data_7HDQ
# 
_entry.id   7HDQ 
# 
_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   7HDQ         pdb_00007hdq 10.2210/pdb7hdq/pdb 
WWPDB D_1001407344 ?            ?                   
# 
_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                        7HDQ 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                           18178.766 2   '3.4.19.121, 3.4.22.-' ? ? 
'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'trifluoroacetic acid'                                               114.023   1   ?                      ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                 78.133    1   ?                      ? ? ? 
4 non-polymer syn '(1S,2S)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]cyclopentan-1-ol' 218.255   1   ?                      ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                                                       35.453    1   ?                      ? ? ? 
6 water       nat water                                                                18.015    426 ?                      ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                               TFA   
3 'DIMETHYL SULFOXIDE'                                                 DMS   
4 '(1S,2S)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]cyclopentan-1-ol' A1A8X 
5 'CHLORIDE ION'                                                       CL    
6 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 
A1A8X non-polymer         . '(1S,2S)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]cyclopentan-1-ol' ? 'C11 H14 N4 O'   218.255 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                 ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                            ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                      ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                              ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                            ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                           ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                              ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                               ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                           ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                        ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                              ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                               ? 'C3 H7 N O3'     105.093 
TFA   non-polymer         . 'trifluoroacetic acid'                                               ? 'C2 H F3 O2'     114.023 
THR   'L-peptide linking' y THREONINE                                                            ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                             ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                               ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TFA   1   201 201  TFA   TFA A . 
D 3 DMS   1   202 301  DMS   DMS A . 
E 4 A1A8X 1   203 201  A1A8X LA1 A . 
F 5 CL    1   204 1    CL    CL  A . 
G 6 HOH   1   301 409  HOH   HOH A . 
G 6 HOH   2   302 292  HOH   HOH A . 
G 6 HOH   3   303 196  HOH   HOH A . 
G 6 HOH   4   304 14   HOH   HOH A . 
G 6 HOH   5   305 625  HOH   HOH A . 
G 6 HOH   6   306 132  HOH   HOH A . 
G 6 HOH   7   307 493  HOH   HOH A . 
G 6 HOH   8   308 1289 HOH   HOH A . 
G 6 HOH   9   309 229  HOH   HOH A . 
G 6 HOH   10  310 209  HOH   HOH A . 
G 6 HOH   11  311 18   HOH   HOH A . 
G 6 HOH   12  312 109  HOH   HOH A . 
G 6 HOH   13  313 153  HOH   HOH A . 
G 6 HOH   14  314 122  HOH   HOH A . 
G 6 HOH   15  315 151  HOH   HOH A . 
G 6 HOH   16  316 3    HOH   HOH A . 
G 6 HOH   17  317 247  HOH   HOH A . 
G 6 HOH   18  318 393  HOH   HOH A . 
G 6 HOH   19  319 76   HOH   HOH A . 
G 6 HOH   20  320 1295 HOH   HOH A . 
G 6 HOH   21  321 1275 HOH   HOH A . 
G 6 HOH   22  322 225  HOH   HOH A . 
G 6 HOH   23  323 351  HOH   HOH A . 
G 6 HOH   24  324 136  HOH   HOH A . 
G 6 HOH   25  325 236  HOH   HOH A . 
G 6 HOH   26  326 124  HOH   HOH A . 
G 6 HOH   27  327 278  HOH   HOH A . 
G 6 HOH   28  328 405  HOH   HOH A . 
G 6 HOH   29  329 15   HOH   HOH A . 
G 6 HOH   30  330 192  HOH   HOH A . 
G 6 HOH   31  331 1301 HOH   HOH A . 
G 6 HOH   32  332 140  HOH   HOH A . 
G 6 HOH   33  333 19   HOH   HOH A . 
G 6 HOH   34  334 296  HOH   HOH A . 
G 6 HOH   35  335 8    HOH   HOH A . 
G 6 HOH   36  336 964  HOH   HOH A . 
G 6 HOH   37  337 241  HOH   HOH A . 
G 6 HOH   38  338 105  HOH   HOH A . 
G 6 HOH   39  339 148  HOH   HOH A . 
G 6 HOH   40  340 630  HOH   HOH A . 
G 6 HOH   41  341 354  HOH   HOH A . 
G 6 HOH   42  342 337  HOH   HOH A . 
G 6 HOH   43  343 164  HOH   HOH A . 
G 6 HOH   44  344 86   HOH   HOH A . 
G 6 HOH   45  345 165  HOH   HOH A . 
G 6 HOH   46  346 469  HOH   HOH A . 
G 6 HOH   47  347 320  HOH   HOH A . 
G 6 HOH   48  348 1290 HOH   HOH A . 
G 6 HOH   49  349 1283 HOH   HOH A . 
G 6 HOH   50  350 85   HOH   HOH A . 
G 6 HOH   51  351 92   HOH   HOH A . 
G 6 HOH   52  352 102  HOH   HOH A . 
G 6 HOH   53  353 195  HOH   HOH A . 
G 6 HOH   54  354 661  HOH   HOH A . 
G 6 HOH   55  355 1300 HOH   HOH A . 
G 6 HOH   56  356 57   HOH   HOH A . 
G 6 HOH   57  357 6    HOH   HOH A . 
G 6 HOH   58  358 42   HOH   HOH A . 
G 6 HOH   59  359 93   HOH   HOH A . 
G 6 HOH   60  360 21   HOH   HOH A . 
G 6 HOH   61  361 5    HOH   HOH A . 
G 6 HOH   62  362 396  HOH   HOH A . 
G 6 HOH   63  363 169  HOH   HOH A . 
G 6 HOH   64  364 155  HOH   HOH A . 
G 6 HOH   65  365 39   HOH   HOH A . 
G 6 HOH   66  366 162  HOH   HOH A . 
G 6 HOH   67  367 139  HOH   HOH A . 
G 6 HOH   68  368 2    HOH   HOH A . 
G 6 HOH   69  369 33   HOH   HOH A . 
G 6 HOH   70  370 66   HOH   HOH A . 
G 6 HOH   71  371 81   HOH   HOH A . 
G 6 HOH   72  372 186  HOH   HOH A . 
G 6 HOH   73  373 36   HOH   HOH A . 
G 6 HOH   74  374 7    HOH   HOH A . 
G 6 HOH   75  375 5    HOH   HOH A . 
G 6 HOH   76  376 138  HOH   HOH A . 
G 6 HOH   77  377 45   HOH   HOH A . 
G 6 HOH   78  378 19   HOH   HOH A . 
G 6 HOH   79  379 56   HOH   HOH A . 
G 6 HOH   80  380 159  HOH   HOH A . 
G 6 HOH   81  381 35   HOH   HOH A . 
G 6 HOH   82  382 939  HOH   HOH A . 
G 6 HOH   83  383 134  HOH   HOH A . 
G 6 HOH   84  384 46   HOH   HOH A . 
G 6 HOH   85  385 26   HOH   HOH A . 
G 6 HOH   86  386 27   HOH   HOH A . 
G 6 HOH   87  387 49   HOH   HOH A . 
G 6 HOH   88  388 140  HOH   HOH A . 
G 6 HOH   89  389 70   HOH   HOH A . 
G 6 HOH   90  390 17   HOH   HOH A . 
G 6 HOH   91  391 58   HOH   HOH A . 
G 6 HOH   92  392 461  HOH   HOH A . 
G 6 HOH   93  393 6    HOH   HOH A . 
G 6 HOH   94  394 333  HOH   HOH A . 
G 6 HOH   95  395 218  HOH   HOH A . 
G 6 HOH   96  396 154  HOH   HOH A . 
G 6 HOH   97  397 366  HOH   HOH A . 
G 6 HOH   98  398 1308 HOH   HOH A . 
G 6 HOH   99  399 115  HOH   HOH A . 
G 6 HOH   100 400 74   HOH   HOH A . 
G 6 HOH   101 401 116  HOH   HOH A . 
G 6 HOH   102 402 13   HOH   HOH A . 
G 6 HOH   103 403 303  HOH   HOH A . 
G 6 HOH   104 404 83   HOH   HOH A . 
G 6 HOH   105 405 121  HOH   HOH A . 
G 6 HOH   106 406 12   HOH   HOH A . 
G 6 HOH   107 407 96   HOH   HOH A . 
G 6 HOH   108 408 199  HOH   HOH A . 
G 6 HOH   109 409 18   HOH   HOH A . 
G 6 HOH   110 410 78   HOH   HOH A . 
G 6 HOH   111 411 1315 HOH   HOH A . 
G 6 HOH   112 412 281  HOH   HOH A . 
G 6 HOH   113 413 34   HOH   HOH A . 
G 6 HOH   114 414 67   HOH   HOH A . 
G 6 HOH   115 415 1310 HOH   HOH A . 
G 6 HOH   116 416 662  HOH   HOH A . 
G 6 HOH   117 417 25   HOH   HOH A . 
G 6 HOH   118 418 17   HOH   HOH A . 
G 6 HOH   119 419 397  HOH   HOH A . 
G 6 HOH   120 420 68   HOH   HOH A . 
G 6 HOH   121 421 123  HOH   HOH A . 
G 6 HOH   122 422 4    HOH   HOH A . 
G 6 HOH   123 423 1094 HOH   HOH A . 
G 6 HOH   124 424 1068 HOH   HOH A . 
G 6 HOH   125 425 1313 HOH   HOH A . 
G 6 HOH   126 426 51   HOH   HOH A . 
G 6 HOH   127 427 125  HOH   HOH A . 
G 6 HOH   128 428 3    HOH   HOH A . 
G 6 HOH   129 429 95   HOH   HOH A . 
G 6 HOH   130 430 53   HOH   HOH A . 
G 6 HOH   131 431 156  HOH   HOH A . 
G 6 HOH   132 432 1279 HOH   HOH A . 
G 6 HOH   133 433 24   HOH   HOH A . 
G 6 HOH   134 434 381  HOH   HOH A . 
G 6 HOH   135 435 4    HOH   HOH A . 
G 6 HOH   136 436 582  HOH   HOH A . 
G 6 HOH   137 437 212  HOH   HOH A . 
G 6 HOH   138 438 1222 HOH   HOH A . 
G 6 HOH   139 439 7    HOH   HOH A . 
G 6 HOH   140 440 16   HOH   HOH A . 
G 6 HOH   141 441 71   HOH   HOH A . 
G 6 HOH   142 442 73   HOH   HOH A . 
G 6 HOH   143 443 1286 HOH   HOH A . 
G 6 HOH   144 444 80   HOH   HOH A . 
G 6 HOH   145 445 1309 HOH   HOH A . 
G 6 HOH   146 446 1189 HOH   HOH A . 
G 6 HOH   147 447 1296 HOH   HOH A . 
G 6 HOH   148 448 2    HOH   HOH A . 
G 6 HOH   149 449 40   HOH   HOH A . 
G 6 HOH   150 450 952  HOH   HOH A . 
G 6 HOH   151 451 94   HOH   HOH A . 
G 6 HOH   152 452 188  HOH   HOH A . 
G 6 HOH   153 453 944  HOH   HOH A . 
G 6 HOH   154 454 1238 HOH   HOH A . 
G 6 HOH   155 455 97   HOH   HOH A . 
G 6 HOH   156 456 104  HOH   HOH A . 
G 6 HOH   157 457 79   HOH   HOH A . 
G 6 HOH   158 458 576  HOH   HOH A . 
G 6 HOH   159 459 330  HOH   HOH A . 
G 6 HOH   160 460 1119 HOH   HOH A . 
G 6 HOH   161 461 107  HOH   HOH A . 
G 6 HOH   162 462 509  HOH   HOH A . 
G 6 HOH   163 463 1134 HOH   HOH A . 
G 6 HOH   164 464 726  HOH   HOH A . 
G 6 HOH   165 465 408  HOH   HOH A . 
G 6 HOH   166 466 163  HOH   HOH A . 
G 6 HOH   167 467 756  HOH   HOH A . 
G 6 HOH   168 468 361  HOH   HOH A . 
G 6 HOH   169 469 126  HOH   HOH A . 
G 6 HOH   170 470 801  HOH   HOH A . 
G 6 HOH   171 471 556  HOH   HOH A . 
G 6 HOH   172 472 319  HOH   HOH A . 
G 6 HOH   173 473 280  HOH   HOH A . 
G 6 HOH   174 474 12   HOH   HOH A . 
G 6 HOH   175 475 63   HOH   HOH A . 
G 6 HOH   176 476 250  HOH   HOH A . 
G 6 HOH   177 477 8    HOH   HOH A . 
G 6 HOH   178 478 1307 HOH   HOH A . 
G 6 HOH   179 479 342  HOH   HOH A . 
G 6 HOH   180 480 1276 HOH   HOH A . 
G 6 HOH   181 481 370  HOH   HOH A . 
G 6 HOH   182 482 1287 HOH   HOH A . 
G 6 HOH   183 483 267  HOH   HOH A . 
G 6 HOH   184 484 1306 HOH   HOH A . 
G 6 HOH   185 485 224  HOH   HOH A . 
G 6 HOH   186 486 695  HOH   HOH A . 
G 6 HOH   187 487 674  HOH   HOH A . 
G 6 HOH   188 488 202  HOH   HOH A . 
G 6 HOH   189 489 326  HOH   HOH A . 
G 6 HOH   190 490 919  HOH   HOH A . 
G 6 HOH   191 491 135  HOH   HOH A . 
G 6 HOH   192 492 309  HOH   HOH A . 
G 6 HOH   193 493 318  HOH   HOH A . 
G 6 HOH   194 494 1299 HOH   HOH A . 
G 6 HOH   195 495 805  HOH   HOH A . 
G 6 HOH   196 496 10   HOH   HOH A . 
G 6 HOH   197 497 711  HOH   HOH A . 
G 6 HOH   198 498 331  HOH   HOH A . 
G 6 HOH   199 499 1314 HOH   HOH A . 
G 6 HOH   200 500 315  HOH   HOH A . 
G 6 HOH   201 501 263  HOH   HOH A . 
G 6 HOH   202 502 521  HOH   HOH A . 
G 6 HOH   203 503 941  HOH   HOH A . 
G 6 HOH   204 504 152  HOH   HOH A . 
G 6 HOH   205 505 208  HOH   HOH A . 
G 6 HOH   206 506 1071 HOH   HOH A . 
G 6 HOH   207 507 180  HOH   HOH A . 
G 6 HOH   208 508 356  HOH   HOH A . 
G 6 HOH   209 509 16   HOH   HOH A . 
G 6 HOH   210 510 350  HOH   HOH A . 
G 6 HOH   211 511 363  HOH   HOH A . 
G 6 HOH   212 512 371  HOH   HOH A . 
G 6 HOH   213 513 1284 HOH   HOH A . 
G 6 HOH   214 514 313  HOH   HOH A . 
G 6 HOH   215 515 772  HOH   HOH A . 
G 6 HOH   216 516 185  HOH   HOH A . 
G 6 HOH   217 517 429  HOH   HOH A . 
G 6 HOH   218 518 70   HOH   HOH A . 
G 6 HOH   219 519 376  HOH   HOH A . 
G 6 HOH   220 520 1074 HOH   HOH A . 
G 6 HOH   221 521 15   HOH   HOH A . 
G 6 HOH   222 522 11   HOH   HOH A . 
G 6 HOH   223 523 346  HOH   HOH A . 
G 6 HOH   224 524 1292 HOH   HOH A . 
G 6 HOH   225 525 1078 HOH   HOH A . 
H 6 HOH   1   201 64   HOH   HOH B . 
H 6 HOH   2   202 549  HOH   HOH B . 
H 6 HOH   3   203 900  HOH   HOH B . 
H 6 HOH   4   204 358  HOH   HOH B . 
H 6 HOH   5   205 364  HOH   HOH B . 
H 6 HOH   6   206 1249 HOH   HOH B . 
H 6 HOH   7   207 758  HOH   HOH B . 
H 6 HOH   8   208 240  HOH   HOH B . 
H 6 HOH   9   209 398  HOH   HOH B . 
H 6 HOH   10  210 531  HOH   HOH B . 
H 6 HOH   11  211 343  HOH   HOH B . 
H 6 HOH   12  212 264  HOH   HOH B . 
H 6 HOH   13  213 1140 HOH   HOH B . 
H 6 HOH   14  214 743  HOH   HOH B . 
H 6 HOH   15  215 353  HOH   HOH B . 
H 6 HOH   16  216 50   HOH   HOH B . 
H 6 HOH   17  217 120  HOH   HOH B . 
H 6 HOH   18  218 131  HOH   HOH B . 
H 6 HOH   19  219 654  HOH   HOH B . 
H 6 HOH   20  220 444  HOH   HOH B . 
H 6 HOH   21  221 232  HOH   HOH B . 
H 6 HOH   22  222 452  HOH   HOH B . 
H 6 HOH   23  223 276  HOH   HOH B . 
H 6 HOH   24  224 54   HOH   HOH B . 
H 6 HOH   25  225 75   HOH   HOH B . 
H 6 HOH   26  226 1278 HOH   HOH B . 
H 6 HOH   27  227 82   HOH   HOH B . 
H 6 HOH   28  228 723  HOH   HOH B . 
H 6 HOH   29  229 1312 HOH   HOH B . 
H 6 HOH   30  230 128  HOH   HOH B . 
H 6 HOH   31  231 205  HOH   HOH B . 
H 6 HOH   32  232 272  HOH   HOH B . 
H 6 HOH   33  233 332  HOH   HOH B . 
H 6 HOH   34  234 69   HOH   HOH B . 
H 6 HOH   35  235 60   HOH   HOH B . 
H 6 HOH   36  236 127  HOH   HOH B . 
H 6 HOH   37  237 282  HOH   HOH B . 
H 6 HOH   38  238 110  HOH   HOH B . 
H 6 HOH   39  239 1    HOH   HOH B . 
H 6 HOH   40  240 133  HOH   HOH B . 
H 6 HOH   41  241 181  HOH   HOH B . 
H 6 HOH   42  242 325  HOH   HOH B . 
H 6 HOH   43  243 143  HOH   HOH B . 
H 6 HOH   44  244 300  HOH   HOH B . 
H 6 HOH   45  245 14   HOH   HOH B . 
H 6 HOH   46  246 30   HOH   HOH B . 
H 6 HOH   47  247 9    HOH   HOH B . 
H 6 HOH   48  248 347  HOH   HOH B . 
H 6 HOH   49  249 271  HOH   HOH B . 
H 6 HOH   50  250 52   HOH   HOH B . 
H 6 HOH   51  251 166  HOH   HOH B . 
H 6 HOH   52  252 144  HOH   HOH B . 
H 6 HOH   53  253 252  HOH   HOH B . 
H 6 HOH   54  254 31   HOH   HOH B . 
H 6 HOH   55  255 172  HOH   HOH B . 
H 6 HOH   56  256 129  HOH   HOH B . 
H 6 HOH   57  257 41   HOH   HOH B . 
H 6 HOH   58  258 150  HOH   HOH B . 
H 6 HOH   59  259 231  HOH   HOH B . 
H 6 HOH   60  260 47   HOH   HOH B . 
H 6 HOH   61  261 10   HOH   HOH B . 
H 6 HOH   62  262 72   HOH   HOH B . 
H 6 HOH   63  263 62   HOH   HOH B . 
H 6 HOH   64  264 103  HOH   HOH B . 
H 6 HOH   65  265 61   HOH   HOH B . 
H 6 HOH   66  266 391  HOH   HOH B . 
H 6 HOH   67  267 11   HOH   HOH B . 
H 6 HOH   68  268 1106 HOH   HOH B . 
H 6 HOH   69  269 243  HOH   HOH B . 
H 6 HOH   70  270 59   HOH   HOH B . 
H 6 HOH   71  271 20   HOH   HOH B . 
H 6 HOH   72  272 242  HOH   HOH B . 
H 6 HOH   73  273 117  HOH   HOH B . 
H 6 HOH   74  274 77   HOH   HOH B . 
H 6 HOH   75  275 84   HOH   HOH B . 
H 6 HOH   76  276 302  HOH   HOH B . 
H 6 HOH   77  277 147  HOH   HOH B . 
H 6 HOH   78  278 114  HOH   HOH B . 
H 6 HOH   79  279 22   HOH   HOH B . 
H 6 HOH   80  280 221  HOH   HOH B . 
H 6 HOH   81  281 43   HOH   HOH B . 
H 6 HOH   82  282 235  HOH   HOH B . 
H 6 HOH   83  283 635  HOH   HOH B . 
H 6 HOH   84  284 1277 HOH   HOH B . 
H 6 HOH   85  285 287  HOH   HOH B . 
H 6 HOH   86  286 13   HOH   HOH B . 
H 6 HOH   87  287 1305 HOH   HOH B . 
H 6 HOH   88  288 416  HOH   HOH B . 
H 6 HOH   89  289 106  HOH   HOH B . 
H 6 HOH   90  290 216  HOH   HOH B . 
H 6 HOH   91  291 175  HOH   HOH B . 
H 6 HOH   92  292 1066 HOH   HOH B . 
H 6 HOH   93  293 89   HOH   HOH B . 
H 6 HOH   94  294 341  HOH   HOH B . 
H 6 HOH   95  295 137  HOH   HOH B . 
H 6 HOH   96  296 160  HOH   HOH B . 
H 6 HOH   97  297 32   HOH   HOH B . 
H 6 HOH   98  298 88   HOH   HOH B . 
H 6 HOH   99  299 112  HOH   HOH B . 
H 6 HOH   100 300 99   HOH   HOH B . 
H 6 HOH   101 301 387  HOH   HOH B . 
H 6 HOH   102 302 1285 HOH   HOH B . 
H 6 HOH   103 303 220  HOH   HOH B . 
H 6 HOH   104 304 311  HOH   HOH B . 
H 6 HOH   105 305 297  HOH   HOH B . 
H 6 HOH   106 306 299  HOH   HOH B . 
H 6 HOH   107 307 101  HOH   HOH B . 
H 6 HOH   108 308 316  HOH   HOH B . 
H 6 HOH   109 309 118  HOH   HOH B . 
H 6 HOH   110 310 38   HOH   HOH B . 
H 6 HOH   111 311 142  HOH   HOH B . 
H 6 HOH   112 312 37   HOH   HOH B . 
H 6 HOH   113 313 704  HOH   HOH B . 
H 6 HOH   114 314 215  HOH   HOH B . 
H 6 HOH   115 315 91   HOH   HOH B . 
H 6 HOH   116 316 170  HOH   HOH B . 
H 6 HOH   117 317 182  HOH   HOH B . 
H 6 HOH   118 318 48   HOH   HOH B . 
H 6 HOH   119 319 1291 HOH   HOH B . 
H 6 HOH   120 320 28   HOH   HOH B . 
H 6 HOH   121 321 141  HOH   HOH B . 
H 6 HOH   122 322 23   HOH   HOH B . 
H 6 HOH   123 323 177  HOH   HOH B . 
H 6 HOH   124 324 161  HOH   HOH B . 
H 6 HOH   125 325 44   HOH   HOH B . 
H 6 HOH   126 326 1274 HOH   HOH B . 
H 6 HOH   127 327 1294 HOH   HOH B . 
H 6 HOH   128 328 1126 HOH   HOH B . 
H 6 HOH   129 329 29   HOH   HOH B . 
H 6 HOH   130 330 100  HOH   HOH B . 
H 6 HOH   131 331 55   HOH   HOH B . 
H 6 HOH   132 332 197  HOH   HOH B . 
H 6 HOH   133 333 98   HOH   HOH B . 
H 6 HOH   134 334 334  HOH   HOH B . 
H 6 HOH   135 335 207  HOH   HOH B . 
H 6 HOH   136 336 717  HOH   HOH B . 
H 6 HOH   137 337 234  HOH   HOH B . 
H 6 HOH   138 338 445  HOH   HOH B . 
H 6 HOH   139 339 619  HOH   HOH B . 
H 6 HOH   140 340 65   HOH   HOH B . 
H 6 HOH   141 341 362  HOH   HOH B . 
H 6 HOH   142 342 339  HOH   HOH B . 
H 6 HOH   143 343 1293 HOH   HOH B . 
H 6 HOH   144 344 178  HOH   HOH B . 
H 6 HOH   145 345 960  HOH   HOH B . 
H 6 HOH   146 346 90   HOH   HOH B . 
H 6 HOH   147 347 623  HOH   HOH B . 
H 6 HOH   148 348 463  HOH   HOH B . 
H 6 HOH   149 349 335  HOH   HOH B . 
H 6 HOH   150 350 191  HOH   HOH B . 
H 6 HOH   151 351 1046 HOH   HOH B . 
H 6 HOH   152 352 1304 HOH   HOH B . 
H 6 HOH   153 353 304  HOH   HOH B . 
H 6 HOH   154 354 87   HOH   HOH B . 
H 6 HOH   155 355 290  HOH   HOH B . 
H 6 HOH   156 356 1280 HOH   HOH B . 
H 6 HOH   157 357 541  HOH   HOH B . 
H 6 HOH   158 358 203  HOH   HOH B . 
H 6 HOH   159 359 479  HOH   HOH B . 
H 6 HOH   160 360 389  HOH   HOH B . 
H 6 HOH   161 361 1077 HOH   HOH B . 
H 6 HOH   162 362 718  HOH   HOH B . 
H 6 HOH   163 363 283  HOH   HOH B . 
H 6 HOH   164 364 1072 HOH   HOH B . 
H 6 HOH   165 365 1316 HOH   HOH B . 
H 6 HOH   166 366 898  HOH   HOH B . 
H 6 HOH   167 367 340  HOH   HOH B . 
H 6 HOH   168 368 373  HOH   HOH B . 
H 6 HOH   169 369 615  HOH   HOH B . 
H 6 HOH   170 370 291  HOH   HOH B . 
H 6 HOH   171 371 1303 HOH   HOH B . 
H 6 HOH   172 372 667  HOH   HOH B . 
H 6 HOH   173 373 190  HOH   HOH B . 
H 6 HOH   174 374 310  HOH   HOH B . 
H 6 HOH   175 375 431  HOH   HOH B . 
H 6 HOH   176 376 149  HOH   HOH B . 
H 6 HOH   177 377 1173 HOH   HOH B . 
H 6 HOH   178 378 1163 HOH   HOH B . 
H 6 HOH   179 379 1000 HOH   HOH B . 
H 6 HOH   180 380 183  HOH   HOH B . 
H 6 HOH   181 381 176  HOH   HOH B . 
H 6 HOH   182 382 418  HOH   HOH B . 
H 6 HOH   183 383 1311 HOH   HOH B . 
H 6 HOH   184 384 424  HOH   HOH B . 
H 6 HOH   185 385 491  HOH   HOH B . 
H 6 HOH   186 386 248  HOH   HOH B . 
H 6 HOH   187 387 470  HOH   HOH B . 
H 6 HOH   188 388 981  HOH   HOH B . 
H 6 HOH   189 389 265  HOH   HOH B . 
H 6 HOH   190 390 1298 HOH   HOH B . 
H 6 HOH   191 391 184  HOH   HOH B . 
H 6 HOH   192 392 360  HOH   HOH B . 
H 6 HOH   193 393 410  HOH   HOH B . 
H 6 HOH   194 394 355  HOH   HOH B . 
H 6 HOH   195 395 566  HOH   HOH B . 
H 6 HOH   196 396 274  HOH   HOH B . 
H 6 HOH   197 397 157  HOH   HOH B . 
H 6 HOH   198 398 314  HOH   HOH B . 
H 6 HOH   199 399 321  HOH   HOH B . 
H 6 HOH   200 400 792  HOH   HOH B . 
H 6 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           7HDQ 
_cell.length_a           88.774 
_cell.length_b           88.774 
_cell.length_c           39.553 
_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                         7HDQ 
_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          7HDQ 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.71 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HDQ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.390 
_reflns.d_resolution_high            0.980 
_reflns.number_obs                   175743 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.500 
_reflns.pdbx_Rmerge_I_obs            0.042 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.300 
_reflns.B_iso_Wilson_estimate        11.570 
_reflns.pdbx_redundancy              6.200 
_reflns.pdbx_Rrim_I_all              0.045 
_reflns.pdbx_Rpim_I_all              0.018 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1084310 
_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 0.980 1.000  ? 26709 8031 ? 1.001 ? ? ? 3.300 ? 0.800  ? ? ? ? ? ? 92.200 1.185 0.617 0.609 
1 2 5.370 44.390 ? 7994  1166 ? 0.027 ? ? ? 6.900 ? 58.400 ? ? ? ? ? ? 99.800 0.030 0.011 0.999 
# 
_refine.entry_id                                 7HDQ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9800 
_refine.ls_d_res_low                             44.3900 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.5200 
_refine.ls_number_reflns_obs                     175663 
_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                          0.1456 
_refine.ls_R_factor_R_work                       0.1450 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1575 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  8468 
_refine.ls_number_reflns_R_work                  167195 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.6369 
_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                            0.1100 
_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                                63.990 
_refine.B_iso_min                                8.610 
_refine.pdbx_overall_phase_error                 17.5500 
_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                       0.9800 
_refine_hist.d_res_low                        44.3900 
_refine_hist.pdbx_number_atoms_ligand         48 
_refine_hist.number_atoms_solvent             426 
_refine_hist.number_atoms_total               3016 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           16.53 
_refine_hist.pdbx_B_iso_mean_solvent          29.61 
_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 
0.9800 0.9900  30 90.0000  5040 . 0.4043 0.4002 . 255 0.0000 5295 . 'X-RAY DIFFRACTION' 
0.9900 1.0000  30 98.0000  5410 . 0.3529 0.3526 . 272 0.0000 5682 . 'X-RAY DIFFRACTION' 
1.0000 1.0200  30 100.0000 5586 . 0.3105 0.2576 . 287 0.0000 5873 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 100.0000 5557 . 0.2597 0.2716 . 247 0.0000 5804 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5568 . 0.2357 0.2461 . 310 0.0000 5878 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 5553 . 0.2115 0.2135 . 290 0.0000 5843 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 5523 . 0.1975 0.2150 . 319 0.0000 5842 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 100.0000 5570 . 0.1840 0.1999 . 257 0.0000 5827 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 100.0000 5590 . 0.1694 0.1895 . 280 0.0000 5870 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5562 . 0.1581 0.1825 . 296 0.0000 5858 . 'X-RAY DIFFRACTION' 
1.1200 1.1400  30 100.0000 5611 . 0.1495 0.1672 . 244 0.0000 5855 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5590 . 0.1410 0.1421 . 268 0.0000 5858 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 5574 . 0.1285 0.1461 . 287 0.0000 5861 . 'X-RAY DIFFRACTION' 
1.1800 1.2100  30 100.0000 5531 . 0.1203 0.1507 . 313 0.0000 5844 . 'X-RAY DIFFRACTION' 
1.2100 1.2400  30 100.0000 5644 . 0.1192 0.1385 . 242 0.0000 5886 . 'X-RAY DIFFRACTION' 
1.2400 1.2600  30 100.0000 5583 . 0.1228 0.1364 . 278 0.0000 5861 . 'X-RAY DIFFRACTION' 
1.2600 1.3000  30 100.0000 5560 . 0.1218 0.1343 . 291 0.0000 5851 . 'X-RAY DIFFRACTION' 
1.3000 1.3300  30 100.0000 5577 . 0.1218 0.1411 . 301 0.0000 5878 . 'X-RAY DIFFRACTION' 
1.3300 1.3700  30 100.0000 5602 . 0.1315 0.1437 . 301 0.0000 5903 . 'X-RAY DIFFRACTION' 
1.3700 1.4100  30 100.0000 5633 . 0.1264 0.1617 . 247 0.0000 5880 . 'X-RAY DIFFRACTION' 
1.4100 1.4600  30 100.0000 5556 . 0.1262 0.1329 . 300 0.0000 5856 . 'X-RAY DIFFRACTION' 
1.4600 1.5200  30 100.0000 5607 . 0.1184 0.1274 . 267 0.0000 5874 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 5600 . 0.1179 0.1294 . 305 0.0000 5905 . 'X-RAY DIFFRACTION' 
1.5900 1.6800  30 100.0000 5600 . 0.1196 0.1318 . 279 0.0000 5879 . 'X-RAY DIFFRACTION' 
1.6800 1.7800  30 100.0000 5629 . 0.1297 0.1440 . 260 0.0000 5889 . 'X-RAY DIFFRACTION' 
1.7800 1.9200  30 100.0000 5593 . 0.1341 0.1355 . 306 0.0000 5899 . 'X-RAY DIFFRACTION' 
1.9200 2.1100  30 100.0000 5638 . 0.1372 0.1481 . 284 0.0000 5922 . 'X-RAY DIFFRACTION' 
2.1100 2.4200  30 100.0000 5623 . 0.1381 0.1333 . 310 0.0000 5933 . 'X-RAY DIFFRACTION' 
2.4200 3.0500  30 100.0000 5698 . 0.1502 0.1647 . 292 0.0000 5990 . 'X-RAY DIFFRACTION' 
3.0500 44.3900 30 100.0000 5787 . 0.1517 0.1759 . 280 0.0000 6067 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDQ 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003639' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDQ 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 6 ? 
# 
_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 7HDQ A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDQ 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 7HDQ SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDQ MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDQ SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDQ MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G 
2 1 B,H         
# 
_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 VAL B 95  ? O VAL B 95  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HDQ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   HD1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HIS 
_pdbx_validate_close_contact.auth_seq_id_1    91 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    305 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.60 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 HH A TYR 42 ? B 1_555 OD1 B ASP 67 ? ? 2_654 1.58 
2 1 O  A ASP 66 ? ? 1_555 HG  B SER 1  ? B 2_655 1.59 
# 
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  ? ? 55.18   -133.14 
2 1 SER A 167 ? B -141.02 21.44   
3 1 HIS B 86  ? ? 57.06   -128.25 
# 
_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 B A HOH 522 ? 5.90 . 
2 1 O ? A HOH 523 ? 5.97 . 
3 1 O ? A HOH 524 ? 6.06 . 
4 1 O ? A HOH 525 ? 7.55 . 
5 1 O ? B HOH 401 ? 6.30 . 
# 
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 
A1A8X N2   N  Y N 1   
A1A8X C3   C  N N 2   
A1A8X C6   C  Y N 3   
A1A8X C9   C  Y N 4   
A1A8X C1   C  N S 5   
A1A8X C10  C  Y N 6   
A1A8X C11  C  Y N 7   
A1A8X C2   C  N N 8   
A1A8X C4   C  N N 9   
A1A8X C5   C  N S 10  
A1A8X C7   C  Y N 11  
A1A8X C8   C  Y N 12  
A1A8X N1   N  N N 13  
A1A8X N3   N  Y N 14  
A1A8X N4   N  Y N 15  
A1A8X O1   O  N N 16  
A1A8X H7   H  N N 17  
A1A8X H6   H  N N 18  
A1A8X H1   H  N N 19  
A1A8X H12  H  N N 20  
A1A8X H13  H  N N 21  
A1A8X H5   H  N N 22  
A1A8X H4   H  N N 23  
A1A8X H9   H  N N 24  
A1A8X H8   H  N N 25  
A1A8X H2   H  N N 26  
A1A8X H11  H  N N 27  
A1A8X H10  H  N N 28  
A1A8X H14  H  N N 29  
A1A8X H3   H  N N 30  
ALA   N    N  N N 31  
ALA   CA   C  N S 32  
ALA   C    C  N N 33  
ALA   O    O  N N 34  
ALA   CB   C  N N 35  
ALA   OXT  O  N N 36  
ALA   H    H  N N 37  
ALA   H2   H  N N 38  
ALA   HA   H  N N 39  
ALA   HB1  H  N N 40  
ALA   HB2  H  N N 41  
ALA   HB3  H  N N 42  
ALA   HXT  H  N N 43  
ARG   N    N  N N 44  
ARG   CA   C  N S 45  
ARG   C    C  N N 46  
ARG   O    O  N N 47  
ARG   CB   C  N N 48  
ARG   CG   C  N N 49  
ARG   CD   C  N N 50  
ARG   NE   N  N N 51  
ARG   CZ   C  N N 52  
ARG   NH1  N  N N 53  
ARG   NH2  N  N N 54  
ARG   OXT  O  N N 55  
ARG   H    H  N N 56  
ARG   H2   H  N N 57  
ARG   HA   H  N N 58  
ARG   HB2  H  N N 59  
ARG   HB3  H  N N 60  
ARG   HG2  H  N N 61  
ARG   HG3  H  N N 62  
ARG   HD2  H  N N 63  
ARG   HD3  H  N N 64  
ARG   HE   H  N N 65  
ARG   HH11 H  N N 66  
ARG   HH12 H  N N 67  
ARG   HH21 H  N N 68  
ARG   HH22 H  N N 69  
ARG   HXT  H  N N 70  
ASN   N    N  N N 71  
ASN   CA   C  N S 72  
ASN   C    C  N N 73  
ASN   O    O  N N 74  
ASN   CB   C  N N 75  
ASN   CG   C  N N 76  
ASN   OD1  O  N N 77  
ASN   ND2  N  N N 78  
ASN   OXT  O  N N 79  
ASN   H    H  N N 80  
ASN   H2   H  N N 81  
ASN   HA   H  N N 82  
ASN   HB2  H  N N 83  
ASN   HB3  H  N N 84  
ASN   HD21 H  N N 85  
ASN   HD22 H  N N 86  
ASN   HXT  H  N N 87  
ASP   N    N  N N 88  
ASP   CA   C  N S 89  
ASP   C    C  N N 90  
ASP   O    O  N N 91  
ASP   CB   C  N N 92  
ASP   CG   C  N N 93  
ASP   OD1  O  N N 94  
ASP   OD2  O  N N 95  
ASP   OXT  O  N N 96  
ASP   H    H  N N 97  
ASP   H2   H  N N 98  
ASP   HA   H  N N 99  
ASP   HB2  H  N N 100 
ASP   HB3  H  N N 101 
ASP   HD2  H  N N 102 
ASP   HXT  H  N N 103 
CL    CL   CL N N 104 
CYS   N    N  N N 105 
CYS   CA   C  N R 106 
CYS   C    C  N N 107 
CYS   O    O  N N 108 
CYS   CB   C  N N 109 
CYS   SG   S  N N 110 
CYS   OXT  O  N N 111 
CYS   H    H  N N 112 
CYS   H2   H  N N 113 
CYS   HA   H  N N 114 
CYS   HB2  H  N N 115 
CYS   HB3  H  N N 116 
CYS   HG   H  N N 117 
CYS   HXT  H  N N 118 
DMS   S    S  N N 119 
DMS   O    O  N N 120 
DMS   C1   C  N N 121 
DMS   C2   C  N N 122 
DMS   H11  H  N N 123 
DMS   H12  H  N N 124 
DMS   H13  H  N N 125 
DMS   H21  H  N N 126 
DMS   H22  H  N N 127 
DMS   H23  H  N N 128 
GLN   N    N  N N 129 
GLN   CA   C  N S 130 
GLN   C    C  N N 131 
GLN   O    O  N N 132 
GLN   CB   C  N N 133 
GLN   CG   C  N N 134 
GLN   CD   C  N N 135 
GLN   OE1  O  N N 136 
GLN   NE2  N  N N 137 
GLN   OXT  O  N N 138 
GLN   H    H  N N 139 
GLN   H2   H  N N 140 
GLN   HA   H  N N 141 
GLN   HB2  H  N N 142 
GLN   HB3  H  N N 143 
GLN   HG2  H  N N 144 
GLN   HG3  H  N N 145 
GLN   HE21 H  N N 146 
GLN   HE22 H  N N 147 
GLN   HXT  H  N N 148 
GLU   N    N  N N 149 
GLU   CA   C  N S 150 
GLU   C    C  N N 151 
GLU   O    O  N N 152 
GLU   CB   C  N N 153 
GLU   CG   C  N N 154 
GLU   CD   C  N N 155 
GLU   OE1  O  N N 156 
GLU   OE2  O  N N 157 
GLU   OXT  O  N N 158 
GLU   H    H  N N 159 
GLU   H2   H  N N 160 
GLU   HA   H  N N 161 
GLU   HB2  H  N N 162 
GLU   HB3  H  N N 163 
GLU   HG2  H  N N 164 
GLU   HG3  H  N N 165 
GLU   HE2  H  N N 166 
GLU   HXT  H  N N 167 
GLY   N    N  N N 168 
GLY   CA   C  N N 169 
GLY   C    C  N N 170 
GLY   O    O  N N 171 
GLY   OXT  O  N N 172 
GLY   H    H  N N 173 
GLY   H2   H  N N 174 
GLY   HA2  H  N N 175 
GLY   HA3  H  N N 176 
GLY   HXT  H  N N 177 
HIS   N    N  N N 178 
HIS   CA   C  N S 179 
HIS   C    C  N N 180 
HIS   O    O  N N 181 
HIS   CB   C  N N 182 
HIS   CG   C  Y N 183 
HIS   ND1  N  Y N 184 
HIS   CD2  C  Y N 185 
HIS   CE1  C  Y N 186 
HIS   NE2  N  Y N 187 
HIS   OXT  O  N N 188 
HIS   H    H  N N 189 
HIS   H2   H  N N 190 
HIS   HA   H  N N 191 
HIS   HB2  H  N N 192 
HIS   HB3  H  N N 193 
HIS   HD1  H  N N 194 
HIS   HD2  H  N N 195 
HIS   HE1  H  N N 196 
HIS   HE2  H  N N 197 
HIS   HXT  H  N N 198 
HOH   O    O  N N 199 
HOH   H1   H  N N 200 
HOH   H2   H  N N 201 
ILE   N    N  N N 202 
ILE   CA   C  N S 203 
ILE   C    C  N N 204 
ILE   O    O  N N 205 
ILE   CB   C  N S 206 
ILE   CG1  C  N N 207 
ILE   CG2  C  N N 208 
ILE   CD1  C  N N 209 
ILE   OXT  O  N N 210 
ILE   H    H  N N 211 
ILE   H2   H  N N 212 
ILE   HA   H  N N 213 
ILE   HB   H  N N 214 
ILE   HG12 H  N N 215 
ILE   HG13 H  N N 216 
ILE   HG21 H  N N 217 
ILE   HG22 H  N N 218 
ILE   HG23 H  N N 219 
ILE   HD11 H  N N 220 
ILE   HD12 H  N N 221 
ILE   HD13 H  N N 222 
ILE   HXT  H  N N 223 
LEU   N    N  N N 224 
LEU   CA   C  N S 225 
LEU   C    C  N N 226 
LEU   O    O  N N 227 
LEU   CB   C  N N 228 
LEU   CG   C  N N 229 
LEU   CD1  C  N N 230 
LEU   CD2  C  N N 231 
LEU   OXT  O  N N 232 
LEU   H    H  N N 233 
LEU   H2   H  N N 234 
LEU   HA   H  N N 235 
LEU   HB2  H  N N 236 
LEU   HB3  H  N N 237 
LEU   HG   H  N N 238 
LEU   HD11 H  N N 239 
LEU   HD12 H  N N 240 
LEU   HD13 H  N N 241 
LEU   HD21 H  N N 242 
LEU   HD22 H  N N 243 
LEU   HD23 H  N N 244 
LEU   HXT  H  N N 245 
LYS   N    N  N N 246 
LYS   CA   C  N S 247 
LYS   C    C  N N 248 
LYS   O    O  N N 249 
LYS   CB   C  N N 250 
LYS   CG   C  N N 251 
LYS   CD   C  N N 252 
LYS   CE   C  N N 253 
LYS   NZ   N  N N 254 
LYS   OXT  O  N N 255 
LYS   H    H  N N 256 
LYS   H2   H  N N 257 
LYS   HA   H  N N 258 
LYS   HB2  H  N N 259 
LYS   HB3  H  N N 260 
LYS   HG2  H  N N 261 
LYS   HG3  H  N N 262 
LYS   HD2  H  N N 263 
LYS   HD3  H  N N 264 
LYS   HE2  H  N N 265 
LYS   HE3  H  N N 266 
LYS   HZ1  H  N N 267 
LYS   HZ2  H  N N 268 
LYS   HZ3  H  N N 269 
LYS   HXT  H  N N 270 
MET   N    N  N N 271 
MET   CA   C  N S 272 
MET   C    C  N N 273 
MET   O    O  N N 274 
MET   CB   C  N N 275 
MET   CG   C  N N 276 
MET   SD   S  N N 277 
MET   CE   C  N N 278 
MET   OXT  O  N N 279 
MET   H    H  N N 280 
MET   H2   H  N N 281 
MET   HA   H  N N 282 
MET   HB2  H  N N 283 
MET   HB3  H  N N 284 
MET   HG2  H  N N 285 
MET   HG3  H  N N 286 
MET   HE1  H  N N 287 
MET   HE2  H  N N 288 
MET   HE3  H  N N 289 
MET   HXT  H  N N 290 
PHE   N    N  N N 291 
PHE   CA   C  N S 292 
PHE   C    C  N N 293 
PHE   O    O  N N 294 
PHE   CB   C  N N 295 
PHE   CG   C  Y N 296 
PHE   CD1  C  Y N 297 
PHE   CD2  C  Y N 298 
PHE   CE1  C  Y N 299 
PHE   CE2  C  Y N 300 
PHE   CZ   C  Y N 301 
PHE   OXT  O  N N 302 
PHE   H    H  N N 303 
PHE   H2   H  N N 304 
PHE   HA   H  N N 305 
PHE   HB2  H  N N 306 
PHE   HB3  H  N N 307 
PHE   HD1  H  N N 308 
PHE   HD2  H  N N 309 
PHE   HE1  H  N N 310 
PHE   HE2  H  N N 311 
PHE   HZ   H  N N 312 
PHE   HXT  H  N N 313 
PRO   N    N  N N 314 
PRO   CA   C  N S 315 
PRO   C    C  N N 316 
PRO   O    O  N N 317 
PRO   CB   C  N N 318 
PRO   CG   C  N N 319 
PRO   CD   C  N N 320 
PRO   OXT  O  N N 321 
PRO   H    H  N N 322 
PRO   HA   H  N N 323 
PRO   HB2  H  N N 324 
PRO   HB3  H  N N 325 
PRO   HG2  H  N N 326 
PRO   HG3  H  N N 327 
PRO   HD2  H  N N 328 
PRO   HD3  H  N N 329 
PRO   HXT  H  N N 330 
SER   N    N  N N 331 
SER   CA   C  N S 332 
SER   C    C  N N 333 
SER   O    O  N N 334 
SER   CB   C  N N 335 
SER   OG   O  N N 336 
SER   OXT  O  N N 337 
SER   H    H  N N 338 
SER   H2   H  N N 339 
SER   HA   H  N N 340 
SER   HB2  H  N N 341 
SER   HB3  H  N N 342 
SER   HG   H  N N 343 
SER   HXT  H  N N 344 
TFA   C1   C  N N 345 
TFA   C2   C  N N 346 
TFA   O    O  N N 347 
TFA   F1   F  N N 348 
TFA   F2   F  N N 349 
TFA   F3   F  N N 350 
TFA   OXT  O  N N 351 
TFA   HXT  H  N N 352 
THR   N    N  N N 353 
THR   CA   C  N S 354 
THR   C    C  N N 355 
THR   O    O  N N 356 
THR   CB   C  N R 357 
THR   OG1  O  N N 358 
THR   CG2  C  N N 359 
THR   OXT  O  N N 360 
THR   H    H  N N 361 
THR   H2   H  N N 362 
THR   HA   H  N N 363 
THR   HB   H  N N 364 
THR   HG1  H  N N 365 
THR   HG21 H  N N 366 
THR   HG22 H  N N 367 
THR   HG23 H  N N 368 
THR   HXT  H  N N 369 
TYR   N    N  N N 370 
TYR   CA   C  N S 371 
TYR   C    C  N N 372 
TYR   O    O  N N 373 
TYR   CB   C  N N 374 
TYR   CG   C  Y N 375 
TYR   CD1  C  Y N 376 
TYR   CD2  C  Y N 377 
TYR   CE1  C  Y N 378 
TYR   CE2  C  Y N 379 
TYR   CZ   C  Y N 380 
TYR   OH   O  N N 381 
TYR   OXT  O  N N 382 
TYR   H    H  N N 383 
TYR   H2   H  N N 384 
TYR   HA   H  N N 385 
TYR   HB2  H  N N 386 
TYR   HB3  H  N N 387 
TYR   HD1  H  N N 388 
TYR   HD2  H  N N 389 
TYR   HE1  H  N N 390 
TYR   HE2  H  N N 391 
TYR   HH   H  N N 392 
TYR   HXT  H  N N 393 
VAL   N    N  N N 394 
VAL   CA   C  N S 395 
VAL   C    C  N N 396 
VAL   O    O  N N 397 
VAL   CB   C  N N 398 
VAL   CG1  C  N N 399 
VAL   CG2  C  N N 400 
VAL   OXT  O  N N 401 
VAL   H    H  N N 402 
VAL   H2   H  N N 403 
VAL   HA   H  N N 404 
VAL   HB   H  N N 405 
VAL   HG11 H  N N 406 
VAL   HG12 H  N N 407 
VAL   HG13 H  N N 408 
VAL   HG21 H  N N 409 
VAL   HG22 H  N N 410 
VAL   HG23 H  N N 411 
VAL   HXT  H  N N 412 
# 
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 
A1A8X C3  C4   sing N N 1   
A1A8X C3  C2   sing N N 2   
A1A8X C4  C5   sing N N 3   
A1A8X C2  C1   sing N N 4   
A1A8X C5  C1   sing N N 5   
A1A8X C5  N1   sing N N 6   
A1A8X C1  O1   sing N N 7   
A1A8X N1  C6   sing N N 8   
A1A8X C10 C9   sing Y N 9   
A1A8X C10 C11  doub Y N 10  
A1A8X C6  C9   doub Y N 11  
A1A8X C6  N2   sing Y N 12  
A1A8X C9  C8   sing Y N 13  
A1A8X C11 N4   sing Y N 14  
A1A8X N2  C7   doub Y N 15  
A1A8X C8  N4   sing Y N 16  
A1A8X C8  N3   doub Y N 17  
A1A8X C7  N3   sing Y N 18  
A1A8X C3  H7   sing N N 19  
A1A8X C3  H6   sing N N 20  
A1A8X C1  H1   sing N N 21  
A1A8X C10 H12  sing N N 22  
A1A8X C11 H13  sing N N 23  
A1A8X C2  H5   sing N N 24  
A1A8X C2  H4   sing N N 25  
A1A8X C4  H9   sing N N 26  
A1A8X C4  H8   sing N N 27  
A1A8X C5  H2   sing N N 28  
A1A8X C7  H11  sing N N 29  
A1A8X N1  H10  sing N N 30  
A1A8X N4  H14  sing N N 31  
A1A8X O1  H3   sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
CYS   N   CA   sing N N 102 
CYS   N   H    sing N N 103 
CYS   N   H2   sing N N 104 
CYS   CA  C    sing N N 105 
CYS   CA  CB   sing N N 106 
CYS   CA  HA   sing N N 107 
CYS   C   O    doub N N 108 
CYS   C   OXT  sing N N 109 
CYS   CB  SG   sing N N 110 
CYS   CB  HB2  sing N N 111 
CYS   CB  HB3  sing N N 112 
CYS   SG  HG   sing N N 113 
CYS   OXT HXT  sing N N 114 
DMS   S   O    doub N N 115 
DMS   S   C1   sing N N 116 
DMS   S   C2   sing N N 117 
DMS   C1  H11  sing N N 118 
DMS   C1  H12  sing N N 119 
DMS   C1  H13  sing N N 120 
DMS   C2  H21  sing N N 121 
DMS   C2  H22  sing N N 122 
DMS   C2  H23  sing N N 123 
GLN   N   CA   sing N N 124 
GLN   N   H    sing N N 125 
GLN   N   H2   sing N N 126 
GLN   CA  C    sing N N 127 
GLN   CA  CB   sing N N 128 
GLN   CA  HA   sing N N 129 
GLN   C   O    doub N N 130 
GLN   C   OXT  sing N N 131 
GLN   CB  CG   sing N N 132 
GLN   CB  HB2  sing N N 133 
GLN   CB  HB3  sing N N 134 
GLN   CG  CD   sing N N 135 
GLN   CG  HG2  sing N N 136 
GLN   CG  HG3  sing N N 137 
GLN   CD  OE1  doub N N 138 
GLN   CD  NE2  sing N N 139 
GLN   NE2 HE21 sing N N 140 
GLN   NE2 HE22 sing N N 141 
GLN   OXT HXT  sing N N 142 
GLU   N   CA   sing N N 143 
GLU   N   H    sing N N 144 
GLU   N   H2   sing N N 145 
GLU   CA  C    sing N N 146 
GLU   CA  CB   sing N N 147 
GLU   CA  HA   sing N N 148 
GLU   C   O    doub N N 149 
GLU   C   OXT  sing N N 150 
GLU   CB  CG   sing N N 151 
GLU   CB  HB2  sing N N 152 
GLU   CB  HB3  sing N N 153 
GLU   CG  CD   sing N N 154 
GLU   CG  HG2  sing N N 155 
GLU   CG  HG3  sing N N 156 
GLU   CD  OE1  doub N N 157 
GLU   CD  OE2  sing N N 158 
GLU   OE2 HE2  sing N N 159 
GLU   OXT HXT  sing N N 160 
GLY   N   CA   sing N N 161 
GLY   N   H    sing N N 162 
GLY   N   H2   sing N N 163 
GLY   CA  C    sing N N 164 
GLY   CA  HA2  sing N N 165 
GLY   CA  HA3  sing N N 166 
GLY   C   O    doub N N 167 
GLY   C   OXT  sing N N 168 
GLY   OXT HXT  sing N N 169 
HIS   N   CA   sing N N 170 
HIS   N   H    sing N N 171 
HIS   N   H2   sing N N 172 
HIS   CA  C    sing N N 173 
HIS   CA  CB   sing N N 174 
HIS   CA  HA   sing N N 175 
HIS   C   O    doub N N 176 
HIS   C   OXT  sing N N 177 
HIS   CB  CG   sing N N 178 
HIS   CB  HB2  sing N N 179 
HIS   CB  HB3  sing N N 180 
HIS   CG  ND1  sing Y N 181 
HIS   CG  CD2  doub Y N 182 
HIS   ND1 CE1  doub Y N 183 
HIS   ND1 HD1  sing N N 184 
HIS   CD2 NE2  sing Y N 185 
HIS   CD2 HD2  sing N N 186 
HIS   CE1 NE2  sing Y N 187 
HIS   CE1 HE1  sing N N 188 
HIS   NE2 HE2  sing N N 189 
HIS   OXT HXT  sing N N 190 
HOH   O   H1   sing N N 191 
HOH   O   H2   sing N N 192 
ILE   N   CA   sing N N 193 
ILE   N   H    sing N N 194 
ILE   N   H2   sing N N 195 
ILE   CA  C    sing N N 196 
ILE   CA  CB   sing N N 197 
ILE   CA  HA   sing N N 198 
ILE   C   O    doub N N 199 
ILE   C   OXT  sing N N 200 
ILE   CB  CG1  sing N N 201 
ILE   CB  CG2  sing N N 202 
ILE   CB  HB   sing N N 203 
ILE   CG1 CD1  sing N N 204 
ILE   CG1 HG12 sing N N 205 
ILE   CG1 HG13 sing N N 206 
ILE   CG2 HG21 sing N N 207 
ILE   CG2 HG22 sing N N 208 
ILE   CG2 HG23 sing N N 209 
ILE   CD1 HD11 sing N N 210 
ILE   CD1 HD12 sing N N 211 
ILE   CD1 HD13 sing N N 212 
ILE   OXT HXT  sing N N 213 
LEU   N   CA   sing N N 214 
LEU   N   H    sing N N 215 
LEU   N   H2   sing N N 216 
LEU   CA  C    sing N N 217 
LEU   CA  CB   sing N N 218 
LEU   CA  HA   sing N N 219 
LEU   C   O    doub N N 220 
LEU   C   OXT  sing N N 221 
LEU   CB  CG   sing N N 222 
LEU   CB  HB2  sing N N 223 
LEU   CB  HB3  sing N N 224 
LEU   CG  CD1  sing N N 225 
LEU   CG  CD2  sing N N 226 
LEU   CG  HG   sing N N 227 
LEU   CD1 HD11 sing N N 228 
LEU   CD1 HD12 sing N N 229 
LEU   CD1 HD13 sing N N 230 
LEU   CD2 HD21 sing N N 231 
LEU   CD2 HD22 sing N N 232 
LEU   CD2 HD23 sing N N 233 
LEU   OXT HXT  sing N N 234 
LYS   N   CA   sing N N 235 
LYS   N   H    sing N N 236 
LYS   N   H2   sing N N 237 
LYS   CA  C    sing N N 238 
LYS   CA  CB   sing N N 239 
LYS   CA  HA   sing N N 240 
LYS   C   O    doub N N 241 
LYS   C   OXT  sing N N 242 
LYS   CB  CG   sing N N 243 
LYS   CB  HB2  sing N N 244 
LYS   CB  HB3  sing N N 245 
LYS   CG  CD   sing N N 246 
LYS   CG  HG2  sing N N 247 
LYS   CG  HG3  sing N N 248 
LYS   CD  CE   sing N N 249 
LYS   CD  HD2  sing N N 250 
LYS   CD  HD3  sing N N 251 
LYS   CE  NZ   sing N N 252 
LYS   CE  HE2  sing N N 253 
LYS   CE  HE3  sing N N 254 
LYS   NZ  HZ1  sing N N 255 
LYS   NZ  HZ2  sing N N 256 
LYS   NZ  HZ3  sing N N 257 
LYS   OXT HXT  sing N N 258 
MET   N   CA   sing N N 259 
MET   N   H    sing N N 260 
MET   N   H2   sing N N 261 
MET   CA  C    sing N N 262 
MET   CA  CB   sing N N 263 
MET   CA  HA   sing N N 264 
MET   C   O    doub N N 265 
MET   C   OXT  sing N N 266 
MET   CB  CG   sing N N 267 
MET   CB  HB2  sing N N 268 
MET   CB  HB3  sing N N 269 
MET   CG  SD   sing N N 270 
MET   CG  HG2  sing N N 271 
MET   CG  HG3  sing N N 272 
MET   SD  CE   sing N N 273 
MET   CE  HE1  sing N N 274 
MET   CE  HE2  sing N N 275 
MET   CE  HE3  sing N N 276 
MET   OXT HXT  sing N N 277 
PHE   N   CA   sing N N 278 
PHE   N   H    sing N N 279 
PHE   N   H2   sing N N 280 
PHE   CA  C    sing N N 281 
PHE   CA  CB   sing N N 282 
PHE   CA  HA   sing N N 283 
PHE   C   O    doub N N 284 
PHE   C   OXT  sing N N 285 
PHE   CB  CG   sing N N 286 
PHE   CB  HB2  sing N N 287 
PHE   CB  HB3  sing N N 288 
PHE   CG  CD1  doub Y N 289 
PHE   CG  CD2  sing Y N 290 
PHE   CD1 CE1  sing Y N 291 
PHE   CD1 HD1  sing N N 292 
PHE   CD2 CE2  doub Y N 293 
PHE   CD2 HD2  sing N N 294 
PHE   CE1 CZ   doub Y N 295 
PHE   CE1 HE1  sing N N 296 
PHE   CE2 CZ   sing Y N 297 
PHE   CE2 HE2  sing N N 298 
PHE   CZ  HZ   sing N N 299 
PHE   OXT HXT  sing N N 300 
PRO   N   CA   sing N N 301 
PRO   N   CD   sing N N 302 
PRO   N   H    sing N N 303 
PRO   CA  C    sing N N 304 
PRO   CA  CB   sing N N 305 
PRO   CA  HA   sing N N 306 
PRO   C   O    doub N N 307 
PRO   C   OXT  sing N N 308 
PRO   CB  CG   sing N N 309 
PRO   CB  HB2  sing N N 310 
PRO   CB  HB3  sing N N 311 
PRO   CG  CD   sing N N 312 
PRO   CG  HG2  sing N N 313 
PRO   CG  HG3  sing N N 314 
PRO   CD  HD2  sing N N 315 
PRO   CD  HD3  sing N N 316 
PRO   OXT HXT  sing N N 317 
SER   N   CA   sing N N 318 
SER   N   H    sing N N 319 
SER   N   H2   sing N N 320 
SER   CA  C    sing N N 321 
SER   CA  CB   sing N N 322 
SER   CA  HA   sing N N 323 
SER   C   O    doub N N 324 
SER   C   OXT  sing N N 325 
SER   CB  OG   sing N N 326 
SER   CB  HB2  sing N N 327 
SER   CB  HB3  sing N N 328 
SER   OG  HG   sing N N 329 
SER   OXT HXT  sing N N 330 
TFA   C1  C2   sing N N 331 
TFA   C1  O    doub N N 332 
TFA   C1  OXT  sing N N 333 
TFA   C2  F1   sing N N 334 
TFA   C2  F2   sing N N 335 
TFA   C2  F3   sing N N 336 
TFA   OXT HXT  sing N N 337 
THR   N   CA   sing N N 338 
THR   N   H    sing N N 339 
THR   N   H2   sing N N 340 
THR   CA  C    sing N N 341 
THR   CA  CB   sing N N 342 
THR   CA  HA   sing N N 343 
THR   C   O    doub N N 344 
THR   C   OXT  sing N N 345 
THR   CB  OG1  sing N N 346 
THR   CB  CG2  sing N N 347 
THR   CB  HB   sing N N 348 
THR   OG1 HG1  sing N N 349 
THR   CG2 HG21 sing N N 350 
THR   CG2 HG22 sing N N 351 
THR   CG2 HG23 sing N N 352 
THR   OXT HXT  sing N N 353 
TYR   N   CA   sing N N 354 
TYR   N   H    sing N N 355 
TYR   N   H2   sing N N 356 
TYR   CA  C    sing N N 357 
TYR   CA  CB   sing N N 358 
TYR   CA  HA   sing N N 359 
TYR   C   O    doub N N 360 
TYR   C   OXT  sing N N 361 
TYR   CB  CG   sing N N 362 
TYR   CB  HB2  sing N N 363 
TYR   CB  HB3  sing N N 364 
TYR   CG  CD1  doub Y N 365 
TYR   CG  CD2  sing Y N 366 
TYR   CD1 CE1  sing Y N 367 
TYR   CD1 HD1  sing N N 368 
TYR   CD2 CE2  doub Y N 369 
TYR   CD2 HD2  sing N N 370 
TYR   CE1 CZ   doub Y N 371 
TYR   CE1 HE1  sing N N 372 
TYR   CE2 CZ   sing Y N 373 
TYR   CE2 HE2  sing N N 374 
TYR   CZ  OH   sing N N 375 
TYR   OH  HH   sing N N 376 
TYR   OXT HXT  sing N N 377 
VAL   N   CA   sing N N 378 
VAL   N   H    sing N N 379 
VAL   N   H2   sing N N 380 
VAL   CA  C    sing N N 381 
VAL   CA  CB   sing N N 382 
VAL   CA  HA   sing N N 383 
VAL   C   O    doub N N 384 
VAL   C   OXT  sing N N 385 
VAL   CB  CG1  sing N N 386 
VAL   CB  CG2  sing N N 387 
VAL   CB  HB   sing N N 388 
VAL   CG1 HG11 sing N N 389 
VAL   CG1 HG12 sing N N 390 
VAL   CG1 HG13 sing N N 391 
VAL   CG2 HG21 sing N N 392 
VAL   CG2 HG22 sing N N 393 
VAL   CG2 HG23 sing N N 394 
VAL   OXT HXT  sing N N 395 
# 
_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                    7HDQ 
_atom_sites.fract_transf_matrix[1][1]   0.011265 
_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]   0.011265 
_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]   0.025283 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    A VAL   A 1 3   ? 19.681 -16.278 22.281  0.78 51.44 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.614 -16.261 22.352  0.22 50.39 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.716 -15.199 22.451  0.78 51.08 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.670 -15.162 22.517  0.22 50.15 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.369 -13.855 22.150  0.78 49.70 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.342 -13.833 22.194  0.22 49.19 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.490 -13.588 22.585  0.78 50.09 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.448 -13.557 22.659  0.22 49.57 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.092 -15.223 23.863  0.78 51.85 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.067 -15.150 23.935  0.22 50.70 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.083 -14.093 24.023  0.78 52.00 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.077 -14.003 24.083  0.22 50.79 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.436 -16.571 24.132  0.78 52.02 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.397 -16.482 24.240  0.22 50.82 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.996 -15.321 21.817  0.78 61.35 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.938 -15.278 21.894  0.22 60.23 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.791 -15.095 24.523  0.78 62.28 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.778 -15.019 24.582  0.22 60.90 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.574 -14.238 24.836  0.78 62.46 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.580 -14.121 24.908  0.22 61.00 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.556 -13.248 24.077  0.78 62.46 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.563 -13.164 24.108  0.22 61.00 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.486 -14.092 23.258  0.78 62.46 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.469 -14.012 23.327  0.22 61.00 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.995 -16.541 24.995  0.78 62.48 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 16.960 -16.424 25.104  0.22 61.04 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.786 -16.750 23.434  0.78 62.48 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.742 -16.669 23.550  0.22 61.04 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.118 -17.260 24.134  0.78 62.48 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.071 -17.179 24.255  0.22 61.04 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.667 -13.016 21.390  1.00 47.63 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.122 -11.671 21.059  1.00 43.67 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 17.977 -10.689 21.295  1.00 40.17 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.857 -11.080 21.640  1.00 39.91 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.681 -11.589 19.630  1.00 42.91 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.664 -11.971 18.576  1.00 41.89 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.557 -11.434 18.540  1.00 41.55 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 19.038 -12.905 17.705  1.00 41.61 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.905 -13.214 21.042  0.78 57.21 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.918 -13.224 21.020  0.22 57.21 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.842 -11.434 21.660  1.00 52.46 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 19.965 -10.676 19.455  1.00 51.55 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.437 -12.190 19.551  1.00 51.55 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.499 -13.158 17.083  1.00 49.99 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.821 -13.258 17.763  1.00 49.99 ?  4   ASN   A HD22 1 
ATOM   46   N  N    . SER   A 1 5   ? 18.262 -9.401  21.106  1.00 36.80 ?  5   SER   A N    1 
ATOM   47   C  CA   . SER   A 1 5   ? 17.348 -8.334  21.495  1.00 33.19 ?  5   SER   A CA   1 
ATOM   48   C  C    . SER   A 1 5   ? 16.456 -7.848  20.355  1.00 28.45 ?  5   SER   A C    1 
ATOM   49   O  O    . SER   A 1 5   ? 15.726 -6.868  20.532  1.00 28.96 ?  5   SER   A O    1 
ATOM   50   C  CB   . SER   A 1 5   ? 18.122 -7.160  22.100  1.00 34.68 ?  5   SER   A CB   1 
ATOM   51   O  OG   . SER   A 1 5   ? 18.981 -6.565  21.144  1.00 35.35 ?  5   SER   A OG   1 
ATOM   52   H  H    . SER   A 1 5   ? 18.991 -9.119  20.745  1.00 44.22 ?  5   SER   A H    1 
ATOM   53   H  HA   . SER   A 1 5   ? 16.765 -8.672  22.188  1.00 39.88 ?  5   SER   A HA   1 
ATOM   54   H  HB2  . SER   A 1 5   ? 17.490 -6.492  22.414  1.00 41.67 ?  5   SER   A HB2  1 
ATOM   55   H  HB3  . SER   A 1 5   ? 18.656 -7.481  22.845  1.00 41.67 ?  5   SER   A HB3  1 
ATOM   56   H  HG   . SER   A 1 5   ? 19.397 -5.919  21.492  1.00 42.48 ?  5   SER   A HG   1 
ATOM   57   N  N    A PHE   A 1 6   ? 16.484 -8.507  19.199  0.78 24.80 ?  6   PHE   A N    1 
ATOM   58   N  N    B PHE   A 1 6   ? 16.506 -8.496  19.195  0.22 26.22 ?  6   PHE   A N    1 
ATOM   59   C  CA   A PHE   A 1 6   ? 15.577 -8.140  18.118  0.78 21.58 ?  6   PHE   A CA   1 
ATOM   60   C  CA   B PHE   A 1 6   ? 15.653 -8.113  18.076  0.22 23.90 ?  6   PHE   A CA   1 
ATOM   61   C  C    A PHE   A 1 6   ? 14.144 -8.512  18.489  0.78 21.42 ?  6   PHE   A C    1 
ATOM   62   C  C    B PHE   A 1 6   ? 14.202 -8.413  18.433  0.22 23.20 ?  6   PHE   A C    1 
ATOM   63   O  O    A PHE   A 1 6   ? 13.888 -9.595  19.021  0.78 22.36 ?  6   PHE   A O    1 
ATOM   64   O  O    B PHE   A 1 6   ? 13.810 -9.579  18.549  0.22 23.04 ?  6   PHE   A O    1 
ATOM   65   C  CB   A PHE   A 1 6   ? 15.987 -8.845  16.827  0.78 19.57 ?  6   PHE   A CB   1 
ATOM   66   C  CB   B PHE   A 1 6   ? 16.079 -8.861  16.817  0.22 22.60 ?  6   PHE   A CB   1 
ATOM   67   C  CG   A PHE   A 1 6   ? 17.277 -8.329  16.236  0.78 18.09 ?  6   PHE   A CG   1 
ATOM   68   C  CG   B PHE   A 1 6   ? 17.328 -8.314  16.181  0.22 21.43 ?  6   PHE   A CG   1 
ATOM   69   C  CD1  A PHE   A 1 6   ? 17.305 -7.127  15.551  0.78 17.33 ?  6   PHE   A CD1  1 
ATOM   70   C  CD1  B PHE   A 1 6   ? 17.282 -7.153  15.427  0.22 20.93 ?  6   PHE   A CD1  1 
ATOM   71   C  CD2  A PHE   A 1 6   ? 18.451 -9.052  16.359  0.78 18.64 ?  6   PHE   A CD2  1 
ATOM   72   C  CD2  B PHE   A 1 6   ? 18.544 -8.961  16.331  0.22 21.09 ?  6   PHE   A CD2  1 
ATOM   73   C  CE1  A PHE   A 1 6   ? 18.484 -6.651  15.005  0.78 17.50 ?  6   PHE   A CE1  1 
ATOM   74   C  CE1  B PHE   A 1 6   ? 18.425 -6.645  14.837  0.22 20.73 ?  6   PHE   A CE1  1 
ATOM   75   C  CE2  A PHE   A 1 6   ? 19.632 -8.584  15.813  0.78 18.72 ?  6   PHE   A CE2  1 
ATOM   76   C  CE2  B PHE   A 1 6   ? 19.691 -8.457  15.742  0.22 20.85 ?  6   PHE   A CE2  1 
ATOM   77   C  CZ   A PHE   A 1 6   ? 19.648 -7.382  15.135  0.78 18.08 ?  6   PHE   A CZ   1 
ATOM   78   C  CZ   B PHE   A 1 6   ? 19.630 -7.297  14.994  0.22 20.70 ?  6   PHE   A CZ   1 
ATOM   79   H  H    A PHE   A 1 6   ? 17.009 -9.165  19.022  0.78 29.81 ?  6   PHE   A H    1 
ATOM   80   H  H    B PHE   A 1 6   ? 17.025 -9.162  19.033  0.22 31.52 ?  6   PHE   A H    1 
ATOM   81   H  HA   A PHE   A 1 6   ? 15.616 -7.187  17.978  0.78 25.95 ?  6   PHE   A HA   1 
ATOM   82   H  HA   B PHE   A 1 6   ? 15.740 -7.162  17.914  0.22 28.74 ?  6   PHE   A HA   1 
ATOM   83   H  HB2  A PHE   A 1 6   ? 16.098 -9.794  17.011  0.78 23.54 ?  6   PHE   A HB2  1 
ATOM   84   H  HB2  B PHE   A 1 6   ? 16.244 -9.789  17.046  0.22 27.17 ?  6   PHE   A HB2  1 
ATOM   85   H  HB3  A PHE   A 1 6   ? 15.284 -8.722  16.170  0.78 23.54 ?  6   PHE   A HB3  1 
ATOM   86   H  HB3  B PHE   A 1 6   ? 15.364 -8.805  16.165  0.22 27.17 ?  6   PHE   A HB3  1 
ATOM   87   H  HD1  A PHE   A 1 6   ? 16.523 -6.634  15.462  0.78 20.85 ?  6   PHE   A HD1  1 
ATOM   88   H  HD1  B PHE   A 1 6   ? 16.473 -6.709  15.318  0.22 25.18 ?  6   PHE   A HD1  1 
ATOM   89   H  HD2  A PHE   A 1 6   ? 18.442 -9.865  16.818  0.78 22.43 ?  6   PHE   A HD2  1 
ATOM   90   H  HD2  B PHE   A 1 6   ? 18.590 -9.742  16.834  0.22 25.37 ?  6   PHE   A HD2  1 
ATOM   91   H  HE1  A PHE   A 1 6   ? 18.494 -5.842  14.549  0.78 21.06 ?  6   PHE   A HE1  1 
ATOM   92   H  HE1  B PHE   A 1 6   ? 18.381 -5.863  14.334  0.22 24.93 ?  6   PHE   A HE1  1 
ATOM   93   H  HE2  A PHE   A 1 6   ? 20.414 -9.078  15.907  0.78 22.52 ?  6   PHE   A HE2  1 
ATOM   94   H  HE2  B PHE   A 1 6   ? 20.503 -8.899  15.850  0.22 25.08 ?  6   PHE   A HE2  1 
ATOM   95   H  HZ   A PHE   A 1 6   ? 20.441 -7.064  14.771  0.78 21.76 ?  6   PHE   A HZ   1 
ATOM   96   H  HZ   B PHE   A 1 6   ? 20.399 -6.956  14.598  0.22 24.89 ?  6   PHE   A HZ   1 
ATOM   97   N  N    A SER   A 1 7   ? 13.202 -7.611  18.202  0.78 20.41 ?  7   SER   A N    1 
ATOM   98   N  N    B SER   A 1 7   ? 13.405 -7.363  18.606  0.22 22.63 ?  7   SER   A N    1 
ATOM   99   C  CA   A SER   A 1 7   ? 11.831 -7.738  18.688  0.78 20.69 ?  7   SER   A CA   1 
ATOM   100  C  CA   B SER   A 1 7   ? 12.038 -7.475  19.091  0.22 22.38 ?  7   SER   A CA   1 
ATOM   101  C  C    A SER   A 1 7   ? 10.824 -7.447  17.581  0.78 18.43 ?  7   SER   A C    1 
ATOM   102  C  C    B SER   A 1 7   ? 11.054 -7.209  17.960  0.22 21.17 ?  7   SER   A C    1 
ATOM   103  O  O    A SER   A 1 7   ? 11.027 -6.549  16.762  0.78 18.59 ?  7   SER   A O    1 
ATOM   104  O  O    B SER   A 1 7   ? 11.306 -6.374  17.086  0.22 21.19 ?  7   SER   A O    1 
ATOM   105  C  CB   A SER   A 1 7   ? 11.589 -6.774  19.856  0.78 23.40 ?  7   SER   A CB   1 
ATOM   106  C  CB   B SER   A 1 7   ? 11.793 -6.472  20.223  0.22 23.07 ?  7   SER   A CB   1 
ATOM   107  O  OG   A SER   A 1 7   ? 10.241 -6.818  20.285  0.78 25.33 ?  7   SER   A OG   1 
ATOM   108  O  OG   B SER   A 1 7   ? 10.435 -6.472  20.624  0.22 23.59 ?  7   SER   A OG   1 
ATOM   109  H  H    A SER   A 1 7   ? 13.337 -6.919  17.714  0.78 24.55 ?  7   SER   A H    1 
ATOM   110  H  H    B SER   A 1 7   ? 13.643 -6.552  18.443  0.22 27.21 ?  7   SER   A H    1 
ATOM   111  H  HA   A SER   A 1 7   ? 11.680 -8.641  19.002  0.78 24.88 ?  7   SER   A HA   1 
ATOM   112  H  HA   B SER   A 1 7   ? 11.884 -8.369  19.433  0.22 26.91 ?  7   SER   A HA   1 
ATOM   113  H  HB2  A SER   A 1 7   ? 12.164 -7.028  20.597  0.78 28.14 ?  7   SER   A HB2  1 
ATOM   114  H  HB2  B SER   A 1 7   ? 12.343 -6.716  20.985  0.22 27.74 ?  7   SER   A HB2  1 
ATOM   115  H  HB3  A SER   A 1 7   ? 11.804 -5.871  19.569  0.78 28.14 ?  7   SER   A HB3  1 
ATOM   116  H  HB3  B SER   A 1 7   ? 12.032 -5.584  19.915  0.22 27.74 ?  7   SER   A HB3  1 
ATOM   117  H  HG   A SER   A 1 7   ? 10.127 -6.282  20.922  0.78 30.46 ?  7   SER   A HG   1 
ATOM   118  H  HG   B SER   A 1 7   ? 10.317 -5.916  21.242  0.22 28.37 ?  7   SER   A HG   1 
ATOM   119  N  N    A GLY   A 1 8   ? 9.723  -8.202  17.575  0.78 16.79 ?  8   GLY   A N    1 
ATOM   120  N  N    B GLY   A 1 8   ? 9.933  -7.930  17.981  0.22 20.12 ?  8   GLY   A N    1 
ATOM   121  C  CA   A GLY   A 1 8   ? 8.639  -7.955  16.646  0.78 16.05 ?  8   GLY   A CA   1 
ATOM   122  C  CA   B GLY   A 1 8   ? 8.852  -7.689  17.049  0.22 18.85 ?  8   GLY   A CA   1 
ATOM   123  C  C    A GLY   A 1 8   ? 8.854  -8.465  15.241  0.78 14.81 ?  8   GLY   A C    1 
ATOM   124  C  C    B GLY   A 1 8   ? 9.048  -8.238  15.655  0.22 17.51 ?  8   GLY   A C    1 
ATOM   125  O  O    A GLY   A 1 8   ? 8.114  -8.060  14.334  0.78 15.86 ?  8   GLY   A O    1 
ATOM   126  O  O    B GLY   A 1 8   ? 8.281  -7.877  14.756  0.22 17.62 ?  8   GLY   A O    1 
ATOM   127  H  H    A GLY   A 1 8   ? 9.586  -8.860  18.109  0.78 20.21 ?  8   GLY   A H    1 
ATOM   128  H  H    B GLY   A 1 8   ? 9.778  -8.568  18.537  0.22 24.20 ?  8   GLY   A H    1 
ATOM   129  H  HA2  A GLY   A 1 8   ? 7.832  -8.363  16.995  0.78 19.31 ?  8   GLY   A HA2  1 
ATOM   130  H  HA2  B GLY   A 1 8   ? 8.040  -8.081  17.403  0.22 22.68 ?  8   GLY   A HA2  1 
ATOM   131  H  HA3  A GLY   A 1 8   ? 8.489  -6.999  16.589  0.78 19.31 ?  8   GLY   A HA3  1 
ATOM   132  H  HA3  B GLY   A 1 8   ? 8.713  -6.732  16.973  0.22 22.68 ?  8   GLY   A HA3  1 
ATOM   133  N  N    A TYR   A 1 9   ? 9.837  -9.338  15.024  0.78 13.70 ?  9   TYR   A N    1 
ATOM   134  N  N    B TYR   A 1 9   ? 10.041 -9.097  15.439  0.22 16.35 ?  9   TYR   A N    1 
ATOM   135  C  CA   A TYR   A 1 9   ? 10.104 -9.881  13.701  0.78 12.58 ?  9   TYR   A CA   1 
ATOM   136  C  CA   B TYR   A 1 9   ? 10.271 -9.642  14.111  0.22 15.40 ?  9   TYR   A CA   1 
ATOM   137  C  C    A TYR   A 1 9   ? 9.232  -11.097 13.422  0.78 12.23 ?  9   TYR   A C    1 
ATOM   138  C  C    B TYR   A 1 9   ? 9.371  -10.847 13.853  0.22 14.47 ?  9   TYR   A C    1 
ATOM   139  O  O    A TYR   A 1 9   ? 8.987  -11.929 14.302  0.78 13.60 ?  9   TYR   A O    1 
ATOM   140  O  O    B TYR   A 1 9   ? 8.890  -11.513 14.775  0.22 14.85 ?  9   TYR   A O    1 
ATOM   141  C  CB   A TYR   A 1 9   ? 11.581 -10.278 13.551  0.78 13.09 ?  9   TYR   A CB   1 
ATOM   142  C  CB   B TYR   A 1 9   ? 11.740 -10.039 13.936  0.22 15.53 ?  9   TYR   A CB   1 
ATOM   143  C  CG   A TYR   A 1 9   ? 12.498 -9.085  13.399  0.78 13.63 ?  9   TYR   A CG   1 
ATOM   144  C  CG   B TYR   A 1 9   ? 12.665 -8.865  13.708  0.22 15.39 ?  9   TYR   A CG   1 
ATOM   145  C  CD1  A TYR   A 1 9   ? 12.822 -8.299  14.493  0.78 14.36 ?  9   TYR   A CD1  1 
ATOM   146  C  CD1  B TYR   A 1 9   ? 12.977 -7.991  14.741  0.22 15.63 ?  9   TYR   A CD1  1 
ATOM   147  C  CD2  A TYR   A 1 9   ? 13.009 -8.727  12.158  0.78 13.51 ?  9   TYR   A CD2  1 
ATOM   148  C  CD2  B TYR   A 1 9   ? 13.224 -8.628  12.458  0.22 15.22 ?  9   TYR   A CD2  1 
ATOM   149  C  CE1  A TYR   A 1 9   ? 13.635 -7.190  14.363  0.78 15.11 ?  9   TYR   A CE1  1 
ATOM   150  C  CE1  B TYR   A 1 9   ? 13.819 -6.915  14.537  0.22 15.85 ?  9   TYR   A CE1  1 
ATOM   151  C  CE2  A TYR   A 1 9   ? 13.822 -7.621  12.015  0.78 13.91 ?  9   TYR   A CE2  1 
ATOM   152  C  CE2  B TYR   A 1 9   ? 14.062 -7.551  12.244  0.22 15.49 ?  9   TYR   A CE2  1 
ATOM   153  C  CZ   A TYR   A 1 9   ? 14.131 -6.854  13.118  0.78 15.03 ?  9   TYR   A CZ   1 
ATOM   154  C  CZ   B TYR   A 1 9   ? 14.358 -6.700  13.286  0.22 15.99 ?  9   TYR   A CZ   1 
ATOM   155  O  OH   A TYR   A 1 9   ? 14.935 -5.753  12.968  0.78 16.62 ?  9   TYR   A OH   1 
ATOM   156  O  OH   B TYR   A 1 9   ? 15.197 -5.629  13.078  0.22 16.75 ?  9   TYR   A OH   1 
ATOM   157  H  H    A TYR   A 1 9   ? 10.355 -9.641  15.636  0.78 16.50 ?  9   TYR   A H    1 
ATOM   158  H  H    B TYR   A 1 9   ? 10.591 -9.374  16.041  0.22 19.67 ?  9   TYR   A H    1 
ATOM   159  H  HA   A TYR   A 1 9   ? 9.909  -9.205  13.034  0.78 15.16 ?  9   TYR   A HA   1 
ATOM   160  H  HA   B TYR   A 1 9   ? 10.067 -8.963  13.451  0.22 18.54 ?  9   TYR   A HA   1 
ATOM   161  H  HB2  A TYR   A 1 9   ? 11.859 -10.778 14.335  0.78 15.76 ?  9   TYR   A HB2  1 
ATOM   162  H  HB2  B TYR   A 1 9   ? 12.041 -10.507 14.728  0.22 18.69 ?  9   TYR   A HB2  1 
ATOM   163  H  HB3  A TYR   A 1 9   ? 11.670 -10.830 12.757  0.78 15.76 ?  9   TYR   A HB3  1 
ATOM   164  H  HB3  B TYR   A 1 9   ? 11.810 -10.624 13.165  0.22 18.69 ?  9   TYR   A HB3  1 
ATOM   165  H  HD1  A TYR   A 1 9   ? 12.475 -8.521  15.331  0.78 17.28 ?  9   TYR   A HD1  1 
ATOM   166  H  HD1  B TYR   A 1 9   ? 12.612 -8.132  15.585  0.22 18.81 ?  9   TYR   A HD1  1 
ATOM   167  H  HD2  A TYR   A 1 9   ? 12.793 -9.241  11.411  0.78 16.26 ?  9   TYR   A HD2  1 
ATOM   168  H  HD2  B TYR   A 1 9   ? 13.028 -9.201  11.752  0.22 18.32 ?  9   TYR   A HD2  1 
ATOM   169  H  HE1  A TYR   A 1 9   ? 13.839 -6.675  15.109  0.78 18.19 ?  9   TYR   A HE1  1 
ATOM   170  H  HE1  B TYR   A 1 9   ? 14.017 -6.337  15.238  0.22 19.08 ?  9   TYR   A HE1  1 
ATOM   171  H  HE2  A TYR   A 1 9   ? 14.159 -7.394  11.179  0.78 16.74 ?  9   TYR   A HE2  1 
ATOM   172  H  HE2  B TYR   A 1 9   ? 14.434 -7.406  11.403  0.22 18.64 ?  9   TYR   A HE2  1 
ATOM   173  H  HH   A TYR   A 1 9   ? 15.059 -5.388  13.716  0.78 20.00 ?  9   TYR   A HH   1 
ATOM   174  H  HH   B TYR   A 1 9   ? 15.290 -5.196  13.792  0.22 20.15 ?  9   TYR   A HH   1 
ATOM   175  N  N    A LEU   A 1 10  ? 8.797  -11.204 12.173  0.78 11.73 ?  10  LEU   A N    1 
ATOM   176  N  N    B LEU   A 1 10  ? 9.143  -11.116 12.569  0.22 13.91 ?  10  LEU   A N    1 
ATOM   177  C  CA   A LEU   A 1 10  ? 8.207  -12.434 11.672  0.78 11.80 ?  10  LEU   A CA   1 
ATOM   178  C  CA   B LEU   A 1 10  ? 8.375  -12.267 12.111  0.22 13.58 ?  10  LEU   A CA   1 
ATOM   179  C  C    A LEU   A 1 10  ? 9.327  -13.378 11.240  0.78 11.91 ?  10  LEU   A C    1 
ATOM   180  C  C    B LEU   A 1 10  ? 9.347  -13.276 11.515  0.22 12.51 ?  10  LEU   A C    1 
ATOM   181  O  O    A LEU   A 1 10  ? 10.302 -12.955 10.611  0.78 12.34 ?  10  LEU   A O    1 
ATOM   182  O  O    B LEU   A 1 10  ? 10.094 -12.950 10.586  0.22 12.62 ?  10  LEU   A O    1 
ATOM   183  C  CB   A LEU   A 1 10  ? 7.308  -12.105 10.482  0.78 12.47 ?  10  LEU   A CB   1 
ATOM   184  C  CB   B LEU   A 1 10  ? 7.337  -11.846 11.070  0.22 14.16 ?  10  LEU   A CB   1 
ATOM   185  C  CG   A LEU   A 1 10  ? 6.606  -13.286 9.821   0.78 15.01 ?  10  LEU   A CG   1 
ATOM   186  C  CG   B LEU   A 1 10  ? 6.549  -12.979 10.404  0.22 14.59 ?  10  LEU   A CG   1 
ATOM   187  C  CD1  A LEU   A 1 10  ? 5.571  -13.887 10.752  0.78 16.42 ?  10  LEU   A CD1  1 
ATOM   188  C  CD1  B LEU   A 1 10  ? 6.005  -13.951 11.439  0.22 15.03 ?  10  LEU   A CD1  1 
ATOM   189  C  CD2  A LEU   A 1 10  ? 5.975  -12.859 8.507   0.78 16.73 ?  10  LEU   A CD2  1 
ATOM   190  C  CD2  B LEU   A 1 10  ? 5.416  -12.405 9.573   0.22 14.95 ?  10  LEU   A CD2  1 
ATOM   191  H  H    A LEU   A 1 10  ? 8.835  -10.569 11.580  0.78 14.14 ?  10  LEU   A H    1 
ATOM   192  H  H    B LEU   A 1 10  ? 9.437  -10.631 11.923  0.22 16.75 ?  10  LEU   A H    1 
ATOM   193  H  HA   A LEU   A 1 10  ? 7.675  -12.854 12.366  0.78 14.21 ?  10  LEU   A HA   1 
ATOM   194  H  HA   B LEU   A 1 10  ? 7.919  -12.676 12.862  0.22 16.35 ?  10  LEU   A HA   1 
ATOM   195  H  HB2  A LEU   A 1 10  ? 6.615  -11.493 10.779  0.78 15.02 ?  10  LEU   A HB2  1 
ATOM   196  H  HB2  B LEU   A 1 10  ? 6.692  -11.261 11.499  0.22 17.04 ?  10  LEU   A HB2  1 
ATOM   197  H  HB3  A LEU   A 1 10  ? 7.846  -11.675 9.801   0.78 15.02 ?  10  LEU   A HB3  1 
ATOM   198  H  HB3  B LEU   A 1 10  ? 7.792  -11.358 10.365  0.22 17.04 ?  10  LEU   A HB3  1 
ATOM   199  H  HG   A LEU   A 1 10  ? 7.262  -13.975 9.624   0.78 18.07 ?  10  LEU   A HG   1 
ATOM   200  H  HG   B LEU   A 1 10  ? 7.138  -13.468 9.809   0.22 17.56 ?  10  LEU   A HG   1 
ATOM   201  H  HD11 A LEU   A 1 10  ? 5.138  -14.633 10.306  0.78 19.76 ?  10  LEU   A HD11 1 
ATOM   202  H  HD11 B LEU   A 1 10  ? 5.529  -14.659 10.982  0.22 18.09 ?  10  LEU   A HD11 1 
ATOM   203  H  HD12 A LEU   A 1 10  ? 6.011  -14.198 11.559  0.78 19.76 ?  10  LEU   A HD12 1 
ATOM   204  H  HD12 B LEU   A 1 10  ? 6.738  -14.327 11.952  0.22 18.09 ?  10  LEU   A HD12 1 
ATOM   205  H  HD13 A LEU   A 1 10  ? 4.914  -13.210 10.974  0.78 19.76 ?  10  LEU   A HD13 1 
ATOM   206  H  HD13 B LEU   A 1 10  ? 5.399  -13.473 12.024  0.22 18.09 ?  10  LEU   A HD13 1 
ATOM   207  H  HD21 A LEU   A 1 10  ? 5.534  -13.627 8.107   0.78 20.14 ?  10  LEU   A HD21 1 
ATOM   208  H  HD21 B LEU   A 1 10  ? 4.952  -13.130 9.131   0.22 18.00 ?  10  LEU   A HD21 1 
ATOM   209  H  HD22 A LEU   A 1 10  ? 5.330  -12.160 8.682   0.78 20.14 ?  10  LEU   A HD22 1 
ATOM   210  H  HD22 B LEU   A 1 10  ? 4.808  -11.927 10.159  0.22 18.00 ?  10  LEU   A HD22 1 
ATOM   211  H  HD23 A LEU   A 1 10  ? 6.671  -12.534 7.917   0.78 20.14 ?  10  LEU   A HD23 1 
ATOM   212  H  HD23 B LEU   A 1 10  ? 5.788  -11.797 8.915   0.22 18.00 ?  10  LEU   A HD23 1 
ATOM   213  N  N    A LYS   A 1 11  ? 9.204  -14.654 11.591  0.78 12.12 ?  11  LYS   A N    1 
ATOM   214  N  N    B LYS   A 1 11  ? 9.345  -14.489 12.057  0.22 11.93 ?  11  LYS   A N    1 
ATOM   215  C  CA   A LYS   A 1 11  ? 10.212 -15.655 11.261  0.78 12.37 ?  11  LYS   A CA   1 
ATOM   216  C  CA   B LYS   A 1 11  ? 10.245 -15.530 11.579  0.22 11.63 ?  11  LYS   A CA   1 
ATOM   217  C  C    A LYS   A 1 11  ? 9.875  -16.254 9.902   0.78 12.50 ?  11  LYS   A C    1 
ATOM   218  C  C    B LYS   A 1 11  ? 9.800  -15.992 10.198  0.22 10.94 ?  11  LYS   A C    1 
ATOM   219  O  O    A LYS   A 1 11  ? 8.807  -16.848 9.740   0.78 14.34 ?  11  LYS   A O    1 
ATOM   220  O  O    B LYS   A 1 11  ? 8.651  -16.409 10.015  0.22 11.05 ?  11  LYS   A O    1 
ATOM   221  C  CB   A LYS   A 1 11  ? 10.235 -16.728 12.349  0.78 12.73 ?  11  LYS   A CB   1 
ATOM   222  C  CB   B LYS   A 1 11  ? 10.256 -16.700 12.561  0.22 11.80 ?  11  LYS   A CB   1 
ATOM   223  C  CG   A LYS   A 1 11  ? 11.240 -17.852 12.158  0.78 13.00 ?  11  LYS   A CG   1 
ATOM   224  C  CG   B LYS   A 1 11  ? 11.338 -17.746 12.301  0.22 11.95 ?  11  LYS   A CG   1 
ATOM   225  C  CD   A LYS   A 1 11  ? 11.321 -18.690 13.438  0.78 13.50 ?  11  LYS   A CD   1 
ATOM   226  C  CD   B LYS   A 1 11  ? 11.350 -18.817 13.393  0.22 12.31 ?  11  LYS   A CD   1 
ATOM   227  C  CE   A LYS   A 1 11  ? 12.302 -19.849 13.327  0.78 13.50 ?  11  LYS   A CE   1 
ATOM   228  C  CE   B LYS   A 1 11  ? 12.474 -19.831 13.196  0.22 12.41 ?  11  LYS   A CE   1 
ATOM   229  N  NZ   A LYS   A 1 11  ? 13.680 -19.400 12.993  0.78 13.51 ?  11  LYS   A NZ   1 
ATOM   230  N  NZ   B LYS   A 1 11  ? 13.824 -19.209 13.285  0.22 12.19 ?  11  LYS   A NZ   1 
ATOM   231  H  H    A LYS   A 1 11  ? 8.526  -14.969 12.015  0.78 14.60 ?  11  LYS   A H    1 
ATOM   232  H  H    B LYS   A 1 11  ? 8.830  -14.727 12.700  0.22 14.37 ?  11  LYS   A H    1 
ATOM   233  H  HA   A LYS   A 1 11  ? 11.085 -15.234 11.209  0.78 14.90 ?  11  LYS   A HA   1 
ATOM   234  H  HA   B LYS   A 1 11  ? 11.140 -15.170 11.502  0.22 14.01 ?  11  LYS   A HA   1 
ATOM   235  H  HB2  A LYS   A 1 11  ? 10.439 -16.294 13.192  0.78 15.34 ?  11  LYS   A HB2  1 
ATOM   236  H  HB2  B LYS   A 1 11  ? 10.394 -16.345 13.451  0.22 14.22 ?  11  LYS   A HB2  1 
ATOM   237  H  HB3  A LYS   A 1 11  ? 9.353  -17.126 12.397  0.78 15.34 ?  11  LYS   A HB3  1 
ATOM   238  H  HB3  B LYS   A 1 11  ? 9.396  -17.145 12.516  0.22 14.22 ?  11  LYS   A HB3  1 
ATOM   239  H  HG2  A LYS   A 1 11  ? 10.951 -18.427 11.430  0.78 15.65 ?  11  LYS   A HG2  1 
ATOM   240  H  HG2  B LYS   A 1 11  ? 11.166 -18.182 11.452  0.22 14.40 ?  11  LYS   A HG2  1 
ATOM   241  H  HG3  A LYS   A 1 11  ? 12.115 -17.483 11.975  0.78 15.65 ?  11  LYS   A HG3  1 
ATOM   242  H  HG3  B LYS   A 1 11  ? 12.205 -17.315 12.289  0.22 14.40 ?  11  LYS   A HG3  1 
ATOM   243  H  HD2  A LYS   A 1 11  ? 11.603 -18.121 14.169  0.78 16.26 ?  11  LYS   A HD2  1 
ATOM   244  H  HD2  B LYS   A 1 11  ? 11.476 -18.392 14.255  0.22 14.82 ?  11  LYS   A HD2  1 
ATOM   245  H  HD3  A LYS   A 1 11  ? 10.440 -19.059 13.628  0.78 16.26 ?  11  LYS   A HD3  1 
ATOM   246  H  HD3  B LYS   A 1 11  ? 10.506 -19.296 13.378  0.22 14.82 ?  11  LYS   A HD3  1 
ATOM   247  H  HE2  A LYS   A 1 11  ? 12.338 -20.316 14.178  0.78 16.26 ?  11  LYS   A HE2  1 
ATOM   248  H  HE2  B LYS   A 1 11  ? 12.412 -20.514 13.884  0.22 14.94 ?  11  LYS   A HE2  1 
ATOM   249  H  HE3  A LYS   A 1 11  ? 12.006 -20.454 12.629  0.78 16.26 ?  11  LYS   A HE3  1 
ATOM   250  H  HE3  B LYS   A 1 11  ? 12.388 -20.237 12.319  0.22 14.94 ?  11  LYS   A HE3  1 
ATOM   251  H  HZ1  A LYS   A 1 11  ? 14.227 -20.100 12.946  0.78 16.27 ?  11  LYS   A HZ1  1 
ATOM   252  H  HZ1  B LYS   A 1 11  ? 14.453 -19.816 13.117  0.22 14.68 ?  11  LYS   A HZ1  1 
ATOM   253  H  HZ2  A LYS   A 1 11  ? 13.680 -18.980 12.207  0.78 16.27 ?  11  LYS   A HZ2  1 
ATOM   254  H  HZ2  B LYS   A 1 11  ? 13.895 -18.549 12.692  0.22 14.68 ?  11  LYS   A HZ2  1 
ATOM   255  H  HZ3  A LYS   A 1 11  ? 13.978 -18.841 13.618  0.78 16.27 ?  11  LYS   A HZ3  1 
ATOM   256  H  HZ3  B LYS   A 1 11  ? 13.954 -18.878 14.101  0.22 14.68 ?  11  LYS   A HZ3  1 
ATOM   257  N  N    A LEU   A 1 12  ? 10.773 -16.110 8.926   0.78 11.36 ?  12  LEU   A N    1 
ATOM   258  N  N    B LEU   A 1 12  ? 10.699 -15.900 9.221   0.22 11.01 ?  12  LEU   A N    1 
ATOM   259  C  CA   A LEU   A 1 12  ? 10.516 -16.690 7.612   0.78 11.98 ?  12  LEU   A CA   1 
ATOM   260  C  CA   B LEU   A 1 12  ? 10.432 -16.386 7.874   0.22 11.08 ?  12  LEU   A CA   1 
ATOM   261  C  C    A LEU   A 1 12  ? 11.104 -18.087 7.470   0.78 11.82 ?  12  LEU   A C    1 
ATOM   262  C  C    B LEU   A 1 12  ? 10.988 -17.786 7.647   0.22 11.43 ?  12  LEU   A C    1 
ATOM   263  O  O    A LEU   A 1 12  ? 10.481 -18.960 6.855   0.78 12.23 ?  12  LEU   A O    1 
ATOM   264  O  O    B LEU   A 1 12  ? 10.299 -18.647 7.093   0.22 11.16 ?  12  LEU   A O    1 
ATOM   265  C  CB   A LEU   A 1 12  ? 11.073 -15.795 6.500   0.78 12.17 ?  12  LEU   A CB   1 
ATOM   266  C  CB   B LEU   A 1 12  ? 11.008 -15.417 6.834   0.22 11.13 ?  12  LEU   A CB   1 
ATOM   267  C  CG   A LEU   A 1 12  ? 10.425 -14.421 6.329   0.78 13.03 ?  12  LEU   A CG   1 
ATOM   268  C  CG   B LEU   A 1 12  ? 10.347 -14.039 6.781   0.22 11.13 ?  12  LEU   A CG   1 
ATOM   269  C  CD1  A LEU   A 1 12  ? 11.141 -13.664 5.230   0.78 13.51 ?  12  LEU   A CD1  1 
ATOM   270  C  CD1  B LEU   A 1 12  ? 10.991 -13.184 5.703   0.22 11.31 ?  12  LEU   A CD1  1 
ATOM   271  C  CD2  A LEU   A 1 12  ? 8.936  -14.553 6.013   0.78 14.00 ?  12  LEU   A CD2  1 
ATOM   272  C  CD2  B LEU   A 1 12  ? 8.849  -14.162 6.542   0.22 11.20 ?  12  LEU   A CD2  1 
ATOM   273  H  H    A LEU   A 1 12  ? 11.524 -15.686 8.993   0.78 13.69 ?  12  LEU   A H    1 
ATOM   274  H  H    B LEU   A 1 12  ? 11.479 -15.543 9.316   0.22 13.27 ?  12  LEU   A H    1 
ATOM   275  H  HA   A LEU   A 1 12  ? 9.557  -16.764 7.485   0.78 14.43 ?  12  LEU   A HA   1 
ATOM   276  H  HA   B LEU   A 1 12  ? 9.473  -16.423 7.743   0.22 13.36 ?  12  LEU   A HA   1 
ATOM   277  H  HB2  A LEU   A 1 12  ? 12.012 -15.648 6.672   0.78 14.66 ?  12  LEU   A HB2  1 
ATOM   278  H  HB2  B LEU   A 1 12  ? 11.948 -15.278 7.029   0.22 13.41 ?  12  LEU   A HB2  1 
ATOM   279  H  HB3  A LEU   A 1 12  ? 10.969 -16.266 5.656   0.78 14.66 ?  12  LEU   A HB3  1 
ATOM   280  H  HB3  B LEU   A 1 12  ? 10.914 -15.817 5.956   0.22 13.41 ?  12  LEU   A HB3  1 
ATOM   281  H  HG   A LEU   A 1 12  ? 10.516 -13.921 7.153   0.78 15.69 ?  12  LEU   A HG   1 
ATOM   282  H  HG   B LEU   A 1 12  ? 10.478 -13.591 7.632   0.22 13.41 ?  12  LEU   A HG   1 
ATOM   283  H  HD11 A LEU   A 1 12  ? 10.730 -12.796 5.122   0.78 16.27 ?  12  LEU   A HD11 1 
ATOM   284  H  HD11 B LEU   A 1 12  ? 10.561 -12.314 5.692   0.22 13.62 ?  12  LEU   A HD11 1 
ATOM   285  H  HD12 A LEU   A 1 12  ? 12.075 -13.564 5.475   0.78 16.27 ?  12  LEU   A HD12 1 
ATOM   286  H  HD12 B LEU   A 1 12  ? 11.934 -13.085 5.901   0.22 13.62 ?  12  LEU   A HD12 1 
ATOM   287  H  HD13 A LEU   A 1 12  ? 11.073 -14.170 4.402   0.78 16.27 ?  12  LEU   A HD13 1 
ATOM   288  H  HD13 B LEU   A 1 12  ? 10.876 -13.621 4.845   0.22 13.62 ?  12  LEU   A HD13 1 
ATOM   289  H  HD21 A LEU   A 1 12  ? 8.582  -13.683 5.778   0.78 16.86 ?  12  LEU   A HD21 1 
ATOM   290  H  HD21 B LEU   A 1 12  ? 8.496  -13.295 6.294   0.22 13.50 ?  12  LEU   A HD21 1 
ATOM   291  H  HD22 A LEU   A 1 12  ? 8.822  -15.169 5.269   0.78 16.86 ?  12  LEU   A HD22 1 
ATOM   292  H  HD22 B LEU   A 1 12  ? 8.697  -14.800 5.828   0.22 13.50 ?  12  LEU   A HD22 1 
ATOM   293  H  HD23 A LEU   A 1 12  ? 8.473  -14.898 6.795   0.78 16.86 ?  12  LEU   A HD23 1 
ATOM   294  H  HD23 B LEU   A 1 12  ? 8.425  -14.472 7.358   0.22 13.50 ?  12  LEU   A HD23 1 
ATOM   295  N  N    A THR   A 1 13  ? 12.307 -18.296 7.998   0.78 11.67 ?  13  THR   A N    1 
ATOM   296  N  N    B THR   A 1 13  ? 12.231 -18.023 8.057   0.22 11.97 ?  13  THR   A N    1 
ATOM   297  C  CA   A THR   A 1 13  ? 13.005 -19.570 7.904   0.78 12.12 ?  13  THR   A CA   1 
ATOM   298  C  CA   B THR   A 1 13  ? 12.852 -19.336 7.964   0.22 12.61 ?  13  THR   A CA   1 
ATOM   299  C  C    A THR   A 1 13  ? 13.773 -19.791 9.201   0.78 12.38 ?  13  THR   A C    1 
ATOM   300  C  C    B THR   A 1 13  ? 13.606 -19.606 9.261   0.22 13.01 ?  13  THR   A C    1 
ATOM   301  O  O    A THR   A 1 13  ? 13.698 -18.992 10.140  0.78 12.19 ?  13  THR   A O    1 
ATOM   302  O  O    B THR   A 1 13  ? 13.463 -18.888 10.256  0.22 13.06 ?  13  THR   A O    1 
ATOM   303  C  CB   A THR   A 1 13  ? 13.976 -19.591 6.718   0.78 12.84 ?  13  THR   A CB   1 
ATOM   304  C  CB   B THR   A 1 13  ? 13.802 -19.420 6.761   0.22 13.16 ?  13  THR   A CB   1 
ATOM   305  O  OG1  A THR   A 1 13  ? 15.037 -18.680 6.997   0.78 12.73 ?  13  THR   A OG1  1 
ATOM   306  O  OG1  B THR   A 1 13  ? 14.771 -18.371 6.852   0.22 13.26 ?  13  THR   A OG1  1 
ATOM   307  C  CG2  A THR   A 1 13  ? 13.298 -19.197 5.412   0.78 14.05 ?  13  THR   A CG2  1 
ATOM   308  C  CG2  B THR   A 1 13  ? 13.046 -19.314 5.449   0.22 13.76 ?  13  THR   A CG2  1 
ATOM   309  H  H    A THR   A 1 13  ? 12.757 -17.697 8.416   0.78 14.06 ?  13  THR   A H    1 
ATOM   310  H  H    B THR   A 1 13  ? 12.742 -17.417 8.386   0.22 14.42 ?  13  THR   A H    1 
ATOM   311  H  HA   A THR   A 1 13  ? 12.369 -20.292 7.785   0.78 14.60 ?  13  THR   A HA   1 
ATOM   312  H  HA   B THR   A 1 13  ? 12.166 -20.012 7.863   0.22 15.19 ?  13  THR   A HA   1 
ATOM   313  H  HB   A THR   A 1 13  ? 14.345 -20.483 6.604   0.78 15.47 ?  13  THR   A HB   1 
ATOM   314  H  HB   B THR   A 1 13  ? 14.259 -20.272 6.769   0.22 15.84 ?  13  THR   A HB   1 
ATOM   315  H  HG1  A THR   A 1 13  ? 15.717 -19.096 7.259   0.78 15.34 ?  13  THR   A HG1  1 
ATOM   316  H  HG1  B THR   A 1 13  ? 15.295 -18.406 6.198   0.22 15.97 ?  13  THR   A HG1  1 
ATOM   317  H  HG21 A THR   A 1 13  ? 13.879 -19.402 4.659   0.78 16.91 ?  13  THR   A HG21 1 
ATOM   318  H  HG21 B THR   A 1 13  ? 13.653 -19.465 4.704   0.22 16.57 ?  13  THR   A HG21 1 
ATOM   319  H  HG22 A THR   A 1 13  ? 12.472 -19.696 5.311   0.78 16.91 ?  13  THR   A HG22 1 
ATOM   320  H  HG22 B THR   A 1 13  ? 12.339 -19.977 5.417   0.22 16.57 ?  13  THR   A HG22 1 
ATOM   321  H  HG23 A THR   A 1 13  ? 13.100 -18.251 5.411   0.78 16.91 ?  13  THR   A HG23 1 
ATOM   322  H  HG23 B THR   A 1 13  ? 12.660 -18.432 5.367   0.22 16.57 ?  13  THR   A HG23 1 
ATOM   323  N  N    A ASP   A 1 14  ? 14.572 -20.858 9.223   0.78 12.92 ?  14  ASP   A N    1 
ATOM   324  N  N    B ASP   A 1 14  ? 14.427 -20.656 9.229   0.22 13.46 ?  14  ASP   A N    1 
ATOM   325  C  CA   A ASP   A 1 14  ? 15.427 -21.116 10.374  0.78 14.04 ?  14  ASP   A CA   1 
ATOM   326  C  CA   B ASP   A 1 14  ? 15.266 -20.994 10.370  0.22 14.09 ?  14  ASP   A CA   1 
ATOM   327  C  C    A ASP   A 1 14  ? 16.246 -19.889 10.767  0.78 13.27 ?  14  ASP   A C    1 
ATOM   328  C  C    B ASP   A 1 14  ? 16.165 -19.829 10.767  0.22 13.29 ?  14  ASP   A C    1 
ATOM   329  O  O    A ASP   A 1 14  ? 16.483 -19.653 11.958  0.78 14.30 ?  14  ASP   A O    1 
ATOM   330  O  O    B ASP   A 1 14  ? 16.373 -19.576 11.959  0.22 13.47 ?  14  ASP   A O    1 
ATOM   331  C  CB   A ASP   A 1 14  ? 16.368 -22.276 10.064  0.78 16.89 ?  14  ASP   A CB   1 
ATOM   332  C  CB   B ASP   A 1 14  ? 16.106 -22.225 10.028  0.22 15.67 ?  14  ASP   A CB   1 
ATOM   333  C  CG   A ASP   A 1 14  ? 17.293 -22.580 11.211  0.78 20.97 ?  14  ASP   A CG   1 
ATOM   334  C  CG   B ASP   A 1 14  ? 16.978 -22.677 11.184  0.22 17.26 ?  14  ASP   A CG   1 
ATOM   335  O  OD1  A ASP   A 1 14  ? 16.789 -22.936 12.296  0.78 22.36 ?  14  ASP   A OD1  1 
ATOM   336  O  OD1  B ASP   A 1 14  ? 16.424 -23.125 12.212  0.22 17.53 ?  14  ASP   A OD1  1 
ATOM   337  O  OD2  A ASP   A 1 14  ? 18.519 -22.447 11.025  0.78 23.69 -1 14  ASP   A OD2  1 
ATOM   338  O  OD2  B ASP   A 1 14  ? 18.216 -22.588 11.063  0.22 18.40 -1 14  ASP   A OD2  1 
ATOM   339  H  H    A ASP   A 1 14  ? 14.644 -21.436 8.585   0.78 15.56 ?  14  ASP   A H    1 
ATOM   340  H  H    B ASP   A 1 14  ? 14.507 -21.184 8.560   0.22 16.20 ?  14  ASP   A H    1 
ATOM   341  H  HA   A ASP   A 1 14  ? 14.875 -21.370 11.128  0.78 16.90 ?  14  ASP   A HA   1 
ATOM   342  H  HA   B ASP   A 1 14  ? 14.702 -21.212 11.127  0.22 16.97 ?  14  ASP   A HA   1 
ATOM   343  H  HB2  A ASP   A 1 14  ? 15.838 -23.073 9.868   0.78 20.33 ?  14  ASP   A HB2  1 
ATOM   344  H  HB2  B ASP   A 1 14  ? 15.510 -22.955 9.782   0.22 18.86 ?  14  ASP   A HB2  1 
ATOM   345  H  HB3  A ASP   A 1 14  ? 16.916 -22.053 9.298   0.78 20.33 ?  14  ASP   A HB3  1 
ATOM   346  H  HB3  B ASP   A 1 14  ? 16.687 -22.014 9.279   0.22 18.86 ?  14  ASP   A HB3  1 
ATOM   347  N  N    . ASN   A 1 15  ? 16.702 -19.101 9.784   1.00 12.82 ?  15  ASN   A N    1 
ATOM   348  C  CA   . ASN   A 1 15  ? 17.688 -18.059 10.048  1.00 13.05 ?  15  ASN   A CA   1 
ATOM   349  C  C    . ASN   A 1 15  ? 17.321 -16.666 9.557   1.00 13.34 ?  15  ASN   A C    1 
ATOM   350  O  O    . ASN   A 1 15  ? 18.092 -15.736 9.806   1.00 14.90 ?  15  ASN   A O    1 
ATOM   351  C  CB   . ASN   A 1 15  ? 19.056 -18.457 9.464   1.00 13.16 ?  15  ASN   A CB   1 
ATOM   352  C  CG   . ASN   A 1 15  ? 19.039 -18.551 7.957   1.00 13.19 ?  15  ASN   A CG   1 
ATOM   353  O  OD1  . ASN   A 1 15  ? 18.310 -19.361 7.379   1.00 14.24 ?  15  ASN   A OD1  1 
ATOM   354  N  ND2  . ASN   A 1 15  ? 19.843 -17.715 7.305   1.00 13.58 ?  15  ASN   A ND2  1 
ATOM   355  H  H    A ASN   A 1 15  ? 16.456 -19.154 8.965   0.78 15.44 ?  15  ASN   A H    1 
ATOM   356  H  H    B ASN   A 1 15  ? 16.509 -19.196 8.953   0.22 15.44 ?  15  ASN   A H    1 
ATOM   357  H  HA   . ASN   A 1 15  ? 17.815 -17.992 11.007  1.00 15.72 ?  15  ASN   A HA   1 
ATOM   358  H  HB2  . ASN   A 1 15  ? 19.718 -17.788 9.720   1.00 15.85 ?  15  ASN   A HB2  1 
ATOM   359  H  HB3  . ASN   A 1 15  ? 19.318 -19.323 9.814   1.00 15.85 ?  15  ASN   A HB3  1 
ATOM   360  H  HD21 . ASN   A 1 15  ? 19.865 -17.722 6.446   1.00 16.35 ?  15  ASN   A HD21 1 
ATOM   361  H  HD22 . ASN   A 1 15  ? 20.337 -17.156 7.741   1.00 16.35 ?  15  ASN   A HD22 1 
ATOM   362  N  N    . VAL   A 1 16  ? 16.184 -16.483 8.888   1.00 12.77 ?  16  VAL   A N    1 
ATOM   363  C  CA   . VAL   A 1 16  ? 15.800 -15.198 8.320   1.00 12.53 ?  16  VAL   A CA   1 
ATOM   364  C  C    . VAL   A 1 16  ? 14.525 -14.702 8.989   1.00 12.18 ?  16  VAL   A C    1 
ATOM   365  O  O    . VAL   A 1 16  ? 13.523 -15.430 9.067   1.00 12.38 ?  16  VAL   A O    1 
ATOM   366  C  CB   . VAL   A 1 16  ? 15.629 -15.265 6.794   1.00 13.15 ?  16  VAL   A CB   1 
ATOM   367  C  CG1  . VAL   A 1 16  ? 15.203 -13.898 6.244   1.00 14.04 ?  16  VAL   A CG1  1 
ATOM   368  C  CG2  . VAL   A 1 16  ? 16.910 -15.745 6.120   1.00 14.07 ?  16  VAL   A CG2  1 
ATOM   369  H  H    . VAL   A 1 16  ? 15.607 -17.107 8.757   1.00 15.38 ?  16  VAL   A H    1 
ATOM   370  H  HA   . VAL   A 1 16  ? 16.501 -14.554 8.509   1.00 15.09 ?  16  VAL   A HA   1 
ATOM   371  H  HB   . VAL   A 1 16  ? 14.931 -15.898 6.587   1.00 15.83 ?  16  VAL   A HB   1 
ATOM   372  H  HG11 . VAL   A 1 16  ? 15.302 -13.907 5.278   1.00 16.90 ?  16  VAL   A HG11 1 
ATOM   373  H  HG12 . VAL   A 1 16  ? 14.274 -13.740 6.476   1.00 16.90 ?  16  VAL   A HG12 1 
ATOM   374  H  HG13 . VAL   A 1 16  ? 15.766 -13.211 6.628   1.00 16.90 ?  16  VAL   A HG13 1 
ATOM   375  H  HG21 . VAL   A 1 16  ? 16.794 -15.708 5.158   1.00 16.94 ?  16  VAL   A HG21 1 
ATOM   376  H  HG22 . VAL   A 1 16  ? 17.646 -15.171 6.386   1.00 16.94 ?  16  VAL   A HG22 1 
ATOM   377  H  HG23 . VAL   A 1 16  ? 17.090 -16.658 6.397   1.00 16.94 ?  16  VAL   A HG23 1 
ATOM   378  N  N    A TYR   A 1 17  ? 14.556 -13.440 9.408   0.78 12.18 ?  17  TYR   A N    1 
ATOM   379  N  N    B TYR   A 1 17  ? 14.572 -13.455 9.457   0.22 11.42 ?  17  TYR   A N    1 
ATOM   380  C  CA   A TYR   A 1 17  ? 13.485 -12.761 10.118  0.78 12.00 ?  17  TYR   A CA   1 
ATOM   381  C  CA   B TYR   A 1 17  ? 13.478 -12.762 10.118  0.22 10.81 ?  17  TYR   A CA   1 
ATOM   382  C  C    A TYR   A 1 17  ? 13.229 -11.426 9.431   0.78 12.23 ?  17  TYR   A C    1 
ATOM   383  C  C    B TYR   A 1 17  ? 13.199 -11.458 9.378   0.22 10.51 ?  17  TYR   A C    1 
ATOM   384  O  O    A TYR   A 1 17  ? 14.159 -10.823 8.889   0.78 11.91 ?  17  TYR   A O    1 
ATOM   385  O  O    B TYR   A 1 17  ? 13.983 -11.023 8.531   0.22 10.30 ?  17  TYR   A O    1 
ATOM   386  C  CB   A TYR   A 1 17  ? 13.926 -12.520 11.559  0.78 12.74 ?  17  TYR   A CB   1 
ATOM   387  C  CB   B TYR   A 1 17  ? 13.836 -12.468 11.581  0.22 10.94 ?  17  TYR   A CB   1 
ATOM   388  C  CG   A TYR   A 1 17  ? 14.143 -13.797 12.340  0.78 13.59 ?  17  TYR   A CG   1 
ATOM   389  C  CG   B TYR   A 1 17  ? 13.956 -13.709 12.435  0.22 10.91 ?  17  TYR   A CG   1 
ATOM   390  C  CD1  A TYR   A 1 17  ? 15.327 -14.525 12.236  0.78 14.68 ?  17  TYR   A CD1  1 
ATOM   391  C  CD1  B TYR   A 1 17  ? 15.078 -14.528 12.361  0.22 11.39 ?  17  TYR   A CD1  1 
ATOM   392  C  CD2  A TYR   A 1 17  ? 13.151 -14.291 13.172  0.78 14.11 ?  17  TYR   A CD2  1 
ATOM   393  C  CD2  B TYR   A 1 17  ? 12.940 -14.069 13.307  0.22 10.71 ?  17  TYR   A CD2  1 
ATOM   394  C  CE1  A TYR   A 1 17  ? 15.512 -15.706 12.946  0.78 15.41 ?  17  TYR   A CE1  1 
ATOM   395  C  CE1  B TYR   A 1 17  ? 15.183 -15.673 13.138  0.22 11.33 ?  17  TYR   A CE1  1 
ATOM   396  C  CE2  A TYR   A 1 17  ? 13.328 -15.468 13.889  0.78 14.83 ?  17  TYR   A CE2  1 
ATOM   397  C  CE2  B TYR   A 1 17  ? 13.035 -15.211 14.086  0.22 10.84 ?  17  TYR   A CE2  1 
ATOM   398  C  CZ   A TYR   A 1 17  ? 14.507 -16.175 13.772  0.78 15.04 ?  17  TYR   A CZ   1 
ATOM   399  C  CZ   B TYR   A 1 17  ? 14.156 -16.011 14.000  0.22 10.98 ?  17  TYR   A CZ   1 
ATOM   400  O  OH   A TYR   A 1 17  ? 14.682 -17.342 14.489  0.78 15.61 ?  17  TYR   A OH   1 
ATOM   401  O  OH   B TYR   A 1 17  ? 14.242 -17.146 14.778  0.22 11.15 ?  17  TYR   A OH   1 
ATOM   402  H  H    A TYR   A 1 17  ? 15.232 -12.921 9.266   0.78 14.68 ?  17  TYR   A H    1 
ATOM   403  H  H    B TYR   A 1 17  ? 15.277 -12.958 9.387   0.22 13.75 ?  17  TYR   A H    1 
ATOM   404  H  HA   A TYR   A 1 17  ? 12.675 -13.297 10.101  0.78 14.46 ?  17  TYR   A HA   1 
ATOM   405  H  HA   B TYR   A 1 17  ? 12.679 -13.313 10.093  0.22 13.03 ?  17  TYR   A HA   1 
ATOM   406  H  HB2  A TYR   A 1 17  ? 14.761 -12.036 11.553  0.78 15.34 ?  17  TYR   A HB2  1 
ATOM   407  H  HB2  B TYR   A 1 17  ? 14.685 -12.005 11.610  0.22 13.18 ?  17  TYR   A HB2  1 
ATOM   408  H  HB3  A TYR   A 1 17  ? 13.244 -12.011 12.013  0.78 15.34 ?  17  TYR   A HB3  1 
ATOM   409  H  HB3  B TYR   A 1 17  ? 13.141 -11.912 11.965  0.22 13.18 ?  17  TYR   A HB3  1 
ATOM   410  H  HD1  A TYR   A 1 17  ? 16.004 -14.223 11.678  0.78 17.67 ?  17  TYR   A HD1  1 
ATOM   411  H  HD1  B TYR   A 1 17  ? 15.769 -14.306 11.780  0.22 13.72 ?  17  TYR   A HD1  1 
ATOM   412  H  HD2  A TYR   A 1 17  ? 12.349 -13.830 13.256  0.78 16.99 ?  17  TYR   A HD2  1 
ATOM   413  H  HD2  B TYR   A 1 17  ? 12.180 -13.539 13.372  0.22 12.90 ?  17  TYR   A HD2  1 
ATOM   414  H  HE1  A TYR   A 1 17  ? 16.310 -16.183 12.869  0.78 18.54 ?  17  TYR   A HE1  1 
ATOM   415  H  HE1  B TYR   A 1 17  ? 15.943 -16.210 13.077  0.22 13.65 ?  17  TYR   A HE1  1 
ATOM   416  H  HE2  A TYR   A 1 17  ? 12.650 -15.782 14.445  0.78 17.86 ?  17  TYR   A HE2  1 
ATOM   417  H  HE2  B TYR   A 1 17  ? 12.348 -15.439 14.668  0.22 13.07 ?  17  TYR   A HE2  1 
ATOM   418  H  HH   A TYR   A 1 17  ? 15.440 -17.661 14.341  0.78 18.78 ?  17  TYR   A HH   1 
ATOM   419  H  HH   B TYR   A 1 17  ? 13.497 -17.308 15.121  0.22 13.43 ?  17  TYR   A HH   1 
ATOM   420  N  N    A ILE   A 1 18  ? 11.977 -10.946 9.453   0.78 11.93 ?  18  ILE   A N    1 
ATOM   421  N  N    B ILE   A 1 18  ? 12.079 -10.818 9.711   0.22 10.32 ?  18  ILE   A N    1 
ATOM   422  C  CA   A ILE   A 1 18  ? 11.601 -9.746  8.704   0.78 11.70 ?  18  ILE   A CA   1 
ATOM   423  C  CA   B ILE   A 1 18  ? 11.690 -9.573  9.050   0.22 10.28 ?  18  ILE   A CA   1 
ATOM   424  C  C    A ILE   A 1 18  ? 10.631 -8.880  9.506   0.78 11.89 ?  18  ILE   A C    1 
ATOM   425  C  C    B ILE   A 1 18  ? 10.811 -8.747  9.980   0.22 10.14 ?  18  ILE   A C    1 
ATOM   426  O  O    A ILE   A 1 18  ? 9.793  -9.383  10.260  0.78 12.26 ?  18  ILE   A O    1 
ATOM   427  O  O    B ILE   A 1 18  ? 9.994  -9.286  10.735  0.22 10.08 ?  18  ILE   A O    1 
ATOM   428  C  CB   A ILE   A 1 18  ? 11.046 -10.128 7.311   0.78 11.64 ?  18  ILE   A CB   1 
ATOM   429  C  CB   B ILE   A 1 18  ? 10.996 -9.839  7.697   0.22 9.94  ?  18  ILE   A CB   1 
ATOM   430  C  CG1  A ILE   A 1 18  ? 11.015 -8.919  6.376   0.78 12.07 ?  18  ILE   A CG1  1 
ATOM   431  C  CG1  B ILE   A 1 18  ? 10.895 -8.539  6.892   0.22 10.45 ?  18  ILE   A CG1  1 
ATOM   432  C  CG2  A ILE   A 1 18  ? 9.687  -10.829 7.422   0.78 11.78 ?  18  ILE   A CG2  1 
ATOM   433  C  CG2  B ILE   A 1 18  ? 9.617  -10.461 7.911   0.22 9.92  ?  18  ILE   A CG2  1 
ATOM   434  C  CD1  A ILE   A 1 18  ? 10.747 -9.300  4.949   0.78 13.51 ?  18  ILE   A CD1  1 
ATOM   435  C  CD1  B ILE   A 1 18  ? 10.488 -8.745  5.450   0.22 11.51 ?  18  ILE   A CD1  1 
ATOM   436  H  H    A ILE   A 1 18  ? 11.329 -11.309 9.887   0.78 14.37 ?  18  ILE   A H    1 
ATOM   437  H  H    B ILE   A 1 18  ? 11.538 -11.086 10.318  0.22 12.44 ?  18  ILE   A H    1 
ATOM   438  H  HA   A ILE   A 1 18  ? 12.407 -9.221  8.556   0.78 14.09 ?  18  ILE   A HA   1 
ATOM   439  H  HA   B ILE   A 1 18  ? 12.494 -9.057  8.871   0.22 12.39 ?  18  ILE   A HA   1 
ATOM   440  H  HB   A ILE   A 1 18  ? 11.666 -10.766 6.922   0.78 14.02 ?  18  ILE   A HB   1 
ATOM   441  H  HB   B ILE   A 1 18  ? 11.540 -10.461 7.197   0.22 11.98 ?  18  ILE   A HB   1 
ATOM   442  H  HG12 A ILE   A 1 18  ? 10.322 -8.310  6.659   0.78 14.54 ?  18  ILE   A HG12 1 
ATOM   443  H  HG12 B ILE   A 1 18  ? 10.235 -7.961  7.306   0.22 12.60 ?  18  ILE   A HG12 1 
ATOM   444  H  HG13 A ILE   A 1 18  ? 11.882 -8.473  6.403   0.78 14.54 ?  18  ILE   A HG13 1 
ATOM   445  H  HG13 B ILE   A 1 18  ? 11.761 -8.098  6.894   0.22 12.60 ?  18  ILE   A HG13 1 
ATOM   446  H  HG21 A ILE   A 1 18  ? 9.447  -11.195 6.553   0.78 14.20 ?  18  ILE   A HG21 1 
ATOM   447  H  HG21 B ILE   A 1 18  ? 9.287  -10.793 7.060   0.22 11.96 ?  18  ILE   A HG21 1 
ATOM   448  H  HG22 A ILE   A 1 18  ? 9.754  -11.545 8.071   0.78 14.20 ?  18  ILE   A HG22 1 
ATOM   449  H  HG22 B ILE   A 1 18  ? 9.696  -11.192 8.542   0.22 11.96 ?  18  ILE   A HG22 1 
ATOM   450  H  HG23 A ILE   A 1 18  ? 9.019  -10.186 7.703   0.78 14.20 ?  18  ILE   A HG23 1 
ATOM   451  H  HG23 B ILE   A 1 18  ? 9.011  -9.787  8.258   0.22 11.96 ?  18  ILE   A HG23 1 
ATOM   452  H  HD11 A ILE   A 1 18  ? 10.825 -8.507  4.389   0.78 16.26 ?  18  ILE   A HD11 1 
ATOM   453  H  HD11 B ILE   A 1 18  ? 10.479 -7.885  4.999   0.22 13.87 ?  18  ILE   A HD11 1 
ATOM   454  H  HD12 A ILE   A 1 18  ? 11.394 -9.963  4.667   0.78 16.26 ?  18  ILE   A HD12 1 
ATOM   455  H  HD12 B ILE   A 1 18  ? 11.129 -9.335  5.023   0.22 13.87 ?  18  ILE   A HD12 1 
ATOM   456  H  HD13 A ILE   A 1 18  ? 9.850  -9.660  4.882   0.78 16.26 ?  18  ILE   A HD13 1 
ATOM   457  H  HD13 B ILE   A 1 18  ? 9.604  -9.141  5.425   0.22 13.87 ?  18  ILE   A HD13 1 
ATOM   458  N  N    A LYS   A 1 19  ? 10.741 -7.559  9.323   0.78 11.91 ?  19  LYS   A N    1 
ATOM   459  N  N    B LYS   A 1 19  ? 10.978 -7.424  9.905   0.22 10.45 ?  19  LYS   A N    1 
ATOM   460  C  CA   A LYS   A 1 19  ? 9.930  -6.600  10.065  0.78 12.70 ?  19  LYS   A CA   1 
ATOM   461  C  CA   B LYS   A 1 19  ? 10.217 -6.478  10.709  0.22 11.71 ?  19  LYS   A CA   1 
ATOM   462  C  C    A LYS   A 1 19  ? 9.748  -5.342  9.228   0.78 12.79 ?  19  LYS   A C    1 
ATOM   463  C  C    B LYS   A 1 19  ? 9.928  -5.243  9.875   0.22 12.40 ?  19  LYS   A C    1 
ATOM   464  O  O    A LYS   A 1 19  ? 10.648 -4.950  8.483   0.78 12.58 ?  19  LYS   A O    1 
ATOM   465  O  O    B LYS   A 1 19  ? 10.776 -4.798  9.098   0.22 12.26 ?  19  LYS   A O    1 
ATOM   466  C  CB   A LYS   A 1 19  ? 10.630 -6.236  11.381  0.78 14.09 ?  19  LYS   A CB   1 
ATOM   467  C  CB   B LYS   A 1 19  ? 10.996 -6.064  11.965  0.22 12.29 ?  19  LYS   A CB   1 
ATOM   468  C  CG   A LYS   A 1 19  ? 9.873  -5.311  12.323  0.78 15.69 ?  19  LYS   A CG   1 
ATOM   469  C  CG   B LYS   A 1 19  ? 10.284 -5.094  12.899  0.22 12.96 ?  19  LYS   A CG   1 
ATOM   470  C  CD   A LYS   A 1 19  ? 10.744 -5.016  13.540  0.78 17.40 ?  19  LYS   A CD   1 
ATOM   471  C  CD   B LYS   A 1 19  ? 11.218 -4.691  14.033  0.22 13.38 ?  19  LYS   A CD   1 
ATOM   472  C  CE   A LYS   A 1 19  ? 10.077 -4.078  14.524  0.78 18.69 ?  19  LYS   A CE   1 
ATOM   473  C  CE   B LYS   A 1 19  ? 10.519 -3.874  15.102  0.22 14.14 ?  19  LYS   A CE   1 
ATOM   474  N  NZ   A LYS   A 1 19  ? 10.971 -3.819  15.685  0.78 19.20 ?  19  LYS   A NZ   1 
ATOM   475  N  NZ   B LYS   A 1 19  ? 11.392 -3.714  16.301  0.22 14.52 ?  19  LYS   A NZ   1 
ATOM   476  H  H    A LYS   A 1 19  ? 11.292 -7.191  8.762   0.78 14.35 ?  19  LYS   A H    1 
ATOM   477  H  H    B LYS   A 1 19  ? 11.547 -7.036  9.378   0.22 12.60 ?  19  LYS   A H    1 
ATOM   478  H  HA   A LYS   A 1 19  ? 9.061  -6.987  10.255  0.78 15.29 ?  19  LYS   A HA   1 
ATOM   479  H  HA   B LYS   A 1 19  ? 9.378  -6.872  10.977  0.22 14.11 ?  19  LYS   A HA   1 
ATOM   480  H  HB2  A LYS   A 1 19  ? 10.804 -7.058  11.862  0.78 16.96 ?  19  LYS   A HB2  1 
ATOM   481  H  HB2  B LYS   A 1 19  ? 11.186 -6.859  12.480  0.22 14.81 ?  19  LYS   A HB2  1 
ATOM   482  H  HB3  A LYS   A 1 19  ? 11.470 -5.804  11.164  0.78 16.96 ?  19  LYS   A HB3  1 
ATOM   483  H  HB3  B LYS   A 1 19  ? 11.828 -5.644  11.693  0.22 14.81 ?  19  LYS   A HB3  1 
ATOM   484  H  HG2  A LYS   A 1 19  ? 9.672  -4.477  11.873  0.78 18.89 ?  19  LYS   A HG2  1 
ATOM   485  H  HG2  B LYS   A 1 19  ? 10.030 -4.294  12.415  0.22 15.61 ?  19  LYS   A HG2  1 
ATOM   486  H  HG3  A LYS   A 1 19  ? 9.057  -5.746  12.621  0.78 18.89 ?  19  LYS   A HG3  1 
ATOM   487  H  HG3  B LYS   A 1 19  ? 9.504  -5.524  13.283  0.22 15.61 ?  19  LYS   A HG3  1 
ATOM   488  H  HD2  A LYS   A 1 19  ? 10.936 -5.848  14.002  0.78 20.94 ?  19  LYS   A HD2  1 
ATOM   489  H  HD2  B LYS   A 1 19  ? 11.563 -5.492  14.454  0.22 16.12 ?  19  LYS   A HD2  1 
ATOM   490  H  HD3  A LYS   A 1 19  ? 11.571 -4.605  13.244  0.78 20.94 ?  19  LYS   A HD3  1 
ATOM   491  H  HD3  B LYS   A 1 19  ? 11.949 -4.162  13.673  0.22 16.12 ?  19  LYS   A HD3  1 
ATOM   492  H  HE2  A LYS   A 1 19  ? 9.891  -3.232  14.086  0.78 22.49 ?  19  LYS   A HE2  1 
ATOM   493  H  HE2  B LYS   A 1 19  ? 10.317 -2.992  14.752  0.22 17.02 ?  19  LYS   A HE2  1 
ATOM   494  H  HE3  A LYS   A 1 19  ? 9.258  -4.479  14.850  0.78 22.49 ?  19  LYS   A HE3  1 
ATOM   495  H  HE3  B LYS   A 1 19  ? 9.706  -4.326  15.373  0.22 17.02 ?  19  LYS   A HE3  1 
ATOM   496  H  HZ1  A LYS   A 1 19  ? 10.562 -3.293  16.271  0.78 23.10 ?  19  LYS   A HZ1  1 
ATOM   497  H  HZ1  B LYS   A 1 19  ? 10.958 -3.265  16.935  0.22 17.48 ?  19  LYS   A HZ1  1 
ATOM   498  H  HZ2  A LYS   A 1 19  ? 11.183 -4.588  16.080  0.78 23.10 ?  19  LYS   A HZ2  1 
ATOM   499  H  HZ2  B LYS   A 1 19  ? 11.621 -4.513  16.618  0.22 17.48 ?  19  LYS   A HZ2  1 
ATOM   500  H  HZ3  A LYS   A 1 19  ? 11.718 -3.422  15.409  0.78 23.10 ?  19  LYS   A HZ3  1 
ATOM   501  H  HZ3  B LYS   A 1 19  ? 12.130 -3.267  16.084  0.22 17.48 ?  19  LYS   A HZ3  1 
ATOM   502  N  N    A ASN   A 1 20  ? 8.576  -4.712  9.352   0.78 13.61 ?  20  ASN   A N    1 
ATOM   503  N  N    B ASN   A 1 20  ? 8.726  -4.701  10.035  0.22 13.78 ?  20  ASN   A N    1 
ATOM   504  C  CA   A ASN   A 1 20  ? 8.351  -3.379  8.795   0.78 14.89 ?  20  ASN   A CA   1 
ATOM   505  C  CA   B ASN   A 1 20  ? 8.331  -3.454  9.385   0.22 15.35 ?  20  ASN   A CA   1 
ATOM   506  C  C    A ASN   A 1 20  ? 8.978  -2.376  9.756   0.78 15.55 ?  20  ASN   A C    1 
ATOM   507  C  C    B ASN   A 1 20  ? 8.811  -2.307  10.263  0.22 15.90 ?  20  ASN   A C    1 
ATOM   508  O  O    A ASN   A 1 20  ? 8.460  -2.149  10.855  0.78 17.15 ?  20  ASN   A O    1 
ATOM   509  O  O    B ASN   A 1 20  ? 8.123  -1.872  11.188  0.22 16.23 ?  20  ASN   A O    1 
ATOM   510  C  CB   A ASN   A 1 20  ? 6.852  -3.134  8.609   0.78 16.19 ?  20  ASN   A CB   1 
ATOM   511  C  CB   B ASN   A 1 20  ? 6.821  -3.421  9.195   0.22 16.36 ?  20  ASN   A CB   1 
ATOM   512  C  CG   A ASN   A 1 20  ? 6.517  -1.711  8.163   0.78 17.81 ?  20  ASN   A CG   1 
ATOM   513  C  CG   B ASN   A 1 20  ? 6.323  -2.077  8.716   0.22 17.32 ?  20  ASN   A CG   1 
ATOM   514  O  OD1  A ASN   A 1 20  ? 5.482  -1.170  8.546   0.78 20.02 ?  20  ASN   A OD1  1 
ATOM   515  O  OD1  B ASN   A 1 20  ? 5.588  -1.388  9.424   0.22 17.92 ?  20  ASN   A OD1  1 
ATOM   516  N  ND2  A ASN   A 1 20  ? 7.364  -1.115  7.338   0.78 18.11 ?  20  ASN   A ND2  1 
ATOM   517  N  ND2  B ASN   A 1 20  ? 6.723  -1.691  7.509   0.22 17.55 ?  20  ASN   A ND2  1 
ATOM   518  H  H    A ASN   A 1 20  ? 7.892  -5.038  9.761   0.78 16.38 ?  20  ASN   A H    1 
ATOM   519  H  H    B ASN   A 1 20  ? 8.108  -5.044  10.517  0.22 16.59 ?  20  ASN   A H    1 
ATOM   520  H  HA   A ASN   A 1 20  ? 8.789  -3.307  7.936   0.78 17.93 ?  20  ASN   A HA   1 
ATOM   521  H  HA   B ASN   A 1 20  ? 8.760  -3.385  8.521   0.22 18.48 ?  20  ASN   A HA   1 
ATOM   522  H  HB2  A ASN   A 1 20  ? 6.517  -3.739  7.932   0.78 19.48 ?  20  ASN   A HB2  1 
ATOM   523  H  HB2  B ASN   A 1 20  ? 6.571  -4.087  8.538   0.22 19.69 ?  20  ASN   A HB2  1 
ATOM   524  H  HB3  A ASN   A 1 20  ? 6.401  -3.303  9.453   0.78 19.48 ?  20  ASN   A HB3  1 
ATOM   525  H  HB3  B ASN   A 1 20  ? 6.392  -3.612  10.043  0.22 19.69 ?  20  ASN   A HB3  1 
ATOM   526  H  HD21 A ASN   A 1 20  ? 7.207  -0.311  7.075   0.78 21.78 ?  20  ASN   A HD21 1 
ATOM   527  H  HD21 B ASN   A 1 20  ? 6.465  -0.936  7.190   0.22 21.12 ?  20  ASN   A HD21 1 
ATOM   528  H  HD22 A ASN   A 1 20  ? 8.073  -1.522  7.082   0.78 21.78 ?  20  ASN   A HD22 1 
ATOM   529  H  HD22 B ASN   A 1 20  ? 7.240  -2.199  7.044   0.22 21.12 ?  20  ASN   A HD22 1 
ATOM   530  N  N    A ALA   A 1 21  ? 10.116 -1.805  9.368   0.78 15.31 ?  21  ALA   A N    1 
ATOM   531  N  N    B ALA   A 1 21  ? 10.006 -1.801  9.968   0.22 16.14 ?  21  ALA   A N    1 
ATOM   532  C  CA   A ALA   A 1 21  ? 10.821 -0.909  10.271  0.78 15.25 ?  21  ALA   A CA   1 
ATOM   533  C  CA   B ALA   A 1 21  ? 10.606 -0.793  10.829  0.22 16.38 ?  21  ALA   A CA   1 
ATOM   534  C  C    A ALA   A 1 21  ? 11.783 -0.030  9.490   0.78 14.79 ?  21  ALA   A C    1 
ATOM   535  C  C    B ALA   A 1 21  ? 11.638 0.004   10.049  0.22 16.38 ?  21  ALA   A C    1 
ATOM   536  O  O    A ALA   A 1 21  ? 12.237 -0.390  8.399   0.78 14.81 ?  21  ALA   A O    1 
ATOM   537  O  O    B ALA   A 1 21  ? 12.140 -0.433  9.010   0.22 16.36 ?  21  ALA   A O    1 
ATOM   538  C  CB   A ALA   A 1 21  ? 11.591 -1.686  11.342  0.78 16.23 ?  21  ALA   A CB   1 
ATOM   539  C  CB   B ALA   A 1 21  ? 11.244 -1.423  12.070  0.22 16.66 ?  21  ALA   A CB   1 
ATOM   540  H  H    A ALA   A 1 21  ? 10.489 -1.920  8.602   0.78 18.43 ?  21  ALA   A H    1 
ATOM   541  H  H    B ALA   A 1 21  ? 10.476 -2.014  9.279   0.22 19.43 ?  21  ALA   A H    1 
ATOM   542  H  HA   A ALA   A 1 21  ? 10.173 -0.335  10.715  0.78 18.36 ?  21  ALA   A HA   1 
ATOM   543  H  HA   B ALA   A 1 21  ? 9.917  -0.180  11.122  0.22 19.71 ?  21  ALA   A HA   1 
ATOM   544  H  HB1  A ALA   A 1 21  ? 12.021 -1.053  11.935  0.78 19.54 ?  21  ALA   A HB1  1 
ATOM   545  H  HB1  B ALA   A 1 21  ? 11.642 -0.723  12.610  0.22 20.05 ?  21  ALA   A HB1  1 
ATOM   546  H  HB2  A ALA   A 1 21  ? 10.965 -2.236  11.842  0.78 19.54 ?  21  ALA   A HB2  1 
ATOM   547  H  HB2  B ALA   A 1 21  ? 10.557 -1.882  12.577  0.22 20.05 ?  21  ALA   A HB2  1 
ATOM   548  H  HB3  A ALA   A 1 21  ? 12.252 -2.245  10.910  0.78 19.54 ?  21  ALA   A HB3  1 
ATOM   549  H  HB3  B ALA   A 1 21  ? 11.926 -2.053  11.790  0.22 20.05 ?  21  ALA   A HB3  1 
ATOM   550  N  N    A ASP   A 1 22  ? 12.067 1.133   10.072  0.78 15.06 ?  22  ASP   A N    1 
ATOM   551  N  N    B ASP   A 1 22  ? 11.940 1.190   10.574  0.22 16.44 ?  22  ASP   A N    1 
ATOM   552  C  CA   A ASP   A 1 22  ? 13.113 2.037   9.614   0.78 15.60 ?  22  ASP   A CA   1 
ATOM   553  C  CA   B ASP   A 1 22  ? 12.981 2.040   10.020  0.22 16.49 ?  22  ASP   A CA   1 
ATOM   554  C  C    A ASP   A 1 22  ? 14.434 1.526   10.184  0.78 14.47 ?  22  ASP   A C    1 
ATOM   555  C  C    B ASP   A 1 22  ? 14.334 1.462   10.409  0.22 15.52 ?  22  ASP   A C    1 
ATOM   556  O  O    A ASP   A 1 22  ? 14.622 1.513   11.404  0.78 15.23 ?  22  ASP   A O    1 
ATOM   557  O  O    B ASP   A 1 22  ? 14.573 1.154   11.581  0.22 15.49 ?  22  ASP   A O    1 
ATOM   558  C  CB   A ASP   A 1 22  ? 12.771 3.431   10.137  0.78 18.83 ?  22  ASP   A CB   1 
ATOM   559  C  CB   B ASP   A 1 22  ? 12.838 3.452   10.584  0.22 17.59 ?  22  ASP   A CB   1 
ATOM   560  C  CG   A ASP   A 1 22  ? 13.808 4.481   9.782   0.78 21.50 ?  22  ASP   A CG   1 
ATOM   561  C  CG   B ASP   A 1 22  ? 13.456 4.505   9.688   0.22 18.35 ?  22  ASP   A CG   1 
ATOM   562  O  OD1  A ASP   A 1 22  ? 14.920 4.119   9.352   0.78 21.99 ?  22  ASP   A OD1  1 
ATOM   563  O  OD1  B ASP   A 1 22  ? 14.458 4.202   9.009   0.22 18.86 ?  22  ASP   A OD1  1 
ATOM   564  O  OD2  A ASP   A 1 22  ? 13.513 5.685   9.950   0.78 23.48 -1 22  ASP   A OD2  1 
ATOM   565  O  OD2  B ASP   A 1 22  ? 12.938 5.642   9.666   0.22 18.61 -1 22  ASP   A OD2  1 
ATOM   566  H  H    A ASP   A 1 22  ? 11.631 1.432   10.758  0.78 18.13 ?  22  ASP   A H    1 
ATOM   567  H  H    B ASP   A 1 22  ? 11.548 1.527   11.262  0.22 19.78 ?  22  ASP   A H    1 
ATOM   568  H  HA   A ASP   A 1 22  ? 13.151 2.041   8.644   0.78 18.78 ?  22  ASP   A HA   1 
ATOM   569  H  HA   B ASP   A 1 22  ? 12.906 2.078   9.051   0.22 19.84 ?  22  ASP   A HA   1 
ATOM   570  H  HB2  A ASP   A 1 22  ? 11.909 3.696   9.777   0.78 22.65 ?  22  ASP   A HB2  1 
ATOM   571  H  HB2  B ASP   A 1 22  ? 11.895 3.654   10.709  0.22 21.17 ?  22  ASP   A HB2  1 
ATOM   572  H  HB3  A ASP   A 1 22  ? 12.723 3.393   11.106  0.78 22.65 ?  22  ASP   A HB3  1 
ATOM   573  H  HB3  B ASP   A 1 22  ? 13.298 3.498   11.435  0.22 21.17 ?  22  ASP   A HB3  1 
ATOM   574  N  N    A ILE   A 1 23  ? 15.344 1.082   9.306   0.78 13.94 ?  23  ILE   A N    1 
ATOM   575  N  N    B ILE   A 1 23  ? 15.220 1.305   9.424   0.22 15.16 ?  23  ILE   A N    1 
ATOM   576  C  CA   A ILE   A 1 23  ? 16.594 0.463   9.755   0.78 13.45 ?  23  ILE   A CA   1 
