C  C   . GLU   B 114 ? 0.1374 0.1218 0.2024 -0.0010 0.0024  0.0051  114 GLU   B C   
5863 O  O   . GLU   B 114 ? 0.1333 0.1291 0.2143 0.0035  -0.0060 0.0113  114 GLU   B O   
5864 C  CB  . GLU   B 114 ? 0.1331 0.1308 0.2160 0.0007  0.0145  0.0021  114 GLU   B CB  
5865 C  CG  . GLU   B 114 ? 0.1387 0.1313 0.2292 -0.0047 0.0021  0.0041  114 GLU   B CG  
5866 C  CD  . GLU   B 114 ? 0.1368 0.1370 0.2412 -0.0071 0.0056  0.0096  114 GLU   B CD  
5867 O  OE1 . GLU   B 114 ? 0.1394 0.1515 0.2231 -0.0091 0.0130  0.0100  114 GLU   B OE1 
5868 O  OE2 . GLU   B 114 ? 0.1360 0.1585 0.2661 -0.0135 0.0131  0.0126  114 GLU   B OE2 
5875 N  N   . ASN   B 115 ? 0.1359 0.1215 0.2019 -0.0018 -0.0016 0.0089  115 ASN   B N   
5876 C  CA  . ASN   B 115 ? 0.1393 0.1266 0.1783 -0.0078 0.0045  0.0091  115 ASN   B CA  
5877 C  C   . ASN   B 115 ? 0.1390 0.1224 0.1850 -0.0048 -0.0060 0.0022  115 ASN   B C   
5878 O  O   . ASN   B 115 ? 0.1497 0.1272 0.1872 -0.0103 0.0012  0.0014  115 ASN   B O   
5879 C  CB  . ASN   B 115 ? 0.1511 0.1433 0.1888 -0.0087 0.0037  0.0066  115 ASN   B CB  
5880 C  CG  . ASN   B 115 ? 0.1536 0.1473 0.1846 0.0008  -0.0011 0.0031  115 ASN   B CG  
5881 O  OD1 . ASN   B 115 ? 0.1967 0.1583 0.2099 -0.0040 0.0065  -0.0052 115 ASN   B OD1 
5882 N  ND2 . ASN   B 115 ? 0.1512 0.1600 0.1801 -0.0022 0.0045  0.0133  115 ASN   B ND2 
5889 N  N   . PHE   B 116 ? 0.1373 0.1281 0.1746 -0.0038 -0.0044 -0.0003 116 PHE   B N   
5890 C  CA  . PHE   B 116 ? 0.1405 0.1319 0.1759 -0.0076 -0.0084 -0.0041 116 PHE   B CA  
5891 C  C   . PHE   B 116 ? 0.1385 0.1193 0.1792 -0.0079 -0.0029 -0.0017 116 PHE   B C   
5892 O  O   . PHE   B 116 ? 0.1481 0.1343 0.1886 -0.0056 -0.0094 0.0033  116 PHE   B O   
5893 C  CB  . PHE   B 116 ? 0.1343 0.1290 0.1743 -0.0040 -0.0083 0.0080  116 PHE   B CB  
5894 C  CG  . PHE   B 116 ? 0.1305 0.1302 0.1731 -0.0080 -0.0048 0.0003  116 PHE   B CG  
5895 C  CD1 . PHE   B 116 ? 0.1394 0.1357 0.1871 -0.0032 -0.0025 -0.0037 116 PHE   B CD1 
5896 C  CD2 . PHE   B 116 ? 0.1406 0.1392 0.1693 -0.0061 -0.0031 -0.0002 116 PHE   B CD2 
5897 C  CE1 . PHE   B 116 ? 0.1471 0.1365 0.1834 -0.0007 -0.0131 0.0037  116 PHE   B CE1 
5898 C  CE2 . PHE   B 116 ? 0.1398 0.1363 0.1799 -0.0028 -0.0054 0.0099  116 PHE   B CE2 
5899 C  CZ  . PHE   B 116 ? 0.1327 0.1426 0.1751 0.0007  -0.0150 0.0100  116 PHE   B CZ  
5909 N  N   . ASN   B 117 ? 0.1432 0.1266 0.1913 -0.0026 -0.0143 0.0088  117 ASN   B N   
5910 C  CA  . ASN   B 117 ? 0.1478 0.1300 0.1969 0.0013  -0.0110 0.0074  117 ASN   B CA  
5911 C  C   . ASN   B 117 ? 0.1505 0.1318 0.2075 -0.0023 -0.0217 0.0095  117 ASN   B C   
5912 O  O   . ASN   B 117 ? 0.1560 0.1379 0.2363 -0.0068 -0.0402 0.0136  117 ASN   B O   
5913 C  CB  . ASN   B 117 ? 0.1494 0.1335 0.2016 0.0044  -0.0193 -0.0034 117 ASN   B CB  
5914 C  CG  . ASN   B 117 ? 0.1425 0.1354 0.2204 0.0013  -0.0083 -0.0082 117 ASN   B CG  
5915 O  OD1 . ASN   B 117 ? 0.1609 0.1352 0.2348 -0.0136 -0.0003 -0.0005 117 ASN   B OD1 
5916 N  ND2 . ASN   B 117 ? 0.1430 0.1381 0.2137 -0.0024 -0.0029 -0.0066 117 ASN   B ND2 
5923 N  N   . GLN   B 118 ? 0.1489 0.1259 0.1982 -0.0058 -0.0189 0.0035  118 GLN   B N   
5924 C  CA  . GLN   B 118 ? 0.1504 0.1258 0.2356 -0.0025 -0.0155 -0.0082 118 GLN   B CA  
5925 C  C   . GLN   B 118 ? 0.1515 0.1265 0.2333 -0.0018 -0.0152 0.0001  118 GLN   B C   
5926 O  O   . GLN   B 118 ? 0.1752 0.1302 0.2623 -0.0082 0.0006  0.0069  118 GLN   B O   
5927 C  CB  . GLN   B 118 ? 0.1607 0.1327 0.2361 0.0021  -0.0212 -0.0069 118 GLN   B CB  
5928 C  CG  . GLN   B 118 ? 0.1688 0.1402 0.2350 0.0076  -0.0149 -0.0148 118 GLN   B CG  
5929 C  CD  . GLN   B 118 ? 0.1676 0.1362 0.2326 0.0087  -0.0185 -0.0168 118 GLN   B CD  
5930 O  OE1 . GLN   B 118 ? 0.1769 0.1335 0.2537 0.0069  -0.0044 -0.0007 118 GLN   B OE1 
5931 N  NE2 . GLN   B 118 ? 0.1764 0.1413 0.2296 0.0070  -0.0154 -0.0036 118 GLN   B NE2 
5940 N  N   . HIS   B 119 ? 0.1591 0.1371 0.1839 -0.0061 -0.0232 0.0114  119 HIS   B N   
5941 C  CA  . HIS   B 119 ? 0.1689 0.1462 0.1748 -0.0059 -0.0231 0.0162  119 HIS   B CA  
5942 C  C   . HIS   B 119 ? 0.1729 0.1504 0.1694 -0.0078 -0.0390 0.0166  119 HIS   B C   
5943 O  O   . HIS   B 119 ? 0.1744 0.1490 0.2009 -0.0268 -0.0294 0.0165  119 HIS   B O   
5944 C  CB  . HIS   B 119 ? 0.1694 0.1495 0.1887 -0.0078 -0.0308 0.0099  119 HIS   B CB  
5945 C  CG  . HIS   B 119 ? 0.1753 0.1681 0.1977 0.0045  -0.0471 -0.0018 119 HIS   B CG  
5946 N  ND1 . HIS   B 119 ? 0.1838 0.1817 0.2407 0.0007  -0.0471 -0.0217 119 HIS   B ND1 
5947 C  CD2 . HIS   B 119 ? 0.1932 0.1901 0.1991 0.0368  -0.0605 -0.0089 119 HIS   B CD2 
5948 C  CE1 . HIS   B 119 ? 0.2052 0.2018 0.2444 0.0164  -0.0598 -0.0331 119 HIS   B CE1 
5949 N  NE2 . HIS   B 119 ? 0.2074 0.2105 0.2227 0.0368  -0.0565 -0.0296 119 HIS   B NE2 
5957 N  N   A GLU   B 120 ? 0.1912 0.1511 0.1660 -0.0130 -0.0506 0.0279  120 GLU   B N   
5958 N  N   B GLU   B 120 ? 0.1931 0.1639 0.1843 -0.0110 -0.0405 0.0199  120 GLU   B N   
5959 C  CA  A GLU   B 120 ? 0.2266 0.1682 0.1752 -0.0092 -0.0558 0.0458  120 GLU   B CA  
5960 C  CA  B GLU   B 120 ? 0.2226 0.1852 0.2037 -0.0084 -0.0410 0.0281  120 GLU   B CA  
5961 C  C   A GLU   B 120 ? 0.2020 0.1552 0.1671 -0.0194 -0.0546 0.0316  120 GLU   B C   
5962 C  C   B GLU   B 120 ? 0.2043 0.1677 0.1822 -0.0178 -0.0410 0.0224  120 GLU   B C   
5963 O  O   A GLU   B 120 ? 0.1915 0.1663 0.1795 -0.0171 -0.0523 0.0206  120 GLU   B O   
5964 O  O   B GLU   B 120 ? 0.1984 0.1747 0.1867 -0.0156 -0.0358 0.0133  120 GLU   B O   
5965 C  CB  A GLU   B 120 ? 0.2815 0.2048 0.2593 0.0043  -0.0728 0.0699  120 GLU   B CB  
5966 C  CB  B GLU   B 120 ? 0.2662 0.2229 0.2758 0.0035  -0.0509 0.0445  120 GLU   B CB  
5967 C  CG  A GLU   B 120 ? 0.3283 0.2695 0.3739 0.0093  -0.0771 0.0860  120 GLU   B CG  
5968 C  CG  B GLU   B 120 ? 0.3030 0.2724 0.3623 0.0090  -0.0530 0.0609  120 GLU   B CG  
5969 C  CD  A GLU   B 120 ? 0.3638 0.3257 0.4742 0.0095  -0.0758 0.0992  120 GLU   B CD  
5970 C  CD  B GLU   B 120 ? 0.3357 0.3188 0.4405 0.0111  -0.0486 0.0710  120 GLU   B CD  
5971 O  OE1 A GLU   B 120 ? 0.3778 0.3471 0.5074 0.0046  -0.0696 0.1120  120 GLU   B OE1 
5972 O  OE1 B GLU   B 120 ? 0.3466 0.3310 0.4668 0.0107  -0.0473 0.0779  120 GLU   B OE1 
5973 O  OE2 A GLU   B 120 ? 0.3781 0.3476 0.5220 0.0084  -0.0722 0.0900  120 GLU   B OE2 
5974 O  OE2 B GLU   B 120 ? 0.3463 0.3322 0.4693 0.0103  -0.0477 0.0721  120 GLU   B OE2 
5987 N  N   . VAL   B 121 ? 0.1935 0.1524 0.1677 -0.0275 -0.0385 0.0285  121 VAL   B N   
5988 C  CA  . VAL   B 121 ? 0.1834 0.1635 0.1614 -0.0238 -0.0345 0.0215  121 VAL   B CA  
5989 C  C   . VAL   B 121 ? 0.1768 0.1569 0.1625 -0.0256 -0.0271 0.0172  121 VAL   B C   
5990 O  O   . VAL   B 121 ? 0.1865 0.1493 0.1707 -0.0357 -0.0387 0.0190  121 VAL   B O   
5991 C  CB  . VAL   B 121 ? 0.2134 0.2036 0.1823 -0.0153 -0.0381 0.0345  121 VAL   B CB  
5992 C  CG1 . VAL   B 121 ? 0.2185 0.2156 0.2203 -0.0286 -0.0304 0.0335  121 VAL   B CG1 
5993 C  CG2 . VAL   B 121 ? 0.2376 0.2316 0.1740 -0.0081 -0.0315 0.0149  121 VAL   B CG2 
6004 N  N   . LEU   B 122 ? 0.1656 0.1480 0.1541 -0.0195 -0.0330 0.0102  122 LEU   B N   
6005 C  CA  . LEU   B 122 ? 0.1561 0.1580 0.1348 -0.0158 -0.0268 0.0117  122 LEU   B CA  
6006 C  C   . LEU   B 122 ? 0.1557 0.1411 0.1356 -0.0285 -0.0178 0.0134  122 LEU   B C   
6007 O  O   . LEU   B 122 ? 0.1632 0.1469 0.1850 -0.0363 -0.0243 0.0099  122 LEU   B O   
6008 C  CB  . LEU   B 122 ? 0.1803 0.1635 0.1808 0.0016  -0.0352 0.0122  122 LEU   B CB  
6009 C  CG  . LEU   B 122 ? 0.1651 0.1777 0.1891 -0.0108 -0.0186 0.0107  122 LEU   B CG  
6010 C  CD1 . LEU   B 122 ? 0.1680 0.2031 0.1867 -0.0220 -0.0253 0.0035  122 LEU   B CD1 
6011 C  CD2 . LEU   B 122 ? 0.1605 0.1799 0.1626 -0.0102 -0.0124 -0.0047 122 LEU   B CD2 
6023 N  N   . LEU   B 123 ? 0.1532 0.1325 0.1424 -0.0212 -0.0211 0.0117  123 LEU   B N   
6024 C  CA  . LEU   B 123 ? 0.1553 0.1388 0.1441 -0.0264 -0.0221 0.0054  123 LEU   B CA  
6025 C  C   . LEU   B 123 ? 0.1483 0.1382 0.1340 -0.0227 -0.0175 0.0038  123 LEU   B C   
6026 O  O   . LEU   B 123 ? 0.1612 0.1380 0.1376 -0.0274 -0.0206 0.0025  123 LEU   B O   
6027 C  CB  . LEU   B 123 ? 0.1638 0.1441 0.1483 -0.0204 -0.0186 0.0008  123 LEU   B CB  
6028 C  CG  . LEU   B 123 ? 0.1585 0.1443 0.1714 -0.0198 -0.0073 0.0104  123 LEU   B CG  
6029 C  CD1 . LEU   B 123 ? 0.1699 0.1469 0.1942 -0.0236 -0.0009 -0.0083 123 LEU   B CD1 
6030 C  CD2 . LEU   B 123 ? 0.1762 0.1534 0.1893 -0.0121 -0.0036 0.0051  123 LEU   B CD2 
6042 N  N   . ALA   B 124 ? 0.1484 0.1338 0.1415 -0.0196 -0.0123 0.0009  124 ALA   B N   
6043 C  CA  . ALA   B 124 ? 0.1432 0.1298 0.1623 -0.0105 -0.0122 -0.0042 124 ALA   B CA  
6044 C  C   . ALA   B 124 ? 0.1373 0.1318 0.1459 -0.0188 -0.0121 -0.0006 124 ALA   B C   
6045 O  O   . ALA   B 124 ? 0.1523 0.1358 0.1555 -0.0157 -0.0142 0.0001  124 ALA   B O   
6046 C  CB  . ALA   B 124 ? 0.1524 0.1360 0.1649 -0.0069 -0.0066 0.0029  124 ALA   B CB  
6052 N  N   . PRO   B 125 ? 0.1494 0.1362 0.1443 -0.0167 -0.0177 0.0111  125 PRO   B N   
6053 C  CA  . PRO   B 125 ? 0.1562 0.1352 0.1656 -0.0195 -0.0115 0.0218  125 PRO   B CA  
6054 C  C   . PRO   B 125 ? 0.1538 0.1311 0.1823 -0.0136 -0.0069 0.0116  125 PRO   B C   
6055 O  O   . PRO   B 125 ? 0.1509 0.1312 0.1944 -0.0077 0.0011  0.0149  125 PRO   B O   
6056 C  CB  . PRO   B 125 ? 0.1618 0.1625 0.1796 -0.0230 -0.0214 0.0348  125 PRO   B CB  
6057 C  CG  . PRO   B 125 ? 0.1670 0.1660 0.1608 -0.0283 -0.0269 0.0171  125 PRO   B CG  
6058 C  CD  . PRO   B 125 ? 0.1652 0.1501 0.1519 -0.0338 -0.0140 0.0004  125 PRO   B CD  
6066 N  N   . LEU   B 126 ? 0.1578 0.1264 0.1994 -0.0151 0.0065  0.0185  126 LEU   B N   
6067 C  CA  . LEU   B 126 ? 0.1626 0.1383 0.2048 -0.0141 0.0099  0.0168  126 LEU   B CA  
6068 C  C   . LEU   B 126 ? 0.1577 0.1531 0.1979 0.0017  0.0136  0.0219  126 LEU   B C   
6069 O  O   . LEU   B 126 ? 0.1823 0.1897 0.2320 0.0263  -0.0104 -0.0101 126 LEU   B O   
6070 C  CB  . LEU   B 126 ? 0.1840 0.1412 0.2340 -0.0212 0.0098  0.0157  126 LEU   B CB  
6071 C  CG  . LEU   B 126 ? 0.2040 0.1500 0.2475 -0.0284 0.0153  -0.0056 126 LEU   B CG  
6072 C  CD1 . LEU   B 126 ? 0.2196 0.1586 0.3064 -0.0224 0.0062  -0.0242 126 LEU   B CD1 
6073 C  CD2 . LEU   B 126 ? 0.2053 0.1676 0.2382 -0.0346 0.0105  -0.0065 126 LEU   B CD2 
6085 N  N   . LEU   B 127 ? 0.1540 0.1388 0.2092 0.0027  0.0219  0.0090  127 LEU   B N   
6086 C  CA  . LEU   B 127 ? 0.1563 0.1441 0.2268 -0.0034 0.0268  0.0216  127 LEU   B CA  
6087 C  C   . LEU   B 127 ? 0.1535 0.1378 0.2290 -0.0004 0.0187  0.0228  127 LEU   B C   
6088 O  O   . LEU   B 127 ? 0.1609 0.1430 0.2261 -0.0160 0.0075  0.0178  127 LEU   B O   
6089 C  CB  . LEU   B 127 ? 0.1716 0.1464 0.2334 -0.0043 0.0204  0.0182  127 LEU   B CB  
6090 C  CG  . LEU   B 127 ? 0.1896 0.1399 0.2456 -0.0014 0.0255  0.0120  127 LEU   B CG  
6091 C  CD1 . LEU   B 127 ? 0.1947 0.1454 0.2563 0.0079  0.0198  0.0097  127 LEU   B CD1 
6092 C  CD2 . LEU   B 127 ? 0.1908 0.1531 0.2725 -0.0145 0.0259  0.0259  127 LEU   B CD2 
6104 N  N   . SER   B 128 ? 0.1625 0.1379 0.2256 0.0031  -0.0010 0.0146  128 SER   B N   
6105 C  CA  . SER   B 128 ? 0.1760 0.1461 0.2246 0.0074  -0.0154 0.0154  128 SER   B CA  
6106 C  C   . SER   B 128 ? 0.1874 0.1504 0.2643 0.0075  -0.0365 0.0170  128 SER   B C   
6107 O  O   . SER   B 128 ? 0.2052 0.1571 0.2980 0.0054  -0.0326 0.0347  128 SER   B O   
6108 C  CB  . SER   B 128 ? 0.1840 0.1493 0.2197 -0.0002 -0.0031 0.0237  128 SER   B CB  
6109 O  OG  . SER   B 128 ? 0.1919 0.1641 0.2139 0.0050  0.0119  0.0324  128 SER   B OG  
6115 N  N   . ALA   B 129 ? 0.2027 0.1626 0.3011 0.0242  -0.0240 0.0076  129 ALA   B N   
6116 C  CA  . ALA   B 129 ? 0.2203 0.1681 0.3054 0.0373  -0.0243 -0.0094 129 ALA   B CA  
6117 C  C   . ALA   B 129 ? 0.2050 0.1587 0.2915 0.0253  -0.0032 -0.0009 129 ALA   B C   
6118 O  O   . ALA   B 129 ? 0.1933 0.1591 0.2849 0.0188  -0.0078 0.0021  129 ALA   B O   
6119 C  CB  . ALA   B 129 ? 0.2478 0.1976 0.3437 0.0400  -0.0031 -0.0151 129 ALA   B CB  
6125 N  N   . GLY   B 130 ? 0.2014 0.1578 0.2882 0.0306  0.0061  -0.0068 130 GLY   B N   
6126 C  CA  . GLY   B 130 ? 0.1982 0.1700 0.2895 0.0339  0.0307  -0.0043 130 GLY   B CA  
6127 C  C   . GLY   B 130 ? 0.2031 0.1734 0.2694 0.0189  0.0263  0.0076  130 GLY   B C   
6128 O  O   . GLY   B 130 ? 0.2153 0.1878 0.2766 0.0176  0.0092  0.0142  130 GLY   B O   
6132 N  N   . ILE   B 131 ? 0.2032 0.1860 0.2799 0.0281  0.0229  0.0071  131 ILE   B N   
6133 C  CA  . ILE   B 131 ? 0.2209 0.2004 0.2790 0.0266  0.0133  0.0238  131 ILE   B CA  
6134 C  C   . ILE   B 131 ? 0.2317 0.1946 0.2363 0.0161  0.0081  0.0297  131 ILE   B C   
6135 O  O   . ILE   B 131 ? 0.2614 0.2139 0.2451 0.0189  -0.0095 0.0313  131 ILE   B O   
6136 C  CB  . ILE   B 131 ? 0.2183 0.2348 0.3172 0.0177  -0.0022 0.0344  131 ILE   B CB  
6137 C  CG1 . ILE   B 131 ? 0.2261 0.2523 0.3306 -0.0107 0.0015  0.0395  131 ILE   B CG1 
6138 C  CG2 . ILE   B 131 ? 0.2140 0.2509 0.3528 0.0291  -0.0010 0.0244  131 ILE   B CG2 
6139 C  CD1 . ILE   B 131 ? 0.2303 0.2704 0.3509 -0.0245 -0.0023 0.0443  131 ILE   B CD1 
6151 N  N   . PHE   B 132 ? 0.2204 0.1769 0.2312 0.0078  0.0205  0.0160  132 PHE   B N   
6152 C  CA  . PHE   B 132 ? 0.2359 0.1780 0.2352 0.0060  0.0414  0.0180  132 PHE   B CA  
6153 C  C   . PHE   B 132 ? 0.2540 0.1948 0.2658 0.0078  0.0547  0.0109  132 PHE   B C   
6154 O  O   . PHE   B 132 ? 0.2720 0.2212 0.2938 0.0002  0.0714  0.0056  132 PHE   B O   
6155 C  CB  . PHE   B 132 ? 0.2180 0.1761 0.2176 0.0116  0.0402  0.0221  132 PHE   B CB  
6156 C  CG  . PHE   B 132 ? 0.2074 0.1802 0.2114 0.0174  0.0165  0.0274  132 PHE   B CG  
6157 C  CD1 . PHE   B 132 ? 0.2164 0.1860 0.2618 0.0135  0.0223  0.0236  132 PHE   B CD1 
6158 C  CD2 . PHE   B 132 ? 0.2079 0.1857 0.1912 0.0224  0.0068  0.0385  132 PHE   B CD2 
6159 C  CE1 . PHE   B 132 ? 0.2184 0.1890 0.2545 0.0057  0.0208  0.0308  132 PHE   B CE1 
6160 C  CE2 . PHE   B 132 ? 0.2192 0.1937 0.2007 0.0210  0.0129  0.0298  132 PHE   B CE2 
6161 C  CZ  . PHE   B 132 ? 0.2200 0.1930 0.2244 0.0122  0.0045  0.0367  132 PHE   B CZ  
6171 N  N   . GLY   B 133 ? 0.2428 0.1795 0.2630 -0.0001 0.0407  0.0387  133 GLY   B N   
6172 C  CA  . GLY   B 133 ? 0.2605 0.1900 0.2820 -0.0244 0.0416  0.0377  133 GLY   B CA  
6173 C  C   . GLY   B 133 ? 0.2687 0.2014 0.2929 -0.0380 0.0500  0.0433  133 GLY   B C   
6174 O  O   . GLY   B 133 ? 0.2880 0.2153 0.3366 -0.0541 0.0471  0.0509  133 GLY   B O   
6178 N  N   . ALA   B 134 ? 0.2430 0.2017 0.2783 -0.0322 0.0479  0.0273  134 ALA   B N   
6179 C  CA  . ALA   B 134 ? 0.2376 0.1948 0.2920 -0.0256 0.0475  0.0186  134 ALA   B CA  
6180 C  C   . ALA   B 134 ? 0.2437 0.1772 0.2968 -0.0175 0.0352  0.0423  134 ALA   B C   
6181 O  O   . ALA   B 134 ? 0.2415 0.2020 0.3101 -0.0029 0.0204  0.0309  134 ALA   B O   
6182 C  CB  . ALA   B 134 ? 0.2317 0.1960 0.2947 -0.0196 0.0354  -0.0031 134 ALA   B CB  
6188 N  N   . ASP   B 135 ? 0.2666 0.1743 0.3087 -0.0210 0.0143  0.0387  135 ASP   B N   
6189 C  CA  . ASP   B 135 ? 0.2873 0.1686 0.3240 -0.0214 0.0000  0.0415  135 ASP   B CA  
6190 C  C   . ASP   B 135 ? 0.2645 0.1558 0.2956 -0.0079 -0.0059 0.0459  135 ASP   B C   
6191 O  O   . ASP   B 135 ? 0.2527 0.1513 0.3064 -0.0121 -0.0009 0.0436  135 ASP   B O   
6192 C  CB  . ASP   B 135 ? 0.3221 0.1845 0.3575 -0.0398 -0.0032 0.0412  135 ASP   B CB  
6193 C  CG  . ASP   B 135 ? 0.3490 0.1889 0.3926 -0.0622 -0.0025 0.0455  135 ASP   B CG  
6194 O  OD1 . ASP   B 135 ? 0.3562 0.1753 0.3831 -0.0367 -0.0142 0.0469  135 ASP   B OD1 
6195 O  OD2 . ASP   B 135 ? 0.3728 0.2314 0.4528 -0.0815 0.0024  0.0303  135 ASP   B OD2 
6200 N  N   . PRO   B 136 ? 0.2487 0.1618 0.2973 0.0177  -0.0314 0.0256  136 PRO   B N   
6201 C  CA  . PRO   B 136 ? 0.2212 0.1565 0.2934 0.0160  -0.0293 0.0145  136 PRO   B CA  
6202 C  C   . PRO   B 136 ? 0.1973 0.1380 0.3060 0.0142  -0.0209 0.0066  136 PRO   B C   
6203 O  O   . PRO   B 136 ? 0.1790 0.1371 0.3017 0.0062  -0.0194 0.0109  136 PRO   B O   
6204 C  CB  . PRO   B 136 ? 0.2284 0.1812 0.3093 0.0312  -0.0303 0.0070  136 PRO   B CB  
6205 C  CG  . PRO   B 136 ? 0.2505 0.1957 0.3297 0.0334  -0.0187 0.0021  136 PRO   B CG  
6206 C  CD  . PRO   B 136 ? 0.2603 0.1864 0.3170 0.0377  -0.0227 0.0061  136 PRO   B CD  
6214 N  N   . ILE   B 137 ? 0.2092 0.1324 0.3123 0.0120  -0.0210 0.0061  137 ILE   B N   
6215 C  CA  . ILE   B 137 ? 0.2168 0.1317 0.3190 -0.0055 -0.0156 0.0052  137 ILE   B CA  
6216 C  C   . ILE   B 137 ? 0.2017 0.1395 0.3121 -0.0058 0.0031  0.0108  137 ILE   B C   
6217 O  O   . ILE   B 137 ? 0.1923 0.1481 0.2945 -0.0086 -0.0024 0.0094  137 ILE   B O   
6218 C  CB  . ILE   B 137 ? 0.2483 0.1424 0.3581 -0.0058 -0.0172 0.0013  137 ILE   B CB  
6219 C  CG1 . ILE   B 137 ? 0.2780 0.1537 0.3925 0.0082  -0.0135 -0.0118 137 ILE   B CG1 
6220 C  CG2 . ILE   B 137 ? 0.2542 0.1496 0.3659 -0.0358 -0.0203 0.0146  137 ILE   B CG2 
6221 C  CD1 . ILE   B 137 ? 0.3028 0.1860 0.4331 0.0180  -0.0169 -0.0078 137 ILE   B CD1 
6233 N  N   . HIS   B 138 ? 0.2029 0.1436 0.3167 -0.0040 0.0135  0.0161  138 HIS   B N   
6234 C  CA  . HIS   B 138 ? 0.2179 0.1484 0.3142 -0.0077 0.0271  0.0174  138 HIS   B CA  
6235 C  C   . HIS   B 138 ? 0.2011 0.1410 0.2939 -0.0039 0.0301  0.0274  138 HIS   B C   
6236 O  O   . HIS   B 138 ? 0.1951 0.1501 0.3245 -0.0031 0.0370  0.0308  138 HIS   B O   
6237 C  CB  . HIS   B 138 ? 0.2531 0.1611 0.3249 -0.0140 0.0541  0.0188  138 HIS   B CB  
6238 C  CG  . HIS   B 138 ? 0.2862 0.1809 0.3388 -0.0184 0.0818  0.0390  138 HIS   B CG  
6239 N  ND1 . HIS   B 138 ? 0.3033 0.2018 0.3781 -0.0131 0.0944  0.0391  138 HIS   B ND1 
6240 C  CD2 . HIS   B 138 ? 0.3070 0.1917 0.3384 -0.0161 0.0950  0.0342  138 HIS   B CD2 
6241 C  CE1 . HIS   B 138 ? 0.3113 0.2085 0.3742 -0.0110 0.1070  0.0370  138 HIS   B CE1 
6242 N  NE2 . HIS   B 138 ? 0.3174 0.1969 0.3438 -0.0082 0.1059  0.0348  138 HIS   B NE2 
6250 N  N   . SER   B 139 ? 0.1934 0.1376 0.2810 0.0012  0.0209  0.0176  139 SER   B N   
6251 C  CA  . SER   B 139 ? 0.1928 0.1338 0.2627 0.0000  0.0185  0.0039  139 SER   B CA  
6252 C  C   . SER   B 139 ? 0.1633 0.1280 0.2667 0.0027  0.0076  0.0030  139 SER   B C   
6253 O  O   . SER   B 139 ? 0.1660 0.1333 0.2600 -0.0006 -0.0003 0.0063  139 SER   B O   
6254 C  CB  . SER   B 139 ? 0.1997 0.1319 0.2698 0.0036  0.0018  -0.0086 139 SER   B CB  
6255 O  OG  . SER   B 139 ? 0.2011 0.1314 0.2737 -0.0006 -0.0150 0.0123  139 SER   B OG  
6261 N  N   . LEU   B 140 ? 0.1636 0.1266 0.2648 -0.0095 0.0118  -0.0059 140 LEU   B N   
6262 C  CA  . LEU   B 140 ? 0.1537 0.1259 0.2614 -0.0062 0.0020  -0.0029 140 LEU   B CA  
6263 C  C   . LEU   B 140 ? 0.1587 0.1314 0.2664 -0.0047 -0.0042 -0.0064 140 LEU   B C   
6264 O  O   . LEU   B 140 ? 0.1556 0.1414 0.2592 -0.0034 -0.0003 0.0066  140 LEU   B O   
6265 C  CB  . LEU   B 140 ? 0.1554 0.1256 0.2688 -0.0100 0.0013  0.0044  140 LEU   B CB  
6266 C  CG  . LEU   B 140 ? 0.1644 0.1298 0.2715 -0.0071 -0.0041 0.0085  140 LEU   B CG  
6267 C  CD1 . LEU   B 140 ? 0.1751 0.1438 0.2932 -0.0119 0.0097  0.0043  140 LEU   B CD1 
6268 C  CD2 . LEU   B 140 ? 0.1904 0.1376 0.2903 -0.0099 -0.0026 -0.0018 140 LEU   B CD2 
6280 N  N   A ARG   B 141 ? 0.1510 0.1343 0.2870 -0.0136 0.0128  -0.0076 141 ARG   B N   
6281 N  N   B ARG   B 141 ? 0.1553 0.1356 0.2716 -0.0024 0.0097  -0.0050 141 ARG   B N   
6282 C  CA  A ARG   B 141 ? 0.1589 0.1300 0.3220 -0.0236 0.0207  -0.0034 141 ARG   B CA  
6283 C  CA  B ARG   B 141 ? 0.1632 0.1354 0.2860 -0.0041 0.0159  -0.0027 141 ARG   B CA  
6284 C  C   A ARG   B 141 ? 0.1567 0.1277 0.3105 -0.0162 0.0154  -0.0002 141 ARG   B C   
6285 C  C   B ARG   B 141 ? 0.1584 0.1307 0.2880 -0.0042 0.0131  -0.0019 141 ARG   B C   
6286 O  O   A ARG   B 141 ? 0.1612 0.1355 0.3153 -0.0214 0.0034  -0.0075 141 ARG   B O   
6287 O  O   B ARG   B 141 ? 0.1579 0.1354 0.2856 -0.0038 0.0018  -0.0067 141 ARG   B O   
6288 C  CB  A ARG   B 141 ? 0.1759 0.1418 0.3464 -0.0389 0.0272  -0.0045 141 ARG   B CB  
6289 C  CB  B ARG   B 141 ? 0.1811 0.1461 0.2891 -0.0084 0.0179  -0.0079 141 ARG   B CB  
6290 C  CG  A ARG   B 141 ? 0.2007 0.1691 0.3558 -0.0407 0.0260  -0.0059 141 ARG   B CG  
6291 C  CG  B ARG   B 141 ? 0.2081 0.1707 0.2903 -0.0050 0.0188  -0.0124 141 ARG   B CG  
6292 C  CD  A ARG   B 141 ? 0.2310 0.1975 0.3592 -0.0375 0.0188  -0.0074 141 ARG   B CD  
6293 C  CD  B ARG   B 141 ? 0.2333 0.1794 0.2728 0.0013  0.0188  -0.0272 141 ARG   B CD  
6294 N  NE  A ARG   B 141 ? 0.2515 0.1967 0.3429 -0.0452 0.0219  -0.0136 141 ARG   B NE  
6295 N  NE  B ARG   B 141 ? 0.2561 0.1917 0.2854 -0.0007 0.0130  -0.0247 141 ARG   B NE  
6296 C  CZ  A ARG   B 141 ? 0.2765 0.1838 0.3192 -0.0425 0.0103  -0.0322 141 ARG   B CZ  
6297 C  CZ  B ARG   B 141 ? 0.2686 0.1889 0.2784 -0.0035 0.0026  -0.0253 141 ARG   B CZ  
6298 N  NH1 A ARG   B 141 ? 0.2858 0.1677 0.3038 -0.0438 0.0026  -0.0409 141 ARG   B NH1 
6299 N  NH1 B ARG   B 141 ? 0.2717 0.1804 0.2663 -0.0085 -0.0106 -0.0288 141 ARG   B NH1 
6300 N  NH2 A ARG   B 141 ? 0.2903 0.1920 0.3310 -0.0293 -0.0001 -0.0278 141 ARG   B NH2 
6301 N  NH2 B ARG   B 141 ? 0.2782 0.1960 0.2939 -0.0011 -0.0079 -0.0145 141 ARG   B NH2 
6328 N  N   . VAL   B 142 ? 0.1644 0.1280 0.2962 -0.0119 0.0129  -0.0033 142 VAL   B N   