ATOM   577  C  CA   B ILE   A 1 23  ? 16.497 0.657   9.698   0.22 14.72 ?  23  ILE   A CA   1 
ATOM   578  C  C    A ILE   A 1 23  ? 17.396 1.397   10.653  0.78 13.60 ?  23  ILE   A C    1 
ATOM   579  C  C    B ILE   A 1 23  ? 17.374 1.533   10.583  0.22 14.94 ?  23  ILE   A C    1 
ATOM   580  O  O    A ILE   A 1 23  ? 18.106 0.938   11.560  0.78 13.79 ?  23  ILE   A O    1 
ATOM   581  O  O    B ILE   A 1 23  ? 18.164 1.021   11.385  0.22 15.18 ?  23  ILE   A O    1 
ATOM   582  C  CB   A ILE   A 1 23  ? 17.414 -0.054  8.548   0.78 12.81 ?  23  ILE   A CB   1 
ATOM   583  C  CB   B ILE   A 1 23  ? 17.201 0.230   8.396   0.22 14.29 ?  23  ILE   A CB   1 
ATOM   584  C  CG1  A ILE   A 1 23  ? 18.546 -0.976  9.012   0.78 12.64 ?  23  ILE   A CG1  1 
ATOM   585  C  CG1  B ILE   A 1 23  ? 18.313 -0.768  8.720   0.22 14.11 ?  23  ILE   A CG1  1 
ATOM   586  C  CG2  A ILE   A 1 23  ? 17.940 1.101   7.695   0.78 12.92 ?  23  ILE   A CG2  1 
ATOM   587  C  CG2  B ILE   A 1 23  ? 17.750 1.441   7.652   0.22 14.18 ?  23  ILE   A CG2  1 
ATOM   588  C  CD1  A ILE   A 1 23  ? 19.258 -1.681  7.868   0.78 12.70 ?  23  ILE   A CD1  1 
ATOM   589  C  CD1  B ILE   A 1 23  ? 18.951 -1.377  7.506   0.22 14.10 ?  23  ILE   A CD1  1 
ATOM   590  H  H    A ILE   A 1 23  ? 15.250 1.117   8.458   0.78 16.79 ?  23  ILE   A H    1 
ATOM   591  H  H    B ILE   A 1 23  ? 15.106 1.558   8.616   0.22 18.25 ?  23  ILE   A H    1 
ATOM   592  H  HA   A ILE   A 1 23  ? 16.371 -0.313  10.293  0.78 16.19 ?  23  ILE   A HA   1 
ATOM   593  H  HA   B ILE   A 1 23  ? 16.308 -0.155  10.190  0.22 17.72 ?  23  ILE   A HA   1 
ATOM   594  H  HB   A ILE   A 1 23  ? 16.818 -0.582  7.995   0.78 15.43 ?  23  ILE   A HB   1 
ATOM   595  H  HB   B ILE   A 1 23  ? 16.554 -0.212  7.825   0.22 17.20 ?  23  ILE   A HB   1 
ATOM   596  H  HG12 A ILE   A 1 23  ? 19.207 -0.452  9.491   0.78 15.22 ?  23  ILE   A HG12 1 
ATOM   597  H  HG12 B ILE   A 1 23  ? 19.005 -0.312  9.224   0.22 16.98 ?  23  ILE   A HG12 1 
ATOM   598  H  HG13 A ILE   A 1 23  ? 18.181 -1.660  9.596   0.78 15.22 ?  23  ILE   A HG13 1 
ATOM   599  H  HG13 B ILE   A 1 23  ? 17.940 -1.489  9.253   0.22 16.98 ?  23  ILE   A HG13 1 
ATOM   600  H  HG21 A ILE   A 1 23  ? 18.302 0.742   6.867   0.78 15.56 ?  23  ILE   A HG21 1 
ATOM   601  H  HG21 B ILE   A 1 23  ? 17.990 1.174   6.749   0.22 17.07 ?  23  ILE   A HG21 1 
ATOM   602  H  HG22 A ILE   A 1 23  ? 17.208 1.704   7.498   0.78 15.56 ?  23  ILE   A HG22 1 
ATOM   603  H  HG22 B ILE   A 1 23  ? 17.067 2.128   7.621   0.22 17.07 ?  23  ILE   A HG22 1 
ATOM   604  H  HG23 A ILE   A 1 23  ? 18.633 1.567   8.184   0.78 15.56 ?  23  ILE   A HG23 1 
ATOM   605  H  HG23 B ILE   A 1 23  ? 18.532 1.772   8.117   0.22 17.07 ?  23  ILE   A HG23 1 
ATOM   606  H  HD11 A ILE   A 1 23  ? 19.898 -2.311  8.234   0.78 15.29 ?  23  ILE   A HD11 1 
ATOM   607  H  HD11 B ILE   A 1 23  ? 19.585 -2.050  7.792   0.22 16.97 ?  23  ILE   A HD11 1 
ATOM   608  H  HD12 A ILE   A 1 23  ? 18.601 -2.151  7.331   0.78 15.29 ?  23  ILE   A HD12 1 
ATOM   609  H  HD12 B ILE   A 1 23  ? 18.259 -1.780  6.960   0.22 16.97 ?  23  ILE   A HD12 1 
ATOM   610  H  HD13 A ILE   A 1 23  ? 19.717 -1.020  7.326   0.78 15.29 ?  23  ILE   A HD13 1 
ATOM   611  H  HD13 B ILE   A 1 23  ? 19.405 -0.680  7.009   0.22 16.97 ?  23  ILE   A HD13 1 
ATOM   612  N  N    A VAL   A 1 24  ? 17.285 2.710   10.437  0.78 14.88 ?  24  VAL   A N    1 
ATOM   613  N  N    B VAL   A 1 24  ? 17.255 2.857   10.460  0.22 15.22 ?  24  VAL   A N    1 
ATOM   614  C  CA   A VAL   A 1 24  ? 17.975 3.669   11.295  0.78 16.37 ?  24  VAL   A CA   1 
ATOM   615  C  CA   B VAL   A 1 24  ? 17.947 3.746   11.388  0.22 15.72 ?  24  VAL   A CA   1 
ATOM   616  C  C    A VAL   A 1 24  ? 17.444 3.584   12.720  0.78 16.78 ?  24  VAL   A C    1 
ATOM   617  C  C    B VAL   A 1 24  ? 17.378 3.594   12.793  0.22 16.24 ?  24  VAL   A C    1 
ATOM   618  O  O    A VAL   A 1 24  ? 18.213 3.478   13.685  0.78 16.96 ?  24  VAL   A O    1 
ATOM   619  O  O    B VAL   A 1 24  ? 18.121 3.586   13.782  0.22 16.14 ?  24  VAL   A O    1 
ATOM   620  C  CB   A VAL   A 1 24  ? 17.838 5.090   10.722  0.78 17.70 ?  24  VAL   A CB   1 
ATOM   621  C  CB   B VAL   A 1 24  ? 17.878 5.202   10.892  0.22 15.69 ?  24  VAL   A CB   1 
ATOM   622  C  CG1  A VAL   A 1 24  ? 18.357 6.125   11.717  0.78 18.92 ?  24  VAL   A CG1  1 
ATOM   623  C  CG1  B VAL   A 1 24  ? 18.303 6.168   11.992  0.22 15.70 ?  24  VAL   A CG1  1 
ATOM   624  C  CG2  A VAL   A 1 24  ? 18.571 5.192   9.392   0.78 18.79 ?  24  VAL   A CG2  1 
ATOM   625  C  CG2  B VAL   A 1 24  ? 18.748 5.380   9.658   0.22 16.02 ?  24  VAL   A CG2  1 
ATOM   626  H  H    A VAL   A 1 24  ? 16.820 3.063   9.807   0.78 17.92 ?  24  VAL   A H    1 
ATOM   627  H  H    B VAL   A 1 24  ? 16.791 3.257   9.856   0.22 18.31 ?  24  VAL   A H    1 
ATOM   628  H  HA   A VAL   A 1 24  ? 18.919 3.452   11.316  0.78 19.70 ?  24  VAL   A HA   1 
ATOM   629  H  HA   B VAL   A 1 24  ? 18.881 3.492   11.419  0.22 18.92 ?  24  VAL   A HA   1 
ATOM   630  H  HB   A VAL   A 1 24  ? 16.902 5.279   10.556  0.78 21.29 ?  24  VAL   A HB   1 
ATOM   631  H  HB   B VAL   A 1 24  ? 16.963 5.411   10.647  0.22 18.88 ?  24  VAL   A HB   1 
ATOM   632  H  HG11 A VAL   A 1 24  ? 18.525 6.956   11.247  0.78 22.76 ?  24  VAL   A HG11 1 
ATOM   633  H  HG11 B VAL   A 1 24  ? 18.537 7.019   11.589  0.22 18.90 ?  24  VAL   A HG11 1 
ATOM   634  H  HG12 A VAL   A 1 24  ? 17.688 6.264   12.404  0.78 22.76 ?  24  VAL   A HG12 1 
ATOM   635  H  HG12 B VAL   A 1 24  ? 17.564 6.290   12.607  0.22 18.90 ?  24  VAL   A HG12 1 
ATOM   636  H  HG13 A VAL   A 1 24  ? 19.180 5.796   12.112  0.78 22.76 ?  24  VAL   A HG13 1 
ATOM   637  H  HG13 B VAL   A 1 24  ? 19.071 5.802   12.458  0.22 18.90 ?  24  VAL   A HG13 1 
ATOM   638  H  HG21 A VAL   A 1 24  ? 18.412 6.069   9.006   0.78 22.61 ?  24  VAL   A HG21 1 
ATOM   639  H  HG21 B VAL   A 1 24  ? 18.669 6.295   9.344   0.22 19.28 ?  24  VAL   A HG21 1 
ATOM   640  H  HG22 A VAL   A 1 24  ? 19.523 5.071   9.545   0.78 22.61 ?  24  VAL   A HG22 1 
ATOM   641  H  HG22 B VAL   A 1 24  ? 19.670 5.188   9.891   0.22 19.28 ?  24  VAL   A HG22 1 
ATOM   642  H  HG23 A VAL   A 1 24  ? 18.243 4.504   8.792   0.78 22.61 ?  24  VAL   A HG23 1 
ATOM   643  H  HG23 B VAL   A 1 24  ? 18.446 4.767   8.968   0.22 19.28 ?  24  VAL   A HG23 1 
ATOM   644  N  N    A GLU   A 1 25  ? 16.120 3.643   12.875  0.78 17.87 ?  25  GLU   A N    1 
ATOM   645  N  N    B GLU   A 1 25  ? 16.054 3.472   12.903  0.22 17.12 ?  25  GLU   A N    1 
ATOM   646  C  CA   A GLU   A 1 25  ? 15.533 3.582   14.209  0.78 19.34 ?  25  GLU   A CA   1 
ATOM   647  C  CA   B GLU   A 1 25  ? 15.433 3.298   14.211  0.22 18.15 ?  25  GLU   A CA   1 
ATOM   648  C  C    A GLU   A 1 25  ? 15.774 2.223   14.853  0.78 18.30 ?  25  GLU   A C    1 
ATOM   649  C  C    B GLU   A 1 25  ? 15.729 1.917   14.786  0.22 17.78 ?  25  GLU   A C    1 
ATOM   650  O  O    A GLU   A 1 25  ? 16.016 2.135   16.061  0.78 18.76 ?  25  GLU   A O    1 
ATOM   651  O  O    B GLU   A 1 25  ? 15.957 1.779   15.994  0.22 17.89 ?  25  GLU   A O    1 
ATOM   652  C  CB   A GLU   A 1 25  ? 14.042 3.918   14.139  0.78 22.27 ?  25  GLU   A CB   1 
ATOM   653  C  CB   B GLU   A 1 25  ? 13.927 3.550   14.115  0.22 19.41 ?  25  GLU   A CB   1 
ATOM   654  C  CG   A GLU   A 1 25  ? 13.774 5.357   13.718  0.78 25.37 ?  25  GLU   A CG   1 
ATOM   655  C  CG   B GLU   A 1 25  ? 13.568 4.990   13.762  0.22 20.96 ?  25  GLU   A CG   1 
ATOM   656  C  CD   A GLU   A 1 25  ? 14.556 6.363   14.539  0.78 28.16 ?  25  GLU   A CD   1 
ATOM   657  C  CD   B GLU   A 1 25  ? 14.026 5.977   14.818  0.22 22.11 ?  25  GLU   A CD   1 
ATOM   658  O  OE1  A GLU   A 1 25  ? 14.647 6.187   15.773  0.78 28.95 ?  25  GLU   A OE1  1 
ATOM   659  O  OE1  B GLU   A 1 25  ? 13.956 5.641   16.019  0.22 22.38 ?  25  GLU   A OE1  1 
ATOM   660  O  OE2  A GLU   A 1 25  ? 15.101 7.317   13.945  0.78 29.15 -1 25  GLU   A OE2  1 
ATOM   661  O  OE2  B GLU   A 1 25  ? 14.466 7.086   14.447  0.22 22.48 -1 25  GLU   A OE2  1 
ATOM   662  H  H    A GLU   A 1 25  ? 15.553 3.723   12.233  0.78 21.49 ?  25  GLU   A H    1 
ATOM   663  H  H    B GLU   A 1 25  ? 15.505 3.494   12.244  0.22 20.60 ?  25  GLU   A H    1 
ATOM   664  H  HA   A GLU   A 1 25  ? 15.961 4.246   14.769  0.78 23.27 ?  25  GLU   A HA   1 
ATOM   665  H  HA   B GLU   A 1 25  ? 15.802 3.951   14.822  0.22 21.83 ?  25  GLU   A HA   1 
ATOM   666  H  HB2  A GLU   A 1 25  ? 13.613 3.339   13.489  0.78 26.78 ?  25  GLU   A HB2  1 
ATOM   667  H  HB2  B GLU   A 1 25  ? 13.549 2.969   13.438  0.22 23.34 ?  25  GLU   A HB2  1 
ATOM   668  H  HB3  A GLU   A 1 25  ? 13.644 3.788   15.013  0.78 26.78 ?  25  GLU   A HB3  1 
ATOM   669  H  HB3  B GLU   A 1 25  ? 13.525 3.356   14.972  0.22 23.34 ?  25  GLU   A HB3  1 
ATOM   670  H  HG2  A GLU   A 1 25  ? 14.043 5.474   12.796  0.78 30.50 ?  25  GLU   A HG2  1 
ATOM   671  H  HG2  B GLU   A 1 25  ? 13.994 5.231   12.925  0.22 25.21 ?  25  GLU   A HG2  1 
ATOM   672  H  HG3  A GLU   A 1 25  ? 12.825 5.545   13.816  0.78 30.50 ?  25  GLU   A HG3  1 
ATOM   673  H  HG3  B GLU   A 1 25  ? 12.605 5.067   13.679  0.22 25.21 ?  25  GLU   A HG3  1 
ATOM   674  N  N    A GLU   A 1 26  ? 15.740 1.153   14.056  0.78 17.98 ?  26  GLU   A N    1 
ATOM   675  N  N    B GLU   A 1 26  ? 15.739 0.882   13.941  0.22 17.39 ?  26  GLU   A N    1 
ATOM   676  C  CA   A GLU   A 1 26  ? 16.038 -0.174  14.585  0.78 17.49 ?  26  GLU   A CA   1 
ATOM   677  C  CA   B GLU   A 1 26  ? 16.095 -0.450  14.421  0.22 17.02 ?  26  GLU   A CA   1 
ATOM   678  C  C    A GLU   A 1 26  ? 17.471 -0.250  15.098  0.78 16.22 ?  26  GLU   A C    1 
ATOM   679  C  C    B GLU   A 1 26  ? 17.517 -0.479  14.957  0.22 16.09 ?  26  GLU   A C    1 
ATOM   680  O  O    A GLU   A 1 26  ? 17.726 -0.760  16.195  0.78 16.56 ?  26  GLU   A O    1 
ATOM   681  O  O    B GLU   A 1 26  ? 17.801 -1.150  15.956  0.22 15.92 ?  26  GLU   A O    1 
ATOM   682  C  CB   A GLU   A 1 26  ? 15.816 -1.225  13.500  0.78 19.33 ?  26  GLU   A CB   1 
ATOM   683  C  CB   B GLU   A 1 26  ? 15.943 -1.480  13.300  0.22 17.66 ?  26  GLU   A CB   1 
ATOM   684  C  CG   A GLU   A 1 26  ? 14.387 -1.670  13.326  0.78 22.76 ?  26  GLU   A CG   1 
ATOM   685  C  CG   B GLU   A 1 26  ? 14.567 -2.099  13.206  0.22 18.13 ?  26  GLU   A CG   1 
ATOM   686  C  CD   A GLU   A 1 26  ? 13.864 -2.475  14.496  0.78 24.64 ?  26  GLU   A CD   1 
ATOM   687  C  CD   B GLU   A 1 26  ? 14.119 -2.734  14.503  0.22 18.16 ?  26  GLU   A CD   1 
ATOM   688  O  OE1  A GLU   A 1 26  ? 14.424 -3.551  14.802  0.78 25.32 ?  26  GLU   A OE1  1 
ATOM   689  O  OE1  B GLU   A 1 26  ? 14.624 -3.823  14.866  0.22 18.26 ?  26  GLU   A OE1  1 
ATOM   690  O  OE2  A GLU   A 1 26  ? 12.882 -2.015  15.106  0.78 26.13 -1 26  GLU   A OE2  1 
ATOM   691  O  OE2  B GLU   A 1 26  ? 13.262 -2.131  15.165  0.22 17.75 -1 26  GLU   A OE2  1 
ATOM   692  H  H    A GLU   A 1 26  ? 15.555 1.176   13.218  0.78 21.63 ?  26  GLU   A H    1 
ATOM   693  H  H    B GLU   A 1 26  ? 15.549 0.924   13.104  0.22 20.92 ?  26  GLU   A H    1 
ATOM   694  H  HA   A GLU   A 1 26  ? 15.439 -0.362  15.322  0.78 21.04 ?  26  GLU   A HA   1 
ATOM   695  H  HA   B GLU   A 1 26  ? 15.507 -0.685  15.151  0.22 20.48 ?  26  GLU   A HA   1 
ATOM   696  H  HB2  A GLU   A 1 26  ? 16.110 -0.856  12.650  0.78 23.25 ?  26  GLU   A HB2  1 
ATOM   697  H  HB2  B GLU   A 1 26  ? 16.129 -1.047  12.450  0.22 21.24 ?  26  GLU   A HB2  1 
ATOM   698  H  HB3  A GLU   A 1 26  ? 16.347 -2.004  13.716  0.78 23.25 ?  26  GLU   A HB3  1 
ATOM   699  H  HB3  B GLU   A 1 26  ? 16.578 -2.199  13.445  0.22 21.24 ?  26  GLU   A HB3  1 
ATOM   700  H  HG2  A GLU   A 1 26  ? 13.820 -0.892  13.258  0.78 27.37 ?  26  GLU   A HG2  1 
ATOM   701  H  HG2  B GLU   A 1 26  ? 13.933 -1.411  12.940  0.22 21.81 ?  26  GLU   A HG2  1 
ATOM   702  H  HG3  A GLU   A 1 26  ? 14.321 -2.208  12.521  0.78 27.37 ?  26  GLU   A HG3  1 
ATOM   703  H  HG3  B GLU   A 1 26  ? 14.581 -2.811  12.558  0.22 21.81 ?  26  GLU   A HG3  1 
ATOM   704  N  N    . ALA   A 1 27  ? 18.427 0.242   14.305  1.00 15.50 ?  27  ALA   A N    1 
ATOM   705  C  CA   . ALA   A 1 27  ? 19.821 0.215   14.732  1.00 15.85 ?  27  ALA   A CA   1 
ATOM   706  C  C    . ALA   A 1 27  ? 20.011 0.996   16.026  1.00 17.95 ?  27  ALA   A C    1 
ATOM   707  O  O    . ALA   A 1 27  ? 20.693 0.531   16.948  1.00 17.83 ?  27  ALA   A O    1 
ATOM   708  C  CB   . ALA   A 1 27  ? 20.721 0.757   13.621  1.00 15.37 ?  27  ALA   A CB   1 
ATOM   709  H  H    A ALA   A 1 27  ? 18.294 0.591   13.528  0.78 18.65 ?  27  ALA   A H    1 
ATOM   710  H  H    B ALA   A 1 27  ? 18.264 0.749   13.627  0.22 18.65 ?  27  ALA   A H    1 
ATOM   711  H  HA   . ALA   A 1 27  ? 20.076 -0.702  14.898  1.00 19.08 ?  27  ALA   A HA   1 
ATOM   712  H  HB1  . ALA   A 1 27  ? 21.645 0.729   13.922  1.00 18.50 ?  27  ALA   A HB1  1 
ATOM   713  H  HB2  . ALA   A 1 27  ? 20.619 0.200   12.831  1.00 18.50 ?  27  ALA   A HB2  1 
ATOM   714  H  HB3  . ALA   A 1 27  ? 20.467 1.668   13.417  1.00 18.50 ?  27  ALA   A HB3  1 
ATOM   715  N  N    A LYS   A 1 28  ? 19.400 2.178   16.122  0.78 19.49 ?  28  LYS   A N    1 
ATOM   716  N  N    B LYS   A 1 28  ? 19.405 2.183   16.123  0.22 20.50 ?  28  LYS   A N    1 
ATOM   717  C  CA   A LYS   A 1 28  ? 19.548 2.984   17.329  0.78 22.46 ?  28  LYS   A CA   1 
ATOM   718  C  CA   B LYS   A 1 28  ? 19.552 2.985   17.334  0.22 23.32 ?  28  LYS   A CA   1 
ATOM   719  C  C    A LYS   A 1 28  ? 18.986 2.273   18.552  0.78 23.51 ?  28  LYS   A C    1 
ATOM   720  C  C    B LYS   A 1 28  ? 18.986 2.273   18.556  0.22 24.05 ?  28  LYS   A C    1 
ATOM   721  O  O    A LYS   A 1 28  ? 19.502 2.448   19.662  0.78 25.27 ?  28  LYS   A O    1 
ATOM   722  O  O    B LYS   A 1 28  ? 19.489 2.459   19.670  0.22 24.87 ?  28  LYS   A O    1 
ATOM   723  C  CB   A LYS   A 1 28  ? 18.894 4.355   17.137  0.78 24.74 ?  28  LYS   A CB   1 
ATOM   724  C  CB   B LYS   A 1 28  ? 18.890 4.353   17.151  0.22 25.29 ?  28  LYS   A CB   1 
ATOM   725  C  CG   A LYS   A 1 28  ? 19.693 5.272   16.220  0.78 27.05 ?  28  LYS   A CG   1 
ATOM   726  C  CG   B LYS   A 1 28  ? 19.651 5.277   16.213  0.22 26.98 ?  28  LYS   A CG   1 
ATOM   727  C  CD   A LYS   A 1 28  ? 19.222 6.713   16.288  0.78 29.86 ?  28  LYS   A CD   1 
ATOM   728  C  CD   B LYS   A 1 28  ? 19.192 6.723   16.335  0.22 28.62 ?  28  LYS   A CD   1 
ATOM   729  C  CE   A LYS   A 1 28  ? 17.928 6.911   15.527  0.78 31.87 ?  28  LYS   A CE   1 
ATOM   730  C  CE   B LYS   A 1 28  ? 17.835 6.942   15.691  0.22 29.69 ?  28  LYS   A CE   1 
ATOM   731  N  NZ   A LYS   A 1 28  ? 17.526 8.344   15.502  0.78 33.12 ?  28  LYS   A NZ   1 
ATOM   732  N  NZ   B LYS   A 1 28  ? 17.462 8.385   15.678  0.22 30.36 ?  28  LYS   A NZ   1 
ATOM   733  H  H    A LYS   A 1 28  ? 18.905 2.526   15.515  0.78 23.45 ?  28  LYS   A H    1 
ATOM   734  H  H    B LYS   A 1 28  ? 18.915 2.538   15.514  0.22 24.65 ?  28  LYS   A H    1 
ATOM   735  H  HA   A LYS   A 1 28  ? 20.489 3.132   17.492  0.78 27.01 ?  28  LYS   A HA   1 
ATOM   736  H  HA   B LYS   A 1 28  ? 20.495 3.133   17.496  0.22 28.04 ?  28  LYS   A HA   1 
ATOM   737  H  HB2  A LYS   A 1 28  ? 18.015 4.237   16.745  0.78 29.74 ?  28  LYS   A HB2  1 
ATOM   738  H  HB2  B LYS   A 1 28  ? 18.001 4.226   16.785  0.22 30.41 ?  28  LYS   A HB2  1 
ATOM   739  H  HB3  A LYS   A 1 28  ? 18.816 4.794   17.999  0.78 29.74 ?  28  LYS   A HB3  1 
ATOM   740  H  HB3  B LYS   A 1 28  ? 18.830 4.791   18.015  0.22 30.41 ?  28  LYS   A HB3  1 
ATOM   741  H  HG2  A LYS   A 1 28  ? 20.626 5.249   16.482  0.78 32.51 ?  28  LYS   A HG2  1 
ATOM   742  H  HG2  B LYS   A 1 28  ? 20.595 5.242   16.428  0.22 32.43 ?  28  LYS   A HG2  1 
ATOM   743  H  HG3  A LYS   A 1 28  ? 19.595 4.968   15.304  0.78 32.51 ?  28  LYS   A HG3  1 
ATOM   744  H  HG3  B LYS   A 1 28  ? 19.505 4.992   15.298  0.22 32.43 ?  28  LYS   A HG3  1 
ATOM   745  H  HD2  A LYS   A 1 28  ? 19.070 6.959   17.214  0.78 35.89 ?  28  LYS   A HD2  1 
ATOM   746  H  HD2  B LYS   A 1 28  ? 19.123 6.959   17.273  0.22 34.40 ?  28  LYS   A HD2  1 
ATOM   747  H  HD3  A LYS   A 1 28  ? 19.897 7.289   15.895  0.78 35.89 ?  28  LYS   A HD3  1 
ATOM   748  H  HD3  B LYS   A 1 28  ? 19.834 7.299   15.892  0.22 34.40 ?  28  LYS   A HD3  1 
ATOM   749  H  HE2  A LYS   A 1 28  ? 18.047 6.612   14.612  0.78 38.29 ?  28  LYS   A HE2  1 
ATOM   750  H  HE2  B LYS   A 1 28  ? 17.862 6.627   14.774  0.22 35.68 ?  28  LYS   A HE2  1 
ATOM   751  H  HE3  A LYS   A 1 28  ? 17.223 6.404   15.958  0.78 38.29 ?  28  LYS   A HE3  1 
ATOM   752  H  HE3  B LYS   A 1 28  ? 17.160 6.458   16.192  0.22 35.68 ?  28  LYS   A HE3  1 
ATOM   753  H  HZ1  A LYS   A 1 28  ? 16.766 8.438   15.051  0.78 39.80 ?  28  LYS   A HZ1  1 
ATOM   754  H  HZ1  B LYS   A 1 28  ? 16.666 8.490   15.296  0.22 36.49 ?  28  LYS   A HZ1  1 
ATOM   755  H  HZ2  A LYS   A 1 28  ? 17.410 8.641   16.333  0.78 39.80 ?  28  LYS   A HZ2  1 
ATOM   756  H  HZ2  B LYS   A 1 28  ? 17.428 8.697   16.511  0.22 36.49 ?  28  LYS   A HZ2  1 
ATOM   757  H  HZ3  A LYS   A 1 28  ? 18.159 8.830   15.107  0.78 39.80 ?  28  LYS   A HZ3  1 
ATOM   758  H  HZ3  B LYS   A 1 28  ? 18.067 8.851   15.219  0.22 36.49 ?  28  LYS   A HZ3  1 
ATOM   759  N  N    . LYS   A 1 29  ? 17.950 1.454   18.371  1.00 23.97 ?  29  LYS   A N    1 
ATOM   760  C  CA   . LYS   A 1 29  ? 17.349 0.741   19.494  1.00 26.23 ?  29  LYS   A CA   1 
ATOM   761  C  C    . LYS   A 1 29  ? 18.172 -0.485  19.883  1.00 24.82 ?  29  LYS   A C    1 
ATOM   762  O  O    . LYS   A 1 29  ? 18.457 -0.704  21.067  1.00 25.49 ?  29  LYS   A O    1 
ATOM   763  C  CB   . LYS   A 1 29  ? 15.921 0.325   19.127  1.00 30.22 ?  29  LYS   A CB   1 
ATOM   764  C  CG   . LYS   A 1 29  ? 15.134 -0.311  20.262  1.00 34.68 ?  29  LYS   A CG   1 
ATOM   765  C  CD   . LYS   A 1 29  ? 14.766 0.719   21.316  1.00 39.02 ?  29  LYS   A CD   1 
ATOM   766  C  CE   . LYS   A 1 29  ? 13.866 0.122   22.386  1.00 41.83 ?  29  LYS   A CE   1 
ATOM   767  N  NZ   . LYS   A 1 29  ? 13.456 1.139   23.392  1.00 43.61 ?  29  LYS   A NZ   1 
ATOM   768  H  H    A LYS   A 1 29  ? 17.582 1.293   17.611  0.78 28.81 ?  29  LYS   A H    1 
ATOM   769  H  H    B LYS   A 1 29  ? 17.577 1.300   17.612  0.22 28.81 ?  29  LYS   A H    1 
ATOM   770  H  HA   . LYS   A 1 29  ? 17.304 1.330   20.261  1.00 31.53 ?  29  LYS   A HA   1 
ATOM   771  H  HB2  . LYS   A 1 29  ? 15.431 1.113   18.839  1.00 36.31 ?  29  LYS   A HB2  1 
ATOM   772  H  HB3  . LYS   A 1 29  ? 15.958 -0.317  18.401  1.00 36.31 ?  29  LYS   A HB3  1 
ATOM   773  H  HG2  . LYS   A 1 29  ? 14.314 -0.693  19.910  1.00 41.67 ?  29  LYS   A HG2  1 
ATOM   774  H  HG3  . LYS   A 1 29  ? 15.670 -1.002  20.683  1.00 41.67 ?  29  LYS   A HG3  1 
ATOM   775  H  HD2  . LYS   A 1 29  ? 15.574 1.042   21.744  1.00 46.88 ?  29  LYS   A HD2  1 
ATOM   776  H  HD3  . LYS   A 1 29  ? 14.292 1.453   20.894  1.00 46.88 ?  29  LYS   A HD3  1 
ATOM   777  H  HE2  . LYS   A 1 29  ? 13.065 -0.233  21.968  1.00 50.25 ?  29  LYS   A HE2  1 
ATOM   778  H  HE3  . LYS   A 1 29  ? 14.344 -0.586  22.846  1.00 50.25 ?  29  LYS   A HE3  1 
ATOM   779  H  HZ1  . LYS   A 1 29  ? 12.931 0.765   24.006  1.00 52.38 ?  29  LYS   A HZ1  1 
ATOM   780  H  HZ2  . LYS   A 1 29  ? 14.175 1.477   23.793  1.00 52.38 ?  29  LYS   A HZ2  1 
ATOM   781  H  HZ3  . LYS   A 1 29  ? 13.011 1.799   22.994  1.00 52.38 ?  29  LYS   A HZ3  1 
ATOM   782  N  N    . VAL   A 1 30  ? 18.549 -1.299  18.898  1.00 23.21 ?  30  VAL   A N    1 
ATOM   783  C  CA   . VAL   A 1 30  ? 19.195 -2.578  19.172  1.00 22.40 ?  30  VAL   A CA   1 
ATOM   784  C  C    . VAL   A 1 30  ? 20.700 -2.424  19.392  1.00 21.18 ?  30  VAL   A C    1 
ATOM   785  O  O    . VAL   A 1 30  ? 21.290 -3.161  20.190  1.00 21.43 ?  30  VAL   A O    1 
ATOM   786  C  CB   . VAL   A 1 30  ? 18.883 -3.553  18.022  1.00 23.19 ?  30  VAL   A CB   1 
ATOM   787  C  CG1  . VAL   A 1 30  ? 19.653 -4.856  18.185  1.00 23.66 ?  30  VAL   A CG1  1 
ATOM   788  C  CG2  . VAL   A 1 30  ? 17.384 -3.822  17.941  1.00 24.07 ?  30  VAL   A CG2  1 
ATOM   789  H  H    . VAL   A 1 30  ? 18.429 -1.142  18.061  1.00 27.91 ?  30  VAL   A H    1 
ATOM   790  H  HA   . VAL   A 1 30  ? 18.811 -2.954  19.978  1.00 26.93 ?  30  VAL   A HA   1 
ATOM   791  H  HB   . VAL   A 1 30  ? 19.153 -3.154  17.182  1.00 27.88 ?  30  VAL   A HB   1 
ATOM   792  H  HG11 . VAL   A 1 30  ? 19.271 -5.524  17.593  1.00 28.45 ?  30  VAL   A HG11 1 
ATOM   793  H  HG12 . VAL   A 1 30  ? 20.581 -4.705  17.955  1.00 28.45 ?  30  VAL   A HG12 1 
ATOM   794  H  HG13 . VAL   A 1 30  ? 19.579 -5.152  19.105  1.00 28.45 ?  30  VAL   A HG13 1 
ATOM   795  H  HG21 . VAL   A 1 30  ? 17.215 -4.475  17.241  1.00 28.94 ?  30  VAL   A HG21 1 
ATOM   796  H  HG22 . VAL   A 1 30  ? 17.079 -4.170  18.795  1.00 28.94 ?  30  VAL   A HG22 1 
ATOM   797  H  HG23 . VAL   A 1 30  ? 16.924 -2.994  17.738  1.00 28.94 ?  30  VAL   A HG23 1 
ATOM   798  N  N    . LYS   A 1 31  ? 21.338 -1.478  18.711  1.00 20.30 ?  31  LYS   A N    1 
ATOM   799  C  CA   . LYS   A 1 31  ? 22.792 -1.378  18.661  1.00 21.27 ?  31  LYS   A CA   1 
ATOM   800  C  C    . LYS   A 1 31  ? 23.400 -2.731  18.284  1.00 19.12 ?  31  LYS   A C    1 
ATOM   801  O  O    . LYS   A 1 31  ? 24.191 -3.300  19.043  1.00 20.12 ?  31  LYS   A O    1 
ATOM   802  C  CB   . LYS   A 1 31  ? 23.377 -0.857  19.966  1.00 27.57 ?  31  LYS   A CB   1 
ATOM   803  C  CG   . LYS   A 1 31  ? 22.698 0.405   20.477  1.00 34.29 ?  31  LYS   A CG   1 
ATOM   804  C  CD   . LYS   A 1 31  ? 23.705 1.468   20.894  1.00 39.64 ?  31  LYS   A CD   1 
ATOM   805  C  CE   . LYS   A 1 31  ? 23.059 2.524   21.784  1.00 43.46 ?  31  LYS   A CE   1 
ATOM   806  N  NZ   . LYS   A 1 31  ? 21.898 3.201   21.139  1.00 45.11 ?  31  LYS   A NZ   1 
ATOM   807  H  H    . LYS   A 1 31  ? 20.936 -0.868  18.259  1.00 24.42 ?  31  LYS   A H    1 
ATOM   808  H  HA   . LYS   A 1 31  ? 23.025 -0.748  17.967  1.00 25.58 ?  31  LYS   A HA   1 
ATOM   809  H  HB2  . LYS   A 1 31  ? 23.290 -1.544  20.642  1.00 33.14 ?  31  LYS   A HB2  1 
ATOM   810  H  HB3  . LYS   A 1 31  ? 24.317 -0.655  19.820  1.00 33.14 ?  31  LYS   A HB3  1 
ATOM   811  H  HG2  . LYS   A 1 31  ? 22.142 0.775   19.773  1.00 41.21 ?  31  LYS   A HG2  1 
ATOM   812  H  HG3  . LYS   A 1 31  ? 22.156 0.181   21.249  1.00 41.21 ?  31  LYS   A HG3  1 
ATOM   813  H  HD2  . LYS   A 1 31  ? 24.427 1.051   21.390  1.00 47.62 ?  31  LYS   A HD2  1 
ATOM   814  H  HD3  . LYS   A 1 31  ? 24.054 1.908   20.102  1.00 47.62 ?  31  LYS   A HD3  1 
ATOM   815  H  HE2  . LYS   A 1 31  ? 22.742 2.099   22.597  1.00 52.20 ?  31  LYS   A HE2  1 
ATOM   816  H  HE3  . LYS   A 1 31  ? 23.718 3.202   22.000  1.00 52.20 ?  31  LYS   A HE3  1 
ATOM   817  H  HZ1  . LYS   A 1 31  ? 21.557 3.812   21.690  1.00 54.19 ?  31  LYS   A HZ1  1 
ATOM   818  H  HZ2  . LYS   A 1 31  ? 22.158 3.603   20.389  1.00 54.19 ?  31  LYS   A HZ2  1 
ATOM   819  H  HZ3  . LYS   A 1 31  ? 21.266 2.605   20.944  1.00 54.19 ?  31  LYS   A HZ3  1 
ATOM   820  N  N    . PRO   A 1 32  ? 23.046 -3.267  17.122  1.00 16.76 ?  32  PRO   A N    1 
ATOM   821  C  CA   . PRO   A 1 32  ? 23.526 -4.595  16.745  1.00 16.69 ?  32  PRO   A CA   1 
ATOM   822  C  C    . PRO   A 1 32  ? 25.027 -4.593  16.530  1.00 16.54 ?  32  PRO   A C    1 
ATOM   823  O  O    . PRO   A 1 32  ? 25.658 -3.554  16.312  1.00 16.58 ?  32  PRO   A O    1 
ATOM   824  C  CB   . PRO   A 1 32  ? 22.790 -4.868  15.429  1.00 17.11 ?  32  PRO   A CB   1 
ATOM   825  C  CG   . PRO   A 1 32  ? 22.600 -3.498  14.844  1.00 15.82 ?  32  PRO   A CG   1 
ATOM   826  C  CD   . PRO   A 1 32  ? 22.310 -2.619  16.025  1.00 16.07 ?  32  PRO   A CD   1 
ATOM   827  H  HA   . PRO   A 1 32  ? 23.287 -5.260  17.407  1.00 20.08 ?  32  PRO   A HA   1 
ATOM   828  H  HB2  . PRO   A 1 32  ? 23.334 -5.428  14.848  1.00 20.59 ?  32  PRO   A HB2  1 
ATOM   829  H  HB3  . PRO   A 1 32  ? 21.934 -5.295  15.610  1.00 20.59 ?  32  PRO   A HB3  1 
ATOM   830  H  HG2  . PRO   A 1 32  ? 23.410 -3.228  14.389  1.00 19.04 ?  32  PRO   A HG2  1 
ATOM   831  H  HG3  . PRO   A 1 32  ? 21.848 -3.516  14.225  1.00 19.04 ?  32  PRO   A HG3  1 
ATOM   832  H  HD2  . PRO   A 1 32  ? 22.653 -1.728  15.855  1.00 19.35 ?  32  PRO   A HD2  1 
ATOM   833  H  HD3  . PRO   A 1 32  ? 21.361 -2.612  16.207  1.00 19.35 ?  32  PRO   A HD3  1 
ATOM   834  N  N    . THR   A 1 33  ? 25.597 -5.795  16.580  1.00 16.67 ?  33  THR   A N    1 
ATOM   835  C  CA   . THR   A 1 33  ? 27.006 -5.945  16.248  1.00 17.03 ?  33  THR   A CA   1 
ATOM   836  C  C    . THR   A 1 33  ? 27.284 -5.481  14.826  1.00 15.27 ?  33  THR   A C    1 
ATOM   837  O  O    . THR   A 1 33  ? 28.312 -4.836  14.568  1.00 15.44 ?  33  THR   A O    1 
ATOM   838  C  CB   . THR   A 1 33  ? 27.421 -7.402  16.442  1.00 18.73 ?  33  THR   A CB   1 
ATOM   839  O  OG1  . THR   A 1 33  ? 27.107 -7.802  17.780  1.00 20.64 ?  33  THR   A OG1  1 
ATOM   840  C  CG2  . THR   A 1 33  ? 28.912 -7.582  16.198  1.00 19.32 ?  33  THR   A CG2  1 
ATOM   841  H  H    . THR   A 1 33  ? 25.198 -6.525  16.792  1.00 20.06 ?  33  THR   A H    1 
ATOM   842  H  HA   . THR   A 1 33  ? 27.538 -5.403  16.851  1.00 20.49 ?  33  THR   A HA   1 
ATOM   843  H  HB   . THR   A 1 33  ? 26.939 -7.971  15.819  1.00 22.53 ?  33  THR   A HB   1 
ATOM   844  H  HG1  . THR   A 1 33  ? 27.527 -7.325  18.333  1.00 24.82 ?  33  THR   A HG1  1 
ATOM   845  H  HG21 . THR   A 1 33  ? 29.190 -8.471  16.476  1.00 23.24 ?  33  THR   A HG21 1 
ATOM   846  H  HG22 . THR   A 1 33  ? 29.111 -7.472  15.257  1.00 23.24 ?  33  THR   A HG22 1 
ATOM   847  H  HG23 . THR   A 1 33  ? 29.411 -6.926  16.709  1.00 23.24 ?  33  THR   A HG23 1 
ATOM   848  N  N    . VAL   A 1 34  ? 26.381 -5.794  13.895  1.00 13.84 ?  34  VAL   A N    1 
ATOM   849  C  CA   . VAL   A 1 34  ? 26.557 -5.461  12.485  1.00 12.64 ?  34  VAL   A CA   1 
ATOM   850  C  C    . VAL   A 1 34  ? 25.250 -4.902  11.932  1.00 11.76 ?  34  VAL   A C    1 
ATOM   851  O  O    . VAL   A 1 34  ? 24.214 -5.577  11.980  1.00 12.68 ?  34  VAL   A O    1 
ATOM   852  C  CB   . VAL   A 1 34  ? 26.997 -6.673  11.641  1.00 13.27 ?  34  VAL   A CB   1 
ATOM   853  C  CG1  . VAL   A 1 34  ? 27.170 -6.267  10.184  1.00 13.45 ?  34  VAL   A CG1  1 
ATOM   854  C  CG2  . VAL   A 1 34  ? 28.283 -7.291  12.193  1.00 14.43 ?  34  VAL   A CG2  1 
ATOM   855  H  H    . VAL   A 1 34  ? 25.645 -6.211  14.058  1.00 16.67 ?  34  VAL   A H    1 
ATOM   856  H  HA   . VAL   A 1 34  ? 27.236 -4.772  12.400  1.00 15.22 ?  34  VAL   A HA   1 
ATOM   857  H  HB   . VAL   A 1 34  ? 26.302 -7.348  11.680  1.00 15.98 ?  34  VAL   A HB   1 
ATOM   858  H  HG11 . VAL   A 1 34  ? 27.657 -6.967  9.722   1.00 16.19 ?  34  VAL   A HG11 1 
ATOM   859  H  HG12 . VAL   A 1 34  ? 26.299 -6.148  9.781   1.00 16.19 ?  34  VAL   A HG12 1 
ATOM   860  H  HG13 . VAL   A 1 34  ? 27.673 -5.437  10.147  1.00 16.19 ?  34  VAL   A HG13 1 
ATOM   861  H  HG21 . VAL   A 1 34  ? 28.552 -8.028  11.620  1.00 17.38 ?  34  VAL   A HG21 1 
ATOM   862  H  HG22 . VAL   A 1 34  ? 28.980 -6.616  12.209  1.00 17.38 ?  34  VAL   A HG22 1 
ATOM   863  H  HG23 . VAL   A 1 34  ? 28.119 -7.618  13.093  1.00 17.38 ?  34  VAL   A HG23 1 
ATOM   864  N  N    . VAL   A 1 35  ? 25.303 -3.684  11.388  1.00 11.14 ?  35  VAL   A N    1 
ATOM   865  C  CA   . VAL   A 1 35  ? 24.264 -3.170  10.504  1.00 10.68 ?  35  VAL   A CA   1 
ATOM   866  C  C    . VAL   A 1 35  ? 24.814 -3.175  9.087   1.00 10.01 ?  35  VAL   A C    1 
ATOM   867  O  O    . VAL   A 1 35  ? 25.958 -2.761  8.852   1.00 10.72 ?  35  VAL   A O    1 
ATOM   868  C  CB   . VAL   A 1 35  ? 23.732 -1.777  10.908  1.00 11.37 ?  35  VAL   A CB   1 
ATOM   869  C  CG1  . VAL   A 1 35  ? 24.809 -0.677  10.790  1.00 11.81 ?  35  VAL   A CG1  1 
ATOM   870  C  CG2  . VAL   A 1 35  ? 22.497 -1.430  10.069  1.00 12.08 ?  35  VAL   A CG2  1 
ATOM   871  H  H    . VAL   A 1 35  ? 25.944 -3.125  11.516  1.00 13.43 ?  35  VAL   A H    1 
ATOM   872  H  HA   . VAL   A 1 35  ? 23.510 -3.783  10.523  1.00 12.87 ?  35  VAL   A HA   1 
ATOM   873  H  HB   . VAL   A 1 35  ? 23.441 -1.809  11.829  1.00 13.69 ?  35  VAL   A HB   1 
ATOM   874  H  HG11 . VAL   A 1 35  ? 24.453 0.157   11.144  1.00 14.22 ?  35  VAL   A HG11 1 
ATOM   875  H  HG12 . VAL   A 1 35  ? 25.586 -0.944  11.304  1.00 14.22 ?  35  VAL   A HG12 1 
ATOM   876  H  HG13 . VAL   A 1 35  ? 25.051 -0.559  9.859   1.00 14.22 ?  35  VAL   A HG13 1 
ATOM   877  H  HG21 . VAL   A 1 35  ? 22.124 -0.591  10.375  1.00 14.55 ?  35  VAL   A HG21 1 
ATOM   878  H  HG22 . VAL   A 1 35  ? 22.761 -1.347  9.132   1.00 14.55 ?  35  VAL   A HG22 1 
ATOM   879  H  HG23 . VAL   A 1 35  ? 21.840 -2.138  10.157  1.00 14.55 ?  35  VAL   A HG23 1 
ATOM   880  N  N    . VAL   A 1 36  ? 23.994 -3.630  8.141   1.00 9.92  ?  36  VAL   A N    1 
ATOM   881  C  CA   . VAL   A 1 36  ? 24.364 -3.642  6.733   1.00 9.54  ?  36  VAL   A CA   1 
ATOM   882  C  C    . VAL   A 1 36  ? 23.900 -2.349  6.076   1.00 9.67  ?  36  VAL   A C    1 
ATOM   883  O  O    . VAL   A 1 36  ? 22.740 -1.942  6.226   1.00 10.26 ?  36  VAL   A O    1 
ATOM   884  C  CB   . VAL   A 1 36  ? 23.757 -4.855  6.015   1.00 9.76  ?  36  VAL   A CB   1 
ATOM   885  C  CG1  . VAL   A 1 36  ? 24.018 -4.773  4.530   1.00 10.22 ?  36  VAL   A CG1  1 
ATOM   886  C  CG2  . VAL   A 1 36  ? 24.313 -6.148  6.589   1.00 10.67 ?  36  VAL   A CG2  1 
ATOM   887  H  H    . VAL   A 1 36  ? 23.199 -3.944  8.288   1.00 11.96 ?  36  VAL   A H    1 
ATOM   888  H  HA   . VAL   A 1 36  ? 25.330 -3.699  6.656   1.00 11.50 ?  36  VAL   A HA   1 
ATOM   889  H  HB   . VAL   A 1 36  ? 22.796 -4.851  6.148   1.00 11.77 ?  36  VAL   A HB   1 
ATOM   890  H  HG11 . VAL   A 1 36  ? 23.890 -5.651  4.138   1.00 12.32 ?  36  VAL   A HG11 1 
ATOM   891  H  HG12 . VAL   A 1 36  ? 23.402 -4.140  4.128   1.00 12.32 ?  36  VAL   A HG12 1 
ATOM   892  H  HG13 . VAL   A 1 36  ? 24.934 -4.481  4.386   1.00 12.32 ?  36  VAL   A HG13 1 
ATOM   893  H  HG21 . VAL   A 1 36  ? 23.924 -6.902  6.113   1.00 12.86 ?  36  VAL   A HG21 1 
ATOM   894  H  HG22 . VAL   A 1 36  ? 25.278 -6.158  6.481   1.00 12.86 ?  36  VAL   A HG22 1 
ATOM   895  H  HG23 . VAL   A 1 36  ? 24.086 -6.205  7.530   1.00 12.86 ?  36  VAL   A HG23 1 
ATOM   896  N  N    . ASN   A 1 37  ? 24.811 -1.718  5.332   1.00 9.17  ?  37  ASN   A N    1 
ATOM   897  C  CA   . ASN   A 1 37  ? 24.478 -0.602  4.464   1.00 9.04  ?  37  ASN   A CA   1 
ATOM   898  C  C    . ASN   A 1 37  ? 24.328 -1.072  3.027   1.00 9.00  ?  37  ASN   A C    1 
ATOM   899  O  O    . ASN   A 1 37  ? 25.111 -1.896  2.539   1.00 9.80  ?  37  ASN   A O    1 
ATOM   900  C  CB   . ASN   A 1 37  ? 25.555 0.476   4.536   1.00 9.31  ?  37  ASN   A CB   1 
ATOM   901  C  CG   . ASN   A 1 37  ? 25.222 1.684   3.686   1.00 9.45  ?  37  ASN   A CG   1 
ATOM   902  O  OD1  . ASN   A 1 37  ? 24.047 2.018   3.507   1.00 10.14 ?  37  ASN   A OD1  1 
ATOM   903  N  ND2  . ASN   A 1 37  ? 26.252 2.342   3.163   1.00 9.73  ?  37  ASN   A ND2  1 
ATOM   904  H  H    . ASN   A 1 37  ? 25.650 -1.920  5.325   1.00 11.06 ?  37  ASN   A H    1 
ATOM   905  H  HA   . ASN   A 1 37  ? 23.640 -0.210  4.755   1.00 10.90 ?  37  ASN   A HA   1 
ATOM   906  H  HB2  . ASN   A 1 37  ? 25.649 0.777   5.456   1.00 11.23 ?  37  ASN   A HB2  1 
ATOM   907  H  HB3  . ASN   A 1 37  ? 26.400 0.106   4.224   1.00 11.23 ?  37  ASN   A HB3  1 
ATOM   908  H  HD21 . ASN   A 1 37  ? 26.113 3.034   2.674   1.00 11.73 ?  37  ASN   A HD21 1 
ATOM   909  H  HD22 . ASN   A 1 37  ? 27.053 2.085   3.318   1.00 11.73 ?  37  ASN   A HD22 1 
ATOM   910  N  N    A ALA   A 1 38  ? 23.317 -0.522  2.351   0.78 9.52  ?  38  ALA   A N    1 
ATOM   911  N  N    B ALA   A 1 38  ? 23.300 -0.550  2.356   0.22 9.36  ?  38  ALA   A N    1 
ATOM   912  C  CA   A ALA   A 1 38  ? 23.115 -0.676  0.912   0.78 9.93  ?  38  ALA   A CA   1 
ATOM   913  C  CA   B ALA   A 1 38  ? 23.095 -0.768  0.925   0.22 9.79  ?  38  ALA   A CA   1 
ATOM   914  C  C    A ALA   A 1 38  ? 24.007 0.336   0.190   0.78 9.48  ?  38  ALA   A C    1 
ATOM   915  C  C    B ALA   A 1 38  ? 23.990 0.215   0.175   0.22 9.79  ?  38  ALA   A C    1 
ATOM   916  O  O    A ALA   A 1 38  ? 23.581 1.426   -0.202  0.78 9.62  ?  38  ALA   A O    1 
ATOM   917  O  O    B ALA   A 1 38  ? 23.556 1.254   -0.330  0.22 9.92  ?  38  ALA   A O    1 
ATOM   918  C  CB   A ALA   A 1 38  ? 21.643 -0.471  0.569   0.78 11.28 ?  38  ALA   A CB   1 
ATOM   919  C  CB   B ALA   A 1 38  ? 21.626 -0.587  0.566   0.22 10.39 ?  38  ALA   A CB   1 
ATOM   920  H  H    A ALA   A 1 38  ? 22.722 -0.024  2.724   0.78 11.47 ?  38  ALA   A H    1 
ATOM   921  H  H    B ALA   A 1 38  ? 22.694 -0.053  2.718   0.22 11.28 ?  38  ALA   A H    1 
ATOM   922  H  HA   A ALA   A 1 38  ? 23.377 -1.567  0.641   0.78 11.98 ?  38  ALA   A HA   1 
ATOM   923  H  HA   B ALA   A 1 38  ? 23.361 -1.672  0.693   0.22 11.80 ?  38  ALA   A HA   1 
ATOM   924  H  HB1  A ALA   A 1 38  ? 21.526 -0.564  -0.387  0.78 13.59 ?  38  ALA   A HB1  1 
ATOM   925  H  HB1  B ALA   A 1 38  ? 21.522 -0.693  -0.391  0.22 12.52 ?  38  ALA   A HB1  1 
ATOM   926  H  HB2  A ALA   A 1 38  ? 21.116 -1.144  1.034   0.78 13.59 ?  38  ALA   A HB2  1 
ATOM   927  H  HB2  B ALA   A 1 38  ? 21.100 -1.255  1.035   0.22 12.52 ?  38  ALA   A HB2  1 
ATOM   928  H  HB3  A ALA   A 1 38  ? 21.371 0.414   0.854   0.78 13.59 ?  38  ALA   A HB3  1 
ATOM   929  H  HB3  B ALA   A 1 38  ? 21.346 0.302   0.832   0.22 12.52 ?  38  ALA   A HB3  1 
ATOM   930  N  N    A ALA   A 1 39  ? 25.275 -0.035  0.026   0.78 9.41  ?  39  ALA   A N    1 
ATOM   931  N  N    B ALA   A 1 39  ? 25.269 -0.135  0.101   0.22 10.04 ?  39  ALA   A N    1 
ATOM   932  C  CA   A ALA   A 1 39  ? 26.315 0.852   -0.469  0.78 9.47  ?  39  ALA   A CA   1 
ATOM   933  C  CA   B ALA   A 1 39  ? 26.305 0.764   -0.376  0.22 9.94  ?  39  ALA   A CA   1 
ATOM   934  C  C    A ALA   A 1 39  ? 26.439 0.795   -1.987  0.78 9.55  ?  39  ALA   A C    1 
ATOM   935  C  C    B ALA   A 1 39  ? 26.444 0.691   -1.892  0.22 9.79  ?  39  ALA   A C    1 
ATOM   936  O  O    A ALA   A 1 39  ? 25.948 -0.123  -2.647  0.78 10.20 ?  39  ALA   A O    1 
ATOM   937  O  O    B ALA   A 1 39  ? 25.981 -0.249  -2.541  0.22 9.59  ?  39  ALA   A O    1 
ATOM   938  C  CB   A ALA   A 1 39  ? 27.652 0.462   0.165   0.78 10.41 ?  39  ALA   A CB   1 
ATOM   939  C  CB   B ALA   A 1 39  ? 27.640 0.402   0.273   0.22 10.20 ?  39  ALA   A CB   1 
ATOM   940  H  H    A ALA   A 1 39  ? 25.561 -0.830  0.205   0.78 11.35 ?  39  ALA   A H    1 
ATOM   941  H  H    B ALA   A 1 39  ? 25.562 -0.914  0.318   0.22 12.11 ?  39  ALA   A H    1 
ATOM   942  H  HA   A ALA   A 1 39  ? 26.099 1.764   -0.212  0.78 11.42 ?  39  ALA   A HA   1 
ATOM   943  H  HA   B ALA   A 1 39  ? 26.079 1.673   -0.131  0.22 11.98 ?  39  ALA   A HA   1 
ATOM   944  H  HB1  A ALA   A 1 39  ? 28.337 1.061   -0.165  0.78 12.55 ?  39  ALA   A HB1  1 
ATOM   945  H  HB1  B ALA   A 1 39  ? 28.321 1.010   -0.052  0.22 12.29 ?  39  ALA   A HB1  1 
ATOM   946  H  HB2  A ALA   A 1 39  ? 27.575 0.546   1.131   0.78 12.55 ?  39  ALA   A HB2  1 
ATOM   947  H  HB2  B ALA   A 1 39  ? 27.551 0.487   1.235   0.22 12.29 ?  39  ALA   A HB2  1 
ATOM   948  H  HB3  A ALA   A 1 39  ? 27.857 -0.451  -0.073  0.78 12.55 ?  39  ALA   A HB3  1 
ATOM   949  H  HB3  B ALA   A 1 39  ? 27.867 -0.510  0.039   0.22 12.29 ?  39  ALA   A HB3  1 
ATOM   950  N  N    A ASN   A 1 40  ? 27.127 1.798   -2.536  0.78 9.83  ?  40  ASN   A N    1 
ATOM   951  N  N    B ASN   A 1 40  ? 27.102 1.705   -2.450  0.22 10.23 ?  40  ASN   A N    1 
ATOM   952  C  CA   A ASN   A 1 40  ? 27.676 1.742   -3.883  0.78 9.94  ?  40  ASN   A CA   1 
ATOM   953  C  CA   B ASN   A 1 40  ? 27.519 1.715   -3.845  0.22 10.46 ?  40  ASN   A CA   1 
ATOM   954  C  C    A ASN   A 1 40  ? 29.202 1.632   -3.807  0.78 9.60  ?  40  ASN   A C    1 
ATOM   955  C  C    B ASN   A 1 40  ? 29.038 1.601   -3.917  0.22 10.42 ?  40  ASN   A C    1 
ATOM   956  O  O    A ASN   A 1 40  ? 29.797 1.736   -2.732  0.78 9.65  ?  40  ASN   A O    1 
ATOM   957  O  O    B ASN   A 1 40  ? 29.738 1.672   -2.903  0.22 10.32 ?  40  ASN   A O    1 
ATOM   958  C  CB   A ASN   A 1 40  ? 27.199 2.924   -4.744  0.78 10.66 ?  40  ASN   A CB   1 
ATOM   959  C  CB   B ASN   A 1 40  ? 27.024 2.977   -4.562  0.22 11.13 ?  40  ASN   A CB   1 
ATOM   960  C  CG   A ASN   A 1 40  ? 27.572 4.275   -4.163  0.78 10.87 ?  40  ASN   A CG   1 
ATOM   961  C  CG   B ASN   A 1 40  ? 27.145 4.221   -3.708  0.22 11.94 ?  40  ASN   A CG   1 
ATOM   962  O  OD1  A ASN   A 1 40  ? 28.733 4.535   -3.853  0.78 11.23 ?  40  ASN   A OD1  1 
ATOM   963  O  OD1  B ASN   A 1 40  ? 28.102 4.381   -2.951  0.22 12.46 ?  40  ASN   A OD1  1 
ATOM   964  N  ND2  A ASN   A 1 40  ? 26.577 5.148   -4.015  0.78 12.30 ?  40  ASN   A ND2  1 
ATOM   965  N  ND2  B ASN   A 1 40  ? 26.163 5.105   -3.817  0.22 12.17 ?  40  ASN   A ND2  1 
ATOM   966  H  H    A ASN   A 1 40  ? 27.304 2.527   -2.128  0.78 11.85 ?  40  ASN   A H    1 
ATOM   967  H  H    B ASN   A 1 40  ? 27.335 2.415   -2.021  0.22 12.34 ?  40  ASN   A H    1 
ATOM   968  H  HA   A ASN   A 1 40  ? 27.360 0.931   -4.310  0.78 11.98 ?  40  ASN   A HA   1 
ATOM   969  H  HA   B ASN   A 1 40  ? 27.130 0.947   -4.297  0.22 12.61 ?  40  ASN   A HA   1 
ATOM   970  H  HB2  A ASN   A 1 40  ? 27.602 2.854   -5.624  0.78 12.85 ?  40  ASN   A HB2  1 
ATOM   971  H  HB2  B ASN   A 1 40  ? 27.555 3.115   -5.361  0.22 13.41 ?  40  ASN   A HB2  1 
ATOM   972  H  HB3  A ASN   A 1 40  ? 26.234 2.884   -4.819  0.78 12.85 ?  40  ASN   A HB3  1 
ATOM   973  H  HB3  B ASN   A 1 40  ? 26.093 2.856   -4.802  0.22 13.41 ?  40  ASN   A HB3  1 
ATOM   974  H  HD21 A ASN   A 1 40  ? 26.734 5.933   -3.695  0.78 14.81 ?  40  ASN   A HD21 1 
ATOM   975  H  HD21 B ASN   A 1 40  ? 26.179 5.826   -3.351  0.22 14.66 ?  40  ASN   A HD21 1 
ATOM   976  H  HD22 A ASN   A 1 40  ? 25.776 4.936   -4.250  0.78 14.81 ?  40  ASN   A HD22 1 
ATOM   977  H  HD22 B ASN   A 1 40  ? 25.510 4.959   -4.360  0.22 14.66 ?  40  ASN   A HD22 1 
ATOM   978  N  N    A VAL   A 1 41  ? 29.832 1.373   -4.956  0.78 9.72  ?  41  VAL   A N    1 
ATOM   979  N  N    B VAL   A 1 41  ? 29.552 1.416   -5.135  0.22 10.59 ?  41  VAL   A N    1 
ATOM   980  C  CA   A VAL   A 1 41  ? 31.260 1.060   -4.974  0.78 10.29 ?  41  VAL   A CA   1 
ATOM   981  C  CA   B VAL   A 1 41  ? 30.975 1.106   -5.285  0.22 10.55 ?  41  VAL   A CA   1 
ATOM   982  C  C    A VAL   A 1 41  ? 32.116 2.219   -4.505  0.78 10.34 ?  41  VAL   A C    1 
ATOM   983  C  C    B VAL   A 1 41  ? 31.861 2.239   -4.781  0.22 10.54 ?  41  VAL   A C    1 
ATOM   984  O  O    A VAL   A 1 41  ? 33.260 2.001   -4.089  0.78 10.94 ?  41  VAL   A O    1 
ATOM   985  O  O    B VAL   A 1 41  ? 33.011 2.003   -4.387  0.22 10.26 ?  41  VAL   A O    1 
ATOM   986  C  CB   A VAL   A 1 41  ? 31.750 0.565   -6.356  0.78 10.79 ?  41  VAL   A CB   1 
ATOM   987  C  CB   B VAL   A 1 41  ? 31.324 0.711   -6.734  0.22 10.59 ?  41  VAL   A CB   1 
ATOM   988  C  CG1  A VAL   A 1 41  ? 31.062 -0.738  -6.730  0.78 11.81 ?  41  VAL   A CG1  1 
ATOM   989  C  CG1  B VAL   A 1 41  ? 30.692 -0.624  -7.088  0.22 10.79 ?  41  VAL   A CG1  1 
ATOM   990  C  CG2  A VAL   A 1 41  ? 31.567 1.628   -7.441  0.78 11.16 ?  41  VAL   A CG2  1 
ATOM   991  C  CG2  B VAL   A 1 41  ? 30.902 1.801   -7.707  0.22 11.00 ?  41  VAL   A CG2  1 
ATOM   992  H  H    A VAL   A 1 41  ? 29.461 1.360   -5.727  0.78 11.72 ?  41  VAL   A H    1 
ATOM   993  H  H    B VAL   A 1 41  ? 29.105 1.452   -5.872  0.22 12.76 ?  41  VAL   A H    1 
ATOM   994  H  HA   A VAL   A 1 41  ? 31.421 0.337   -4.348  0.78 12.41 ?  41  VAL   A HA   1 
ATOM   995  H  HA   B VAL   A 1 41  ? 31.162 0.333   -4.731  0.22 12.71 ?  41  VAL   A HA   1 
ATOM   996  H  HB   A VAL   A 1 41  ? 32.703 0.375   -6.294  0.78 13.01 ?  41  VAL   A HB   1 
ATOM   997  H  HB   B VAL   A 1 41  ? 32.286 0.608   -6.801  0.22 12.76 ?  41  VAL   A HB   1 
ATOM   998  H  HG11 A VAL   A 1 41  ? 31.403 -1.047  -7.583  0.78 14.23 ?  41  VAL   A HG11 1 
ATOM   999  H  HG11 B VAL   A 1 41  ? 30.885 -0.828  -8.014  0.22 13.00 ?  41  VAL   A HG11 1 
ATOM   1000 H  HG12 A VAL   A 1 41  ? 31.241 -1.403  -6.043  0.78 14.23 ?  41  VAL   A HG12 1 
ATOM   1001 H  HG12 B VAL   A 1 41  ? 31.069 -1.312  -6.513  0.22 13.00 ?  41  VAL   A HG12 1 
ATOM   1002 H  HG13 A VAL   A 1 41  ? 30.105 -0.583  -6.793  0.78 14.23 ?  41  VAL   A HG13 1 
ATOM   1003 H  HG13 B VAL   A 1 41  ? 29.736 -0.570  -6.950  0.22 13.00 ?  41  VAL   A HG13 1 
ATOM   1004 H  HG21 A VAL   A 1 41  ? 31.817 1.245   -8.299  0.78 13.45 ?  41  VAL   A HG21 1 
ATOM   1005 H  HG21 B VAL   A 1 41  ? 31.198 1.557   -8.597  0.22 13.25 ?  41  VAL   A HG21 1 
ATOM   1006 H  HG22 A VAL   A 1 41  ? 30.641 1.902   -7.458  0.78 13.45 ?  41  VAL   A HG22 1 
ATOM   1007 H  HG22 B VAL   A 1 41  ? 29.936 1.886   -7.694  0.22 13.25 ?  41  VAL   A HG22 1 
ATOM   1008 H  HG23 A VAL   A 1 41  ? 32.138 2.385   -7.240  0.78 13.45 ?  41  VAL   A HG23 1 
ATOM   1009 H  HG23 B VAL   A 1 41  ? 31.312 2.637   -7.440  0.22 13.25 ?  41  VAL   A HG23 1 
ATOM   1010 N  N    A TYR   A 1 42  ? 31.608 3.452   -4.591  0.78 10.83 ?  42  TYR   A N    1 
ATOM   1011 N  N    B TYR   A 1 42  ? 31.367 3.478   -4.800  0.22 10.87 ?  42  TYR   A N    1 
ATOM   1012 C  CA   A TYR   A 1 42  ? 32.339 4.643   -4.175  0.78 10.64 ?  42  TYR   A CA   1 
ATOM   1013 C  CA   B TYR   A 1 42  ? 32.153 4.625   -4.356  0.22 11.25 ?  42  TYR   A CA   1 
ATOM   1014 C  C    A TYR   A 1 42  ? 32.076 5.016   -2.727  0.78 10.29 ?  42  TYR   A C    1 
ATOM   1015 C  C    B TYR   A 1 42  ? 31.877 5.023   -2.913  0.22 11.06 ?  42  TYR   A C    1 
ATOM   1016 O  O    A TYR   A 1 42  ? 32.644 6.003   -2.236  0.78 10.82 ?  42  TYR   A O    1 
ATOM   1017 O  O    B TYR   A 1 42  ? 32.450 6.009   -2.437  0.22 11.42 ?  42  TYR   A O    1 
ATOM   1018 C  CB   A TYR   A 1 42  ? 31.988 5.831   -5.091  0.78 11.42 ?  42  TYR   A CB   1 
ATOM   1019 C  CB   B TYR   A 1 42  ? 31.922 5.828   -5.275  0.22 12.09 ?  42  TYR   A CB   1 
ATOM   1020 C  CG   A TYR   A 1 42  ? 32.146 5.516   -6.565  0.78 12.65 ?  42  TYR   A CG   1 
ATOM   1021 C  CG   B TYR   A 1 42  ? 32.191 5.532   -6.728  0.22 12.95 ?  42  TYR   A CG   1 
ATOM   1022 C  CD1  A TYR   A 1 42  ? 33.399 5.324   -7.122  0.78 13.50 ?  42  TYR   A CD1  1 
ATOM   1023 C  CD1  B TYR   A 1 42  ? 33.482 5.301   -7.183  0.22 13.58 ?  42  TYR   A CD1  1 
ATOM   1024 C  CD2  A TYR   A 1 42  ? 31.041 5.387   -7.396  0.78 14.18 ?  42  TYR   A CD2  1 
ATOM   1025 C  CD2  B TYR   A 1 42  ? 31.154 5.480   -7.644  0.22 13.40 ?  42  TYR   A CD2  1 
ATOM   1026 C  CE1  A TYR   A 1 42  ? 33.552 5.021   -8.468  0.78 13.85 ?  42  TYR   A CE1  1 
ATOM   1027 C  CE1  B TYR   A 1 42  ? 33.728 5.024   -8.515  0.22 14.00 ?  42  TYR   A CE1  1 
ATOM   1028 C  CE2  A TYR   A 1 42  ? 31.184 5.087   -8.743  0.78 15.03 ?  42  TYR   A CE2  1 
ATOM   1029 C  CE2  B TYR   A 1 42  ? 31.388 5.207   -8.973  0.22 14.08 ?  42  TYR   A CE2  1 
ATOM   1030 C  CZ   A TYR   A 1 42  ? 32.445 4.907   -9.272  0.78 14.70 ?  42  TYR   A CZ   1 
ATOM   1031 C  CZ   B TYR   A 1 42  ? 32.676 4.981   -9.406  0.22 14.36 ?  42  TYR   A CZ   1 
ATOM   1032 O  OH   A TYR   A 1 42  ? 32.598 4.606   -10.607 0.78 16.06 ?  42  TYR   A OH   1 
ATOM   1033 O  OH   B TYR   A 1 42  ? 32.905 4.708   -10.733 0.22 15.26 ?  42  TYR   A OH   1 
ATOM   1034 H  H    A TYR   A 1 42  ? 30.826 3.628   -4.895  0.78 13.05 ?  42  TYR   A H    1 
ATOM   1035 H  H    B TYR   A 1 42  ? 30.574 3.680   -5.078  0.22 13.09 ?  42  TYR   A H    1 
ATOM   1036 H  HA   A TYR   A 1 42  ? 33.292 4.480   -4.268  0.78 12.82 ?  42  TYR   A HA   1 
ATOM   1037 H  HA   B TYR   A 1 42  ? 33.089 4.392   -4.418  0.22 13.55 ?  42  TYR   A HA   1 
ATOM   1038 H  HB2  A TYR   A 1 42  ? 31.064 6.086   -4.936  0.78 13.76 ?  42  TYR   A HB2  1 
ATOM   1039 H  HB2  B TYR   A 1 42  ? 30.999 6.113   -5.197  0.22 14.57 ?  42  TYR   A HB2  1 
ATOM   1040 H  HB3  A TYR   A 1 42  ? 32.572 6.580   -4.880  0.78 13.76 ?  42  TYR   A HB3  1 
ATOM   1041 H  HB3  B TYR   A 1 42  ? 32.515 6.545   -5.003  0.22 14.57 ?  42  TYR   A HB3  1 
ATOM   1042 H  HD1  A TYR   A 1 42  ? 34.155 5.400   -6.583  0.78 16.26 ?  42  TYR   A HD1  1 
ATOM   1043 H  HD1  B TYR   A 1 42  ? 34.194 5.329   -6.581  0.22 16.35 ?  42  TYR   A HD1  1 
ATOM   1044 H  HD2  A TYR   A 1 42  ? 30.189 5.514   -7.043  0.78 17.07 ?  42  TYR   A HD2  1 
ATOM   1045 H  HD2  B TYR   A 1 42  ? 30.284 5.633   -7.354  0.22 16.14 ?  42  TYR   A HD2  1 
ATOM   1046 H  HE1  A TYR   A 1 42  ? 34.402 4.899   -8.825  0.78 16.68 ?  42  TYR   A HE1  1 
ATOM   1047 H  HE1  B TYR   A 1 42  ? 34.599 4.872   -8.808  0.22 16.86 ?  42  TYR   A HE1  1 
ATOM   1048 H  HE2  A TYR   A 1 42  ? 30.435 5.013   -9.288  0.78 18.09 ?  42  TYR   A HE2  1 
ATOM   1049 H  HE2  B TYR   A 1 42  ? 30.681 5.178   -9.573  0.22 16.96 ?  42  TYR   A HE2  1 
ATOM   1050 H  HH   A TYR   A 1 42  ? 33.415 4.519   -10.793 0.78 19.32 ?  42  TYR   A HH   1 
ATOM   1051 H  HH   B TYR   A 1 42  ? 33.678 4.399   -10.828 0.22 18.37 ?  42  TYR   A HH   1 
ATOM   1052 N  N    A LEU   A 1 43  ? 31.235 4.247   -2.037  0.78 9.91  ?  43  LEU   A N    1 
ATOM   1053 N  N    B LEU   A 1 43  ? 31.020 4.284   -2.211  0.22 10.70 ?  43  LEU   A N    1 
ATOM   1054 C  CA   A LEU   A 1 43  ? 30.784 4.590   -0.694  0.78 9.75  ?  43  LEU   A CA   1 
ATOM   1055 C  CA   B LEU   A 1 43  ? 30.665 4.586   -0.825  0.22 10.57 ?  43  LEU   A CA   1 
ATOM   1056 C  C    A LEU   A 1 43  ? 30.303 6.039   -0.615  0.78 9.67  ?  43  LEU   A C    1 
ATOM   1057 C  C    B LEU   A 1 43  ? 30.195 6.029   -0.661  0.22 10.83 ?  43  LEU   A C    1 
ATOM   1058 O  O    A LEU   A 1 43  ? 30.563 6.751   0.357   0.78 10.94 ?  43  LEU   A O    1 
ATOM   1059 O  O    B LEU   A 1 43  ? 30.518 6.703   0.318   0.22 11.14 ?  43  LEU   A O    1 
ATOM   1060 C  CB   A LEU   A 1 43  ? 31.830 4.285   0.375   0.78 10.13 ?  43  LEU   A CB   1 
ATOM   1061 C  CB   B LEU   A 1 43  ? 31.800 4.256   0.144   0.22 10.37 ?  43  LEU   A CB   1 
ATOM   1062 C  CG   A LEU   A 1 43  ? 32.330 2.839   0.478   0.78 10.40 ?  43  LEU   A CG   1 
ATOM   1063 C  CG   B LEU   A 1 43  ? 32.213 2.784   0.199   0.22 10.03 ?  43  LEU   A CG   1 
ATOM   1064 C  CD1  A LEU   A 1 43  ? 33.366 2.744   1.591   0.78 10.95 ?  43  LEU   A CD1  1 
ATOM   1065 C  CD1  B LEU   A 1 43  ? 33.302 2.585   1.238   0.22 9.99  ?  43  LEU   A CD1  1 
ATOM   1066 C  CD2  A LEU   A 1 43  ? 31.200 1.860   0.721   0.78 10.94 ?  43  LEU   A CD2  1 
ATOM   1067 C  CD2  B LEU   A 1 43  ? 31.015 1.888   0.487   0.22 10.13 ?  43  LEU   A CD2  1 
ATOM   1068 H  H    A LEU   A 1 43  ? 30.908 3.502   -2.328  0.78 11.94 ?  43  LEU   A H    1 
ATOM   1069 H  H    B LEU   A 1 43  ? 30.621 3.592   -2.521  0.22 12.89 ?  43  LEU   A H    1 
ATOM   1070 H  HA   A LEU   A 1 43  ? 30.017 4.033   -0.493  0.78 11.76 ?  43  LEU   A HA   1 
ATOM   1071 H  HA   B LEU   A 1 43  ? 29.915 4.025   -0.586  0.22 12.74 ?  43  LEU   A HA   1 
ATOM   1072 H  HB2  A LEU   A 1 43  ? 32.604 4.849   0.213   0.78 12.22 ?  43  LEU   A HB2  1 
ATOM   1073 H  HB2  B LEU   A 1 43  ? 32.581 4.771   -0.110  0.22 12.49 ?  43  LEU   A HB2  1 
ATOM   1074 H  HB3  A LEU   A 1 43  ? 31.447 4.512   1.238   0.78 12.22 ?  43  LEU   A HB3  1 
ATOM   1075 H  HB3  B LEU   A 1 43  ? 31.520 4.512   1.039   0.22 12.49 ?  43  LEU   A HB3  1 
ATOM   1076 H  HG   A LEU   A 1 43  ? 32.770 2.598   -0.354  0.78 12.54 ?  43  LEU   A HG   1 
ATOM   1077 H  HG   B LEU   A 1 43  ? 32.575 2.529   -0.664  0.22 12.09 ?  43  LEU   A HG   1 
ATOM   1078 H  HD11 A LEU   A 1 43  ? 33.681 1.829   1.651   0.78 13.20 ?  43  LEU   A HD11 1 
ATOM   1079 H  HD11 B LEU   A 1 43  ? 33.554 1.649   1.255   0.22 12.05 ?  43  LEU   A HD11 1 
ATOM   1080 H  HD12 A LEU   A 1 43  ? 34.105 3.337   1.390   0.78 13.20 ?  43  LEU   A HD12 1 
ATOM   1081 H  HD12 B LEU   A 1 43  ? 34.068 3.131   1.002   0.22 12.05 ?  43  LEU   A HD12 1 
ATOM   1082 H  HD13 A LEU   A 1 43  ? 32.950 3.005   2.429   0.78 13.20 ?  43  LEU   A HD13 1 
ATOM   1083 H  HD13 B LEU   A 1 43  ? 32.962 2.851   2.107   0.22 12.05 ?  43  LEU   A HD13 1 
ATOM   1084 H  HD21 A LEU   A 1 43  ? 31.576 0.980   0.865   0.78 13.18 ?  43  LEU   A HD21 1 
ATOM   1085 H  HD21 B LEU   A 1 43  ? 31.332 1.002   0.719   0.22 12.21 ?  43  LEU   A HD21 1 
ATOM   1086 H  HD22 A LEU   A 1 43  ? 30.707 2.146   1.505   0.78 13.18 ?  43  LEU   A HD22 1 
ATOM   1087 H  HD22 B LEU   A 1 43  ? 30.511 2.264   1.226   0.22 12.21 ?  43  LEU   A HD22 1 
ATOM   1088 H  HD23 A LEU   A 1 43  ? 30.622 1.856   -0.055  0.78 13.18 ?  43  LEU   A HD23 1 
ATOM   1089 H  HD23 B LEU   A 1 43  ? 30.456 1.844   -0.305  0.22 12.21 ?  43  LEU   A HD23 1 
ATOM   1090 N  N    A LYS   A 1 44  ? 29.574 6.470   -1.648  0.78 10.12 ?  44  LYS   A N    1 
ATOM   1091 N  N    B LYS   A 1 44  ? 29.412 6.502   -1.628  0.22 11.06 ?  44  LYS   A N    1 
ATOM   1092 C  CA   A LYS   A 1 44  ? 28.921 7.777   -1.658  0.78 10.44 ?  44  LYS   A CA   1 
ATOM   1093 C  CA   B LYS   A 1 44  ? 28.780 7.818   -1.556  0.22 11.47 ?  44  LYS   A CA   1 
ATOM   1094 C  C    A LYS   A 1 44  ? 27.496 7.586   -1.153  0.78 9.79  ?  44  LYS   A C    1 
ATOM   1095 C  C    B LYS   A 1 44  ? 27.352 7.617   -1.062  0.22 10.78 ?  44  LYS   A C    1 
ATOM   1096 O  O    A LYS   A 1 44  ? 26.636 7.049   -1.862  0.78 10.75 ?  44  LYS   A O    1 
ATOM   1097 O  O    B LYS   A 1 44  ? 26.464 7.223   -1.822  0.22 10.98 ?  44  LYS   A O    1 
ATOM   1098 C  CB   A LYS   A 1 44  ? 28.951 8.392   -3.054  0.78 12.66 ?  44  LYS   A CB   1 
ATOM   1099 C  CB   B LYS   A 1 44  ? 28.848 8.527   -2.906  0.22 12.81 ?  44  LYS   A CB   1 
ATOM   1100 C  CG   A LYS   A 1 44  ? 30.330 8.862   -3.498  0.78 15.70 ?  44  LYS   A CG   1 
ATOM   1101 C  CG   B LYS   A 1 44  ? 30.232 9.087   -3.221  0.22 14.18 ?  44  LYS   A CG   1 
ATOM   1102 C  CD   A LYS   A 1 44  ? 30.992 9.782   -2.475  0.78 20.81 ?  44  LYS   A CD   1 
ATOM   1103 C  CD   B LYS   A 1 44  ? 30.804 9.823   -2.013  0.22 16.01 ?  44  LYS   A CD   1 
ATOM   1104 C  CE   A LYS   A 1 44  ? 32.327 10.302  -2.973  0.78 23.66 ?  44  LYS   A CE   1 
ATOM   1105 C  CE   B LYS   A 1 44  ? 31.920 10.773  -2.392  0.22 16.76 ?  44  LYS   A CE   1 
ATOM   1106 N  NZ   A LYS   A 1 44  ? 33.178 10.803  -1.857  0.78 25.00 ?  44  LYS   A NZ   1 
ATOM   1107 N  NZ   B LYS   A 1 44  ? 32.325 11.614  -1.231  0.22 17.02 ?  44  LYS   A NZ   1 
ATOM   1108 H  H    A LYS   A 1 44  ? 29.444 6.012   -2.366  0.78 12.20 ?  44  LYS   A H    1 
ATOM   1109 H  H    B LYS   A 1 44  ? 29.231 6.076   -2.352  0.22 13.33 ?  44  LYS   A H    1 
ATOM   1110 H  HA   A LYS   A 1 44  ? 29.375 8.364   -1.035  0.78 12.58 ?  44  LYS   A HA   1 
ATOM   1111 H  HA   B LYS   A 1 44  ? 29.227 8.350   -0.885  0.22 13.82 ?  44  LYS   A HA   1 
ATOM   1112 H  HB2  A LYS   A 1 44  ? 28.647 7.733   -3.695  0.78 15.25 ?  44  LYS   A HB2  1 
ATOM   1113 H  HB2  B LYS   A 1 44  ? 28.618 7.897   -3.610  0.22 15.42 ?  44  LYS   A HB2  1 
ATOM   1114 H  HB3  A LYS   A 1 44  ? 28.363 9.162   -3.067  0.78 15.25 ?  44  LYS   A HB3  1 
ATOM   1115 H  HB3  B LYS   A 1 44  ? 28.222 9.269   -2.912  0.22 15.42 ?  44  LYS   A HB3  1 
ATOM   1116 H  HG2  A LYS   A 1 44  ? 30.906 8.093   -3.630  0.78 18.90 ?  44  LYS   A HG2  1 
ATOM   1117 H  HG2  B LYS   A 1 44  ? 30.831 8.358   -3.452  0.22 17.07 ?  44  LYS   A HG2  1 
ATOM   1118 H  HG3  A LYS   A 1 44  ? 30.246 9.358   -4.332  0.78 18.90 ?  44  LYS   A HG3  1 
ATOM   1119 H  HG3  B LYS   A 1 44  ? 30.169 9.716   -3.959  0.22 17.07 ?  44  LYS   A HG3  1 
ATOM   1120 H  HD2  A LYS   A 1 44  ? 30.405 10.533  -2.296  0.78 25.03 ?  44  LYS   A HD2  1 
ATOM   1121 H  HD2  B LYS   A 1 44  ? 30.093 10.329  -1.585  0.22 19.27 ?  44  LYS   A HD2  1 
ATOM   1122 H  HD3  A LYS   A 1 44  ? 31.156 9.282   -1.658  0.78 25.03 ?  44  LYS   A HD3  1 
ATOM   1123 H  HD3  B LYS   A 1 44  ? 31.165 9.167   -1.389  0.22 19.27 ?  44  LYS   A HD3  1 
ATOM   1124 H  HE2  A LYS   A 1 44  ? 32.804 9.583   -3.417  0.78 28.45 ?  44  LYS   A HE2  1 
ATOM   1125 H  HE2  B LYS   A 1 44  ? 32.690 10.259  -2.683  0.22 20.17 ?  44  LYS   A HE2  1 
ATOM   1126 H  HE3  A LYS   A 1 44  ? 32.173 11.033  -3.589  0.78 28.45 ?  44  LYS   A HE3  1 
ATOM   1127 H  HE3  B LYS   A 1 44  ? 31.613 11.355  -3.103  0.22 20.17 ?  44  LYS   A HE3  1 
ATOM   1128 H  HZ1  A LYS   A 1 44  ? 33.953 11.103  -2.177  0.78 30.05 ?  44  LYS   A HZ1  1 
ATOM   1129 H  HZ1  B LYS   A 1 44  ? 32.980 12.164  -1.471  0.22 20.47 ?  44  LYS   A HZ1  1 
ATOM   1130 H  HZ2  A LYS   A 1 44  ? 32.764 11.469  -1.434  0.78 30.05 ?  44  LYS   A HZ2  1 
ATOM   1131 H  HZ2  B LYS   A 1 44  ? 31.631 12.092  -0.947  0.22 20.47 ?  44  LYS   A HZ2  1 
ATOM   1132 H  HZ3  A LYS   A 1 44  ? 33.339 10.148  -1.277  0.78 30.05 ?  44  LYS   A HZ3  1 
ATOM   1133 H  HZ3  B LYS   A 1 44  ? 32.610 11.095  -0.565  0.22 20.47 ?  44  LYS   A HZ3  1 
ATOM   1134 N  N    A HIS   A 1 45  ? 27.255 8.005   0.086   0.78 9.45  ?  45  HIS   A N    1 
ATOM   1135 N  N    B HIS   A 1 45  ? 27.143 7.888   0.225   0.22 10.57 ?  45  HIS   A N    1 
ATOM   1136 C  CA   A HIS   A 1 45  ? 26.030 7.648   0.801   0.78 9.75  ?  45  HIS   A CA   1 
ATOM   1137 C  CA   B HIS   A 1 45  ? 25.873 7.594   0.889   0.22 10.41 ?  45  HIS   A CA   1 
ATOM   1138 C  C    A HIS   A 1 45  ? 24.985 8.747   0.626   0.78 10.54 ?  45  HIS   A C    1 
ATOM   1139 C  C    B HIS   A 1 45  ? 24.945 8.803   0.777   0.22 10.46 ?  45  HIS   A C    1 
ATOM   1140 O  O    A HIS   A 1 45  ? 24.710 9.532   1.533   0.78 12.45 ?  45  HIS   A O    1 
ATOM   1141 O  O    B HIS   A 1 45  ? 24.622 9.484   1.751   0.22 10.91 ?  45  HIS   A O    1 
ATOM   1142 C  CB   A HIS   A 1 45  ? 26.345 7.426   2.272   0.78 9.43  ?  45  HIS   A CB   1 
ATOM   1143 C  CB   B HIS   A 1 45  ? 26.119 7.208   2.339   0.22 10.36 ?  45  HIS   A CB   1 
ATOM   1144 C  CG   A HIS   A 1 45  ? 27.449 6.449   2.510   0.78 9.47  ?  45  HIS   A CG   1 
ATOM   1145 C  CG   B HIS   A 1 45  ? 27.312 6.328   2.531   0.22 9.44  ?  45  HIS   A CG   1 
ATOM   1146 N  ND1  A HIS   A 1 45  ? 27.423 5.157   2.027   0.78 10.04 ?  45  HIS   A ND1  1 
ATOM   1147 N  ND1  B HIS   A 1 45  ? 27.391 5.056   2.006   0.22 9.24  ?  45  HIS   A ND1  1 
ATOM   1148 C  CD2  A HIS   A 1 45  ? 28.626 6.591   3.171   0.78 9.93  ?  45  HIS   A CD2  1 
ATOM   1149 C  CD2  B HIS   A 1 45  ? 28.479 6.542   3.184   0.22 9.66  ?  45  HIS   A CD2  1 
ATOM   1150 C  CE1  A HIS   A 1 45  ? 28.537 4.545   2.395   0.78 9.75  ?  45  HIS   A CE1  1 
ATOM   1151 C  CE1  B HIS   A 1 45  ? 28.555 4.523   2.333   0.22 9.41  ?  45  HIS   A CE1  1 
ATOM   1152 N  NE2  A HIS   A 1 45  ? 29.284 5.391   3.088   0.78 10.14 ?  45  HIS   A NE2  1 
ATOM   1153 N  NE2  B HIS   A 1 45  ? 29.234 5.404   3.047   0.22 9.79  ?  45  HIS   A NE2  1 
ATOM   1154 H  H    A HIS   A 1 45  ? 27.790 8.508   0.542   0.78 11.39 ?  45  HIS   A H    1 
ATOM   1155 H  H    B HIS   A 1 45  ? 27.730 8.249   0.742   0.22 12.73 ?  45  HIS   A H    1 
ATOM   1156 H  HA   A HIS   A 1 45  ? 25.672 6.830   0.432   0.78 11.76 ?  45  HIS   A HA   1 
ATOM   1157 H  HA   B HIS   A 1 45  ? 25.449 6.847   0.441   0.22 12.55 ?  45  HIS   A HA   1 
ATOM   1158 H  HB2  A HIS   A 1 45  ? 26.599 8.274   2.670   0.78 11.37 ?  45  HIS   A HB2  1 
ATOM   1159 H  HB2  B HIS   A 1 45  ? 26.257 8.016   2.857   0.22 12.49 ?  45  HIS   A HB2  1 
ATOM   1160 H  HB3  A HIS   A 1 45  ? 25.548 7.086   2.711   0.78 11.37 ?  45  HIS   A HB3  1 
ATOM   1161 H  HB3  B HIS   A 1 45  ? 25.342 6.735   2.671   0.22 12.49 ?  45  HIS   A HB3  1 
ATOM   1162 H  HD2  A HIS   A 1 45  ? 28.936 7.361   3.600   0.78 11.97 ?  45  HIS   A HD2  1 
ATOM   1163 H  HD2  B HIS   A 1 45  ? 28.723 7.317   3.639   0.22 11.64 ?  45  HIS   A HD2  1 
ATOM   1164 H  HE1  A HIS   A 1 45  ? 28.755 3.661   2.210   0.78 11.75 ?  45  HIS   A HE1  1 
ATOM   1165 H  HE1  B HIS   A 1 45  ? 28.844 3.671   2.102   0.22 11.35 ?  45  HIS   A HE1  1 
ATOM   1166 H  HE2  A HIS   A 1 45  ? 30.056 5.214   3.432   0.78 12.23 ?  45  HIS   A HE2  1 
ATOM   1167 H  HE2  B HIS   A 1 45  ? 30.019 5.283   3.373   0.22 11.80 ?  45  HIS   A HE2  1 
ATOM   1168 N  N    A GLY   A 1 46  ? 24.373 8.783   -0.554  0.78 11.04 ?  46  GLY   A N    1 
ATOM   1169 N  N    B GLY   A 1 46  ? 24.505 9.051   -0.457  0.22 10.52 ?  46  GLY   A N    1 
ATOM   1170 C  CA   A GLY   A 1 46  ? 23.538 9.916   -0.916  0.78 11.82 ?  46  GLY   A CA   1 
ATOM   1171 C  CA   B GLY   A 1 46  ? 23.718 10.238  -0.737  0.22 10.35 ?  46  GLY   A CA   1 
ATOM   1172 C  C    A GLY   A 1 46  ? 22.058 9.782   -0.613  0.78 12.31 ?  46  GLY   A C    1 
ATOM   1173 C  C    B GLY   A 1 46  ? 22.239 10.088  -0.462  0.22 9.96  ?  46  GLY   A C    1 
ATOM   1174 O  O    A GLY   A 1 46  ? 21.404 10.769  -0.252  0.78 13.60 ?  46  GLY   A O    1 
ATOM   1175 O  O    B GLY   A 1 46  ? 21.566 11.076  -0.153  0.22 10.29 ?  46  GLY   A O    1 
ATOM   1176 H  H    A GLY   A 1 46  ? 24.414 8.175   -1.154  0.78 13.31 ?  46  GLY   A H    1 
ATOM   1177 H  H    B GLY   A 1 46  ? 24.646 8.552   -1.134  0.22 12.68 ?  46  GLY   A H    1 
ATOM   1178 H  HA2  A GLY   A 1 46  ? 23.854 10.706  -0.449  0.78 14.24 ?  46  GLY   A HA2  1 
ATOM   1179 H  HA2  B GLY   A 1 46  ? 24.054 10.975  -0.206  0.22 12.48 ?  46  GLY   A HA2  1 
ATOM   1180 H  HA3  A GLY   A 1 46  ? 23.624 10.080  -1.867  0.78 14.24 ?  46  GLY   A HA3  1 
ATOM   1181 H  HA3  B GLY   A 1 46  ? 23.820 10.466  -1.673  0.22 12.48 ?  46  GLY   A HA3  1 
ATOM   1182 N  N    A GLY   A 1 47  ? 21.505 8.583   -0.778  0.78 12.03 ?  47  GLY   A N    1 
ATOM   1183 N  N    B GLY   A 1 47  ? 21.706 8.877   -0.587  0.22 9.89  ?  47  GLY   A N    1 
ATOM   1184 C  CA   A GLY   A 1 47  ? 20.074 8.381   -0.676  0.78 12.15 ?  47  GLY   A CA   1 
ATOM   1185 C  CA   B GLY   A 1 47  ? 20.281 8.674   -0.414  0.22 10.64 ?  47  GLY   A CA   1 
ATOM   1186 C  C    A GLY   A 1 47  ? 19.750 6.956   -0.279  0.78 11.54 ?  47  GLY   A C    1 
ATOM   1187 C  C    B GLY   A 1 47  ? 19.959 7.217   -0.165  0.22 10.96 ?  47  GLY   A C    1 
ATOM   1188 O  O    A GLY   A 1 47  ? 20.639 6.126   -0.065  0.78 11.59 ?  47  GLY   A O    1 
ATOM   1189 O  O    B GLY   A 1 47  ? 20.844 6.363   -0.067  0.22 11.38 ?  47  GLY   A O    1 
ATOM   1190 H  H    A GLY   A 1 47  ? 21.945 7.861   -0.931  0.78 14.49 ?  47  GLY   A H    1 
ATOM   1191 H  H    B GLY   A 1 47  ? 22.148 8.166   -0.770  0.22 11.92 ?  47  GLY   A H    1 
ATOM   1192 H  HA2  A GLY   A 1 47  ? 19.697 8.986   -0.014  0.78 14.64 ?  47  GLY   A HA2  1 
ATOM   1193 H  HA2  B GLY   A 1 47  ? 19.960 9.205   0.335   0.22 12.82 ?  47  GLY   A HA2  1 
ATOM   1194 H  HA3  A GLY   A 1 47  ? 19.655 8.564   -1.533  0.78 14.64 ?  47  GLY   A HA3  1 
ATOM   1195 H  HA3  B GLY   A 1 47  ? 19.814 8.956   -1.215  0.22 12.82 ?  47  GLY   A HA3  1 
ATOM   1196 N  N    A GLY   A 1 48  ? 18.454 6.666   -0.194  0.78 12.03 ?  48  GLY   A N    1 
ATOM   1197 N  N    B GLY   A 1 48  ? 18.661 6.944   -0.059  0.22 11.62 ?  48  GLY   A N    1 
ATOM   1198 C  CA   A GLY   A 1 48  ? 18.043 5.347   0.238   0.78 12.06 ?  48  GLY   A CA   1 
ATOM   1199 C  CA   B GLY   A 1 48  ? 18.203 5.596   0.206   0.22 11.49 ?  48  GLY   A CA   1 
ATOM   1200 C  C    A GLY   A 1 48  ? 18.566 5.049   1.628   0.78 11.53 ?  48  GLY   A C    1 
ATOM   1201 C  C    B GLY   A 1 48  ? 18.583 5.145   1.604   0.22 11.00 ?  48  GLY   A C    1 
ATOM   1202 O  O    A GLY   A 1 48  ? 18.769 5.951   2.453   0.78 11.82 ?  48  GLY   A O    1 
ATOM   1203 O  O    B GLY   A 1 48  ? 18.611 5.928   2.559   0.22 10.89 ?  48  GLY   A O    1 
ATOM   1204 H  H    A GLY   A 1 48  ? 17.806 7.209   -0.363  0.78 14.49 ?  48  GLY   A H    1 
ATOM   1205 H  H    B GLY   A 1 48  ? 18.036 7.526   -0.130  0.22 14.00 ?  48  GLY   A H    1 
ATOM   1206 H  HA2  A GLY   A 1 48  ? 17.076 5.286   0.249   0.78 14.53 ?  48  GLY   A HA2  1 
ATOM   1207 H  HA2  B GLY   A 1 48  ? 17.239 5.557   0.114   0.22 13.84 ?  48  GLY   A HA2  1 
ATOM   1208 H  HA3  A GLY   A 1 48  ? 18.395 4.681   -0.370  0.78 14.53 ?  48  GLY   A HA3  1 
ATOM   1209 H  HA3  B GLY   A 1 48  ? 18.603 4.984   -0.427  0.22 13.84 ?  48  GLY   A HA3  1 
ATOM   1210 N  N    A VAL   A 1 49  ? 18.793 3.759   1.892   0.78 10.85 ?  49  VAL   A N    1 
ATOM   1211 N  N    B VAL   A 1 49  ? 18.883 3.850   1.722   0.22 10.61 ?  49  VAL   A N    1 
ATOM   1212 C  CA   A VAL   A 1 49  ? 19.330 3.340   3.185   0.78 11.10 ?  49  VAL   A CA   1 
ATOM   1213 C  CA   B VAL   A 1 49  ? 19.359 3.314   2.993   0.22 10.23 ?  49  VAL   A CA   1 
ATOM   1214 C  C    A VAL   A 1 49  ? 20.637 4.064   3.490   0.78 9.96  ?  49  VAL   A C    1 
ATOM   1215 C  C    B VAL   A 1 49  ? 20.684 3.956   3.378   0.22 9.14  ?  49  VAL   A C    1 
ATOM   1216 O  O    A VAL   A 1 49  ? 20.856 4.523   4.615   0.78 10.24 ?  49  VAL   A O    1 
ATOM   1217 O  O    B VAL   A 1 49  ? 20.922 4.264   4.552   0.22 8.61  ?  49  VAL   A O    1 
ATOM   1218 C  CB   A VAL   A 1 49  ? 19.503 1.807   3.217   0.78 11.68 ?  49  VAL   A CB   1 
ATOM   1219 C  CB   B VAL   A 1 49  ? 19.477 1.780   2.913   0.22 10.62 ?  49  VAL   A CB   1 
ATOM   1220 C  CG1  A VAL   A 1 49  ? 20.350 1.375   4.412   0.78 11.81 ?  49  VAL   A CG1  1 
ATOM   1221 C  CG1  B VAL   A 1 49  ? 20.204 1.241   4.136   0.22 10.82 ?  49  VAL   A CG1  1 
ATOM   1222 C  CG2  A VAL   A 1 49  ? 18.139 1.121   3.250   0.78 13.60 ?  49  VAL   A CG2  1 
ATOM   1223 C  CG2  B VAL   A 1 49  ? 18.102 1.146   2.775   0.22 10.73 ?  49  VAL   A CG2  1 
ATOM   1224 H  H    A VAL   A 1 49  ? 18.641 3.112   1.347   0.78 13.07 ?  49  VAL   A H    1 
ATOM   1225 H  H    B VAL   A 1 49  ? 18.823 3.272   1.089   0.22 12.79 ?  49  VAL   A H    1 
ATOM   1226 H  HA   A VAL   A 1 49  ? 18.694 3.570   3.880   0.78 13.38 ?  49  VAL   A HA   1 
ATOM   1227 H  HA   B VAL   A 1 49  ? 18.711 3.524   3.685   0.22 12.33 ?  49  VAL   A HA   1 
ATOM   1228 H  HB   A VAL   A 1 49  ? 19.957 1.520   2.407   0.78 14.07 ?  49  VAL   A HB   1 
ATOM   1229 H  HB   B VAL   A 1 49  ? 19.996 1.545   2.128   0.22 12.80 ?  49  VAL   A HB   1 
ATOM   1230 H  HG11 A VAL   A 1 49  ? 20.207 0.429   4.567   0.78 14.23 ?  49  VAL   A HG11 1 
ATOM   1231 H  HG11 B VAL   A 1 49  ? 19.924 0.326   4.288   0.22 13.04 ?  49  VAL   A HG11 1 
ATOM   1232 H  HG12 A VAL   A 1 49  ? 21.279 1.546   4.218   0.78 14.23 ?  49  VAL   A HG12 1 
ATOM   1233 H  HG12 B VAL   A 1 49  ? 21.160 1.274   3.979   0.22 13.04 ?  49  VAL   A HG12 1 
ATOM   1234 H  HG13 A VAL   A 1 49  ? 20.065 1.882   5.189   0.78 14.23 ?  49  VAL   A HG13 1 
ATOM   1235 H  HG13 B VAL   A 1 49  ? 19.971 1.783   4.905   0.22 13.04 ?  49  VAL   A HG13 1 
ATOM   1236 H  HG21 A VAL   A 1 49  ? 18.266 0.161   3.260   0.78 16.37 ?  49  VAL   A HG21 1 
ATOM   1237 H  HG21 B VAL   A 1 49  ? 18.204 0.183   2.719   0.22 12.93 ?  49  VAL   A HG21 1 
ATOM   1238 H  HG22 A VAL   A 1 49  ? 17.667 1.403   4.050   0.78 16.37 ?  49  VAL   A HG22 1 
ATOM   1239 H  HG22 B VAL   A 1 49  ? 17.570 1.378   3.553   0.22 12.93 ?  49  VAL   A HG22 1 
ATOM   1240 H  HG23 A VAL   A 1 49  ? 17.635 1.382   2.462   0.78 16.37 ?  49  VAL   A HG23 1 
ATOM   1241 H  HG23 B VAL   A 1 49  ? 17.679 1.483   1.971   0.22 12.93 ?  49  VAL   A HG23 1 
ATOM   1242 N  N    A ALA   A 1 50  ? 21.541 4.132   2.508   0.78 9.75  ?  50  ALA   A N    1 
ATOM   1243 N  N    B ALA   A 1 50  ? 21.575 4.144   2.404   0.22 8.99  ?  50  ALA   A N    1 
ATOM   1244 C  CA   A ALA   A 1 50  ? 22.863 4.700   2.765   0.78 9.47  ?  50  ALA   A CA   1 
ATOM   1245 C  CA   B ALA   A 1 50  ? 22.891 4.704   2.696   0.22 9.23  ?  50  ALA   A CA   1 
ATOM   1246 C  C    A ALA   A 1 50  ? 22.766 6.158   3.191   0.78 9.14  ?  50  ALA   A C    1 
ATOM   1247 C  C    B ALA   A 1 50  ? 22.783 6.150   3.162   0.22 9.32  ?  50  ALA   A C    1 
ATOM   1248 O  O    A ALA   A 1 50  ? 23.409 6.579   4.159   0.78 9.81  ?  50  ALA   A O    1 
ATOM   1249 O  O    B ALA   A 1 50  ? 23.419 6.547   4.144   0.22 9.42  ?  50  ALA   A O    1 
ATOM   1250 C  CB   A ALA   A 1 50  ? 23.742 4.561   1.527   0.78 9.21  ?  50  ALA   A CB   1 
ATOM   1251 C  CB   B ALA   A 1 50  ? 23.781 4.594   1.458   0.22 9.33  ?  50  ALA   A CB   1 
ATOM   1252 H  H    A ALA   A 1 50  ? 21.412 3.863   1.698   0.78 11.76 ?  50  ALA   A H    1 
ATOM   1253 H  H    B ALA   A 1 50  ? 21.442 3.956   1.576   0.22 10.85 ?  50  ALA   A H    1 
ATOM   1254 H  HA   A ALA   A 1 50  ? 23.281 4.211   3.487   0.78 11.41 ?  50  ALA   A HA   1 
ATOM   1255 H  HA   B ALA   A 1 50  ? 23.302 4.197   3.409   0.22 11.13 ?  50  ALA   A HA   1 
ATOM   1256 H  HB1  A ALA   A 1 50  ? 24.611 4.947   1.715   0.78 11.11 ?  50  ALA   A HB1  1 
ATOM   1257 H  HB1  B ALA   A 1 50  ? 24.675 4.893   1.679   0.22 11.26 ?  50  ALA   A HB1  1 
ATOM   1258 H  HB2  A ALA   A 1 50  ? 23.832 3.624   1.306   0.78 11.11 ?  50  ALA   A HB2  1 
ATOM   1259 H  HB2  B ALA   A 1 50  ? 23.804 3.668   1.169   0.22 11.26 ?  50  ALA   A HB2  1 
ATOM   1260 H  HB3  A ALA   A 1 50  ? 23.323 5.037   0.789   0.78 11.11 ?  50  ALA   A HB3  1 
ATOM   1261 H  HB3  B ALA   A 1 50  ? 23.409 5.147   0.751   0.22 11.26 ?  50  ALA   A HB3  1 
ATOM   1262 N  N    . GLY   A 1 51  ? 21.981 6.952   2.463   1.00 9.79  ?  51  GLY   A N    1 
ATOM   1263 C  CA   . GLY   A 1 51  ? 21.825 8.342   2.848   1.00 10.19 ?  51  GLY   A CA   1 
ATOM   1264 C  C    . GLY   A 1 51  ? 21.229 8.482   4.232   1.00 10.03 ?  51  GLY   A C    1 
ATOM   1265 O  O    . GLY   A 1 51  ? 21.619 9.368   4.996   1.00 10.75 ?  51  GLY   A O    1 
ATOM   1266 H  H    A GLY   A 1 51  ? 21.544 6.716   1.758   0.78 11.80 ?  51  GLY   A H    1 
ATOM   1267 H  H    B GLY   A 1 51  ? 21.522 6.714   1.773   0.22 11.80 ?  51  GLY   A H    1 
ATOM   1268 H  HA2  . GLY   A 1 51  ? 22.689 8.780   2.844   1.00 12.29 ?  51  GLY   A HA2  1 
ATOM   1269 H  HA3  . GLY   A 1 51  ? 21.247 8.795   2.212   1.00 12.29 ?  51  GLY   A HA3  1 
ATOM   1270 N  N    . ALA   A 1 52  ? 20.274 7.609   4.572   1.00 10.17 ?  52  ALA   A N    1 
ATOM   1271 C  CA   . ALA   A 1 52  ? 19.640 7.660   5.888   1.00 10.79 ?  52  ALA   A CA   1 
ATOM   1272 C  C    . ALA   A 1 52  ? 20.613 7.259   6.997   1.00 10.12 ?  52  ALA   A C    1 
ATOM   1273 O  O    . ALA   A 1 52  ? 20.696 7.923   8.036   1.00 10.95 ?  52  ALA   A O    1 
ATOM   1274 C  CB   . ALA   A 1 52  ? 18.389 6.774   5.899   1.00 12.39 ?  52  ALA   A CB   1 
ATOM   1275 H  H    . ALA   A 1 52  ? 19.990 6.971   4.063   1.00 12.26 ?  52  ALA   A H    1 
ATOM   1276 H  HA   . ALA   A 1 52  ? 19.355 8.565   6.058   1.00 13.00 ?  52  ALA   A HA   1 
ATOM   1277 H  HB1  . ALA   A 1 52  ? 17.974 6.821   6.777   1.00 14.93 ?  52  ALA   A HB1  1 
ATOM   1278 H  HB2  . ALA   A 1 52  ? 17.765 7.096   5.226   1.00 14.93 ?  52  ALA   A HB2  1 
ATOM   1279 H  HB3  . ALA   A 1 52  ? 18.640 5.858   5.702   1.00 14.93 ?  52  ALA   A HB3  1 
ATOM   1280 N  N    A LEU   A 1 53  ? 21.336 6.152   6.816   0.78 10.01 ?  53  LEU   A N    1 
ATOM   1281 N  N    B LEU   A 1 53  ? 21.356 6.167   6.789   0.22 10.04 ?  53  LEU   A N    1 
ATOM   1282 C  CA   A LEU   A 1 53  ? 22.321 5.756   7.822   0.78 10.12 ?  53  LEU   A CA   1 
ATOM   1283 C  CA   B LEU   A 1 53  ? 22.323 5.722   7.790   0.22 10.11 ?  53  LEU   A CA   1 
ATOM   1284 C  C    A LEU   A 1 53  ? 23.356 6.854   8.010   0.78 9.94  ?  53  LEU   A C    1 
ATOM   1285 C  C    B LEU   A 1 53  ? 23.419 6.759   7.993   0.22 9.83  ?  53  LEU   A C    1 
ATOM   1286 O  O    A LEU   A 1 53  ? 23.672 7.245   9.138   0.78 10.69 ?  53  LEU   A O    1 
ATOM   1287 O  O    B LEU   A 1 53  ? 23.852 7.003   9.124   0.22 9.89  ?  53  LEU   A O    1 
ATOM   1288 C  CB   A LEU   A 1 53  ? 23.006 4.439   7.431   0.78 10.57 ?  53  LEU   A CB   1 
ATOM   1289 C  CB   B LEU   A 1 53  ? 22.935 4.382   7.370   0.22 10.57 ?  53  LEU   A CB   1 
ATOM   1290 C  CG   A LEU   A 1 53  ? 22.168 3.154   7.494   0.78 11.13 ?  53  LEU   A CG   1 
ATOM   1291 C  CG   B LEU   A 1 53  ? 22.035 3.144   7.427   0.22 10.96 ?  53  LEU   A CG   1 
ATOM   1292 C  CD1  A LEU   A 1 53  ? 22.950 1.990   6.911   0.78 11.78 ?  53  LEU   A CD1  1 
ATOM   1293 C  CD1  B LEU   A 1 53  ? 22.715 1.969   6.746   0.22 11.10 ?  53  LEU   A CD1  1 
ATOM   1294 C  CD2  A LEU   A 1 53  ? 21.727 2.834   8.911   0.78 12.86 ?  53  LEU   A CD2  1 
ATOM   1295 C  CD2  B LEU   A 1 53  ? 21.690 2.792   8.863   0.22 11.56 ?  53  LEU   A CD2  1 
ATOM   1296 H  H    A LEU   A 1 53  ? 21.280 5.622   6.136   0.78 12.06 ?  53  LEU   A H    1 
ATOM   1297 H  H    B LEU   A 1 53  ? 21.319 5.671   6.085   0.22 12.10 ?  53  LEU   A H    1 
ATOM   1298 H  HA   A LEU   A 1 53  ? 21.872 5.618   8.669   0.78 12.20 ?  53  LEU   A HA   1 
ATOM   1299 H  HA   B LEU   A 1 53  ? 21.868 5.592   8.636   0.22 12.19 ?  53  LEU   A HA   1 
ATOM   1300 H  HB2  A LEU   A 1 53  ? 23.329 4.522   6.520   0.78 12.74 ?  53  LEU   A HB2  1 
ATOM   1301 H  HB2  B LEU   A 1 53  ? 23.243 4.463   6.455   0.22 12.74 ?  53  LEU   A HB2  1 
ATOM   1302 H  HB3  A LEU   A 1 53  ? 23.765 4.304   8.023   0.78 12.74 ?  53  LEU   A HB3  1 
ATOM   1303 H  HB3  B LEU   A 1 53  ? 23.693 4.201   7.947   0.22 12.74 ?  53  LEU   A HB3  1 
ATOM   1304 H  HG   A LEU   A 1 53  ? 21.373 3.274   6.948   0.78 13.41 ?  53  LEU   A HG   1 
ATOM   1305 H  HG   B LEU   A 1 53  ? 21.208 3.327   6.951   0.22 13.20 ?  53  LEU   A HG   1 
ATOM   1306 H  HD11 A LEU   A 1 53  ? 22.402 1.188   6.955   0.78 14.19 ?  53  LEU   A HD11 1 
ATOM   1307 H  HD11 B LEU   A 1 53  ? 22.133 1.195   6.793   0.22 13.38 ?  53  LEU   A HD11 1 
ATOM   1308 H  HD12 A LEU   A 1 53  ? 23.171 2.185   5.985   0.78 14.19 ?  53  LEU   A HD12 1 
ATOM   1309 H  HD12 B LEU   A 1 53  ? 22.889 2.197   5.819   0.22 13.38 ?  53  LEU   A HD12 1 
ATOM   1310 H  HD13 A LEU   A 1 53  ? 23.761 1.864   7.425   0.78 14.19 ?  53  LEU   A HD13 1 
ATOM   1311 H  HD13 B LEU   A 1 53  ? 23.551 1.783   7.203   0.22 13.38 ?  53  LEU   A HD13 1 
ATOM   1312 H  HD21 A LEU   A 1 53  ? 21.230 1.999   8.906   0.78 15.49 ?  53  LEU   A HD21 1 
ATOM   1313 H  HD21 B LEU   A 1 53  ? 21.179 1.967   8.873   0.22 13.93 ?  53  LEU   A HD21 1 
ATOM   1314 H  HD22 A LEU   A 1 53  ? 22.509 2.751   9.474   0.78 15.49 ?  53  LEU   A HD22 1 
ATOM   1315 H  HD22 B LEU   A 1 53  ? 22.512 2.678   9.365   0.22 13.93 ?  53  LEU   A HD22 1 
ATOM   1316 H  HD23 A LEU   A 1 53  ? 21.158 3.551   9.233   0.78 15.49 ?  53  LEU   A HD23 1 
ATOM   1317 H  HD23 B LEU   A 1 53  ? 21.165 3.511   9.247   0.22 13.93 ?  53  LEU   A HD23 1 
ATOM   1318 N  N    . ASN   A 1 54  ? 23.887 7.374   6.907   1.00 9.64  ?  54  ASN   A N    1 
ATOM   1319 C  CA   . ASN   A 1 54  ? 24.935 8.375   7.025   1.00 9.67  ?  54  ASN   A CA   1 
ATOM   1320 C  C    . ASN   A 1 54  ? 24.424 9.624   7.747   1.00 10.15 ?  54  ASN   A C    1 
ATOM   1321 O  O    . ASN   A 1 54  ? 25.120 10.181  8.610   1.00 10.47 ?  54  ASN   A O    1 
ATOM   1322 C  CB   . ASN   A 1 54  ? 25.491 8.732   5.656   1.00 9.89  ?  54  ASN   A CB   1 
ATOM   1323 C  CG   . ASN   A 1 54  ? 26.502 9.837   5.757   1.00 9.96  ?  54  ASN   A CG   1 
ATOM   1324 O  OD1  . ASN   A 1 54  ? 27.513 9.696   6.454   1.00 10.17 ?  54  ASN   A OD1  1 
ATOM   1325 N  ND2  . ASN   A 1 54  ? 26.230 10.960  5.111   1.00 10.89 ?  54  ASN   A ND2  1 
ATOM   1326 H  H    A ASN   A 1 54  ? 23.655 7.174   6.103   0.78 11.63 ?  54  ASN   A H    1 
ATOM   1327 H  H    B ASN   A 1 54  ? 23.605 7.235   6.106   0.22 11.63 ?  54  ASN   A H    1 
ATOM   1328 H  HA   . ASN   A 1 54  ? 25.653 8.004   7.551   1.00 11.66 ?  54  ASN   A HA   1 
ATOM   1329 H  HB2  . ASN   A 1 54  ? 25.931 7.944   5.280   1.00 11.92 ?  54  ASN   A HB2  1 
ATOM   1330 H  HB3  . ASN   A 1 54  ? 24.769 9.014   5.076   1.00 11.92 ?  54  ASN   A HB3  1 
ATOM   1331 H  HD21 . ASN   A 1 54  ? 26.774 11.617  5.151   1.00 13.12 ?  54  ASN   A HD21 1 
ATOM   1332 H  HD22 . ASN   A 1 54  ? 25.503 11.021  4.651   1.00 13.12 ?  54  ASN   A HD22 1 
ATOM   1333 N  N    A LYS   A 1 55  ? 23.215 10.081  7.401   0.78 10.37 ?  55  LYS   A N    1 
ATOM   1334 N  N    B LYS   A 1 55  ? 23.208 10.074  7.418   0.22 10.47 ?  55  LYS   A N    1 
ATOM   1335 C  CA   A LYS   A 1 55  ? 22.626 11.231  8.078   0.78 10.76 ?  55  LYS   A CA   1 
ATOM   1336 C  CA   B LYS   A 1 55  ? 22.650 11.245  8.087   0.22 10.97 ?  55  LYS   A CA   1 
ATOM   1337 C  C    A LYS   A 1 55  ? 22.554 10.999  9.580   0.78 11.07 ?  55  LYS   A C    1 
ATOM   1338 C  C    B LYS   A 1 55  ? 22.524 11.011  9.588   0.22 11.22 ?  55  LYS   A C    1 
ATOM   1339 O  O    A LYS   A 1 55  ? 22.858 11.901  10.373  0.78 11.81 ?  55  LYS   A O    1 
ATOM   1340 O  O    B LYS   A 1 55  ? 22.751 11.927  10.389  0.22 11.50 ?  55  LYS   A O    1 
ATOM   1341 C  CB   A LYS   A 1 55  ? 21.242 11.510  7.489   0.78 11.43 ?  55  LYS   A CB   1 
ATOM   1342 C  CB   B LYS   A 1 55  ? 21.295 11.606  7.471   0.22 11.45 ?  55  LYS   A CB   1 
ATOM   1343 C  CG   A LYS   A 1 55  ? 20.463 12.627  8.160   0.78 12.57 ?  55  LYS   A CG   1 
ATOM   1344 C  CG   B LYS   A 1 55  ? 20.682 12.907  7.990   0.22 12.06 ?  55  LYS   A CG   1 
ATOM   1345 C  CD   A LYS   A 1 55  ? 19.138 12.851  7.432   0.78 13.84 ?  55  LYS   A CD   1 
ATOM   1346 C  CD   B LYS   A 1 55  ? 19.333 13.191  7.328   0.22 12.78 ?  55  LYS   A CD   1 
ATOM   1347 C  CE   A LYS   A 1 55  ? 18.296 13.937  8.076   0.78 15.23 ?  55  LYS   A CE   1 
ATOM   1348 C  CE   B LYS   A 1 55  ? 18.661 14.426  7.916   0.22 13.74 ?  55  LYS   A CE   1 
ATOM   1349 N  NZ   A LYS   A 1 55  ? 16.985 14.090  7.387   0.78 15.52 ?  55  LYS   A NZ   1 
ATOM   1350 N  NZ   B LYS   A 1 55  ? 17.338 14.709  7.286   0.22 14.06 ?  55  LYS   A NZ   1 
ATOM   1351 H  H    A LYS   A 1 55  ? 22.713 9.737   6.787   0.78 12.50 ?  55  LYS   A H    1 
ATOM   1352 H  H    B LYS   A 1 55  ? 22.694 9.723   6.821   0.22 12.62 ?  55  LYS   A H    1 
ATOM   1353 H  HA   A LYS   A 1 55  ? 23.183 12.008  7.923   0.78 12.96 ?  55  LYS   A HA   1 
ATOM   1354 H  HA   B LYS   A 1 55  ? 23.248 11.996  7.954   0.22 13.21 ?  55  LYS   A HA   1 
ATOM   1355 H  HB2  A LYS   A 1 55  ? 21.346 11.750  6.557   0.78 13.77 ?  55  LYS   A HB2  1 
ATOM   1356 H  HB2  B LYS   A 1 55  ? 21.406 11.699  6.512   0.22 13.79 ?  55  LYS   A HB2  1 
ATOM   1357 H  HB3  A LYS   A 1 55  ? 20.708 10.702  7.560   0.78 13.77 ?  55  LYS   A HB3  1 
ATOM   1358 H  HB3  B LYS   A 1 55  ? 20.666 10.893  7.659   0.22 13.79 ?  55  LYS   A HB3  1 
ATOM   1359 H  HG2  A LYS   A 1 55  ? 20.269 12.383  9.080   0.78 15.14 ?  55  LYS   A HG2  1 
ATOM   1360 H  HG2  B LYS   A 1 55  ? 20.541 12.836  8.947   0.22 14.53 ?  55  LYS   A HG2  1 
ATOM   1361 H  HG3  A LYS   A 1 55  ? 20.976 13.447  8.126   0.78 15.14 ?  55  LYS   A HG3  1 
ATOM   1362 H  HG3  B LYS   A 1 55  ? 21.280 13.645  7.791   0.22 14.53 ?  55  LYS   A HG3  1 
ATOM   1363 H  HD2  A LYS   A 1 55  ? 19.322 13.111  6.517   0.78 16.67 ?  55  LYS   A HD2  1 
ATOM   1364 H  HD2  B LYS   A 1 55  ? 19.470 13.341  6.380   0.22 15.39 ?  55  LYS   A HD2  1 
ATOM   1365 H  HD3  A LYS   A 1 55  ? 18.627 12.023  7.446   0.78 16.67 ?  55  LYS   A HD3  1 
ATOM   1366 H  HD3  B LYS   A 1 55  ? 18.746 12.431  7.465   0.22 15.39 ?  55  LYS   A HD3  1 
ATOM   1367 H  HE2  A LYS   A 1 55  ? 18.129 13.703  9.003   0.78 18.34 ?  55  LYS   A HE2  1 
ATOM   1368 H  HE2  B LYS   A 1 55  ? 18.520 14.288  8.866   0.22 16.55 ?  55  LYS   A HE2  1 
ATOM   1369 H  HE3  A LYS   A 1 55  ? 18.771 14.780  8.023   0.78 18.34 ?  55  LYS   A HE3  1 
ATOM   1370 H  HE3  B LYS   A 1 55  ? 19.234 15.196  7.773   0.22 16.55 ?  55  LYS   A HE3  1 
ATOM   1371 H  HZ1  A LYS   A 1 55  ? 16.508 14.729  7.779   0.78 18.67 ?  55  LYS   A HZ1  1 
ATOM   1372 H  HZ1  B LYS   A 1 55  ? 16.913 15.342  7.745   0.22 16.93 ?  55  LYS   A HZ1  1 
ATOM   1373 H  HZ2  A LYS   A 1 55  ? 17.114 14.307  6.533   0.78 18.67 ?  55  LYS   A HZ2  1 
ATOM   1374 H  HZ2  B LYS   A 1 55  ? 17.453 14.988  6.449   0.22 16.93 ?  55  LYS   A HZ2  1 
ATOM   1375 H  HZ3  A LYS   A 1 55  ? 16.530 13.325  7.424   0.78 18.67 ?  55  LYS   A HZ3  1 
ATOM   1376 H  HZ3  B LYS   A 1 55  ? 16.839 13.972  7.281   0.22 16.93 ?  55  LYS   A HZ3  1 
ATOM   1377 N  N    . ALA   A 1 56  ? 22.169 9.787   9.990   1.00 11.28 ?  56  ALA   A N    1 
ATOM   1378 C  CA   . ALA   A 1 56  ? 22.050 9.465   11.406  1.00 12.36 ?  56  ALA   A CA   1 
ATOM   1379 C  C    . ALA   A 1 56  ? 23.392 9.492   12.128  1.00 12.12 ?  56  ALA   A C    1 
ATOM   1380 O  O    . ALA   A 1 56  ? 23.416 9.688   13.344  1.00 13.37 ?  56  ALA   A O    1 
ATOM   1381 C  CB   . ALA   A 1 56  ? 21.366 8.103   11.580  1.00 13.18 ?  56  ALA   A CB   1 
ATOM   1382 H  H    A ALA   A 1 56  ? 21.966 9.135   9.465   0.78 13.60 ?  56  ALA   A H    1 
ATOM   1383 H  H    B ALA   A 1 56  ? 21.987 9.131   9.463   0.22 13.60 ?  56  ALA   A H    1 
ATOM   1384 H  HA   . ALA   A 1 56  ? 21.484 10.119  11.830  1.00 14.88 ?  56  ALA   A HA   1 
ATOM   1385 H  HB1  . ALA   A 1 56  ? 21.283 7.906   12.529  1.00 15.88 ?  56  ALA   A HB1  1 
ATOM   1386 H  HB2  . ALA   A 1 56  ? 20.486 8.139   11.174  1.00 15.88 ?  56  ALA   A HB2  1 
ATOM   1387 H  HB3  . ALA   A 1 56  ? 21.901 7.418   11.149  1.00 15.88 ?  56  ALA   A HB3  1 
ATOM   1388 N  N    . THR   A 1 57  ? 24.502 9.301   11.410  1.00 11.05 ?  57  THR   A N    1 
ATOM   1389 C  CA   . THR   A 1 57  ? 25.845 9.434   11.980  1.00 11.20 ?  57  THR   A CA   1 
ATOM   1390 C  C    . THR   A 1 57  ? 26.395 10.854  11.892  1.00 11.72 ?  57  THR   A C    1 
ATOM   1391 O  O    . THR   A 1 57  ? 27.582 11.068  12.180  1.00 11.92 ?  57  THR   A O    1 
ATOM   1392 C  CB   . THR   A 1 57  ? 26.858 8.484   11.310  1.00 11.31 ?  57  THR   A CB   1 
ATOM   1393 O  OG1  . THR   A 1 57  ? 27.234 8.983   10.014  1.00 10.93 ?  57  THR   A OG1  1 
ATOM   1394 C  CG2  . THR   A 1 57  ? 26.332 7.069   11.208  1.00 11.24 ?  57  THR   A CG2  1 
ATOM   1395 H  H    . THR   A 1 57  ? 24.503 9.076   10.578  1.00 13.31 ?  57  THR   A H    1 
ATOM   1396 H  HA   . THR   A 1 57  ? 25.801 9.182   12.923  1.00 13.50 ?  57  THR   A HA   1 
ATOM   1397 H  HB   . THR   A 1 57  ? 27.658 8.447   11.868  1.00 13.63 ?  57  THR   A HB   1 
ATOM   1398 H  HG1  . THR   A 1 57  ? 26.555 9.043   9.527   1.00 13.17 ?  57  THR   A HG1  1 
ATOM   1399 H  HG21 . THR   A 1 57  ? 26.943 6.522   10.688  1.00 13.54 ?  57  THR   A HG21 1 
ATOM   1400 H  HG22 . THR   A 1 57  ? 26.242 6.680   12.093  1.00 13.54 ?  57  THR   A HG22 1 
ATOM   1401 H  HG23 . THR   A 1 57  ? 25.466 7.063   10.776  1.00 13.54 ?  57  THR   A HG23 1 
ATOM   1402 N  N    A ASN   A 1 58  ? 25.587 11.830  11.491  0.78 12.10 ?  58  ASN   A N    1 
ATOM   1403 N  N    B ASN   A 1 58  ? 25.563 11.817  11.503  0.22 11.49 ?  58  ASN   A N    1 
ATOM   1404 C  CA   A ASN   A 1 58  ? 26.068 13.210  11.409  0.78 13.18 ?  58  ASN   A CA   1 
ATOM   1405 C  CA   B ASN   A 1 58  ? 25.991 13.204  11.332  0.22 11.62 ?  58  ASN   A CA   1 
ATOM   1406 C  C    A ASN   A 1 58  ? 27.184 13.345  10.366  0.78 12.05 ?  58  ASN   A C    1 
ATOM   1407 C  C    B ASN   A 1 58  ? 27.194 13.298  10.394  0.22 11.15 ?  58  ASN   A C    1 
ATOM   1408 O  O    A ASN   A 1 58  ? 28.066 14.201  10.489  0.78 12.62 ?  58  ASN   A O    1 
ATOM   1409 O  O    B ASN   A 1 58  ? 28.139 14.055  10.626  0.22 11.36 ?  58  ASN   A O    1 
ATOM   1410 C  CB   A ASN   A 1 58  ? 26.501 13.713  12.804  0.78 15.44 ?  58  ASN   A CB   1 
ATOM   1411 C  CB   B ASN   A 1 58  ? 26.259 13.887  12.677  0.22 12.30 ?  58  ASN   A CB   1 
ATOM   1412 C  CG   A ASN   A 1 58  ? 26.957 15.176  12.820  0.78 16.96 ?  58  ASN   A CG   1 
ATOM   1413 C  CG   B ASN   A 1 58  ? 26.317 15.394  12.560  0.22 13.42 ?  58  ASN   A CG   1 
ATOM   1414 O  OD1  A ASN   A 1 58  ? 26.352 16.034  12.186  0.78 17.98 ?  58  ASN   A OD1  1 
ATOM   1415 O  OD1  B ASN   A 1 58  ? 25.614 15.990  11.737  0.22 13.77 ?  58  ASN   A OD1  1 
ATOM   1416 N  ND2  A ASN   A 1 58  ? 28.016 15.464  13.574  0.78 17.44 ?  58  ASN   A ND2  1 
ATOM   1417 N  ND2  B ASN   A 1 58  ? 27.164 16.021  13.378  0.22 14.16 ?  58  ASN   A ND2  1 
ATOM   1418 H  H    A ASN   A 1 58  ? 24.767 11.718  11.261  0.78 14.57 ?  58  ASN   A H    1 
ATOM   1419 H  H    B ASN   A 1 58  ? 24.732 11.685  11.326  0.22 13.84 ?  58  ASN   A H    1 
ATOM   1420 H  HA   A ASN   A 1 58  ? 25.331 13.764  11.119  0.78 15.87 ?  58  ASN   A HA   1 
ATOM   1421 H  HA   B ASN   A 1 58  ? 25.265 13.683  10.914  0.22 14.00 ?  58  ASN   A HA   1 
ATOM   1422 H  HB2  A ASN   A 1 58  ? 25.744 13.629  13.417  0.78 18.59 ?  58  ASN   A HB2  1 
ATOM   1423 H  HB2  B ASN   A 1 58  ? 25.546 13.669  13.294  0.22 14.81 ?  58  ASN   A HB2  1 
ATOM   1424 H  HB3  A ASN   A 1 58  ? 27.238 13.181  13.129  0.78 18.59 ?  58  ASN   A HB3  1 
ATOM   1425 H  HB3  B ASN   A 1 58  ? 27.110 13.575  13.028  0.22 14.81 ?  58  ASN   A HB3  1 
ATOM   1426 H  HD21 A ASN   A 1 58  ? 28.300 16.276  13.621  0.78 20.98 ?  58  ASN   A HD21 1 
ATOM   1427 H  HD21 B ASN   A 1 58  ? 27.250 16.876  13.347  0.22 17.05 ?  58  ASN   A HD21 1 
ATOM   1428 H  HD22 A ASN   A 1 58  ? 28.413 14.842  14.010  0.78 20.98 ?  58  ASN   A HD22 1 
ATOM   1429 H  HD22 B ASN   A 1 58  ? 27.639 15.566  13.939  0.22 17.05 ?  58  ASN   A HD22 1 
ATOM   1430 N  N    . ASN   A 1 59  ? 27.150 12.515  9.317   1.00 10.82 ?  59  ASN   A N    1 
ATOM   1431 C  CA   . ASN   A 1 59  ? 28.133 12.489  8.229   1.00 10.69 ?  59  ASN   A CA   1 
ATOM   1432 C  C    . ASN   A 1 59  ? 29.452 11.816  8.612   1.00 10.42 ?  59  ASN   A C    1 
ATOM   1433 O  O    . ASN   A 1 59  ? 30.367 11.772  7.782   1.00 10.57 ?  59  ASN   A O    1 
ATOM   1434 C  CB   . ASN   A 1 59  ? 28.407 13.876  7.617   1.00 11.04 ?  59  ASN   A CB   1 
ATOM   1435 C  CG   . ASN   A 1 59  ? 28.766 13.808  6.153   1.00 11.10 ?  59  ASN   A CG   1 
ATOM   1436 O  OD1  . ASN   A 1 59  ? 28.060 13.190  5.357   1.00 11.30 ?  59  ASN   A OD1  1 
ATOM   1437 N  ND2  . ASN   A 1 59  ? 29.854 14.469  5.779   1.00 11.51 ?  59  ASN   A ND2  1 
ATOM   1438 H  H    A ASN   A 1 59  ? 26.528 11.931  9.205   0.78 13.04 ?  59  ASN   A H    1 
ATOM   1439 H  H    B ASN   A 1 59  ? 26.514 11.951  9.184   0.22 13.04 ?  59  ASN   A H    1 
ATOM   1440 H  HA   . ASN   A 1 59  ? 27.752 11.954  7.520   1.00 12.89 ?  59  ASN   A HA   1 
ATOM   1441 H  HB2  . ASN   A 1 59  ? 27.611 14.426  7.694   1.00 13.30 ?  59  ASN   A HB2  1 
ATOM   1442 H  HB3  . ASN   A 1 59  ? 29.146 14.294  8.078   1.00 13.30 ?  59  ASN   A HB3  1 
ATOM   1443 H  HD21 . ASN   A 1 59  ? 30.105 14.464  4.956   1.00 13.86 ?  59  ASN   A HD21 1 
ATOM   1444 H  HD22 . ASN   A 1 59  ? 30.328 14.892  6.365   1.00 13.86 ?  59  ASN   A HD22 1 
ATOM   1445 N  N    . ALA   A 1 60  ? 29.580 11.268  9.820   1.00 10.30 ?  60  ALA   A N    1 
ATOM   1446 C  CA   . ALA   A 1 60  ? 30.821 10.585  10.170  1.00 10.40 ?  60  ALA   A CA   1 
ATOM   1447 C  C    . ALA   A 1 60  ? 31.044 9.352   9.303   1.00 10.54 ?  60  ALA   A C    1 
ATOM   1448 O  O    . ALA   A 1 60  ? 32.188 9.033   8.965   1.00 10.98 ?  60  ALA   A O    1 
ATOM   1449 C  CB   . ALA   A 1 60  ? 30.822 10.224  11.652  1.00 11.31 ?  60  ALA   A CB   1 
ATOM   1450 H  H    . ALA   A 1 60  ? 28.982 11.276  10.435  1.00 12.41 ?  60  ALA   A H    1 
ATOM   1451 H  HA   . ALA   A 1 60  ? 31.562 11.192  10.013  1.00 12.53 ?  60  ALA   A HA   1 
ATOM   1452 H  HB1  . ALA   A 1 60  ? 31.653 9.774   11.869  1.00 13.62 ?  60  ALA   A HB1  1 
ATOM   1453 H  HB2  . ALA   A 1 60  ? 30.743 11.040  12.177  1.00 13.62 ?  60  ALA   A HB2  1 
ATOM   1454 H  HB3  . ALA   A 1 60  ? 30.070 9.641   11.838  1.00 13.62 ?  60  ALA   A HB3  1 
ATOM   1455 N  N    . MET   A 1 61  ? 29.972 8.654   8.926   1.00 10.29 ?  61  MET   A N    1 
ATOM   1456 C  CA   . MET   A 1 61  ? 30.107 7.518   8.021   1.00 10.01 ?  61  MET   A CA   1 
ATOM   1457 C  C    . MET   A 1 61  ? 30.729 7.944   6.695   1.00 9.95  ?  61  MET   A C    1 
ATOM   1458 O  O    . MET   A 1 61  ? 31.618 7.261   6.170   1.00 10.32 ?  61  MET   A O    1 
ATOM   1459 C  CB   . MET   A 1 61  ? 28.743 6.853   7.819   1.00 9.86  ?  61  MET   A CB   1 
ATOM   1460 C  CG   . MET   A 1 61  ? 28.750 5.698   6.826   1.00 10.48 ?  61  MET   A CG   1 
ATOM   1461 S  SD   . MET   A 1 61  ? 27.123 4.939   6.645   1.00 11.50 ?  61  MET   A SD   1 
ATOM   1462 C  CE   . MET   A 1 61  ? 27.007 4.048   8.202   1.00 12.85 ?  61  MET   A CE   1 
ATOM   1463 H  H    . MET   A 1 61  ? 29.165 8.823   9.174   1.00 12.41 ?  61  MET   A H    1 
ATOM   1464 H  HA   . MET   A 1 61  ? 30.688 6.865   8.438   1.00 12.06 ?  61  MET   A HA   1 
ATOM   1465 H  HB2  . MET   A 1 61  ? 28.440 6.499   8.671   1.00 11.89 ?  61  MET   A HB2  1 
ATOM   1466 H  HB3  . MET   A 1 61  ? 28.115 7.512   7.496   1.00 11.89 ?  61  MET   A HB3  1 
ATOM   1467 H  HG2  . MET   A 1 61  ? 29.012 6.024   5.952   1.00 12.63 ?  61  MET   A HG2  1 
ATOM   1468 H  HG3  . MET   A 1 61  ? 29.363 5.014   7.128   1.00 12.63 ?  61  MET   A HG3  1 
ATOM   1469 H  HE1  . MET   A 1 61  ? 26.173 3.551   8.226   1.00 15.48 ?  61  MET   A HE1  1 
ATOM   1470 H  HE2  . MET   A 1 61  ? 27.757 3.434   8.273   1.00 15.48 ?  61  MET   A HE2  1 
ATOM   1471 H  HE3  . MET   A 1 61  ? 27.033 4.683   8.936   1.00 15.48 ?  61  MET   A HE3  1 
ATOM   1472 N  N    . GLN   A 1 62  ? 30.279 9.074   6.141   1.00 9.90  ?  62  GLN   A N    1 
ATOM   1473 C  CA   . GLN   A 1 62  ? 30.838 9.547   4.879   1.00 10.11 ?  62  GLN   A CA   1 
ATOM   1474 C  C    . GLN   A 1 62  ? 32.311 9.922   5.018   1.00 10.08 ?  62  GLN   A C    1 
ATOM   1475 O  O    . GLN   A 1 62  ? 33.116 9.616   4.132   1.00 10.69 ?  62  GLN   A O    1 
ATOM   1476 C  CB   . GLN   A 1 62  ? 30.033 10.732  4.350   1.00 10.40 ?  62  GLN   A CB   1 
ATOM   1477 C  CG   . GLN   A 1 62  ? 30.401 11.097  2.920   1.00 10.11 ?  62  GLN   A CG   1 
ATOM   1478 C  CD   . GLN   A 1 62  ? 30.069 9.968   1.971   1.00 10.41 ?  62  GLN   A CD   1 
ATOM   1479 O  OE1  . GLN   A 1 62  ? 28.888 9.659   1.771   1.00 11.09 ?  62  GLN   A OE1  1 
ATOM   1480 N  NE2  . GLN   A 1 62  ? 31.082 9.297   1.441   1.00 11.05 ?  62  GLN   A NE2  1 
ATOM   1481 H  H    . GLN   A 1 62  ? 29.664 9.571   6.475   1.00 11.94 ?  62  GLN   A H    1 
ATOM   1482 H  HA   . GLN   A 1 62  ? 30.781 8.829   4.231   1.00 12.19 ?  62  GLN   A HA   1 
ATOM   1483 H  HB2  . GLN   A 1 62  ? 29.089 10.511  4.372   1.00 12.54 ?  62  GLN   A HB2  1 
ATOM   1484 H  HB3  . GLN   A 1 62  ? 30.205 11.507  4.911   1.00 12.54 ?  62  GLN   A HB3  1 
ATOM   1485 H  HG2  . GLN   A 1 62  ? 29.892 11.877  2.649   1.00 12.18 ?  62  GLN   A HG2  1 
ATOM   1486 H  HG3  . GLN   A 1 62  ? 31.351 11.274  2.864   1.00 12.18 ?  62  GLN   A HG3  1 
ATOM   1487 H  HE21 . GLN   A 1 62  ? 31.890 9.528   1.617   1.00 13.31 ?  62  GLN   A HE21 1 
ATOM   1488 H  HE22 . GLN   A 1 62  ? 30.927 8.639   0.909   1.00 13.31 ?  62  GLN   A HE22 1 
ATOM   1489 N  N    . VAL   A 1 63  ? 32.676 10.605  6.106   1.00 10.65 ?  63  VAL   A N    1 
ATOM   1490 C  CA   . VAL   A 1 63  ? 34.068 11.001  6.305   1.00 11.61 ?  63  VAL   A CA   1 
ATOM   1491 C  C    . VAL   A 1 63  ? 34.966 9.769   6.366   1.00 11.03 ?  63  VAL   A C    1 
ATOM   1492 O  O    . VAL   A 1 63  ? 36.013 9.701   5.707   1.00 11.44 ?  63  VAL   A O    1 
ATOM   1493 C  CB   . VAL   A 1 63  ? 34.187 11.882  7.562   1.00 12.99 ?  63  VAL   A CB   1 
ATOM   1494 C  CG1  . VAL   A 1 63  ? 35.637 12.137  7.903   1.00 15.21 ?  63  VAL   A CG1  1 
ATOM   1495 C  CG2  . VAL   A 1 63  ? 33.454 13.204  7.347   1.00 13.30 ?  63  VAL   A CG2  1 
ATOM   1496 H  H    . VAL   A 1 63  ? 32.136 10.847  6.739   1.00 12.83 ?  63  VAL   A H    1 
ATOM   1497 H  HA   . VAL   A 1 63  ? 34.343 11.533  5.546   1.00 13.99 ?  63  VAL   A HA   1 
ATOM   1498 H  HB   . VAL   A 1 63  ? 33.779 11.423  8.315   1.00 15.65 ?  63  VAL   A HB   1 
ATOM   1499 H  HG11 . VAL   A 1 63  ? 35.686 12.872  8.530   1.00 18.31 ?  63  VAL   A HG11 1 
ATOM   1500 H  HG12 . VAL   A 1 63  ? 36.018 11.337  8.296   1.00 18.31 ?  63  VAL   A HG12 1 
ATOM   1501 H  HG13 . VAL   A 1 63  ? 36.113 12.366  7.087   1.00 18.31 ?  63  VAL   A HG13 1 
ATOM   1502 H  HG21 . VAL   A 1 63  ? 33.550 13.754  8.142   1.00 16.01 ?  63  VAL   A HG21 1 
ATOM   1503 H  HG22 . VAL   A 1 63  ? 33.841 13.662  6.583   1.00 16.01 ?  63  VAL   A HG22 1 
ATOM   1504 H  HG23 . VAL   A 1 63  ? 32.515 13.025  7.183   1.00 16.01 ?  63  VAL   A HG23 1 
ATOM   1505 N  N    . GLU   A 1 64  ? 34.550 8.765   7.139   1.00 10.88 ?  64  GLU   A N    1 
ATOM   1506 C  CA   . GLU   A 1 64  ? 35.308 7.522   7.233   1.00 10.93 ?  64  GLU   A CA   1 
ATOM   1507 C  C    . GLU   A 1 64  ? 35.394 6.832   5.880   1.00 10.57 ?  64  GLU   A C    1 
ATOM   1508 O  O    . GLU   A 1 64  ? 36.446 6.289   5.504   1.00 10.96 ?  64  GLU   A O    1 
ATOM   1509 C  CB   . GLU   A 1 64  ? 34.624 6.614   8.251   1.00 11.29 ?  64  GLU   A CB   1 
ATOM   1510 C  CG   . GLU   A 1 64  ? 35.283 5.268   8.417   1.00 12.00 ?  64  GLU   A CG   1 
ATOM   1511 C  CD   . GLU   A 1 64  ? 34.400 4.272   9.143   1.00 12.64 ?  64  GLU   A CD   1 
ATOM   1512 O  OE1  . GLU   A 1 64  ? 33.156 4.369   9.010   1.00 13.61 ?  64  GLU   A OE1  1 
ATOM   1513 O  OE2  . GLU   A 1 64  ? 34.945 3.378   9.831   1.00 12.75 -1 64  GLU   A OE2  1 
ATOM   1514 H  H    . GLU   A 1 64  ? 33.828 8.773   7.606   1.00 13.12 ?  64  GLU   A H    1 
ATOM   1515 H  HA   . GLU   A 1 64  ? 36.208 7.720   7.540   1.00 13.18 ?  64  GLU   A HA   1 
ATOM   1516 H  HB2  . GLU   A 1 64  ? 34.638 7.063   9.116   1.00 13.61 ?  64  GLU   A HB2  1 
ATOM   1517 H  HB3  . GLU   A 1 64  ? 33.709 6.477   7.970   1.00 13.61 ?  64  GLU   A HB3  1 
ATOM   1518 H  HG2  . GLU   A 1 64  ? 35.492 4.897   7.542   1.00 14.45 ?  64  GLU   A HG2  1 
ATOM   1519 H  HG3  . GLU   A 1 64  ? 36.097 5.376   8.929   1.00 14.45 ?  64  GLU   A HG3  1 
ATOM   1520 N  N    . SER   A 1 65  ? 34.277 6.824   5.148   1.00 10.11 ?  65  SER   A N    1 
ATOM   1521 C  CA   . SER   A 1 65  ? 34.221 6.160   3.852   1.00 10.12 ?  65  SER   A CA   1 
ATOM   1522 C  C    . SER   A 1 65  ? 35.141 6.829   2.841   1.00 10.48 ?  65  SER   A C    1 
ATOM   1523 O  O    . SER   A 1 65  ? 35.773 6.149   2.025   1.00 11.30 ?  65  SER   A O    1 
ATOM   1524 C  CB   . SER   A 1 65  ? 32.784 6.174   3.328   1.00 10.03 ?  65  SER   A CB   1 
ATOM   1525 O  OG   . SER   A 1 65  ? 31.934 5.355   4.123   1.00 10.80 ?  65  SER   A OG   1 
ATOM   1526 H  H    . SER   A 1 65  ? 33.542 7.201   5.381   1.00 12.19 ?  65  SER   A H    1 
ATOM   1527 H  HA   . SER   A 1 65  ? 34.501 5.236   3.949   1.00 12.20 ?  65  SER   A HA   1 
ATOM   1528 H  HB2  . SER   A 1 65  ? 32.454 7.084   3.343   1.00 12.10 ?  65  SER   A HB2  1 
ATOM   1529 H  HB3  . SER   A 1 65  ? 32.782 5.838   2.417   1.00 12.10 ?  65  SER   A HB3  1 
ATOM   1530 H  HG   . SER   A 1 65  ? 31.928 5.640   4.918   1.00 13.02 ?  65  SER   A HG   1 
ATOM   1531 N  N    . ASP   A 1 66  ? 35.215 8.162   2.861   1.00 10.57 ?  66  ASP   A N    1 
ATOM   1532 C  CA   . ASP   A 1 66  ? 36.069 8.866   1.910   1.00 11.64 ?  66  ASP   A CA   1 
ATOM   1533 C  C    . ASP   A 1 66  ? 37.535 8.512   2.136   1.00 11.46 ?  66  ASP   A C    1 
ATOM   1534 O  O    . ASP   A 1 66  ? 38.300 8.339   1.177   1.00 12.37 ?  66  ASP   A O    1 
ATOM   1535 C  CB   . ASP   A 1 66  ? 35.850 10.372  2.025   1.00 12.56 ?  66  ASP   A CB   1 
ATOM   1536 C  CG   . ASP   A 1 66  ? 34.513 10.836  1.431   1.00 14.18 ?  66  ASP   A CG   1 
ATOM   1537 O  OD1  . ASP   A 1 66  ? 33.787 10.042  0.790   1.00 14.37 ?  66  ASP   A OD1  1 
ATOM   1538 O  OD2  . ASP   A 1 66  ? 34.209 12.037  1.593   1.00 16.95 -1 66  ASP   A OD2  1 
ATOM   1539 H  H    . ASP   A 1 66  ? 34.778 8.674   3.402   1.00 12.74 ?  66  ASP   A H    1 
ATOM   1540 H  HA   . ASP   A 1 66  ? 35.828 8.598   1.010   1.00 14.02 ?  66  ASP   A HA   1 
ATOM   1541 H  HB2  . ASP   A 1 66  ? 35.860 10.621  2.963   1.00 15.13 ?  66  ASP   A HB2  1 
ATOM   1542 H  HB3  . ASP   A 1 66  ? 36.566 10.829  1.555   1.00 15.13 ?  66  ASP   A HB3  1 
ATOM   1543 N  N    . ASP   A 1 67  ? 37.942 8.382   3.400   1.00 11.76 ?  67  ASP   A N    1 
ATOM   1544 C  CA   . ASP   A 1 67  ? 39.297 7.931   3.694   1.00 12.39 ?  67  ASP   A CA   1 
ATOM   1545 C  C    . ASP   A 1 67  ? 39.512 6.496   3.227   1.00 12.38 ?  67  ASP   A C    1 
ATOM   1546 O  O    . ASP   A 1 67  ? 40.566 6.168   2.674   1.00 13.04 ?  67  ASP   A O    1 
ATOM   1547 C  CB   . ASP   A 1 67  ? 39.571 8.062   5.189   1.00 13.80 ?  67  ASP   A CB   1 
ATOM   1548 C  CG   . ASP   A 1 67  ? 40.866 7.399   5.602   1.00 15.01 ?  67  ASP   A CG   1 
ATOM   1549 O  OD1  . ASP   A 1 67  ? 41.945 8.025   5.453   1.00 17.77 ?  67  ASP   A OD1  1 
ATOM   1550 O  OD2  . ASP   A 1 67  ? 40.809 6.240   6.072   1.00 14.76 -1 67  ASP   A OD2  1 
ATOM   1551 H  H    . ASP   A 1 67  ? 37.462 8.553   4.089   1.00 14.17 ?  67  ASP   A H    1 
ATOM   1552 H  HA   . ASP   A 1 67  ? 39.926 8.495   3.217   1.00 14.92 ?  67  ASP   A HA   1 
ATOM   1553 H  HB2  . ASP   A 1 67  ? 39.626 8.999   5.412   1.00 16.61 ?  67  ASP   A HB2  1 
ATOM   1554 H  HB3  . ASP   A 1 67  ? 38.850 7.637   5.675   1.00 16.61 ?  67  ASP   A HB3  1 
ATOM   1555 N  N    . TYR   A 1 68  ? 38.517 5.622   3.429   1.00 11.81 ?  68  TYR   A N    1 
ATOM   1556 C  CA   . TYR   A 1 68  ? 38.631 4.243   2.953   1.00 12.18 ?  68  TYR   A CA   1 
ATOM   1557 C  C    . TYR   A 1 68  ? 38.870 4.191   1.443   1.00 11.70 ?  68  TYR   A C    1 
ATOM   1558 O  O    . TYR   A 1 68  ? 39.750 3.459   0.968   1.00 12.36 ?  68  TYR   A O    1 
ATOM   1559 C  CB   . TYR   A 1 68  ? 37.381 3.420   3.336   1.00 12.50 ?  68  TYR   A CB   1 
ATOM   1560 C  CG   . TYR   A 1 68  ? 37.404 2.034   2.708   1.00 13.65 ?  68  TYR   A CG   1 
ATOM   1561 C  CD1  . TYR   A 1 68  ? 36.948 1.840   1.407   1.00 14.84 ?  68  TYR   A CD1  1 
ATOM   1562 C  CD2  . TYR   A 1 68  ? 37.940 0.948   3.378   1.00 15.36 ?  68  TYR   A CD2  1 
ATOM   1563 C  CE1  . TYR   A 1 68  ? 37.011 0.621   0.793   1.00 16.39 ?  68  TYR   A CE1  1 
ATOM   1564 C  CE2  . TYR   A 1 68  ? 38.003 -0.311  2.762   1.00 16.00 ?  68  TYR   A CE2  1 
ATOM   1565 C  CZ   . TYR   A 1 68  ? 37.545 -0.447  1.470   1.00 16.39 ?  68  TYR   A CZ   1 
ATOM   1566 O  OH   . TYR   A 1 68  ? 37.626 -1.662  0.843   1.00 17.49 ?  68  TYR   A OH   1 
ATOM   1567 H  H    . TYR   A 1 68  ? 37.774 5.800   3.829   1.00 14.23 ?  68  TYR   A H    1 
ATOM   1568 H  HA   . TYR   A 1 68  ? 39.392 3.831   3.385   1.00 14.67 ?  68  TYR   A HA   1 
ATOM   1569 H  HB2  . TYR   A 1 68  ? 37.353 3.313   4.298   1.00 15.05 ?  68  TYR   A HB2  1 
ATOM   1570 H  HB3  . TYR   A 1 68  ? 36.587 3.881   3.023   1.00 15.05 ?  68  TYR   A HB3  1 
ATOM   1571 H  HD1  . TYR   A 1 68  ? 36.603 2.568   0.936   1.00 17.86 ?  68  TYR   A HD1  1 
ATOM   1572 H  HD2  . TYR   A 1 68  ? 38.269 1.056   4.239   1.00 18.49 ?  68  TYR   A HD2  1 
ATOM   1573 H  HE1  . TYR   A 1 68  ? 36.696 0.519   -0.077  1.00 19.73 ?  68  TYR   A HE1  1 
ATOM   1574 H  HE2  . TYR   A 1 68  ? 38.365 -1.040  3.207   1.00 19.25 ?  68  TYR   A HE2  1 
ATOM   1575 H  HH   . TYR   A 1 68  ? 37.953 -2.231  1.371   1.00 21.04 ?  68  TYR   A HH   1 
ATOM   1576 N  N    . ILE   A 1 69  ? 38.081 4.948   0.671   1.00 11.41 ?  69  ILE   A N    1 
ATOM   1577 C  CA   . ILE   A 1 69  ? 38.216 4.941   -0.785  1.00 11.34 ?  69  ILE   A CA   1 
ATOM   1578 C  C    . ILE   A 1 69  ? 39.551 5.550   -1.213  1.00 11.26 ?  69  ILE   A C    1 
ATOM   1579 O  O    . ILE   A 1 69  ? 40.198 5.065   -2.149  1.00 11.76 ?  69  ILE   A O    1 
ATOM   1580 C  CB   . ILE   A 1 69  ? 37.016 5.654   -1.442  1.00 12.14 ?  69  ILE   A CB   1 
ATOM   1581 C  CG1  . ILE   A 1 69  ? 35.702 4.919   -1.164  1.00 12.83 ?  69  ILE   A CG1  1 
ATOM   1582 C  CG2  . ILE   A 1 69  ? 37.247 5.851   -2.947  1.00 13.36 ?  69  ILE   A CG2  1 
ATOM   1583 C  CD1  . ILE   A 1 69  ? 35.540 3.628   -1.935  1.00 13.65 ?  69  ILE   A CD1  1 
ATOM   1584 H  H    . ILE   A 1 69  ? 37.472 5.472   0.968   1.00 13.75 ?  69  ILE   A H    1 
ATOM   1585 H  HA   . ILE   A 1 69  ? 38.211 4.019   -1.085  1.00 13.67 ?  69  ILE   A HA   1 
ATOM   1586 H  HB   . ILE   A 1 69  ? 36.947 6.530   -1.041  1.00 14.63 ?  69  ILE   A HB   1 
ATOM   1587 H  HG12 . ILE   A 1 69  ? 35.660 4.704   -0.218  1.00 15.45 ?  69  ILE   A HG12 1 
ATOM   1588 H  HG13 . ILE   A 1 69  ? 34.966 5.500   -1.401  1.00 15.45 ?  69  ILE   A HG13 1 
ATOM   1589 H  HG21 . ILE   A 1 69  ? 36.402 6.073   -3.369  1.00 16.09 ?  69  ILE   A HG21 1 
ATOM   1590 H  HG22 . ILE   A 1 69  ? 37.878 6.581   -3.079  1.00 16.09 ?  69  ILE   A HG22 1 
ATOM   1591 H  HG23 . ILE   A 1 69  ? 37.602 5.035   -3.328  1.00 16.09 ?  69  ILE   A HG23 1 
ATOM   1592 H  HD11 . ILE   A 1 69  ? 34.741 3.177   -1.623  1.00 16.44 ?  69  ILE   A HD11 1 
ATOM   1593 H  HD12 . ILE   A 1 69  ? 35.455 3.832   -2.880  1.00 16.44 ?  69  ILE   A HD12 1 
ATOM   1594 H  HD13 . ILE   A 1 69  ? 36.316 3.067   -1.785  1.00 16.44 ?  69  ILE   A HD13 1 
ATOM   1595 N  N    . ALA   A 1 70  ? 39.971 6.633   -0.557  1.00 11.74 ?  70  ALA   A N    1 
ATOM   1596 C  CA   . ALA   A 1 70  ? 41.250 7.238   -0.912  1.00 12.69 ?  70  ALA   A CA   1 
ATOM   1597 C  C    . ALA   A 1 70  ? 42.397 6.251   -0.744  1.00 13.08 ?  70  ALA   A C    1 
ATOM   1598 O  O    . ALA   A 1 70  ? 43.365 6.285   -1.509  1.00 14.92 ?  70  ALA   A O    1 
ATOM   1599 C  CB   . ALA   A 1 70  ? 41.498 8.482   -0.059  1.00 13.17 ?  70  ALA   A CB   1 
ATOM   1600 H  H    . ALA   A 1 70  ? 39.542 7.028   0.075   1.00 14.15 ?  70  ALA   A H    1 
ATOM   1601 H  HA   . ALA   A 1 70  ? 41.220 7.520   -1.841  1.00 15.29 ?  70  ALA   A HA   1 
ATOM   1602 H  HB1  . ALA   A 1 70  ? 42.357 8.869   -0.310  1.00 15.85 ?  70  ALA   A HB1  1 
ATOM   1603 H  HB2  . ALA   A 1 70  ? 40.791 9.124   -0.212  1.00 15.85 ?  70  ALA   A HB2  1 
ATOM   1604 H  HB3  . ALA   A 1 70  ? 41.519 8.224   0.877   1.00 15.85 ?  70  ALA   A HB3  1 
ATOM   1605 N  N    . THR   A 1 71  ? 42.293 5.353   0.236   1.00 12.50 ?  71  THR   A N    1 
ATOM   1606 C  CA   . THR   A 1 71  ? 43.345 4.374   0.486   1.00 13.91 ?  71  THR   A CA   1 
ATOM   1607 C  C    . THR   A 1 71  ? 43.225 3.152   -0.414  1.00 14.05 ?  71  THR   A C    1 
ATOM   1608 O  O    . THR   A 1 71  ? 44.239 2.644   -0.914  1.00 15.78 ?  71  THR   A O    1 
ATOM   1609 C  CB   . THR   A 1 71  ? 43.276 3.922   1.942   1.00 15.55 ?  71  THR   A CB   1 
ATOM   1610 O  OG1  . THR   A 1 71  ? 43.519 5.047   2.794   1.00 16.70 ?  71  THR   A OG1  1 
ATOM   1611 C  CG2  . THR   A 1 71  ? 44.291 2.819   2.232   1.00 17.04 ?  71  THR   A CG2  1 
ATOM   1612 H  H    . THR   A 1 71  ? 41.620 5.287   0.762   1.00 15.06 ?  71  THR   A H    1 
ATOM   1613 H  HA   . THR   A 1 71  ? 44.210 4.781   0.329   1.00 16.74 ?  71  THR   A HA   1 
ATOM   1614 H  HB   . THR   A 1 71  ? 42.388 3.561   2.117   1.00 18.72 ?  71  THR   A HB   1 
ATOM   1615 H  HG1  . THR   A 1 71  ? 43.472 4.797   3.596   1.00 20.10 ?  71  THR   A HG1  1 
ATOM   1616 H  HG21 . THR   A 1 71  ? 44.418 2.734   3.190   1.00 20.51 ?  71  THR   A HG21 1 
ATOM   1617 H  HG22 . THR   A 1 71  ? 43.983 1.970   1.880   1.00 20.51 ?  71  THR   A HG22 1 
ATOM   1618 H  HG23 . THR   A 1 71  ? 45.145 3.040   1.824   1.00 20.51 ?  71  THR   A HG23 1 
ATOM   1619 N  N    . ASN   A 1 72  ? 41.999 2.650   -0.608  1.00 13.24 ?  72  ASN   A N    1 
ATOM   1620 C  CA   . ASN   A 1 72  ? 41.778 1.322   -1.161  1.00 13.40 ?  72  ASN   A CA   1 
ATOM   1621 C  C    . ASN   A 1 72  ? 41.153 1.307   -2.542  1.00 13.70 ?  72  ASN   A C    1 
ATOM   1622 O  O    . ASN   A 1 72  ? 41.159 0.249   -3.185  1.00 14.74 ?  72  ASN   A O    1 
ATOM   1623 C  CB   . ASN   A 1 72  ? 40.887 0.510   -0.214  1.00 14.18 ?  72  ASN   A CB   1 
ATOM   1624 C  CG   . ASN   A 1 72  ? 41.510 0.348   1.152   1.00 15.38 ?  72  ASN   A CG   1 
ATOM   1625 O  OD1  . ASN   A 1 72  ? 41.069 0.954   2.129   1.00 16.97 ?  72  ASN   A OD1  1 
ATOM   1626 N  ND2  . ASN   A 1 72  ? 42.553 -0.447  1.224   1.00 15.70 ?  72  ASN   A ND2  1 
ATOM   1627 H  H    . ASN   A 1 72  ? 41.272 3.077   -0.431  1.00 15.94 ?  72  ASN   A H    1 
ATOM   1628 H  HA   . ASN   A 1 72  ? 42.630 0.870   -1.227  1.00 16.14 ?  72  ASN   A HA   1 
ATOM   1629 H  HB2  . ASN   A 1 72  ? 40.037 0.965   -0.111  1.00 17.08 ?  72  ASN   A HB2  1 