6329 C  CA  . VAL   B 142 ? 0.1530 0.1298 0.2875 -0.0068 0.0167  -0.0032 142 VAL   B CA  
6330 C  C   . VAL   B 142 ? 0.1434 0.1286 0.2749 -0.0090 -0.0009 -0.0064 142 VAL   B C   
6331 O  O   . VAL   B 142 ? 0.1542 0.1315 0.2808 0.0022  0.0055  0.0005  142 VAL   B O   
6332 C  CB  . VAL   B 142 ? 0.1604 0.1441 0.2864 -0.0014 0.0224  0.0069  142 VAL   B CB  
6333 C  CG1 . VAL   B 142 ? 0.1552 0.1437 0.2908 -0.0019 0.0210  -0.0047 142 VAL   B CG1 
6334 C  CG2 . VAL   B 142 ? 0.1868 0.1480 0.2881 0.0006  0.0138  0.0089  142 VAL   B CG2 
6345 N  N   . CYS   B 143 ? 0.1388 0.1336 0.2547 -0.0043 -0.0001 0.0025  143 CYS   B N   
6346 C  CA  . CYS   B 143 ? 0.1390 0.1355 0.2588 -0.0085 0.0040  0.0062  143 CYS   B CA  
6347 C  C   . CYS   B 143 ? 0.1404 0.1328 0.2655 -0.0071 0.0045  -0.0011 143 CYS   B C   
6348 O  O   . CYS   B 143 ? 0.1414 0.1370 0.2704 -0.0070 -0.0109 -0.0023 143 CYS   B O   
6349 C  CB  . CYS   B 143 ? 0.1491 0.1395 0.2444 -0.0094 -0.0067 0.0063  143 CYS   B CB  
6350 S  SG  . CYS   B 143 ? 0.1528 0.1549 0.2447 -0.0050 -0.0024 0.0041  143 CYS   B SG  
6356 N  N   . VAL   B 144 ? 0.1448 0.1305 0.2856 -0.0095 -0.0067 -0.0125 144 VAL   B N   
6357 C  CA  . VAL   B 144 ? 0.1492 0.1422 0.3054 -0.0149 -0.0163 -0.0201 144 VAL   B CA  
6358 C  C   . VAL   B 144 ? 0.1425 0.1442 0.3085 -0.0079 -0.0135 -0.0019 144 VAL   B C   
6359 O  O   . VAL   B 144 ? 0.1571 0.1657 0.3205 0.0053  -0.0091 0.0140  144 VAL   B O   
6360 C  CB  . VAL   B 144 ? 0.1723 0.1603 0.3609 -0.0108 -0.0243 -0.0370 144 VAL   B CB  
6361 C  CG1 . VAL   B 144 ? 0.2031 0.2010 0.3893 -0.0066 -0.0126 -0.0258 144 VAL   B CG1 
6362 C  CG2 . VAL   B 144 ? 0.1846 0.1625 0.3485 -0.0023 -0.0332 -0.0454 144 VAL   B CG2 
6372 N  N   . ASP   B 145 ? 0.1471 0.1361 0.3210 -0.0069 -0.0070 -0.0119 145 ASP   B N   
6373 C  CA  . ASP   B 145 ? 0.1458 0.1383 0.3531 -0.0047 0.0022  -0.0131 145 ASP   B CA  
6374 C  C   . ASP   B 145 ? 0.1435 0.1495 0.3349 -0.0069 0.0007  -0.0036 145 ASP   B C   
6375 O  O   . ASP   B 145 ? 0.1466 0.1587 0.3774 -0.0104 0.0029  -0.0170 145 ASP   B O   
6376 C  CB  . ASP   B 145 ? 0.1584 0.1507 0.3930 -0.0160 0.0115  0.0004  145 ASP   B CB  
6377 C  CG  . ASP   B 145 ? 0.1783 0.1580 0.4438 -0.0180 0.0244  0.0049  145 ASP   B CG  
6378 O  OD1 . ASP   B 145 ? 0.1814 0.1652 0.4388 -0.0281 -0.0093 -0.0076 145 ASP   B OD1 
6379 O  OD2 . ASP   B 145 ? 0.2054 0.1634 0.4890 -0.0256 0.0497  0.0118  145 ASP   B OD2 
6384 N  N   . THR   B 146 ? 0.1359 0.1286 0.2916 -0.0158 -0.0047 0.0008  146 THR   B N   
6385 C  CA  . THR   B 146 ? 0.1412 0.1316 0.2708 -0.0100 0.0061  0.0016  146 THR   B CA  
6386 C  C   . THR   B 146 ? 0.1432 0.1343 0.2561 -0.0048 0.0004  0.0023  146 THR   B C   
6387 O  O   . THR   B 146 ? 0.1469 0.1310 0.2573 -0.0042 -0.0080 0.0081  146 THR   B O   
6388 C  CB  . THR   B 146 ? 0.1460 0.1357 0.2728 -0.0098 0.0142  0.0030  146 THR   B CB  
6389 O  OG1 . THR   B 146 ? 0.1504 0.1320 0.2840 -0.0081 0.0159  0.0120  146 THR   B OG1 
6390 C  CG2 . THR   B 146 ? 0.1624 0.1423 0.2629 -0.0071 0.0034  -0.0002 146 THR   B CG2 
6398 N  N   . VAL   B 147 ? 0.1499 0.1386 0.2308 -0.0065 0.0075  0.0069  147 VAL   B N   
6399 C  CA  . VAL   B 147 ? 0.1512 0.1359 0.2253 -0.0107 -0.0094 0.0027  147 VAL   B CA  
6400 C  C   . VAL   B 147 ? 0.1486 0.1340 0.2459 -0.0173 -0.0078 -0.0032 147 VAL   B C   
6401 O  O   . VAL   B 147 ? 0.1636 0.1421 0.2540 -0.0206 -0.0335 -0.0039 147 VAL   B O   
6402 C  CB  . VAL   B 147 ? 0.1489 0.1485 0.2196 -0.0117 -0.0174 0.0036  147 VAL   B CB  
6403 C  CG1 . VAL   B 147 ? 0.1544 0.1622 0.2060 -0.0165 -0.0208 0.0051  147 VAL   B CG1 
6404 C  CG2 . VAL   B 147 ? 0.1578 0.1462 0.2213 -0.0097 -0.0084 0.0107  147 VAL   B CG2 
6414 N  N   . ARG   B 148 ? 0.1468 0.1380 0.2457 -0.0098 -0.0248 -0.0052 148 ARG   B N   
6415 C  CA  . ARG   B 148 ? 0.1524 0.1452 0.2344 -0.0064 -0.0338 -0.0120 148 ARG   B CA  
6416 C  C   . ARG   B 148 ? 0.1639 0.1519 0.2185 -0.0116 -0.0331 0.0032  148 ARG   B C   
6417 O  O   . ARG   B 148 ? 0.1834 0.1774 0.2197 -0.0280 -0.0459 0.0113  148 ARG   B O   
6418 C  CB  . ARG   B 148 ? 0.1591 0.1573 0.2283 -0.0032 -0.0370 -0.0063 148 ARG   B CB  
6419 C  CG  . ARG   B 148 ? 0.1579 0.1724 0.2487 -0.0061 -0.0336 -0.0199 148 ARG   B CG  
6420 C  CD  . ARG   B 148 ? 0.1641 0.1880 0.2697 0.0055  -0.0283 -0.0330 148 ARG   B CD  
6421 N  NE  . ARG   B 148 ? 0.1702 0.1824 0.2648 0.0218  -0.0388 -0.0294 148 ARG   B NE  
6422 C  CZ  . ARG   B 148 ? 0.1637 0.1739 0.2471 0.0129  -0.0332 -0.0250 148 ARG   B CZ  
6423 N  NH1 . ARG   B 148 ? 0.1559 0.1755 0.2514 0.0068  -0.0105 -0.0252 148 ARG   B NH1 
6424 N  NH2 . ARG   B 148 ? 0.1822 0.1620 0.2364 0.0121  -0.0234 -0.0173 148 ARG   B NH2 
6438 N  N   . THR   B 149 ? 0.1620 0.1466 0.2198 -0.0144 -0.0361 -0.0021 149 THR   B N   
6439 C  CA  . THR   B 149 ? 0.1704 0.1535 0.2044 -0.0186 -0.0401 0.0115  149 THR   B CA  
6440 C  C   . THR   B 149 ? 0.1726 0.1511 0.1881 -0.0158 -0.0387 0.0031  149 THR   B C   
6441 O  O   . THR   B 149 ? 0.1785 0.1439 0.2084 -0.0212 -0.0263 0.0038  149 THR   B O   
6442 C  CB  . THR   B 149 ? 0.1732 0.1511 0.2087 -0.0178 -0.0346 -0.0002 149 THR   B CB  
6443 O  OG1 . THR   B 149 ? 0.1715 0.1559 0.1969 -0.0247 -0.0370 0.0105  149 THR   B OG1 
6444 C  CG2 . THR   B 149 ? 0.1842 0.1584 0.2149 -0.0104 -0.0237 0.0049  149 THR   B CG2 
6452 N  N   . ASN   B 150 ? 0.1720 0.1530 0.1859 -0.0190 -0.0401 0.0011  150 ASN   B N   
6453 C  CA  . ASN   B 150 ? 0.1845 0.1706 0.1852 -0.0274 -0.0382 0.0012  150 ASN   B CA  
6454 C  C   . ASN   B 150 ? 0.1712 0.1613 0.1721 -0.0227 -0.0237 -0.0019 150 ASN   B C   
6455 O  O   . ASN   B 150 ? 0.1754 0.1563 0.2054 -0.0295 -0.0472 0.0058  150 ASN   B O   
6456 C  CB  . ASN   B 150 ? 0.2163 0.2103 0.1927 -0.0294 -0.0503 0.0153  150 ASN   B CB  
6457 C  CG  . ASN   B 150 ? 0.2446 0.2474 0.2419 -0.0300 -0.0578 0.0336  150 ASN   B CG  
6458 O  OD1 . ASN   B 150 ? 0.2520 0.2681 0.2580 -0.0396 -0.0718 0.0302  150 ASN   B OD1 
6459 N  ND2 . ASN   B 150 ? 0.2593 0.2673 0.2839 -0.0170 -0.0667 0.0810  150 ASN   B ND2 
6466 N  N   . VAL   B 151 ? 0.1635 0.1558 0.1739 -0.0223 -0.0331 0.0014  151 VAL   B N   
6467 C  CA  . VAL   B 151 ? 0.1667 0.1534 0.1835 -0.0288 -0.0285 -0.0007 151 VAL   B CA  
6468 C  C   . VAL   B 151 ? 0.1681 0.1494 0.1788 -0.0320 -0.0254 -0.0018 151 VAL   B C   
6469 O  O   . VAL   B 151 ? 0.1759 0.1556 0.2099 -0.0245 -0.0179 -0.0160 151 VAL   B O   
6470 C  CB  . VAL   B 151 ? 0.1881 0.1625 0.1894 -0.0138 -0.0250 -0.0014 151 VAL   B CB  
6471 C  CG1 . VAL   B 151 ? 0.1918 0.1754 0.2295 -0.0186 -0.0216 0.0007  151 VAL   B CG1 
6472 C  CG2 . VAL   B 151 ? 0.1955 0.1793 0.1926 -0.0024 -0.0196 0.0079  151 VAL   B CG2 
6482 N  N   . TYR   B 152 ? 0.1634 0.1445 0.1740 -0.0272 -0.0193 -0.0016 152 TYR   B N   
6483 C  CA  . TYR   B 152 ? 0.1690 0.1604 0.1646 -0.0278 -0.0148 -0.0066 152 TYR   B CA  
6484 C  C   . TYR   B 152 ? 0.1651 0.1456 0.1576 -0.0240 -0.0168 -0.0127 152 TYR   B C   
6485 O  O   . TYR   B 152 ? 0.1760 0.1443 0.1652 -0.0265 -0.0162 -0.0012 152 TYR   B O   
6486 C  CB  . TYR   B 152 ? 0.1842 0.1833 0.1658 -0.0312 -0.0147 0.0019  152 TYR   B CB  
6487 C  CG  . TYR   B 152 ? 0.1982 0.1928 0.1627 -0.0455 -0.0140 -0.0032 152 TYR   B CG  
6488 C  CD1 . TYR   B 152 ? 0.2113 0.2063 0.1500 -0.0358 -0.0269 0.0079  152 TYR   B CD1 
6489 C  CD2 . TYR   B 152 ? 0.2240 0.2117 0.1632 -0.0433 -0.0090 -0.0013 152 TYR   B CD2 
6490 C  CE1 . TYR   B 152 ? 0.2327 0.2310 0.1801 -0.0349 -0.0356 0.0209  152 TYR   B CE1 
6491 C  CE2 . TYR   B 152 ? 0.2371 0.2359 0.1644 -0.0431 -0.0278 -0.0124 152 TYR   B CE2 
6492 C  CZ  . TYR   B 152 ? 0.2441 0.2526 0.1715 -0.0373 -0.0465 0.0156  152 TYR   B CZ  
6493 O  OH  . TYR   B 152 ? 0.2714 0.2891 0.1948 -0.0287 -0.0531 0.0208  152 TYR   B OH  
6503 N  N   . LEU   B 153 ? 0.1663 0.1367 0.1683 -0.0292 -0.0149 -0.0063 153 LEU   B N   
6504 C  CA  . LEU   B 153 ? 0.1661 0.1354 0.1613 -0.0239 -0.0038 -0.0046 153 LEU   B CA  
6505 C  C   . LEU   B 153 ? 0.1678 0.1360 0.1652 -0.0269 -0.0057 -0.0184 153 LEU   B C   
6506 O  O   . LEU   B 153 ? 0.1758 0.1620 0.1879 -0.0189 -0.0077 -0.0388 153 LEU   B O   
6507 C  CB  . LEU   B 153 ? 0.1662 0.1384 0.1780 -0.0259 -0.0043 -0.0038 153 LEU   B CB  
6508 C  CG  . LEU   B 153 ? 0.1597 0.1458 0.2008 -0.0267 -0.0070 -0.0045 153 LEU   B CG  
6509 C  CD1 . LEU   B 153 ? 0.1740 0.1591 0.2116 -0.0276 -0.0020 0.0076  153 LEU   B CD1 
6510 C  CD2 . LEU   B 153 ? 0.1631 0.1567 0.2041 -0.0269 0.0072  0.0122  153 LEU   B CD2 
6522 N  N   . ALA   B 154 ? 0.1603 0.1399 0.1865 -0.0071 -0.0076 -0.0143 154 ALA   B N   
6523 C  CA  . ALA   B 154 ? 0.1762 0.1514 0.2077 -0.0046 -0.0093 -0.0267 154 ALA   B CA  
6524 C  C   . ALA   B 154 ? 0.1949 0.1536 0.2217 0.0036  -0.0293 -0.0283 154 ALA   B C   
6525 O  O   . ALA   B 154 ? 0.2427 0.1529 0.2474 0.0078  -0.0221 -0.0088 154 ALA   B O   
6526 C  CB  . ALA   B 154 ? 0.1674 0.1776 0.2316 -0.0059 -0.0051 -0.0385 154 ALA   B CB  
6532 N  N   . VAL   B 155 ? 0.1565 0.1444 0.2404 -0.0058 -0.0003 -0.0212 155 VAL   B N   
6533 C  CA  . VAL   B 155 ? 0.1531 0.1408 0.2581 -0.0023 -0.0147 -0.0136 155 VAL   B CA  
6534 C  C   . VAL   B 155 ? 0.1511 0.1430 0.2521 -0.0006 -0.0133 -0.0301 155 VAL   B C   
6535 O  O   . VAL   B 155 ? 0.1695 0.1603 0.2954 0.0068  -0.0162 -0.0539 155 VAL   B O   
6536 C  CB  . VAL   B 155 ? 0.1550 0.1582 0.2977 -0.0036 -0.0156 -0.0022 155 VAL   B CB  
6537 C  CG1 . VAL   B 155 ? 0.1582 0.1587 0.2955 -0.0116 -0.0159 -0.0045 155 VAL   B CG1 
6538 C  CG2 . VAL   B 155 ? 0.1544 0.1733 0.3332 -0.0022 -0.0266 0.0213  155 VAL   B CG2 
6548 N  N   A PHE   B 156 ? 0.1390 0.1495 0.2704 0.0030  -0.0094 -0.0241 156 PHE   B N   
6549 N  N   B PHE   B 156 ? 0.1601 0.1596 0.2507 0.0072  -0.0050 -0.0305 156 PHE   B N   
6550 C  CA  A PHE   B 156 ? 0.1407 0.1472 0.2943 0.0062  -0.0124 -0.0264 156 PHE   B CA  
6551 C  CA  B PHE   B 156 ? 0.1751 0.1781 0.2548 0.0139  0.0020  -0.0353 156 PHE   B CA  
6552 C  C   A PHE   B 156 ? 0.1460 0.1602 0.3366 0.0133  -0.0272 -0.0410 156 PHE   B C   
6553 C  C   B PHE   B 156 ? 0.1911 0.1965 0.2650 0.0198  0.0064  -0.0490 156 PHE   B C   
6554 O  O   A PHE   B 156 ? 0.1778 0.1797 0.3611 0.0262  -0.0239 -0.0606 156 PHE   B O   
6555 O  O   B PHE   B 156 ? 0.2055 0.2105 0.2731 0.0225  0.0146  -0.0533 156 PHE   B O   
6556 C  CB  A PHE   B 156 ? 0.1451 0.1440 0.2799 0.0034  -0.0077 -0.0076 156 PHE   B CB  
6557 C  CB  B PHE   B 156 ? 0.1775 0.1796 0.2471 0.0144  0.0013  -0.0214 156 PHE   B CB  
6558 C  CG  A PHE   B 156 ? 0.1471 0.1589 0.2885 -0.0001 -0.0042 0.0024  156 PHE   B CG  
6559 C  CG  B PHE   B 156 ? 0.1807 0.1894 0.2523 0.0151  -0.0017 -0.0084 156 PHE   B CG  
6560 C  CD1 A PHE   B 156 ? 0.1540 0.1844 0.3170 0.0037  0.0036  0.0230  156 PHE   B CD1 
6561 C  CD1 B PHE   B 156 ? 0.1849 0.2032 0.2790 0.0176  -0.0029 0.0094  156 PHE   B CD1 
6562 C  CD2 A PHE   B 156 ? 0.1582 0.1730 0.2826 0.0116  -0.0124 0.0037  156 PHE   B CD2 
6563 C  CD2 B PHE   B 156 ? 0.1865 0.1972 0.2461 0.0184  -0.0090 0.0001  156 PHE   B CD2 
6564 C  CE1 A PHE   B 156 ? 0.1576 0.2012 0.3203 0.0084  0.0003  0.0199  156 PHE   B CE1 
6565 C  CE1 B PHE   B 156 ? 0.1875 0.2130 0.2844 0.0196  -0.0075 0.0158  156 PHE   B CE1 
6566 C  CE2 A PHE   B 156 ? 0.1644 0.1941 0.3029 0.0156  -0.0169 0.0048  156 PHE   B CE2 
6567 C  CE2 B PHE   B 156 ? 0.1905 0.2092 0.2622 0.0195  -0.0131 0.0099  156 PHE   B CE2 
6568 C  CZ  A PHE   B 156 ? 0.1531 0.2014 0.3153 0.0144  -0.0215 0.0075  156 PHE   B CZ  
6569 C  CZ  B PHE   B 156 ? 0.1859 0.2134 0.2742 0.0197  -0.0192 0.0126  156 PHE   B CZ  
6588 N  N   A ASP   B 157 ? 0.1384 0.1473 0.3644 0.0104  -0.0464 -0.0225 157 ASP   B N   
6589 N  N   B ASP   B 157 ? 0.1989 0.1994 0.2735 0.0229  0.0039  -0.0468 157 ASP   B N   
6590 C  CA  A ASP   B 157 ? 0.1579 0.1578 0.3917 0.0075  -0.0398 -0.0276 157 ASP   B CA  
6591 C  CA  B ASP   B 157 ? 0.2083 0.2082 0.2769 0.0231  -0.0008 -0.0481 157 ASP   B CA  
6592 C  C   A ASP   B 157 ? 0.1520 0.1532 0.3978 0.0065  -0.0388 -0.0470 157 ASP   B C   
6593 C  C   B ASP   B 157 ? 0.2118 0.2174 0.2745 0.0230  0.0040  -0.0704 157 ASP   B C   
6594 O  O   A ASP   B 157 ? 0.1353 0.1375 0.3852 0.0082  -0.0419 -0.0200 157 ASP   B O   
6595 O  O   B ASP   B 157 ? 0.2049 0.2178 0.2767 0.0217  0.0120  -0.0700 157 ASP   B O   
6596 C  CB  A ASP   B 157 ? 0.1945 0.1802 0.3954 -0.0033 -0.0588 -0.0076 157 ASP   B CB  
6597 C  CB  B ASP   B 157 ? 0.2155 0.2126 0.2726 0.0233  -0.0187 -0.0269 157 ASP   B CB  
6598 C  CG  A ASP   B 157 ? 0.2462 0.2066 0.4122 -0.0058 -0.0358 -0.0032 157 ASP   B CG  
6599 C  CG  B ASP   B 157 ? 0.2255 0.2201 0.2772 0.0217  -0.0303 -0.0196 157 ASP   B CG  
6600 O  OD1 A ASP   B 157 ? 0.2588 0.2075 0.4251 0.0040  -0.0208 -0.0023 157 ASP   B OD1 
6601 O  OD1 B ASP   B 157 ? 0.2232 0.2186 0.2692 0.0286  -0.0504 -0.0184 157 ASP   B OD1 
6602 O  OD2 A ASP   B 157 ? 0.2831 0.2274 0.4324 -0.0041 -0.0217 -0.0014 157 ASP   B OD2 
6603 O  OD2 B ASP   B 157 ? 0.2370 0.2257 0.2962 0.0153  -0.0062 -0.0125 157 ASP   B OD2 
6612 N  N   A LYS   B 158 ? 0.1572 0.1895 0.4194 0.0035  -0.0227 -0.0840 158 LYS   B N   
6613 N  N   B LYS   B 158 ? 0.2201 0.2355 0.2817 0.0223  0.0009  -0.0858 158 LYS   B N   
6614 C  CA  A LYS   B 158 ? 0.1768 0.2192 0.4179 -0.0008 -0.0096 -0.1068 158 LYS   B CA  
6615 C  CA  B LYS   B 158 ? 0.2341 0.2517 0.3081 0.0224  -0.0016 -0.0948 158 LYS   B CA  
6616 C  C   A LYS   B 158 ? 0.1762 0.2006 0.4253 0.0016  -0.0293 -0.1027 158 LYS   B C   
6617 C  C   B LYS   B 158 ? 0.2311 0.2392 0.3229 0.0240  -0.0180 -0.0827 158 LYS   B C   
6618 O  O   A LYS   B 158 ? 0.1724 0.1985 0.4396 -0.0004 -0.0261 -0.1083 158 LYS   B O   
6619 O  O   B LYS   B 158 ? 0.2332 0.2420 0.3169 0.0222  -0.0188 -0.0781 158 LYS   B O   
6620 C  CB  A LYS   B 158 ? 0.2030 0.2711 0.4106 -0.0009 0.0027  -0.1245 158 LYS   B CB  
6621 C  CB  B LYS   B 158 ? 0.2531 0.2814 0.3292 0.0219  0.0028  -0.1055 158 LYS   B CB  
6622 C  CG  A LYS   B 158 ? 0.2396 0.3227 0.4120 0.0025  0.0051  -0.1350 158 LYS   B CG  
6623 C  CG  B LYS   B 158 ? 0.2762 0.3073 0.3527 0.0212  0.0036  -0.1098 158 LYS   B CG  
6624 C  CD  A LYS   B 158 ? 0.2642 0.3679 0.4104 0.0036  0.0024  -0.1342 158 LYS   B CD  
6625 C  CD  B LYS   B 158 ? 0.2950 0.3316 0.3711 0.0189  0.0045  -0.1096 158 LYS   B CD  
6626 C  CE  A LYS   B 158 ? 0.2835 0.4030 0.4217 0.0052  -0.0064 -0.1279 158 LYS   B CE  
6627 C  CE  B LYS   B 158 ? 0.3089 0.3484 0.3902 0.0185  0.0010  -0.1062 158 LYS   B CE  
6628 N  NZ  A LYS   B 158 ? 0.2861 0.4218 0.4197 0.0036  -0.0088 -0.1248 158 LYS   B NZ  
6629 N  NZ  B LYS   B 158 ? 0.3135 0.3561 0.3931 0.0149  0.0005  -0.1062 158 LYS   B NZ  
6656 N  N   A ASN   B 159 ? 0.1787 0.1832 0.4445 0.0113  -0.0467 -0.0759 159 ASN   B N   
6657 N  N   B ASN   B 159 ? 0.2228 0.2226 0.3481 0.0279  -0.0337 -0.0673 159 ASN   B N   
6658 C  CA  A ASN   B 159 ? 0.1988 0.1745 0.4452 0.0237  -0.0635 -0.0589 159 ASN   B CA  
6659 C  CA  B ASN   B 159 ? 0.2192 0.2058 0.3704 0.0305  -0.0468 -0.0615 159 ASN   B CA  
6660 C  C   A ASN   B 159 ? 0.1883 0.1596 0.4304 0.0180  -0.0818 -0.0485 159 ASN   B C   
6661 C  C   B ASN   B 159 ? 0.2004 0.1789 0.3875 0.0286  -0.0606 -0.0635 159 ASN   B C   
6662 O  O   A ASN   B 159 ? 0.1909 0.1503 0.4470 -0.0081 -0.0909 -0.0221 159 ASN   B O   
6663 O  O   B ASN   B 159 ? 0.2005 0.1724 0.3933 0.0300  -0.0559 -0.0621 159 ASN   B O   
6664 C  CB  A ASN   B 159 ? 0.2278 0.1923 0.4583 0.0331  -0.0612 -0.0603 159 ASN   B CB  
6665 C  CB  B ASN   B 159 ? 0.2316 0.2173 0.3721 0.0331  -0.0474 -0.0562 159 ASN   B CB  
6666 C  CG  A ASN   B 159 ? 0.2592 0.2167 0.4778 0.0325  -0.0685 -0.0660 159 ASN   B CG  
6667 C  CG  B ASN   B 159 ? 0.2472 0.2323 0.3837 0.0353  -0.0527 -0.0523 159 ASN   B CG  
6668 O  OD1 A ASN   B 159 ? 0.2767 0.2257 0.4780 0.0387  -0.0609 -0.0763 159 ASN   B OD1 
6669 O  OD1 B ASN   B 159 ? 0.2564 0.2399 0.3819 0.0399  -0.0517 -0.0506 159 ASN   B OD1 
6670 N  ND2 A ASN   B 159 ? 0.2654 0.2303 0.4890 0.0311  -0.0721 -0.0547 159 ASN   B ND2 
6671 N  ND2 B ASN   B 159 ? 0.2495 0.2399 0.3904 0.0374  -0.0507 -0.0456 159 ASN   B ND2 
6684 N  N   . LEU   B 160 ? 0.1824 0.1687 0.4133 0.0160  -0.0698 -0.0567 160 LEU   B N   
6685 C  CA  . LEU   B 160 ? 0.1777 0.1651 0.3925 0.0170  -0.0531 -0.0317 160 LEU   B CA  
6686 C  C   . LEU   B 160 ? 0.1704 0.1525 0.3795 0.0008  -0.0351 -0.0406 160 LEU   B C   
6687 O  O   . LEU   B 160 ? 0.1503 0.1605 0.3899 0.0007  -0.0442 -0.0251 160 LEU   B O   
6688 C  CB  . LEU   B 160 ? 0.1735 0.1717 0.3696 0.0102  -0.0547 -0.0245 160 LEU   B CB  
6689 C  CG  . LEU   B 160 ? 0.1749 0.1834 0.3447 0.0108  -0.0455 -0.0152 160 LEU   B CG  
6690 C  CD1 . LEU   B 160 ? 0.1974 0.2026 0.3411 0.0012  -0.0243 -0.0136 160 LEU   B CD1 
6691 C  CD2 . LEU   B 160 ? 0.1788 0.1873 0.3449 0.0195  -0.0450 -0.0238 160 LEU   B CD2 
6704 N  N   A TYR   B 161 ? 0.1742 0.1576 0.3754 -0.0126 -0.0097 -0.0585 161 TYR   B N   
6705 N  N   B TYR   B 161 ? 0.1787 0.1625 0.3623 -0.0062 -0.0153 -0.0519 161 TYR   B N   
6706 C  CA  A TYR   B 161 ? 0.1772 0.1563 0.3604 -0.0203 0.0169  -0.0560 161 TYR   B CA  
6707 C  CA  B TYR   B 161 ? 0.1869 0.1674 0.3403 -0.0092 0.0044  -0.0509 161 TYR   B CA  
6708 C  C   A TYR   B 161 ? 0.1755 0.1560 0.3533 -0.0176 0.0170  -0.0521 161 TYR   B C   
6709 C  C   B TYR   B 161 ? 0.1833 0.1647 0.3426 -0.0105 0.0080  -0.0530 161 TYR   B C   
6710 O  O   A TYR   B 161 ? 0.1736 0.1591 0.3488 -0.0222 0.0168  -0.0397 161 TYR   B O   
6711 O  O   B TYR   B 161 ? 0.1837 0.1692 0.3369 -0.0115 0.0083  -0.0438 161 TYR   B O   
6712 C  CB  A TYR   B 161 ? 0.1867 0.1629 0.3482 -0.0287 0.0329  -0.0628 161 TYR   B CB  
6713 C  CB  B TYR   B 161 ? 0.2018 0.1783 0.3170 -0.0090 0.0136  -0.0502 161 TYR   B CB  
6714 C  CG  A TYR   B 161 ? 0.2130 0.1730 0.3294 -0.0360 0.0429  -0.0735 161 TYR   B CG  
6715 C  CG  B TYR   B 161 ? 0.2279 0.1941 0.2962 -0.0137 0.0178  -0.0516 161 TYR   B CG  
6716 C  CD1 A TYR   B 161 ? 0.2163 0.1717 0.3229 -0.0479 0.0481  -0.0749 161 TYR   B CD1 
6717 C  CD1 B TYR   B 161 ? 0.2349 0.1987 0.2872 -0.0178 0.0236  -0.0523 161 TYR   B CD1 
6718 C  CD2 A TYR   B 161 ? 0.2351 0.1864 0.3147 -0.0284 0.0369  -0.0730 161 TYR   B CD2 
6719 C  CD2 B TYR   B 161 ? 0.2432 0.2041 0.2811 -0.0100 0.0145  -0.0483 161 TYR   B CD2 
6720 C  CE1 A TYR   B 161 ? 0.2379 0.1918 0.3221 -0.0521 0.0473  -0.0716 161 TYR   B CE1 
6721 C  CE1 B TYR   B 161 ? 0.2493 0.2123 0.2856 -0.0216 0.0232  -0.0483 161 TYR   B CE1 
6722 C  CE2 A TYR   B 161 ? 0.2537 0.2058 0.3254 -0.0371 0.0399  -0.0665 161 TYR   B CE2 
6723 C  CE2 B TYR   B 161 ? 0.2570 0.2171 0.2876 -0.0153 0.0187  -0.0436 161 TYR   B CE2 
6724 C  CZ  A TYR   B 161 ? 0.2573 0.2061 0.3221 -0.0544 0.0354  -0.0626 161 TYR   B CZ  
6725 C  CZ  B TYR   B 161 ? 0.2620 0.2199 0.2849 -0.0239 0.0165  -0.0416 161 TYR   B CZ  
6726 O  OH  A TYR   B 161 ? 0.2858 0.2326 0.3449 -0.0548 0.0299  -0.0558 161 TYR   B OH  
6727 O  OH  B TYR   B 161 ? 0.2797 0.2352 0.2999 -0.0259 0.0168  -0.0385 161 TYR   B OH  
6746 N  N   . ASP   B 162 ? 0.1831 0.1629 0.3648 -0.0114 0.0010  -0.0664 162 ASP   B N   
6747 C  CA  . ASP   B 162 ? 0.1917 0.1652 0.3722 -0.0053 -0.0132 -0.0672 162 ASP   B CA  
6748 C  C   . ASP   B 162 ? 0.1905 0.1568 0.3723 -0.0101 -0.0224 -0.0456 162 ASP   B C   
6749 O  O   . ASP   B 162 ? 0.1943 0.1623 0.3837 -0.0184 -0.0395 -0.0366 162 ASP   B O   
6750 C  CB  . ASP   B 162 ? 0.2075 0.1740 0.4033 0.0031  -0.0107 -0.0899 162 ASP   B CB  
6751 C  CG  . ASP   B 162 ? 0.2130 0.2044 0.4371 0.0107  -0.0143 -0.1063 162 ASP   B CG  
6752 O  OD1 . ASP   B 162 ? 0.2147 0.2289 0.4341 -0.0028 -0.0022 -0.1002 162 ASP   B OD1 
6753 O  OD2 . ASP   B 162 ? 0.2279 0.2316 0.4647 0.0305  -0.0215 -0.1099 162 ASP   B OD2 
6759 N  N   . LYS   B 163 ? 0.1874 0.1468 0.3628 -0.0154 -0.0381 -0.0294 163 LYS   B N   
6760 C  CA  . LYS   B 163 ? 0.1979 0.1562 0.3704 -0.0179 -0.0311 -0.0162 163 LYS   B CA  
6761 C  C   . LYS   B 163 ? 0.1688 0.1481 0.3517 -0.0169 -0.0274 -0.0047 163 LYS   B C   
6762 O  O   . LYS   B 163 ? 0.1653 0.1678 0.3741 -0.0220 -0.0273 0.0100  163 LYS   B O   
6763 C  CB  . LYS   B 163 ? 0.2495 0.1931 0.4041 -0.0151 -0.0410 0.0019  163 LYS   B CB  
6764 C  CG  . LYS   B 163 ? 0.3322 0.2795 0.4620 -0.0165 -0.0332 0.0051  163 LYS   B CG  
6765 C  CD  . LYS   B 163 ? 0.4086 0.3652 0.5294 -0.0255 -0.0311 0.0081  163 LYS   B CD  
6766 C  CE  . LYS   B 163 ? 0.4722 0.4311 0.5709 -0.0308 -0.0281 0.0058  163 LYS   B CE  
6767 N  NZ  . LYS   B 163 ? 0.5030 0.4705 0.5984 -0.0339 -0.0277 -0.0005 163 LYS   B NZ  
6781 N  N   . LEU   B 164 ? 0.1545 0.1405 0.3249 -0.0093 -0.0224 -0.0054 164 LEU   B N   
6782 C  CA  . LEU   B 164 ? 0.1591 0.1429 0.3069 -0.0112 -0.0302 -0.0032 164 LEU   B CA  
6783 C  C   . LEU   B 164 ? 0.1717 0.1504 0.3118 -0.0174 -0.0375 0.0117  164 LEU   B C   
6784 O  O   . LEU   B 164 ? 0.1644 0.1738 0.3328 -0.0197 -0.0405 0.0002  164 LEU   B O   
6785 C  CB  . LEU   B 164 ? 0.1550 0.1416 0.2885 -0.0095 -0.0247 -0.0049 164 LEU   B CB  
6786 C  CG  . LEU   B 164 ? 0.1681 0.1589 0.2812 -0.0075 -0.0181 0.0008  164 LEU   B CG  
6787 C  CD1 . LEU   B 164 ? 0.1779 0.1586 0.2781 -0.0183 -0.0260 -0.0135 164 LEU   B CD1 
6788 C  CD2 . LEU   B 164 ? 0.1829 0.1881 0.3011 -0.0129 -0.0033 -0.0157 164 LEU   B CD2 