ATOM   1630 H  HB3  . ASN   A 1 72  ? 40.752 -0.373  -0.589  1.00 17.08 ?  72  ASN   A HB3  1 
ATOM   1631 H  HD21 . ASN   A 1 72  ? 42.945 -0.566  1.980   1.00 18.90 ?  72  ASN   A HD21 1 
ATOM   1632 H  HD22 . ASN   A 1 72  ? 42.840 -0.845  0.521   1.00 18.90 ?  72  ASN   A HD22 1 
ATOM   1633 N  N    . GLY   A 1 73  ? 40.607 2.423   -3.009  1.00 13.17 ?  73  GLY   A N    1 
ATOM   1634 C  CA   . GLY   A 1 73  ? 39.865 2.431   -4.242  1.00 12.81 ?  73  GLY   A CA   1 
ATOM   1635 C  C    . GLY   A 1 73  ? 38.471 1.856   -4.067  1.00 12.12 ?  73  GLY   A C    1 
ATOM   1636 O  O    . GLY   A 1 73  ? 38.086 1.397   -2.985  1.00 12.91 ?  73  GLY   A O    1 
ATOM   1637 H  H    . GLY   A 1 73  ? 40.662 3.198   -2.630  1.00 15.86 ?  73  GLY   A H    1 
ATOM   1638 H  HA2  . GLY   A 1 73  ? 39.791 3.345   -4.569  1.00 15.42 ?  73  GLY   A HA2  1 
ATOM   1639 H  HA3  . GLY   A 1 73  ? 40.339 1.909   -4.912  1.00 15.42 ?  73  GLY   A HA3  1 
ATOM   1640 N  N    . PRO   A 1 74  ? 37.691 1.878   -5.147  1.00 12.42 ?  74  PRO   A N    1 
ATOM   1641 C  CA   . PRO   A 1 74  ? 36.294 1.444   -5.067  1.00 12.65 ?  74  PRO   A CA   1 
ATOM   1642 C  C    . PRO   A 1 74  ? 36.147 -0.037  -4.747  1.00 12.21 ?  74  PRO   A C    1 
ATOM   1643 O  O    . PRO   A 1 74  ? 37.018 -0.868  -5.026  1.00 13.01 ?  74  PRO   A O    1 
ATOM   1644 C  CB   . PRO   A 1 74  ? 35.747 1.747   -6.468  1.00 14.37 ?  74  PRO   A CB   1 
ATOM   1645 C  CG   . PRO   A 1 74  ? 36.692 2.741   -7.062  1.00 17.08 ?  74  PRO   A CG   1 
ATOM   1646 C  CD   . PRO   A 1 74  ? 38.031 2.399   -6.481  1.00 14.63 ?  74  PRO   A CD   1 
ATOM   1647 H  HA   . PRO   A 1 74  ? 35.809 1.970   -4.408  1.00 15.24 ?  74  PRO   A HA   1 
ATOM   1648 H  HB2  . PRO   A 1 74  ? 35.727 0.930   -6.990  1.00 17.30 ?  74  PRO   A HB2  1 
ATOM   1649 H  HB3  . PRO   A 1 74  ? 34.853 2.124   -6.393  1.00 17.30 ?  74  PRO   A HB3  1 
ATOM   1650 H  HG2  . PRO   A 1 74  ? 36.706 2.645   -8.026  1.00 20.55 ?  74  PRO   A HG2  1 
ATOM   1651 H  HG3  . PRO   A 1 74  ? 36.430 3.637   -6.808  1.00 20.55 ?  74  PRO   A HG3  1 
ATOM   1652 H  HD2  . PRO   A 1 74  ? 38.472 1.716   -7.013  1.00 17.61 ?  74  PRO   A HD2  1 
ATOM   1653 H  HD3  . PRO   A 1 74  ? 38.579 3.201   -6.414  1.00 17.61 ?  74  PRO   A HD3  1 
ATOM   1654 N  N    . LEU   A 1 75  ? 35.001 -0.358  -4.158  1.00 11.41 ?  75  LEU   A N    1 
ATOM   1655 C  CA   . LEU   A 1 75  ? 34.598 -1.748  -4.008  1.00 11.13 ?  75  LEU   A CA   1 
ATOM   1656 C  C    . LEU   A 1 75  ? 34.206 -2.323  -5.367  1.00 11.80 ?  75  LEU   A C    1 
ATOM   1657 O  O    . LEU   A 1 75  ? 34.076 -1.606  -6.363  1.00 12.97 ?  75  LEU   A O    1 
ATOM   1658 C  CB   . LEU   A 1 75  ? 33.419 -1.875  -3.041  1.00 11.36 ?  75  LEU   A CB   1 
ATOM   1659 C  CG   . LEU   A 1 75  ? 33.632 -1.447  -1.591  1.00 13.02 ?  75  LEU   A CG   1 
ATOM   1660 C  CD1  . LEU   A 1 75  ? 32.344 -1.614  -0.794  1.00 15.07 ?  75  LEU   A CD1  1 
ATOM   1661 C  CD2  . LEU   A 1 75  ? 34.772 -2.172  -0.923  1.00 16.02 ?  75  LEU   A CD2  1 
ATOM   1662 H  H    . LEU   A 1 75  ? 34.439 0.209   -3.841  1.00 13.75 ?  75  LEU   A H    1 
ATOM   1663 H  HA   . LEU   A 1 75  ? 35.342 -2.263  -3.665  1.00 13.41 ?  75  LEU   A HA   1 
ATOM   1664 H  HB2  . LEU   A 1 75  ? 32.692 -1.342  -3.387  1.00 13.69 ?  75  LEU   A HB2  1 
ATOM   1665 H  HB3  . LEU   A 1 75  ? 33.153 -2.807  -3.022  1.00 13.69 ?  75  LEU   A HB3  1 
ATOM   1666 H  HG   . LEU   A 1 75  ? 33.860 -0.504  -1.585  1.00 15.68 ?  75  LEU   A HG   1 
ATOM   1667 H  HD11 . LEU   A 1 75  ? 32.504 -1.333  0.120   1.00 18.14 ?  75  LEU   A HD11 1 
ATOM   1668 H  HD12 . LEU   A 1 75  ? 31.660 -1.056  -1.197  1.00 18.14 ?  75  LEU   A HD12 1 
ATOM   1669 H  HD13 . LEU   A 1 75  ? 32.079 -2.542  -0.819  1.00 18.14 ?  75  LEU   A HD13 1 
ATOM   1670 H  HD21 . LEU   A 1 75  ? 34.836 -1.882  0.001   1.00 19.28 ?  75  LEU   A HD21 1 
ATOM   1671 H  HD22 . LEU   A 1 75  ? 34.608 -3.126  -0.960  1.00 19.28 ?  75  LEU   A HD22 1 
ATOM   1672 H  HD23 . LEU   A 1 75  ? 35.601 -1.963  -1.389  1.00 19.28 ?  75  LEU   A HD23 1 
ATOM   1673 N  N    . LYS   A 1 76  ? 34.021 -3.643  -5.390  1.00 12.23 ?  76  LYS   A N    1 
ATOM   1674 C  CA   . LYS   A 1 76  ? 33.413 -4.355  -6.509  1.00 12.85 ?  76  LYS   A CA   1 
ATOM   1675 C  C    . LYS   A 1 76  ? 31.902 -4.439  -6.304  1.00 11.22 ?  76  LYS   A C    1 
ATOM   1676 O  O    . LYS   A 1 76  ? 31.428 -4.564  -5.179  1.00 11.18 ?  76  LYS   A O    1 
ATOM   1677 C  CB   . LYS   A 1 76  ? 33.952 -5.798  -6.575  1.00 14.67 ?  76  LYS   A CB   1 
ATOM   1678 C  CG   . LYS   A 1 76  ? 35.461 -5.912  -6.776  1.00 16.00 ?  76  LYS   A CG   1 
ATOM   1679 C  CD   . LYS   A 1 76  ? 35.981 -7.316  -6.567  1.00 17.36 ?  76  LYS   A CD   1 
ATOM   1680 C  CE   . LYS   A 1 76  ? 37.476 -7.376  -6.791  1.00 20.04 ?  76  LYS   A CE   1 
ATOM   1681 N  NZ   . LYS   A 1 76  ? 38.028 -8.723  -6.546  1.00 20.93 ?  76  LYS   A NZ   1 
ATOM   1682 H  H    . LYS   A 1 76  ? 34.250 -4.165  -4.743  1.00 14.74 ?  76  LYS   A H    1 
ATOM   1683 H  HA   . LYS   A 1 76  ? 33.603 -3.901  -7.345  1.00 15.47 ?  76  LYS   A HA   1 
ATOM   1684 H  HB2  . LYS   A 1 76  ? 33.730 -6.248  -5.746  1.00 17.66 ?  76  LYS   A HB2  1 
ATOM   1685 H  HB3  . LYS   A 1 76  ? 33.522 -6.252  -7.317  1.00 17.66 ?  76  LYS   A HB3  1 
ATOM   1686 H  HG2  . LYS   A 1 76  ? 35.679 -5.643  -7.682  1.00 19.26 ?  76  LYS   A HG2  1 
ATOM   1687 H  HG3  . LYS   A 1 76  ? 35.908 -5.330  -6.141  1.00 19.26 ?  76  LYS   A HG3  1 
ATOM   1688 H  HD2  . LYS   A 1 76  ? 35.794 -7.598  -5.657  1.00 20.89 ?  76  LYS   A HD2  1 
ATOM   1689 H  HD3  . LYS   A 1 76  ? 35.551 -7.917  -7.199  1.00 20.89 ?  76  LYS   A HD3  1 
ATOM   1690 H  HE2  . LYS   A 1 76  ? 37.668 -7.133  -7.709  1.00 24.10 ?  76  LYS   A HE2  1 
ATOM   1691 H  HE3  . LYS   A 1 76  ? 37.910 -6.758  -6.183  1.00 24.10 ?  76  LYS   A HE3  1 
ATOM   1692 H  HZ1  . LYS   A 1 76  ? 38.906 -8.725  -6.686  1.00 25.17 ?  76  LYS   A HZ1  1 
ATOM   1693 H  HZ2  . LYS   A 1 76  ? 37.868 -8.973  -5.706  1.00 25.17 ?  76  LYS   A HZ2  1 
ATOM   1694 H  HZ3  . LYS   A 1 76  ? 37.648 -9.315  -7.096  1.00 25.17 ?  76  LYS   A HZ3  1 
ATOM   1695 N  N    . VAL   A 1 77  ? 31.142 -4.409  -7.404  1.00 11.82 ?  77  VAL   A N    1 
ATOM   1696 C  CA   . VAL   A 1 77  ? 29.735 -4.798  -7.313  1.00 11.69 ?  77  VAL   A CA   1 
ATOM   1697 C  C    . VAL   A 1 77  ? 29.676 -6.253  -6.871  1.00 11.15 ?  77  VAL   A C    1 
ATOM   1698 O  O    . VAL   A 1 77  ? 30.325 -7.122  -7.462  1.00 11.59 ?  77  VAL   A O    1 
ATOM   1699 C  CB   . VAL   A 1 77  ? 28.999 -4.576  -8.644  1.00 12.65 ?  77  VAL   A CB   1 
ATOM   1700 C  CG1  . VAL   A 1 77  ? 27.544 -5.029  -8.527  1.00 13.39 ?  77  VAL   A CG1  1 
ATOM   1701 C  CG2  . VAL   A 1 77  ? 29.062 -3.113  -9.055  1.00 14.11 ?  77  VAL   A CG2  1 
ATOM   1702 H  H    . VAL   A 1 77  ? 31.414 -4.172  -8.184  1.00 14.24 ?  77  VAL   A H    1 
ATOM   1703 H  HA   . VAL   A 1 77  ? 29.303 -4.259  -6.634  1.00 14.08 ?  77  VAL   A HA   1 
ATOM   1704 H  HB   . VAL   A 1 77  ? 29.430 -5.101  -9.337  1.00 15.23 ?  77  VAL   A HB   1 
ATOM   1705 H  HG11 . VAL   A 1 77  ? 27.059 -4.723  -9.307  1.00 16.13 ?  77  VAL   A HG11 1 
ATOM   1706 H  HG12 . VAL   A 1 77  ? 27.518 -5.996  -8.476  1.00 16.13 ?  77  VAL   A HG12 1 
ATOM   1707 H  HG13 . VAL   A 1 77  ? 27.161 -4.642  -7.724  1.00 16.13 ?  77  VAL   A HG13 1 
ATOM   1708 H  HG21 . VAL   A 1 77  ? 28.560 -2.996  -9.876  1.00 16.99 ?  77  VAL   A HG21 1 
ATOM   1709 H  HG22 . VAL   A 1 77  ? 28.674 -2.572  -8.349  1.00 16.99 ?  77  VAL   A HG22 1 
ATOM   1710 H  HG23 . VAL   A 1 77  ? 29.988 -2.861  -9.193  1.00 16.99 ?  77  VAL   A HG23 1 
ATOM   1711 N  N    . GLY   A 1 78  ? 28.904 -6.521  -5.818  1.00 11.15 ?  78  GLY   A N    1 
ATOM   1712 C  CA   . GLY   A 1 78  ? 28.877 -7.811  -5.156  1.00 11.13 ?  78  GLY   A CA   1 
ATOM   1713 C  C    . GLY   A 1 78  ? 29.803 -7.907  -3.963  1.00 10.41 ?  78  GLY   A C    1 
ATOM   1714 O  O    . GLY   A 1 78  ? 29.749 -8.913  -3.238  1.00 11.14 ?  78  GLY   A O    1 
ATOM   1715 H  H    . GLY   A 1 78  ? 28.360 -5.947  -5.470  1.00 13.44 ?  78  GLY   A H    1 
ATOM   1716 H  HA2  . GLY   A 1 78  ? 27.976 -7.993  -4.858  1.00 13.41 ?  78  GLY   A HA2  1 
ATOM   1717 H  HA3  . GLY   A 1 78  ? 29.131 -8.495  -5.796  1.00 13.41 ?  78  GLY   A HA3  1 
ATOM   1718 N  N    . GLY   A 1 79  ? 30.656 -6.901  -3.746  1.00 10.66 ?  79  GLY   A N    1 
ATOM   1719 C  CA   . GLY   A 1 79  ? 31.622 -6.913  -2.674  1.00 10.89 ?  79  GLY   A CA   1 
ATOM   1720 C  C    . GLY   A 1 79  ? 31.180 -6.118  -1.456  1.00 10.44 ?  79  GLY   A C    1 
ATOM   1721 O  O    . GLY   A 1 79  ? 30.063 -5.611  -1.370  1.00 10.98 ?  79  GLY   A O    1 
ATOM   1722 H  H    . GLY   A 1 79  ? 30.684 -6.184  -4.224  1.00 12.85 ?  79  GLY   A H    1 
ATOM   1723 H  HA2  . GLY   A 1 79  ? 31.779 -7.836  -2.402  1.00 13.12 ?  79  GLY   A HA2  1 
ATOM   1724 H  HA3  . GLY   A 1 79  ? 32.459 -6.548  -2.996  1.00 13.12 ?  79  GLY   A HA3  1 
ATOM   1725 N  N    . SER   A 1 80  ? 32.093 -6.026  -0.492  1.00 11.24 ?  80  SER   A N    1 
ATOM   1726 C  CA   . SER   A 1 80  ? 31.780 -5.392  0.778   1.00 10.59 ?  80  SER   A CA   1 
ATOM   1727 C  C    . SER   A 1 80  ? 33.056 -4.944  1.471   1.00 10.42 ?  80  SER   A C    1 
ATOM   1728 O  O    . SER   A 1 80  ? 34.168 -5.379  1.135   1.00 11.97 ?  80  SER   A O    1 
ATOM   1729 C  CB   . SER   A 1 80  ? 31.027 -6.357  1.697   1.00 11.76 ?  80  SER   A CB   1 
ATOM   1730 O  OG   . SER   A 1 80  ? 31.866 -7.403  2.164   1.00 13.19 ?  80  SER   A OG   1 
ATOM   1731 H  H    . SER   A 1 80  ? 32.900 -6.312  -0.558  1.00 13.54 ?  80  SER   A H    1 
ATOM   1732 H  HA   . SER   A 1 80  ? 31.223 -4.612  0.604   1.00 12.76 ?  80  SER   A HA   1 
ATOM   1733 H  HB2  . SER   A 1 80  ? 30.690 -5.861  2.457   1.00 14.17 ?  80  SER   A HB2  1 
ATOM   1734 H  HB3  . SER   A 1 80  ? 30.287 -6.743  1.200   1.00 14.17 ?  80  SER   A HB3  1 
ATOM   1735 H  HG   . SER   A 1 80  ? 32.167 -7.839  1.505   1.00 15.89 ?  80  SER   A HG   1 
ATOM   1736 N  N    . CYS   A 1 81  ? 32.870 -4.097  2.483   1.00 10.18 ?  81  CYS   A N    1 
ATOM   1737 C  CA   . CYS   A 1 81  ? 33.927 -3.814  3.442   1.00 10.41 ?  81  CYS   A CA   1 
ATOM   1738 C  C    . CYS   A 1 81  ? 33.291 -3.579  4.803   1.00 10.22 ?  81  CYS   A C    1 
ATOM   1739 O  O    . CYS   A 1 81  ? 32.127 -3.179  4.898   1.00 11.42 ?  81  CYS   A O    1 
ATOM   1740 C  CB   . CYS   A 1 81  ? 34.800 -2.623  3.021   1.00 11.02 ?  81  CYS   A CB   1 
ATOM   1741 S  SG   . CYS   A 1 81  ? 33.903 -1.045  3.043   1.00 11.39 ?  81  CYS   A SG   1 
ATOM   1742 H  H    . CYS   A 1 81  ? 32.135 -3.667  2.637   1.00 12.27 ?  81  CYS   A H    1 
ATOM   1743 H  HA   . CYS   A 1 81  ? 34.500 -4.594  3.511   1.00 12.54 ?  81  CYS   A HA   1 
ATOM   1744 H  HB2  . CYS   A 1 81  ? 35.555 -2.556  3.631   1.00 13.27 ?  81  CYS   A HB2  1 
ATOM   1745 H  HB3  . CYS   A 1 81  ? 35.126 -2.777  2.117   1.00 13.27 ?  81  CYS   A HB3  1 
ATOM   1746 H  HG   . CYS   A 1 81  ? 34.645 -0.166  2.706   1.00 13.73 ?  81  CYS   A HG   1 
ATOM   1747 N  N    . VAL   A 1 82  ? 34.064 -3.837  5.853   1.00 10.65 ?  82  VAL   A N    1 
ATOM   1748 C  CA   . VAL   A 1 82  ? 33.646 -3.592  7.226   1.00 11.07 ?  82  VAL   A CA   1 
ATOM   1749 C  C    . VAL   A 1 82  ? 34.249 -2.276  7.694   1.00 11.17 ?  82  VAL   A C    1 
ATOM   1750 O  O    . VAL   A 1 82  ? 35.474 -2.101  7.672   1.00 12.16 ?  82  VAL   A O    1 
ATOM   1751 C  CB   . VAL   A 1 82  ? 34.072 -4.733  8.161   1.00 12.65 ?  82  VAL   A CB   1 
ATOM   1752 C  CG1  . VAL   A 1 82  ? 33.632 -4.435  9.583   1.00 14.15 ?  82  VAL   A CG1  1 
ATOM   1753 C  CG2  . VAL   A 1 82  ? 33.501 -6.057  7.694   1.00 13.37 ?  82  VAL   A CG2  1 
ATOM   1754 H  H    . VAL   A 1 82  ? 34.864 -4.167  5.791   1.00 12.84 ?  82  VAL   A H    1 
ATOM   1755 H  HA   . VAL   A 1 82  ? 32.680 -3.516  7.254   1.00 13.35 ?  82  VAL   A HA   1 
ATOM   1756 H  HB   . VAL   A 1 82  ? 35.038 -4.801  8.157   1.00 15.24 ?  82  VAL   A HB   1 
ATOM   1757 H  HG11 . VAL   A 1 82  ? 33.710 -5.243  10.113  1.00 17.03 ?  82  VAL   A HG11 1 
ATOM   1758 H  HG12 . VAL   A 1 82  ? 34.197 -3.740  9.957   1.00 17.03 ?  82  VAL   A HG12 1 
ATOM   1759 H  HG13 . VAL   A 1 82  ? 32.706 -4.138  9.574   1.00 17.03 ?  82  VAL   A HG13 1 
ATOM   1760 H  HG21 . VAL   A 1 82  ? 33.751 -6.748  8.325   1.00 16.09 ?  82  VAL   A HG21 1 
ATOM   1761 H  HG22 . VAL   A 1 82  ? 32.534 -5.984  7.648   1.00 16.09 ?  82  VAL   A HG22 1 
ATOM   1762 H  HG23 . VAL   A 1 82  ? 33.859 -6.262  6.817   1.00 16.09 ?  82  VAL   A HG23 1 
ATOM   1763 N  N    . LEU   A 1 83  ? 33.394 -1.357  8.126   1.00 11.01 ?  83  LEU   A N    1 
ATOM   1764 C  CA   . LEU   A 1 83  ? 33.814 -0.089  8.699   1.00 10.80 ?  83  LEU   A CA   1 
ATOM   1765 C  C    . LEU   A 1 83  ? 33.100 0.091   10.034  1.00 10.81 ?  83  LEU   A C    1 
ATOM   1766 O  O    . LEU   A 1 83  ? 32.383 -0.800  10.504  1.00 11.43 ?  83  LEU   A O    1 
ATOM   1767 C  CB   . LEU   A 1 83  ? 33.559 1.066   7.718   1.00 11.18 ?  83  LEU   A CB   1 
ATOM   1768 C  CG   . LEU   A 1 83  ? 34.454 1.073   6.474   1.00 11.95 ?  83  LEU   A CG   1 
ATOM   1769 C  CD1  . LEU   A 1 83  ? 34.002 2.111   5.466   1.00 12.68 ?  83  LEU   A CD1  1 
ATOM   1770 C  CD2  . LEU   A 1 83  ? 35.920 1.300   6.863   1.00 12.70 ?  83  LEU   A CD2  1 
ATOM   1771 H  H    . LEU   A 1 83  ? 32.537 -1.447  8.086   1.00 13.26 ?  83  LEU   A H    1 
ATOM   1772 H  HA   . LEU   A 1 83  ? 34.768 -0.122  8.872   1.00 13.02 ?  83  LEU   A HA   1 
ATOM   1773 H  HB2  . LEU   A 1 83  ? 32.642 1.020   7.408   1.00 13.47 ?  83  LEU   A HB2  1 
ATOM   1774 H  HB3  . LEU   A 1 83  ? 33.702 1.908   8.180   1.00 13.47 ?  83  LEU   A HB3  1 
ATOM   1775 H  HG   . LEU   A 1 83  ? 34.403 0.203   6.052   1.00 14.40 ?  83  LEU   A HG   1 
ATOM   1776 H  HD11 . LEU   A 1 83  ? 34.595 2.077   4.696   1.00 15.27 ?  83  LEU   A HD11 1 
ATOM   1777 H  HD12 . LEU   A 1 83  ? 33.096 1.903   5.193   1.00 15.27 ?  83  LEU   A HD12 1 
ATOM   1778 H  HD13 . LEU   A 1 83  ? 34.039 2.986   5.875   1.00 15.27 ?  83  LEU   A HD13 1 
ATOM   1779 H  HD21 . LEU   A 1 83  ? 36.442 1.463   6.058   1.00 15.30 ?  83  LEU   A HD21 1 
ATOM   1780 H  HD22 . LEU   A 1 83  ? 35.979 2.072   7.451   1.00 15.30 ?  83  LEU   A HD22 1 
ATOM   1781 H  HD23 . LEU   A 1 83  ? 36.260 0.514   7.319   1.00 15.30 ?  83  LEU   A HD23 1 
ATOM   1782 N  N    . SER   A 1 84  ? 33.314 1.242   10.664  1.00 11.39 ?  84  SER   A N    1 
ATOM   1783 C  CA   . SER   A 1 84  ? 32.680 1.498   11.947  1.00 11.58 ?  84  SER   A CA   1 
ATOM   1784 C  C    . SER   A 1 84  ? 31.161 1.575   11.805  1.00 11.42 ?  84  SER   A C    1 
ATOM   1785 O  O    . SER   A 1 84  ? 30.632 2.040   10.797  1.00 11.86 ?  84  SER   A O    1 
ATOM   1786 C  CB   . SER   A 1 84  ? 33.179 2.821   12.516  1.00 12.68 ?  84  SER   A CB   1 
ATOM   1787 O  OG   . SER   A 1 84  ? 32.549 3.102   13.751  1.00 13.46 ?  84  SER   A OG   1 
ATOM   1788 H  H    . SER   A 1 84  ? 33.810 1.886   10.364  1.00 13.72 ?  84  SER   A H    1 
ATOM   1789 H  HA   . SER   A 1 84  ? 32.909 0.789   12.565  1.00 13.95 ?  84  SER   A HA   1 
ATOM   1790 H  HB2  . SER   A 1 84  ? 34.141 2.773   12.644  1.00 15.27 ?  84  SER   A HB2  1 
ATOM   1791 H  HB3  . SER   A 1 84  ? 32.969 3.535   11.889  1.00 15.27 ?  84  SER   A HB3  1 
ATOM   1792 H  HG   . SER   A 1 84  ? 32.838 3.831   14.061  1.00 16.21 ?  84  SER   A HG   1 
ATOM   1793 N  N    . GLY   A 1 85  ? 30.457 1.154   12.855  1.00 12.36 ?  85  GLY   A N    1 
ATOM   1794 C  CA   . GLY   A 1 85  ? 29.035 1.389   12.957  1.00 13.01 ?  85  GLY   A CA   1 
ATOM   1795 C  C    . GLY   A 1 85  ? 28.669 2.705   13.603  1.00 12.61 ?  85  GLY   A C    1 
ATOM   1796 O  O    . GLY   A 1 85  ? 27.478 3.019   13.722  1.00 13.29 ?  85  GLY   A O    1 
ATOM   1797 H  H    . GLY   A 1 85  ? 30.797 0.729   13.525  1.00 14.88 ?  85  GLY   A H    1 
ATOM   1798 H  HA2  . GLY   A 1 85  ? 28.653 1.371   12.068  1.00 15.66 ?  85  GLY   A HA2  1 
ATOM   1799 H  HA3  . GLY   A 1 85  ? 28.638 0.678   13.475  1.00 15.66 ?  85  GLY   A HA3  1 
ATOM   1800 N  N    . HIS   A 1 86  ? 29.658 3.483   14.033  1.00 12.31 ?  86  HIS   A N    1 
ATOM   1801 C  CA   . HIS   A 1 86  ? 29.436 4.814   14.605  1.00 12.80 ?  86  HIS   A CA   1 
ATOM   1802 C  C    . HIS   A 1 86  ? 28.458 4.689   15.766  1.00 13.37 ?  86  HIS   A C    1 
ATOM   1803 O  O    . HIS   A 1 86  ? 28.649 3.814   16.626  1.00 14.51 ?  86  HIS   A O    1 
ATOM   1804 C  CB   . HIS   A 1 86  ? 29.052 5.797   13.506  1.00 12.66 ?  86  HIS   A CB   1 
ATOM   1805 C  CG   . HIS   A 1 86  ? 30.102 5.905   12.460  1.00 12.70 ?  86  HIS   A CG   1 
ATOM   1806 N  ND1  . HIS   A 1 86  ? 31.186 6.746   12.588  1.00 13.80 ?  86  HIS   A ND1  1 
ATOM   1807 C  CD2  . HIS   A 1 86  ? 30.287 5.212   11.315  1.00 12.74 ?  86  HIS   A CD2  1 
ATOM   1808 C  CE1  . HIS   A 1 86  ? 31.975 6.591   11.540  1.00 13.58 ?  86  HIS   A CE1  1 
ATOM   1809 N  NE2  . HIS   A 1 86  ? 31.460 5.657   10.762  1.00 12.85 ?  86  HIS   A NE2  1 
ATOM   1810 H  H    . HIS   A 1 86  ? 30.486 3.257   14.018  1.00 14.83 ?  86  HIS   A H    1 
ATOM   1811 H  HA   . HIS   A 1 86  ? 30.273 5.127   14.976  1.00 15.42 ?  86  HIS   A HA   1 
ATOM   1812 H  HB2  . HIS   A 1 86  ? 28.230 5.506   13.080  1.00 15.25 ?  86  HIS   A HB2  1 
ATOM   1813 H  HB3  . HIS   A 1 86  ? 28.925 6.683   13.892  1.00 15.25 ?  86  HIS   A HB3  1 
ATOM   1814 H  HD2  . HIS   A 1 86  ? 29.727 4.551   10.969  1.00 15.35 ?  86  HIS   A HD2  1 
ATOM   1815 H  HE1  . HIS   A 1 86  ? 32.763 7.057   11.371  1.00 16.35 ?  86  HIS   A HE1  1 
ATOM   1816 H  HE2  . HIS   A 1 86  ? 31.794 5.385   10.011  1.00 15.48 ?  86  HIS   A HE2  1 
ATOM   1817 N  N    . ASN   A 1 87  ? 27.445 5.539   15.845  1.00 14.22 ?  87  ASN   A N    1 
ATOM   1818 C  CA   . ASN   A 1 87  ? 26.469 5.521   16.917  1.00 15.12 ?  87  ASN   A CA   1 
ATOM   1819 C  C    . ASN   A 1 87  ? 25.343 4.529   16.678  1.00 16.32 ?  87  ASN   A C    1 
ATOM   1820 O  O    . ASN   A 1 87  ? 24.426 4.462   17.499  1.00 18.63 ?  87  ASN   A O    1 
ATOM   1821 C  CB   . ASN   A 1 87  ? 25.874 6.924   17.086  1.00 15.95 ?  87  ASN   A CB   1 
ATOM   1822 C  CG   . ASN   A 1 87  ? 25.353 7.506   15.775  1.00 16.70 ?  87  ASN   A CG   1 
ATOM   1823 O  OD1  . ASN   A 1 87  ? 25.988 7.401   14.726  1.00 17.18 ?  87  ASN   A OD1  1 
ATOM   1824 N  ND2  . ASN   A 1 87  ? 24.189 8.121   15.835  1.00 17.67 ?  87  ASN   A ND2  1 
ATOM   1825 H  H    . ASN   A 1 87  ? 27.294 6.152   15.266  1.00 17.12 ?  87  ASN   A H    1 
ATOM   1826 H  HA   . ASN   A 1 87  ? 26.905 5.272   17.749  1.00 18.20 ?  87  ASN   A HA   1 
ATOM   1827 H  HB2  . ASN   A 1 87  ? 25.132 6.878   17.718  1.00 19.20 ?  87  ASN   A HB2  1 
ATOM   1828 H  HB3  . ASN   A 1 87  ? 26.560 7.515   17.430  1.00 19.20 ?  87  ASN   A HB3  1 
ATOM   1829 H  HD21 . ASN   A 1 87  ? 23.854 8.464   15.126  1.00 21.26 ?  87  ASN   A HD21 1 
ATOM   1830 H  HD22 . ASN   A 1 87  ? 23.772 8.187   16.587  1.00 21.26 ?  87  ASN   A HD22 1 
ATOM   1831 N  N    . LEU   A 1 88  ? 25.393 3.755   15.596  1.00 15.33 ?  88  LEU   A N    1 
ATOM   1832 C  CA   . LEU   A 1 88  ? 24.283 2.888   15.209  1.00 15.38 ?  88  LEU   A CA   1 
ATOM   1833 C  C    . LEU   A 1 88  ? 24.506 1.412   15.513  1.00 15.16 ?  88  LEU   A C    1 
ATOM   1834 O  O    . LEU   A 1 88  ? 23.530 0.676   15.696  1.00 16.32 ?  88  LEU   A O    1 
ATOM   1835 C  CB   . LEU   A 1 88  ? 24.019 3.037   13.709  1.00 15.92 ?  88  LEU   A CB   1 
ATOM   1836 C  CG   . LEU   A 1 88  ? 23.727 4.453   13.212  1.00 17.26 ?  88  LEU   A CG   1 
ATOM   1837 C  CD1  . LEU   A 1 88  ? 23.545 4.450   11.706  1.00 17.60 ?  88  LEU   A CD1  1 
ATOM   1838 C  CD2  . LEU   A 1 88  ? 22.500 5.034   13.904  1.00 19.13 ?  88  LEU   A CD2  1 
ATOM   1839 H  H    . LEU   A 1 88  ? 26.069 3.712   15.070  1.00 18.45 ?  88  LEU   A H    1 
ATOM   1840 H  HA   . LEU   A 1 88  ? 23.487 3.170   15.683  1.00 18.51 ?  88  LEU   A HA   1 
ATOM   1841 H  HB2  . LEU   A 1 88  ? 24.792 2.720   13.225  1.00 19.16 ?  88  LEU   A HB2  1 
ATOM   1842 H  HB3  . LEU   A 1 88  ? 23.247 2.494   13.481  1.00 19.16 ?  88  LEU   A HB3  1 
ATOM   1843 H  HG   . LEU   A 1 88  ? 24.484 5.023   13.417  1.00 20.77 ?  88  LEU   A HG   1 
ATOM   1844 H  HD11 . LEU   A 1 88  ? 23.381 5.358   11.402  1.00 21.18 ?  88  LEU   A HD11 1 
ATOM   1845 H  HD12 . LEU   A 1 88  ? 24.350 4.103   11.289  1.00 21.18 ?  88  LEU   A HD12 1 
ATOM   1846 H  HD13 . LEU   A 1 88  ? 22.787 3.886   11.479  1.00 21.18 ?  88  LEU   A HD13 1 
ATOM   1847 H  HD21 . LEU   A 1 88  ? 22.282 5.886   13.494  1.00 23.01 ?  88  LEU   A HD21 1 
ATOM   1848 H  HD22 . LEU   A 1 88  ? 21.761 4.418   13.802  1.00 23.01 ?  88  LEU   A HD22 1 
ATOM   1849 H  HD23 . LEU   A 1 88  ? 22.701 5.162   14.844  1.00 23.01 ?  88  LEU   A HD23 1 
ATOM   1850 N  N    . ALA   A 1 89  ? 25.758 0.966   15.552  1.00 14.56 ?  89  ALA   A N    1 
ATOM   1851 C  CA   . ALA   A 1 89  ? 26.104 -0.446  15.643  1.00 14.23 ?  89  ALA   A CA   1 
ATOM   1852 C  C    . ALA   A 1 89  ? 27.590 -0.512  15.951  1.00 14.46 ?  89  ALA   A C    1 
ATOM   1853 O  O    . ALA   A 1 89  ? 28.303 0.483   15.824  1.00 15.01 ?  89  ALA   A O    1 
ATOM   1854 C  CB   . ALA   A 1 89  ? 25.817 -1.162  14.322  1.00 13.71 ?  89  ALA   A CB   1 
ATOM   1855 H  H    . ALA   A 1 89  ? 26.444 1.484   15.519  1.00 17.53 ?  89  ALA   A H    1 
ATOM   1856 H  HA   . ALA   A 1 89  ? 25.604 -0.867  16.361  1.00 17.13 ?  89  ALA   A HA   1 
ATOM   1857 H  HB1  . ALA   A 1 89  ? 26.082 -2.095  14.407  1.00 16.50 ?  89  ALA   A HB1  1 
ATOM   1858 H  HB2  . ALA   A 1 89  ? 24.867 -1.109  14.130  1.00 16.50 ?  89  ALA   A HB2  1 
ATOM   1859 H  HB3  . ALA   A 1 89  ? 26.324 -0.740  13.615  1.00 16.50 ?  89  ALA   A HB3  1 
ATOM   1860 N  N    . LYS   A 1 90  ? 28.070 -1.692  16.339  1.00 15.20 ?  90  LYS   A N    1 
ATOM   1861 C  CA   . LYS   A 1 90  ? 29.515 -1.846  16.476  1.00 15.98 ?  90  LYS   A CA   1 
ATOM   1862 C  C    . LYS   A 1 90  ? 30.203 -1.651  15.128  1.00 14.78 ?  90  LYS   A C    1 
ATOM   1863 O  O    . LYS   A 1 90  ? 31.135 -0.840  14.997  1.00 15.82 ?  90  LYS   A O    1 
ATOM   1864 C  CB   . LYS   A 1 90  ? 29.857 -3.207  17.082  1.00 18.64 ?  90  LYS   A CB   1 
ATOM   1865 C  CG   . LYS   A 1 90  ? 31.336 -3.353  17.408  1.00 23.03 ?  90  LYS   A CG   1 
ATOM   1866 C  CD   . LYS   A 1 90  ? 31.595 -4.571  18.278  1.00 27.70 ?  90  LYS   A CD   1 
ATOM   1867 C  CE   . LYS   A 1 90  ? 33.019 -4.584  18.819  1.00 31.84 ?  90  LYS   A CE   1 
ATOM   1868 N  NZ   . LYS   A 1 90  ? 34.016 -5.037  17.809  1.00 34.22 ?  90  LYS   A NZ   1 
ATOM   1869 H  H    . LYS   A 1 90  ? 27.599 -2.384  16.524  1.00 18.30 ?  90  LYS   A H    1 
ATOM   1870 H  HA   . LYS   A 1 90  ? 29.848 -1.162  17.074  1.00 19.24 ?  90  LYS   A HA   1 
ATOM   1871 H  HB2  . LYS   A 1 90  ? 29.354 -3.320  17.906  1.00 22.43 ?  90  LYS   A HB2  1 
ATOM   1872 H  HB3  . LYS   A 1 90  ? 29.618 -3.905  16.452  1.00 22.43 ?  90  LYS   A HB3  1 
ATOM   1873 H  HG2  . LYS   A 1 90  ? 31.837 -3.455  16.585  1.00 27.69 ?  90  LYS   A HG2  1 
ATOM   1874 H  HG3  . LYS   A 1 90  ? 31.636 -2.566  17.890  1.00 27.69 ?  90  LYS   A HG3  1 
ATOM   1875 H  HD2  . LYS   A 1 90  ? 30.985 -4.563  19.033  1.00 33.29 ?  90  LYS   A HD2  1 
ATOM   1876 H  HD3  . LYS   A 1 90  ? 31.464 -5.375  17.751  1.00 33.29 ?  90  LYS   A HD3  1 
ATOM   1877 H  HE2  . LYS   A 1 90  ? 33.260 -3.685  19.095  1.00 38.27 ?  90  LYS   A HE2  1 
ATOM   1878 H  HE3  . LYS   A 1 90  ? 33.064 -5.186  19.578  1.00 38.27 ?  90  LYS   A HE3  1 
ATOM   1879 H  HZ1  . LYS   A 1 90  ? 33.813 -5.858  17.530  1.00 41.12 ?  90  LYS   A HZ1  1 
ATOM   1880 H  HZ2  . LYS   A 1 90  ? 34.016 -4.485  17.112  1.00 41.12 ?  90  LYS   A HZ2  1 
ATOM   1881 H  HZ3  . LYS   A 1 90  ? 34.830 -5.049  18.170  1.00 41.12 ?  90  LYS   A HZ3  1 
ATOM   1882 N  N    . HIS   A 1 91  ? 29.730 -2.367  14.106  1.00 13.04 ?  91  HIS   A N    1 
ATOM   1883 C  CA   . HIS   A 1 91  ? 30.300 -2.345  12.773  1.00 12.60 ?  91  HIS   A CA   1 
ATOM   1884 C  C    . HIS   A 1 91  ? 29.207 -2.062  11.758  1.00 11.62 ?  91  HIS   A C    1 
ATOM   1885 O  O    . HIS   A 1 91  ? 28.041 -2.409  11.964  1.00 12.06 ?  91  HIS   A O    1 
ATOM   1886 C  CB   . HIS   A 1 91  ? 30.894 -3.712  12.395  1.00 14.88 ?  91  HIS   A CB   1 
ATOM   1887 C  CG   . HIS   A 1 91  ? 31.887 -4.239  13.380  1.00 19.11 ?  91  HIS   A CG   1 
ATOM   1888 N  ND1  . HIS   A 1 91  ? 33.166 -3.737  13.489  1.00 21.22 ?  91  HIS   A ND1  1 
ATOM   1889 C  CD2  . HIS   A 1 91  ? 31.797 -5.237  14.291  1.00 20.94 ?  91  HIS   A CD2  1 
ATOM   1890 C  CE1  . HIS   A 1 91  ? 33.819 -4.398  14.429  1.00 21.99 ?  91  HIS   A CE1  1 
ATOM   1891 N  NE2  . HIS   A 1 91  ? 33.010 -5.314  14.932  1.00 22.28 ?  91  HIS   A NE2  1 
ATOM   1892 H  H    . HIS   A 1 91  ? 29.049 -2.905  14.173  1.00 15.71 ?  91  HIS   A H    1 
ATOM   1893 H  HA   . HIS   A 1 91  ? 30.985 -1.668  12.710  1.00 15.18 ?  91  HIS   A HA   1 
ATOM   1894 H  HB2  . HIS   A 1 91  ? 30.175 -4.361  12.327  1.00 17.91 ?  91  HIS   A HB2  1 
ATOM   1895 H  HB3  . HIS   A 1 91  ? 31.342 -3.631  11.537  1.00 17.91 ?  91  HIS   A HB3  1 
ATOM   1896 H  HD1  . HIS   A 1 91  ? 33.490 -3.093  13.016  1.00 25.52 ?  91  HIS   A HD1  1 
ATOM   1897 H  HD2  . HIS   A 1 91  ? 31.055 -5.769  14.455  1.00 25.18 ?  91  HIS   A HD2  1 
ATOM   1898 H  HE1  . HIS   A 1 91  ? 34.700 -4.240  14.690  1.00 26.45 ?  91  HIS   A HE1  1 
ATOM   1899 N  N    . CYS   A 1 92  ? 29.603 -1.459  10.642  1.00 11.13 ?  92  CYS   A N    1 
ATOM   1900 C  CA   . CYS   A 1 92  ? 28.762 -1.384  9.455   1.00 10.77 ?  92  CYS   A CA   1 
ATOM   1901 C  C    . CYS   A 1 92  ? 29.406 -2.207  8.348   1.00 10.30 ?  92  CYS   A C    1 
ATOM   1902 O  O    . CYS   A 1 92  ? 30.567 -1.961  7.976   1.00 10.99 ?  92  CYS   A O    1 
ATOM   1903 C  CB   . CYS   A 1 92  ? 28.545 0.059   8.997   1.00 10.94 ?  92  CYS   A CB   1 
ATOM   1904 S  SG   . CYS   A 1 92  ? 27.527 0.162   7.494   1.00 10.28 ?  92  CYS   A SG   1 
ATOM   1905 H  H    . CYS   A 1 92  ? 30.368 -1.072  10.546  1.00 13.42 ?  92  CYS   A H    1 
ATOM   1906 H  HA   . CYS   A 1 92  ? 27.896 -1.768  9.657   1.00 12.98 ?  92  CYS   A HA   1 
ATOM   1907 H  HB2  . CYS   A 1 92  ? 28.088 0.552   9.698   1.00 13.19 ?  92  CYS   A HB2  1 
ATOM   1908 H  HB3  . CYS   A 1 92  ? 29.402 0.467   8.807   1.00 13.19 ?  92  CYS   A HB3  1 
ATOM   1909 H  HG   . CYS   A 1 92  ? 27.380 1.311   7.194   1.00 12.40 ?  92  CYS   A HG   1 
ATOM   1910 N  N    . LEU   A 1 93  ? 28.664 -3.196  7.848   1.00 10.11 ?  93  LEU   A N    1 
ATOM   1911 C  CA   . LEU   A 1 93  ? 29.062 -3.955  6.668   1.00 9.95  ?  93  LEU   A CA   1 
ATOM   1912 C  C    . LEU   A 1 93  ? 28.464 -3.260  5.449   1.00 9.32  ?  93  LEU   A C    1 
ATOM   1913 O  O    . LEU   A 1 93  ? 27.249 -3.320  5.226   1.00 9.76  ?  93  LEU   A O    1 
ATOM   1914 C  CB   . LEU   A 1 93  ? 28.575 -5.400  6.774   1.00 10.49 ?  93  LEU   A CB   1 
ATOM   1915 C  CG   . LEU   A 1 93  ? 28.963 -6.295  5.602   1.00 10.57 ?  93  LEU   A CG   1 
ATOM   1916 C  CD1  . LEU   A 1 93  ? 30.466 -6.553  5.599   1.00 12.00 ?  93  LEU   A CD1  1 
ATOM   1917 C  CD2  . LEU   A 1 93  ? 28.194 -7.623  5.625   1.00 11.37 ?  93  LEU   A CD2  1 
ATOM   1918 H  H    . LEU   A 1 93  ? 27.913 -3.445  8.189   1.00 12.19 ?  93  LEU   A H    1 
ATOM   1919 H  HA   . LEU   A 1 93  ? 30.024 -3.954  6.593   1.00 11.99 ?  93  LEU   A HA   1 
ATOM   1920 H  HB2  . LEU   A 1 93  ? 28.944 -5.792  7.581   1.00 12.64 ?  93  LEU   A HB2  1 
ATOM   1921 H  HB3  . LEU   A 1 93  ? 27.606 -5.397  6.831   1.00 12.64 ?  93  LEU   A HB3  1 
ATOM   1922 H  HG   . LEU   A 1 93  ? 28.745 -5.847  4.777   1.00 12.74 ?  93  LEU   A HG   1 
ATOM   1923 H  HD11 . LEU   A 1 93  ? 30.686 -7.179  4.891   1.00 14.45 ?  93  LEU   A HD11 1 
ATOM   1924 H  HD12 . LEU   A 1 93  ? 30.938 -5.718  5.459   1.00 14.45 ?  93  LEU   A HD12 1 
ATOM   1925 H  HD13 . LEU   A 1 93  ? 30.731 -6.935  6.460   1.00 14.45 ?  93  LEU   A HD13 1 
ATOM   1926 H  HD21 . LEU   A 1 93  ? 28.477 -8.162  4.863   1.00 13.70 ?  93  LEU   A HD21 1 
ATOM   1927 H  HD22 . LEU   A 1 93  ? 28.391 -8.094  6.448   1.00 13.70 ?  93  LEU   A HD22 1 
ATOM   1928 H  HD23 . LEU   A 1 93  ? 27.246 -7.441  5.562   1.00 13.70 ?  93  LEU   A HD23 1 
ATOM   1929 N  N    . HIS   A 1 94  ? 29.310 -2.568  4.686   1.00 9.33  ?  94  HIS   A N    1 
ATOM   1930 C  CA   . HIS   A 1 94  ? 28.885 -1.891  3.462   1.00 9.19  ?  94  HIS   A CA   1 
ATOM   1931 C  C    . HIS   A 1 94  ? 28.888 -2.925  2.350   1.00 9.28  ?  94  HIS   A C    1 
ATOM   1932 O  O    . HIS   A 1 94  ? 29.950 -3.441  1.999   1.00 11.00 ?  94  HIS   A O    1 
ATOM   1933 C  CB   . HIS   A 1 94  ? 29.834 -0.744  3.121   1.00 9.34  ?  94  HIS   A CB   1 
ATOM   1934 C  CG   . HIS   A 1 94  ? 29.832 0.347   4.137   1.00 9.45  ?  94  HIS   A CG   1 
ATOM   1935 N  ND1  . HIS   A 1 94  ? 28.952 1.407   4.089   1.00 9.61  ?  94  HIS   A ND1  1 
ATOM   1936 C  CD2  . HIS   A 1 94  ? 30.581 0.517   5.250   1.00 10.12 ?  94  HIS   A CD2  1 
ATOM   1937 C  CE1  . HIS   A 1 94  ? 29.168 2.184   5.135   1.00 9.95  ?  94  HIS   A CE1  1 
ATOM   1938 N  NE2  . HIS   A 1 94  ? 30.153 1.670   5.852   1.00 10.30 ?  94  HIS   A NE2  1 
ATOM   1939 H  H    . HIS   A 1 94  ? 30.149 -2.473  4.863   1.00 11.25 ?  94  HIS   A H    1 
ATOM   1940 H  HA   . HIS   A 1 94  ? 27.984 -1.544  3.573   1.00 11.08 ?  94  HIS   A HA   1 
ATOM   1941 H  HB2  . HIS   A 1 94  ? 30.731 -1.091  3.056   1.00 11.27 ?  94  HIS   A HB2  1 
ATOM   1942 H  HB3  . HIS   A 1 94  ? 29.559 -0.361  2.271   1.00 11.27 ?  94  HIS   A HB3  1 
ATOM   1943 H  HD2  . HIS   A 1 94  ? 31.258 -0.039  5.551   1.00 12.20 ?  94  HIS   A HD2  1 
ATOM   1944 H  HE1  . HIS   A 1 94  ? 28.698 2.967   5.328   1.00 12.00 ?  94  HIS   A HE1  1 
ATOM   1945 H  HE2  . HIS   A 1 94  ? 30.466 2.013   6.573   1.00 12.41 ?  94  HIS   A HE2  1 
ATOM   1946 N  N    . VAL   A 1 95  ? 27.713 -3.250  1.810   1.00 8.95  ?  95  VAL   A N    1 
ATOM   1947 C  CA   . VAL   A 1 95  ? 27.566 -4.282  0.788   1.00 9.02  ?  95  VAL   A CA   1 
ATOM   1948 C  C    . VAL   A 1 95  ? 27.015 -3.646  -0.474  1.00 8.86  ?  95  VAL   A C    1 
ATOM   1949 O  O    . VAL   A 1 95  ? 26.014 -2.922  -0.417  1.00 9.90  ?  95  VAL   A O    1 
ATOM   1950 C  CB   . VAL   A 1 95  ? 26.639 -5.423  1.244   1.00 9.83  ?  95  VAL   A CB   1 
ATOM   1951 C  CG1  . VAL   A 1 95  ? 26.533 -6.470  0.150   1.00 10.69 ?  95  VAL   A CG1  1 
ATOM   1952 C  CG2  . VAL   A 1 95  ? 27.147 -6.037  2.531   1.00 10.13 ?  95  VAL   A CG2  1 
ATOM   1953 H  H    . VAL   A 1 95  ? 26.962 -2.877  2.025   1.00 10.80 ?  95  VAL   A H    1 
ATOM   1954 H  HA   . VAL   A 1 95  ? 28.432 -4.659  0.587   1.00 10.88 ?  95  VAL   A HA   1 
ATOM   1955 H  HB   . VAL   A 1 95  ? 25.755 -5.073  1.413   1.00 11.85 ?  95  VAL   A HB   1 
ATOM   1956 H  HG11 . VAL   A 1 95  ? 26.141 -7.283  0.519   1.00 12.89 ?  95  VAL   A HG11 1 
ATOM   1957 H  HG12 . VAL   A 1 95  ? 25.968 -6.135  -0.564  1.00 12.89 ?  95  VAL   A HG12 1 
ATOM   1958 H  HG13 . VAL   A 1 95  ? 27.419 -6.669  -0.195  1.00 12.89 ?  95  VAL   A HG13 1 
ATOM   1959 H  HG21 . VAL   A 1 95  ? 26.592 -6.799  2.760   1.00 12.21 ?  95  VAL   A HG21 1 
ATOM   1960 H  HG22 . VAL   A 1 95  ? 28.066 -6.322  2.407   1.00 12.21 ?  95  VAL   A HG22 1 
ATOM   1961 H  HG23 . VAL   A 1 95  ? 27.100 -5.372  3.237   1.00 12.21 ?  95  VAL   A HG23 1 
ATOM   1962 N  N    . VAL   A 1 96  ? 27.640 -3.939  -1.611  1.00 9.11  ?  96  VAL   A N    1 
ATOM   1963 C  CA   . VAL   A 1 96  ? 27.224 -3.383  -2.892  1.00 9.71  ?  96  VAL   A CA   1 
ATOM   1964 C  C    . VAL   A 1 96  ? 26.418 -4.428  -3.657  1.00 9.97  ?  96  VAL   A C    1 
ATOM   1965 O  O    . VAL   A 1 96  ? 26.976 -5.374  -4.221  1.00 10.94 ?  96  VAL   A O    1 
ATOM   1966 C  CB   . VAL   A 1 96  ? 28.418 -2.905  -3.723  1.00 10.06 ?  96  VAL   A CB   1 
ATOM   1967 C  CG1  . VAL   A 1 96  ? 27.912 -2.269  -4.996  1.00 10.29 ?  96  VAL   A CG1  1 
ATOM   1968 C  CG2  . VAL   A 1 96  ? 29.277 -1.933  -2.923  1.00 10.74 ?  96  VAL   A CG2  1 
ATOM   1969 H  H    . VAL   A 1 96  ? 28.329 -4.461  -1.667  1.00 10.99 ?  96  VAL   A H    1 
ATOM   1970 H  HA   . VAL   A 1 96  ? 26.653 -2.618  -2.730  1.00 11.71 ?  96  VAL   A HA   1 
ATOM   1971 H  HB   . VAL   A 1 96  ? 28.969 -3.661  -3.962  1.00 12.13 ?  96  VAL   A HB   1 
ATOM   1972 H  HG11 . VAL   A 1 96  ? 28.644 -1.781  -5.409  1.00 12.40 ?  96  VAL   A HG11 1 
ATOM   1973 H  HG12 . VAL   A 1 96  ? 27.599 -2.961  -5.591  1.00 12.40 ?  96  VAL   A HG12 1 
ATOM   1974 H  HG13 . VAL   A 1 96  ? 27.193 -1.657  -4.778  1.00 12.40 ?  96  VAL   A HG13 1 
ATOM   1975 H  HG21 . VAL   A 1 96  ? 29.978 -1.581  -3.492  1.00 12.94 ?  96  VAL   A HG21 1 
ATOM   1976 H  HG22 . VAL   A 1 96  ? 28.719 -1.206  -2.598  1.00 12.94 ?  96  VAL   A HG22 1 
ATOM   1977 H  HG23 . VAL   A 1 96  ? 29.670 -2.403  -2.168  1.00 12.94 ?  96  VAL   A HG23 1 
ATOM   1978 N  N    A GLY   A 1 97  ? 25.099 -4.278  -3.668  0.78 10.08 ?  97  GLY   A N    1 
ATOM   1979 N  N    B GLY   A 1 97  ? 25.102 -4.237  -3.709  0.22 10.39 ?  97  GLY   A N    1 
ATOM   1980 C  CA   A GLY   A 1 97  ? 24.279 -5.035  -4.578  0.78 10.55 ?  97  GLY   A CA   1 
ATOM   1981 C  CA   B GLY   A 1 97  ? 24.262 -5.014  -4.587  0.22 10.86 ?  97  GLY   A CA   1 
ATOM   1982 C  C    A GLY   A 1 97  ? 24.290 -4.374  -5.942  0.78 10.75 ?  97  GLY   A C    1 
ATOM   1983 C  C    B GLY   A 1 97  ? 24.186 -4.384  -5.964  0.22 11.30 ?  97  GLY   A C    1 
ATOM   1984 O  O    A GLY   A 1 97  ? 24.593 -3.184  -6.072  0.78 11.40 ?  97  GLY   A O    1 
ATOM   1985 O  O    B GLY   A 1 97  ? 24.395 -3.178  -6.129  0.22 11.36 ?  97  GLY   A O    1 
ATOM   1986 H  H    A GLY   A 1 97  ? 24.660 -3.731  -3.159  0.78 12.15 ?  97  GLY   A H    1 
ATOM   1987 H  H    B GLY   A 1 97  ? 24.672 -3.654  -3.237  0.22 12.53 ?  97  GLY   A H    1 
ATOM   1988 H  HA2  A GLY   A 1 97  ? 24.631 -5.936  -4.652  0.78 12.72 ?  97  GLY   A HA2  1 
ATOM   1989 H  HA2  B GLY   A 1 97  ? 24.626 -5.909  -4.664  0.22 13.09 ?  97  GLY   A HA2  1 
ATOM   1990 H  HA3  A GLY   A 1 97  ? 23.368 -5.077  -4.244  0.78 12.72 ?  97  GLY   A HA3  1 
ATOM   1991 H  HA3  B GLY   A 1 97  ? 23.366 -5.070  -4.222  0.22 13.09 ?  97  GLY   A HA3  1 
ATOM   1992 N  N    A PRO   A 1 98  ? 23.957 -5.122  -6.989  0.78 10.77 ?  98  PRO   A N    1 
ATOM   1993 N  N    B PRO   A 1 98  ? 23.882 -5.186  -6.983  0.22 11.59 ?  98  PRO   A N    1 
ATOM   1994 C  CA   A PRO   A 1 98  ? 23.844 -4.502  -8.313  0.78 11.84 ?  98  PRO   A CA   1 
ATOM   1995 C  CA   B PRO   A 1 98  ? 23.788 -4.638  -8.341  0.22 12.24 ?  98  PRO   A CA   1 
ATOM   1996 C  C    A PRO   A 1 98  ? 22.718 -3.474  -8.352  0.78 11.82 ?  98  PRO   A C    1 
ATOM   1997 C  C    B PRO   A 1 98  ? 22.659 -3.626  -8.464  0.22 12.68 ?  98  PRO   A C    1 
ATOM   1998 O  O    A PRO   A 1 98  ? 21.638 -3.681  -7.796  0.78 12.27 ?  98  PRO   A O    1 
ATOM   1999 O  O    B PRO   A 1 98  ? 21.640 -3.705  -7.775  0.22 12.76 ?  98  PRO   A O    1 
ATOM   2000 C  CB   A PRO   A 1 98  ? 23.554 -5.693  -9.233  0.78 12.05 ?  98  PRO   A CB   1 
ATOM   2001 C  CB   B PRO   A 1 98  ? 23.526 -5.877  -9.206  0.22 12.06 ?  98  PRO   A CB   1 
ATOM   2002 C  CG   A PRO   A 1 98  ? 22.894 -6.701  -8.333  0.78 12.48 ?  98  PRO   A CG   1 
ATOM   2003 C  CG   B PRO   A 1 98  ? 22.934 -6.878  -8.266  0.22 11.95 ?  98  PRO   A CG   1 
ATOM   2004 C  CD   A PRO   A 1 98  ? 23.625 -6.560  -7.018  0.78 11.45 ?  98  PRO   A CD   1 
ATOM   2005 C  CD   B PRO   A 1 98  ? 23.622 -6.635  -6.954  0.22 11.54 ?  98  PRO   A CD   1 
ATOM   2006 H  HA   A PRO   A 1 98  ? 24.686 -4.085  -8.566  0.78 14.26 ?  98  PRO   A HA   1 
ATOM   2007 H  HA   B PRO   A 1 98  ? 24.625 -4.223  -8.602  0.22 14.74 ?  98  PRO   A HA   1 
ATOM   2008 H  HB2  A PRO   A 1 98  ? 22.955 -5.417  -9.942  0.78 14.51 ?  98  PRO   A HB2  1 
ATOM   2009 H  HB2  B PRO   A 1 98  ? 22.902 -5.654  -9.914  0.22 14.53 ?  98  PRO   A HB2  1 
ATOM   2010 H  HB3  A PRO   A 1 98  ? 24.383 -6.042  -9.592  0.78 14.51 ?  98  PRO   A HB3  1 
ATOM   2011 H  HB3  B PRO   A 1 98  ? 24.364 -6.200  -9.572  0.22 14.53 ?  98  PRO   A HB3  1 
ATOM   2012 H  HG2  A PRO   A 1 98  ? 21.953 -6.483  -8.232  0.78 15.03 ?  98  PRO   A HG2  1 
ATOM   2013 H  HG2  B PRO   A 1 98  ? 21.979 -6.724  -8.188  0.22 14.40 ?  98  PRO   A HG2  1 
ATOM   2014 H  HG3  A PRO   A 1 98  ? 23.007 -7.591  -8.697  0.78 15.03 ?  98  PRO   A HG3  1 
ATOM   2015 H  HG3  B PRO   A 1 98  ? 23.115 -7.772  -8.588  0.22 14.40 ?  98  PRO   A HG3  1 
ATOM   2016 H  HD2  A PRO   A 1 98  ? 23.038 -6.787  -6.277  0.78 13.79 ?  98  PRO   A HD2  1 
ATOM   2017 H  HD2  B PRO   A 1 98  ? 23.036 -6.861  -6.215  0.22 13.91 ?  98  PRO   A HD2  1 
ATOM   2018 H  HD3  A PRO   A 1 98  ? 24.431 -7.096  -7.014  0.78 13.79 ?  98  PRO   A HD3  1 
ATOM   2019 H  HD3  B PRO   A 1 98  ? 24.459 -7.121  -6.912  0.22 13.91 ?  98  PRO   A HD3  1 
ATOM   2020 N  N    A ASN   A 1 99  ? 22.985 -2.349  -9.014  0.78 12.61 ?  99  ASN   A N    1 
ATOM   2021 N  N    B ASN   A 1 99  ? 22.858 -2.661  -9.358  0.22 13.23 ?  99  ASN   A N    1 
ATOM   2022 C  CA   A ASN   A 1 99  ? 21.997 -1.292  -9.226  0.78 13.78 ?  99  ASN   A CA   1 
ATOM   2023 C  CA   B ASN   A 1 99  ? 21.887 -1.605  -9.615  0.22 14.51 ?  99  ASN   A CA   1 
ATOM   2024 C  C    A ASN   A 1 99  ? 21.440 -1.455  -10.638 0.78 15.02 ?  99  ASN   A C    1 
ATOM   2025 C  C    B ASN   A 1 99  ? 21.167 -1.898  -10.925 0.22 16.01 ?  99  ASN   A C    1 
ATOM   2026 O  O    A ASN   A 1 99  ? 22.135 -1.199  -11.629 0.78 16.13 ?  99  ASN   A O    1 
ATOM   2027 O  O    B ASN   A 1 99  ? 21.800 -1.962  -11.985 0.22 15.82 ?  99  ASN   A O    1 
ATOM   2028 C  CB   A ASN   A 1 99  ? 22.627 0.089   -9.021  0.78 13.95 ?  99  ASN   A CB   1 
ATOM   2029 C  CB   B ASN   A 1 99  ? 22.591 -0.252  -9.692  0.22 15.01 ?  99  ASN   A CB   1 
ATOM   2030 C  CG   A ASN   A 1 99  ? 21.595 1.224   -9.013  0.78 14.21 ?  99  ASN   A CG   1 
ATOM   2031 C  CG   B ASN   A 1 99  ? 21.627 0.899   -9.815  0.22 15.40 ?  99  ASN   A CG   1 
ATOM   2032 O  OD1  A ASN   A 1 99  ? 20.598 1.177   -9.734  0.78 14.71 ?  99  ASN   A OD1  1 
ATOM   2033 O  OD1  B ASN   A 1 99  ? 20.638 0.820   -10.541 0.22 15.38 ?  99  ASN   A OD1  1 
ATOM   2034 N  ND2  A ASN   A 1 99  ? 21.846 2.252   -8.204  0.78 14.66 ?  99  ASN   A ND2  1 
ATOM   2035 N  ND2  B ASN   A 1 99  ? 21.908 1.982   -9.102  0.22 15.63 ?  99  ASN   A ND2  1 
ATOM   2036 H  H    A ASN   A 1 99  ? 23.756 -2.167  -9.348  0.78 15.19 ?  99  ASN   A H    1 
ATOM   2037 H  H    B ASN   A 1 99  ? 23.575 -2.587  -9.829  0.22 15.93 ?  99  ASN   A H    1 
ATOM   2038 H  HA   A ASN   A 1 99  ? 21.273 -1.398  -8.580  0.78 16.59 ?  99  ASN   A HA   1 
ATOM   2039 H  HA   B ASN   A 1 99  ? 21.234 -1.578  -8.899  0.22 17.47 ?  99  ASN   A HA   1 
ATOM   2040 H  HB2  A ASN   A 1 99  ? 23.095 0.104   -8.169  0.78 16.79 ?  99  ASN   A HB2  1 
ATOM   2041 H  HB2  B ASN   A 1 99  ? 23.114 -0.120  -8.891  0.22 18.07 ?  99  ASN   A HB2  1 
ATOM   2042 H  HB3  A ASN   A 1 99  ? 23.249 0.257   -9.743  0.78 16.79 ?  99  ASN   A HB3  1 
ATOM   2043 H  HB3  B ASN   A 1 99  ? 23.160 -0.235  -10.472 0.22 18.07 ?  99  ASN   A HB3  1 
ATOM   2044 H  HD21 A ASN   A 1 99  ? 21.294 2.911   -8.166  0.78 17.65 ?  99  ASN   A HD21 1 
ATOM   2045 H  HD21 B ASN   A 1 99  ? 21.380 2.656   -9.142  0.22 18.81 ?  99  ASN   A HD21 1 
ATOM   2046 H  HD22 A ASN   A 1 99  ? 22.555 2.255   -7.721  0.78 17.65 ?  99  ASN   A HD22 1 
ATOM   2047 H  HD22 B ASN   A 1 99  ? 22.605 2.019   -8.593  0.22 18.81 ?  99  ASN   A HD22 1 
ATOM   2048 N  N    A VAL   A 1 100 ? 20.186 -1.904  -10.721 0.78 15.84 ?  100 VAL   A N    1 
ATOM   2049 N  N    B VAL   A 1 100 ? 19.843 -2.054  -10.849 0.22 18.09 ?  100 VAL   A N    1 
ATOM   2050 C  CA   A VAL   A 1 100 ? 19.550 -2.119  -12.016 0.78 17.77 ?  100 VAL   A CA   1 
ATOM   2051 C  CA   B VAL   A 1 100 ? 19.056 -2.366  -12.039 0.22 20.10 ?  100 VAL   A CA   1 
ATOM   2052 C  C    A VAL   A 1 100 ? 19.439 -0.811  -12.785 0.78 18.16 ?  100 VAL   A C    1 
ATOM   2053 C  C    B VAL   A 1 100 ? 18.988 -1.166  -12.972 0.22 21.62 ?  100 VAL   A C    1 
ATOM   2054 O  O    A VAL   A 1 100 ? 19.509 -0.799  -14.020 0.78 19.44 ?  100 VAL   A O    1 
ATOM   2055 O  O    B VAL   A 1 100 ? 19.125 -1.305  -14.193 0.22 21.75 ?  100 VAL   A O    1 
ATOM   2056 C  CB   A VAL   A 1 100 ? 18.188 -2.818  -11.831 0.78 19.52 ?  100 VAL   A CB   1 
ATOM   2057 C  CB   B VAL   A 1 100 ? 17.655 -2.863  -11.640 0.22 20.58 ?  100 VAL   A CB   1 
ATOM   2058 C  CG1  A VAL   A 1 100 ? 17.496 -3.030  -13.172 0.78 20.45 ?  100 VAL   A CG1  1 
ATOM   2059 C  CG1  B VAL   A 1 100 ? 16.705 -2.795  -12.828 0.22 20.86 ?  100 VAL   A CG1  1 
ATOM   2060 C  CG2  A VAL   A 1 100 ? 18.379 -4.144  -11.113 0.78 20.15 ?  100 VAL   A CG2  1 
ATOM   2061 C  CG2  B VAL   A 1 100 ? 17.738 -4.279  -11.110 0.22 20.86 ?  100 VAL   A CG2  1 
ATOM   2062 H  H    A VAL   A 1 100 ? 19.682 -2.089  -10.039 0.78 19.06 ?  100 VAL   A H    1 
ATOM   2063 H  H    B VAL   A 1 100 ? 19.383 -1.979  -10.127 0.22 21.76 ?  100 VAL   A H    1 
ATOM   2064 H  HA   A VAL   A 1 100 ? 20.110 -2.709  -12.533 0.78 21.38 ?  100 VAL   A HA   1 
ATOM   2065 H  HA   B VAL   A 1 100 ? 19.492 -3.082  -12.521 0.22 24.17 ?  100 VAL   A HA   1 
ATOM   2066 H  HB   A VAL   A 1 100 ? 17.615 -2.260  -11.283 0.78 23.48 ?  100 VAL   A HB   1 
ATOM   2067 H  HB   B VAL   A 1 100 ? 17.301 -2.294  -10.938 0.22 24.75 ?  100 VAL   A HB   1 
ATOM   2068 H  HG11 A VAL   A 1 100 ? 16.727 -3.608  -13.042 0.78 24.59 ?  100 VAL   A HG11 1 
ATOM   2069 H  HG11 B VAL   A 1 100 ? 15.939 -3.361  -12.649 0.22 25.09 ?  100 VAL   A HG11 1 
ATOM   2070 H  HG12 A VAL   A 1 100 ? 17.207 -2.173  -13.522 0.78 24.59 ?  100 VAL   A HG12 1 
ATOM   2071 H  HG12 B VAL   A 1 100 ? 16.411 -1.878  -12.952 0.22 25.09 ?  100 VAL   A HG12 1 
ATOM   2072 H  HG13 A VAL   A 1 100 ? 18.119 -3.447  -13.788 0.78 24.59 ?  100 VAL   A HG13 1 
ATOM   2073 H  HG13 B VAL   A 1 100 ? 17.166 -3.108  -13.621 0.22 25.09 ?  100 VAL   A HG13 1 
ATOM   2074 H  HG21 A VAL   A 1 100 ? 17.534 -4.618  -11.093 0.78 24.24 ?  100 VAL   A HG21 1 
ATOM   2075 H  HG21 B VAL   A 1 100 ? 16.846 -4.586  -10.890 0.22 25.08 ?  100 VAL   A HG21 1 
ATOM   2076 H  HG22 A VAL   A 1 100 ? 19.042 -4.668  -11.589 0.78 24.24 ?  100 VAL   A HG22 1 
ATOM   2077 H  HG22 B VAL   A 1 100 ? 18.125 -4.848  -11.794 0.22 25.08 ?  100 VAL   A HG22 1 
ATOM   2078 H  HG23 A VAL   A 1 100 ? 18.683 -3.973  -10.207 0.78 24.24 ?  100 VAL   A HG23 1 
ATOM   2079 H  HG23 B VAL   A 1 100 ? 18.297 -4.285  -10.318 0.22 25.08 ?  100 VAL   A HG23 1 
ATOM   2080 N  N    A ASN   A 1 101 ? 19.277 0.307   -12.085 0.78 19.38 ?  101 ASN   A N    1 
ATOM   2081 N  N    B ASN   A 1 101 ? 18.763 0.027   -12.417 0.22 22.71 ?  101 ASN   A N    1 
ATOM   2082 C  CA   A ASN   A 1 101 ? 19.227 1.588   -12.777 0.78 21.09 ?  101 ASN   A CA   1 
ATOM   2083 C  CA   B ASN   A 1 101 ? 18.689 1.222   -13.249 0.22 23.60 ?  101 ASN   A CA   1 
ATOM   2084 C  C    A ASN   A 1 101 ? 20.588 2.023   -13.324 0.78 23.67 ?  101 ASN   A C    1 
ATOM   2085 C  C    B ASN   A 1 101 ? 19.991 1.450   -14.004 0.22 24.44 ?  101 ASN   A C    1 
ATOM   2086 O  O    A ASN   A 1 101 ? 20.669 3.091   -13.943 0.78 25.88 ?  101 ASN   A O    1 
ATOM   2087 O  O    B ASN   A 1 101 ? 19.975 1.956   -15.132 0.22 24.10 ?  101 ASN   A O    1 
ATOM   2088 C  CB   A ASN   A 1 101 ? 18.580 2.630   -11.863 0.78 20.79 ?  101 ASN   A CB   1 
ATOM   2089 C  CB   B ASN   A 1 101 ? 18.332 2.428   -12.381 0.22 23.52 ?  101 ASN   A CB   1 
ATOM   2090 C  CG   A ASN   A 1 101 ? 17.205 2.179   -11.370 0.78 20.29 ?  101 ASN   A CG   1 
ATOM   2091 C  CG   B ASN   A 1 101 ? 17.121 2.169   -11.506 0.22 23.23 ?  101 ASN   A CG   1 
ATOM   2092 O  OD1  A ASN   A 1 101 ? 16.411 1.626   -12.137 0.78 20.50 ?  101 ASN   A OD1  1 
ATOM   2093 O  OD1  B ASN   A 1 101 ? 16.099 1.672   -11.979 0.22 22.95 ?  101 ASN   A OD1  1 
ATOM   2094 N  ND2  A ASN   A 1 101 ? 16.931 2.385   -10.089 0.78 19.98 ?  101 ASN   A ND2  1 
ATOM   2095 N  ND2  B ASN   A 1 101 ? 17.239 2.482   -10.219 0.22 23.25 ?  101 ASN   A ND2  1 
ATOM   2096 H  H    A ASN   A 1 101 ? 19.189 0.354   -11.231 0.78 23.31 ?  101 ASN   A H    1 
ATOM   2097 H  H    B ASN   A 1 101 ? 18.655 0.169   -11.576 0.22 27.31 ?  101 ASN   A H    1 
ATOM   2098 H  HA   A ASN   A 1 101 ? 18.645 1.491   -13.541 0.78 25.36 ?  101 ASN   A HA   1 
ATOM   2099 H  HA   B ASN   A 1 101 ? 17.983 1.115   -13.902 0.22 28.38 ?  101 ASN   A HA   1 
ATOM   2100 H  HB2  A ASN   A 1 101 ? 19.146 2.781   -11.091 0.78 25.00 ?  101 ASN   A HB2  1 
ATOM   2101 H  HB2  B ASN   A 1 101 ? 19.077 2.632   -11.800 0.22 28.28 ?  101 ASN   A HB2  1 
ATOM   2102 H  HB3  A ASN   A 1 101 ? 18.470 3.464   -12.360 0.78 25.00 ?  101 ASN   A HB3  1 
ATOM   2103 H  HB3  B ASN   A 1 101 ? 18.133 3.195   -12.949 0.22 28.28 ?  101 ASN   A HB3  1 
ATOM   2104 H  HD21 A ASN   A 1 101 ? 16.167 2.149   -9.774  0.78 24.03 ?  101 ASN   A HD21 1 
ATOM   2105 H  HD21 B ASN   A 1 101 ? 16.579 2.354   -9.680  0.22 27.95 ?  101 ASN   A HD21 1 
ATOM   2106 H  HD22 A ASN   A 1 101 ? 17.507 2.770   -9.582  0.78 24.03 ?  101 ASN   A HD22 1 
ATOM   2107 H  HD22 B ASN   A 1 101 ? 17.973 2.819   -9.924  0.22 27.95 ?  101 ASN   A HD22 1 
ATOM   2108 N  N    A LYS   A 1 102 ? 21.636 1.208   -13.132 0.78 25.06 ?  102 LYS   A N    1 
ATOM   2109 N  N    B LYS   A 1 102 ? 21.122 1.071   -13.412 0.22 25.53 ?  102 LYS   A N    1 
ATOM   2110 C  CA   A LYS   A 1 102 ? 22.932 1.380   -13.782 0.78 26.44 ?  102 LYS   A CA   1 
ATOM   2111 C  CA   B LYS   A 1 102 ? 22.404 1.132   -14.101 0.22 26.20 ?  102 LYS   A CA   1 
ATOM   2112 C  C    A LYS   A 1 102 ? 23.252 0.270   -14.776 0.78 26.89 ?  102 LYS   A C    1 
ATOM   2113 C  C    B LYS   A 1 102 ? 22.631 -0.058  -15.024 0.22 25.85 ?  102 LYS   A C    1 
ATOM   2114 O  O    A LYS   A 1 102 ? 24.338 0.284   -15.363 0.78 27.28 ?  102 LYS   A O    1 
ATOM   2115 O  O    B LYS   A 1 102 ? 23.658 -0.102  -15.709 0.22 25.92 ?  102 LYS   A O    1 
ATOM   2116 C  CB   A LYS   A 1 102 ? 24.060 1.426   -12.741 0.78 27.88 ?  102 LYS   A CB   1 
ATOM   2117 C  CB   B LYS   A 1 102 ? 23.546 1.203   -13.085 0.22 27.16 ?  102 LYS   A CB   1 
ATOM   2118 C  CG   A LYS   A 1 102 ? 23.970 2.558   -11.740 0.78 29.32 ?  102 LYS   A CG   1 
ATOM   2119 C  CG   B LYS   A 1 102 ? 23.605 2.504   -12.303 0.22 27.99 ?  102 LYS   A CG   1 
ATOM   2120 C  CD   A LYS   A 1 102 ? 25.140 2.509   -10.763 0.78 30.82 ?  102 LYS   A CD   1 
ATOM   2121 C  CD   B LYS   A 1 102 ? 24.599 2.423   -11.155 0.22 28.77 ?  102 LYS   A CD   1 
ATOM   2122 C  CE   A LYS   A 1 102 ? 25.061 3.636   -9.746  0.78 32.25 ?  102 LYS   A CE   1 
ATOM   2123 C  CE   B LYS   A 1 102 ? 24.646 3.729   -10.375 0.22 29.36 ?  102 LYS   A CE   1 
ATOM   2124 N  NZ   A LYS   A 1 102 ? 26.166 3.568   -8.745  0.78 32.81 ?  102 LYS   A NZ   1 
ATOM   2125 N  NZ   B LYS   A 1 102 ? 25.313 3.572   -9.053  0.22 29.72 ?  102 LYS   A NZ   1 
ATOM   2126 H  H    A LYS   A 1 102 ? 21.617 0.521   -12.612 0.78 30.13 ?  102 LYS   A H    1 
ATOM   2127 H  H    B LYS   A 1 102 ? 21.168 0.770   -12.606 0.22 30.70 ?  102 LYS   A H    1 
ATOM   2128 H  HA   A LYS   A 1 102 ? 22.934 2.218   -14.265 0.78 31.78 ?  102 LYS   A HA   1 
ATOM   2129 H  HA   B LYS   A 1 102 ? 22.428 1.947   -14.630 0.22 31.50 ?  102 LYS   A HA   1 
ATOM   2130 H  HB2  A LYS   A 1 102 ? 24.055 0.592   -12.244 0.78 33.52 ?  102 LYS   A HB2  1 
ATOM   2131 H  HB2  B LYS   A 1 102 ? 23.443 0.477   -12.453 0.22 32.65 ?  102 LYS   A HB2  1 
ATOM   2132 H  HB3  A LYS   A 1 102 ? 24.908 1.515   -13.209 0.78 33.52 ?  102 LYS   A HB3  1 
ATOM   2133 H  HB3  B LYS   A 1 102 ? 24.385 1.106   -13.560 0.22 32.65 ?  102 LYS   A HB3  1 
ATOM   2134 H  HG2  A LYS   A 1 102 ? 23.997 3.406   -12.210 0.78 35.24 ?  102 LYS   A HG2  1 
ATOM   2135 H  HG2  B LYS   A 1 102 ? 23.885 3.220   -12.895 0.22 33.64 ?  102 LYS   A HG2  1 
ATOM   2136 H  HG3  A LYS   A 1 102 ? 23.146 2.475   -11.236 0.78 35.24 ?  102 LYS   A HG3  1 
ATOM   2137 H  HG3  B LYS   A 1 102 ? 22.730 2.696   -11.933 0.22 33.64 ?  102 LYS   A HG3  1 
ATOM   2138 H  HD2  A LYS   A 1 102 ? 25.125 1.664   -10.287 0.78 37.05 ?  102 LYS   A HD2  1 
ATOM   2139 H  HD2  B LYS   A 1 102 ? 24.332 1.715   -10.547 0.22 34.58 ?  102 LYS   A HD2  1 
ATOM   2140 H  HD3  A LYS   A 1 102 ? 25.972 2.600   -11.256 0.78 37.05 ?  102 LYS   A HD3  1 
ATOM   2141 H  HD3  B LYS   A 1 102 ? 25.485 2.246   -11.509 0.22 34.58 ?  102 LYS   A HD3  1 
ATOM   2142 H  HE2  A LYS   A 1 102 ? 25.123 4.486   -10.210 0.78 38.76 ?  102 LYS   A HE2  1 
ATOM   2143 H  HE2  B LYS   A 1 102 ? 25.142 4.387   -10.888 0.22 35.29 ?  102 LYS   A HE2  1 
ATOM   2144 H  HE3  A LYS   A 1 102 ? 24.217 3.575   -9.272  0.78 38.76 ?  102 LYS   A HE3  1 
ATOM   2145 H  HE3  B LYS   A 1 102 ? 23.740 4.040   -10.222 0.22 35.29 ?  102 LYS   A HE3  1 
ATOM   2146 H  HZ1  A LYS   A 1 102 ? 26.091 4.238   -8.166  0.78 39.43 ?  102 LYS   A HZ1  1 
ATOM   2147 H  HZ1  B LYS   A 1 102 ? 25.324 4.352   -8.624  0.22 35.72 ?  102 LYS   A HZ1  1 
ATOM   2148 H  HZ2  A LYS   A 1 102 ? 26.127 2.796   -8.303  0.78 39.43 ?  102 LYS   A HZ2  1 
ATOM   2149 H  HZ2  B LYS   A 1 102 ? 24.873 2.976   -8.559  0.22 35.72 ?  102 LYS   A HZ2  1 
ATOM   2150 H  HZ3  A LYS   A 1 102 ? 26.952 3.626   -9.157  0.78 39.43 ?  102 LYS   A HZ3  1 
ATOM   2151 H  HZ3  B LYS   A 1 102 ? 26.150 3.292   -9.166  0.22 35.72 ?  102 LYS   A HZ3  1 
ATOM   2152 N  N    A GLY   A 1 103 ? 22.361 -0.702  -14.962 0.78 27.39 ?  103 GLY   A N    1 
ATOM   2153 N  N    B GLY   A 1 103 ? 21.716 -1.025  -15.048 0.22 25.64 ?  103 GLY   A N    1 
ATOM   2154 C  CA   A GLY   A 1 103 ? 22.609 -1.789  -15.891 0.78 27.05 ?  103 GLY   A CA   1 
ATOM   2155 C  CA   B GLY   A 1 103 ? 21.851 -2.166  -15.930 0.22 25.21 ?  103 GLY   A CA   1 
ATOM   2156 C  C    A GLY   A 1 103 ? 23.442 -2.933  -15.355 0.78 26.82 ?  103 GLY   A C    1 
ATOM   2157 C  C    B GLY   A 1 103 ? 22.804 -3.236  -15.453 0.22 24.94 ?  103 GLY   A C    1 
ATOM   2158 O  O    A GLY   A 1 103 ? 23.994 -3.701  -16.148 0.78 27.96 ?  103 GLY   A O    1 
ATOM   2159 O  O    B GLY   A 1 103 ? 23.241 -4.064  -16.258 0.22 24.98 ?  103 GLY   A O    1 
ATOM   2160 H  H    A GLY   A 1 103 ? 21.605 -0.755  -14.562 0.78 32.93 ?  103 GLY   A H    1 
ATOM   2161 H  H    B GLY   A 1 103 ? 21.008 -1.037  -14.558 0.22 30.82 ?  103 GLY   A H    1 
ATOM   2162 H  HA2  A GLY   A 1 103 ? 21.759 -2.154  -16.184 0.78 32.52 ?  103 GLY   A HA2  1 
ATOM   2163 H  HA2  B GLY   A 1 103 ? 20.983 -2.577  -16.044 0.22 30.31 ?  103 GLY   A HA2  1 
ATOM   2164 H  HA3  A GLY   A 1 103 ? 23.065 -1.439  -16.673 0.78 32.52 ?  103 GLY   A HA3  1 
ATOM   2165 H  HA3  B GLY   A 1 103 ? 22.151 -1.854  -16.800 0.22 30.31 ?  103 GLY   A HA3  1 
ATOM   2166 N  N    A GLU   A 1 104 ? 23.541 -3.085  -14.038 0.78 24.56 ?  104 GLU   A N    1 
ATOM   2167 N  N    B GLU   A 1 104 ? 23.135 -3.255  -14.165 0.22 24.59 ?  104 GLU   A N    1 
ATOM   2168 C  CA   A GLU   A 1 104 ? 24.420 -4.083  -13.443 0.78 23.04 ?  104 GLU   A CA   1 
ATOM   2169 C  CA   B GLU   A 1 104 ? 24.098 -4.214  -13.650 0.22 24.29 ?  104 GLU   A CA   1 
ATOM   2170 C  C    A GLU   A 1 104 ? 23.735 -5.444  -13.331 0.78 23.48 ?  104 GLU   A C    1 
ATOM   2171 C  C    B GLU   A 1 104 ? 23.472 -5.603  -13.516 0.22 24.39 ?  104 GLU   A C    1 
ATOM   2172 O  O    A GLU   A 1 104 ? 22.515 -5.543  -13.164 0.78 23.93 ?  104 GLU   A O    1 
ATOM   2173 O  O    B GLU   A 1 104 ? 22.252 -5.763  -13.418 0.22 24.24 ?  104 GLU   A O    1 
ATOM   2174 C  CB   A GLU   A 1 104 ? 24.930 -3.586  -12.086 0.78 21.00 ?  104 GLU   A CB   1 
ATOM   2175 C  CB   B GLU   A 1 104 ? 24.662 -3.736  -12.310 0.22 24.06 ?  104 GLU   A CB   1 
ATOM   2176 C  CG   A GLU   A 1 104 ? 25.858 -2.373  -12.255 0.78 20.27 ?  104 GLU   A CG   1 
ATOM   2177 C  CG   B GLU   A 1 104 ? 25.471 -2.448  -12.423 0.22 24.14 ?  104 GLU   A CG   1 
ATOM   2178 C  CD   A GLU   A 1 104 ? 26.158 -1.588  -10.987 0.78 19.19 ?  104 GLU   A CD   1 
ATOM   2179 C  CD   B GLU   A 1 104 ? 25.844 -1.860  -11.075 0.22 24.24 ?  104 GLU   A CD   1 
ATOM   2180 O  OE1  A GLU   A 1 104 ? 25.586 -1.879  -9.917  0.78 17.69 ?  104 GLU   A OE1  1 
ATOM   2181 O  OE1  B GLU   A 1 104 ? 25.362 -2.370  -10.043 0.22 24.25 ?  104 GLU   A OE1  1 
ATOM   2182 O  OE2  A GLU   A 1 104 ? 26.982 -0.648  -11.084 0.78 19.84 -1 104 GLU   A OE2  1 
ATOM   2183 O  OE2  B GLU   A 1 104 ? 26.617 -0.879  -11.049 0.22 24.52 -1 104 GLU   A OE2  1 
ATOM   2184 H  H    A GLU   A 1 104 ? 23.108 -2.612  -13.465 0.78 29.52 ?  104 GLU   A H    1 
ATOM   2185 H  H    B GLU   A 1 104 ? 22.817 -2.717  -13.575 0.22 29.57 ?  104 GLU   A H    1 
ATOM   2186 H  HA   A GLU   A 1 104 ? 25.193 -4.190  -14.019 0.78 27.70 ?  104 GLU   A HA   1 
ATOM   2187 H  HA   B GLU   A 1 104 ? 24.838 -4.279  -14.272 0.22 29.21 ?  104 GLU   A HA   1 
ATOM   2188 H  HB2  A GLU   A 1 104 ? 24.177 -3.324  -11.535 0.78 25.26 ?  104 GLU   A HB2  1 
ATOM   2189 H  HB2  B GLU   A 1 104 ? 23.929 -3.574  -11.698 0.22 28.93 ?  104 GLU   A HB2  1 
ATOM   2190 H  HB3  A GLU   A 1 104 ? 25.433 -4.296  -11.654 0.78 25.26 ?  104 GLU   A HB3  1 
ATOM   2191 H  HB3  B GLU   A 1 104 ? 25.247 -4.424  -11.952 0.22 28.93 ?  104 GLU   A HB3  1 
ATOM   2192 H  HG2  A GLU   A 1 104 ? 26.705 -2.680  -12.606 0.78 24.38 ?  104 GLU   A HG2  1 
ATOM   2193 H  HG2  B GLU   A 1 104 ? 26.291 -2.631  -12.913 0.22 29.02 ?  104 GLU   A HG2  1 
ATOM   2194 H  HG3  A GLU   A 1 104 ? 25.446 -1.757  -12.880 0.78 24.38 ?  104 GLU   A HG3  1 
ATOM   2195 H  HG3  B GLU   A 1 104 ? 24.947 -1.784  -12.898 0.22 29.02 ?  104 GLU   A HG3  1 
ATOM   2196 N  N    A ASP   A 1 105 ? 24.546 -6.498  -13.424 0.78 24.25 ?  105 ASP   A N    1 
ATOM   2197 N  N    B ASP   A 1 105 ? 24.339 -6.612  -13.511 0.22 24.75 ?  105 ASP   A N    1 
ATOM   2198 C  CA   A ASP   A 1 105 ? 24.048 -7.864  -13.562 0.78 25.71 ?  105 ASP   A CA   1 
ATOM   2199 C  CA   B ASP   A 1 105 ? 23.912 -8.006  -13.534 0.22 25.44 ?  105 ASP   A CA   1 
ATOM   2200 C  C    A ASP   A 1 105 ? 23.354 -8.322  -12.282 0.78 22.98 ?  105 ASP   A C    1 
ATOM   2201 C  C    B ASP   A 1 105 ? 23.253 -8.372  -12.209 0.22 24.78 ?  105 ASP   A C    1 
ATOM   2202 O  O    A ASP   A 1 105 ? 23.983 -8.407  -11.226 0.78 20.93 ?  105 ASP   A O    1 
ATOM   2203 O  O    B ASP   A 1 105 ? 23.906 -8.370  -11.161 0.22 24.48 ?  105 ASP   A O    1 
ATOM   2204 C  CB   A ASP   A 1 105 ? 25.225 -8.783  -13.887 0.78 29.18 ?  105 ASP   A CB   1 
ATOM   2205 C  CB   B ASP   A 1 105 ? 25.128 -8.895  -13.787 0.22 26.67 ?  105 ASP   A CB   1 
ATOM   2206 C  CG   A ASP   A 1 105 ? 24.797 -10.204 -14.174 0.78 32.28 ?  105 ASP   A CG   1 
ATOM   2207 C  CG   B ASP   A 1 105 ? 24.787 -10.374 -13.787 0.22 27.80 ?  105 ASP   A CG   1 
ATOM   2208 O  OD1  A ASP   A 1 105 ? 23.578 -10.447 -14.268 0.78 33.05 ?  105 ASP   A OD1  1 
ATOM   2209 O  OD1  B ASP   A 1 105 ? 23.590 -10.716 -13.886 0.22 27.93 ?  105 ASP   A OD1  1 
ATOM   2210 O  OD2  A ASP   A 1 105 ? 25.685 -11.075 -14.310 0.78 33.79 -1 105 ASP   A OD2  1 
ATOM   2211 O  OD2  B ASP   A 1 105 ? 25.722 -11.196 -13.680 0.22 28.44 -1 105 ASP   A OD2  1 
ATOM   2212 H  H    A ASP   A 1 105 ? 25.407 -6.444  -13.414 0.78 29.16 ?  105 ASP   A H    1 
ATOM   2213 H  H    B ASP   A 1 105 ? 25.188 -6.511  -13.486 0.22 29.76 ?  105 ASP   A H    1 
ATOM   2214 H  HA   A ASP   A 1 105 ? 23.412 -7.908  -14.290 0.78 30.91 ?  105 ASP   A HA   1 
ATOM   2215 H  HA   B ASP   A 1 105 ? 23.272 -8.147  -14.248 0.22 30.58 ?  105 ASP   A HA   1 
ATOM   2216 H  HB2  A ASP   A 1 105 ? 25.684 -8.443  -14.674 0.78 35.07 ?  105 ASP   A HB2  1 
ATOM   2217 H  HB2  B ASP   A 1 105 ? 25.507 -8.669  -14.653 0.22 32.06 ?  105 ASP   A HB2  1 
ATOM   2218 H  HB3  A ASP   A 1 105 ? 25.835 -8.799  -13.133 0.78 35.07 ?  105 ASP   A HB3  1 
ATOM   2219 H  HB3  B ASP   A 1 105 ? 25.784 -8.741  -13.090 0.22 32.06 ?  105 ASP   A HB3  1 
ATOM   2220 N  N    A ILE   A 1 106 ? 22.065 -8.654  -12.386 0.78 23.10 ?  106 ILE   A N    1 
ATOM   2221 N  N    B ILE   A 1 106 ? 21.958 -8.695  -12.258 0.22 24.53 ?  106 ILE   A N    1 
ATOM   2222 C  CA   A ILE   A 1 106 ? 21.294 -9.052  -11.212 0.78 22.59 ?  106 ILE   A CA   1 
ATOM   2223 C  CA   B ILE   A 1 106 ? 21.240 -9.071  -11.047 0.22 24.25 ?  106 ILE   A CA   1 
ATOM   2224 C  C    A ILE   A 1 106 ? 21.826 -10.336 -10.599 0.78 21.50 ?  106 ILE   A C    1 
ATOM   2225 C  C    B ILE   A 1 106 ? 21.779 -10.370 -10.468 0.22 23.87 ?  106 ILE   A C    1 
ATOM   2226 O  O    A ILE   A 1 106 ? 21.613 -10.581 -9.408  0.78 20.44 ?  106 ILE   A O    1 
ATOM   2227 O  O    B ILE   A 1 106 ? 21.589 -10.639 -9.276  0.22 23.61 ?  106 ILE   A O    1 
ATOM   2228 C  CB   A ILE   A 1 106 ? 19.787 -9.147  -11.551 0.78 24.09 ?  106 ILE   A CB   1 
ATOM   2229 C  CB   B ILE   A 1 106 ? 19.721 -9.135  -11.314 0.22 24.62 ?  106 ILE   A CB   1 
ATOM   2230 C  CG1  A ILE   A 1 106 ? 18.944 -9.204  -10.274 0.78 24.90 ?  106 ILE   A CG1  1 
ATOM   2231 C  CG1  B ILE   A 1 106 ? 18.936 -9.243  -10.002 0.22 24.76 ?  106 ILE   A CG1  1 
ATOM   2232 C  CG2  A ILE   A 1 106 ? 19.502 -10.369 -12.409 0.78 24.72 ?  106 ILE   A CG2  1 
ATOM   2233 C  CG2  B ILE   A 1 106 ? 19.389 -10.311 -12.220 0.22 24.83 ?  106 ILE   A CG2  1 
ATOM   2234 C  CD1  A ILE   A 1 106 ? 19.087 -7.984  -9.390  0.78 25.30 ?  106 ILE   A CD1  1 
ATOM   2235 C  CD1  B ILE   A 1 106 ? 19.185 -8.101  -9.036  0.22 24.78 ?  106 ILE   A CD1  1 
ATOM   2236 H  H    A ILE   A 1 106 ? 21.628 -8.657  -13.118 0.78 27.77 ?  106 ILE   A H    1 
ATOM   2237 H  H    B ILE   A 1 106 ? 21.482 -8.709  -12.970 0.22 29.49 ?  106 ILE   A H    1 
ATOM   2238 H  HA   A ILE   A 1 106 ? 21.403 -8.369  -10.543 0.78 27.17 ?  106 ILE   A HA   1 
ATOM   2239 H  HA   B ILE   A 1 106 ? 21.395 -8.384  -10.385 0.22 29.15 ?  106 ILE   A HA   1 
ATOM   2240 H  HB   A ILE   A 1 106 ? 19.535 -8.355  -12.051 0.78 28.96 ?  106 ILE   A HB   1 
ATOM   2241 H  HB   B ILE   A 1 106 ? 19.452 -8.318  -11.763 0.22 29.60 ?  106 ILE   A HB   1 
ATOM   2242 H  HG12 A ILE   A 1 106 ? 18.009 -9.280  -10.520 0.78 29.93 ?  106 ILE   A HG12 1 
ATOM   2243 H  HG12 B ILE   A 1 106 ? 17.986 -9.251  -10.205 0.22 29.76 ?  106 ILE   A HG12 1 
ATOM   2244 H  HG13 A ILE   A 1 106 ? 19.211 -9.978  -9.756  0.78 29.93 ?  106 ILE   A HG13 1 
ATOM   2245 H  HG13 B ILE   A 1 106 ? 19.180 -10.067 -9.555  0.22 29.76 ?  106 ILE   A HG13 1 
ATOM   2246 H  HG21 A ILE   A 1 106 ? 18.613 -10.285 -12.790 0.78 29.72 ?  106 ILE   A HG21 1 
ATOM   2247 H  HG21 B ILE   A 1 106 ? 18.470 -10.229 -12.519 0.22 29.85 ?  106 ILE   A HG21 1 
ATOM   2248 H  HG22 A ILE   A 1 106 ? 20.163 -10.416 -13.116 0.78 29.72 ?  106 ILE   A HG22 1 
ATOM   2249 H  HG22 B ILE   A 1 106 ? 19.988 -10.297 -12.982 0.22 29.85 ?  106 ILE   A HG22 1 
ATOM   2250 H  HG23 A ILE   A 1 106 ? 19.550 -11.163 -11.855 0.78 29.72 ?  106 ILE   A HG23 1 
ATOM   2251 H  HG23 B ILE   A 1 106 ? 19.503 -11.136 -11.723 0.22 29.85 ?  106 ILE   A HG23 1 
ATOM   2252 H  HD11 A ILE   A 1 106 ? 18.348 -7.960  -8.766  0.78 30.41 ?  106 ILE   A HD11 1 
ATOM   2253 H  HD11 B ILE   A 1 106 ? 18.485 -8.096  -8.366  0.22 29.80 ?  106 ILE   A HD11 1 
ATOM   2254 H  HD12 A ILE   A 1 106 ? 19.927 -8.040  -8.906  0.78 30.41 ?  106 ILE   A HD12 1 
ATOM   2255 H  HD12 B ILE   A 1 106 ? 20.048 -8.229  -8.610  0.22 29.80 ?  106 ILE   A HD12 1 
ATOM   2256 H  HD13 A ILE   A 1 106 ? 19.077 -7.189  -9.946  0.78 30.41 ?  106 ILE   A HD13 1 
ATOM   2257 H  HD13 B ILE   A 1 106 ? 19.178 -7.265  -9.527  0.22 29.80 ?  106 ILE   A HD13 1 
ATOM   2258 N  N    A GLN   A 1 107 ? 22.522 -11.164 -11.387 0.78 22.23 ?  107 GLN   A N    1 
ATOM   2259 N  N    B GLN   A 1 107 ? 22.458 -11.184 -11.281 0.22 23.91 ?  107 GLN   A N    1 
ATOM   2260 C  CA   A GLN   A 1 107 ? 23.145 -12.369 -10.847 0.78 24.67 ?  107 GLN   A CA   1 
ATOM   2261 C  CA   B GLN   A 1 107 ? 23.095 -12.387 -10.760 0.22 23.99 ?  107 GLN   A CA   1 
ATOM   2262 C  C    A GLN   A 1 107 ? 24.115 -12.036 -9.721  0.78 22.17 ?  107 GLN   A C    1 
ATOM   2263 C  C    B GLN   A 1 107 ? 24.171 -12.060 -9.735  0.22 21.50 ?  107 GLN   A C    1 
ATOM   2264 O  O    A GLN   A 1 107 ? 24.335 -12.860 -8.825  0.78 23.31 ?  107 GLN   A O    1 
ATOM   2265 O  O    B GLN   A 1 107 ? 24.539 -12.931 -8.939  0.22 22.04 ?  107 GLN   A O    1 
ATOM   2266 C  CB   A GLN   A 1 107 ? 23.862 -13.129 -11.969 0.78 29.54 ?  107 GLN   A CB   1 
ATOM   2267 C  CB   B GLN   A 1 107 ? 23.675 -13.222 -11.906 0.22 26.49 ?  107 GLN   A CB   1 
ATOM   2268 C  CG   A GLN   A 1 107 ? 23.010 -13.355 -13.217 0.78 34.59 ?  107 GLN   A CG   1 
ATOM   2269 C  CG   B GLN   A 1 107 ? 22.625 -13.743 -12.881 0.22 28.81 ?  107 GLN   A CG   1 
ATOM   2270 C  CD   A GLN   A 1 107 ? 21.742 -14.134 -12.930 0.78 38.94 ?  107 GLN   A CD   1 
ATOM   2271 C  CD   B GLN   A 1 107 ? 21.515 -14.516 -12.191 0.22 30.75 ?  107 GLN   A CD   1 
ATOM   2272 O  OE1  A GLN   A 1 107 ? 21.781 -15.202 -12.318 0.78 40.49 ?  107 GLN   A OE1  1 
ATOM   2273 O  OE1  B GLN   A 1 107 ? 21.770 -15.328 -11.301 0.22 31.38 ?  107 GLN   A OE1  1 
ATOM   2274 N  NE2  A GLN   A 1 107 ? 20.606 -13.600 -13.368 0.78 40.10 ?  107 GLN   A NE2  1 
ATOM   2275 N  NE2  B GLN   A 1 107 ? 20.275 -14.258 -12.594 0.22 31.30 ?  107 GLN   A NE2  1 
ATOM   2276 H  H    A GLN   A 1 107 ? 22.639 -11.055 -12.228 0.78 26.73 ?  107 GLN   A H    1 
ATOM   2277 H  H    B GLN   A 1 107 ? 22.561 -11.062 -12.126 0.22 28.75 ?  107 GLN   A H    1 
ATOM   2278 H  HA   A GLN   A 1 107 ? 22.466 -12.954 -10.483 0.78 29.66 ?  107 GLN   A HA   1 
ATOM   2279 H  HA   B GLN   A 1 107 ? 22.426 -12.921 -10.314 0.22 28.85 ?  107 GLN   A HA   1 
ATOM   2280 H  HB2  A GLN   A 1 107 ? 24.649 -12.629 -12.238 0.78 35.51 ?  107 GLN   A HB2  1 
ATOM   2281 H  HB2  B GLN   A 1 107 ? 24.300 -12.677 -12.410 0.22 31.85 ?  107 GLN   A HB2  1 
ATOM   2282 H  HB3  A GLN   A 1 107 ? 24.129 -14.003 -11.640 0.78 35.51 ?  107 GLN   A HB3  1 
ATOM   2283 H  HB3  B GLN   A 1 107 ? 24.136 -13.988 -11.533 0.22 31.85 ?  107 GLN   A HB3  1 
ATOM   2284 H  HG2  A GLN   A 1 107 ? 22.756 -12.498 -13.595 0.78 41.56 ?  107 GLN   A HG2  1 
ATOM   2285 H  HG2  B GLN   A 1 107 ? 22.224 -12.992 -13.345 0.22 34.63 ?  107 GLN   A HG2  1 
ATOM   2286 H  HG3  A GLN   A 1 107 ? 23.529 -13.855 -13.866 0.78 41.56 ?  107 GLN   A HG3  1 
ATOM   2287 H  HG3  B GLN   A 1 107 ? 23.051 -14.338 -13.517 0.22 34.63 ?  107 GLN   A HG3  1 
ATOM   2288 H  HE21 A GLN   A 1 107 ? 20.617 -12.851 -13.791 0.78 48.18 ?  107 GLN   A HE21 1 
ATOM   2289 H  HE21 B GLN   A 1 107 ? 20.137 -13.682 -13.217 0.22 37.62 ?  107 GLN   A HE21 1 
ATOM   2290 H  HE22 A GLN   A 1 107 ? 19.860 -14.005 -13.229 0.78 48.18 ?  107 GLN   A HE22 1 
ATOM   2291 H  HE22 B GLN   A 1 107 ? 19.610 -14.667 -12.233 0.22 37.62 ?  107 GLN   A HE22 1 
ATOM   2292 N  N    . LEU   A 1 108 ? 24.680 -10.825 -9.729  1.00 18.55 ?  108 LEU   A N    1 
ATOM   2293 C  CA   . LEU   A 1 108 ? 25.605 -10.409 -8.685  1.00 15.53 ?  108 LEU   A CA   1 
ATOM   2294 C  C    . LEU   A 1 108 ? 24.917 -10.249 -7.339  1.00 13.39 ?  108 LEU   A C    1 
ATOM   2295 O  O    . LEU   A 1 108 ? 25.606 -10.088 -6.327  1.00 13.68 ?  108 LEU   A O    1 
ATOM   2296 C  CB   . LEU   A 1 108 ? 26.321 -9.112  -9.087  1.00 15.17 ?  108 LEU   A CB   1 
ATOM   2297 C  CG   . LEU   A 1 108 ? 27.306 -9.301  -10.242 1.00 16.89 ?  108 LEU   A CG   1 
ATOM   2298 C  CD1  . LEU   A 1 108 ? 27.797 -7.962  -10.768 1.00 17.44 ?  108 LEU   A CD1  1 
ATOM   2299 C  CD2  . LEU   A 1 108 ? 28.488 -10.164 -9.818  1.00 19.01 ?  108 LEU   A CD2  1 
ATOM   2300 H  H    A LEU   A 1 108 ? 24.537 -10.227 -10.325 0.78 22.32 ?  108 LEU   A H    1 
ATOM   2301 H  H    B LEU   A 1 108 ? 24.516 -10.225 -10.317 0.22 22.32 ?  108 LEU   A H    1 
ATOM   2302 H  HA   . LEU   A 1 108 ? 26.279 -11.094 -8.575  1.00 18.69 ?  108 LEU   A HA   1 
ATOM   2303 H  HB2  . LEU   A 1 108 ? 25.659 -8.459  -9.364  1.00 18.27 ?  108 LEU   A HB2  1 
ATOM   2304 H  HB3  . LEU   A 1 108 ? 26.817 -8.776  -8.325  1.00 18.27 ?  108 LEU   A HB3  1 
ATOM   2305 H  HG   . LEU   A 1 108 ? 26.852 -9.756  -10.968 1.00 20.32 ?  108 LEU   A HG   1 
ATOM   2306 H  HD11 . LEU   A 1 108 ? 28.387 -8.117  -11.527 1.00 20.99 ?  108 LEU   A HD11 1 
ATOM   2307 H  HD12 . LEU   A 1 108 ? 27.038 -7.429  -11.045 1.00 20.99 ?  108 LEU   A HD12 1 
ATOM   2308 H  HD13 . LEU   A 1 108 ? 28.286 -7.504  -10.065 1.00 20.99 ?  108 LEU   A HD13 1 
ATOM   2309 H  HD21 . LEU   A 1 108 ? 29.178 -10.101 -10.493 1.00 22.87 ?  108 LEU   A HD21 1 
ATOM   2310 H  HD22 . LEU   A 1 108 ? 28.820 -9.841  -8.967  1.00 22.87 ?  108 LEU   A HD22 1 
ATOM   2311 H  HD23 . LEU   A 1 108 ? 28.189 -11.083 -9.730  1.00 22.87 ?  108 LEU   A HD23 1 
ATOM   2312 N  N    . LEU   A 1 109 ? 23.584 -10.300 -7.292  1.00 12.96 ?  109 LEU   A N    1 
ATOM   2313 C  CA   . LEU   A 1 109 ? 22.897 -10.170 -6.015  1.00 11.91 ?  109 LEU   A CA   1 
ATOM   2314 C  C    . LEU   A 1 109 ? 23.246 -11.323 -5.081  1.00 11.17 ?  109 LEU   A C    1 
ATOM   2315 O  O    . LEU   A 1 109 ? 23.387 -11.128 -3.868  1.00 11.73 ?  109 LEU   A O    1 
ATOM   2316 C  CB   . LEU   A 1 109 ? 21.390 -10.085 -6.253  1.00 12.59 ?  109 LEU   A CB   1 
ATOM   2317 C  CG   . LEU   A 1 109 ? 20.505 -9.807  -5.039  1.00 12.38 ?  109 LEU   A CG   1 
ATOM   2318 C  CD1  . LEU   A 1 109 ? 20.941 -8.537  -4.323  1.00 12.99 ?  109 LEU   A CD1  1 
ATOM   2319 C  CD2  . LEU   A 1 109 ? 19.045 -9.703  -5.466  1.00 13.49 ?  109 LEU   A CD2  1 
ATOM   2320 H  H    . LEU   A 1 109 ? 23.065 -10.399 -7.970  1.00 15.60 ?  109 LEU   A H    1 
ATOM   2321 H  HA   . LEU   A 1 109 ? 23.181 -9.348  -5.587  1.00 14.34 ?  109 LEU   A HA   1 
ATOM   2322 H  HB2  . LEU   A 1 109 ? 21.227 -9.373  -6.890  1.00 15.17 ?  109 LEU   A HB2  1 
ATOM   2323 H  HB3  . LEU   A 1 109 ? 21.096 -10.927 -6.630  1.00 15.17 ?  109 LEU   A HB3  1 
ATOM   2324 H  HG   . LEU   A 1 109 ? 20.581 -10.544 -4.415  1.00 14.91 ?  109 LEU   A HG   1 
ATOM   2325 H  HD11 . LEU   A 1 109 ? 20.268 -8.295  -3.667  1.00 15.64 ?  109 LEU   A HD11 1 
ATOM   2326 H  HD12 . LEU   A 1 109 ? 21.790 -8.693  -3.885  1.00 15.64 ?  109 LEU   A HD12 1 
ATOM   2327 H  HD13 . LEU   A 1 109 ? 21.031 -7.820  -4.976  1.00 15.64 ?  109 LEU   A HD13 1 
ATOM   2328 H  HD21 . LEU   A 1 109 ? 18.513 -9.403  -4.712  1.00 16.24 ?  109 LEU   A HD21 1 
ATOM   2329 H  HD22 . LEU   A 1 109 ? 18.968 -9.077  -6.198  1.00 16.24 ?  109 LEU   A HD22 1 
ATOM   2330 H  HD23 . LEU   A 1 109 ? 18.736 -10.584 -5.753  1.00 16.24 ?  109 LEU   A HD23 1 
ATOM   2331 N  N    . LYS   A 1 110 ? 23.387 -12.538 -5.618  1.00 11.05 ?  110 LYS   A N    1 
ATOM   2332 C  CA   . LYS   A 1 110 ? 23.766 -13.657 -4.760  1.00 11.24 ?  110 LYS   A CA   1 
ATOM   2333 C  C    . LYS   A 1 110 ? 25.152 -13.432 -4.161  1.00 10.86 ?  110 LYS   A C    1 
ATOM   2334 O  O    . LYS   A 1 110 ? 25.361 -13.627 -2.961  1.00 11.01 ?  110 LYS   A O    1 
ATOM   2335 C  CB   . LYS   A 1 110 ? 23.685 -14.983 -5.522  1.00 12.11 ?  110 LYS   A CB   1 
ATOM   2336 C  CG   . LYS   A 1 110 ? 23.887 -16.197 -4.617  1.00 12.12 ?  110 LYS   A CG   1 
ATOM   2337 C  CD   . LYS   A 1 110 ? 23.667 -17.518 -5.333  1.00 12.75 ?  110 LYS   A CD   1 
ATOM   2338 C  CE   . LYS   A 1 110 ? 23.769 -18.689 -4.373  1.00 13.55 ?  110 LYS   A CE   1 
ATOM   2339 N  NZ   . LYS   A 1 110 ? 22.586 -18.821 -3.483  1.00 14.27 ?  110 LYS   A NZ   1 
ATOM   2340 H  H    . LYS   A 1 110 ? 23.263 -12.742 -6.444  1.00 13.32 ?  110 LYS   A H    1 
ATOM   2341 H  HA   . LYS   A 1 110 ? 23.134 -13.712 -4.022  1.00 13.55 ?  110 LYS   A HA   1 
ATOM   2342 H  HB2  . LYS   A 1 110 ? 22.808 -15.059 -5.931  1.00 14.59 ?  110 LYS   A HB2  1 
ATOM   2343 H  HB3  . LYS   A 1 110 ? 24.373 -14.999 -6.200  1.00 14.59 ?  110 LYS   A HB3  1 
ATOM   2344 H  HG2  . LYS   A 1 110 ? 24.792 -16.190 -4.271  1.00 14.60 ?  110 LYS   A HG2  1 
ATOM   2345 H  HG3  . LYS   A 1 110 ? 23.254 -16.152 -3.880  1.00 14.60 ?  110 LYS   A HG3  1 
ATOM   2346 H  HD2  . LYS   A 1 110 ? 22.788 -17.528 -5.733  1.00 15.35 ?  110 LYS   A HD2  1 
ATOM   2347 H  HD3  . LYS   A 1 110 ? 24.352 -17.628 -6.015  1.00 15.35 ?  110 LYS   A HD3  1 
ATOM   2348 H  HE2  . LYS   A 1 110 ? 23.851 -19.511 -4.881  1.00 16.32 ?  110 LYS   A HE2  1 
ATOM   2349 H  HE3  . LYS   A 1 110 ? 24.550 -18.571 -3.809  1.00 16.32 ?  110 LYS   A HE3  1 
ATOM   2350 H  HZ1  . LYS   A 1 110 ? 22.683 -19.515 -2.940  1.00 17.18 ?  110 LYS   A HZ1  1 
ATOM   2351 H  HZ2  . LYS   A 1 110 ? 22.487 -18.080 -2.996  1.00 17.18 ?  110 LYS   A HZ2  1 
ATOM   2352 H  HZ3  . LYS   A 1 110 ? 21.849 -18.937 -3.975  1.00 17.18 ?  110 LYS   A HZ3  1 
ATOM   2353 N  N    . SER   A 1 111 ? 26.108 -12.998 -4.985  1.00 11.15 ?  111 SER   A N    1 
ATOM   2354 C  CA   . SER   A 1 111 ? 27.442 -12.687 -4.476  1.00 11.36 ?  111 SER   A CA   1 
ATOM   2355 C  C    . SER   A 1 111 ? 27.378 -11.639 -3.369  1.00 10.94 ?  111 SER   A C    1 
ATOM   2356 O  O    . SER   A 1 111 ? 28.080 -11.742 -2.356  1.00 11.52 ?  111 SER   A O    1 
ATOM   2357 C  CB   . SER   A 1 111 ? 28.320 -12.191 -5.625  1.00 12.58 ?  111 SER   A CB   1 
ATOM   2358 O  OG   . SER   A 1 111 ? 28.428 -13.189 -6.630  1.00 14.73 ?  111 SER   A OG   1 
ATOM   2359 H  H    . SER   A 1 111 ? 26.006 -12.876 -5.827  1.00 13.43 ?  111 SER   A H    1 
ATOM   2360 H  HA   . SER   A 1 111 ? 27.842 -13.491 -4.113  1.00 13.69 ?  111 SER   A HA   1 
ATOM   2361 H  HB2  . SER   A 1 111 ? 27.911 -11.398 -6.013  1.00 15.15 ?  111 SER   A HB2  1 
ATOM   2362 H  HB3  . SER   A 1 111 ? 29.198 -11.975 -5.280  1.00 15.15 ?  111 SER   A HB3  1 
ATOM   2363 H  HG   . SER   A 1 111 ? 28.925 -12.906 -7.256  1.00 17.73 ?  111 SER   A HG   1 
ATOM   2364 N  N    . ALA   A 1 112 ? 26.535 -10.621 -3.547  1.00 11.19 ?  112 ALA   A N    1 
ATOM   2365 C  CA   . ALA   A 1 112 ? 26.393 -9.582  -2.530  1.00 10.84 ?  112 ALA   A CA   1 
ATOM   2366 C  C    . ALA   A 1 112 ? 25.915 -10.178 -1.208  1.00 10.81 ?  112 ALA   A C    1 
ATOM   2367 O  O    . ALA   A 1 112 ? 26.467 -9.884  -0.141  1.00 10.95 ?  112 ALA   A O    1 
ATOM   2368 C  CB   . ALA   A 1 112 ? 25.439 -8.490  -3.028  1.00 11.30 ?  112 ALA   A CB   1 
ATOM   2369 H  H    . ALA   A 1 112 ? 26.043 -10.505 -4.239  1.00 13.49 ?  112 ALA   A H    1 
ATOM   2370 H  HA   . ALA   A 1 112 ? 27.253 -9.167  -2.372  1.00 13.07 ?  112 ALA   A HA   1 
ATOM   2371 H  HB1  . ALA   A 1 112 ? 25.367 -7.793  -2.348  1.00 13.61 ?  112 ALA   A HB1  1 
ATOM   2372 H  HB2  . ALA   A 1 112 ? 25.788 -8.109  -3.847  1.00 13.61 ?  112 ALA   A HB2  1 
ATOM   2373 H  HB3  . ALA   A 1 112 ? 24.563 -8.876  -3.189  1.00 13.61 ?  112 ALA   A HB3  1 
ATOM   2374 N  N    . TYR   A 1 113 ? 24.883 -11.024 -1.255  1.00 10.80 ?  113 TYR   A N    1 
ATOM   2375 C  CA   . TYR   A 1 113 ? 24.380 -11.627 -0.023  1.00 10.62 ?  113 TYR   A CA   1 
ATOM   2376 C  C    . TYR   A 1 113 ? 25.387 -12.575 0.623   1.00 10.33 ?  113 TYR   A C    1 
ATOM   2377 O  O    . TYR   A 1 113 ? 25.346 -12.763 1.843   1.00 10.77 ?  113 TYR   A O    1 
ATOM   2378 C  CB   . TYR   A 1 113 ? 23.062 -12.360 -0.287  1.00 10.85 ?  113 TYR   A CB   1 
ATOM   2379 C  CG   . TYR   A 1 113 ? 21.841 -11.468 -0.192  1.00 10.72 ?  113 TYR   A CG   1 
ATOM   2380 C  CD1  . TYR   A 1 113 ? 21.485 -10.875 1.015   1.00 10.76 ?  113 TYR   A CD1  1 
ATOM   2381 C  CD2  . TYR   A 1 113 ? 21.031 -11.235 -1.295  1.00 11.04 ?  113 TYR   A CD2  1 
ATOM   2382 C  CE1  . TYR   A 1 113 ? 20.359 -10.074 1.123   1.00 10.95 ?  113 TYR   A CE1  1 
ATOM   2383 C  CE2  . TYR   A 1 113 ? 19.879 -10.433 -1.191  1.00 11.04 ?  113 TYR   A CE2  1 
ATOM   2384 C  CZ   . TYR   A 1 113 ? 19.560 -9.858  0.021   1.00 11.00 ?  113 TYR   A CZ   1 
ATOM   2385 O  OH   . TYR   A 1 113 ? 18.437 -9.074  0.155   1.00 11.47 ?  113 TYR   A OH   1 
ATOM   2386 H  H    . TYR   A 1 113 ? 24.463 -11.250 -1.968  1.00 13.01 ?  113 TYR   A H    1 
ATOM   2387 H  HA   . TYR   A 1 113 ? 24.201 -10.922 0.616   1.00 12.80 ?  113 TYR   A HA   1 
ATOM   2388 H  HB2  . TYR   A 1 113 ? 23.084 -12.729 -1.183  1.00 13.07 ?  113 TYR   A HB2  1 
ATOM   2389 H  HB3  . TYR   A 1 113 ? 22.963 -13.069 0.362   1.00 13.07 ?  113 TYR   A HB3  1 
ATOM   2390 H  HD1  . TYR   A 1 113 ? 22.015 -11.022 1.766   1.00 12.97 ?  113 TYR   A HD1  1 
ATOM   2391 H  HD2  . TYR   A 1 113 ? 21.238 -11.628 -2.109  1.00 13.31 ?  113 TYR   A HD2  1 
ATOM   2392 H  HE1  . TYR   A 1 113 ? 20.138 -9.691  1.943   1.00 13.19 ?  113 TYR   A HE1  1 
ATOM   2393 H  HE2  . TYR   A 1 113 ? 19.334 -10.279 -1.932  1.00 13.30 ?  113 TYR   A HE2  1 
ATOM   2394 H  HH   . TYR   A 1 113 ? 18.038 -9.022  -0.588  1.00 13.83 ?  113 TYR   A HH   1 
ATOM   2395 N  N    . GLU   A 1 114 ? 26.287 -13.189 -0.160  1.00 10.46 ?  114 GLU   A N    1 
ATOM   2396 C  CA   . GLU   A 1 114 ? 27.278 -14.088 0.434   1.00 10.68 ?  114 GLU   A CA   1 
ATOM   2397 C  C    . GLU   A 1 114 ? 28.130 -13.380 1.482   1.00 10.72 ?  114 GLU   A C    1 
ATOM   2398 O  O    . GLU   A 1 114 ? 28.607 -14.014 2.433   1.00 11.08 ?  114 GLU   A O    1 
ATOM   2399 C  CB   . GLU   A 1 114 ? 28.147 -14.729 -0.659  1.00 10.99 ?  114 GLU   A CB   1 
ATOM   2400 C  CG   . GLU   A 1 114 ? 27.379 -15.784 -1.437  1.00 11.35 ?  114 GLU   A CG   1 
ATOM   2401 C  CD   . GLU   A 1 114 ? 28.080 -16.317 -2.680  1.00 11.64 ?  114 GLU   A CD   1 
ATOM   2402 O  OE1  . GLU   A 1 114 ? 29.034 -15.687 -3.182  1.00 11.86 ?  114 GLU   A OE1  1 
ATOM   2403 O  OE2  . GLU   A 1 114 ? 27.631 -17.380 -3.166  1.00 12.82 -1 114 GLU   A OE2  1 
ATOM   2404 H  H    . GLU   A 1 114 ? 26.347 -13.095 -1.021  1.00 12.60 ?  114 GLU   A H    1 
ATOM   2405 H  HA   . GLU   A 1 114 ? 26.807 -14.802 0.877   1.00 12.87 ?  114 GLU   A HA   1 
ATOM   2406 H  HB2  . GLU   A 1 114 ? 28.429 -14.045 -1.290  1.00 13.25 ?  114 GLU   A HB2  1 
ATOM   2407 H  HB3  . GLU   A 1 114 ? 28.912 -15.153 -0.255  1.00 13.25 ?  114 GLU   A HB3  1 
ATOM   2408 H  HG2  . GLU   A 1 114 ? 27.210 -16.537 -0.850  1.00 13.67 ?  114 GLU   A HG2  1 
ATOM   2409 H  HG3  . GLU   A 1 114 ? 26.529 -15.404 -1.723  1.00 13.67 ?  114 GLU   A HG3  1 
ATOM   2410 N  N    . ASN   A 1 115 ? 28.312 -12.062 1.349   1.00 10.59 ?  115 ASN   A N    1 
ATOM   2411 C  CA   . ASN   A 1 115 ? 29.080 -11.333 2.354   1.00 10.91 ?  115 ASN   A CA   1 
ATOM   2412 C  C    . ASN   A 1 115 ? 28.467 -11.465 3.741   1.00 10.86 ?  115 ASN   A C    1 
ATOM   2413 O  O    . ASN   A 1 115 ? 29.183 -11.396 4.747   1.00 11.06 ?  115 ASN   A O    1 
ATOM   2414 C  CB   . ASN   A 1 115 ? 29.181 -9.857  1.973   1.00 11.39 ?  115 ASN   A CB   1 
ATOM   2415 C  CG   . ASN   A 1 115 ? 29.979 -9.637  0.708   1.00 11.88 ?  115 ASN   A CG   1 
ATOM   2416 O  OD1  . ASN   A 1 115 ? 31.203 -9.732  0.721   1.00 15.29 ?  115 ASN   A OD1  1 
ATOM   2417 N  ND2  . ASN   A 1 115 ? 29.299 -9.335  -0.382  1.00 11.20 ?  115 ASN   A ND2  1 
ATOM   2418 H  H    . ASN   A 1 115 ? 28.011 -11.578 0.702   1.00 12.76 ?  115 ASN   A H    1 
ATOM   2419 H  HA   . ASN   A 1 115 ? 29.979 -11.696 2.389   1.00 13.15 ?  115 ASN   A HA   1 
ATOM   2420 H  HB2  . ASN   A 1 115 ? 28.288 -9.504  1.841   1.00 13.73 ?  115 ASN   A HB2  1 
ATOM   2421 H  HB3  . ASN   A 1 115 ? 29.619 -9.378  2.700   1.00 13.73 ?  115 ASN   A HB3  1 
ATOM   2422 H  HD21 . ASN   A 1 115 ? 29.712 -9.194  -1.121  1.00 13.49 ?  115 ASN   A HD21 1 
ATOM   2423 H  HD22 . ASN   A 1 115 ? 28.438 -9.303  -0.357  1.00 13.49 ?  115 ASN   A HD22 1 
ATOM   2424 N  N    . PHE   A 1 116 ? 27.141 -11.626 3.822   1.00 10.77 ?  116 PHE   A N    1 
ATOM   2425 C  CA   . PHE   A 1 116 ? 26.492 -11.727 5.126   1.00 10.64 ?  116 PHE   A CA   1 
ATOM   2426 C  C    . PHE   A 1 116 ? 26.971 -12.958 5.895   1.00 10.84 ?  116 PHE   A C    1 
ATOM   2427 O  O    . PHE   A 1 116 ? 26.897 -12.979 7.124   1.00 11.53 ?  116 PHE   A O    1 
ATOM   2428 C  CB   . PHE   A 1 116 ? 24.965 -11.857 4.988   1.00 10.85 ?  116 PHE   A CB   1 
ATOM   2429 C  CG   . PHE   A 1 116 ? 24.210 -10.606 4.539   1.00 10.66 ?  116 PHE   A CG   1 
ATOM   2430 C  CD1  . PHE   A 1 116 ? 24.780 -9.572  3.804   1.00 10.69 ?  116 PHE   A CD1  1 
ATOM   2431 C  CD2  . PHE   A 1 116 ? 22.852 -10.506 4.856   1.00 11.09 ?  116 PHE   A CD2  1 
ATOM   2432 C  CE1  . PHE   A 1 116 ? 24.010 -8.492  3.398   1.00 10.91 ?  116 PHE   A CE1  1 
ATOM   2433 C  CE2  . PHE   A 1 116 ? 22.090 -9.432  4.456   1.00 11.27 ?  116 PHE   A CE2  1 
ATOM   2434 C  CZ   . PHE   A 1 116 ? 22.663 -8.424  3.729   1.00 10.78 ?  116 PHE   A CZ   1 
ATOM   2435 H  H    . PHE   A 1 116 ? 26.604 -11.669 3.145   1.00 12.98 ?  116 PHE   A H    1 
ATOM   2436 H  HA   . PHE   A 1 116 ? 26.687 -10.936 5.650   1.00 12.83 ?  116 PHE   A HA   1 
ATOM   2437 H  HB2  . PHE   A 1 116 ? 24.780 -12.556 4.338   1.00 13.08 ?  116 PHE   A HB2  1 
ATOM   2438 H  HB3  . PHE   A 1 116 ? 24.607 -12.120 5.849   1.00 13.08 ?  116 PHE   A HB3  1 
ATOM   2439 H  HD1  . PHE   A 1 116 ? 25.676 -9.626  3.570   1.00 12.89 ?  116 PHE   A HD1  1 
ATOM   2440 H  HD2  . PHE   A 1 116 ? 22.447 -11.198 5.340   1.00 13.36 ?  116 PHE   A HD2  1 
ATOM   2441 H  HE1  . PHE   A 1 116 ? 24.401 -7.804  2.912   1.00 13.15 ?  116 PHE   A HE1  1 
ATOM   2442 H  HE2  . PHE   A 1 116 ? 21.189 -9.394  4.687   1.00 13.58 ?  116 PHE   A HE2  1 
ATOM   2443 H  HZ   . PHE   A 1 116 ? 22.156 -7.690  3.473   1.00 12.99 ?  116 PHE   A HZ   1 
ATOM   2444 N  N    . ASN   A 1 117 ? 27.407 -14.011 5.189   1.00 10.96 ?  117 ASN   A N    1 
ATOM   2445 C  CA   . ASN   A 1 117 ? 27.779 -15.256 5.856   1.00 11.25 ?  117 ASN   A CA   1 
ATOM   2446 C  C    . ASN   A 1 117 ? 29.044 -15.134 6.688   1.00 11.67 ?  117 ASN   A C    1 
ATOM   2447 O  O    . ASN   A 1 117 ? 29.343 -16.053 7.460   1.00 12.82 ?  117 ASN   A O    1 
ATOM   2448 C  CB   . ASN   A 1 117 ? 27.895 -16.384 4.835   1.00 11.59 ?  117 ASN   A CB   1 
ATOM   2449 C  CG   . ASN   A 1 117 ? 26.543 -16.770 4.300   1.00 11.39 ?  117 ASN   A CG   1 
ATOM   2450 O  OD1  . ASN   A 1 117 ? 25.570 -16.792 5.053   1.00 12.31 ?  117 ASN   A OD1  1 
ATOM   2451 N  ND2  . ASN   A 1 117 ? 26.452 -17.029 3.007   1.00 11.44 ?  117 ASN   A ND2  1 
ATOM   2452 H  H    . ASN   A 1 117 ? 27.480 -14.028 4.328   1.00 13.21 ?  117 ASN   A H    1 
ATOM   2453 H  HA   . ASN   A 1 117 ? 27.057 -15.489 6.464   1.00 13.56 ?  117 ASN   A HA   1 
ATOM   2454 H  HB2  . ASN   A 1 117 ? 28.446 -16.091 4.095   1.00 13.96 ?  117 ASN   A HB2  1 
ATOM   2455 H  HB3  . ASN   A 1 117 ? 28.279 -17.161 5.263   1.00 13.96 ?  117 ASN   A HB3  1 
ATOM   2456 H  HD21 . ASN   A 1 117 ? 25.698 -17.244 2.667   1.00 13.78 ?  117 ASN   A HD21 1 
ATOM   2457 H  HD22 . ASN   A 1 117 ? 27.157 -16.989 2.513   1.00 13.78 ?  117 ASN   A HD22 1 
ATOM   2458 N  N    . GLN   A 1 118 ? 29.773 -14.026 6.563   1.00 11.98 ?  118 GLN   A N    1 
ATOM   2459 C  CA   . GLN   A 1 118 ? 30.956 -13.789 7.377   1.00 12.52 ?  118 GLN   A CA   1 
ATOM   2460 C  C    . GLN   A 1 118 ? 30.620 -13.216 8.747   1.00 12.35 ?  118 GLN   A C    1 
ATOM   2461 O  O    . GLN   A 1 118 ? 31.539 -12.929 9.524   1.00 13.94 ?  118 GLN   A O    1 
ATOM   2462 C  CB   . GLN   A 1 118 ? 31.944 -12.886 6.631   1.00 12.56 ?  118 GLN   A CB   1 
ATOM   2463 C  CG   . GLN   A 1 118 ? 32.415 -13.471 5.309   1.00 12.27 ?  118 GLN   A CG   1 
ATOM   2464 C  CD   . GLN   A 1 118 ? 33.244 -14.732 5.486   1.00 12.71 ?  118 GLN   A CD   1 
ATOM   2465 O  OE1  . GLN   A 1 118 ? 34.108 -14.799 6.370   1.00 13.67 ?  118 GLN   A OE1  1 
ATOM   2466 N  NE2  . GLN   A 1 118 ? 32.992 -15.736 4.643   1.00 12.84 ?  118 GLN   A NE2  1 
ATOM   2467 H  H    . GLN   A 1 118 ? 29.593 -13.382 6.013   1.00 14.44 ?  118 GLN   A H    1 
ATOM   2468 H  HA   . GLN   A 1 118 ? 31.390 -14.644 7.520   1.00 15.08 ?  118 GLN   A HA   1 
ATOM   2469 H  HB2  . GLN   A 1 118 ? 31.514 -12.037 6.452   1.00 15.13 ?  118 GLN   A HB2  1 
ATOM   2470 H  HB3  . GLN   A 1 118 ? 32.722 -12.752 7.195   1.00 15.13 ?  118 GLN   A HB3  1 
ATOM   2471 H  HG2  . GLN   A 1 118 ? 31.643 -13.686 4.761   1.00 14.78 ?  118 GLN   A HG2  1 
ATOM   2472 H  HG3  . GLN   A 1 118 ? 32.969 -12.814 4.853   1.00 14.78 ?  118 GLN   A HG3  1 
ATOM   2473 H  HE21 . GLN   A 1 118 ? 32.375 -15.652 4.039   1.00 15.46 ?  118 GLN   A HE21 1 
ATOM   2474 H  HE22 . GLN   A 1 118 ? 33.426 -16.474 4.701   1.00 15.46 ?  118 GLN   A HE22 1 
ATOM   2475 N  N    . HIS   A 1 119 ? 29.333 -13.065 9.068   1.00 12.00 ?  119 HIS   A N    1 
ATOM   2476 C  CA   . HIS   A 1 119 ? 28.887 -12.458 10.317  1.00 12.40 ?  119 HIS   A CA   1 
ATOM   2477 C  C    . HIS   A 1 119 ? 27.751 -13.281 10.898  1.00 12.67 ?  119 HIS   A C    1 
ATOM   2478 O  O    . HIS   A 1 119 ? 26.797 -13.607 10.187  1.00 13.21 ?  119 HIS   A O    1 
ATOM   2479 C  CB   . HIS   A 1 119 ? 28.432 -11.023 10.050  1.00 12.83 ?  119 HIS   A CB   1 
ATOM   2480 C  CG   . HIS   A 1 119 ? 29.505 -10.215 9.419   1.00 14.43 ?  119 HIS   A CG   1 
ATOM   2481 N  ND1  . HIS   A 1 119 ? 30.492 -9.606  10.159  1.00 16.67 ?  119 HIS   A ND1  1 
ATOM   2482 C  CD2  . HIS   A 1 119 ? 29.826 -10.025 8.119   1.00 15.17 ?  119 HIS   A CD2  1 
ATOM   2483 C  CE1  . HIS   A 1 119 ? 31.350 -9.030  9.338   1.00 16.86 ?  119 HIS   A CE1  1 
ATOM   2484 N  NE2  . HIS   A 1 119 ? 30.976 -9.276  8.096   1.00 16.63 ?  119 HIS   A NE2  1 
ATOM   2485 H  H    . HIS   A 1 119 ? 28.678 -13.324 8.567   1.00 14.46 ?  119 HIS   A H    1 
ATOM   2486 H  HA   . HIS   A 1 119 ? 29.623 -12.446 10.953  1.00 14.93 ?  119 HIS   A HA   1 
ATOM   2487 H  HB2  . HIS   A 1 119 ? 27.669 -11.045 9.453   1.00 15.45 ?  119 HIS   A HB2  1 
ATOM   2488 H  HB3  . HIS   A 1 119 ? 28.193 -10.611 10.892  1.00 15.45 ?  119 HIS   A HB3  1 
ATOM   2489 H  HD2  . HIS   A 1 119 ? 29.354 -10.342 7.378   1.00 18.26 ?  119 HIS   A HD2  1 
ATOM   2490 H  HE1  . HIS   A 1 119 ? 32.092 -8.532  9.588   1.00 20.28 ?  119 HIS   A HE1  1 
ATOM   2491 H  HE2  . HIS   A 1 119 ? 31.370 -8.990  7.384   1.00 20.01 ?  119 HIS   A HE2  1 
ATOM   2492 N  N    . GLU   A 1 120 ? 27.843 -13.596 12.191  1.00 13.79 ?  120 GLU   A N    1 
ATOM   2493 C  CA   . GLU   A 1 120 ? 26.886 -14.525 12.786  1.00 16.06 ?  120 GLU   A CA   1 
ATOM   2494 C  C    . GLU   A 1 120 ? 25.472 -13.955 12.857  1.00 14.46 ?  120 GLU   A C    1 
ATOM   2495 O  O    . GLU   A 1 120 ? 24.496 -14.714 12.743  1.00 14.38 ?  120 GLU   A O    1 
ATOM   2496 C  CB   . GLU   A 1 120 ? 27.364 -14.944 14.177  1.00 22.02 ?  120 GLU   A CB   1 
ATOM   2497 C  CG   . GLU   A 1 120 ? 28.554 -15.891 14.168  1.00 31.12 ?  120 GLU   A CG   1 
ATOM   2498 C  CD   . GLU   A 1 120 ? 28.739 -16.596 15.498  1.00 40.62 ?  120 GLU   A CD   1 
ATOM   2499 O  OE1  . GLU   A 1 120 ? 28.262 -16.067 16.524  1.00 42.11 ?  120 GLU   A OE1  1 
ATOM   2500 O  OE2  . GLU   A 1 120 ? 29.359 -17.681 15.517  1.00 44.90 -1 120 GLU   A OE2  1 
ATOM   2501 H  H    . GLU   A 1 120 ? 28.446 -13.297 12.733  1.00 16.61 ?  120 GLU   A H    1 
ATOM   2502 H  HA   . GLU   A 1 120 ? 26.852 -15.322 12.242  1.00 19.32 ?  120 GLU   A HA   1 
ATOM   2503 H  HB2  . GLU   A 1 120 ? 27.628 -14.158 14.679  1.00 26.48 ?  120 GLU   A HB2  1 
ATOM   2504 H  HB3  . GLU   A 1 120 ? 26.640 -15.398 14.639  1.00 26.48 ?  120 GLU   A HB3  1 
ATOM   2505 H  HG2  . GLU   A 1 120 ? 28.426 -16.561 13.476  1.00 37.40 ?  120 GLU   A HG2  1 
ATOM   2506 H  HG3  . GLU   A 1 120 ? 29.366 -15.389 13.998  1.00 37.40 ?  120 GLU   A HG3  1 
ATOM   2507 N  N    . VAL   A 1 121 ? 25.342 -12.646 13.082  1.00 13.60 ?  121 VAL   A N    1 
ATOM   2508 C  CA   . VAL   A 1 121 ? 24.050 -11.976 13.207  1.00 13.72 ?  121 VAL   A CA   1 
ATOM   2509 C  C    . VAL   A 1 121 ? 24.156 -10.595 12.570  1.00 12.47 ?  121 VAL   A C    1 
ATOM   2510 O  O    . VAL   A 1 121 ? 25.127 -9.869  12.808  1.00 13.22 ?  121 VAL   A O    1 
ATOM   2511 C  CB   . VAL   A 1 121 ? 23.618 -11.828 14.684  1.00 16.61 ?  121 VAL   A CB   1 
ATOM   2512 C  CG1  . VAL   A 1 121 ? 22.243 -11.164 14.781  1.00 17.26 ?  121 VAL   A CG1  1 
ATOM   2513 C  CG2  . VAL   A 1 121 ? 23.612 -13.165 15.403  1.00 18.81 ?  121 VAL   A CG2  1 
ATOM   2514 H  H    . VAL   A 1 121 ? 26.010 -12.108 13.168  1.00 16.38 ?  121 VAL   A H    1 
ATOM   2515 H  HA   . VAL   A 1 121 ? 23.373 -12.489 12.738  1.00 16.52 ?  121 VAL   A HA   1 
ATOM   2516 H  HB   . VAL   A 1 121 ? 24.251 -11.254 15.138  1.00 19.98 ?  121 VAL   A HB   1 
ATOM   2517 H  HG11 . VAL   A 1 121 ? 21.922 -11.233 15.694  1.00 20.77 ?  121 VAL   A HG11 1 
ATOM   2518 H  HG12 . VAL   A 1 121 ? 22.322 -10.229 14.531  1.00 20.77 ?  121 VAL   A HG12 1 
ATOM   2519 H  HG13 . VAL   A 1 121 ? 21.629 -11.617 14.181  1.00 20.77 ?  121 VAL   A HG13 1 
ATOM   2520 H  HG21 . VAL   A 1 121 ? 23.267 -13.037 16.306  1.00 22.62 ?  121 VAL   A HG21 1 
ATOM   2521 H  HG22 . VAL   A 1 121 ? 23.036 -13.783 14.923  1.00 22.62 ?  121 VAL   A HG22 1 
ATOM   2522 H  HG23 . VAL   A 1 121 ? 24.513 -13.511 15.442  1.00 22.62 ?  121 VAL   A HG23 1 
ATOM   2523 N  N    . LEU   A 1 122 ? 23.139 -10.206 11.792  1.00 11.96 ?  122 LEU   A N    1 
ATOM   2524 C  CA   . LEU   A 1 122 ? 23.138 -8.905  11.127  1.00 11.63 ?  122 LEU   A CA   1 
ATOM   2525 C  C    . LEU   A 1 122 ? 21.740 -8.312  11.085  1.00 11.49 ?  122 LEU   A C    1 
ATOM   2526 O  O    . LEU   A 1 122 ? 20.748 -9.031  10.955  1.00 12.38 ?  122 LEU   A O    1 
ATOM   2527 C  CB   . LEU   A 1 122 ? 23.556 -8.997  9.655   1.00 13.03 ?  122 LEU   A CB   1 
ATOM   2528 C  CG   . LEU   A 1 122 ? 24.759 -9.859  9.299   1.00 12.95 ?  122 LEU   A CG   1 
ATOM   2529 C  CD1  . LEU   A 1 122 ? 24.348 -11.303 9.071   1.00 13.91 ?  122 LEU   A CD1  1 
ATOM   2530 C  CD2  . LEU   A 1 122 ? 25.450 -9.288  8.070   1.00 12.59 ?  122 LEU   A CD2  1 
ATOM   2531 H  H    . LEU   A 1 122 ? 22.437 -10.681 11.629  1.00 14.41 ?  122 LEU   A H    1 
ATOM   2532 H  HA   . LEU   A 1 122 ? 23.733 -8.291  11.590  1.00 14.01 ?  122 LEU   A HA   1 
ATOM   2533 H  HB2  . LEU   A 1 122 ? 22.810 -9.347  9.150   1.00 15.69 ?  122 LEU   A HB2  1 
ATOM   2534 H  HB3  . LEU   A 1 122 ? 23.759 -8.101  9.343   1.00 15.69 ?  122 LEU   A HB3  1 
ATOM   2535 H  HG   . LEU   A 1 122 ? 25.402 -9.841  10.028  1.00 15.59 ?  122 LEU   A HG   1 
ATOM   2536 H  HD11 . LEU   A 1 122 ? 25.119 -11.815 8.785   1.00 16.75 ?  122 LEU   A HD11 1 
ATOM   2537 H  HD12 . LEU   A 1 122 ? 24.000 -11.666 9.901   1.00 16.75 ?  122 LEU   A HD12 1 
ATOM   2538 H  HD13 . LEU   A 1 122 ? 23.661 -11.330 8.385   1.00 16.75 ?  122 LEU   A HD13 1 
ATOM   2539 H  HD21 . LEU   A 1 122 ? 26.192 -9.865  7.818   1.00 15.16 ?  122 LEU   A HD21 1 
ATOM   2540 H  HD22 . LEU   A 1 122 ? 24.813 -9.236  7.341   1.00 15.16 ?  122 LEU   A HD22 1 
ATOM   2541 H  HD23 . LEU   A 1 122 ? 25.787 -8.399  8.277   1.00 15.16 ?  122 LEU   A HD23 1 
ATOM   2542 N  N    A LEU   A 1 123 ? 21.678 -6.988  11.209  0.78 11.36 ?  123 LEU   A N    1 
ATOM   2543 N  N    B LEU   A 1 123 ? 21.687 -6.980  11.146  0.22 11.24 ?  123 LEU   A N    1 
ATOM   2544 C  CA   A LEU   A 1 123 ? 20.518 -6.189  10.837  0.78 11.17 ?  123 LEU   A CA   1 
ATOM   2545 C  CA   B LEU   A 1 123 ? 20.493 -6.198  10.844  0.22 11.14 ?  123 LEU   A CA   1 
ATOM   2546 C  C    A LEU   A 1 123 ? 20.764 -5.686  9.425   0.78 10.28 ?  123 LEU   A C    1 
ATOM   2547 C  C    B LEU   A 1 123 ? 20.702 -5.579  9.466   0.22 10.45 ?  123 LEU   A C    1 
ATOM   2548 O  O    A LEU   A 1 123 ? 21.831 -5.133  9.151   0.78 10.70 ?  123 LEU   A O    1 
ATOM   2549 O  O    B LEU   A 1 123 ? 21.676 -4.849  9.260   0.22 10.39 ?  123 LEU   A O    1 
ATOM   2550 C  CB   A LEU   A 1 123 ? 20.393 -4.992  11.780  0.78 11.51 ?  123 LEU   A CB   1 
ATOM   2551 C  CB   B LEU   A 1 123 ? 20.299 -5.100  11.894  0.22 11.64 ?  123 LEU   A CB   1 
ATOM   2552 C  CG   A LEU   A 1 123 ? 19.317 -3.951  11.461  0.78 12.39 ?  123 LEU   A CG   1 
ATOM   2553 C  CG   B LEU   A 1 123 ? 19.368 -3.948  11.489  0.22 11.49 ?  123 LEU   A CG   1 
ATOM   2554 C  CD1  A LEU   A 1 123 ? 17.929 -4.574  11.470  0.78 13.25 ?  123 LEU   A CD1  1 
ATOM   2555 C  CD1  B LEU   A 1 123 ? 17.922 -4.419  11.403  0.22 11.54 ?  123 LEU   A CD1  1 
ATOM   2556 C  CD2  A LEU   A 1 123 ? 19.395 -2.787  12.448  0.78 13.13 ?  123 LEU   A CD2  1 
ATOM   2557 C  CD2  B LEU   A 1 123 ? 19.504 -2.761  12.432  0.22 11.60 ?  123 LEU   A CD2  1 
ATOM   2558 H  H    A LEU   A 1 123 ? 22.329 -6.514  11.517  0.78 13.69 ?  123 LEU   A H    1 
ATOM   2559 H  H    B LEU   A 1 123 ? 22.365 -6.488  11.351  0.22 13.55 ?  123 LEU   A H    1 
ATOM   2560 H  HA   A LEU   A 1 123 ? 19.709 -6.723  10.862  0.78 13.46 ?  123 LEU   A HA   1 
ATOM   2561 H  HA   B LEU   A 1 123 ? 19.708 -6.765  10.828  0.22 13.43 ?  123 LEU   A HA   1 
ATOM   2562 H  HB2  A LEU   A 1 123 ? 20.197 -5.331  12.669  0.78 13.86 ?  123 LEU   A HB2  1 
ATOM   2563 H  HB2  B LEU   A 1 123 ? 19.927 -5.507  12.699  0.22 14.02 ?  123 LEU   A HB2  1 
ATOM   2564 H  HB3  A LEU   A 1 123 ? 21.238 -4.527  11.793  0.78 13.86 ?  123 LEU   A HB3  1 
ATOM   2565 H  HB3  B LEU   A 1 123 ? 21.165 -4.716  12.105  0.22 14.02 ?  123 LEU   A HB3  1 
ATOM   2566 H  HG   A LEU   A 1 123 ? 19.471 -3.591  10.573  0.78 14.93 ?  123 LEU   A HG   1 
ATOM   2567 H  HG   B LEU   A 1 123 ? 19.616 -3.626  10.612  0.22 13.84 ?  123 LEU   A HG   1 
ATOM   2568 H  HD11 A LEU   A 1 123 ? 17.268 -3.882  11.313  0.78 15.95 ?  123 LEU   A HD11 1 
ATOM   2569 H  HD11 B LEU   A 1 123 ? 17.362 -3.671  11.147  0.22 13.90 ?  123 LEU   A HD11 1 
ATOM   2570 H  HD12 A LEU   A 1 123 ? 17.880 -5.243  10.769  0.78 15.95 ?  123 LEU   A HD12 1 
ATOM   2571 H  HD12 B LEU   A 1 123 ? 17.856 -5.124  10.737  0.22 13.90 ?  123 LEU   A HD12 1 
ATOM   2572 H  HD13 A LEU   A 1 123 ? 17.776 -4.989  12.334  0.78 15.95 ?  123 LEU   A HD13 1 
ATOM   2573 H  HD13 B LEU   A 1 123 ? 17.646 -4.759  12.269  0.22 13.90 ?  123 LEU   A HD13 1 
ATOM   2574 H  HD21 A LEU   A 1 123 ? 18.706 -2.138  12.232  0.78 15.81 ?  123 LEU   A HD21 1 
ATOM   2575 H  HD21 B LEU   A 1 123 ? 18.901 -2.059  12.138  0.22 13.97 ?  123 LEU   A HD21 1 
ATOM   2576 H  HD22 A LEU   A 1 123 ? 19.254 -3.127  13.348  0.78 15.81 ?  123 LEU   A HD22 1 
ATOM   2577 H  HD22 B LEU   A 1 123 ? 19.273 -3.042  13.330  0.22 13.97 ?  123 LEU   A HD22 1 
ATOM   2578 H  HD23 A LEU   A 1 123 ? 20.269 -2.376  12.383  0.78 15.81 ?  123 LEU   A HD23 1 
ATOM   2579 H  HD23 B LEU   A 1 123 ? 20.419 -2.443  12.406  0.22 13.97 ?  123 LEU   A HD23 1 
ATOM   2580 N  N    . ALA   A 1 124 ? 19.800 -5.862  8.530   1.00 10.09 ?  124 ALA   A N    1 
ATOM   2581 C  CA   . ALA   A 1 124 ? 20.056 -5.562  7.133   1.00 10.25 ?  124 ALA   A CA   1 
ATOM   2582 C  C    . ALA   A 1 124 ? 18.821 -5.106  6.375   1.00 9.86  ?  124 ALA   A C    1 
ATOM   2583 O  O    . ALA   A 1 124 ? 17.692 -5.469  6.736   1.00 10.84 ?  124 ALA   A O    1 
ATOM   2584 C  CB   . ALA   A 1 124 ? 20.633 -6.794  6.419   1.00 10.98 ?  124 ALA   A CB   1 
ATOM   2585 H  H    A ALA   A 1 124 ? 19.007 -6.149  8.705   0.78 12.16 ?  124 ALA   A H    1 
ATOM   2586 H  H    B ALA   A 1 124 ? 19.047 -6.253  8.677   0.22 12.16 ?  124 ALA   A H    1 
ATOM   2587 H  HA   . ALA   A 1 124 ? 20.727 -4.865  7.097   1.00 12.35 ?  124 ALA   A HA   1 
ATOM   2588 H  HB1  . ALA   A 1 124 ? 20.801 -6.576  5.488   1.00 13.23 ?  124 ALA   A HB1  1 
ATOM   2589 H  HB2  . ALA   A 1 124 ? 21.474 -7.042  6.849   1.00 13.23 ?  124 ALA   A HB2  1 
ATOM   2590 H  HB3  . ALA   A 1 124 ? 20.005 -7.524  6.483   1.00 13.23 ?  124 ALA   A HB3  1 
ATOM   2591 N  N    A PRO   A 1 125 ? 19.016 -4.371  5.277   0.78 9.90  ?  125 PRO   A N    1 
ATOM   2592 N  N    B PRO   A 1 125 ? 18.997 -4.266  5.361   0.22 9.93  ?  125 PRO   A N    1 
ATOM   2593 C  CA   A PRO   A 1 125 ? 17.957 -4.131  4.296   0.78 10.09 ?  125 PRO   A CA   1 
ATOM   2594 C  CA   B PRO   A 1 125 ? 17.906 -3.968  4.434   0.22 10.06 ?  125 PRO   A CA   1 
ATOM   2595 C  C    A PRO   A 1 125 ? 17.995 -5.206  3.214   0.78 9.91  ?  125 PRO   A C    1 
ATOM   2596 C  C    B PRO   A 1 125 ? 17.929 -5.003  3.312   0.22 10.10 ?  125 PRO   A C    1 
ATOM   2597 O  O    A PRO   A 1 125 ? 18.958 -5.967  3.092   0.78 10.65 ?  125 PRO   A O    1 
ATOM   2598 O  O    B PRO   A 1 125 ? 18.838 -5.832  3.223   0.22 10.11 ?  125 PRO   A O    1 
ATOM   2599 C  CB   A PRO   A 1 125 ? 18.403 -2.794  3.690   0.78 10.34 ?  125 PRO   A CB   1 
ATOM   2600 C  CB   B PRO   A 1 125 ? 18.303 -2.584  3.905   0.22 10.19 ?  125 PRO   A CB   1 
ATOM   2601 C  CG   A PRO   A 1 125 ? 19.915 -2.964  3.595   0.78 9.93  ?  125 PRO   A CG   1 
ATOM   2602 C  CG   B PRO   A 1 125 ? 19.794 -2.656  3.845   0.22 10.33 ?  125 PRO   A CG   1 
ATOM   2603 C  CD   A PRO   A 1 125 ? 20.296 -3.775  4.835   0.78 9.88  ?  125 PRO   A CD   1 
ATOM   2604 C  CD   B PRO   A 1 125 ? 20.212 -3.491  5.036   0.22 10.23 ?  125 PRO   A CD   1 
ATOM   2605 H  HA   A PRO   A 1 125 ? 17.080 -4.069  4.704   0.78 12.16 ?  125 PRO   A HA   1 
ATOM   2606 H  HA   B PRO   A 1 125 ? 17.049 -3.924  4.898   0.22 12.12 ?  125 PRO   A HA   1 
ATOM   2607 H  HB2  A PRO   A 1 125 ? 18.000 -2.678  2.811   0.78 12.46 ?  125 PRO   A HB2  1 
ATOM   2608 H  HB2  B PRO   A 1 125 ? 17.926 -2.446  3.024   0.22 12.29 ?  125 PRO   A HB2  1 
ATOM   2609 H  HB3  A PRO   A 1 125 ? 18.161 -2.066  4.282   0.78 12.46 ?  125 PRO   A HB3  1 
ATOM   2610 H  HB3  B PRO   A 1 125 ? 18.011 -1.885  4.519   0.22 12.29 ?  125 PRO   A HB3  1 
ATOM   2611 H  HG2  A PRO   A 1 125 ? 20.140 -3.451  2.783   0.78 11.97 ?  125 PRO   A HG2  1 
ATOM   2612 H  HG2  B PRO   A 1 125 ? 20.060 -3.085  3.018   0.22 12.45 ?  125 PRO   A HG2  1 
ATOM   2613 H  HG3  A PRO   A 1 125 ? 20.343 -2.095  3.601   0.78 11.97 ?  125 PRO   A HG3  1 
ATOM   2614 H  HG3  B PRO   A 1 125 ? 20.171 -1.766  3.901   0.22 12.45 ?  125 PRO   A HG3  1 
ATOM   2615 H  HD2  A PRO   A 1 125 ? 20.940 -4.463  4.600   0.78 11.92 ?  125 PRO   A HD2  1 
ATOM   2616 H  HD2  B PRO   A 1 125 ? 20.941 -4.084  4.790   0.22 12.33 ?  125 PRO   A HD2  1 
ATOM   2617 H  HD3  A PRO   A 1 125 ? 20.648 -3.183  5.521   0.78 11.92 ?  125 PRO   A HD3  1 
ATOM   2618 H  HD3  B PRO   A 1 125 ? 20.462 -2.916  5.778   0.22 12.33 ?  125 PRO   A HD3  1 
ATOM   2619 N  N    A LEU   A 1 126 ? 16.941 -5.227  2.396   0.78 10.12 ?  126 LEU   A N    1 
ATOM   2620 N  N    B LEU   A 1 126 ? 16.915 -4.946  2.447   0.22 10.37 ?  126 LEU   A N    1 
ATOM   2621 C  CA   A LEU   A 1 126 ? 16.947 -6.047  1.191   0.78 10.69 ?  126 LEU   A CA   1 
ATOM   2622 C  CA   B LEU   A 1 126 ? 16.905 -5.809  1.269   0.22 9.95  ?  126 LEU   A CA   1 
ATOM   2623 C  C    A LEU   A 1 126 ? 17.862 -5.426  0.138   0.78 10.88 ?  126 LEU   A C    1 
ATOM   2624 C  C    B LEU   A 1 126 ? 17.886 -5.260  0.238   0.22 9.69  ?  126 LEU   A C    1 
ATOM   2625 O  O    A LEU   A 1 126 ? 17.598 -4.328  -0.365  0.78 11.74 ?  126 LEU   A O    1 
ATOM   2626 O  O    B LEU   A 1 126 ? 17.755 -4.116  -0.207  0.22 9.85  ?  126 LEU   A O    1 
ATOM   2627 C  CB   A LEU   A 1 126 ? 15.533 -6.207  0.645   0.78 11.29 ?  126 LEU   A CB   1 
ATOM   2628 C  CB   B LEU   A 1 126 ? 15.505 -5.895  0.669   0.22 10.07 ?  126 LEU   A CB   1 
ATOM   2629 C  CG   A LEU   A 1 126 ? 14.649 -7.174  1.432   0.78 12.28 ?  126 LEU   A CG   1 
ATOM   2630 C  CG   B LEU   A 1 126 ? 14.479 -6.719  1.445   0.22 9.74  ?  126 LEU   A CG   1 
ATOM   2631 C  CD1  A LEU   A 1 126 ? 13.210 -7.056  0.976   0.78 13.78 ?  126 LEU   A CD1  1 
ATOM   2632 C  CD1  B LEU   A 1 126 ? 13.117 -6.613  0.776   0.22 10.05 ?  126 LEU   A CD1  1 
ATOM   2633 C  CD2  A LEU   A 1 126 ? 15.131 -8.610  1.273   0.78 12.06 ?  126 LEU   A CD2  1 
ATOM   2634 C  CD2  B LEU   A 1 126 ? 14.907 -8.177  1.552   0.22 9.74  ?  126 LEU   A CD2  1 
ATOM   2635 H  H    A LEU   A 1 126 ? 16.224 -4.763  2.507   0.78 12.19 ?  126 LEU   A H    1 
ATOM   2636 H  H    B LEU   A 1 126 ? 16.222 -4.426  2.502   0.22 12.50 ?  126 LEU   A H    1 
ATOM   2637 H  HA   A LEU   A 1 126 ? 17.292 -6.919  1.403   0.78 12.89 ?  126 LEU   A HA   1 
ATOM   2638 H  HA   B LEU   A 1 126 ? 17.192 -6.700  1.523   0.22 11.99 ?  126 LEU   A HA   1 
ATOM   2639 H  HB2  A LEU   A 1 126 ? 15.092 -5.341  0.655   0.78 13.61 ?  126 LEU   A HB2  1 
ATOM   2640 H  HB2  B LEU   A 1 126 ? 15.149 -4.998  0.591   0.22 12.13 ?  126 LEU   A HB2  1 
ATOM   2641 H  HB3  A LEU   A 1 126 ? 15.584 -6.534  -0.267  0.78 13.61 ?  126 LEU   A HB3  1 
ATOM   2642 H  HB3  B LEU   A 1 126 ? 15.579 -6.289  -0.214  0.22 12.13 ?  126 LEU   A HB3  1 
ATOM   2643 H  HG   A LEU   A 1 126 ? 14.687 -6.951  2.375   0.78 14.79 ?  126 LEU   A HG   1 
ATOM   2644 H  HG   B LEU   A 1 126 ? 14.399 -6.363  2.344   0.22 11.74 ?  126 LEU   A HG   1 
ATOM   2645 H  HD11 A LEU   A 1 126 ? 12.664 -7.679  1.482   0.78 16.59 ?  126 LEU   A HD11 1 
ATOM   2646 H  HD11 B LEU   A 1 126 ? 12.475 -7.140  1.277   0.22 12.11 ?  126 LEU   A HD11 1 
ATOM   2647 H  HD12 A LEU   A 1 126 ? 12.906 -6.150  1.127   0.78 16.59 ?  126 LEU   A HD12 1 
ATOM   2648 H  HD12 B LEU   A 1 126 ? 12.843 -5.683  0.760   0.22 12.11 ?  126 LEU   A HD12 1 
ATOM   2649 H  HD13 A LEU   A 1 126 ? 13.161 -7.270  0.030   0.78 16.59 ?  126 LEU   A HD13 1 
ATOM   2650 H  HD13 B LEU   A 1 126 ? 13.184 -6.953  -0.132  0.22 12.11 ?  126 LEU   A HD13 1 
ATOM   2651 H  HD21 A LEU   A 1 126 ? 14.476 -9.209  1.658   0.78 14.52 ?  126 LEU   A HD21 1 
ATOM   2652 H  HD21 B LEU   A 1 126 ? 14.170 -8.698  1.905   0.22 11.74 ?  126 LEU   A HD21 1 
ATOM   2653 H  HD22 A LEU   A 1 126 ? 15.241 -8.801  0.327   0.78 14.52 ?  126 LEU   A HD22 1 
ATOM   2654 H  HD22 B LEU   A 1 126 ? 15.149 -8.500  0.670   0.22 11.74 ?  126 LEU   A HD22 1 
ATOM   2655 H  HD23 A LEU   A 1 126 ? 15.982 -8.710  1.729   0.78 14.52 ?  126 LEU   A HD23 1 
ATOM   2656 H  HD23 B LEU   A 1 126 ? 15.671 -8.239  2.147   0.22 11.74 ?  126 LEU   A HD23 1 
ATOM   2657 N  N    A LEU   A 1 127 ? 18.934 -6.134  -0.204  0.78 11.04 ?  127 LEU   A N    1 
ATOM   2658 N  N    B LEU   A 1 127 ? 18.867 -6.070  -0.148  0.22 9.61  ?  127 LEU   A N    1 
ATOM   2659 C  CA   A LEU   A 1 127 ? 19.899 -5.632  -1.169  0.78 10.72 ?  127 LEU   A CA   1 
ATOM   2660 C  CA   B LEU   A 1 127 ? 19.884 -5.599  -1.077  0.22 9.45  ?  127 LEU   A CA   1 
ATOM   2661 C  C    A LEU   A 1 127 ? 19.264 -5.462  -2.540  0.78 10.25 ?  127 LEU   A C    1 
ATOM   2662 C  C    B LEU   A 1 127 ? 19.317 -5.472  -2.485  0.22 9.19  ?  127 LEU   A C    1 
ATOM   2663 O  O    A LEU   A 1 127 ? 18.429 -6.262  -2.976  0.78 10.88 ?  127 LEU   A O    1 
ATOM   2664 O  O    B LEU   A 1 127 ? 18.506 -6.289  -2.930  0.22 9.28  ?  127 LEU   A O    1 
ATOM   2665 C  CB   A LEU   A 1 127 ? 21.080 -6.596  -1.279  0.78 11.78 ?  127 LEU   A CB   1 
ATOM   2666 C  CB   B LEU   A 1 127 ? 21.086 -6.542  -1.075  0.22 9.55  ?  127 LEU   A CB   1 
ATOM   2667 C  CG   A LEU   A 1 127 ? 21.871 -6.896  -0.007  0.78 12.74 ?  127 LEU   A CG   1 
ATOM   2668 C  CG   B LEU   A 1 127 ? 21.904 -6.588  0.216   0.22 9.53  ?  127 LEU   A CG   1 
ATOM   2669 C  CD1  A LEU   A 1 127 ? 22.970 -7.902  -0.294  0.78 12.55 ?  127 LEU   A CD1  1 
ATOM   2670 C  CD1  B LEU   A 1 127 ? 23.047 -7.576  0.069   0.22 9.90  ?  127 LEU   A CD1  1 
ATOM   2671 C  CD2  A LEU   A 1 127 ? 22.465 -5.634  0.558   0.78 13.58 ?  127 LEU   A CD2  1 
ATOM   2672 C  CD2  B LEU   A 1 127 ? 22.436 -5.212  0.585   0.22 9.98  ?  127 LEU   A CD2  1 
ATOM   2673 H  H    A LEU   A 1 127 ? 19.122 -6.910  0.119   0.78 13.30 ?  127 LEU   A H    1 
ATOM   2674 H  H    B LEU   A 1 127 ? 18.967 -6.886  0.112   0.22 11.59 ?  127 LEU   A H    1 
ATOM   2675 H  HA   A LEU   A 1 127 ? 20.233 -4.774  -0.870  0.78 12.92 ?  127 LEU   A HA   1 
ATOM   2676 H  HA   B LEU   A 1 127 ? 20.185 -4.722  -0.799  0.22 11.40 ?  127 LEU   A HA   1 
ATOM   2677 H  HB2  A LEU   A 1 127 ? 20.746 -7.443  -1.609  0.78 14.20 ?  127 LEU   A HB2  1 
ATOM   2678 H  HB2  B LEU   A 1 127 ? 20.771 -7.442  -1.247  0.22 11.52 ?  127 LEU   A HB2  1 
ATOM   2679 H  HB3  A LEU   A 1 127 ? 21.708 -6.227  -1.917  0.78 14.20 ?  127 LEU   A HB3  1 
ATOM   2680 H  HB3  B LEU   A 1 127 ? 21.688 -6.270  -1.785  0.22 11.52 ?  127 LEU   A HB3  1 
ATOM   2681 H  HG   A LEU   A 1 127 ? 21.278 -7.284  0.660   0.78 15.34 ?  127 LEU   A HG   1 