6800 N  N   . VAL   B 165 ? 0.2045 0.1568 0.3263 -0.0274 -0.0531 0.0004  165 VAL   B N   
6801 C  CA  . VAL   B 165 ? 0.2485 0.1642 0.3359 -0.0366 -0.0772 -0.0047 165 VAL   B CA  
6802 C  C   . VAL   B 165 ? 0.2830 0.1820 0.3776 -0.0420 -0.1093 0.0022  165 VAL   B C   
6803 O  O   . VAL   B 165 ? 0.3082 0.1979 0.3921 -0.0477 -0.1167 0.0102  165 VAL   B O   
6804 C  CB  . VAL   B 165 ? 0.2774 0.1856 0.3338 -0.0255 -0.0485 -0.0219 165 VAL   B CB  
6805 C  CG1 . VAL   B 165 ? 0.2987 0.2031 0.3509 -0.0273 -0.0344 -0.0238 165 VAL   B CG1 
6806 C  CG2 . VAL   B 165 ? 0.2762 0.1875 0.3240 -0.0260 -0.0368 -0.0118 165 VAL   B CG2 
6816 N  N   . SER   B 166 ? 0.2963 0.1684 0.4206 -0.0461 -0.1242 -0.0203 166 SER   B N   
6817 C  CA  . SER   B 166 ? 0.2965 0.1758 0.4779 -0.0431 -0.1076 -0.0276 166 SER   B CA  
6818 C  C   . SER   B 166 ? 0.2718 0.1928 0.4992 -0.0501 -0.0944 -0.0039 166 SER   B C   
6819 O  O   . SER   B 166 ? 0.2736 0.2143 0.5413 -0.0711 -0.0953 -0.0342 166 SER   B O   
6820 C  CB  . SER   B 166 ? 0.2968 0.1767 0.5057 -0.0409 -0.1038 -0.0357 166 SER   B CB  
6821 O  OG  . SER   B 166 ? 0.2799 0.1799 0.5315 -0.0270 -0.1024 -0.0101 166 SER   B OG  
6827 N  N   . SER   B 167 ? 0.2435 0.1771 0.4708 -0.0479 -0.1031 0.0411  167 SER   B N   
6828 C  CA  . SER   B 167 ? 0.2351 0.1923 0.4578 -0.0413 -0.0704 0.0521  167 SER   B CA  
6829 C  C   . SER   B 167 ? 0.2237 0.2051 0.4302 -0.0512 -0.0636 0.0786  167 SER   B C   
6830 O  O   . SER   B 167 ? 0.2192 0.2261 0.4362 -0.0598 -0.0591 0.0783  167 SER   B O   
6831 C  CB  . SER   B 167 ? 0.2211 0.1939 0.4701 -0.0400 -0.0358 0.0436  167 SER   B CB  
6832 O  OG  . SER   B 167 ? 0.2129 0.2070 0.4632 -0.0321 -0.0203 0.0465  167 SER   B OG  
6838 N  N   . PHE   B 168 ? 0.2228 0.2021 0.4173 -0.0481 -0.0531 0.0762  168 PHE   B N   
6839 C  CA  . PHE   B 168 ? 0.2131 0.1959 0.3642 -0.0482 -0.0435 0.0474  168 PHE   B CA  
6840 C  C   . PHE   B 168 ? 0.1840 0.1776 0.2921 -0.0293 -0.0270 0.0186  168 PHE   B C   
6841 O  O   . PHE   B 168 ? 0.2062 0.1707 0.2821 -0.0073 -0.0170 -0.0002 168 PHE   B O   
6842 C  CB  . PHE   B 168 ? 0.2233 0.2015 0.3772 -0.0564 -0.0475 0.0557  168 PHE   B CB  
6843 C  CG  . PHE   B 168 ? 0.2497 0.1868 0.3702 -0.0544 -0.0432 0.0400  168 PHE   B CG  
6844 C  CD1 . PHE   B 168 ? 0.2707 0.1938 0.3731 -0.0553 -0.0564 0.0276  168 PHE   B CD1 
6845 C  CD2 . PHE   B 168 ? 0.2381 0.1739 0.3709 -0.0539 -0.0397 0.0405  168 PHE   B CD2 
6846 C  CE1 . PHE   B 168 ? 0.2814 0.1928 0.3622 -0.0485 -0.0444 0.0437  168 PHE   B CE1 
6847 C  CE2 . PHE   B 168 ? 0.2697 0.1856 0.3686 -0.0335 -0.0409 0.0410  168 PHE   B CE2 
6848 C  CZ  . PHE   B 168 ? 0.2753 0.1773 0.3616 -0.0307 -0.0453 0.0548  168 PHE   B CZ  
6858 N  N   . LEU   B 169 ? 0.2119 0.1867 0.2867 -0.0009 0.0033  -0.0031 169 LEU   B N   
6859 C  CA  . LEU   B 169 ? 0.2583 0.2220 0.3118 -0.0048 0.0123  -0.0315 169 LEU   B CA  
6860 C  C   . LEU   B 169 ? 0.3007 0.2510 0.3641 0.0058  0.0132  -0.0498 169 LEU   B C   
6861 O  O   . LEU   B 169 ? 0.3207 0.2680 0.4126 -0.0029 0.0132  -0.0648 169 LEU   B O   
6862 C  CB  . LEU   B 169 ? 0.2851 0.2615 0.3278 -0.0107 0.0105  -0.0035 169 LEU   B CB  
6863 C  CG  . LEU   B 169 ? 0.3227 0.2979 0.3644 -0.0027 0.0138  0.0026  169 LEU   B CG  
6864 C  CD1 . LEU   B 169 ? 0.3360 0.3123 0.3710 -0.0033 0.0116  0.0169  169 LEU   B CD1 
6865 C  CD2 . LEU   B 169 ? 0.3206 0.3038 0.3719 0.0066  0.0274  -0.0077 169 LEU   B CD2 
6866 O  OXT . LEU   B 169 ? 0.3207 0.2663 0.3705 0.0377  0.0311  -0.0457 169 LEU   B OXT 
6878 N  N2  B A1BBK C .   ? 0.1296 0.2070 0.2370 0.0002  -0.0271 -0.0009 201 A1BBK A N2  
6879 C  C3  B A1BBK C .   ? 0.1529 0.2104 0.2236 -0.0159 -0.0042 -0.0016 201 A1BBK A C3  
6880 C  C6  B A1BBK C .   ? 0.1133 0.1985 0.2382 -0.0180 -0.0229 0.0003  201 A1BBK A C6  
6881 C  C9  B A1BBK C .   ? 0.2221 0.2641 0.2405 -0.0388 0.0145  -0.0131 201 A1BBK A C9  
6882 C  C12 B A1BBK C .   ? 0.2249 0.2702 0.2507 -0.0401 0.0161  -0.0058 201 A1BBK A C12 
6883 C  C1  B A1BBK C .   ? 0.2103 0.2538 0.2313 -0.0407 0.0247  -0.0140 201 A1BBK A C1  
6884 C  C10 B A1BBK C .   ? 0.2345 0.2789 0.2564 -0.0340 0.0149  -0.0003 201 A1BBK A C10 
6885 C  C11 B A1BBK C .   ? 0.2307 0.2778 0.2545 -0.0385 0.0181  -0.0026 201 A1BBK A C11 
6886 C  C13 B A1BBK C .   ? 0.2353 0.2759 0.2542 -0.0373 0.0145  0.0024  201 A1BBK A C13 
6887 C  C2  B A1BBK C .   ? 0.1836 0.2412 0.2235 -0.0424 0.0217  -0.0157 201 A1BBK A C2  
6888 C  C4  B A1BBK C .   ? 0.1363 0.2046 0.2292 -0.0118 -0.0025 -0.0016 201 A1BBK A C4  
6889 C  C5  B A1BBK C .   ? 0.1271 0.2033 0.2400 -0.0142 -0.0020 0.0013  201 A1BBK A C5  
6890 C  C7  B A1BBK C .   ? 0.1373 0.2056 0.2238 -0.0045 -0.0152 0.0014  201 A1BBK A C7  
6891 C  C8  B A1BBK C .   ? 0.1523 0.2170 0.2326 -0.0050 -0.0196 0.0079  201 A1BBK A C8  
6892 N  N1  B A1BBK C .   ? 0.1641 0.2229 0.2192 -0.0288 0.0083  -0.0006 201 A1BBK A N1  
6893 N  N3  B A1BBK C .   ? 0.1496 0.2134 0.2280 -0.0091 -0.0052 0.0111  201 A1BBK A N3  
6894 N  N4  B A1BBK C .   ? 0.1528 0.2136 0.2335 -0.0161 -0.0180 0.0046  201 A1BBK A N4  
6895 O  O1  B A1BBK C .   ? 0.2135 0.2439 0.2200 -0.0367 0.0319  -0.0245 201 A1BBK A O1  
6896 O  O2  B A1BBK C .   ? 0.2358 0.2761 0.2596 -0.0346 0.0115  0.0004  201 A1BBK A O2  
6913 CL CL  B CL    D .   ? 0.1913 0.1545 0.2335 -0.0169 0.0259  0.0096  202 CL    A CL  
6914 O  O   A HOH   E .   ? 0.3728 0.6131 0.4256 -0.0788 0.0092  0.0598  301 HOH   A O   
6915 O  O   . HOH   E .   ? 0.4305 0.2384 0.4872 -0.0408 -0.0339 0.0256  302 HOH   A O   
6916 O  O   . HOH   E .   ? 0.7868 0.6355 0.3623 -0.1525 0.0002  0.2191  303 HOH   A O   
6917 O  O   . HOH   E .   ? 0.7252 0.5612 0.6684 -0.1177 0.2156  0.2061  304 HOH   A O   
6918 O  O   . HOH   E .   ? 0.6617 0.7235 0.6550 -0.0673 -0.1308 -0.1246 305 HOH   A O   
6919 O  O   . HOH   E .   ? 0.6360 0.5030 0.3345 0.2268  -0.1397 0.0489  306 HOH   A O   
6920 O  O   . HOH   E .   ? 0.6166 0.4838 0.6425 -0.1184 0.1308  0.1955  307 HOH   A O   
6921 O  O   . HOH   E .   ? 0.3390 0.3670 0.1771 -0.0666 0.0361  0.0196  308 HOH   A O   
6922 O  O   . HOH   E .   ? 0.3466 0.6153 0.6665 0.0828  0.1283  0.1580  309 HOH   A O   
6923 O  O   . HOH   E .   ? 0.8222 0.5852 0.6662 0.0549  -0.1275 0.0441  310 HOH   A O   
6924 O  O   . HOH   E .   ? 0.3559 0.3188 0.5142 -0.0752 -0.1398 0.1744  311 HOH   A O   
6925 O  O   . HOH   E .   ? 0.5194 0.2329 0.6122 0.0553  -0.0375 -0.0272 312 HOH   A O   
6926 O  O   . HOH   E .   ? 0.2280 0.1853 0.2740 0.0378  -0.0380 -0.0047 313 HOH   A O   
6927 O  O   . HOH   E .   ? 0.1907 0.4736 0.3375 0.0914  -0.0096 0.0154  314 HOH   A O   
6928 O  O   . HOH   E .   ? 0.2847 0.5617 0.4282 0.0194  -0.0227 0.0552  315 HOH   A O   
6929 O  O   . HOH   E .   ? 0.4644 0.4135 0.4204 -0.1780 -0.0113 0.1337  316 HOH   A O   
6930 O  O   . HOH   E .   ? 0.1794 0.1905 0.2694 -0.0256 0.0165  0.0350  317 HOH   A O   
6931 O  O   . HOH   E .   ? 0.2531 0.2169 0.2146 -0.0519 0.0150  0.0426  318 HOH   A O   
6932 O  O   . HOH   E .   ? 0.6702 0.6615 0.3793 -0.0844 0.0032  0.1127  319 HOH   A O   
6933 O  O   A HOH   E .   ? 0.3343 0.2926 0.3875 -0.0128 0.1114  -0.0040 320 HOH   A O   
6934 O  O   . HOH   E .   ? 0.2997 0.2109 0.2787 -0.0015 0.0323  0.0074  321 HOH   A O   
6935 O  O   . HOH   E .   ? 0.6703 0.7507 0.5673 -0.0053 -0.0338 -0.0627 322 HOH   A O   
6936 O  O   . HOH   E .   ? 0.2362 0.2014 0.3491 -0.0491 0.0094  -0.0275 323 HOH   A O   
6937 O  O   . HOH   E .   ? 0.1693 0.3852 0.3165 -0.0164 0.0291  0.0673  324 HOH   A O   
6938 O  O   . HOH   E .   ? 0.2710 0.2519 0.3405 -0.0143 0.0761  0.0450  325 HOH   A O   
6939 O  O   . HOH   E .   ? 0.4686 0.2025 0.2465 0.0179  0.0178  0.0107  326 HOH   A O   
6940 O  O   . HOH   E .   ? 0.2409 0.3466 0.3903 -0.0519 -0.0757 0.1263  327 HOH   A O   
6941 O  O   . HOH   E .   ? 0.3908 0.3603 0.4602 -0.0601 0.1819  0.0391  328 HOH   A O   
6942 O  O   . HOH   E .   ? 0.5269 0.4011 0.5655 0.1123  -0.0189 0.0894  329 HOH   A O   
6943 O  O   . HOH   E .   ? 0.5041 0.6651 0.5149 0.0111  0.2498  -0.1103 330 HOH   A O   
6944 O  O   . HOH   E .   ? 0.1768 0.1635 0.2650 -0.0298 -0.0034 0.0092  331 HOH   A O   
6945 O  O   . HOH   E .   ? 0.3088 0.2296 0.2629 -0.0380 0.0356  -0.0182 332 HOH   A O   
6946 O  O   . HOH   E .   ? 0.2203 0.2324 0.3736 0.0109  -0.0585 0.0558  333 HOH   A O   
6947 O  O   . HOH   E .   ? 0.2113 0.3620 0.4841 -0.0210 0.0306  -0.1001 334 HOH   A O   
6948 O  O   . HOH   E .   ? 1.2190 1.1322 0.9550 0.0027  -0.0618 -0.0478 335 HOH   A O   
6949 O  O   . HOH   E .   ? 0.3944 0.3951 0.5140 -0.1622 -0.1026 0.2214  336 HOH   A O   
6950 O  O   . HOH   E .   ? 0.4740 0.5742 0.5838 0.1988  0.0545  -0.1232 337 HOH   A O   
6951 O  O   . HOH   E .   ? 0.1638 0.1942 0.2932 0.0036  -0.0355 -0.0486 338 HOH   A O   
6952 O  O   . HOH   E .   ? 0.4091 0.3209 0.3818 -0.1013 0.0025  -0.0327 339 HOH   A O   
6953 O  O   . HOH   E .   ? 0.3264 0.5955 0.6358 -0.0378 -0.1036 0.2247  340 HOH   A O   
6954 O  O   . HOH   E .   ? 0.5573 0.6401 0.4649 0.1212  -0.0511 0.1534  341 HOH   A O   
6955 O  O   . HOH   E .   ? 0.4744 0.5979 0.3365 -0.1424 0.1108  0.0879  342 HOH   A O   
6956 O  O   . HOH   E .   ? 0.2622 0.4126 0.3978 0.1012  -0.0898 -0.0517 343 HOH   A O   
6957 O  O   . HOH   E .   ? 0.4131 0.4842 0.4883 0.2260  0.0591  0.0316  344 HOH   A O   
6958 O  O   . HOH   E .   ? 0.3799 0.4380 0.2690 -0.1655 -0.0230 -0.0635 345 HOH   A O   
6959 O  O   . HOH   E .   ? 0.6802 0.5018 0.5836 -0.0100 -0.1030 -0.0044 346 HOH   A O   
6960 O  O   . HOH   E .   ? 0.2739 0.3514 0.3810 -0.0608 0.1018  -0.0582 347 HOH   A O   
6961 O  O   . HOH   E .   ? 0.3887 0.4531 0.2513 -0.0731 0.0568  0.0315  348 HOH   A O   
6962 O  O   . HOH   E .   ? 0.2758 0.4742 0.5830 -0.0432 0.0683  0.2510  349 HOH   A O   
6963 O  O   . HOH   E .   ? 0.2214 0.2109 0.2884 0.0291  0.0110  0.0368  350 HOH   A O   
6964 O  O   . HOH   E .   ? 0.7039 0.7000 0.8441 -0.0729 -0.1026 0.1288  351 HOH   A O   
6965 O  O   . HOH   E .   ? 0.1582 0.2125 0.2268 0.0052  -0.0071 0.0412  352 HOH   A O   
6966 O  O   A HOH   E .   ? 0.1863 0.3520 0.2333 0.0395  0.0182  0.0476  353 HOH   A O   
6967 O  O   . HOH   E .   ? 0.1899 0.1848 0.2359 0.0159  -0.0263 0.0244  354 HOH   A O   
6968 O  O   . HOH   E .   ? 0.5099 0.3847 0.3713 -0.1529 -0.1461 0.0297  355 HOH   A O   
6969 O  O   . HOH   E .   ? 0.5562 0.2084 0.4263 0.0606  -0.1357 0.0340  356 HOH   A O   
6970 O  O   . HOH   E .   ? 0.3019 0.3665 0.4702 -0.0315 -0.0831 -0.1068 357 HOH   A O   
6971 O  O   . HOH   E .   ? 0.2159 0.2169 0.3915 0.0186  0.0994  -0.0158 358 HOH   A O   
6972 O  O   . HOH   E .   ? 0.4315 0.7577 0.5635 -0.0888 -0.1696 0.0572  359 HOH   A O   
6973 O  O   . HOH   E .   ? 0.3297 0.3738 0.4492 -0.1518 0.1175  -0.0545 360 HOH   A O   
6974 O  O   . HOH   E .   ? 0.3051 0.4488 0.3917 -0.0596 -0.0848 0.0123  361 HOH   A O   
6975 O  O   . HOH   E .   ? 0.1395 0.1378 0.1690 -0.0036 0.0089  0.0099  362 HOH   A O   
6976 O  O   . HOH   E .   ? 0.6097 0.4996 0.3620 0.1024  0.0836  0.1768  363 HOH   A O   
6977 O  O   . HOH   E .   ? 0.1617 0.1920 0.2620 0.0023  0.0040  0.0064  364 HOH   A O   
6978 O  O   . HOH   E .   ? 0.1868 0.2370 0.2203 -0.0208 -0.0046 0.0810  365 HOH   A O   
6979 O  O   . HOH   E .   ? 0.1752 0.1475 0.2487 -0.0125 0.0207  -0.0083 366 HOH   A O   
6980 O  O   . HOH   E .   ? 0.2674 0.4594 0.3767 -0.0405 0.0321  -0.0011 367 HOH   A O   
6981 O  O   . HOH   E .   ? 0.2176 0.2389 0.2455 -0.0320 -0.0393 0.0445  368 HOH   A O   
6982 O  O   . HOH   E .   ? 0.2271 0.2776 0.4190 0.0330  0.1102  -0.0482 369 HOH   A O   
6983 O  O   . HOH   E .   ? 0.1573 0.1742 0.1751 -0.0037 -0.0142 -0.0103 370 HOH   A O   
6984 O  O   . HOH   E .   ? 0.2354 0.2007 0.2111 -0.0004 0.0284  0.0183  371 HOH   A O   
6985 O  O   . HOH   E .   ? 0.2101 0.1960 0.2572 -0.0223 0.0081  0.0279  372 HOH   A O   
6986 O  O   . HOH   E .   ? 0.5716 0.7442 0.6335 -0.1197 0.0832  -0.0881 373 HOH   A O   
6987 O  O   . HOH   E .   ? 0.4027 0.2394 0.3286 0.1102  0.0418  0.0471  374 HOH   A O   
6988 O  O   . HOH   E .   ? 0.4321 0.2420 0.4855 -0.1032 0.0930  0.0350  375 HOH   A O   
6989 O  O   . HOH   E .   ? 0.3715 0.2609 0.5609 -0.0684 0.0235  -0.0173 376 HOH   A O   
6990 O  O   . HOH   E .   ? 0.3269 0.4238 0.4926 -0.0701 0.1412  0.0096  377 HOH   A O   
6991 O  O   . HOH   E .   ? 0.1939 0.1456 0.1746 -0.0206 0.0199  0.0034  378 HOH   A O   
6992 O  O   . HOH   E .   ? 0.1574 0.1787 0.2015 0.0052  -0.0223 -0.0234 379 HOH   A O   
6993 O  O   . HOH   E .   ? 0.2067 0.1926 0.2915 -0.0005 -0.0413 -0.0113 380 HOH   A O   
6994 O  O   . HOH   E .   ? 0.4514 0.2678 0.3375 -0.1567 0.1217  -0.0625 381 HOH   A O   
6995 O  O   A HOH   E .   ? 0.1489 0.1680 0.1824 0.0106  -0.0191 0.0086  382 HOH   A O   
6996 O  O   . HOH   E .   ? 0.3274 0.2807 0.3565 -0.0113 -0.0458 0.0968  383 HOH   A O   
6997 O  O   . HOH   E .   ? 0.3397 0.7042 0.3532 0.1636  0.0905  -0.0587 384 HOH   A O   
6998 O  O   . HOH   E .   ? 0.1780 0.2796 0.2624 0.0526  0.0367  0.0637  385 HOH   A O   
6999 O  O   . HOH   E .   ? 0.5204 0.6748 0.5725 0.0373  0.0875  0.0493  386 HOH   A O   
7000 O  O   . HOH   E .   ? 0.2524 0.2663 0.3507 0.0255  0.0137  0.0889  387 HOH   A O   
7001 O  O   . HOH   E .   ? 0.1471 0.1499 0.1958 0.0007  -0.0225 0.0058  388 HOH   A O   
7002 O  O   . HOH   E .   ? 0.2690 0.4680 0.3670 0.0517  0.0828  0.2261  389 HOH   A O   
7003 O  O   . HOH   E .   ? 0.3060 0.3284 0.2365 0.0104  0.0659  0.0095  390 HOH   A O   
7004 O  O   . HOH   E .   ? 0.2637 0.2017 0.3573 0.0102  -0.0514 0.0181  391 HOH   A O   
7005 O  O   . HOH   E .   ? 0.2779 0.4116 0.4160 -0.0400 0.1263  -0.0594 392 HOH   A O   
7006 O  O   . HOH   E .   ? 0.5739 0.5992 0.5081 0.1310  -0.1355 -0.1444 393 HOH   A O   
7007 O  O   . HOH   E .   ? 0.3663 0.3243 0.2870 -0.0434 -0.1173 0.0738  394 HOH   A O   
7008 O  O   . HOH   E .   ? 0.1894 0.2749 0.3553 -0.0299 0.0738  0.0388  395 HOH   A O   
7009 O  O   B HOH   E .   ? 0.1511 0.2946 0.2463 -0.0426 0.0085  0.0420  396 HOH   A O   
7010 O  O   . HOH   E .   ? 0.2270 0.2308 0.2949 -0.0226 -0.0140 0.0789  397 HOH   A O   
7011 O  O   A HOH   E .   ? 0.3788 0.5609 0.3260 0.1465  -0.0064 -0.0369 398 HOH   A O   
7012 O  O   . HOH   E .   ? 0.3306 0.2597 0.2525 -0.0504 -0.0955 0.0277  399 HOH   A O   
7013 O  O   . HOH   E .   ? 0.1969 0.1948 0.3823 0.0376  0.0992  0.0773  400 HOH   A O   
7014 O  O   A HOH   E .   ? 0.2975 0.2088 0.4171 -0.0086 0.0845  0.0117  401 HOH   A O   
7015 O  O   . HOH   E .   ? 0.6223 0.6241 0.6903 -0.0282 -0.1298 0.2090  402 HOH   A O   
7016 O  O   . HOH   E .   ? 0.4853 0.4149 0.6354 0.1439  0.0872  -0.1387 403 HOH   A O   
7017 O  O   . HOH   E .   ? 0.5358 0.3896 0.3061 -0.0912 0.0137  0.0161  404 HOH   A O   
7018 O  O   A HOH   E .   ? 0.2944 0.2296 0.3095 0.0325  0.0935  0.0809  405 HOH   A O   
7019 O  O   . HOH   E .   ? 0.2160 0.2020 0.3353 0.0200  -0.0598 0.0277  406 HOH   A O   
7020 O  O   . HOH   E .   ? 0.5067 0.2787 0.3651 -0.1278 0.0386  0.0482  407 HOH   A O   
7021 O  O   . HOH   E .   ? 0.2567 0.2296 0.2776 -0.0474 -0.0090 0.0465  408 HOH   A O   
7022 O  O   . HOH   E .   ? 0.3888 0.6717 0.4498 -0.0677 0.0086  0.1777  409 HOH   A O   
7023 O  O   . HOH   E .   ? 0.6262 0.4670 0.4439 -0.1174 -0.0120 0.1279  410 HOH   A O   
7024 O  O   . HOH   E .   ? 0.4280 0.3548 0.4730 0.1133  0.0619  0.0074  411 HOH   A O   
7025 O  O   . HOH   E .   ? 0.1747 0.1937 0.3763 0.0085  0.0045  0.0322  412 HOH   A O   
7026 O  O   . HOH   E .   ? 0.2260 0.3109 0.2963 -0.0245 -0.0559 0.0707  413 HOH   A O   
7027 O  O   . HOH   E .   ? 0.4590 0.5642 0.5928 0.2587  0.1442  0.0408  414 HOH   A O   
7028 O  O   . HOH   E .   ? 0.2926 0.6402 0.1958 0.0184  0.0659  0.0347  415 HOH   A O   
7029 O  O   . HOH   E .   ? 0.2135 0.2866 0.4832 -0.0182 -0.0354 0.0515  416 HOH   A O   
7030 O  O   . HOH   E .   ? 0.2934 0.3439 0.7276 -0.0250 0.0235  -0.0562 417 HOH   A O   
7031 O  O   . HOH   E .   ? 0.4602 0.6757 0.3552 -0.0864 -0.0291 0.1332  418 HOH   A O   
7032 O  O   . HOH   E .   ? 0.2469 0.4085 0.2738 0.1405  -0.0054 0.0368  419 HOH   A O   
7033 O  O   . HOH   E .   ? 0.5970 0.6051 0.2897 0.0114  -0.0082 0.1261  420 HOH   A O   
7034 O  O   . HOH   E .   ? 0.2281 0.1735 0.1814 -0.0128 0.0135  0.0148  421 HOH   A O   
7035 O  O   . HOH   E .   ? 0.2367 0.2641 0.3207 -0.0078 -0.0218 -0.0086 422 HOH   A O   
7036 O  O   . HOH   E .   ? 0.3184 0.1421 0.2245 -0.0010 -0.0597 0.0217  423 HOH   A O   
7037 O  O   . HOH   E .   ? 0.1758 0.2337 0.2948 -0.0159 0.0002  0.0447  424 HOH   A O   
7038 O  O   . HOH   E .   ? 0.2683 0.3130 0.4038 -0.0067 -0.0340 -0.0989 425 HOH   A O   
7039 O  O   . HOH   E .   ? 0.5867 0.6961 0.3672 0.0533  0.2417  -0.0689 426 HOH   A O   
7040 O  O   . HOH   E .   ? 0.6753 0.4593 0.5841 0.1708  -0.0935 0.1562  427 HOH   A O   
7041 O  O   . HOH   E .   ? 0.6331 0.4525 0.4353 -0.0133 -0.1552 -0.0306 428 HOH   A O   
7042 O  O   . HOH   E .   ? 0.3849 0.2576 0.5526 -0.0724 -0.2355 0.1127  429 HOH   A O   
7043 O  O   . HOH   E .   ? 0.7152 0.8583 0.7810 0.0331  -0.0458 -0.0349 430 HOH   A O   
7044 O  O   A HOH   E .   ? 0.2096 0.1327 0.1340 -0.0055 0.0066  0.0185  431 HOH   A O   
7045 O  O   . HOH   E .   ? 0.3113 0.4623 0.5801 -0.0081 0.1143  -0.1871 432 HOH   A O   
7046 O  O   . HOH   E .   ? 0.3134 0.1894 0.3298 0.0252  -0.0047 0.0032  433 HOH   A O   
7047 O  O   . HOH   E .   ? 0.7307 0.7177 0.7183 -0.1261 0.0663  -0.1291 434 HOH   A O   
7048 O  O   . HOH   E .   ? 0.3725 0.3025 0.2096 -0.0828 0.0093  0.0572  435 HOH   A O   
7049 O  O   . HOH   E .   ? 0.5755 0.6479 0.5995 0.0238  0.0686  0.1942  436 HOH   A O   
7050 O  O   . HOH   E .   ? 0.4450 0.3840 0.3431 0.2435  -0.0400 -0.0289 437 HOH   A O   
7051 O  O   . HOH   E .   ? 0.1991 0.2249 0.4542 -0.0033 -0.0748 0.0471  438 HOH   A O   
7052 O  O   B HOH   E .   ? 0.2947 0.3310 0.2859 0.0277  -0.0696 -0.0361 439 HOH   A O   
7053 O  O   . HOH   E .   ? 0.7936 0.5530 0.7999 0.0413  -0.0981 0.1852  440 HOH   A O   
7054 O  O   A HOH   E .   ? 0.2207 0.1729 0.2836 0.0091  -0.0806 0.0119  441 HOH   A O   
7055 O  O   . HOH   E .   ? 0.2663 0.2990 0.2838 0.0121  -0.0004 -0.0474 442 HOH   A O   
7056 O  O   . HOH   E .   ? 0.2318 0.2275 0.3443 0.0112  0.0343  0.0522  443 HOH   A O   
7057 O  O   . HOH   E .   ? 0.6755 0.8779 0.6224 0.2339  -0.1155 0.2927  444 HOH   A O   
7058 O  O   . HOH   E .   ? 0.5632 0.5685 0.6503 0.0245  -0.0927 -0.1459 445 HOH   A O   
7059 O  O   . HOH   E .   ? 0.8004 0.6470 0.7579 0.0078  -0.0587 -0.0698 446 HOH   A O   
7060 O  O   B HOH   E .   ? 0.1866 0.1958 0.2140 -0.0335 -0.0435 0.0584  447 HOH   A O   
7061 O  O   . HOH   E .   ? 0.4362 0.4035 0.6731 -0.0232 0.0289  -0.1241 448 HOH   A O   
7062 O  O   A HOH   E .   ? 0.2028 0.2282 0.2996 0.0317  0.0146  0.0761  449 HOH   A O   
7063 O  O   . HOH   E .   ? 0.6470 0.7248 0.5426 -0.0897 0.1275  0.1094  450 HOH   A O   
7064 O  O   . HOH   E .   ? 0.4668 0.3371 0.3345 0.0589  0.0745  0.0136  451 HOH   A O   
7065 O  O   . HOH   E .   ? 0.4168 0.4520 0.3942 0.2189  -0.0560 0.0385  452 HOH   A O   
7066 O  O   . HOH   E .   ? 0.4004 0.5709 0.4249 0.0373  0.1371  -0.0438 453 HOH   A O   
7067 O  O   . HOH   E .   ? 0.5268 0.5988 0.4696 0.0023  -0.0432 0.1345  454 HOH   A O   
7068 O  O   . HOH   E .   ? 0.8093 0.7492 0.4840 0.0354  -0.0926 -0.0617 455 HOH   A O   
7069 O  O   . HOH   E .   ? 0.2765 0.2713 0.3983 -0.0219 0.0041  -0.0523 456 HOH   A O   
7070 O  O   . HOH   E .   ? 0.4098 0.5718 0.5649 -0.1414 0.1686  -0.1109 457 HOH   A O   
7071 O  O   . HOH   E .   ? 0.3019 0.3984 0.6213 0.0280  -0.0771 -0.0805 458 HOH   A O   
7072 O  O   . HOH   E .   ? 0.4219 0.5520 0.5523 0.0756  -0.0200 0.1851  459 HOH   A O   
7073 O  O   . HOH   E .   ? 0.3264 0.2732 0.3949 -0.0946 0.0689  -0.0444 460 HOH   A O   
7074 O  O   . HOH   E .   ? 0.2748 0.4676 0.5613 0.0466  -0.0144 -0.1703 461 HOH   A O   
7075 O  O   . HOH   E .   ? 0.4040 0.4892 0.4904 -0.1549 0.0406  0.0159  462 HOH   A O   
7076 O  O   . HOH   E .   ? 0.5719 0.3850 0.7462 0.1374  -0.0162 0.2255  463 HOH   A O   
7077 O  O   . HOH   E .   ? 0.4515 0.5636 0.4209 0.0609  -0.0844 -0.0835 464 HOH   A O   
7078 O  O   . HOH   E .   ? 0.3709 0.3051 0.4022 0.0063  0.1182  0.0133  465 HOH   A O   
7079 O  O   . HOH   E .   ? 0.2647 0.1798 0.2745 0.0238  -0.0743 -0.0187 466 HOH   A O   
7080 O  O   . HOH   E .   ? 0.3971 0.7327 0.3989 -0.0913 -0.1147 0.2175  467 HOH   A O   
7081 O  O   . HOH   E .   ? 0.5960 0.4787 0.5189 0.0274  0.1358  0.0618  468 HOH   A O   
7082 O  O   . HOH   E .   ? 0.7313 0.6997 0.6545 0.0696  0.0743  0.2139  469 HOH   A O   
7083 O  O   . HOH   E .   ? 0.6038 0.5681 0.4385 0.1413  -0.0519 -0.0604 470 HOH   A O   
7084 O  O   . HOH   E .   ? 0.2821 0.3136 0.2614 0.0528  0.0015  0.0251  471 HOH   A O   
7085 O  O   . HOH   E .   ? 0.4245 0.4723 0.5184 -0.2034 -0.0196 -0.0012 472 HOH   A O   
7086 O  O   . HOH   E .   ? 0.5413 0.3191 0.3707 -0.0417 -0.1546 0.0306  473 HOH   A O   
7087 O  O   . HOH   E .   ? 0.6804 0.7462 0.7098 -0.1256 -0.1349 0.0226  474 HOH   A O   
7088 O  O   . HOH   E .   ? 0.4343 0.5240 0.3284 0.0333  0.0007  0.0392  475 HOH   A O   
7089 O  O   . HOH   E .   ? 0.6151 0.4402 0.5308 -0.0066 -0.0634 -0.1317 476 HOH   A O   