ATOM   2682 H  HG   B LEU   A 1 127 ? 21.337 -6.897  0.941   0.22 11.50 ?  127 LEU   A HG   1 
ATOM   2683 H  HD11 A LEU   A 1 127 ? 23.446 -8.097  0.532   0.78 15.12 ?  127 LEU   A HD11 1 
ATOM   2684 H  HD11 B LEU   A 1 127 ? 23.628 -7.507  0.843   0.22 11.94 ?  127 LEU   A HD11 1 
ATOM   2685 H  HD12 A LEU   A 1 127 ? 22.575 -8.716  -0.644  0.78 15.12 ?  127 LEU   A HD12 1 
ATOM   2686 H  HD12 B LEU   A 1 127 ? 22.685 -8.474  0.007   0.22 11.94 ?  127 LEU   A HD12 1 
ATOM   2687 H  HD13 A LEU   A 1 127 ? 23.581 -7.524  -0.944  0.78 15.12 ?  127 LEU   A HD13 1 
ATOM   2688 H  HD13 B LEU   A 1 127 ? 23.546 -7.364  -0.736  0.22 11.94 ?  127 LEU   A HD13 1 
ATOM   2689 H  HD21 A LEU   A 1 127 ? 23.036 -5.859  1.308   0.78 16.36 ?  127 LEU   A HD21 1 
ATOM   2690 H  HD21 B LEU   A 1 127 ? 23.078 -5.307  1.307   0.22 12.03 ?  127 LEU   A HD21 1 
ATOM   2691 H  HD22 A LEU   A 1 127 ? 22.985 -5.196  -0.135  0.78 16.36 ?  127 LEU   A HD22 1 
ATOM   2692 H  HD22 B LEU   A 1 127 ? 22.867 -4.825  -0.192  0.22 12.03 ?  127 LEU   A HD22 1 
ATOM   2693 H  HD23 A LEU   A 1 127 ? 21.747 -5.052  0.850   0.78 16.36 ?  127 LEU   A HD23 1 
ATOM   2694 H  HD23 B LEU   A 1 127 ? 21.697 -4.655  0.869   0.22 12.03 ?  127 LEU   A HD23 1 
ATOM   2695 N  N    A SER   A 1 128 ? 19.697 -4.414  -3.230  0.78 10.41 ?  128 SER   A N    1 
ATOM   2696 N  N    B SER   A 1 128 ? 19.755 -4.427  -3.183  0.22 9.45  ?  128 SER   A N    1 
ATOM   2697 C  CA   A SER   A 1 128 ? 19.276 -4.042  -4.573  0.78 10.71 ?  128 SER   A CA   1 
ATOM   2698 C  CA   B SER   A 1 128 ? 19.375 -4.075  -4.547  0.22 9.63  ?  128 SER   A CA   1 
ATOM   2699 C  C    A SER   A 1 128 ? 17.816 -3.605  -4.660  0.78 10.72 ?  128 SER   A C    1 
ATOM   2700 C  C    B SER   A 1 128 ? 17.932 -3.599  -4.678  0.22 9.94  ?  128 SER   A C    1 
ATOM   2701 O  O    A SER   A 1 128 ? 17.358 -3.283  -5.757  0.78 12.32 ?  128 SER   A O    1 
ATOM   2702 O  O    B SER   A 1 128 ? 17.514 -3.263  -5.790  0.22 9.96  ?  128 SER   A O    1 
ATOM   2703 C  CB   A SER   A 1 128 ? 19.610 -5.103  -5.633  0.78 11.24 ?  128 SER   A CB   1 
ATOM   2704 C  CB   B SER   A 1 128 ? 19.668 -5.178  -5.576  0.22 9.75  ?  128 SER   A CB   1 
ATOM   2705 O  OG   A SER   A 1 128 ? 21.018 -5.319  -5.682  0.78 11.81 ?  128 SER   A OG   1 
ATOM   2706 O  OG   B SER   A 1 128 ? 21.067 -5.379  -5.701  0.22 10.05 ?  128 SER   A OG   1 
ATOM   2707 H  H    A SER   A 1 128 ? 20.301 -3.874  -2.919  0.78 12.54 ?  128 SER   A H    1 
ATOM   2708 H  H    B SER   A 1 128 ? 20.320 -3.865  -2.857  0.22 11.40 ?  128 SER   A H    1 
ATOM   2709 H  HA   A SER   A 1 128 ? 19.799 -3.268  -4.812  0.78 12.91 ?  128 SER   A HA   1 
ATOM   2710 H  HA   B SER   A 1 128 ? 19.930 -3.326  -4.802  0.22 11.61 ?  128 SER   A HA   1 
ATOM   2711 H  HB2  A SER   A 1 128 ? 19.163 -5.932  -5.410  0.78 13.54 ?  128 SER   A HB2  1 
ATOM   2712 H  HB2  B SER   A 1 128 ? 19.250 -6.002  -5.291  0.22 11.75 ?  128 SER   A HB2  1 
ATOM   2713 H  HB3  A SER   A 1 128 ? 19.301 -4.783  -6.501  0.78 13.54 ?  128 SER   A HB3  1 
ATOM   2714 H  HB3  B SER   A 1 128 ? 19.308 -4.905  -6.439  0.22 11.75 ?  128 SER   A HB3  1 
ATOM   2715 H  HG   A SER   A 1 128 ? 21.410 -4.606  -5.886  0.78 14.23 ?  128 SER   A HG   1 
ATOM   2716 H  HG   B SER   A 1 128 ? 21.436 -4.666  -5.951  0.22 12.12 ?  128 SER   A HG   1 
ATOM   2717 N  N    A ALA   A 1 129 ? 17.088 -3.550  -3.544  0.78 11.38 ?  129 ALA   A N    1 
ATOM   2718 N  N    B ALA   A 1 129 ? 17.171 -3.535  -3.589  0.22 10.56 ?  129 ALA   A N    1 
ATOM   2719 C  CA   A ALA   A 1 129 ? 15.720 -3.061  -3.533  0.78 12.19 ?  129 ALA   A CA   1 
ATOM   2720 C  CA   B ALA   A 1 129 ? 15.806 -3.032  -3.622  0.22 11.15 ?  129 ALA   A CA   1 
ATOM   2721 C  C    A ALA   A 1 129 ? 15.712 -1.531  -3.506  0.78 11.61 ?  129 ALA   A C    1 
ATOM   2722 C  C    B ALA   A 1 129 ? 15.821 -1.517  -3.414  0.22 11.29 ?  129 ALA   A C    1 
ATOM   2723 O  O    A ALA   A 1 129 ? 16.754 -0.868  -3.593  0.78 11.60 ?  129 ALA   A O    1 
ATOM   2724 O  O    B ALA   A 1 129 ? 16.876 -0.876  -3.425  0.22 11.30 ?  129 ALA   A O    1 
ATOM   2725 C  CB   A ALA   A 1 129 ? 14.953 -3.667  -2.357  0.78 13.41 ?  129 ALA   A CB   1 
ATOM   2726 C  CB   B ALA   A 1 129 ? 14.946 -3.783  -2.606  0.22 11.36 ?  129 ALA   A CB   1 
ATOM   2727 H  H    A ALA   A 1 129 ? 17.378 -3.795  -2.768  0.78 13.71 ?  129 ALA   A H    1 
ATOM   2728 H  H    B ALA   A 1 129 ? 17.431 -3.774  -2.805  0.22 12.73 ?  129 ALA   A H    1 
ATOM   2729 H  HA   A ALA   A 1 129 ? 15.287 -3.343  -4.349  0.78 14.69 ?  129 ALA   A HA   1 
ATOM   2730 H  HA   B ALA   A 1 129 ? 15.437 -3.202  -4.498  0.22 13.44 ?  129 ALA   A HA   1 
ATOM   2731 H  HB1  A ALA   A 1 129 ? 14.042 -3.338  -2.373  0.78 16.15 ?  129 ALA   A HB1  1 
ATOM   2732 H  HB1  B ALA   A 1 129 ? 14.118 -3.296  -2.467  0.22 13.69 ?  129 ALA   A HB1  1 
ATOM   2733 H  HB2  A ALA   A 1 129 ? 14.958 -4.634  -2.441  0.78 16.15 ?  129 ALA   A HB2  1 
ATOM   2734 H  HB2  B ALA   A 1 129 ? 14.759 -4.665  -2.950  0.22 13.69 ?  129 ALA   A HB2  1 
ATOM   2735 H  HB3  A ALA   A 1 129 ? 15.385 -3.407  -1.527  0.78 16.15 ?  129 ALA   A HB3  1 
ATOM   2736 H  HB3  B ALA   A 1 129 ? 15.432 -3.849  -1.767  0.22 13.69 ?  129 ALA   A HB3  1 
ATOM   2737 N  N    A GLY   A 1 130 ? 14.514 -0.959  -3.407  0.78 12.02 ?  130 GLY   A N    1 
ATOM   2738 N  N    B GLY   A 1 130 ? 14.646 -0.924  -3.224  0.22 11.79 ?  130 GLY   A N    1 
ATOM   2739 C  CA   A GLY   A 1 130 ? 14.399 0.487   -3.358  0.78 12.45 ?  130 GLY   A CA   1 
ATOM   2740 C  CA   B GLY   A 1 130 ? 14.589 0.518   -3.063  0.22 12.09 ?  130 GLY   A CA   1 
ATOM   2741 C  C    A GLY   A 1 130 ? 15.014 1.123   -4.587  0.78 11.84 ?  130 GLY   A C    1 
ATOM   2742 C  C    B GLY   A 1 130 ? 15.082 1.204   -4.321  0.22 12.16 ?  130 GLY   A C    1 
ATOM   2743 O  O    A GLY   A 1 130 ? 14.805 0.672   -5.717  0.78 11.81 ?  130 GLY   A O    1 
ATOM   2744 O  O    B GLY   A 1 130 ? 14.682 0.862   -5.439  0.22 11.96 ?  130 GLY   A O    1 
ATOM   2745 H  H    A GLY   A 1 130 ? 13.770 -1.386  -3.373  0.78 14.48 ?  130 GLY   A H    1 
ATOM   2746 H  H    B GLY   A 1 130 ? 13.887 -1.321  -3.185  0.22 14.20 ?  130 GLY   A H    1 
ATOM   2747 H  HA2  A GLY   A 1 130 ? 13.462 0.735   -3.308  0.78 15.00 ?  130 GLY   A HA2  1 
ATOM   2748 H  HA2  B GLY   A 1 130 ? 13.677 0.802   -2.872  0.22 14.56 ?  130 GLY   A HA2  1 
ATOM   2749 H  HA3  A GLY   A 1 130 ? 14.854 0.824   -2.573  0.78 15.00 ?  130 GLY   A HA3  1 
ATOM   2750 H  HA3  B GLY   A 1 130 ? 15.156 0.778   -2.323  0.22 14.56 ?  130 GLY   A HA3  1 
ATOM   2751 N  N    A ILE   A 1 131 ? 15.788 2.193   -4.366  0.78 12.24 ?  131 ILE   A N    1 
ATOM   2752 N  N    B ILE   A 1 131 ? 15.978 2.179   -4.143  0.22 12.73 ?  131 ILE   A N    1 
ATOM   2753 C  CA   A ILE   A 1 131 ? 16.354 2.972   -5.466  0.78 12.04 ?  131 ILE   A CA   1 
ATOM   2754 C  CA   B ILE   A 1 131 ? 16.477 2.956   -5.275  0.22 13.07 ?  131 ILE   A CA   1 
ATOM   2755 C  C    A ILE   A 1 131 ? 17.413 2.217   -6.262  0.78 11.44 ?  131 ILE   A C    1 
ATOM   2756 C  C    B ILE   A 1 131 ? 17.349 2.127   -6.213  0.22 13.24 ?  131 ILE   A C    1 
ATOM   2757 O  O    A ILE   A 1 131 ? 17.871 2.732   -7.292  0.78 11.97 ?  131 ILE   A O    1 
ATOM   2758 O  O    B ILE   A 1 131 ? 17.471 2.471   -7.394  0.22 13.50 ?  131 ILE   A O    1 
ATOM   2759 C  CB   A ILE   A 1 131 ? 16.871 4.353   -4.999  0.78 13.60 ?  131 ILE   A CB   1 
ATOM   2760 C  CB   B ILE   A 1 131 ? 17.180 4.249   -4.807  0.22 13.19 ?  131 ILE   A CB   1 
ATOM   2761 C  CG1  A ILE   A 1 131 ? 18.136 4.214   -4.142  0.78 14.53 ?  131 ILE   A CG1  1 
ATOM   2762 C  CG1  B ILE   A 1 131 ? 18.198 3.961   -3.700  0.22 13.53 ?  131 ILE   A CG1  1 
ATOM   2763 C  CG2  A ILE   A 1 131 ? 15.771 5.120   -4.254  0.78 14.68 ?  131 ILE   A CG2  1 
ATOM   2764 C  CG2  B ILE   A 1 131 ? 16.157 5.255   -4.315  0.22 13.23 ?  131 ILE   A CG2  1 
ATOM   2765 C  CD1  A ILE   A 1 131 ? 18.763 5.554   -3.759  0.78 16.10 ?  131 ILE   A CD1  1 
ATOM   2766 C  CD1  B ILE   A 1 131 ? 18.931 5.201   -3.215  0.22 13.67 ?  131 ILE   A CD1  1 
ATOM   2767 H  H    A ILE   A 1 131 ? 15.984 2.490   -3.583  0.78 14.74 ?  131 ILE   A H    1 
ATOM   2768 H  H    B ILE   A 1 131 ? 16.303 2.402   -3.382  0.22 15.33 ?  131 ILE   A H    1 
ATOM   2769 H  HA   A ILE   A 1 131 ? 15.634 3.150   -6.083  0.78 14.50 ?  131 ILE   A HA   1 
ATOM   2770 H  HA   B ILE   A 1 131 ? 15.715 3.235   -5.800  0.22 15.74 ?  131 ILE   A HA   1 
ATOM   2771 H  HB   A ILE   A 1 131 ? 17.100 4.861   -5.790  0.78 16.37 ?  131 ILE   A HB   1 
ATOM   2772 H  HB   B ILE   A 1 131 ? 17.649 4.639   -5.563  0.22 15.88 ?  131 ILE   A HB   1 
ATOM   2773 H  HG12 A ILE   A 1 131 ? 17.911 3.743   -3.325  0.78 17.50 ?  131 ILE   A HG12 1 
ATOM   2774 H  HG12 B ILE   A 1 131 ? 17.736 3.589   -2.933  0.22 16.29 ?  131 ILE   A HG12 1 
ATOM   2775 H  HG13 A ILE   A 1 131 ? 18.802 3.711   -4.638  0.78 17.50 ?  131 ILE   A HG13 1 
ATOM   2776 H  HG13 B ILE   A 1 131 ? 18.850 3.330   -4.032  0.22 16.29 ?  131 ILE   A HG13 1 
ATOM   2777 H  HG21 A ILE   A 1 131 ? 16.065 6.031   -4.108  0.78 17.67 ?  131 ILE   A HG21 1 
ATOM   2778 H  HG21 B ILE   A 1 131 ? 16.581 6.122   -4.225  0.22 15.93 ?  131 ILE   A HG21 1 
ATOM   2779 H  HG22 A ILE   A 1 131 ? 14.964 5.113   -4.792  0.78 17.67 ?  131 ILE   A HG22 1 
ATOM   2780 H  HG22 B ILE   A 1 131 ? 15.432 5.307   -4.957  0.22 15.93 ?  131 ILE   A HG22 1 
ATOM   2781 H  HG23 A ILE   A 1 131 ? 15.603 4.683   -3.404  0.78 17.67 ?  131 ILE   A HG23 1 
ATOM   2782 H  HG23 B ILE   A 1 131 ? 15.816 4.959   -3.457  0.22 15.93 ?  131 ILE   A HG23 1 
ATOM   2783 H  HD11 A ILE   A 1 131 ? 19.611 5.391   -3.317  0.78 19.37 ?  131 ILE   A HD11 1 
ATOM   2784 H  HD11 B ILE   A 1 131 ? 19.765 4.933   -2.800  0.22 16.46 ?  131 ILE   A HD11 1 
ATOM   2785 H  HD12 A ILE   A 1 131 ? 18.905 6.078   -4.563  0.78 19.37 ?  131 ILE   A HD12 1 
ATOM   2786 H  HD12 B ILE   A 1 131 ? 19.105 5.784   -3.970  0.22 16.46 ?  131 ILE   A HD12 1 
ATOM   2787 H  HD13 A ILE   A 1 131 ? 18.163 6.025   -3.160  0.78 19.37 ?  131 ILE   A HD13 1 
ATOM   2788 H  HD13 B ILE   A 1 131 ? 18.372 5.665   -2.571  0.22 16.46 ?  131 ILE   A HD13 1 
ATOM   2789 N  N    A PHE   A 1 132 ? 17.803 1.006   -5.834  0.78 10.83 ?  132 PHE   A N    1 
ATOM   2790 N  N    B PHE   A 1 132 ? 17.935 1.025   -5.737  0.22 13.08 ?  132 PHE   A N    1 
ATOM   2791 C  CA   A PHE   A 1 132 ? 18.668 0.167   -6.657  0.78 11.29 ?  132 PHE   A CA   1 
ATOM   2792 C  CA   B PHE   A 1 132 ? 18.816 0.236   -6.595  0.22 13.16 ?  132 PHE   A CA   1 
ATOM   2793 C  C    A PHE   A 1 132 ? 17.902 -0.600  -7.735  0.78 12.09 ?  132 PHE   A C    1 
ATOM   2794 C  C    B PHE   A 1 132 ? 18.069 -0.412  -7.757  0.22 13.23 ?  132 PHE   A C    1 
ATOM   2795 O  O    A PHE   A 1 132 ? 18.537 -1.241  -8.578  0.78 12.58 ?  132 PHE   A O    1 
ATOM   2796 O  O    B PHE   A 1 132 ? 18.705 -0.813  -8.737  0.22 13.34 ?  132 PHE   A O    1 
ATOM   2797 C  CB   A PHE   A 1 132 ? 19.491 -0.806  -5.798  0.78 11.04 ?  132 PHE   A CB   1 
ATOM   2798 C  CB   B PHE   A 1 132 ? 19.585 -0.808  -5.778  0.22 13.11 ?  132 PHE   A CB   1 
ATOM   2799 C  CG   A PHE   A 1 132 ? 20.731 -0.197  -5.159  0.78 10.72 ?  132 PHE   A CG   1 
ATOM   2800 C  CG   B PHE   A 1 132 ? 20.768 -0.250  -5.019  0.22 13.08 ?  132 PHE   A CG   1 
ATOM   2801 C  CD1  A PHE   A 1 132 ? 20.633 0.847   -4.254  0.78 11.19 ?  132 PHE   A CD1  1 
ATOM   2802 C  CD1  B PHE   A 1 132 ? 20.595 0.379   -3.796  0.22 13.16 ?  132 PHE   A CD1  1 
ATOM   2803 C  CD2  A PHE   A 1 132 ? 21.988 -0.731  -5.414  0.78 11.06 ?  132 PHE   A CD2  1 
ATOM   2804 C  CD2  B PHE   A 1 132 ? 22.054 -0.379  -5.521  0.22 13.03 ?  132 PHE   A CD2  1 
ATOM   2805 C  CE1  A PHE   A 1 132 ? 21.772 1.375   -3.646  0.78 11.40 ?  132 PHE   A CE1  1 
ATOM   2806 C  CE1  B PHE   A 1 132 ? 21.680 0.883   -3.096  0.22 12.95 ?  132 PHE   A CE1  1 
ATOM   2807 C  CE2  A PHE   A 1 132 ? 23.125 -0.210  -4.808  0.78 11.79 ?  132 PHE   A CE2  1 
ATOM   2808 C  CE2  B PHE   A 1 132 ? 23.144 0.121   -4.824  0.22 13.14 ?  132 PHE   A CE2  1 
ATOM   2809 C  CZ   A PHE   A 1 132 ? 23.013 0.851   -3.926  0.78 11.84 ?  132 PHE   A CZ   1 
ATOM   2810 C  CZ   B PHE   A 1 132 ? 22.956 0.753   -3.610  0.22 12.90 ?  132 PHE   A CZ   1 
ATOM   2811 H  H    A PHE   A 1 132 ? 17.580 0.652   -5.074  0.78 13.06 ?  132 PHE   A H    1 
ATOM   2812 H  H    B PHE   A 1 132 ? 17.827 0.713   -4.945  0.22 15.75 ?  132 PHE   A H    1 
ATOM   2813 H  HA   A PHE   A 1 132 ? 19.296 0.744   -7.108  0.78 13.60 ?  132 PHE   A HA   1 
ATOM   2814 H  HA   B PHE   A 1 132 ? 19.474 0.834   -6.977  0.22 15.85 ?  132 PHE   A HA   1 
ATOM   2815 H  HB2  A PHE   A 1 132 ? 18.928 -1.142  -5.081  0.78 13.30 ?  132 PHE   A HB2  1 
ATOM   2816 H  HB2  B PHE   A 1 132 ? 18.984 -1.198  -5.128  0.22 15.78 ?  132 PHE   A HB2  1 
ATOM   2817 H  HB3  A PHE   A 1 132 ? 19.780 -1.547  -6.357  0.78 13.30 ?  132 PHE   A HB3  1 
ATOM   2818 H  HB3  B PHE   A 1 132 ? 19.918 -1.495  -6.378  0.22 15.78 ?  132 PHE   A HB3  1 
ATOM   2819 H  HD1  A PHE   A 1 132 ? 19.804 1.213   -4.056  0.78 13.48 ?  132 PHE   A HD1  1 
ATOM   2820 H  HD1  B PHE   A 1 132 ? 19.740 0.469   -3.442  0.22 15.85 ?  132 PHE   A HD1  1 
ATOM   2821 H  HD2  A PHE   A 1 132 ? 22.073 -1.447  -6.009  0.78 13.33 ?  132 PHE   A HD2  1 
ATOM   2822 H  HD2  B PHE   A 1 132 ? 22.189 -0.801  -6.338  0.22 15.69 ?  132 PHE   A HD2  1 
ATOM   2823 H  HE1  A PHE   A 1 132 ? 21.698 2.089   -3.054  0.78 13.73 ?  132 PHE   A HE1  1 
ATOM   2824 H  HE1  B PHE   A 1 132 ? 21.552 1.304   -2.276  0.22 15.60 ?  132 PHE   A HE1  1 
ATOM   2825 H  HE2  A PHE   A 1 132 ? 23.961 -0.572  -5.007  0.78 14.20 ?  132 PHE   A HE2  1 
ATOM   2826 H  HE2  B PHE   A 1 132 ? 24.002 0.032   -5.176  0.22 15.82 ?  132 PHE   A HE2  1 
ATOM   2827 H  HZ   A PHE   A 1 132 ? 23.775 1.204   -3.526  0.78 14.27 ?  132 PHE   A HZ   1 
ATOM   2828 H  HZ   B PHE   A 1 132 ? 23.687 1.088   -3.142  0.22 15.53 ?  132 PHE   A HZ   1 
ATOM   2829 N  N    A GLY   A 1 133 ? 16.568 -0.567  -7.727  0.78 12.33 ?  133 GLY   A N    1 
ATOM   2830 N  N    B GLY   A 1 133 ? 16.743 -0.533  -7.673  0.22 13.16 ?  133 GLY   A N    1 
ATOM   2831 C  CA   A GLY   A 1 133 ? 15.791 -0.931  -8.897  0.78 13.02 ?  133 GLY   A CA   1 
ATOM   2832 C  CA   B GLY   A 1 133 ? 15.918 -0.834  -8.825  0.22 13.01 ?  133 GLY   A CA   1 
ATOM   2833 C  C    A GLY   A 1 133 ? 15.462 -2.399  -9.100  0.78 13.31 ?  133 GLY   A C    1 
ATOM   2834 C  C    B GLY   A 1 133 ? 15.388 -2.251  -8.919  0.22 12.82 ?  133 GLY   A C    1 
ATOM   2835 O  O    A GLY   A 1 133 ? 14.828 -2.723  -10.111 0.78 14.40 ?  133 GLY   A O    1 
ATOM   2836 O  O    B GLY   A 1 133 ? 14.495 -2.497  -9.739  0.22 12.80 ?  133 GLY   A O    1 
ATOM   2837 H  H    A GLY   A 1 133 ? 16.088 -0.335  -7.047  0.78 14.85 ?  133 GLY   A H    1 
ATOM   2838 H  H    B GLY   A 1 133 ? 16.298 -0.444  -6.945  0.22 15.84 ?  133 GLY   A H    1 
ATOM   2839 H  HA2  A GLY   A 1 133 ? 14.949 -0.450  -8.865  0.78 15.68 ?  133 GLY   A HA2  1 
ATOM   2840 H  HA2  B GLY   A 1 133 ? 15.149 -0.243  -8.816  0.22 15.67 ?  133 GLY   A HA2  1 
ATOM   2841 H  HA3  A GLY   A 1 133 ? 16.270 -0.631  -9.684  0.78 15.68 ?  133 GLY   A HA3  1 
ATOM   2842 H  HA3  B GLY   A 1 133 ? 16.424 -0.645  -9.632  0.22 15.67 ?  133 GLY   A HA3  1 
ATOM   2843 N  N    A ALA   A 1 134 ? 15.864 -3.296  -8.202  0.78 12.76 ?  134 ALA   A N    1 
ATOM   2844 N  N    B ALA   A 1 134 ? 15.893 -3.188  -8.121  0.22 12.70 ?  134 ALA   A N    1 
ATOM   2845 C  CA   A ALA   A 1 134 ? 15.523 -4.701  -8.368  0.78 13.56 ?  134 ALA   A CA   1 
ATOM   2846 C  CA   B ALA   A 1 134 ? 15.479 -4.575  -8.266  0.22 12.71 ?  134 ALA   A CA   1 
ATOM   2847 C  C    A ALA   A 1 134 ? 14.159 -5.000  -7.749  0.78 13.63 ?  134 ALA   A C    1 
ATOM   2848 C  C    B ALA   A 1 134 ? 14.197 -4.852  -7.482  0.22 12.30 ?  134 ALA   A C    1 
ATOM   2849 O  O    A ALA   A 1 134 ? 13.594 -4.202  -6.996  0.78 14.45 ?  134 ALA   A O    1 
ATOM   2850 O  O    B ALA   A 1 134 ? 13.826 -4.118  -6.561  0.22 12.39 ?  134 ALA   A O    1 
ATOM   2851 C  CB   A ALA   A 1 134 ? 16.597 -5.605  -7.763  0.78 14.57 ?  134 ALA   A CB   1 
ATOM   2852 C  CB   B ALA   A 1 134 ? 16.584 -5.527  -7.810  0.22 13.18 ?  134 ALA   A CB   1 
ATOM   2853 H  H    A ALA   A 1 134 ? 16.339 -3.116  -7.503  0.78 15.37 ?  134 ALA   A H    1 
ATOM   2854 H  H    B ALA   A 1 134 ? 16.470 -3.044  -7.494  0.22 15.30 ?  134 ALA   A H    1 
ATOM   2855 H  HA   A ALA   A 1 134 ? 15.469 -4.896  -9.318  0.78 16.33 ?  134 ALA   A HA   1 
ATOM   2856 H  HA   B ALA   A 1 134 ? 15.304 -4.747  -9.206  0.22 15.30 ?  134 ALA   A HA   1 
ATOM   2857 H  HB1  A ALA   A 1 134 ? 16.346 -6.529  -7.909  0.78 17.54 ?  134 ALA   A HB1  1 
ATOM   2858 H  HB1  B ALA   A 1 134 ? 16.277 -6.439  -7.930  0.22 15.87 ?  134 ALA   A HB1  1 
ATOM   2859 H  HB2  A ALA   A 1 134 ? 17.446 -5.420  -8.200  0.78 17.54 ?  134 ALA   A HB2  1 
ATOM   2860 H  HB2  B ALA   A 1 134 ? 17.376 -5.370  -8.347  0.22 15.87 ?  134 ALA   A HB2  1 
ATOM   2861 H  HB3  A ALA   A 1 134 ? 16.666 -5.421  -6.816  0.78 17.54 ?  134 ALA   A HB3  1 
ATOM   2862 H  HB3  B ALA   A 1 134 ? 16.776 -5.360  -6.876  0.22 15.87 ?  134 ALA   A HB3  1 
ATOM   2863 N  N    A ASP   A 1 135 ? 13.625 -6.169  -8.094  0.78 14.18 ?  135 ASP   A N    1 
ATOM   2864 N  N    B ASP   A 1 135 ? 13.524 -5.933  -7.864  0.22 12.42 ?  135 ASP   A N    1 
ATOM   2865 C  CA   A ASP   A 1 135 ? 12.373 -6.651  -7.521  0.78 15.37 ?  135 ASP   A CA   1 
ATOM   2866 C  CA   B ASP   A 1 135 ? 12.279 -6.337  -7.222  0.22 12.48 ?  135 ASP   A CA   1 
ATOM   2867 C  C    A ASP   A 1 135 ? 12.622 -7.090  -6.083  0.78 14.73 ?  135 ASP   A C    1 
ATOM   2868 C  C    B ASP   A 1 135 ? 12.575 -6.810  -5.804  0.22 11.86 ?  135 ASP   A C    1 
ATOM   2869 O  O    A ASP   A 1 135 ? 13.418 -8.011  -5.857  0.78 14.59 ?  135 ASP   A O    1 
ATOM   2870 O  O    B ASP   A 1 135 ? 13.310 -7.792  -5.631  0.22 11.68 ?  135 ASP   A O    1 
ATOM   2871 C  CB   A ASP   A 1 135 ? 11.889 -7.837  -8.351  0.78 17.90 ?  135 ASP   A CB   1 
ATOM   2872 C  CB   B ASP   A 1 135 ? 11.647 -7.472  -8.022  0.22 12.97 ?  135 ASP   A CB   1 
ATOM   2873 C  CG   A ASP   A 1 135 ? 10.609 -8.470  -7.811  0.78 20.21 ?  135 ASP   A CG   1 
ATOM   2874 C  CG   B ASP   A 1 135 ? 10.220 -7.776  -7.588  0.22 13.69 ?  135 ASP   A CG   1 
ATOM   2875 O  OD1  A ASP   A 1 135 ? 10.063 -7.991  -6.796  0.78 20.34 ?  135 ASP   A OD1  1 
ATOM   2876 O  OD1  B ASP   A 1 135 ? 9.855  -7.431  -6.443  0.22 13.99 ?  135 ASP   A OD1  1 
ATOM   2877 O  OD2  A ASP   A 1 135 ? 10.143 -9.455  -8.423  0.78 22.64 -1 135 ASP   A OD2  1 
ATOM   2878 O  OD2  B ASP   A 1 135 ? 9.466  -8.369  -8.391  0.22 14.30 -1 135 ASP   A OD2  1 
ATOM   2879 H  H    A ASP   A 1 135 ? 13.972 -6.705  -8.668  0.78 17.07 ?  135 ASP   A H    1 
ATOM   2880 H  H    B ASP   A 1 135 ? 13.772 -6.454  -8.496  0.22 14.96 ?  135 ASP   A H    1 
ATOM   2881 H  HA   A ASP   A 1 135 ? 11.704 -5.946  -7.553  0.78 18.50 ?  135 ASP   A HA   1 
ATOM   2882 H  HA   B ASP   A 1 135 ? 11.657 -5.589  -7.209  0.22 15.04 ?  135 ASP   A HA   1 
ATOM   2883 H  HB2  A ASP   A 1 135 ? 11.707 -7.536  -9.252  0.78 21.54 ?  135 ASP   A HB2  1 
ATOM   2884 H  HB2  B ASP   A 1 135 ? 11.647 -7.229  -8.962  0.22 15.63 ?  135 ASP   A HB2  1 
ATOM   2885 H  HB3  A ASP   A 1 135 ? 12.579 -8.515  -8.356  0.78 21.54 ?  135 ASP   A HB3  1 
ATOM   2886 H  HB3  B ASP   A 1 135 ? 12.171 -8.277  -7.889  0.22 15.63 ?  135 ASP   A HB3  1 
ATOM   2887 N  N    A PRO   A 1 136 ? 11.987 -6.465  -5.088  0.78 14.29 ?  136 PRO   A N    1 
ATOM   2888 N  N    B PRO   A 1 136 ? 12.045 -6.152  -4.770  0.22 11.39 ?  136 PRO   A N    1 
ATOM   2889 C  CA   A PRO   A 1 136 ? 12.237 -6.868  -3.692  0.78 14.11 ?  136 PRO   A CA   1 
ATOM   2890 C  CA   B PRO   A 1 136 ? 12.324 -6.603  -3.396  0.22 11.48 ?  136 PRO   A CA   1 
ATOM   2891 C  C    A PRO   A 1 136 ? 11.827 -8.297  -3.379  0.78 13.28 ?  136 PRO   A C    1 
ATOM   2892 C  C    B PRO   A 1 136 ? 11.862 -8.022  -3.103  0.22 11.27 ?  136 PRO   A C    1 
ATOM   2893 O  O    A PRO   A 1 136 ? 12.436 -8.926  -2.505  0.78 12.90 ?  136 PRO   A O    1 
ATOM   2894 O  O    B PRO   A 1 136 ? 12.435 -8.678  -2.224  0.22 10.76 ?  136 PRO   A O    1 
ATOM   2895 C  CB   A PRO   A 1 136 ? 11.438 -5.839  -2.878  0.78 15.24 ?  136 PRO   A CB   1 
ATOM   2896 C  CB   B PRO   A 1 136 ? 11.609 -5.553  -2.530  0.22 11.80 ?  136 PRO   A CB   1 
ATOM   2897 C  CG   A PRO   A 1 136 ? 10.391 -5.331  -3.822  0.78 15.87 ?  136 PRO   A CG   1 
ATOM   2898 C  CG   B PRO   A 1 136 ? 10.619 -4.908  -3.448  0.22 12.13 ?  136 PRO   A CG   1 
ATOM   2899 C  CD   A PRO   A 1 136 ? 11.005 -5.371  -5.186  0.78 15.16 ?  136 PRO   A CD   1 
ATOM   2900 C  CD   B PRO   A 1 136 ? 11.242 -4.920  -4.794  0.22 11.47 ?  136 PRO   A CD   1 
ATOM   2901 H  HA   A PRO   A 1 136 ? 13.181 -6.761  -3.480  0.78 16.99 ?  136 PRO   A HA   1 
ATOM   2902 H  HA   B PRO   A 1 136 ? 13.273 -6.547  -3.218  0.22 13.83 ?  136 PRO   A HA   1 
ATOM   2903 H  HB2  A PRO   A 1 136 ? 11.029 -6.274  -2.112  0.78 18.34 ?  136 PRO   A HB2  1 
ATOM   2904 H  HB2  B PRO   A 1 136 ? 11.157 -5.980  -1.788  0.22 14.22 ?  136 PRO   A HB2  1 
ATOM   2905 H  HB3  A PRO   A 1 136 ? 12.025 -5.120  -2.590  0.78 18.34 ?  136 PRO   A HB3  1 
ATOM   2906 H  HB3  B PRO   A 1 136 ? 12.250 -4.894  -2.208  0.22 14.22 ?  136 PRO   A HB3  1 
ATOM   2907 H  HG2  A PRO   A 1 136 ? 9.615  -5.904  -3.783  0.78 19.10 ?  136 PRO   A HG2  1 
ATOM   2908 H  HG2  B PRO   A 1 136 ? 9.797  -5.423  -3.454  0.22 14.61 ?  136 PRO   A HG2  1 
ATOM   2909 H  HG3  A PRO   A 1 136 ? 10.160 -4.419  -3.587  0.78 19.10 ?  136 PRO   A HG3  1 
ATOM   2910 H  HG3  B PRO   A 1 136 ? 10.449 -3.996  -3.164  0.22 14.61 ?  136 PRO   A HG3  1 
ATOM   2911 H  HD2  A PRO   A 1 136 ? 10.329 -5.591  -5.850  0.78 18.25 ?  136 PRO   A HD2  1 
ATOM   2912 H  HD2  B PRO   A 1 136 ? 10.555 -4.968  -5.480  0.22 13.82 ?  136 PRO   A HD2  1 
ATOM   2913 H  HD3  A PRO   A 1 136 ? 11.445 -4.533  -5.392  0.78 18.25 ?  136 PRO   A HD3  1 
ATOM   2914 H  HD3  B PRO   A 1 136 ? 11.813 -4.144  -4.917  0.22 13.82 ?  136 PRO   A HD3  1 
ATOM   2915 N  N    A ILE   A 1 137 ? 10.793 -8.821  -4.041  0.78 13.26 ?  137 ILE   A N    1 
ATOM   2916 N  N    B ILE   A 1 137 ? 10.844 -8.520  -3.809  0.22 11.52 ?  137 ILE   A N    1 
ATOM   2917 C  CA   A ILE   A 1 137 ? 10.428 -10.221 -3.843  0.78 13.71 ?  137 ILE   A CA   1 
ATOM   2918 C  CA   B ILE   A 1 137 ? 10.417 -9.904  -3.612  0.22 11.68 ?  137 ILE   A CA   1 
ATOM   2919 C  C    A ILE   A 1 137 ? 11.588 -11.119 -4.240  0.78 13.26 ?  137 ILE   A C    1 
ATOM   2920 C  C    B ILE   A 1 137 ? 11.518 -10.868 -4.040  0.22 11.95 ?  137 ILE   A C    1 
ATOM   2921 O  O    A ILE   A 1 137 ? 11.911 -12.095 -3.550  0.78 13.57 ?  137 ILE   A O    1 
ATOM   2922 O  O    B ILE   A 1 137 ? 11.808 -11.854 -3.350  0.22 11.77 ?  137 ILE   A O    1 
ATOM   2923 C  CB   A ILE   A 1 137 ? 9.141  -10.562 -4.621  0.78 15.06 ?  137 ILE   A CB   1 
ATOM   2924 C  CB   B ILE   A 1 137 ? 9.093  -10.167 -4.356  0.22 12.02 ?  137 ILE   A CB   1 
ATOM   2925 C  CG1  A ILE   A 1 137 ? 7.958  -9.725  -4.122  0.78 17.00 ?  137 ILE   A CG1  1 
ATOM   2926 C  CG1  B ILE   A 1 137 ? 7.966  -9.315  -3.761  0.22 12.67 ?  137 ILE   A CG1  1 
ATOM   2927 C  CG2  A ILE   A 1 137 ? 8.833  -12.058 -4.507  0.78 16.05 ?  137 ILE   A CG2  1 
ATOM   2928 C  CG2  B ILE   A 1 137 ? 8.734  -11.649 -4.308  0.22 12.11 ?  137 ILE   A CG2  1 
ATOM   2929 C  CD1  A ILE   A 1 137 ? 6.700  -9.912  -4.940  0.78 18.54 ?  137 ILE   A CD1  1 
ATOM   2930 C  CD1  B ILE   A 1 137 ? 6.681  -9.360  -4.553  0.22 13.16 ?  137 ILE   A CD1  1 
ATOM   2931 H  H    A ILE   A 1 137 ? 10.302 -8.393  -4.600  0.78 15.96 ?  137 ILE   A H    1 
ATOM   2932 H  H    B ILE   A 1 137 ? 10.391 -8.079  -4.395  0.22 13.88 ?  137 ILE   A H    1 
ATOM   2933 H  HA   A ILE   A 1 137 ? 10.256 -10.369 -2.903  0.78 16.50 ?  137 ILE   A HA   1 
ATOM   2934 H  HA   B ILE   A 1 137 ? 10.251 -10.040 -2.666  0.22 14.07 ?  137 ILE   A HA   1 
ATOM   2935 H  HB   A ILE   A 1 137 ? 9.284  -10.352 -5.555  0.78 18.12 ?  137 ILE   A HB   1 
ATOM   2936 H  HB   B ILE   A 1 137 ? 9.207  -9.909  -5.282  0.22 14.48 ?  137 ILE   A HB   1 
ATOM   2937 H  HG12 A ILE   A 1 137 ? 7.761  -9.975  -3.205  0.78 20.46 ?  137 ILE   A HG12 1 
ATOM   2938 H  HG12 B ILE   A 1 137 ? 7.771  -9.632  -2.865  0.22 15.26 ?  137 ILE   A HG12 1 
ATOM   2939 H  HG13 A ILE   A 1 137 ? 8.201  -8.784  -4.159  0.78 20.46 ?  137 ILE   A HG13 1 
ATOM   2940 H  HG13 B ILE   A 1 137 ? 8.254  -8.389  -3.726  0.22 15.26 ?  137 ILE   A HG13 1 
ATOM   2941 H  HG21 A ILE   A 1 137 ? 7.934  -12.237 -4.823  0.78 19.32 ?  137 ILE   A HG21 1 
ATOM   2942 H  HG21 B ILE   A 1 137 ? 7.816  -11.769 -4.596  0.22 14.59 ?  137 ILE   A HG21 1 
ATOM   2943 H  HG22 A ILE   A 1 137 ? 9.469  -12.552 -5.046  0.78 19.32 ?  137 ILE   A HG22 1 
ATOM   2944 H  HG22 B ILE   A 1 137 ? 9.328  -12.134 -4.901  0.22 14.59 ?  137 ILE   A HG22 1 
ATOM   2945 H  HG23 A ILE   A 1 137 ? 8.910  -12.324 -3.577  0.78 19.32 ?  137 ILE   A HG23 1 
ATOM   2946 H  HG23 B ILE   A 1 137 ? 8.838  -11.967 -3.399  0.22 14.59 ?  137 ILE   A HG23 1 
ATOM   2947 H  HD11 A ILE   A 1 137 ? 5.982  -10.193 -4.353  0.78 22.30 ?  137 ILE   A HD11 1 
ATOM   2948 H  HD11 B ILE   A 1 137 ? 5.968  -9.686  -3.981  0.22 15.84 ?  137 ILE   A HD11 1 
ATOM   2949 H  HD12 A ILE   A 1 137 ? 6.482  -9.069  -5.359  0.78 22.30 ?  137 ILE   A HD12 1 
ATOM   2950 H  HD12 B ILE   A 1 137 ? 6.476  -8.468  -4.867  0.22 15.84 ?  137 ILE   A HD12 1 
ATOM   2951 H  HD13 A ILE   A 1 137 ? 6.857  -10.582 -5.621  0.78 22.30 ?  137 ILE   A HD13 1 
ATOM   2952 H  HD13 B ILE   A 1 137 ? 6.795  -9.956  -5.311  0.22 15.84 ?  137 ILE   A HD13 1 
ATOM   2953 N  N    A HIS   A 1 138 ? 12.240 -10.791 -5.358  0.78 13.28 ?  138 HIS   A N    1 
ATOM   2954 N  N    B HIS   A 1 138 ? 12.152 -10.597 -5.185  0.22 12.40 ?  138 HIS   A N    1 
ATOM   2955 C  CA   A HIS   A 1 138 ? 13.428 -11.526 -5.768  0.78 13.50 ?  138 HIS   A CA   1 
ATOM   2956 C  CA   B HIS   A 1 138 ? 13.251 -11.438 -5.649  0.22 12.72 ?  138 HIS   A CA   1 
ATOM   2957 C  C    A HIS   A 1 138 ? 14.558 -11.360 -4.759  0.78 12.87 ?  138 HIS   A C    1 
ATOM   2958 C  C    B HIS   A 1 138 ? 14.447 -11.350 -4.709  0.22 12.41 ?  138 HIS   A C    1 
ATOM   2959 O  O    A HIS   A 1 138 ? 15.236 -12.336 -4.414  0.78 13.28 ?  138 HIS   A O    1 
ATOM   2960 O  O    B HIS   A 1 138 ? 15.074 -12.367 -4.390  0.22 12.49 ?  138 HIS   A O    1 
ATOM   2961 C  CB   A HIS   A 1 138 ? 13.852 -11.086 -7.168  0.78 14.47 ?  138 HIS   A CB   1 
ATOM   2962 C  CB   B HIS   A 1 138 ? 13.649 -11.031 -7.068  0.22 13.10 ?  138 HIS   A CB   1 
ATOM   2963 C  CG   A HIS   A 1 138 ? 15.103 -11.749 -7.644  0.78 15.62 ?  138 HIS   A CG   1 
ATOM   2964 C  CG   B HIS   A 1 138 ? 14.960 -11.599 -7.514  0.22 13.49 ?  138 HIS   A CG   1 
ATOM   2965 N  ND1  A HIS   A 1 138 ? 15.193 -13.109 -7.854  0.78 16.94 ?  138 HIS   A ND1  1 
ATOM   2966 N  ND1  B HIS   A 1 138 ? 15.106 -12.909 -7.916  0.22 14.05 ?  138 HIS   A ND1  1 
ATOM   2967 C  CD2  A HIS   A 1 138 ? 16.325 -11.242 -7.925  0.78 15.75 ?  138 HIS   A CD2  1 
ATOM   2968 C  CD2  B HIS   A 1 138 ? 16.187 -11.035 -7.613  0.22 13.43 ?  138 HIS   A CD2  1 
ATOM   2969 C  CE1  A HIS   A 1 138 ? 16.414 -13.408 -8.258  0.78 17.11 ?  138 HIS   A CE1  1 
ATOM   2970 C  CE1  B HIS   A 1 138 ? 16.367 -13.126 -8.248  0.22 13.99 ?  138 HIS   A CE1  1 
ATOM   2971 N  NE2  A HIS   A 1 138 ? 17.121 -12.293 -8.310  0.78 16.28 ?  138 HIS   A NE2  1 
ATOM   2972 N  NE2  B HIS   A 1 138 ? 17.044 -12.005 -8.074  0.22 13.80 ?  138 HIS   A NE2  1 
ATOM   2973 H  H    A HIS   A 1 138 ? 12.012 -10.149 -5.894  0.78 15.99 ?  138 HIS   A H    1 
ATOM   2974 H  H    B HIS   A 1 138 ? 11.963 -9.936  -5.704  0.22 14.93 ?  138 HIS   A H    1 
ATOM   2975 H  HA   A HIS   A 1 138 ? 13.204 -12.466 -5.817  0.78 16.25 ?  138 HIS   A HA   1 
ATOM   2976 H  HA   B HIS   A 1 138 ? 12.954 -12.358 -5.671  0.22 15.32 ?  138 HIS   A HA   1 
ATOM   2977 H  HB2  A HIS   A 1 138 ? 13.141 -11.307 -7.798  0.78 17.42 ?  138 HIS   A HB2  1 
ATOM   2978 H  HB2  B HIS   A 1 138 ? 12.965 -11.343 -7.685  0.22 15.78 ?  138 HIS   A HB2  1 
ATOM   2979 H  HB3  A HIS   A 1 138 ? 14.002 -10.129 -7.170  0.78 17.42 ?  138 HIS   A HB3  1 
ATOM   2980 H  HB3  B HIS   A 1 138 ? 13.712 -10.064 -7.112  0.22 15.78 ?  138 HIS   A HB3  1 
ATOM   2981 H  HD1  A HIS   A 1 138 ? 14.551 -13.672 -7.747  0.78 20.39 ?  138 HIS   A HD1  1 
ATOM   2982 H  HD1  B HIS   A 1 138 ? 14.475 -13.493 -7.948  0.22 16.92 ?  138 HIS   A HD1  1 
ATOM   2983 H  HD2  A HIS   A 1 138 ? 16.574 -10.347 -7.871  0.78 18.96 ?  138 HIS   A HD2  1 
ATOM   2984 H  HD2  B HIS   A 1 138 ? 16.408 -10.156 -7.409  0.22 16.17 ?  138 HIS   A HD2  1 
ATOM   2985 H  HE1  A HIS   A 1 138 ? 16.724 -14.257 -8.468  0.78 20.58 ?  138 HIS   A HE1  1 
ATOM   2986 H  HE1  B HIS   A 1 138 ? 16.717 -13.933 -8.552  0.22 16.84 ?  138 HIS   A HE1  1 
ATOM   2987 N  N    . SER   A 1 139 ? 14.777 -10.139 -4.264  1.00 12.20 ?  139 SER   A N    1 
ATOM   2988 C  CA   . SER   A 1 139 ? 15.854 -9.956  -3.301  1.00 11.94 ?  139 SER   A CA   1 
ATOM   2989 C  C    . SER   A 1 139 ? 15.645 -10.803 -2.053  1.00 11.68 ?  139 SER   A C    1 
ATOM   2990 O  O    . SER   A 1 139 ? 16.597 -11.394 -1.530  1.00 11.89 ?  139 SER   A O    1 
ATOM   2991 C  CB   . SER   A 1 139 ? 15.989 -8.481  -2.938  1.00 12.04 ?  139 SER   A CB   1 
ATOM   2992 O  OG   . SER   A 1 139 ? 17.074 -8.315  -2.044  1.00 12.42 ?  139 SER   A OG   1 
ATOM   2993 H  H    A SER   A 1 139 ? 14.333 -9.428  -4.463  0.78 14.70 ?  139 SER   A H    1 
ATOM   2994 H  H    B SER   A 1 139 ? 14.386 -9.410  -4.502  0.22 14.70 ?  139 SER   A H    1 
ATOM   2995 H  HA   . SER   A 1 139 ? 16.690 -10.231 -3.711  1.00 14.38 ?  139 SER   A HA   1 
ATOM   2996 H  HB2  . SER   A 1 139 ? 16.153 -7.959  -3.741  1.00 14.51 ?  139 SER   A HB2  1 
ATOM   2997 H  HB3  . SER   A 1 139 ? 15.170 -8.178  -2.507  1.00 14.51 ?  139 SER   A HB3  1 
ATOM   2998 H  HG   . SER   A 1 139 ? 17.155 -7.503  -1.833  1.00 14.97 ?  139 SER   A HG   1 
ATOM   2999 N  N    . LEU   A 1 140 ? 14.408 -10.866 -1.554  1.00 11.90 ?  140 LEU   A N    1 
ATOM   3000 C  CA   . LEU   A 1 140 ? 14.136 -11.680 -0.372  1.00 11.54 ?  140 LEU   A CA   1 
ATOM   3001 C  C    . LEU   A 1 140 ? 14.401 -13.155 -0.652  1.00 11.80 ?  140 LEU   A C    1 
ATOM   3002 O  O    . LEU   A 1 140 ? 14.950 -13.873 0.196   1.00 12.37 ?  140 LEU   A O    1 
ATOM   3003 C  CB   . LEU   A 1 140 ? 12.695 -11.457 0.085   1.00 12.15 ?  140 LEU   A CB   1 
ATOM   3004 C  CG   . LEU   A 1 140 ? 12.235 -12.305 1.268   1.00 12.61 ?  140 LEU   A CG   1 
ATOM   3005 C  CD1  . LEU   A 1 140 ? 13.156 -12.141 2.467   1.00 12.68 ?  140 LEU   A CD1  1 
ATOM   3006 C  CD2  . LEU   A 1 140 ? 10.790 -11.971 1.640   1.00 13.29 ?  140 LEU   A CD2  1 
ATOM   3007 H  H    . LEU   A 1 140 ? 13.721 -10.453 -1.875  1.00 14.34 ?  140 LEU   A H    1 
ATOM   3008 H  HA   . LEU   A 1 140 ? 14.724 -11.402 0.342   1.00 13.91 ?  140 LEU   A HA   1 
ATOM   3009 H  HB2  . LEU   A 1 140 ? 12.596 -10.532 0.338   1.00 14.64 ?  140 LEU   A HB2  1 
ATOM   3010 H  HB3  . LEU   A 1 140 ? 12.107 -11.659 -0.660  1.00 14.64 ?  140 LEU   A HB3  1 
ATOM   3011 H  HG   . LEU   A 1 140 ? 12.249 -13.241 1.007   1.00 15.19 ?  140 LEU   A HG   1 
ATOM   3012 H  HD11 . LEU   A 1 140 ? 12.773 -12.609 3.226   1.00 15.27 ?  140 LEU   A HD11 1 
ATOM   3013 H  HD12 . LEU   A 1 140 ? 14.023 -12.533 2.249   1.00 15.27 ?  140 LEU   A HD12 1 
ATOM   3014 H  HD13 . LEU   A 1 140 ? 13.257 -11.204 2.665   1.00 15.27 ?  140 LEU   A HD13 1 
ATOM   3015 H  HD21 . LEU   A 1 140 ? 10.520 -12.532 2.389   1.00 16.01 ?  140 LEU   A HD21 1 
ATOM   3016 H  HD22 . LEU   A 1 140 ? 10.736 -11.038 1.892   1.00 16.01 ?  140 LEU   A HD22 1 
ATOM   3017 H  HD23 . LEU   A 1 140 ? 10.217 -12.145 0.878   1.00 16.01 ?  140 LEU   A HD23 1 
ATOM   3018 N  N    . ARG   A 1 141 ? 14.003 -13.626 -1.837  1.00 12.44 ?  141 ARG   A N    1 
ATOM   3019 C  CA   . ARG   A 1 141 ? 14.242 -15.014 -2.209  1.00 13.46 ?  141 ARG   A CA   1 
ATOM   3020 C  C    . ARG   A 1 141 ? 15.736 -15.322 -2.235  1.00 12.79 ?  141 ARG   A C    1 
ATOM   3021 O  O    . ARG   A 1 141 ? 16.185 -16.341 -1.694  1.00 12.92 ?  141 ARG   A O    1 
ATOM   3022 C  CB   . ARG   A 1 141 ? 13.606 -15.274 -3.577  1.00 15.28 ?  141 ARG   A CB   1 
ATOM   3023 C  CG   . ARG   A 1 141 ? 13.606 -16.716 -4.024  1.00 17.96 ?  141 ARG   A CG   1 
ATOM   3024 C  CD   . ARG   A 1 141 ? 12.578 -17.489 -3.267  1.00 20.42 ?  141 ARG   A CD   1 
ATOM   3025 N  NE   . ARG   A 1 141 ? 13.188 -18.265 -2.202  1.00 21.29 ?  141 ARG   A NE   1 
ATOM   3026 C  CZ   . ARG   A 1 141 ? 12.506 -18.841 -1.221  1.00 22.44 ?  141 ARG   A CZ   1 
ATOM   3027 N  NH1  . ARG   A 1 141 ? 11.214 -18.615 -1.051  1.00 21.96 ?  141 ARG   A NH1  1 
ATOM   3028 N  NH2  . ARG   A 1 141 ? 13.139 -19.658 -0.385  1.00 23.50 ?  141 ARG   A NH2  1 
ATOM   3029 H  H    . ARG   A 1 141 ? 13.600 -13.162 -2.441  1.00 14.98 ?  141 ARG   A H    1 
ATOM   3030 H  HA   . ARG   A 1 141 ? 13.823 -15.599 -1.562  1.00 16.21 ?  141 ARG   A HA   1 
ATOM   3031 H  HB2  . ARG   A 1 141 ? 12.687 -14.968 -3.554  1.00 18.39 ?  141 ARG   A HB2  1 
ATOM   3032 H  HB3  . ARG   A 1 141 ? 14.097 -14.764 -4.242  1.00 18.39 ?  141 ARG   A HB3  1 
ATOM   3033 H  HG2  . ARG   A 1 141 ? 13.395 -16.762 -4.972  1.00 21.61 ?  141 ARG   A HG2  1 
ATOM   3034 H  HG3  . ARG   A 1 141 ? 14.479 -17.112 -3.857  1.00 21.61 ?  141 ARG   A HG3  1 
ATOM   3035 H  HD2  . ARG   A 1 141 ? 11.942 -16.876 -2.863  1.00 24.55 ?  141 ARG   A HD2  1 
ATOM   3036 H  HD3  . ARG   A 1 141 ? 12.119 -18.094 -3.871  1.00 24.55 ?  141 ARG   A HD3  1 
ATOM   3037 H  HE   . ARG   A 1 141 ? 14.023 -18.451 -2.270  1.00 25.61 ?  141 ARG   A HE   1 
ATOM   3038 H  HH11 . ARG   A 1 141 ? 10.787 -18.101 -1.593  1.00 26.40 ?  141 ARG   A HH11 1 
ATOM   3039 H  HH12 . ARG   A 1 141 ? 10.790 -18.999 -0.406  1.00 26.40 ?  141 ARG   A HH12 1 
ATOM   3040 H  HH21 . ARG   A 1 141 ? 13.980 -19.807 -0.484  1.00 28.26 ?  141 ARG   A HH21 1 
ATOM   3041 H  HH22 . ARG   A 1 141 ? 12.711 -20.027 0.264   1.00 28.26 ?  141 ARG   A HH22 1 
ATOM   3042 N  N    . VAL   A 1 142 ? 16.527 -14.454 -2.873  1.00 12.07 ?  142 VAL   A N    1 
ATOM   3043 C  CA   . VAL   A 1 142 ? 17.972 -14.670 -2.909  1.00 12.06 ?  142 VAL   A CA   1 
ATOM   3044 C  C    . VAL   A 1 142 ? 18.548 -14.650 -1.500  1.00 11.47 ?  142 VAL   A C    1 
ATOM   3045 O  O    . VAL   A 1 142 ? 19.413 -15.464 -1.159  1.00 11.92 ?  142 VAL   A O    1 
ATOM   3046 C  CB   . VAL   A 1 142 ? 18.663 -13.651 -3.834  1.00 12.36 ?  142 VAL   A CB   1 
ATOM   3047 C  CG1  . VAL   A 1 142 ? 20.174 -13.864 -3.803  1.00 12.48 ?  142 VAL   A CG1  1 
ATOM   3048 C  CG2  . VAL   A 1 142 ? 18.145 -13.788 -5.255  1.00 13.68 ?  142 VAL   A CG2  1 
ATOM   3049 H  H    . VAL   A 1 142 ? 16.257 -13.741 -3.282  1.00 14.54 ?  142 VAL   A H    1 
ATOM   3050 H  HA   . VAL   A 1 142 ? 18.141 -15.542 -3.280  1.00 14.53 ?  142 VAL   A HA   1 
ATOM   3051 H  HB   . VAL   A 1 142 ? 18.478 -12.744 -3.527  1.00 14.89 ?  142 VAL   A HB   1 
ATOM   3052 H  HG11 . VAL   A 1 142 ? 20.578 -13.379 -4.540  1.00 15.04 ?  142 VAL   A HG11 1 
ATOM   3053 H  HG12 . VAL   A 1 142 ? 20.527 -13.531 -2.961  1.00 15.04 ?  142 VAL   A HG12 1 
ATOM   3054 H  HG13 . VAL   A 1 142 ? 20.358 -14.810 -3.889  1.00 15.04 ?  142 VAL   A HG13 1 
ATOM   3055 H  HG21 . VAL   A 1 142 ? 18.616 -13.159 -5.825  1.00 16.47 ?  142 VAL   A HG21 1 
ATOM   3056 H  HG22 . VAL   A 1 142 ? 18.311 -14.695 -5.557  1.00 16.47 ?  142 VAL   A HG22 1 
ATOM   3057 H  HG23 . VAL   A 1 142 ? 17.198 -13.600 -5.263  1.00 16.47 ?  142 VAL   A HG23 1 
ATOM   3058 N  N    . CYS   A 1 143 ? 18.078 -13.729 -0.659  1.00 11.49 ?  143 CYS   A N    1 
ATOM   3059 C  CA   . CYS   A 1 143 ? 18.547 -13.682 0.720   1.00 11.53 ?  143 CYS   A CA   1 
ATOM   3060 C  C    . CYS   A 1 143 ? 18.327 -15.024 1.413   1.00 11.69 ?  143 CYS   A C    1 
ATOM   3061 O  O    . CYS   A 1 143 ? 19.252 -15.609 1.980   1.00 11.73 ?  143 CYS   A O    1 
ATOM   3062 C  CB   . CYS   A 1 143 ? 17.813 -12.572 1.465   1.00 11.80 ?  143 CYS   A CB   1 
ATOM   3063 S  SG   . CYS   A 1 143 ? 18.321 -12.393 3.187   1.00 12.45 ?  143 CYS   A SG   1 
ATOM   3064 H  H    . CYS   A 1 143 ? 17.492 -13.135 -0.863  1.00 13.84 ?  143 CYS   A H    1 
ATOM   3065 H  HA   . CYS   A 1 143 ? 19.492 -13.490 0.729   1.00 13.89 ?  143 CYS   A HA   1 
ATOM   3066 H  HB2  . CYS   A 1 143 ? 17.979 -11.729 1.016   1.00 14.22 ?  143 CYS   A HB2  1 
ATOM   3067 H  HB3  . CYS   A 1 143 ? 16.863 -12.763 1.456   1.00 14.22 ?  143 CYS   A HB3  1 
ATOM   3068 H  HG   . CYS   A 1 143 ? 17.743 -11.464 3.667   1.00 14.99 ?  143 CYS   A HG   1 
ATOM   3069 N  N    . VAL   A 1 144 ? 17.098 -15.531 1.363   1.00 12.26 ?  144 VAL   A N    1 
ATOM   3070 C  CA   . VAL   A 1 144 ? 16.765 -16.765 2.065   1.00 13.47 ?  144 VAL   A CA   1 
ATOM   3071 C  C    . VAL   A 1 144 ? 17.574 -17.934 1.525   1.00 13.24 ?  144 VAL   A C    1 
ATOM   3072 O  O    . VAL   A 1 144 ? 17.944 -18.848 2.274   1.00 13.69 ?  144 VAL   A O    1 
ATOM   3073 C  CB   . VAL   A 1 144 ? 15.248 -17.008 1.965   1.00 16.64 ?  144 VAL   A CB   1 
ATOM   3074 C  CG1  . VAL   A 1 144 ? 14.893 -18.433 2.324   1.00 18.51 ?  144 VAL   A CG1  1 
ATOM   3075 C  CG2  . VAL   A 1 144 ? 14.505 -15.997 2.840   1.00 16.68 ?  144 VAL   A CG2  1 
ATOM   3076 H  H    . VAL   A 1 144 ? 16.439 -15.180 0.927   1.00 14.77 ?  144 VAL   A H    1 
ATOM   3077 H  HA   . VAL   A 1 144 ? 16.980 -16.657 2.997   1.00 16.22 ?  144 VAL   A HA   1 
ATOM   3078 H  HB   . VAL   A 1 144 ? 14.962 -16.855 1.048   1.00 20.03 ?  144 VAL   A HB   1 
ATOM   3079 H  HG11 . VAL   A 1 144 ? 13.942 -18.481 2.522   1.00 22.26 ?  144 VAL   A HG11 1 
ATOM   3080 H  HG12 . VAL   A 1 144 ? 15.100 -19.010 1.574   1.00 22.26 ?  144 VAL   A HG12 1 
ATOM   3081 H  HG13 . VAL   A 1 144 ? 15.403 -18.697 3.103   1.00 22.26 ?  144 VAL   A HG13 1 
ATOM   3082 H  HG21 . VAL   A 1 144 ? 13.547 -16.164 2.786   1.00 20.07 ?  144 VAL   A HG21 1 
ATOM   3083 H  HG22 . VAL   A 1 144 ? 14.801 -16.087 3.758   1.00 20.07 ?  144 VAL   A HG22 1 
ATOM   3084 H  HG23 . VAL   A 1 144 ? 14.693 -15.096 2.521   1.00 20.07 ?  144 VAL   A HG23 1 
ATOM   3085 N  N    . ASP   A 1 145 ? 17.836 -17.946 0.221   1.00 13.29 ?  145 ASP   A N    1 
ATOM   3086 C  CA   . ASP   A 1 145 ? 18.540 -19.054 -0.416  1.00 13.98 ?  145 ASP   A CA   1 
ATOM   3087 C  C    . ASP   A 1 145 ? 20.063 -18.907 -0.380  1.00 13.64 ?  145 ASP   A C    1 
ATOM   3088 O  O    . ASP   A 1 145 ? 20.765 -19.799 -0.869  1.00 15.69 ?  145 ASP   A O    1 
ATOM   3089 C  CB   . ASP   A 1 145 ? 18.088 -19.192 -1.871  1.00 15.87 ?  145 ASP   A CB   1 
ATOM   3090 C  CG   . ASP   A 1 145 ? 16.636 -19.625 -1.998  1.00 17.78 ?  145 ASP   A CG   1 
ATOM   3091 O  OD1  . ASP   A 1 145 ? 16.076 -20.176 -1.026  1.00 18.21 ?  145 ASP   A OD1  1 
ATOM   3092 O  OD2  . ASP   A 1 145 ? 16.058 -19.409 -3.081  1.00 19.10 -1 145 ASP   A OD2  1 
ATOM   3093 H  H    . ASP   A 1 145 ? 17.602 -17.321 -0.326  1.00 16.01 ?  145 ASP   A H    1 
ATOM   3094 H  HA   . ASP   A 1 145 ? 18.309 -19.874 0.047   1.00 16.84 ?  145 ASP   A HA   1 
ATOM   3095 H  HB2  . ASP   A 1 145 ? 18.189 -18.338 -2.314  1.00 19.09 ?  145 ASP   A HB2  1 
ATOM   3096 H  HB3  . ASP   A 1 145 ? 18.638 -19.862 -2.306  1.00 19.09 ?  145 ASP   A HB3  1 
ATOM   3097 N  N    . THR   A 1 146 ? 20.590 -17.817 0.172   1.00 12.37 ?  146 THR   A N    1 
ATOM   3098 C  CA   . THR   A 1 146 ? 22.031 -17.567 0.184   1.00 11.91 ?  146 THR   A CA   1 
ATOM   3099 C  C    . THR   A 1 146 ? 22.599 -17.378 1.578   1.00 11.81 ?  146 THR   A C    1 
ATOM   3100 O  O    . THR   A 1 146 ? 23.681 -17.906 1.882   1.00 12.82 ?  146 THR   A O    1 
ATOM   3101 C  CB   . THR   A 1 146 ? 22.352 -16.315 -0.657  1.00 11.89 ?  146 THR   A CB   1 
ATOM   3102 O  OG1  . THR   A 1 146 ? 21.823 -16.478 -1.973  1.00 12.43 ?  146 THR   A OG1  1 
ATOM   3103 C  CG2  . THR   A 1 146 ? 23.852 -16.079 -0.752  1.00 12.39 ?  146 THR   A CG2  1 
ATOM   3104 H  H    . THR   A 1 146 ? 20.129 -17.196 0.546   1.00 14.89 ?  146 THR   A H    1 
ATOM   3105 H  HA   . THR   A 1 146 ? 22.488 -18.316 -0.220  1.00 14.35 ?  146 THR   A HA   1 
ATOM   3106 H  HB   . THR   A 1 146 ? 21.951 -15.535 -0.243  1.00 14.32 ?  146 THR   A HB   1 
ATOM   3107 H  HG1  . THR   A 1 146 ? 20.983 -16.554 -1.938  1.00 14.97 ?  146 THR   A HG1  1 
ATOM   3108 H  HG21 . THR   A 1 146 ? 24.036 -15.413 -1.432  1.00 14.93 ?  146 THR   A HG21 1 
ATOM   3109 H  HG22 . THR   A 1 146 ? 24.194 -15.769 0.097   1.00 14.93 ?  146 THR   A HG22 1 
ATOM   3110 H  HG23 . THR   A 1 146 ? 24.298 -16.907 -0.994  1.00 14.93 ?  146 THR   A HG23 1 
ATOM   3111 N  N    . VAL   A 1 147 ? 21.917 -16.607 2.420   1.00 11.56 ?  147 VAL   A N    1 
ATOM   3112 C  CA   . VAL   A 1 147 ? 22.412 -16.307 3.755   1.00 11.58 ?  147 VAL   A CA   1 
ATOM   3113 C  C    . VAL   A 1 147 ? 22.095 -17.476 4.675   1.00 11.95 ?  147 VAL   A C    1 
ATOM   3114 O  O    . VAL   A 1 147 ? 20.952 -17.950 4.736   1.00 12.70 ?  147 VAL   A O    1 
ATOM   3115 C  CB   . VAL   A 1 147 ? 21.798 -15.001 4.280   1.00 11.84 ?  147 VAL   A CB   1 
ATOM   3116 C  CG1  . VAL   A 1 147 ? 22.344 -14.700 5.655   1.00 12.92 ?  147 VAL   A CG1  1 
ATOM   3117 C  CG2  . VAL   A 1 147 ? 22.063 -13.861 3.320   1.00 12.18 ?  147 VAL   A CG2  1 
ATOM   3118 H  H    . VAL   A 1 147 ? 21.154 -16.253 2.244   1.00 13.93 ?  147 VAL   A H    1 
ATOM   3119 H  HA   . VAL   A 1 147 ? 23.375 -16.199 3.719   1.00 13.95 ?  147 VAL   A HA   1 
ATOM   3120 H  HB   . VAL   A 1 147 ? 20.839 -15.109 4.358   1.00 14.27 ?  147 VAL   A HB   1 
ATOM   3121 H  HG11 . VAL   A 1 147 ? 22.117 -13.790 5.894   1.00 15.56 ?  147 VAL   A HG11 1 
ATOM   3122 H  HG12 . VAL   A 1 147 ? 21.952 -15.317 6.295   1.00 15.56 ?  147 VAL   A HG12 1 
ATOM   3123 H  HG13 . VAL   A 1 147 ? 23.309 -14.807 5.643   1.00 15.56 ?  147 VAL   A HG13 1 
ATOM   3124 H  HG21 . VAL   A 1 147 ? 21.735 -13.037 3.716   1.00 14.67 ?  147 VAL   A HG21 1 
ATOM   3125 H  HG22 . VAL   A 1 147 ? 23.017 -13.796 3.164   1.00 14.67 ?  147 VAL   A HG22 1 
ATOM   3126 H  HG23 . VAL   A 1 147 ? 21.599 -14.036 2.489   1.00 14.67 ?  147 VAL   A HG23 1 
ATOM   3127 N  N    . ARG   A 1 148 ? 23.120 -17.949 5.383   1.00 12.34 ?  148 ARG   A N    1 
ATOM   3128 C  CA   . ARG   A 1 148 ? 22.994 -19.025 6.350   1.00 12.66 ?  148 ARG   A CA   1 
ATOM   3129 C  C    . ARG   A 1 148 ? 23.126 -18.549 7.783   1.00 12.80 ?  148 ARG   A C    1 
ATOM   3130 O  O    . ARG   A 1 148 ? 22.721 -19.273 8.701   1.00 14.52 ?  148 ARG   A O    1 
ATOM   3131 C  CB   . ARG   A 1 148 ? 24.035 -20.121 6.068   1.00 13.17 ?  148 ARG   A CB   1 
ATOM   3132 C  CG   . ARG   A 1 148 ? 23.871 -20.764 4.700   1.00 14.46 ?  148 ARG   A CG   1 
ATOM   3133 C  CD   . ARG   A 1 148 ? 24.952 -21.795 4.399   1.00 15.19 ?  148 ARG   A CD   1 
ATOM   3134 N  NE   . ARG   A 1 148 ? 26.288 -21.209 4.424   1.00 14.94 ?  148 ARG   A NE   1 
ATOM   3135 C  CZ   . ARG   A 1 148 ? 26.797 -20.470 3.448   1.00 14.45 ?  148 ARG   A CZ   1 
ATOM   3136 N  NH1  . ARG   A 1 148 ? 26.119 -20.239 2.337   1.00 14.87 ?  148 ARG   A NH1  1 
ATOM   3137 N  NH2  . ARG   A 1 148 ? 28.018 -19.946 3.593   1.00 14.89 ?  148 ARG   A NH2  1 
ATOM   3138 H  H    . ARG   A 1 148 ? 23.932 -17.652 5.301   1.00 14.86 ?  148 ARG   A H    1 
ATOM   3139 H  HA   . ARG   A 1 148 ? 22.118 -19.420 6.248   1.00 15.25 ?  148 ARG   A HA   1 
ATOM   3140 H  HB2  . ARG   A 1 148 ? 24.922 -19.744 6.114   1.00 15.85 ?  148 ARG   A HB2  1 
ATOM   3141 H  HB3  . ARG   A 1 148 ? 23.935 -20.824 6.732   1.00 15.85 ?  148 ARG   A HB3  1 
ATOM   3142 H  HG2  . ARG   A 1 148 ? 23.009 -21.205 4.659   1.00 17.40 ?  148 ARG   A HG2  1 
ATOM   3143 H  HG3  . ARG   A 1 148 ? 23.920 -20.069 4.023   1.00 17.40 ?  148 ARG   A HG3  1 
ATOM   3144 H  HD2  . ARG   A 1 148 ? 24.918 -22.498 5.068   1.00 18.28 ?  148 ARG   A HD2  1 
ATOM   3145 H  HD3  . ARG   A 1 148 ? 24.797 -22.172 3.515   1.00 18.28 ?  148 ARG   A HD3  1 
ATOM   3146 H  HE   . ARG   A 1 148 ? 26.777 -21.357 5.110   1.00 17.98 ?  148 ARG   A HE   1 
ATOM   3147 H  HH11 . ARG   A 1 148 ? 25.331 -20.562 2.234   1.00 17.90 ?  148 ARG   A HH11 1 
ATOM   3148 H  HH12 . ARG   A 1 148 ? 26.464 -19.748 1.718   1.00 17.90 ?  148 ARG   A HH12 1 
ATOM   3149 H  HH21 . ARG   A 1 148 ? 28.462 -20.089 4.313   1.00 17.92 ?  148 ARG   A HH21 1 
ATOM   3150 H  HH22 . ARG   A 1 148 ? 28.355 -19.459 2.968   1.00 17.92 ?  148 ARG   A HH22 1 
ATOM   3151 N  N    . THR   A 1 149 ? 23.676 -17.358 7.992   1.00 13.01 ?  149 THR   A N    1 
ATOM   3152 C  CA   . THR   A 1 149 ? 23.758 -16.754 9.307   1.00 13.17 ?  149 THR   A CA   1 
ATOM   3153 C  C    . THR   A 1 149 ? 22.433 -16.059 9.618   1.00 12.53 ?  149 THR   A C    1 
ATOM   3154 O  O    . THR   A 1 149 ? 21.494 -16.059 8.813   1.00 13.33 ?  149 THR   A O    1 
ATOM   3155 C  CB   . THR   A 1 149 ? 24.957 -15.817 9.361   1.00 13.50 ?  149 THR   A CB   1 
ATOM   3156 O  OG1  . THR   A 1 149 ? 24.829 -14.887 8.285   1.00 13.54 ?  149 THR   A OG1  1 
ATOM   3157 C  CG2  . THR   A 1 149 ? 26.262 -16.610 9.232   1.00 13.88 ?  149 THR   A CG2  1 
ATOM   3158 H  H    . THR   A 1 149 ? 24.027 -16.871 7.369   1.00 15.66 ?  149 THR   A H    1 
ATOM   3159 H  HA   . THR   A 1 149 ? 23.890 -17.455 9.964   1.00 15.86 ?  149 THR   A HA   1 
ATOM   3160 H  HB   . THR   A 1 149 ? 24.953 -15.342 10.204  1.00 16.26 ?  149 THR   A HB   1 
ATOM   3161 H  HG1  . THR   A 1 149 ? 25.479 -14.355 8.284   1.00 16.30 ?  149 THR   A HG1  1 
ATOM   3162 H  HG21 . THR   A 1 149 ? 27.022 -16.011 9.289   1.00 16.71 ?  149 THR   A HG21 1 
ATOM   3163 H  HG22 . THR   A 1 149 ? 26.326 -17.267 9.946   1.00 16.71 ?  149 THR   A HG22 1 
ATOM   3164 H  HG23 . THR   A 1 149 ? 26.292 -17.076 8.379   1.00 16.71 ?  149 THR   A HG23 1 
ATOM   3165 N  N    . ASN   A 1 150 ? 22.319 -15.512 10.821  1.00 12.72 ?  150 ASN   A N    1 
ATOM   3166 C  CA   . ASN   A 1 150 ? 21.038 -15.007 11.316  1.00 13.49 ?  150 ASN   A CA   1 
ATOM   3167 C  C    . ASN   A 1 150 ? 20.850 -13.564 10.862  1.00 12.69 ?  150 ASN   A C    1 
ATOM   3168 O  O    . ASN   A 1 150 ? 21.593 -12.668 11.286  1.00 13.90 ?  150 ASN   A O    1 
ATOM   3169 C  CB   . ASN   A 1 150 ? 20.990 -15.123 12.834  1.00 16.04 ?  150 ASN   A CB   1 
ATOM   3170 C  CG   . ASN   A 1 150 ? 20.869 -16.557 13.294  1.00 20.15 ?  150 ASN   A CG   1 
ATOM   3171 O  OD1  . ASN   A 1 150 ? 20.270 -17.387 12.609  1.00 21.38 ?  150 ASN   A OD1  1 
ATOM   3172 N  ND2  . ASN   A 1 150 ? 21.446 -16.864 14.451  1.00 22.48 ?  150 ASN   A ND2  1 
ATOM   3173 H  H    . ASN   A 1 150 ? 22.967 -15.432 11.377  1.00 15.32 ?  150 ASN   A H    1 
ATOM   3174 H  HA   . ASN   A 1 150 ? 20.315 -15.545 10.948  1.00 16.25 ?  150 ASN   A HA   1 
ATOM   3175 H  HB2  . ASN   A 1 150 ? 21.805 -14.757 13.209  1.00 19.30 ?  150 ASN   A HB2  1 
ATOM   3176 H  HB3  . ASN   A 1 150 ? 20.219 -14.643 13.169  1.00 19.30 ?  150 ASN   A HB3  1 
ATOM   3177 H  HD21 . ASN   A 1 150 ? 21.408 -17.672 14.755  1.00 27.03 ?  150 ASN   A HD21 1 
ATOM   3178 H  HD22 . ASN   A 1 150 ? 21.853 -16.258 14.906  1.00 27.03 ?  150 ASN   A HD22 1 
ATOM   3179 N  N    . VAL   A 1 151 ? 19.860 -13.336 10.005  1.00 12.20 ?  151 VAL   A N    1 
ATOM   3180 C  CA   . VAL   A 1 151 ? 19.646 -12.028 9.403   1.00 12.32 ?  151 VAL   A CA   1 
ATOM   3181 C  C    . VAL   A 1 151 ? 18.261 -11.510 9.770   1.00 12.08 ?  151 VAL   A C    1 
ATOM   3182 O  O    . VAL   A 1 151 ? 17.255 -12.222 9.634   1.00 13.30 ?  151 VAL   A O    1 
ATOM   3183 C  CB   . VAL   A 1 151 ? 19.941 -12.018 7.887   1.00 13.52 ?  151 VAL   A CB   1 
ATOM   3184 C  CG1  . VAL   A 1 151 ? 19.117 -13.040 7.130   1.00 14.74 ?  151 VAL   A CG1  1 
ATOM   3185 C  CG2  . VAL   A 1 151 ? 19.752 -10.615 7.305   1.00 13.69 ?  151 VAL   A CG2  1 
ATOM   3186 H  H    . VAL   A 1 151 ? 19.292 -13.935 9.753   1.00 14.70 ?  151 VAL   A H    1 
ATOM   3187 H  HA   . VAL   A 1 151 ? 20.286 -11.420 9.798   1.00 14.84 ?  151 VAL   A HA   1 
ATOM   3188 H  HB   . VAL   A 1 151 ? 20.875 -12.257 7.754   1.00 16.28 ?  151 VAL   A HB   1 
ATOM   3189 H  HG11 . VAL   A 1 151 ? 19.325 -12.986 6.182   1.00 17.74 ?  151 VAL   A HG11 1 
ATOM   3190 H  HG12 . VAL   A 1 151 ? 19.333 -13.931 7.458   1.00 17.74 ?  151 VAL   A HG12 1 
ATOM   3191 H  HG13 . VAL   A 1 151 ? 18.175 -12.860 7.270   1.00 17.74 ?  151 VAL   A HG13 1 
ATOM   3192 H  HG21 . VAL   A 1 151 ? 20.067 -10.608 6.384   1.00 16.49 ?  151 VAL   A HG21 1 
ATOM   3193 H  HG22 . VAL   A 1 151 ? 18.811 -10.383 7.331   1.00 16.49 ?  151 VAL   A HG22 1 
ATOM   3194 H  HG23 . VAL   A 1 151 ? 20.266 -9.983  7.831   1.00 16.49 ?  151 VAL   A HG23 1 
ATOM   3195 N  N    . TYR   A 1 152 ? 18.246 -10.267 10.261  1.00 12.02 ?  152 TYR   A N    1 
ATOM   3196 C  CA   . TYR   A 1 152 ? 17.055 -9.536  10.657  1.00 11.55 ?  152 TYR   A CA   1 
ATOM   3197 C  C    . TYR   A 1 152 ? 16.864 -8.434  9.628   1.00 11.24 ?  152 TYR   A C    1 
ATOM   3198 O  O    . TYR   A 1 152 ? 17.641 -7.472  9.585   1.00 11.68 ?  152 TYR   A O    1 
ATOM   3199 C  CB   . TYR   A 1 152 ? 17.249 -8.991  12.068  1.00 12.21 ?  152 TYR   A CB   1 
ATOM   3200 C  CG   . TYR   A 1 152 ? 17.210 -10.123 13.060  1.00 13.18 ?  152 TYR   A CG   1 
ATOM   3201 C  CD1  . TYR   A 1 152 ? 18.344 -10.873 13.339  1.00 14.82 ?  152 TYR   A CD1  1 
ATOM   3202 C  CD2  . TYR   A 1 152 ? 16.023 -10.492 13.671  1.00 13.77 ?  152 TYR   A CD2  1 
ATOM   3203 C  CE1  . TYR   A 1 152 ? 18.310 -11.940 14.214  1.00 16.45 ?  152 TYR   A CE1  1 
ATOM   3204 C  CE2  . TYR   A 1 152 ? 15.974 -11.569 14.555  1.00 15.43 ?  152 TYR   A CE2  1 
ATOM   3205 C  CZ   . TYR   A 1 152 ? 17.122 -12.286 14.821  1.00 16.22 ?  152 TYR   A CZ   1 
ATOM   3206 O  OH   . TYR   A 1 152 ? 17.085 -13.356 15.691  1.00 18.45 ?  152 TYR   A OH   1 
ATOM   3207 H  H    . TYR   A 1 152 ? 18.968 -9.797  10.358  1.00 14.48 ?  152 TYR   A H    1 
ATOM   3208 H  HA   . TYR   A 1 152 ? 16.287 -10.124 10.640  1.00 13.92 ?  152 TYR   A HA   1 
ATOM   3209 H  HB2  . TYR   A 1 152 ? 18.113 -8.563  12.132  1.00 14.71 ?  152 TYR   A HB2  1 
ATOM   3210 H  HB3  . TYR   A 1 152 ? 16.543 -8.367  12.281  1.00 14.71 ?  152 TYR   A HB3  1 
ATOM   3211 H  HD1  . TYR   A 1 152 ? 19.147 -10.643 12.924  1.00 17.84 ?  152 TYR   A HD1  1 
ATOM   3212 H  HD2  . TYR   A 1 152 ? 15.242 -10.014 13.489  1.00 16.57 ?  152 TYR   A HD2  1 
ATOM   3213 H  HE1  . TYR   A 1 152 ? 19.085 -12.417 14.392  1.00 19.80 ?  152 TYR   A HE1  1 
ATOM   3214 H  HE2  . TYR   A 1 152 ? 15.173 -11.795 14.966  1.00 18.57 ?  152 TYR   A HE2  1 
ATOM   3215 H  HH   . TYR   A 1 152 ? 16.306 -13.444 15.994  1.00 22.19 ?  152 TYR   A HH   1 
ATOM   3216 N  N    A LEU   A 1 153 ? 15.853 -8.593  8.779   0.78 11.32 ?  153 LEU   A N    1 
ATOM   3217 N  N    B LEU   A 1 153 ? 15.834 -8.576  8.802   0.22 11.07 ?  153 LEU   A N    1 
ATOM   3218 C  CA   A LEU   A 1 153 ? 15.598 -7.698  7.660   0.78 11.35 ?  153 LEU   A CA   1 
ATOM   3219 C  CA   B LEU   A 1 153 ? 15.561 -7.628  7.736   0.22 10.93 ?  153 LEU   A CA   1 
ATOM   3220 C  C    A LEU   A 1 153 ? 14.596 -6.620  8.047   0.78 11.67 ?  153 LEU   A C    1 
ATOM   3221 C  C    B LEU   A 1 153 ? 14.628 -6.527  8.216   0.22 11.20 ?  153 LEU   A C    1 
ATOM   3222 O  O    A LEU   A 1 153 ? 13.480 -6.924  8.485   0.78 12.18 ?  153 LEU   A O    1 
ATOM   3223 O  O    B LEU   A 1 153 ? 13.663 -6.780  8.946   0.22 11.28 ?  153 LEU   A O    1 
ATOM   3224 C  CB   A LEU   A 1 153 ? 15.039 -8.487  6.477   0.78 11.58 ?  153 LEU   A CB   1 
ATOM   3225 C  CB   B LEU   A 1 153 ? 14.936 -8.344  6.540   0.22 10.90 ?  153 LEU   A CB   1 
ATOM   3226 C  CG   A LEU   A 1 153 ? 15.970 -9.516  5.834   0.78 11.83 ?  153 LEU   A CG   1 
ATOM   3227 C  CG   B LEU   A 1 153 ? 15.850 -9.346  5.835   0.22 10.89 ?  153 LEU   A CG   1 
ATOM   3228 C  CD1  A LEU   A 1 153 ? 15.188 -10.415 4.892   0.78 12.32 ?  153 LEU   A CD1  1 
ATOM   3229 C  CD1  B LEU   A 1 153 ? 15.048 -10.170 4.849   0.22 11.12 ?  153 LEU   A CD1  1 
ATOM   3230 C  CD2  A LEU   A 1 153 ? 17.103 -8.819  5.090   0.78 12.21 ?  153 LEU   A CD2  1 
ATOM   3231 C  CD2  B LEU   A 1 153 ? 16.996 -8.630  5.134   0.22 11.17 ?  153 LEU   A CD2  1 
ATOM   3232 H  H    A LEU   A 1 153 ? 15.277 -9.237  8.842   0.78 13.64 ?  153 LEU   A H    1 
ATOM   3233 H  H    B LEU   A 1 153 ? 15.272 -9.229  8.841   0.22 13.34 ?  153 LEU   A H    1 
ATOM   3234 H  HA   A LEU   A 1 153 ? 16.430 -7.280  7.397   0.78 13.67 ?  153 LEU   A HA   1 
ATOM   3235 H  HA   B LEU   A 1 153 ? 16.393 -7.225  7.453   0.22 13.17 ?  153 LEU   A HA   1 
ATOM   3236 H  HB2  A LEU   A 1 153 ? 14.248 -8.960  6.774   0.78 13.96 ?  153 LEU   A HB2  1 
ATOM   3237 H  HB2  B LEU   A 1 153 ? 14.152 -8.825  6.845   0.22 13.13 ?  153 LEU   A HB2  1 
ATOM   3238 H  HB3  A LEU   A 1 153 ? 14.793 -7.851  5.785   0.78 13.96 ?  153 LEU   A HB3  1 
ATOM   3239 H  HB3  B LEU   A 1 153 ? 14.676 -7.675  5.887   0.22 13.13 ?  153 LEU   A HB3  1 
ATOM   3240 H  HG   A LEU   A 1 153 ? 16.364 -10.069 6.530   0.78 14.25 ?  153 LEU   A HG   1 
ATOM   3241 H  HG   B LEU   A 1 153 ? 16.230 -9.948  6.495   0.22 13.12 ?  153 LEU   A HG   1 
ATOM   3242 H  HD11 A LEU   A 1 153 ? 15.757 -11.145 4.605   0.78 14.84 ?  153 LEU   A HD11 1 
ATOM   3243 H  HD11 B LEU   A 1 153 ? 15.639 -10.803 4.414   0.22 13.39 ?  153 LEU   A HD11 1 
ATOM   3244 H  HD12 A LEU   A 1 153 ? 14.415 -10.763 5.360   0.78 14.84 ?  153 LEU   A HD12 1 
ATOM   3245 H  HD12 B LEU   A 1 153 ? 14.349 -10.642 5.328   0.22 13.39 ?  153 LEU   A HD12 1 
ATOM   3246 H  HD13 A LEU   A 1 153 ? 14.904 -9.893  4.125   0.78 14.84 ?  153 LEU   A HD13 1 
ATOM   3247 H  HD13 B LEU   A 1 153 ? 14.655 -9.576  4.190   0.22 13.39 ?  153 LEU   A HD13 1 
ATOM   3248 H  HD21 A LEU   A 1 153 ? 17.690 -9.490  4.714   0.78 14.71 ?  153 LEU   A HD21 1 
ATOM   3249 H  HD21 B LEU   A 1 153 ? 17.493 -9.274  4.608   0.22 13.46 ?  153 LEU   A HD21 1 
ATOM   3250 H  HD22 A LEU   A 1 153 ? 16.721 -8.275  4.385   0.78 14.71 ?  153 LEU   A HD22 1 
ATOM   3251 H  HD22 B LEU   A 1 153 ? 16.630 -7.942  4.557   0.22 13.46 ?  153 LEU   A HD22 1 
ATOM   3252 H  HD23 A LEU   A 1 153 ? 17.592 -8.261  5.713   0.78 14.71 ?  153 LEU   A HD23 1 
ATOM   3253 H  HD23 B LEU   A 1 153 ? 17.574 -8.229  5.802   0.22 13.46 ?  153 LEU   A HD23 1 
ATOM   3254 N  N    A ALA   A 1 154 ? 14.990 -5.366  7.850   0.78 11.44 ?  154 ALA   A N    1 
ATOM   3255 N  N    B ALA   A 1 154 ? 14.924 -5.301  7.790   0.22 11.57 ?  154 ALA   A N    1 
ATOM   3256 C  CA   A ALA   A 1 154 ? 14.114 -4.218  8.047   0.78 11.82 ?  154 ALA   A CA   1 
ATOM   3257 C  CA   B ALA   A 1 154 ? 14.139 -4.120  8.123   0.22 12.02 ?  154 ALA   A CA   1 
ATOM   3258 C  C    A ALA   A 1 154 ? 13.622 -3.728  6.691   0.78 11.40 ?  154 ALA   A C    1 
ATOM   3259 C  C    B ALA   A 1 154 ? 13.599 -3.518  6.836   0.22 12.18 ?  154 ALA   A C    1 
ATOM   3260 O  O    A ALA   A 1 154 ? 14.425 -3.372  5.824   0.78 12.01 ?  154 ALA   A O    1 
ATOM   3261 O  O    B ALA   A 1 154 ? 14.374 -3.120  5.960   0.22 11.99 ?  154 ALA   A O    1 
ATOM   3262 C  CB   A ALA   A 1 154 ? 14.843 -3.091  8.776   0.78 12.78 ?  154 ALA   A CB   1 
ATOM   3263 C  CB   B ALA   A 1 154 ? 15.001 -3.085  8.845   0.22 12.35 ?  154 ALA   A CB   1 
ATOM   3264 H  H    A ALA   A 1 154 ? 15.784 -5.149  7.591   0.78 13.79 ?  154 ALA   A H    1 
ATOM   3265 H  H    B ALA   A 1 154 ? 15.600 -5.129  7.290   0.22 13.94 ?  154 ALA   A H    1 
ATOM   3266 H  HA   A ALA   A 1 154 ? 13.347 -4.484  8.581   0.78 14.24 ?  154 ALA   A HA   1 
ATOM   3267 H  HA   B ALA   A 1 154 ? 13.393 -4.366  8.694   0.22 14.48 ?  154 ALA   A HA   1 
ATOM   3268 H  HB1  A ALA   A 1 154 ? 14.231 -2.344  8.891   0.78 15.39 ?  154 ALA   A HB1  1 
ATOM   3269 H  HB1  B ALA   A 1 154 ? 14.452 -2.311  9.049   0.22 14.88 ?  154 ALA   A HB1  1 
ATOM   3270 H  HB2  A ALA   A 1 154 ? 15.141 -3.409  9.640   0.78 15.39 ?  154 ALA   A HB2  1 
ATOM   3271 H  HB2  B ALA   A 1 154 ? 15.345 -3.475  9.660   0.22 14.88 ?  154 ALA   A HB2  1 
ATOM   3272 H  HB3  A ALA   A 1 154 ? 15.604 -2.811  8.243   0.78 15.39 ?  154 ALA   A HB3  1 
ATOM   3273 H  HB3  B ALA   A 1 154 ? 15.733 -2.827  8.262   0.22 14.88 ?  154 ALA   A HB3  1 
ATOM   3274 N  N    A VAL   A 1 155 ? 12.302 -3.703  6.518   0.48 9.58  ?  155 VAL   A N    1 
ATOM   3275 N  N    B VAL   A 1 155 ? 12.276 -3.431  6.736   0.22 12.10 ?  155 VAL   A N    1 
ATOM   3276 C  CA   A VAL   A 1 155 ? 11.649 -3.209  5.310   0.48 11.91 ?  155 VAL   A CA   1 
ATOM   3277 C  CA   B VAL   A 1 155 ? 11.599 -2.869  5.573   0.22 13.22 ?  155 VAL   A CA   1 
ATOM   3278 C  CA   T VAL   A 1 155 ? 11.622 -3.268  5.305   0.30 13.55 ?  155 VAL   A CA   1 
ATOM   3279 C  C    A VAL   A 1 155 ? 10.926 -1.915  5.667   0.48 13.49 ?  155 VAL   A C    1 
ATOM   3280 C  C    B VAL   A 1 155 ? 10.612 -1.841  6.101   0.22 14.59 ?  155 VAL   A C    1 
ATOM   3281 C  C    T VAL   A 1 155 ? 11.003 -1.901  5.608   0.30 13.62 ?  155 VAL   A C    1 
ATOM   3282 O  O    A VAL   A 1 155 ? 9.982  -1.926  6.466   0.48 13.95 ?  155 VAL   A O    1 
ATOM   3283 O  O    B VAL   A 1 155 ? 9.646  -2.200  6.784   0.22 14.85 ?  155 VAL   A O    1 
ATOM   3284 O  O    T VAL   A 1 155 ? 10.167 -1.768  6.501   0.30 13.59 ?  155 VAL   A O    1 
ATOM   3285 C  CB   A VAL   A 1 155 ? 10.671 -4.249  4.741   0.48 12.66 ?  155 VAL   A CB   1 
ATOM   3286 C  CB   B VAL   A 1 155 ? 10.877 -3.945  4.751   0.22 12.97 ?  155 VAL   A CB   1 
ATOM   3287 C  CB   T VAL   A 1 155 ? 10.590 -4.289  4.784   0.30 13.54 ?  155 VAL   A CB   1 
ATOM   3288 C  CG1  A VAL   A 1 155 ? 9.977  -3.710  3.500   0.48 13.55 ?  155 VAL   A CG1  1 
ATOM   3289 C  CG1  B VAL   A 1 155 ? 10.094 -3.306  3.614   0.22 13.22 ?  155 VAL   A CG1  1 
ATOM   3290 C  CG1  T VAL   A 1 155 ? 9.893  -3.761  3.542   0.30 13.92 ?  155 VAL   A CG1  1 
ATOM   3291 C  CG2  A VAL   A 1 155 ? 11.402 -5.549  4.427   0.48 13.18 ?  155 VAL   A CG2  1 
ATOM   3292 C  CG2  B VAL   A 1 155 ? 11.875 -4.966  4.213   0.22 12.59 ?  155 VAL   A CG2  1 
ATOM   3293 C  CG2  T VAL   A 1 155 ? 11.267 -5.622  4.486   0.30 13.59 ?  155 VAL   A CG2  1 
ATOM   3294 H  H    A VAL   A 1 155 ? 11.745 -4.002  7.104   0.48 11.56 ?  155 VAL   A H    1 
ATOM   3295 H  H    B VAL   A 1 155 ? 11.733 -3.683  7.357   0.22 14.57 ?  155 VAL   A H    1 
ATOM   3296 H  HA   A VAL   A 1 155 ? 12.320 -3.016  4.636   0.48 14.35 ?  155 VAL   A HA   1 
ATOM   3297 H  HA   B VAL   A 1 155 ? 12.242 -2.416  5.003   0.22 15.92 ?  155 VAL   A HA   1 
ATOM   3298 H  HB   A VAL   A 1 155 ? 9.990  -4.438  5.407   0.48 15.24 ?  155 VAL   A HB   1 
ATOM   3299 H  HB   B VAL   A 1 155 ? 10.248 -4.408  5.327   0.22 15.62 ?  155 VAL   A HB   1 
ATOM   3300 H  HB   T VAL   A 1 155 ? 9.920  -4.439  5.469   0.30 16.31 ?  155 VAL   A HB   1 
ATOM   3301 H  HG11 A VAL   A 1 155 ? 9.489  -4.431  3.074   0.48 16.32 ?  155 VAL   A HG11 1 
ATOM   3302 H  HG11 B VAL   A 1 155 ? 9.841  -3.998  2.983   0.22 15.92 ?  155 VAL   A HG11 1 
ATOM   3303 H  HG11 T VAL   A 1 155 ? 9.367  -4.475  3.148   0.30 16.76 ?  155 VAL   A HG11 1 
ATOM   3304 H  HG12 A VAL   A 1 155 ? 9.362  -3.003  3.757   0.48 16.32 ?  155 VAL   A HG12 1 
ATOM   3305 H  HG12 B VAL   A 1 155 ? 9.298  -2.881  3.973   0.22 15.92 ?  155 VAL   A HG12 1 
ATOM   3306 H  HG12 T VAL   A 1 155 ? 9.314  -3.024  3.790   0.30 16.76 ?  155 VAL   A HG12 1 
ATOM   3307 H  HG13 A VAL   A 1 155 ? 10.646 -3.359  2.890   0.48 16.32 ?  155 VAL   A HG13 1 
ATOM   3308 H  HG13 B VAL   A 1 155 ? 10.654 -2.648  3.176   0.22 15.92 ?  155 VAL   A HG13 1 
ATOM   3309 H  HG13 T VAL   A 1 155 ? 10.563 -3.458  2.908   0.30 16.76 ?  155 VAL   A HG13 1 
ATOM   3310 H  HG21 A VAL   A 1 155 ? 10.785 -6.165  4.005   0.48 15.87 ?  155 VAL   A HG21 1 
ATOM   3311 H  HG21 B VAL   A 1 155 ? 11.397 -5.626  3.687   0.22 15.16 ?  155 VAL   A HG21 1 
ATOM   3312 H  HG21 T VAL   A 1 155 ? 10.603 -6.250  4.164   0.30 16.37 ?  155 VAL   A HG21 1 
ATOM   3313 H  HG22 A VAL   A 1 155 ? 12.140 -5.356  3.825   0.48 15.87 ?  155 VAL   A HG22 1 
ATOM   3314 H  HG22 B VAL   A 1 155 ? 12.526 -4.509  3.658   0.22 15.16 ?  155 VAL   A HG22 1 
ATOM   3315 H  HG22 T VAL   A 1 155 ? 11.948 -5.484  3.806   0.30 16.37 ?  155 VAL   A HG22 1 
ATOM   3316 H  HG23 A VAL   A 1 155 ? 11.741 -5.930  5.251   0.48 15.87 ?  155 VAL   A HG23 1 
ATOM   3317 H  HG23 B VAL   A 1 155 ? 12.321 -5.397  4.959   0.22 15.16 ?  155 VAL   A HG23 1 
ATOM   3318 H  HG23 T VAL   A 1 155 ? 11.677 -5.958  5.298   0.30 16.37 ?  155 VAL   A HG23 1 
ATOM   3319 N  N    A PHE   A 1 156 ? 11.363 -0.800  5.070   0.48 15.11 ?  156 PHE   A N    1 
ATOM   3320 N  N    B PHE   A 1 156 ? 10.844 -0.564  5.788   0.22 15.59 ?  156 PHE   A N    1 
ATOM   3321 N  N    T PHE   A 1 156 ? 11.435 -0.885  4.854   0.30 13.89 ?  156 PHE   A N    1 
ATOM   3322 C  CA   A PHE   A 1 156 ? 10.823 0.509   5.442   0.48 17.07 ?  156 PHE   A CA   1 
ATOM   3323 C  CA   B PHE   A 1 156 ? 10.029 0.483   6.394   0.22 16.61 ?  156 PHE   A CA   1 
ATOM   3324 C  CA   T PHE   A 1 156 ? 11.019 0.489   5.132   0.30 14.22 ?  156 PHE   A CA   1 
ATOM   3325 C  C    A PHE   A 1 156 ? 9.355  0.644   5.052   0.48 17.15 ?  156 PHE   A C    1 
ATOM   3326 C  C    B PHE   A 1 156 ? 8.635  0.558   5.783   0.22 17.74 ?  156 PHE   A C    1 
ATOM   3327 C  C    T PHE   A 1 156 ? 9.556  0.718   4.778   0.30 14.67 ?  156 PHE   A C    1 
ATOM   3328 O  O    A PHE   A 1 156 ? 8.530  1.122   5.842   0.48 17.86 ?  156 PHE   A O    1 
ATOM   3329 O  O    B PHE   A 1 156 ? 7.649  0.742   6.506   0.22 17.87 ?  156 PHE   A O    1 
ATOM   3330 O  O    T PHE   A 1 156 ? 8.825  1.382   5.524   0.30 14.73 ?  156 PHE   A O    1 
ATOM   3331 C  CB   A PHE   A 1 156 ? 11.653 1.620   4.794   0.48 18.66 ?  156 PHE   A CB   1 
ATOM   3332 C  CB   B PHE   A 1 156 ? 10.717 1.843   6.284   0.22 17.03 ?  156 PHE   A CB   1 
ATOM   3333 C  CB   T PHE   A 1 156 ? 11.901 1.455   4.339   0.30 13.76 ?  156 PHE   A CB   1 
ATOM   3334 C  CG   A PHE   A 1 156 ? 11.162 3.005   5.114   0.48 19.75 ?  156 PHE   A CG   1 
ATOM   3335 C  CG   B PHE   A 1 156 ? 9.862  2.981   6.762   0.22 17.48 ?  156 PHE   A CG   1 
ATOM   3336 C  CG   T PHE   A 1 156 ? 11.562 2.911   4.548   0.30 13.58 ?  156 PHE   A CG   1 
ATOM   3337 C  CD1  A PHE   A 1 156 ? 11.121 3.443   6.427   0.48 20.15 ?  156 PHE   A CD1  1 
ATOM   3338 C  CD1  B PHE   A 1 156 ? 9.743  3.252   8.114   0.22 17.64 ?  156 PHE   A CD1  1 
ATOM   3339 C  CD1  T PHE   A 1 156 ? 11.928 3.556   5.722   0.30 14.36 ?  156 PHE   A CD1  1 
ATOM   3340 C  CD2  A PHE   A 1 156 ? 10.756 3.869   4.109   0.48 20.48 ?  156 PHE   A CD2  1 
ATOM   3341 C  CD2  B PHE   A 1 156 ? 9.157  3.765   5.862   0.22 17.55 ?  156 PHE   A CD2  1 
ATOM   3342 C  CD2  T PHE   A 1 156 ? 10.892 3.633   3.572   0.30 13.85 ?  156 PHE   A CD2  1 
ATOM   3343 C  CE1  A PHE   A 1 156 ? 10.677 4.712   6.734   0.48 20.81 ?  156 PHE   A CE1  1 
ATOM   3344 C  CE1  B PHE   A 1 156 ? 8.949  4.292   8.561   0.22 17.82 ?  156 PHE   A CE1  1 
ATOM   3345 C  CE1  T PHE   A 1 156 ? 11.622 4.888   5.923   0.30 15.06 ?  156 PHE   A CE1  1 
ATOM   3346 C  CE2  A PHE   A 1 156 ? 10.305 5.143   4.410   0.48 21.04 ?  156 PHE   A CE2  1 
ATOM   3347 C  CE2  B PHE   A 1 156 ? 8.360  4.804   6.299   0.22 17.72 ?  156 PHE   A CE2  1 
ATOM   3348 C  CE2  T PHE   A 1 156 ? 10.586 4.968   3.767   0.30 14.42 ?  156 PHE   A CE2  1 
ATOM   3349 C  CZ   A PHE   A 1 156 ? 10.270 5.565   5.725   0.48 21.12 ?  156 PHE   A CZ   1 
ATOM   3350 C  CZ   B PHE   A 1 156 ? 8.257  5.070   7.652   0.22 17.70 ?  156 PHE   A CZ   1 
ATOM   3351 C  CZ   T PHE   A 1 156 ? 10.953 5.596   4.945   0.30 14.86 ?  156 PHE   A CZ   1 
ATOM   3352 H  H    A PHE   A 1 156 ? 11.970 -0.779  4.456   0.48 18.18 ?  156 PHE   A H    1 
ATOM   3353 H  H    B PHE   A 1 156 ? 11.446 -0.282  5.241   0.22 18.76 ?  156 PHE   A H    1 
ATOM   3354 H  H    T PHE   A 1 156 ? 11.970 -0.970  4.186   0.30 16.73 ?  156 PHE   A H    1 
ATOM   3355 H  HA   A PHE   A 1 156 ? 10.890 0.616   6.401   0.48 20.54 ?  156 PHE   A HA   1 
ATOM   3356 H  HA   B PHE   A 1 156 ? 9.923  0.285   7.334   0.22 19.99 ?  156 PHE   A HA   1 
ATOM   3357 H  HA   T PHE   A 1 156 ? 11.137 0.667   6.077   0.30 17.12 ?  156 PHE   A HA   1 
ATOM   3358 H  HB2  A PHE   A 1 156 ? 12.573 1.550   5.105   0.48 22.44 ?  156 PHE   A HB2  1 
ATOM   3359 H  HB2  B PHE   A 1 156 ? 11.525 1.830   6.823   0.22 20.49 ?  156 PHE   A HB2  1 
ATOM   3360 H  HB2  T PHE   A 1 156 ? 12.822 1.321   4.607   0.30 16.57 ?  156 PHE   A HB2  1 
ATOM   3361 H  HB3  A PHE   A 1 156 ? 11.628 1.511   3.830   0.48 22.44 ?  156 PHE   A HB3  1 
ATOM   3362 H  HB3  B PHE   A 1 156 ? 10.945 2.011   5.355   0.22 20.49 ?  156 PHE   A HB3  1 
ATOM   3363 H  HB3  T PHE   A 1 156 ? 11.800 1.260   3.395   0.30 16.57 ?  156 PHE   A HB3  1 
ATOM   3364 H  HD1  A PHE   A 1 156 ? 11.396 2.874   7.110   0.48 24.24 ?  156 PHE   A HD1  1 
ATOM   3365 H  HD1  B PHE   A 1 156 ? 10.205 2.734   8.730   0.22 21.22 ?  156 PHE   A HD1  1 
ATOM   3366 H  HD1  T PHE   A 1 156 ? 12.375 3.078   6.389   0.30 17.29 ?  156 PHE   A HD1  1 
ATOM   3367 H  HD2  A PHE   A 1 156 ? 10.782 3.586   3.223   0.48 24.63 ?  156 PHE   A HD2  1 
ATOM   3368 H  HD2  B PHE   A 1 156 ? 9.229  3.596   4.950   0.22 21.12 ?  156 PHE   A HD2  1 
ATOM   3369 H  HD2  T PHE   A 1 156 ? 10.640 3.210   2.784   0.30 16.68 ?  156 PHE   A HD2  1 
ATOM   3370 H  HE1  A PHE   A 1 156 ? 10.652 4.995   7.620   0.48 25.03 ?  156 PHE   A HE1  1 
ATOM   3371 H  HE1  B PHE   A 1 156 ? 8.879  4.469   9.472   0.22 21.44 ?  156 PHE   A HE1  1 
ATOM   3372 H  HE1  T PHE   A 1 156 ? 11.868 5.304   6.718   0.30 18.12 ?  156 PHE   A HE1  1 
ATOM   3373 H  HE2  A PHE   A 1 156 ? 10.035 5.713   3.729   0.48 25.30 ?  156 PHE   A HE2  1 
ATOM   3374 H  HE2  B PHE   A 1 156 ? 7.902  5.332   5.683   0.22 21.32 ?  156 PHE   A HE2  1 
ATOM   3375 H  HE2  T PHE   A 1 156 ? 10.132 5.440   3.112   0.30 17.36 ?  156 PHE   A HE2  1 
ATOM   3376 H  HZ   A PHE   A 1 156 ? 9.969  6.421   5.931   0.48 25.40 ?  156 PHE   A HZ   1 
ATOM   3377 H  HZ   B PHE   A 1 156 ? 7.724  5.774   7.948   0.22 21.29 ?  156 PHE   A HZ   1 
ATOM   3378 H  HZ   T PHE   A 1 156 ? 10.746 6.490   5.081   0.30 17.89 ?  156 PHE   A HZ   1 
ATOM   3379 N  N    A ASP   A 1 157 ? 9.014  0.240   3.835   0.48 16.95 ?  157 ASP   A N    1 
ATOM   3380 N  N    B ASP   A 1 157 ? 8.528  0.435   4.463   0.22 18.40 ?  157 ASP   A N    1 
ATOM   3381 N  N    T ASP   A 1 157 ? 9.121  0.193   3.640   0.30 15.29 ?  157 ASP   A N    1 
ATOM   3382 C  CA   A ASP   A 1 157 ? 7.697  0.512   3.277   0.48 17.85 ?  157 ASP   A CA   1 
ATOM   3383 C  CA   B ASP   A 1 157 ? 7.250  0.654   3.799   0.22 19.56 ?  157 ASP   A CA   1 
ATOM   3384 C  CA   T ASP   A 1 157 ? 7.805  0.478   3.089   0.30 15.85 ?  157 ASP   A CA   1 
ATOM   3385 C  C    A ASP   A 1 157 ? 6.700  -0.527  3.784   0.48 17.95 ?  157 ASP   A C    1 
ATOM   3386 C  C    B ASP   A 1 157 ? 6.261  -0.449  4.157   0.22 20.00 ?  157 ASP   A C    1 
ATOM   3387 C  C    T ASP   A 1 157 ? 6.791  -0.504  3.667   0.30 16.74 ?  157 ASP   A C    1 
ATOM   3388 O  O    A ASP   A 1 157 ? 6.856  -1.724  3.511   0.48 17.16 ?  157 ASP   A O    1 
ATOM   3389 O  O    B ASP   A 1 157 ? 6.598  -1.637  4.130   0.22 19.91 ?  157 ASP   A O    1 
ATOM   3390 O  O    T ASP   A 1 157 ? 6.921  -1.718  3.475   0.30 16.22 ?  157 ASP   A O    1 
ATOM   3391 C  CB   A ASP   A 1 157 ? 7.800  0.473   1.756   0.48 19.09 ?  157 ASP   A CB   1 
ATOM   3392 C  CB   B ASP   A 1 157 ? 7.444  0.731   2.287   0.22 20.38 ?  157 ASP   A CB   1 
ATOM   3393 C  CB   T ASP   A 1 157 ? 7.886  0.332   1.573   0.30 15.73 ?  157 ASP   A CB   1 
ATOM   3394 C  CG   A ASP   A 1 157 ? 6.545  0.958   1.081   0.48 20.55 ?  157 ASP   A CG   1 
ATOM   3395 C  CG   B ASP   A 1 157 ? 6.174  1.118   1.557   0.22 21.20 ?  157 ASP   A CG   1 
ATOM   3396 C  CG   T ASP   A 1 157 ? 6.738  0.981   0.871   0.30 15.17 ?  157 ASP   A CG   1 
ATOM   3397 O  OD1  A ASP   A 1 157 ? 6.294  2.177   1.104   0.48 22.43 ?  157 ASP   A OD1  1 
ATOM   3398 O  OD1  B ASP   A 1 157 ? 5.225  0.307   1.554   0.22 20.82 ?  157 ASP   A OD1  1 
ATOM   3399 O  OD1  T ASP   A 1 157 ? 5.624  0.437   0.975   0.30 15.11 ?  157 ASP   A OD1  1 
ATOM   3400 O  OD2  A ASP   A 1 157 ? 5.801  0.113   0.538   0.48 20.07 -1 157 ASP   A OD2  1 
ATOM   3401 O  OD2  B ASP   A 1 157 ? 6.117  2.234   1.001   0.22 22.17 -1 157 ASP   A OD2  1 
ATOM   3402 O  OD2  T ASP   A 1 157 ? 6.941  2.030   0.228   0.30 14.02 -1 157 ASP   A OD2  1 
ATOM   3403 H  H    A ASP   A 1 157 ? 9.538  -0.206  3.307   0.48 20.40 ?  157 ASP   A H    1 
ATOM   3404 H  H    B ASP   A 1 157 ? 9.172  0.231   3.936   0.22 22.13 ?  157 ASP   A H    1 
ATOM   3405 H  H    T ASP   A 1 157 ? 9.588  -0.337  3.148   0.30 18.40 ?  157 ASP   A H    1 
ATOM   3406 H  HA   A ASP   A 1 157 ? 7.406  1.394   3.550   0.48 21.48 ?  157 ASP   A HA   1 
ATOM   3407 H  HA   B ASP   A 1 157 ? 6.880  1.497   4.096   0.22 23.53 ?  157 ASP   A HA   1 
ATOM   3408 H  HA   T ASP   A 1 157 ? 7.538  1.386   3.308   0.30 19.08 ?  157 ASP   A HA   1 
ATOM   3409 H  HB2  A ASP   A 1 157 ? 8.568  1.011   1.480   0.48 22.96 ?  157 ASP   A HB2  1 
ATOM   3410 H  HB2  B ASP   A 1 157 ? 8.132  1.386   2.093   0.22 24.51 ?  157 ASP   A HB2  1 
ATOM   3411 H  HB2  T ASP   A 1 157 ? 8.708  0.731   1.257   0.30 18.93 ?  157 ASP   A HB2  1 
ATOM   3412 H  HB3  A ASP   A 1 157 ? 7.934  -0.444  1.472   0.48 22.96 ?  157 ASP   A HB3  1 
ATOM   3413 H  HB3  B ASP   A 1 157 ? 7.710  -0.137  1.954   0.22 24.51 ?  157 ASP   A HB3  1 
ATOM   3414 H  HB3  T ASP   A 1 157 ? 7.875  -0.613  1.349   0.30 18.93 ?  157 ASP   A HB3  1 
ATOM   3415 N  N    A LYS   A 1 158 ? 5.685  -0.075  4.533   0.48 19.40 ?  158 LYS   A N    1 
ATOM   3416 N  N    B LYS   A 1 158 ? 5.032  -0.047  4.490   0.22 20.34 ?  158 LYS   A N    1 
ATOM   3417 N  N    T LYS   A 1 158 ? 5.782  0.019   4.372   0.30 18.36 ?  158 LYS   A N    1 
ATOM   3418 C  CA   A LYS   A 1 158 ? 4.719  -1.010  5.110   0.48 20.57 ?  158 LYS   A CA   1 
ATOM   3419 C  CA   B LYS   A 1 158 ? 4.006  -1.005  4.888   0.22 20.88 ?  158 LYS   A CA   1 
ATOM   3420 C  CA   T LYS   A 1 158 ? 4.796  -0.858  5.000   0.30 20.07 ?  158 LYS   A CA   1 
ATOM   3421 C  C    A LYS   A 1 158 ? 3.971  -1.764  4.021   0.48 19.80 ?  158 LYS   A C    1 
ATOM   3422 C  C    B LYS   A 1 158 ? 3.557  -1.850  3.702   0.22 20.09 ?  158 LYS   A C    1 
ATOM   3423 C  C    T LYS   A 1 158 ? 4.030  -1.662  3.958   0.30 20.04 ?  158 LYS   A C    1 
ATOM   3424 O  O    A LYS   A 1 158 ? 3.757  -2.978  4.129   0.48 20.12 ?  158 LYS   A O    1 
ATOM   3425 O  O    B LYS   A 1 158 ? 3.601  -3.085  3.749   0.22 19.76 ?  158 LYS   A O    1 
ATOM   3426 O  O    T LYS   A 1 158 ? 3.792  -2.862  4.140   0.30 20.25 ?  158 LYS   A O    1 
ATOM   3427 C  CB   A LYS   A 1 158 ? 3.738  -0.279  6.031   0.48 22.35 ?  158 LYS   A CB   1 
ATOM   3428 C  CB   B LYS   A 1 158 ? 2.812  -0.258  5.492   0.22 22.01 ?  158 LYS   A CB   1 
ATOM   3429 C  CB   T LYS   A 1 158 ? 3.833  -0.051  5.873   0.30 21.76 ?  158 LYS   A CB   1 
ATOM   3430 C  CG   A LYS   A 1 158 ? 2.507  -1.104  6.438   0.48 24.38 ?  158 LYS   A CG   1 
ATOM   3431 C  CG   B LYS   A 1 158 ? 2.223  -0.888  6.750   0.22 22.94 ?  158 LYS   A CG   1 
ATOM   3432 C  CG   T LYS   A 1 158 ? 2.616  -0.840  6.356   0.30 23.52 ?  158 LYS   A CG   1 
ATOM   3433 C  CD   A LYS   A 1 158 ? 2.863  -2.368  7.224   0.48 25.92 ?  158 LYS   A CD   1 
ATOM   3434 C  CD   B LYS   A 1 158 ? 2.212  -2.408  6.682   0.22 23.58 ?  158 LYS   A CD   1 
ATOM   3435 C  CD   T LYS   A 1 158 ? 3.009  -2.050  7.199   0.30 25.00 ?  158 LYS   A CD   1 
ATOM   3436 C  CE   A LYS   A 1 158 ? 1.607  -3.044  7.771   0.48 27.13 ?  158 LYS   A CE   1 
ATOM   3437 C  CE   B LYS   A 1 158 ? 1.148  -2.998  7.588   0.22 24.04 ?  158 LYS   A CE   1 
ATOM   3438 C  CE   T LYS   A 1 158 ? 1.783  -2.857  7.611   0.30 26.15 ?  158 LYS   A CE   1 
ATOM   3439 N  NZ   A LYS   A 1 158 ? 1.882  -4.373  8.392   0.48 27.81 ?  158 LYS   A NZ   1 
ATOM   3440 N  NZ   B LYS   A 1 158 ? 1.343  -4.459  7.802   0.22 24.21 ?  158 LYS   A NZ   1 
ATOM   3441 N  NZ   T LYS   A 1 158 ? 2.135  -4.060  8.419   0.30 26.80 ?  158 LYS   A NZ   1 
ATOM   3442 H  H    A LYS   A 1 158 ? 5.552  0.749   4.721   0.48 23.33 ?  158 LYS   A H    1 
ATOM   3443 H  H    B LYS   A 1 158 ? 4.772  0.773   4.495   0.22 24.46 ?  158 LYS   A H    1 
ATOM   3444 H  H    T LYS   A 1 158 ? 5.653  0.859   4.501   0.30 22.09 ?  158 LYS   A H    1 
ATOM   3445 H  HA   A LYS   A 1 158 ? 5.200  -1.662  5.649   0.48 24.74 ?  158 LYS   A HA   1 
ATOM   3446 H  HA   B LYS   A 1 158 ? 4.378  -1.593  5.561   0.22 25.11 ?  158 LYS   A HA   1 
ATOM   3447 H  HA   T LYS   A 1 158 ? 5.261  -1.485  5.576   0.30 24.14 ?  158 LYS   A HA   1 
ATOM   3448 H  HB2  A LYS   A 1 158 ? 4.204  -0.025  6.845   0.48 26.88 ?  158 LYS   A HB2  1 
ATOM   3449 H  HB2  B LYS   A 1 158 ? 3.092  0.642   5.723   0.22 26.47 ?  158 LYS   A HB2  1 
ATOM   3450 H  HB2  T LYS   A 1 158 ? 4.312  0.260   6.660   0.30 26.17 ?  158 LYS   A HB2  1 
ATOM   3451 H  HB3  A LYS   A 1 158 ? 3.423  0.516   5.576   0.48 26.88 ?  158 LYS   A HB3  1 
ATOM   3452 H  HB3  B LYS   A 1 158 ? 2.103  -0.216  4.830   0.22 26.47 ?  158 LYS   A HB3  1 
ATOM   3453 H  HB3  T LYS   A 1 158 ? 3.512  0.709   5.365   0.30 26.17 ?  158 LYS   A HB3  1 
ATOM   3454 H  HG2  A LYS   A 1 158 ? 1.943  -0.557  7.003   0.48 29.31 ?  158 LYS   A HG2  1 
ATOM   3455 H  HG2  B LYS   A 1 158 ? 2.755  -0.621  7.516   0.22 27.58 ?  158 LYS   A HG2  1 
ATOM   3456 H  HG2  T LYS   A 1 158 ? 2.066  -0.263  6.906   0.30 28.28 ?  158 LYS   A HG2  1 
ATOM   3457 H  HG3  A LYS   A 1 158 ? 2.012  -1.368  5.645   0.48 29.31 ?  158 LYS   A HG3  1 
ATOM   3458 H  HG3  B LYS   A 1 158 ? 1.308  -0.584  6.859   0.22 27.58 ?  158 LYS   A HG3  1 
ATOM   3459 H  HG3  T LYS   A 1 158 ? 2.100  -1.153  5.594   0.30 28.28 ?  158 LYS   A HG3  1 
ATOM   3460 H  HD2  A LYS   A 1 158 ? 3.319  -2.995  6.643   0.48 31.16 ?  158 LYS   A HD2  1 
ATOM   3461 H  HD2  B LYS   A 1 158 ? 2.026  -2.687  5.773   0.22 28.36 ?  158 LYS   A HD2  1 
ATOM   3462 H  HD2  T LYS   A 1 158 ? 3.593  -2.630  6.685   0.30 30.05 ?  158 LYS   A HD2  1 
ATOM   3463 H  HD3  A LYS   A 1 158 ? 3.427  -2.131  7.975   0.48 31.16 ?  158 LYS   A HD3  1 
ATOM   3464 H  HD3  B LYS   A 1 158 ? 3.077  -2.747  6.968   0.22 28.36 ?  158 LYS   A HD3  1 
ATOM   3465 H  HD3  T LYS   A 1 158 ? 3.459  -1.748  8.004   0.30 30.05 ?  158 LYS   A HD3  1 
ATOM   3466 H  HE2  A LYS   A 1 158 ? 1.208  -2.474  8.447   0.48 32.61 ?  158 LYS   A HE2  1 
ATOM   3467 H  HE2  B LYS   A 1 158 ? 1.185  -2.555  8.448   0.22 28.91 ?  158 LYS   A HE2  1 
ATOM   3468 H  HE2  T LYS   A 1 158 ? 1.197  -2.298  8.144   0.30 31.44 ?  158 LYS   A HE2  1 
ATOM   3469 H  HE3  A LYS   A 1 158 ? 0.981  -3.178  7.044   0.48 32.61 ?  158 LYS   A HE3  1 
ATOM   3470 H  HE3  B LYS   A 1 158 ? 0.278  -2.864  7.179   0.22 28.91 ?  158 LYS   A HE3  1 
ATOM   3471 H  HE3  T LYS   A 1 158 ? 1.319  -3.158  6.814   0.30 31.44 ?  158 LYS   A HE3  1 
ATOM   3472 H  HZ1  A LYS   A 1 158 ? 1.125  -4.730  8.696   0.48 33.43 ?  158 LYS   A HZ1  1 
ATOM   3473 H  HZ1  B LYS   A 1 158 ? 0.711  -4.771  8.345   0.22 29.10 ?  158 LYS   A HZ1  1 
ATOM   3474 H  HZ1  T LYS   A 1 158 ? 1.397  -4.506  8.641   0.30 32.22 ?  158 LYS   A HZ1  1 
ATOM   3475 H  HZ2  A LYS   A 1 158 ? 2.238  -4.923  7.789   0.48 33.43 ?  158 LYS   A HZ2  1 
ATOM   3476 H  HZ2  B LYS   A 1 158 ? 1.297  -4.890  7.025   0.22 29.10 ?  158 LYS   A HZ2  1 
ATOM   3477 H  HZ2  T LYS   A 1 158 ? 2.666  -4.598  7.948   0.30 32.22 ?  158 LYS   A HZ2  1 
ATOM   3478 H  HZ3  A LYS   A 1 158 ? 2.451  -4.281  9.070   0.48 33.43 ?  158 LYS   A HZ3  1 
ATOM   3479 H  HZ3  B LYS   A 1 158 ? 2.140  -4.608  8.169   0.22 29.10 ?  158 LYS   A HZ3  1 
ATOM   3480 H  HZ3  T LYS   A 1 158 ? 2.558  -3.815  9.162   0.30 32.22 ?  158 LYS   A HZ3  1 
ATOM   3481 N  N    A ASN   A 1 159 ? 3.565  -1.066  2.962   0.48 19.75 ?  159 ASN   A N    1 
ATOM   3482 N  N    B ASN   A 1 159 ? 3.110  -1.196  2.626   0.22 19.86 ?  159 ASN   A N    1 
ATOM   3483 N  N    T ASN   A 1 159 ? 3.628  -1.023  2.867   0.30 20.23 ?  159 ASN   A N    1 
ATOM   3484 C  CA   A ASN   A 1 159 ? 2.882  -1.754  1.875   0.48 19.38 ?  159 ASN   A CA   1 
ATOM   3485 C  CA   B ASN   A 1 159 ? 2.645  -1.933  1.455   0.22 19.56 ?  159 ASN   A CA   1 
ATOM   3486 C  CA   T ASN   A 1 159 ? 2.893  -1.722  1.821   0.30 20.29 ?  159 ASN   A CA   1 
ATOM   3487 C  C    A ASN   A 1 159 ? 3.764  -2.848  1.277   0.48 18.44 ?  159 ASN   A C    1 
ATOM   3488 C  C    B ASN   A 1 159 ? 3.728  -2.861  0.934   0.22 18.75 ?  159 ASN   A C    1 
ATOM   3489 C  C    T ASN   A 1 159 ? 3.728  -2.834  1.191   0.30 20.13 ?  159 ASN   A C    1 
ATOM   3490 O  O    A ASN   A 1 159 ? 3.298  -3.966  1.029   0.48 17.65 ?  159 ASN   A O    1 
ATOM   3491 O  O    B ASN   A 1 159 ? 3.444  -3.995  0.531   0.22 18.68 ?  159 ASN   A O    1 
ATOM   3492 O  O    T ASN   A 1 159 ? 3.199  -3.888  0.847   0.30 19.92 ?  159 ASN   A O    1 
ATOM   3493 C  CB   A ASN   A 1 159 ? 2.397  -0.740  0.835   0.48 20.44 ?  159 ASN   A CB   1 
ATOM   3494 C  CB   B ASN   A 1 159 ? 2.199  -0.964  0.360   0.22 19.99 ?  159 ASN   A CB   1 
ATOM   3495 C  CB   T ASN   A 1 159 ? 2.390  -0.739  0.761   0.30 20.91 ?  159 ASN   A CB   1 
ATOM   3496 C  CG   A ASN   A 1 159 ? 1.185  0.048   1.317   0.48 21.98 ?  159 ASN   A CG   1 
ATOM   3497 C  CG   B ASN   A 1 159 ? 0.707  -0.698  0.389   0.22 20.30 ?  159 ASN   A CG   1 
ATOM   3498 C  CG   T ASN   A 1 159 ? 1.195  0.068   1.240   0.30 21.74 ?  159 ASN   A CG   1 
ATOM   3499 O  OD1  A ASN   A 1 159 ? 0.363  -0.470  2.070   0.48 23.02 ?  159 ASN   A OD1  1 
ATOM   3500 O  OD1  B ASN   A 1 159 ? 0.080  -0.716  1.448   0.22 20.72 ?  159 ASN   A OD1  1 
ATOM   3501 O  OD1  T ASN   A 1 159 ? 0.397  -0.409  2.045   0.30 22.33 ?  159 ASN   A OD1  1 
ATOM   3502 N  ND2  A ASN   A 1 159 ? 1.070  1.302   0.886   0.48 22.69 ?  159 ASN   A ND2  1 
ATOM   3503 N  ND2  B ASN   A 1 159 ? 0.129  -0.456  -0.781  0.22 20.25 ?  159 ASN   A ND2  1 
ATOM   3504 N  ND2  T ASN   A 1 159 ? 1.067  1.292   0.747   0.30 22.11 ?  159 ASN   A ND2  1 
ATOM   3505 H  H    A ASN   A 1 159 ? 3.681  -0.220  2.854   0.48 23.75 ?  159 ASN   A H    1 
ATOM   3506 H  H    B ASN   A 1 159 ? 3.076  -0.343  2.547   0.22 23.89 ?  159 ASN   A H    1 
ATOM   3507 H  H    T ASN   A 1 159 ? 3.762  -0.188  2.714   0.30 24.33 ?  159 ASN   A H    1 
ATOM   3508 H  HA   A ASN   A 1 159 ? 2.099  -2.186  2.240   0.48 23.31 ?  159 ASN   A HA   1 
ATOM   3509 H  HA   B ASN   A 1 159 ? 1.884  -2.477  1.701   0.22 23.53 ?  159 ASN   A HA   1 
ATOM   3510 H  HA   T ASN   A 1 159 ? 2.120  -2.144  2.220   0.30 24.41 ?  159 ASN   A HA   1 
ATOM   3511 H  HB2  A ASN   A 1 159 ? 3.102  -0.104  0.647   0.48 24.58 ?  159 ASN   A HB2  1 
ATOM   3512 H  HB2  B ASN   A 1 159 ? 2.659  -0.118  0.478   0.22 24.04 ?  159 ASN   A HB2  1 
ATOM   3513 H  HB2  T ASN   A 1 159 ? 3.099  -0.119  0.538   0.30 25.15 ?  159 ASN   A HB2  1 
ATOM   3514 H  HB3  A ASN   A 1 159 ? 2.143  -1.209  0.026   0.48 24.58 ?  159 ASN   A HB3  1 
ATOM   3515 H  HB3  B ASN   A 1 159 ? 2.417  -1.340  -0.508  0.22 24.04 ?  159 ASN   A HB3  1 
ATOM   3516 H  HB3  T ASN   A 1 159 ? 2.122  -1.237  -0.030  0.30 25.15 ?  159 ASN   A HB3  1 
ATOM   3517 H  HD21 A ASN   A 1 159 ? 0.400  1.784   1.132   0.48 27.28 ?  159 ASN   A HD21 1 
ATOM   3518 H  HD21 B ASN   A 1 159 ? -0.716 -0.297  -0.818  0.22 24.35 ?  159 ASN   A HD21 1 
ATOM   3519 H  HD21 T ASN   A 1 159 ? 0.405  1.784   0.988   0.30 26.59 ?  159 ASN   A HD21 1 
ATOM   3520 H  HD22 A ASN   A 1 159 ? 1.667  1.632   0.365   0.48 27.28 ?  159 ASN   A HD22 1 
ATOM   3521 H  HD22 B ASN   A 1 159 ? 0.598  -0.456  -1.502  0.22 24.35 ?  159 ASN   A HD22 1 
ATOM   3522 H  HD22 T ASN   A 1 159 ? 1.646  1.591   0.189   0.30 26.59 ?  159 ASN   A HD22 1 
ATOM   3523 N  N    A LEU   A 1 160 ? 5.055  -2.573  1.096   0.48 17.41 ?  160 LEU   A N    1 
ATOM   3524 N  N    B LEU   A 1 160 ? 4.979  -2.403  0.936   0.22 17.56 ?  160 LEU   A N    1 
ATOM   3525 N  N    T LEU   A 1 160 ? 5.030  -2.613  1.055   0.30 19.74 ?  160 LEU   A N    1 
ATOM   3526 C  CA   A LEU   A 1 160 ? 5.935  -3.602  0.549   0.48 16.43 ?  160 LEU   A CA   1 
ATOM   3527 C  CA   B LEU   A 1 160 ? 6.068  -3.279  0.528   0.22 16.49 ?  160 LEU   A CA   1 
ATOM   3528 C  CA   T LEU   A 1 160 ? 5.906  -3.642  0.505   0.30 19.34 ?  160 LEU   A CA   1 
ATOM   3529 C  C    A LEU   A 1 160 ? 6.123  -4.748  1.534   0.48 15.16 ?  160 LEU   A C    1 
ATOM   3530 C  C    B LEU   A 1 160 ? 6.187  -4.469  1.471   0.22 15.27 ?  160 LEU   A C    1 
ATOM   3531 O  O    A LEU   A 1 160 ? 6.133  -5.921  1.138   0.48 14.86 ?  160 LEU   A O    1 
ATOM   3532 O  O    B LEU   A 1 160 ? 6.209  -5.626  1.034   0.22 14.74 ?  160 LEU   A O    1 
ATOM   3533 C  CB   A LEU   A 1 160 ? 7.281  -2.998  0.160   0.48 16.28 ?  160 LEU   A CB   1 
ATOM   3534 C  CB   B LEU   A 1 160 ? 7.384  -2.505  0.478   0.22 16.50 ?  160 LEU   A CB   1 
ATOM   3535 C  CB   T LEU   A 1 160 ? 7.265  -3.055  0.128   0.30 18.87 ?  160 LEU   A CB   1 
ATOM   3536 C  CG   A LEU   A 1 160 ? 8.317  -4.022  -0.302  0.48 16.88 ?  160 LEU   A CG   1 
ATOM   3537 C  CG   B LEU   A 1 160 ? 8.533  -3.416  0.051   0.22 16.73 ?  160 LEU   A CG   1 
ATOM   3538 C  CG   T LEU   A 1 160 ? 8.315  -4.077  -0.307  0.30 18.72 ?  160 LEU   A CG   1 
ATOM   3539 C  CD1  A LEU   A 1 160 ? 7.800  -4.799  -1.496  0.48 17.84 ?  160 LEU   A CD1  1 
ATOM   3540 C  CD1  B LEU   A 1 160 ? 8.161  -4.117  -1.244  0.22 16.82 ?  160 LEU   A CD1  1 
ATOM   3541 C  CD1  T LEU   A 1 160 ? 7.863  -4.820  -1.549  0.30 18.97 ?  160 LEU   A CD1  1 
ATOM   3542 C  CD2  A LEU   A 1 160 ? 9.621  -3.331  -0.641  0.48 17.18 ?  160 LEU   A CD2  1 
ATOM   3543 C  CD2  B LEU   A 1 160 ? 9.826  -2.644  -0.102  0.22 16.78 ?  160 LEU   A CD2  1 
ATOM   3544 C  CD2  T LEU   A 1 160 ? 9.647  -3.394  -0.548  0.30 18.61 ?  160 LEU   A CD2  1 
ATOM   3545 H  H    A LEU   A 1 160 ? 5.442  -1.828  1.297   0.48 20.95 ?  160 LEU   A H    1 
ATOM   3546 H  H    B LEU   A 1 160 ? 5.218  -1.607  1.160   0.22 21.13 ?  160 LEU   A H    1 
ATOM   3547 H  H    T LEU   A 1 160 ? 5.434  -1.884  1.276   0.30 23.74 ?  160 LEU   A H    1 
ATOM   3548 H  HA   A LEU   A 1 160 ? 5.528  -3.963  -0.247  0.48 19.77 ?  160 LEU   A HA   1 
ATOM   3549 H  HA   B LEU   A 1 160 ? 5.865  -3.607  -0.359  0.22 19.85 ?  160 LEU   A HA   1 
ATOM   3550 H  HB2  A LEU   A 1 160 ? 7.145  -2.368  -0.566  0.48 19.59 ?  160 LEU   A HB2  1 
ATOM   3551 H  HB2  B LEU   A 1 160 ? 7.317  -1.772  -0.160  0.22 19.86 ?  160 LEU   A HB2  1 
ATOM   3552 H  HB2  T LEU   A 1 160 ? 7.142  -2.423  -0.600  0.30 22.70 ?  160 LEU   A HB2  1 
ATOM   3553 H  HB3  A LEU   A 1 160 ? 7.653  -2.538  0.928   0.48 19.59 ?  160 LEU   A HB3  1 
ATOM   3554 H  HB3  B LEU   A 1 160 ? 7.589  -2.163  1.363   0.22 19.86 ?  160 LEU   A HB3  1 
ATOM   3555 H  HB3  T LEU   A 1 160 ? 7.626  -2.599  0.902   0.30 22.70 ?  160 LEU   A HB3  1 
ATOM   3556 H  HG   A LEU   A 1 160 ? 8.496  -4.651  0.415   0.48 20.31 ?  160 LEU   A HG   1 
ATOM   3557 H  HG   B LEU   A 1 160 ? 8.674  -4.094  0.731   0.22 20.13 ?  160 LEU   A HG   1 
ATOM   3558 H  HG   T LEU   A 1 160 ? 8.437  -4.725  0.405   0.30 22.52 ?  160 LEU   A HG   1 
ATOM   3559 H  HD11 A LEU   A 1 160 ? 8.510  -5.363  -1.834  0.48 21.46 ?  160 LEU   A HD11 1 
ATOM   3560 H  HD11 B LEU   A 1 160 ? 8.953  -4.523  -1.603  0.22 20.24 ?  160 LEU   A HD11 1 
ATOM   3561 H  HD11 T LEU   A 1 160 ? 8.575  -5.410  -1.839  0.30 22.82 ?  160 LEU   A HD11 1 
ATOM   3562 H  HD12 A LEU   A 1 160 ? 7.049  -5.346  -1.217  0.48 21.46 ?  160 LEU   A HD12 1 
ATOM   3563 H  HD12 B LEU   A 1 160 ? 7.501  -4.806  -1.063  0.22 20.24 ?  160 LEU   A HD12 1 
ATOM   3564 H  HD12 T LEU   A 1 160 ? 7.070  -5.336  -1.336  0.30 22.82 ?  160 LEU   A HD12 1 
ATOM   3565 H  HD13 A LEU   A 1 160 ? 7.518  -4.172  -2.181  0.48 21.46 ?  160 LEU   A HD13 1 
ATOM   3566 H  HD13 B LEU   A 1 160 ? 7.801  -3.464  -1.868  0.22 20.24 ?  160 LEU   A HD13 1 
ATOM   3567 H  HD13 T LEU   A 1 160 ? 7.662  -4.175  -2.245  0.30 22.82 ?  160 LEU   A HD13 1 
ATOM   3568 H  HD21 A LEU   A 1 160 ? 10.267 -3.997  -0.930  0.48 20.67 ?  160 LEU   A HD21 1 
ATOM   3569 H  HD21 B LEU   A 1 160 ? 10.530 -3.261  -0.356  0.22 20.19 ?  160 LEU   A HD21 1 
ATOM   3570 H  HD21 T LEU   A 1 160 ? 10.298 -4.060  -0.821  0.30 22.39 ?  160 LEU   A HD21 1 
ATOM   3571 H  HD22 A LEU   A 1 160 ? 9.465  -2.691  -1.353  0.48 20.67 ?  160 LEU   A HD22 1 
ATOM   3572 H  HD22 B LEU   A 1 160 ? 9.710  -1.971  -0.788  0.22 20.19 ?  160 LEU   A HD22 1 
ATOM   3573 H  HD22 T LEU   A 1 160 ? 9.540  -2.730  -1.247  0.30 22.39 ?  160 LEU   A HD22 1 
ATOM   3574 H  HD23 A LEU   A 1 160 ? 9.952  -2.873  0.148   0.48 20.67 ?  160 LEU   A HD23 1 
ATOM   3575 H  HD23 B LEU   A 1 160 ? 10.043 -2.224  0.745   0.22 20.19 ?  160 LEU   A HD23 1 
ATOM   3576 H  HD23 T LEU   A 1 160 ? 9.937  -2.966  0.273   0.30 22.39 ?  160 LEU   A HD23 1 
ATOM   3577 N  N    A TYR   A 1 161 ? 6.288  -4.429  2.817   0.78 15.72 ?  161 TYR   A N    1 
ATOM   3578 N  N    B TYR   A 1 161 ? 6.274  -4.199  2.774   0.22 14.96 ?  161 TYR   A N    1 
ATOM   3579 C  CA   A TYR   A 1 161 ? 6.416  -5.471  3.827   0.78 15.46 ?  161 TYR   A CA   1 
ATOM   3580 C  CA   B TYR   A 1 161 ? 6.397  -5.277  3.749   0.22 14.61 ?  161 TYR   A CA   1 
ATOM   3581 C  C    A TYR   A 1 161 ? 5.253  -6.452  3.749   0.78 15.83 ?  161 TYR   A C    1 
ATOM   3582 C  C    B TYR   A 1 161 ? 5.228  -6.252  3.664   0.22 15.23 ?  161 TYR   A C    1 
ATOM   3583 O  O    A TYR   A 1 161 ? 5.449  -7.671  3.666   0.78 15.29 ?  161 TYR   A O    1 
ATOM   3584 O  O    B TYR   A 1 161 ? 5.393  -7.443  3.951   0.22 15.12 ?  161 TYR   A O    1 
ATOM   3585 C  CB   A TYR   A 1 161 ? 6.500  -4.842  5.218   0.78 15.62 ?  161 TYR   A CB   1 
ATOM   3586 C  CB   B TYR   A 1 161 ? 6.509  -4.677  5.152   0.22 13.92 ?  161 TYR   A CB   1 
ATOM   3587 C  CG   A TYR   A 1 161 ? 6.412  -5.870  6.304   0.78 15.33 ?  161 TYR   A CG   1 
ATOM   3588 C  CG   B TYR   A 1 161 ? 6.376  -5.667  6.285   0.22 13.33 ?  161 TYR   A CG   1 
ATOM   3589 C  CD1  A TYR   A 1 161 ? 7.524  -6.603  6.674   0.78 15.37 ?  161 TYR   A CD1  1 
ATOM   3590 C  CD1  B TYR   A 1 161 ? 5.130  -5.979  6.810   0.22 13.38 ?  161 TYR   A CD1  1 
ATOM   3591 C  CD2  A TYR   A 1 161 ? 5.210  -6.125  6.951   0.78 15.42 ?  161 TYR   A CD2  1 
ATOM   3592 C  CD2  B TYR   A 1 161 ? 7.494  -6.271  6.848   0.22 12.97 ?  161 TYR   A CD2  1 
ATOM   3593 C  CE1  A TYR   A 1 161 ? 7.448  -7.563  7.653   0.78 15.16 ?  161 TYR   A CE1  1 
ATOM   3594 C  CE1  B TYR   A 1 161 ? 4.995  -6.877  7.846   0.22 13.51 ?  161 TYR   A CE1  1 
ATOM   3595 C  CE2  A TYR   A 1 161 ? 5.120  -7.086  7.934   0.78 15.28 ?  161 TYR   A CE2  1 
ATOM   3596 C  CE2  B TYR   A 1 161 ? 7.370  -7.172  7.891   0.22 13.20 ?  161 TYR   A CE2  1 
ATOM   3597 C  CZ   A TYR   A 1 161 ? 6.245  -7.804  8.281   0.78 15.37 ?  161 TYR   A CZ   1 
ATOM   3598 C  CZ   B TYR   A 1 161 ? 6.115  -7.470  8.385   0.22 13.83 ?  161 TYR   A CZ   1 
ATOM   3599 O  OH   A TYR   A 1 161 ? 6.180  -8.767  9.261   0.78 15.91 ?  161 TYR   A OH   1 
ATOM   3600 O  OH   B TYR   A 1 161 ? 5.973  -8.362  9.422   0.22 14.83 ?  161 TYR   A OH   1 
ATOM   3601 H  H    A TYR   A 1 161 ? 6.329  -3.628  3.125   0.78 18.92 ?  161 TYR   A H    1 
ATOM   3602 H  H    B TYR   A 1 161 ? 6.270  -3.406  3.113   0.22 18.00 ?  161 TYR   A H    1 
ATOM   3603 H  HA   A TYR   A 1 161 ? 7.233  -5.967  3.676   0.78 18.61 ?  161 TYR   A HA   1 
ATOM   3604 H  HA   B TYR   A 1 161 ? 7.215  -5.766  3.569   0.22 17.59 ?  161 TYR   A HA   1 
ATOM   3605 H  HB2  A TYR   A 1 161 ? 7.350  -4.383  5.310   0.78 18.81 ?  161 TYR   A HB2  1 
ATOM   3606 H  HB2  B TYR   A 1 161 ? 7.377  -4.253  5.238   0.22 16.76 ?  161 TYR   A HB2  1 
ATOM   3607 H  HB3  A TYR   A 1 161 ? 5.768  -4.219  5.334   0.78 18.81 ?  161 TYR   A HB3  1 
ATOM   3608 H  HB3  B TYR   A 1 161 ? 5.811  -4.015  5.261   0.22 16.76 ?  161 TYR   A HB3  1 
ATOM   3609 H  HD1  A TYR   A 1 161 ? 8.335  -6.451  6.248   0.78 18.50 ?  161 TYR   A HD1  1 
ATOM   3610 H  HD1  B TYR   A 1 161 ? 4.369  -5.586  6.449   0.22 16.11 ?  161 TYR   A HD1  1 
ATOM   3611 H  HD2  A TYR   A 1 161 ? 4.448  -5.646  6.716   0.78 18.56 ?  161 TYR   A HD2  1 
ATOM   3612 H  HD2  B TYR   A 1 161 ? 8.340  -6.071  6.514   0.22 15.62 ?  161 TYR   A HD2  1 
ATOM   3613 H  HE1  A TYR   A 1 161 ? 8.204  -8.051  7.891   0.78 18.24 ?  161 TYR   A HE1  1 
ATOM   3614 H  HE1  B TYR   A 1 161 ? 4.152  -7.078  8.183   0.22 16.27 ?  161 TYR   A HE1  1 
ATOM   3615 H  HE2  A TYR   A 1 161 ? 4.305  -7.247  8.363   0.78 18.39 ?  161 TYR   A HE2  1 
ATOM   3616 H  HE2  B TYR   A 1 161 ? 8.127  -7.572  8.259   0.22 15.90 ?  161 TYR   A HE2  1 
ATOM   3617 H  HH   A TYR   A 1 161 ? 6.925  -9.127  9.372   0.78 19.15 ?  161 TYR   A HH   1 
ATOM   3618 H  HH   B TYR   A 1 161 ? 5.160  -8.445  9.622   0.22 17.85 ?  161 TYR   A HH   1 
ATOM   3619 N  N    A ASP   A 1 162 ? 4.025  -5.933  3.785   0.78 16.50 ?  162 ASP   A N    1 
ATOM   3620 N  N    B ASP   A 1 162 ? 4.045  -5.773  3.268   0.22 15.77 ?  162 ASP   A N    1 
ATOM   3621 C  CA   A ASP   A 1 162 ? 2.858  -6.805  3.695   0.78 17.58 ?  162 ASP   A CA   1 
ATOM   3622 C  CA   B ASP   A 1 162 ? 2.873  -6.644  3.243   0.22 16.70 ?  162 ASP   A CA   1 
ATOM   3623 C  C    A ASP   A 1 162 ? 2.891  -7.624  2.415   0.78 17.59 ?  162 ASP   A C    1 
ATOM   3624 C  C    B ASP   A 1 162 ? 2.962  -7.686  2.131   0.22 17.14 ?  162 ASP   A C    1 
ATOM   3625 O  O    A ASP   A 1 162 ? 2.546  -8.814  2.419   0.78 18.57 ?  162 ASP   A O    1 
ATOM   3626 O  O    B ASP   A 1 162 ? 2.590  -8.848  2.335   0.22 17.40 ?  162 ASP   A O    1 
ATOM   3627 C  CB   A ASP   A 1 162 ? 1.571  -5.981  3.757   0.78 18.89 ?  162 ASP   A CB   1 
ATOM   3628 C  CB   B ASP   A 1 162 ? 1.591  -5.817  3.120   0.22 17.30 ?  162 ASP   A CB   1 
ATOM   3629 C  CG   A ASP   A 1 162 ? 1.292  -5.426  5.134   0.78 20.47 ?  162 ASP   A CG   1 
ATOM   3630 C  CG   B ASP   A 1 162 ? 1.115  -5.266  4.452   0.22 17.70 ?  162 ASP   A CG   1 
ATOM   3631 O  OD1  A ASP   A 1 162 ? 1.934  -5.864  6.108   0.78 21.25 ?  162 ASP   A OD1  1 
ATOM   3632 O  OD1  B ASP   A 1 162 ? 1.706  -5.607  5.497   0.22 17.75 ?  162 ASP   A OD1  1 
ATOM   3633 O  OD2  A ASP   A 1 162 ? 0.407  -4.552  5.241   0.78 22.03 -1 162 ASP   A OD2  1 
ATOM   3634 O  OD2  B ASP   A 1 162 ? 0.137  -4.490  4.452   0.22 17.90 -1 162 ASP   A OD2  1 
ATOM   3635 H  H    A ASP   A 1 162 ? 3.844  -5.096  3.868   0.78 19.85 ?  162 ASP   A H    1 
ATOM   3636 H  H    B ASP   A 1 162 ? 3.900  -4.959  3.022   0.22 18.98 ?  162 ASP   A H    1 
ATOM   3637 H  HA   A ASP   A 1 162 ? 2.854  -7.419  4.445   0.78 21.15 ?  162 ASP   A HA   1 
ATOM   3638 H  HA   B ASP   A 1 162 ? 2.837  -7.126  4.077   0.22 20.09 ?  162 ASP   A HA   1 
ATOM   3639 H  HB2  A ASP   A 1 162 ? 1.638  -5.232  3.147   0.78 22.72 ?  162 ASP   A HB2  1 
ATOM   3640 H  HB2  B ASP   A 1 162 ? 1.753  -5.061  2.539   0.22 20.81 ?  162 ASP   A HB2  1 
ATOM   3641 H  HB3  A ASP   A 1 162 ? 0.819  -6.543  3.515   0.78 22.72 ?  162 ASP   A HB3  1 
ATOM   3642 H  HB3  B ASP   A 1 162 ? 0.888  -6.377  2.757   0.22 20.81 ?  162 ASP   A HB3  1 
ATOM   3643 N  N    A LYS   A 1 163 ? 3.299  -7.004  1.304   0.78 18.19 ?  163 LYS   A N    1 
ATOM   3644 N  N    B LYS   A 1 163 ? 3.445  -7.297  0.948   0.22 17.39 ?  163 LYS   A N    1 
ATOM   3645 C  CA   A LYS   A 1 163 ? 3.400  -7.753  0.057   0.78 18.85 ?  163 LYS   A CA   1 
ATOM   3646 C  CA   B LYS   A 1 163 ? 3.575  -8.263  -0.140  0.22 17.66 ?  163 LYS   A CA   1 
ATOM   3647 C  C    A LYS   A 1 163 ? 4.478  -8.828  0.143   0.78 18.15 ?  163 LYS   A C    1 
ATOM   3648 C  C    B LYS   A 1 163 ? 4.691  -9.262  0.147   0.22 16.93 ?  163 LYS   A C    1 
ATOM   3649 O  O    A LYS   A 1 163 ? 4.311  -9.923  -0.405  0.78 17.59 ?  163 LYS   A O    1 
ATOM   3650 O  O    B LYS   A 1 163 ? 4.576  -10.447 -0.188  0.22 16.93 ?  163 LYS   A O    1 
ATOM   3651 C  CB   A LYS   A 1 163 ? 3.668  -6.820  -1.125  0.78 21.19 ?  163 LYS   A CB   1 
ATOM   3652 C  CB   B LYS   A 1 163 ? 3.824  -7.534  -1.461  0.22 19.10 ?  163 LYS   A CB   1 
ATOM   3653 C  CG   A LYS   A 1 163 ? 3.749  -7.564  -2.453  0.78 24.12 ?  163 LYS   A CG   1 
ATOM   3654 C  CG   B LYS   A 1 163 ? 3.088  -8.138  -2.645  0.22 20.56 ?  163 LYS   A CG   1 
ATOM   3655 C  CD   A LYS   A 1 163 ? 4.178  -6.667  -3.599  0.78 27.24 ?  163 LYS   A CD   1 
ATOM   3656 C  CD   B LYS   A 1 163 ? 3.600  -7.598  -3.969  0.22 21.79 ?  163 LYS   A CD   1 
ATOM   3657 C  CE   A LYS   A 1 163 ? 4.100  -7.414  -4.925  0.78 29.48 ?  163 LYS   A CE   1 
ATOM   3658 C  CE   B LYS   A 1 163 ? 2.892  -8.264  -5.138  0.22 22.66 ?  163 LYS   A CE   1 
ATOM   3659 N  NZ   A LYS   A 1 163 ? 4.693  -6.647  -6.055  0.78 30.79 ?  163 LYS   A NZ   1 
ATOM   3660 N  NZ   B LYS   A 1 163 ? 3.833  -8.663  -6.221  0.22 23.16 ?  163 LYS   A NZ   1 
ATOM   3661 H  H    A LYS   A 1 163 ? 3.509  -6.162  1.250   0.78 21.88 ?  163 LYS   A H    1 
ATOM   3662 H  H    B LYS   A 1 163 ? 3.700  -6.498  0.753   0.22 20.93 ?  163 LYS   A H    1 
ATOM   3663 H  HA   A LYS   A 1 163 ? 2.551  -8.191  -0.104  0.78 22.68 ?  163 LYS   A HA   1 
ATOM   3664 H  HA   B LYS   A 1 163 ? 2.745  -8.753  -0.229  0.22 21.25 ?  163 LYS   A HA   1 
ATOM   3665 H  HB2  A LYS   A 1 163 ? 2.945  -6.169  -1.193  0.78 25.49 ?  163 LYS   A HB2  1 
ATOM   3666 H  HB2  B LYS   A 1 163 ? 3.533  -6.613  -1.373  0.22 22.98 ?  163 LYS   A HB2  1 
ATOM   3667 H  HB3  A LYS   A 1 163 ? 4.509  -6.360  -0.987  0.78 25.49 ?  163 LYS   A HB3  1 
ATOM   3668 H  HB3  B LYS   A 1 163 ? 4.773  -7.561  -1.662  0.22 22.98 ?  163 LYS   A HB3  1 
ATOM   3669 H  HG2  A LYS   A 1 163 ? 4.397  -8.281  -2.382  0.78 29.00 ?  163 LYS   A HG2  1 
ATOM   3670 H  HG2  B LYS   A 1 163 ? 3.212  -9.099  -2.643  0.22 24.73 ?  163 LYS   A HG2  1 
ATOM   3671 H  HG3  A LYS   A 1 163 ? 2.874  -7.928  -2.665  0.78 29.00 ?  163 LYS   A HG3  1 
ATOM   3672 H  HG3  B LYS   A 1 163 ? 2.144  -7.922  -2.579  0.22 24.73 ?  163 LYS   A HG3  1 
ATOM   3673 H  HD2  A LYS   A 1 163 ? 3.589  -5.899  -3.645  0.78 32.74 ?  163 LYS   A HD2  1 
ATOM   3674 H  HD2  B LYS   A 1 163 ? 3.433  -6.643  -4.015  0.22 26.20 ?  163 LYS   A HD2  1 
ATOM   3675 H  HD3  A LYS   A 1 163 ? 5.095  -6.384  -3.459  0.78 32.74 ?  163 LYS   A HD3  1 
ATOM   3676 H  HD3  B LYS   A 1 163 ? 4.551  -7.775  -4.043  0.22 26.20 ?  163 LYS   A HD3  1 
ATOM   3677 H  HE2  A LYS   A 1 163 ? 4.573  -8.256  -4.843  0.78 35.43 ?  163 LYS   A HE2  1 
ATOM   3678 H  HE2  B LYS   A 1 163 ? 2.441  -9.062  -4.821  0.22 27.24 ?  163 LYS   A HE2  1 
ATOM   3679 H  HE3  A LYS   A 1 163 ? 3.169  -7.581  -5.136  0.78 35.43 ?  163 LYS   A HE3  1 
ATOM   3680 H  HE3  B LYS   A 1 163 ? 2.247  -7.644  -5.512  0.22 27.24 ?  163 LYS   A HE3  1 
ATOM   3681 H  HZ1  A LYS   A 1 163 ? 4.628  -7.117  -6.809  0.78 37.00 ?  163 LYS   A HZ1  1 
ATOM   3682 H  HZ1  B LYS   A 1 163 ? 3.382  -9.029  -6.895  0.22 27.85 ?  163 LYS   A HZ1  1 
ATOM   3683 H  HZ2  A LYS   A 1 163 ? 4.262  -5.875  -6.158  0.78 37.00 ?  163 LYS   A HZ2  1 
ATOM   3684 H  HZ2  B LYS   A 1 163 ? 4.273  -7.949  -6.519  0.22 27.85 ?  163 LYS   A HZ2  1 
ATOM   3685 H  HZ3  A LYS   A 1 163 ? 5.552  -6.479  -5.893  0.78 37.00 ?  163 LYS   A HZ3  1 
ATOM   3686 H  HZ3  B LYS   A 1 163 ? 4.420  -9.255  -5.910  0.22 27.85 ?  163 LYS   A HZ3  1 
ATOM   3687 N  N    A LEU   A 1 164 ? 5.598  -8.533  0.804   0.78 16.49 ?  164 LEU   A N    1 
ATOM   3688 N  N    B LEU   A 1 164 ? 5.772  -8.798  0.779   0.22 16.09 ?  164 LEU   A N    1 
ATOM   3689 C  CA   A LEU   A 1 164 ? 6.664  -9.529  0.904   0.78 15.99 ?  164 LEU   A CA   1 
ATOM   3690 C  CA   B LEU   A 1 164 ? 6.882  -9.679  1.128   0.22 15.65 ?  164 LEU   A CA   1 
ATOM   3691 C  C    A LEU   A 1 164 ? 6.231  -10.723 1.745   0.78 16.21 ?  164 LEU   A C    1 
ATOM   3692 C  C    B LEU   A 1 164 ? 6.428  -10.782 2.071   0.22 16.08 ?  164 LEU   A C    1 
ATOM   3693 O  O    A LEU   A 1 164 ? 6.530  -11.874 1.401   0.78 15.97 ?  164 LEU   A O    1 
ATOM   3694 O  O    B LEU   A 1 164 ? 6.802  -11.949 1.902   0.22 16.09 ?  164 LEU   A O    1 
ATOM   3695 C  CB   A LEU   A 1 164 ? 7.916  -8.892  1.492   0.78 15.54 ?  164 LEU   A CB   1 
ATOM   3696 C  CB   B LEU   A 1 164 ? 7.996  -8.861  1.785   0.22 14.99 ?  164 LEU   A CB   1 
ATOM   3697 C  CG   A LEU   A 1 164 ? 8.672  -7.963  0.543   0.78 15.49 ?  164 LEU   A CG   1 
ATOM   3698 C  CG   B LEU   A 1 164 ? 8.790  -7.880  0.917   0.22 14.73 ?  164 LEU   A CG   1 
ATOM   3699 C  CD1  A LEU   A 1 164 ? 9.618  -7.088  1.334   0.78 14.86 ?  164 LEU   A CD1  1 
ATOM   3700 C  CD1  B LEU   A 1 164 ? 9.586  -6.913  1.788   0.22 14.75 ?  164 LEU   A CD1  1 
ATOM   3701 C  CD2  A LEU   A 1 164 ? 9.435  -8.745  -0.520  0.78 16.20 ?  164 LEU   A CD2  1 
ATOM   3702 C  CD2  B LEU   A 1 164 ? 9.720  -8.627  -0.028  0.22 14.55 ?  164 LEU   A CD2  1 
ATOM   3703 H  H    A LEU   A 1 164 ? 5.765  -7.773  1.196   0.78 19.85 ?  164 LEU   A H    1 
ATOM   3704 H  H    B LEU   A 1 164 ? 5.877  -7.986  1.023   0.22 19.36 ?  164 LEU   A H    1 
ATOM   3705 H  HA   A LEU   A 1 164 ? 6.876  -9.840  0.016   0.78 19.24 ?  164 LEU   A HA   1 
ATOM   3706 H  HA   B LEU   A 1 164 ? 7.235  -10.093 0.327   0.22 18.84 ?  164 LEU   A HA   1 
ATOM   3707 H  HB2  A LEU   A 1 164 ? 7.671  -8.366  2.269   0.78 18.70 ?  164 LEU   A HB2  1 
ATOM   3708 H  HB2  B LEU   A 1 164 ? 7.600  -8.341  2.501   0.22 18.04 ?  164 LEU   A HB2  1 
ATOM   3709 H  HB3  A LEU   A 1 164 ? 8.529  -9.595  1.752   0.78 18.70 ?  164 LEU   A HB3  1 
ATOM   3710 H  HB3  B LEU   A 1 164 ? 8.639  -9.480  2.162   0.22 18.04 ?  164 LEU   A HB3  1 
ATOM   3711 H  HG   A LEU   A 1 164 ? 8.040  -7.382  0.090   0.78 18.65 ?  164 LEU   A HG   1 
ATOM   3712 H  HG   B LEU   A 1 164 ? 8.173  -7.357  0.383   0.22 17.73 ?  164 LEU   A HG   1 
ATOM   3713 H  HD11 A LEU   A 1 164 ? 10.109 -6.517  0.724   0.78 17.89 ?  164 LEU   A HD11 1 
ATOM   3714 H  HD11 B LEU   A 1 164 ? 10.117 -6.335  1.216   0.22 17.75 ?  164 LEU   A HD11 1 
ATOM   3715 H  HD12 A LEU   A 1 164 ? 9.102  -6.546  1.952   0.78 17.89 ?  164 LEU   A HD12 1 
ATOM   3716 H  HD12 B LEU   A 1 164 ? 8.971  -6.378  2.315   0.22 17.75 ?  164 LEU   A HD12 1 
ATOM   3717 H  HD13 A LEU   A 1 164 ? 10.234 -7.654  1.826   0.78 17.89 ?  164 LEU   A HD13 1 
ATOM   3718 H  HD13 B LEU   A 1 164 ? 10.169 -7.420  2.375   0.22 17.75 ?  164 LEU   A HD13 1 
ATOM   3719 H  HD21 A LEU   A 1 164 ? 9.937  -8.124  -1.073  0.78 19.50 ?  164 LEU   A HD21 1 
ATOM   3720 H  HD21 B LEU   A 1 164 ? 10.216 -7.982  -0.558  0.22 17.52 ?  164 LEU   A HD21 1 
ATOM   3721 H  HD22 A LEU   A 1 164 ? 10.043 -9.362  -0.083  0.78 19.50 ?  164 LEU   A HD22 1 
ATOM   3722 H  HD22 B LEU   A 1 164 ? 10.333 -9.168  0.494   0.22 17.52 ?  164 LEU   A HD22 1 
ATOM   3723 H  HD23 A LEU   A 1 164 ? 8.802  -9.236  -1.066  0.78 19.50 ?  164 LEU   A HD23 1 
ATOM   3724 H  HD23 B LEU   A 1 164 ? 9.188  -9.193  -0.608  0.22 17.52 ?  164 LEU   A HD23 1 
ATOM   3725 N  N    A VAL   A 1 165 ? 5.552  -10.462 2.860   0.78 15.57 ?  165 VAL   A N    1 
ATOM   3726 N  N    B VAL   A 1 165 ? 5.624  -10.431 3.073   0.22 16.35 ?  165 VAL   A N    1 
ATOM   3727 C  CA   A VAL   A 1 165 ? 5.074  -11.543 3.719   0.78 15.44 ?  165 VAL   A CA   1 
ATOM   3728 C  CA   B VAL   A 1 165 ? 5.157  -11.426 4.032   0.22 16.73 ?  165 VAL   A CA   1 
ATOM   3729 C  C    A VAL   A 1 165 ? 4.059  -12.399 2.975   0.78 15.42 ?  165 VAL   A C    1 
ATOM   3730 C  C    B VAL   A 1 165 ? 4.035  -12.269 3.439   0.22 16.54 ?  165 VAL   A C    1 
ATOM   3731 O  O    A VAL   A 1 165 ? 4.175  -13.630 2.921   0.78 14.91 ?  165 VAL   A O    1 
ATOM   3732 O  O    B VAL   A 1 165 ? 3.991  -13.488 3.641   0.22 16.64 ?  165 VAL   A O    1 
ATOM   3733 C  CB   A VAL   A 1 165 ? 4.489  -10.965 5.021   0.78 15.36 ?  165 VAL   A CB   1 
ATOM   3734 C  CB   B VAL   A 1 165 ? 4.769  -10.748 5.362   0.22 17.22 ?  165 VAL   A CB   1 