7090 O  O   . HOH   E .   ? 0.2902 0.3540 0.6381 -0.0138 0.1228  -0.0966 477 HOH   A O   
7091 O  O   . HOH   E .   ? 0.4345 0.4473 0.5633 -0.1162 0.0651  0.0845  478 HOH   A O   
7092 O  O   . HOH   E .   ? 0.7730 0.4730 0.3579 -0.0298 -0.1442 0.0331  479 HOH   A O   
7093 O  O   . HOH   E .   ? 0.3229 0.4911 0.4670 0.0017  0.1363  0.1070  480 HOH   A O   
7094 O  O   . HOH   E .   ? 0.3464 0.2541 0.7005 0.0247  0.0828  0.0857  481 HOH   A O   
7095 O  O   . HOH   E .   ? 0.8174 0.7680 0.6104 0.1879  -0.1431 -0.0990 482 HOH   A O   
7096 O  O   . HOH   E .   ? 0.8018 0.6412 0.7746 -0.0610 0.0713  -0.1168 483 HOH   A O   
7097 O  O   . HOH   E .   ? 0.8560 0.8559 0.6200 -0.0916 0.1055  0.1986  484 HOH   A O   
7098 O  O   . HOH   E .   ? 0.5016 0.5451 0.3944 -0.0640 -0.0564 -0.0227 485 HOH   A O   
7099 O  O   . HOH   E .   ? 0.2592 0.2439 0.6638 0.0029  -0.1015 0.0235  486 HOH   A O   
7100 O  O   . HOH   E .   ? 0.5037 0.3682 0.2872 -0.0956 0.1621  -0.0543 487 HOH   A O   
7101 O  O   . HOH   E .   ? 0.5855 0.6339 0.7307 0.0506  0.2744  -0.1189 488 HOH   A O   
7102 O  O   . HOH   E .   ? 0.6189 0.7038 0.6669 0.1357  -0.1237 0.1018  489 HOH   A O   
7103 O  O   . HOH   E .   ? 0.2589 0.5583 0.3862 0.0877  0.0826  0.2589  490 HOH   A O   
7104 O  O   . HOH   E .   ? 0.6873 0.4152 0.4863 -0.0473 0.0882  0.0139  491 HOH   A O   
7105 O  O   . HOH   E .   ? 0.4932 0.5390 0.4814 0.0462  -0.0557 -0.0528 492 HOH   A O   
7106 O  O   . HOH   E .   ? 0.6839 0.4816 0.5652 -0.1055 -0.0767 -0.0921 493 HOH   A O   
7107 O  O   . HOH   E .   ? 0.4987 0.3410 0.4537 -0.0098 0.2030  0.0389  494 HOH   A O   
7108 O  O   . HOH   E .   ? 0.3044 0.4894 0.3839 -0.0173 -0.0392 -0.0703 495 HOH   A O   
7109 O  O   . HOH   E .   ? 0.2884 0.4064 0.3754 0.0819  -0.0534 0.0872  496 HOH   A O   
7110 O  O   . HOH   E .   ? 0.2969 0.4996 0.5521 0.0609  -0.0986 -0.0046 497 HOH   A O   
7111 O  O   . HOH   E .   ? 0.4693 0.8850 0.6910 -0.0336 -0.0723 0.2290  498 HOH   A O   
7112 O  O   . HOH   E .   ? 0.6560 0.2910 0.4630 -0.0397 0.1506  0.0408  499 HOH   A O   
7113 O  O   B HOH   E .   ? 0.3480 0.3227 0.2399 0.0109  0.0227  0.0615  500 HOH   A O   
7114 O  O   . HOH   E .   ? 0.6053 0.8666 0.6020 0.1079  -0.0544 0.1651  501 HOH   A O   
7115 O  O   . HOH   E .   ? 0.5608 0.2777 0.4227 -0.0114 -0.0419 0.1063  502 HOH   A O   
7116 O  O   . HOH   E .   ? 0.5339 0.7605 0.6273 0.3081  -0.0179 0.1840  503 HOH   A O   
7117 O  O   . HOH   E .   ? 0.3450 0.2738 0.4858 -0.0230 0.0055  0.0633  504 HOH   A O   
7118 O  O   A HOH   E .   ? 0.3001 0.5998 0.2857 0.1242  0.0867  0.1170  505 HOH   A O   
7119 O  O   . HOH   E .   ? 0.7091 0.5893 0.4966 -0.0916 -0.1204 -0.1323 506 HOH   A O   
7120 O  O   . HOH   E .   ? 0.3104 0.6686 0.5198 0.0427  0.0735  -0.0494 507 HOH   A O   
7121 O  O   . HOH   E .   ? 0.5125 0.7563 0.5242 -0.0813 -0.0677 0.1334  508 HOH   A O   
7122 O  O   . HOH   E .   ? 0.5082 0.5854 0.4705 0.1353  0.0240  0.1737  509 HOH   A O   
7123 O  O   . HOH   E .   ? 0.2968 0.5060 0.6088 -0.0453 -0.0847 0.3149  510 HOH   A O   
7124 O  O   . HOH   F .   ? 0.2356 0.2286 0.2919 0.0139  0.0539  0.0360  201 HOH   B O   
7125 O  O   . HOH   F .   ? 0.3445 0.4451 0.7210 -0.0015 -0.0040 -0.0725 202 HOH   B O   
7126 O  O   . HOH   F .   ? 0.3473 0.2373 0.5853 -0.0095 0.1991  0.0272  203 HOH   B O   
7127 O  O   . HOH   F .   ? 0.3427 0.5685 0.4915 -0.0262 0.1796  -0.1823 204 HOH   B O   
7128 O  O   . HOH   F .   ? 0.7547 0.3938 0.4390 0.0603  0.0616  -0.0208 205 HOH   B O   
7129 O  O   . HOH   F .   ? 0.4820 0.6835 0.3059 -0.0942 -0.1296 0.0061  206 HOH   B O   
7130 O  O   . HOH   F .   ? 0.3275 0.5300 0.2620 -0.0261 -0.0255 -0.1311 207 HOH   B O   
7131 O  O   . HOH   F .   ? 0.5378 0.4135 0.4462 -0.0273 0.0020  -0.2065 208 HOH   B O   
7132 O  O   . HOH   F .   ? 0.2819 0.7003 0.3949 0.0789  0.0223  0.2462  209 HOH   B O   
7133 O  O   . HOH   F .   ? 0.3540 0.4160 0.5579 -0.0842 0.0247  -0.1352 210 HOH   B O   
7134 O  O   . HOH   F .   ? 0.1762 0.2135 0.3108 -0.0205 -0.0076 0.0167  211 HOH   B O   
7135 O  O   . HOH   F .   ? 0.1921 0.2393 0.3030 0.0039  0.0243  -0.0264 212 HOH   B O   
7136 O  O   . HOH   F .   ? 0.2863 0.2031 0.4934 0.0073  0.1299  0.0706  213 HOH   B O   
7137 O  O   . HOH   F .   ? 0.7886 0.5425 0.4708 0.2610  -0.0462 -0.1182 214 HOH   B O   
7138 O  O   . HOH   F .   ? 0.5116 0.6090 0.4382 0.3005  -0.1309 -0.0287 215 HOH   B O   
7139 O  O   . HOH   F .   ? 0.3827 0.3960 0.3606 0.0102  -0.1113 0.0537  216 HOH   B O   
7140 O  O   . HOH   F .   ? 0.2719 0.2763 0.6172 0.0617  -0.0850 0.0171  217 HOH   B O   
7141 O  O   . HOH   F .   ? 0.6573 0.7039 0.5809 0.2196  0.0522  0.0168  218 HOH   B O   
7142 O  O   . HOH   F .   ? 0.4502 0.5872 0.4391 0.2704  0.0299  0.0238  219 HOH   B O   
7143 O  O   . HOH   F .   ? 0.1809 0.2366 0.3750 -0.0172 0.0175  -0.0227 220 HOH   B O   
7144 O  O   . HOH   F .   ? 0.3824 0.5446 0.6432 0.2434  0.0608  -0.0615 221 HOH   B O   
7145 O  O   . HOH   F .   ? 0.5912 0.8034 0.4605 0.3089  0.1033  0.1427  222 HOH   B O   
7146 O  O   . HOH   F .   ? 0.4369 0.3835 0.6217 -0.0027 -0.1532 -0.0788 223 HOH   B O   
7147 O  O   . HOH   F .   ? 0.1862 0.1522 0.3668 -0.0128 -0.0244 -0.0283 224 HOH   B O   
7148 O  O   . HOH   F .   ? 0.2515 0.6019 0.5509 0.1405  -0.0491 -0.0773 225 HOH   B O   
7149 O  O   . HOH   F .   ? 0.2392 0.1905 0.2639 -0.0280 0.0752  -0.0125 226 HOH   B O   
7150 O  O   . HOH   F .   ? 0.6104 0.3350 0.3745 -0.2475 0.0004  0.0102  227 HOH   B O   
7151 O  O   . HOH   F .   ? 0.2456 0.2488 0.3635 -0.0383 0.0112  -0.0402 228 HOH   B O   
7152 O  O   . HOH   F .   ? 0.3627 0.3390 0.4094 0.0399  -0.1131 -0.0074 229 HOH   B O   
7153 O  O   . HOH   F .   ? 0.4152 0.4046 0.4239 -0.1013 0.1327  -0.0948 230 HOH   B O   
7154 O  O   . HOH   F .   ? 0.5528 0.2172 0.3186 -0.0052 -0.0806 0.0077  231 HOH   B O   
7155 O  O   . HOH   F .   ? 0.3087 0.3468 0.3422 -0.1122 0.0481  -0.0313 232 HOH   B O   
7156 O  O   . HOH   F .   ? 0.2109 0.1451 0.3714 0.0149  -0.0447 -0.0093 233 HOH   B O   
7157 O  O   . HOH   F .   ? 0.4944 0.4563 0.4211 0.0467  0.1039  -0.1925 234 HOH   B O   
7158 O  O   . HOH   F .   ? 0.3897 0.2017 0.2151 0.0273  -0.0796 -0.0058 235 HOH   B O   
7159 O  O   . HOH   F .   ? 0.4214 0.3094 0.2265 0.0468  0.0794  0.0337  236 HOH   B O   
7160 O  O   . HOH   F .   ? 0.2656 0.2783 0.3467 0.0135  0.0127  -0.1010 237 HOH   B O   
7161 O  O   . HOH   F .   ? 0.6337 0.4754 0.3192 -0.0805 0.0531  -0.0106 238 HOH   B O   
7162 O  O   . HOH   F .   ? 0.2920 0.3424 0.3340 -0.0777 0.0478  -0.0528 239 HOH   B O   
7163 O  O   . HOH   F .   ? 0.4425 0.3069 0.4729 -0.1238 -0.0574 -0.0201 240 HOH   B O   
7164 O  O   . HOH   F .   ? 0.3843 0.3194 0.5356 -0.0505 -0.0821 0.1217  241 HOH   B O   
7165 O  O   . HOH   F .   ? 0.2295 0.3529 0.2801 -0.0244 -0.0253 0.0656  242 HOH   B O   
7166 O  O   . HOH   F .   ? 0.2629 0.2270 0.3084 0.0631  0.0532  -0.0160 243 HOH   B O   
7167 O  O   . HOH   F .   ? 0.3105 0.1930 0.6428 -0.0044 -0.1135 -0.0156 244 HOH   B O   
7168 O  O   . HOH   F .   ? 0.2520 0.3278 0.2385 -0.0607 0.0238  0.0454  245 HOH   B O   
7169 O  O   . HOH   F .   ? 0.5350 0.4406 0.6489 0.0837  -0.0508 0.2847  246 HOH   B O   
7170 O  O   . HOH   F .   ? 0.1647 0.1542 0.1599 -0.0092 -0.0102 -0.0071 247 HOH   B O   
7171 O  O   . HOH   F .   ? 0.3830 0.2624 0.4550 0.0368  -0.1099 -0.1256 248 HOH   B O   
7172 O  O   . HOH   F .   ? 0.1620 0.1372 0.1705 -0.0013 -0.0136 0.0052  249 HOH   B O   
7173 O  O   . HOH   F .   ? 0.2564 0.2351 0.2908 0.0837  -0.0913 -0.0625 250 HOH   B O   
7174 O  O   . HOH   F .   ? 0.2318 0.2015 0.2310 -0.0332 -0.0393 0.0238  251 HOH   B O   
7175 O  O   . HOH   F .   ? 0.3611 0.3003 0.3263 -0.0477 0.0257  -0.0517 252 HOH   B O   
7176 O  O   . HOH   F .   ? 0.3716 0.2827 0.4292 0.0669  -0.0691 -0.0791 253 HOH   B O   
7177 O  O   . HOH   F .   ? 0.1756 0.1776 0.3359 -0.0226 -0.0205 0.0099  254 HOH   B O   
7178 O  O   . HOH   F .   ? 0.1643 0.1610 0.2857 -0.0059 0.0045  -0.0063 255 HOH   B O   
7179 O  O   . HOH   F .   ? 0.2362 0.4275 0.3619 -0.0592 -0.0746 -0.0647 256 HOH   B O   
7180 O  O   . HOH   F .   ? 0.3407 0.2472 0.1999 0.0433  -0.0372 -0.0116 257 HOH   B O   
7181 O  O   . HOH   F .   ? 0.3347 0.4971 0.3418 -0.0158 -0.0920 0.0438  258 HOH   B O   
7182 O  O   . HOH   F .   ? 0.3565 0.4281 0.2778 -0.0144 0.0784  0.0022  259 HOH   B O   
7183 O  O   . HOH   F .   ? 0.5766 0.6385 0.3879 -0.0429 -0.0186 0.0373  260 HOH   B O   
7184 O  O   . HOH   F .   ? 0.2301 0.1638 0.2123 -0.0284 -0.0495 0.0233  261 HOH   B O   
7185 O  O   . HOH   F .   ? 0.3107 0.4368 0.2860 -0.1108 -0.0539 -0.0352 262 HOH   B O   
7186 O  O   . HOH   F .   ? 0.2239 0.2177 0.3490 -0.0051 -0.0595 -0.0287 263 HOH   B O   
7187 O  O   . HOH   F .   ? 0.3136 0.2279 0.4685 0.0282  0.0604  0.0708  264 HOH   B O   
7188 O  O   . HOH   F .   ? 0.1992 0.2325 0.3262 0.0129  -0.0059 -0.0026 265 HOH   B O   
7189 O  O   . HOH   F .   ? 0.1992 0.2699 0.2804 0.0272  0.0399  0.0841  266 HOH   B O   
7190 O  O   . HOH   F .   ? 0.1516 0.1749 0.2339 -0.0035 0.0015  0.0196  267 HOH   B O   
7191 O  O   . HOH   F .   ? 0.3755 0.3832 0.4573 0.1415  -0.0628 -0.1141 268 HOH   B O   
7192 O  O   . HOH   F .   ? 0.2263 0.5343 0.4833 0.0014  -0.0164 -0.1465 269 HOH   B O   
7193 O  O   . HOH   F .   ? 0.2571 0.2045 0.3123 -0.0519 0.0273  -0.0138 270 HOH   B O   
7194 O  O   . HOH   F .   ? 0.3306 0.4993 0.6678 -0.1170 -0.0374 -0.1389 271 HOH   B O   
7195 O  O   . HOH   F .   ? 0.2817 0.3933 0.3916 0.0344  0.1259  0.0400  272 HOH   B O   
7196 O  O   . HOH   F .   ? 0.4509 0.2769 0.4784 -0.0348 -0.1223 -0.0420 273 HOH   B O   
7197 O  O   . HOH   F .   ? 0.2027 0.1893 0.1749 -0.0471 -0.0523 0.0201  274 HOH   B O   
7198 O  O   . HOH   F .   ? 0.2393 0.2427 0.5249 -0.0621 0.0016  0.1369  275 HOH   B O   
7199 O  O   . HOH   F .   ? 0.2512 0.2745 0.2062 0.0044  0.0023  -0.0012 276 HOH   B O   
7200 O  O   . HOH   F .   ? 0.2336 0.2610 0.2310 -0.0400 -0.0479 -0.0316 277 HOH   B O   
7201 O  O   . HOH   F .   ? 0.3177 0.7463 0.7436 0.1423  -0.0833 -0.1106 278 HOH   B O   
7202 O  O   . HOH   F .   ? 0.2281 0.1648 0.2379 -0.0254 -0.0249 0.0154  279 HOH   B O   
7203 O  O   . HOH   F .   ? 0.7814 0.6687 0.3865 0.0813  -0.0167 0.1356  280 HOH   B O   
7204 O  O   . HOH   F .   ? 0.2564 0.2973 0.2654 -0.0468 -0.0791 0.0271  281 HOH   B O   
7205 O  O   . HOH   F .   ? 0.4297 0.3948 0.6173 -0.1699 -0.0104 0.1341  282 HOH   B O   
7206 O  O   . HOH   F .   ? 0.4345 0.4903 0.3302 0.0164  0.0056  -0.0487 283 HOH   B O   
7207 O  O   . HOH   F .   ? 0.1890 0.1671 0.2053 -0.0012 0.0107  -0.0010 284 HOH   B O   
7208 O  O   . HOH   F .   ? 0.5050 0.4217 0.4431 -0.0133 0.0406  0.0891  285 HOH   B O   
7209 O  O   . HOH   F .   ? 0.3259 0.3184 0.2994 -0.0424 0.0497  -0.1287 286 HOH   B O   
7210 O  O   . HOH   F .   ? 0.2397 0.3569 0.3438 -0.0258 0.0290  -0.1127 287 HOH   B O   
7211 O  O   . HOH   F .   ? 0.2681 0.4151 0.2615 0.1175  -0.0411 -0.0431 288 HOH   B O   
7212 O  O   . HOH   F .   ? 0.1959 0.4181 0.4872 0.0543  -0.0263 -0.1574 289 HOH   B O   
7213 O  O   . HOH   F .   ? 0.1822 0.1722 0.3414 -0.0147 0.0029  0.0015  290 HOH   B O   
7214 O  O   . HOH   F .   ? 0.2994 0.4852 0.5230 -0.0906 -0.1169 0.0614  291 HOH   B O   
7215 O  O   . HOH   F .   ? 0.5239 0.5180 0.5062 0.2193  0.0008  0.1193  292 HOH   B O   
7216 O  O   . HOH   F .   ? 0.4124 0.2188 0.4556 -0.0750 -0.2329 0.0712  293 HOH   B O   
7217 O  O   . HOH   F .   ? 0.3862 0.2591 0.2380 0.0224  -0.0984 -0.0035 294 HOH   B O   
7218 O  O   . HOH   F .   ? 0.4574 0.4748 0.3865 -0.2171 0.1466  -0.0334 295 HOH   B O   
7219 O  O   . HOH   F .   ? 0.1736 0.2177 0.1716 -0.0165 -0.0226 0.0218  296 HOH   B O   
7220 O  O   . HOH   F .   ? 0.2724 0.2605 0.3145 -0.0109 -0.0945 0.0344  297 HOH   B O   
7221 O  O   . HOH   F .   ? 0.4772 0.5494 0.4755 0.0095  -0.1627 0.0291  298 HOH   B O   
7222 O  O   . HOH   F .   ? 0.4366 0.5131 0.6703 0.0424  0.0613  0.0272  299 HOH   B O   
7223 O  O   . HOH   F .   ? 0.4194 0.3913 0.2607 0.0834  -0.0785 0.0762  300 HOH   B O   
7224 O  O   . HOH   F .   ? 0.2831 0.6981 0.2678 0.1022  -0.0602 -0.0931 301 HOH   B O   
7225 O  O   . HOH   F .   ? 0.4140 0.5075 0.8024 -0.0230 -0.1069 0.2530  302 HOH   B O   
7226 O  O   . HOH   F .   ? 0.7253 0.4657 0.5253 0.1433  0.1622  0.0323  303 HOH   B O   
7227 O  O   . HOH   F .   ? 0.3006 0.3090 0.3621 -0.0319 0.1037  -0.0844 304 HOH   B O   
7228 O  O   . HOH   F .   ? 0.1878 0.1791 0.2739 0.0108  -0.0008 0.0250  305 HOH   B O   
7229 O  O   . HOH   F .   ? 0.2442 0.1847 0.2688 -0.0233 -0.0302 0.0006  306 HOH   B O   
7230 O  O   . HOH   F .   ? 0.2332 0.6187 0.5325 -0.1172 -0.0399 0.0274  307 HOH   B O   
7231 O  O   . HOH   F .   ? 0.2246 0.3675 0.6164 0.0799  -0.0550 -0.1697 308 HOH   B O   
7232 O  O   . HOH   F .   ? 0.6087 0.4144 0.3763 0.2722  0.1715  0.1018  309 HOH   B O   
7233 O  O   . HOH   F .   ? 0.6186 0.2878 0.3414 0.0647  0.0874  0.0904  310 HOH   B O   
7234 O  O   . HOH   F .   ? 0.2123 0.1737 0.3428 0.0297  -0.0816 0.0167  311 HOH   B O   
7235 O  O   . HOH   F .   ? 0.4646 0.3110 0.2427 -0.1856 0.0444  -0.0123 312 HOH   B O   
7236 O  O   . HOH   F .   ? 0.4687 0.5266 0.2636 0.0158  0.1267  0.1105  313 HOH   B O   
7237 O  O   . HOH   F .   ? 0.1798 0.1585 0.3535 0.0060  0.0014  0.0035  314 HOH   B O   
7238 O  O   . HOH   F .   ? 0.1812 0.2684 0.2328 -0.0085 -0.0179 0.0631  315 HOH   B O   
7239 O  O   . HOH   F .   ? 0.3437 0.1977 0.3664 0.0645  0.0870  0.0122  316 HOH   B O   
7240 O  O   . HOH   F .   ? 0.2415 0.3255 0.3776 0.0801  -0.0547 -0.1101 317 HOH   B O   
7241 O  O   . HOH   F .   ? 0.5256 0.4318 0.2610 -0.0080 -0.0172 -0.0467 318 HOH   B O   
7242 O  O   . HOH   F .   ? 0.2765 0.1684 0.2864 -0.0238 -0.0363 0.0388  319 HOH   B O   
7243 O  O   . HOH   F .   ? 0.1724 0.2031 0.3210 -0.0337 -0.0122 0.0072  320 HOH   B O   
7244 O  O   . HOH   F .   ? 0.3872 0.2303 0.2981 0.1203  0.0954  0.0314  321 HOH   B O   
7245 O  O   . HOH   F .   ? 0.2215 0.3220 0.5316 -0.0274 -0.0818 -0.0126 322 HOH   B O   
7246 O  O   . HOH   F .   ? 0.4781 0.6424 0.4559 0.1634  -0.0670 0.0987  323 HOH   B O   
7247 O  O   . HOH   F .   ? 0.2392 0.1945 0.1958 -0.0058 0.0101  0.0202  324 HOH   B O   
7248 O  O   . HOH   F .   ? 0.1714 0.1722 0.3453 -0.0110 -0.0062 -0.0162 325 HOH   B O   
7249 O  O   . HOH   F .   ? 0.6139 0.5236 0.7335 0.1895  -0.0861 0.1941  326 HOH   B O   
7250 O  O   . HOH   F .   ? 0.3369 0.2462 0.2590 0.0362  -0.0333 0.0264  327 HOH   B O   
7251 O  O   . HOH   F .   ? 0.5345 0.3717 0.4088 -0.0929 0.0623  0.0784  328 HOH   B O   
7252 O  O   . HOH   F .   ? 0.5518 0.3979 0.4589 -0.0562 0.1333  -0.1603 329 HOH   B O   
7253 O  O   . HOH   F .   ? 0.5905 0.4142 0.4434 0.1012  0.1807  0.1839  330 HOH   B O   
7254 O  O   . HOH   F .   ? 0.4765 0.3264 0.5587 0.1339  0.2407  0.1811  331 HOH   B O   
7255 O  O   . HOH   F .   ? 0.2018 0.1983 0.2999 0.0251  0.0427  0.0307  332 HOH   B O   
7256 O  O   . HOH   F .   ? 0.2836 0.2175 0.3384 -0.0050 -0.0126 0.0381  333 HOH   B O   
7257 O  O   . HOH   F .   ? 0.2722 0.2010 0.3899 0.0328  -0.0853 -0.0506 334 HOH   B O   
7258 O  O   . HOH   F .   ? 0.5069 0.4297 0.5603 0.0485  -0.0050 0.0531  335 HOH   B O   
7259 O  O   . HOH   F .   ? 0.2973 0.3541 0.5798 -0.0972 -0.1770 0.1839  336 HOH   B O   
7260 O  O   . HOH   F .   ? 0.1921 0.1549 0.2550 0.0039  -0.0129 0.0146  337 HOH   B O   
7261 O  O   . HOH   F .   ? 0.8500 0.2834 0.4232 0.1066  -0.1233 -0.0337 338 HOH   B O   
7262 O  O   . HOH   F .   ? 0.5699 0.4982 0.5595 -0.1107 -0.0951 -0.1352 339 HOH   B O   
7263 O  O   . HOH   F .   ? 0.4990 0.4756 0.2350 0.1382  -0.0790 -0.0222 340 HOH   B O   
7264 O  O   . HOH   F .   ? 0.4879 0.7069 0.4465 -0.1126 -0.1050 0.2085  341 HOH   B O   
7265 O  O   . HOH   F .   ? 0.4212 0.5290 0.4563 -0.1346 -0.0609 -0.0572 342 HOH   B O   
7266 O  O   . HOH   F .   ? 0.6407 0.5876 0.5948 -0.1162 -0.0663 0.1609  343 HOH   B O   
7267 O  O   . HOH   F .   ? 0.5848 0.6172 0.7799 -0.0409 -0.0360 -0.0155 344 HOH   B O   
7268 O  O   . HOH   F .   ? 0.4858 0.4016 0.3442 0.0532  -0.1175 -0.1065 345 HOH   B O   
7269 O  O   . HOH   F .   ? 0.2188 0.2467 0.3731 -0.0178 0.0779  -0.0475 346 HOH   B O   
7270 O  O   . HOH   F .   ? 0.3621 0.4827 0.5747 -0.1567 0.0054  -0.0252 347 HOH   B O   
7271 O  O   . HOH   F .   ? 0.4519 0.6484 0.6147 0.0271  -0.1205 -0.0060 348 HOH   B O   
7272 O  O   . HOH   F .   ? 0.2518 0.6479 0.3201 0.1548  -0.0765 -0.1532 349 HOH   B O   
7273 O  O   . HOH   F .   ? 0.5055 0.5871 0.6331 -0.1323 0.0354  0.1211  350 HOH   B O   
7274 O  O   . HOH   F .   ? 0.3440 0.2389 0.5145 -0.0552 -0.0765 -0.0421 351 HOH   B O   
7275 O  O   . HOH   F .   ? 0.5580 0.5925 0.3784 -0.0503 -0.1279 0.0215  352 HOH   B O   
7276 O  O   . HOH   F .   ? 0.4347 0.6182 0.7174 0.0723  0.0538  -0.0901 353 HOH   B O   
7277 O  O   . HOH   F .   ? 0.5080 0.5400 0.4746 0.1890  -0.1044 0.1112  354 HOH   B O   
7278 O  O   . HOH   F .   ? 0.2603 0.4276 0.4879 0.0530  0.0305  0.0161  355 HOH   B O   
7279 O  O   . HOH   F .   ? 0.3969 0.2290 0.3283 -0.0809 0.0263  -0.0856 356 HOH   B O   
7280 O  O   . HOH   F .   ? 0.4998 0.3166 0.5613 -0.1198 0.1535  -0.0115 357 HOH   B O   
7281 O  O   . HOH   F .   ? 0.3649 0.2549 0.4464 -0.0754 -0.0104 -0.0332 358 HOH   B O   
7282 O  O   . HOH   F .   ? 0.5591 0.3589 0.4970 0.0480  0.1752  -0.0684 359 HOH   B O   
7283 O  O   . HOH   F .   ? 0.5604 0.3707 0.5470 -0.0235 -0.1484 -0.0695 360 HOH   B O   
7284 O  O   . HOH   F .   ? 0.6206 0.2610 0.3727 -0.0389 0.0260  0.0742  361 HOH   B O   
7285 O  O   . HOH   F .   ? 0.5218 0.4335 0.5870 0.0239  0.1081  0.1015  362 HOH   B O   
7286 O  O   . HOH   F .   ? 0.4141 0.6841 0.3688 0.2057  0.0003  0.0546  363 HOH   B O   
7287 O  O   . HOH   F .   ? 0.2349 0.4027 0.7281 -0.0811 -0.0777 -0.0544 364 HOH   B O   
7288 O  O   . HOH   F .   ? 0.5281 0.6071 0.5308 -0.0989 -0.0119 -0.1121 365 HOH   B O   
7289 O  O   . HOH   F .   ? 0.5878 0.5090 0.5061 0.0658  -0.0275 0.0493  366 HOH   B O   
7290 O  O   . HOH   F .   ? 0.5744 0.3194 0.5583 -0.1511 -0.0185 0.0188  367 HOH   B O   
7291 O  O   . HOH   F .   ? 0.3202 0.3287 0.5430 0.0317  -0.1638 -0.0115 368 HOH   B O   
7292 O  O   . HOH   F .   ? 0.6226 0.4979 0.4481 0.0964  0.0338  0.0535  369 HOH   B O   
7293 O  O   . HOH   F .   ? 0.5798 0.5893 0.3583 0.2040  -0.1770 0.0427  370 HOH   B O   
7294 O  O   . HOH   F .   ? 0.4486 0.6188 0.5436 0.2599  0.1120  0.1759  371 HOH   B O   
7295 O  O   . HOH   F .   ? 0.4377 0.3556 0.3269 0.0915  -0.1116 -0.0501 372 HOH   B O   
7296 O  O   . HOH   F .   ? 0.7133 0.3942 0.3531 -0.0420 -0.1249 -0.1029 373 HOH   B O   
7297 O  O   . HOH   F .   ? 0.4526 0.4676 0.5205 -0.0262 -0.0860 -0.0200 374 HOH   B O   
7298 O  O   . HOH   F .   ? 0.8144 0.8301 0.6343 0.2433  -0.0857 0.0498  375 HOH   B O   
7299 O  O   . HOH   F .   ? 0.4172 0.6743 0.6506 0.1275  -0.0232 -0.0576 376 HOH   B O   
7300 O  O   . HOH   F .   ? 0.5294 0.7828 0.4579 -0.1498 0.0239  -0.1493 377 HOH   B O   
7301 O  O   . HOH   F .   ? 0.2388 0.3880 0.4145 0.0188  -0.0428 -0.0518 378 HOH   B O   
7302 O  O   . HOH   F .   ? 0.3233 0.6244 0.2284 0.0035  -0.0036 0.0318  379 HOH   B O   
7303 O  O   . HOH   F .   ? 0.5462 0.6845 0.6502 0.1721  0.0549  0.2446  380 HOH   B O   
7304 O  O   . HOH   F .   ? 0.5513 0.7637 0.7515 -0.1045 0.2147  0.0671  381 HOH   B O   
7305 O  O   . HOH   F .   ? 0.7179 0.3899 0.5029 -0.0604 -0.0509 -0.0108 382 HOH   B O   
7306 O  O   . HOH   F .   ? 0.2877 0.2906 0.3171 0.0190  0.0162  0.0211  383 HOH   B O   
7307 O  O   . HOH   F .   ? 0.6813 0.3569 0.4598 0.0091  0.0997  -0.0682 384 HOH   B O   
7308 O  O   . HOH   F .   ? 0.4984 0.8998 0.5675 0.1473  0.1057  -0.0344 385 HOH   B O   
7309 O  O   . HOH   F .   ? 0.7988 0.6053 0.5031 0.2330  0.0582  -0.0128 386 HOH   B O   
7310 O  O   . HOH   F .   ? 0.6374 0.4860 0.5401 -0.0820 0.0969  -0.0170 387 HOH   B O   
7311 O  O   . HOH   F .   ? 0.2511 0.4736 0.4321 -0.0586 -0.0973 -0.0547 388 HOH   B O   
7312 O  O   . HOH   F .   ? 0.5804 0.5004 0.3334 -0.0477 0.1097  -0.0369 389 HOH   B O   
7313 O  O   . HOH   F .   ? 0.4890 0.4291 0.4932 -0.2100 -0.0157 0.1012  390 HOH   B O   
7314 O  O   . HOH   F .   ? 0.4761 0.2584 0.3919 0.1010  -0.0681 0.0133  391 HOH   B O   
7315 O  O   . HOH   F .   ? 0.6260 0.5870 0.5277 0.1296  0.0699  -0.0031 392 HOH   B O   
7316 O  O   . HOH   F .   ? 0.2738 0.5254 0.6931 -0.1679 -0.0567 -0.0600 393 HOH   B O   
7317 O  O   . HOH   F .   ? 0.3850 0.2453 0.4966 -0.0487 -0.0557 0.0799  394 HOH   B O   
7318 O  O   . HOH   F .   ? 0.2182 0.2923 0.5484 -0.0597 -0.0835 0.0198  395 HOH   B O   
7319 O  O   . HOH   F .   ? 0.3435 0.4353 0.4354 0.0211  0.0308  -0.1108 396 HOH   B O   
7320 O  O   . HOH   F .   ? 0.5070 0.6319 0.4913 0.1288  0.0200  -0.1056 397 HOH   B O   
7321 O  O   . HOH   F .   ? 0.4896 0.4791 0.4881 0.0681  0.1099  0.0685  398 HOH   B O   
7322 O  O   . HOH   F .   ? 0.5000 0.5644 0.5206 -0.0487 -0.1630 0.1956  399 HOH   B O   
7323 O  O   . HOH   F .   ? 0.5770 0.4085 0.3622 -0.2522 -0.0337 0.1029  400 HOH   B O   
7324 O  O   . HOH   F .   ? 0.6422 0.5322 0.3971 0.1428  -0.0665 -0.0497 401 HOH   B O   
# 