ATOM   3735 C  CG1  A VAL   A 1 165 ? 3.764  -12.046 5.823   0.78 15.60 ?  165 VAL   A CG1  1 
ATOM   3736 C  CG1  B VAL   A 1 165 ? 3.540  -11.401 5.983   0.22 17.60 ?  165 VAL   A CG1  1 
ATOM   3737 C  CG2  A VAL   A 1 165 ? 5.589  -10.293 5.853   0.78 15.50 ?  165 VAL   A CG2  1 
ATOM   3738 C  CG2  B VAL   A 1 165 ? 5.948  -10.800 6.330   0.22 17.34 ?  165 VAL   A CG2  1 
ATOM   3739 H  H    A VAL   A 1 165 ? 5.348  -9.672  3.140   0.78 18.74 ?  165 VAL   A H    1 
ATOM   3740 H  H    B VAL   A 1 165 ? 5.337  -9.632  3.217   0.22 19.68 ?  165 VAL   A H    1 
ATOM   3741 H  HA   A VAL   A 1 165 ? 5.824  -12.107 3.959   0.78 18.58 ?  165 VAL   A HA   1 
ATOM   3742 H  HA   B VAL   A 1 165 ? 5.888  -12.025 4.228   0.22 20.13 ?  165 VAL   A HA   1 
ATOM   3743 H  HB   A VAL   A 1 165 ? 3.841  -10.281 4.796   0.78 18.49 ?  165 VAL   A HB   1 
ATOM   3744 H  HB   B VAL   A 1 165 ? 4.562  -9.813  5.201   0.22 20.72 ?  165 VAL   A HB   1 
ATOM   3745 H  HG11 A VAL   A 1 165 ? 3.642  -11.733 6.736   0.78 18.78 ?  165 VAL   A HG11 1 
ATOM   3746 H  HG11 B VAL   A 1 165 ? 3.418  -11.043 6.877   0.22 21.17 ?  165 VAL   A HG11 1 
ATOM   3747 H  HG12 A VAL   A 1 165 ? 2.895  -12.209 5.418   0.78 18.78 ?  165 VAL   A HG12 1 
ATOM   3748 H  HG12 B VAL   A 1 165 ? 2.760  -11.196 5.444   0.22 21.17 ?  165 VAL   A HG12 1 
ATOM   3749 H  HG13 A VAL   A 1 165 ? 4.292  -12.854 5.818   0.78 18.78 ?  165 VAL   A HG13 1 
ATOM   3750 H  HG13 B VAL   A 1 165 ? 3.676  -12.359 6.034   0.22 21.17 ?  165 VAL   A HG13 1 
ATOM   3751 H  HG21 A VAL   A 1 165 ? 5.199  -9.948  6.674   0.78 18.66 ?  165 VAL   A HG21 1 
ATOM   3752 H  HG21 B VAL   A 1 165 ? 5.720  -10.315 7.138   0.22 20.86 ?  165 VAL   A HG21 1 
ATOM   3753 H  HG22 A VAL   A 1 165 ? 6.273  -10.946 6.061   0.78 18.66 ?  165 VAL   A HG22 1 
ATOM   3754 H  HG22 B VAL   A 1 165 ? 6.140  -11.728 6.545   0.22 20.86 ?  165 VAL   A HG22 1 
ATOM   3755 H  HG23 A VAL   A 1 165 ? 5.971  -9.563  5.340   0.78 18.66 ?  165 VAL   A HG23 1 
ATOM   3756 H  HG23 B VAL   A 1 165 ? 6.722  -10.393 5.908   0.22 20.86 ?  165 VAL   A HG23 1 
ATOM   3757 N  N    A SER   A 1 166 ? 3.051  -11.755 2.382   0.78 16.13 ?  166 SER   A N    1 
ATOM   3758 N  N    B SER   A 1 166 ? 3.131  -11.652 2.681   0.22 16.19 ?  166 SER   A N    1 
ATOM   3759 C  CA   A SER   A 1 166 ? 1.939  -12.495 1.798   0.78 17.02 ?  166 SER   A CA   1 
ATOM   3760 C  CA   B SER   A 1 166 ? 1.972  -12.360 2.148   0.22 15.58 ?  166 SER   A CA   1 
ATOM   3761 C  C    A SER   A 1 166 ? 2.382  -13.338 0.618   0.78 17.92 ?  166 SER   A C    1 
ATOM   3762 C  C    B SER   A 1 166 ? 2.276  -13.169 0.890   0.22 15.74 ?  166 SER   A C    1 
ATOM   3763 O  O    A SER   A 1 166 ? 1.765  -14.375 0.337   0.78 19.67 ?  166 SER   A O    1 
ATOM   3764 O  O    B SER   A 1 166 ? 1.333  -13.622 0.232   0.22 15.95 ?  166 SER   A O    1 
ATOM   3765 C  CB   A SER   A 1 166 ? 0.839  -11.531 1.348   0.78 18.17 ?  166 SER   A CB   1 
ATOM   3766 C  CB   B SER   A 1 166 ? 0.834  -11.377 1.867   0.22 15.33 ?  166 SER   A CB   1 
ATOM   3767 O  OG   A SER   A 1 166 ? 0.168  -10.944 2.452   0.78 19.57 ?  166 SER   A OG   1 
ATOM   3768 O  OG   B SER   A 1 166 ? 1.117  -10.620 0.706   0.22 15.12 ?  166 SER   A OG   1 
ATOM   3769 H  H    A SER   A 1 166 ? 2.989  -10.903 2.313   0.78 19.42 ?  166 SER   A H    1 
ATOM   3770 H  H    B SER   A 1 166 ? 3.161  -10.816 2.470   0.22 19.48 ?  166 SER   A H    1 
ATOM   3771 H  HA   A SER   A 1 166 ? 1.562  -13.093 2.461   0.78 20.48 ?  166 SER   A HA   1 
ATOM   3772 H  HA   B SER   A 1 166 ? 1.656  -12.982 2.812   0.22 18.75 ?  166 SER   A HA   1 
ATOM   3773 H  HB2  A SER   A 1 166 ? 1.233  -10.834 0.800   0.78 21.86 ?  166 SER   A HB2  1 
ATOM   3774 H  HB2  B SER   A 1 166 ? 0.009  -11.873 1.728   0.22 18.45 ?  166 SER   A HB2  1 
ATOM   3775 H  HB3  A SER   A 1 166 ? 0.180  -12.021 0.830   0.78 21.86 ?  166 SER   A HB3  1 
ATOM   3776 H  HB3  B SER   A 1 166 ? 0.729  -10.779 2.629   0.22 18.45 ?  166 SER   A HB3  1 
ATOM   3777 H  HG   A SER   A 1 166 ? -0.412 -10.400 2.181   0.78 23.54 ?  166 SER   A HG   1 
ATOM   3778 H  HG   B SER   A 1 166 ? 1.856  -10.232 0.796   0.22 18.20 ?  166 SER   A HG   1 
ATOM   3779 N  N    A SER   A 1 167 ? 3.430  -12.906 -0.085  0.78 16.64 ?  167 SER   A N    1 
ATOM   3780 N  N    B SER   A 1 167 ? 3.550  -13.382 0.540   0.22 15.98 ?  167 SER   A N    1 
ATOM   3781 C  CA   A SER   A 1 167 ? 3.914  -13.605 -1.262  0.78 17.71 ?  167 SER   A CA   1 
ATOM   3782 C  CA   B SER   A 1 167 ? 3.853  -14.137 -0.672  0.22 16.10 ?  167 SER   A CA   1 
ATOM   3783 C  C    A SER   A 1 167 ? 5.056  -14.564 -0.953  0.78 18.03 ?  167 SER   A C    1 
ATOM   3784 C  C    B SER   A 1 167 ? 5.048  -15.066 -0.495  0.22 16.00 ?  167 SER   A C    1 
ATOM   3785 O  O    A SER   A 1 167 ? 5.544  -15.232 -1.871  0.78 19.18 ?  167 SER   A O    1 
ATOM   3786 O  O    B SER   A 1 167 ? 5.658  -15.471 -1.492  0.22 16.53 ?  167 SER   A O    1 
ATOM   3787 C  CB   A SER   A 1 167 ? 4.350  -12.599 -2.340  0.78 17.92 ?  167 SER   A CB   1 
ATOM   3788 C  CB   B SER   A 1 167 ? 4.142  -13.204 -1.850  0.22 16.58 ?  167 SER   A CB   1 
ATOM   3789 O  OG   A SER   A 1 167 ? 5.415  -11.774 -1.882  0.78 18.13 ?  167 SER   A OG   1 
ATOM   3790 O  OG   B SER   A 1 167 ? 5.392  -12.554 -1.686  0.22 17.16 ?  167 SER   A OG   1 
ATOM   3791 H  H    A SER   A 1 167 ? 3.879  -12.185 0.104   0.78 20.02 ?  167 SER   A H    1 
ATOM   3792 H  H    B SER   A 1 167 ? 4.242  -13.114 0.985   0.22 19.23 ?  167 SER   A H    1 
ATOM   3793 H  HA   A SER   A 1 167 ? 3.185  -14.122 -1.628  0.78 21.31 ?  167 SER   A HA   1 
ATOM   3794 H  HA   B SER   A 1 167 ? 3.082  -14.680 -0.898  0.22 19.37 ?  167 SER   A HA   1 
ATOM   3795 H  HB2  A SER   A 1 167 ? 4.649  -13.085 -3.123  0.78 21.56 ?  167 SER   A HB2  1 
ATOM   3796 H  HB2  B SER   A 1 167 ? 4.163  -13.728 -2.666  0.22 19.95 ?  167 SER   A HB2  1 
ATOM   3797 H  HB3  A SER   A 1 167 ? 3.585  -12.040 -2.580  0.78 21.56 ?  167 SER   A HB3  1 
ATOM   3798 H  HB3  B SER   A 1 167 ? 3.443  -12.535 -1.900  0.22 19.95 ?  167 SER   A HB3  1 
ATOM   3799 H  HG   A SER   A 1 167 ? 5.145  -11.323 -1.217  0.78 21.81 ?  167 SER   A HG   1 
ATOM   3800 H  HG   B SER   A 1 167 ? 5.388  -12.102 -0.976  0.22 20.64 ?  167 SER   A HG   1 
ATOM   3801 N  N    A PHE   A 1 168 ? 5.487  -14.659 0.305   0.78 17.01 ?  168 PHE   A N    1 
ATOM   3802 N  N    B PHE   A 1 168 ? 5.389  -15.428 0.738   0.22 15.48 ?  168 PHE   A N    1 
ATOM   3803 C  CA   A PHE   A 1 168 ? 6.661  -15.464 0.618   0.78 17.29 ?  168 PHE   A CA   1 
ATOM   3804 C  CA   B PHE   A 1 168 ? 6.654  -16.101 0.997   0.22 15.50 ?  168 PHE   A CA   1 
ATOM   3805 C  C    A PHE   A 1 168 ? 6.346  -16.945 0.498   0.78 18.41 ?  168 PHE   A C    1 
ATOM   3806 C  C    B PHE   A 1 168 ? 6.551  -17.616 0.865   0.22 15.57 ?  168 PHE   A C    1 
ATOM   3807 O  O    A PHE   A 1 168 ? 5.365  -17.431 1.069   0.78 20.21 ?  168 PHE   A O    1 
ATOM   3808 O  O    B PHE   A 1 168 ? 7.418  -18.245 0.246   0.22 14.75 ?  168 PHE   A O    1 
ATOM   3809 C  CB   A PHE   A 1 168 ? 7.171  -15.193 2.029   0.78 16.56 ?  168 PHE   A CB   1 
ATOM   3810 C  CB   B PHE   A 1 168 ? 7.169  -15.715 2.386   0.22 15.58 ?  168 PHE   A CB   1 
ATOM   3811 C  CG   A PHE   A 1 168 ? 8.431  -15.953 2.347   0.78 15.91 ?  168 PHE   A CG   1 
ATOM   3812 C  CG   B PHE   A 1 168 ? 8.424  -16.430 2.778   0.22 15.81 ?  168 PHE   A CG   1 
ATOM   3813 C  CD1  A PHE   A 1 168 ? 9.620  -15.591 1.750   0.78 16.24 ?  168 PHE   A CD1  1 
ATOM   3814 C  CD1  B PHE   A 1 168 ? 9.620  -16.142 2.148   0.22 16.15 ?  168 PHE   A CD1  1 
ATOM   3815 C  CD2  A PHE   A 1 168 ? 8.428  -17.050 3.198   0.78 15.96 ?  168 PHE   A CD2  1 
ATOM   3816 C  CD2  B PHE   A 1 168 ? 8.409  -17.394 3.771   0.22 16.04 ?  168 PHE   A CD2  1 
ATOM   3817 C  CE1  A PHE   A 1 168 ? 10.786 -16.286 2.010   0.78 15.50 ?  168 PHE   A CE1  1 
ATOM   3818 C  CE1  B PHE   A 1 168 ? 10.778 -16.800 2.500   0.22 16.20 ?  168 PHE   A CE1  1 
ATOM   3819 C  CE2  A PHE   A 1 168 ? 9.602  -17.746 3.464   0.78 16.05 ?  168 PHE   A CE2  1 
ATOM   3820 C  CE2  B PHE   A 1 168 ? 9.566  -18.053 4.130   0.22 16.33 ?  168 PHE   A CE2  1 
ATOM   3821 C  CZ   A PHE   A 1 168 ? 10.777 -17.362 2.867   0.78 15.83 ?  168 PHE   A CZ   1 
ATOM   3822 C  CZ   B PHE   A 1 168 ? 10.752 -17.755 3.491   0.22 16.51 ?  168 PHE   A CZ   1 
ATOM   3823 H  H    A PHE   A 1 168 ? 5.123  -14.266 0.984   0.78 20.46 ?  168 PHE   A H    1 
ATOM   3824 H  H    B PHE   A 1 168 ? 4.906  -15.305 1.437   0.22 18.63 ?  168 PHE   A H    1 
ATOM   3825 H  HA   A PHE   A 1 168 ? 7.369  -15.246 -0.009  0.78 20.80 ?  168 PHE   A HA   1 
ATOM   3826 H  HA   B PHE   A 1 168 ? 7.306  -15.803 0.349   0.22 18.65 ?  168 PHE   A HA   1 
ATOM   3827 H  HB2  A PHE   A 1 168 ? 7.358  -14.246 2.122   0.78 19.92 ?  168 PHE   A HB2  1 
ATOM   3828 H  HB2  B PHE   A 1 168 ? 7.355  -14.762 2.396   0.22 18.75 ?  168 PHE   A HB2  1 
ATOM   3829 H  HB3  A PHE   A 1 168 ? 6.490  -15.461 2.666   0.78 19.92 ?  168 PHE   A HB3  1 
ATOM   3830 H  HB3  B PHE   A 1 168 ? 6.489  -15.925 3.044   0.22 18.75 ?  168 PHE   A HB3  1 
ATOM   3831 H  HD1  A PHE   A 1 168 ? 9.643  -14.865 1.171   0.78 19.54 ?  168 PHE   A HD1  1 
ATOM   3832 H  HD1  B PHE   A 1 168 ? 9.645  -15.498 1.478   0.22 19.43 ?  168 PHE   A HD1  1 
ATOM   3833 H  HD2  A PHE   A 1 168 ? 7.634  -17.315 3.605   0.78 19.21 ?  168 PHE   A HD2  1 
ATOM   3834 H  HD2  B PHE   A 1 168 ? 7.610  -17.596 4.204   0.22 19.30 ?  168 PHE   A HD2  1 
ATOM   3835 H  HE1  A PHE   A 1 168 ? 11.587 -16.026 1.608   0.78 18.65 ?  168 PHE   A HE1  1 
ATOM   3836 H  HE1  B PHE   A 1 168 ? 11.578 -16.598 2.071   0.22 19.49 ?  168 PHE   A HE1  1 
ATOM   3837 H  HE2  A PHE   A 1 168 ? 9.585  -18.478 4.042   0.78 19.31 ?  168 PHE   A HE2  1 
ATOM   3838 H  HE2  B PHE   A 1 168 ? 9.545  -18.699 4.800   0.22 19.65 ?  168 PHE   A HE2  1 
ATOM   3839 H  HZ   A PHE   A 1 168 ? 11.563 -17.830 3.042   0.78 19.05 ?  168 PHE   A HZ   1 
ATOM   3840 H  HZ   B PHE   A 1 168 ? 11.533 -18.198 3.729   0.22 19.87 ?  168 PHE   A HZ   1 
ATOM   3841 N  N    A LEU   A 1 169 ? 7.211  -17.673 -0.201  0.78 20.10 ?  169 LEU   A N    1 
ATOM   3842 N  N    B LEU   A 1 169 ? 5.512  -18.211 1.437   0.22 16.72 ?  169 LEU   A N    1 
ATOM   3843 C  CA   A LEU   A 1 169 ? 7.005  -19.101 -0.371  0.78 23.11 ?  169 LEU   A CA   1 
ATOM   3844 C  CA   B LEU   A 1 169 ? 5.371  -19.660 1.438   0.22 18.44 ?  169 LEU   A CA   1 
ATOM   3845 C  C    A LEU   A 1 169 ? 7.832  -19.883 0.640   0.78 23.55 ?  169 LEU   A C    1 
ATOM   3846 C  C    B LEU   A 1 169 ? 5.129  -20.214 0.040   0.22 19.37 ?  169 LEU   A C    1 
ATOM   3847 O  O    A LEU   A 1 169 ? 7.276  -20.409 1.608   0.78 23.88 ?  169 LEU   A O    1 
ATOM   3848 O  O    B LEU   A 1 169 ? 5.621  -21.289 -0.306  0.22 19.64 ?  169 LEU   A O    1 
ATOM   3849 C  CB   A LEU   A 1 169 ? 7.338  -19.531 -1.803  0.78 24.97 ?  169 LEU   A CB   1 
ATOM   3850 C  CB   B LEU   A 1 169 ? 4.216  -20.068 2.342   0.22 19.25 ?  169 LEU   A CB   1 
ATOM   3851 C  CG   A LEU   A 1 169 ? 7.048  -20.996 -2.146  0.78 26.71 ?  169 LEU   A CG   1 
ATOM   3852 C  CG   B LEU   A 1 169 ? 4.566  -20.789 3.628   0.22 20.08 ?  169 LEU   A CG   1 
ATOM   3853 C  CD1  A LEU   A 1 169 ? 5.633  -21.391 -1.746  0.78 27.19 ?  169 LEU   A CD1  1 
ATOM   3854 C  CD1  B LEU   A 1 169 ? 3.290  -21.152 4.346   0.22 20.54 ?  169 LEU   A CD1  1 
ATOM   3855 C  CD2  A LEU   A 1 169 ? 7.270  -21.258 -3.630  0.78 27.25 ?  169 LEU   A CD2  1 
ATOM   3856 C  CD2  B LEU   A 1 169 ? 5.385  -22.022 3.317   0.22 20.30 ?  169 LEU   A CD2  1 
ATOM   3857 O  OXT  A LEU   A 1 169 ? 9.056  -19.996 0.527   0.78 23.07 -1 169 LEU   A OXT  1 
ATOM   3858 O  OXT  B LEU   A 1 169 ? 4.429  -19.610 -0.770  0.22 20.11 -1 169 LEU   A OXT  1 
ATOM   3859 H  H    A LEU   A 1 169 ? 7.920  -17.363 -0.578  0.78 24.18 ?  169 LEU   A H    1 
ATOM   3860 H  H    B LEU   A 1 169 ? 4.871  -17.796 1.836   0.22 20.12 ?  169 LEU   A H    1 
ATOM   3861 H  HA   A LEU   A 1 169 ? 6.074  -19.301 -0.204  0.78 27.79 ?  169 LEU   A HA   1 
ATOM   3862 H  HA   B LEU   A 1 169 ? 6.186  -20.053 1.784   0.22 22.19 ?  169 LEU   A HA   1 
ATOM   3863 H  HB2  A LEU   A 1 169 ? 6.818  -18.984 -2.412  0.78 30.02 ?  169 LEU   A HB2  1 
ATOM   3864 H  HB2  B LEU   A 1 169 ? 3.702  -19.288 2.575   0.22 23.16 ?  169 LEU   A HB2  1 
ATOM   3865 H  HB3  A LEU   A 1 169 ? 8.281  -19.380 -1.957  0.78 30.02 ?  169 LEU   A HB3  1 
ATOM   3866 H  HB3  B LEU   A 1 169 ? 3.660  -20.670 1.850   0.22 23.16 ?  169 LEU   A HB3  1 
ATOM   3867 H  HG   A LEU   A 1 169 ? 7.662  -21.561 -1.653  0.78 32.11 ?  169 LEU   A HG   1 
ATOM   3868 H  HG   B LEU   A 1 169 ? 5.085  -20.198 4.190   0.22 24.16 ?  169 LEU   A HG   1 
ATOM   3869 H  HD11 A LEU   A 1 169 ? 5.422  -22.252 -2.140  0.78 32.68 ?  169 LEU   A HD11 1 
ATOM   3870 H  HD11 B LEU   A 1 169 ? 3.505  -21.408 5.253   0.22 24.70 ?  169 LEU   A HD11 1 
ATOM   3871 H  HD12 A LEU   A 1 169 ? 5.581  -21.449 -0.779  0.78 32.68 ?  169 LEU   A HD12 1 
ATOM   3872 H  HD12 B LEU   A 1 169 ? 2.699  -20.382 4.346   0.22 24.70 ?  169 LEU   A HD12 1 
ATOM   3873 H  HD13 A LEU   A 1 169 ? 5.013  -20.719 -2.072  0.78 32.68 ?  169 LEU   A HD13 1 
ATOM   3874 H  HD13 B LEU   A 1 169 ? 2.868  -21.889 3.878   0.22 24.70 ?  169 LEU   A HD13 1 
ATOM   3875 H  HD21 A LEU   A 1 169 ? 7.086  -22.193 -3.817  0.78 32.75 ?  169 LEU   A HD21 1 
ATOM   3876 H  HD21 B LEU   A 1 169 ? 5.456  -22.556 4.118   0.22 24.41 ?  169 LEU   A HD21 1 
ATOM   3877 H  HD22 A LEU   A 1 169 ? 6.669  -20.695 -4.144  0.78 32.75 ?  169 LEU   A HD22 1 
ATOM   3878 H  HD22 B LEU   A 1 169 ? 4.943  -22.524 2.615   0.22 24.41 ?  169 LEU   A HD22 1 
ATOM   3879 H  HD23 A LEU   A 1 169 ? 8.190  -21.051 -3.853  0.78 32.75 ?  169 LEU   A HD23 1 
ATOM   3880 H  HD23 B LEU   A 1 169 ? 6.269  -21.754 3.023   0.22 24.41 ?  169 LEU   A HD23 1 
ATOM   3881 N  N    A SER   B 1 1   ? 50.719 -9.214  -23.753 0.78 29.06 ?  1   SER   B N    1 
ATOM   3882 N  N    B SER   B 1 1   ? 50.692 -9.207  -23.754 0.22 28.11 ?  1   SER   B N    1 
ATOM   3883 C  CA   A SER   B 1 1   ? 51.219 -10.270 -22.849 0.78 28.93 ?  1   SER   B CA   1 
ATOM   3884 C  CA   B SER   B 1 1   ? 51.201 -10.216 -22.801 0.22 28.10 ?  1   SER   B CA   1 
ATOM   3885 C  C    A SER   B 1 1   ? 50.147 -11.312 -22.580 0.78 27.08 ?  1   SER   B C    1 
ATOM   3886 C  C    B SER   B 1 1   ? 50.146 -11.283 -22.548 0.22 27.32 ?  1   SER   B C    1 
ATOM   3887 O  O    A SER   B 1 1   ? 48.952 -11.104 -22.838 0.78 26.34 ?  1   SER   B O    1 
ATOM   3888 O  O    B SER   B 1 1   ? 48.983 -11.131 -22.929 0.22 27.10 ?  1   SER   B O    1 
ATOM   3889 C  CB   A SER   B 1 1   ? 51.692 -9.675  -21.527 0.78 29.73 ?  1   SER   B CB   1 
ATOM   3890 C  CB   B SER   B 1 1   ? 51.598 -9.557  -21.484 0.22 28.36 ?  1   SER   B CB   1 
ATOM   3891 O  OG   A SER   B 1 1   ? 50.595 -9.420  -20.672 0.78 31.63 ?  1   SER   B OG   1 
ATOM   3892 O  OG   B SER   B 1 1   ? 50.494 -9.504  -20.601 0.22 29.04 ?  1   SER   B OG   1 
ATOM   3893 H  H1   A SER   B 1 1   ? 50.555 -9.569  -24.550 0.78 34.93 ?  1   SER   B H1   1 
ATOM   3894 H  H1   B SER   B 1 1   ? 51.379 -8.746  -24.078 0.22 33.78 ?  1   SER   B H1   1 
ATOM   3895 H  H2   A SER   B 1 1   ? 49.975 -8.873  -23.414 0.78 34.93 ?  1   SER   B H2   1 
ATOM   3896 H  H2   B SER   B 1 1   ? 50.269 -9.621  -24.416 0.22 33.78 ?  1   SER   B H2   1 
ATOM   3897 H  H3   A SER   B 1 1   ? 51.339 -8.583  -23.824 0.78 34.93 ?  1   SER   B H3   1 
ATOM   3898 H  H3   B SER   B 1 1   ? 50.135 -8.664  -23.330 0.22 33.78 ?  1   SER   B H3   1 
ATOM   3899 H  HA   A SER   B 1 1   ? 51.970 -10.702 -23.278 0.78 34.77 ?  1   SER   B HA   1 
ATOM   3900 H  HA   B SER   B 1 1   ? 51.981 -10.634 -23.187 0.22 33.77 ?  1   SER   B HA   1 
ATOM   3901 H  HB2  A SER   B 1 1   ? 52.291 -10.308 -21.101 0.78 35.73 ?  1   SER   B HB2  1 
ATOM   3902 H  HB2  B SER   B 1 1   ? 52.312 -10.076 -21.084 0.22 34.09 ?  1   SER   B HB2  1 
ATOM   3903 H  HB3  A SER   B 1 1   ? 52.155 -8.843  -21.699 0.78 35.73 ?  1   SER   B HB3  1 
ATOM   3904 H  HB3  B SER   B 1 1   ? 51.902 -8.653  -21.661 0.22 34.09 ?  1   SER   B HB3  1 
ATOM   3905 H  HG   A SER   B 1 1   ? 50.808 -8.839  -20.104 0.78 38.01 ?  1   SER   B HG   1 
ATOM   3906 H  HG   B SER   B 1 1   ? 50.552 -8.823  -20.116 0.22 34.90 ?  1   SER   B HG   1 
ATOM   3907 N  N    A MET   B 1 2   ? 50.597 -12.434 -22.038 0.78 26.01 ?  2   MET   B N    1 
ATOM   3908 N  N    B MET   B 1 2   ? 50.563 -12.358 -21.888 0.22 26.77 ?  2   MET   B N    1 
ATOM   3909 C  CA   A MET   B 1 2   ? 49.784 -13.630 -21.868 0.78 25.84 ?  2   MET   B CA   1 
ATOM   3910 C  CA   B MET   B 1 2   ? 49.747 -13.554 -21.712 0.22 26.27 ?  2   MET   B CA   1 
ATOM   3911 C  C    A MET   B 1 2   ? 49.547 -13.834 -20.380 0.78 23.25 ?  2   MET   B C    1 
ATOM   3912 C  C    B MET   B 1 2   ? 49.480 -13.746 -20.226 0.22 24.29 ?  2   MET   B C    1 
ATOM   3913 O  O    A MET   B 1 2   ? 50.484 -14.131 -19.633 0.78 23.36 ?  2   MET   B O    1 
ATOM   3914 O  O    B MET   B 1 2   ? 50.385 -14.113 -19.469 0.22 24.44 ?  2   MET   B O    1 
ATOM   3915 C  CB   A MET   B 1 2   ? 50.519 -14.819 -22.474 0.78 30.10 ?  2   MET   B CB   1 
ATOM   3916 C  CB   B MET   B 1 2   ? 50.485 -14.754 -22.290 0.22 27.99 ?  2   MET   B CB   1 
ATOM   3917 C  CG   A MET   B 1 2   ? 49.683 -16.074 -22.640 0.78 33.69 ?  2   MET   B CG   1 
ATOM   3918 C  CG   B MET   B 1 2   ? 49.598 -15.904 -22.736 0.22 29.47 ?  2   MET   B CG   1 
ATOM   3919 S  SD   A MET   B 1 2   ? 50.548 -17.302 -23.635 0.78 37.26 ?  2   MET   B SD   1 
ATOM   3920 S  SD   B MET   B 1 2   ? 50.501 -17.048 -23.787 0.22 30.86 ?  2   MET   B SD   1 
ATOM   3921 C  CE   A MET   B 1 2   ? 51.085 -16.273 -24.996 0.78 37.68 ?  2   MET   B CE   1 
ATOM   3922 C  CE   B MET   B 1 2   ? 51.394 -15.890 -24.815 0.22 31.13 ?  2   MET   B CE   1 
ATOM   3923 H  H    A MET   B 1 2   ? 51.402 -12.535 -21.750 0.78 31.26 ?  2   MET   B H    1 
ATOM   3924 H  H    B MET   B 1 2   ? 51.343 -12.424 -21.532 0.22 32.18 ?  2   MET   B H    1 
ATOM   3925 H  HA   A MET   B 1 2   ? 48.937 -13.530 -22.327 0.78 31.06 ?  2   MET   B HA   1 
ATOM   3926 H  HA   B MET   B 1 2   ? 48.912 -13.457 -22.194 0.22 31.58 ?  2   MET   B HA   1 
ATOM   3927 H  HB2  A MET   B 1 2   ? 50.837 -14.536 -23.341 0.78 36.17 ?  2   MET   B HB2  1 
ATOM   3928 H  HB2  B MET   B 1 2   ? 50.989 -14.415 -23.041 0.22 33.64 ?  2   MET   B HB2  1 
ATOM   3929 H  HB3  A MET   B 1 2   ? 51.272 -15.055 -21.913 0.78 36.17 ?  2   MET   B HB3  1 
ATOM   3930 H  HB3  B MET   B 1 2   ? 51.093 -15.115 -21.633 0.22 33.64 ?  2   MET   B HB3  1 
ATOM   3931 H  HG2  A MET   B 1 2   ? 49.502 -16.457 -21.764 0.78 40.49 ?  2   MET   B HG2  1 
ATOM   3932 H  HG2  B MET   B 1 2   ? 49.285 -16.390 -21.955 0.22 35.42 ?  2   MET   B HG2  1 
ATOM   3933 H  HG3  A MET   B 1 2   ? 48.854 -15.858 -23.092 0.78 40.49 ?  2   MET   B HG3  1 
ATOM   3934 H  HG3  B MET   B 1 2   ? 48.846 -15.567 -23.241 0.22 35.42 ?  2   MET   B HG3  1 
ATOM   3935 H  HE1  A MET   B 1 2   ? 51.254 -16.834 -25.757 0.78 45.27 ?  2   MET   B HE1  1 
ATOM   3936 H  HE1  B MET   B 1 2   ? 51.647 -16.340 -25.618 0.22 37.41 ?  2   MET   B HE1  1 
ATOM   3937 H  HE2  A MET   B 1 2   ? 50.377 -15.637 -25.195 0.78 45.27 ?  2   MET   B HE2  1 
ATOM   3938 H  HE2  B MET   B 1 2   ? 50.814 -15.135 -25.023 0.22 37.41 ?  2   MET   B HE2  1 
ATOM   3939 H  HE3  A MET   B 1 2   ? 51.894 -15.794 -24.744 0.78 45.27 ?  2   MET   B HE3  1 
ATOM   3940 H  HE3  B MET   B 1 2   ? 52.185 -15.580 -24.336 0.22 37.41 ?  2   MET   B HE3  1 
ATOM   3941 N  N    A VAL   B 1 3   ? 48.300 -13.655 -19.950 0.78 21.09 ?  3   VAL   B N    1 
ATOM   3942 N  N    B VAL   B 1 3   ? 48.242 -13.492 -19.811 0.22 22.14 ?  3   VAL   B N    1 
ATOM   3943 C  CA   A VAL   B 1 3   ? 47.891 -13.911 -18.576 0.78 19.90 ?  3   VAL   B CA   1 
ATOM   3944 C  CA   B VAL   B 1 3   ? 47.804 -13.757 -18.447 0.22 20.18 ?  3   VAL   B CA   1 
ATOM   3945 C  C    A VAL   B 1 3   ? 46.653 -14.798 -18.600 0.78 18.21 ?  3   VAL   B C    1 
ATOM   3946 C  C    B VAL   B 1 3   ? 46.552 -14.619 -18.488 0.22 18.18 ?  3   VAL   B C    1 
ATOM   3947 O  O    A VAL   B 1 3   ? 45.928 -14.875 -19.594 0.78 18.62 ?  3   VAL   B O    1 
ATOM   3948 O  O    B VAL   B 1 3   ? 45.722 -14.507 -19.395 0.22 17.96 ?  3   VAL   B O    1 
ATOM   3949 C  CB   A VAL   B 1 3   ? 47.614 -12.611 -17.788 0.78 21.39 ?  3   VAL   B CB   1 
ATOM   3950 C  CB   B VAL   B 1 3   ? 47.547 -12.466 -17.639 0.22 20.49 ?  3   VAL   B CB   1 
ATOM   3951 C  CG1  A VAL   B 1 3   ? 48.885 -11.770 -17.675 0.78 22.03 ?  3   VAL   B CG1  1 
ATOM   3952 C  CG1  B VAL   B 1 3   ? 48.823 -11.645 -17.523 0.22 20.68 ?  3   VAL   B CG1  1 
ATOM   3953 C  CG2  A VAL   B 1 3   ? 46.492 -11.823 -18.444 0.78 22.23 ?  3   VAL   B CG2  1 
ATOM   3954 C  CG2  B VAL   B 1 3   ? 46.429 -11.654 -18.271 0.22 20.66 ?  3   VAL   B CG2  1 
ATOM   3955 H  H    A VAL   B 1 3   ? 47.657 -13.392 -20.452 0.78 25.37 ?  3   VAL   B H    1 
ATOM   3956 H  H    B VAL   B 1 3   ? 47.634 -13.154 -20.316 0.22 26.63 ?  3   VAL   B H    1 
ATOM   3957 H  HA   A VAL   B 1 3   ? 48.597 -14.395 -18.116 0.78 23.94 ?  3   VAL   B HA   1 
ATOM   3958 H  HA   B VAL   B 1 3   ? 48.496 -14.258 -17.993 0.22 24.28 ?  3   VAL   B HA   1 
ATOM   3959 H  HB   A VAL   B 1 3   ? 47.329 -12.844 -16.890 0.78 25.73 ?  3   VAL   B HB   1 
ATOM   3960 H  HB   B VAL   B 1 3   ? 47.268 -12.714 -16.744 0.22 24.64 ?  3   VAL   B HB   1 
ATOM   3961 H  HG11 A VAL   B 1 3   ? 48.684 -10.968 -17.169 0.78 26.49 ?  3   VAL   B HG11 1 
ATOM   3962 H  HG11 B VAL   B 1 3   ? 48.639 -10.852 -16.997 0.22 24.87 ?  3   VAL   B HG11 1 
ATOM   3963 H  HG12 A VAL   B 1 3   ? 49.564 -12.290 -17.217 0.78 26.49 ?  3   VAL   B HG12 1 
ATOM   3964 H  HG12 B VAL   B 1 3   ? 49.505 -12.181 -17.088 0.22 24.87 ?  3   VAL   B HG12 1 
ATOM   3965 H  HG13 A VAL   B 1 3   ? 49.187 -11.537 -18.565 0.78 26.49 ?  3   VAL   B HG13 1 
ATOM   3966 H  HG13 B VAL   B 1 3   ? 49.118 -11.393 -18.412 0.22 24.87 ?  3   VAL   B HG13 1 
ATOM   3967 H  HG21 A VAL   B 1 3   ? 46.429 -10.955 -18.020 0.78 26.73 ?  3   VAL   B HG21 1 
ATOM   3968 H  HG21 B VAL   B 1 3   ? 46.384 -10.791 -17.833 0.22 24.85 ?  3   VAL   B HG21 1 
ATOM   3969 H  HG22 A VAL   B 1 3   ? 46.688 -11.719 -19.388 0.78 26.73 ?  3   VAL   B HG22 1 
ATOM   3970 H  HG22 B VAL   B 1 3   ? 46.617 -11.539 -19.215 0.22 24.85 ?  3   VAL   B HG22 1 
ATOM   3971 H  HG23 A VAL   B 1 3   ? 45.657 -12.306 -18.332 0.78 26.73 ?  3   VAL   B HG23 1 
ATOM   3972 H  HG23 B VAL   B 1 3   ? 45.589 -12.128 -18.157 0.22 24.85 ?  3   VAL   B HG23 1 
ATOM   3973 N  N    . ASN   B 1 4   ? 46.419 -15.483 -17.483 1.00 16.74 ?  4   ASN   B N    1 
ATOM   3974 C  CA   . ASN   B 1 4   ? 45.284 -16.403 -17.375 1.00 15.95 ?  4   ASN   B CA   1 
ATOM   3975 C  C    . ASN   B 1 4   ? 45.234 -17.368 -18.559 1.00 16.12 ?  4   ASN   B C    1 
ATOM   3976 O  O    . ASN   B 1 4   ? 44.173 -17.633 -19.123 1.00 16.89 ?  4   ASN   B O    1 
ATOM   3977 C  CB   . ASN   B 1 4   ? 43.957 -15.653 -17.215 1.00 15.20 ?  4   ASN   B CB   1 
ATOM   3978 C  CG   . ASN   B 1 4   ? 43.909 -14.829 -15.949 1.00 14.40 ?  4   ASN   B CG   1 
ATOM   3979 O  OD1  . ASN   B 1 4   ? 44.194 -15.333 -14.862 1.00 14.13 ?  4   ASN   B OD1  1 
ATOM   3980 N  ND2  . ASN   B 1 4   ? 43.571 -13.548 -16.083 1.00 15.21 ?  4   ASN   B ND2  1 
ATOM   3981 H  H    A ASN   B 1 4   ? 46.903 -15.437 -16.776 0.78 20.15 ?  4   ASN   B H    1 
ATOM   3982 H  H    B ASN   B 1 4   ? 46.980 -15.552 -16.838 0.22 20.15 ?  4   ASN   B H    1 
ATOM   3983 H  HA   . ASN   B 1 4   ? 45.409 -16.936 -16.572 1.00 19.20 ?  4   ASN   B HA   1 
ATOM   3984 H  HB2  . ASN   B 1 4   ? 43.833 -15.057 -17.967 1.00 18.29 ?  4   ASN   B HB2  1 
ATOM   3985 H  HB3  . ASN   B 1 4   ? 43.231 -16.298 -17.179 1.00 18.29 ?  4   ASN   B HB3  1 
ATOM   3986 H  HD21 . ASN   B 1 4   ? 43.536 -13.034 -15.391 1.00 18.30 ?  4   ASN   B HD21 1 
ATOM   3987 H  HD22 . ASN   B 1 4   ? 43.386 -13.227 -16.860 1.00 18.30 ?  4   ASN   B HD22 1 
ATOM   3988 N  N    . SER   B 1 5   ? 46.395 -17.900 -18.939 1.00 17.34 ?  5   SER   B N    1 
ATOM   3989 C  CA   . SER   B 1 5   ? 46.489 -18.814 -20.077 1.00 19.99 ?  5   SER   B CA   1 
ATOM   3990 C  C    . SER   B 1 5   ? 46.477 -20.251 -19.565 1.00 21.31 ?  5   SER   B C    1 
ATOM   3991 O  O    . SER   B 1 5   ? 47.483 -20.954 -19.555 1.00 23.57 ?  5   SER   B O    1 
ATOM   3992 C  CB   . SER   B 1 5   ? 47.737 -18.512 -20.902 1.00 21.92 ?  5   SER   B CB   1 
ATOM   3993 O  OG   . SER   B 1 5   ? 48.914 -18.700 -20.135 1.00 24.33 ?  5   SER   B OG   1 
ATOM   3994 H  H    . SER   B 1 5   ? 47.147 -17.755 -18.548 1.00 20.87 ?  5   SER   B H    1 
ATOM   3995 H  HA   . SER   B 1 5   ? 45.714 -18.698 -20.645 1.00 24.04 ?  5   SER   B HA   1 
ATOM   3996 H  HB2  . SER   B 1 5   ? 47.756 -19.101 -21.674 1.00 26.36 ?  5   SER   B HB2  1 
ATOM   3997 H  HB3  . SER   B 1 5   ? 47.685 -17.589 -21.194 1.00 26.36 ?  5   SER   B HB3  1 
ATOM   3998 H  HG   . SER   B 1 5   ? 48.977 -19.503 -19.897 1.00 29.25 ?  5   SER   B HG   1 
ATOM   3999 N  N    . PHE   B 1 6   ? 45.296 -20.668 -19.123 1.00 21.54 ?  6   PHE   B N    1 
ATOM   4000 C  CA   . PHE   B 1 6   ? 45.100 -22.012 -18.607 1.00 20.94 ?  6   PHE   B CA   1 
ATOM   4001 C  C    . PHE   B 1 6   ? 45.024 -22.999 -19.762 1.00 23.92 ?  6   PHE   B C    1 
ATOM   4002 O  O    . PHE   B 1 6   ? 44.352 -22.745 -20.766 1.00 26.14 ?  6   PHE   B O    1 
ATOM   4003 C  CB   . PHE   B 1 6   ? 43.805 -22.066 -17.798 1.00 18.69 ?  6   PHE   B CB   1 
ATOM   4004 C  CG   . PHE   B 1 6   ? 43.821 -21.206 -16.565 1.00 16.56 ?  6   PHE   B CG   1 
ATOM   4005 C  CD1  . PHE   B 1 6   ? 44.326 -21.696 -15.376 1.00 15.55 ?  6   PHE   B CD1  1 
ATOM   4006 C  CD2  . PHE   B 1 6   ? 43.336 -19.903 -16.598 1.00 16.00 ?  6   PHE   B CD2  1 
ATOM   4007 C  CE1  . PHE   B 1 6   ? 44.333 -20.914 -14.235 1.00 15.10 ?  6   PHE   B CE1  1 
ATOM   4008 C  CE2  . PHE   B 1 6   ? 43.350 -19.109 -15.460 1.00 16.20 ?  6   PHE   B CE2  1 
ATOM   4009 C  CZ   . PHE   B 1 6   ? 43.854 -19.611 -14.279 1.00 15.36 ?  6   PHE   B CZ   1 
ATOM   4010 H  H    . PHE   B 1 6   ? 44.582 -20.191 -19.118 1.00 25.91 ?  6   PHE   B H    1 
ATOM   4011 H  HA   . PHE   B 1 6   ? 45.838 -22.259 -18.029 1.00 25.18 ?  6   PHE   B HA   1 
ATOM   4012 H  HB2  . PHE   B 1 6   ? 43.074 -21.764 -18.362 1.00 22.48 ?  6   PHE   B HB2  1 
ATOM   4013 H  HB3  . PHE   B 1 6   ? 43.646 -22.981 -17.519 1.00 22.48 ?  6   PHE   B HB3  1 
ATOM   4014 H  HD1  . PHE   B 1 6   ? 44.656 -22.564 -15.340 1.00 18.72 ?  6   PHE   B HD1  1 
ATOM   4015 H  HD2  . PHE   B 1 6   ? 42.990 -19.564 -17.391 1.00 19.26 ?  6   PHE   B HD2  1 
ATOM   4016 H  HE1  . PHE   B 1 6   ? 44.685 -21.251 -13.441 1.00 18.18 ?  6   PHE   B HE1  1 
ATOM   4017 H  HE2  . PHE   B 1 6   ? 43.016 -18.240 -15.492 1.00 19.50 ?  6   PHE   B HE2  1 
ATOM   4018 H  HZ   . PHE   B 1 6   ? 43.865 -19.086 -13.511 1.00 18.48 ?  6   PHE   B HZ   1 
ATOM   4019 N  N    . SER   B 1 7   ? 45.725 -24.125 -19.622 1.00 25.07 ?  7   SER   B N    1 
ATOM   4020 C  CA   . SER   B 1 7   ? 45.806 -25.118 -20.683 1.00 27.47 ?  7   SER   B CA   1 
ATOM   4021 C  C    . SER   B 1 7   ? 45.750 -26.517 -20.090 1.00 26.34 ?  7   SER   B C    1 
ATOM   4022 O  O    . SER   B 1 7   ? 46.333 -26.779 -19.035 1.00 27.24 ?  7   SER   B O    1 
ATOM   4023 C  CB   . SER   B 1 7   ? 47.103 -24.958 -21.487 1.00 30.65 ?  7   SER   B CB   1 
ATOM   4024 O  OG   . SER   B 1 7   ? 47.089 -25.772 -22.647 1.00 32.53 ?  7   SER   B OG   1 
ATOM   4025 H  H    . SER   B 1 7   ? 46.170 -24.338 -18.912 1.00 30.14 ?  7   SER   B H    1 
ATOM   4026 H  HA   . SER   B 1 7   ? 45.056 -25.015 -21.286 1.00 33.03 ?  7   SER   B HA   1 
ATOM   4027 H  HB2  . SER   B 1 7   ? 47.194 -24.031 -21.753 1.00 36.84 ?  7   SER   B HB2  1 
ATOM   4028 H  HB3  . SER   B 1 7   ? 47.855 -25.217 -20.929 1.00 36.84 ?  7   SER   B HB3  1 
ATOM   4029 H  HG   . SER   B 1 7   ? 47.805 -25.673 -23.076 1.00 39.10 ?  7   SER   B HG   1 
ATOM   4030 N  N    . GLY   B 1 8   ? 45.048 -27.413 -20.782 1.00 26.16 ?  8   GLY   B N    1 
ATOM   4031 C  CA   . GLY   B 1 8   ? 45.012 -28.804 -20.390 1.00 25.38 ?  8   GLY   B CA   1 
ATOM   4032 C  C    . GLY   B 1 8   ? 44.058 -29.126 -19.269 1.00 23.89 ?  8   GLY   B C    1 
ATOM   4033 O  O    . GLY   B 1 8   ? 44.193 -30.186 -18.645 1.00 25.15 ?  8   GLY   B O    1 
ATOM   4034 H  H    . GLY   B 1 8   ? 44.585 -27.231 -21.481 1.00 31.44 ?  8   GLY   B H    1 
ATOM   4035 H  HA2  . GLY   B 1 8   ? 44.759 -29.340 -21.157 1.00 30.51 ?  8   GLY   B HA2  1 
ATOM   4036 H  HA3  . GLY   B 1 8   ? 45.895 -29.077 -20.107 1.00 30.51 ?  8   GLY   B HA3  1 
ATOM   4037 N  N    . TYR   B 1 9   ? 43.079 -28.265 -19.000 1.00 22.14 ?  9   TYR   B N    1 
ATOM   4038 C  CA   . TYR   B 1 9   ? 42.111 -28.538 -17.950 1.00 19.99 ?  9   TYR   B CA   1 
ATOM   4039 C  C    . TYR   B 1 9   ? 40.933 -29.333 -18.480 1.00 19.43 ?  9   TYR   B C    1 
ATOM   4040 O  O    . TYR   B 1 9   ? 40.525 -29.197 -19.637 1.00 21.52 ?  9   TYR   B O    1 
ATOM   4041 C  CB   . TYR   B 1 9   ? 41.595 -27.251 -17.312 1.00 19.06 ?  9   TYR   B CB   1 
ATOM   4042 C  CG   . TYR   B 1 9   ? 42.617 -26.616 -16.402 1.00 18.30 ?  9   TYR   B CG   1 
ATOM   4043 C  CD1  . TYR   B 1 9   ? 43.698 -25.929 -16.927 1.00 19.00 ?  9   TYR   B CD1  1 
ATOM   4044 C  CD2  . TYR   B 1 9   ? 42.521 -26.730 -15.022 1.00 17.63 ?  9   TYR   B CD2  1 
ATOM   4045 C  CE1  . TYR   B 1 9   ? 44.652 -25.361 -16.107 1.00 19.27 ?  9   TYR   B CE1  1 
ATOM   4046 C  CE2  . TYR   B 1 9   ? 43.472 -26.163 -14.191 1.00 18.10 ?  9   TYR   B CE2  1 
ATOM   4047 C  CZ   . TYR   B 1 9   ? 44.538 -25.480 -14.741 1.00 18.95 ?  9   TYR   B CZ   1 
ATOM   4048 O  OH   . TYR   B 1 9   ? 45.486 -24.923 -13.920 1.00 19.65 ?  9   TYR   B OH   1 
ATOM   4049 H  H    . TYR   B 1 9   ? 42.940 -27.531 -19.424 1.00 26.62 ?  9   TYR   B H    1 
ATOM   4050 H  HA   . TYR   B 1 9   ? 42.529 -29.065 -17.258 1.00 24.05 ?  9   TYR   B HA   1 
ATOM   4051 H  HB2  . TYR   B 1 9   ? 41.361 -26.612 -18.007 1.00 22.93 ?  9   TYR   B HB2  1 
ATOM   4052 H  HB3  . TYR   B 1 9   ? 40.814 -27.466 -16.782 1.00 22.93 ?  9   TYR   B HB3  1 
ATOM   4053 H  HD1  . TYR   B 1 9   ? 43.777 -25.850 -17.852 1.00 22.86 ?  9   TYR   B HD1  1 
ATOM   4054 H  HD2  . TYR   B 1 9   ? 41.800 -27.199 -14.653 1.00 21.21 ?  9   TYR   B HD2  1 
ATOM   4055 H  HE1  . TYR   B 1 9   ? 45.364 -24.906 -16.478 1.00 23.18 ?  9   TYR   B HE1  1 
ATOM   4056 H  HE2  . TYR   B 1 9   ? 43.387 -26.254 -13.269 1.00 21.78 ?  9   TYR   B HE2  1 
ATOM   4057 H  HH   . TYR   B 1 9   ? 46.068 -24.541 -14.383 1.00 23.64 ?  9   TYR   B HH   1 
ATOM   4058 N  N    . LEU   B 1 10  ? 40.396 -30.178 -17.609 1.00 17.82 ?  10  LEU   B N    1 
ATOM   4059 C  CA   . LEU   B 1 10  ? 39.194 -30.945 -17.881 1.00 17.89 ?  10  LEU   B CA   1 
ATOM   4060 C  C    . LEU   B 1 10  ? 38.005 -30.187 -17.308 1.00 17.32 ?  10  LEU   B C    1 
ATOM   4061 O  O    . LEU   B 1 10  ? 38.031 -29.765 -16.147 1.00 17.08 ?  10  LEU   B O    1 
ATOM   4062 C  CB   . LEU   B 1 10  ? 39.312 -32.320 -17.226 1.00 18.99 ?  10  LEU   B CB   1 
ATOM   4063 C  CG   . LEU   B 1 10  ? 38.173 -33.287 -17.526 1.00 20.57 ?  10  LEU   B CG   1 
ATOM   4064 C  CD1  . LEU   B 1 10  ? 38.258 -33.803 -18.956 1.00 22.05 ?  10  LEU   B CD1  1 
ATOM   4065 C  CD2  . LEU   B 1 10  ? 38.167 -34.430 -16.528 1.00 22.01 ?  10  LEU   B CD2  1 
ATOM   4066 H  H    . LEU   B 1 10  ? 40.720 -30.329 -16.823 1.00 21.44 ?  10  LEU   B H    1 
ATOM   4067 H  HA   . LEU   B 1 10  ? 39.073 -31.056 -18.835 1.00 21.53 ?  10  LEU   B HA   1 
ATOM   4068 H  HB2  . LEU   B 1 10  ? 40.135 -32.737 -17.532 1.00 22.84 ?  10  LEU   B HB2  1 
ATOM   4069 H  HB3  . LEU   B 1 10  ? 39.348 -32.204 -16.264 1.00 22.84 ?  10  LEU   B HB3  1 
ATOM   4070 H  HG   . LEU   B 1 10  ? 37.333 -32.817 -17.433 1.00 24.73 ?  10  LEU   B HG   1 
ATOM   4071 H  HD11 . LEU   B 1 10  ? 37.538 -34.437 -19.104 1.00 26.52 ?  10  LEU   B HD11 1 
ATOM   4072 H  HD12 . LEU   B 1 10  ? 38.166 -33.053 -19.566 1.00 26.52 ?  10  LEU   B HD12 1 
ATOM   4073 H  HD13 . LEU   B 1 10  ? 39.114 -34.236 -19.087 1.00 26.52 ?  10  LEU   B HD13 1 
ATOM   4074 H  HD21 . LEU   B 1 10  ? 37.441 -35.031 -16.748 1.00 26.47 ?  10  LEU   B HD21 1 
ATOM   4075 H  HD22 . LEU   B 1 10  ? 39.015 -34.894 -16.580 1.00 26.47 ?  10  LEU   B HD22 1 
ATOM   4076 H  HD23 . LEU   B 1 10  ? 38.040 -34.064 -15.639 1.00 26.47 ?  10  LEU   B HD23 1 
ATOM   4077 N  N    . LYS   B 1 11  ? 36.975 -30.007 -18.126 1.00 18.34 ?  11  LYS   B N    1 
ATOM   4078 C  CA   . LYS   B 1 11  ? 35.782 -29.286 -17.709 1.00 20.58 ?  11  LYS   B CA   1 
ATOM   4079 C  C    . LYS   B 1 11  ? 34.906 -30.208 -16.868 1.00 19.72 ?  11  LYS   B C    1 
ATOM   4080 O  O    . LYS   B 1 11  ? 34.529 -31.296 -17.318 1.00 21.38 ?  11  LYS   B O    1 
ATOM   4081 C  CB   . LYS   B 1 11  ? 35.032 -28.813 -18.954 1.00 24.62 ?  11  LYS   B CB   1 
ATOM   4082 C  CG   . LYS   B 1 11  ? 33.878 -27.861 -18.696 1.00 28.27 ?  11  LYS   B CG   1 
ATOM   4083 C  CD   . LYS   B 1 11  ? 33.148 -27.544 -19.997 1.00 31.20 ?  11  LYS   B CD   1 
ATOM   4084 C  CE   . LYS   B 1 11  ? 32.124 -26.437 -19.815 1.00 33.25 ?  11  LYS   B CE   1 
ATOM   4085 N  NZ   . LYS   B 1 11  ? 32.771 -25.127 -19.539 1.00 34.31 ?  11  LYS   B NZ   1 
ATOM   4086 H  H    . LYS   B 1 11  ? 36.938 -30.301 -18.933 1.00 22.07 ?  11  LYS   B H    1 
ATOM   4087 H  HA   . LYS   B 1 11  ? 36.030 -28.514 -17.178 1.00 24.75 ?  11  LYS   B HA   1 
ATOM   4088 H  HB2  . LYS   B 1 11  ? 35.661 -28.354 -19.536 1.00 29.60 ?  11  LYS   B HB2  1 
ATOM   4089 H  HB3  . LYS   B 1 11  ? 34.674 -29.588 -19.412 1.00 29.60 ?  11  LYS   B HB3  1 
ATOM   4090 H  HG2  . LYS   B 1 11  ? 33.248 -28.275 -18.085 1.00 33.99 ?  11  LYS   B HG2  1 
ATOM   4091 H  HG3  . LYS   B 1 11  ? 34.217 -27.032 -18.325 1.00 33.99 ?  11  LYS   B HG3  1 
ATOM   4092 H  HD2  . LYS   B 1 11  ? 33.792 -27.253 -20.662 1.00 37.50 ?  11  LYS   B HD2  1 
ATOM   4093 H  HD3  . LYS   B 1 11  ? 32.685 -28.339 -20.306 1.00 37.50 ?  11  LYS   B HD3  1 
ATOM   4094 H  HE2  . LYS   B 1 11  ? 31.598 -26.352 -20.627 1.00 39.96 ?  11  LYS   B HE2  1 
ATOM   4095 H  HE3  . LYS   B 1 11  ? 31.548 -26.659 -19.067 1.00 39.96 ?  11  LYS   B HE3  1 
ATOM   4096 H  HZ1  . LYS   B 1 11  ? 32.153 -24.491 -19.472 1.00 41.23 ?  11  LYS   B HZ1  1 
ATOM   4097 H  HZ2  . LYS   B 1 11  ? 33.228 -25.168 -18.778 1.00 41.23 ?  11  LYS   B HZ2  1 
ATOM   4098 H  HZ3  . LYS   B 1 11  ? 33.329 -24.919 -20.201 1.00 41.23 ?  11  LYS   B HZ3  1 
ATOM   4099 N  N    . LEU   B 1 12  ? 34.581 -29.778 -15.650 1.00 17.65 ?  12  LEU   B N    1 
ATOM   4100 C  CA   . LEU   B 1 12  ? 33.624 -30.483 -14.805 1.00 17.44 ?  12  LEU   B CA   1 
ATOM   4101 C  C    . LEU   B 1 12  ? 32.233 -29.876 -14.896 1.00 17.29 ?  12  LEU   B C    1 
ATOM   4102 O  O    . LEU   B 1 12  ? 31.247 -30.595 -15.071 1.00 17.67 ?  12  LEU   B O    1 
ATOM   4103 C  CB   . LEU   B 1 12  ? 34.088 -30.496 -13.342 1.00 16.90 ?  12  LEU   B CB   1 
ATOM   4104 C  CG   . LEU   B 1 12  ? 35.425 -31.180 -13.065 1.00 16.78 ?  12  LEU   B CG   1 
ATOM   4105 C  CD1  . LEU   B 1 12  ? 35.767 -31.138 -11.586 1.00 17.19 ?  12  LEU   B CD1  1 
ATOM   4106 C  CD2  . LEU   B 1 12  ? 35.416 -32.615 -13.575 1.00 17.27 ?  12  LEU   B CD2  1 
ATOM   4107 H  H    . LEU   B 1 12  ? 34.903 -29.068 -15.288 1.00 21.23 ?  12  LEU   B H    1 
ATOM   4108 H  HA   . LEU   B 1 12  ? 33.552 -31.399 -15.106 1.00 20.99 ?  12  LEU   B HA   1 
ATOM   4109 H  HB2  . LEU   B 1 12  ? 34.160 -29.581 -13.037 1.00 20.33 ?  12  LEU   B HB2  1 
ATOM   4110 H  HB3  . LEU   B 1 12  ? 33.411 -30.957 -12.816 1.00 20.33 ?  12  LEU   B HB3  1 
ATOM   4111 H  HG   . LEU   B 1 12  ? 36.119 -30.703 -13.540 1.00 20.20 ?  12  LEU   B HG   1 
ATOM   4112 H  HD11 . LEU   B 1 12  ? 36.624 -31.579 -11.449 1.00 20.68 ?  12  LEU   B HD11 1 
ATOM   4113 H  HD12 . LEU   B 1 12  ? 35.822 -30.216 -11.298 1.00 20.68 ?  12  LEU   B HD12 1 
ATOM   4114 H  HD13 . LEU   B 1 12  ? 35.077 -31.603 -11.087 1.00 20.68 ?  12  LEU   B HD13 1 
ATOM   4115 H  HD21 . LEU   B 1 12  ? 36.211 -33.068 -13.256 1.00 20.78 ?  12  LEU   B HD21 1 
ATOM   4116 H  HD22 . LEU   B 1 12  ? 34.622 -33.063 -13.244 1.00 20.78 ?  12  LEU   B HD22 1 
ATOM   4117 H  HD23 . LEU   B 1 12  ? 35.408 -32.603 -14.546 1.00 20.78 ?  12  LEU   B HD23 1 
ATOM   4118 N  N    . THR   B 1 13  ? 32.143 -28.559 -14.768 1.00 17.43 ?  13  THR   B N    1 
ATOM   4119 C  CA   . THR   B 1 13  ? 30.919 -27.807 -14.972 1.00 17.51 ?  13  THR   B CA   1 
ATOM   4120 C  C    . THR   B 1 13  ? 31.249 -26.611 -15.856 1.00 19.54 ?  13  THR   B C    1 
ATOM   4121 O  O    . THR   B 1 13  ? 32.393 -26.420 -16.286 1.00 20.22 ?  13  THR   B O    1 
ATOM   4122 C  CB   . THR   B 1 13  ? 30.320 -27.336 -13.642 1.00 16.96 ?  13  THR   B CB   1 
ATOM   4123 O  OG1  . THR   B 1 13  ? 31.166 -26.320 -13.090 1.00 16.86 ?  13  THR   B OG1  1 
ATOM   4124 C  CG2  . THR   B 1 13  ? 30.189 -28.493 -12.652 1.00 17.50 ?  13  THR   B CG2  1 
ATOM   4125 H  H    . THR   B 1 13  ? 32.808 -28.057 -14.549 1.00 20.98 ?  13  THR   B H    1 
ATOM   4126 H  HA   . THR   B 1 13  ? 30.264 -28.362 -15.420 1.00 21.06 ?  13  THR   B HA   1 
ATOM   4127 H  HB   . THR   B 1 13  ? 29.432 -26.968 -13.796 1.00 20.41 ?  13  THR   B HB   1 
ATOM   4128 H  HG1  . THR   B 1 13  ? 30.863 -25.556 -13.285 1.00 20.28 ?  13  THR   B HG1  1 
ATOM   4129 H  HG21 . THR   B 1 13  ? 29.701 -28.204 -11.863 1.00 21.06 ?  13  THR   B HG21 1 
ATOM   4130 H  HG22 . THR   B 1 13  ? 29.710 -29.229 -13.065 1.00 21.06 ?  13  THR   B HG22 1 
ATOM   4131 H  HG23 . THR   B 1 13  ? 31.068 -28.801 -12.383 1.00 21.06 ?  13  THR   B HG23 1 
ATOM   4132 N  N    A ASP   B 1 14  ? 30.233 -25.788 -16.117 0.78 20.58 ?  14  ASP   B N    1 
ATOM   4133 N  N    B ASP   B 1 14  ? 30.238 -25.776 -16.110 0.22 20.47 ?  14  ASP   B N    1 
ATOM   4134 C  CA   A ASP   B 1 14  ? 30.437 -24.626 -16.973 0.78 22.11 ?  14  ASP   B CA   1 
ATOM   4135 C  CA   B ASP   B 1 14  ? 30.434 -24.621 -16.979 0.22 21.37 ?  14  ASP   B CA   1 
ATOM   4136 C  C    A ASP   B 1 14  ? 31.531 -23.707 -16.442 0.78 20.38 ?  14  ASP   B C    1 
ATOM   4137 C  C    B ASP   B 1 14  ? 31.437 -23.623 -16.417 0.22 19.63 ?  14  ASP   B C    1 
ATOM   4138 O  O    A ASP   B 1 14  ? 32.166 -22.991 -17.225 0.78 21.59 ?  14  ASP   B O    1 
ATOM   4139 O  O    B ASP   B 1 14  ? 31.897 -22.748 -17.160 0.22 19.79 ?  14  ASP   B O    1 
ATOM   4140 C  CB   A ASP   B 1 14  ? 29.128 -23.853 -17.133 0.78 25.76 ?  14  ASP   B CB   1 
ATOM   4141 C  CB   B ASP   B 1 14  ? 29.105 -23.908 -17.233 0.22 23.90 ?  14  ASP   B CB   1 
ATOM   4142 C  CG   A ASP   B 1 14  ? 28.165 -24.521 -18.090 0.78 29.36 ?  14  ASP   B CG   1 
ATOM   4143 C  CG   B ASP   B 1 14  ? 28.214 -24.662 -18.202 0.22 26.20 ?  14  ASP   B CG   1 
ATOM   4144 O  OD1  A ASP   B 1 14  ? 28.587 -25.418 -18.853 0.78 30.44 ?  14  ASP   B OD1  1 
ATOM   4145 O  OD1  B ASP   B 1 14  ? 28.752 -25.365 -19.084 0.22 26.96 ?  14  ASP   B OD1  1 
ATOM   4146 O  OD2  A ASP   B 1 14  ? 26.978 -24.140 -18.081 0.78 30.74 -1 14  ASP   B OD2  1 
ATOM   4147 O  OD2  B ASP   B 1 14  ? 26.976 -24.554 -18.081 0.22 26.93 -1 14  ASP   B OD2  1 
ATOM   4148 H  H    A ASP   B 1 14  ? 29.436 -25.872 -15.807 0.78 24.75 ?  14  ASP   B H    1 
ATOM   4149 H  H    B ASP   B 1 14  ? 29.442 -25.855 -15.793 0.22 24.62 ?  14  ASP   B H    1 
ATOM   4150 H  HA   A ASP   B 1 14  ? 30.716 -24.924 -17.847 0.78 26.59 ?  14  ASP   B HA   1 
ATOM   4151 H  HA   B ASP   B 1 14  ? 30.772 -24.929 -17.832 0.22 25.70 ?  14  ASP   B HA   1 
ATOM   4152 H  HB2  A ASP   B 1 14  ? 28.679 -23.799 -16.275 0.78 30.97 ?  14  ASP   B HB2  1 
ATOM   4153 H  HB2  B ASP   B 1 14  ? 28.628 -23.823 -16.394 0.22 28.74 ?  14  ASP   B HB2  1 
ATOM   4154 H  HB3  A ASP   B 1 14  ? 29.319 -22.962 -17.465 0.78 30.97 ?  14  ASP   B HB3  1 
ATOM   4155 H  HB3  B ASP   B 1 14  ? 29.289 -23.024 -17.598 0.22 28.74 ?  14  ASP   B HB3  1 
ATOM   4156 N  N    . ASN   B 1 15  ? 31.771 -23.712 -15.127 1.00 17.88 ?  15  ASN   B N    1 
ATOM   4157 C  CA   . ASN   B 1 15  ? 32.728 -22.789 -14.522 1.00 15.32 ?  15  ASN   B CA   1 
ATOM   4158 C  C    . ASN   B 1 15  ? 33.824 -23.443 -13.688 1.00 13.84 ?  15  ASN   B C    1 
ATOM   4159 O  O    . ASN   B 1 15  ? 34.672 -22.716 -13.160 1.00 14.40 ?  15  ASN   B O    1 
ATOM   4160 C  CB   . ASN   B 1 15  ? 32.007 -21.736 -13.662 1.00 15.24 ?  15  ASN   B CB   1 
ATOM   4161 C  CG   . ASN   B 1 15  ? 31.388 -22.332 -12.419 1.00 14.84 ?  15  ASN   B CG   1 
ATOM   4162 O  OD1  . ASN   B 1 15  ? 30.447 -23.127 -12.506 1.00 16.53 ?  15  ASN   B OD1  1 
ATOM   4163 N  ND2  . ASN   B 1 15  ? 31.911 -21.973 -11.258 1.00 14.49 ?  15  ASN   B ND2  1 
ATOM   4164 H  H    A ASN   B 1 15  ? 31.389 -24.241 -14.565 0.78 21.51 ?  15  ASN   B H    1 
ATOM   4165 H  H    B ASN   B 1 15  ? 31.436 -24.282 -14.576 0.22 21.51 ?  15  ASN   B H    1 
ATOM   4166 H  HA   . ASN   B 1 15  ? 33.176 -22.307 -15.227 1.00 18.44 ?  15  ASN   B HA   1 
ATOM   4167 H  HB2  . ASN   B 1 15  ? 32.649 -21.056 -13.387 1.00 18.35 ?  15  ASN   B HB2  1 
ATOM   4168 H  HB3  . ASN   B 1 15  ? 31.299 -21.325 -14.183 1.00 18.35 ?  15  ASN   B HB3  1 
ATOM   4169 H  HD21 . ASN   B 1 15  ? 31.594 -22.285 -10.522 1.00 17.44 ?  15  ASN   B HD21 1 
ATOM   4170 H  HD22 . ASN   B 1 15  ? 32.576 -21.419 -11.231 1.00 17.44 ?  15  ASN   B HD22 1 
ATOM   4171 N  N    . VAL   B 1 16  ? 33.839 -24.768 -13.544 1.00 13.81 ?  16  VAL   B N    1 
ATOM   4172 C  CA   . VAL   B 1 16  ? 34.837 -25.462 -12.738 1.00 13.81 ?  16  VAL   B CA   1 
ATOM   4173 C  C    . VAL   B 1 16  ? 35.632 -26.401 -13.631 1.00 13.89 ?  16  VAL   B C    1 
ATOM   4174 O  O    . VAL   B 1 16  ? 35.057 -27.277 -14.293 1.00 14.83 ?  16  VAL   B O    1 
ATOM   4175 C  CB   . VAL   B 1 16  ? 34.209 -26.226 -11.560 1.00 13.99 ?  16  VAL   B CB   1 
ATOM   4176 C  CG1  . VAL   B 1 16  ? 35.294 -26.955 -10.771 1.00 13.96 ?  16  VAL   B CG1  1 
ATOM   4177 C  CG2  . VAL   B 1 16  ? 33.410 -25.279 -10.665 1.00 14.53 ?  16  VAL   B CG2  1 
ATOM   4178 H  H    . VAL   B 1 16  ? 33.260 -25.296 -13.907 1.00 16.63 ?  16  VAL   B H    1 
ATOM   4179 H  HA   . VAL   B 1 16  ? 35.452 -24.807 -12.368 1.00 16.63 ?  16  VAL   B HA   1 
ATOM   4180 H  HB   . VAL   B 1 16  ? 33.598 -26.895 -11.910 1.00 16.85 ?  16  VAL   B HB   1 
ATOM   4181 H  HG11 . VAL   B 1 16  ? 34.923 -27.245 -9.924  1.00 16.80 ?  16  VAL   B HG11 1 
ATOM   4182 H  HG12 . VAL   B 1 16  ? 35.600 -27.719 -11.279 1.00 16.80 ?  16  VAL   B HG12 1 
ATOM   4183 H  HG13 . VAL   B 1 16  ? 36.031 -26.341 -10.615 1.00 16.80 ?  16  VAL   B HG13 1 
ATOM   4184 H  HG21 . VAL   B 1 16  ? 33.071 -25.779 -9.907  1.00 17.49 ?  16  VAL   B HG21 1 
ATOM   4185 H  HG22 . VAL   B 1 16  ? 33.993 -24.569 -10.363 1.00 17.49 ?  16  VAL   B HG22 1 
ATOM   4186 H  HG23 . VAL   B 1 16  ? 32.674 -24.912 -11.178 1.00 17.49 ?  16  VAL   B HG23 1 
ATOM   4187 N  N    . TYR   B 1 17  ? 36.955 -26.236 -13.605 1.00 13.96 ?  17  TYR   B N    1 
ATOM   4188 C  CA   . TYR   B 1 17  ? 37.900 -26.983 -14.419 1.00 14.23 ?  17  TYR   B CA   1 
ATOM   4189 C  C    . TYR   B 1 17  ? 38.951 -27.592 -13.504 1.00 13.66 ?  17  TYR   B C    1 
ATOM   4190 O  O    . TYR   B 1 17  ? 39.228 -27.065 -12.422 1.00 13.81 ?  17  TYR   B O    1 
ATOM   4191 C  CB   . TYR   B 1 17  ? 38.601 -26.057 -15.422 1.00 16.79 ?  17  TYR   B CB   1 
ATOM   4192 C  CG   . TYR   B 1 17  ? 37.671 -25.286 -16.325 1.00 20.17 ?  17  TYR   B CG   1 
ATOM   4193 C  CD1  . TYR   B 1 17  ? 37.090 -24.092 -15.912 1.00 21.60 ?  17  TYR   B CD1  1 
ATOM   4194 C  CD2  . TYR   B 1 17  ? 37.375 -25.752 -17.598 1.00 22.37 ?  17  TYR   B CD2  1 
ATOM   4195 C  CE1  . TYR   B 1 17  ? 36.237 -23.385 -16.744 1.00 23.06 ?  17  TYR   B CE1  1 
ATOM   4196 C  CE2  . TYR   B 1 17  ? 36.527 -25.054 -18.436 1.00 23.90 ?  17  TYR   B CE2  1 
ATOM   4197 C  CZ   . TYR   B 1 17  ? 35.957 -23.874 -18.004 1.00 24.47 ?  17  TYR   B CZ   1 
ATOM   4198 O  OH   . TYR   B 1 17  ? 35.115 -23.180 -18.839 1.00 25.87 ?  17  TYR   B OH   1 
ATOM   4199 H  H    . TYR   B 1 17  ? 37.349 -25.656 -13.102 1.00 16.81 ?  17  TYR   B H    1 
ATOM   4200 H  HA   . TYR   B 1 17  ? 37.441 -27.694 -14.903 1.00 17.13 ?  17  TYR   B HA   1 
ATOM   4201 H  HB2  . TYR   B 1 17  ? 39.141 -25.418 -14.935 1.00 20.20 ?  17  TYR   B HB2  1 
ATOM   4202 H  HB3  . TYR   B 1 17  ? 39.164 -26.597 -15.993 1.00 20.20 ?  17  TYR   B HB3  1 
ATOM   4203 H  HD1  . TYR   B 1 17  ? 37.277 -23.763 -15.063 1.00 25.97 ?  17  TYR   B HD1  1 
ATOM   4204 H  HD2  . TYR   B 1 17  ? 37.751 -26.547 -17.896 1.00 26.90 ?  17  TYR   B HD2  1 
ATOM   4205 H  HE1  . TYR   B 1 17  ? 35.854 -22.587 -16.456 1.00 27.73 ?  17  TYR   B HE1  1 
ATOM   4206 H  HE2  . TYR   B 1 17  ? 36.334 -25.380 -19.287 1.00 28.74 ?  17  TYR   B HE2  1 
ATOM   4207 H  HH   . TYR   B 1 17  ? 35.031 -23.582 -19.572 1.00 31.10 ?  17  TYR   B HH   1 
ATOM   4208 N  N    . ILE   B 1 18  ? 39.564 -28.692 -13.940 1.00 13.81 ?  18  ILE   B N    1 
ATOM   4209 C  CA   . ILE   B 1 18  ? 40.495 -29.410 -13.078 1.00 13.82 ?  18  ILE   B CA   1 
ATOM   4210 C  C    . ILE   B 1 18  ? 41.653 -29.956 -13.901 1.00 14.09 ?  18  ILE   B C    1 
ATOM   4211 O  O    . ILE   B 1 18  ? 41.486 -30.355 -15.059 1.00 15.31 ?  18  ILE   B O    1 
ATOM   4212 C  CB   . ILE   B 1 18  ? 39.753 -30.512 -12.276 1.00 14.24 ?  18  ILE   B CB   1 
ATOM   4213 C  CG1  . ILE   B 1 18  ? 40.615 -31.035 -11.124 1.00 14.57 ?  18  ILE   B CG1  1 
ATOM   4214 C  CG2  . ILE   B 1 18  ? 39.267 -31.637 -13.199 1.00 14.51 ?  18  ILE   B CG2  1 
ATOM   4215 C  CD1  . ILE   B 1 18  ? 39.815 -31.854 -10.117 1.00 16.05 ?  18  ILE   B CD1  1 
ATOM   4216 H  H    . ILE   B 1 18  ? 39.457 -29.043 -14.718 1.00 16.63 ?  18  ILE   B H    1 
ATOM   4217 H  HA   . ILE   B 1 18  ? 40.857 -28.792 -12.429 1.00 16.64 ?  18  ILE   B HA   1 
ATOM   4218 H  HB   . ILE   B 1 18  ? 38.965 -30.110 -11.878 1.00 17.14 ?  18  ILE   B HB   1 
ATOM   4219 H  HG12 . ILE   B 1 18  ? 41.314 -31.600 -11.480 1.00 17.54 ?  18  ILE   B HG12 1 
ATOM   4220 H  HG13 . ILE   B 1 18  ? 41.001 -30.280 -10.652 1.00 17.54 ?  18  ILE   B HG13 1 
ATOM   4221 H  HG21 . ILE   B 1 18  ? 38.674 -32.222 -12.699 1.00 17.47 ?  18  ILE   B HG21 1 
ATOM   4222 H  HG22 . ILE   B 1 18  ? 38.789 -31.242 -13.943 1.00 17.47 ?  18  ILE   B HG22 1 
ATOM   4223 H  HG23 . ILE   B 1 18  ? 40.032 -32.136 -13.519 1.00 17.47 ?  18  ILE   B HG23 1 
ATOM   4224 H  HD11 . ILE   B 1 18  ? 40.400 -32.119 -9.388  1.00 19.31 ?  18  ILE   B HD11 1 
ATOM   4225 H  HD12 . ILE   B 1 18  ? 39.086 -31.313 -9.773  1.00 19.31 ?  18  ILE   B HD12 1 
ATOM   4226 H  HD13 . ILE   B 1 18  ? 39.461 -32.642 -10.558 1.00 19.31 ?  18  ILE   B HD13 1 
ATOM   4227 N  N    . LYS   B 1 19  ? 42.833 -29.998 -13.278 1.00 14.67 ?  19  LYS   B N    1 
ATOM   4228 C  CA   . LYS   B 1 19  ? 44.043 -30.471 -13.931 1.00 15.44 ?  19  LYS   B CA   1 
ATOM   4229 C  C    . LYS   B 1 19  ? 44.943 -31.145 -12.907 1.00 15.28 ?  19  LYS   B C    1 
ATOM   4230 O  O    . LYS   B 1 19  ? 45.022 -30.714 -11.755 1.00 14.51 ?  19  LYS   B O    1 
ATOM   4231 C  CB   . LYS   B 1 19  ? 44.806 -29.304 -14.573 1.00 17.01 ?  19  LYS   B CB   1 
ATOM   4232 C  CG   . LYS   B 1 19  ? 46.024 -29.703 -15.390 1.00 18.94 ?  19  LYS   B CG   1 
ATOM   4233 C  CD   . LYS   B 1 19  ? 46.739 -28.461 -15.913 1.00 20.59 ?  19  LYS   B CD   1 
ATOM   4234 C  CE   . LYS   B 1 19  ? 47.891 -28.819 -16.830 1.00 22.66 ?  19  LYS   B CE   1 
ATOM   4235 N  NZ   . LYS   B 1 19  ? 48.612 -27.613 -17.315 1.00 23.51 ?  19  LYS   B NZ   1 
ATOM   4236 H  H    . LYS   B 1 19  ? 42.949 -29.747 -12.456 1.00 17.66 ?  19  LYS   B H    1 
ATOM   4237 H  HA   . LYS   B 1 19  ? 43.808 -31.112 -14.618 1.00 18.58 ?  19  LYS   B HA   1 
ATOM   4238 H  HB2  . LYS   B 1 19  ? 44.199 -28.832 -15.164 1.00 20.47 ?  19  LYS   B HB2  1 
ATOM   4239 H  HB3  . LYS   B 1 19  ? 45.102 -28.704 -13.867 1.00 20.47 ?  19  LYS   B HB3  1 
ATOM   4240 H  HG2  . LYS   B 1 19  ? 46.636 -30.204 -14.831 1.00 22.79 ?  19  LYS   B HG2  1 
ATOM   4241 H  HG3  . LYS   B 1 19  ? 45.736 -30.240 -16.146 1.00 22.79 ?  19  LYS   B HG3  1 
ATOM   4242 H  HD2  . LYS   B 1 19  ? 46.108 -27.918 -16.412 1.00 24.76 ?  19  LYS   B HD2  1 
ATOM   4243 H  HD3  . LYS   B 1 19  ? 47.091 -27.959 -15.161 1.00 24.76 ?  19  LYS   B HD3  1 
ATOM   4244 H  HE2  . LYS   B 1 19  ? 48.520 -29.378 -16.345 1.00 27.25 ?  19  LYS   B HE2  1 
ATOM   4245 H  HE3  . LYS   B 1 19  ? 47.545 -29.300 -17.600 1.00 27.25 ?  19  LYS   B HE3  1 
ATOM   4246 H  HZ1  . LYS   B 1 19  ? 49.233 -27.850 -17.908 1.00 28.27 ?  19  LYS   B HZ1  1 
ATOM   4247 H  HZ2  . LYS   B 1 19  ? 48.040 -27.054 -17.705 1.00 28.27 ?  19  LYS   B HZ2  1 
ATOM   4248 H  HZ3  . LYS   B 1 19  ? 49.005 -27.199 -16.634 1.00 28.27 ?  19  LYS   B HZ3  1 
ATOM   4249 N  N    . ASN   B 1 20  ? 45.635 -32.193 -13.343 1.00 16.41 ?  20  ASN   B N    1 
ATOM   4250 C  CA   . ASN   B 1 20  ? 46.666 -32.830 -12.531 1.00 17.22 ?  20  ASN   B CA   1 
ATOM   4251 C  C    . ASN   B 1 20  ? 47.938 -32.010 -12.716 1.00 17.73 ?  20  ASN   B C    1 
ATOM   4252 O  O    . ASN   B 1 20  ? 48.592 -32.086 -13.761 1.00 19.55 ?  20  ASN   B O    1 
ATOM   4253 C  CB   . ASN   B 1 20  ? 46.838 -34.280 -12.975 1.00 18.83 ?  20  ASN   B CB   1 
ATOM   4254 C  CG   . ASN   B 1 20  ? 47.996 -34.988 -12.296 1.00 20.38 ?  20  ASN   B CG   1 
ATOM   4255 O  OD1  . ASN   B 1 20  ? 48.664 -35.829 -12.907 1.00 22.82 ?  20  ASN   B OD1  1 
ATOM   4256 N  ND2  . ASN   B 1 20  ? 48.231 -34.674 -11.032 1.00 19.85 ?  20  ASN   B ND2  1 
ATOM   4257 H  H    . ASN   B 1 20  ? 45.525 -32.556 -14.113 1.00 19.74 ?  20  ASN   B H    1 
ATOM   4258 H  HA   . ASN   B 1 20  ? 46.398 -32.813 -11.596 1.00 20.72 ?  20  ASN   B HA   1 
ATOM   4259 H  HB2  . ASN   B 1 20  ? 46.028 -34.770 -12.763 1.00 22.65 ?  20  ASN   B HB2  1 
ATOM   4260 H  HB3  . ASN   B 1 20  ? 46.992 -34.292 -13.931 1.00 22.65 ?  20  ASN   B HB3  1 
ATOM   4261 H  HD21 . ASN   B 1 20  ? 48.882 -35.043 -10.614 1.00 23.87 ?  20  ASN   B HD21 1 
ATOM   4262 H  HD22 . ASN   B 1 20  ? 47.740 -34.090 -10.629 1.00 23.87 ?  20  ASN   B HD22 1 
ATOM   4263 N  N    . ALA   B 1 21  ? 48.290 -31.207 -11.708 1.00 17.23 ?  21  ALA   B N    1 
ATOM   4264 C  CA   . ALA   B 1 21  ? 49.407 -30.287 -11.849 1.00 17.86 ?  21  ALA   B CA   1 
ATOM   4265 C  C    . ALA   B 1 21  ? 49.863 -29.789 -10.485 1.00 16.79 ?  21  ALA   B C    1 
ATOM   4266 O  O    . ALA   B 1 21  ? 49.114 -29.811 -9.502  1.00 16.72 ?  21  ALA   B O    1 
ATOM   4267 C  CB   . ALA   B 1 21  ? 49.033 -29.105 -12.743 1.00 19.18 ?  21  ALA   B CB   1 
ATOM   4268 H  H    . ALA   B 1 21  ? 47.899 -31.186 -10.940 1.00 20.74 ?  21  ALA   B H    1 
ATOM   4269 H  HA   . ALA   B 1 21  ? 50.148 -30.760 -12.261 1.00 21.49 ?  21  ALA   B HA   1 
ATOM   4270 H  HB1  . ALA   B 1 21  ? 49.822 -28.563 -12.874 1.00 23.07 ?  21  ALA   B HB1  1 
ATOM   4271 H  HB2  . ALA   B 1 21  ? 48.718 -29.449 -13.592 1.00 23.07 ?  21  ALA   B HB2  1 
ATOM   4272 H  HB3  . ALA   B 1 21  ? 48.335 -28.594 -12.309 1.00 23.07 ?  21  ALA   B HB3  1 
ATOM   4273 N  N    . ASP   B 1 22  ? 51.122 -29.350 -10.461 1.00 15.97 ?  22  ASP   B N    1 
ATOM   4274 C  CA   . ASP   B 1 22  ? 51.736 -28.647 -9.339  1.00 15.53 ?  22  ASP   B CA   1 
ATOM   4275 C  C    . ASP   B 1 22  ? 51.327 -27.178 -9.429  1.00 14.24 ?  22  ASP   B C    1 
ATOM   4276 O  O    . ASP   B 1 22  ? 51.633 -26.511 -10.421 1.00 14.49 ?  22  ASP   B O    1 
ATOM   4277 C  CB   . ASP   B 1 22  ? 53.253 -28.818 -9.502  1.00 17.04 ?  22  ASP   B CB   1 
ATOM   4278 C  CG   . ASP   B 1 22  ? 54.082 -28.060 -8.471  1.00 18.69 ?  22  ASP   B CG   1 
ATOM   4279 O  OD1  . ASP   B 1 22  ? 53.702 -26.952 -8.054  1.00 18.79 ?  22  ASP   B OD1  1 
ATOM   4280 O  OD2  . ASP   B 1 22  ? 55.167 -28.567 -8.106  1.00 21.09 -1 22  ASP   B OD2  1 
ATOM   4281 H  H    . ASP   B 1 22  ? 51.668 -29.463 -11.119 1.00 19.22 ?  22  ASP   B H    1 
ATOM   4282 H  HA   . ASP   B 1 22  ? 51.449 -29.030 -8.491  1.00 18.69 ?  22  ASP   B HA   1 
ATOM   4283 H  HB2  . ASP   B 1 22  ? 53.478 -29.756 -9.430  1.00 20.51 ?  22  ASP   B HB2  1 
ATOM   4284 H  HB3  . ASP   B 1 22  ? 53.511 -28.481 -10.374 1.00 20.51 ?  22  ASP   B HB3  1 
ATOM   4285 N  N    . ILE   B 1 23  ? 50.617 -26.682 -8.410  1.00 13.43 ?  23  ILE   B N    1 
ATOM   4286 C  CA   . ILE   B 1 23  ? 50.022 -25.344 -8.484  1.00 12.56 ?  23  ILE   B CA   1 
ATOM   4287 C  C    . ILE   B 1 23  ? 51.076 -24.254 -8.622  1.00 12.34 ?  23  ILE   B C    1 
ATOM   4288 O  O    . ILE   B 1 23  ? 50.808 -23.207 -9.218  1.00 12.14 ?  23  ILE   B O    1 
ATOM   4289 C  CB   . ILE   B 1 23  ? 49.087 -25.098 -7.285  1.00 13.15 ?  23  ILE   B CB   1 
ATOM   4290 C  CG1  . ILE   B 1 23  ? 48.257 -23.829 -7.493  1.00 13.81 ?  23  ILE   B CG1  1 
ATOM   4291 C  CG2  . ILE   B 1 23  ? 49.862 -25.059 -5.984  1.00 14.27 ?  23  ILE   B CG2  1 
ATOM   4292 C  CD1  . ILE   B 1 23  ? 47.140 -23.663 -6.480  1.00 14.39 ?  23  ILE   B CD1  1 
ATOM   4293 H  H    . ILE   B 1 23  ? 50.473 -27.097 -7.671  1.00 16.18 ?  23  ILE   B H    1 
ATOM   4294 H  HA   . ILE   B 1 23  ? 49.475 -25.310 -9.283  1.00 15.13 ?  23  ILE   B HA   1 
ATOM   4295 H  HB   . ILE   B 1 23  ? 48.469 -25.845 -7.240  1.00 15.84 ?  23  ILE   B HB   1 
ATOM   4296 H  HG12 . ILE   B 1 23  ? 48.843 -23.055 -7.421  1.00 16.62 ?  23  ILE   B HG12 1 
ATOM   4297 H  HG13 . ILE   B 1 23  ? 47.859 -23.852 -8.380  1.00 16.62 ?  23  ILE   B HG13 1 
ATOM   4298 H  HG21 . ILE   B 1 23  ? 49.237 -25.052 -5.245  1.00 17.18 ?  23  ILE   B HG21 1 
ATOM   4299 H  HG22 . ILE   B 1 23  ? 50.430 -25.843 -5.932  1.00 17.18 ?  23  ILE   B HG22 1 
ATOM   4300 H  HG23 . ILE   B 1 23  ? 50.407 -24.255 -5.966  1.00 17.18 ?  23  ILE   B HG23 1 
ATOM   4301 H  HD11 . ILE   B 1 23  ? 46.614 -22.883 -6.717  1.00 17.33 ?  23  ILE   B HD11 1 
ATOM   4302 H  HD12 . ILE   B 1 23  ? 46.582 -24.457 -6.501  1.00 17.33 ?  23  ILE   B HD12 1 
ATOM   4303 H  HD13 . ILE   B 1 23  ? 47.526 -23.551 -5.601  1.00 17.33 ?  23  ILE   B HD13 1 
ATOM   4304 N  N    . VAL   B 1 24  ? 52.269 -24.457 -8.061  1.00 12.73 ?  24  VAL   B N    1 
ATOM   4305 C  CA   . VAL   B 1 24  ? 53.347 -23.479 -8.230  1.00 13.31 ?  24  VAL   B CA   1 
ATOM   4306 C  C    . VAL   B 1 24  ? 53.799 -23.433 -9.682  1.00 13.84 ?  24  VAL   B C    1 
ATOM   4307 O  O    . VAL   B 1 24  ? 53.945 -22.356 -10.276 1.00 14.13 ?  24  VAL   B O    1 
ATOM   4308 C  CB   . VAL   B 1 24  ? 54.526 -23.805 -7.291  1.00 14.19 ?  24  VAL   B CB   1 
ATOM   4309 C  CG1  . VAL   B 1 24  ? 55.736 -22.933 -7.629  1.00 14.94 ?  24  VAL   B CG1  1 
ATOM   4310 C  CG2  . VAL   B 1 24  ? 54.128 -23.619 -5.848  1.00 15.65 ?  24  VAL   B CG2  1 
ATOM   4311 H  H    . VAL   B 1 24  ? 52.476 -25.134 -7.580  1.00 15.33 ?  24  VAL   B H    1 
ATOM   4312 H  HA   . VAL   B 1 24  ? 53.019 -22.600 -7.993  1.00 16.03 ?  24  VAL   B HA   1 
ATOM   4313 H  HB   . VAL   B 1 24  ? 54.784 -24.733 -7.409  1.00 17.09 ?  24  VAL   B HB   1 
ATOM   4314 H  HG11 . VAL   B 1 24  ? 56.334 -22.914 -6.865  1.00 17.99 ?  24  VAL   B HG11 1 
ATOM   4315 H  HG12 . VAL   B 1 24  ? 56.193 -23.312 -8.394  1.00 17.99 ?  24  VAL   B HG12 1 
ATOM   4316 H  HG13 . VAL   B 1 24  ? 55.431 -22.035 -7.830  1.00 17.99 ?  24  VAL   B HG13 1 
ATOM   4317 H  HG21 . VAL   B 1 24  ? 54.859 -23.898 -5.277  1.00 18.84 ?  24  VAL   B HG21 1 
ATOM   4318 H  HG22 . VAL   B 1 24  ? 53.929 -22.681 -5.695  1.00 18.84 ?  24  VAL   B HG22 1 
ATOM   4319 H  HG23 . VAL   B 1 24  ? 53.340 -24.157 -5.665  1.00 18.84 ?  24  VAL   B HG23 1 
ATOM   4320 N  N    . GLU   B 1 25  ? 54.059 -24.606 -10.268 1.00 14.77 ?  25  GLU   B N    1 
ATOM   4321 C  CA   . GLU   B 1 25  ? 54.452 -24.648 -11.670 1.00 16.37 ?  25  GLU   B CA   1 
ATOM   4322 C  C    . GLU   B 1 25  ? 53.346 -24.103 -12.559 1.00 15.00 ?  25  GLU   B C    1 
ATOM   4323 O  O    . GLU   B 1 25  ? 53.614 -23.380 -13.527 1.00 15.83 ?  25  GLU   B O    1 
ATOM   4324 C  CB   . GLU   B 1 25  ? 54.837 -26.075 -12.062 1.00 20.75 ?  25  GLU   B CB   1 
ATOM   4325 C  CG   . GLU   B 1 25  ? 56.132 -26.533 -11.409 1.00 26.62 ?  25  GLU   B CG   1 
ATOM   4326 C  CD   . GLU   B 1 25  ? 57.243 -25.493 -11.485 1.00 31.77 ?  25  GLU   B CD   1 
ATOM   4327 O  OE1  . GLU   B 1 25  ? 57.652 -25.132 -12.609 1.00 34.18 ?  25  GLU   B OE1  1 
ATOM   4328 O  OE2  . GLU   B 1 25  ? 57.693 -25.017 -10.418 1.00 34.09 -1 25  GLU   B OE2  1 
ATOM   4329 H  H    . GLU   B 1 25  ? 54.011 -25.376 -9.879  1.00 17.77 ?  25  GLU   B H    1 
ATOM   4330 H  HA   . GLU   B 1 25  ? 55.215 -24.070 -11.795 1.00 19.70 ?  25  GLU   B HA   1 
ATOM   4331 H  HB2  . GLU   B 1 25  ? 54.132 -26.683 -11.782 1.00 24.96 ?  25  GLU   B HB2  1 
ATOM   4332 H  HB3  . GLU   B 1 25  ? 54.950 -26.120 -13.023 1.00 24.96 ?  25  GLU   B HB3  1 
ATOM   4333 H  HG2  . GLU   B 1 25  ? 55.974 -26.700 -10.472 1.00 32.00 ?  25  GLU   B HG2  1 
ATOM   4334 H  HG3  . GLU   B 1 25  ? 56.438 -27.340 -11.851 1.00 32.00 ?  25  GLU   B HG3  1 
ATOM   4335 N  N    . GLU   B 1 26  ? 52.092 -24.415 -12.228 1.00 14.30 ?  26  GLU   B N    1 
ATOM   4336 C  CA   . GLU   B 1 26  ? 50.969 -23.886 -12.993 1.00 14.58 ?  26  GLU   B CA   1 
ATOM   4337 C  C    . GLU   B 1 26  ? 50.919 -22.369 -12.907 1.00 13.76 ?  26  GLU   B C    1 
ATOM   4338 O  O    . GLU   B 1 26  ? 50.711 -21.687 -13.916 1.00 14.81 ?  26  GLU   B O    1 
ATOM   4339 C  CB   . GLU   B 1 26  ? 49.656 -24.474 -12.476 1.00 16.53 ?  26  GLU   B CB   1 
ATOM   4340 C  CG   . GLU   B 1 26  ? 49.211 -25.751 -13.162 1.00 20.20 ?  26  GLU   B CG   1 
ATOM   4341 C  CD   . GLU   B 1 26  ? 48.952 -25.582 -14.657 1.00 21.46 ?  26  GLU   B CD   1 
ATOM   4342 O  OE1  . GLU   B 1 26  ? 47.974 -24.917 -15.062 1.00 21.72 ?  26  GLU   B OE1  1 
ATOM   4343 O  OE2  . GLU   B 1 26  ? 49.732 -26.145 -15.434 1.00 23.91 -1 26  GLU   B OE2  1 
ATOM   4344 H  H    . GLU   B 1 26  ? 51.865 -24.934 -11.575 1.00 17.22 ?  26  GLU   B H    1 
ATOM   4345 H  HA   . GLU   B 1 26  ? 51.070 -24.132 -13.923 1.00 17.56 ?  26  GLU   B HA   1 
ATOM   4346 H  HB2  . GLU   B 1 26  ? 49.750 -24.670 -11.531 1.00 19.90 ?  26  GLU   B HB2  1 
ATOM   4347 H  HB3  . GLU   B 1 26  ? 48.950 -23.817 -12.601 1.00 19.90 ?  26  GLU   B HB3  1 
ATOM   4348 H  HG2  . GLU   B 1 26  ? 49.908 -26.411 -13.054 1.00 24.29 ?  26  GLU   B HG2  1 
ATOM   4349 H  HG3  . GLU   B 1 26  ? 48.388 -26.057 -12.753 1.00 24.29 ?  26  GLU   B HG3  1 
ATOM   4350 N  N    . ALA   B 1 27  ? 51.073 -21.823 -11.700 1.00 12.81 ?  27  ALA   B N    1 
ATOM   4351 C  CA   . ALA   B 1 27  ? 51.029 -20.375 -11.552 1.00 13.10 ?  27  ALA   B CA   1 
ATOM   4352 C  C    . ALA   B 1 27  ? 52.097 -19.709 -12.410 1.00 14.29 ?  27  ALA   B C    1 
ATOM   4353 O  O    . ALA   B 1 27  ? 51.834 -18.703 -13.088 1.00 14.90 ?  27  ALA   B O    1 
ATOM   4354 C  CB   . ALA   B 1 27  ? 51.181 -19.989 -10.079 1.00 13.20 ?  27  ALA   B CB   1 
ATOM   4355 H  H    . ALA   B 1 27  ? 51.192 -22.261 -10.966 1.00 15.43 ?  27  ALA   B H    1 
ATOM   4356 H  HA   . ALA   B 1 27  ? 50.170 -20.050 -11.850 1.00 15.78 ?  27  ALA   B HA   1 
ATOM   4357 H  HB1  . ALA   B 1 27  ? 51.145 -19.022 -9.998  1.00 15.89 ?  27  ALA   B HB1  1 
ATOM   4358 H  HB2  . ALA   B 1 27  ? 50.452 -20.387 -9.573  1.00 15.89 ?  27  ALA   B HB2  1 
ATOM   4359 H  HB3  . ALA   B 1 27  ? 52.030 -20.318 -9.748  1.00 15.89 ?  27  ALA   B HB3  1 
ATOM   4360 N  N    . LYS   B 1 28  ? 53.312 -20.262 -12.405 1.00 15.72 ?  28  LYS   B N    1 
ATOM   4361 C  CA   . LYS   B 1 28  ? 54.388 -19.641 -13.168 1.00 17.87 ?  28  LYS   B CA   1 
ATOM   4362 C  C    . LYS   B 1 28  ? 54.130 -19.714 -14.668 1.00 18.55 ?  28  LYS   B C    1 
ATOM   4363 O  O    . LYS   B 1 28  ? 54.543 -18.814 -15.409 1.00 19.71 ?  28  LYS   B O    1 
ATOM   4364 C  CB   . LYS   B 1 28  ? 55.737 -20.252 -12.780 1.00 21.09 ?  28  LYS   B CB   1 
ATOM   4365 C  CG   . LYS   B 1 28  ? 56.156 -19.883 -11.360 1.00 24.08 ?  28  LYS   B CG   1 
ATOM   4366 C  CD   . LYS   B 1 28  ? 57.578 -20.308 -11.034 1.00 28.85 ?  28  LYS   B CD   1 
ATOM   4367 C  CE   . LYS   B 1 28  ? 57.658 -21.778 -10.700 1.00 33.00 ?  28  LYS   B CE   1 
ATOM   4368 N  NZ   . LYS   B 1 28  ? 59.012 -22.148 -10.201 1.00 34.98 ?  28  LYS   B NZ   1 
ATOM   4369 H  H    . LYS   B 1 28  ? 53.531 -20.978 -11.981 1.00 18.93 ?  28  LYS   B H    1 
ATOM   4370 H  HA   . LYS   B 1 28  ? 54.421 -18.703 -12.932 1.00 21.50 ?  28  LYS   B HA   1 
ATOM   4371 H  HB2  . LYS   B 1 28  ? 55.680 -21.217 -12.831 1.00 25.36 ?  28  LYS   B HB2  1 
ATOM   4372 H  HB3  . LYS   B 1 28  ? 56.420 -19.923 -13.385 1.00 25.36 ?  28  LYS   B HB3  1 
ATOM   4373 H  HG2  . LYS   B 1 28  ? 56.097 -18.918 -11.256 1.00 28.96 ?  28  LYS   B HG2  1 
ATOM   4374 H  HG3  . LYS   B 1 28  ? 55.558 -20.319 -10.733 1.00 28.96 ?  28  LYS   B HG3  1 
ATOM   4375 H  HD2  . LYS   B 1 28  ? 58.144 -20.137 -11.803 1.00 34.68 ?  28  LYS   B HD2  1 
ATOM   4376 H  HD3  . LYS   B 1 28  ? 57.892 -19.802 -10.268 1.00 34.68 ?  28  LYS   B HD3  1 
ATOM   4377 H  HE2  . LYS   B 1 28  ? 57.011 -21.984 -10.008 1.00 39.66 ?  28  LYS   B HE2  1 
ATOM   4378 H  HE3  . LYS   B 1 28  ? 57.474 -22.299 -11.497 1.00 39.66 ?  28  LYS   B HE3  1 
ATOM   4379 H  HZ1  . LYS   B 1 28  ? 59.039 -23.016 -10.010 1.00 42.03 ?  28  LYS   B HZ1  1 
ATOM   4380 H  HZ2  . LYS   B 1 28  ? 59.624 -21.968 -10.822 1.00 42.03 ?  28  LYS   B HZ2  1 
ATOM   4381 H  HZ3  . LYS   B 1 28  ? 59.202 -21.683 -9.466  1.00 42.03 ?  28  LYS   B HZ3  1 
ATOM   4382 N  N    . LYS   B 1 29  ? 53.429 -20.752 -15.128 1.00 19.58 ?  29  LYS   B N    1 
ATOM   4383 C  CA   . LYS   B 1 29  ? 53.134 -20.891 -16.552 1.00 22.48 ?  29  LYS   B CA   1 
ATOM   4384 C  C    . LYS   B 1 29  ? 51.889 -20.112 -16.966 1.00 21.32 ?  29  LYS   B C    1 
ATOM   4385 O  O    . LYS   B 1 29  ? 51.876 -19.487 -18.032 1.00 22.52 ?  29  LYS   B O    1 
ATOM   4386 C  CB   . LYS   B 1 29  ? 52.960 -22.368 -16.906 1.00 27.53 ?  29  LYS   B CB   1 
ATOM   4387 C  CG   . LYS   B 1 29  ? 52.859 -22.644 -18.399 1.00 32.16 ?  29  LYS   B CG   1 
ATOM   4388 C  CD   . LYS   B 1 29  ? 53.128 -24.109 -18.723 1.00 35.78 ?  29  LYS   B CD   1 
ATOM   4389 C  CE   . LYS   B 1 29  ? 52.048 -25.024 -18.166 1.00 38.53 ?  29  LYS   B CE   1 
ATOM   4390 N  NZ   . LYS   B 1 29  ? 52.320 -26.455 -18.484 1.00 39.94 ?  29  LYS   B NZ   1 
ATOM   4391 H  H    . LYS   B 1 29  ? 53.128 -21.391 -14.634 1.00 23.55 ?  29  LYS   B H    1 
ATOM   4392 H  HA   . LYS   B 1 29  ? 53.882 -20.546 -17.058 1.00 27.03 ?  29  LYS   B HA   1 
ATOM   4393 H  HB2  . LYS   B 1 29  ? 53.723 -22.860 -16.567 1.00 33.09 ?  29  LYS   B HB2  1 
ATOM   4394 H  HB3  . LYS   B 1 29  ? 52.147 -22.695 -16.491 1.00 33.09 ?  29  LYS   B HB3  1 
ATOM   4395 H  HG2  . LYS   B 1 29  ? 51.965 -22.425 -18.705 1.00 38.65 ?  29  LYS   B HG2  1 
ATOM   4396 H  HG3  . LYS   B 1 29  ? 53.514 -22.104 -18.870 1.00 38.65 ?  29  LYS   B HG3  1 
ATOM   4397 H  HD2  . LYS   B 1 29  ? 53.155 -24.224 -19.686 1.00 42.99 ?  29  LYS   B HD2  1 
ATOM   4398 H  HD3  . LYS   B 1 29  ? 53.977 -24.372 -18.332 1.00 42.99 ?  29  LYS   B HD3  1 
ATOM   4399 H  HE2  . LYS   B 1 29  ? 52.014 -24.930 -17.201 1.00 46.29 ?  29  LYS   B HE2  1 
ATOM   4400 H  HE3  . LYS   B 1 29  ? 51.193 -24.784 -18.557 1.00 46.29 ?  29  LYS   B HE3  1 
ATOM   4401 H  HZ1  . LYS   B 1 29  ? 51.676 -26.970 -18.149 1.00 47.99 ?  29  LYS   B HZ1  1 
ATOM   4402 H  HZ2  . LYS   B 1 29  ? 52.353 -26.571 -19.366 1.00 47.99 ?  29  LYS   B HZ2  1 
ATOM   4403 H  HZ3  . LYS   B 1 29  ? 53.100 -26.702 -18.132 1.00 47.99 ?  29  LYS   B HZ3  1 
ATOM   4404 N  N    . VAL   B 1 30  ? 50.832 -20.157 -16.149 1.00 19.54 ?  30  VAL   B N    1 
ATOM   4405 C  CA   . VAL   B 1 30  ? 49.541 -19.569 -16.516 1.00 19.70 ?  30  VAL   B CA   1 
ATOM   4406 C  C    . VAL   B 1 30  ? 49.547 -18.054 -16.368 1.00 19.09 ?  30  VAL   B C    1 
ATOM   4407 O  O    . VAL   B 1 30  ? 48.808 -17.350 -17.073 1.00 20.06 ?  30  VAL   B O    1 
ATOM   4408 C  CB   . VAL   B 1 30  ? 48.432 -20.184 -15.639 1.00 20.30 ?  30  VAL   B CB   1 
ATOM   4409 C  CG1  . VAL   B 1 30  ? 47.142 -19.370 -15.723 1.00 20.24 ?  30  VAL   B CG1  1 
ATOM   4410 C  CG2  . VAL   B 1 30  ? 48.184 -21.636 -16.025 1.00 21.16 ?  30  VAL   B CG2  1 
ATOM   4411 H  H    . VAL   B 1 30  ? 50.832 -20.540 -15.371 1.00 23.50 ?  30  VAL   B H    1 
ATOM   4412 H  HA   . VAL   B 1 30  ? 49.342 -19.799 -17.440 1.00 23.69 ?  30  VAL   B HA   1 
ATOM   4413 H  HB   . VAL   B 1 30  ? 48.720 -20.176 -14.711 1.00 24.41 ?  30  VAL   B HB   1 
ATOM   4414 H  HG11 . VAL   B 1 30  ? 46.397 -19.944 -15.478 1.00 24.35 ?  30  VAL   B HG11 1 
ATOM   4415 H  HG12 . VAL   B 1 30  ? 47.192 -18.623 -15.108 1.00 24.35 ?  30  VAL   B HG12 1 
ATOM   4416 H  HG13 . VAL   B 1 30  ? 47.021 -19.058 -16.630 1.00 24.35 ?  30  VAL   B HG13 1 
ATOM   4417 H  HG21 . VAL   B 1 30  ? 47.490 -22.006 -15.449 1.00 25.45 ?  30  VAL   B HG21 1 
ATOM   4418 H  HG22 . VAL   B 1 30  ? 47.891 -21.672 -16.950 1.00 25.45 ?  30  VAL   B HG22 1 
ATOM   4419 H  HG23 . VAL   B 1 30  ? 49.003 -22.138 -15.915 1.00 25.45 ?  30  VAL   B HG23 1 
ATOM   4420 N  N    . LYS   B 1 31  ? 50.324 -17.547 -15.426 1.00 18.63 ?  31  LYS   B N    1 
ATOM   4421 C  CA   . LYS   B 1 31  ? 50.355 -16.139 -15.061 1.00 19.07 ?  31  LYS   B CA   1 
ATOM   4422 C  C    . LYS   B 1 31  ? 48.952 -15.672 -14.677 1.00 16.84 ?  31  LYS   B C    1 
ATOM   4423 O  O    . LYS   B 1 31  ? 48.413 -14.744 -15.295 1.00 17.79 ?  31  LYS   B O    1 
ATOM   4424 C  CB   . LYS   B 1 31  ? 50.991 -15.320 -16.189 1.00 22.45 ?  31  LYS   B CB   1 
ATOM   4425 C  CG   . LYS   B 1 31  ? 52.414 -15.776 -16.524 1.00 25.83 ?  31  LYS   B CG   1 
ATOM   4426 C  CD   . LYS   B 1 31  ? 52.991 -15.001 -17.698 1.00 29.44 ?  31  LYS   B CD   1 
ATOM   4427 C  CE   . LYS   B 1 31  ? 54.468 -15.288 -17.892 1.00 32.47 ?  31  LYS   B CE   1 
ATOM   4428 N  NZ   . LYS   B 1 31  ? 55.228 -14.974 -16.654 1.00 33.99 ?  31  LYS   B NZ   1 
ATOM   4429 H  H    . LYS   B 1 31  ? 50.858 -18.035 -14.966 1.00 22.42 ?  31  LYS   B H    1 
ATOM   4430 H  HA   . LYS   B 1 31  ? 50.903 -16.057 -14.279 1.00 22.94 ?  31  LYS   B HA   1 
ATOM   4431 H  HB2  . LYS   B 1 31  ? 50.451 -15.409 -16.992 1.00 26.99 ?  31  LYS   B HB2  1 
ATOM   4432 H  HB3  . LYS   B 1 31  ? 51.028 -14.395 -15.913 1.00 26.99 ?  31  LYS   B HB3  1 
ATOM   4433 H  HG2  . LYS   B 1 31  ? 52.976 -15.636 -15.745 1.00 31.05 ?  31  LYS   B HG2  1 
ATOM   4434 H  HG3  . LYS   B 1 31  ? 52.399 -16.722 -16.756 1.00 31.05 ?  31  LYS   B HG3  1 
ATOM   4435 H  HD2  . LYS   B 1 31  ? 52.520 -15.258 -18.506 1.00 35.38 ?  31  LYS   B HD2  1 
ATOM   4436 H  HD3  . LYS   B 1 31  ? 52.882 -14.054 -17.532 1.00 35.38 ?  31  LYS   B HD3  1 
ATOM   4437 H  HE2  . LYS   B 1 31  ? 54.596 -16.229 -18.099 1.00 39.02 ?  31  LYS   B HE2  1 
ATOM   4438 H  HE3  . LYS   B 1 31  ? 54.814 -14.735 -18.612 1.00 39.02 ?  31  LYS   B HE3  1 
ATOM   4439 H  HZ1  . LYS   B 1 31  ? 56.102 -14.997 -16.818 1.00 40.84 ?  31  LYS   B HZ1  1 
ATOM   4440 H  HZ2  . LYS   B 1 31  ? 55.009 -14.162 -16.363 1.00 40.84 ?  31  LYS   B HZ2  1 
ATOM   4441 H  HZ3  . LYS   B 1 31  ? 55.036 -15.569 -16.020 1.00 40.84 ?  31  LYS   B HZ3  1 
ATOM   4442 N  N    . PRO   B 1 32  ? 48.335 -16.279 -13.654 1.00 14.31 ?  32  PRO   B N    1 
ATOM   4443 C  CA   . PRO   B 1 32  ? 46.955 -15.919 -13.304 1.00 13.17 ?  32  PRO   B CA   1 
ATOM   4444 C  C    . PRO   B 1 32  ? 46.870 -14.571 -12.607 1.00 13.14 ?  32  PRO   B C    1 
ATOM   4445 O  O    . PRO   B 1 32  ? 47.791 -14.143 -11.906 1.00 14.49 ?  32  PRO   B O    1 
ATOM   4446 C  CB   . PRO   B 1 32  ? 46.546 -17.037 -12.340 1.00 13.28 ?  32  PRO   B CB   1 
ATOM   4447 C  CG   . PRO   B 1 32  ? 47.832 -17.390 -11.656 1.00 13.89 ?  32  PRO   B CG   1 
ATOM   4448 C  CD   . PRO   B 1 32  ? 48.893 -17.276 -12.717 1.00 14.28 ?  32  PRO   B CD   1 
ATOM   4449 H  HA   . PRO   B 1 32  ? 46.381 -15.930 -14.085 1.00 15.85 ?  32  PRO   B HA   1 
ATOM   4450 H  HB2  . PRO   B 1 32  ? 45.890 -16.705 -11.704 1.00 16.00 ?  32  PRO   B HB2  1 
ATOM   4451 H  HB3  . PRO   B 1 32  ? 46.194 -17.792 -12.838 1.00 16.00 ?  32  PRO   B HB3  1 
ATOM   4452 H  HG2  . PRO   B 1 32  ? 48.002 -16.764 -10.933 1.00 16.73 ?  32  PRO   B HG2  1 
ATOM   4453 H  HG3  . PRO   B 1 32  ? 47.785 -18.298 -11.316 1.00 16.73 ?  32  PRO   B HG3  1 
ATOM   4454 H  HD2  . PRO   B 1 32  ? 49.720 -16.950 -12.328 1.00 17.19 ?  32  PRO   B HD2  1 
ATOM   4455 H  HD3  . PRO   B 1 32  ? 49.015 -18.127 -13.159 1.00 17.19 ?  32  PRO   B HD3  1 
ATOM   4456 N  N    . THR   B 1 33  ? 45.716 -13.920 -12.777 1.00 13.10 ?  33  THR   B N    1 
ATOM   4457 C  CA   . THR   B 1 33  ? 45.419 -12.742 -11.972 1.00 13.33 ?  33  THR   B CA   1 
ATOM   4458 C  C    . THR   B 1 33  ? 45.369 -13.093 -10.490 1.00 12.79 ?  33  THR   B C    1 
ATOM   4459 O  O    . THR   B 1 33  ? 45.838 -12.313 -9.648  1.00 13.90 ?  33  THR   B O    1 
ATOM   4460 C  CB   . THR   B 1 33  ? 44.099 -12.116 -12.426 1.00 13.93 ?  33  THR   B CB   1 
ATOM   4461 O  OG1  . THR   B 1 33  ? 44.152 -11.856 -13.832 1.00 14.00 ?  33  THR   B OG1  1 
ATOM   4462 C  CG2  . THR   B 1 33  ? 43.827 -10.819 -11.673 1.00 14.96 ?  33  THR   B CG2  1 
ATOM   4463 H  H    . THR   B 1 33  ? 45.095 -14.144 -13.335 1.00 15.77 ?  33  THR   B H    1 
ATOM   4464 H  HA   . THR   B 1 33  ? 46.116 -12.087 -12.100 1.00 16.06 ?  33  THR   B HA   1 
ATOM   4465 H  HB   . THR   B 1 33  ? 43.366 -12.731 -12.243 1.00 16.77 ?  33  THR   B HB   1 
ATOM   4466 H  HG1  . THR   B 1 33  ? 43.431 -11.497 -14.087 1.00 16.86 ?  33  THR   B HG1  1 
ATOM   4467 H  HG21 . THR   B 1 33  ? 43.076 -10.355 -12.070 1.00 18.00 ?  33  THR   B HG21 1 
ATOM   4468 H  HG22 . THR   B 1 33  ? 43.626 -11.009 -10.743 1.00 18.00 ?  33  THR   B HG22 1 
ATOM   4469 H  HG23 . THR   B 1 33  ? 44.610 -10.247 -11.715 1.00 18.00 ?  33  THR   B HG23 1 
ATOM   4470 N  N    . VAL   B 1 34  ? 44.822 -14.268 -10.153 1.00 12.16 ?  34  VAL   B N    1 
ATOM   4471 C  CA   . VAL   B 1 34  ? 44.629 -14.669 -8.762  1.00 11.50 ?  34  VAL   B CA   1 
ATOM   4472 C  C    . VAL   B 1 34  ? 45.063 -16.120 -8.600  1.00 10.74 ?  34  VAL   B C    1 
ATOM   4473 O  O    . VAL   B 1 34  ? 44.536 -17.011 -9.278  1.00 11.38 ?  34  VAL   B O    1 
ATOM   4474 C  CB   . VAL   B 1 34  ? 43.164 -14.532 -8.309  1.00 12.62 ?  34  VAL   B CB   1 
ATOM   4475 C  CG1  . VAL   B 1 34  ? 43.015 -14.985 -6.860  1.00 12.91 ?  34  VAL   B CG1  1 
ATOM   4476 C  CG2  . VAL   B 1 34  ? 42.654 -13.109 -8.499  1.00 13.58 ?  34  VAL   B CG2  1 
ATOM   4477 H  H    . VAL   B 1 34  ? 44.562 -14.860 -10.719 1.00 14.64 ?  34  VAL   B H    1 
ATOM   4478 H  HA   . VAL   B 1 34  ? 45.183 -14.117 -8.182  1.00 13.85 ?  34  VAL   B HA   1 
ATOM   4479 H  HB   . VAL   B 1 34  ? 42.618 -15.115 -8.857  1.00 15.20 ?  34  VAL   B HB   1 
ATOM   4480 H  HG11 . VAL   B 1 34  ? 42.163 -14.669 -6.516  1.00 15.55 ?  34  VAL   B HG11 1 
ATOM   4481 H  HG12 . VAL   B 1 34  ? 43.043 -15.955 -6.822  1.00 15.55 ?  34  VAL   B HG12 1 
ATOM   4482 H  HG13 . VAL   B 1 34  ? 43.739 -14.612 -6.332  1.00 15.55 ?  34  VAL   B HG13 1 
ATOM   4483 H  HG21 . VAL   B 1 34  ? 41.737 -13.059 -8.182  1.00 16.35 ?  34  VAL   B HG21 1 
ATOM   4484 H  HG22 . VAL   B 1 34  ? 43.213 -12.501 -7.996  1.00 16.35 ?  34  VAL   B HG22 1 
ATOM   4485 H  HG23 . VAL   B 1 34  ? 42.687 -12.886 -9.444  1.00 16.35 ?  34  VAL   B HG23 1 
ATOM   4486 N  N    . VAL   B 1 35  ? 45.978 -16.368 -7.668  1.00 10.37 ?  35  VAL   B N    1 
ATOM   4487 C  CA   . VAL   B 1 35  ? 46.216 -17.710 -7.145  1.00 10.10 ?  35  VAL   B CA   1 
ATOM   4488 C  C    . VAL   B 1 35  ? 45.678 -17.762 -5.724  1.00 9.69  ?  35  VAL   B C    1 
ATOM   4489 O  O    . VAL   B 1 35  ? 45.899 -16.836 -4.935  1.00 10.30 ?  35  VAL   B O    1 
ATOM   4490 C  CB   . VAL   B 1 35  ? 47.699 -18.127 -7.232  1.00 10.76 ?  35  VAL   B CB   1 
ATOM   4491 C  CG1  . VAL   B 1 35  ? 48.594 -17.282 -6.328  1.00 11.47 ?  35  VAL   B CG1  1 
ATOM   4492 C  CG2  . VAL   B 1 35  ? 47.852 -19.622 -6.905  1.00 11.33 ?  35  VAL   B CG2  1 
ATOM   4493 H  H    . VAL   B 1 35  ? 46.484 -15.767 -7.313  1.00 12.50 ?  35  VAL   B H    1 
ATOM   4494 H  HA   . VAL   B 1 35  ? 45.700 -18.342 -7.673  1.00 12.18 ?  35  VAL   B HA   1 
ATOM   4495 H  HB   . VAL   B 1 35  ? 48.000 -18.007 -8.146  1.00 12.97 ?  35  VAL   B HB   1 
ATOM   4496 H  HG11 . VAL   B 1 35  ? 49.518 -17.510 -6.505  1.00 13.82 ?  35  VAL   B HG11 1 
ATOM   4497 H  HG12 . VAL   B 1 35  ? 48.433 -16.350 -6.519  1.00 13.82 ?  35  VAL   B HG12 1 
ATOM   4498 H  HG13 . VAL   B 1 35  ? 48.375 -17.478 -5.403  1.00 13.82 ?  35  VAL   B HG13 1 
ATOM   4499 H  HG21 . VAL   B 1 35  ? 48.778 -19.883 -7.009  1.00 13.65 ?  35  VAL   B HG21 1 
ATOM   4500 H  HG22 . VAL   B 1 35  ? 47.568 -19.779 -5.986  1.00 13.65 ?  35  VAL   B HG22 1 
ATOM   4501 H  HG23 . VAL   B 1 35  ? 47.292 -20.144 -7.508  1.00 13.65 ?  35  VAL   B HG23 1 
ATOM   4502 N  N    . VAL   B 1 36  ? 44.953 -18.835 -5.405  1.00 9.72  ?  36  VAL   B N    1 
ATOM   4503 C  CA   . VAL   B 1 36  ? 44.412 -19.043 -4.072  1.00 9.55  ?  36  VAL   B CA   1 
ATOM   4504 C  C    . VAL   B 1 36  ? 45.423 -19.806 -3.225  1.00 9.28  ?  36  VAL   B C    1 
ATOM   4505 O  O    . VAL   B 1 36  ? 45.964 -20.840 -3.649  1.00 10.48 ?  36  VAL   B O    1 
ATOM   4506 C  CB   . VAL   B 1 36  ? 43.075 -19.799 -4.144  1.00 10.03 ?  36  VAL   B CB   1 
ATOM   4507 C  CG1  . VAL   B 1 36  ? 42.577 -20.162 -2.755  1.00 10.42 ?  36  VAL   B CG1  1 
ATOM   4508 C  CG2  . VAL   B 1 36  ? 42.044 -18.968 -4.890  1.00 10.41 ?  36  VAL   B CG2  1 
ATOM   4509 H  H    . VAL   B 1 36  ? 44.765 -19.471 -5.957  1.00 11.72 ?  36  VAL   B H    1 
ATOM   4510 H  HA   . VAL   B 1 36  ? 44.249 -18.183 -3.655  1.00 11.52 ?  36  VAL   B HA   1 
ATOM   4511 H  HB   . VAL   B 1 36  ? 43.206 -20.624 -4.639  1.00 12.10 ?  36  VAL   B HB   1 
ATOM   4512 H  HG11 . VAL   B 1 36  ? 41.639 -20.396 -2.812  1.00 12.56 ?  36  VAL   B HG11 1 
ATOM   4513 H  HG12 . VAL   B 1 36  ? 43.089 -20.908 -2.418  1.00 12.56 ?  36  VAL   B HG12 1 
ATOM   4514 H  HG13 . VAL   B 1 36  ? 42.687 -19.389 -2.175  1.00 12.56 ?  36  VAL   B HG13 1 
ATOM   4515 H  HG21 . VAL   B 1 36  ? 41.204 -19.444 -4.905  1.00 12.54 ?  36  VAL   B HG21 1 
ATOM   4516 H  HG22 . VAL   B 1 36  ? 41.941 -18.116 -4.437  1.00 12.54 ?  36  VAL   B HG22 1 
ATOM   4517 H  HG23 . VAL   B 1 36  ? 42.359 -18.819 -5.799  1.00 12.54 ?  36  VAL   B HG23 1 
ATOM   4518 N  N    . ASN   B 1 37  ? 45.649 -19.309 -2.011  1.00 9.69  ?  37  ASN   B N    1 
ATOM   4519 C  CA   . ASN   B 1 37  ? 46.403 -20.032 -1.001  1.00 10.05 ?  37  ASN   B CA   1 
ATOM   4520 C  C    . ASN   B 1 37  ? 45.455 -20.706 -0.017  1.00 9.87  ?  37  ASN   B C    1 
ATOM   4521 O  O    . ASN   B 1 37  ? 44.449 -20.127 0.403   1.00 10.57 ?  37  ASN   B O    1 
ATOM   4522 C  CB   . ASN   B 1 37  ? 47.330 -19.086 -0.238  1.00 10.01 ?  37  ASN   B CB   1 
ATOM   4523 C  CG   . ASN   B 1 37  ? 48.188 -19.805 0.772   1.00 10.25 ?  37  ASN   B CG   1 
ATOM   4524 O  OD1  . ASN   B 1 37  ? 48.529 -20.981 0.593   1.00 10.96 ?  37  ASN   B OD1  1 
ATOM   4525 N  ND2  . ASN   B 1 37  ? 48.542 -19.105 1.845   1.00 10.48 ?  37  ASN   B ND2  1 
ATOM   4526 H  H    . ASN   B 1 37  ? 45.372 -18.538 -1.739  1.00 11.68 ?  37  ASN   B H    1 
ATOM   4527 H  HA   . ASN   B 1 37  ? 46.942 -20.720 -1.421  1.00 12.12 ?  37  ASN   B HA   1 
ATOM   4528 H  HB2  . ASN   B 1 37  ? 47.919 -18.650 -0.871  1.00 12.07 ?  37  ASN   B HB2  1 
ATOM   4529 H  HB3  . ASN   B 1 37  ? 46.797 -18.430 0.234   1.00 12.07 ?  37  ASN   B HB3  1 
ATOM   4530 H  HD21 . ASN   B 1 37  ? 49.038 -19.466 2.450   1.00 12.63 ?  37  ASN   B HD21 1 
ATOM   4531 H  HD22 . ASN   B 1 37  ? 48.288 -18.294 1.935   1.00 12.63 ?  37  ASN   B HD22 1 
ATOM   4532 N  N    . ALA   B 1 38  ? 45.806 -21.940 0.358   1.00 10.08 ?  38  ALA   B N    1 
ATOM   4533 C  CA   . ALA   B 1 38  ? 45.153 -22.687 1.435   1.00 10.65 ?  38  ALA   B CA   1 
ATOM   4534 C  C    . ALA   B 1 38  ? 45.740 -22.203 2.760   1.00 10.55 ?  38  ALA   B C    1 
ATOM   4535 O  O    . ALA   B 1 38  ? 46.648 -22.808 3.342   1.00 11.28 ?  38  ALA   B O    1 
ATOM   4536 C  CB   . ALA   B 1 38  ? 45.372 -24.182 1.240   1.00 11.83 ?  38  ALA   B CB   1 
ATOM   4537 H  H    . ALA   B 1 38  ? 46.459 -22.374 0.004   1.00 12.15 ?  38  ALA   B H    1 
ATOM   4538 H  HA   . ALA   B 1 38  ? 44.200 -22.505 1.430   1.00 12.83 ?  38  ALA   B HA   1 
ATOM   4539 H  HB1  . ALA   B 1 38  ? 44.923 -24.664 1.960   1.00 14.25 ?  38  ALA   B HB1  1 
ATOM   4540 H  HB2  . ALA   B 1 38  ? 44.990 -24.448 0.387   1.00 14.25 ?  38  ALA   B HB2  1 
ATOM   4541 H  HB3  . ALA   B 1 38  ? 46.318 -24.372 1.257   1.00 14.25 ?  38  ALA   B HB3  1 
ATOM   4542 N  N    . ALA   B 1 39  ? 45.227 -21.060 3.220   1.00 10.55 ?  39  ALA   B N    1 
ATOM   4543 C  CA   . ALA   B 1 39  ? 45.771 -20.322 4.350   1.00 10.94 ?  39  ALA   B CA   1 
ATOM   4544 C  C    . ALA   B 1 39  ? 45.151 -20.765 5.674   1.00 10.90 ?  39  ALA   B C    1 
ATOM   4545 O  O    . ALA   B 1 39  ? 44.124 -21.443 5.723   1.00 11.79 ?  39  ALA   B O    1 
ATOM   4546 C  CB   . ALA   B 1 39  ? 45.534 -18.820 4.152   1.00 11.42 ?  39  ALA   B CB   1 
ATOM   4547 H  H    . ALA   B 1 39  ? 44.535 -20.684 2.872   1.00 12.72 ?  39  ALA   B H    1 
ATOM   4548 H  HA   . ALA   B 1 39  ? 46.724 -20.472 4.398   1.00 13.18 ?  39  ALA   B HA   1 
ATOM   4549 H  HB1  . ALA   B 1 39  ? 45.901 -18.341 4.911   1.00 13.76 ?  39  ALA   B HB1  1 
ATOM   4550 H  HB2  . ALA   B 1 39  ? 45.979 -18.536 3.336   1.00 13.76 ?  39  ALA   B HB2  1 
ATOM   4551 H  HB3  . ALA   B 1 39  ? 44.582 -18.654 4.084   1.00 13.76 ?  39  ALA   B HB3  1 
ATOM   4552 N  N    . ASN   B 1 40  ? 45.793 -20.339 6.761   1.00 11.62 ?  40  ASN   B N    1 
ATOM   4553 C  CA   . ASN   B 1 40  ? 45.233 -20.383 8.103   1.00 12.13 ?  40  ASN   B CA   1 
ATOM   4554 C  C    . ASN   B 1 40  ? 45.060 -18.954 8.627   1.00 11.99 ?  40  ASN   B C    1 
ATOM   4555 O  O    . ASN   B 1 40  ? 45.471 -17.974 7.994   1.00 11.92 ?  40  ASN   B O    1 
ATOM   4556 C  CB   . ASN   B 1 40  ? 46.083 -21.256 9.042   1.00 13.33 ?  40  ASN   B CB   1 
ATOM   4557 C  CG   . ASN   B 1 40  ? 47.539 -20.854 9.062   1.00 14.37 ?  40  ASN   B CG   1 
ATOM   4558 O  OD1  . ASN   B 1 40  ? 47.861 -19.675 9.115   1.00 16.08 ?  40  ASN   B OD1  1 
ATOM   4559 N  ND2  . ASN   B 1 40  ? 48.429 -21.833 9.026   1.00 14.25 ?  40  ASN   B ND2  1 
ATOM   4560 H  H    . ASN   B 1 40  ? 46.584 -20.008 6.736   1.00 14.00 ?  40  ASN   B H    1 
ATOM   4561 H  HA   . ASN   B 1 40  ? 44.350 -20.781 8.059   1.00 14.61 ?  40  ASN   B HA   1 
ATOM   4562 H  HB2  . ASN   B 1 40  ? 45.737 -21.177 9.944   1.00 16.05 ?  40  ASN   B HB2  1 
ATOM   4563 H  HB3  . ASN   B 1 40  ? 46.033 -22.177 8.745   1.00 16.05 ?  40  ASN   B HB3  1 
ATOM   4564 H  HD21 . ASN   B 1 40  ? 49.270 -21.655 9.038   1.00 17.16 ?  40  ASN   B HD21 1 
ATOM   4565 H  HD22 . ASN   B 1 40  ? 48.164 -22.651 8.988   1.00 17.16 ?  40  ASN   B HD22 1 
ATOM   4566 N  N    . VAL   B 1 41  ? 44.410 -18.827 9.786   1.00 12.33 ?  41  VAL   B N    1 
ATOM   4567 C  CA   . VAL   B 1 41  ? 43.953 -17.507 10.230  1.00 13.16 ?  41  VAL   B CA   1 
ATOM   4568 C  C    . VAL   B 1 41  ? 45.106 -16.558 10.532  1.00 12.99 ?  41  VAL   B C    1 
ATOM   4569 O  O    . VAL   B 1 41  ? 44.930 -15.339 10.452  1.00 13.03 ?  41  VAL   B O    1 
ATOM   4570 C  CB   . VAL   B 1 41  ? 42.975 -17.590 11.418  1.00 14.38 ?  41  VAL   B CB   1 
ATOM   4571 C  CG1  . VAL   B 1 41  ? 41.682 -18.281 11.008  1.00 15.25 ?  41  VAL   B CG1  1 
ATOM   4572 C  CG2  . VAL   B 1 41  ? 43.629 -18.272 12.609  1.00 15.49 ?  41  VAL   B CG2  1 
ATOM   4573 H  H    . VAL   B 1 41  ? 44.225 -19.470 10.315  1.00 14.85 ?  41  VAL   B H    1 
ATOM   4574 H  HA   . VAL   B 1 41  ? 43.458 -17.107 9.501   1.00 15.85 ?  41  VAL   B HA   1 
ATOM   4575 H  HB   . VAL   B 1 41  ? 42.746 -16.688 11.693  1.00 17.31 ?  41  VAL   B HB   1 
ATOM   4576 H  HG11 . VAL   B 1 41  ? 41.076 -18.292 11.767  1.00 18.36 ?  41  VAL   B HG11 1 
ATOM   4577 H  HG12 . VAL   B 1 41  ? 41.283 -17.792 10.273  1.00 18.36 ?  41  VAL   B HG12 1 
ATOM   4578 H  HG13 . VAL   B 1 41  ? 41.884 -19.189 10.734  1.00 18.36 ?  41  VAL   B HG13 1 
ATOM   4579 H  HG21 . VAL   B 1 41  ? 42.992 -18.314 13.338  1.00 18.65 ?  41  VAL   B HG21 1 
ATOM   4580 H  HG22 . VAL   B 1 41  ? 43.897 -19.169 12.353  1.00 18.65 ?  41  VAL   B HG22 1 
ATOM   4581 H  HG23 . VAL   B 1 41  ? 44.407 -17.759 12.880  1.00 18.65 ?  41  VAL   B HG23 1 
ATOM   4582 N  N    . TYR   B 1 42  ? 46.276 -17.075 10.909  1.00 13.23 ?  42  TYR   B N    1 
ATOM   4583 C  CA   . TYR   B 1 42  ? 47.436 -16.227 11.171  1.00 13.80 ?  42  TYR   B CA   1 
ATOM   4584 C  C    . TYR   B 1 42  ? 48.400 -16.155 9.988   1.00 12.96 ?  42  TYR   B C    1 
ATOM   4585 O  O    . TYR   B 1 42  ? 49.489 -15.581 10.120  1.00 13.83 ?  42  TYR   B O    1 
ATOM   4586 C  CB   . TYR   B 1 42  ? 48.135 -16.634 12.475  1.00 15.56 ?  42  TYR   B CB   1 
ATOM   4587 C  CG   . TYR   B 1 42  ? 47.523 -15.963 13.702  1.00 16.11 ?  42  TYR   B CG   1 
ATOM   4588 C  CD1  . TYR   B 1 42  ? 47.739 -14.611 13.950  1.00 15.23 ?  42  TYR   B CD1  1 
ATOM   4589 C  CD2  . TYR   B 1 42  ? 46.732 -16.669 14.595  1.00 18.16 ?  42  TYR   B CD2  1 
ATOM   4590 C  CE1  . TYR   B 1 42  ? 47.186 -13.983 15.051  1.00 16.28 ?  42  TYR   B CE1  1 
ATOM   4591 C  CE2  . TYR   B 1 42  ? 46.178 -16.048 15.706  1.00 18.35 ?  42  TYR   B CE2  1 
ATOM   4592 C  CZ   . TYR   B 1 42  ? 46.408 -14.701 15.926  1.00 18.53 ?  42  TYR   B CZ   1 
ATOM   4593 O  OH   . TYR   B 1 42  ? 45.867 -14.068 17.026  1.00 21.19 ?  42  TYR   B OH   1 
ATOM   4594 H  H    . TYR   B 1 42  ? 46.422 -17.921 11.004  1.00 15.93 ?  42  TYR   B H    1 
ATOM   4595 H  HA   . TYR   B 1 42  ? 47.108 -15.329 11.307  1.00 16.61 ?  42  TYR   B HA   1 
ATOM   4596 H  HB2  . TYR   B 1 42  ? 48.062 -17.593 12.590  1.00 18.73 ?  42  TYR   B HB2  1 
ATOM   4597 H  HB3  . TYR   B 1 42  ? 49.069 -16.375 12.424  1.00 18.73 ?  42  TYR   B HB3  1 
ATOM   4598 H  HD1  . TYR   B 1 42  ? 48.267 -14.120 13.356  1.00 18.34 ?  42  TYR   B HD1  1 
ATOM   4599 H  HD2  . TYR   B 1 42  ? 46.572 -17.574 14.445  1.00 21.85 ?  42  TYR   B HD2  1 
ATOM   4600 H  HE1  . TYR   B 1 42  ? 47.348 -13.080 15.198  1.00 19.59 ?  42  TYR   B HE1  1 
ATOM   4601 H  HE2  . TYR   B 1 42  ? 45.648 -16.533 16.295  1.00 22.07 ?  42  TYR   B HE2  1 
ATOM   4602 H  HH   . TYR   B 1 42  ? 46.093 -13.261 17.027  1.00 25.48 ?  42  TYR   B HH   1 
ATOM   4603 N  N    . LEU   B 1 43  ? 48.000 -16.673 8.827   1.00 11.88 ?  43  LEU   B N    1 
ATOM   4604 C  CA   . LEU   B 1 43  ? 48.809 -16.604 7.615   1.00 11.71 ?  43  LEU   B CA   1 
ATOM   4605 C  C    . LEU   B 1 43  ? 50.221 -17.117 7.869   1.00 12.02 ?  43  LEU   B C    1 
ATOM   4606 O  O    . LEU   B 1 43  ? 51.205 -16.525 7.421   1.00 12.53 ?  43  LEU   B O    1 
ATOM   4607 C  CB   . LEU   B 1 43  ? 48.825 -15.199 7.005   1.00 11.97 ?  43  LEU   B CB   1 
ATOM   4608 C  CG   . LEU   B 1 43  ? 47.466 -14.583 6.644   1.00 12.01 ?  43  LEU   B CG   1 
ATOM   4609 C  CD1  . LEU   B 1 43  ? 47.685 -13.196 6.044   1.00 13.42 ?  43  LEU   B CD1  1 
ATOM   4610 C  CD2  . LEU   B 1 43  ? 46.688 -15.473 5.687   1.00 12.57 ?  43  LEU   B CD2  1 
ATOM   4611 H  H    . LEU   B 1 43  ? 47.251 -17.081 8.716   1.00 14.31 ?  43  LEU   B H    1 
ATOM   4612 H  HA   . LEU   B 1 43  ? 48.408 -17.195 6.955   1.00 14.11 ?  43  LEU   B HA   1 
ATOM   4613 H  HB2  . LEU   B 1 43  ? 49.253 -14.602 7.636   1.00 14.42 ?  43  LEU   B HB2  1 
ATOM   4614 H  HB3  . LEU   B 1 43  ? 49.345 -15.233 6.189   1.00 14.42 ?  43  LEU   B HB3  1 
ATOM   4615 H  HG   . LEU   B 1 43  ? 46.942 -14.475 7.453   1.00 14.46 ?  43  LEU   B HG   1 
ATOM   4616 H  HD11 . LEU   B 1 43  ? 46.825 -12.809 5.820   1.00 16.16 ?  43  LEU   B HD11 1 
ATOM   4617 H  HD12 . LEU   B 1 43  ? 48.139 -12.637 6.697   1.00 16.16 ?  43  LEU   B HD12 1 
ATOM   4618 H  HD13 . LEU   B 1 43  ? 48.230 -13.280 5.246   1.00 16.16 ?  43  LEU   B HD13 1 
ATOM   4619 H  HD21 . LEU   B 1 43  ? 45.886 -15.006 5.403   1.00 15.14 ?  43  LEU   B HD21 1 
ATOM   4620 H  HD22 . LEU   B 1 43  ? 47.245 -15.672 4.920   1.00 15.14 ?  43  LEU   B HD22 1 
ATOM   4621 H  HD23 . LEU   B 1 43  ? 46.449 -16.293 6.146   1.00 15.14 ?  43  LEU   B HD23 1 
ATOM   4622 N  N    . LYS   B 1 44  ? 50.316 -18.237 8.590   1.00 12.03 ?  44  LYS   B N    1 
ATOM   4623 C  CA   . LYS   B 1 44  ? 51.580 -18.919 8.831   1.00 12.74 ?  44  LYS   B CA   1 
ATOM   4624 C  C    . LYS   B 1 44  ? 51.696 -20.035 7.800   1.00 12.17 ?  44  LYS   B C    1 
ATOM   4625 O  O    . LYS   B 1 44  ? 51.002 -21.053 7.890   1.00 13.42 ?  44  LYS   B O    1 
ATOM   4626 C  CB   . LYS   B 1 44  ? 51.638 -19.438 10.267  1.00 14.51 ?  44  LYS   B CB   1 
ATOM   4627 C  CG   . LYS   B 1 44  ? 51.817 -18.332 11.300  1.00 17.03 ?  44  LYS   B CG   1 
ATOM   4628 C  CD   . LYS   B 1 44  ? 53.015 -17.459 10.918  1.00 19.95 ?  44  LYS   B CD   1 
ATOM   4629 C  CE   . LYS   B 1 44  ? 53.481 -16.559 12.035  1.00 22.67 ?  44  LYS   B CE   1 
ATOM   4630 N  NZ   . LYS   B 1 44  ? 54.686 -15.775 11.653  1.00 23.99 ?  44  LYS   B NZ   1 
ATOM   4631 H  H    . LYS   B 1 44  ? 49.639 -18.622 8.958   1.00 14.49 ?  44  LYS   B H    1 
ATOM   4632 H  HA   . LYS   B 1 44  ? 52.314 -18.308 8.675   1.00 15.34 ?  44  LYS   B HA   1 
ATOM   4633 H  HB2  . LYS   B 1 44  ? 50.804 -19.897 10.469  1.00 17.46 ?  44  LYS   B HB2  1 
ATOM   4634 H  HB3  . LYS   B 1 44  ? 52.381 -20.049 10.354  1.00 17.46 ?  44  LYS   B HB3  1 
ATOM   4635 H  HG2  . LYS   B 1 44  ? 51.021 -17.782 11.328  1.00 20.50 ?  44  LYS   B HG2  1 
ATOM   4636 H  HG3  . LYS   B 1 44  ? 51.988 -18.732 12.171  1.00 20.50 ?  44  LYS   B HG3  1 
ATOM   4637 H  HD2  . LYS   B 1 44  ? 53.750 -18.040 10.652  1.00 23.99 ?  44  LYS   B HD2  1 
ATOM   4638 H  HD3  . LYS   B 1 44  ? 52.757 -16.893 10.173  1.00 23.99 ?  44  LYS   B HD3  1 
ATOM   4639 H  HE2  . LYS   B 1 44  ? 52.776 -15.931 12.232  1.00 27.26 ?  44  LYS   B HE2  1 
ATOM   4640 H  HE3  . LYS   B 1 44  ? 53.693 -17.097 12.813  1.00 27.26 ?  44  LYS   B HE3  1 
ATOM   4641 H  HZ1  . LYS   B 1 44  ? 54.933 -15.253 12.328  1.00 28.84 ?  44  LYS   B HZ1  1 
ATOM   4642 H  HZ2  . LYS   B 1 44  ? 55.356 -16.323 11.448  1.00 28.84 ?  44  LYS   B HZ2  1 
ATOM   4643 H  HZ3  . LYS   B 1 44  ? 54.504 -15.265 10.944  1.00 28.84 ?  44  LYS   B HZ3  1 
ATOM   4644 N  N    . HIS   B 1 45  ? 52.545 -19.816 6.798   1.00 11.85 ?  45  HIS   B N    1 
ATOM   4645 C  CA   . HIS   B 1 45  ? 52.568 -20.645 5.594   1.00 11.81 ?  45  HIS   B CA   1 
ATOM   4646 C  C    . HIS   B 1 45  ? 53.583 -21.774 5.755   1.00 13.97 ?  45  HIS   B C    1 
ATOM   4647 O  O    . HIS   B 1 45  ? 54.638 -21.796 5.130   1.00 16.36 ?  45  HIS   B O    1 
ATOM   4648 C  CB   . HIS   B 1 45  ? 52.885 -19.787 4.380   1.00 11.84 ?  45  HIS   B CB   1 
ATOM   4649 C  CG   . HIS   B 1 45  ? 52.011 -18.585 4.265   1.00 11.84 ?  45  HIS   B CG   1 
ATOM   4650 N  ND1  . HIS   B 1 45  ? 50.633 -18.662 4.240   1.00 11.98 ?  45  HIS   B ND1  1 
ATOM   4651 C  CD2  . HIS   B 1 45  ? 52.328 -17.271 4.187   1.00 12.58 ?  45  HIS   B CD2  1 
ATOM   4652 C  CE1  . HIS   B 1 45  ? 50.146 -17.440 4.136   1.00 11.66 ?  45  HIS   B CE1  1 
ATOM   4653 N  NE2  . HIS   B 1 45  ? 51.150 -16.579 4.101   1.00 12.13 ?  45  HIS   B NE2  1 
ATOM   4654 H  H    . HIS   B 1 45  ? 53.117 -19.173 6.789   1.00 14.27 ?  45  HIS   B H    1 
ATOM   4655 H  HA   . HIS   B 1 45  ? 51.687 -21.038 5.464   1.00 14.23 ?  45  HIS   B HA   1 
ATOM   4656 H  HB2  . HIS   B 1 45  ? 53.804 -19.488 4.439   1.00 14.26 ?  45  HIS   B HB2  1 
ATOM   4657 H  HB3  . HIS   B 1 45  ? 52.765 -20.326 3.579   1.00 14.26 ?  45  HIS   B HB3  1 
ATOM   4658 H  HD2  . HIS   B 1 45  ? 53.183 -16.906 4.186   1.00 15.15 ?  45  HIS   B HD2  1 
ATOM   4659 H  HE1  . HIS   B 1 45  ? 49.243 -17.224 4.083   1.00 14.05 ?  45  HIS   B HE1  1 
ATOM   4660 H  HE2  . HIS   B 1 45  ? 51.069 -15.725 4.038   1.00 14.61 ?  45  HIS   B HE2  1 
ATOM   4661 N  N    . GLY   B 1 46  ? 53.226 -22.736 6.597   1.00 14.88 ?  46  GLY   B N    1 
ATOM   4662 C  CA   . GLY   B 1 46  ? 54.156 -23.794 6.944   1.00 16.55 ?  46  GLY   B CA   1 
ATOM   4663 C  C    . GLY   B 1 46  ? 54.201 -24.986 6.009   1.00 18.03 ?  46  GLY   B C    1 
ATOM   4664 O  O    . GLY   B 1 46  ? 55.271 -25.385 5.540   1.00 21.15 ?  46  GLY   B O    1 
ATOM   4665 H  H    . GLY   B 1 46  ? 52.456 -22.785 6.990   1.00 17.91 ?  46  GLY   B H    1 
ATOM   4666 H  HA2  . GLY   B 1 46  ? 55.045 -23.415 6.989   1.00 19.92 ?  46  GLY   B HA2  1 
ATOM   4667 H  HA3  . GLY   B 1 46  ? 53.926 -24.126 7.824   1.00 19.92 ?  46  GLY   B HA3  1 
ATOM   4668 N  N    . GLY   B 1 47  ? 53.043 -25.576 5.731   1.00 17.50 ?  47  GLY   B N    1 
ATOM   4669 C  CA   . GLY   B 1 47  ? 52.983 -26.869 5.079   1.00 15.49 ?  47  GLY   B CA   1 
ATOM   4670 C  C    . GLY   B 1 47  ? 52.065 -26.850 3.872   1.00 13.34 ?  47  GLY   B C    1 
ATOM   4671 O  O    . GLY   B 1 47  ? 51.416 -25.845 3.576   1.00 13.50 ?  47  GLY   B O    1 
ATOM   4672 H  H    . GLY   B 1 47  ? 52.272 -25.251 5.934   1.00 21.05 ?  47  GLY   B H    1 
ATOM   4673 H  HA2  . GLY   B 1 47  ? 53.871 -27.130 4.786   1.00 18.65 ?  47  GLY   B HA2  1 
ATOM   4674 H  HA3  . GLY   B 1 47  ? 52.660 -27.535 5.708   1.00 18.65 ?  47  GLY   B HA3  1 
ATOM   4675 N  N    . GLY   B 1 48  ? 52.026 -27.991 3.184   1.00 12.74 ?  48  GLY   B N    1 
ATOM   4676 C  CA   . GLY   B 1 48  ? 51.098 -28.138 2.077   1.00 12.51 ?  48  GLY   B CA   1 
ATOM   4677 C  C    . GLY   B 1 48  ? 51.233 -27.030 1.058   1.00 12.22 ?  48  GLY   B C    1 
ATOM   4678 O  O    . GLY   B 1 48  ? 52.334 -26.564 0.744   1.00 12.81 ?  48  GLY   B O    1 
ATOM   4679 H  H    . GLY   B 1 48  ? 52.528 -28.670 3.327   1.00 15.34 ?  48  GLY   B H    1 
ATOM   4680 H  HA2  . GLY   B 1 48  ? 51.255 -28.986 1.633   1.00 15.06 ?  48  GLY   B HA2  1 
ATOM   4681 H  HA3  . GLY   B 1 48  ? 50.188 -28.133 2.415   1.00 15.06 ?  48  GLY   B HA3  1 
ATOM   4682 N  N    . VAL   B 1 49  ? 50.085 -26.601 0.526   1.00 11.91 ?  49  VAL   B N    1 
ATOM   4683 C  CA   . VAL   B 1 49  ? 50.063 -25.573 -0.513  1.00 11.98 ?  49  VAL   B CA   1 
ATOM   4684 C  C    . VAL   B 1 49  ? 50.723 -24.287 -0.025  1.00 11.39 ?  49  VAL   B C    1 
ATOM   4685 O  O    . VAL   B 1 49  ? 51.512 -23.668 -0.747  1.00 11.76 ?  49  VAL   B O    1 
ATOM   4686 C  CB   . VAL   B 1 49  ? 48.618 -25.324 -0.989  1.00 13.13 ?  49  VAL   B CB   1 
ATOM   4687 C  CG1  . VAL   B 1 49  ? 48.541 -24.087 -1.873  1.00 13.04 ?  49  VAL   B CG1  1 
ATOM   4688 C  CG2  . VAL   B 1 49  ? 48.068 -26.548 -1.725  1.00 14.58 ?  49  VAL   B CG2  1 
ATOM   4689 H  H    . VAL   B 1 49  ? 49.299 -26.893 0.745   1.00 14.35 ?  49  VAL   B H    1 
ATOM   4690 H  HA   . VAL   B 1 49  ? 50.566 -25.892 -1.279  1.00 14.43 ?  49  VAL   B HA   1 
ATOM   4691 H  HB   . VAL   B 1 49  ? 48.056 -25.168 -0.217  1.00 15.81 ?  49  VAL   B HB   1 
ATOM   4692 H  HG11 . VAL   B 1 49  ? 47.705 -24.104 -2.368  1.00 15.70 ?  49  VAL   B HG11 1 
ATOM   4693 H  HG12 . VAL   B 1 49  ? 48.572 -23.293 -1.315  1.00 15.70 ?  49  VAL   B HG12 1 
ATOM   4694 H  HG13 . VAL   B 1 49  ? 49.287 -24.089 -2.491  1.00 15.70 ?  49  VAL   B HG13 1 
ATOM   4695 H  HG21 . VAL   B 1 49  ? 47.159 -26.365 -2.013  1.00 17.55 ?  49  VAL   B HG21 1 
ATOM   4696 H  HG22 . VAL   B 1 49  ? 48.627 -26.731 -2.498  1.00 17.55 ?  49  VAL   B HG22 1 
ATOM   4697 H  HG23 . VAL   B 1 49  ? 48.078 -27.308 -1.124  1.00 17.55 ?  49  VAL   B HG23 1 
ATOM   4698 N  N    . ALA   B 1 50  ? 50.381 -23.842 1.186   1.00 10.91 ?  50  ALA   B N    1 
ATOM   4699 C  CA   . ALA   B 1 50  ? 50.900 -22.564 1.664   1.00 10.77 ?  50  ALA   B CA   1 
ATOM   4700 C  C    . ALA   B 1 50  ? 52.420 -22.593 1.768   1.00 11.08 ?  50  ALA   B C    1 
ATOM   4701 O  O    . ALA   B 1 50  ? 53.098 -21.625 1.398   1.00 11.26 ?  50  ALA   B O    1 
ATOM   4702 C  CB   . ALA   B 1 50  ? 50.267 -22.204 3.009   1.00 11.27 ?  50  ALA   B CB   1 
ATOM   4703 H  H    . ALA   B 1 50  ? 49.864 -24.255 1.735   1.00 13.15 ?  50  ALA   B H    1 
ATOM   4704 H  HA   . ALA   B 1 50  ? 50.668 -21.875 1.033   1.00 12.98 ?  50  ALA   B HA   1 
ATOM   4705 H  HB1  . ALA   B 1 50  ? 50.623 -21.353 3.311   1.00 13.58 ?  50  ALA   B HB1  1 
ATOM   4706 H  HB2  . ALA   B 1 50  ? 49.303 -22.134 2.897   1.00 13.58 ?  50  ALA   B HB2  1 
ATOM   4707 H  HB3  . ALA   B 1 50  ? 50.471 -22.896 3.658   1.00 13.58 ?  50  ALA   B HB3  1 
ATOM   4708 N  N    . GLY   B 1 51  ? 52.973 -23.689 2.284   1.00 11.82 ?  51  GLY   B N    1 
ATOM   4709 C  CA   . GLY   B 1 51  ? 54.418 -23.791 2.358   1.00 12.36 ?  51  GLY   B CA   1 
ATOM   4710 C  C    . GLY   B 1 51  ? 55.065 -23.742 0.990   1.00 11.97 ?  51  GLY   B C    1 
ATOM   4711 O  O    . GLY   B 1 51  ? 56.105 -23.104 0.807   1.00 12.71 ?  51  GLY   B O    1 
ATOM   4712 H  H    . GLY   B 1 51  ? 52.547 -24.370 2.589   1.00 14.24 ?  51  GLY   B H    1 
ATOM   4713 H  HA2  . GLY   B 1 51  ? 54.770 -23.058 2.888   1.00 14.89 ?  51  GLY   B HA2  1 
ATOM   4714 H  HA3  . GLY   B 1 51  ? 54.666 -24.626 2.784   1.00 14.89 ?  51  GLY   B HA3  1 
ATOM   4715 N  N    . ALA   B 1 52  ? 54.456 -24.403 0.008   1.00 11.88 ?  52  ALA   B N    1 
ATOM   4716 C  CA   . ALA   B 1 52  ? 55.015 -24.410 -1.336  1.00 12.41 ?  52  ALA   B CA   1 
ATOM   4717 C  C    . ALA   B 1 52  ? 54.934 -23.035 -1.990  1.00 11.40 ?  52  ALA   B C    1 
ATOM   4718 O  O    . ALA   B 1 52  ? 55.902 -22.587 -2.622  1.00 12.19 ?  52  ALA   B O    1 
ATOM   4719 C  CB   . ALA   B 1 52  ? 54.308 -25.458 -2.189  1.00 12.98 ?  52  ALA   B CB   1 
ATOM   4720 H  H    . ALA   B 1 52  ? 53.719 -24.840 0.093   1.00 14.31 ?  52  ALA   B H    1 
ATOM   4721 H  HA   . ALA   B 1 52  ? 55.949 -24.653 -1.281  1.00 14.94 ?  52  ALA   B HA   1 
ATOM   4722 H  HB1  . ALA   B 1 52  ? 54.695 -25.454 -3.080  1.00 15.64 ?  52  ALA   B HB1  1 
ATOM   4723 H  HB2  . ALA   B 1 52  ? 54.436 -26.332 -1.782  1.00 15.64 ?  52  ALA   B HB2  1 
ATOM   4724 H  HB3  . ALA   B 1 52  ? 53.364 -25.250 -2.236  1.00 15.64 ?  52  ALA   B HB3  1 
ATOM   4725 N  N    . LEU   B 1 53  ? 53.789 -22.357 -1.875  1.00 11.12 ?  53  LEU   B N    1 
ATOM   4726 C  CA   . LEU   B 1 53  ? 53.679 -21.018 -2.443  1.00 11.03 ?  53  LEU   B CA   1 
ATOM   4727 C  C    . LEU   B 1 53  ? 54.690 -20.080 -1.796  1.00 11.10 ?  53  LEU   B C    1 
ATOM   4728 O  O    . LEU   B 1 53  ? 55.389 -19.329 -2.483  1.00 11.90 ?  53  LEU   B O    1 
ATOM   4729 C  CB   . LEU   B 1 53  ? 52.255 -20.480 -2.264  1.00 11.84 ?  53  LEU   B CB   1 
ATOM   4730 C  CG   . LEU   B 1 53  ? 51.126 -21.213 -2.994  1.00 12.36 ?  53  LEU   B CG   1 
ATOM   4731 C  CD1  . LEU   B 1 53  ? 49.787 -20.604 -2.643  1.00 13.74 ?  53  LEU   B CD1  1 
ATOM   4732 C  CD2  . LEU   B 1 53  ? 51.338 -21.196 -4.501  1.00 14.32 ?  53  LEU   B CD2  1 
ATOM   4733 H  H    . LEU   B 1 53  ? 53.083 -22.641 -1.480  1.00 13.40 ?  53  LEU   B H    1 
ATOM   4734 H  HA   . LEU   B 1 53  ? 53.874 -21.058 -3.395  1.00 13.29 ?  53  LEU   B HA   1 
ATOM   4735 H  HB2  . LEU   B 1 53  ? 52.045 -20.502 -1.320  1.00 14.26 ?  53  LEU   B HB2  1 
ATOM   4736 H  HB3  . LEU   B 1 53  ? 52.241 -19.563 -2.576  1.00 14.26 ?  53  LEU   B HB3  1 
ATOM   4737 H  HG   . LEU   B 1 53  ? 51.115 -22.140 -2.703  1.00 14.89 ?  53  LEU   B HG   1 
ATOM   4738 H  HD11 . LEU   B 1 53  ? 49.088 -21.090 -3.111  1.00 16.54 ?  53  LEU   B HD11 1 
ATOM   4739 H  HD12 . LEU   B 1 53  ? 49.650 -20.676 -1.683  1.00 16.54 ?  53  LEU   B HD12 1 
ATOM   4740 H  HD13 . LEU   B 1 53  ? 49.782 -19.675 -2.910  1.00 16.54 ?  53  LEU   B HD13 1 
ATOM   4741 H  HD21 . LEU   B 1 53  ? 50.608 -21.667 -4.928  1.00 17.24 ?  53  LEU   B HD21 1 
ATOM   4742 H  HD22 . LEU   B 1 53  ? 51.364 -20.277 -4.805  1.00 17.24 ?  53  LEU   B HD22 1 
ATOM   4743 H  HD23 . LEU   B 1 53  ? 52.179 -21.637 -4.708  1.00 17.24 ?  53  LEU   B HD23 1 
ATOM   4744 N  N    . ASN   B 1 54  ? 54.780 -20.107 -0.470  1.00 10.81 ?  54  ASN   B N    1 
ATOM   4745 C  CA   . ASN   B 1 54  ? 55.694 -19.194 0.199   1.00 11.90 ?  54  ASN   B CA   1 
ATOM   4746 C  C    . ASN   B 1 54  ? 57.138 -19.469 -0.202  1.00 12.25 ?  54  ASN   B C    1 
ATOM   4747 O  O    . ASN   B 1 54  ? 57.917 -18.533 -0.429  1.00 12.56 ?  54  ASN   B O    1 
ATOM   4748 C  CB   . ASN   B 1 54  ? 55.540 -19.280 1.708   1.00 12.36 ?  54  ASN   B CB   1 
ATOM   4749 C  CG   . ASN   B 1 54  ? 56.515 -18.364 2.419   1.00 12.65 ?  54  ASN   B CG   1 
ATOM   4750 O  OD1  . ASN   B 1 54  ? 56.529 -17.152 2.177   1.00 12.60 ?  54  ASN   B OD1  1 
ATOM   4751 N  ND2  . ASN   B 1 54  ? 57.354 -18.932 3.274   1.00 14.33 ?  54  ASN   B ND2  1 
ATOM   4752 H  H    . ASN   B 1 54  ? 54.338 -20.632 0.048   1.00 13.03 ?  54  ASN   B H    1 
ATOM   4753 H  HA   . ASN   B 1 54  ? 55.482 -18.291 -0.070  1.00 14.33 ?  54  ASN   B HA   1 
ATOM   4754 H  HB2  . ASN   B 1 54  ? 54.639 -19.013 1.952   1.00 14.89 ?  54  ASN   B HB2  1 
ATOM   4755 H  HB3  . ASN   B 1 54  ? 55.711 -20.188 1.999   1.00 14.89 ?  54  ASN   B HB3  1 
ATOM   4756 H  HD21 . ASN   B 1 54  ? 57.930 -18.450 3.695   1.00 17.26 ?  54  ASN   B HD21 1 
ATOM   4757 H  HD22 . ASN   B 1 54  ? 57.323 -19.780 3.410   1.00 17.26 ?  54  ASN   B HD22 1 
ATOM   4758 N  N    . LYS   B 1 55  ? 57.523 -20.747 -0.267  1.00 12.61 ?  55  LYS   B N    1 
ATOM   4759 C  CA   . LYS   B 1 55  ? 58.879 -21.089 -0.686  1.00 13.39 ?  55  LYS   B CA   1 
ATOM   4760 C  C    . LYS   B 1 55  ? 59.172 -20.553 -2.081  1.00 13.27 ?  55  LYS   B C    1 
ATOM   4761 O  O    . LYS   B 1 55  ? 60.273 -20.052 -2.341  1.00 13.91 ?  55  LYS   B O    1 
ATOM   4762 C  CB   . LYS   B 1 55  ? 59.078 -22.604 -0.626  1.00 15.26 ?  55  LYS   B CB   1 
ATOM   4763 C  CG   . LYS   B 1 55  ? 60.443 -23.079 -1.083  1.00 19.41 ?  55  LYS   B CG   1 
ATOM   4764 C  CD   . LYS   B 1 55  ? 60.601 -24.578 -0.894  1.00 22.98 ?  55  LYS   B CD   1 
ATOM   4765 C  CE   . LYS   B 1 55  ? 60.620 -24.963 0.583   1.00 26.30 ?  55  LYS   B CE   1 
ATOM   4766 N  NZ   . LYS   B 1 55  ? 61.032 -26.372 0.788   1.00 27.79 ?  55  LYS   B NZ   1 
ATOM   4767 H  H    . LYS   B 1 55  ? 57.023 -21.422 -0.080  1.00 15.19 ?  55  LYS   B H    1 
ATOM   4768 H  HA   . LYS   B 1 55  ? 59.508 -20.680 -0.072  1.00 16.12 ?  55  LYS   B HA   1 
ATOM   4769 H  HB2  . LYS   B 1 55  ? 58.956 -22.887 0.293   1.00 18.36 ?  55  LYS   B HB2  1 
ATOM   4770 H  HB3  . LYS   B 1 55  ? 58.416 -23.027 -1.190  1.00 18.36 ?  55  LYS   B HB3  1 
ATOM   4771 H  HG2  . LYS   B 1 55  ? 60.554 -22.880 -2.027  1.00 23.34 ?  55  LYS   B HG2  1 
ATOM   4772 H  HG3  . LYS   B 1 55  ? 61.131 -22.632 -0.564  1.00 23.34 ?  55  LYS   B HG3  1 
ATOM   4773 H  HD2  . LYS   B 1 55  ? 59.856 -25.036 -1.316  1.00 27.63 ?  55  LYS   B HD2  1 
ATOM   4774 H  HD3  . LYS   B 1 55  ? 61.439 -24.867 -1.290  1.00 27.63 ?  55  LYS   B HD3  1 
ATOM   4775 H  HE2  . LYS   B 1 55  ? 61.245 -24.383 1.050   1.00 31.62 ?  55  LYS   B HE2  1 
ATOM   4776 H  HE3  . LYS   B 1 55  ? 59.727 -24.848 0.950   1.00 31.62 ?  55  LYS   B HE3  1 
ATOM   4777 H  HZ1  . LYS   B 1 55  ? 61.012 -26.567 1.656   1.00 33.40 ?  55  LYS   B HZ1  1 
ATOM   4778 H  HZ2  . LYS   B 1 55  ? 60.475 -26.914 0.356   1.00 33.40 ?  55  LYS   B HZ2  1 
ATOM   4779 H  HZ3  . LYS   B 1 55  ? 61.856 -26.493 0.481   1.00 33.40 ?  55  LYS   B HZ3  1 
ATOM   4780 N  N    . ALA   B 1 56  ? 58.199 -20.638 -2.991  1.00 12.74 ?  56  ALA   B N    1 
ATOM   4781 C  CA   . ALA   B 1 56  ? 58.415 -20.136 -4.343  1.00 13.34 ?  56  ALA   B CA   1 
ATOM   4782 C  C    . ALA   B 1 56  ? 58.691 -18.640 -4.343  1.00 13.44 ?  56  ALA   B C    1 
ATOM   4783 O  O    . ALA   B 1 56  ? 59.409 -18.141 -5.221  1.00 14.72 ?  56  ALA   B O    1 
ATOM   4784 C  CB   . ALA   B 1 56  ? 57.215 -20.467 -5.232  1.00 14.28 ?  56  ALA   B CB   1 
ATOM   4785 H  H    . ALA   B 1 56  ? 57.416 -20.969 -2.849  1.00 15.34 ?  56  ALA   B H    1 
ATOM   4786 H  HA   . ALA   B 1 56  ? 59.190 -20.573 -4.717  1.00 16.06 ?  56  ALA   B HA   1 
ATOM   4787 H  HB1  . ALA   B 1 56  ? 57.384 -20.129 -6.128  1.00 17.20 ?  56  ALA   B HB1  1 
ATOM   4788 H  HB2  . ALA   B 1 56  ? 57.103 -21.430 -5.261  1.00 17.20 ?  56  ALA   B HB2  1 
ATOM   4789 H  HB3  . ALA   B 1 56  ? 56.421 -20.050 -4.867  1.00 17.20 ?  56  ALA   B HB3  1 
ATOM   4790 N  N    . THR   B 1 57  ? 58.128 -17.908 -3.378  1.00 13.26 ?  57  THR   B N    1 
ATOM   4791 C  CA   . THR   B 1 57  ? 58.364 -16.473 -3.257  1.00 13.44 ?  57  THR   B CA   1 
ATOM   4792 C  C    . THR   B 1 57  ? 59.618 -16.144 -2.453  1.00 14.53 ?  57  THR   B C    1 
ATOM   4793 O  O    . THR   B 1 57  ? 59.857 -14.967 -2.153  1.00 14.78 ?  57  THR   B O    1 
ATOM   4794 C  CB   . THR   B 1 57  ? 57.165 -15.745 -2.617  1.00 12.59 ?  57  THR   B CB   1 
ATOM   4795 O  OG1  . THR   B 1 57  ? 57.146 -15.959 -1.199  1.00 12.76 ?  57  THR   B OG1  1 
ATOM   4796 C  CG2  . THR   B 1 57  ? 55.840 -16.161 -3.244  1.00 12.57 ?  57  THR   B CG2  1 
ATOM   4797 H  H    . THR   B 1 57  ? 57.589 -18.223 -2.780  1.00 15.97 ?  57  THR   B H    1 
ATOM   4798 H  HA   . THR   B 1 57  ? 58.477 -16.108 -4.148  1.00 16.19 ?  57  THR   B HA   1 
ATOM   4799 H  HB   . THR   B 1 57  ? 57.269 -14.794 -2.778  1.00 15.17 ?  57  THR   B HB   1 
ATOM   4800 H  HG1  . THR   B 1 57  ? 57.076 -16.782 -1.034  1.00 15.36 ?  57  THR   B HG1  1 
ATOM   4801 H  HG21 . THR   B 1 57  ? 55.118 -15.632 -2.872  1.00 15.15 ?  57  THR   B HG21 1 
ATOM   4802 H  HG22 . THR   B 1 57  ? 55.870 -16.026 -4.203  1.00 15.15 ?  57  THR   B HG22 1 
ATOM   4803 H  HG23 . THR   B 1 57  ? 55.667 -17.097 -3.064  1.00 15.15 ?  57  THR   B HG23 1 
ATOM   4804 N  N    . ASN   B 1 58  ? 60.420 -17.145 -2.097  1.00 14.99 ?  58  ASN   B N    1 
ATOM   4805 C  CA   . ASN   B 1 58  ? 61.618 -16.927 -1.291  1.00 17.97 ?  58  ASN   B CA   1 
ATOM   4806 C  C    . ASN   B 1 58  ? 61.280 -16.219 0.022   1.00 15.29 ?  58  ASN   B C    1 
ATOM   4807 O  O    . ASN   B 1 58  ? 62.018 -15.345 0.490   1.00 16.15 ?  58  ASN   B O    1 
ATOM   4808 C  CB   . ASN   B 1 58  ? 62.701 -16.176 -2.074  1.00 27.27 ?  58  ASN   B CB   1 
ATOM   4809 C  CG   . ASN   B 1 58  ? 64.069 -16.289 -1.429  1.00 37.61 ?  58  ASN   B CG   1 
ATOM   4810 O  OD1  . ASN   B 1 58  ? 64.378 -17.283 -0.772  1.00 40.63 ?  58  ASN   B OD1  1 
ATOM   4811 N  ND2  . ASN   B 1 58  ? 64.898 -15.267 -1.614  1.00 41.22 ?  58  ASN   B ND2  1 
ATOM   4812 H  H    . ASN   B 1 58  ? 60.289 -17.970 -2.310  1.00 18.05 ?  58  ASN   B H    1 
ATOM   4813 H  HA   . ASN   B 1 58  ? 61.984 -17.797 -1.066  1.00 21.62 ?  58  ASN   B HA   1 
ATOM   4814 H  HB2  . ASN   B 1 58  ? 62.760 -16.546 -2.972  1.00 32.78 ?  58  ASN   B HB2  1 
ATOM   4815 H  HB3  . ASN   B 1 58  ? 62.469 -15.237 -2.117  1.00 32.78 ?  58  ASN   B HB3  1 
ATOM   4816 H  HD21 . ASN   B 1 58  ? 65.687 -15.284 -1.270  1.00 49.52 ?  58  ASN   B HD21 1 
ATOM   4817 H  HD22 . ASN   B 1 58  ? 64.646 -14.589 -2.078  1.00 49.52 ?  58  ASN   B HD22 1 
ATOM   4818 N  N    . ASN   B 1 59  ? 60.154 -16.606 0.624   1.00 14.44 ?  59  ASN   B N    1 
ATOM   4819 C  CA   . ASN   B 1 59  ? 59.676 -16.136 1.928   1.00 14.33 ?  59  ASN   B CA   1 
ATOM   4820 C  C    . ASN   B 1 59  ? 59.084 -14.728 1.878   1.00 13.81 ?  59  ASN   B C    1 
ATOM   4821 O  O    . ASN   B 1 59  ? 58.658 -14.222 2.926   1.00 13.76 ?  59  ASN   B O    1 
ATOM   4822 C  CB   . ASN   B 1 59  ? 60.747 -16.201 3.034   1.00 15.44 ?  59  ASN   B CB   1 
ATOM   4823 C  CG   . ASN   B 1 59  ? 60.158 -16.370 4.419   1.00 16.72 ?  59  ASN   B CG   1 
ATOM   4824 O  OD1  . ASN   B 1 59  ? 59.335 -17.257 4.654   1.00 17.00 ?  59  ASN   B OD1  1 
ATOM   4825 N  ND2  . ASN   B 1 59  ? 60.581 -15.520 5.350   1.00 17.72 ?  59  ASN   B ND2  1 
ATOM   4826 H  H    . ASN   B 1 59  ? 59.616 -17.184 0.276   1.00 17.38 ?  59  ASN   B H    1 
ATOM   4827 H  HA   . ASN   B 1 59  ? 58.965 -16.730 2.205   1.00 17.25 ?  59  ASN   B HA   1 
ATOM   4828 H  HB2  . ASN   B 1 59  ? 61.332 -16.959 2.872   1.00 18.59 ?  59  ASN   B HB2  1 
ATOM   4829 H  HB3  . ASN   B 1 59  ? 61.260 -15.380 3.033   1.00 18.59 ?  59  ASN   B HB3  1 
ATOM   4830 H  HD21 . ASN   B 1 59  ? 60.274 -15.571 6.153   1.00 21.32 ?  59  ASN   B HD21 1 
ATOM   4831 H  HD22 . ASN   B 1 59  ? 61.153 -14.913 5.147   1.00 21.32 ?  59  ASN   B HD22 1 
ATOM   4832 N  N    . ALA   B 1 60  ? 59.025 -14.081 0.709   1.00 13.42 ?  60  ALA   B N    1 
ATOM   4833 C  CA   . ALA   B 1 60  ? 58.428 -12.751 0.637   1.00 13.77 ?  60  ALA   B CA   1 
ATOM   4834 C  C    . ALA   B 1 60  ? 56.959 -12.778 1.044   1.00 12.89 ?  60  ALA   B C    1 
ATOM   4835 O  O    . ALA   B 1 60  ? 56.458 -11.827 1.658   1.00 13.21 ?  60  ALA   B O    1 
ATOM   4836 C  CB   . ALA   B 1 60  ? 58.585 -12.173 -0.771  1.00 14.46 ?  60  ALA   B CB   1 
ATOM   4837 H  H    . ALA   B 1 60  ? 59.311 -14.393 -0.039  1.00 16.16 ?  60  ALA   B H    1 
ATOM   4838 H  HA   . ALA   B 1 60  ? 58.894 -12.169 1.252   1.00 16.58 ?  60  ALA   B HA   1 
ATOM   4839 H  HB1  . ALA   B 1 60  ? 58.187 -11.292 -0.797  1.00 17.40 ?  60  ALA   B HB1  1 
ATOM   4840 H  HB2  . ALA   B 1 60  ? 59.532 -12.116 -0.984  1.00 17.40 ?  60  ALA   B HB2  1 
ATOM   4841 H  HB3  . ALA   B 1 60  ? 58.141 -12.759 -1.405  1.00 17.40 ?  60  ALA   B HB3  1 
ATOM   4842 N  N    . MET   B 1 61  ? 56.245 -13.850 0.691   1.00 12.35 ?  61  MET   B N    1 
ATOM   4843 C  CA   . MET   B 1 61  ? 54.850 -13.973 1.091   1.00 12.01 ?  61  MET   B CA   1 
ATOM   4844 C  C    . MET   B 1 61  ? 54.716 -13.982 2.614   1.00 12.02 ?  61  MET   B C    1 
ATOM   4845 O  O    . MET   B 1 61  ? 53.820 -13.334 3.169   1.00 11.67 ?  61  MET   B O    1 
ATOM   4846 C  CB   . MET   B 1 61  ? 54.262 -15.238 0.459   1.00 11.98 ?  61  MET   B CB   1 
ATOM   4847 C  CG   . MET   B 1 61  ? 52.824 -15.536 0.887   1.00 11.58 ?  61  MET   B CG   1 
ATOM   4848 S  SD   . MET   B 1 61  ? 52.187 -17.038 0.115   1.00 12.22 ?  61  MET   B SD   1 
ATOM   4849 C  CE   . MET   B 1 61  ? 51.927 -16.432 -1.550  1.00 13.25 ?  61  MET   B CE   1 
ATOM   4850 H  H    . MET   B 1 61  ? 56.547 -14.515 0.228   1.00 14.88 ?  61  MET   B H    1 
ATOM   4851 H  HA   . MET   B 1 61  ? 54.358 -13.218 0.733   1.00 14.46 ?  61  MET   B HA   1 
ATOM   4852 H  HB2  . MET   B 1 61  ? 54.266 -15.138 -0.509  1.00 14.43 ?  61  MET   B HB2  1 
ATOM   4853 H  HB3  . MET   B 1 61  ? 54.809 -15.998 0.709   1.00 14.43 ?  61  MET   B HB3  1 
ATOM   4854 H  HG2  . MET   B 1 61  ? 52.793 -15.662 1.850   1.00 13.96 ?  61  MET   B HG2  1 
ATOM   4855 H  HG3  . MET   B 1 61  ? 52.251 -14.796 0.630   1.00 13.96 ?  61  MET   B HG3  1 
ATOM   4856 H  HE1  . MET   B 1 61  ? 51.527 -17.134 -2.084  1.00 15.96 ?  61  MET   B HE1  1 
ATOM   4857 H  HE2  . MET   B 1 61  ? 51.331 -15.662 -1.521  1.00 15.96 ?  61  MET   B HE2  1 
ATOM   4858 H  HE3  . MET   B 1 61  ? 52.780 -16.170 -1.929  1.00 15.96 ?  61  MET   B HE3  1 
ATOM   4859 N  N    . GLN   B 1 62  ? 55.603 -14.696 3.311   1.00 12.12 ?  62  GLN   B N    1 
ATOM   4860 C  CA   . GLN   B 1 62  ? 55.498 -14.760 4.766   1.00 12.48 ?  62  GLN   B CA   1 
ATOM   4861 C  C    . GLN   B 1 62  ? 55.783 -13.408 5.405   1.00 12.72 ?  62  GLN   B C    1 
ATOM   4862 O  O    . GLN   B 1 62  ? 55.095 -13.007 6.351   1.00 13.03 ?  62  GLN   B O    1 
ATOM   4863 C  CB   . GLN   B 1 62  ? 56.451 -15.814 5.329   1.00 12.69 ?  62  GLN   B CB   1 
ATOM   4864 C  CG   . GLN   B 1 62  ? 56.228 -16.084 6.807   1.00 13.02 ?  62  GLN   B CG   1 
ATOM   4865 C  CD   . GLN   B 1 62  ? 54.851 -16.674 7.054   1.00 12.43 ?  62  GLN   B CD   1 
ATOM   4866 O  OE1  . GLN   B 1 62  ? 54.594 -17.825 6.705   1.00 12.91 ?  62  GLN   B OE1  1 
ATOM   4867 N  NE2  . GLN   B 1 62  ? 53.943 -15.876 7.614   1.00 12.89 ?  62  GLN   B NE2  1 
ATOM   4868 H  H    . GLN   B 1 62  ? 56.256 -15.141 2.971   1.00 14.60 ?  62  GLN   B H    1 
ATOM   4869 H  HA   . GLN   B 1 62  ? 54.591 -15.014 4.998   1.00 15.03 ?  62  GLN   B HA   1 
ATOM   4870 H  HB2  . GLN   B 1 62  ? 56.320 -16.646 4.848   1.00 15.28 ?  62  GLN   B HB2  1 
ATOM   4871 H  HB3  . GLN   B 1 62  ? 57.364 -15.505 5.214   1.00 15.28 ?  62  GLN   B HB3  1 
ATOM   4872 H  HG2  . GLN   B 1 62  ? 56.891 -16.722 7.116   1.00 15.68 ?  62  GLN   B HG2  1 
ATOM   4873 H  HG3  . GLN   B 1 62  ? 56.303 -15.255 7.303   1.00 15.68 ?  62  GLN   B HG3  1 
ATOM   4874 H  HE21 . GLN   B 1 62  ? 54.155 -15.070 7.833   1.00 15.52 ?  62  GLN   B HE21 1 
ATOM   4875 H  HE22 . GLN   B 1 62  ? 53.150 -16.168 7.765   1.00 15.52 ?  62  GLN   B HE22 1 
ATOM   4876 N  N    . VAL   B 1 63  ? 56.799 -12.694 4.916   1.00 13.26 ?  63  VAL   B N    1 
ATOM   4877 C  CA   . VAL   B 1 63  ? 57.107 -11.379 5.472   1.00 14.06 ?  63  VAL   B CA   1 
ATOM   4878 C  C    . VAL   B 1 63  ? 55.917 -10.445 5.292   1.00 13.39 ?  63  VAL   B C    1 
ATOM   4879 O  O    . VAL   B 1 63  ? 55.507 -9.742  6.225   1.00 13.93 ?  63  VAL   B O    1 
ATOM   4880 C  CB   . VAL   B 1 63  ? 58.398 -10.821 4.850   1.00 15.50 ?  63  VAL   B CB   1 
ATOM   4881 C  CG1  . VAL   B 1 63  ? 58.632 -9.390  5.312   1.00 16.11 ?  63  VAL   B CG1  1 
ATOM   4882 C  CG2  . VAL   B 1 63  ? 59.576 -11.704 5.238   1.00 16.20 ?  63  VAL   B CG2  1 
ATOM   4883 H  H    . VAL   B 1 63  ? 57.311 -12.942 4.267   1.00 15.97 ?  63  VAL   B H    1 
ATOM   4884 H  HA   . VAL   B 1 63  ? 57.263 -11.479 6.421   1.00 16.92 ?  63  VAL   B HA   1 
ATOM   4885 H  HB   . VAL   B 1 63  ? 58.327 -10.827 3.883   1.00 18.66 ?  63  VAL   B HB   1 
ATOM   4886 H  HG11 . VAL   B 1 63  ? 59.551 -9.145  5.124   1.00 19.39 ?  63  VAL   B HG11 1 
ATOM   4887 H  HG12 . VAL   B 1 63  ? 58.027 -8.804  4.836   1.00 19.39 ?  63  VAL   B HG12 1 
ATOM   4888 H  HG13 . VAL   B 1 63  ? 58.466 -9.340  6.267   1.00 19.39 ?  63  VAL   B HG13 1 
ATOM   4889 H  HG21 . VAL   B 1 63  ? 60.391 -11.330 4.866   1.00 19.49 ?  63  VAL   B HG21 1 
ATOM   4890 H  HG22 . VAL   B 1 63  ? 59.642 -11.732 6.208   1.00 19.49 ?  63  VAL   B HG22 1 
ATOM   4891 H  HG23 . VAL   B 1 63  ? 59.434 -12.598 4.893   1.00 19.49 ?  63  VAL   B HG23 1 
ATOM   4892 N  N    . GLU   B 1 64  ? 55.342 -10.431 4.086   1.00 13.00 ?  64  GLU   B N    1 
ATOM   4893 C  CA   . GLU   B 1 64  ? 54.176 -9.592  3.813   1.00 12.51 ?  64  GLU   B CA   1 
ATOM   4894 C  C    . GLU   B 1 64  ? 52.998 -9.990  4.693   1.00 12.12 ?  64  GLU   B C    1 
ATOM   4895 O  O    . GLU   B 1 64  ? 52.257 -9.130  5.197   1.00 12.81 ?  64  GLU   B O    1 
ATOM   4896 C  CB   . GLU   B 1 64  ? 53.807 -9.745  2.338   1.00 12.73 ?  64  GLU   B CB   1 
ATOM   4897 C  CG   . GLU   B 1 64  ? 52.546 -9.006  1.904   1.00 12.96 ?  64  GLU   B CG   1 
ATOM   4898 C  CD   . GLU   B 1 64  ? 52.008 -9.502  0.569   1.00 13.63 ?  64  GLU   B CD   1 
ATOM   4899 O  OE1  . GLU   B 1 64  ? 52.186 -10.708 0.247   1.00 14.37 ?  64  GLU   B OE1  1 
ATOM   4900 O  OE2  . GLU   B 1 64  ? 51.390 -8.684  -0.151  1.00 14.21 -1 64  GLU   B OE2  1 
ATOM   4901 H  H    . GLU   B 1 64  ? 55.613 -10.894 3.409   1.00 15.65 ?  64  GLU   B H    1 
ATOM   4902 H  HA   . GLU   B 1 64  ? 54.397 -8.664  3.987   1.00 15.07 ?  64  GLU   B HA   1 
ATOM   4903 H  HB2  . GLU   B 1 64  ? 54.537 -9.400  1.799   1.00 15.33 ?  64  GLU   B HB2  1 
ATOM   4904 H  HB3  . GLU   B 1 64  ? 53.675 -10.683 2.150   1.00 15.33 ?  64  GLU   B HB3  1 
ATOM   4905 H  HG2  . GLU   B 1 64  ? 51.843 -9.132  2.568   1.00 15.60 ?  64  GLU   B HG2  1 
ATOM   4906 H  HG3  . GLU   B 1 64  ? 52.741 -8.061  1.814   1.00 15.60 ?  64  GLU   B HG3  1 
ATOM   4907 N  N    . SER   B 1 65  ? 52.812 -11.295 4.880   1.00 11.74 ?  65  SER   B N    1 
ATOM   4908 C  CA   . SER   B 1 65  ? 51.701 -11.799 5.675   1.00 12.07 ?  65  SER   B CA   1 
ATOM   4909 C  C    . SER   B 1 65  ? 51.837 -11.405 7.140   1.00 12.17 ?  65  SER   B C    1 
ATOM   4910 O  O    . SER   B 1 65  ? 50.844 -11.029 7.778   1.00 12.58 ?  65  SER   B O    1 
ATOM   4911 C  CB   . SER   B 1 65  ? 51.618 -13.318 5.538   1.00 12.24 ?  65  SER   B CB   1 
ATOM   4912 O  OG   . SER   B 1 65  ? 51.273 -13.717 4.215   1.00 12.31 ?  65  SER   B OG   1 
ATOM   4913 H  H    . SER   B 1 65  ? 53.320 -11.916 4.560   1.00 14.15 ?  65  SER   B H    1 
ATOM   4914 H  HA   . SER   B 1 65  ? 50.872 -11.421 5.336   1.00 14.54 ?  65  SER   B HA   1 
ATOM   4915 H  HB2  . SER   B 1 65  ? 52.474 -13.702 5.764   1.00 14.74 ?  65  SER   B HB2  1 
ATOM   4916 H  HB3  . SER   B 1 65  ? 50.935 -13.648 6.148   1.00 14.74 ?  65  SER   B HB3  1 
ATOM   4917 H  HG   . SER   B 1 65  ? 51.849 -13.429 3.671   1.00 14.83 ?  65  SER   B HG   1 
ATOM   4918 N  N    . ASP   B 1 66  ? 53.045 -11.515 7.702   1.00 12.79 ?  66  ASP   B N    1 
ATOM   4919 C  CA   . ASP   B 1 66  ? 53.242 -11.122 9.095   1.00 12.85 ?  66  ASP   B CA   1 
ATOM   4920 C  C    . ASP   B 1 66  ? 52.929 -9.644  9.299   1.00 12.91 ?  66  ASP   B C    1 
ATOM   4921 O  O    . ASP   B 1 66  ? 52.345 -9.260  10.319  1.00 13.50 ?  66  ASP   B O    1 
ATOM   4922 C  CB   . ASP   B 1 66  ? 54.672 -11.433 9.538   1.00 14.14 ?  66  ASP   B CB   1 
ATOM   4923 C  CG   . ASP   B 1 66  ? 54.932 -12.926 9.704   1.00 16.22 ?  66  ASP   B CG   1 
ATOM   4924 O  OD1  . ASP   B 1 66  ? 53.977 -13.732 9.638   1.00 16.88 ?  66  ASP   B OD1  1 
ATOM   4925 O  OD2  . ASP   B 1 66  ? 56.109 -13.294 9.909   1.00 18.79 -1 66  ASP   B OD2  1 
ATOM   4926 H  H    . ASP   B 1 66  ? 53.741 -11.822 7.309   1.00 15.40 ?  66  ASP   B H    1 
ATOM   4927 H  HA   . ASP   B 1 66  ? 52.641 -11.628 9.660   1.00 15.48 ?  66  ASP   B HA   1 
ATOM   4928 H  HB2  . ASP   B 1 66  ? 55.292 -11.097 8.871   1.00 17.02 ?  66  ASP   B HB2  1 
ATOM   4929 H  HB3  . ASP   B 1 66  ? 54.841 -10.998 10.392  1.00 17.02 ?  66  ASP   B HB3  1 
ATOM   4930 N  N    . ASP   B 1 67  ? 53.303 -8.798  8.339   1.00 12.62 ?  67  ASP   B N    1 
ATOM   4931 C  CA   . ASP   B 1 67  ? 52.957 -7.385  8.430   1.00 13.60 ?  67  ASP   B CA   1 
ATOM   4932 C  C    . ASP   B 1 67  ? 51.446 -7.173  8.341   1.00 13.57 ?  67  ASP   B C    1 
ATOM   4933 O  O    . ASP   B 1 67  ? 50.881 -6.369  9.091   1.00 14.10 ?  67  ASP   B O    1 
ATOM   4934 C  CB   . ASP   B 1 67  ? 53.684 -6.613  7.338   1.00 14.81 ?  67  ASP   B CB   1 
ATOM   4935 C  CG   . ASP   B 1 67  ? 53.263 -5.171  7.293   1.00 16.27 ?  67  ASP   B CG   1 
ATOM   4936 O  OD1  . ASP   B 1 67  ? 53.754 -4.367  8.120   1.00 17.04 ?  67  ASP   B OD1  1 
ATOM   4937 O  OD2  . ASP   B 1 67  ? 52.406 -4.858  6.448   1.00 17.41 -1 67  ASP   B OD2  1 
ATOM   4938 H  H    . ASP   B 1 67  ? 53.757 -9.014  7.639   1.00 15.20 ?  67  ASP   B H    1 
ATOM   4939 H  HA   . ASP   B 1 67  ? 53.259 -7.042  9.284   1.00 16.37 ?  67  ASP   B HA   1 
ATOM   4940 H  HB2  . ASP   B 1 67  ? 54.642 -6.637  7.506   1.00 17.82 ?  67  ASP   B HB2  1 
ATOM   4941 H  HB3  . ASP   B 1 67  ? 53.494 -7.017  6.474   1.00 17.82 ?  67  ASP   B HB3  1 
ATOM   4942 N  N    . TYR   B 1 68  ? 50.768 -7.906  7.451   1.00 13.06 ?  68  TYR   B N    1 
ATOM   4943 C  CA   . TYR   B 1 68  ? 49.310 -7.825  7.379   1.00 13.61 ?  68  TYR   B CA   1 
ATOM   4944 C  C    . TYR   B 1 68  ? 48.674 -8.167  8.723   1.00 13.30 ?  68  TYR   B C    1 
ATOM   4945 O  O    . TYR   B 1 68  ? 47.746 -7.484  9.175   1.00 14.02 ?  68  TYR   B O    1 
ATOM   4946 C  CB   . TYR   B 1 68  ? 48.771 -8.757  6.286   1.00 14.59 ?  68  TYR   B CB   1 
ATOM   4947 C  CG   . TYR   B 1 68  ? 47.266 -8.906  6.351   1.00 15.83 ?  68  TYR   B CG   1 
ATOM   4948 C  CD1  . TYR   B 1 68  ? 46.678 -9.858  7.178   1.00 16.64 ?  68  TYR   B CD1  1 
ATOM   4949 C  CD2  . TYR   B 1 68  ? 46.438 -8.076  5.620   1.00 16.92 ?  68  TYR   B CD2  1 
ATOM   4950 C  CE1  . TYR   B 1 68  ? 45.313 -9.978  7.273   1.00 18.06 ?  68  TYR   B CE1  1 
ATOM   4951 C  CE2  . TYR   B 1 68  ? 45.057 -8.197  5.700   1.00 17.59 ?  68  TYR   B CE2  1 
ATOM   4952 C  CZ   . TYR   B 1 68  ? 44.514 -9.147  6.531   1.00 18.12 ?  68  TYR   B CZ   1 
ATOM   4953 O  OH   . TYR   B 1 68  ? 43.147 -9.263  6.621   1.00 19.45 ?  68  TYR   B OH   1 
ATOM   4954 H  H    . TYR   B 1 68  ? 51.125 -8.457  6.888   1.00 15.73 ?  68  TYR   B H    1 
ATOM   4955 H  HA   . TYR   B 1 68  ? 49.060 -6.922  7.151   1.00 16.39 ?  68  TYR   B HA   1 
ATOM   4956 H  HB2  . TYR   B 1 68  ? 48.997 -8.394  5.418   1.00 17.56 ?  68  TYR   B HB2  1 
ATOM   4957 H  HB3  . TYR   B 1 68  ? 49.164 -9.639  6.393   1.00 17.56 ?  68  TYR   B HB3  1 
ATOM   4958 H  HD1  . TYR   B 1 68  ? 47.217 -10.423 7.686   1.00 20.02 ?  68  TYR   B HD1  1 
ATOM   4959 H  HD2  . TYR   B 1 68  ? 46.808 -7.428  5.072   1.00 20.36 ?  68  TYR   B HD2  1 
ATOM   4960 H  HE1  . TYR   B 1 68  ? 44.932 -10.628 7.825   1.00 21.73 ?  68  TYR   B HE1  1 
ATOM   4961 H  HE2  . TYR   B 1 68  ? 44.502 -7.634  5.211   1.00 21.16 ?  68  TYR   B HE2  1 
ATOM   4962 H  HH   . TYR   B 1 68  ? 42.762 -8.704  6.117   1.00 23.40 ?  68  TYR   B HH   1 
ATOM   4963 N  N    . ILE   B 1 69  ? 49.153 -9.234  9.369   1.00 13.34 ?  69  ILE   B N    1 
ATOM   4964 C  CA   . ILE   B 1 69  ? 48.593 -9.664  10.647  1.00 13.98 ?  69  ILE   B CA   1 
ATOM   4965 C  C    . ILE   B 1 69  ? 48.849 -8.622  11.730  1.00 13.71 ?  69  ILE   B C    1 
ATOM   4966 O  O    . ILE   B 1 69  ? 47.978 -8.343  12.559  1.00 13.96 ?  69  ILE   B O    1 
ATOM   4967 C  CB   . ILE   B 1 69  ? 49.170 -11.041 11.033  1.00 14.82 ?  69  ILE   B CB   1 
ATOM   4968 C  CG1  . ILE   B 1 69  ? 48.638 -12.145 10.108  1.00 14.96 ?  69  ILE   B CG1  1 
ATOM   4969 C  CG2  . ILE   B 1 69  ? 48.894 -11.354 12.499  1.00 15.64 ?  69  ILE   B CG2  1 
ATOM   4970 C  CD1  . ILE   B 1 69  ? 47.163 -12.456 10.270  1.00 15.42 ?  69  ILE   B CD1  1 
ATOM   4971 H  H    . ILE   B 1 69  ? 49.801 -9.720  9.091   1.00 16.07 ?  69  ILE   B H    1 
ATOM   4972 H  HA   . ILE   B 1 69  ? 47.634 -9.760  10.553  1.00 16.83 ?  69  ILE   B HA   1 
ATOM   4973 H  HB   . ILE   B 1 69  ? 50.133 -10.997 10.920  1.00 17.84 ?  69  ILE   B HB   1 
ATOM   4974 H  HG12 . ILE   B 1 69  ? 48.786 -11.870 9.189   1.00 18.01 ?  69  ILE   B HG12 1 
ATOM   4975 H  HG13 . ILE   B 1 69  ? 49.136 -12.959 10.287  1.00 18.01 ?  69  ILE   B HG13 1 
ATOM   4976 H  HG21 . ILE   B 1 69  ? 49.023 -12.305 12.644  1.00 18.82 ?  69  ILE   B HG21 1 
ATOM   4977 H  HG22 . ILE   B 1 69  ? 49.513 -10.854 13.056  1.00 18.82 ?  69  ILE   B HG22 1 
ATOM   4978 H  HG23 . ILE   B 1 69  ? 47.981 -11.110 12.710  1.00 18.82 ?  69  ILE   B HG23 1 
ATOM   4979 H  HD11 . ILE   B 1 69  ? 46.931 -13.173 9.663   1.00 18.56 ?  69  ILE   B HD11 1 
ATOM   4980 H  HD12 . ILE   B 1 69  ? 46.997 -12.730 11.185  1.00 18.56 ?  69  ILE   B HD12 1 
ATOM   4981 H  HD13 . ILE   B 1 69  ? 46.648 -11.663 10.062  1.00 18.56 ?  69  ILE   B HD13 1 
ATOM   4982 N  N    . ALA   B 1 70  ? 50.047 -8.043  11.759  1.00 13.78 ?  70  ALA   B N    1 
ATOM   4983 C  CA   . ALA   B 1 70  ? 50.332 -7.006  12.746  1.00 13.55 ?  70  ALA   B CA   1 
ATOM   4984 C  C    . ALA   B 1 70  ? 49.341 -5.856  12.629  1.00 13.72 ?  70  ALA   B C    1 
ATOM   4985 O  O    . ALA   B 1 70  ? 48.901 -5.301  13.642  1.00 14.26 ?  70  ALA   B O    1 
ATOM   4986 C  CB   . ALA   B 1 70  ? 51.767 -6.508  12.580  1.00 14.25 ?  70  ALA   B CB   1 
ATOM   4987 H  H    . ALA   B 1 70  ? 50.693 -8.233  11.235  1.00 16.59 ?  70  ALA   B H    1 
ATOM   4988 H  HA   . ALA   B 1 70  ? 50.248 -7.383  13.636  1.00 16.32 ?  70  ALA   B HA   1 
ATOM   4989 H  HB1  . ALA   B 1 70  ? 51.951 -5.844  13.263  1.00 17.16 ?  70  ALA   B HB1  1 
ATOM   4990 H  HB2  . ALA   B 1 70  ? 52.374 -7.259  12.677  1.00 17.16 ?  70  ALA   B HB2  1 
ATOM   4991 H  HB3  . ALA   B 1 70  ? 51.865 -6.115  11.699  1.00 17.16 ?  70  ALA   B HB3  1 
ATOM   4992 N  N    . THR   B 1 71  ? 48.967 -5.493  11.402  1.00 14.29 ?  71  THR   B N    1 
ATOM   4993 C  CA   . THR   B 1 71  ? 48.082 -4.353  11.187  1.00 15.26 ?  71  THR   B CA   1 
ATOM   4994 C  C    . THR   B 1 71  ? 46.613 -4.709  11.391  1.00 15.79 ?  71  THR   B C    1 
ATOM   4995 O  O    . THR   B 1 71  ? 45.839 -3.886  11.901  1.00 17.33 ?  71  THR   B O    1 
ATOM   4996 C  CB   . THR   B 1 71  ? 48.306 -3.790  9.782   1.00 17.09 ?  71  THR   B CB   1 
ATOM   4997 O  OG1  . THR   B 1 71  ? 49.636 -3.267  9.684   1.00 18.93 ?  71  THR   B OG1  1 
ATOM   4998 C  CG2  . THR   B 1 71  ? 47.301 -2.689  9.459   1.00 17.87 ?  71  THR   B CG2  1 
ATOM   4999 H  H    . THR   B 1 71  ? 49.214 -5.888  10.682  1.00 17.20 ?  71  THR   B H    1 
ATOM   5000 H  HA   . THR   B 1 71  ? 48.303 -3.658  11.821  1.00 18.37 ?  71  THR   B HA   1 
ATOM   5001 H  HB   . THR   B 1 71  ? 48.198 -4.498  9.127   1.00 20.56 ?  71  THR   B HB   1 
ATOM   5002 H  HG1  . THR   B 1 71  ? 49.766 -2.946  8.915   1.00 22.78 ?  71  THR   B HG1  1 
ATOM   5003 H  HG21 . THR   B 1 71  ? 47.608 -2.173  8.694   1.00 21.51 ?  71  THR   B HG21 1 
ATOM   5004 H  HG22 . THR   B 1 71  ? 46.436 -3.073  9.249   1.00 21.51 ?  71  THR   B HG22 1 
ATOM   5005 H  HG23 . THR   B 1 71  ? 47.207 -2.091  10.218  1.00 21.51 ?  71  THR   B HG23 1 
ATOM   5006 N  N    . ASN   B 1 72  ? 46.211 -5.924  11.003  1.00 15.39 ?  72  ASN   B N    1 
ATOM   5007 C  CA   . ASN   B 1 72  ? 44.805 -6.283  10.876  1.00 15.86 ?  72  ASN   B CA   1 
ATOM   5008 C  C    . ASN   B 1 72  ? 44.333 -7.379  11.819  1.00 16.40 ?  72  ASN   B C    1 
ATOM   5009 O  O    . ASN   B 1 72  ? 43.117 -7.542  11.981  1.00 17.66 ?  72  ASN   B O    1 
ATOM   5010 C  CB   . ASN   B 1 72  ? 44.500 -6.711  9.432   1.00 16.73 ?  72  ASN   B CB   1 
ATOM   5011 C  CG   . ASN   B 1 72  ? 44.780 -5.607  8.439   1.00 17.77 ?  72  ASN   B CG   1 
ATOM   5012 O  OD1  . ASN   B 1 72  ? 45.791 -5.620  7.735   1.00 18.72 ?  72  ASN   B OD1  1 
ATOM   5013 N  ND2  . ASN   B 1 72  ? 43.907 -4.620  8.408   1.00 19.03 ?  72  ASN   B ND2  1 
ATOM   5014 H  H    . ASN   B 1 72  ? 46.750 -6.572  10.799  1.00 18.53 ?  72  ASN   B H    1 
ATOM   5015 H  HA   . ASN   B 1 72  ? 44.273 -5.497  11.058  1.00 19.09 ?  72  ASN   B HA   1 
ATOM   5016 H  HB2  . ASN   B 1 72  ? 45.057 -7.474  9.201   1.00 20.13 ?  72  ASN   B HB2  1 
ATOM   5017 H  HB3  . ASN   B 1 72  ? 43.563 -6.953  9.362   1.00 20.13 ?  72  ASN   B HB3  1 
ATOM   5018 H  HD21 . ASN   B 1 72  ? 44.019 -3.967  7.861   1.00 22.90 ?  72  ASN   B HD21 1 
ATOM   5019 H  HD22 . ASN   B 1 72  ? 43.214 -4.640  8.918   1.00 22.90 ?  72  ASN   B HD22 1 
ATOM   5020 N  N    . GLY   B 1 73  ? 45.236 -8.128  12.443  1.00 15.90 ?  73  GLY   B N    1 
ATOM   5021 C  CA   . GLY   B 1 73  ? 44.841 -9.268  13.234  1.00 15.23 ?  73  GLY   B CA   1 
ATOM   5022 C  C    . GLY   B 1 73  ? 44.474 -10.452 12.366  1.00 14.13 ?  73  GLY   B C    1 
ATOM   5023 O  O    . GLY   B 1 73  ? 44.465 -10.376 11.135  1.00 14.11 ?  73  GLY   B O    1 
ATOM   5024 H  H    . GLY   B 1 73  ? 46.085 -7.992  12.420  1.00 19.14 ?  73  GLY   B H    1 
ATOM   5025 H  HA2  . GLY   B 1 73  ? 45.572 -9.525  13.820  1.00 18.33 ?  73  GLY   B HA2  1 
ATOM   5026 H  HA3  . GLY   B 1 73  ? 44.076 -9.033  13.785  1.00 18.33 ?  73  GLY   B HA3  1 
ATOM   5027 N  N    . PRO   B 1 74  ? 44.162 -11.573 13.005  1.00 14.09 ?  74  PRO   B N    1 
ATOM   5028 C  CA   . PRO   B 1 74  ? 43.908 -12.805 12.260  1.00 13.68 ?  74  PRO   B CA   1 
ATOM   5029 C  C    . PRO   B 1 74  ? 42.607 -12.751 11.468  1.00 13.37 ?  74  PRO   B C    1 
ATOM   5030 O  O    . PRO   B 1 74  ? 41.663 -12.014 11.781  1.00 14.28 ?  74  PRO   B O    1 
ATOM   5031 C  CB   . PRO   B 1 74  ? 43.838 -13.869 13.362  1.00 14.79 ?  74  PRO   B CB   1 
ATOM   5032 C  CG   . PRO   B 1 74  ? 43.410 -13.122 14.575  1.00 16.55 ?  74  PRO   B CG   1 
ATOM   5033 C  CD   . PRO   B 1 74  ? 44.057 -11.773 14.460  1.00 15.73 ?  74  PRO   B CD   1 
ATOM   5034 H  HA   . PRO   B 1 74  ? 44.654 -12.998 11.662  1.00 16.47 ?  74  PRO   B HA   1 
ATOM   5035 H  HB2  . PRO   B 1 74  ? 43.184 -14.542 13.121  1.00 17.81 ?  74  PRO   B HB2  1 
ATOM   5036 H  HB3  . PRO   B 1 74  ? 44.714 -14.266 13.490  1.00 17.81 ?  74  PRO   B HB3  1 
ATOM   5037 H  HG2  . PRO   B 1 74  ? 42.444 -13.039 14.583  1.00 19.92 ?  74  PRO   B HG2  1 
ATOM   5038 H  HG3  . PRO   B 1 74  ? 43.723 -13.584 15.367  1.00 19.92 ?  74  PRO   B HG3  1 
ATOM   5039 H  HD2  . PRO   B 1 74  ? 43.490 -11.090 14.860  1.00 18.93 ?  74  PRO   B HD2  1 
ATOM   5040 H  HD3  . PRO   B 1 74  ? 44.939 -11.780 14.863  1.00 18.93 ?  74  PRO   B HD3  1 
ATOM   5041 N  N    . LEU   B 1 75  ? 42.578 -13.571 10.420  1.00 12.56 ?  75  LEU   B N    1 
ATOM   5042 C  CA   . LEU   B 1 75  ? 41.367 -13.788 9.653   1.00 12.45 ?  75  LEU   B CA   1 
ATOM   5043 C  C    . LEU   B 1 75  ? 40.396 -14.651 10.455  1.00 12.84 ?  75  LEU   B C    1 
ATOM   5044 O  O    . LEU   B 1 75  ? 40.735 -15.202 11.504  1.00 13.95 ?  75  LEU   B O    1 
ATOM   5045 C  CB   . LEU   B 1 75  ? 41.693 -14.494 8.335   1.00 12.89 ?  75  LEU   B CB   1 
ATOM   5046 C  CG   . LEU   B 1 75  ? 42.545 -13.748 7.302   1.00 14.59 ?  75  LEU   B CG   1 
ATOM   5047 C  CD1  . LEU   B 1 75  ? 42.705 -14.567 6.022   1.00 16.26 ?  75  LEU   B CD1  1 
ATOM   5048 C  CD2  . LEU   B 1 75  ? 41.974 -12.392 6.984   1.00 17.88 ?  75  LEU   B CD2  1 
ATOM   5049 H  H    . LEU   B 1 75  ? 43.258 -14.016 10.131  1.00 15.12 ?  75  LEU   B H    1 
ATOM   5050 H  HA   . LEU   B 1 75  ? 40.941 -12.944 9.457   1.00 14.99 ?  75  LEU   B HA   1 
ATOM   5051 H  HB2  . LEU   B 1 75  ? 42.165 -15.318 8.541   1.00 15.53 ?  75  LEU   B HB2  1 
ATOM   5052 H  HB3  . LEU   B 1 75  ? 40.856 -14.715 7.895   1.00 15.53 ?  75  LEU   B HB3  1 
ATOM   5053 H  HG   . LEU   B 1 75  ? 43.431 -13.615 7.671   1.00 17.57 ?  75  LEU   B HG   1 
ATOM   5054 H  HD11 . LEU   B 1 75  ? 43.254 -14.066 5.392   1.00 19.57 ?  75  LEU   B HD11 1 
ATOM   5055 H  HD12 . LEU   B 1 75  ? 43.139 -15.409 6.233   1.00 19.57 ?  75  LEU   B HD12 1 
ATOM   5056 H  HD13 . LEU   B 1 75  ? 41.832 -14.731 5.636   1.00 19.57 ?  75  LEU   B HD13 1 
ATOM   5057 H  HD21 . LEU   B 1 75  ? 42.488 -11.991 6.266   1.00 21.51 ?  75  LEU   B HD21 1 
ATOM   5058 H  HD22 . LEU   B 1 75  ? 41.049 -12.495 6.713   1.00 21.51 ?  75  LEU   B HD22 1 
ATOM   5059 H  HD23 . LEU   B 1 75  ? 42.026 -11.835 7.778   1.00 21.51 ?  75  LEU   B HD23 1 
ATOM   5060 N  N    . LYS   B 1 76  ? 39.167 -14.751 9.950   1.00 14.39 ?  76  LYS   B N    1 
ATOM   5061 C  CA   . LYS   B 1 76  ? 38.184 -15.713 10.431  1.00 15.62 ?  76  LYS   B CA   1 
ATOM   5062 C  C    . LYS   B 1 76  ? 38.269 -16.985 9.590   1.00 14.19 ?  76  LYS   B C    1 
ATOM   5063 O  O    . LYS   B 1 76  ? 38.534 -16.928 8.390   1.00 13.61 ?  76  LYS   B O    1 
ATOM   5064 C  CB   . LYS   B 1 76  ? 36.763 -15.144 10.266  1.00 18.16 ?  76  LYS   B CB   1 
ATOM   5065 C  CG   . LYS   B 1 76  ? 36.493 -13.748 10.865  1.00 20.42 ?  76  LYS   B CG   1 
ATOM   5066 C  CD   . LYS   B 1 76  ? 35.084 -13.219 10.506  1.00 21.70 ?  76  LYS   B CD   1 
ATOM   5067 C  CE   . LYS   B 1 76  ? 34.813 -11.848 11.116  1.00 23.54 ?  76  LYS   B CE   1 
ATOM   5068 N  NZ   . LYS   B 1 76  ? 33.505 -11.274 10.685  1.00 24.00 ?  76  LYS   B NZ   1 
ATOM   5069 H  H    . LYS   B 1 76  ? 38.877 -14.260 9.313   1.00 17.32 ?  76  LYS   B H    1 
ATOM   5070 H  HA   . LYS   B 1 76  ? 38.339 -15.933 11.363  1.00 18.80 ?  76  LYS   B HA   1 
ATOM   5071 H  HB2  . LYS   B 1 76  ? 36.568 -15.091 9.316   1.00 21.84 ?  76  LYS   B HB2  1 
ATOM   5072 H  HB3  . LYS   B 1 76  ? 36.139 -15.759 10.684  1.00 21.84 ?  76  LYS   B HB3  1 
ATOM   5073 H  HG2  . LYS   B 1 76  ? 36.561 -13.798 11.831  1.00 24.56 ?  76  LYS   B HG2  1 
ATOM   5074 H  HG3  . LYS   B 1 76  ? 37.149 -13.121 10.518  1.00 24.56 ?  76  LYS   B HG3  1 
ATOM   5075 H  HD2  . LYS   B 1 76  ? 35.009 -13.140 9.541   1.00 26.09 ?  76  LYS   B HD2  1 
ATOM   5076 H  HD3  . LYS   B 1 76  ? 34.416 -13.836 10.843  1.00 26.09 ?  76  LYS   B HD3  1 
ATOM   5077 H  HE2  . LYS   B 1 76  ? 34.802 -11.929 12.082  1.00 28.31 ?  76  LYS   B HE2  1 
ATOM   5078 H  HE3  . LYS   B 1 76  ? 35.514 -11.236 10.841  1.00 28.31 ?  76  LYS   B HE3  1 
ATOM   5079 H  HZ1  . LYS   B 1 76  ? 33.382 -10.475 11.060  1.00 28.86 ?  76  LYS   B HZ1  1 
ATOM   5080 H  HZ2  . LYS   B 1 76  ? 33.487 -11.181 9.799   1.00 28.86 ?  76  LYS   B HZ2  1 
ATOM   5081 H  HZ3  . LYS   B 1 76  ? 32.838 -11.812 10.930  1.00 28.86 ?  76  LYS   B HZ3  1 
ATOM   5082 N  N    . VAL   B 1 77  ? 38.023 -18.140 10.218  1.00 14.43 ?  77  VAL   B N    1 
ATOM   5083 C  CA   . VAL   B 1 77  ? 37.819 -19.352 9.431   1.00 14.43 ?  77  VAL   B CA   1 
ATOM   5084 C  C    . VAL   B 1 77  ? 36.624 -19.119 8.518   1.00 13.37 ?  77  VAL   B C    1 
ATOM   5085 O  O    . VAL   B 1 77  ? 35.560 -18.668 8.966   1.00 13.57 ?  77  VAL   B O    1 
ATOM   5086 C  CB   . VAL   B 1 77  ? 37.626 -20.578 10.336  1.00 15.93 ?  77  VAL   B CB   1 
ATOM   5087 C  CG1  . VAL   B 1 77  ? 37.328 -21.808 9.490   1.00 16.90 ?  77  VAL   B CG1  1 
ATOM   5088 C  CG2  . VAL   B 1 77  ? 38.863 -20.812 11.196  1.00 17.46 ?  77  VAL   B CG2  1 
ATOM   5089 H  H    . VAL   B 1 77  ? 37.969 -18.247 11.065  1.00 17.37 ?  77  VAL   B H    1 
ATOM   5090 H  HA   . VAL   B 1 77  ? 38.593 -19.508 8.871   1.00 17.37 ?  77  VAL   B HA   1 
ATOM   5091 H  HB   . VAL   B 1 77  ? 36.867 -20.425 10.925  1.00 19.17 ?  77  VAL   B HB   1 
ATOM   5092 H  HG11 . VAL   B 1 77  ? 37.397 -22.597 10.050  1.00 20.34 ?  77  VAL   B HG11 1 
ATOM   5093 H  HG12 . VAL   B 1 77  ? 36.425 -21.739 9.133   1.00 20.34 ?  77  VAL   B HG12 1 
ATOM   5094 H  HG13 . VAL   B 1 77  ? 37.968 -21.857 8.767   1.00 20.34 ?  77  VAL   B HG13 1 
ATOM   5095 H  HG21 . VAL   B 1 77  ? 38.724 -21.607 11.732  1.00 21.01 ?  77  VAL   B HG21 1 
ATOM   5096 H  HG22 . VAL   B 1 77  ? 39.628 -20.929 10.614  1.00 21.01 ?  77  VAL   B HG22 1 
ATOM   5097 H  HG23 . VAL   B 1 77  ? 38.994 -20.042 11.769  1.00 21.01 ?  77  VAL   B HG23 1 
ATOM   5098 N  N    . GLY   B 1 78  ? 36.801 -19.399 7.228   1.00 12.85 ?  78  GLY   B N    1 
ATOM   5099 C  CA   . GLY   B 1 78  ? 35.821 -19.073 6.219   1.00 12.74 ?  78  GLY   B CA   1 
ATOM   5100 C  C    . GLY   B 1 78  ? 36.060 -17.757 5.517   1.00 12.13 ?  78  GLY   B C    1 
ATOM   5101 O  O    . GLY   B 1 78  ? 35.374 -17.471 4.530   1.00 12.79 ?  78  GLY   B O    1 
ATOM   5102 H  H    . GLY   B 1 78  ? 37.499 -19.788 6.912   1.00 15.48 ?  78  GLY   B H    1 
ATOM   5103 H  HA2  . GLY   B 1 78  ? 35.810 -19.766 5.546   1.00 15.34 ?  78  GLY   B HA2  1 
ATOM   5104 H  HA3  . GLY   B 1 78  ? 34.941 -19.030 6.626   1.00 15.34 ?  78  GLY   B HA3  1 
ATOM   5105 N  N    . GLY   B 1 79  ? 37.010 -16.951 6.000   1.00 12.13 ?  79  GLY   B N    1 
ATOM   5106 C  CA   . GLY   B 1 79  ? 37.310 -15.656 5.426   1.00 11.89 ?  79  GLY   B CA   1 
ATOM   5107 C  C    . GLY   B 1 79  ? 38.545 -15.678 4.531   1.00 11.41 ?  79  GLY   B C    1 
ATOM   5108 O  O    . GLY   B 1 79  ? 39.160 -16.714 4.279   1.00 12.03 ?  79  GLY   B O    1 
ATOM   5109 H  H    . GLY   B 1 79  ? 37.514 -17.145 6.666   1.00 14.61 ?  79  GLY   B H    1 
ATOM   5110 H  HA2  . GLY   B 1 79  ? 36.555 -15.349 4.896   1.00 14.33 ?  79  GLY   B HA2  1 
ATOM   5111 H  HA3  . GLY   B 1 79  ? 37.464 -15.013 6.135   1.00 14.33 ?  79  GLY   B HA3  1 
ATOM   5112 N  N    . SER   B 1 80  ? 38.909 -14.484 4.054   1.00 11.45 ?  80  SER   B N    1 
ATOM   5113 C  CA   . SER   B 1 80  ? 40.022 -14.349 3.122   1.00 11.36 ?  80  SER   B CA   1 
ATOM   5114 C  C    . SER   B 1 80  ? 40.599 -12.941 3.184   1.00 11.35 ?  80  SER   B C    1 
ATOM   5115 O  O    . SER   B 1 80  ? 39.978 -12.007 3.700   1.00 12.45 ?  80  SER   B O    1 
ATOM   5116 C  CB   . SER   B 1 80  ? 39.584 -14.631 1.681   1.00 11.49 ?  80  SER   B CB   1 
ATOM   5117 O  OG   . SER   B 1 80  ? 38.728 -13.615 1.189   1.00 12.86 ?  80  SER   B OG   1 
ATOM   5118 H  H    . SER   B 1 80  ? 38.529 -13.739 4.253   1.00 13.80 ?  80  SER   B H    1 
ATOM   5119 H  HA   . SER   B 1 80  ? 40.711 -14.979 3.364   1.00 13.69 ?  80  SER   B HA   1 
ATOM   5120 H  HB2  . SER   B 1 80  ? 40.366 -14.674 1.110   1.00 13.85 ?  80  SER   B HB2  1 
ATOM   5121 H  HB3  . SER   B 1 80  ? 39.108 -15.476 1.652   1.00 13.85 ?  80  SER   B HB3  1 
ATOM   5122 H  HG   . SER   B 1 80  ? 38.034 -13.566 1.666   1.00 15.49 ?  80  SER   B HG   1 
ATOM   5123 N  N    . CYS   B 1 81  ? 41.784 -12.795 2.595   1.00 11.10 ?  81  CYS   B N    1 
ATOM   5124 C  CA   . CYS   B 1 81  ? 42.329 -11.483 2.283   1.00 11.20 ?  81  CYS   B CA   1 
ATOM   5125 C  C    . CYS   B 1 81  ? 43.101 -11.565 0.974   1.00 10.42 ?  81  CYS   B C    1 
ATOM   5126 O  O    . CYS   B 1 81  ? 43.609 -12.627 0.594   1.00 11.34 ?  81  CYS   B O    1 
ATOM   5127 C  CB   . CYS   B 1 81  ? 43.226 -10.929 3.403   1.00 11.87 ?  81  CYS   B CB   1 
ATOM   5128 S  SG   . CYS   B 1 81  ? 44.746 -11.865 3.652   1.00 12.46 ?  81  CYS   B SG   1 
ATOM   5129 H  H    . CYS   B 1 81  ? 42.298 -13.449 2.359   1.00 13.37 ?  81  CYS   B H    1 
ATOM   5130 H  HA   . CYS   B 1 81  ? 41.593 -10.860 2.161   1.00 13.49 ?  81  CYS   B HA   1 
ATOM   5131 H  HB2  . CYS   B 1 81  ? 43.472 -10.016 3.186   1.00 14.30 ?  81  CYS   B HB2  1 
ATOM   5132 H  HB3  . CYS   B 1 81  ? 42.726 -10.940 4.238   1.00 14.30 ?  81  CYS   B HB3  1 
ATOM   5133 H  HG   . CYS   B 1 81  ? 45.375 -11.367 4.544   1.00 15.01 ?  81  CYS   B HG   1 
ATOM   5134 N  N    . VAL   B 1 82  ? 43.198 -10.419 0.300   1.00 10.92 ?  82  VAL   B N    1 
ATOM   5135 C  CA   . VAL   B 1 82  ? 43.960 -10.294 -0.938  1.00 11.10 ?  82  VAL   B CA   1 
ATOM   5136 C  C    . VAL   B 1 82  ? 45.303 -9.656  -0.622  1.00 11.34 ?  82  VAL   B C    1 
ATOM   5137 O  O    . VAL   B 1 82  ? 45.356 -8.541  -0.087  1.00 12.32 ?  82  VAL   B O    1 
ATOM   5138 C  CB   . VAL   B 1 82  ? 43.212 -9.452  -1.981  1.00 12.18 ?  82  VAL   B CB   1 
ATOM   5139 C  CG1  . VAL   B 1 82  ? 44.056 -9.304  -3.243  1.00 13.70 ?  82  VAL   B CG1  1 
ATOM   5140 C  CG2  . VAL   B 1 82  ? 41.857 -10.048 -2.296  1.00 12.90 ?  82  VAL   B CG2  1 
ATOM   5141 H  H    . VAL   B 1 82  ? 42.818 -9.682  0.546   1.00 13.16 ?  82  VAL   B H    1 
ATOM   5142 H  HA   . VAL   B 1 82  ? 44.117 -11.173 -1.311  1.00 13.37 ?  82  VAL   B HA   1 
ATOM   5143 H  HB   . VAL   B 1 82  ? 43.062 -8.565  -1.619  1.00 14.67 ?  82  VAL   B HB   1 
ATOM   5144 H  HG11 . VAL   B 1 82  ? 43.494 -8.984  -3.966  1.00 16.50 ?  82  VAL   B HG11 1 
ATOM   5145 H  HG12 . VAL   B 1 82  ? 44.768 -8.660  -3.075  1.00 16.50 ?  82  VAL   B HG12 1 
ATOM   5146 H  HG13 . VAL   B 1 82  ? 44.437 -10.163 -3.474  1.00 16.50 ?  82  VAL   B HG13 1 
ATOM   5147 H  HG21 . VAL   B 1 82  ? 41.427 -9.517  -2.986  1.00 15.53 ?  82  VAL   B HG21 1 
ATOM   5148 H  HG22 . VAL   B 1 82  ? 41.977 -10.960 -2.612  1.00 15.53 ?  82  VAL   B HG22 1 
ATOM   5149 H  HG23 . VAL   B 1 82  ? 41.314 -10.048 -1.493  1.00 15.53 ?  82  VAL   B HG23 1 
ATOM   5150 N  N    . LEU   B 1 83  ? 46.380 -10.344 -0.986  1.00 11.01 ?  83  LEU   B N    1 
ATOM   5151 C  CA   . LEU   B 1 83  ? 47.740 -9.831  -0.868  1.00 11.12 ?  83  LEU   B CA   1 
ATOM   5152 C  C    . LEU   B 1 83  ? 48.441 -9.972  -2.219  1.00 11.17 ?  83  LEU   B C    1 
ATOM   5153 O  O    . LEU   B 1 83  ? 47.837 -10.384 -3.218  1.00 11.13 ?  83  LEU   B O    1 
ATOM   5154 C  CB   . LEU   B 1 83  ? 48.494 -10.497 0.292   1.00 11.41 ?  83  LEU   B CB   1 
ATOM   5155 C  CG   . LEU   B 1 83  ? 47.979 -10.140 1.691   1.00 12.68 ?  83  LEU   B CG   1 
ATOM   5156 C  CD1  . LEU   B 1 83  ? 48.603 -11.009 2.762   1.00 13.59 ?  83  LEU   B CD1  1 
ATOM   5157 C  CD2  . LEU   B 1 83  ? 48.193 -8.660  2.014   1.00 13.51 ?  83  LEU   B CD2  1 
ATOM   5158 H  H    . LEU   B 1 83  ? 46.341 -11.138 -1.319  1.00 13.26 ?  83  LEU   B H    1 
ATOM   5159 H  HA   . LEU   B 1 83  ? 47.685 -8.886  -0.674  1.00 13.40 ?  83  LEU   B HA   1 
ATOM   5160 H  HB2  . LEU   B 1 83  ? 48.429 -11.455 0.194   1.00 13.74 ?  83  LEU   B HB2  1 
ATOM   5161 H  HB3  . LEU   B 1 83  ? 49.423 -10.223 0.246   1.00 13.74 ?  83  LEU   B HB3  1 
ATOM   5162 H  HG   . LEU   B 1 83  ? 47.025 -10.299 1.709   1.00 15.28 ?  83  LEU   B HG   1 
ATOM   5163 H  HD11 . LEU   B 1 83  ? 48.240 -10.754 3.626   1.00 16.37 ?  83  LEU   B HD11 1 
ATOM   5164 H  HD12 . LEU   B 1 83  ? 48.385 -11.938 2.577   1.00 16.37 ?  83  LEU   B HD12 1 
ATOM   5165 H  HD13 . LEU   B 1 83  ? 49.562 -10.886 2.755   1.00 16.37 ?  83  LEU   B HD13 1 
ATOM   5166 H  HD21 . LEU   B 1 83  ? 47.975 -8.508  2.946   1.00 16.27 ?  83  LEU   B HD21 1 
ATOM   5167 H  HD22 . LEU   B 1 83  ? 49.118 -8.430  1.846   1.00 16.27 ?  83  LEU   B HD22 1 
ATOM   5168 H  HD23 . LEU   B 1 83  ? 47.611 -8.126  1.448   1.00 16.27 ?  83  LEU   B HD23 1 
ATOM   5169 N  N    . SER   B 1 84  ? 49.717 -9.596  -2.269  1.00 11.98 ?  84  SER   B N    1 
ATOM   5170 C  CA   . SER   B 1 84  ? 50.450 -9.707  -3.519  1.00 12.11 ?  84  SER   B CA   1 
ATOM   5171 C  C    . SER   B 1 84  ? 50.600 -11.165 -3.941  1.00 11.53 ?  84  SER   B C    1 
ATOM   5172 O  O    . SER   B 1 84  ? 50.719 -12.067 -3.111  1.00 11.29 ?  84  SER   B O    1 
ATOM   5173 C  CB   . SER   B 1 84  ? 51.847 -9.110  -3.364  1.00 13.83 ?  84  SER   B CB   1 
ATOM   5174 O  OG   . SER   B 1 84  ? 52.595 -9.321  -4.545  1.00 15.36 ?  84  SER   B OG   1 
ATOM   5175 H  H    . SER   B 1 84  ? 50.164 -9.270  -1.608  1.00 14.44 ?  84  SER   B H    1 
ATOM   5176 H  HA   . SER   B 1 84  ? 49.983 -9.225  -4.218  1.00 14.59 ?  84  SER   B HA   1 
ATOM   5177 H  HB2  . SER   B 1 84  ? 51.771 -8.155  -3.194  1.00 16.66 ?  84  SER   B HB2  1 
ATOM   5178 H  HB3  . SER   B 1 84  ? 52.301 -9.542  -2.624  1.00 16.66 ?  84  SER   B HB3  1 
ATOM   5179 H  HG   . SER   B 1 84  ? 53.363 -8.981  -4.466  1.00 18.48 ?  84  SER   B HG   1 
ATOM   5180 N  N    . GLY   B 1 85  ? 50.667 -11.380 -5.250  1.00 12.53 ?  85  GLY   B N    1 
ATOM   5181 C  CA   . GLY   B 1 85  ? 51.012 -12.671 -5.797  1.00 12.84 ?  85  GLY   B CA   1 
ATOM   5182 C  C    . GLY   B 1 85  ? 52.485 -12.874 -6.094  1.00 12.12 ?  85  GLY   B C    1 
ATOM   5183 O  O    . GLY   B 1 85  ? 52.861 -13.955 -6.552  1.00 12.57 ?  85  GLY   B O    1 
ATOM   5184 H  H    . GLY   B 1 85  ? 50.520 -10.778 -5.844  1.00 15.10 ?  85  GLY   B H    1 
ATOM   5185 H  HA2  . GLY   B 1 85  ? 50.737 -13.360 -5.173  1.00 15.46 ?  85  GLY   B HA2  1 
ATOM   5186 H  HA3  . GLY   B 1 85  ? 50.524 -12.803 -6.621  1.00 15.46 ?  85  GLY   B HA3  1 
ATOM   5187 N  N    . HIS   B 1 86  ? 53.338 -11.878 -5.862  1.00 12.30 ?  86  HIS   B N    1 
ATOM   5188 C  CA   . HIS   B 1 86  ? 54.800 -12.049 -5.949  1.00 12.49 ?  86  HIS   B CA   1 
ATOM   5189 C  C    . HIS   B 1 86  ? 55.168 -12.559 -7.341  1.00 12.68 ?  86  HIS   B C    1 
ATOM   5190 O  O    . HIS   B 1 86  ? 54.774 -11.943 -8.344  1.00 13.68 ?  86  HIS   B O    1 
ATOM   5191 C  CB   . HIS   B 1 86  ? 55.286 -12.895 -4.774  1.00 12.67 ?  86  HIS   B CB   1 
ATOM   5192 C  CG   . HIS   B 1 86  ? 54.979 -12.286 -3.447  1.00 12.72 ?  86  HIS   B CG   1 
ATOM   5193 N  ND1  . HIS   B 1 86  ? 55.811 -11.374 -2.832  1.00 14.23 ?  86  HIS   B ND1  1 
ATOM   5194 C  CD2  . HIS   B 1 86  ? 53.909 -12.433 -2.633  1.00 13.04 ?  86  HIS   B CD2  1 
ATOM   5195 C  CE1  . HIS   B 1 86  ? 55.258 -10.982 -1.698  1.00 14.28 ?  86  HIS   B CE1  1 
ATOM   5196 N  NE2  . HIS   B 1 86  ? 54.103 -11.607 -1.556  1.00 13.43 ?  86  HIS   B NE2  1 
ATOM   5197 H  H    . HIS   B 1 86  ? 53.099 -11.082 -5.648  1.00 14.81 ?  86  HIS   B H    1 
ATOM   5198 H  HA   . HIS   B 1 86  ? 55.209 -11.179 -5.852  1.00 15.05 ?  86  HIS   B HA   1 
ATOM   5199 H  HB2  . HIS   B 1 86  ? 54.865 -13.767 -4.812  1.00 15.26 ?  86  HIS   B HB2  1 
ATOM   5200 H  HB3  . HIS   B 1 86  ? 56.253 -12.995 -4.837  1.00 15.26 ?  86  HIS   B HB3  1 
ATOM   5201 H  HD2  . HIS   B 1 86  ? 53.165 -12.977 -2.787  1.00 15.70 ?  86  HIS   B HD2  1 
ATOM   5202 H  HE1  . HIS   B 1 86  ? 55.629 -10.383 -1.093  1.00 17.20 ?  86  HIS   B HE1  1 
ATOM   5203 H  HE2  . HIS   B 1 86  ? 53.568 -11.526 -0.887  1.00 16.17 ?  86  HIS   B HE2  1 
ATOM   5204 N  N    . ASN   B 1 87  ? 55.937 -13.641 -7.454  1.00 13.08 ?  87  ASN   B N    1 
ATOM   5205 C  CA   . ASN   B 1 87  ? 56.328 -14.211 -8.733  1.00 13.42 ?  87  ASN   B CA   1 
ATOM   5206 C  C    . ASN   B 1 87  ? 55.342 -15.256 -9.235  1.00 13.10 ?  87  ASN   B C    1 
ATOM   5207 O  O    . ASN   B 1 87  ? 55.654 -15.968 -10.196 1.00 14.97 ?  87  ASN   B O    1 
ATOM   5208 C  CB   . ASN   B 1 87  ? 57.721 -14.838 -8.620  1.00 15.27 ?  87  ASN   B CB   1 
ATOM   5209 C  CG   . ASN   B 1 87  ? 57.777 -15.962 -7.590  1.00 16.34 ?  87  ASN   B CG   1 
ATOM   5210 O  OD1  . ASN   B 1 87  ? 57.145 -15.891 -6.531  1.00 15.55 ?  87  ASN   B OD1  1 
ATOM   5211 N  ND2  . ASN   B 1 87  ? 58.516 -17.024 -7.915  1.00 18.51 ?  87  ASN   B ND2  1 
ATOM   5212 H  H    . ASN   B 1 87  ? 56.242 -14.083 -6.780  1.00 15.75 ?  87  ASN   B H    1 
ATOM   5213 H  HA   . ASN   B 1 87  ? 56.366 -13.504 -9.390  1.00 16.17 ?  87  ASN   B HA   1 
ATOM   5214 H  HB2  . ASN   B 1 87  ? 57.970 -15.204 -9.484  1.00 18.38 ?  87  ASN   B HB2  1 
ATOM   5215 H  HB3  . ASN   B 1 87  ? 58.347 -14.153 -8.352  1.00 18.38 ?  87  ASN   B HB3  1 
ATOM   5216 H  HD21 . ASN   B 1 87  ? 58.580 -17.682 -7.371  1.00 22.27 ?  87  ASN   B HD21 1 
ATOM   5217 H  HD22 . ASN   B 1 87  ? 58.934 -17.043 -8.669  1.00 22.27 ?  87  ASN   B HD22 1 
ATOM   5218 N  N    . LEU   B 1 88  ? 54.165 -15.361 -8.609  1.00 12.25 ?  88  LEU   B N    1 
ATOM   5219 C  CA   . LEU   B 1 88  ? 53.183 -16.392 -8.932  1.00 12.34 ?  88  LEU   B CA   1 
ATOM   5220 C  C    . LEU   B 1 88  ? 51.948 -15.877 -9.653  1.00 12.19 ?  88  LEU   B C    1 
ATOM   5221 O  O    . LEU   B 1 88  ? 51.341 -16.627 -10.427 1.00 13.74 ?  88  LEU   B O    1 
ATOM   5222 C  CB   . LEU   B 1 88  ? 52.719 -17.076 -7.643  1.00 13.24 ?  88  LEU   B CB   1 
ATOM   5223 C  CG   . LEU   B 1 88  ? 53.848 -17.713 -6.844  1.00 15.52 ?  88  LEU   B CG   1 
ATOM   5224 C  CD1  . LEU   B 1 88  ? 53.346 -18.100 -5.464  1.00 17.18 ?  88  LEU   B CD1  1 
ATOM   5225 C  CD2  . LEU   B 1 88  ? 54.396 -18.915 -7.586  1.00 18.69 ?  88  LEU   B CD2  1 
ATOM   5226 H  H    . LEU   B 1 88  ? 53.911 -14.838 -7.968  1.00 14.76 ?  88  LEU   B H    1 
ATOM   5227 H  HA   . LEU   B 1 88  ? 53.599 -17.058 -9.491  1.00 14.86 ?  88  LEU   B HA   1 
ATOM   5228 H  HB2  . LEU   B 1 88  ? 52.288 -16.421 -7.071  1.00 15.95 ?  88  LEU   B HB2  1 
ATOM   5229 H  HB3  . LEU   B 1 88  ? 52.088 -17.778 -7.869  1.00 15.95 ?  88  LEU   B HB3  1 
ATOM   5230 H  HG   . LEU   B 1 88  ? 54.566 -17.069 -6.732  1.00 18.68 ?  88  LEU   B HG   1 
ATOM   5231 H  HD11 . LEU   B 1 88  ? 53.998 -18.680 -5.040  1.00 20.67 ?  88  LEU   B HD11 1 
ATOM   5232 H  HD12 . LEU   B 1 88  ? 53.223 -17.296 -4.934  1.00 20.67 ?  88  LEU   B HD12 1 
ATOM   5233 H  HD13 . LEU   B 1 88  ? 52.501 -18.566 -5.558  1.00 20.67 ?  88  LEU   B HD13 1 
ATOM   5234 H  HD21 . LEU   B 1 88  ? 55.039 -19.369 -7.020  1.00 22.49 ?  88  LEU   B HD21 1 
ATOM   5235 H  HD22 . LEU   B 1 88  ? 53.663 -19.512 -7.802  1.00 22.49 ?  88  LEU   B HD22 1 
ATOM   5236 H  HD23 . LEU   B 1 88  ? 54.828 -18.613 -8.400  1.00 22.49 ?  88  LEU   B HD23 1 
ATOM   5237 N  N    . ALA   B 1 89  ? 51.550 -14.636 -9.394  1.00 11.65 ?  89  ALA   B N    1 
ATOM   5238 C  CA   . ALA   B 1 89  ? 50.253 -14.145 -9.834  1.00 11.08 ?  89  ALA   B CA   1 
ATOM   5239 C  C    . ALA   B 1 89  ? 50.224 -12.654 -9.557  1.00 11.69 ?  89  ALA   B C    1 
ATOM   5240 O  O    . ALA   B 1 89  ? 51.068 -12.134 -8.827  1.00 12.47 ?  89  ALA   B O    1 
ATOM   5241 C  CB   . ALA   B 1 89  ? 49.122 -14.820 -9.065  1.00 11.45 ?  89  ALA   B CB   1 
ATOM   5242 H  H    . ALA   B 1 89  ? 52.008 -14.052 -8.950  1.00 14.04 ?  89  ALA   B H    1 
ATOM   5243 H  HA   . ALA   B 1 89  ? 50.136 -14.299 -10.784 1.00 13.35 ?  89  ALA   B HA   1 
ATOM   5244 H  HB1  . ALA   B 1 89  ? 48.272 -14.485 -9.398  1.00 13.79 ?  89  ALA   B HB1  1 
ATOM   5245 H  HB2  . ALA   B 1 89  ? 49.175 -15.779 -9.211  1.00 13.79 ?  89  ALA   B HB2  1 
ATOM   5246 H  HB3  . ALA   B 1 89  ? 49.215 -14.620 -8.126  1.00 13.79 ?  89  ALA   B HB3  1 
ATOM   5247 N  N    . LYS   B 1 90  ? 49.227 -11.966 -10.112 1.00 12.56 ?  90  LYS   B N    1 
ATOM   5248 C  CA   . LYS   B 1 90  ? 49.038 -10.576 -9.711  1.00 12.81 ?  90  LYS   B CA   1 
ATOM   5249 C  C    . LYS   B 1 90  ? 48.725 -10.497 -8.223  1.00 12.42 ?  90  LYS   B C    1 
ATOM   5250 O  O    . LYS   B 1 90  ? 49.364 -9.739  -7.475  1.00 13.76 ?  90  LYS   B O    1 
ATOM   5251 C  CB   . LYS   B 1 90  ? 47.955 -9.916  -10.566 1.00 14.18 ?  90  LYS   B CB   1 
ATOM   5252 C  CG   . LYS   B 1 90  ? 47.670 -8.472  -10.194 1.00 15.00 ?  90  LYS   B CG   1 
ATOM   5253 C  CD   . LYS   B 1 90  ? 48.894 -7.591  -10.264 1.00 17.99 ?  90  LYS   B CD   1 
ATOM   5254 C  CE   . LYS   B 1 90  ? 48.465 -6.159  -10.045 1.00 20.22 ?  90  LYS   B CE   1 
ATOM   5255 N  NZ   . LYS   B 1 90  ? 49.615 -5.235  -9.905  1.00 20.07 ?  90  LYS   B NZ   1 
ATOM   5256 H  H    . LYS   B 1 90  ? 48.670 -12.272 -10.694 1.00 15.13 ?  90  LYS   B H    1 
ATOM   5257 H  HA   . LYS   B 1 90  ? 49.865 -10.102 -9.862  1.00 15.42 ?  90  LYS   B HA   1 
ATOM   5258 H  HB2  . LYS   B 1 90  ? 48.242 -9.929  -11.496 1.00 17.07 ?  90  LYS   B HB2  1 
ATOM   5259 H  HB3  . LYS   B 1 90  ? 47.131 -10.417 -10.475 1.00 17.07 ?  90  LYS   B HB3  1 
ATOM   5260 H  HG2  . LYS   B 1 90  ? 47.008 -8.112  -10.805 1.00 18.05 ?  90  LYS   B HG2  1 
ATOM   5261 H  HG3  . LYS   B 1 90  ? 47.327 -8.439  -9.284  1.00 18.05 ?  90  LYS   B HG3  1 
ATOM   5262 H  HD2  . LYS   B 1 90  ? 49.523 -7.840  -9.565  1.00 21.65 ?  90  LYS   B HD2  1 
ATOM   5263 H  HD3  . LYS   B 1 90  ? 49.307 -7.669  -11.139 1.00 21.65 ?  90  LYS   B HD3  1 
ATOM   5264 H  HE2  . LYS   B 1 90  ? 47.941 -5.862  -10.807 1.00 24.32 ?  90  LYS   B HE2  1 
ATOM   5265 H  HE3  . LYS   B 1 90  ? 47.939 -6.099  -9.235  1.00 24.32 ?  90  LYS   B HE3  1 
ATOM   5266 H  HZ1  . LYS   B 1 90  ? 49.328 -4.399  -9.780  1.00 24.14 ?  90  LYS   B HZ1  1 
ATOM   5267 H  HZ2  . LYS   B 1 90  ? 50.117 -5.471  -9.208  1.00 24.14 ?  90  LYS   B HZ2  1 
ATOM   5268 H  HZ3  . LYS   B 1 90  ? 50.119 -5.255  -10.641 1.00 24.14 ?  90  LYS   B HZ3  1 
ATOM   5269 N  N    . HIS   B 1 91  ? 47.772 -11.318 -7.772  1.00 11.06 ?  91  HIS   B N    1 
ATOM   5270 C  CA   . HIS   B 1 91  ? 47.311 -11.339 -6.398  1.00 11.10 ?  91  HIS   B CA   1 
ATOM   5271 C  C    . HIS   B 1 91  ? 47.310 -12.765 -5.878  1.00 10.54 ?  91  HIS   B C    1 
ATOM   5272 O  O    . HIS   B 1 91  ? 47.075 -13.720 -6.629  1.00 10.97 ?  91  HIS   B O    1 
ATOM   5273 C  CB   . HIS   B 1 91  ? 45.860 -10.852 -6.278  1.00 12.57 ?  91  HIS   B CB   1 
ATOM   5274 C  CG   . HIS   B 1 91  ? 45.647 -9.448  -6.719  1.00 15.86 ?  91  HIS   B CG   1 
ATOM   5275 N  ND1  . HIS   B 1 91  ? 46.250 -8.373  -6.102  1.00 18.55 ?  91  HIS   B ND1  1 
ATOM   5276 C  CD2  . HIS   B 1 91  ? 44.863 -8.935  -7.691  1.00 18.19 ?  91  HIS   B CD2  1 
ATOM   5277 C  CE1  . HIS   B 1 91  ? 45.867 -7.256  -6.695  1.00 19.53 ?  91  HIS   B CE1  1 
ATOM   5278 N  NE2  . HIS   B 1 91  ? 45.019 -7.570  -7.659  1.00 19.50 ?  91  HIS   B NE2  1 
ATOM   5279 H  H    . HIS   B 1 91  ? 47.364 -11.894 -8.269  1.00 13.32 ?  91  HIS   B H    1 
ATOM   5280 H  HA   . HIS   B 1 91  ? 47.884 -10.782 -5.839  1.00 13.37 ?  91  HIS   B HA   1 
ATOM   5281 H  HB2  . HIS   B 1 91  ? 45.295 -11.418 -6.822  1.00 15.13 ?  91  HIS   B HB2  1 
ATOM   5282 H  HB3  . HIS   B 1 91  ? 45.587 -10.912 -5.347  1.00 15.13 ?  91  HIS   B HB3  1 
ATOM   5283 H  HD1  . HIS   B 1 91  ? 46.799 -8.421  -5.441  1.00 22.31 ?  91  HIS   B HD1  1 
ATOM   5284 H  HD2  . HIS   B 1 91  ? 44.328 -9.405  -8.282  1.00 21.88 ?  91  HIS   B HD2  1 
ATOM   5285 H  HE1  . HIS   B 1 91  ? 46.142 -6.393  -6.462  1.00 23.50 ?  91  HIS   B HE1  1 
ATOM   5286 N  N    . CYS   B 1 92  ? 47.509 -12.895 -4.575  1.00 10.23 ?  92  CYS   B N    1 
ATOM   5287 C  CA   . CYS   B 1 92  ? 47.206 -14.128 -3.861  1.00 10.15 ?  92  CYS   B CA   1 
ATOM   5288 C  C    . CYS   B 1 92  ? 45.985 -13.895 -2.981  1.00 9.72  ?  92  CYS   B C    1 
ATOM   5289 O  O    . CYS   B 1 92  ? 45.984 -12.996 -2.129  1.00 10.74 ?  92  CYS   B O    1 
ATOM   5290 C  CB   . CYS   B 1 92  ? 48.382 -14.586 -3.005  1.00 10.56 ?  92  CYS   B CB   1 
ATOM   5291 S  SG   . CYS   B 1 92  ? 48.028 -16.125 -2.116  1.00 10.45 ?  92  CYS   B SG   1 
ATOM   5292 H  H    . CYS   B 1 92  ? 47.845 -12.276 -4.070  1.00 12.34 ?  92  CYS   B H    1 
ATOM   5293 H  HA   . CYS   B 1 92  ? 47.009 -14.826 -4.504  1.00 12.24 ?  92  CYS   B HA   1 
ATOM   5294 H  HB2  . CYS   B 1 92  ? 49.152 -14.729 -3.570  1.00 12.73 ?  92  CYS   B HB2  1 
ATOM   5295 H  HB3  . CYS   B 1 92  ? 48.573 -13.898 -2.345  1.00 12.73 ?  92  CYS   B HB3  1 
ATOM   5296 H  HG   . CYS   B 1 92  ? 48.999 -16.437 -1.490  1.00 12.60 ?  92  CYS   B HG   1 
ATOM   5297 N  N    . LEU   B 1 93  ? 44.949 -14.698 -3.199  1.00 9.93  ?  93  LEU   B N    1 
ATOM   5298 C  CA   . LEU   B 1 93  ? 43.776 -14.715 -2.333  1.00 10.11 ?  93  LEU   B CA   1 
ATOM   5299 C  C    . LEU   B 1 93  ? 44.003 -15.779 -1.267  1.00 9.52  ?  93  LEU   B C    1 
ATOM   5300 O  O    . LEU   B 1 93  ? 43.950 -16.981 -1.558  1.00 10.27 ?  93  LEU   B O    1 
ATOM   5301 C  CB   . LEU   B 1 93  ? 42.508 -15.007 -3.136  1.00 10.49 ?  93  LEU   B CB   1 
ATOM   5302 C  CG   . LEU   B 1 93  ? 41.218 -15.035 -2.316  1.00 10.90 ?  93  LEU   B CG   1 
ATOM   5303 C  CD1  . LEU   B 1 93  ? 40.857 -13.651 -1.808  1.00 11.32 ?  93  LEU   B CD1  1 
ATOM   5304 C  CD2  . LEU   B 1 93  ? 40.081 -15.622 -3.137  1.00 11.48 ?  93  LEU   B CD2  1 
ATOM   5305 H  H    . LEU   B 1 93  ? 44.902 -15.267 -3.858  1.00 11.97 ?  93  LEU   B H    1 
ATOM   5306 H  HA   . LEU   B 1 93  ? 43.684 -13.853 -1.904  1.00 12.19 ?  93  LEU   B HA   1 
ATOM   5307 H  HB2  . LEU   B 1 93  ? 42.405 -14.313 -3.810  1.00 12.64 ?  93  LEU   B HB2  1 
ATOM   5308 H  HB3  . LEU   B 1 93  ? 42.601 -15.866 -3.565  1.00 12.64 ?  93  LEU   B HB3  1 
ATOM   5309 H  HG   . LEU   B 1 93  ? 41.347 -15.606 -1.545  1.00 13.13 ?  93  LEU   B HG   1 
ATOM   5310 H  HD11 . LEU   B 1 93  ? 40.010 -13.694 -1.342  1.00 13.63 ?  93  LEU   B HD11 1 
ATOM   5311 H  HD12 . LEU   B 1 93  ? 41.553 -13.346 -1.202  1.00 13.63 ?  93  LEU   B HD12 1 
ATOM   5312 H  HD13 . LEU   B 1 93  ? 40.790 -13.044 -2.563  1.00 13.63 ?  93  LEU   B HD13 1 
ATOM   5313 H  HD21 . LEU   B 1 93  ? 39.273 -15.630 -2.597  1.00 13.83 ?  93  LEU   B HD21 1 
ATOM   5314 H  HD22 . LEU   B 1 93  ? 39.945 -15.077 -3.926  1.00 13.83 ?  93  LEU   B HD22 1 
ATOM   5315 H  HD23 . LEU   B 1 93  ? 40.312 -16.528 -3.395  1.00 13.83 ?  93  LEU   B HD23 1 
ATOM   5316 N  N    . HIS   B 1 94  ? 44.279 -15.342 -0.042  1.00 9.63  ?  94  HIS   B N    1 
ATOM   5317 C  CA   . HIS   B 1 94  ? 44.499 -16.249 1.078   1.00 9.68  ?  94  HIS   B CA   1 
ATOM   5318 C  C    . HIS   B 1 94  ? 43.140 -16.609 1.660   1.00 9.94  ?  94  HIS   B C    1 
ATOM   5319 O  O    . HIS   B 1 94  ? 42.466 -15.738 2.212   1.00 11.42 ?  94  HIS   B O    1 
ATOM   5320 C  CB   . HIS   B 1 94  ? 45.374 -15.569 2.130   1.00 9.99  ?  94  HIS   B CB   1 
ATOM   5321 C  CG   . HIS   B 1 94  ? 46.757 -15.272 1.655   1.00 10.16 ?  94  HIS   B CG   1 
ATOM   5322 N  ND1  . HIS   B 1 94  ? 47.784 -16.187 1.740   1.00 10.43 ?  94  HIS   B ND1  1 
ATOM   5323 C  CD2  . HIS   B 1 94  ? 47.268 -14.164 1.062   1.00 10.58 ?  94  HIS   B CD2  1 
ATOM   5324 C  CE1  . HIS   B 1 94  ? 48.874 -15.641 1.231   1.00 10.52 ?  94  HIS   B CE1  1 
ATOM   5325 N  NE2  . HIS   B 1 94  ? 48.590 -14.418 0.809   1.00 10.72 ?  94  HIS   B NE2  1 
ATOM   5326 H  H    . HIS   B 1 94  ? 44.346 -14.509 0.169   1.00 11.61 ?  94  HIS   B H    1 
ATOM   5327 H  HA   . HIS   B 1 94  ? 44.939 -17.057 0.769   1.00 11.67 ?  94  HIS   B HA   1 
ATOM   5328 H  HB2  . HIS   B 1 94  ? 44.960 -14.733 2.383   1.00 12.04 ?  94  HIS   B HB2  1 
ATOM   5329 H  HB3  . HIS   B 1 94  ? 45.444 -16.155 2.897   1.00 12.04 ?  94  HIS   B HB3  1 
ATOM   5330 H  HD2  . HIS   B 1 94  ? 46.811 -13.383 0.860   1.00 12.75 ?  94  HIS   B HD2  1 
ATOM   5331 H  HE1  . HIS   B 1 94  ? 49.703 -16.060 1.172   1.00 12.68 ?  94  HIS   B HE1  1 
ATOM   5332 H  HE2  . HIS   B 1 94  ? 49.147 -13.880 0.439   1.00 12.92 ?  94  HIS   B HE2  1 
ATOM   5333 N  N    . VAL   B 1 95  ? 42.710 -17.863 1.505   1.00 10.12 ?  95  VAL   B N    1 
ATOM   5334 C  CA   . VAL   B 1 95  ? 41.383 -18.301 1.938   1.00 10.39 ?  95  VAL   B CA   1 
ATOM   5335 C  C    . VAL   B 1 95  ? 41.553 -19.337 3.033   1.00 10.52 ?  95  VAL   B C    1 
ATOM   5336 O  O    . VAL   B 1 95  ? 42.329 -20.285 2.875   1.00 11.06 ?  95  VAL   B O    1 
ATOM   5337 C  CB   . VAL   B 1 95  ? 40.560 -18.906 0.784   1.00 10.21 ?  95  VAL   B CB   1 
ATOM   5338 C  CG1  . VAL   B 1 95  ? 39.187 -19.340 1.276   1.00 11.69 ?  95  VAL   B CG1  1 
ATOM   5339 C  CG2  . VAL   B 1 95  ? 40.443 -17.924 -0.359  1.00 10.52 ?  95  VAL   B CG2  1 
ATOM   5340 H  H    . VAL   B 1 95  ? 43.174 -18.490 1.143   1.00 12.20 ?  95  VAL   B H    1 
ATOM   5341 H  HA   . VAL   B 1 95  ? 40.890 -17.548 2.300   1.00 12.52 ?  95  VAL   B HA   1 
ATOM   5342 H  HB   . VAL   B 1 95  ? 41.014 -19.693 0.451   1.00 12.31 ?  95  VAL   B HB   1 
ATOM   5343 H  HG11 . VAL   B 1 95  ? 38.620 -19.530 0.506   1.00 14.08 ?  95  VAL   B HG11 1 
ATOM   5344 H  HG12 . VAL   B 1 95  ? 39.274 -20.137 1.820   1.00 14.08 ?  95  VAL   B HG12 1 
ATOM   5345 H  HG13 . VAL   B 1 95  ? 38.792 -18.622 1.797   1.00 14.08 ?  95  VAL   B HG13 1 
ATOM   5346 H  HG21 . VAL   B 1 95  ? 39.859 -18.298 -1.038  1.00 12.68 ?  95  VAL   B HG21 1 
ATOM   5347 H  HG22 . VAL   B 1 95  ? 40.064 -17.094 -0.022  1.00 12.68 ?  95  VAL   B HG22 1 
ATOM   5348 H  HG23 . VAL   B 1 95  ? 41.321 -17.762 -0.726  1.00 12.68 ?  95  VAL   B HG23 1 
ATOM   5349 N  N    . VAL   B 1 96  ? 40.818 -19.172 4.128   1.00 10.93 ?  96  VAL   B N    1 
ATOM   5350 C  CA   . VAL   B 1 96  ? 40.904 -20.085 5.268   1.00 11.04 ?  96  VAL   B CA   1 
ATOM   5351 C  C    . VAL   B 1 96  ? 39.716 -21.045 5.223   1.00 11.53 ?  96  VAL   B C    1 
ATOM   5352 O  O    . VAL   B 1 96  ? 38.596 -20.690 5.605   1.00 12.26 ?  96  VAL   B O    1 
ATOM   5353 C  CB   . VAL   B 1 96  ? 40.954 -19.334 6.601   1.00 11.75 ?  96  VAL   B CB   1 
ATOM   5354 C  CG1  . VAL   B 1 96  ? 41.125 -20.324 7.747   1.00 12.74 ?  96  VAL   B CG1  1 
ATOM   5355 C  CG2  . VAL   B 1 96  ? 42.067 -18.292 6.611   1.00 12.73 ?  96  VAL   B CG2  1 
ATOM   5356 H  H    . VAL   B 1 96  ? 40.254 -18.532 4.244   1.00 13.18 ?  96  VAL   B H    1 
ATOM   5357 H  HA   . VAL   B 1 96  ? 41.717 -20.610 5.195   1.00 13.31 ?  96  VAL   B HA   1 
ATOM   5358 H  HB   . VAL   B 1 96  ? 40.113 -18.872 6.737   1.00 14.16 ?  96  VAL   B HB   1 
ATOM   5359 H  HG11 . VAL   B 1 96  ? 41.318 -19.835 8.565   1.00 15.35 ?  96  VAL   B HG11 1 
ATOM   5360 H  HG12 . VAL   B 1 96  ? 40.308 -20.835 7.857   1.00 15.35 ?  96  VAL   B HG12 1 
ATOM   5361 H  HG13 . VAL   B 1 96  ? 41.864 -20.922 7.545   1.00 15.35 ?  96  VAL   B HG13 1 
ATOM   5362 H  HG21 . VAL   B 1 96  ? 42.112 -17.880 7.491   1.00 15.33 ?  96  VAL   B HG21 1 
ATOM   5363 H  HG22 . VAL   B 1 96  ? 42.910 -18.720 6.404   1.00 15.33 ?  96  VAL   B HG22 1 
ATOM   5364 H  HG23 . VAL   B 1 96  ? 41.869 -17.612 5.945   1.00 15.33 ?  96  VAL   B HG23 1 
ATOM   5365 N  N    . GLY   B 1 97  ? 39.953 -22.277 4.780   1.00 11.55 ?  97  GLY   B N    1 
ATOM   5366 C  CA   . GLY   B 1 97  ? 38.978 -23.330 4.936   1.00 12.12 ?  97  GLY   B CA   1 
ATOM   5367 C  C    . GLY   B 1 97  ? 39.100 -23.939 6.318   1.00 13.20 ?  97  GLY   B C    1 
ATOM   5368 O  O    . GLY   B 1 97  ? 40.139 -23.809 6.980   1.00 13.81 ?  97  GLY   B O    1 
ATOM   5369 H  H    . GLY   B 1 97  ? 40.683 -22.520 4.389   1.00 13.92 ?  97  GLY   B H    1 
ATOM   5370 H  HA2  . GLY   B 1 97  ? 38.084 -22.960 4.818   1.00 14.61 ?  97  GLY   B HA2  1 
ATOM   5371 H  HA3  . GLY   B 1 97  ? 39.121 -24.013 4.261   1.00 14.61 ?  97  GLY   B HA3  1 
ATOM   5372 N  N    . PRO   B 1 98  ? 38.052 -24.620 6.783   1.00 13.89 ?  98  PRO   B N    1 
ATOM   5373 C  CA   . PRO   B 1 98  ? 38.147 -25.317 8.069   1.00 14.62 ?  98  PRO   B CA   1 
ATOM   5374 C  C    . PRO   B 1 98  ? 39.171 -26.441 8.027   1.00 14.23 ?  98  PRO   B C    1 
ATOM   5375 O  O    . PRO   B 1 98  ? 39.277 -27.180 7.047   1.00 14.52 ?  98  PRO   B O    1 
ATOM   5376 C  CB   . PRO   B 1 98  ? 36.728 -25.856 8.279   1.00 14.96 ?  98  PRO   B CB   1 
ATOM   5377 C  CG   . PRO   B 1 98  ? 36.173 -25.999 6.910   1.00 14.83 ?  98  PRO   B CG   1 
ATOM   5378 C  CD   . PRO   B 1 98  ? 36.739 -24.825 6.146   1.00 13.99 ?  98  PRO   B CD   1 
ATOM   5379 H  HA   . PRO   B 1 98  ? 38.374 -24.694 8.770   1.00 17.60 ?  98  PRO   B HA   1 
ATOM   5380 H  HB2  . PRO   B 1 98  ? 36.768 -26.716 8.725   1.00 18.01 ?  98  PRO   B HB2  1 
ATOM   5381 H  HB3  . PRO   B 1 98  ? 36.211 -25.221 8.794   1.00 18.01 ?  98  PRO   B HB3  1 
ATOM   5382 H  HG2  . PRO   B 1 98  ? 36.468 -26.840 6.522   1.00 17.85 ?  98  PRO   B HG2  1 
ATOM   5383 H  HG3  . PRO   B 1 98  ? 35.205 -25.957 6.942   1.00 17.85 ?  98  PRO   B HG3  1 
ATOM   5384 H  HD2  . PRO   B 1 98  ? 36.838 -25.052 5.203   1.00 16.85 ?  98  PRO   B HD2  1 
ATOM   5385 H  HD3  . PRO   B 1 98  ? 36.181 -24.042 6.263   1.00 16.85 ?  98  PRO   B HD3  1 
ATOM   5386 N  N    . ASN   B 1 99  ? 39.922 -26.566 9.111   1.00 15.40 ?  99  ASN   B N    1 
ATOM   5387 C  CA   . ASN   B 1 99  ? 40.900 -27.639 9.275   1.00 16.11 ?  99  ASN   B CA   1 
ATOM   5388 C  C    . ASN   B 1 99  ? 40.267 -28.718 10.151  1.00 18.76 ?  99  ASN   B C    1 
ATOM   5389 O  O    . ASN   B 1 99  ? 40.190 -28.573 11.373  1.00 19.38 ?  99  ASN   B O    1 
ATOM   5390 C  CB   . ASN   B 1 99  ? 42.172 -27.082 9.899   1.00 16.30 ?  99  ASN   B CB   1 
ATOM   5391 C  CG   . ASN   B 1 99  ? 43.302 -28.087 9.908   1.00 17.55 ?  99  ASN   B CG   1 
ATOM   5392 O  OD1  . ASN   B 1 99  ? 43.075 -29.280 10.065  1.00 18.35 ?  99  ASN   B OD1  1 
ATOM   5393 N  ND2  . ASN   B 1 99  ? 44.523 -27.609 9.737   1.00 18.05 ?  99  ASN   B ND2  1 
ATOM   5394 H  H    . ASN   B 1 99  ? 39.884 -26.029 9.779   1.00 18.53 ?  99  ASN   B H    1 
ATOM   5395 H  HA   . ASN   B 1 99  ? 41.114 -28.027 8.412   1.00 19.39 ?  99  ASN   B HA   1 
ATOM   5396 H  HB2  . ASN   B 1 99  ? 42.456 -26.310 9.396   1.00 19.62 ?  99  ASN   B HB2  1 
ATOM   5397 H  HB3  . ASN   B 1 99  ? 41.981 -26.833 10.820  1.00 19.62 ?  99  ASN   B HB3  1 
ATOM   5398 H  HD21 . ASN   B 1 99  ? 45.196 -28.142 9.733   1.00 21.71 ?  99  ASN   B HD21 1 
ATOM   5399 H  HD22 . ASN   B 1 99  ? 44.637 -26.764 9.633   1.00 21.71 ?  99  ASN   B HD22 1 
ATOM   5400 N  N    A VAL   B 1 100 ? 39.800 -29.797 9.517   0.78 20.55 ?  100 VAL   B N    1 
ATOM   5401 N  N    B VAL   B 1 100 ? 39.798 -29.795 9.512   0.22 21.00 ?  100 VAL   B N    1 
ATOM   5402 C  CA   A VAL   B 1 100 ? 39.176 -30.890 10.261  0.78 23.44 ?  100 VAL   B CA   1 
ATOM   5403 C  CA   B VAL   B 1 100 ? 39.178 -30.897 10.245  0.22 23.38 ?  100 VAL   B CA   1 
ATOM   5404 C  C    A VAL   B 1 100 ? 40.178 -31.551 11.197  0.78 23.92 ?  100 VAL   B C    1 
ATOM   5405 C  C    B VAL   B 1 100 ? 40.176 -31.550 11.191  0.22 24.14 ?  100 VAL   B C    1 
ATOM   5406 O  O    A VAL   B 1 100 ? 39.806 -32.047 12.267  0.78 24.57 ?  100 VAL   B O    1 
ATOM   5407 O  O    B VAL   B 1 100 ? 39.801 -32.028 12.269  0.22 24.45 ?  100 VAL   B O    1 
ATOM   5408 C  CB   A VAL   B 1 100 ? 38.536 -31.904 9.291   0.78 26.13 ?  100 VAL   B CB   1 
ATOM   5409 C  CB   B VAL   B 1 100 ? 38.556 -31.913 9.263   0.22 24.89 ?  100 VAL   B CB   1 
ATOM   5410 C  CG1  A VAL   B 1 100 ? 38.053 -33.138 10.045  0.78 27.41 ?  100 VAL   B CG1  1 
ATOM   5411 C  CG1  B VAL   B 1 100 ? 38.036 -33.136 10.007  0.22 25.50 ?  100 VAL   B CG1  1 
ATOM   5412 C  CG2  A VAL   B 1 100 ? 37.384 -31.262 8.537   0.78 26.81 ?  100 VAL   B CG2  1 
ATOM   5413 C  CG2  B VAL   B 1 100 ? 37.435 -31.263 8.465   0.22 25.46 ?  100 VAL   B CG2  1 
ATOM   5414 H  H    A VAL   B 1 100 ? 39.826 -29.914 8.664   0.78 24.72 ?  100 VAL   B H    1 
ATOM   5415 H  H    B VAL   B 1 100 ? 39.821 -29.906 8.659   0.22 25.25 ?  100 VAL   B H    1 
ATOM   5416 H  HA   A VAL   B 1 100 ? 38.459 -30.523 10.803  0.78 28.18 ?  100 VAL   B HA   1 
ATOM   5417 H  HA   B VAL   B 1 100 ? 38.454 -30.543 10.784  0.22 28.11 ?  100 VAL   B HA   1 
ATOM   5418 H  HB   A VAL   B 1 100 ? 39.199 -32.190 8.645   0.78 31.41 ?  100 VAL   B HB   1 
ATOM   5419 H  HB   B VAL   B 1 100 ? 39.235 -32.210 8.638   0.22 29.93 ?  100 VAL   B HB   1 
ATOM   5420 H  HG11 A VAL   B 1 100 ? 37.457 -33.646 9.470   0.78 32.95 ?  100 VAL   B HG11 1 
ATOM   5421 H  HG11 B VAL   B 1 100 ? 37.461 -33.646 9.413   0.22 30.66 ?  100 VAL   B HG11 1 
ATOM   5422 H  HG12 A VAL   B 1 100 ? 38.817 -33.685 10.290  0.78 32.95 ?  100 VAL   B HG12 1 
ATOM   5423 H  HG12 B VAL   B 1 100 ? 38.787 -33.683 10.286  0.22 30.66 ?  100 VAL   B HG12 1 
ATOM   5424 H  HG13 A VAL   B 1 100 ? 37.577 -32.857 10.843  0.78 32.95 ?  100 VAL   B HG13 1 
ATOM   5425 H  HG13 B VAL   B 1 100 ? 37.530 -32.843 10.781  0.22 30.66 ?  100 VAL   B HG13 1 
ATOM   5426 H  HG21 A VAL   B 1 100 ? 37.002 -31.915 7.929   0.78 32.23 ?  100 VAL   B HG21 1 
ATOM   5427 H  HG21 B VAL   B 1 100 ? 37.054 -31.921 7.861   0.22 30.60 ?  100 VAL   B HG21 1 
ATOM   5428 H  HG22 A VAL   B 1 100 ? 36.712 -30.973 9.175   0.78 32.23 ?  100 VAL   B HG22 1 
ATOM   5429 H  HG22 B VAL   B 1 100 ? 36.754 -30.945 9.079   0.22 30.60 ?  100 VAL   B HG22 1 
ATOM   5430 H  HG23 A VAL   B 1 100 ? 37.718 -30.501 8.040   0.78 32.23 ?  100 VAL   B HG23 1 
ATOM   5431 H  HG23 B VAL   B 1 100 ? 37.797 -30.521 7.958   0.22 30.60 ?  100 VAL   B HG23 1 
ATOM   5432 N  N    . ASN   B 1 101 ? 41.455 -31.588 10.811  1.00 24.69 ?  101 ASN   B N    1 
ATOM   5433 C  CA   . ASN   B 1 101 ? 42.487 -32.132 11.690  1.00 26.67 ?  101 ASN   B CA   1 
ATOM   5434 C  C    . ASN   B 1 101 ? 42.685 -31.300 12.951  1.00 29.00 ?  101 ASN   B C    1 
ATOM   5435 O  O    . ASN   B 1 101 ? 43.324 -31.779 13.897  1.00 30.15 ?  101 ASN   B O    1 
ATOM   5436 C  CB   . ASN   B 1 101 ? 43.813 -32.268 10.936  1.00 26.72 ?  101 ASN   B CB   1 
ATOM   5437 C  CG   . ASN   B 1 101 ? 43.802 -33.412 9.942   1.00 26.72 ?  101 ASN   B CG   1 
ATOM   5438 O  OD1  . ASN   B 1 101 ? 43.135 -34.418 10.154  1.00 27.32 ?  101 ASN   B OD1  1 
ATOM   5439 N  ND2  . ASN   B 1 101 ? 44.537 -33.261 8.849   1.00 26.42 ?  101 ASN   B ND2  1 
ATOM   5440 H  H    A ASN   B 1 101 ? 41.738 -31.319 10.044  0.78 29.68 ?  101 ASN   B H    1 
ATOM   5441 H  H    B ASN   B 1 101 ? 41.743 -31.311 10.048  0.22 29.68 ?  101 ASN   B H    1 
ATOM   5442 H  HA   . ASN   B 1 101 ? 42.216 -33.018 11.967  1.00 32.07 ?  101 ASN   B HA   1 
ATOM   5443 H  HB2  . ASN   B 1 101 ? 43.991 -31.453 10.445  1.00 32.12 ?  101 ASN   B HB2  1 
ATOM   5444 H  HB3  . ASN   B 1 101 ? 44.524 -32.433 11.576  1.00 32.12 ?  101 ASN   B HB3  1 
ATOM   5445 H  HD21 . ASN   B 1 101 ? 44.562 -33.887 8.258   1.00 31.75 ?  101 ASN   B HD21 1 
ATOM   5446 H  HD22 . ASN   B 1 101 ? 44.984 -32.539 8.730   1.00 31.75 ?  101 ASN   B HD22 1 
ATOM   5447 N  N    . LYS   B 1 102 ? 42.164 -30.071 12.978  1.00 31.44 ?  102 LYS   B N    1 
ATOM   5448 C  CA   . LYS   B 1 102 ? 42.147 -29.230 14.167  1.00 34.30 ?  102 LYS   B CA   1 
ATOM   5449 C  C    . LYS   B 1 102 ? 40.771 -29.176 14.820  1.00 33.58 ?  102 LYS   B C    1 
ATOM   5450 O  O    . LYS   B 1 102 ? 40.560 -28.370 15.730  1.00 34.48 ?  102 LYS   B O    1 
ATOM   5451 C  CB   . LYS   B 1 102 ? 42.585 -27.806 13.820  1.00 38.39 ?  102 LYS   B CB   1 
ATOM   5452 C  CG   . LYS   B 1 102 ? 44.048 -27.652 13.445  1.00 42.04 ?  102 LYS   B CG   1 
ATOM   5453 C  CD   . LYS   B 1 102 ? 44.323 -26.231 12.975  1.00 45.35 ?  102 LYS   B CD   1 
ATOM   5454 C  CE   . LYS   B 1 102 ? 45.805 -25.972 12.771  1.00 47.71 ?  102 LYS   B CE   1 
ATOM   5455 N  NZ   . LYS   B 1 102 ? 46.051 -24.579 12.300  1.00 49.03 ?  102 LYS   B NZ   1 
ATOM   5456 H  H    . LYS   B 1 102 ? 41.800 -29.692 12.296  1.00 37.78 ?  102 LYS   B H    1 
ATOM   5457 H  HA   . LYS   B 1 102 ? 42.777 -29.585 14.812  1.00 41.22 ?  102 LYS   B HA   1 
ATOM   5458 H  HB2  . LYS   B 1 102 ? 42.056 -27.496 13.069  1.00 46.12 ?  102 LYS   B HB2  1 
ATOM   5459 H  HB3  . LYS   B 1 102 ? 42.420 -27.237 14.589  1.00 46.12 ?  102 LYS   B HB3  1 
ATOM   5460 H  HG2  . LYS   B 1 102 ? 44.603 -27.832 14.220  1.00 50.50 ?  102 LYS   B HG2  1 
ATOM   5461 H  HG3  . LYS   B 1 102 ? 44.264 -28.263 12.723  1.00 50.50 ?  102 LYS   B HG3  1 
ATOM   5462 H  HD2  . LYS   B 1 102 ? 43.872 -26.084 12.128  1.00 54.47 ?  102 LYS   B HD2  1 
ATOM   5463 H  HD3  . LYS   B 1 102 ? 43.994 -25.606 13.640  1.00 54.47 ?  102 LYS   B HD3  1 
ATOM   5464 H  HE2  . LYS   B 1 102 ? 46.270 -26.095 13.614  1.00 57.31 ?  102 LYS   B HE2  1 
ATOM   5465 H  HE3  . LYS   B 1 102 ? 46.150 -26.585 12.104  1.00 57.31 ?  102 LYS   B HE3  1 
ATOM   5466 H  HZ1  . LYS   B 1 102 ? 46.923 -24.445 12.187  1.00 58.89 ?  102 LYS   B HZ1  1 
ATOM   5467 H  HZ2  . LYS   B 1 102 ? 45.634 -24.443 11.525  1.00 58.89 ?  102 LYS   B HZ2  1 
ATOM   5468 H  HZ3  . LYS   B 1 102 ? 45.743 -23.997 12.899  1.00 58.89 ?  102 LYS   B HZ3  1 
ATOM   5469 N  N    . GLY   B 1 103 ? 39.826 -29.993 14.361  1.00 32.39 ?  103 GLY   B N    1 
ATOM   5470 C  CA   . GLY   B 1 103 ? 38.501 -30.028 14.946  1.00 31.67 ?  103 GLY   B CA   1 
ATOM   5471 C  C    . GLY   B 1 103 ? 37.560 -28.942 14.479  1.00 30.27 ?  103 GLY   B C    1 
ATOM   5472 O  O    . GLY   B 1 103 ? 36.475 -28.797 15.053  1.00 30.75 ?  103 GLY   B O    1 
ATOM   5473 H  H    . GLY   B 1 103 ? 39.932 -30.538 13.706  1.00 38.92 ?  103 GLY   B H    1 
ATOM   5474 H  HA2  . GLY   B 1 103 ? 38.088 -30.878 14.737  1.00 38.06 ?  103 GLY   B HA2  1 
ATOM   5475 H  HA3  . GLY   B 1 103 ? 38.582 -29.964 15.912  1.00 38.06 ?  103 GLY   B HA3  1 
ATOM   5476 N  N    A GLU   B 1 104 ? 37.935 -28.176 13.458  0.78 28.85 ?  104 GLU   B N    1 
ATOM   5477 N  N    B GLU   B 1 104 ? 37.928 -28.181 13.454  0.22 29.78 ?  104 GLU   B N    1 
ATOM   5478 C  CA   A GLU   B 1 104 ? 37.102 -27.078 12.993  0.78 27.20 ?  104 GLU   B CA   1 
ATOM   5479 C  CA   B GLU   B 1 104 ? 37.080 -27.098 12.981  0.22 28.94 ?  104 GLU   B CA   1 
ATOM   5480 C  C    A GLU   B 1 104 ? 35.929 -27.603 12.171  0.78 27.77 ?  104 GLU   B C    1 
ATOM   5481 C  C    B GLU   B 1 104 ? 35.926 -27.644 12.147  0.22 29.05 ?  104 GLU   B C    1 
ATOM   5482 O  O    A GLU   B 1 104 ? 35.984 -28.690 11.588  0.78 28.73 ?  104 GLU   B O    1 
ATOM   5483 O  O    B GLU   B 1 104 ? 36.018 -28.714 11.538  0.22 29.31 ?  104 GLU   B O    1 
ATOM   5484 C  CB   A GLU   B 1 104 ? 37.941 -26.082 12.190  0.78 25.81 ?  104 GLU   B CB   1 
ATOM   5485 C  CB   B GLU   B 1 104 ? 37.908 -26.093 12.180  0.22 28.13 ?  104 GLU   B CB   1 
ATOM   5486 C  CG   A GLU   B 1 104 ? 39.033 -25.440 13.037  0.78 24.50 ?  104 GLU   B CG   1 
ATOM   5487 C  CG   B GLU   B 1 104 ? 39.000 -25.436 13.014  0.22 27.43 ?  104 GLU   B CG   1 
ATOM   5488 C  CD   A GLU   B 1 104 ? 39.982 -24.559 12.251  0.78 23.01 ?  104 GLU   B CD   1 
ATOM   5489 C  CD   B GLU   B 1 104 ? 39.931 -24.565 12.195  0.22 26.87 ?  104 GLU   B CD   1 
ATOM   5490 O  OE1  A GLU   B 1 104 ? 39.978 -24.599 11.003  0.78 21.11 ?  104 GLU   B OE1  1 
ATOM   5491 O  OE1  B GLU   B 1 104 ? 39.839 -24.588 10.949  0.22 26.42 ?  104 GLU   B OE1  1 
ATOM   5492 O  OE2  A GLU   B 1 104 ? 40.748 -23.822 12.901  0.78 23.21 -1 104 GLU   B OE2  1 
ATOM   5493 O  OE2  B GLU   B 1 104 ? 40.760 -23.855 12.801  0.22 26.85 -1 104 GLU   B OE2  1 
ATOM   5494 H  H    A GLU   B 1 104 ? 38.670 -28.271 13.021  0.78 34.68 ?  104 GLU   B H    1 
ATOM   5495 H  H    B GLU   B 1 104 ? 38.664 -28.271 13.020  0.22 35.79 ?  104 GLU   B H    1 
ATOM   5496 H  HA   A GLU   B 1 104 ? 36.744 -26.610 13.763  0.78 32.70 ?  104 GLU   B HA   1 
ATOM   5497 H  HA   B GLU   B 1 104 ? 36.705 -26.634 13.745  0.22 34.79 ?  104 GLU   B HA   1 
ATOM   5498 H  HB2  A GLU   B 1 104 ? 38.364 -26.542 11.449  0.78 31.03 ?  104 GLU   B HB2  1 
ATOM   5499 H  HB2  B GLU   B 1 104 ? 38.332 -26.550 11.437  0.22 33.81 ?  104 GLU   B HB2  1 
ATOM   5500 H  HB3  A GLU   B 1 104 ? 37.364 -25.375 11.858  0.78 31.03 ?  104 GLU   B HB3  1 
ATOM   5501 H  HB3  B GLU   B 1 104 ? 37.322 -25.393 11.849  0.22 33.81 ?  104 GLU   B HB3  1 
ATOM   5502 H  HG2  A GLU   B 1 104 ? 38.621 -24.887 13.721  0.78 29.46 ?  104 GLU   B HG2  1 
ATOM   5503 H  HG2  B GLU   B 1 104 ? 38.586 -24.877 13.692  0.22 32.97 ?  104 GLU   B HG2  1 
ATOM   5504 H  HG3  A GLU   B 1 104 ? 39.560 -26.139 13.459  0.78 29.46 ?  104 GLU   B HG3  1 
ATOM   5505 H  HG3  B GLU   B 1 104 ? 39.532 -26.128 13.440  0.22 32.97 ?  104 GLU   B HG3  1 
ATOM   5506 N  N    A ASP   B 1 105 ? 34.857 -26.815 12.139  0.78 27.20 ?  105 ASP   B N    1 
ATOM   5507 N  N    B ASP   B 1 105 ? 34.829 -26.890 12.129  0.22 28.68 ?  105 ASP   B N    1 
ATOM   5508 C  CA   A ASP   B 1 105 ? 33.578 -27.269 11.606  0.78 27.64 ?  105 ASP   B CA   1 
ATOM   5509 C  CA   B ASP   B 1 105 ? 33.576 -27.373 11.562  0.22 28.60 ?  105 ASP   B CA   1 
ATOM   5510 C  C    A ASP   B 1 105 ? 33.630 -27.318 10.084  0.78 25.91 ?  105 ASP   B C    1 
ATOM   5511 C  C    B ASP   B 1 105 ? 33.656 -27.389 10.040  0.22 27.83 ?  105 ASP   B C    1 
ATOM   5512 O  O    A ASP   B 1 105 ? 33.773 -26.282 9.425   0.78 25.06 ?  105 ASP   B O    1 
ATOM   5513 O  O    B ASP   B 1 105 ? 33.882 -26.351 9.409   0.22 27.51 ?  105 ASP   B O    1 
ATOM   5514 C  CB   A ASP   B 1 105 ? 32.463 -26.336 12.076  0.78 30.85 ?  105 ASP   B CB   1 
ATOM   5515 C  CB   B ASP   B 1 105 ? 32.427 -26.482 12.030  0.22 29.31 ?  105 ASP   B CB   1 
ATOM   5516 C  CG   A ASP   B 1 105 ? 31.085 -26.828 11.677  0.78 33.63 ?  105 ASP   B CG   1 
ATOM   5517 C  CG   B ASP   B 1 105 ? 31.066 -27.080 11.725  0.22 30.11 ?  105 ASP   B CG   1 
ATOM   5518 O  OD1  A ASP   B 1 105 ? 30.992 -27.895 11.034  0.78 33.78 ?  105 ASP   B OD1  1 
ATOM   5519 O  OD1  B ASP   B 1 105 ? 31.010 -28.095 11.000  0.22 30.21 ?  105 ASP   B OD1  1 
ATOM   5520 O  OD2  A ASP   B 1 105 ? 30.090 -26.146 12.007  0.78 35.09 -1 105 ASP   B OD2  1 
ATOM   5521 O  OD2  B ASP   B 1 105 ? 30.052 -26.540 12.218  0.22 30.30 -1 105 ASP   B OD2  1 
ATOM   5522 H  H    A ASP   B 1 105 ? 34.848 -26.003 12.420  0.78 32.70 ?  105 ASP   B H    1 
ATOM   5523 H  H    B ASP   B 1 105 ? 34.788 -26.092 12.436  0.22 34.47 ?  105 ASP   B H    1 
ATOM   5524 H  HA   A ASP   B 1 105 ? 33.387 -28.162 11.938  0.78 33.23 ?  105 ASP   B HA   1 
ATOM   5525 H  HA   B ASP   B 1 105 ? 33.402 -28.276 11.871  0.22 34.37 ?  105 ASP   B HA   1 
ATOM   5526 H  HB2  A ASP   B 1 105 ? 32.502 -26.258 13.046  0.78 37.07 ?  105 ASP   B HB2  1 
ATOM   5527 H  HB2  B ASP   B 1 105 ? 32.494 -26.353 12.991  0.22 35.23 ?  105 ASP   B HB2  1 
ATOM   5528 H  HB3  A ASP   B 1 105 ? 32.588 -25.464 11.672  0.78 37.07 ?  105 ASP   B HB3  1 
ATOM   5529 H  HB3  B ASP   B 1 105 ? 32.486 -25.623 11.579  0.22 35.23 ?  105 ASP   B HB3  1 
ATOM   5530 N  N    A ILE   B 1 106 ? 33.489 -28.524 9.527   0.78 25.33 ?  106 ILE   B N    1 
ATOM   5531 N  N    B ILE   B 1 106 ? 33.463 -28.573 9.452   0.22 27.24 ?  106 ILE   B N    1 
ATOM   5532 C  CA   A ILE   B 1 106 ? 33.481 -28.705 8.081   0.78 24.59 ?  106 ILE   B CA   1 
ATOM   5533 C  CA   B ILE   B 1 106 ? 33.476 -28.719 8.001   0.22 26.78 ?  106 ILE   B CA   1 
ATOM   5534 C  C    A ILE   B 1 106 ? 32.379 -27.889 7.411   0.78 23.48 ?  106 ILE   B C    1 
ATOM   5535 C  C    B ILE   B 1 106 ? 32.375 -27.900 7.338   0.22 26.24 ?  106 ILE   B C    1 
ATOM   5536 O  O    A ILE   B 1 106 ? 32.479 -27.570 6.222   0.78 22.33 ?  106 ILE   B O    1 
ATOM   5537 O  O    B ILE   B 1 106 ? 32.459 -27.607 6.140   0.22 25.91 ?  106 ILE   B O    1 
ATOM   5538 C  CB   A ILE   B 1 106 ? 33.392 -30.214 7.752   0.78 25.83 ?  106 ILE   B CB   1 
ATOM   5539 C  CB   B ILE   B 1 106 ? 33.389 -30.218 7.631   0.22 26.96 ?  106 ILE   B CB   1 
ATOM   5540 C  CG1  A ILE   B 1 106 ? 33.652 -30.470 6.268   0.78 26.16 ?  106 ILE   B CG1  1 
ATOM   5541 C  CG1  B ILE   B 1 106 ? 33.642 -30.432 6.136   0.22 26.91 ?  106 ILE   B CG1  1 
ATOM   5542 C  CG2  A ILE   B 1 106 ? 32.035 -30.774 8.164   0.78 26.63 ?  106 ILE   B CG2  1 
ATOM   5543 C  CG2  B ILE   B 1 106 ? 32.035 -30.792 8.029   0.22 27.19 ?  106 ILE   B CG2  1 
ATOM   5544 C  CD1  A ILE   B 1 106 ? 35.010 -30.000 5.806   0.78 26.04 ?  106 ILE   B CD1  1 
ATOM   5545 C  CD1  B ILE   B 1 106 ? 34.993 -29.940 5.672   0.22 26.84 ?  106 ILE   B CD1  1 
ATOM   5546 H  H    A ILE   B 1 106 ? 33.403 -29.253 9.974   0.78 30.45 ?  106 ILE   B H    1 
ATOM   5547 H  H    B ILE   B 1 106 ? 33.334 -29.307 9.877   0.22 32.75 ?  106 ILE   B H    1 
ATOM   5548 H  HA   A ILE   B 1 106 ? 34.324 -28.381 7.739   0.78 29.56 ?  106 ILE   B HA   1 
ATOM   5549 H  HA   B ILE   B 1 106 ? 34.322 -28.383 7.674   0.22 32.19 ?  106 ILE   B HA   1 
ATOM   5550 H  HB   A ILE   B 1 106 ? 34.074 -30.678 8.264   0.78 31.06 ?  106 ILE   B HB   1 
ATOM   5551 H  HB   B ILE   B 1 106 ? 34.075 -30.693 8.124   0.22 32.40 ?  106 ILE   B HB   1 
ATOM   5552 H  HG12 A ILE   B 1 106 ? 33.599 -31.426 6.101   0.78 31.45 ?  106 ILE   B HG12 1 
ATOM   5553 H  HG12 B ILE   B 1 106 ? 33.595 -31.384 5.944   0.22 32.35 ?  106 ILE   B HG12 1 
ATOM   5554 H  HG13 A ILE   B 1 106 ? 32.982 -30.008 5.745   0.78 31.45 ?  106 ILE   B HG13 1 
ATOM   5555 H  HG13 B ILE   B 1 106 ? 32.964 -29.963 5.628   0.22 32.35 ?  106 ILE   B HG13 1 
ATOM   5556 H  HG21 A ILE   B 1 106 ? 32.051 -31.741 8.079   0.78 32.01 ?  106 ILE   B HG21 1 
ATOM   5557 H  HG21 B ILE   B 1 106 ? 32.053 -31.754 7.907   0.22 32.68 ?  106 ILE   B HG21 1 
ATOM   5558 H  HG22 A ILE   B 1 106 ? 31.858 -30.530 9.088   0.78 32.01 ?  106 ILE   B HG22 1 
ATOM   5559 H  HG22 B ILE   B 1 106 ? 31.864 -30.581 8.960   0.22 32.68 ?  106 ILE   B HG22 1 
ATOM   5560 H  HG23 A ILE   B 1 106 ? 31.348 -30.404 7.589   0.78 32.01 ?  106 ILE   B HG23 1 
ATOM   5561 H  HG23 B ILE   B 1 106 ? 31.346 -30.401 7.469   0.22 32.68 ?  106 ILE   B HG23 1 
ATOM   5562 H  HD11 A ILE   B 1 106 ? 35.215 -30.414 4.955   0.78 31.30 ?  106 ILE   B HD11 1 
ATOM   5563 H  HD11 B ILE   B 1 106 ? 35.184 -30.319 4.801   0.22 32.27 ?  106 ILE   B HD11 1 
ATOM   5564 H  HD12 A ILE   B 1 106 ? 34.995 -29.034 5.709   0.78 31.30 ?  106 ILE   B HD12 1 
ATOM   5565 H  HD12 B ILE   B 1 106 ? 34.974 -28.972 5.615   0.22 32.27 ?  106 ILE   B HD12 1 
ATOM   5566 H  HD13 A ILE   B 1 106 ? 35.675 -30.256 6.467   0.78 31.30 ?  106 ILE   B HD13 1 
ATOM   5567 H  HD13 B ILE   B 1 106 ? 35.667 -30.223 6.310   0.22 32.27 ?  106 ILE   B HD13 1 
ATOM   5568 N  N    A GLN   B 1 107 ? 31.332 -27.521 8.153   0.78 24.12 ?  107 GLN   B N    1 
ATOM   5569 N  N    B GLN   B 1 107 ? 31.340 -27.518 8.090   0.22 26.14 ?  107 GLN   B N    1 
ATOM   5570 C  CA   A GLN   B 1 107 ? 30.256 -26.719 7.579   0.78 24.65 ?  107 GLN   B CA   1 
ATOM   5571 C  CA   B GLN   B 1 107 ? 30.259 -26.716 7.528   0.22 25.97 ?  107 GLN   B CA   1 
ATOM   5572 C  C    A GLN   B 1 107 ? 30.746 -25.370 7.062   0.78 22.41 ?  107 GLN   B C    1 
ATOM   5573 C  C    B GLN   B 1 107 ? 30.738 -25.348 7.058   0.22 23.27 ?  107 GLN   B C    1 
ATOM   5574 O  O    A GLN   B 1 107 ? 30.106 -24.790 6.181   0.78 22.93 ?  107 GLN   B O    1 
ATOM   5575 O  O    B GLN   B 1 107 ? 30.077 -24.729 6.218   0.22 23.43 ?  107 GLN   B O    1 
ATOM   5576 C  CB   A GLN   B 1 107 ? 29.148 -26.519 8.618   0.78 28.85 ?  107 GLN   B CB   1 
ATOM   5577 C  CB   B GLN   B 1 107 ? 29.140 -26.561 8.563   0.22 28.72 ?  107 GLN   B CB   1 
ATOM   5578 C  CG   A GLN   B 1 107 ? 27.820 -26.024 8.051   0.78 32.97 ?  107 GLN   B CG   1 
ATOM   5579 C  CG   B GLN   B 1 107 ? 27.817 -26.048 8.005   0.22 31.13 ?  107 GLN   B CG   1 
ATOM   5580 C  CD   A GLN   B 1 107 ? 27.747 -24.511 7.943   0.78 36.19 ?  107 GLN   B CD   1 
ATOM   5581 C  CD   B GLN   B 1 107 ? 27.718 -24.533 8.013   0.22 33.06 ?  107 GLN   B CD   1 
ATOM   5582 O  OE1  A GLN   B 1 107 ? 28.577 -23.795 8.505   0.78 37.37 ?  107 GLN   B OE1  1 
ATOM   5583 O  OE1  B GLN   B 1 107 ? 28.550 -23.847 8.608   0.22 33.67 ?  107 GLN   B OE1  1 
ATOM   5584 N  NE2  A GLN   B 1 107 ? 26.746 -24.016 7.221   0.78 37.15 ?  107 GLN   B NE2  1 
ATOM   5585 N  NE2  B GLN   B 1 107 ? 26.694 -24.004 7.353   0.22 33.74 ?  107 GLN   B NE2  1 
ATOM   5586 H  H    A GLN   B 1 107 ? 31.227 -27.715 8.979   0.78 29.00 ?  107 GLN   B H    1 
ATOM   5587 H  H    B GLN   B 1 107 ? 31.241 -27.711 8.919   0.22 31.43 ?  107 GLN   B H    1 
ATOM   5588 H  HA   A GLN   B 1 107 ? 29.872 -27.205 6.831   0.78 29.64 ?  107 GLN   B HA   1 
ATOM   5589 H  HA   B GLN   B 1 107 ? 29.887 -27.184 6.764   0.22 31.23 ?  107 GLN   B HA   1 
ATOM   5590 H  HB2  A GLN   B 1 107 ? 28.980 -27.366 9.054   0.78 34.68 ?  107 GLN   B HB2  1 
ATOM   5591 H  HB2  B GLN   B 1 107 ? 28.969 -27.425 8.962   0.22 34.52 ?  107 GLN   B HB2  1 
ATOM   5592 H  HB3  A GLN   B 1 107 ? 29.452 -25.870 9.271   0.78 34.68 ?  107 GLN   B HB3  1 
ATOM   5593 H  HB3  B GLN   B 1 107 ? 29.434 -25.939 9.246   0.22 34.52 ?  107 GLN   B HB3  1 
ATOM   5594 H  HG2  A GLN   B 1 107 ? 27.696 -26.390 7.162   0.78 39.62 ?  107 GLN   B HG2  1 
ATOM   5595 H  HG2  B GLN   B 1 107 ? 27.720 -26.347 7.088   0.22 37.41 ?  107 GLN   B HG2  1 
ATOM   5596 H  HG3  A GLN   B 1 107 ? 27.099 -26.320 8.633   0.78 39.62 ?  107 GLN   B HG3  1 
ATOM   5597 H  HG3  B GLN   B 1 107 ? 27.089 -26.401 8.545   0.22 37.41 ?  107 GLN   B HG3  1 
ATOM   5598 H  HE21 A GLN   B 1 107 ? 26.184 -24.547 6.841   0.78 44.64 ?  107 GLN   B HE21 1 
ATOM   5599 H  HE21 B GLN   B 1 107 ? 26.132 -24.514 6.948   0.22 40.54 ?  107 GLN   B HE21 1 
ATOM   5600 H  HE22 A GLN   B 1 107 ? 26.657 -23.165 7.132   0.78 44.64 ?  107 GLN   B HE22 1 
ATOM   5601 H  HE22 B GLN   B 1 107 ? 26.593 -23.150 7.331   0.22 40.54 ?  107 GLN   B HE22 1 
ATOM   5602 N  N    . LEU   B 1 108 ? 31.871 -24.865 7.574   1.00 20.58 ?  108 LEU   B N    1 
ATOM   5603 C  CA   . LEU   B 1 108 ? 32.410 -23.566 7.165   1.00 18.00 ?  108 LEU   B CA   1 
ATOM   5604 C  C    . LEU   B 1 108 ? 33.059 -23.586 5.790   1.00 15.86 ?  108 LEU   B C    1 
ATOM   5605 O  O    . LEU   B 1 108 ? 33.496 -22.529 5.306   1.00 15.38 ?  108 LEU   B O    1 
ATOM   5606 C  CB   . LEU   B 1 108 ? 33.411 -23.076 8.208   1.00 18.75 ?  108 LEU   B CB   1 
ATOM   5607 C  CG   . LEU   B 1 108 ? 32.779 -22.629 9.525   1.00 20.31 ?  108 LEU   B CG   1 
ATOM   5608 C  CD1  . LEU   B 1 108 ? 33.812 -22.570 10.633  1.00 20.59 ?  108 LEU   B CD1  1 
ATOM   5609 C  CD2  . LEU   B 1 108 ? 32.121 -21.273 9.344   1.00 21.71 ?  108 LEU   B CD2  1 
ATOM   5610 H  H    A LEU   B 1 108 ? 32.339 -25.259 8.174   0.78 24.75 ?  108 LEU   B H    1 
ATOM   5611 H  H    B LEU   B 1 108 ? 32.338 -25.268 8.169   0.22 24.75 ?  108 LEU   B H    1 
ATOM   5612 H  HA   . LEU   B 1 108 ? 31.683 -22.928 7.133   1.00 21.66 ?  108 LEU   B HA   1 
ATOM   5613 H  HB2  . LEU   B 1 108 ? 34.026 -23.797 8.409   1.00 22.55 ?  108 LEU   B HB2  1 
ATOM   5614 H  HB3  . LEU   B 1 108 ? 33.894 -22.321 7.844   1.00 22.55 ?  108 LEU   B HB3  1 
ATOM   5615 H  HG   . LEU   B 1 108 ? 32.090 -23.265 9.787   1.00 24.43 ?  108 LEU   B HG   1 
ATOM   5616 H  HD11 . LEU   B 1 108 ? 33.375 -22.308 11.460  1.00 24.76 ?  108 LEU   B HD11 1 
ATOM   5617 H  HD12 . LEU   B 1 108 ? 34.215 -23.445 10.735  1.00 24.76 ?  108 LEU   B HD12 1 
ATOM   5618 H  HD13 . LEU   B 1 108 ? 34.488 -21.917 10.396  1.00 24.76 ?  108 LEU   B HD13 1 
ATOM   5619 H  HD21 . LEU   B 1 108 ? 31.789 -20.966 10.202  1.00 26.11 ?  108 LEU   B HD21 1 
ATOM   5620 H  HD22 . LEU   B 1 108 ? 32.779 -20.650 9.001   1.00 26.11 ?  108 LEU   B HD22 1 
ATOM   5621 H  HD23 . LEU   B 1 108 ? 31.386 -21.359 8.717   1.00 26.11 ?  108 LEU   B HD23 1 
ATOM   5622 N  N    . LEU   B 1 109 ? 33.119 -24.752 5.155   1.00 14.91 ?  109 LEU   B N    1 
ATOM   5623 C  CA   . LEU   B 1 109 ? 33.747 -24.860 3.847   1.00 13.95 ?  109 LEU   B CA   1 
ATOM   5624 C  C    . LEU   B 1 109 ? 32.983 -24.077 2.788   1.00 13.33 ?  109 LEU   B C    1 
ATOM   5625 O  O    . LEU   B 1 109 ? 33.598 -23.484 1.895   1.00 13.08 ?  109 LEU   B O    1 
ATOM   5626 C  CB   . LEU   B 1 109 ? 33.861 -26.335 3.466   1.00 13.96 ?  109 LEU   B CB   1 
ATOM   5627 C  CG   . LEU   B 1 109 ? 34.644 -26.671 2.201   1.00 14.02 ?  109 LEU   B CG   1 
ATOM   5628 C  CD1  . LEU   B 1 109 ? 36.031 -26.025 2.213   1.00 13.81 ?  109 LEU   B CD1  1 
ATOM   5629 C  CD2  . LEU   B 1 109 ? 34.759 -28.178 2.061   1.00 15.12 ?  109 LEU   B CD2  1 
ATOM   5630 H  H    . LEU   B 1 109 ? 32.810 -25.492 5.456   1.00 17.95 ?  109 LEU   B H    1 
ATOM   5631 H  HA   . LEU   B 1 109 ? 34.641 -24.499 3.892   1.00 16.80 ?  109 LEU   B HA   1 
ATOM   5632 H  HB2  . LEU   B 1 109 ? 34.295 -26.804 4.195   1.00 16.81 ?  109 LEU   B HB2  1 
ATOM   5633 H  HB3  . LEU   B 1 109 ? 32.966 -26.692 3.348   1.00 16.81 ?  109 LEU   B HB3  1 
ATOM   5634 H  HG   . LEU   B 1 109 ? 34.157 -26.340 1.426   1.00 16.88 ?  109 LEU   B HG   1 
ATOM   5635 H  HD11 . LEU   B 1 109 ? 36.555 -26.388 1.481   1.00 16.63 ?  109 LEU   B HD11 1 
ATOM   5636 H  HD12 . LEU   B 1 109 ? 35.933 -25.068 2.108   1.00 16.63 ?  109 LEU   B HD12 1 
ATOM   5637 H  HD13 . LEU   B 1 109 ? 36.463 -26.227 3.058   1.00 16.63 ?  109 LEU   B HD13 1 
ATOM   5638 H  HD21 . LEU   B 1 109 ? 35.324 -28.383 1.299   1.00 18.19 ?  109 LEU   B HD21 1 
ATOM   5639 H  HD22 . LEU   B 1 109 ? 35.149 -28.541 2.870   1.00 18.19 ?  109 LEU   B HD22 1 
ATOM   5640 H  HD23 . LEU   B 1 109 ? 33.873 -28.554 1.923   1.00 18.19 ?  109 LEU   B HD23 1 
ATOM   5641 N  N    . LYS   B 1 110 ? 31.650 -24.049 2.864   1.00 13.13 ?  110 LYS   B N    1 
ATOM   5642 C  CA   . LYS   B 1 110 ? 30.896 -23.286 1.875   1.00 12.94 ?  110 LYS   B CA   1 
ATOM   5643 C  C    . LYS   B 1 110 ? 31.232 -21.799 1.966   1.00 12.47 ?  110 LYS   B C    1 
ATOM   5644 O  O    . LYS   B 1 110 ? 31.486 -21.147 0.949   1.00 12.54 ?  110 LYS   B O    1 
ATOM   5645 C  CB   . LYS   B 1 110 ? 29.392 -23.539 2.020   1.00 13.55 ?  110 LYS   B CB   1 
ATOM   5646 C  CG   . LYS   B 1 110 ? 28.576 -22.910 0.891   1.00 13.81 ?  110 LYS   B CG   1 
ATOM   5647 C  CD   . LYS   B 1 110 ? 27.120 -23.346 0.926   1.00 14.05 ?  110 LYS   B CD   1 
ATOM   5648 C  CE   . LYS   B 1 110 ? 26.349 -22.806 -0.272  1.00 14.89 ?  110 LYS   B CE   1 
ATOM   5649 N  NZ   . LYS   B 1 110 ? 26.681 -23.513 -1.542  1.00 14.99 ?  110 LYS   B NZ   1 
ATOM   5650 H  H    . LYS   B 1 110 ? 31.175 -24.454 3.453   1.00 15.81 ?  110 LYS   B H    1 
ATOM   5651 H  HA   . LYS   B 1 110 ? 31.154 -23.590 0.988   1.00 15.58 ?  110 LYS   B HA   1 
ATOM   5652 H  HB2  . LYS   B 1 110 ? 29.229 -24.498 2.007   1.00 16.32 ?  110 LYS   B HB2  1 
ATOM   5653 H  HB3  . LYS   B 1 110 ? 29.086 -23.164 2.857   1.00 16.32 ?  110 LYS   B HB3  1 
ATOM   5654 H  HG2  . LYS   B 1 110 ? 28.596 -21.947 0.979   1.00 16.63 ?  110 LYS   B HG2  1 
ATOM   5655 H  HG3  . LYS   B 1 110 ? 28.944 -23.181 0.038   1.00 16.63 ?  110 LYS   B HG3  1 
ATOM   5656 H  HD2  . LYS   B 1 110 ? 27.071 -24.321 0.906   1.00 16.91 ?  110 LYS   B HD2  1 
ATOM   5657 H  HD3  . LYS   B 1 110 ? 26.698 -23.014 1.737   1.00 16.91 ?  110 LYS   B HD3  1 
ATOM   5658 H  HE2  . LYS   B 1 110 ? 25.397 -22.912 -0.112  1.00 17.93 ?  110 LYS   B HE2  1 
ATOM   5659 H  HE3  . LYS   B 1 110 ? 26.564 -21.868 -0.384  1.00 17.93 ?  110 LYS   B HE3  1 
ATOM   5660 H  HZ1  . LYS   B 1 110 ? 26.217 -23.166 -2.214  1.00 18.04 ?  110 LYS   B HZ1  1 
ATOM   5661 H  HZ2  . LYS   B 1 110 ? 27.552 -23.426 -1.715  1.00 18.04 ?  110 LYS   B HZ2  1 
ATOM   5662 H  HZ3  . LYS   B 1 110 ? 26.488 -24.378 -1.467  1.00 18.04 ?  110 LYS   B HZ3  1 
ATOM   5663 N  N    . SER   B 1 111 ? 31.256 -21.248 3.185   1.00 13.13 ?  111 SER   B N    1 
ATOM   5664 C  CA   . SER   B 1 111 ? 31.643 -19.847 3.358   1.00 12.99 ?  111 SER   B CA   1 
ATOM   5665 C  C    . SER   B 1 111 ? 33.021 -19.585 2.768   1.00 12.32 ?  111 SER   B C    1 
ATOM   5666 O  O    . SER   B 1 111 ? 33.245 -18.551 2.120   1.00 12.26 ?  111 SER   B O    1 
ATOM   5667 C  CB   . SER   B 1 111 ? 31.638 -19.483 4.841   1.00 14.08 ?  111 SER   B CB   1 
ATOM   5668 O  OG   . SER   B 1 111 ? 30.329 -19.476 5.367   1.00 15.50 ?  111 SER   B OG   1 
ATOM   5669 H  H    . SER   B 1 111 ? 31.059 -21.662 3.911   1.00 15.81 ?  111 SER   B H    1 
ATOM   5670 H  HA   . SER   B 1 111 ? 31.005 -19.280 2.901   1.00 15.64 ?  111 SER   B HA   1 
ATOM   5671 H  HB2  . SER   B 1 111 ? 32.161 -20.135 5.329   1.00 16.95 ?  111 SER   B HB2  1 
ATOM   5672 H  HB3  . SER   B 1 111 ? 32.014 -18.601 4.951   1.00 16.95 ?  111 SER   B HB3  1 
ATOM   5673 H  HG   . SER   B 1 111 ? 30.339 -19.277 6.188   1.00 18.66 ?  111 SER   B HG   1 
ATOM   5674 N  N    . ALA   B 1 112 ? 33.961 -20.504 2.994   1.00 12.07 ?  112 ALA   B N    1 
ATOM   5675 C  CA   . ALA   B 1 112 ? 35.305 -20.339 2.450   1.00 11.85 ?  112 ALA   B CA   1 
ATOM   5676 C  C    . ALA   B 1 112 ? 35.271 -20.234 0.928   1.00 11.38 ?  112 ALA   B C    1 
ATOM   5677 O  O    . ALA   B 1 112 ? 35.898 -19.345 0.335   1.00 11.81 ?  112 ALA   B O    1 
ATOM   5678 C  CB   . ALA   B 1 112 ? 36.201 -21.491 2.911   1.00 12.37 ?  112 ALA   B CB   1 
ATOM   5679 H  H    . ALA   B 1 112 ? 33.847 -21.222 3.465   1.00 14.54 ?  112 ALA   B H    1 
ATOM   5680 H  HA   . ALA   B 1 112 ? 35.681 -19.519 2.797   1.00 14.28 ?  112 ALA   B HA   1 
ATOM   5681 H  HB1  . ALA   B 1 112 ? 37.091 -21.363 2.544   1.00 14.90 ?  112 ALA   B HB1  1 
ATOM   5682 H  HB2  . ALA   B 1 112 ? 36.246 -21.490 3.883   1.00 14.90 ?  112 ALA   B HB2  1 
ATOM   5683 H  HB3  . ALA   B 1 112 ? 35.832 -22.330 2.600   1.00 14.90 ?  112 ALA   B HB3  1 
ATOM   5684 N  N    . TYR   B 1 113 ? 34.537 -21.137 0.273   1.00 11.64 ?  113 TYR   B N    1 
ATOM   5685 C  CA   . TYR   B 1 113 ? 34.463 -21.093 -1.181  1.00 11.20 ?  113 TYR   B CA   1 
ATOM   5686 C  C    . TYR   B 1 113 ? 33.754 -19.846 -1.698  1.00 10.96 ?  113 TYR   B C    1 
ATOM   5687 O  O    . TYR   B 1 113 ? 34.027 -19.417 -2.823  1.00 10.94 ?  113 TYR   B O    1 
ATOM   5688 C  CB   . TYR   B 1 113 ? 33.790 -22.353 -1.728  1.00 11.68 ?  113 TYR   B CB   1 
ATOM   5689 C  CG   . TYR   B 1 113 ? 34.749 -23.502 -1.995  1.00 12.00 ?  113 TYR   B CG   1 
ATOM   5690 C  CD1  . TYR   B 1 113 ? 35.740 -23.396 -2.963  1.00 12.54 ?  113 TYR   B CD1  1 
ATOM   5691 C  CD2  . TYR   B 1 113 ? 34.651 -24.696 -1.292  1.00 12.34 ?  113 TYR   B CD2  1 
ATOM   5692 C  CE1  . TYR   B 1 113 ? 36.621 -24.432 -3.212  1.00 12.47 ?  113 TYR   B CE1  1 
ATOM   5693 C  CE2  . TYR   B 1 113 ? 35.519 -25.743 -1.539  1.00 12.40 ?  113 TYR   B CE2  1 
ATOM   5694 C  CZ   . TYR   B 1 113 ? 36.500 -25.609 -2.503  1.00 12.52 ?  113 TYR   B CZ   1 
ATOM   5695 O  OH   . TYR   B 1 113 ? 37.382 -26.628 -2.777  1.00 13.53 ?  113 TYR   B OH   1 
ATOM   5696 H  H    . TYR   B 1 113 ? 34.074 -21.765 0.647   1.00 14.03 ?  113 TYR   B H    1 
ATOM   5697 H  HA   . TYR   B 1 113 ? 35.364 -21.077 -1.518  1.00 13.50 ?  113 TYR   B HA   1 
ATOM   5698 H  HB2  . TYR   B 1 113 ? 33.132 -22.668 -1.085  1.00 14.07 ?  113 TYR   B HB2  1 
ATOM   5699 H  HB3  . TYR   B 1 113 ? 33.350 -22.135 -2.563  1.00 14.07 ?  113 TYR   B HB3  1 
ATOM   5700 H  HD1  . TYR   B 1 113 ? 35.826 -22.601 -3.446  1.00 15.10 ?  113 TYR   B HD1  1 
ATOM   5701 H  HD2  . TYR   B 1 113 ? 33.986 -24.790 -0.650  1.00 14.86 ?  113 TYR   B HD2  1 
ATOM   5702 H  HE1  . TYR   B 1 113 ? 37.279 -24.341 -3.872  1.00 15.02 ?  113 TYR   B HE1  1 
ATOM   5703 H  HE2  . TYR   B 1 113 ? 35.435 -26.539 -1.069  1.00 14.94 ?  113 TYR   B HE2  1 
ATOM   5704 H  HH   . TYR   B 1 113 ? 37.174 -27.314 -2.344  1.00 16.29 ?  113 TYR   B HH   1 
ATOM   5705 N  N    . GLU   B 1 114 ? 32.826 -19.269 -0.923  1.00 11.26 ?  114 GLU   B N    1 
ATOM   5706 C  CA   . GLU   B 1 114 ? 32.144 -18.058 -1.375  1.00 11.29 ?  114 GLU   B CA   1 
ATOM   5707 C  C    . GLU   B 1 114 ? 33.129 -16.937 -1.673  1.00 11.25 ?  114 GLU   B C    1 
ATOM   5708 O  O    . GLU   B 1 114 ? 32.847 -16.074 -2.507  1.00 11.44 ?  114 GLU   B O    1 
ATOM   5709 C  CB   . GLU   B 1 114 ? 31.081 -17.629 -0.358  1.00 11.61 ?  114 GLU   B CB   1 
ATOM   5710 C  CG   . GLU   B 1 114 ? 29.861 -18.548 -0.422  1.00 11.59 ?  114 GLU   B CG   1 
ATOM   5711 C  CD   . GLU   B 1 114 ? 28.848 -18.364 0.694   1.00 11.95 ?  114 GLU   B CD   1 
ATOM   5712 O  OE1  . GLU   B 1 114 ? 29.140 -17.750 1.740   1.00 12.24 ?  114 GLU   B OE1  1 
ATOM   5713 O  OE2  . GLU   B 1 114 ? 27.725 -18.899 0.529   1.00 12.83 -1 114 GLU   B OE2  1 
ATOM   5714 H  H    . GLU   B 1 114 ? 32.570 -19.563 -0.152  1.00 13.57 ?  114 GLU   B H    1 
ATOM   5715 H  HA   . GLU   B 1 114 ? 31.688 -18.256 -2.199  1.00 13.60 ?  114 GLU   B HA   1 
ATOM   5716 H  HB2  . GLU   B 1 114 ? 31.452 -17.681 0.539   1.00 13.99 ?  114 GLU   B HB2  1 
ATOM   5717 H  HB3  . GLU   B 1 114 ? 30.793 -16.728 -0.554  1.00 13.99 ?  114 GLU   B HB3  1 
ATOM   5718 H  HG2  . GLU   B 1 114 ? 29.408 -18.395 -1.262  1.00 13.96 ?  114 GLU   B HG2  1 
ATOM   5719 H  HG3  . GLU   B 1 114 ? 30.171 -19.470 -0.384  1.00 13.96 ?  114 GLU   B HG3  1 
ATOM   5720 N  N    . ASN   B 1 115 ? 34.295 -16.935 -1.024  1.00 11.19 ?  115 ASN   B N    1 
ATOM   5721 C  CA   . ASN   B 1 115 ? 35.284 -15.901 -1.322  1.00 10.69 ?  115 ASN   B CA   1 
ATOM   5722 C  C    . ASN   B 1 115 ? 35.692 -15.921 -2.789  1.00 10.47 ?  115 ASN   B C    1 
ATOM   5723 O  O    . ASN   B 1 115 ? 36.078 -14.881 -3.345  1.00 11.03 ?  115 ASN   B O    1 
ATOM   5724 C  CB   . ASN   B 1 115 ? 36.526 -16.080 -0.445  1.00 11.23 ?  115 ASN   B CB   1 
ATOM   5725 C  CG   . ASN   B 1 115 ? 36.265 -15.807 1.016   1.00 11.81 ?  115 ASN   B CG   1 
ATOM   5726 O  OD1  . ASN   B 1 115 ? 36.275 -14.659 1.456   1.00 13.63 ?  115 ASN   B OD1  1 
ATOM   5727 N  ND2  . ASN   B 1 115 ? 36.092 -16.869 1.794   1.00 11.85 ?  115 ASN   B ND2  1 
ATOM   5728 H  H    . ASN   B 1 115 ? 34.532 -17.499 -0.411  1.00 13.48 ?  115 ASN   B H    1 
ATOM   5729 H  HA   . ASN   B 1 115 ? 34.905 -15.032 -1.126  1.00 12.88 ?  115 ASN   B HA   1 
ATOM   5730 H  HB2  . ASN   B 1 115 ? 36.846 -16.991 -0.529  1.00 13.53 ?  115 ASN   B HB2  1 
ATOM   5731 H  HB3  . ASN   B 1 115 ? 37.212 -15.460 -0.741  1.00 13.53 ?  115 ASN   B HB3  1 
ATOM   5732 H  HD21 . ASN   B 1 115 ? 35.947 -16.766 2.638   1.00 14.28 ?  115 ASN   B HD21 1 
ATOM   5733 H  HD22 . ASN   B 1 115 ? 36.106 -17.659 1.457   1.00 14.28 ?  115 ASN   B HD22 1 
ATOM   5734 N  N    . PHE   B 1 116 ? 35.660 -17.098 -3.425  1.00 10.28 ?  116 PHE   B N    1 
ATOM   5735 C  CA   . PHE   B 1 116 ? 36.089 -17.191 -4.814  1.00 10.80 ?  116 PHE   B CA   1 
ATOM   5736 C  C    . PHE   B 1 116 ? 35.188 -16.368 -5.723  1.00 10.53 ?  116 PHE   B C    1 
ATOM   5737 O  O    . PHE   B 1 116 ? 35.620 -15.946 -6.800  1.00 10.93 ?  116 PHE   B O    1 
ATOM   5738 C  CB   . PHE   B 1 116 ? 36.053 -18.637 -5.329  1.00 10.65 ?  116 PHE   B CB   1 
ATOM   5739 C  CG   . PHE   B 1 116 ? 37.128 -19.588 -4.781  1.00 10.53 ?  116 PHE   B CG   1 
ATOM   5740 C  CD1  . PHE   B 1 116 ? 37.782 -19.405 -3.570  1.00 11.36 ?  116 PHE   B CD1  1 
ATOM   5741 C  CD2  . PHE   B 1 116 ? 37.429 -20.727 -5.515  1.00 11.02 ?  116 PHE   B CD2  1 
ATOM   5742 C  CE1  . PHE   B 1 116 ? 38.717 -20.340 -3.116  1.00 11.46 ?  116 PHE   B CE1  1 
ATOM   5743 C  CE2  . PHE   B 1 116 ? 38.358 -21.662 -5.069  1.00 10.91 ?  116 PHE   B CE2  1 
ATOM   5744 C  CZ   . PHE   B 1 116 ? 39.001 -21.472 -3.876  1.00 11.24 ?  116 PHE   B CZ   1 
ATOM   5745 H  H    . PHE   B 1 116 ? 35.395 -17.846 -3.079  1.00 12.39 ?  116 PHE   B H    1 
ATOM   5746 H  HA   . PHE   B 1 116 ? 36.995 -16.860 -4.894  1.00 13.01 ?  116 PHE   B HA   1 
ATOM   5747 H  HB2  . PHE   B 1 116 ? 35.185 -19.017 -5.101  1.00 12.84 ?  116 PHE   B HB2  1 
ATOM   5748 H  HB3  . PHE   B 1 116 ? 36.145 -18.617 -6.294  1.00 12.84 ?  116 PHE   B HB3  1 
ATOM   5749 H  HD1  . PHE   B 1 116 ? 37.585 -18.656 -3.053  1.00 13.69 ?  116 PHE   B HD1  1 
ATOM   5750 H  HD2  . PHE   B 1 116 ? 36.992 -20.875 -6.321  1.00 13.28 ?  116 PHE   B HD2  1 
ATOM   5751 H  HE1  . PHE   B 1 116 ? 39.158 -20.205 -2.308  1.00 13.81 ?  116 PHE   B HE1  1 
ATOM   5752 H  HE2  . PHE   B 1 116 ? 38.551 -22.410 -5.583  1.00 13.14 ?  116 PHE   B HE2  1 
ATOM   5753 H  HZ   . PHE   B 1 116 ? 39.637 -22.084 -3.581  1.00 13.55 ?  116 PHE   B HZ   1 
ATOM   5754 N  N    . ASN   B 1 117 ? 33.921 -16.165 -5.333  1.00 10.95 ?  117 ASN   B N    1 
ATOM   5755 C  CA   . ASN   B 1 117 ? 32.969 -15.464 -6.197  1.00 11.22 ?  117 ASN   B CA   1 
ATOM   5756 C  C    . ASN   B 1 117 ? 33.278 -13.984 -6.354  1.00 11.41 ?  117 ASN   B C    1 
ATOM   5757 O  O    . ASN   B 1 117 ? 32.677 -13.329 -7.211  1.00 12.84 ?  117 ASN   B O    1 
ATOM   5758 C  CB   . ASN   B 1 117 ? 31.544 -15.683 -5.708  1.00 11.23 ?  117 ASN   B CB   1 
ATOM   5759 C  CG   . ASN   B 1 117 ? 31.092 -17.095 -5.961  1.00 11.47 ?  117 ASN   B CG   1 
ATOM   5760 O  OD1  . ASN   B 1 117 ? 31.447 -17.686 -6.982  1.00 12.35 ?  117 ASN   B OD1  1 
ATOM   5761 N  ND2  . ASN   B 1 117 ? 30.363 -17.669 -5.019  1.00 11.68 ?  117 ASN   B ND2  1 
ATOM   5762 H  H    . ASN   B 1 117 ? 33.596 -16.424 -4.574  1.00 13.20 ?  117 ASN   B H    1 
ATOM   5763 H  HA   . ASN   B 1 117 ? 33.034 -15.862 -7.075  1.00 13.52 ?  117 ASN   B HA   1 
ATOM   5764 H  HB2  . ASN   B 1 117 ? 31.503 -15.518 -4.750  1.00 13.53 ?  117 ASN   B HB2  1 
ATOM   5765 H  HB3  . ASN   B 1 117 ? 30.952 -15.075 -6.176  1.00 13.53 ?  117 ASN   B HB3  1 
ATOM   5766 H  HD21 . ASN   B 1 117 ? 30.082 -18.474 -5.122  1.00 14.07 ?  117 ASN   B HD21 1 
ATOM   5767 H  HD22 . ASN   B 1 117 ? 30.144 -17.224 -4.315  1.00 14.07 ?  117 ASN   B HD22 1 
ATOM   5768 N  N    . GLN   B 1 118 ? 34.221 -13.460 -5.581  1.00 11.14 ?  118 GLN   B N    1 
ATOM   5769 C  CA   . GLN   B 1 118 ? 34.651 -12.073 -5.718  1.00 11.77 ?  118 GLN   B CA   1 
ATOM   5770 C  C    . GLN   B 1 118 ? 35.718 -11.883 -6.790  1.00 12.02 ?  118 GLN   B C    1 
ATOM   5771 O  O    . GLN   B 1 118 ? 36.191 -10.755 -6.971  1.00 13.12 ?  118 GLN   B O    1 
ATOM   5772 C  CB   . GLN   B 1 118 ? 35.123 -11.536 -4.365  1.00 12.21 ?  118 GLN   B CB   1 
ATOM   5773 C  CG   . GLN   B 1 118 ? 34.041 -11.577 -3.296  1.00 12.21 ?  118 GLN   B CG   1 
ATOM   5774 C  CD   . GLN   B 1 118 ? 32.866 -10.670 -3.626  1.00 12.39 ?  118 GLN   B CD   1 
ATOM   5775 O  OE1  . GLN   B 1 118 ? 33.050 -9.528  -4.062  1.00 13.22 ?  118 GLN   B OE1  1 
ATOM   5776 N  NE2  . GLN   B 1 118 ? 31.651 -11.170 -3.426  1.00 12.60 ?  118 GLN   B NE2  1 
ATOM   5777 H  H    . GLN   B 1 118 ? 34.648 -13.888 -4.962  1.00 13.42 ?  118 GLN   B H    1 
ATOM   5778 H  HA   . GLN   B 1 118 ? 33.883 -11.547 -5.989  1.00 14.18 ?  118 GLN   B HA   1 
ATOM   5779 H  HB2  . GLN   B 1 118 ? 35.872 -12.060 -4.057  1.00 14.71 ?  118 GLN   B HB2  1 
ATOM   5780 H  HB3  . GLN   B 1 118 ? 35.393 -10.604 -4.475  1.00 14.71 ?  118 GLN   B HB3  1 
ATOM   5781 H  HG2  . GLN   B 1 118 ? 33.708 -12.485 -3.216  1.00 14.71 ?  118 GLN   B HG2  1 
ATOM   5782 H  HG3  . GLN   B 1 118 ? 34.419 -11.287 -2.449  1.00 14.71 ?  118 GLN   B HG3  1 
ATOM   5783 H  HE21 . GLN   B 1 118 ? 31.561 -11.974 -3.124  1.00 15.17 ?  118 GLN   B HE21 1 
ATOM   5784 H  HE22 . GLN   B 1 118 ? 30.962 -10.695 -3.598  1.00 15.17 ?  118 GLN   B HE22 1 
ATOM   5785 N  N    . HIS   B 1 119 ? 36.068 -12.943 -7.524  1.00 11.31 ?  119 HIS   B N    1 
ATOM   5786 C  CA   . HIS   B 1 119 ? 37.110 -12.896 -8.543  1.00 11.82 ?  119 HIS   B CA   1 
ATOM   5787 C  C    . HIS   B 1 119 ? 36.633 -13.629 -9.782  1.00 11.68 ?  119 HIS   B C    1 
ATOM   5788 O  O    . HIS   B 1 119 ? 36.129 -14.748 -9.682  1.00 12.16 ?  119 HIS   B O    1 
ATOM   5789 C  CB   . HIS   B 1 119 ? 38.391 -13.526 -7.994  1.00 12.26 ?  119 HIS   B CB   1 
ATOM   5790 C  CG   . HIS   B 1 119 ? 38.876 -12.818 -6.776  1.00 13.22 ?  119 HIS   B CG   1 
ATOM   5791 N  ND1  . HIS   B 1 119 ? 39.668 -11.692 -6.841  1.00 14.72 ?  119 HIS   B ND1  1 
ATOM   5792 C  CD2  . HIS   B 1 119 ? 38.585 -13.001 -5.468  1.00 14.37 ?  119 HIS   B CD2  1 
ATOM   5793 C  CE1  . HIS   B 1 119 ? 39.879 -11.239 -5.619  1.00 15.89 ?  119 HIS   B CE1  1 
ATOM   5794 N  NE2  . HIS   B 1 119 ? 39.227 -12.009 -4.769  1.00 15.89 ?  119 HIS   B NE2  1 
ATOM   5795 H  H    . HIS   B 1 119 ? 35.700 -13.720 -7.454  1.00 13.62 ?  119 HIS   B H    1 
ATOM   5796 H  HA   . HIS   B 1 119 ? 37.291 -11.972 -8.783  1.00 14.24 ?  119 HIS   B HA   1 
ATOM   5797 H  HB2  . HIS   B 1 119 ? 38.216 -14.447 -7.765  1.00 14.77 ?  119 HIS   B HB2  1 
ATOM   5798 H  HB3  . HIS   B 1 119 ? 39.083 -13.472 -8.674  1.00 14.77 ?  119 HIS   B HB3  1 
ATOM   5799 H  HD2  . HIS   B 1 119 ? 38.052 -13.675 -5.111  1.00 17.30 ?  119 HIS   B HD2  1 
ATOM   5800 H  HE1  . HIS   B 1 119 ? 40.408 -10.506 -5.394  1.00 19.12 ?  119 HIS   B HE1  1 
ATOM   5801 H  HE2  . HIS   B 1 119 ? 39.231 -11.923 -3.913  1.00 19.12 ?  119 HIS   B HE2  1 
ATOM   5802 N  N    . GLU   B 1 120 ? 36.785 -13.006 -10.950 1.00 12.18 ?  120 GLU   B N    1 
ATOM   5803 C  CA   . GLU   B 1 120 ? 36.195 -13.588 -12.151 1.00 13.86 ?  120 GLU   B CA   1 
ATOM   5804 C  C    . GLU   B 1 120 ? 36.867 -14.891 -12.565 1.00 12.60 ?  120 GLU   B C    1 
ATOM   5805 O  O    . GLU   B 1 120 ? 36.203 -15.766 -13.132 1.00 12.75 ?  120 GLU   B O    1 
ATOM   5806 C  CB   . GLU   B 1 120 ? 36.206 -12.579 -13.295 1.00 18.80 ?  120 GLU   B CB   1 
ATOM   5807 C  CG   . GLU   B 1 120 ? 35.240 -11.427 -13.080 1.00 25.77 ?  120 GLU   B CG   1 
ATOM   5808 C  CD   . GLU   B 1 120 ? 35.100 -10.539 -14.300 1.00 32.76 ?  120 GLU   B CD   1 
ATOM   5809 O  OE1  . GLU   B 1 120 ? 36.113 -10.323 -15.000 1.00 35.38 ?  120 GLU   B OE1  1 
ATOM   5810 O  OE2  . GLU   B 1 120 ? 33.976 -10.059 -14.558 1.00 35.77 -1 120 GLU   B OE2  1 
ATOM   5811 H  H    . GLU   B 1 120 ? 37.207 -12.263 -11.074 1.00 14.67 ?  120 GLU   B H    1 
ATOM   5812 H  HA   . GLU   B 1 120 ? 35.271 -13.793 -11.966 1.00 16.69 ?  120 GLU   B HA   1 
ATOM   5813 H  HB2  . GLU   B 1 120 ? 37.093 -12.203 -13.386 1.00 22.62 ?  120 GLU   B HB2  1 
ATOM   5814 H  HB3  . GLU   B 1 120 ? 35.949 -13.027 -14.118 1.00 22.62 ?  120 GLU   B HB3  1 
ATOM   5815 H  HG2  . GLU   B 1 120 ? 34.360 -11.784 -12.865 1.00 30.97 ?  120 GLU   B HG2  1 
ATOM   5816 H  HG3  . GLU   B 1 120 ? 35.558 -10.875 -12.350 1.00 30.97 ?  120 GLU   B HG3  1 
ATOM   5817 N  N    . VAL   B 1 121 ? 38.167 -15.037 -12.306 1.00 12.12 ?  121 VAL   B N    1 
ATOM   5818 C  CA   . VAL   B 1 121 ? 38.915 -16.243 -12.656 1.00 12.01 ?  121 VAL   B CA   1 
ATOM   5819 C  C    . VAL   B 1 121 ? 40.026 -16.446 -11.632 1.00 11.50 ?  121 VAL   B C    1 
ATOM   5820 O  O    . VAL   B 1 121 ? 40.702 -15.488 -11.235 1.00 12.22 ?  121 VAL   B O    1 
ATOM   5821 C  CB   . VAL   B 1 121 ? 39.437 -16.193 -14.113 1.00 13.90 ?  121 VAL   B CB   1 
ATOM   5822 C  CG1  . VAL   B 1 121 ? 40.295 -14.960 -14.363 1.00 14.97 ?  121 VAL   B CG1  1 
ATOM   5823 C  CG2  . VAL   B 1 121 ? 40.187 -17.468 -14.462 1.00 15.05 ?  121 VAL   B CG2  1 
ATOM   5824 H  H    . VAL   B 1 121 ? 38.652 -14.433 -11.929 1.00 14.60 ?  121 VAL   B H    1 
ATOM   5825 H  HA   . VAL   B 1 121 ? 38.312 -16.997 -12.594 1.00 14.47 ?  121 VAL   B HA   1 
ATOM   5826 H  HB   . VAL   B 1 121 ? 38.673 -16.141 -14.711 1.00 16.73 ?  121 VAL   B HB   1 
ATOM   5827 H  HG11 . VAL   B 1 121 ? 40.611 -14.972 -15.282 1.00 18.02 ?  121 VAL   B HG11 1 
ATOM   5828 H  HG12 . VAL   B 1 121 ? 39.759 -14.164 -14.213 1.00 18.02 ?  121 VAL   B HG12 1 
ATOM   5829 H  HG13 . VAL   B 1 121 ? 41.051 -14.968 -13.756 1.00 18.02 ?  121 VAL   B HG13 1 
ATOM   5830 H  HG21 . VAL   B 1 121 ? 40.385 -17.467 -15.414 1.00 18.12 ?  121 VAL   B HG21 1 
ATOM   5831 H  HG22 . VAL   B 1 121 ? 41.014 -17.499 -13.956 1.00 18.12 ?  121 VAL   B HG22 1 
ATOM   5832 H  HG23 . VAL   B 1 121 ? 39.633 -18.232 -14.243 1.00 18.12 ?  121 VAL   B HG23 1 
ATOM   5833 N  N    . LEU   B 1 122 ? 40.211 -17.701 -11.199 1.00 10.97 ?  122 LEU   B N    1 
ATOM   5834 C  CA   . LEU   B 1 122 ? 41.196 -18.049 -10.176 1.00 10.65 ?  122 LEU   B CA   1 
ATOM   5835 C  C    . LEU   B 1 122 ? 41.852 -19.382 -10.502 1.00 10.62 ?  122 LEU   B C    1 
ATOM   5836 O  O    . LEU   B 1 122 ? 41.193 -20.303 -11.000 1.00 11.71 ?  122 LEU   B O    1 
ATOM   5837 C  CB   . LEU   B 1 122 ? 40.542 -18.278 -8.799  1.00 12.41 ?  122 LEU   B CB   1 
ATOM   5838 C  CG   . LEU   B 1 122 ? 39.511 -17.256 -8.310  1.00 12.30 ?  122 LEU   B CG   1 
ATOM   5839 C  CD1  . LEU   B 1 122 ? 38.108 -17.618 -8.768  1.00 13.33 ?  122 LEU   B CD1  1 
ATOM   5840 C  CD2  . LEU   B 1 122 ? 39.571 -17.139 -6.800  1.00 12.09 ?  122 LEU   B CD2  1 
ATOM   5841 H  H    . LEU   B 1 122 ? 39.766 -18.380 -11.488 1.00 13.22 ?  122 LEU   B H    1 
ATOM   5842 H  HA   . LEU   B 1 122 ? 41.871 -17.353 -10.103 1.00 12.84 ?  122 LEU   B HA   1 
ATOM   5843 H  HB2  . LEU   B 1 122 ? 40.097 -19.136 -8.822  1.00 14.95 ?  122 LEU   B HB2  1 
ATOM   5844 H  HB3  . LEU   B 1 122 ? 41.248 -18.300 -8.135  1.00 14.95 ?  122 LEU   B HB3  1 
ATOM   5845 H  HG   . LEU   B 1 122 ? 39.729 -16.388 -8.684  1.00 14.81 ?  122 LEU   B HG   1 
ATOM   5846 H  HD11 . LEU   B 1 122 ? 37.486 -16.964 -8.415  1.00 16.06 ?  122 LEU   B HD11 1 
ATOM   5847 H  HD12 . LEU   B 1 122 ? 38.081 -17.612 -9.737  1.00 16.06 ?  122 LEU   B HD12 1 
ATOM   5848 H  HD13 . LEU   B 1 122 ? 37.887 -18.500 -8.435  1.00 16.06 ?  122 LEU   B HD13 1 
ATOM   5849 H  HD21 . LEU   B 1 122 ? 38.891 -16.518 -6.502  1.00 14.57 ?  122 LEU   B HD21 1 
ATOM   5850 H  HD22 . LEU   B 1 122 ? 39.419 -18.013 -6.408  1.00 14.57 ?  122 LEU   B HD22 1 
ATOM   5851 H  HD23 . LEU   B 1 122 ? 40.451 -16.813 -6.544  1.00 14.57 ?  122 LEU   B HD23 1 
ATOM   5852 N  N    . LEU   B 1 123 ? 43.139 -19.489 -10.145 1.00 10.48 ?  123 LEU   B N    1 
ATOM   5853 C  CA   . LEU   B 1 123 ? 43.853 -20.757 -10.024 1.00 10.83 ?  123 LEU   B CA   1 
ATOM   5854 C  C    . LEU   B 1 123 ? 43.827 -21.144 -8.549  1.00 10.39 ?  123 LEU   B C    1 
ATOM   5855 O  O    . LEU   B 1 123 ? 44.178 -20.316 -7.698  1.00 10.85 ?  123 LEU   B O    1 
ATOM   5856 C  CB   . LEU   B 1 123 ? 45.302 -20.574 -10.487 1.00 10.96 ?  123 LEU   B CB   1 
ATOM   5857 C  CG   . LEU   B 1 123 ? 46.249 -21.754 -10.240 1.00 11.51 ?  123 LEU   B CG   1 
ATOM   5858 C  CD1  . LEU   B 1 123 ? 45.832 -22.998 -11.024 1.00 12.23 ?  123 LEU   B CD1  1 
ATOM   5859 C  CD2  . LEU   B 1 123 ? 47.670 -21.362 -10.602 1.00 12.29 ?  123 LEU   B CD2  1 
ATOM   5860 H  H    . LEU   B 1 123 ? 43.637 -18.809 -9.957  1.00 12.63 ?  123 LEU   B H    1 
ATOM   5861 H  HA   . LEU   B 1 123 ? 43.413 -21.447 -10.551 1.00 13.05 ?  123 LEU   B HA   1 
ATOM   5862 H  HB2  . LEU   B 1 123 ? 45.290 -20.413 -11.445 1.00 13.21 ?  123 LEU   B HB2  1 
ATOM   5863 H  HB3  . LEU   B 1 123 ? 45.670 -19.809 -10.032 1.00 13.21 ?  123 LEU   B HB3  1 
ATOM   5864 H  HG   . LEU   B 1 123 ? 46.238 -21.985 -9.298  1.00 13.87 ?  123 LEU   B HG   1 
ATOM   5865 H  HD11 . LEU   B 1 123 ? 46.471 -23.706 -10.848 1.00 14.73 ?  123 LEU   B HD11 1 
ATOM   5866 H  HD12 . LEU   B 1 123 ? 44.948 -23.266 -10.740 1.00 14.73 ?  123 LEU   B HD12 1 
ATOM   5867 H  HD13 . LEU   B 1 123 ? 45.829 -22.782 -11.970 1.00 14.73 ?  123 LEU   B HD13 1 
ATOM   5868 H  HD21 . LEU   B 1 123 ? 48.259 -22.115 -10.441 1.00 14.80 ?  123 LEU   B HD21 1 
ATOM   5869 H  HD22 . LEU   B 1 123 ? 47.701 -21.112 -11.539 1.00 14.80 ?  123 LEU   B HD22 1 
ATOM   5870 H  HD23 . LEU   B 1 123 ? 47.938 -20.609 -10.051 1.00 14.80 ?  123 LEU   B HD23 1 
ATOM   5871 N  N    . ALA   B 1 124 ? 43.396 -22.373 -8.239  1.00 10.34 ?  124 ALA   B N    1 
ATOM   5872 C  CA   . ALA   B 1 124 ? 43.145 -22.700 -6.843  1.00 10.53 ?  124 ALA   B CA   1 
ATOM   5873 C  C    . ALA   B 1 124 ? 43.415 -24.158 -6.511  1.00 10.27 ?  124 ALA   B C    1 
ATOM   5874 O  O    . ALA   B 1 124 ? 43.281 -25.032 -7.377  1.00 10.91 ?  124 ALA   B O    1 
ATOM   5875 C  CB   . ALA   B 1 124 ? 41.688 -22.385 -6.471  1.00 11.07 ?  124 ALA   B CB   1 
ATOM   5876 H  H    . ALA   B 1 124 ? 43.228 -23.012 -8.802  1.00 12.46 ?  124 ALA   B H    1 
ATOM   5877 H  HA   . ALA   B 1 124 ? 43.718 -22.144 -6.298  1.00 12.69 ?  124 ALA   B HA   1 
ATOM   5878 H  HB1  . ALA   B 1 124 ? 41.542 -22.603 -5.538  1.00 13.34 ?  124 ALA   B HB1  1 
ATOM   5879 H  HB2  . ALA   B 1 124 ? 41.524 -21.436 -6.616  1.00 13.34 ?  124 ALA   B HB2  1 
ATOM   5880 H  HB3  . ALA   B 1 124 ? 41.095 -22.908 -7.032  1.00 13.34 ?  124 ALA   B HB3  1 
ATOM   5881 N  N    . PRO   B 1 125 ? 43.708 -24.447 -5.247  1.00 10.51 ?  125 PRO   B N    1 
ATOM   5882 C  CA   . PRO   B 1 125 ? 43.651 -25.813 -4.726  1.00 11.04 ?  125 PRO   B CA   1 
ATOM   5883 C  C    . PRO   B 1 125 ? 42.250 -26.090 -4.185  1.00 11.32 ?  125 PRO   B C    1 
ATOM   5884 O  O    . PRO   B 1 125 ? 41.452 -25.176 -3.974  1.00 11.76 ?  125 PRO   B O    1 
ATOM   5885 C  CB   . PRO   B 1 125 ? 44.629 -25.734 -3.548  1.00 12.15 ?  125 PRO   B CB   1 
ATOM   5886 C  CG   . PRO   B 1 125 ? 44.371 -24.343 -2.980  1.00 12.10 ?  125 PRO   B CG   1 
ATOM   5887 C  CD   . PRO   B 1 125 ? 44.035 -23.476 -4.186  1.00 11.14 ?  125 PRO   B CD   1 
ATOM   5888 H  HA   . PRO   B 1 125 ? 43.929 -26.484 -5.368  1.00 13.30 ?  125 PRO   B HA   1 
ATOM   5889 H  HB2  . PRO   B 1 125 ? 44.420 -26.416 -2.888  1.00 14.64 ?  125 PRO   B HB2  1 
ATOM   5890 H  HB3  . PRO   B 1 125 ? 45.538 -25.813 -3.862  1.00 14.64 ?  125 PRO   B HB3  1 
ATOM   5891 H  HG2  . PRO   B 1 125 ? 43.616 -24.364 -2.363  1.00 14.57 ?  125 PRO   B HG2  1 
ATOM   5892 H  HG3  . PRO   B 1 125 ? 45.164 -24.010 -2.528  1.00 14.57 ?  125 PRO   B HG3  1 
ATOM   5893 H  HD2  . PRO   B 1 125 ? 43.274 -22.905 -4.001  1.00 13.43 ?  125 PRO   B HD2  1 
ATOM   5894 H  HD3  . PRO   B 1 125 ? 44.814 -22.945 -4.444  1.00 13.43 ?  125 PRO   B HD3  1 
ATOM   5895 N  N    . LEU   B 1 126 ? 41.985 -27.368 -3.904  1.00 11.95 ?  126 LEU   B N    1 
ATOM   5896 C  CA   . LEU   B 1 126 ? 40.764 -27.737 -3.193  1.00 12.42 ?  126 LEU   B CA   1 
ATOM   5897 C  C    . LEU   B 1 126 ? 40.882 -27.336 -1.731  1.00 12.58 ?  126 LEU   B C    1 
ATOM   5898 O  O    . LEU   B 1 126 ? 41.770 -27.805 -1.013  1.00 14.45 ?  126 LEU   B O    1 
ATOM   5899 C  CB   . LEU   B 1 126 ? 40.508 -29.235 -3.306  1.00 13.79 ?  126 LEU   B CB   1 
ATOM   5900 C  CG   . LEU   B 1 126 ? 39.990 -29.715 -4.664  1.00 14.83 ?  126 LEU   B CG   1 
ATOM   5901 C  CD1  . LEU   B 1 126 ? 40.045 -31.222 -4.768  1.00 16.87 ?  126 LEU   B CD1  1 
ATOM   5902 C  CD2  . LEU   B 1 126 ? 38.566 -29.220 -4.907  1.00 14.98 ?  126 LEU   B CD2  1 
ATOM   5903 H  H    . LEU   B 1 126 ? 42.494 -28.034 -4.097  1.00 14.40 ?  126 LEU   B H    1 
ATOM   5904 H  HA   . LEU   B 1 126 ? 40.013 -27.261 -3.579  1.00 14.96 ?  126 LEU   B HA   1 
ATOM   5905 H  HB2  . LEU   B 1 126 ? 41.339 -29.698 -3.129  1.00 16.60 ?  126 LEU   B HB2  1 
ATOM   5906 H  HB3  . LEU   B 1 126 ? 39.849 -29.481 -2.640  1.00 16.60 ?  126 LEU   B HB3  1 
ATOM   5907 H  HG   . LEU   B 1 126 ? 40.558 -29.347 -5.362  1.00 17.85 ?  126 LEU   B HG   1 
ATOM   5908 H  HD11 . LEU   B 1 126 ? 39.711 -31.490 -5.640  1.00 20.30 ?  126 LEU   B HD11 1 
ATOM   5909 H  HD12 . LEU   B 1 126 ? 40.960 -31.516 -4.658  1.00 20.30 ?  126 LEU   B HD12 1 
ATOM   5910 H  HD13 . LEU   B 1 126 ? 39.486 -31.606 -4.071  1.00 20.30 ?  126 LEU   B HD13 1 
ATOM   5911 H  HD21 . LEU   B 1 126 ? 38.226 -29.630 -5.717  1.00 18.03 ?  126 LEU   B HD21 1 
ATOM   5912 H  HD22 . LEU   B 1 126 ? 38.014 -29.466 -4.151  1.00 18.03 ?  126 LEU   B HD22 1 
ATOM   5913 H  HD23 . LEU   B 1 126 ? 38.580 -28.253 -5.007  1.00 18.03 ?  126 LEU   B HD23 1 
ATOM   5914 N  N    . LEU   B 1 127 ? 39.960 -26.495 -1.278  1.00 12.75 ?  127 LEU   B N    1 
ATOM   5915 C  CA   . LEU   B 1 127 ? 40.011 -26.006 0.088   1.00 12.95 ?  127 LEU   B CA   1 
ATOM   5916 C  C    . LEU   B 1 127 ? 39.740 -27.126 1.082   1.00 12.59 ?  127 LEU   B C    1 
ATOM   5917 O  O    . LEU   B 1 127 ? 38.919 -28.023 0.850   1.00 13.13 ?  127 LEU   B O    1 
ATOM   5918 C  CB   . LEU   B 1 127 ? 38.989 -24.884 0.292   1.00 13.49 ?  127 LEU   B CB   1 
ATOM   5919 C  CG   . LEU   B 1 127 ? 39.163 -23.620 -0.555  1.00 13.81 ?  127 LEU   B CG   1 
ATOM   5920 C  CD1  . LEU   B 1 127 ? 38.036 -22.648 -0.249  1.00 13.91 ?  127 LEU   B CD1  1 
ATOM   5921 C  CD2  . LEU   B 1 127 ? 40.515 -22.968 -0.318  1.00 14.52 ?  127 LEU   B CD2  1 
ATOM   5922 H  H    . LEU   B 1 127 ? 39.295 -26.189 -1.739  1.00 15.35 ?  127 LEU   B H    1 
ATOM   5923 H  HA   . LEU   B 1 127 ? 40.893 -25.644 0.266   1.00 15.59 ?  127 LEU   B HA   1 
ATOM   5924 H  HB2  . LEU   B 1 127 ? 38.106 -25.236 0.099   1.00 16.24 ?  127 LEU   B HB2  1 
ATOM   5925 H  HB3  . LEU   B 1 127 ? 39.022 -24.606 1.223   1.00 16.24 ?  127 LEU   B HB3  1 
ATOM   5926 H  HG   . LEU   B 1 127 ? 39.095 -23.850 -1.491  1.00 16.63 ?  127 LEU   B HG   1 
ATOM   5927 H  HD11 . LEU   B 1 127 ? 38.154 -21.841 -0.779  1.00 16.75 ?  127 LEU   B HD11 1 
ATOM   5928 H  HD12 . LEU   B 1 127 ? 37.185 -23.061 -0.467  1.00 16.75 ?  127 LEU   B HD12 1 
ATOM   5929 H  HD13 . LEU   B 1 127 ? 38.056 -22.421 0.697   1.00 16.75 ?  127 LEU   B HD13 1 
ATOM   5930 H  HD21 . LEU   B 1 127 ? 40.550 -22.122 -0.798  1.00 17.48 ?  127 LEU   B HD21 1 
ATOM   5931 H  HD22 . LEU   B 1 127 ? 40.630 -22.808 0.633   1.00 17.48 ?  127 LEU   B HD22 1 
ATOM   5932 H  HD23 . LEU   B 1 127 ? 41.209 -23.559 -0.642  1.00 17.48 ?  127 LEU   B HD23 1 
ATOM   5933 N  N    . SER   B 1 128 ? 40.423 -27.043 2.215   1.00 12.65 ?  128 SER   B N    1 
ATOM   5934 C  CA   . SER   B 1 128 ? 40.310 -27.959 3.340   1.00 13.03 ?  128 SER   B CA   1 
ATOM   5935 C  C    . SER   B 1 128 ? 40.800 -29.366 3.021   1.00 14.20 ?  128 SER   B C    1 
ATOM   5936 O  O    . SER   B 1 128 ? 40.706 -30.245 3.879   1.00 15.40 ?  128 SER   B O    1 
ATOM   5937 C  CB   . SER   B 1 128 ? 38.911 -27.964 3.969   1.00 13.64 ?  128 SER   B CB   1 
ATOM   5938 O  OG   . SER   B 1 128 ? 38.598 -26.691 4.525   1.00 14.23 ?  128 SER   B OG   1 
ATOM   5939 H  H    . SER   B 1 128 ? 41.000 -26.422 2.362   1.00 15.23 ?  128 SER   B H    1 
ATOM   5940 H  HA   . SER   B 1 128 ? 40.900 -27.627 4.025   1.00 15.69 ?  128 SER   B HA   1 
ATOM   5941 H  HB2  . SER   B 1 128 ? 38.255 -28.189 3.290   1.00 16.42 ?  128 SER   B HB2  1 
ATOM   5942 H  HB3  . SER   B 1 128 ? 38.888 -28.634 4.678   1.00 16.42 ?  128 SER   B HB3  1 
ATOM   5943 H  HG   . SER   B 1 128 ? 39.164 -26.493 5.113   1.00 17.13 ?  128 SER   B HG   1 
ATOM   5944 N  N    . ALA   B 1 129 ? 41.375 -29.587 1.838   1.00 15.40 ?  129 ALA   B N    1 
ATOM   5945 C  CA   . ALA   B 1 129 ? 41.921 -30.888 1.483   1.00 16.38 ?  129 ALA   B CA   1 
ATOM   5946 C  C    . ALA   B 1 129 ? 43.317 -31.063 2.072   1.00 15.42 ?  129 ALA   B C    1 
ATOM   5947 O  O    . ALA   B 1 129 ? 43.878 -30.162 2.710   1.00 15.21 ?  129 ALA   B O    1 
ATOM   5948 C  CB   . ALA   B 1 129 ? 41.964 -31.054 -0.033  1.00 18.60 ?  129 ALA   B CB   1 
ATOM   5949 H  H    . ALA   B 1 129 ? 41.464 -28.993 1.220   1.00 18.53 ?  129 ALA   B H    1 
ATOM   5950 H  HA   . ALA   B 1 129 ? 41.353 -31.580 1.846   1.00 19.71 ?  129 ALA   B HA   1 
ATOM   5951 H  HB1  . ALA   B 1 129 ? 42.322 -31.932 -0.244  1.00 22.37 ?  129 ALA   B HB1  1 
ATOM   5952 H  HB2  . ALA   B 1 129 ? 41.065 -30.970 -0.382  1.00 22.37 ?  129 ALA   B HB2  1 
ATOM   5953 H  HB3  . ALA   B 1 129 ? 42.535 -30.366 -0.411  1.00 22.37 ?  129 ALA   B HB3  1 
ATOM   5954 N  N    . GLY   B 1 130 ? 43.881 -32.248 1.844   1.00 15.19 ?  130 GLY   B N    1 
ATOM   5955 C  CA   . GLY   B 1 130 ? 45.270 -32.481 2.192   1.00 15.91 ?  130 GLY   B CA   1 
ATOM   5956 C  C    . GLY   B 1 130 ? 45.482 -32.391 3.684   1.00 16.01 ?  130 GLY   B C    1 
ATOM   5957 O  O    . GLY   B 1 130 ? 44.781 -33.032 4.479   1.00 16.82 ?  130 GLY   B O    1 
ATOM   5958 H  H    . GLY   B 1 130 ? 43.485 -32.924 1.488   1.00 18.29 ?  130 GLY   B H    1 
ATOM   5959 H  HA2  . GLY   B 1 130 ? 45.540 -33.365 1.894   1.00 19.15 ?  130 GLY   B HA2  1 
ATOM   5960 H  HA3  . GLY   B 1 130 ? 45.832 -31.822 1.756   1.00 19.15 ?  130 GLY   B HA3  1 
ATOM   5961 N  N    . ILE   B 1 131 ? 46.458 -31.565 4.073   1.00 15.91 ?  131 ILE   B N    1 
ATOM   5962 C  CA   . ILE   B 1 131 ? 46.809 -31.429 5.480   1.00 16.66 ?  131 ILE   B CA   1 
ATOM   5963 C  C    . ILE   B 1 131 ? 45.692 -30.820 6.311   1.00 15.82 ?  131 ILE   B C    1 
ATOM   5964 O  O    . ILE   B 1 131 ? 45.765 -30.879 7.542   1.00 17.44 ?  131 ILE   B O    1 
ATOM   5965 C  CB   . ILE   B 1 131 ? 48.137 -30.665 5.674   1.00 18.46 ?  131 ILE   B CB   1 
ATOM   5966 C  CG1  . ILE   B 1 131 ? 47.988 -29.186 5.284   1.00 19.60 ?  131 ILE   B CG1  1 
ATOM   5967 C  CG2  . ILE   B 1 131 ? 49.255 -31.332 4.873   1.00 19.47 ?  131 ILE   B CG2  1 
ATOM   5968 C  CD1  . ILE   B 1 131 ? 49.211 -28.340 5.599   1.00 20.77 ?  131 ILE   B CD1  1 
ATOM   5969 H  H    . ILE   B 1 131 ? 46.924 -31.073 3.542   1.00 19.15 ?  131 ILE   B H    1 
ATOM   5970 H  HA   . ILE   B 1 131 ? 46.944 -32.320 5.829   1.00 20.05 ?  131 ILE   B HA   1 
ATOM   5971 H  HB   . ILE   B 1 131 ? 48.366 -30.708 6.616   1.00 22.21 ?  131 ILE   B HB   1 
ATOM   5972 H  HG12 . ILE   B 1 131 ? 47.824 -29.133 4.330   1.00 23.57 ?  131 ILE   B HG12 1 
ATOM   5973 H  HG13 . ILE   B 1 131 ? 47.236 -28.802 5.766   1.00 23.57 ?  131 ILE   B HG13 1 
ATOM   5974 H  HG21 . ILE   B 1 131 ? 50.098 -30.932 5.126   1.00 23.42 ?  131 ILE   B HG21 1 
ATOM   5975 H  HG22 . ILE   B 1 131 ? 49.258 -32.279 5.071   1.00 23.42 ?  131 ILE   B HG22 1 
ATOM   5976 H  HG23 . ILE   B 1 131 ? 49.086 -31.189 3.928   1.00 23.42 ?  131 ILE   B HG23 1 
ATOM   5977 H  HD11 . ILE   B 1 131 ? 49.008 -27.410 5.413   1.00 24.98 ?  131 ILE   B HD11 1 
ATOM   5978 H  HD12 . ILE   B 1 131 ? 49.436 -28.447 6.537   1.00 24.98 ?  131 ILE   B HD12 1 
ATOM   5979 H  HD13 . ILE   B 1 131 ? 49.951 -28.635 5.046   1.00 24.98 ?  131 ILE   B HD13 1 
ATOM   5980 N  N    . PHE   B 1 132 ? 44.662 -30.243 5.678   1.00 14.78 ?  132 PHE   B N    1 
ATOM   5981 C  CA   . PHE   B 1 132 ? 43.503 -29.740 6.408   1.00 15.13 ?  132 PHE   B CA   1 
ATOM   5982 C  C    . PHE   B 1 132 ? 42.480 -30.831 6.732   1.00 16.68 ?  132 PHE   B C    1 
ATOM   5983 O  O    . PHE   B 1 132 ? 41.571 -30.585 7.532   1.00 18.45 ?  132 PHE   B O    1 
ATOM   5984 C  CB   . PHE   B 1 132 ? 42.828 -28.605 5.628   1.00 14.14 ?  132 PHE   B CB   1 
ATOM   5985 C  CG   . PHE   B 1 132 ? 43.528 -27.264 5.739   1.00 14.04 ?  132 PHE   B CG   1 
ATOM   5986 C  CD1  . PHE   B 1 132 ? 44.822 -27.084 5.270   1.00 15.21 ?  132 PHE   B CD1  1 
ATOM   5987 C  CD2  . PHE   B 1 132 ? 42.859 -26.166 6.268   1.00 13.71 ?  132 PHE   B CD2  1 
ATOM   5988 C  CE1  . PHE   B 1 132 ? 45.443 -25.844 5.362   1.00 15.96 ?  132 PHE   B CE1  1 
ATOM   5989 C  CE2  . PHE   B 1 132 ? 43.471 -24.924 6.350   1.00 14.23 ?  132 PHE   B CE2  1 
ATOM   5990 C  CZ   . PHE   B 1 132 ? 44.760 -24.767 5.901   1.00 15.36 ?  132 PHE   B CZ   1 
ATOM   5991 H  H    . PHE   B 1 132 ? 44.612 -30.131 4.824   1.00 17.79 ?  132 PHE   B H    1 
ATOM   5992 H  HA   . PHE   B 1 132 ? 43.808 -29.369 7.248   1.00 18.21 ?  132 PHE   B HA   1 
ATOM   5993 H  HB2  . PHE   B 1 132 ? 42.809 -28.844 4.689   1.00 17.02 ?  132 PHE   B HB2  1 
ATOM   5994 H  HB3  . PHE   B 1 132 ? 41.922 -28.493 5.958   1.00 17.02 ?  132 PHE   B HB3  1 
ATOM   5995 H  HD1  . PHE   B 1 132 ? 45.285 -27.807 4.911   1.00 18.31 ?  132 PHE   B HD1  1 
ATOM   5996 H  HD2  . PHE   B 1 132 ? 41.987 -26.268 6.572   1.00 16.51 ?  132 PHE   B HD2  1 
ATOM   5997 H  HE1  . PHE   B 1 132 ? 46.316 -25.737 5.057   1.00 19.21 ?  132 PHE   B HE1  1 
ATOM   5998 H  HE2  . PHE   B 1 132 ? 43.014 -24.200 6.719   1.00 17.13 ?  132 PHE   B HE2  1 
ATOM   5999 H  HZ   . PHE   B 1 132 ? 45.177 -23.934 5.965   1.00 18.49 ?  132 PHE   B HZ   1 
ATOM   6000 N  N    . GLY   B 1 133 ? 42.583 -32.020 6.130   1.00 16.48 ?  133 GLY   B N    1 
ATOM   6001 C  CA   . GLY   B 1 133 ? 41.866 -33.184 6.620   1.00 17.12 ?  133 GLY   B CA   1 
ATOM   6002 C  C    . GLY   B 1 133 ? 40.470 -33.447 6.084   1.00 17.59 ?  133 GLY   B C    1 
ATOM   6003 O  O    . GLY   B 1 133 ? 39.878 -34.466 6.458   1.00 19.73 ?  133 GLY   B O    1 
ATOM   6004 H  H    . GLY   B 1 133 ? 43.076 -32.172 5.439   1.00 19.83 ?  133 GLY   B H    1 
ATOM   6005 H  HA2  . GLY   B 1 133 ? 42.401 -33.967 6.430   1.00 20.60 ?  133 GLY   B HA2  1 
ATOM   6006 H  HA3  . GLY   B 1 133 ? 41.787 -33.105 7.580   1.00 20.60 ?  133 GLY   B HA3  1 
ATOM   6007 N  N    . ALA   B 1 134 ? 39.909 -32.581 5.247   1.00 16.68 ?  134 ALA   B N    1 
ATOM   6008 C  CA   . ALA   B 1 134 ? 38.586 -32.870 4.713   1.00 16.52 ?  134 ALA   B CA   1 
ATOM   6009 C  C    . ALA   B 1 134 ? 38.679 -33.863 3.561   1.00 16.91 ?  134 ALA   B C    1 
ATOM   6010 O  O    . ALA   B 1 134 ? 39.734 -34.050 2.947   1.00 18.04 ?  134 ALA   B O    1 
ATOM   6011 C  CB   . ALA   B 1 134 ? 37.899 -31.591 4.237   1.00 17.07 ?  134 ALA   B CB   1 
ATOM   6012 H  H    . ALA   B 1 134 ? 40.258 -31.832 4.986   1.00 20.08 ?  134 ALA   B H    1 
ATOM   6013 H  HA   . ALA   B 1 134 ? 38.041 -33.258 5.415   1.00 19.88 ?  134 ALA   B HA   1 
ATOM   6014 H  HB1  . ALA   B 1 134 ? 37.015 -31.815 3.901   1.00 20.54 ?  134 ALA   B HB1  1 
ATOM   6015 H  HB2  . ALA   B 1 134 ? 37.820 -30.975 4.983   1.00 20.54 ?  134 ALA   B HB2  1 
ATOM   6016 H  HB3  . ALA   B 1 134 ? 38.428 -31.190 3.531   1.00 20.54 ?  134 ALA   B HB3  1 
ATOM   6017 N  N    . ASP   B 1 135 ? 37.550 -34.499 3.275   1.00 17.12 ?  135 ASP   B N    1 
ATOM   6018 C  CA   . ASP   B 1 135 ? 37.450 -35.395 2.133   1.00 17.83 ?  135 ASP   B CA   1 
ATOM   6019 C  C    . ASP   B 1 135 ? 37.549 -34.556 0.866   1.00 16.74 ?  135 ASP   B C    1 
ATOM   6020 O  O    . ASP   B 1 135 ? 36.700 -33.679 0.649   1.00 16.45 ?  135 ASP   B O    1 
ATOM   6021 C  CB   . ASP   B 1 135 ? 36.104 -36.118 2.187   1.00 19.59 ?  135 ASP   B CB   1 
ATOM   6022 C  CG   . ASP   B 1 135 ? 35.908 -37.099 1.046   1.00 21.33 ?  135 ASP   B CG   1 
ATOM   6023 O  OD1  . ASP   B 1 135 ? 36.781 -37.168 0.157   1.00 20.88 ?  135 ASP   B OD1  1 
ATOM   6024 O  OD2  . ASP   B 1 135 ? 34.882 -37.823 1.055   1.00 24.23 -1 135 ASP   B OD2  1 
ATOM   6025 H  H    . ASP   B 1 135 ? 36.824 -34.427 3.730   1.00 20.60 ?  135 ASP   B H    1 
ATOM   6026 H  HA   . ASP   B 1 135 ? 38.168 -36.049 2.164   1.00 21.45 ?  135 ASP   B HA   1 
ATOM   6027 H  HB2  . ASP   B 1 135 ? 36.052 -36.618 3.012   1.00 23.57 ?  135 ASP   B HB2  1 
ATOM   6028 H  HB3  . ASP   B 1 135 ? 35.397 -35.458 2.146   1.00 23.57 ?  135 ASP   B HB3  1 
ATOM   6029 N  N    . PRO   B 1 136 ? 38.555 -34.765 0.016   1.00 16.83 ?  136 PRO   B N    1 
ATOM   6030 C  CA   . PRO   B 1 136 ? 38.654 -33.937 -1.196  1.00 15.97 ?  136 PRO   B CA   1 
ATOM   6031 C  C    . PRO   B 1 136 ? 37.465 -34.085 -2.122  1.00 15.59 ?  136 PRO   B C    1 
ATOM   6032 O  O    . PRO   B 1 136 ? 37.146 -33.137 -2.849  1.00 14.84 ?  136 PRO   B O    1 
ATOM   6033 C  CB   . PRO   B 1 136 ? 39.963 -34.410 -1.846  1.00 16.89 ?  136 PRO   B CB   1 
ATOM   6034 C  CG   . PRO   B 1 136 ? 40.160 -35.802 -1.319  1.00 18.13 ?  136 PRO   B CG   1 
ATOM   6035 C  CD   . PRO   B 1 136 ? 39.622 -35.775 0.083   1.00 17.63 ?  136 PRO   B CD   1 
ATOM   6036 H  HA   . PRO   B 1 136 ? 38.744 -33.002 -0.959  1.00 19.22 ?  136 PRO   B HA   1 
ATOM   6037 H  HB2  . PRO   B 1 136 ? 39.869 -34.419 -2.814  1.00 20.32 ?  136 PRO   B HB2  1 
ATOM   6038 H  HB3  . PRO   B 1 136 ? 40.692 -33.832 -1.577  1.00 20.32 ?  136 PRO   B HB3  1 
ATOM   6039 H  HG2  . PRO   B 1 136 ? 39.665 -36.436 -1.863  1.00 21.81 ?  136 PRO   B HG2  1 
ATOM   6040 H  HG3  . PRO   B 1 136 ? 41.106 -36.023 -1.316  1.00 21.81 ?  136 PRO   B HG3  1 
ATOM   6041 H  HD2  . PRO   B 1 136 ? 39.251 -36.641 0.321   1.00 21.22 ?  136 PRO   B HD2  1 
ATOM   6042 H  HD3  . PRO   B 1 136 ? 40.310 -35.500 0.710   1.00 21.22 ?  136 PRO   B HD3  1 
ATOM   6043 N  N    . ILE   B 1 137 ? 36.806 -35.251 -2.128  1.00 15.82 ?  137 ILE   B N    1 
ATOM   6044 C  CA   . ILE   B 1 137 ? 35.588 -35.418 -2.917  1.00 16.20 ?  137 ILE   B CA   1 
ATOM   6045 C  C    . ILE   B 1 137 ? 34.513 -34.452 -2.437  1.00 15.81 ?  137 ILE   B C    1 
ATOM   6046 O  O    . ILE   B 1 137 ? 33.793 -33.844 -3.238  1.00 15.25 ?  137 ILE   B O    1 
ATOM   6047 C  CB   . ILE   B 1 137 ? 35.119 -36.887 -2.864  1.00 18.26 ?  137 ILE   B CB   1 
ATOM   6048 C  CG1  . ILE   B 1 137 ? 36.123 -37.788 -3.586  1.00 20.76 ?  137 ILE   B CG1  1 
ATOM   6049 C  CG2  . ILE   B 1 137 ? 33.722 -37.033 -3.469  1.00 18.70 ?  137 ILE   B CG2  1 
ATOM   6050 C  CD1  . ILE   B 1 137 ? 35.792 -39.271 -3.519  1.00 22.89 ?  137 ILE   B CD1  1 
ATOM   6051 H  H    . ILE   B 1 137 ? 37.042 -35.955 -1.693  1.00 19.04 ?  137 ILE   B H    1 
ATOM   6052 H  HA   . ILE   B 1 137 ? 35.779 -35.211 -3.846  1.00 19.50 ?  137 ILE   B HA   1 
ATOM   6053 H  HB   . ILE   B 1 137 ? 35.072 -37.164 -1.940  1.00 21.97 ?  137 ILE   B HB   1 
ATOM   6054 H  HG12 . ILE   B 1 137 ? 36.157 -37.541 -4.522  1.00 24.97 ?  137 ILE   B HG12 1 
ATOM   6055 H  HG13 . ILE   B 1 137 ? 36.995 -37.669 -3.181  1.00 24.97 ?  137 ILE   B HG13 1 
ATOM   6056 H  HG21 . ILE   B 1 137 ? 33.458 -37.970 -3.463  1.00 22.50 ?  137 ILE   B HG21 1 
ATOM   6057 H  HG22 . ILE   B 1 137 ? 33.085 -36.529 -2.944  1.00 22.50 ?  137 ILE   B HG22 1 
ATOM   6058 H  HG23 . ILE   B 1 137 ? 33.734 -36.707 -4.383  1.00 22.50 ?  137 ILE   B HG23 1 
ATOM   6059 H  HD11 . ILE   B 1 137 ? 36.447 -39.750 -4.046  1.00 27.52 ?  137 ILE   B HD11 1 
ATOM   6060 H  HD12 . ILE   B 1 137 ? 35.826 -39.567 -2.595  1.00 27.52 ?  137 ILE   B HD12 1 
ATOM   6061 H  HD13 . ILE   B 1 137 ? 34.909 -39.430 -3.887  1.00 27.52 ?  137 ILE   B HD13 1 
ATOM   6062 N  N    . HIS   B 1 138 ? 34.388 -34.296 -1.122  1.00 16.05 ?  138 HIS   B N    1 
ATOM   6063 C  CA   . HIS   B 1 138 ? 33.433 -33.333 -0.590  1.00 16.26 ?  138 HIS   B CA   1 
ATOM   6064 C  C    . HIS   B 1 138 ? 33.852 -31.903 -0.904  1.00 15.38 ?  138 HIS   B C    1 
ATOM   6065 O  O    . HIS   B 1 138 ? 33.005 -31.056 -1.205  1.00 15.78 ?  138 HIS   B O    1 
ATOM   6066 C  CB   . HIS   B 1 138 ? 33.299 -33.514 0.912   1.00 17.43 ?  138 HIS   B CB   1 
ATOM   6067 C  CG   . HIS   B 1 138 ? 32.364 -32.533 1.540   1.00 18.25 ?  138 HIS   B CG   1 
ATOM   6068 N  ND1  . HIS   B 1 138 ? 31.023 -32.476 1.220   1.00 19.77 ?  138 HIS   B ND1  1 
ATOM   6069 C  CD2  . HIS   B 1 138 ? 32.579 -31.546 2.440   1.00 18.95 ?  138 HIS   B CD2  1 
ATOM   6070 C  CE1  . HIS   B 1 138 ? 30.450 -31.510 1.913   1.00 19.69 ?  138 HIS   B CE1  1 
ATOM   6071 N  NE2  . HIS   B 1 138 ? 31.370 -30.932 2.665   1.00 19.20 ?  138 HIS   B NE2  1 
ATOM   6072 H  H    . HIS   B 1 138 ? 34.845 -34.723 -0.534  1.00 19.31 ?  138 HIS   B H    1 
ATOM   6073 H  HA   . HIS   B 1 138 ? 32.566 -33.496 -0.996  1.00 19.57 ?  138 HIS   B HA   1 
ATOM   6074 H  HB2  . HIS   B 1 138 ? 32.956 -34.405 1.091   1.00 20.97 ?  138 HIS   B HB2  1 
ATOM   6075 H  HB3  . HIS   B 1 138 ? 34.166 -33.403 1.322   1.00 20.97 ?  138 HIS   B HB3  1 
ATOM   6076 H  HD1  . HIS   B 1 138 ? 30.621 -32.999 0.664   1.00 23.78 ?  138 HIS   B HD1  1 
ATOM   6077 H  HD2  . HIS   B 1 138 ? 33.383 -31.332 2.845   1.00 22.79 ?  138 HIS   B HD2  1 
ATOM   6078 H  HE1  . HIS   B 1 138 ? 29.544 -31.284 1.880   1.00 23.68 ?  138 HIS   B HE1  1 
ATOM   6079 N  N    . SER   B 1 139 ? 35.146 -31.607 -0.826  1.00 14.86 ?  139 SER   B N    1 
ATOM   6080 C  CA   . SER   B 1 139 ? 35.585 -30.256 -1.144  1.00 14.30 ?  139 SER   B CA   1 
ATOM   6081 C  C    . SER   B 1 139 ? 35.246 -29.904 -2.585  1.00 13.35 ?  139 SER   B C    1 
ATOM   6082 O  O    . SER   B 1 139 ? 34.796 -28.788 -2.866  1.00 13.19 ?  139 SER   B O    1 
ATOM   6083 C  CB   . SER   B 1 139 ? 37.079 -30.118 -0.875  1.00 14.65 ?  139 SER   B CB   1 
ATOM   6084 O  OG   . SER   B 1 139 ? 37.497 -28.798 -1.175  1.00 14.70 ?  139 SER   B OG   1 
ATOM   6085 H  H    . SER   B 1 139 ? 35.765 -32.153 -0.603  1.00 17.88 ?  139 SER   B H    1 
ATOM   6086 H  HA   . SER   B 1 139 ? 35.112 -29.634 -0.571  1.00 17.22 ?  139 SER   B HA   1 
ATOM   6087 H  HB2  . SER   B 1 139 ? 37.251 -30.299 0.062   1.00 17.64 ?  139 SER   B HB2  1 
ATOM   6088 H  HB3  . SER   B 1 139 ? 37.565 -30.742 -1.434  1.00 17.64 ?  139 SER   B HB3  1 
ATOM   6089 H  HG   . SER   B 1 139 ? 37.128 -28.250 -0.656  1.00 17.69 ?  139 SER   B HG   1 
ATOM   6090 N  N    . LEU   B 1 140 ? 35.431 -30.852 -3.508  1.00 13.15 ?  140 LEU   B N    1 
ATOM   6091 C  CA   . LEU   B 1 140 ? 35.069 -30.607 -4.897  1.00 13.19 ?  140 LEU   B CA   1 
ATOM   6092 C  C    . LEU   B 1 140 ? 33.567 -30.383 -5.032  1.00 13.56 ?  140 LEU   B C    1 
ATOM   6093 O  O    . LEU   B 1 140 ? 33.131 -29.495 -5.770  1.00 13.78 ?  140 LEU   B O    1 
ATOM   6094 C  CB   . LEU   B 1 140 ? 35.542 -31.767 -5.771  1.00 13.34 ?  140 LEU   B CB   1 
ATOM   6095 C  CG   . LEU   B 1 140 ? 35.170 -31.665 -7.244  1.00 13.67 ?  140 LEU   B CG   1 
ATOM   6096 C  CD1  . LEU   B 1 140 ? 35.741 -30.392 -7.851  1.00 14.74 ?  140 LEU   B CD1  1 
ATOM   6097 C  CD2  . LEU   B 1 140 ? 35.642 -32.894 -7.985  1.00 14.82 ?  140 LEU   B CD2  1 
ATOM   6098 H  H    . LEU   B 1 140 ? 35.757 -31.631 -3.357  1.00 15.84 ?  140 LEU   B H    1 
ATOM   6099 H  HA   . LEU   B 1 140 ? 35.522 -29.802 -5.199  1.00 15.89 ?  140 LEU   B HA   1 
ATOM   6100 H  HB2  . LEU   B 1 140 ? 36.512 -31.818 -5.720  1.00 16.06 ?  140 LEU   B HB2  1 
ATOM   6101 H  HB3  . LEU   B 1 140 ? 35.157 -32.587 -5.433  1.00 16.06 ?  140 LEU   B HB3  1 
ATOM   6102 H  HG   . LEU   B 1 140 ? 34.205 -31.614 -7.320  1.00 16.46 ?  140 LEU   B HG   1 
ATOM   6103 H  HD11 . LEU   B 1 140 ? 35.610 -30.418 -8.811  1.00 17.74 ?  140 LEU   B HD11 1 
ATOM   6104 H  HD12 . LEU   B 1 140 ? 35.279 -29.623 -7.477  1.00 17.74 ?  140 LEU   B HD12 1 
ATOM   6105 H  HD13 . LEU   B 1 140 ? 36.687 -30.340 -7.646  1.00 17.74 ?  140 LEU   B HD13 1 
ATOM   6106 H  HD21 . LEU   B 1 140 ? 35.391 -32.804 -8.917  1.00 17.84 ?  140 LEU   B HD21 1 
ATOM   6107 H  HD22 . LEU   B 1 140 ? 36.600 -32.961 -7.898  1.00 17.84 ?  140 LEU   B HD22 1 
ATOM   6108 H  HD23 . LEU   B 1 140 ? 35.209 -33.667 -7.595  1.00 17.84 ?  140 LEU   B HD23 1 
ATOM   6109 N  N    . ARG   B 1 141 ? 32.767 -31.175 -4.315  1.00 13.64 ?  141 ARG   B N    1 
ATOM   6110 C  CA   . ARG   B 1 141 ? 31.316 -30.994 -4.292  1.00 14.68 ?  141 ARG   B CA   1 
ATOM   6111 C  C    . ARG   B 1 141 ? 30.939 -29.581 -3.865  1.00 14.13 ?  141 ARG   B C    1 
ATOM   6112 O  O    . ARG   B 1 141 ? 30.133 -28.905 -4.521  1.00 14.17 ?  141 ARG   B O    1 
ATOM   6113 C  CB   . ARG   B 1 141 ? 30.736 -32.020 -3.310  1.00 16.09 ?  141 ARG   B CB   1 
ATOM   6114 C  CG   . ARG   B 1 141 ? 29.268 -31.910 -2.982  1.00 17.87 ?  141 ARG   B CG   1 
ATOM   6115 C  CD   . ARG   B 1 141 ? 28.470 -32.544 -4.055  1.00 19.40 ?  141 ARG   B CD   1 
ATOM   6116 N  NE   . ARG   B 1 141 ? 28.219 -31.631 -5.159  1.00 19.78 ?  141 ARG   B NE   1 
ATOM   6117 C  CZ   . ARG   B 1 141 ? 28.197 -31.981 -6.437  1.00 19.26 ?  141 ARG   B CZ   1 
ATOM   6118 N  NH1  . ARG   B 1 141 ? 28.612 -33.173 -6.837  1.00 19.16 ?  141 ARG   B NH1  1 
ATOM   6119 N  NH2  . ARG   B 1 141 ? 27.739 -31.114 -7.335  1.00 19.96 ?  141 ARG   B NH2  1 
ATOM   6120 H  H    . ARG   B 1 141 ? 33.044 -31.825 -3.829  1.00 16.42 ?  141 ARG   B H    1 
ATOM   6121 H  HA   . ARG   B 1 141 ? 30.949 -31.161 -5.172  1.00 17.67 ?  141 ARG   B HA   1 
ATOM   6122 H  HB2  . ARG   B 1 141 ? 30.892 -32.909 -3.675  1.00 19.36 ?  141 ARG   B HB2  1 
ATOM   6123 H  HB3  . ARG   B 1 141 ? 31.220 -31.943 -2.473  1.00 19.36 ?  141 ARG   B HB3  1 
ATOM   6124 H  HG2  . ARG   B 1 141 ? 29.095 -32.367 -2.146  1.00 21.50 ?  141 ARG   B HG2  1 
ATOM   6125 H  HG3  . ARG   B 1 141 ? 29.014 -30.974 -2.911  1.00 21.50 ?  141 ARG   B HG3  1 
ATOM   6126 H  HD2  . ARG   B 1 141 ? 28.950 -33.321 -4.391  1.00 23.34 ?  141 ARG   B HD2  1 
ATOM   6127 H  HD3  . ARG   B 1 141 ? 27.621 -32.824 -3.688  1.00 23.34 ?  141 ARG   B HD3  1 
ATOM   6128 H  HE   . ARG   B 1 141 ? 28.046 -30.812 -4.965  1.00 23.79 ?  141 ARG   B HE   1 
ATOM   6129 H  HH11 . ARG   B 1 141 ? 28.902 -33.747 -6.268  1.00 23.04 ?  141 ARG   B HH11 1 
ATOM   6130 H  HH12 . ARG   B 1 141 ? 28.601 -33.369 -7.672  1.00 23.04 ?  141 ARG   B HH12 1 
ATOM   6131 H  HH21 . ARG   B 1 141 ? 27.473 -30.333 -7.086  1.00 24.01 ?  141 ARG   B HH21 1 
ATOM   6132 H  HH22 . ARG   B 1 141 ? 27.742 -31.317 -8.172  1.00 24.01 ?  141 ARG   B HH22 1 
ATOM   6133 N  N    . VAL   B 1 142 ? 31.489 -29.133 -2.740  1.00 13.74 ?  142 VAL   B N    1 
ATOM   6134 C  CA   . VAL   B 1 142 ? 31.150 -27.801 -2.254  1.00 13.66 ?  142 VAL   B CA   1 
ATOM   6135 C  C    . VAL   B 1 142 ? 31.621 -26.744 -3.244  1.00 13.45 ?  142 VAL   B C    1 
ATOM   6136 O  O    . VAL   B 1 142 ? 30.920 -25.757 -3.500  1.00 13.76 ?  142 VAL   B O    1 
ATOM   6137 C  CB   . VAL   B 1 142 ? 31.698 -27.571 -0.833  1.00 14.34 ?  142 VAL   B CB   1 
ATOM   6138 C  CG1  . VAL   B 1 142 ? 31.380 -26.154 -0.361  1.00 14.21 ?  142 VAL   B CG1  1 
ATOM   6139 C  CG2  . VAL   B 1 142 ? 31.121 -28.596 0.128   1.00 15.35 ?  142 VAL   B CG2  1 
ATOM   6140 H  H    . VAL   B 1 142 ? 32.052 -29.564 -2.253  1.00 16.54 ?  142 VAL   B H    1 
ATOM   6141 H  HA   . VAL   B 1 142 ? 30.190 -27.731 -2.200  1.00 16.44 ?  142 VAL   B HA   1 
ATOM   6142 H  HB   . VAL   B 1 142 ? 32.665 -27.678 -0.840  1.00 17.26 ?  142 VAL   B HB   1 
ATOM   6143 H  HG11 . VAL   B 1 142 ? 31.561 -26.092 0.589   1.00 17.11 ?  142 VAL   B HG11 1 
ATOM   6144 H  HG12 . VAL   B 1 142 ? 31.940 -25.526 -0.845  1.00 17.11 ?  142 VAL   B HG12 1 
ATOM   6145 H  HG13 . VAL   B 1 142 ? 30.446 -25.969 -0.534  1.00 17.11 ?  142 VAL   B HG13 1 
ATOM   6146 H  HG21 . VAL   B 1 142 ? 31.444 -28.410 1.022   1.00 18.47 ?  142 VAL   B HG21 1 
ATOM   6147 H  HG22 . VAL   B 1 142 ? 30.152 -28.535 0.106   1.00 18.47 ?  142 VAL   B HG22 1 
ATOM   6148 H  HG23 . VAL   B 1 142 ? 31.401 -29.483 -0.148  1.00 18.47 ?  142 VAL   B HG23 1 
ATOM   6149 N  N    . CYS   B 1 143 ? 32.804 -26.940 -3.831  1.00 13.08 ?  143 CYS   B N    1 
ATOM   6150 C  CA   . CYS   B 1 143 ? 33.296 -25.999 -4.833  1.00 12.83 ?  143 CYS   B CA   1 
ATOM   6151 C  C    . CYS   B 1 143 ? 32.293 -25.854 -5.973  1.00 12.76 ?  143 CYS   B C    1 
ATOM   6152 O  O    . CYS   B 1 143 ? 31.887 -24.742 -6.333  1.00 13.09 ?  143 CYS   B O    1 
ATOM   6153 C  CB   . CYS   B 1 143 ? 34.655 -26.482 -5.355  1.00 13.24 ?  143 CYS   B CB   1 
ATOM   6154 S  SG   . CYS   B 1 143 ? 35.402 -25.388 -6.574  1.00 13.71 ?  143 CYS   B SG   1 
ATOM   6155 H  H    . CYS   B 1 143 ? 33.339 -27.594 -3.666  1.00 15.76 ?  143 CYS   B H    1 
ATOM   6156 H  HA   . CYS   B 1 143 ? 33.429 -25.128 -4.429  1.00 15.45 ?  143 CYS   B HA   1 
ATOM   6157 H  HB2  . CYS   B 1 143 ? 35.275 -26.560 -4.612  1.00 15.95 ?  143 CYS   B HB2  1 
ATOM   6158 H  HB3  . CYS   B 1 143 ? 34.541 -27.348 -5.770  1.00 15.95 ?  143 CYS   B HB3  1 
ATOM   6159 H  HG   . CYS   B 1 143 ? 36.473 -25.825 -6.894  1.00 16.51 ?  143 CYS   B HG   1 
ATOM   6160 N  N    . VAL   B 1 144 ? 31.885 -26.976 -6.559  1.00 13.33 ?  144 VAL   B N    1 
ATOM   6161 C  CA   . VAL   B 1 144 ? 30.980 -26.925 -7.703  1.00 14.19 ?  144 VAL   B CA   1 
ATOM   6162 C  C    . VAL   B 1 144 ? 29.641 -26.305 -7.321  1.00 14.26 ?  144 VAL   B C    1 
ATOM   6163 O  O    . VAL   B 1 144 ? 29.025 -25.592 -8.122  1.00 15.34 ?  144 VAL   B O    1 
ATOM   6164 C  CB   . VAL   B 1 144 ? 30.818 -28.337 -8.276  1.00 16.51 ?  144 VAL   B CB   1 
ATOM   6165 C  CG1  . VAL   B 1 144 ? 29.531 -28.472 -9.086  1.00 18.59 ?  144 VAL   B CG1  1 
ATOM   6166 C  CG2  . VAL   B 1 144 ? 32.058 -28.730 -9.082  1.00 16.95 ?  144 VAL   B CG2  1 
ATOM   6167 H  H    . VAL   B 1 144 ? 32.129 -27.769 -6.334  1.00 16.05 ?  144 VAL   B H    1 
ATOM   6168 H  HA   . VAL   B 1 144 ? 31.368 -26.370 -8.395  1.00 17.08 ?  144 VAL   B HA   1 
ATOM   6169 H  HB   . VAL   B 1 144 ? 30.755 -28.960 -7.533  1.00 19.87 ?  144 VAL   B HB   1 
ATOM   6170 H  HG11 . VAL   B 1 144 ? 29.600 -29.267 -9.642  1.00 22.36 ?  144 VAL   B HG11 1 
ATOM   6171 H  HG12 . VAL   B 1 144 ? 28.783 -28.567 -8.476  1.00 22.36 ?  144 VAL   B HG12 1 
ATOM   6172 H  HG13 . VAL   B 1 144 ? 29.423 -27.691 -9.641  1.00 22.36 ?  144 VAL   B HG13 1 
ATOM   6173 H  HG21 . VAL   B 1 144 ? 31.936 -29.628 -9.429  1.00 20.40 ?  144 VAL   B HG21 1 
ATOM   6174 H  HG22 . VAL   B 1 144 ? 32.165 -28.105 -9.816  1.00 20.40 ?  144 VAL   B HG22 1 
ATOM   6175 H  HG23 . VAL   B 1 144 ? 32.833 -28.699 -8.503  1.00 20.40 ?  144 VAL   B HG23 1 
ATOM   6176 N  N    . ASP   B 1 145 ? 29.175 -26.553 -6.101  1.00 14.53 ?  145 ASP   B N    1 
ATOM   6177 C  CA   . ASP   B 1 145 ? 27.864 -26.085 -5.670  1.00 15.23 ?  145 ASP   B CA   1 
ATOM   6178 C  C    . ASP   B 1 145 ? 27.893 -24.660 -5.125  1.00 14.70 ?  145 ASP   B C    1 
ATOM   6179 O  O    . ASP   B 1 145 ? 26.834 -24.119 -4.782  1.00 16.81 ?  145 ASP   B O    1 
ATOM   6180 C  CB   . ASP   B 1 145 ? 27.285 -27.011 -4.591  1.00 16.86 ?  145 ASP   B CB   1 
ATOM   6181 C  CG   . ASP   B 1 145 ? 26.929 -28.387 -5.103  1.00 18.76 ?  145 ASP   B CG   1 
ATOM   6182 O  OD1  . ASP   B 1 145 ? 26.821 -28.570 -6.330  1.00 19.15 ?  145 ASP   B OD1  1 
ATOM   6183 O  OD2  . ASP   B 1 145 ? 26.751 -29.279 -4.251  1.00 20.94 -1 145 ASP   B OD2  1 
ATOM   6184 H  H    . ASP   B 1 145 ? 29.615 -26.975 -5.497  1.00 17.49 ?  145 ASP   B H    1 
ATOM   6185 H  HA   . ASP   B 1 145 ? 27.272 -26.085 -6.433  1.00 18.33 ?  145 ASP   B HA   1 
ATOM   6186 H  HB2  . ASP   B 1 145 ? 27.930 -27.125 -3.891  1.00 20.29 ?  145 ASP   B HB2  1 
ATOM   6187 H  HB3  . ASP   B 1 145 ? 26.471 -26.609 -4.246  1.00 20.29 ?  145 ASP   B HB3  1 
ATOM   6188 N  N    . THR   B 1 146 ? 29.069 -24.044 -5.023  1.00 13.22 ?  146 THR   B N    1 
ATOM   6189 C  CA   . THR   B 1 146 ? 29.203 -22.724 -4.412  1.00 12.78 ?  146 THR   B CA   1 
ATOM   6190 C  C    . THR   B 1 146 ? 29.834 -21.692 -5.328  1.00 12.51 ?  146 THR   B C    1 
ATOM   6191 O  O    . THR   B 1 146 ? 29.376 -20.535 -5.371  1.00 12.84 ?  146 THR   B O    1 
ATOM   6192 C  CB   . THR   B 1 146 ? 30.032 -22.829 -3.123  1.00 12.94 ?  146 THR   B CB   1 
ATOM   6193 O  OG1  . THR   B 1 146 ? 29.463 -23.822 -2.259  1.00 13.26 ?  146 THR   B OG1  1 
ATOM   6194 C  CG2  . THR   B 1 146 ? 30.100 -21.487 -2.414  1.00 13.36 ?  146 THR   B CG2  1 
ATOM   6195 H  H    . THR   B 1 146 ? 29.816 -24.375 -5.301  1.00 15.92 ?  146 THR   B H    1 
ATOM   6196 H  HA   . THR   B 1 146 ? 28.326 -22.398 -4.179  1.00 15.39 ?  146 THR   B HA   1 
ATOM   6197 H  HB   . THR   B 1 146 ? 30.937 -23.088 -3.353  1.00 15.59 ?  146 THR   B HB   1 
ATOM   6198 H  HG1  . THR   B 1 146 ? 29.491 -24.577 -2.646  1.00 15.97 ?  146 THR   B HG1  1 
ATOM   6199 H  HG21 . THR   B 1 146 ? 30.439 -21.608 -1.517  1.00 16.09 ?  146 THR   B HG21 1 
ATOM   6200 H  HG22 . THR   B 1 146 ? 30.693 -20.886 -2.897  1.00 16.09 ?  146 THR   B HG22 1 
ATOM   6201 H  HG23 . THR   B 1 146 ? 29.217 -21.091 -2.371  1.00 16.09 ?  146 THR   B HG23 1 
ATOM   6202 N  N    . VAL   B 1 147 ? 30.895 -22.065 -6.033  1.00 12.64 ?  147 VAL   B N    1 
ATOM   6203 C  CA   . VAL   B 1 147 ? 31.617 -21.122 -6.873  1.00 12.23 ?  147 VAL   B CA   1 
ATOM   6204 C  C    . VAL   B 1 147 ? 30.883 -20.993 -8.195  1.00 12.38 ?  147 VAL   B C    1 
ATOM   6205 O  O    . VAL   B 1 147 ? 30.515 -21.999 -8.820  1.00 13.41 ?  147 VAL   B O    1 
ATOM   6206 C  CB   . VAL   B 1 147 ? 33.067 -21.585 -7.082  1.00 12.26 ?  147 VAL   B CB   1 
ATOM   6207 C  CG1  . VAL   B 1 147 ? 33.827 -20.560 -7.902  1.00 12.28 ?  147 VAL   B CG1  1 
ATOM   6208 C  CG2  . VAL   B 1 147 ? 33.749 -21.793 -5.747  1.00 12.55 ?  147 VAL   B CG2  1 
ATOM   6209 H  H    . VAL   B 1 147 ? 31.221 -22.868 -6.055  1.00 15.22 ?  147 VAL   B H    1 
ATOM   6210 H  HA   . VAL   B 1 147 ? 31.638 -20.256 -6.442  1.00 14.74 ?  147 VAL   B HA   1 
ATOM   6211 H  HB   . VAL   B 1 147 ? 33.075 -22.431 -7.567  1.00 14.76 ?  147 VAL   B HB   1 
ATOM   6212 H  HG11 . VAL   B 1 147 ? 34.771 -20.780 -7.891  1.00 14.79 ?  147 VAL   B HG11 1 
ATOM   6213 H  HG12 . VAL   B 1 147 ? 33.497 -20.569 -8.814  1.00 14.79 ?  147 VAL   B HG12 1 
ATOM   6214 H  HG13 . VAL   B 1 147 ? 33.689 -19.682 -7.509  1.00 14.79 ?  147 VAL   B HG13 1 
ATOM   6215 H  HG21 . VAL   B 1 147 ? 34.689 -21.989 -5.900  1.00 15.11 ?  147 VAL   B HG21 1 
ATOM   6216 H  HG22 . VAL   B 1 147 ? 33.662 -20.984 -5.223  1.00 15.11 ?  147 VAL   B HG22 1 
ATOM   6217 H  HG23 . VAL   B 1 147 ? 33.329 -22.536 -5.288  1.00 15.11 ?  147 VAL   B HG23 1 
ATOM   6218 N  N    . ARG   B 1 148 ? 30.674 -19.743 -8.620  1.00 12.39 ?  148 ARG   B N    1 
ATOM   6219 C  CA   . ARG   B 1 148 ? 30.046 -19.427 -9.894  1.00 12.56 ?  148 ARG   B CA   1 
ATOM   6220 C  C    . ARG   B 1 148 ? 30.998 -18.754 -10.870 1.00 12.54 ?  148 ARG   B C    1 
ATOM   6221 O  O    . ARG   B 1 148 ? 30.712 -18.734 -12.070 1.00 13.99 ?  148 ARG   B O    1 
ATOM   6222 C  CB   . ARG   B 1 148 ? 28.805 -18.544 -9.676  1.00 12.88 ?  148 ARG   B CB   1 
ATOM   6223 C  CG   . ARG   B 1 148 ? 27.731 -19.254 -8.857  1.00 13.78 ?  148 ARG   B CG   1 
ATOM   6224 C  CD   . ARG   B 1 148 ? 26.523 -18.378 -8.537  1.00 14.52 ?  148 ARG   B CD   1 
ATOM   6225 N  NE   . ARG   B 1 148 ? 26.908 -17.174 -7.814  1.00 14.56 ?  148 ARG   B NE   1 
ATOM   6226 C  CZ   . ARG   B 1 148 ? 27.210 -17.134 -6.523  1.00 13.36 ?  148 ARG   B CZ   1 
ATOM   6227 N  NH1  . ARG   B 1 148 ? 27.144 -18.214 -5.760  1.00 13.42 ?  148 ARG   B NH1  1 
ATOM   6228 N  NH2  . ARG   B 1 148 ? 27.610 -15.983 -5.988  1.00 13.48 ?  148 ARG   B NH2  1 
ATOM   6229 H  H    . ARG   B 1 148 ? 30.898 -19.044 -8.163  1.00 14.93 ?  148 ARG   B H    1 
ATOM   6230 H  HA   . ARG   B 1 148 ? 29.748 -20.252 -10.299 1.00 15.13 ?  148 ARG   B HA   1 
ATOM   6231 H  HB2  . ARG   B 1 148 ? 29.065 -17.739 -9.198  1.00 15.51 ?  148 ARG   B HB2  1 
ATOM   6232 H  HB3  . ARG   B 1 148 ? 28.426 -18.312 -10.538 1.00 15.51 ?  148 ARG   B HB3  1 
ATOM   6233 H  HG2  . ARG   B 1 148 ? 27.413 -20.023 -9.359  1.00 16.60 ?  148 ARG   B HG2  1 
ATOM   6234 H  HG3  . ARG   B 1 148 ? 28.114 -19.547 -8.017  1.00 16.60 ?  148 ARG   B HG3  1 
ATOM   6235 H  HD2  . ARG   B 1 148 ? 26.094 -18.113 -9.365  1.00 17.48 ?  148 ARG   B HD2  1 
ATOM   6236 H  HD3  . ARG   B 1 148 ? 25.901 -18.884 -7.986  1.00 17.48 ?  148 ARG   B HD3  1 
ATOM   6237 H  HE   . ARG   B 1 148 ? 26.946 -16.441 -8.254  1.00 17.52 ?  148 ARG   B HE   1 
ATOM   6238 H  HH11 . ARG   B 1 148 ? 26.881 -18.966 -6.087  1.00 16.16 ?  148 ARG   B HH11 1 
ATOM   6239 H  HH12 . ARG   B 1 148 ? 27.337 -18.164 -4.920  1.00 16.16 ?  148 ARG   B HH12 1 
ATOM   6240 H  HH21 . ARG   B 1 148 ? 27.665 -15.280 -6.478  1.00 16.23 ?  148 ARG   B HH21 1 
ATOM   6241 H  HH22 . ARG   B 1 148 ? 27.811 -15.943 -5.153  1.00 16.23 ?  148 ARG   B HH22 1 
ATOM   6242 N  N    . THR   B 1 149 ? 32.105 -18.195 -10.384 1.00 12.42 ?  149 THR   B N    1 
ATOM   6243 C  CA   . THR   B 1 149 ? 33.146 -17.639 -11.234 1.00 12.55 ?  149 THR   B CA   1 
ATOM   6244 C  C    . THR   B 1 149 ? 34.035 -18.779 -11.740 1.00 12.15 ?  149 THR   B C    1 
ATOM   6245 O  O    . THR   B 1 149 ? 33.841 -19.950 -11.401 1.00 12.82 ?  149 THR   B O    1 
ATOM   6246 C  CB   . THR   B 1 149 ? 33.923 -16.586 -10.454 1.00 12.60 ?  149 THR   B CB   1 
ATOM   6247 O  OG1  . THR   B 1 149 ? 34.378 -17.183 -9.237  1.00 12.49 ?  149 THR   B OG1  1 
ATOM   6248 C  CG2  . THR   B 1 149 ? 33.037 -15.368 -10.166 1.00 13.47 ?  149 THR   B CG2  1 
ATOM   6249 H  H    . THR   B 1 149 ? 32.270 -18.119 -9.545  1.00 14.96 ?  149 THR   B H    1 
ATOM   6250 H  HA   . THR   B 1 149 ? 32.738 -17.206 -12.001 1.00 15.12 ?  149 THR   B HA   1 
ATOM   6251 H  HB   . THR   B 1 149 ? 34.689 -16.303 -10.973 1.00 15.18 ?  149 THR   B HB   1 
ATOM   6252 H  HG1  . THR   B 1 149 ? 34.801 -16.612 -8.781  1.00 15.05 ?  149 THR   B HG1  1 
ATOM   6253 H  HG21 . THR   B 1 149 ? 33.544 -14.697 -9.679  1.00 16.22 ?  149 THR   B HG21 1 
ATOM   6254 H  HG22 . THR   B 1 149 ? 32.728 -14.978 -11.001 1.00 16.22 ?  149 THR   B HG22 1 
ATOM   6255 H  HG23 . THR   B 1 149 ? 32.268 -15.627 -9.637  1.00 16.22 ?  149 THR   B HG23 1 
ATOM   6256 N  N    . ASN   B 1 150 ? 35.003 -18.458 -12.587 1.00 12.29 ?  150 ASN   B N    1 
ATOM   6257 C  CA   . ASN   B 1 150 ? 35.766 -19.486 -13.287 1.00 12.73 ?  150 ASN   B CA   1 
ATOM   6258 C  C    . ASN   B 1 150 ? 36.933 -19.932 -12.416 1.00 12.35 ?  150 ASN   B C    1 
ATOM   6259 O  O    . ASN   B 1 150 ? 37.862 -19.158 -12.159 1.00 13.03 ?  150 ASN   B O    1 
ATOM   6260 C  CB   . ASN   B 1 150 ? 36.234 -18.951 -14.633 1.00 14.11 ?  150 ASN   B CB   1 
ATOM   6261 C  CG   . ASN   B 1 150 ? 35.088 -18.723 -15.571 1.00 17.02 ?  150 ASN   B CG   1 
ATOM   6262 O  OD1  . ASN   B 1 150 ? 34.201 -19.558 -15.672 1.00 18.00 ?  150 ASN   B OD1  1 
ATOM   6263 N  ND2  . ASN   B 1 150 ? 35.071 -17.579 -16.232 1.00 18.78 ?  150 ASN   B ND2  1 
ATOM   6264 H  H    . ASN   B 1 150 ? 35.248 -17.649 -12.769 1.00 14.80 ?  150 ASN   B H    1 
ATOM   6265 H  HA   . ASN   B 1 150 ? 35.185 -20.251 -13.451 1.00 15.34 ?  150 ASN   B HA   1 
ATOM   6266 H  HB2  . ASN   B 1 150 ? 36.687 -18.105 -14.501 1.00 16.99 ?  150 ASN   B HB2  1 
ATOM   6267 H  HB3  . ASN   B 1 150 ? 36.830 -19.594 -15.043 1.00 16.99 ?  150 ASN   B HB3  1 
ATOM   6268 H  HD21 . ASN   B 1 150 ? 34.428 -17.403 -16.780 1.00 22.59 ?  150 ASN   B HD21 1 
ATOM   6269 H  HD22 . ASN   B 1 150 ? 35.707 -17.011 -16.125 1.00 22.59 ?  150 ASN   B HD22 1 
ATOM   6270 N  N    . VAL   B 1 151 ? 36.889 -21.181 -11.962 1.00 12.02 ?  151 VAL   B N    1 
ATOM   6271 C  CA   . VAL   B 1 151 ? 37.910 -21.708 -11.070 1.00 12.09 ?  151 VAL   B CA   1 
ATOM   6272 C  C    . VAL   B 1 151 ? 38.615 -22.880 -11.742 1.00 11.94 ?  151 VAL   B C    1 
ATOM   6273 O  O    . VAL   B 1 151 ? 37.973 -23.817 -12.243 1.00 12.86 ?  151 VAL   B O    1 
ATOM   6274 C  CB   . VAL   B 1 151 ? 37.355 -22.042 -9.670  1.00 13.26 ?  151 VAL   B CB   1 
ATOM   6275 C  CG1  . VAL   B 1 151 ? 36.193 -23.040 -9.748  1.00 14.09 ?  151 VAL   B CG1  1 
ATOM   6276 C  CG2  . VAL   B 1 151 ? 38.469 -22.532 -8.754  1.00 13.79 ?  151 VAL   B CG2  1 
ATOM   6277 H  H    . VAL   B 1 151 ? 36.269 -21.750 -12.165 1.00 14.48 ?  151 VAL   B H    1 
ATOM   6278 H  HA   . VAL   B 1 151 ? 38.577 -21.014 -10.947 1.00 14.57 ?  151 VAL   B HA   1 
ATOM   6279 H  HB   . VAL   B 1 151 ? 37.004 -21.221 -9.285  1.00 15.97 ?  151 VAL   B HB   1 
ATOM   6280 H  HG11 . VAL   B 1 151 ? 35.876 -23.224 -8.850  1.00 16.96 ?  151 VAL   B HG11 1 
ATOM   6281 H  HG12 . VAL   B 1 151 ? 35.477 -22.655 -10.279 1.00 16.96 ?  151 VAL   B HG12 1 
ATOM   6282 H  HG13 . VAL   B 1 151 ? 36.507 -23.859 -10.163 1.00 16.96 ?  151 VAL   B HG13 1 
ATOM   6283 H  HG21 . VAL   B 1 151 ? 38.119 -22.608 -7.851  1.00 16.60 ?  151 VAL   B HG21 1 
ATOM   6284 H  HG22 . VAL   B 1 151 ? 38.776 -23.397 -9.063  1.00 16.60 ?  151 VAL   B HG22 1 
ATOM   6285 H  HG23 . VAL   B 1 151 ? 39.198 -21.893 -8.771  1.00 16.60 ?  151 VAL   B HG23 1 
ATOM   6286 N  N    . TYR   B 1 152 ? 39.947 -22.795 -11.759 1.00 11.41 ?  152 TYR   B N    1 
ATOM   6287 C  CA   . TYR   B 1 152 ? 40.850 -23.773 -12.344 1.00 11.68 ?  152 TYR   B CA   1 
ATOM   6288 C  C    . TYR   B 1 152 ? 41.573 -24.447 -11.183 1.00 11.17 ?  152 TYR   B C    1 
ATOM   6289 O  O    . TYR   B 1 152 ? 42.414 -23.826 -10.524 1.00 11.61 ?  152 TYR   B O    1 
ATOM   6290 C  CB   . TYR   B 1 152 ? 41.819 -23.061 -13.290 1.00 12.56 ?  152 TYR   B CB   1 
ATOM   6291 C  CG   . TYR   B 1 152 ? 41.137 -22.597 -14.556 1.00 13.23 ?  152 TYR   B CG   1 
ATOM   6292 C  CD1  . TYR   B 1 152 ? 40.477 -21.371 -14.619 1.00 13.79 ?  152 TYR   B CD1  1 
ATOM   6293 C  CD2  . TYR   B 1 152 ? 41.132 -23.403 -15.681 1.00 14.28 ?  152 TYR   B CD2  1 
ATOM   6294 C  CE1  . TYR   B 1 152 ? 39.831 -20.971 -15.779 1.00 15.00 ?  152 TYR   B CE1  1 
ATOM   6295 C  CE2  . TYR   B 1 152 ? 40.496 -23.014 -16.839 1.00 15.16 ?  152 TYR   B CE2  1 
ATOM   6296 C  CZ   . TYR   B 1 152 ? 39.849 -21.794 -16.889 1.00 15.51 ?  152 TYR   B CZ   1 
ATOM   6297 O  OH   . TYR   B 1 152 ? 39.218 -21.422 -18.055 1.00 17.62 ?  152 TYR   B OH   1 
ATOM   6298 H  H    . TYR   B 1 152 ? 40.378 -22.136 -11.401 1.00 13.75 ?  152 TYR   B H    1 
ATOM   6299 H  HA   . TYR   B 1 152 ? 40.344 -24.439 -12.842 1.00 14.07 ?  152 TYR   B HA   1 
ATOM   6300 H  HB2  . TYR   B 1 152 ? 42.184 -22.284 -12.837 1.00 15.13 ?  152 TYR   B HB2  1 
ATOM   6301 H  HB3  . TYR   B 1 152 ? 42.533 -23.670 -13.533 1.00 15.13 ?  152 TYR   B HB3  1 
ATOM   6302 H  HD1  . TYR   B 1 152 ? 40.462 -20.817 -13.870 1.00 16.60 ?  152 TYR   B HD1  1 
ATOM   6303 H  HD2  . TYR   B 1 152 ? 41.563 -24.230 -15.650 1.00 17.19 ?  152 TYR   B HD2  1 
ATOM   6304 H  HE1  . TYR   B 1 152 ? 39.399 -20.151 -15.814 1.00 18.06 ?  152 TYR   B HE1  1 
ATOM   6305 H  HE2  . TYR   B 1 152 ? 40.509 -23.572 -17.582 1.00 18.25 ?  152 TYR   B HE2  1 
ATOM   6306 H  HH   . TYR   B 1 152 ? 39.322 -22.023 -18.633 1.00 21.20 ?  152 TYR   B HH   1 
ATOM   6307 N  N    . LEU   B 1 153 ? 41.212 -25.705 -10.917 1.00 11.28 ?  153 LEU   B N    1 
ATOM   6308 C  CA   . LEU   B 1 153 ? 41.721 -26.454 -9.778  1.00 11.34 ?  153 LEU   B CA   1 
ATOM   6309 C  C    . LEU   B 1 153 ? 42.954 -27.251 -10.171 1.00 11.35 ?  153 LEU   B C    1 
ATOM   6310 O  O    . LEU   B 1 153 ? 42.934 -27.985 -11.162 1.00 12.71 ?  153 LEU   B O    1 
ATOM   6311 C  CB   . LEU   B 1 153 ? 40.643 -27.413 -9.267  1.00 11.63 ?  153 LEU   B CB   1 
ATOM   6312 C  CG   . LEU   B 1 153 ? 39.383 -26.758 -8.698  1.00 12.72 ?  153 LEU   B CG   1 
ATOM   6313 C  CD1  . LEU   B 1 153 ? 38.290 -27.804 -8.527  1.00 13.63 ?  153 LEU   B CD1  1 
ATOM   6314 C  CD2  . LEU   B 1 153 ? 39.678 -26.082 -7.374  1.00 13.13 ?  153 LEU   B CD2  1 
ATOM   6315 H  H    . LEU   B 1 153 ? 40.643 -26.157 -11.396 1.00 13.59 ?  153 LEU   B H    1 
ATOM   6316 H  HA   . LEU   B 1 153 ? 41.947 -25.841 -9.068  1.00 13.67 ?  153 LEU   B HA   1 
ATOM   6317 H  HB2  . LEU   B 1 153 ? 40.365 -27.986 -9.997  1.00 14.02 ?  153 LEU   B HB2  1 
ATOM   6318 H  HB3  . LEU   B 1 153 ? 41.027 -27.957 -8.559  1.00 14.02 ?  153 LEU   B HB3  1 
ATOM   6319 H  HG   . LEU   B 1 153 ? 39.063 -26.081 -9.317  1.00 15.32 ?  153 LEU   B HG   1 
ATOM   6320 H  HD11 . LEU   B 1 153 ? 37.487 -27.365 -8.202  1.00 16.41 ?  153 LEU   B HD11 1 
ATOM   6321 H  HD12 . LEU   B 1 153 ? 38.120 -28.218 -9.382  1.00 16.41 ?  153 LEU   B HD12 1 
ATOM   6322 H  HD13 . LEU   B 1 153 ? 38.590 -28.463 -7.885  1.00 16.41 ?  153 LEU   B HD13 1 
ATOM   6323 H  HD21 . LEU   B 1 153 ? 38.861 -25.716 -7.008  1.00 15.81 ?  153 LEU   B HD21 1 
ATOM   6324 H  HD22 . LEU   B 1 153 ? 40.057 -26.733 -6.762  1.00 15.81 ?  153 LEU   B HD22 1 
ATOM   6325 H  HD23 . LEU   B 1 153 ? 40.322 -25.363 -7.522  1.00 15.81 ?  153 LEU   B HD23 1 
ATOM   6326 N  N    . ALA   B 1 154 ? 44.009 -27.136 -9.371  1.00 11.64 ?  154 ALA   B N    1 
ATOM   6327 C  CA   . ALA   B 1 154 ? 45.234 -27.901 -9.561  1.00 12.99 ?  154 ALA   B CA   1 
ATOM   6328 C  C    . ALA   B 1 154 ? 45.298 -28.975 -8.486  1.00 13.69 ?  154 ALA   B C    1 
ATOM   6329 O  O    . ALA   B 1 154 ? 45.219 -28.674 -7.288  1.00 14.52 ?  154 ALA   B O    1 
ATOM   6330 C  CB   . ALA   B 1 154 ? 46.460 -26.992 -9.497  1.00 13.70 ?  154 ALA   B CB   1 
ATOM   6331 H  H    . ALA   B 1 154 ? 44.034 -26.605 -8.693  1.00 14.03 ?  154 ALA   B H    1 
ATOM   6332 H  HA   . ALA   B 1 154 ? 45.218 -28.332 -10.427 1.00 15.64 ?  154 ALA   B HA   1 
ATOM   6333 H  HB1  . ALA   B 1 154 ? 47.260 -27.524 -9.625  1.00 16.49 ?  154 ALA   B HB1  1 
ATOM   6334 H  HB2  . ALA   B 1 154 ? 46.395 -26.321 -10.198 1.00 16.49 ?  154 ALA   B HB2  1 
ATOM   6335 H  HB3  . ALA   B 1 154 ? 46.490 -26.555 -8.630  1.00 16.49 ?  154 ALA   B HB3  1 
ATOM   6336 N  N    . VAL   B 1 155 ? 45.420 -30.223 -8.918  1.00 12.89 ?  155 VAL   B N    1 
ATOM   6337 C  CA   . VAL   B 1 155 ? 45.527 -31.367 -8.021  1.00 12.81 ?  155 VAL   B CA   1 
ATOM   6338 C  C    . VAL   B 1 155 ? 46.868 -32.035 -8.300  1.00 12.86 ?  155 VAL   B C    1 
ATOM   6339 O  O    . VAL   B 1 155 ? 47.102 -32.529 -9.410  1.00 14.90 ?  155 VAL   B O    1 
ATOM   6340 C  CB   . VAL   B 1 155 ? 44.369 -32.360 -8.212  1.00 14.47 ?  155 VAL   B CB   1 
ATOM   6341 C  CG1  . VAL   B 1 155 ? 44.548 -33.562 -7.294  1.00 13.96 ?  155 VAL   B CG1  1 
ATOM   6342 C  CG2  . VAL   B 1 155 ? 43.034 -31.673 -7.944  1.00 15.35 ?  155 VAL   B CG2  1 
ATOM   6343 H  H    . VAL   B 1 155 ? 45.454 -30.442 -9.752  1.00 15.52 ?  155 VAL   B H    1 
ATOM   6344 H  HA   . VAL   B 1 155 ? 45.521 -31.064 -7.101  1.00 15.42 ?  155 VAL   B HA   1 
ATOM   6345 H  HB   . VAL   B 1 155 ? 44.364 -32.675 -9.129  1.00 17.42 ?  155 VAL   B HB   1 
ATOM   6346 H  HG11 . VAL   B 1 155 ? 43.723 -34.071 -7.267  1.00 16.81 ?  155 VAL   B HG11 1 
ATOM   6347 H  HG12 . VAL   B 1 155 ? 45.266 -34.123 -7.637  1.00 16.81 ?  155 VAL   B HG12 1 
ATOM   6348 H  HG13 . VAL   B 1 155 ? 44.773 -33.252 -6.401  1.00 16.81 ?  155 VAL   B HG13 1 
ATOM   6349 H  HG21 . VAL   B 1 155 ? 42.323 -32.326 -8.029  1.00 18.47 ?  155 VAL   B HG21 1 
ATOM   6350 H  HG22 . VAL   B 1 155 ? 43.045 -31.310 -7.044  1.00 18.47 ?  155 VAL   B HG22 1 
ATOM   6351 H  HG23 . VAL   B 1 155 ? 42.912 -30.960 -8.588  1.00 18.47 ?  155 VAL   B HG23 1 
ATOM   6352 N  N    . PHE   B 1 156 ? 47.731 -32.084 -7.283  1.00 13.29 ?  156 PHE   B N    1 
ATOM   6353 C  CA   . PHE   B 1 156 ? 49.109 -32.541 -7.482  1.00 14.62 ?  156 PHE   B CA   1 
ATOM   6354 C  C    . PHE   B 1 156 ? 49.203 -34.043 -7.764  1.00 15.53 ?  156 PHE   B C    1 
ATOM   6355 O  O    . PHE   B 1 156 ? 49.923 -34.472 -8.677  1.00 17.75 ?  156 PHE   B O    1 
ATOM   6356 C  CB   . PHE   B 1 156 ? 49.943 -32.167 -6.256  1.00 14.81 ?  156 PHE   B CB   1 
ATOM   6357 C  CG   . PHE   B 1 156 ? 51.366 -32.632 -6.316  1.00 15.17 ?  156 PHE   B CG   1 
ATOM   6358 C  CD1  . PHE   B 1 156 ? 52.248 -32.097 -7.237  1.00 16.97 ?  156 PHE   B CD1  1 
ATOM   6359 C  CD2  . PHE   B 1 156 ? 51.830 -33.585 -5.431  1.00 15.68 ?  156 PHE   B CD2  1 
ATOM   6360 C  CE1  . PHE   B 1 156 ? 53.569 -32.511 -7.284  1.00 17.72 ?  156 PHE   B CE1  1 
ATOM   6361 C  CE2  . PHE   B 1 156 ? 53.150 -34.004 -5.473  1.00 17.16 ?  156 PHE   B CE2  1 
ATOM   6362 C  CZ   . PHE   B 1 156 ? 54.012 -33.469 -6.406  1.00 17.76 ?  156 PHE   B CZ   1 
ATOM   6363 H  H    . PHE   B 1 156 ? 47.546 -31.867 -6.472  1.00 16.01 ?  156 PHE   B H    1 
ATOM   6364 H  HA   . PHE   B 1 156 ? 49.481 -32.076 -8.244  1.00 17.60 ?  156 PHE   B HA   1 
ATOM   6365 H  HB2  . PHE   B 1 156 ? 49.954 -31.202 -6.172  1.00 17.82 ?  156 PHE   B HB2  1 
ATOM   6366 H  HB3  . PHE   B 1 156 ? 49.539 -32.562 -5.468  1.00 17.82 ?  156 PHE   B HB3  1 
ATOM   6367 H  HD1  . PHE   B 1 156 ? 51.954 -31.449 -7.834  1.00 20.42 ?  156 PHE   B HD1  1 
ATOM   6368 H  HD2  . PHE   B 1 156 ? 51.244 -33.953 -4.805  1.00 18.87 ?  156 PHE   B HD2  1 
ATOM   6369 H  HE1  . PHE   B 1 156 ? 54.150 -32.147 -7.913  1.00 21.32 ?  156 PHE   B HE1  1 
ATOM   6370 H  HE2  . PHE   B 1 156 ? 53.448 -34.659 -4.878  1.00 20.65 ?  156 PHE   B HE2  1 
ATOM   6371 H  HZ   . PHE   B 1 156 ? 54.899 -33.754 -6.435  1.00 21.37 ?  156 PHE   B HZ   1 
ATOM   6372 N  N    . ASP   B 1 157 ? 48.539 -34.864 -6.961  1.00 15.86 ?  157 ASP   B N    1 
ATOM   6373 C  CA   . ASP   B 1 157 ? 48.686 -36.311 -7.060  1.00 17.15 ?  157 ASP   B CA   1 
ATOM   6374 C  C    . ASP   B 1 157 ? 47.772 -36.855 -8.154  1.00 17.43 ?  157 ASP   B C    1 
ATOM   6375 O  O    . ASP   B 1 157 ? 46.546 -36.735 -8.055  1.00 17.07 ?  157 ASP   B O    1 
ATOM   6376 C  CB   . ASP   B 1 157 ? 48.328 -36.925 -5.714  1.00 18.86 ?  157 ASP   B CB   1 
ATOM   6377 C  CG   . ASP   B 1 157 ? 48.479 -38.434 -5.699  1.00 20.72 ?  157 ASP   B CG   1 
ATOM   6378 O  OD1  . ASP   B 1 157 ? 48.805 -39.034 -6.752  1.00 21.03 ?  157 ASP   B OD1  1 
ATOM   6379 O  OD2  . ASP   B 1 157 ? 48.283 -39.018 -4.616  1.00 22.73 -1 157 ASP   B OD2  1 
ATOM   6380 H  H    . ASP   B 1 157 ? 48.002 -34.610 -6.345  1.00 19.09 ?  157 ASP   B H    1 
ATOM   6381 H  HA   . ASP   B 1 157 ? 49.607 -36.543 -7.275  1.00 20.64 ?  157 ASP   B HA   1 
ATOM   6382 H  HB2  . ASP   B 1 157 ? 48.903 -36.542 -5.033  1.00 22.69 ?  157 ASP   B HB2  1 
ATOM   6383 H  HB3  . ASP   B 1 157 ? 47.400 -36.713 -5.512  1.00 22.69 ?  157 ASP   B HB3  1 
ATOM   6384 N  N    . LYS   B 1 158 ? 48.367 -37.472 -9.184  1.00 18.45 ?  158 LYS   B N    1 
ATOM   6385 C  CA   . LYS   B 1 158 ? 47.591 -38.086 -10.265 1.00 19.58 ?  158 LYS   B CA   1 
ATOM   6386 C  C    . LYS   B 1 158 ? 46.528 -39.050 -9.735  1.00 19.32 ?  158 LYS   B C    1 
ATOM   6387 O  O    . LYS   B 1 158 ? 45.424 -39.142 -10.289 1.00 19.45 ?  158 LYS   B O    1 
ATOM   6388 C  CB   . LYS   B 1 158 ? 48.538 -38.813 -11.229 1.00 21.24 ?  158 LYS   B CB   1 
ATOM   6389 C  CG   . LYS   B 1 158 ? 47.853 -39.715 -12.246 1.00 23.91 ?  158 LYS   B CG   1 
ATOM   6390 C  CD   . LYS   B 1 158 ? 47.010 -38.929 -13.228 1.00 26.34 ?  158 LYS   B CD   1 
ATOM   6391 C  CE   . LYS   B 1 158 ? 46.402 -39.845 -14.275 1.00 28.62 ?  158 LYS   B CE   1 
ATOM   6392 N  NZ   . LYS   B 1 158 ? 45.350 -39.153 -15.071 1.00 29.56 ?  158 LYS   B NZ   1 
ATOM   6393 H  H    . LYS   B 1 158 ? 49.222 -37.542 -9.283  1.00 22.20 ?  158 LYS   B H    1 
ATOM   6394 H  HA   . LYS   B 1 158 ? 47.143 -37.387 -10.769 1.00 23.55 ?  158 LYS   B HA   1 
ATOM   6395 H  HB2  . LYS   B 1 158 ? 49.046 -38.151 -11.729 1.00 25.54 ?  158 LYS   B HB2  1 
ATOM   6396 H  HB3  . LYS   B 1 158 ? 49.147 -39.363 -10.713 1.00 25.54 ?  158 LYS   B HB3  1 
ATOM   6397 H  HG2  . LYS   B 1 158 ? 48.534 -40.187 -12.752 1.00 28.75 ?  158 LYS   B HG2  1 
ATOM   6398 H  HG3  . LYS   B 1 158 ? 47.283 -40.360 -11.795 1.00 28.75 ?  158 LYS   B HG3  1 
ATOM   6399 H  HD2  . LYS   B 1 158 ? 46.290 -38.486 -12.754 1.00 31.67 ?  158 LYS   B HD2  1 
ATOM   6400 H  HD3  . LYS   B 1 158 ? 47.568 -38.277 -13.681 1.00 31.67 ?  158 LYS   B HD3  1 
ATOM   6401 H  HE2  . LYS   B 1 158 ? 47.095 -40.141 -14.884 1.00 34.40 ?  158 LYS   B HE2  1 
ATOM   6402 H  HE3  . LYS   B 1 158 ? 45.996 -40.609 -13.836 1.00 34.40 ?  158 LYS   B HE3  1 
ATOM   6403 H  HZ1  . LYS   B 1 158 ? 45.009 -39.709 -15.675 1.00 35.52 ?  158 LYS   B HZ1  1 
ATOM   6404 H  HZ2  . LYS   B 1 158 ? 44.697 -38.872 -14.535 1.00 35.52 ?  158 LYS   B HZ2  1 
ATOM   6405 H  HZ3  . LYS   B 1 158 ? 45.701 -38.450 -15.490 1.00 35.52 ?  158 LYS   B HZ3  1 
ATOM   6406 N  N    . ASN   B 1 159 ? 46.852 -39.808 -8.685  1.00 19.52 ?  159 ASN   B N    1 
ATOM   6407 C  CA   . ASN   B 1 159 ? 45.896 -40.786 -8.173  1.00 19.90 ?  159 ASN   B CA   1 
ATOM   6408 C  C    . ASN   B 1 159 ? 44.704 -40.113 -7.492  1.00 19.15 ?  159 ASN   B C    1 
ATOM   6409 O  O    . ASN   B 1 159 ? 43.570 -40.603 -7.594  1.00 19.73 ?  159 ASN   B O    1 
ATOM   6410 C  CB   . ASN   B 1 159 ? 46.609 -41.765 -7.243  1.00 21.32 ?  159 ASN   B CB   1 
ATOM   6411 C  CG   . ASN   B 1 159 ? 47.640 -42.606 -7.972  1.00 23.38 ?  159 ASN   B CG   1 
ATOM   6412 O  OD1  . ASN   B 1 159 ? 47.388 -43.100 -9.079  1.00 23.91 ?  159 ASN   B OD1  1 
ATOM   6413 N  ND2  . ASN   B 1 159 ? 48.808 -42.781 -7.355  1.00 24.05 ?  159 ASN   B ND2  1 
ATOM   6414 H  H    . ASN   B 1 159 ? 47.599 -39.767 -8.265  1.00 23.48 ?  159 ASN   B H    1 
ATOM   6415 H  HA   . ASN   B 1 159 ? 45.558 -41.299 -8.926  1.00 23.94 ?  159 ASN   B HA   1 
ATOM   6416 H  HB2  . ASN   B 1 159 ? 47.067 -41.269 -6.548  1.00 25.64 ?  159 ASN   B HB2  1 
ATOM   6417 H  HB3  . ASN   B 1 159 ? 45.960 -42.368 -6.859  1.00 25.64 ?  159 ASN   B HB3  1 
ATOM   6418 H  HD21 . ASN   B 1 159 ? 49.431 -43.250 -7.727  1.00 28.92 ?  159 ASN   B HD21 1 
ATOM   6419 H  HD22 . ASN   B 1 159 ? 48.943 -42.440 -6.577  1.00 28.92 ?  159 ASN   B HD22 1 
ATOM   6420 N  N    . LEU   B 1 160 ? 44.921 -38.981 -6.815  1.00 18.19 ?  160 LEU   B N    1 
ATOM   6421 C  CA   . LEU   B 1 160 ? 43.785 -38.246 -6.273  1.00 17.40 ?  160 LEU   B CA   1 
ATOM   6422 C  C    . LEU   B 1 160 ? 42.994 -37.583 -7.389  1.00 16.73 ?  160 LEU   B C    1 
ATOM   6423 O  O    . LEU   B 1 160 ? 41.757 -37.583 -7.367  1.00 16.11 ?  160 LEU   B O    1 
ATOM   6424 C  CB   . LEU   B 1 160 ? 44.254 -37.213 -5.251  1.00 17.00 ?  160 LEU   B CB   1 
ATOM   6425 C  CG   . LEU   B 1 160 ? 43.130 -36.316 -4.716  1.00 16.56 ?  160 LEU   B CG   1 
ATOM   6426 C  CD1  . LEU   B 1 160 ? 42.015 -37.148 -4.094  1.00 17.32 ?  160 LEU   B CD1  1 
ATOM   6427 C  CD2  . LEU   B 1 160 ? 43.675 -35.318 -3.716  1.00 16.65 ?  160 LEU   B CD2  1 
ATOM   6428 H  H    . LEU   B 1 160 ? 45.699 -38.632 -6.667  1.00 21.89 ?  160 LEU   B H    1 
ATOM   6429 H  HA   . LEU   B 1 160 ? 43.205 -38.874 -5.826  1.00 20.94 ?  160 LEU   B HA   1 
ATOM   6430 H  HB2  . LEU   B 1 160 ? 44.656 -37.684 -4.499  1.00 20.46 ?  160 LEU   B HB2  1 
ATOM   6431 H  HB3  . LEU   B 1 160 ? 44.926 -36.644 -5.669  1.00 20.46 ?  160 LEU   B HB3  1 
ATOM   6432 H  HG   . LEU   B 1 160 ? 42.754 -35.819 -5.454  1.00 19.93 ?  160 LEU   B HG   1 
ATOM   6433 H  HD11 . LEU   B 1 160 ? 41.387 -36.552 -3.663  1.00 20.84 ?  160 LEU   B HD11 1 
ATOM   6434 H  HD12 . LEU   B 1 160 ? 41.566 -37.655 -4.790  1.00 20.84 ?  160 LEU   B HD12 1 
ATOM   6435 H  HD13 . LEU   B 1 160 ? 42.399 -37.756 -3.440  1.00 20.84 ?  160 LEU   B HD13 1 
ATOM   6436 H  HD21 . LEU   B 1 160 ? 42.948 -34.751 -3.417  1.00 20.03 ?  160 LEU   B HD21 1 
ATOM   6437 H  HD22 . LEU   B 1 160 ? 44.053 -35.798 -2.963  1.00 20.03 ?  160 LEU   B HD22 1 
ATOM   6438 H  HD23 . LEU   B 1 160 ? 44.360 -34.782 -4.146  1.00 20.03 ?  160 LEU   B HD23 1 
ATOM   6439 N  N    . TYR   B 1 161 ? 43.691 -37.017 -8.376  1.00 16.60 ?  161 TYR   B N    1 
ATOM   6440 C  CA   . TYR   B 1 161 ? 43.017 -36.443 -9.536  1.00 16.32 ?  161 TYR   B CA   1 
ATOM   6441 C  C    . TYR   B 1 161 ? 42.077 -37.460 -10.167 1.00 16.32 ?  161 TYR   B C    1 
ATOM   6442 O  O    . TYR   B 1 161 ? 40.908 -37.163 -10.430 1.00 16.07 ?  161 TYR   B O    1 
ATOM   6443 C  CB   . TYR   B 1 161 ? 44.057 -35.950 -10.551 1.00 16.94 ?  161 TYR   B CB   1 
ATOM   6444 C  CG   . TYR   B 1 161 ? 43.480 -35.489 -11.867 1.00 17.52 ?  161 TYR   B CG   1 
ATOM   6445 C  CD1  . TYR   B 1 161 ? 43.076 -34.170 -12.042 1.00 17.56 ?  161 TYR   B CD1  1 
ATOM   6446 C  CD2  . TYR   B 1 161 ? 43.325 -36.370 -12.933 1.00 18.15 ?  161 TYR   B CD2  1 
ATOM   6447 C  CE1  . TYR   B 1 161 ? 42.543 -33.741 -13.233 1.00 18.77 ?  161 TYR   B CE1  1 
ATOM   6448 C  CE2  . TYR   B 1 161 ? 42.785 -35.949 -14.129 1.00 19.15 ?  161 TYR   B CE2  1 
ATOM   6449 C  CZ   . TYR   B 1 161 ? 42.399 -34.631 -14.274 1.00 19.40 ?  161 TYR   B CZ   1 
ATOM   6450 O  OH   . TYR   B 1 161 ? 41.861 -34.198 -15.462 1.00 21.31 ?  161 TYR   B OH   1 
ATOM   6451 H  H    . TYR   B 1 161 ? 44.545 -36.951 -8.401  1.00 19.98 ?  161 TYR   B H    1 
ATOM   6452 H  HA   . TYR   B 1 161 ? 42.486 -35.681 -9.257  1.00 19.63 ?  161 TYR   B HA   1 
ATOM   6453 H  HB2  . TYR   B 1 161 ? 44.534 -35.196 -10.165 1.00 20.38 ?  161 TYR   B HB2  1 
ATOM   6454 H  HB3  . TYR   B 1 161 ? 44.676 -36.667 -10.740 1.00 20.38 ?  161 TYR   B HB3  1 
ATOM   6455 H  HD1  . TYR   B 1 161 ? 43.170 -33.560 -11.345 1.00 21.13 ?  161 TYR   B HD1  1 
ATOM   6456 H  HD2  . TYR   B 1 161 ? 43.582 -37.257 -12.837 1.00 21.84 ?  161 TYR   B HD2  1 
ATOM   6457 H  HE1  . TYR   B 1 161 ? 42.276 -32.850 -13.334 1.00 22.58 ?  161 TYR   B HE1  1 
ATOM   6458 H  HE2  . TYR   B 1 161 ? 42.684 -36.547 -14.836 1.00 23.04 ?  161 TYR   B HE2  1 
ATOM   6459 H  HH   . TYR   B 1 161 ? 41.814 -34.839 -16.007 1.00 25.63 ?  161 TYR   B HH   1 
ATOM   6460 N  N    . ASP   B 1 162 ? 42.570 -38.681 -10.392 1.00 16.81 ?  162 ASP   B N    1 
ATOM   6461 C  CA   . ASP   B 1 162 ? 41.743 -39.717 -11.004 1.00 17.43 ?  162 ASP   B CA   1 
ATOM   6462 C  C    . ASP   B 1 162 ? 40.537 -40.055 -10.134 1.00 16.85 ?  162 ASP   B C    1 
ATOM   6463 O  O    . ASP   B 1 162 ? 39.431 -40.268 -10.649 1.00 17.05 ?  162 ASP   B O    1 
ATOM   6464 C  CB   . ASP   B 1 162 ? 42.577 -40.977 -11.253 1.00 18.90 ?  162 ASP   B CB   1 
ATOM   6465 C  CG   . ASP   B 1 162 ? 43.580 -40.819 -12.384 1.00 20.33 ?  162 ASP   B CG   1 
ATOM   6466 O  OD1  . ASP   B 1 162 ? 43.451 -39.875 -13.186 1.00 20.85 ?  162 ASP   B OD1  1 
ATOM   6467 O  OD2  . ASP   B 1 162 ? 44.486 -41.674 -12.488 1.00 21.90 -1 162 ASP   B OD2  1 
ATOM   6468 H  H    . ASP   B 1 162 ? 43.372 -38.923 -10.207 1.00 20.22 ?  162 ASP   B H    1 
ATOM   6469 H  HA   . ASP   B 1 162 ? 41.417 -39.399 -11.857 1.00 20.97 ?  162 ASP   B HA   1 
ATOM   6470 H  HB2  . ASP   B 1 162 ? 43.081 -41.188 -10.454 1.00 22.74 ?  162 ASP   B HB2  1 
ATOM   6471 H  HB3  . ASP   B 1 162 ? 41.986 -41.707 -11.482 1.00 22.74 ?  162 ASP   B HB3  1 
ATOM   6472 N  N    A LYS   B 1 163 ? 40.731 -40.131 -8.817  0.78 15.89 ?  163 LYS   B N    1 
ATOM   6473 N  N    B LYS   B 1 163 ? 40.727 -40.117 -8.814  0.22 17.23 ?  163 LYS   B N    1 
ATOM   6474 C  CA   A LYS   B 1 163 ? 39.609 -40.410 -7.927  0.78 16.52 ?  163 LYS   B CA   1 
ATOM   6475 C  CA   B LYS   B 1 163 ? 39.606 -40.416 -7.926  0.22 18.12 ?  163 LYS   B CA   1 
ATOM   6476 C  C    A LYS   B 1 163 ? 38.565 -39.303 -7.998  0.78 15.36 ?  163 LYS   B C    1 
ATOM   6477 C  C    B LYS   B 1 163 ? 38.567 -39.299 -7.952  0.22 16.31 ?  163 LYS   B C    1 
ATOM   6478 O  O    A LYS   B 1 163 ? 37.356 -39.575 -8.017  0.78 16.43 ?  163 LYS   B O    1 
ATOM   6479 O  O    B LYS   B 1 163 ? 37.360 -39.563 -7.884  0.22 16.53 ?  163 LYS   B O    1 
ATOM   6480 C  CB   A LYS   B 1 163 ? 40.099 -40.582 -6.491  0.78 19.18 ?  163 LYS   B CB   1 
ATOM   6481 C  CB   B LYS   B 1 163 ? 40.106 -40.645 -6.501  0.22 20.99 ?  163 LYS   B CB   1 
ATOM   6482 C  CG   A LYS   B 1 163 ? 39.022 -41.118 -5.571  0.78 23.73 ?  163 LYS   B CG   1 
ATOM   6483 C  CG   B LYS   B 1 163 ? 39.026 -41.151 -5.563  0.22 24.16 ?  163 LYS   B CG   1 
ATOM   6484 C  CD   A LYS   B 1 163 ? 39.447 -41.145 -4.117  0.78 28.23 ?  163 LYS   B CD   1 
ATOM   6485 C  CD   B LYS   B 1 163 ? 39.503 -41.233 -4.127  0.22 27.10 ?  163 LYS   B CD   1 
ATOM   6486 C  CE   A LYS   B 1 163 ? 38.376 -41.821 -3.270  0.78 31.87 ?  163 LYS   B CE   1 
ATOM   6487 C  CE   B LYS   B 1 163 ? 38.447 -41.892 -3.254  0.22 29.78 ?  163 LYS   B CE   1 
ATOM   6488 N  NZ   A LYS   B 1 163 ? 38.510 -41.518 -1.819  0.78 34.02 ?  163 LYS   B NZ   1 
ATOM   6489 N  NZ   B LYS   B 1 163 ? 38.663 -41.630 -1.806  0.22 30.92 ?  163 LYS   B NZ   1 
ATOM   6490 H  H    A LYS   B 1 163 ? 41.491 -40.027 -8.423  0.78 19.13 ?  163 LYS   B H    1 
ATOM   6491 H  H    B LYS   B 1 163 ? 41.482 -39.998 -8.415  0.22 20.73 ?  163 LYS   B H    1 
ATOM   6492 H  HA   A LYS   B 1 163 ? 39.190 -41.236 -8.205  0.78 19.88 ?  163 LYS   B HA   1 
ATOM   6493 H  HA   B LYS   B 1 163 ? 39.177 -41.232 -8.225  0.22 21.80 ?  163 LYS   B HA   1 
ATOM   6494 H  HB2  A LYS   B 1 163 ? 40.841 -41.210 -6.485  0.78 23.08 ?  163 LYS   B HB2  1 
ATOM   6495 H  HB2  B LYS   B 1 163 ? 40.818 -41.305 -6.517  0.22 25.25 ?  163 LYS   B HB2  1 
ATOM   6496 H  HB3  A LYS   B 1 163 ? 40.388 -39.724 -6.149  0.78 23.08 ?  163 LYS   B HB3  1 
ATOM   6497 H  HB3  B LYS   B 1 163 ? 40.441 -39.808 -6.144  0.22 25.25 ?  163 LYS   B HB3  1 
ATOM   6498 H  HG2  A LYS   B 1 163 ? 38.235 -40.557 -5.641  0.78 28.53 ?  163 LYS   B HG2  1 
ATOM   6499 H  HG2  B LYS   B 1 163 ? 38.268 -40.547 -5.593  0.22 29.05 ?  163 LYS   B HG2  1 
ATOM   6500 H  HG3  A LYS   B 1 163 ? 38.804 -42.028 -5.836  0.78 28.53 ?  163 LYS   B HG3  1 
ATOM   6501 H  HG3  B LYS   B 1 163 ? 38.755 -42.040 -5.842  0.22 29.05 ?  163 LYS   B HG3  1 
ATOM   6502 H  HD2  A LYS   B 1 163 ? 40.271 -41.650 -4.030  0.78 33.93 ?  163 LYS   B HD2  1 
ATOM   6503 H  HD2  B LYS   B 1 163 ? 40.314 -41.764 -4.084  0.22 32.57 ?  163 LYS   B HD2  1 
ATOM   6504 H  HD3  A LYS   B 1 163 ? 39.567 -40.238 -3.798  0.78 33.93 ?  163 LYS   B HD3  1 
ATOM   6505 H  HD3  B LYS   B 1 163 ? 39.667 -40.338 -3.789  0.22 32.57 ?  163 LYS   B HD3  1 
ATOM   6506 H  HE2  A LYS   B 1 163 ? 37.500 -41.524 -3.564  0.78 38.30 ?  163 LYS   B HE2  1 
ATOM   6507 H  HE2  B LYS   B 1 163 ? 37.572 -41.550 -3.498  0.22 35.79 ?  163 LYS   B HE2  1 
ATOM   6508 H  HE3  A LYS   B 1 163 ? 38.449 -42.781 -3.382  0.78 38.30 ?  163 LYS   B HE3  1 
ATOM   6509 H  HE3  B LYS   B 1 163 ? 38.477 -42.852 -3.395  0.22 35.79 ?  163 LYS   B HE3  1 
ATOM   6510 H  HZ1  A LYS   B 1 163 ? 37.866 -41.929 -1.363  0.78 40.88 ?  163 LYS   B HZ1  1 
ATOM   6511 H  HZ1  B LYS   B 1 163 ? 38.027 -42.029 -1.328  0.22 37.16 ?  163 LYS   B HZ1  1 
ATOM   6512 H  HZ2  A LYS   B 1 163 ? 39.300 -41.799 -1.523  0.78 40.88 ?  163 LYS   B HZ2  1 
ATOM   6513 H  HZ2  B LYS   B 1 163 ? 39.455 -41.946 -1.556  0.22 37.16 ?  163 LYS   B HZ2  1 
ATOM   6514 H  HZ3  A LYS   B 1 163 ? 38.445 -40.641 -1.685  0.78 40.88 ?  163 LYS   B HZ3  1 
ATOM   6515 H  HZ3  B LYS   B 1 163 ? 38.636 -40.754 -1.649  0.22 37.16 ?  163 LYS   B HZ3  1 
ATOM   6516 N  N    . LEU   B 1 164 ? 39.019 -38.048 -8.044  1.00 14.95 ?  164 LEU   B N    1 
ATOM   6517 C  CA   . LEU   B 1 164 ? 38.101 -36.912 -8.090  1.00 14.35 ?  164 LEU   B CA   1 
ATOM   6518 C  C    . LEU   B 1 164 ? 37.320 -36.888 -9.398  1.00 14.55 ?  164 LEU   B C    1 
ATOM   6519 O  O    . LEU   B 1 164 ? 36.097 -36.694 -9.400  1.00 15.67 ?  164 LEU   B O    1 
ATOM   6520 C  CB   . LEU   B 1 164 ? 38.894 -35.614 -7.922  1.00 13.87 ?  164 LEU   B CB   1 
ATOM   6521 C  CG   . LEU   B 1 164 ? 39.431 -35.333 -6.524  1.00 14.65 ?  164 LEU   B CG   1 
ATOM   6522 C  CD1  . LEU   B 1 164 ? 40.520 -34.268 -6.586  1.00 14.53 ?  164 LEU   B CD1  1 
ATOM   6523 C  CD2  . LEU   B 1 164 ? 38.314 -34.902 -5.593  1.00 16.15 ?  164 LEU   B CD2  1 
ATOM   6524 H  H    A LEU   B 1 164 ? 39.854 -37.829 -8.049  0.78 18.00 ?  164 LEU   B H    1 
ATOM   6525 H  H    B LEU   B 1 164 ? 39.854 -37.831 -8.087  0.22 18.00 ?  164 LEU   B H    1 
ATOM   6526 H  HA   . LEU   B 1 164 ? 37.472 -36.982 -7.363  1.00 17.28 ?  164 LEU   B HA   1 
ATOM   6527 H  HB2  . LEU   B 1 164 ? 39.659 -35.640 -8.523  1.00 16.69 ?  164 LEU   B HB2  1 
ATOM   6528 H  HB3  . LEU   B 1 164 ? 38.322 -34.872 -8.167  1.00 16.69 ?  164 LEU   B HB3  1 
ATOM   6529 H  HG   . LEU   B 1 164 ? 39.828 -36.138 -6.169  1.00 17.64 ?  164 LEU   B HG   1 
ATOM   6530 H  HD11 . LEU   B 1 164 ? 40.842 -34.090 -5.687  1.00 17.49 ?  164 LEU   B HD11 1 
ATOM   6531 H  HD12 . LEU   B 1 164 ? 41.251 -34.590 -7.138  1.00 17.49 ?  164 LEU   B HD12 1 
ATOM   6532 H  HD13 . LEU   B 1 164 ? 40.153 -33.455 -6.970  1.00 17.49 ?  164 LEU   B HD13 1 
ATOM   6533 H  HD21 . LEU   B 1 164 ? 38.688 -34.686 -4.725  1.00 19.43 ?  164 LEU   B HD21 1 
ATOM   6534 H  HD22 . LEU   B 1 164 ? 37.870 -34.123 -5.964  1.00 19.43 ?  164 LEU   B HD22 1 
ATOM   6535 H  HD23 . LEU   B 1 164 ? 37.679 -35.632 -5.506  1.00 19.43 ?  164 LEU   B HD23 1 
ATOM   6536 N  N    . VAL   B 1 165 ? 38.011 -37.060 -10.525 1.00 16.14 ?  165 VAL   B N    1 
ATOM   6537 C  CA   . VAL   B 1 165 ? 37.356 -36.999 -11.829 1.00 17.45 ?  165 VAL   B CA   1 
ATOM   6538 C  C    . VAL   B 1 165 ? 36.431 -38.194 -12.013 1.00 19.15 ?  165 VAL   B C    1 
ATOM   6539 O  O    . VAL   B 1 165 ? 35.268 -38.052 -12.413 1.00 20.22 ?  165 VAL   B O    1 
ATOM   6540 C  CB   . VAL   B 1 165 ? 38.405 -36.922 -12.953 1.00 18.58 ?  165 VAL   B CB   1 
ATOM   6541 C  CG1  . VAL   B 1 165 ? 37.750 -37.043 -14.310 1.00 19.83 ?  165 VAL   B CG1  1 
ATOM   6542 C  CG2  . VAL   B 1 165 ? 39.197 -35.630 -12.852 1.00 18.26 ?  165 VAL   B CG2  1 
ATOM   6543 H  H    . VAL   B 1 165 ? 38.861 -37.205 -10.563 1.00 19.42 ?  165 VAL   B H    1 
ATOM   6544 H  HA   . VAL   B 1 165 ? 36.819 -36.197 -11.875 1.00 20.99 ?  165 VAL   B HA   1 
ATOM   6545 H  HB   . VAL   B 1 165 ? 39.034 -37.655 -12.855 1.00 22.36 ?  165 VAL   B HB   1 
ATOM   6546 H  HG11 . VAL   B 1 165 ? 38.374 -36.751 -14.991 1.00 23.85 ?  165 VAL   B HG11 1 
ATOM   6547 H  HG12 . VAL   B 1 165 ? 37.516 -37.975 -14.460 1.00 23.85 ?  165 VAL   B HG12 1 
ATOM   6548 H  HG13 . VAL   B 1 165 ? 36.955 -36.494 -14.327 1.00 23.85 ?  165 VAL   B HG13 1 
ATOM   6549 H  HG21 . VAL   B 1 165 ? 39.833 -35.588 -13.585 1.00 21.97 ?  165 VAL   B HG21 1 
ATOM   6550 H  HG22 . VAL   B 1 165 ? 38.585 -34.879 -12.904 1.00 21.97 ?  165 VAL   B HG22 1 
ATOM   6551 H  HG23 . VAL   B 1 165 ? 39.671 -35.612 -12.005 1.00 21.97 ?  165 VAL   B HG23 1 
ATOM   6552 N  N    . SER   B 1 166 ? 36.943 -39.395 -11.728 1.00 19.94 ?  166 SER   B N    1 
ATOM   6553 C  CA   . SER   B 1 166 ? 36.188 -40.607 -12.010 1.00 21.12 ?  166 SER   B CA   1 
ATOM   6554 C  C    . SER   B 1 166 ? 34.932 -40.698 -11.158 1.00 21.44 ?  166 SER   B C    1 
ATOM   6555 O  O    . SER   B 1 166 ? 33.961 -41.322 -11.580 1.00 22.86 ?  166 SER   B O    1 
ATOM   6556 C  CB   . SER   B 1 166 ? 37.056 -41.860 -11.836 1.00 21.86 ?  166 SER   B CB   1 
ATOM   6557 O  OG   . SER   B 1 166 ? 37.429 -42.064 -10.483 1.00 21.68 ?  166 SER   B OG   1 
ATOM   6558 H  H    . SER   B 1 166 ? 37.721 -39.533 -11.383 1.00 23.98 ?  166 SER   B H    1 
ATOM   6559 H  HA   . SER   B 1 166 ? 35.908 -40.586 -12.939 1.00 25.40 ?  166 SER   B HA   1 
ATOM   6560 H  HB2  . SER   B 1 166 ? 36.554 -42.633 -12.139 1.00 26.29 ?  166 SER   B HB2  1 
ATOM   6561 H  HB3  . SER   B 1 166 ? 37.857 -41.761 -12.376 1.00 26.29 ?  166 SER   B HB3  1 
ATOM   6562 H  HG   . SER   B 1 166 ? 37.883 -41.410 -10.214 1.00 26.07 ?  166 SER   B HG   1 
ATOM   6563 N  N    . SER   B 1 167 ? 34.917 -40.087 -9.975  1.00 19.96 ?  167 SER   B N    1 
ATOM   6564 C  CA   . SER   B 1 167 ? 33.765 -40.147 -9.081  1.00 19.57 ?  167 SER   B CA   1 
ATOM   6565 C  C    . SER   B 1 167 ? 32.844 -38.931 -9.176  1.00 19.18 ?  167 SER   B C    1 
ATOM   6566 O  O    . SER   B 1 167 ? 31.765 -38.938 -8.570  1.00 19.33 ?  167 SER   B O    1 
ATOM   6567 C  CB   . SER   B 1 167 ? 34.222 -40.330 -7.628  1.00 19.37 ?  167 SER   B CB   1 
ATOM   6568 O  OG   . SER   B 1 167 ? 34.885 -39.172 -7.147  1.00 19.04 ?  167 SER   B OG   1 
ATOM   6569 H  H    . SER   B 1 167 ? 35.568 -39.632 -9.670  1.00 24.01 ?  167 SER   B H    1 
ATOM   6570 H  HA   . SER   B 1 167 ? 33.236 -40.928 -9.317  1.00 23.54 ?  167 SER   B HA   1 
ATOM   6571 H  HB2  . SER   B 1 167 ? 33.443 -40.509 -7.077  1.00 23.30 ?  167 SER   B HB2  1 
ATOM   6572 H  HB3  . SER   B 1 167 ? 34.831 -41.090 -7.588  1.00 23.30 ?  167 SER   B HB3  1 
ATOM   6573 H  HG   . SER   B 1 167 ? 35.558 -39.017 -7.626  1.00 22.91 ?  167 SER   B HG   1 
ATOM   6574 N  N    . PHE   B 1 168 ? 33.221 -37.893 -9.924  1.00 18.57 ?  168 PHE   B N    1 
ATOM   6575 C  CA   . PHE   B 1 168 ? 32.382 -36.695 -9.985  1.00 17.83 ?  168 PHE   B CA   1 
ATOM   6576 C  C    . PHE   B 1 168 ? 31.072 -36.960 -10.723 1.00 15.90 ?  168 PHE   B C    1 
ATOM   6577 O  O    . PHE   B 1 168 ? 30.026 -36.370 -10.388 1.00 16.50 ?  168 PHE   B O    1 
ATOM   6578 C  CB   . PHE   B 1 168 ? 33.141 -35.551 -10.652 1.00 18.62 ?  168 PHE   B CB   1 
ATOM   6579 C  CG   . PHE   B 1 168 ? 32.331 -34.302 -10.778 1.00 18.74 ?  168 PHE   B CG   1 
ATOM   6580 C  CD1  . PHE   B 1 168 ? 32.003 -33.567 -9.648  1.00 19.60 ?  168 PHE   B CD1  1 
ATOM   6581 C  CD2  . PHE   B 1 168 ? 31.882 -33.868 -12.008 1.00 18.13 ?  168 PHE   B CD2  1 
ATOM   6582 C  CE1  . PHE   B 1 168 ? 31.238 -32.423 -9.741  1.00 19.99 ?  168 PHE   B CE1  1 
ATOM   6583 C  CE2  . PHE   B 1 168 ? 31.127 -32.707 -12.114 1.00 18.90 ?  168 PHE   B CE2  1 
ATOM   6584 C  CZ   . PHE   B 1 168 ? 30.800 -31.985 -10.975 1.00 19.11 ?  168 PHE   B CZ   1 
ATOM   6585 H  H    . PHE   B 1 168 ? 33.939 -37.856 -10.395 1.00 22.34 ?  168 PHE   B H    1 
ATOM   6586 H  HA   . PHE   B 1 168 ? 32.157 -36.423 -9.084  1.00 21.45 ?  168 PHE   B HA   1 
ATOM   6587 H  HB2  . PHE   B 1 168 ? 33.921 -35.344 -10.120 1.00 22.40 ?  168 PHE   B HB2  1 
ATOM   6588 H  HB3  . PHE   B 1 168 ? 33.402 -35.823 -11.542 1.00 22.40 ?  168 PHE   B HB3  1 
ATOM   6589 H  HD1  . PHE   B 1 168 ? 32.289 -33.865 -8.814  1.00 23.58 ?  168 PHE   B HD1  1 
ATOM   6590 H  HD2  . PHE   B 1 168 ? 32.096 -34.347 -12.774 1.00 21.81 ?  168 PHE   B HD2  1 
ATOM   6591 H  HE1  . PHE   B 1 168 ? 31.024 -31.943 -8.974  1.00 24.05 ?  168 PHE   B HE1  1 
ATOM   6592 H  HE2  . PHE   B 1 168 ? 30.826 -32.418 -12.949 1.00 22.73 ?  168 PHE   B HE2  1 
ATOM   6593 H  HZ   . PHE   B 1 168 ? 30.288 -31.212 -11.046 1.00 22.99 ?  168 PHE   B HZ   1 
ATOM   6594 N  N    . LEU   B 1 169 ? 31.109 -37.841 -11.722 1.00 16.05 ?  169 LEU   B N    1 
ATOM   6595 C  CA   . LEU   B 1 169 ? 29.934 -38.157 -12.525 1.00 18.07 ?  169 LEU   B CA   1 
ATOM   6596 C  C    . LEU   B 1 169 ? 29.926 -39.600 -13.018 1.00 20.62 ?  169 LEU   B C    1 
ATOM   6597 O  O    . LEU   B 1 169 ? 29.007 -40.030 -13.718 1.00 23.14 ?  169 LEU   B O    1 
ATOM   6598 C  CB   . LEU   B 1 169 ? 29.847 -37.215 -13.727 1.00 19.95 ?  169 LEU   B CB   1 
ATOM   6599 C  CG   . LEU   B 1 169 ? 28.580 -36.363 -13.810 1.00 22.91 ?  169 LEU   B CG   1 
ATOM   6600 C  CD1  . LEU   B 1 169 ? 28.510 -35.663 -15.154 1.00 23.96 ?  169 LEU   B CD1  1 
ATOM   6601 C  CD2  . LEU   B 1 169 ? 27.330 -37.195 -13.571 1.00 22.95 ?  169 LEU   B CD2  1 
ATOM   6602 O  OXT  . LEU   B 1 169 ? 30.852 -40.352 -12.731 1.00 21.48 -1 169 LEU   B OXT  1 
ATOM   6603 H  H    . LEU   B 1 169 ? 31.815 -38.269 -11.967 1.00 19.32 ?  169 LEU   B H    1 
ATOM   6604 H  HA   . LEU   B 1 169 ? 29.148 -38.021 -11.978 1.00 21.74 ?  169 LEU   B HA   1 
ATOM   6605 H  HB2  . LEU   B 1 169 ? 30.601 -36.604 -13.701 1.00 24.00 ?  169 LEU   B HB2  1 
ATOM   6606 H  HB3  . LEU   B 1 169 ? 29.889 -37.741 -14.542 1.00 24.00 ?  169 LEU   B HB3  1 
ATOM   6607 H  HG   . LEU   B 1 169 ? 28.616 -35.677 -13.123 1.00 27.55 ?  169 LEU   B HG   1 
ATOM   6608 H  HD11 . LEU   B 1 169 ? 27.715 -35.108 -15.179 1.00 28.81 ?  169 LEU   B HD11 1 
ATOM   6609 H  HD12 . LEU   B 1 169 ? 29.302 -35.115 -15.263 1.00 28.81 ?  169 LEU   B HD12 1 
ATOM   6610 H  HD13 . LEU   B 1 169 ? 28.470 -36.333 -15.853 1.00 28.81 ?  169 LEU   B HD13 1 
ATOM   6611 H  HD21 . LEU   B 1 169 ? 26.574 -36.764 -13.993 1.00 27.60 ?  169 LEU   B HD21 1 
ATOM   6612 H  HD22 . LEU   B 1 169 ? 27.464 -38.079 -13.951 1.00 27.60 ?  169 LEU   B HD22 1 
ATOM   6613 H  HD23 . LEU   B 1 169 ? 27.182 -37.267 -12.616 1.00 27.60 ?  169 LEU   B HD23 1 
HETATM 6614 C  C1   T TFA   C 2 .   ? 12.145 -1.273  1.496   0.30 11.12 ?  201 TFA   A C1   1 
HETATM 6615 C  C2   T TFA   C 2 .   ? 12.767 -1.723  0.145   0.30 13.68 ?  201 TFA   A C2   1 
HETATM 6616 O  O    T TFA   C 2 .   ? 12.846 -1.562  2.475   0.30 9.61  ?  201 TFA   A O    1 
HETATM 6617 F  F1   T TFA   C 2 .   ? 12.797 -3.064  0.085   0.30 14.68 ?  201 TFA   A F1   1 
HETATM 6618 F  F2   T TFA   C 2 .   ? 12.064 -1.316  -0.924  0.30 14.21 ?  201 TFA   A F2   1 
HETATM 6619 F  F3   T TFA   C 2 .   ? 14.021 -1.293  -0.046  0.30 15.02 ?  201 TFA   A F3   1 
HETATM 6620 O  OXT  T TFA   C 2 .   ? 11.061 -0.692  1.414   0.30 11.58 ?  201 TFA   A OXT  1 
HETATM 6621 S  S    B DMS   D 3 .   ? 12.629 5.470   6.379   0.22 24.99 ?  202 DMS   A S    1 
HETATM 6622 O  O    B DMS   D 3 .   ? 13.876 6.320   6.375   0.22 25.07 ?  202 DMS   A O    1 
HETATM 6623 C  C1   B DMS   D 3 .   ? 12.091 5.340   4.650   0.22 25.13 ?  202 DMS   A C1   1 
HETATM 6624 C  C2   B DMS   D 3 .   ? 11.321 6.491   7.107   0.22 25.27 ?  202 DMS   A C2   1 
HETATM 6625 H  H11  B DMS   D 3 .   ? 12.903 4.992   4.101   0.22 30.21 ?  202 DMS   A H11  1 
HETATM 6626 H  H12  B DMS   D 3 .   ? 11.795 6.291   4.382   0.22 30.21 ?  202 DMS   A H12  1 
HETATM 6627 H  H13  B DMS   D 3 .   ? 11.317 4.655   4.674   0.22 30.21 ?  202 DMS   A H13  1 
HETATM 6628 H  H21  B DMS   D 3 .   ? 11.565 7.469   6.896   0.22 30.38 ?  202 DMS   A H21  1 
HETATM 6629 H  H22  B DMS   D 3 .   ? 10.486 6.182   6.600   0.22 30.38 ?  202 DMS   A H22  1 
HETATM 6630 H  H23  B DMS   D 3 .   ? 11.293 6.283   8.127   0.22 30.38 ?  202 DMS   A H23  1 
HETATM 6631 N  N2   B A1A8X E 4 .   ? 13.787 0.084   5.030   0.22 12.38 ?  203 A1A8X A N2   1 
HETATM 6632 C  C3   B A1A8X E 4 .   ? 15.242 -1.327  0.051   0.22 13.70 ?  203 A1A8X A C3   1 
HETATM 6633 C  C6   B A1A8X E 4 .   ? 14.109 0.874   3.942   0.22 12.66 ?  203 A1A8X A C6   1 
HETATM 6634 C  C9   B A1A8X E 4 .   ? 14.764 2.140   4.212   0.22 11.89 ?  203 A1A8X A C9   1 
HETATM 6635 C  C1   B A1A8X E 4 .   ? 15.235 -1.738  2.513   0.22 13.12 ?  203 A1A8X A C1   1 
HETATM 6636 C  C10  B A1A8X E 4 .   ? 15.304 3.299   3.546   0.22 11.73 ?  203 A1A8X A C10  1 
HETATM 6637 C  C11  B A1A8X E 4 .   ? 15.801 4.184   4.482   0.22 11.24 ?  203 A1A8X A C11  1 
HETATM 6638 C  C2   B A1A8X E 4 .   ? 15.993 -2.004  1.186   0.22 13.39 ?  203 A1A8X A C2   1 
HETATM 6639 C  C4   B A1A8X E 4 .   ? 13.868 -0.940  0.588   0.22 13.79 ?  203 A1A8X A C4   1 
HETATM 6640 C  C5   B A1A8X E 4 .   ? 13.899 -0.965  2.143   0.22 13.33 ?  203 A1A8X A C5   1 
HETATM 6641 C  C7   B A1A8X E 4 .   ? 14.077 0.511   6.290   0.22 11.41 ?  203 A1A8X A C7   1 
HETATM 6642 C  C8   B A1A8X E 4 .   ? 14.999 2.432   5.589   0.22 11.82 ?  203 A1A8X A C8   1 
HETATM 6643 N  N1   B A1A8X E 4 .   ? 13.783 0.392   2.693   0.22 13.28 ?  203 A1A8X A N1   1 
HETATM 6644 N  N3   B A1A8X E 4 .   ? 14.666 1.642   6.648   0.22 12.04 ?  203 A1A8X A N3   1 
HETATM 6645 N  N4   B A1A8X E 4 .   ? 15.623 3.643   5.767   0.22 11.23 ?  203 A1A8X A N4   1 
HETATM 6646 O  O1   B A1A8X E 4 .   ? 14.938 -2.923  3.179   0.22 12.71 ?  203 A1A8X A O1   1 
HETATM 6647 H  H7   B A1A8X E 4 .   ? 15.804 -0.462  -0.365  0.22 16.49 ?  203 A1A8X A H7   1 
HETATM 6648 H  H6   B A1A8X E 4 .   ? 15.198 -1.956  -0.852  0.22 16.49 ?  203 A1A8X A H6   1 
HETATM 6649 H  H1   B A1A8X E 4 .   ? 15.867 -1.064  3.148   0.22 15.80 ?  203 A1A8X A H1   1 
HETATM 6650 H  H12  B A1A8X E 4 .   ? 15.346 3.531   2.479   0.22 14.13 ?  203 A1A8X A H12  1 
HETATM 6651 H  H13  B A1A8X E 4 .   ? 16.292 5.162   4.473   0.22 13.54 ?  203 A1A8X A H13  1 
HETATM 6652 H  H5   B A1A8X E 4 .   ? 17.052 -1.666  1.239   0.22 16.12 ?  203 A1A8X A H5   1 
HETATM 6653 H  H4   B A1A8X E 4 .   ? 16.112 -3.086  1.019   0.22 16.12 ?  203 A1A8X A H4   1 
HETATM 6654 H  H9   B A1A8X E 4 .   ? 13.082 -1.620  0.177   0.22 16.61 ?  203 A1A8X A H9   1 
HETATM 6655 H  H8   B A1A8X E 4 .   ? 13.524 0.038   0.195   0.22 16.61 ?  203 A1A8X A H8   1 
HETATM 6656 H  H2   B A1A8X E 4 .   ? 13.013 -1.572  2.497   0.22 16.05 ?  203 A1A8X A H2   1 
HETATM 6657 H  H11  B A1A8X E 4 .   ? 13.808 -0.144  7.157   0.22 13.74 ?  203 A1A8X A H11  1 
HETATM 6658 H  H10  B A1A8X E 4 .   ? 13.398 1.061   2.005   0.22 15.99 ?  203 A1A8X A H10  1 
HETATM 6659 H  H14  B A1A8X E 4 .   ? 15.884 4.071   6.625   0.22 13.53 ?  203 A1A8X A H14  1 
HETATM 6660 H  H3   B A1A8X E 4 .   ? 15.462 -3.016  3.987   0.22 15.30 ?  203 A1A8X A H3   1 
HETATM 6661 CL CL   B CL    F 5 .   ? 15.928 2.729   -0.978  0.22 17.80 ?  204 CL    A CL   1 
HETATM 6662 O  O    . HOH   G 6 .   ? -0.448 -2.950  2.994   1.00 36.39 ?  301 HOH   A O    1 
HETATM 6663 O  O    . HOH   G 6 .   ? 14.767 -4.666  20.557  1.00 41.68 ?  302 HOH   A O    1 
HETATM 6664 O  O    A HOH   G 6 .   ? 4.681  3.932   0.658   0.78 22.76 ?  303 HOH   A O    1 
HETATM 6665 O  O    B HOH   G 6 .   ? 5.162  4.465   0.880   0.22 33.60 ?  304 HOH   A O    1 
HETATM 6666 O  O    . HOH   G 6 .   ? 34.355 -1.864  12.472  1.00 37.99 ?  305 HOH   A O    1 
HETATM 6667 O  O    . HOH   G 6 .   ? 11.019 1.667   12.806  1.00 23.90 ?  306 HOH   A O    1 
HETATM 6668 O  O    . HOH   G 6 .   ? 7.629  -6.377  -6.592  1.00 38.72 ?  307 HOH   A O    1 
HETATM 6669 O  O    . HOH   G 6 .   ? 18.573 -2.410  -16.361 1.00 42.63 ?  308 HOH   A O    1 
HETATM 6670 O  O    . HOH   G 6 .   ? 12.102 0.347   14.856  1.00 34.20 ?  309 HOH   A O    1 
HETATM 6671 O  O    . HOH   G 6 .   ? 15.143 -12.252 18.654  1.00 36.57 ?  310 HOH   A O    1 
HETATM 6672 O  O    . HOH   G 6 .   ? 22.706 12.484  1.651   1.00 14.30 ?  311 HOH   A O    1 
HETATM 6673 O  O    . HOH   G 6 .   ? 28.868 0.464   -9.748  1.00 20.84 ?  312 HOH   A O    1 
HETATM 6674 O  O    . HOH   G 6 .   ? 17.095 -18.037 15.062  1.00 25.41 ?  313 HOH   A O    1 
HETATM 6675 O  O    . HOH   G 6 .   ? 24.061 3.921   -4.762  1.00 24.03 ?  314 HOH   A O    1 
HETATM 6676 O  O    . HOH   G 6 .   ? 19.830 -12.520 -8.931  1.00 25.09 ?  315 HOH   A O    1 
HETATM 6677 O  O    . HOH   G 6 .   ? 26.892 4.160   -0.657  1.00 12.18 ?  316 HOH   A O    1 
HETATM 6678 O  O    . HOH   G 6 .   ? 0.708  -4.283  0.198   1.00 29.13 ?  317 HOH   A O    1 
HETATM 6679 O  O    . HOH   G 6 .   ? 3.596  -9.366  9.805   1.00 28.08 ?  318 HOH   A O    1 
HETATM 6680 O  O    . HOH   G 6 .   ? 42.433 10.572  5.169   1.00 19.50 ?  319 HOH   A O    1 
HETATM 6681 O  O    . HOH   G 6 .   ? 28.243 -6.310  19.598  1.00 40.84 ?  320 HOH   A O    1 
HETATM 6682 O  O    . HOH   G 6 .   ? 14.435 -24.700 11.566  1.00 36.26 ?  321 HOH   A O    1 
HETATM 6683 O  O    . HOH   G 6 .   ? 33.982 -1.065  -8.924  1.00 27.94 ?  322 HOH   A O    1 
HETATM 6684 O  O    . HOH   G 6 .   ? 6.743  -3.259  12.936  1.00 27.98 ?  323 HOH   A O    1 
HETATM 6685 O  O    . HOH   G 6 .   ? 14.740 -13.986 16.687  1.00 23.56 ?  324 HOH   A O    1 
HETATM 6686 O  O    . HOH   G 6 .   ? 36.152 -5.105  -0.572  1.00 28.71 ?  325 HOH   A O    1 
HETATM 6687 O  O    . HOH   G 6 .   ? 30.204 -13.311 -8.573  1.00 23.51 ?  326 HOH   A O    1 
HETATM 6688 O  O    . HOH   G 6 .   ? 16.203 16.647  8.680   1.00 29.22 ?  327 HOH   A O    1 
HETATM 6689 O  O    . HOH   G 6 .   ? 9.462  -12.332 17.228  1.00 57.97 ?  328 HOH   A O    1 
HETATM 6690 O  O    . HOH   G 6 .   ? 26.468 -19.331 -1.803  1.00 13.84 ?  329 HOH   A O    1 
HETATM 6691 O  O    . HOH   G 6 .   ? 14.038 -4.553  -11.856 1.00 31.65 ?  330 HOH   A O    1 
HETATM 6692 O  O    . HOH   G 6 .   ? 11.669 -10.824 -10.129 1.00 41.46 ?  331 HOH   A O    1 
HETATM 6693 O  O    . HOH   G 6 .   ? 31.015 -18.105 7.805   1.00 19.28 ?  332 HOH   A O    1 
HETATM 6694 O  O    B HOH   G 6 .   ? 14.238 7.914   10.193  0.22 21.00 ?  333 HOH   A O    1 
HETATM 6695 O  O    . HOH   G 6 .   ? 15.553 11.897  7.913   1.00 35.46 ?  334 HOH   A O    1 
HETATM 6696 O  O    . HOH   G 6 .   ? 27.873 0.834   -7.139  1.00 13.36 ?  335 HOH   A O    1 
HETATM 6697 O  O    . HOH   G 6 .   ? 28.220 -0.084  -13.397 1.00 35.81 ?  336 HOH   A O    1 
HETATM 6698 O  O    . HOH   G 6 .   ? 27.337 13.762  2.832   1.00 31.37 ?  337 HOH   A O    1 
HETATM 6699 O  O    . HOH   G 6 .   ? 7.944  -12.560 -0.781  1.00 20.68 ?  338 HOH   A O    1 
HETATM 6700 O  O    . HOH   G 6 .   ? 13.987 -4.959  17.530  1.00 24.89 ?  339 HOH   A O    1 
HETATM 6701 O  O    . HOH   G 6 .   ? 18.676 -19.361 13.535  1.00 34.06 ?  340 HOH   A O    1 
HETATM 6702 O  O    . HOH   G 6 .   ? 42.557 4.316   5.328   1.00 31.28 ?  341 HOH   A O    1 
HETATM 6703 O  O    . HOH   G 6 .   ? 18.901 -21.979 7.031   1.00 32.30 ?  342 HOH   A O    1 
HETATM 6704 O  O    . HOH   G 6 .   ? 37.566 2.790   10.175  1.00 28.12 ?  343 HOH   A O    1 
HETATM 6705 O  O    A HOH   G 6 .   ? 6.957  -8.147  11.887  0.78 18.62 ?  344 HOH   A O    1 
HETATM 6706 O  O    . HOH   G 6 .   ? 44.325 7.106   6.362   1.00 25.66 ?  345 HOH   A O    1 
HETATM 6707 O  O    . HOH   G 6 .   ? 38.274 10.086  7.148   1.00 28.81 ?  346 HOH   A O    1 
HETATM 6708 O  O    . HOH   G 6 .   ? 20.576 -19.730 -5.056  1.00 26.36 ?  347 HOH   A O    1 
HETATM 6709 O  O    . HOH   G 6 .   ? -0.659 -8.377  2.168   1.00 42.52 ?  348 HOH   A O    1 
HETATM 6710 O  O    . HOH   G 6 .   ? 15.188 3.967   17.881  1.00 39.50 ?  349 HOH   A O    1 
HETATM 6711 O  O    . HOH   G 6 .   ? 24.539 1.971   -7.004  1.00 18.89 ?  350 HOH   A O    1 
HETATM 6712 O  O    . HOH   G 6 .   ? 39.719 -1.029  -5.226  1.00 19.98 ?  351 HOH   A O    1 
HETATM 6713 O  O    . HOH   G 6 .   ? 31.682 8.257   14.789  1.00 23.84 ?  352 HOH   A O    1 
HETATM 6714 O  O    . HOH   G 6 .   ? 14.464 -0.495  -12.048 1.00 22.38 ?  353 HOH   A O    1 
HETATM 6715 O  O    . HOH   G 6 .   ? 9.153  -10.105 19.428  1.00 37.25 ?  354 HOH   A O    1 
HETATM 6716 O  O    . HOH   G 6 .   ? 22.366 5.348   19.033  1.00 39.90 ?  355 HOH   A O    1 
HETATM 6717 O  O    . HOH   G 6 .   ? 9.877  -21.362 5.733   1.00 17.84 ?  356 HOH   A O    1 
HETATM 6718 O  O    B HOH   G 6 .   ? 22.548 5.508   -2.009  0.22 16.58 ?  357 HOH   A O    1 
HETATM 6719 O  O    . HOH   G 6 .   ? 38.560 4.973   6.934   1.00 15.36 ?  358 HOH   A O    1 
HETATM 6720 O  O    . HOH   G 6 .   ? 26.808 11.410  1.638   1.00 15.77 ?  359 HOH   A O    1 
HETATM 6721 O  O    A HOH   G 6 .   ? 14.627 -3.641  3.122   0.78 14.46 ?  360 HOH   A O    1 
HETATM 6722 O  O    B HOH   G 6 .   ? 21.222 -2.516  -1.903  0.22 22.46 ?  361 HOH   A O    1 
HETATM 6723 O  O    . HOH   G 6 .   ? 22.231 -19.233 11.391  1.00 34.68 ?  362 HOH   A O    1 
HETATM 6724 O  O    . HOH   G 6 .   ? 14.318 -21.193 -4.220  1.00 28.82 ?  363 HOH   A O    1 
HETATM 6725 O  O    . HOH   G 6 .   ? 13.509 -15.225 -7.405  1.00 25.28 ?  364 HOH   A O    1 
HETATM 6726 O  O    . HOH   G 6 .   ? 13.178 -1.453  -6.571  1.00 15.59 ?  365 HOH   A O    1 
HETATM 6727 O  O    . HOH   G 6 .   ? 37.349 11.951  4.882   1.00 32.37 ?  366 HOH   A O    1 
HETATM 6728 O  O    . HOH   G 6 .   ? 17.110 -17.770 -5.014  1.00 25.55 ?  367 HOH   A O    1 
HETATM 6729 O  O    . HOH   G 6 .   ? 23.993 -2.095  -2.080  1.00 10.30 ?  368 HOH   A O    1 
HETATM 6730 O  O    A HOH   G 6 .   ? 14.274 0.587   6.825   0.78 18.41 ?  369 HOH   A O    1 
HETATM 6731 O  O    . HOH   G 6 .   ? 35.783 -12.664 6.804   1.00 15.67 ?  370 HOH   A O    1 
HETATM 6732 O  O    . HOH   G 6 .   ? 31.729 -9.361  -6.702  1.00 21.92 ?  371 HOH   A O    1 
HETATM 6733 O  O    . HOH   G 6 .   ? 16.521 -22.055 0.935   1.00 26.91 ?  372 HOH   A O    1 
HETATM 6734 O  O    A HOH   G 6 .   ? 17.483 -1.700  0.461   0.78 18.03 ?  373 HOH   A O    1 
HETATM 6735 O  O    B HOH   G 6 .   ? 15.216 7.963   4.611   0.22 22.61 ?  374 HOH   A O    1 
HETATM 6736 O  O    . HOH   G 6 .   ? 30.803 3.090   8.251   1.00 11.51 ?  375 HOH   A O    1 
HETATM 6737 O  O    . HOH   G 6 .   ? 21.881 -21.891 8.445   1.00 28.84 ?  376 HOH   A O    1 
HETATM 6738 O  O    . HOH   G 6 .   ? 33.649 -7.143  4.258   1.00 16.25 ?  377 HOH   A O    1 
HETATM 6739 O  O    . HOH   G 6 .   ? 31.060 -13.940 -2.478  1.00 13.45 ?  378 HOH   A O    1 
HETATM 6740 O  O    . HOH   G 6 .   ? 18.618 9.445   9.055   1.00 20.42 ?  379 HOH   A O    1 
HETATM 6741 O  O    . HOH   G 6 .   ? 43.934 8.448   -3.145  1.00 23.95 ?  380 HOH   A O    1 
HETATM 6742 O  O    . HOH   G 6 .   ? 24.280 -7.787  14.446  1.00 16.52 ?  381 HOH   A O    1 
HETATM 6743 O  O    . HOH   G 6 .   ? 37.266 -2.851  9.663   1.00 38.93 ?  382 HOH   A O    1 
HETATM 6744 O  O    . HOH   G 6 .   ? 31.660 -7.281  -9.898  1.00 20.63 ?  383 HOH   A O    1 
HETATM 6745 O  O    . HOH   G 6 .   ? 27.510 -10.627 14.032  1.00 16.63 ?  384 HOH   A O    1 
HETATM 6746 O  O    . HOH   G 6 .   ? 25.639 -0.792  -7.351  1.00 14.72 ?  385 HOH   A O    1 
HETATM 6747 O  O    . HOH   G 6 .   ? 24.354 3.583   -1.794  1.00 13.99 ?  386 HOH   A O    1 
HETATM 6748 O  O    . HOH   G 6 .   ? 17.001 -19.267 4.916   1.00 14.47 ?  387 HOH   A O    1 
HETATM 6749 O  O    T HOH   G 6 .   ? 15.398 -0.408  2.409   0.30 12.28 ?  388 HOH   A O    1 
HETATM 6750 O  O    . HOH   G 6 .   ? 11.693 -10.709 17.036  1.00 22.86 ?  389 HOH   A O    1 
HETATM 6751 O  O    A HOH   G 6 .   ? 21.229 -2.384  -2.039  0.78 14.73 ?  390 HOH   A O    1 
HETATM 6752 O  O    . HOH   G 6 .   ? 32.783 -9.219  5.942   1.00 19.89 ?  391 HOH   A O    1 
HETATM 6753 O  O    . HOH   G 6 .   ? 22.635 -11.948 21.786  1.00 43.69 ?  392 HOH   A O    1 
HETATM 6754 O  O    . HOH   G 6 .   ? 21.285 3.055   -0.283  1.00 13.76 ?  393 HOH   A O    1 
HETATM 6755 O  O    . HOH   G 6 .   ? 21.779 -13.797 -8.095  1.00 38.68 ?  394 HOH   A O    1 
HETATM 6756 O  O    . HOH   G 6 .   ? 43.359 7.859   2.664   1.00 23.30 ?  395 HOH   A O    1 
HETATM 6757 O  O    . HOH   G 6 .   ? 24.720 -17.527 12.703  1.00 23.33 ?  396 HOH   A O    1 
HETATM 6758 O  O    . HOH   G 6 .   ? 21.257 10.348  15.051  1.00 33.30 ?  397 HOH   A O    1 
HETATM 6759 O  O    . HOH   G 6 .   ? 27.273 -5.959  -13.972 1.00 36.63 ?  398 HOH   A O    1 
HETATM 6760 O  O    A HOH   G 6 .   ? 11.057 -0.366  1.964   0.48 19.80 ?  399 HOH   A O    1 
HETATM 6761 O  O    . HOH   G 6 .   ? 15.189 -21.559 14.244  1.00 17.29 ?  400 HOH   A O    1 
HETATM 6762 O  O    . HOH   G 6 .   ? 37.574 -2.017  5.751   1.00 25.84 ?  401 HOH   A O    1 
HETATM 6763 O  O    B HOH   G 6 .   ? 6.143  4.038   3.205   0.22 21.79 ?  402 HOH   A O    1 
HETATM 6764 O  O    A HOH   G 6 .   ? 15.796 -0.932  5.292   0.78 18.92 ?  403 HOH   A O    1 
HETATM 6765 O  O    . HOH   G 6 .   ? 30.746 1.883   16.661  1.00 19.87 ?  404 HOH   A O    1 
HETATM 6766 O  O    . HOH   G 6 .   ? 30.097 -10.097 12.947  1.00 21.62 ?  405 HOH   A O    1 
HETATM 6767 O  O    . HOH   G 6 .   ? 23.452 11.365  4.088   1.00 11.64 ?  406 HOH   A O    1 
HETATM 6768 O  O    . HOH   G 6 .   ? 15.079 -8.090  -9.640  1.00 21.43 ?  407 HOH   A O    1 
HETATM 6769 O  O    . HOH   G 6 .   ? 23.873 -15.712 -9.123  1.00 34.32 ?  408 HOH   A O    1 
HETATM 6770 O  O    B HOH   G 6 .   ? 10.643 6.563   11.117  0.22 22.35 ?  409 HOH   A O    1 
HETATM 6771 O  O    A HOH   G 6 .   ? 20.071 4.555   -7.532  0.78 17.01 ?  410 HOH   A O    1 
HETATM 6772 O  O    . HOH   G 6 .   ? 27.391 2.296   18.710  1.00 28.49 ?  411 HOH   A O    1 
HETATM 6773 O  O    . HOH   G 6 .   ? 30.945 6.224   -12.307 1.00 30.44 ?  412 HOH   A O    1 
HETATM 6774 O  O    . HOH   G 6 .   ? 14.041 -23.049 7.440   1.00 17.43 ?  413 HOH   A O    1 
HETATM 6775 O  O    . HOH   G 6 .   ? 20.543 -20.018 2.780   1.00 17.55 ?  414 HOH   A O    1 
HETATM 6776 O  O    . HOH   G 6 .   ? 28.530 -10.631 -14.015 1.00 40.35 ?  415 HOH   A O    1 
HETATM 6777 O  O    . HOH   G 6 .   ? 8.394  -21.401 4.078   1.00 44.16 ?  416 HOH   A O    1 
HETATM 6778 O  O    . HOH   G 6 .   ? 23.909 -20.281 -1.367  1.00 15.79 ?  417 HOH   A O    1 
HETATM 6779 O  O    B HOH   G 6 .   ? 10.888 0.473   2.545   0.22 22.54 ?  418 HOH   A O    1 
HETATM 6780 O  O    . HOH   G 6 .   ? 41.583 1.555   4.920   1.00 38.86 ?  419 HOH   A O    1 
HETATM 6781 O  O    . HOH   G 6 .   ? 38.084 -1.344  -2.007  1.00 18.45 ?  420 HOH   A O    1 
HETATM 6782 O  O    . HOH   G 6 .   ? 30.361 -12.934 13.482  1.00 19.66 ?  421 HOH   A O    1 
HETATM 6783 O  O    B HOH   G 6 .   ? 18.657 -1.532  -1.195  0.22 18.17 ?  422 HOH   A O    1 
HETATM 6784 O  O    . HOH   G 6 .   ? -1.535 -4.884  7.675   1.00 40.20 ?  423 HOH   A O    1 
HETATM 6785 O  O    . HOH   G 6 .   ? 40.897 -8.256  -6.797  1.00 35.48 ?  424 HOH   A O    1 
HETATM 6786 O  O    . HOH   G 6 .   ? 15.821 2.107   24.803  1.00 47.36 ?  425 HOH   A O    1 
HETATM 6787 O  O    . HOH   G 6 .   ? 10.348 -13.690 -1.604  1.00 16.15 ?  426 HOH   A O    1 
HETATM 6788 O  O    . HOH   G 6 .   ? 32.596 -4.298  -9.939  1.00 27.88 ?  427 HOH   A O    1 
HETATM 6789 O  O    B HOH   G 6 .   ? 11.899 -1.837  -2.800  0.22 12.40 ?  428 HOH   A O    1 
HETATM 6790 O  O    . HOH   G 6 .   ? 36.734 -4.940  5.369   1.00 24.01 ?  429 HOH   A O    1 
HETATM 6791 O  O    . HOH   G 6 .   ? 35.015 -5.219  -3.129  1.00 17.62 ?  430 HOH   A O    1 
HETATM 6792 O  O    . HOH   G 6 .   ? 32.556 -10.661 3.153   1.00 30.35 ?  431 HOH   A O    1 
HETATM 6793 O  O    . HOH   G 6 .   ? 44.926 -0.596  2.951   1.00 41.38 ?  432 HOH   A O    1 
HETATM 6794 O  O    A HOH   G 6 .   ? 6.473  -5.590  11.217  0.78 18.22 ?  433 HOH   A O    1 
HETATM 6795 O  O    . HOH   G 6 .   ? 5.269  2.839   5.112   1.00 31.97 ?  434 HOH   A O    1 
HETATM 6796 O  O    A HOH   G 6 .   ? 18.942 -0.656  -1.610  0.78 12.56 ?  435 HOH   A O    1 
HETATM 6797 O  O    . HOH   G 6 .   ? 16.232 -14.233 20.225  1.00 46.70 ?  436 HOH   A O    1 
HETATM 6798 O  O    . HOH   G 6 .   ? 27.151 -3.226  19.242  1.00 34.96 ?  437 HOH   A O    1 
HETATM 6799 O  O    . HOH   G 6 .   ? 22.662 8.154   18.380  1.00 44.58 ?  438 HOH   A O    1 
HETATM 6800 O  O    A HOH   G 6 .   ? 16.010 6.968   3.012   0.78 14.35 ?  439 HOH   A O    1 
HETATM 6801 O  O    . HOH   G 6 .   ? 18.825 1.981   -0.662  1.00 13.68 ?  440 HOH   A O    1 
HETATM 6802 O  O    . HOH   G 6 .   ? 23.602 -8.019  17.084  1.00 21.54 ?  441 HOH   A O    1 
HETATM 6803 O  O    . HOH   G 6 .   ? 37.693 -8.823  -3.525  1.00 24.76 ?  442 HOH   A O    1 
HETATM 6804 O  O    . HOH   G 6 .   ? 21.289 -9.239  21.361  1.00 46.91 ?  443 HOH   A O    1 
HETATM 6805 O  O    . HOH   G 6 .   ? 23.324 -20.926 1.337   1.00 17.96 ?  444 HOH   A O    1 
HETATM 6806 O  O    . HOH   G 6 .   ? 10.393 -22.165 -1.152  1.00 46.14 ?  445 HOH   A O    1 
HETATM 6807 O  O    . HOH   G 6 .   ? 20.567 -17.818 24.812  1.00 48.19 ?  446 HOH   A O    1 
HETATM 6808 O  O    . HOH   G 6 .   ? 19.560 -10.992 24.083  1.00 63.99 ?  447 HOH   A O    1 
HETATM 6809 O  O    B HOH   G 6 .   ? 13.303 2.463   0.482   0.22 22.99 ?  448 HOH   A O    1 
HETATM 6810 O  O    A HOH   G 6 .   ? 16.242 2.961   -1.420  0.78 15.13 ?  449 HOH   A O    1 
HETATM 6811 O  O    . HOH   G 6 .   ? 9.443  -16.239 -1.903  1.00 38.09 ?  450 HOH   A O    1 
HETATM 6812 O  O    . HOH   G 6 .   ? 34.406 -8.073  -0.583  1.00 27.68 ?  451 HOH   A O    1 
HETATM 6813 O  O    . HOH   G 6 .   ? 23.181 7.578   -3.180  1.00 28.99 ?  452 HOH   A O    1 
HETATM 6814 O  O    . HOH   G 6 .   ? 18.406 -16.063 16.420  1.00 35.69 ?  453 HOH   A O    1 
HETATM 6815 O  O    . HOH   G 6 .   ? 18.467 4.926   -15.125 1.00 42.34 ?  454 HOH   A O    1 
HETATM 6816 O  O    . HOH   G 6 .   ? 30.585 14.775  2.760   1.00 18.09 ?  455 HOH   A O    1 
HETATM 6817 O  O    . HOH   G 6 .   ? 31.321 -12.770 -0.016  1.00 19.04 ?  456 HOH   A O    1 
HETATM 6818 O  O    A HOH   G 6 .   ? 14.020 -0.325  3.487   0.48 30.62 ?  457 HOH   A O    1 
HETATM 6819 O  O    . HOH   G 6 .   ? 21.572 -14.731 18.019  1.00 50.83 ?  458 HOH   A O    1 
HETATM 6820 O  O    . HOH   G 6 .   ? 29.848 -16.072 10.687  1.00 34.14 ?  459 HOH   A O    1 
HETATM 6821 O  O    . HOH   G 6 .   ? 27.733 7.096   -6.383  1.00 33.51 ?  460 HOH   A O    1 
HETATM 6822 O  O    . HOH   G 6 .   ? 25.391 8.237   -4.820  1.00 27.01 ?  461 HOH   A O    1 
HETATM 6823 O  O    . HOH   G 6 .   ? 32.513 -15.894 10.811  1.00 33.30 ?  462 HOH   A O    1 
HETATM 6824 O  O    . HOH   G 6 .   ? 29.712 -1.966  -12.736 1.00 43.03 ?  463 HOH   A O    1 
HETATM 6825 O  O    . HOH   G 6 .   ? 24.861 5.681   20.765  1.00 48.91 ?  464 HOH   A O    1 
HETATM 6826 O  O    . HOH   G 6 .   ? 23.137 -22.297 -3.378  1.00 34.43 ?  465 HOH   A O    1 
HETATM 6827 O  O    . HOH   G 6 .   ? 19.828 -17.303 -5.063  1.00 23.12 ?  466 HOH   A O    1 
HETATM 6828 O  O    . HOH   G 6 .   ? 24.623 14.568  7.822   1.00 33.54 ?  467 HOH   A O    1 
HETATM 6829 O  O    . HOH   G 6 .   ? 26.852 11.645  -1.238  1.00 29.56 ?  468 HOH   A O    1 
HETATM 6830 O  O    . HOH   G 6 .   ? 15.705 -21.475 3.666   1.00 23.54 ?  469 HOH   A O    1 
HETATM 6831 O  O    . HOH   G 6 .   ? 27.519 -11.328 16.531  1.00 35.53 ?  470 HOH   A O    1 
HETATM 6832 O  O    . HOH   G 6 .   ? 39.629 -7.018  -3.523  1.00 44.29 ?  471 HOH   A O    1 
HETATM 6833 O  O    . HOH   G 6 .   ? 18.766 10.860  11.372  1.00 31.49 ?  472 HOH   A O    1 
HETATM 6834 O  O    A HOH   G 6 .   ? 21.941 5.279   -5.825  0.78 28.48 ?  473 HOH   A O    1 
HETATM 6835 O  O    B HOH   G 6 .   ? 8.960  4.435   2.491   0.22 24.53 ?  474 HOH   A O    1 
HETATM 6836 O  O    . HOH   G 6 .   ? 23.506 13.713  5.507   1.00 18.03 ?  475 HOH   A O    1 
HETATM 6837 O  O    . HOH   G 6 .   ? 25.768 10.772  -3.719  1.00 24.43 ?  476 HOH   A O    1 
HETATM 6838 O  O    B HOH   G 6 .   ? 16.453 7.958   8.852   0.22 17.24 ?  477 HOH   A O    1 
HETATM 6839 O  O    . HOH   G 6 .   ? 12.271 1.630   17.378  1.00 40.03 ?  478 HOH   A O    1 
HETATM 6840 O  O    . HOH   G 6 .   ? 11.007 -14.985 -6.072  1.00 32.63 ?  479 HOH   A O    1 
HETATM 6841 O  O    . HOH   G 6 .   ? 12.018 -13.429 16.431  1.00 49.36 ?  480 HOH   A O    1 
HETATM 6842 O  O    . HOH   G 6 .   ? 18.058 -16.218 -8.797  1.00 39.94 ?  481 HOH   A O    1 
HETATM 6843 O  O    . HOH   G 6 .   ? 28.873 8.997   17.442  1.00 34.41 ?  482 HOH   A O    1 
HETATM 6844 O  O    . HOH   G 6 .   ? 13.941 -10.328 -10.861 1.00 32.52 ?  483 HOH   A O    1 
HETATM 6845 O  O    . HOH   G 6 .   ? 35.243 7.447   12.176  1.00 43.29 ?  484 HOH   A O    1 
HETATM 6846 O  O    . HOH   G 6 .   ? 15.617 -17.129 -6.955  1.00 30.73 ?  485 HOH   A O    1 
HETATM 6847 O  O    . HOH   G 6 .   ? 17.386 -18.767 19.844  1.00 50.55 ?  486 HOH   A O    1 
HETATM 6848 O  O    . HOH   G 6 .   ? 40.983 -3.972  -0.367  1.00 35.39 ?  487 HOH   A O    1 
HETATM 6849 O  O    . HOH   G 6 .   ? 16.782 -20.537 16.167  1.00 27.93 ?  488 HOH   A O    1 
HETATM 6850 O  O    . HOH   G 6 .   ? 20.458 -16.102 -7.373  1.00 27.73 ?  489 HOH   A O    1 
HETATM 6851 O  O    . HOH   G 6 .   ? 30.861 0.681   19.170  1.00 38.21 ?  490 HOH   A O    1 
HETATM 6852 O  O    . HOH   G 6 .   ? 23.096 11.809  -4.043  1.00 18.82 ?  491 HOH   A O    1 
HETATM 6853 O  O    . HOH   G 6 .   ? 41.701 9.284   -4.118  1.00 29.23 ?  492 HOH   A O    1 
HETATM 6854 O  O    . HOH   G 6 .   ? 44.532 10.447  -1.605  1.00 30.44 ?  493 HOH   A O    1 
HETATM 6855 O  O    . HOH   G 6 .   ? 23.275 -12.870 19.353  1.00 43.81 ?  494 HOH   A O    1 
HETATM 6856 O  O    . HOH   G 6 .   ? 18.396 -23.170 1.924   1.00 42.95 ?  495 HOH   A O    1 
HETATM 6857 O  O    B HOH   G 6 .   ? 10.991 0.206   -0.651  0.22 23.84 ?  496 HOH   A O    1 
HETATM 6858 O  O    . HOH   G 6 .   ? 15.888 -6.889  -11.792 1.00 42.64 ?  497 HOH   A O    1 
HETATM 6859 O  O    . HOH   G 6 .   ? 39.162 2.427   7.529   1.00 31.81 ?  498 HOH   A O    1 
HETATM 6860 O  O    . HOH   G 6 .   ? 28.606 -7.898  -15.285 1.00 45.46 ?  499 HOH   A O    1 
HETATM 6861 O  O    . HOH   G 6 .   ? 31.394 -0.560  -10.577 1.00 29.17 ?  500 HOH   A O    1 
HETATM 6862 O  O    . HOH   G 6 .   ? 40.492 -0.276  -7.844  1.00 32.49 ?  501 HOH   A O    1 
HETATM 6863 O  O    . HOH   G 6 .   ? 28.572 -4.666  -12.314 1.00 35.47 ?  502 HOH   A O    1 
HETATM 6864 O  O    . HOH   G 6 .   ? 13.986 -25.266 8.927   1.00 32.71 ?  503 HOH   A O    1 
HETATM 6865 O  O    . HOH   G 6 .   ? 19.998 -22.369 4.197   1.00 27.54 ?  504 HOH   A O    1 
HETATM 6866 O  O    . HOH   G 6 .   ? 16.178 -23.371 5.715   1.00 29.86 ?  505 HOH   A O    1 
HETATM 6867 O  O    . HOH   G 6 .   ? 30.716 -5.813  -11.903 1.00 46.33 ?  506 HOH   A O    1 
HETATM 6868 O  O    . HOH   G 6 .   ? 37.379 -6.647  7.515   1.00 25.05 ?  507 HOH   A O    1 
HETATM 6869 O  O    . HOH   G 6 .   ? 30.751 5.808   -14.713 1.00 35.85 ?  508 HOH   A O    1 
HETATM 6870 O  O    B HOH   G 6 .   ? 5.906  6.923   1.248   0.22 25.17 ?  509 HOH   A O    1 
HETATM 6871 O  O    . HOH   G 6 .   ? 23.082 -23.754 1.617   1.00 31.47 ?  510 HOH   A O    1 
HETATM 6872 O  O    . HOH   G 6 .   ? 39.537 0.047   6.536   1.00 28.30 ?  511 HOH   A O    1 
HETATM 6873 O  O    . HOH   G 6 .   ? 28.972 14.379  0.852   1.00 47.16 ?  512 HOH   A O    1 
HETATM 6874 O  O    . HOH   G 6 .   ? 8.030  -3.086  -5.723  1.00 42.42 ?  513 HOH   A O    1 
HETATM 6875 O  O    . HOH   G 6 .   ? 38.083 13.909  6.737   1.00 49.71 ?  514 HOH   A O    1 
HETATM 6876 O  O    . HOH   G 6 .   ? 17.364 -6.624  -14.157 1.00 38.43 ?  515 HOH   A O    1 
HETATM 6877 O  O    . HOH   G 6 .   ? 21.989 -24.014 4.458   1.00 25.87 ?  516 HOH   A O    1 
HETATM 6878 O  O    . HOH   G 6 .   ? 36.467 -6.560  10.144  1.00 42.47 ?  517 HOH   A O    1 
HETATM 6879 O  O    T HOH   G 6 .   ? 11.901 -2.135  -3.625  0.30 11.50 ?  518 HOH   A O    1 
HETATM 6880 O  O    A HOH   G 6 .   ? 14.846 8.664   4.913   0.78 41.27 ?  519 HOH   A O    1 
HETATM 6881 O  O    . HOH   G 6 .   ? 24.019 9.016   -7.250  1.00 35.14 ?  520 HOH   A O    1 
HETATM 6882 O  O    B HOH   G 6 .   ? 8.480  7.411   1.989   0.22 26.77 ?  521 HOH   A O    1 
HETATM 6883 O  O    B HOH   G 6 .   ? 5.865  6.871   4.639   0.22 19.78 ?  522 HOH   A O    1 
HETATM 6884 O  O    . HOH   G 6 .   ? 16.434 -21.103 18.778  1.00 36.59 ?  523 HOH   A O    1 
HETATM 6885 O  O    . HOH   G 6 .   ? 15.847 -12.244 27.496  1.00 43.67 ?  524 HOH   A O    1 
HETATM 6886 O  O    . HOH   G 6 .   ? 14.703 -22.821 19.859  1.00 35.88 ?  525 HOH   A O    1 
HETATM 6887 O  O    . HOH   H 6 .   ? 29.822 -22.414 5.483   1.00 20.04 ?  201 HOH   B O    1 
HETATM 6888 O  O    . HOH   H 6 .   ? 41.820 -35.954 -17.271 1.00 30.91 ?  202 HOH   B O    1 
HETATM 6889 O  O    . HOH   H 6 .   ? 49.302 -22.694 -19.771 1.00 45.92 ?  203 HOH   B O    1 
HETATM 6890 O  O    . HOH   H 6 .   ? 48.144 -6.882  15.511  1.00 32.00 ?  204 HOH   B O    1 
HETATM 6891 O  O    . HOH   H 6 .   ? 59.172 -18.734 6.745   1.00 36.97 ?  205 HOH   B O    1 
HETATM 6892 O  O    . HOH   H 6 .   ? 37.980 -39.439 -0.172  1.00 42.05 ?  206 HOH   B O    1 
HETATM 6893 O  O    . HOH   H 6 .   ? 41.374 -7.760  5.475   1.00 38.87 ?  207 HOH   B O    1 
HETATM 6894 O  O    . HOH   H 6 .   ? 27.730 -29.201 -1.848  1.00 35.60 ?  208 HOH   B O    1 
HETATM 6895 O  O    . HOH   H 6 .   ? 27.806 -41.811 -15.176 1.00 35.61 ?  209 HOH   B O    1 
HETATM 6896 O  O    . HOH   H 6 .   ? 52.897 -13.467 -20.348 1.00 32.85 ?  210 HOH   B O    1 
HETATM 6897 O  O    . HOH   H 6 .   ? 55.435 -16.568 -14.417 1.00 33.87 ?  211 HOH   B O    1 
HETATM 6898 O  O    . HOH   H 6 .   ? 58.202 -12.924 8.370   1.00 32.12 ?  212 HOH   B O    1 
HETATM 6899 O  O    . HOH   H 6 .   ? 57.126 -26.874 -7.667  1.00 39.10 ?  213 HOH   B O    1 
HETATM 6900 O  O    . HOH   H 6 .   ? 56.369 -19.713 7.175   1.00 31.12 ?  214 HOH   B O    1 
HETATM 6901 O  O    . HOH   H 6 .   ? 50.257 -3.370  7.126   1.00 36.59 ?  215 HOH   B O    1 
HETATM 6902 O  O    . HOH   H 6 .   ? 30.201 -41.025 -8.158  1.00 16.45 ?  216 HOH   B O    1 
HETATM 6903 O  O    . HOH   H 6 .   ? 54.461 -9.363  -8.814  1.00 19.88 ?  217 HOH   B O    1 
HETATM 6904 O  O    . HOH   H 6 .   ? 50.762 -6.124  0.145   1.00 26.12 ?  218 HOH   B O    1 
HETATM 6905 O  O    . HOH   H 6 .   ? 47.397 -7.351  -3.939  1.00 38.47 ?  219 HOH   B O    1 
HETATM 6906 O  O    . HOH   H 6 .   ? 44.437 -7.220  2.037   1.00 34.72 ?  220 HOH   B O    1 
HETATM 6907 O  O    . HOH   H 6 .   ? 29.895 -26.293 3.983   1.00 27.91 ?  221 HOH   B O    1 
HETATM 6908 O  O    . HOH   H 6 .   ? 57.744 -24.471 5.053   1.00 35.91 ?  222 HOH   B O    1 
HETATM 6909 O  O    . HOH   H 6 .   ? 29.836 -34.223 -0.441  1.00 34.61 ?  223 HOH   B O    1 
HETATM 6910 O  O    . HOH   H 6 .   ? 57.427 -16.270 -12.200 1.00 18.69 ?  224 HOH   B O    1 
HETATM 6911 O  O    . HOH   H 6 .   ? 34.528 -36.381 -7.231  1.00 18.39 ?  225 HOH   B O    1 
HETATM 6912 O  O    . HOH   H 6 .   ? 37.064 -19.795 -18.126 1.00 36.92 ?  226 HOH   B O    1 
HETATM 6913 O  O    . HOH   H 6 .   ? 41.508 -39.163 -14.923 1.00 22.23 ?  227 HOH   B O    1 
HETATM 6914 O  O    . HOH   H 6 .   ? 45.148 -34.980 6.855   1.00 40.96 ?  228 HOH   B O    1 
HETATM 6915 O  O    . HOH   H 6 .   ? 48.575 -36.504 -15.528 1.00 44.16 ?  229 HOH   B O    1 
HETATM 6916 O  O    . HOH   H 6 .   ? 40.664 -16.047 14.076  1.00 24.36 ?  230 HOH   B O    1 
HETATM 6917 O  O    . HOH   H 6 .   ? 30.894 -28.757 4.249   1.00 25.37 ?  231 HOH   B O    1 
HETATM 6918 O  O    . HOH   H 6 .   ? 39.322 -10.879 6.077   1.00 26.53 ?  232 HOH   B O    1 
HETATM 6919 O  O    . HOH   H 6 .   ? 56.689 -30.805 -7.783  1.00 34.08 ?  233 HOH   B O    1 
HETATM 6920 O  O    . HOH   H 6 .   ? 32.801 -43.782 -11.392 1.00 19.55 ?  234 HOH   B O    1 
HETATM 6921 O  O    . HOH   H 6 .   ? 51.688 -6.460  4.361   1.00 19.61 ?  235 HOH   B O    1 
HETATM 6922 O  O    . HOH   H 6 .   ? 41.381 -9.610  13.038  1.00 22.38 ?  236 HOH   B O    1 
HETATM 6923 O  O    . HOH   H 6 .   ? 35.926 -43.266 -8.548  1.00 32.05 ?  237 HOH   B O    1 
HETATM 6924 O  O    . HOH   H 6 .   ? 35.079 -7.994  -3.070  1.00 17.93 ?  238 HOH   B O    1 
HETATM 6925 O  O    . HOH   H 6 .   ? 50.725 -12.967 -0.529  1.00 11.70 ?  239 HOH   B O    1 
HETATM 6926 O  O    . HOH   H 6 .   ? 44.496 -27.740 -0.752  1.00 22.26 ?  240 HOH   B O    1 
HETATM 6927 O  O    . HOH   H 6 .   ? 28.376 -19.700 -13.127 1.00 23.25 ?  241 HOH   B O    1 
HETATM 6928 O  O    . HOH   H 6 .   ? 46.414 -1.582  13.275  1.00 30.12 ?  242 HOH   B O    1 
HETATM 6929 O  O    . HOH   H 6 .   ? 43.165 -32.395 -17.069 1.00 22.76 ?  243 HOH   B O    1 
HETATM 6930 O  O    . HOH   H 6 .   ? 25.468 -25.968 -1.348  1.00 32.29 ?  244 HOH   B O    1 
HETATM 6931 O  O    . HOH   H 6 .   ? 42.565 -25.365 2.627   1.00 15.26 ?  245 HOH   B O    1 
HETATM 6932 O  O    . HOH   H 6 .   ? 39.491 -11.118 0.311   1.00 16.16 ?  246 HOH   B O    1 
HETATM 6933 O  O    . HOH   H 6 .   ? 42.629 -22.864 3.818   1.00 11.55 ?  247 HOH   B O    1 
HETATM 6934 O  O    . HOH   H 6 .   ? 38.950 -11.973 12.309  1.00 34.48 ?  248 HOH   B O    1 
HETATM 6935 O  O    . HOH   H 6 .   ? 31.773 -17.949 -14.502 1.00 31.93 ?  249 HOH   B O    1 
HETATM 6936 O  O    . HOH   H 6 .   ? 57.606 -24.386 -3.856  1.00 21.15 ?  250 HOH   B O    1 
HETATM 6937 O  O    . HOH   H 6 .   ? 44.958 -43.554 -10.508 1.00 27.28 ?  251 HOH   B O    1 
HETATM 6938 O  O    . HOH   H 6 .   ? 34.278 -18.473 11.415  1.00 25.61 ?  252 HOH   B O    1 
HETATM 6939 O  O    . HOH   H 6 .   ? 48.013 -24.449 -17.794 1.00 30.27 ?  253 HOH   B O    1 
HETATM 6940 O  O    . HOH   H 6 .   ? 40.298 -12.760 -11.546 1.00 14.86 ?  254 HOH   B O    1 
HETATM 6941 O  O    . HOH   H 6 .   ? 34.935 -24.625 13.843  1.00 32.10 ?  255 HOH   B O    1 
HETATM 6942 O  O    . HOH   H 6 .   ? 43.077 -43.252 -8.263  1.00 29.08 ?  256 HOH   B O    1 
HETATM 6943 O  O    . HOH   H 6 .   ? 38.455 -11.034 -2.285  1.00 18.79 ?  257 HOH   B O    1 
HETATM 6944 O  O    . HOH   H 6 .   ? 58.177 -10.647 -4.101  1.00 20.53 ?  258 HOH   B O    1 
HETATM 6945 O  O    . HOH   H 6 .   ? 51.556 -13.838 11.013  1.00 27.68 ?  259 HOH   B O    1 
HETATM 6946 O  O    . HOH   H 6 .   ? 29.700 -25.232 -10.830 1.00 16.22 ?  260 HOH   B O    1 
HETATM 6947 O  O    . HOH   H 6 .   ? 30.856 -15.736 2.638   1.00 13.28 ?  261 HOH   B O    1 
HETATM 6948 O  O    . HOH   H 6 .   ? 41.861 -23.493 9.254   1.00 17.00 ?  262 HOH   B O    1 
HETATM 6949 O  O    . HOH   H 6 .   ? 33.509 -17.002 8.015   1.00 18.86 ?  263 HOH   B O    1 
HETATM 6950 O  O    . HOH   H 6 .   ? 27.123 -31.828 -9.981  1.00 20.25 ?  264 HOH   B O    1 
HETATM 6951 O  O    . HOH   H 6 .   ? 57.491 -9.229  1.382   1.00 19.52 ?  265 HOH   B O    1 
HETATM 6952 O  O    . HOH   H 6 .   ? 50.962 -39.949 -8.304  1.00 34.19 ?  266 HOH   B O    1 
HETATM 6953 O  O    . HOH   H 6 .   ? 43.330 -15.787 -12.187 1.00 13.89 ?  267 HOH   B O    1 
HETATM 6954 O  O    . HOH   H 6 .   ? 57.151 -12.128 12.257  1.00 38.36 ?  268 HOH   B O    1 
HETATM 6955 O  O    . HOH   H 6 .   ? 28.459 -30.861 -14.719 1.00 27.94 ?  269 HOH   B O    1 
HETATM 6956 O  O    . HOH   H 6 .   ? 48.002 -22.754 5.820   1.00 17.07 ?  270 HOH   B O    1 
HETATM 6957 O  O    . HOH   H 6 .   ? 49.318 -28.695 -6.914  1.00 15.27 ?  271 HOH   B O    1 
HETATM 6958 O  O    . HOH   H 6 .   ? 56.141 -23.489 -14.791 1.00 26.91 ?  272 HOH   B O    1 
HETATM 6959 O  O    . HOH   H 6 .   ? 42.355 -9.892  9.315   1.00 20.22 ?  273 HOH   B O    1 
HETATM 6960 O  O    . HOH   H 6 .   ? 28.260 -34.368 -9.454  1.00 18.19 ?  274 HOH   B O    1 
HETATM 6961 O  O    . HOH   H 6 .   ? 56.959 -8.646  8.398   1.00 18.70 ?  275 HOH   B O    1 
HETATM 6962 O  O    . HOH   H 6 .   ? 49.797 -0.473  10.186  1.00 32.07 ?  276 HOH   B O    1 
HETATM 6963 O  O    . HOH   H 6 .   ? 42.383 -34.711 3.752   1.00 26.06 ?  277 HOH   B O    1 
HETATM 6964 O  O    . HOH   H 6 .   ? 46.603 -31.264 -4.796  1.00 23.66 ?  278 HOH   B O    1 
HETATM 6965 O  O    . HOH   H 6 .   ? 48.406 -25.039 3.082   1.00 13.02 ?  279 HOH   B O    1 
HETATM 6966 O  O    . HOH   H 6 .   ? 30.573 -42.245 -10.610 1.00 28.88 ?  280 HOH   B O    1 
HETATM 6967 O  O    . HOH   H 6 .   ? 27.927 -22.898 -7.995  1.00 17.49 ?  281 HOH   B O    1 
HETATM 6968 O  O    . HOH   H 6 .   ? 27.571 -26.738 -15.669 1.00 33.18 ?  282 HOH   B O    1 
HETATM 6969 O  O    . HOH   H 6 .   ? 37.399 -35.659 7.247   1.00 32.87 ?  283 HOH   B O    1 
HETATM 6970 O  O    . HOH   H 6 .   ? 34.925 -33.386 -19.236 1.00 34.98 ?  284 HOH   B O    1 
HETATM 6971 O  O    . HOH   H 6 .   ? 46.850 -29.521 9.825   1.00 30.81 ?  285 HOH   B O    1 
HETATM 6972 O  O    . HOH   H 6 .   ? 48.709 -20.004 5.894   1.00 14.00 ?  286 HOH   B O    1 
HETATM 6973 O  O    . HOH   H 6 .   ? 41.181 -5.471  11.530  1.00 43.74 ?  287 HOH   B O    1 
HETATM 6974 O  O    . HOH   H 6 .   ? 42.832 -20.308 -20.787 1.00 38.03 ?  288 HOH   B O    1 
HETATM 6975 O  O    . HOH   H 6 .   ? 33.485 -15.296 -13.945 1.00 20.84 ?  289 HOH   B O    1 
HETATM 6976 O  O    . HOH   H 6 .   ? 59.780 -15.288 8.107   1.00 31.14 ?  290 HOH   B O    1 
HETATM 6977 O  O    . HOH   H 6 .   ? 34.435 -12.749 2.584   1.00 25.41 ?  291 HOH   B O    1 
HETATM 6978 O  O    . HOH   H 6 .   ? 36.791 -12.768 -1.519  1.00 26.52 ?  292 HOH   B O    1 
HETATM 6979 O  O    . HOH   H 6 .   ? 47.068 -33.988 -4.635  1.00 16.97 ?  293 HOH   B O    1 
HETATM 6980 O  O    . HOH   H 6 .   ? 43.590 -15.397 18.210  1.00 31.90 ?  294 HOH   B O    1 
HETATM 6981 O  O    . HOH   H 6 .   ? 51.219 -37.574 -9.641  1.00 26.00 ?  295 HOH   B O    1 
HETATM 6982 O  O    . HOH   H 6 .   ? 42.636 -12.333 -18.534 1.00 29.30 ?  296 HOH   B O    1 
HETATM 6983 O  O    . HOH   H 6 .   ? 40.214 -10.829 -9.546  1.00 16.70 ?  297 HOH   B O    1 
HETATM 6984 O  O    . HOH   H 6 .   ? 52.537 -10.414 12.968  1.00 22.68 ?  298 HOH   B O    1 
HETATM 6985 O  O    . HOH   H 6 .   ? 44.614 -27.456 1.976   1.00 15.30 ?  299 HOH   B O    1 
HETATM 6986 O  O    . HOH   H 6 .   ? 45.331 -33.382 -15.971 1.00 23.38 ?  300 HOH   B O    1 
HETATM 6987 O  O    . HOH   H 6 .   ? 42.222 -10.006 -14.972 1.00 35.57 ?  301 HOH   B O    1 
HETATM 6988 O  O    . HOH   H 6 .   ? 51.644 -6.023  -7.975  1.00 46.65 ?  302 HOH   B O    1 
HETATM 6989 O  O    . HOH   H 6 .   ? 49.950 -24.648 5.799   1.00 33.49 ?  303 HOH   B O    1 
HETATM 6990 O  O    . HOH   H 6 .   ? 37.531 -18.127 13.099  1.00 30.26 ?  304 HOH   B O    1 
HETATM 6991 O  O    . HOH   H 6 .   ? 35.074 -33.568 4.524   1.00 28.63 ?  305 HOH   B O    1 
HETATM 6992 O  O    . HOH   H 6 .   ? 45.910 -40.412 -3.617  1.00 29.93 ?  306 HOH   B O    1 
HETATM 6993 O  O    . HOH   H 6 .   ? 53.481 -30.191 4.459   1.00 18.32 ?  307 HOH   B O    1 
HETATM 6994 O  O    . HOH   H 6 .   ? 52.601 -35.666 -8.580  1.00 29.06 ?  308 HOH   B O    1 
HETATM 6995 O  O    . HOH   H 6 .   ? 52.520 -29.249 -13.039 1.00 24.56 ?  309 HOH   B O    1 
HETATM 6996 O  O    . HOH   H 6 .   ? 25.935 -21.485 -3.531  1.00 15.83 ?  310 HOH   B O    1 
HETATM 6997 O  O    . HOH   H 6 .   ? 44.025 -29.356 -4.681  1.00 23.22 ?  311 HOH   B O    1 
HETATM 6998 O  O    . HOH   H 6 .   ? 37.819 -10.249 -10.792 1.00 17.00 ?  312 HOH   B O    1 
HETATM 6999 O  O    . HOH   H 6 .   ? 62.822 -20.156 -0.857  1.00 37.27 ?  313 HOH   B O    1 
HETATM 7000 O  O    . HOH   H 6 .   ? 53.195 -16.099 -12.760 1.00 28.02 ?  314 HOH   B O    1 
HETATM 7001 O  O    . HOH   H 6 .   ? 41.739 -8.066  1.358   1.00 24.85 ?  315 HOH   B O    1 
HETATM 7002 O  O    . HOH   H 6 .   ? 62.730 -13.594 4.672   1.00 26.97 ?  316 HOH   B O    1 
HETATM 7003 O  O    . HOH   H 6 .   ? 38.331 -9.356  -13.283 1.00 29.43 ?  317 HOH   B O    1 
HETATM 7004 O  O    . HOH   H 6 .   ? 32.807 -34.593 -5.938  1.00 16.62 ?  318 HOH   B O    1 
HETATM 7005 O  O    . HOH   H 6 .   ? 48.130 -32.607 -16.653 1.00 41.80 ?  319 HOH   B O    1 
HETATM 7006 O  O    . HOH   H 6 .   ? 26.323 -21.030 -6.259  1.00 15.94 ?  320 HOH   B O    1 
HETATM 7007 O  O    . HOH   H 6 .   ? 57.648 -22.046 3.124   1.00 27.86 ?  321 HOH   B O    1 
HETATM 7008 O  O    . HOH   H 6 .   ? 43.209 -21.423 10.642  1.00 16.23 ?  322 HOH   B O    1 
HETATM 7009 O  O    . HOH   H 6 .   ? 37.135 -30.576 -21.053 1.00 30.16 ?  323 HOH   B O    1 
HETATM 7010 O  O    . HOH   H 6 .   ? 59.953 -17.179 -10.537 1.00 32.53 ?  324 HOH   B O    1 
HETATM 7011 O  O    . HOH   H 6 .   ? 38.335 -12.742 7.889   1.00 18.09 ?  325 HOH   B O    1 
HETATM 7012 O  O    . HOH   H 6 .   ? 51.403 -32.986 -10.823 1.00 39.50 ?  326 HOH   B O    1 
HETATM 7013 O  O    . HOH   H 6 .   ? 44.145 -1.743  7.589   1.00 44.54 ?  327 HOH   B O    1 
HETATM 7014 O  O    . HOH   H 6 .   ? 41.225 -24.517 15.806  1.00 42.77 ?  328 HOH   B O    1 
HETATM 7015 O  O    . HOH   H 6 .   ? 36.717 -12.406 4.262   1.00 17.70 ?  329 HOH   B O    1 
HETATM 7016 O  O    . HOH   H 6 .   ? 44.618 -24.575 9.539   1.00 19.64 ?  330 HOH   B O    1 
HETATM 7017 O  O    . HOH   H 6 .   ? 43.113 -34.616 0.079   1.00 19.66 ?  331 HOH   B O    1 
HETATM 7018 O  O    . HOH   H 6 .   ? 53.642 -12.548 -22.284 1.00 35.31 ?  332 HOH   B O    1 
HETATM 7019 O  O    . HOH   H 6 .   ? 47.197 -24.489 8.132   1.00 24.85 ?  333 HOH   B O    1 
HETATM 7020 O  O    . HOH   H 6 .   ? 27.959 -14.805 -9.449  1.00 35.01 ?  334 HOH   B O    1 
HETATM 7021 O  O    . HOH   H 6 .   ? 48.579 -11.927 -13.881 1.00 25.88 ?  335 HOH   B O    1 
HETATM 7022 O  O    . HOH   H 6 .   ? 33.638 -31.194 11.047  1.00 33.53 ?  336 HOH   B O    1 
HETATM 7023 O  O    . HOH   H 6 .   ? 42.851 -43.477 -14.372 1.00 42.29 ?  337 HOH   B O    1 
HETATM 7024 O  O    . HOH   H 6 .   ? 45.684 -36.273 -16.113 1.00 34.48 ?  338 HOH   B O    1 
HETATM 7025 O  O    . HOH   H 6 .   ? 46.871 -19.829 12.221  1.00 29.92 ?  339 HOH   B O    1 
HETATM 7026 O  O    . HOH   H 6 .   ? 47.470 -27.433 2.002   1.00 14.42 ?  340 HOH   B O    1 
HETATM 7027 O  O    . HOH   H 6 .   ? 28.888 -42.937 -12.412 1.00 36.47 ?  341 HOH   B O    1 
HETATM 7028 O  O    . HOH   H 6 .   ? 39.470 -23.595 -20.378 1.00 36.07 ?  342 HOH   B O    1 
HETATM 7029 O  O    . HOH   H 6 .   ? 37.026 -15.070 -16.533 1.00 40.08 ?  343 HOH   B O    1 
HETATM 7030 O  O    . HOH   H 6 .   ? 37.019 -45.206 -9.761  1.00 37.28 ?  344 HOH   B O    1 
HETATM 7031 O  O    . HOH   H 6 .   ? 38.409 -12.263 -16.305 1.00 42.28 ?  345 HOH   B O    1 
HETATM 7032 O  O    . HOH   H 6 .   ? 32.997 -14.686 1.042   1.00 18.31 ?  346 HOH   B O    1 
HETATM 7033 O  O    . HOH   H 6 .   ? 33.632 -9.656  -8.771  1.00 31.76 ?  347 HOH   B O    1 
HETATM 7034 O  O    . HOH   H 6 .   ? 39.803 -44.298 -11.232 1.00 36.23 ?  348 HOH   B O    1 
HETATM 7035 O  O    . HOH   H 6 .   ? 27.784 -26.570 -0.588  1.00 31.20 ?  349 HOH   B O    1 
HETATM 7036 O  O    . HOH   H 6 .   ? 40.402 -43.490 -9.128  1.00 26.47 ?  350 HOH   B O    1 
HETATM 7037 O  O    . HOH   H 6 .   ? 62.540 -20.075 -4.872  1.00 43.48 ?  351 HOH   B O    1 
HETATM 7038 O  O    . HOH   H 6 .   ? 38.582 -22.284 15.057  1.00 40.57 ?  352 HOH   B O    1 
HETATM 7039 O  O    . HOH   H 6 .   ? 55.643 -8.258  10.803  1.00 24.92 ?  353 HOH   B O    1 
HETATM 7040 O  O    . HOH   H 6 .   ? 34.591 -10.301 7.548   1.00 23.39 ?  354 HOH   B O    1 
HETATM 7041 O  O    . HOH   H 6 .   ? 56.590 -7.313  3.074   1.00 27.05 ?  355 HOH   B O    1 
HETATM 7042 O  O    . HOH   H 6 .   ? 44.139 -37.305 -17.820 1.00 33.18 ?  356 HOH   B O    1 
HETATM 7043 O  O    . HOH   H 6 .   ? 36.099 -8.533  -9.740  1.00 35.29 ?  357 HOH   B O    1 
HETATM 7044 O  O    . HOH   H 6 .   ? 23.152 -23.647 6.810   1.00 35.12 ?  358 HOH   B O    1 
HETATM 7045 O  O    . HOH   H 6 .   ? 43.165 -12.667 -21.211 1.00 40.36 ?  359 HOH   B O    1 
HETATM 7046 O  O    . HOH   H 6 .   ? 61.505 -19.910 1.598   1.00 33.48 ?  360 HOH   B O    1 
HETATM 7047 O  O    . HOH   H 6 .   ? 34.146 -7.697  11.414  1.00 39.77 ?  361 HOH   B O    1 
HETATM 7048 O  O    . HOH   H 6 .   ? 56.898 -21.531 -16.403 1.00 41.27 ?  362 HOH   B O    1 
HETATM 7049 O  O    . HOH   H 6 .   ? 40.239 -8.823  9.892   1.00 34.00 ?  363 HOH   B O    1 
HETATM 7050 O  O    . HOH   H 6 .   ? 27.105 -25.960 -11.364 1.00 32.76 ?  364 HOH   B O    1 
HETATM 7051 O  O    . HOH   H 6 .   ? 54.155 -5.684  2.968   1.00 36.42 ?  365 HOH   B O    1 
HETATM 7052 O  O    . HOH   H 6 .   ? 32.540 -23.653 14.089  1.00 39.63 ?  366 HOH   B O    1 
HETATM 7053 O  O    . HOH   H 6 .   ? 36.202 -8.697  8.981   1.00 37.77 ?  367 HOH   B O    1 
HETATM 7054 O  O    . HOH   H 6 .   ? 58.990 -10.459 9.139   1.00 39.57 ?  368 HOH   B O    1 
HETATM 7055 O  O    . HOH   H 6 .   ? 48.367 -26.499 8.765   1.00 38.16 ?  369 HOH   B O    1 
HETATM 7056 O  O    . HOH   H 6 .   ? 40.061 -11.366 -13.966 1.00 32.77 ?  370 HOH   B O    1 
HETATM 7057 O  O    . HOH   H 6 .   ? 41.818 -10.061 -17.479 1.00 51.48 ?  371 HOH   B O    1 
HETATM 7058 O  O    . HOH   H 6 .   ? 39.860 -7.017  7.813   1.00 42.37 ?  372 HOH   B O    1 
HETATM 7059 O  O    . HOH   H 6 .   ? 55.979 -7.753  -0.632  1.00 34.32 ?  373 HOH   B O    1 
HETATM 7060 O  O    . HOH   H 6 .   ? 52.057 -12.858 13.332  1.00 33.70 ?  374 HOH   B O    1 
HETATM 7061 O  O    . HOH   H 6 .   ? 63.083 -12.388 6.842   1.00 36.98 ?  375 HOH   B O    1 
HETATM 7062 O  O    . HOH   H 6 .   ? 38.018 -10.586 10.020  1.00 29.95 ?  376 HOH   B O    1 
HETATM 7063 O  O    . HOH   H 6 .   ? 41.838 -6.732  -4.900  1.00 44.25 ?  377 HOH   B O    1 
HETATM 7064 O  O    . HOH   H 6 .   ? 44.031 -5.595  -3.563  1.00 43.80 ?  378 HOH   B O    1 
HETATM 7065 O  O    . HOH   H 6 .   ? 42.623 -17.080 -23.174 1.00 44.41 ?  379 HOH   B O    1 
HETATM 7066 O  O    . HOH   H 6 .   ? 36.516 -22.781 13.281  1.00 25.04 ?  380 HOH   B O    1 
HETATM 7067 O  O    . HOH   H 6 .   ? 52.850 -29.878 7.117   1.00 23.72 ?  381 HOH   B O    1 
HETATM 7068 O  O    . HOH   H 6 .   ? 40.088 -7.548  3.151   1.00 33.38 ?  382 HOH   B O    1 
HETATM 7069 O  O    . HOH   H 6 .   ? 39.709 -14.066 15.730  1.00 49.20 ?  383 HOH   B O    1 
HETATM 7070 O  O    . HOH   H 6 .   ? 60.477 -22.256 2.767   1.00 50.13 ?  384 HOH   B O    1 
HETATM 7071 O  O    . HOH   H 6 .   ? 46.795 -5.370  2.868   1.00 40.86 ?  385 HOH   B O    1 
HETATM 7072 O  O    . HOH   H 6 .   ? 23.897 -20.822 -7.715  1.00 28.18 ?  386 HOH   B O    1 
HETATM 7073 O  O    . HOH   H 6 .   ? 35.412 -33.721 7.301   1.00 41.08 ?  387 HOH   B O    1 
HETATM 7074 O  O    . HOH   H 6 .   ? 25.824 -18.945 -11.939 1.00 37.64 ?  388 HOH   B O    1 
HETATM 7075 O  O    . HOH   H 6 .   ? 35.343 -20.313 13.288  1.00 30.46 ?  389 HOH   B O    1 
HETATM 7076 O  O    . HOH   H 6 .   ? 40.927 -9.794  15.793  1.00 46.84 ?  390 HOH   B O    1 
HETATM 7077 O  O    . HOH   H 6 .   ? 40.687 -6.653  -0.889  1.00 24.32 ?  391 HOH   B O    1 
HETATM 7078 O  O    . HOH   H 6 .   ? 44.096 -31.772 -3.827  1.00 33.87 ?  392 HOH   B O    1 
HETATM 7079 O  O    . HOH   H 6 .   ? 27.896 -27.081 2.225   1.00 30.49 ?  393 HOH   B O    1 
HETATM 7080 O  O    . HOH   H 6 .   ? 26.606 -27.987 -13.465 1.00 34.38 ?  394 HOH   B O    1 
HETATM 7081 O  O    . HOH   H 6 .   ? 34.387 -33.442 9.610   1.00 33.68 ?  395 HOH   B O    1 
HETATM 7082 O  O    . HOH   H 6 .   ? 24.578 -20.636 -10.497 1.00 36.17 ?  396 HOH   B O    1 
HETATM 7083 O  O    . HOH   H 6 .   ? 26.861 -30.704 -12.666 1.00 28.01 ?  397 HOH   B O    1 
HETATM 7084 O  O    . HOH   H 6 .   ? 50.650 -30.813 8.677   1.00 28.86 ?  398 HOH   B O    1 
HETATM 7085 O  O    . HOH   H 6 .   ? 57.597 -6.507  -2.393  1.00 33.38 ?  399 HOH   B O    1 
HETATM 7086 O  O    . HOH   H 6 .   ? 45.794 -20.182 15.174  1.00 50.46 ?  400 HOH   B O    1 
HETATM 7087 O  O    . HOH   H 6 .   ? 40.867 -11.785 -22.337 1.00 42.17 ?  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   ? 0.6338 0.6339 0.6866 -0.0026 -0.0199 0.0764  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.6296 0.6318 0.6531 -0.0062 -0.0146 0.0457  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.6325 0.6325 0.6756 -0.0043 -0.0185 0.0759  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.6279 0.6303 0.6472 -0.0072 -0.0147 0.0477  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.6195 0.6228 0.6462 -0.0093 -0.0228 0.0766  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.6174 0.6216 0.6300 -0.0110 -0.0203 0.0606  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.6214 0.6247 0.6571 -0.0079 -0.0247 0.0778  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.6200 0.6236 0.6397 -0.0103 -0.0211 0.0602  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.6419 0.6393 0.6890 -0.0021 -0.0136 0.0741  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.6345 0.6359 0.6561 -0.0052 -0.0103 0.0386  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.6454 0.6409 0.6895 -0.0006 -0.0126 0.0731  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.6366 0.6373 0.6559 -0.0043 -0.0089 0.0355  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.6447 0.6425 0.6894 -0.0022 -0.0114 0.0742  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.6368 0.6383 0.6558 -0.0047 -0.0087 0.0358  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.6014 0.6086 0.5996 -0.0160 -0.0249 0.0742  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.5642 0.5784 0.5167 -0.0287 -0.0304 0.0828  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.5154 0.5432 0.4676 -0.0418 -0.0220 0.0660  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.5160 0.5433 0.4571 -0.0445 -0.0229 0.0713  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.5717 0.5808 0.4779 -0.0291 -0.0420 0.1084  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.5749 0.5792 0.4374 -0.0307 -0.0536 0.1329  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.5776 0.5778 0.4234 -0.0329 -0.0586 0.1421  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.5736 0.5779 0.4297 -0.0289 -0.0586 0.1433  4   ASN   A ND2 
46   N  N   . SER   A 5   ? 0.4634 0.5028 0.4321 -0.0535 -0.0115 0.0456  5   SER   A N   
47   C  CA  . SER   A 5   ? 0.4088 0.4600 0.3922 -0.0657 0.0012  0.0210  5   SER   A CA  
48   C  C   . SER   A 5   ? 0.3495 0.4063 0.3253 -0.0715 0.0146  0.0040  5   SER   A C   
49   O  O   . SER   A 5   ? 0.3579 0.4157 0.3266 -0.0579 0.0091  -0.0075 5   SER   A O   
50   C  CB  . SER   A 5   ? 0.4150 0.4701 0.4327 -0.0712 0.0002  0.0123  5   SER   A CB  
51   O  OG  . SER   A 5   ? 0.4184 0.4759 0.4490 -0.0749 0.0012  0.0081  5   SER   A OG  
57   N  N   A PHE   A 6   ? 0.2996 0.3722 0.2704 -0.0959 0.0323  0.0070  6   PHE   A N   
58   N  N   B PHE   A 6   ? 0.3274 0.3746 0.2942 -0.0656 0.0157  0.0004  6   PHE   A N   
59   C  CA  A PHE   A 6   ? 0.2592 0.3381 0.2225 -0.1071 0.0426  0.0193  6   PHE   A CA  
60   C  CA  B PHE   A 6   ? 0.3058 0.3412 0.2612 -0.0570 0.0151  -0.0005 6   PHE   A CA  
61   C  C   A PHE   A 6   ? 0.2535 0.3372 0.2231 -0.1145 0.0504  0.0118  6   PHE   A C   
62   C  C   B PHE   A 6   ? 0.2994 0.3283 0.2537 -0.0526 0.0182  -0.0041 6   PHE   A C   
63   O  O   A PHE   A 6   ? 0.2595 0.3422 0.2478 -0.1133 0.0563  0.0226  6   PHE   A O   
64   O  O   B PHE   A 6   ? 0.3013 0.3293 0.2448 -0.0547 0.0169  -0.0008 6   PHE   A O   
65   C  CB  A PHE   A 6   ? 0.2398 0.3070 0.1966 -0.0964 0.0348  0.0323  6   PHE   A CB  
66   C  CB  B PHE   A 6   ? 0.2931 0.3215 0.2440 -0.0501 0.0105  0.0010  6   PHE   A CB  
67   C  CG  A PHE   A 6   ? 0.2254 0.2802 0.1816 -0.0829 0.0271  0.0310  6   PHE   A CG  
68   C  CG  B PHE   A 6   ? 0.2825 0.3037 0.2279 -0.0435 0.0065  0.0022  6   PHE   A CG  
69   C  CD1 A PHE   A 6   ? 0.2191 0.2691 0.1701 -0.0774 0.0182  0.0297  6   PHE   A CD1 
70   C  CD1 B PHE   A 6   ? 0.2782 0.2964 0.2208 -0.0403 0.0030  0.0023  6   PHE   A CD1 
71   C  CD2 A PHE   A 6   ? 0.2308 0.2726 0.2049 -0.0659 0.0296  0.0293  6   PHE   A CD2 
72   C  CD2 B PHE   A 6   ? 0.2805 0.2967 0.2243 -0.0384 0.0069  0.0039  6   PHE   A CD2 
73   C  CE1 A PHE   A 6   ? 0.2218 0.2624 0.1808 -0.0717 0.0243  0.0311  6   PHE   A CE1 
74   C  CE1 B PHE   A 6   ? 0.2769 0.2922 0.2184 -0.0378 0.0039  0.0039  6   PHE   A CE1 
75   C  CE2 A PHE   A 6   ? 0.2306 0.2665 0.2142 -0.0598 0.0271  0.0259  6   PHE   A CE2 
76   C  CE2 B PHE   A 6   ? 0.2790 0.2927 0.2205 -0.0359 0.0057  0.0055  6   PHE   A CE2 
77   C  CZ  A PHE   A 6   ? 0.2254 0.2630 0.1987 -0.0664 0.0287  0.0246  6   PHE   A CZ  
78   C  CZ  B PHE   A 6   ? 0.2775 0.2912 0.2177 -0.0363 0.0043  0.0047  6   PHE   A CZ  
97   N  N   A SER   A 7   ? 0.2425 0.3282 0.2049 -0.1164 0.0552  -0.0029 7   SER   A N   
98   N  N   B SER   A 7   ? 0.2909 0.3136 0.2554 -0.0450 0.0213  -0.0107 7   SER   A N   
99   C  CA  A SER   A 7   ? 0.2458 0.3232 0.2170 -0.1029 0.0552  -0.0148 7   SER   A CA  
100  C  CA  B SER   A 7   ? 0.2843 0.3004 0.2656 -0.0359 0.0220  -0.0185 7   SER   A CA  
101  C  C   A SER   A 7   ? 0.2288 0.2821 0.1893 -0.0965 0.0552  -0.0129 7   SER   A C   
102  C  C   B SER   A 7   ? 0.2707 0.2835 0.2503 -0.0281 0.0272  -0.0164 7   SER   A C   
103  O  O   A SER   A 7   ? 0.2401 0.2741 0.1919 -0.1046 0.0565  -0.0103 7   SER   A O   
104  O  O   B SER   A 7   ? 0.2719 0.2830 0.2502 -0.0251 0.0252  -0.0156 7   SER   A O   
105  C  CB  A SER   A 7   ? 0.2707 0.3582 0.2602 -0.0866 0.0588  -0.0157 7   SER   A CB  
106  C  CB  B SER   A 7   ? 0.2892 0.3031 0.2842 -0.0356 0.0182  -0.0251 7   SER   A CB  
107  O  OG  A SER   A 7   ? 0.2896 0.3738 0.2992 -0.0772 0.0530  -0.0185 7   SER   A OG  
108  O  OG  B SER   A 7   ? 0.2921 0.3042 0.3002 -0.0354 0.0131  -0.0316 7   SER   A OG  
119  N  N   A GLY   A 8   ? 0.2090 0.2527 0.1764 -0.0799 0.0472  -0.0194 8   GLY   A N   
120  N  N   B GLY   A 8   ? 0.2579 0.2692 0.2374 -0.0244 0.0323  -0.0167 8   GLY   A N   
121  C  CA  A GLY   A 8   ? 0.1967 0.2282 0.1848 -0.0537 0.0449  -0.0181 8   GLY   A CA  
122  C  CA  B GLY   A 8   ? 0.2434 0.2521 0.2209 -0.0224 0.0327  -0.0166 8   GLY   A CA  
123  C  C   A GLY   A 8   ? 0.1777 0.2068 0.1782 -0.0387 0.0389  -0.0054 8   GLY   A C   
124  C  C   B GLY   A 8   ? 0.2281 0.2345 0.2027 -0.0210 0.0321  -0.0146 8   GLY   A C   
125  O  O   A GLY   A 8   ? 0.1873 0.2123 0.2031 -0.0191 0.0351  -0.0234 8   GLY   A O   
126  O  O   B GLY   A 8   ? 0.2279 0.2340 0.2077 -0.0195 0.0348  -0.0194 8   GLY   A O   
133  N  N   A TYR   A 9   ? 0.1583 0.1905 0.1717 -0.0331 0.0287  0.0146  9   TYR   A N   
134  N  N   B TYR   A 9   ? 0.2121 0.2189 0.1902 -0.0192 0.0272  -0.0059 9   TYR   A N   
135  C  CA  A TYR   A 9   ? 0.1482 0.1793 0.1507 -0.0325 0.0232  0.0130  9   TYR   A CA  
136  C  CA  B TYR   A 9   ? 0.1983 0.2044 0.1824 -0.0157 0.0263  -0.0006 9   TYR   A CA  
137  C  C   A TYR   A 9   ? 0.1512 0.1629 0.1505 -0.0252 0.0301  0.0245  9   TYR   A C   
138  C  C   B TYR   A 9   ? 0.1881 0.1906 0.1711 -0.0087 0.0281  0.0018  9   TYR   A C   
139  O  O   A TYR   A 9   ? 0.1757 0.1718 0.1693 -0.0210 0.0266  0.0215  9   TYR   A O   
140  O  O   B TYR   A 9   ? 0.1914 0.1918 0.1811 -0.0092 0.0308  -0.0035 9   TYR   A O   
141  C  CB  A TYR   A 9   ? 0.1427 0.1963 0.1583 -0.0230 0.0228  0.0038  9   TYR   A CB  
142  C  CB  B TYR   A 9   ? 0.1942 0.2067 0.1891 -0.0184 0.0220  0.0002  9   TYR   A CB  
143  C  CG  A TYR   A 9   ? 0.1383 0.2069 0.1728 -0.0186 0.0283  -0.0061 9   TYR   A CG  
144  C  CG  B TYR   A 9   ? 0.1884 0.2086 0.1876 -0.0212 0.0198  -0.0005 9   TYR   A CG  
145  C  CD1 A TYR   A 9   ? 0.1443 0.2186 0.1825 -0.0305 0.0374  -0.0142 9   TYR   A CD1 
146  C  CD1 B TYR   A 9   ? 0.1895 0.2127 0.1916 -0.0251 0.0185  -0.0024 9   TYR   A CD1 
147  C  CD2 A TYR   A 9   ? 0.1343 0.2019 0.1769 -0.0139 0.0174  0.0028  9   TYR   A CD2 
148  C  CD2 B TYR   A 9   ? 0.1856 0.2079 0.1848 -0.0206 0.0177  0.0007  9   TYR   A CD2 
149  C  CE1 A TYR   A 9   ? 0.1489 0.2250 0.2001 -0.0360 0.0384  -0.0206 9   TYR   A CE1 
150  C  CE1 B TYR   A 9   ? 0.1904 0.2145 0.1974 -0.0275 0.0174  -0.0029 9   TYR   A CE1 
151  C  CE2 A TYR   A 9   ? 0.1363 0.2143 0.1778 -0.0207 0.0276  0.0029  9   TYR   A CE2 
152  C  CE2 B TYR   A 9   ? 0.1870 0.2121 0.1893 -0.0215 0.0204  0.0023  9   TYR   A CE2 
153  C  CZ  A TYR   A 9   ? 0.1379 0.2265 0.2065 -0.0395 0.0501  -0.0104 9   TYR   A CZ  
154  C  CZ  B TYR   A 9   ? 0.1911 0.2166 0.1997 -0.0264 0.0232  0.0026  9   TYR   A CZ  
155  O  OH  A TYR   A 9   ? 0.1532 0.2389 0.2395 -0.0563 0.0535  -0.0160 9   TYR   A OH  
156  O  OH  B TYR   A 9   ? 0.1996 0.2236 0.2132 -0.0291 0.0294  0.0081  9   TYR   A OH  
175  N  N   A LEU   A 10  ? 0.1461 0.1488 0.1509 -0.0281 0.0165  0.0293  10  LEU   A N   
176  N  N   B LEU   A 10  ? 0.1783 0.1818 0.1685 -0.0057 0.0191  0.0104  10  LEU   A N   
177  C  CA  A LEU   A 10  ? 0.1361 0.1523 0.1598 -0.0284 0.0166  0.0354  10  LEU   A CA  
178  C  CA  B LEU   A 10  ? 0.1718 0.1754 0.1687 -0.0040 0.0180  0.0132  10  LEU   A CA  
179  C  C   A LEU   A 10  ? 0.1388 0.1483 0.1655 -0.0258 0.0122  0.0462  10  LEU   A C   
180  C  C   B LEU   A 10  ? 0.1635 0.1646 0.1473 -0.0110 0.0154  0.0215  10  LEU   A C   
181  O  O   A LEU   A 10  ? 0.1414 0.1411 0.1863 -0.0213 0.0229  0.0474  10  LEU   A O   
182  O  O   B LEU   A 10  ? 0.1640 0.1637 0.1518 -0.0141 0.0239  0.0273  10  LEU   A O   
183  C  CB  A LEU   A 10  ? 0.1387 0.1618 0.1732 -0.0296 0.0057  0.0329  10  LEU   A CB  
184  C  CB  B LEU   A 10  ? 0.1768 0.1798 0.1814 0.0004  0.0103  0.0125  10  LEU   A CB  
185  C  CG  A LEU   A 10  ? 0.1608 0.1825 0.2272 -0.0139 -0.0125 0.0273  10  LEU   A CG  
186  C  CG  B LEU   A 10  ? 0.1821 0.1868 0.1853 0.0087  -0.0019 0.0125  10  LEU   A CG  
187  C  CD1 A LEU   A 10  ? 0.1748 0.1915 0.2575 -0.0245 -0.0130 0.0426  10  LEU   A CD1 
188  C  CD1 B LEU   A 10  ? 0.1854 0.1895 0.1961 0.0075  -0.0120 0.0141  10  LEU   A CD1 
189  C  CD2 A LEU   A 10  ? 0.1741 0.2034 0.2583 0.0019  -0.0011 0.0144  10  LEU   A CD2 
190  C  CD2 B LEU   A 10  ? 0.1880 0.1927 0.1874 0.0182  -0.0076 0.0128  10  LEU   A CD2 
213  N  N   A LYS   A 11  ? 0.1448 0.1530 0.1628 -0.0285 0.0084  0.0415  11  LYS   A N   
214  N  N   B LYS   A 11  ? 0.1594 0.1556 0.1383 -0.0170 0.0051  0.0209  11  LYS   A N   
215  C  CA  A LYS   A 11  ? 0.1437 0.1506 0.1756 -0.0389 0.0125  0.0380  11  LYS   A CA  
216  C  CA  B LYS   A 11  ? 0.1571 0.1458 0.1390 -0.0201 0.0027  0.0186  11  LYS   A CA  
217  C  C   A LYS   A 11  ? 0.1364 0.1565 0.1823 -0.0320 0.0149  0.0290  11  LYS   A C   
218  C  C   B LYS   A 11  ? 0.1472 0.1342 0.1341 -0.0263 0.0032  0.0065  11  LYS   A C   
219  O  O   A LYS   A 11  ? 0.1454 0.1834 0.2161 -0.0516 0.0236  0.0115  11  LYS   A O   
220  O  O   B LYS   A 11  ? 0.1440 0.1276 0.1481 -0.0314 0.0071  -0.0095 11  LYS   A O   
221  C  CB  A LYS   A 11  ? 0.1633 0.1460 0.1745 -0.0362 0.0047  0.0350  11  LYS   A CB  
222  C  CB  B LYS   A 11  ? 0.1647 0.1423 0.1414 -0.0165 0.0015  0.0217  11  LYS   A CB  
223  C  CG  A LYS   A 11  ? 0.1739 0.1440 0.1758 -0.0348 0.0115  0.0388  11  LYS   A CG  
224  C  CG  B LYS   A 11  ? 0.1701 0.1424 0.1416 -0.0115 0.0019  0.0237  11  LYS   A CG  
225  C  CD  A LYS   A 11  ? 0.1868 0.1444 0.1819 -0.0265 0.0099  0.0328  11  LYS   A CD  
226  C  CD  B LYS   A 11  ? 0.1750 0.1435 0.1491 -0.0091 0.0021  0.0262  11  LYS   A CD  
227  C  CE  A LYS   A 11  ? 0.1904 0.1418 0.1808 -0.0235 0.0057  0.0308  11  LYS   A CE  
228  C  CE  B LYS   A 11  ? 0.1779 0.1442 0.1493 -0.0082 0.0002  0.0324  11  LYS   A CE  
229  N  NZ  A LYS   A 11  ? 0.1853 0.1419 0.1863 -0.0162 -0.0070 0.0256  11  LYS   A NZ  
230  N  NZ  B LYS   A 11  ? 0.1758 0.1455 0.1418 -0.0059 -0.0005 0.0404  11  LYS   A NZ  
257  N  N   A LEU   A 12  ? 0.1256 0.1424 0.1636 -0.0266 0.0139  0.0269  12  LEU   A N   
258  N  N   B LEU   A 12  ? 0.1428 0.1405 0.1349 -0.0205 0.0017  0.0072  12  LEU   A N   
259  C  CA  A LEU   A 12  ? 0.1299 0.1498 0.1754 -0.0201 0.0107  0.0294  12  LEU   A CA  
260  C  CA  B LEU   A 12  ? 0.1396 0.1472 0.1343 -0.0167 0.0071  0.0072  12  LEU   A CA  
261  C  C   A LEU   A 12  ? 0.1359 0.1420 0.1712 -0.0228 0.0115  0.0278  12  LEU   A C   
262  C  C   B LEU   A 12  ? 0.1450 0.1522 0.1370 -0.0123 0.0163  0.0202  12  LEU   A C   
263  O  O   A LEU   A 12  ? 0.1431 0.1449 0.1767 -0.0250 0.0073  0.0099  12  LEU   A O   
264  O  O   B LEU   A 12  ? 0.1437 0.1507 0.1296 -0.0063 0.0227  0.0302  12  LEU   A O   
265  C  CB  A LEU   A 12  ? 0.1341 0.1467 0.1816 -0.0124 0.0086  0.0314  12  LEU   A CB  
266  C  CB  B LEU   A 12  ? 0.1341 0.1471 0.1416 -0.0175 0.0064  0.0007  12  LEU   A CB  
267  C  CG  A LEU   A 12  ? 0.1503 0.1519 0.1930 -0.0069 0.0154  0.0246  12  LEU   A CG  
268  C  CG  B LEU   A 12  ? 0.1293 0.1427 0.1509 -0.0181 0.0117  -0.0013 12  LEU   A CG  
269  C  CD1 A LEU   A 12  ? 0.1645 0.1521 0.1967 0.0031  0.0329  0.0395  12  LEU   A CD1 
270  C  CD1 B LEU   A 12  ? 0.1270 0.1441 0.1585 -0.0176 0.0114  -0.0046 12  LEU   A CD1 
271  C  CD2 A LEU   A 12  ? 0.1524 0.1569 0.2227 -0.0046 0.0078  0.0152  12  LEU   A CD2 
272  C  CD2 B LEU   A 12  ? 0.1264 0.1435 0.1556 -0.0187 0.0148  -0.0065 12  LEU   A CD2 
295  N  N   A THR   A 13  ? 0.1258 0.1348 0.1829 -0.0195 0.0082  0.0294  13  THR   A N   
296  N  N   B THR   A 13  ? 0.1507 0.1540 0.1500 -0.0131 0.0150  0.0176  13  THR   A N   
297  C  CA  A THR   A 13  ? 0.1265 0.1388 0.1953 -0.0197 0.0143  0.0283  13  THR   A CA  
298  C  CA  B THR   A 13  ? 0.1542 0.1625 0.1625 -0.0175 0.0224  0.0171  13  THR   A CA  
299  C  C   A THR   A 13  ? 0.1315 0.1394 0.1995 -0.0208 0.0111  0.0408  13  THR   A C   
300  C  C   B THR   A 13  ? 0.1583 0.1681 0.1678 -0.0231 0.0209  0.0184  13  THR   A C   
301  O  O   A THR   A 13  ? 0.1300 0.1386 0.1944 -0.0140 0.0119  0.0320  13  THR   A O   
302  O  O   B THR   A 13  ? 0.1621 0.1718 0.1624 -0.0256 0.0176  0.0208  13  THR   A O   
303  C  CB  A THR   A 13  ? 0.1340 0.1526 0.2013 -0.0172 0.0107  0.0359  13  THR   A CB  
304  C  CB  B THR   A 13  ? 0.1538 0.1719 0.1741 -0.0134 0.0284  0.0174  13  THR   A CB  
305  O  OG1 A THR   A 13  ? 0.1307 0.1482 0.2050 -0.0168 -0.0005 0.0483  13  THR   A OG1 
306  O  OG1 B THR   A 13  ? 0.1467 0.1749 0.1824 -0.0118 0.0418  0.0196  13  THR   A OG1 
307  C  CG2 A THR   A 13  ? 0.1438 0.1752 0.2147 -0.0246 0.0190  0.0222  13  THR   A CG2 
308  C  CG2 B THR   A 13  ? 0.1585 0.1800 0.1844 -0.0123 0.0276  0.0098  13  THR   A CG2 
323  N  N   A ASP   A 14  ? 0.1361 0.1422 0.2126 -0.0228 0.0053  0.0511  14  ASP   A N   
324  N  N   B ASP   A 14  ? 0.1583 0.1685 0.1844 -0.0250 0.0147  0.0208  14  ASP   A N   
325  C  CA  A ASP   A 14  ? 0.1415 0.1528 0.2390 -0.0182 -0.0043 0.0675  14  ASP   A CA  
326  C  CA  B ASP   A 14  ? 0.1583 0.1704 0.2068 -0.0251 0.0067  0.0334  14  ASP   A CA  
327  C  C   A ASP   A 14  ? 0.1427 0.1581 0.2036 -0.0214 -0.0144 0.0589  14  ASP   A C   
328  C  C   B ASP   A 14  ? 0.1490 0.1615 0.1943 -0.0272 0.0003  0.0459  14  ASP   A C   
329  O  O   A ASP   A 14  ? 0.1621 0.1747 0.2065 -0.0353 -0.0235 0.0604  14  ASP   A O   
330  O  O   B ASP   A 14  ? 0.1534 0.1670 0.1915 -0.0357 -0.0012 0.0514  14  ASP   A O   
331  C  CB  A ASP   A 14  ? 0.1598 0.1814 0.3007 -0.0195 0.0036  0.0960  14  ASP   A CB  
332  C  CB  B ASP   A 14  ? 0.1675 0.1848 0.2430 -0.0230 0.0024  0.0385  14  ASP   A CB  
333  C  CG  A ASP   A 14  ? 0.1816 0.2369 0.3783 -0.0178 0.0096  0.0957  14  ASP   A CG  
334  C  CG  B ASP   A 14  ? 0.1708 0.2055 0.2793 -0.0261 0.0011  0.0413  14  ASP   A CG  
335  O  OD1 A ASP   A 14  ? 0.1920 0.2548 0.4027 -0.0055 -0.0083 0.0950  14  ASP   A OD1 
336  O  OD1 B ASP   A 14  ? 0.1717 0.2058 0.2886 -0.0314 0.0023  0.0448  14  ASP   A OD1 
337  O  OD2 A ASP   A 14  ? 0.1996 0.2743 0.4264 -0.0179 0.0047  0.0803  14  ASP   A OD2 
338  O  OD2 B ASP   A 14  ? 0.1740 0.2243 0.3007 -0.0251 -0.0074 0.0366  14  ASP   A OD2 
347  N  N   . ASN   A 15  ? 0.1395 0.1471 0.2005 -0.0235 0.0006  0.0525  15  ASN   A N   
348  C  CA  . ASN   A 15  ? 0.1375 0.1490 0.2094 -0.0214 -0.0057 0.0454  15  ASN   A CA  
349  C  C   . ASN   A 15  ? 0.1366 0.1452 0.2250 -0.0240 0.0017  0.0399  15  ASN   A C   
350  O  O   . ASN   A 15  ? 0.1429 0.1482 0.2751 -0.0198 -0.0197 0.0389  15  ASN   A O   
351  C  CB  . ASN   A 15  ? 0.1359 0.1481 0.2160 -0.0165 -0.0042 0.0401  15  ASN   A CB  
352  C  CG  . ASN   A 15  ? 0.1324 0.1548 0.2138 -0.0113 0.0022  0.0315  15  ASN   A CG  
353  O  OD1 . ASN   A 15  ? 0.1496 0.1610 0.2304 -0.0241 0.0005  0.0290  15  ASN   A OD1 
354  N  ND2 . ASN   A 15  ? 0.1339 0.1686 0.2136 -0.0145 0.0125  0.0303  15  ASN   A ND2 
362  N  N   . VAL   A 16  ? 0.1346 0.1416 0.2090 -0.0182 0.0022  0.0472  16  VAL   A N   
363  C  CA  . VAL   A 16  ? 0.1296 0.1451 0.2014 -0.0174 0.0057  0.0487  16  VAL   A CA  
364  C  C   . VAL   A 16  ? 0.1295 0.1475 0.1859 -0.0210 -0.0015 0.0452  16  VAL   A C   
365  O  O   . VAL   A 16  ? 0.1234 0.1427 0.2042 -0.0222 0.0102  0.0335  16  VAL   A O   
366  C  CB  . VAL   A 16  ? 0.1423 0.1600 0.1972 0.0010  0.0212  0.0556  16  VAL   A CB  
367  C  CG1 . VAL   A 16  ? 0.1549 0.1732 0.2053 0.0045  0.0228  0.0494  16  VAL   A CG1 
368  C  CG2 . VAL   A 16  ? 0.1520 0.1705 0.2120 0.0060  0.0393  0.0503  16  VAL   A CG2 
378  N  N   A TYR   A 17  ? 0.1307 0.1455 0.1867 -0.0155 0.0115  0.0466  17  TYR   A N   
379  N  N   B TYR   A 17  ? 0.1332 0.1405 0.1601 -0.0222 0.0054  0.0378  17  TYR   A N   
380  C  CA  A TYR   A 17  ? 0.1310 0.1484 0.1766 -0.0183 0.0092  0.0485  17  TYR   A CA  
381  C  CA  B TYR   A 17  ? 0.1360 0.1354 0.1393 -0.0251 0.0085  0.0277  17  TYR   A CA  
382  C  C   A TYR   A 17  ? 0.1311 0.1440 0.1895 -0.0186 0.0083  0.0373  17  TYR   A C   
383  C  C   B TYR   A 17  ? 0.1324 0.1336 0.1335 -0.0221 0.0200  0.0170  17  TYR   A C   
384  O  O   A TYR   A 17  ? 0.1260 0.1420 0.1846 -0.0236 0.0050  0.0421  17  TYR   A O   
385  O  O   B TYR   A 17  ? 0.1292 0.1291 0.1331 -0.0171 0.0247  0.0127  17  TYR   A O   
386  C  CB  A TYR   A 17  ? 0.1432 0.1513 0.1895 -0.0229 0.0015  0.0524  17  TYR   A CB  
387  C  CB  B TYR   A 17  ? 0.1450 0.1316 0.1389 -0.0310 -0.0011 0.0274  17  TYR   A CB  
388  C  CG  A TYR   A 17  ? 0.1625 0.1647 0.1889 -0.0236 -0.0070 0.0434  17  TYR   A CG  
389  C  CG  B TYR   A 17  ? 0.1524 0.1303 0.1317 -0.0345 -0.0129 0.0230  17  TYR   A CG  
390  C  CD1 A TYR   A 17  ? 0.1783 0.1721 0.2073 -0.0056 -0.0109 0.0467  17  TYR   A CD1 
391  C  CD1 B TYR   A 17  ? 0.1557 0.1339 0.1432 -0.0301 -0.0143 0.0255  17  TYR   A CD1 
392  C  CD2 A TYR   A 17  ? 0.1770 0.1761 0.1829 -0.0275 -0.0067 0.0387  17  TYR   A CD2 
393  C  CD2 B TYR   A 17  ? 0.1572 0.1268 0.1228 -0.0401 -0.0163 0.0260  17  TYR   A CD2 
394  C  CE1 A TYR   A 17  ? 0.1932 0.1772 0.2150 -0.0112 -0.0188 0.0412  17  TYR   A CE1 
395  C  CE1 B TYR   A 17  ? 0.1558 0.1313 0.1435 -0.0311 -0.0186 0.0271  17  TYR   A CE1 
396  C  CE2 A TYR   A 17  ? 0.1937 0.1759 0.1941 -0.0226 -0.0082 0.0275  17  TYR   A CE2 
397  C  CE2 B TYR   A 17  ? 0.1617 0.1245 0.1258 -0.0380 -0.0197 0.0263  17  TYR   A CE2 
398  C  CZ  A TYR   A 17  ? 0.1996 0.1741 0.1978 -0.0126 -0.0185 0.0365  17  TYR   A CZ  
399  C  CZ  B TYR   A 17  ? 0.1634 0.1227 0.1311 -0.0355 -0.0191 0.0281  17  TYR   A CZ  
400  O  OH  A TYR   A 17  ? 0.2118 0.1757 0.2054 -0.0064 -0.0107 0.0323  17  TYR   A OH  
401  O  OH  B TYR   A 17  ? 0.1791 0.1142 0.1303 -0.0264 -0.0128 0.0299  17  TYR   A OH  
420  N  N   A ILE   A 18  ? 0.1352 0.1418 0.1764 -0.0200 0.0075  0.0434  18  ILE   A N   
421  N  N   B ILE   A 18  ? 0.1313 0.1373 0.1234 -0.0238 0.0285  0.0199  18  ILE   A N   
422  C  CA  A ILE   A 18  ? 0.1422 0.1347 0.1676 -0.0171 0.0091  0.0329  18  ILE   A CA  
423  C  CA  B ILE   A 18  ? 0.1330 0.1412 0.1165 -0.0195 0.0319  0.0107  18  ILE   A CA  
424  C  C   A ILE   A 18  ? 0.1388 0.1447 0.1685 -0.0265 0.0064  0.0313  18  ILE   A C   
425  C  C   B ILE   A 18  ? 0.1328 0.1541 0.0983 -0.0194 0.0260  0.0057  18  ILE   A C   
426  O  O   A ILE   A 18  ? 0.1356 0.1584 0.1719 -0.0285 0.0091  0.0405  18  ILE   A O   
427  O  O   B ILE   A 18  ? 0.1293 0.1582 0.0957 -0.0215 0.0287  0.0044  18  ILE   A O   
428  C  CB  A ILE   A 18  ? 0.1538 0.1358 0.1525 -0.0016 0.0111  0.0341  18  ILE   A CB  
429  C  CB  B ILE   A 18  ? 0.1326 0.1360 0.1089 -0.0130 0.0411  0.0086  18  ILE   A CB  
430  C  CG1 A ILE   A 18  ? 0.1612 0.1446 0.1530 0.0112  0.0051  0.0402  18  ILE   A CG1 
431  C  CG1 B ILE   A 18  ? 0.1375 0.1403 0.1194 -0.0138 0.0479  0.0082  18  ILE   A CG1 
432  C  CG2 A ILE   A 18  ? 0.1540 0.1349 0.1589 -0.0056 0.0087  0.0209  18  ILE   A CG2 
433  C  CG2 B ILE   A 18  ? 0.1306 0.1388 0.1077 -0.0171 0.0383  0.0166  18  ILE   A CG2 
434  C  CD1 A ILE   A 18  ? 0.1815 0.1618 0.1700 0.0199  0.0032  0.0367  18  ILE   A CD1 
435  C  CD1 B ILE   A 18  ? 0.1459 0.1465 0.1450 -0.0137 0.0403  -0.0022 18  ILE   A CD1 
458  N  N   A LYS   A 19  ? 0.1385 0.1477 0.1665 -0.0191 0.0344  0.0274  19  LYS   A N   
459  N  N   B LYS   A 19  ? 0.1391 0.1618 0.0962 -0.0129 0.0239  -0.0002 19  LYS   A N   
460  C  CA  A LYS   A 19  ? 0.1499 0.1567 0.1758 -0.0144 0.0395  0.0282  19  LYS   A CA  
461  C  CA  B LYS   A 19  ? 0.1521 0.1736 0.1191 -0.0064 0.0244  -0.0028 19  LYS   A CA  
462  C  C   A LYS   A 19  ? 0.1431 0.1514 0.1915 -0.0057 0.0375  0.0385  19  LYS   A C   
463  C  C   B LYS   A 19  ? 0.1591 0.1814 0.1305 0.0005  0.0301  -0.0021 19  LYS   A C   
464  O  O   A LYS   A 19  ? 0.1394 0.1482 0.1901 -0.0010 0.0247  0.0480  19  LYS   A O   
465  O  O   B LYS   A 19  ? 0.1597 0.1786 0.1277 -0.0018 0.0306  0.0030  19  LYS   A O   
466  C  CB  A LYS   A 19  ? 0.1629 0.1804 0.1920 -0.0156 0.0373  0.0208  19  LYS   A CB  
467  C  CB  B LYS   A 19  ? 0.1565 0.1801 0.1305 -0.0072 0.0233  -0.0095 19  LYS   A CB  
468  C  CG  A LYS   A 19  ? 0.1959 0.1978 0.2026 -0.0216 0.0285  0.0115  19  LYS   A CG  
469  C  CG  B LYS   A 19  ? 0.1636 0.1845 0.1443 -0.0076 0.0178  -0.0081 19  LYS   A CG  
470  C  CD  A LYS   A 19  ? 0.2274 0.2212 0.2126 -0.0327 0.0269  0.0096  19  LYS   A CD  
471  C  CD  B LYS   A 19  ? 0.1685 0.1904 0.1496 -0.0123 0.0184  -0.0052 19  LYS   A CD  
472  C  CE  A LYS   A 19  ? 0.2499 0.2355 0.2248 -0.0470 0.0254  0.0069  19  LYS   A CE  
473  C  CE  B LYS   A 19  ? 0.1725 0.1993 0.1652 -0.0155 0.0173  -0.0050 19  LYS   A CE  
474  N  NZ  A LYS   A 19  ? 0.2617 0.2485 0.2193 -0.0566 0.0274  0.0001  19  LYS   A NZ  
475  N  NZ  B LYS   A 19  ? 0.1773 0.2034 0.1710 -0.0188 0.0214  -0.0088 19  LYS   A NZ  
502  N  N   A ASN   A 20  ? 0.1490 0.1589 0.2091 -0.0075 0.0396  0.0452  20  ASN   A N   
503  N  N   B ASN   A 20  ? 0.1680 0.1941 0.1614 0.0058  0.0326  -0.0092 20  ASN   A N   
504  C  CA  A ASN   A 20  ? 0.1620 0.1764 0.2275 0.0127  0.0473  0.0335  20  ASN   A CA  
505  C  CA  B ASN   A 20  ? 0.1775 0.2092 0.1967 0.0090  0.0301  -0.0087 20  ASN   A CA  
506  C  C   A ASN   A 20  ? 0.1767 0.1748 0.2391 0.0038  0.0681  0.0093  20  ASN   A C   
507  C  C   B ASN   A 20  ? 0.1835 0.2106 0.2099 0.0041  0.0353  -0.0152 20  ASN   A C   
508  O  O   A ASN   A 20  ? 0.2027 0.1891 0.2597 -0.0174 0.0755  -0.0123 20  ASN   A O   
509  O  O   B ASN   A 20  ? 0.1837 0.2130 0.2201 0.0031  0.0478  -0.0225 20  ASN   A O   
510  C  CB  A ASN   A 20  ? 0.1742 0.1935 0.2473 0.0319  0.0483  0.0532  20  ASN   A CB  
511  C  CB  B ASN   A 20  ? 0.1843 0.2206 0.2166 0.0177  0.0241  -0.0024 20  ASN   A CB  
512  C  CG  A ASN   A 20  ? 0.1935 0.2095 0.2736 0.0537  0.0598  0.0620  20  ASN   A CG  
513  C  CG  B ASN   A 20  ? 0.1941 0.2294 0.2345 0.0277  0.0195  0.0070  20  ASN   A CG  
514  O  OD1 A ASN   A 20  ? 0.2214 0.2217 0.3175 0.0687  0.0804  0.0593  20  ASN   A OD1 
515  O  OD1 B ASN   A 20  ? 0.2058 0.2342 0.2411 0.0326  0.0163  0.0149  20  ASN   A OD1 
516  N  ND2 A ASN   A 20  ? 0.1901 0.2101 0.2878 0.0510  0.0508  0.0652  20  ASN   A ND2 
517  N  ND2 B ASN   A 20  ? 0.1937 0.2305 0.2428 0.0311  0.0160  0.0088  20  ASN   A ND2 
530  N  N   A ALA   A 21  ? 0.1768 0.1727 0.2323 0.0103  0.0569  0.0082  21  ALA   A N   
531  N  N   B ALA   A 21  ? 0.1906 0.2107 0.2121 -0.0031 0.0233  -0.0125 21  ALA   A N   
532  C  CA  A ALA   A 21  ? 0.1840 0.1711 0.2246 -0.0000 0.0562  0.0103  21  ALA   A CA  
533  C  CA  B ALA   A 21  ? 0.1949 0.2100 0.2173 -0.0113 0.0166  -0.0068 21  ALA   A CA  
534  C  C   A ALA   A 21  ? 0.1728 0.1679 0.2214 0.0017  0.0577  0.0153  21  ALA   A C   
535  C  C   B ALA   A 21  ? 0.1956 0.2073 0.2194 -0.0141 0.0108  -0.0006 21  ALA   A C   
536  O  O   A ALA   A 21  ? 0.1702 0.1787 0.2140 0.0025  0.0463  0.0133  21  ALA   A O   
537  O  O   B ALA   A 21  ? 0.1956 0.2101 0.2157 -0.0179 0.0125  0.0060  21  ALA   A O   
538  C  CB  A ALA   A 21  ? 0.2059 0.1839 0.2270 -0.0137 0.0528  0.0147  21  ALA   A CB  
539  C  CB  B ALA   A 21  ? 0.1972 0.2122 0.2237 -0.0108 0.0151  -0.0075 21  ALA   A CB  
550  N  N   A ASP   A 22  ? 0.1746 0.1630 0.2346 -0.0099 0.0561  0.0199  22  ASP   A N   
551  N  N   B ASP   A 22  ? 0.1948 0.2031 0.2267 -0.0149 0.0030  0.0003  22  ASP   A N   
552  C  CA  A ASP   A 22  ? 0.1782 0.1689 0.2457 -0.0095 0.0390  0.0264  22  ASP   A CA  
553  C  CA  B ASP   A 22  ? 0.1923 0.2030 0.2312 -0.0150 -0.0022 0.0072  22  ASP   A CA  
554  C  C   A ASP   A 22  ? 0.1628 0.1819 0.2052 -0.0149 0.0479  0.0277  22  ASP   A C   
555  C  C   B ASP   A 22  ? 0.1854 0.2005 0.2038 -0.0238 0.0011  0.0108  22  ASP   A C   
556  O  O   A ASP   A 22  ? 0.1683 0.1988 0.2116 -0.0121 0.0581  0.0293  22  ASP   A O   
557  O  O   B ASP   A 22  ? 0.1816 0.2000 0.2067 -0.0334 0.0059  0.0172  22  ASP   A O   
558  C  CB  A ASP   A 22  ? 0.2017 0.1796 0.3341 -0.0079 0.0135  0.0213  22  ASP   A CB  
559  C  CB  B ASP   A 22  ? 0.1969 0.2055 0.2661 -0.0088 -0.0045 0.0114  22  ASP   A CB  
560  C  CG  A ASP   A 22  ? 0.2156 0.1935 0.4079 -0.0109 -0.0158 0.0372  22  ASP   A CG  
561  C  CG  B ASP   A 22  ? 0.1936 0.2070 0.2966 -0.0041 -0.0068 0.0162  22  ASP   A CG  
562  O  OD1 A ASP   A 22  ? 0.1988 0.1943 0.4426 -0.0245 -0.0386 0.0691  22  ASP   A OD1 
563  O  OD1 B ASP   A 22  ? 0.1956 0.2059 0.3150 0.0017  -0.0015 0.0212  22  ASP   A OD1 
564  O  OD2 A ASP   A 22  ? 0.2410 0.2059 0.4453 -0.0062 -0.0186 0.0191  22  ASP   A OD2 
565  O  OD2 B ASP   A 22  ? 0.1892 0.2117 0.3063 -0.0015 -0.0100 0.0167  22  ASP   A OD2 
574  N  N   A ILE   A 23  ? 0.1612 0.1802 0.1884 -0.0132 0.0394  0.0266  23  ILE   A N   
575  N  N   B ILE   A 23  ? 0.1870 0.2009 0.1881 -0.0176 0.0048  0.0104  23  ILE   A N   
576  C  CA  A ILE   A 23  ? 0.1615 0.1764 0.1731 -0.0158 0.0316  0.0315  23  ILE   A CA  
577  C  CA  B ILE   A 23  ? 0.1867 0.1965 0.1762 -0.0142 0.0164  0.0054  23  ILE   A CA  
578  C  C   A ILE   A 23  ? 0.1640 0.1867 0.1660 -0.0151 0.0419  0.0258  23  ILE   A C   
579  C  C   B ILE   A 23  ? 0.1896 0.1976 0.1805 -0.0121 0.0239  -0.0011 23  ILE   A C   
580  O  O   A ILE   A 23  ? 0.1670 0.1958 0.1610 -0.0149 0.0405  0.0186  23  ILE   A O   
581  O  O   B ILE   A 23  ? 0.1904 0.2011 0.1854 -0.0106 0.0241  -0.0047 23  ILE   A O   
582  C  CB  A ILE   A 23  ? 0.1660 0.1724 0.1483 -0.0068 0.0197  0.0294  23  ILE   A CB  
583  C  CB  B ILE   A 23  ? 0.1852 0.1938 0.1638 -0.0117 0.0164  0.0059  23  ILE   A CB  
584  C  CG1 A ILE   A 23  ? 0.1728 0.1718 0.1356 -0.0059 0.0150  0.0244  23  ILE   A CG1 
585  C  CG1 B ILE   A 23  ? 0.1858 0.1950 0.1552 -0.0063 0.0185  0.0042  23  ILE   A CG1 
586  C  CG2 A ILE   A 23  ? 0.1689 0.1710 0.1509 -0.0072 0.0262  0.0301  23  ILE   A CG2 
587  C  CG2 B ILE   A 23  ? 0.1828 0.1926 0.1634 -0.0141 0.0137  0.0140  23  ILE   A CG2 
588  C  CD1 A ILE   A 23  ? 0.1761 0.1663 0.1400 -0.0117 0.0017  0.0120  23  ILE   A CD1 
589  C  CD1 B ILE   A 23  ? 0.1869 0.1959 0.1527 -0.0008 0.0152  0.0050  23  ILE   A CD1 
612  N  N   A VAL   A 24  ? 0.1756 0.1935 0.1964 -0.0230 0.0469  0.0194  24  VAL   A N   
613  N  N   B VAL   A 24  ? 0.1949 0.1977 0.1855 -0.0128 0.0270  -0.0055 24  VAL   A N   
614  C  CA  A VAL   A 24  ? 0.1948 0.2046 0.2224 -0.0316 0.0506  0.0099  24  VAL   A CA  
615  C  CA  B VAL   A 24  ? 0.2021 0.2009 0.1943 -0.0172 0.0266  -0.0131 24  VAL   A CA  
616  C  C   A VAL   A 24  ? 0.2002 0.2173 0.2199 -0.0379 0.0559  -0.0027 24  VAL   A C   
617  C  C   B VAL   A 24  ? 0.2092 0.2087 0.1990 -0.0261 0.0299  -0.0125 24  VAL   A C   
618  O  O   A VAL   A 24  ? 0.2116 0.2175 0.2152 -0.0259 0.0536  -0.0179 24  VAL   A O   
619  O  O   B VAL   A 24  ? 0.2134 0.2072 0.1926 -0.0226 0.0297  -0.0197 24  VAL   A O   
620  C  CB  A VAL   A 24  ? 0.2044 0.2132 0.2547 -0.0338 0.0542  0.0149  24  VAL   A CB  
621  C  CB  B VAL   A 24  ? 0.2008 0.1992 0.1961 -0.0131 0.0266  -0.0212 24  VAL   A CB  
622  C  CG1 A VAL   A 24  ? 0.2133 0.2215 0.2842 -0.0321 0.0435  0.0075  24  VAL   A CG1 
623  C  CG1 B VAL   A 24  ? 0.2000 0.1985 0.1982 -0.0126 0.0299  -0.0253 24  VAL   A CG1 
624  C  CG2 A VAL   A 24  ? 0.2159 0.2243 0.2738 -0.0289 0.0715  0.0326  24  VAL   A CG2 
625  C  CG2 B VAL   A 24  ? 0.2040 0.2025 0.2021 -0.0101 0.0252  -0.0204 24  VAL   A CG2 
644  N  N   A GLU   A 25  ? 0.2063 0.2430 0.2295 -0.0422 0.0712  -0.0045 25  GLU   A N   
645  N  N   B GLU   A 25  ? 0.2155 0.2220 0.2130 -0.0358 0.0365  -0.0069 25  GLU   A N   
646  C  CA  A GLU   A 25  ? 0.2257 0.2709 0.2383 -0.0371 0.0786  -0.0167 25  GLU   A CA  
647  C  CA  B GLU   A 25  ? 0.2246 0.2362 0.2288 -0.0440 0.0413  -0.0051 25  GLU   A CA  
648  C  C   A GLU   A 25  ? 0.2134 0.2741 0.2079 -0.0515 0.0814  -0.0252 25  GLU   A C   
649  C  C   B GLU   A 25  ? 0.2214 0.2403 0.2139 -0.0479 0.0449  -0.0074 25  GLU   A C   
650  O  O   A GLU   A 25  ? 0.2203 0.2791 0.2133 -0.0566 0.0850  -0.0262 25  GLU   A O   
651  O  O   B GLU   A 25  ? 0.2245 0.2411 0.2141 -0.0500 0.0432  -0.0091 25  GLU   A O   
652  C  CB  A GLU   A 25  ? 0.2543 0.2980 0.2938 -0.0247 0.0901  -0.0154 25  GLU   A CB  
653  C  CB  B GLU   A 25  ? 0.2369 0.2446 0.2559 -0.0477 0.0442  -0.0004 25  GLU   A CB  
654  C  CG  A GLU   A 25  ? 0.2820 0.3218 0.3601 -0.0208 0.0774  -0.0181 25  GLU   A CG  
655  C  CG  B GLU   A 25  ? 0.2505 0.2546 0.2912 -0.0490 0.0412  0.0037  25  GLU   A CG  
656  C  CD  A GLU   A 25  ? 0.3022 0.3432 0.4247 -0.0165 0.0630  -0.0185 25  GLU   A CD  
657  C  CD  B GLU   A 25  ? 0.2582 0.2628 0.3190 -0.0521 0.0389  0.0065  25  GLU   A CD  
658  O  OE1 A GLU   A 25  ? 0.3115 0.3516 0.4367 -0.0130 0.0473  -0.0206 25  GLU   A OE1 
659  O  OE1 B GLU   A 25  ? 0.2607 0.2668 0.3226 -0.0495 0.0381  0.0053  25  GLU   A OE1 
660  O  OE2 A GLU   A 25  ? 0.3059 0.3493 0.4525 -0.0173 0.0648  -0.0233 25  GLU   A OE2 
661  O  OE2 B GLU   A 25  ? 0.2619 0.2634 0.3289 -0.0558 0.0417  0.0089  25  GLU   A OE2 
674  N  N   A GLU   A 26  ? 0.2028 0.2746 0.2055 -0.0605 0.0800  -0.0312 26  GLU   A N   
675  N  N   B GLU   A 26  ? 0.2157 0.2410 0.2040 -0.0514 0.0522  -0.0098 26  GLU   A N   
676  C  CA  A GLU   A 26  ? 0.2108 0.2733 0.1805 -0.0760 0.0629  -0.0249 26  GLU   A CA  
677  C  CA  B GLU   A 26  ? 0.2140 0.2397 0.1930 -0.0560 0.0523  -0.0120 26  GLU   A CA  
678  C  C   A GLU   A 26  ? 0.2110 0.2560 0.1494 -0.0705 0.0525  -0.0146 26  GLU   A C   
679  C  C   B GLU   A 26  ? 0.2086 0.2367 0.1662 -0.0615 0.0516  -0.0081 26  GLU   A C   
680  O  O   A GLU   A 26  ? 0.2205 0.2588 0.1500 -0.0740 0.0574  -0.0125 26  GLU   A O   
681  O  O   B GLU   A 26  ? 0.2102 0.2350 0.1598 -0.0604 0.0525  -0.0045 26  GLU   A O   
682  C  CB  A GLU   A 26  ? 0.2326 0.2862 0.2158 -0.0885 0.0578  -0.0101 26  GLU   A CB  
683  C  CB  B GLU   A 26  ? 0.2195 0.2376 0.2138 -0.0571 0.0504  -0.0144 26  GLU   A CB  
684  C  CG  A GLU   A 26  ? 0.2625 0.3096 0.2926 -0.0919 0.0546  -0.0075 26  GLU   A CG  
685  C  CG  B GLU   A 26  ? 0.2234 0.2358 0.2295 -0.0571 0.0642  -0.0197 26  GLU   A CG  
686  C  CD  A GLU   A 26  ? 0.2823 0.3263 0.3275 -0.0983 0.0653  -0.0076 26  GLU   A CD  
687  C  CD  B GLU   A 26  ? 0.2243 0.2337 0.2321 -0.0619 0.0870  -0.0254 26  GLU   A CD  
688  O  OE1 A GLU   A 26  ? 0.2821 0.3546 0.3253 -0.0821 0.0885  -0.0281 26  GLU   A OE1 
689  O  OE1 B GLU   A 26  ? 0.2177 0.2458 0.2302 -0.0500 0.0992  -0.0512 26  GLU   A OE1 
690  O  OE2 A GLU   A 26  ? 0.3070 0.3277 0.3583 -0.1007 0.0474  -0.0059 26  GLU   A OE2 
691  O  OE2 B GLU   A 26  ? 0.2288 0.2282 0.2175 -0.0692 0.1106  -0.0154 26  GLU   A OE2 
704  N  N   . ALA   A 27  ? 0.2007 0.2363 0.1518 -0.0691 0.0488  -0.0097 27  ALA   A N   
705  C  CA  . ALA   A 27  ? 0.2125 0.2474 0.1424 -0.0640 0.0455  -0.0058 27  ALA   A CA  
706  C  C   . ALA   A 27  ? 0.2519 0.2740 0.1560 -0.0762 0.0539  -0.0254 27  ALA   A C   
707  O  O   . ALA   A 27  ? 0.2571 0.2641 0.1562 -0.0819 0.0397  -0.0174 27  ALA   A O   
708  C  CB  . ALA   A 27  ? 0.1960 0.2350 0.1531 -0.0603 0.0342  -0.0036 27  ALA   A CB  
715  N  N   A LYS   A 28  ? 0.2796 0.2932 0.1679 -0.0719 0.0519  -0.0564 28  LYS   A N   
716  N  N   B LYS   A 28  ? 0.2823 0.3029 0.1936 -0.0702 0.0553  -0.0311 28  LYS   A N   
717  C  CA  A LYS   A 28  ? 0.3172 0.3236 0.2126 -0.0637 0.0503  -0.0727 28  LYS   A CA  
718  C  CA  B LYS   A 28  ? 0.3144 0.3341 0.2374 -0.0632 0.0553  -0.0337 28  LYS   A CA  
719  C  C   A LYS   A 28  ? 0.3360 0.3518 0.2054 -0.0684 0.0588  -0.0569 28  LYS   A C   
720  C  C   B LYS   A 28  ? 0.3318 0.3546 0.2274 -0.0674 0.0672  -0.0344 28  LYS   A C   
721  O  O   A LYS   A 28  ? 0.3471 0.3643 0.2487 -0.0676 0.0366  -0.0574 28  LYS   A O   
722  O  O   B LYS   A 28  ? 0.3375 0.3610 0.2464 -0.0652 0.0608  -0.0352 28  LYS   A O   
723  C  CB  A LYS   A 28  ? 0.3387 0.3322 0.2689 -0.0462 0.0423  -0.0949 28  LYS   A CB  
724  C  CB  B LYS   A 28  ? 0.3289 0.3453 0.2869 -0.0514 0.0427  -0.0339 28  LYS   A CB  
725  C  CG  A LYS   A 28  ? 0.3590 0.3404 0.3283 -0.0328 0.0333  -0.1029 28  LYS   A CG  
726  C  CG  B LYS   A 28  ? 0.3418 0.3542 0.3290 -0.0416 0.0313  -0.0322 28  LYS   A CG  
727  C  CD  A LYS   A 28  ? 0.3767 0.3550 0.4029 -0.0207 0.0227  -0.0949 28  LYS   A CD  
728  C  CD  B LYS   A 28  ? 0.3531 0.3626 0.3718 -0.0339 0.0213  -0.0293 28  LYS   A CD  
729  C  CE  A LYS   A 28  ? 0.3898 0.3666 0.4543 -0.0130 0.0173  -0.0941 28  LYS   A CE  
730  C  CE  B LYS   A 28  ? 0.3614 0.3683 0.3984 -0.0290 0.0150  -0.0288 28  LYS   A CE  
731  N  NZ  A LYS   A 28  ? 0.3972 0.3725 0.4886 -0.0080 0.0172  -0.1012 28  LYS   A NZ  
732  N  NZ  B LYS   A 28  ? 0.3663 0.3709 0.4163 -0.0261 0.0128  -0.0302 28  LYS   A NZ  
759  N  N   . LYS   A 29  ? 0.3414 0.3670 0.2022 -0.0749 0.0817  -0.0360 29  LYS   A N   
760  C  CA  . LYS   A 29  ? 0.3660 0.3999 0.2305 -0.0829 0.1003  -0.0229 29  LYS   A CA  
761  C  C   . LYS   A 29  ? 0.3605 0.3921 0.1903 -0.0973 0.0916  -0.0159 29  LYS   A C   
762  O  O   . LYS   A 29  ? 0.3737 0.4036 0.1911 -0.0919 0.0868  -0.0132 29  LYS   A O   
763  C  CB  . LYS   A 29  ? 0.3968 0.4421 0.3092 -0.0717 0.1163  -0.0152 29  LYS   A CB  
764  C  CG  . LYS   A 29  ? 0.4310 0.4813 0.4053 -0.0596 0.1111  -0.0091 29  LYS   A CG  
765  C  CD  . LYS   A 29  ? 0.4655 0.5152 0.5018 -0.0496 0.1022  -0.0079 29  LYS   A CD  
766  C  CE  . LYS   A 29  ? 0.4804 0.5418 0.5672 -0.0429 0.0983  -0.0127 29  LYS   A CE  
767  N  NZ  . LYS   A 29  ? 0.4951 0.5523 0.6094 -0.0386 0.0956  -0.0159 29  LYS   A NZ  
782  N  N   . VAL   A 30  ? 0.3407 0.3711 0.1703 -0.1140 0.0845  -0.0118 30  VAL   A N   
783  C  CA  . VAL   A 30  ? 0.3332 0.3528 0.1651 -0.1224 0.0533  0.0127  30  VAL   A CA  
784  C  C   . VAL   A 30  ? 0.3351 0.3377 0.1321 -0.1194 0.0350  0.0259  30  VAL   A C   
785  O  O   . VAL   A 30  ? 0.3432 0.3396 0.1315 -0.1175 0.0303  0.0302  30  VAL   A O   
786  C  CB  . VAL   A 30  ? 0.3278 0.3498 0.2035 -0.1364 0.0301  0.0157  30  VAL   A CB  
787  C  CG1 . VAL   A 30  ? 0.3282 0.3470 0.2239 -0.1389 0.0162  0.0216  30  VAL   A CG1 
788  C  CG2 . VAL   A 30  ? 0.3260 0.3536 0.2349 -0.1427 0.0330  0.0135  30  VAL   A CG2 
798  N  N   . LYS   A 31  ? 0.3277 0.3244 0.1193 -0.1204 0.0175  0.0205  31  LYS   A N   
799  C  CA  . LYS   A 31  ? 0.3415 0.3269 0.1399 -0.1080 -0.0085 0.0140  31  LYS   A CA  
800  C  C   . LYS   A 31  ? 0.3109 0.2983 0.1172 -0.0928 -0.0102 0.0539  31  LYS   A C   
801  O  O   . LYS   A 31  ? 0.3165 0.3096 0.1384 -0.0868 -0.0264 0.0695  31  LYS   A O   
802  C  CB  . LYS   A 31  ? 0.4060 0.3705 0.2709 -0.1026 -0.0277 -0.0047 31  LYS   A CB  
803  C  CG  . LYS   A 31  ? 0.4648 0.4154 0.4228 -0.0868 -0.0493 -0.0182 31  LYS   A CG  
804  C  CD  . LYS   A 31  ? 0.5136 0.4555 0.5371 -0.0718 -0.0648 -0.0284 31  LYS   A CD  
805  C  CE  . LYS   A 31  ? 0.5495 0.4929 0.6088 -0.0600 -0.0770 -0.0369 31  LYS   A CE  
806  N  NZ  . LYS   A 31  ? 0.5608 0.5059 0.6474 -0.0542 -0.0874 -0.0435 31  LYS   A NZ  
820  N  N   . PRO   A 32  ? 0.2714 0.2611 0.1044 -0.0837 -0.0064 0.0354  32  PRO   A N   
821  C  CA  . PRO   A 32  ? 0.2620 0.2415 0.1305 -0.0746 -0.0180 0.0451  32  PRO   A CA  
822  C  C   . PRO   A 32  ? 0.2578 0.2342 0.1364 -0.0609 -0.0291 0.0552  32  PRO   A C   
823  O  O   . PRO   A 32  ? 0.2520 0.2279 0.1498 -0.0632 -0.0394 0.0546  32  PRO   A O   
824  C  CB  . PRO   A 32  ? 0.2561 0.2479 0.1461 -0.0722 -0.0192 0.0413  32  PRO   A CB  
825  C  CG  . PRO   A 32  ? 0.2485 0.2537 0.0990 -0.0725 -0.0261 0.0354  32  PRO   A CG  
826  C  CD  . PRO   A 32  ? 0.2543 0.2539 0.1026 -0.0760 -0.0161 0.0359  32  PRO   A CD  
834  N  N   . THR   A 33  ? 0.2635 0.2309 0.1390 -0.0573 -0.0292 0.0524  33  THR   A N   
835  C  CA  . THR   A 33  ? 0.2590 0.2359 0.1522 -0.0441 -0.0394 0.0560  33  THR   A CA  
836  C  C   . THR   A 33  ? 0.2280 0.2169 0.1352 -0.0457 -0.0324 0.0460  33  THR   A C   
837  O  O   . THR   A 33  ? 0.2176 0.2163 0.1526 -0.0479 -0.0520 0.0476  33  THR   A O   
838  C  CB  . THR   A 33  ? 0.2826 0.2600 0.1691 -0.0356 -0.0484 0.0789  33  THR   A CB  
839  O  OG1 . THR   A 33  ? 0.3050 0.2756 0.2034 -0.0224 -0.0376 0.0919  33  THR   A OG1 
840  C  CG2 . THR   A 33  ? 0.2859 0.2684 0.1798 -0.0295 -0.0599 0.0820  33  THR   A CG2 
848  N  N   . VAL   A 34  ? 0.2021 0.1977 0.1263 -0.0427 -0.0215 0.0444  34  VAL   A N   
849  C  CA  . VAL   A 34  ? 0.1789 0.1829 0.1183 -0.0357 -0.0168 0.0368  34  VAL   A CA  
850  C  C   . VAL   A 34  ? 0.1694 0.1727 0.1049 -0.0318 -0.0020 0.0302  34  VAL   A C   
851  O  O   . VAL   A 34  ? 0.1684 0.1715 0.1421 -0.0385 -0.0014 0.0344  34  VAL   A O   
852  C  CB  . VAL   A 34  ? 0.1849 0.1788 0.1404 -0.0348 -0.0102 0.0247  34  VAL   A CB  
853  C  CG1 . VAL   A 34  ? 0.1900 0.1798 0.1412 -0.0309 -0.0010 0.0168  34  VAL   A CG1 
854  C  CG2 . VAL   A 34  ? 0.1879 0.1868 0.1737 -0.0236 -0.0234 0.0227  34  VAL   A CG2 
864  N  N   . VAL   A 35  ? 0.1555 0.1597 0.1082 -0.0309 -0.0074 0.0208  35  VAL   A N   
865  C  CA  . VAL   A 35  ? 0.1463 0.1524 0.1069 -0.0267 -0.0038 0.0163  35  VAL   A CA  
866  C  C   . VAL   A 35  ? 0.1373 0.1387 0.1042 -0.0180 -0.0007 0.0127  35  VAL   A C   
867  O  O   . VAL   A 35  ? 0.1293 0.1506 0.1274 -0.0248 0.0103  0.0131  35  VAL   A O   
868  C  CB  . VAL   A 35  ? 0.1510 0.1624 0.1185 -0.0163 0.0113  0.0086  35  VAL   A CB  
869  C  CG1 . VAL   A 35  ? 0.1571 0.1633 0.1282 -0.0121 0.0009  0.0055  35  VAL   A CG1 
870  C  CG2 . VAL   A 35  ? 0.1474 0.1626 0.1488 -0.0108 0.0158  0.0006  35  VAL   A CG2 
880  N  N   . VAL   A 36  ? 0.1284 0.1378 0.1107 -0.0234 0.0078  0.0195  36  VAL   A N   
881  C  CA  . VAL   A 36  ? 0.1236 0.1252 0.1136 -0.0144 0.0019  0.0103  36  VAL   A CA  
882  C  C   . VAL   A 36  ? 0.1206 0.1300 0.1166 -0.0157 0.0060  0.0091  36  VAL   A C   
883  O  O   . VAL   A 36  ? 0.1222 0.1296 0.1379 -0.0080 0.0164  0.0147  36  VAL   A O   
884  C  CB  . VAL   A 36  ? 0.1211 0.1212 0.1286 -0.0122 -0.0021 0.0105  36  VAL   A CB  
885  C  CG1 . VAL   A 36  ? 0.1324 0.1208 0.1351 -0.0133 0.0041  -0.0030 36  VAL   A CG1 
886  C  CG2 . VAL   A 36  ? 0.1320 0.1242 0.1491 -0.0134 -0.0010 0.0208  36  VAL   A CG2 
896  N  N   . ASN   A 37  ? 0.1104 0.1223 0.1156 -0.0068 0.0034  0.0153  37  ASN   A N   
897  C  CA  . ASN   A 37  ? 0.1147 0.1184 0.1102 -0.0019 0.0072  0.0183  37  ASN   A CA  
898  C  C   . ASN   A 37  ? 0.1132 0.1146 0.1143 -0.0027 0.0107  0.0178  37  ASN   A C   
899  O  O   . ASN   A 37  ? 0.1231 0.1246 0.1246 0.0041  0.0109  0.0077  37  ASN   A O   
900  C  CB  . ASN   A 37  ? 0.1162 0.1174 0.1201 -0.0017 0.0044  0.0072  37  ASN   A CB  
901  C  CG  . ASN   A 37  ? 0.1156 0.1171 0.1265 0.0010  0.0027  0.0120  37  ASN   A CG  
902  O  OD1 . ASN   A 37  ? 0.1149 0.1189 0.1514 0.0007  0.0056  0.0164  37  ASN   A OD1 
903  N  ND2 . ASN   A 37  ? 0.1162 0.1195 0.1340 -0.0023 -0.0040 0.0256  37  ASN   A ND2 
910  N  N   A ALA   A 38  ? 0.1125 0.1273 0.1218 -0.0006 0.0102  0.0097  38  ALA   A N   
911  N  N   B ALA   A 38  ? 0.1162 0.1243 0.1150 0.0001  0.0070  0.0109  38  ALA   A N   
912  C  CA  A ALA   A 38  ? 0.1232 0.1342 0.1199 -0.0022 0.0034  0.0105  38  ALA   A CA  
913  C  CA  B ALA   A 38  ? 0.1212 0.1316 0.1190 0.0004  -0.0010 0.0091  38  ALA   A CA  
914  C  C   A ALA   A 38  ? 0.1208 0.1266 0.1127 0.0025  -0.0041 0.0069  38  ALA   A C   
915  C  C   B ALA   A 38  ? 0.1204 0.1298 0.1219 0.0054  -0.0086 0.0030  38  ALA   A C   
916  O  O   A ALA   A 38  ? 0.1216 0.1258 0.1182 0.0061  -0.0039 0.0031  38  ALA   A O   
917  O  O   B ALA   A 38  ? 0.1188 0.1290 0.1291 0.0048  -0.0160 0.0089  38  ALA   A O   
918  C  CB  A ALA   A 38  ? 0.1301 0.1626 0.1358 -0.0152 0.0004  0.0047  38  ALA   A CB  
919  C  CB  B ALA   A 38  ? 0.1252 0.1431 0.1265 -0.0055 -0.0044 0.0056  38  ALA   A CB  
930  N  N   A ALA   A 39  ? 0.1199 0.1174 0.1202 0.0022  0.0035  0.0067  39  ALA   A N   
931  N  N   B ALA   A 39  ? 0.1231 0.1315 0.1270 0.0070  -0.0058 -0.0027 39  ALA   A N   
932  C  CA  A ALA   A 39  ? 0.1230 0.1179 0.1190 -0.0054 0.0078  0.0054  39  ALA   A CA  
933  C  CA  B ALA   A 39  ? 0.1263 0.1292 0.1221 0.0043  -0.0036 -0.0023 39  ALA   A CA  
934  C  C   A ALA   A 39  ? 0.1207 0.1167 0.1253 -0.0008 0.0076  0.0089  39  ALA   A C   
935  C  C   B ALA   A 39  ? 0.1280 0.1292 0.1148 -0.0005 -0.0039 0.0014  39  ALA   A C   
936  O  O   A ALA   A 39  ? 0.1316 0.1222 0.1337 -0.0069 0.0134  0.0131  39  ALA   A O   
937  O  O   B ALA   A 39  ? 0.1313 0.1303 0.1028 -0.0037 -0.0127 0.0014  39  ALA   A O   
938  C  CB  A ALA   A 39  ? 0.1297 0.1417 0.1243 -0.0080 -0.0034 0.0008  39  ALA   A CB  
939  C  CB  B ALA   A 39  ? 0.1274 0.1346 0.1255 0.0033  -0.0036 0.0006  39  ALA   A CB  
950  N  N   A ASN   A 40  ? 0.1280 0.1211 0.1243 -0.0068 0.0180  0.0068  40  ASN   A N   
951  N  N   B ASN   A 40  ? 0.1327 0.1323 0.1239 -0.0046 0.0029  0.0029  40  ASN   A N   
952  C  CA  A ASN   A 40  ? 0.1397 0.1177 0.1202 -0.0032 0.0087  0.0030  40  ASN   A CA  
953  C  CA  B ASN   A 40  ? 0.1391 0.1315 0.1268 -0.0050 0.0029  0.0065  40  ASN   A CA  
954  C  C   A ASN   A 40  ? 0.1408 0.1096 0.1141 -0.0059 0.0242  0.0101  40  ASN   A C   
955  C  C   B ASN   A 40  ? 0.1436 0.1283 0.1239 -0.0019 0.0088  0.0127  40  ASN   A C   
956  O  O   A ASN   A 40  ? 0.1377 0.1098 0.1193 -0.0096 0.0231  0.0152  40  ASN   A O   
957  O  O   B ASN   A 40  ? 0.1413 0.1268 0.1241 -0.0010 0.0080  0.0132  40  ASN   A O   
958  C  CB  A ASN   A 40  ? 0.1490 0.1240 0.1322 0.0068  0.0043  0.0057  40  ASN   A CB  
959  C  CB  B ASN   A 40  ? 0.1424 0.1348 0.1457 -0.0100 0.0005  0.0059  40  ASN   A CB  
960  C  CG  A ASN   A 40  ? 0.1443 0.1236 0.1449 0.0032  0.0089  0.0152  40  ASN   A CG  
961  C  CG  B ASN   A 40  ? 0.1446 0.1412 0.1676 -0.0154 -0.0038 0.0079  40  ASN   A CG  
962  O  OD1 A ASN   A 40  ? 0.1493 0.1178 0.1595 -0.0019 0.0161  0.0078  40  ASN   A OD1 
963  O  OD1 B ASN   A 40  ? 0.1436 0.1482 0.1817 -0.0091 -0.0084 0.0122  40  ASN   A OD1 
964  N  ND2 A ASN   A 40  ? 0.1396 0.1384 0.1892 0.0063  0.0026  -0.0020 40  ASN   A ND2 
965  N  ND2 B ASN   A 40  ? 0.1458 0.1398 0.1768 -0.0196 0.0059  0.0018  40  ASN   A ND2 
978  N  N   A VAL   A 41  ? 0.1426 0.1141 0.1127 -0.0029 0.0181  0.0135  41  VAL   A N   
979  N  N   B VAL   A 41  ? 0.1497 0.1302 0.1223 -0.0015 0.0113  0.0244  41  VAL   A N   
980  C  CA  A VAL   A 41  ? 0.1400 0.1238 0.1273 -0.0016 0.0194  0.0124  41  VAL   A CA  
981  C  CA  B VAL   A 41  ? 0.1504 0.1342 0.1161 -0.0028 0.0154  0.0268  41  VAL   A CA  
982  C  C   A VAL   A 41  ? 0.1340 0.1194 0.1397 -0.0017 0.0231  0.0151  41  VAL   A C   
983  C  C   B VAL   A 41  ? 0.1511 0.1362 0.1132 -0.0050 0.0201  0.0217  41  VAL   A C   
984  O  O   A VAL   A 41  ? 0.1396 0.1161 0.1598 0.0013  0.0140  0.0076  41  VAL   A O   
985  O  O   B VAL   A 41  ? 0.1527 0.1331 0.1041 -0.0054 0.0164  0.0068  41  VAL   A O   
986  C  CB  A VAL   A 41  ? 0.1497 0.1328 0.1276 -0.0032 0.0300  0.0080  41  VAL   A CB  
987  C  CB  B VAL   A 41  ? 0.1533 0.1357 0.1133 -0.0028 0.0231  0.0360  41  VAL   A CB  
988  C  CG1 A VAL   A 41  ? 0.1592 0.1439 0.1457 -0.0006 0.0245  0.0048  41  VAL   A CG1 
989  C  CG1 B VAL   A 41  ? 0.1582 0.1378 0.1139 -0.0046 0.0325  0.0293  41  VAL   A CG1 
990  C  CG2 A VAL   A 41  ? 0.1621 0.1405 0.1215 -0.0039 0.0387  0.0077  41  VAL   A CG2 
991  C  CG2 B VAL   A 41  ? 0.1544 0.1398 0.1237 -0.0000 0.0143  0.0324  41  VAL   A CG2 
1010 N  N   A TYR   A 42  ? 0.1266 0.1156 0.1692 -0.0030 0.0256  0.0197  42  TYR   A N   
1011 N  N   B TYR   A 42  ? 0.1494 0.1407 0.1227 -0.0033 0.0202  0.0276  42  TYR   A N   
1012 C  CA  A TYR   A 42  ? 0.1346 0.1109 0.1587 -0.0055 0.0281  0.0194  42  TYR   A CA  
1013 C  CA  B TYR   A 42  ? 0.1502 0.1458 0.1314 -0.0025 0.0248  0.0236  42  TYR   A CA  
1014 C  C   A TYR   A 42  ? 0.1225 0.1119 0.1566 -0.0049 0.0151  0.0208  42  TYR   A C   
1015 C  C   B TYR   A 42  ? 0.1463 0.1455 0.1282 -0.0007 0.0197  0.0314  42  TYR   A C   
1016 O  O   A TYR   A 42  ? 0.1255 0.1165 0.1691 -0.0152 0.0138  0.0015  42  TYR   A O   
1017 O  O   B TYR   A 42  ? 0.1461 0.1495 0.1382 -0.0038 0.0208  0.0296  42  TYR   A O   
1018 C  CB  A TYR   A 42  ? 0.1568 0.1204 0.1566 -0.0029 0.0323  0.0237  42  TYR   A CB  
1019 C  CB  B TYR   A 42  ? 0.1576 0.1539 0.1480 -0.0039 0.0223  0.0143  42  TYR   A CB  
1020 C  CG  A TYR   A 42  ? 0.1844 0.1351 0.1610 -0.0067 0.0287  0.0388  42  TYR   A CG  
1021 C  CG  B TYR   A 42  ? 0.1669 0.1646 0.1607 -0.0083 0.0194  0.0073  42  TYR   A CG  
1022 C  CD1 A TYR   A 42  ? 0.1937 0.1532 0.1662 -0.0119 0.0355  0.0397  42  TYR   A CD1 
1023 C  CD1 B TYR   A 42  ? 0.1731 0.1718 0.1710 -0.0094 0.0165  0.0020  42  TYR   A CD1 
1024 C  CD2 A TYR   A 42  ? 0.2036 0.1597 0.1753 -0.0040 0.0247  0.0331  42  TYR   A CD2 
1025 C  CD2 B TYR   A 42  ? 0.1704 0.1743 0.1644 -0.0103 0.0218  0.0029  42  TYR   A CD2 
1026 C  CE1 A TYR   A 42  ? 0.2050 0.1650 0.1563 -0.0206 0.0424  0.0322  42  TYR   A CE1 
1027 C  CE1 B TYR   A 42  ? 0.1795 0.1777 0.1749 -0.0126 0.0174  -0.0043 42  TYR   A CE1 
1028 C  CE2 A TYR   A 42  ? 0.2166 0.1740 0.1804 -0.0176 0.0332  0.0390  42  TYR   A CE2 
1029 C  CE2 B TYR   A 42  ? 0.1767 0.1821 0.1763 -0.0168 0.0197  0.0014  42  TYR   A CE2 
1030 C  CZ  A TYR   A 42  ? 0.2217 0.1767 0.1599 -0.0271 0.0424  0.0309  42  TYR   A CZ  
1031 C  CZ  B TYR   A 42  ? 0.1844 0.1841 0.1773 -0.0172 0.0207  -0.0036 42  TYR   A CZ  
1032 O  OH  A TYR   A 42  ? 0.2320 0.1985 0.1795 -0.0451 0.0378  0.0152  42  TYR   A OH  
1033 O  OH  B TYR   A 42  ? 0.1948 0.1942 0.1908 -0.0214 0.0183  -0.0075 42  TYR   A OH  
1052 N  N   A LEU   A 43  ? 0.1215 0.1104 0.1445 -0.0064 0.0104  0.0030  43  LEU   A N   
1053 N  N   B LEU   A 43  ? 0.1408 0.1400 0.1257 0.0030  0.0123  0.0292  43  LEU   A N   
1054 C  CA  A LEU   A 43  ? 0.1188 0.1113 0.1406 -0.0089 0.0104  0.0017  43  LEU   A CA  
1055 C  CA  B LEU   A 43  ? 0.1402 0.1359 0.1256 0.0004  0.0027  0.0216  43  LEU   A CA  
1056 C  C   A LEU   A 43  ? 0.1169 0.1175 0.1330 -0.0035 0.0108  0.0044  43  LEU   A C   
1057 C  C   B LEU   A 43  ? 0.1421 0.1378 0.1317 -0.0019 0.0027  0.0184  43  LEU   A C   
1058 O  O   A LEU   A 43  ? 0.1420 0.1217 0.1522 0.0049  -0.0048 0.0029  43  LEU   A O   
1059 O  O   B LEU   A 43  ? 0.1478 0.1383 0.1370 -0.0022 0.0019  0.0186  43  LEU   A O   
1060 C  CB  A LEU   A 43  ? 0.1275 0.1086 0.1489 -0.0077 0.0113  0.0032  43  LEU   A CB  
1061 C  CB  B LEU   A 43  ? 0.1366 0.1285 0.1287 0.0004  -0.0029 0.0223  43  LEU   A CB  
1062 C  CG  A LEU   A 43  ? 0.1339 0.1122 0.1491 -0.0034 0.0087  0.0024  43  LEU   A CG  
1063 C  CG  B LEU   A 43  ? 0.1332 0.1250 0.1228 0.0025  -0.0051 0.0181  43  LEU   A CG  
1064 C  CD1 A LEU   A 43  ? 0.1390 0.1196 0.1575 -0.0071 -0.0046 0.0029  43  LEU   A CD1 
1065 C  CD1 B LEU   A 43  ? 0.1338 0.1248 0.1211 0.0049  -0.0009 0.0169  43  LEU   A CD1 
1066 C  CD2 A LEU   A 43  ? 0.1428 0.1164 0.1563 -0.0062 0.0020  0.0099  43  LEU   A CD2 
1067 C  CD2 B LEU   A 43  ? 0.1363 0.1258 0.1228 -0.0010 -0.0053 0.0246  43  LEU   A CD2 
1090 N  N   A LYS   A 44  ? 0.1277 0.1184 0.1385 -0.0024 0.0089  0.0090  44  LYS   A N   
1091 N  N   B LYS   A 44  ? 0.1453 0.1385 0.1365 -0.0019 -0.0007 0.0174  44  LYS   A N   
1092 C  CA  A LYS   A 44  ? 0.1416 0.1174 0.1376 -0.0051 0.0198  0.0162  44  LYS   A CA  
1093 C  CA  B LYS   A 44  ? 0.1535 0.1407 0.1415 -0.0017 -0.0017 0.0174  44  LYS   A CA  
1094 C  C   A LYS   A 44  ? 0.1315 0.1159 0.1245 0.0014  0.0045  0.0141  44  LYS   A C   
1095 C  C   B LYS   A 44  ? 0.1488 0.1361 0.1247 0.0023  -0.0039 0.0088  44  LYS   A C   
1096 O  O   A LYS   A 44  ? 0.1356 0.1283 0.1447 0.0053  0.0024  0.0010  44  LYS   A O   
1097 O  O   B LYS   A 44  ? 0.1504 0.1391 0.1275 0.0040  -0.0044 -0.0023 44  LYS   A O   
1098 C  CB  A LYS   A 44  ? 0.1729 0.1322 0.1759 0.0029  0.0396  0.0276  44  LYS   A CB  
1099 C  CB  B LYS   A 44  ? 0.1663 0.1527 0.1676 -0.0027 0.0015  0.0252  44  LYS   A CB  
1100 C  CG  A LYS   A 44  ? 0.2025 0.1594 0.2348 0.0019  0.0651  0.0349  44  LYS   A CG  
1101 C  CG  B LYS   A 44  ? 0.1768 0.1621 0.1998 -0.0046 0.0040  0.0241  44  LYS   A CG  
1102 C  CD  A LYS   A 44  ? 0.2350 0.2166 0.3392 -0.0025 0.0633  0.0252  44  LYS   A CD  
1103 C  CD  B LYS   A 44  ? 0.1880 0.1755 0.2448 -0.0022 -0.0005 0.0158  44  LYS   A CD  
1104 C  CE  A LYS   A 44  ? 0.2490 0.2435 0.4066 0.0001  0.0557  0.0194  44  LYS   A CE  
1105 C  CE  B LYS   A 44  ? 0.1879 0.1747 0.2741 -0.0023 -0.0092 0.0166  44  LYS   A CE  
1106 N  NZ  A LYS   A 44  ? 0.2535 0.2616 0.4347 -0.0023 0.0461  0.0138  44  LYS   A NZ  
1107 N  NZ  B LYS   A 44  ? 0.1890 0.1744 0.2831 -0.0047 -0.0186 0.0238  44  LYS   A NZ  
1134 N  N   A HIS   A 45  ? 0.1204 0.1099 0.1286 -0.0016 0.0006  0.0153  45  HIS   A N   
1135 N  N   B HIS   A 45  ? 0.1461 0.1310 0.1243 0.0034  -0.0082 0.0077  45  HIS   A N   
1136 C  CA  A HIS   A 45  ? 0.1178 0.1183 0.1344 -0.0006 -0.0068 0.0046  45  HIS   A CA  
1137 C  CA  B HIS   A 45  ? 0.1406 0.1284 0.1266 0.0045  -0.0013 0.0062  45  HIS   A CA  
1138 C  C   A HIS   A 45  ? 0.1230 0.1279 0.1495 -0.0002 -0.0036 0.0088  45  HIS   A C   
1139 C  C   B HIS   A 45  ? 0.1386 0.1294 0.1294 0.0083  0.0052  0.0079  45  HIS   A C   
1140 O  O   A HIS   A 45  ? 0.1467 0.1430 0.1831 0.0207  -0.0116 -0.0056 45  HIS   A O   
1141 O  O   B HIS   A 45  ? 0.1436 0.1318 0.1390 0.0114  0.0088  0.0055  45  HIS   A O   
1142 C  CB  A HIS   A 45  ? 0.1153 0.1153 0.1277 -0.0050 -0.0050 0.0003  45  HIS   A CB  
1143 C  CB  B HIS   A 45  ? 0.1387 0.1221 0.1329 0.0052  0.0018  0.0049  45  HIS   A CB  
1144 C  CG  A HIS   A 45  ? 0.1145 0.1220 0.1231 -0.0059 -0.0041 0.0091  45  HIS   A CG  
1145 C  CG  B HIS   A 45  ? 0.1301 0.1106 0.1179 0.0012  0.0095  -0.0016 45  HIS   A CG  
1146 N  ND1 A HIS   A 45  ? 0.1137 0.1282 0.1395 -0.0048 -0.0040 0.0189  45  HIS   A ND1 
1147 N  ND1 B HIS   A 45  ? 0.1280 0.1076 0.1155 -0.0004 0.0092  -0.0046 45  HIS   A ND1 
1148 C  CD2 A HIS   A 45  ? 0.1127 0.1270 0.1375 -0.0126 -0.0101 0.0201  45  HIS   A CD2 
1149 C  CD2 B HIS   A 45  ? 0.1280 0.1138 0.1252 0.0020  0.0138  0.0064  45  HIS   A CD2 
1150 C  CE1 A HIS   A 45  ? 0.1141 0.1330 0.1231 -0.0063 -0.0049 0.0216  45  HIS   A CE1 
1151 C  CE1 B HIS   A 45  ? 0.1284 0.1124 0.1167 0.0007  0.0140  0.0039  45  HIS   A CE1 
1152 N  NE2 A HIS   A 45  ? 0.1148 0.1379 0.1326 -0.0081 -0.0061 0.0203  45  HIS   A NE2 
1153 N  NE2 B HIS   A 45  ? 0.1294 0.1168 0.1256 0.0023  0.0178  0.0064  45  HIS   A NE2 
1168 N  N   A GLY   A 46  ? 0.1359 0.1280 0.1558 0.0003  -0.0220 0.0065  46  GLY   A N   
1169 N  N   B GLY   A 46  ? 0.1422 0.1303 0.1271 0.0144  -0.0066 0.0049  46  GLY   A N   
1170 C  CA  A GLY   A 46  ? 0.1443 0.1299 0.1750 0.0044  -0.0229 0.0090  46  GLY   A CA  
1171 C  CA  B GLY   A 46  ? 0.1434 0.1263 0.1237 0.0152  -0.0172 0.0077  46  GLY   A CA  
1172 C  C   A GLY   A 46  ? 0.1477 0.1309 0.1890 0.0108  -0.0270 0.0215  46  GLY   A C   
1173 C  C   B GLY   A 46  ? 0.1432 0.1169 0.1183 0.0179  -0.0290 0.0067  46  GLY   A C   
1174 O  O   A GLY   A 46  ? 0.1521 0.1398 0.2248 0.0105  -0.0358 -0.0043 46  GLY   A O   
1175 O  O   B GLY   A 46  ? 0.1495 0.1153 0.1261 0.0271  -0.0324 0.0084  46  GLY   A O   
1182 N  N   A GLY   A 47  ? 0.1501 0.1359 0.1711 0.0148  -0.0276 0.0164  47  GLY   A N   
1183 N  N   B GLY   A 47  ? 0.1374 0.1160 0.1223 0.0144  -0.0364 -0.0007 47  GLY   A N   
1184 C  CA  A GLY   A 47  ? 0.1480 0.1375 0.1763 0.0096  -0.0421 0.0054  47  GLY   A CA  
1185 C  CA  B GLY   A 47  ? 0.1418 0.1245 0.1379 0.0097  -0.0440 -0.0133 47  GLY   A CA  
1186 C  C   A GLY   A 47  ? 0.1448 0.1254 0.1682 0.0097  -0.0459 -0.0038 47  GLY   A C   
1187 C  C   B GLY   A 47  ? 0.1419 0.1301 0.1443 0.0087  -0.0411 -0.0190 47  GLY   A C   
1188 O  O   A GLY   A 47  ? 0.1425 0.1247 0.1734 0.0178  -0.0421 0.0122  47  GLY   A O   
1189 O  O   B GLY   A 47  ? 0.1432 0.1342 0.1549 0.0150  -0.0338 -0.0122 47  GLY   A O   
1196 N  N   A GLY   A 48  ? 0.1423 0.1267 0.1882 0.0118  -0.0534 -0.0092 48  GLY   A N   
1197 N  N   B GLY   A 48  ? 0.1434 0.1354 0.1627 0.0038  -0.0372 -0.0221 48  GLY   A N   
1198 C  CA  A GLY   A 48  ? 0.1332 0.1236 0.2014 0.0085  -0.0417 -0.0107 48  GLY   A CA  
1199 C  CA  B GLY   A 48  ? 0.1394 0.1359 0.1611 0.0014  -0.0254 -0.0252 48  GLY   A CA  
1200 C  C   A GLY   A 48  ? 0.1225 0.1301 0.1855 0.0018  -0.0184 -0.0103 48  GLY   A C   
1201 C  C   B GLY   A 48  ? 0.1347 0.1363 0.1471 -0.0023 -0.0092 -0.0157 48  GLY   A C   
1202 O  O   A GLY   A 48  ? 0.1338 0.1324 0.1829 0.0024  -0.0121 -0.0154 48  GLY   A O   
1203 O  O   B GLY   A 48  ? 0.1388 0.1348 0.1403 0.0018  -0.0050 -0.0169 48  GLY   A O   
1210 N  N   A VAL   A 49  ? 0.1150 0.1224 0.1747 -0.0022 -0.0109 -0.0070 49  VAL   A N   
1211 N  N   B VAL   A 49  ? 0.1290 0.1334 0.1408 -0.0102 -0.0025 -0.0095 49  VAL   A N   
1212 C  CA  A VAL   A 49  ? 0.1286 0.1285 0.1647 -0.0018 0.0079  -0.0061 49  VAL   A CA  
1213 C  CA  B VAL   A 49  ? 0.1286 0.1281 0.1319 -0.0163 0.0063  -0.0031 49  VAL   A CA  
1214 C  C   A VAL   A 49  ? 0.1233 0.1177 0.1374 0.0057  0.0057  -0.0013 49  VAL   A C   
1215 C  C   B VAL   A 49  ? 0.1156 0.1167 0.1151 -0.0035 0.0077  0.0032  49  VAL   A C   
1216 O  O   A VAL   A 49  ? 0.1336 0.1196 0.1360 -0.0024 0.0164  -0.0044 49  VAL   A O   
1217 O  O   B VAL   A 49  ? 0.1111 0.1093 0.1069 -0.0001 0.0085  0.0004  49  VAL   A O   
1218 C  CB  A VAL   A 49  ? 0.1496 0.1271 0.1670 -0.0038 0.0022  -0.0015 49  VAL   A CB  
1219 C  CB  B VAL   A 49  ? 0.1431 0.1274 0.1329 -0.0313 0.0066  -0.0107 49  VAL   A CB  
1220 C  CG1 A VAL   A 49  ? 0.1591 0.1202 0.1695 -0.0014 -0.0135 0.0077  49  VAL   A CG1 
1221 C  CG1 B VAL   A 49  ? 0.1502 0.1275 0.1334 -0.0350 0.0071  -0.0156 49  VAL   A CG1 
1222 C  CG2 A VAL   A 49  ? 0.1666 0.1413 0.2088 -0.0212 -0.0055 0.0038  49  VAL   A CG2 
1223 C  CG2 B VAL   A 49  ? 0.1484 0.1276 0.1318 -0.0422 0.0087  -0.0137 49  VAL   A CG2 
1242 N  N   A ALA   A 50  ? 0.1210 0.1175 0.1321 0.0006  -0.0081 0.0047  50  ALA   A N   
1243 N  N   B ALA   A 50  ? 0.1126 0.1178 0.1114 -0.0005 0.0048  0.0057  50  ALA   A N   
1244 C  CA  A ALA   A 50  ? 0.1152 0.1156 0.1288 -0.0042 -0.0040 0.0056  50  ALA   A CA  
1245 C  CA  B ALA   A 50  ? 0.1132 0.1185 0.1190 -0.0006 0.0012  0.0050  50  ALA   A CA  
1246 C  C   A ALA   A 50  ? 0.1108 0.1195 0.1171 -0.0042 -0.0032 0.0006  50  ALA   A C   
1247 C  C   B ALA   A 50  ? 0.1137 0.1184 0.1219 0.0017  -0.0038 0.0021  50  ALA   A C   
1248 O  O   A ALA   A 50  ? 0.1140 0.1232 0.1355 -0.0025 -0.0037 0.0010  50  ALA   A O   
1249 O  O   B ALA   A 50  ? 0.1135 0.1185 0.1261 0.0039  -0.0040 0.0019  50  ALA   A O   
1250 C  CB  A ALA   A 50  ? 0.1150 0.1180 0.1171 -0.0059 -0.0011 0.0043  50  ALA   A CB  
1251 C  CB  B ALA   A 50  ? 0.1136 0.1216 0.1195 -0.0009 0.0056  -0.0002 50  ALA   A CB  
1262 N  N   . GLY   A 51  ? 0.1180 0.1183 0.1356 0.0029  -0.0102 -0.0014 51  GLY   A N   
1263 C  CA  . GLY   A 51  ? 0.1318 0.1153 0.1402 0.0052  -0.0166 -0.0032 51  GLY   A CA  
1264 C  C   . GLY   A 51  ? 0.1167 0.1196 0.1446 0.0038  -0.0092 -0.0062 51  GLY   A C   
1265 O  O   . GLY   A 51  ? 0.1208 0.1311 0.1564 0.0007  -0.0115 -0.0115 51  GLY   A O   
1270 N  N   . ALA   A 52  ? 0.1164 0.1308 0.1391 0.0038  -0.0038 -0.0191 52  ALA   A N   
1271 C  CA  . ALA   A 52  ? 0.1182 0.1397 0.1520 -0.0011 0.0011  -0.0156 52  ALA   A CA  
1272 C  C   . ALA   A 52  ? 0.1183 0.1403 0.1260 -0.0107 0.0062  -0.0080 52  ALA   A C   
1273 O  O   . ALA   A 52  ? 0.1258 0.1474 0.1429 -0.0048 0.0081  -0.0173 52  ALA   A O   
1274 C  CB  . ALA   A 52  ? 0.1281 0.1711 0.1717 -0.0091 0.0021  -0.0094 52  ALA   A CB  
1280 N  N   A LEU   A 53  ? 0.1157 0.1387 0.1258 -0.0080 0.0044  -0.0099 53  LEU   A N   
1281 N  N   B LEU   A 53  ? 0.1209 0.1382 0.1222 -0.0066 0.0063  -0.0032 53  LEU   A N   
1282 C  CA  A LEU   A 53  ? 0.1262 0.1391 0.1194 -0.0075 0.0006  -0.0012 53  LEU   A CA  
1283 C  CA  B LEU   A 53  ? 0.1266 0.1366 0.1211 -0.0027 0.0074  0.0028  53  LEU   A CA  
1284 C  C   A LEU   A 53  ? 0.1265 0.1391 0.1120 0.0008  0.0043  -0.0014 53  LEU   A C   
1285 C  C   B LEU   A 53  ? 0.1228 0.1354 0.1151 0.0001  0.0075  0.0021  53  LEU   A C   
1286 O  O   A LEU   A 53  ? 0.1374 0.1448 0.1241 -0.0103 -0.0015 -0.0010 53  LEU   A O   
1287 O  O   B LEU   A 53  ? 0.1228 0.1338 0.1191 -0.0039 0.0097  0.0036  53  LEU   A O   
1288 C  CB  A LEU   A 53  ? 0.1322 0.1425 0.1270 -0.0136 0.0013  0.0013  53  LEU   A CB  
1289 C  CB  B LEU   A 53  ? 0.1346 0.1359 0.1310 -0.0016 0.0099  0.0043  53  LEU   A CB  
1290 C  CG  A LEU   A 53  ? 0.1522 0.1479 0.1229 -0.0207 -0.0010 -0.0020 53  LEU   A CG  
1291 C  CG  B LEU   A 53  ? 0.1444 0.1356 0.1362 -0.0021 0.0139  0.0035  53  LEU   A CG  
1292 C  CD1 A LEU   A 53  ? 0.1641 0.1537 0.1298 -0.0122 -0.0031 -0.0027 53  LEU   A CD1 
1293 C  CD1 B LEU   A 53  ? 0.1465 0.1372 0.1382 0.0034  0.0104  0.0079  53  LEU   A CD1 
1294 C  CD2 A LEU   A 53  ? 0.1775 0.1625 0.1487 -0.0336 0.0131  -0.0000 53  LEU   A CD2 
1295 C  CD2 B LEU   A 53  ? 0.1553 0.1402 0.1438 -0.0055 0.0195  -0.0006 53  LEU   A CD2 
1318 N  N   . ASN   A 54  ? 0.1189 0.1336 0.1138 0.0001  -0.0003 0.0004  54  ASN   A N   
1319 C  CA  . ASN   A 54  ? 0.1105 0.1290 0.1281 -0.0044 -0.0075 -0.0020 54  ASN   A CA  
1320 C  C   . ASN   A 54  ? 0.1220 0.1348 0.1289 -0.0113 0.0001  -0.0017 54  ASN   A C   
1321 O  O   . ASN   A 54  ? 0.1249 0.1405 0.1325 -0.0055 -0.0070 -0.0149 54  ASN   A O   
1322 C  CB  . ASN   A 54  ? 0.1067 0.1265 0.1424 -0.0080 -0.0097 -0.0014 54  ASN   A CB  
1323 C  CG  . ASN   A 54  ? 0.1113 0.1293 0.1378 0.0004  -0.0041 0.0050  54  ASN   A CG  
1324 O  OD1 . ASN   A 54  ? 0.1121 0.1307 0.1436 -0.0040 -0.0082 0.0040  54  ASN   A OD1 
1325 N  ND2 . ASN   A 54  ? 0.1231 0.1348 0.1559 -0.0097 -0.0142 0.0108  54  ASN   A ND2 
1333 N  N   A LYS   A 55  ? 0.1172 0.1372 0.1397 -0.0020 -0.0043 -0.0105 55  LYS   A N   
1334 N  N   B LYS   A 55  ? 0.1251 0.1422 0.1307 -0.0061 0.0005  -0.0072 55  LYS   A N   
1335 C  CA  A LYS   A 55  ? 0.1259 0.1410 0.1418 0.0017  -0.0075 -0.0117 55  LYS   A CA  
1336 C  CA  B LYS   A 55  ? 0.1311 0.1492 0.1363 -0.0030 0.0009  -0.0115 55  LYS   A CA  
1337 C  C   A LYS   A 55  ? 0.1250 0.1503 0.1454 -0.0038 -0.0023 -0.0202 55  LYS   A C   
1338 C  C   B LYS   A 55  ? 0.1318 0.1549 0.1394 -0.0049 0.0008  -0.0183 55  LYS   A C   
1339 O  O   A LYS   A 55  ? 0.1363 0.1618 0.1507 0.0031  -0.0032 -0.0333 55  LYS   A O   
1340 O  O   B LYS   A 55  ? 0.1378 0.1588 0.1405 -0.0004 -0.0006 -0.0242 55  LYS   A O   
1341 C  CB  A LYS   A 55  ? 0.1312 0.1431 0.1599 0.0119  -0.0109 -0.0184 55  LYS   A CB  
1342 C  CB  B LYS   A 55  ? 0.1336 0.1514 0.1500 0.0007  0.0027  -0.0125 55  LYS   A CB  
1343 C  CG  A LYS   A 55  ? 0.1450 0.1631 0.1696 0.0142  -0.0125 -0.0145 55  LYS   A CG  
1344 C  CG  B LYS   A 55  ? 0.1361 0.1594 0.1629 0.0032  0.0047  -0.0169 55  LYS   A CG  
1345 C  CD  A LYS   A 55  ? 0.1560 0.1838 0.1862 0.0232  -0.0027 -0.0094 55  LYS   A CD  
1346 C  CD  B LYS   A 55  ? 0.1432 0.1639 0.1785 0.0055  0.0078  -0.0200 55  LYS   A CD  
1347 C  CE  A LYS   A 55  ? 0.1679 0.2054 0.2054 0.0237  -0.0165 -0.0120 55  LYS   A CE  
1348 C  CE  B LYS   A 55  ? 0.1552 0.1716 0.1954 0.0063  0.0081  -0.0212 55  LYS   A CE  
1349 N  NZ  A LYS   A 55  ? 0.1735 0.2094 0.2066 0.0307  -0.0272 -0.0076 55  LYS   A NZ  
1350 N  NZ  B LYS   A 55  ? 0.1589 0.1760 0.1993 0.0100  0.0083  -0.0223 55  LYS   A NZ  
1377 N  N   . ALA   A 56  ? 0.1290 0.1589 0.1410 -0.0105 0.0032  -0.0204 56  ALA   A N   
1378 C  CA  . ALA   A 56  ? 0.1450 0.1785 0.1459 -0.0130 0.0112  -0.0267 56  ALA   A CA  
1379 C  C   . ALA   A 56  ? 0.1482 0.1886 0.1236 -0.0118 0.0108  -0.0290 56  ALA   A C   
1380 O  O   . ALA   A 56  ? 0.1551 0.2172 0.1356 0.0008  0.0169  -0.0228 56  ALA   A O   
1381 C  CB  . ALA   A 56  ? 0.1514 0.1957 0.1539 -0.0210 0.0150  -0.0074 56  ALA   A CB  
1388 N  N   . THR   A 57  ? 0.1349 0.1634 0.1215 -0.0131 0.0053  -0.0195 57  THR   A N   
1389 C  CA  . THR   A 57  ? 0.1410 0.1629 0.1217 -0.0115 -0.0010 -0.0164 57  THR   A CA  
1390 C  C   . THR   A 57  ? 0.1394 0.1666 0.1393 -0.0070 -0.0077 -0.0207 57  THR   A C   
1391 O  O   . THR   A 57  ? 0.1338 0.1666 0.1524 -0.0085 -0.0131 -0.0295 57  THR   A O   
1392 C  CB  . THR   A 57  ? 0.1370 0.1636 0.1290 -0.0091 -0.0047 -0.0137 57  THR   A CB  
1393 O  OG1 . THR   A 57  ? 0.1260 0.1554 0.1337 -0.0070 -0.0025 -0.0092 57  THR   A OG1 
1394 C  CG2 . THR   A 57  ? 0.1386 0.1645 0.1239 -0.0114 -0.0015 -0.0048 57  THR   A CG2 
1402 N  N   A ASN   A 58  ? 0.1388 0.1668 0.1540 -0.0085 -0.0027 -0.0281 58  ASN   A N   
1403 N  N   B ASN   A 58  ? 0.1378 0.1598 0.1389 -0.0047 -0.0011 -0.0269 58  ASN   A N   
1404 C  CA  A ASN   A 58  ? 0.1545 0.1627 0.1835 -0.0125 0.0007  -0.0294 58  ASN   A CA  
1405 C  CA  B ASN   A 58  ? 0.1420 0.1515 0.1481 -0.0035 0.0047  -0.0319 58  ASN   A CA  
1406 C  C   A ASN   A 58  ? 0.1392 0.1441 0.1746 -0.0034 -0.0054 -0.0214 58  ASN   A C   
1407 C  C   B ASN   A 58  ? 0.1335 0.1425 0.1476 -0.0031 -0.0048 -0.0215 58  ASN   A C   
1408 O  O   A ASN   A 58  ? 0.1448 0.1495 0.1852 -0.0151 -0.0051 -0.0227 58  ASN   A O   
1409 O  O   B ASN   A 58  ? 0.1361 0.1465 0.1489 -0.0074 -0.0076 -0.0179 58  ASN   A O   
1410 C  CB  A ASN   A 58  ? 0.1800 0.1838 0.2230 -0.0134 0.0115  -0.0338 58  ASN   A CB  
1411 C  CB  B ASN   A 58  ? 0.1536 0.1535 0.1602 -0.0002 0.0224  -0.0466 58  ASN   A CB  
1412 C  CG  A ASN   A 58  ? 0.1856 0.1955 0.2635 0.0029  -0.0091 -0.0279 58  ASN   A CG  
1413 C  CG  B ASN   A 58  ? 0.1629 0.1567 0.1902 0.0046  0.0241  -0.0467 58  ASN   A CG  
1414 O  OD1 A ASN   A 58  ? 0.1938 0.1998 0.2894 0.0261  -0.0113 -0.0037 58  ASN   A OD1 
1415 O  OD1 B ASN   A 58  ? 0.1597 0.1546 0.2090 0.0100  0.0322  -0.0502 58  ASN   A OD1 
1416 N  ND2 A ASN   A 58  ? 0.1891 0.1967 0.2769 0.0005  -0.0222 -0.0411 58  ASN   A ND2 
1417 N  ND2 B ASN   A 58  ? 0.1715 0.1633 0.2033 -0.0011 0.0178  -0.0455 58  ASN   A ND2 
1430 N  N   . ASN   A 59  ? 0.1251 0.1333 0.1527 -0.0069 -0.0101 -0.0176 59  ASN   A N   
1431 C  CA  . ASN   A 59  ? 0.1295 0.1270 0.1497 -0.0035 -0.0085 -0.0122 59  ASN   A CA  
1432 C  C   . ASN   A 59  ? 0.1313 0.1303 0.1343 -0.0043 -0.0062 -0.0112 59  ASN   A C   
1433 O  O   . ASN   A 59  ? 0.1257 0.1331 0.1426 -0.0064 -0.0023 -0.0012 59  ASN   A O   
1434 C  CB  . ASN   A 59  ? 0.1326 0.1276 0.1591 0.0031  -0.0174 -0.0166 59  ASN   A CB  
1435 C  CG  . ASN   A 59  ? 0.1327 0.1276 0.1613 -0.0002 -0.0264 -0.0018 59  ASN   A CG  
1436 O  OD1 . ASN   A 59  ? 0.1417 0.1406 0.1470 -0.0112 -0.0257 0.0050  59  ASN   A OD1 
1437 N  ND2 . ASN   A 59  ? 0.1403 0.1321 0.1649 -0.0123 -0.0178 0.0007  59  ASN   A ND2 
1445 N  N   . ALA   A 60  ? 0.1213 0.1301 0.1398 -0.0036 -0.0046 -0.0055 60  ALA   A N   
1446 C  CA  . ALA   A 60  ? 0.1210 0.1337 0.1405 -0.0042 -0.0101 -0.0015 60  ALA   A CA  
1447 C  C   . ALA   A 60  ? 0.1218 0.1324 0.1465 -0.0033 -0.0063 -0.0039 60  ALA   A C   
1448 O  O   . ALA   A 60  ? 0.1199 0.1316 0.1657 -0.0044 -0.0071 -0.0089 60  ALA   A O   
1449 C  CB  . ALA   A 60  ? 0.1333 0.1439 0.1524 -0.0016 -0.0114 -0.0168 60  ALA   A CB  
1455 N  N   . MET   A 61  ? 0.1199 0.1295 0.1416 -0.0071 -0.0036 -0.0060 61  MET   A N   
1456 C  CA  . MET   A 61  ? 0.1222 0.1244 0.1336 -0.0066 -0.0006 -0.0013 61  MET   A CA  
1457 C  C   . MET   A 61  ? 0.1155 0.1214 0.1411 -0.0053 -0.0044 -0.0010 61  MET   A C   
1458 O  O   . MET   A 61  ? 0.1225 0.1210 0.1487 -0.0031 0.0079  0.0062  61  MET   A O   
1459 C  CB  . MET   A 61  ? 0.1230 0.1262 0.1254 -0.0065 0.0004  -0.0031 61  MET   A CB  
1460 C  CG  . MET   A 61  ? 0.1185 0.1325 0.1472 -0.0045 0.0019  -0.0057 61  MET   A CG  
1461 S  SD  . MET   A 61  ? 0.1262 0.1315 0.1793 -0.0110 -0.0019 -0.0177 61  MET   A SD  
1462 C  CE  . MET   A 61  ? 0.1469 0.1441 0.1973 -0.0150 0.0172  -0.0129 61  MET   A CE  
1472 N  N   . GLN   A 62  ? 0.1154 0.1217 0.1391 -0.0090 -0.0038 -0.0056 62  GLN   A N   
1473 C  CA  . GLN   A 62  ? 0.1213 0.1156 0.1472 -0.0046 0.0013  0.0014  62  GLN   A CA  
1474 C  C   . GLN   A 62  ? 0.1188 0.1092 0.1549 -0.0008 0.0057  0.0016  62  GLN   A C   
1475 O  O   . GLN   A 62  ? 0.1227 0.1267 0.1567 -0.0006 0.0037  0.0040  62  GLN   A O   
1476 C  CB  . GLN   A 62  ? 0.1175 0.1194 0.1584 -0.0027 0.0003  0.0003  62  GLN   A CB  
1477 C  CG  . GLN   A 62  ? 0.1275 0.1143 0.1422 -0.0059 -0.0052 0.0149  62  GLN   A CG  
1478 C  CD  . GLN   A 62  ? 0.1316 0.1220 0.1420 -0.0002 0.0055  0.0135  62  GLN   A CD  
1479 O  OE1 . GLN   A 62  ? 0.1328 0.1296 0.1588 -0.0037 0.0016  0.0024  62  GLN   A OE1 
1480 N  NE2 . GLN   A 62  ? 0.1356 0.1316 0.1526 0.0011  0.0011  -0.0033 62  GLN   A NE2 
1489 N  N   . VAL   A 63  ? 0.1168 0.1217 0.1661 -0.0064 0.0067  -0.0150 63  VAL   A N   
1490 C  CA  . VAL   A 63  ? 0.1206 0.1313 0.1893 -0.0122 0.0017  -0.0112 63  VAL   A CA  
1491 C  C   . VAL   A 63  ? 0.1110 0.1304 0.1778 -0.0094 -0.0051 -0.0134 63  VAL   A C   
1492 O  O   . VAL   A 63  ? 0.1159 0.1317 0.1871 -0.0133 -0.0019 -0.0085 63  VAL   A O   
1493 C  CB  . VAL   A 63  ? 0.1277 0.1482 0.2179 -0.0130 -0.0083 -0.0358 63  VAL   A CB  
1494 C  CG1 . VAL   A 63  ? 0.1506 0.1694 0.2581 -0.0112 -0.0098 -0.0603 63  VAL   A CG1 
1495 C  CG2 . VAL   A 63  ? 0.1412 0.1420 0.2220 -0.0137 0.0077  -0.0323 63  VAL   A CG2 
1505 N  N   . GLU   A 64  ? 0.1162 0.1342 0.1631 -0.0028 -0.0010 -0.0077 64  GLU   A N   
1506 C  CA  . GLU   A 64  ? 0.1136 0.1345 0.1673 -0.0066 -0.0042 0.0032  64  GLU   A CA  
1507 C  C   . GLU   A 64  ? 0.1118 0.1285 0.1612 -0.0102 0.0016  0.0045  64  GLU   A C   
1508 O  O   . GLU   A 64  ? 0.1199 0.1352 0.1615 -0.0012 0.0012  -0.0019 64  GLU   A O   
1509 C  CB  . GLU   A 64  ? 0.1212 0.1432 0.1647 -0.0075 0.0023  -0.0047 64  GLU   A CB  
1510 C  CG  . GLU   A 64  ? 0.1340 0.1474 0.1743 -0.0128 0.0018  0.0021  64  GLU   A CG  
1511 C  CD  . GLU   A 64  ? 0.1475 0.1537 0.1789 -0.0125 0.0093  -0.0006 64  GLU   A CD  
1512 O  OE1 . GLU   A 64  ? 0.1421 0.1685 0.2065 -0.0189 0.0148  0.0025  64  GLU   A OE1 
1513 O  OE2 . GLU   A 64  ? 0.1657 0.1551 0.1637 -0.0248 -0.0019 0.0034  64  GLU   A OE2 
1520 N  N   . SER   A 65  ? 0.1089 0.1260 0.1493 0.0008  0.0014  0.0045  65  SER   A N   
1521 C  CA  . SER   A 65  ? 0.1187 0.1193 0.1465 -0.0025 -0.0017 -0.0004 65  SER   A CA  
1522 C  C   . SER   A 65  ? 0.1194 0.1279 0.1508 -0.0041 -0.0021 -0.0020 65  SER   A C   
1523 O  O   . SER   A 65  ? 0.1272 0.1337 0.1685 0.0005  0.0122  -0.0050 65  SER   A O   
1524 C  CB  . SER   A 65  ? 0.1185 0.1234 0.1394 -0.0076 0.0024  0.0088  65  SER   A CB  
1525 O  OG  . SER   A 65  ? 0.1185 0.1396 0.1524 -0.0077 -0.0060 0.0087  65  SER   A OG  
1531 N  N   . ASP   A 66  ? 0.1200 0.1254 0.1563 -0.0068 0.0115  0.0018  66  ASP   A N   
1532 C  CA  . ASP   A 66  ? 0.1300 0.1355 0.1766 -0.0010 0.0103  0.0123  66  ASP   A CA  
1533 C  C   . ASP   A 66  ? 0.1247 0.1311 0.1797 -0.0063 0.0078  0.0183  66  ASP   A C   
1534 O  O   . ASP   A 66  ? 0.1306 0.1438 0.1955 -0.0032 0.0231  0.0210  66  ASP   A O   
1535 C  CB  . ASP   A 66  ? 0.1366 0.1397 0.2009 0.0058  0.0109  0.0250  66  ASP   A CB  
1536 C  CG  . ASP   A 66  ? 0.1605 0.1551 0.2230 0.0007  -0.0007 0.0405  66  ASP   A CG  
1537 O  OD1 . ASP   A 66  ? 0.1564 0.1876 0.2019 -0.0043 -0.0018 0.0467  66  ASP   A OD1 
1538 O  OD2 . ASP   A 66  ? 0.1775 0.1624 0.3040 0.0149  -0.0154 0.0199  66  ASP   A OD2 
1543 N  N   . ASP   A 67  ? 0.1213 0.1339 0.1916 -0.0040 0.0098  0.0147  67  ASP   A N   
1544 C  CA  . ASP   A 67  ? 0.1206 0.1480 0.2022 -0.0035 0.0053  0.0263  67  ASP   A CA  
1545 C  C   . ASP   A 67  ? 0.1241 0.1488 0.1974 0.0018  0.0151  0.0265  67  ASP   A C   
1546 O  O   . ASP   A 67  ? 0.1233 0.1586 0.2134 0.0037  0.0296  0.0338  67  ASP   A O   
1547 C  CB  . ASP   A 67  ? 0.1329 0.1609 0.2305 -0.0038 -0.0144 0.0330  67  ASP   A CB  
1548 C  CG  . ASP   A 67  ? 0.1282 0.1720 0.2702 -0.0019 -0.0279 0.0390  67  ASP   A CG  
1549 O  OD1 . ASP   A 67  ? 0.1365 0.1895 0.3492 -0.0075 -0.0356 0.0470  67  ASP   A OD1 
1550 O  OD2 . ASP   A 67  ? 0.1330 0.1792 0.2488 0.0041  -0.0144 0.0243  67  ASP   A OD2 
1555 N  N   . TYR   A 68  ? 0.1261 0.1370 0.1857 0.0021  0.0172  0.0249  68  TYR   A N   
1556 C  CA  . TYR   A 68  ? 0.1381 0.1367 0.1880 0.0023  0.0259  0.0255  68  TYR   A CA  
1557 C  C   . TYR   A 68  ? 0.1301 0.1314 0.1832 -0.0020 0.0243  0.0186  68  TYR   A C   
1558 O  O   . TYR   A 68  ? 0.1362 0.1405 0.1928 0.0081  0.0294  0.0189  68  TYR   A O   
1559 C  CB  . TYR   A 68  ? 0.1444 0.1301 0.2005 0.0127  0.0418  0.0278  68  TYR   A CB  
1560 C  CG  . TYR   A 68  ? 0.1483 0.1501 0.2204 0.0067  0.0562  0.0304  68  TYR   A CG  
1561 C  CD1 . TYR   A 68  ? 0.1565 0.1584 0.2489 -0.0195 0.0437  -0.0063 68  TYR   A CD1 
1562 C  CD2 . TYR   A 68  ? 0.1662 0.1523 0.2652 0.0100  0.0602  0.0319  68  TYR   A CD2 
1563 C  CE1 . TYR   A 68  ? 0.1645 0.1695 0.2888 -0.0172 0.0510  -0.0128 68  TYR   A CE1 
1564 C  CE2 . TYR   A 68  ? 0.1641 0.1608 0.2829 0.0011  0.0683  0.0104  68  TYR   A CE2 
1565 C  CZ  . TYR   A 68  ? 0.1641 0.1630 0.2955 -0.0184 0.0534  -0.0135 68  TYR   A CZ  
1566 O  OH  . TYR   A 68  ? 0.1870 0.1618 0.3158 -0.0154 0.0227  -0.0288 68  TYR   A OH  
1576 N  N   . ILE   A 69  ? 0.1233 0.1287 0.1816 0.0013  0.0159  0.0214  69  ILE   A N   
1577 C  CA  . ILE   A 69  ? 0.1336 0.1321 0.1652 0.0033  0.0132  0.0064  69  ILE   A CA  
1578 C  C   . ILE   A 69  ? 0.1354 0.1340 0.1582 0.0060  0.0186  0.0160  69  ILE   A C   
1579 O  O   . ILE   A 69  ? 0.1416 0.1440 0.1614 0.0001  0.0226  0.0198  69  ILE   A O   
1580 C  CB  . ILE   A 69  ? 0.1365 0.1539 0.1711 0.0052  0.0167  0.0023  69  ILE   A CB  
1581 C  CG1 . ILE   A 69  ? 0.1381 0.1660 0.1833 0.0043  0.0179  -0.0131 69  ILE   A CG1 
1582 C  CG2 . ILE   A 69  ? 0.1570 0.1732 0.1775 0.0107  0.0018  -0.0005 69  ILE   A CG2 
1583 C  CD1 . ILE   A 69  ? 0.1371 0.1765 0.2051 -0.0028 0.0173  -0.0184 69  ILE   A CD1 
1595 N  N   . ALA   A 70  ? 0.1432 0.1347 0.1683 -0.0031 0.0219  0.0151  70  ALA   A N   
1596 C  CA  . ALA   A 70  ? 0.1458 0.1462 0.1903 -0.0133 0.0293  0.0186  70  ALA   A CA  
1597 C  C   . ALA   A 70  ? 0.1444 0.1596 0.1928 -0.0107 0.0358  0.0197  70  ALA   A C   
1598 O  O   . ALA   A 70  ? 0.1613 0.1917 0.2139 0.0063  0.0471  0.0395  70  ALA   A O   
1599 C  CB  . ALA   A 70  ? 0.1483 0.1419 0.2100 -0.0156 0.0222  0.0145  70  ALA   A CB  
1605 N  N   . THR   A 71  ? 0.1347 0.1544 0.1858 -0.0019 0.0203  0.0221  71  THR   A N   
1606 C  CA  . THR   A 71  ? 0.1453 0.1740 0.2090 0.0079  0.0228  0.0238  71  THR   A CA  
1607 C  C   . THR   A 71  ? 0.1368 0.1680 0.2291 0.0124  0.0286  0.0207  71  THR   A C   
1608 O  O   . THR   A 71  ? 0.1406 0.1916 0.2672 0.0088  0.0445  -0.0036 71  THR   A O   
1609 C  CB  . THR   A 71  ? 0.1694 0.1943 0.2273 0.0168  -0.0085 0.0343  71  THR   A CB  
1610 O  OG1 . THR   A 71  ? 0.1940 0.2127 0.2279 0.0088  -0.0276 0.0232  71  THR   A OG1 
1611 C  CG2 . THR   A 71  ? 0.1796 0.2102 0.2577 0.0245  -0.0150 0.0541  71  THR   A CG2 
1619 N  N   . ASN   A 72  ? 0.1409 0.1521 0.2099 0.0116  0.0234  0.0205  72  ASN   A N   
1620 C  CA  . ASN   A 72  ? 0.1435 0.1494 0.2164 0.0162  0.0357  0.0196  72  ASN   A CA  
1621 C  C   . ASN   A 72  ? 0.1555 0.1499 0.2153 0.0104  0.0534  0.0112  72  ASN   A C   
1622 O  O   . ASN   A 72  ? 0.1715 0.1477 0.2408 0.0128  0.0460  -0.0027 72  ASN   A O   
1623 C  CB  . ASN   A 72  ? 0.1635 0.1528 0.2225 0.0150  0.0326  0.0286  72  ASN   A CB  
1624 C  CG  . ASN   A 72  ? 0.1891 0.1649 0.2305 0.0273  0.0334  0.0259  72  ASN   A CG  
1625 O  OD1 . ASN   A 72  ? 0.2060 0.1944 0.2446 0.0274  0.0418  0.0287  72  ASN   A OD1 
1626 N  ND2 . ASN   A 72  ? 0.2004 0.1660 0.2303 0.0505  0.0187  0.0188  72  ASN   A ND2 
1633 N  N   . GLY   A 73  ? 0.1541 0.1492 0.1972 0.0050  0.0428  0.0154  73  GLY   A N   
1634 C  CA  . GLY   A 73  ? 0.1598 0.1434 0.1834 -0.0040 0.0388  0.0166  73  GLY   A CA  
1635 C  C   . GLY   A 73  ? 0.1620 0.1334 0.1653 -0.0001 0.0440  0.0286  73  GLY   A C   
1636 O  O   . GLY   A 73  ? 0.1616 0.1411 0.1877 0.0092  0.0357  0.0291  73  GLY   A O   
1640 N  N   . PRO   A 74  ? 0.1695 0.1387 0.1638 -0.0085 0.0463  0.0160  74  PRO   A N   
1641 C  CA  . PRO   A 74  ? 0.1626 0.1387 0.1795 -0.0034 0.0469  0.0151  74  PRO   A CA  
1642 C  C   . PRO   A 74  ? 0.1581 0.1283 0.1774 -0.0009 0.0338  0.0070  74  PRO   A C   
1643 O  O   . PRO   A 74  ? 0.1668 0.1329 0.1944 0.0026  0.0351  -0.0039 74  PRO   A O   
1644 C  CB  . PRO   A 74  ? 0.1756 0.1672 0.2031 0.0018  0.0443  0.0290  74  PRO   A CB  
1645 C  CG  . PRO   A 74  ? 0.2056 0.2014 0.2419 -0.0136 0.0375  0.0204  74  PRO   A CG  
1646 C  CD  . PRO   A 74  ? 0.1887 0.1802 0.1868 -0.0195 0.0366  0.0094  74  PRO   A CD  
1654 N  N   . LEU   A 75  ? 0.1542 0.1153 0.1640 -0.0008 0.0274  0.0074  75  LEU   A N   
1655 C  CA  . LEU   A 75  ? 0.1562 0.1228 0.1438 -0.0014 0.0133  0.0087  75  LEU   A CA  
1656 C  C   . LEU   A 75  ? 0.1661 0.1317 0.1504 0.0014  0.0125  0.0143  75  LEU   A C   
1657 O  O   . LEU   A 75  ? 0.1983 0.1457 0.1489 0.0103  0.0065  0.0036  75  LEU   A O   
1658 C  CB  . LEU   A 75  ? 0.1602 0.1335 0.1382 -0.0108 0.0101  0.0209  75  LEU   A CB  
1659 C  CG  . LEU   A 75  ? 0.1756 0.1654 0.1538 -0.0375 0.0109  0.0137  75  LEU   A CG  
1660 C  CD1 . LEU   A 75  ? 0.1859 0.2128 0.1740 -0.0354 0.0072  0.0004  75  LEU   A CD1 
1661 C  CD2 . LEU   A 75  ? 0.2031 0.1989 0.2067 -0.0105 0.0110  0.0116  75  LEU   A CD2 
1673 N  N   . LYS   A 76  ? 0.1683 0.1345 0.1620 -0.0057 0.0165  -0.0035 76  LYS   A N   
1674 C  CA  . LYS   A 76  ? 0.1663 0.1546 0.1673 -0.0120 0.0172  -0.0152 76  LYS   A CA  
1675 C  C   . LYS   A 76  ? 0.1640 0.1330 0.1294 -0.0042 0.0158  0.0017  76  LYS   A C   
1676 O  O   . LYS   A 76  ? 0.1657 0.1269 0.1321 -0.0021 0.0159  0.0080  76  LYS   A O   
1677 C  CB  . LYS   A 76  ? 0.1658 0.1782 0.2133 -0.0003 0.0242  -0.0403 76  LYS   A CB  
1678 C  CG  . LYS   A 76  ? 0.1775 0.1719 0.2585 0.0115  0.0172  -0.0410 76  LYS   A CG  
1679 C  CD  . LYS   A 76  ? 0.1868 0.1681 0.3047 0.0168  0.0045  -0.0460 76  LYS   A CD  
1680 C  CE  . LYS   A 76  ? 0.2077 0.1921 0.3615 0.0060  0.0111  -0.0493 76  LYS   A CE  
1681 N  NZ  . LYS   A 76  ? 0.2104 0.1850 0.3996 -0.0109 0.0059  -0.0582 76  LYS   A NZ  
1695 N  N   . VAL   A 77  ? 0.1739 0.1388 0.1363 -0.0019 0.0269  0.0071  77  VAL   A N   
1696 C  CA  . VAL   A 77  ? 0.1696 0.1405 0.1339 0.0041  0.0225  0.0069  77  VAL   A CA  
1697 C  C   . VAL   A 77  ? 0.1568 0.1369 0.1299 0.0068  0.0134  0.0018  77  VAL   A C   
1698 O  O   . VAL   A 77  ? 0.1657 0.1388 0.1358 0.0095  0.0308  -0.0047 77  VAL   A O   
1699 C  CB  . VAL   A 77  ? 0.1857 0.1586 0.1362 0.0066  0.0213  0.0120  77  VAL   A CB  
1700 C  CG1 . VAL   A 77  ? 0.1754 0.1779 0.1556 0.0138  0.0112  0.0050  77  VAL   A CG1 
1701 C  CG2 . VAL   A 77  ? 0.2141 0.1714 0.1507 -0.0001 0.0061  0.0170  77  VAL   A CG2 
1711 N  N   . GLY   A 78  ? 0.1523 0.1367 0.1348 0.0062  0.0246  0.0016  78  GLY   A N   
1712 C  CA  . GLY   A 78  ? 0.1507 0.1285 0.1437 0.0010  0.0242  0.0130  78  GLY   A CA  
1713 C  C   . GLY   A 78  ? 0.1377 0.1215 0.1363 0.0049  0.0231  0.0085  78  GLY   A C   
1714 O  O   . GLY   A 78  ? 0.1351 0.1296 0.1587 0.0008  0.0189  0.0210  78  GLY   A O   
1718 N  N   . GLY   A 79  ? 0.1435 0.1227 0.1389 0.0035  0.0181  0.0132  79  GLY   A N   
1719 C  CA  . GLY   A 79  ? 0.1387 0.1214 0.1536 0.0022  0.0174  0.0144  79  GLY   A CA  
1720 C  C   . GLY   A 79  ? 0.1302 0.1201 0.1463 -0.0018 0.0162  0.0071  79  GLY   A C   
1721 O  O   . GLY   A 79  ? 0.1342 0.1316 0.1514 0.0167  0.0126  0.0057  79  GLY   A O   
1725 N  N   . SER   A 80  ? 0.1256 0.1356 0.1657 0.0002  0.0158  0.0009  80  SER   A N   
1726 C  CA  . SER   A 80  ? 0.1225 0.1292 0.1504 0.0012  0.0095  0.0063  80  SER   A CA  
1727 C  C   . SER   A 80  ? 0.1219 0.1287 0.1453 0.0004  0.0083  0.0154  80  SER   A C   
1728 O  O   . SER   A 80  ? 0.1250 0.1506 0.1794 0.0055  0.0136  0.0014  80  SER   A O   
1729 C  CB  . SER   A 80  ? 0.1356 0.1321 0.1791 -0.0045 0.0103  0.0046  80  SER   A CB  
1730 O  OG  . SER   A 80  ? 0.1594 0.1325 0.2093 0.0051  -0.0033 0.0192  80  SER   A OG  
1736 N  N   . CYS   A 81  ? 0.1159 0.1274 0.1436 -0.0011 -0.0012 0.0142  81  CYS   A N   
1737 C  CA  . CYS   A 81  ? 0.1166 0.1366 0.1422 -0.0034 -0.0094 0.0234  81  CYS   A CA  
1738 C  C   . CYS   A 81  ? 0.1160 0.1290 0.1432 -0.0115 -0.0066 0.0196  81  CYS   A C   
1739 O  O   . CYS   A 81  ? 0.1168 0.1541 0.1629 -0.0000 -0.0024 0.0295  81  CYS   A O   
1740 C  CB  . CYS   A 81  ? 0.1226 0.1371 0.1588 -0.0099 -0.0035 0.0269  81  CYS   A CB  
1741 S  SG  . CYS   A 81  ? 0.1378 0.1299 0.1652 -0.0143 0.0014  0.0145  81  CYS   A SG  
1747 N  N   . VAL   A 82  ? 0.1241 0.1364 0.1443 -0.0014 -0.0126 0.0159  82  VAL   A N   
1748 C  CA  . VAL   A 82  ? 0.1349 0.1427 0.1432 0.0012  -0.0082 0.0259  82  VAL   A CA  
1749 C  C   . VAL   A 82  ? 0.1296 0.1475 0.1473 -0.0013 -0.0094 0.0242  82  VAL   A C   
1750 O  O   . VAL   A 82  ? 0.1233 0.1566 0.1823 -0.0011 -0.0024 0.0031  82  VAL   A O   
1751 C  CB  . VAL   A 82  ? 0.1656 0.1565 0.1587 -0.0028 -0.0024 0.0304  82  VAL   A CB  
1752 C  CG1 . VAL   A 82  ? 0.1849 0.1711 0.1815 0.0024  0.0040  0.0334  82  VAL   A CG1 
1753 C  CG2 . VAL   A 82  ? 0.1719 0.1609 0.1751 -0.0052 -0.0127 0.0406  82  VAL   A CG2 
1763 N  N   . LEU   A 83  ? 0.1244 0.1431 0.1507 -0.0122 -0.0111 0.0143  83  LEU   A N   
1764 C  CA  . LEU   A 83  ? 0.1264 0.1439 0.1400 -0.0147 -0.0100 0.0102  83  LEU   A CA  
1765 C  C   . LEU   A 83  ? 0.1314 0.1484 0.1311 -0.0140 -0.0126 0.0142  83  LEU   A C   
1766 O  O   . LEU   A 83  ? 0.1429 0.1510 0.1404 -0.0147 -0.0097 0.0171  83  LEU   A O   
1767 C  CB  . LEU   A 83  ? 0.1338 0.1510 0.1400 -0.0088 -0.0127 0.0130  83  LEU   A CB  
1768 C  CG  . LEU   A 83  ? 0.1485 0.1634 0.1423 -0.0076 0.0008  0.0076  83  LEU   A CG  
1769 C  CD1 . LEU   A 83  ? 0.1653 0.1685 0.1478 -0.0184 -0.0018 0.0261  83  LEU   A CD1 
1770 C  CD2 . LEU   A 83  ? 0.1452 0.1715 0.1659 -0.0049 0.0097  0.0170  83  LEU   A CD2 
1782 N  N   . SER   A 84  ? 0.1455 0.1514 0.1358 -0.0138 -0.0117 0.0194  84  SER   A N   
1783 C  CA  . SER   A 84  ? 0.1580 0.1595 0.1224 -0.0158 -0.0155 0.0166  84  SER   A CA  
1784 C  C   . SER   A 84  ? 0.1598 0.1591 0.1152 -0.0245 -0.0015 0.0117  84  SER   A C   
1785 O  O   . SER   A 84  ? 0.1539 0.1710 0.1258 -0.0188 -0.0117 0.0092  84  SER   A O   
1786 C  CB  . SER   A 84  ? 0.1611 0.1829 0.1377 -0.0127 -0.0137 0.0075  84  SER   A CB  
1787 O  OG  . SER   A 84  ? 0.1637 0.2052 0.1425 -0.0098 -0.0162 -0.0024 84  SER   A OG  
1793 N  N   . GLY   A 85  ? 0.1727 0.1725 0.1242 -0.0251 0.0042  0.0112  85  GLY   A N   
1794 C  CA  . GLY   A 85  ? 0.1771 0.1778 0.1392 -0.0270 0.0105  0.0031  85  GLY   A CA  
1795 C  C   . GLY   A 85  ? 0.1707 0.1825 0.1259 -0.0238 0.0009  0.0009  85  GLY   A C   
1796 O  O   . GLY   A 85  ? 0.1668 0.1950 0.1431 -0.0321 0.0113  -0.0090 85  GLY   A O   
1800 N  N   . HIS   A 86  ? 0.1691 0.1735 0.1253 -0.0241 -0.0051 0.0012  86  HIS   A N   
1801 C  CA  . HIS   A 86  ? 0.1840 0.1830 0.1194 -0.0248 -0.0060 0.0010  86  HIS   A CA  
1802 C  C   . HIS   A 86  ? 0.1995 0.1965 0.1119 -0.0246 -0.0102 -0.0000 86  HIS   A C   
1803 O  O   . HIS   A 86  ? 0.2084 0.2198 0.1232 -0.0180 0.0008  0.0017  86  HIS   A O   
1804 C  CB  . HIS   A 86  ? 0.1840 0.1743 0.1228 -0.0185 -0.0007 0.0042  86  HIS   A CB  
1805 C  CG  . HIS   A 86  ? 0.1776 0.1754 0.1295 -0.0108 0.0016  0.0126  86  HIS   A CG  
1806 N  ND1 . HIS   A 86  ? 0.1841 0.1740 0.1663 -0.0209 -0.0019 0.0094  86  HIS   A ND1 
1807 C  CD2 . HIS   A 86  ? 0.1789 0.1715 0.1337 0.0027  0.0090  0.0120  86  HIS   A CD2 
1808 C  CE1 . HIS   A 86  ? 0.1809 0.1725 0.1627 -0.0147 0.0151  0.0120  86  HIS   A CE1 
1809 N  NE2 . HIS   A 86  ? 0.1783 0.1629 0.1470 0.0021  0.0159  0.0233  86  HIS   A NE2 
1817 N  N   . ASN   A 87  ? 0.2100 0.2047 0.1257 -0.0225 0.0150  -0.0109 87  ASN   A N   
1818 C  CA  . ASN   A 87  ? 0.2298 0.2159 0.1288 -0.0178 0.0342  -0.0161 87  ASN   A CA  
1819 C  C   . ASN   A 87  ? 0.2292 0.2294 0.1614 -0.0261 0.0534  -0.0052 87  ASN   A C   
1820 O  O   . ASN   A 87  ? 0.2534 0.2462 0.2084 -0.0378 0.0842  -0.0159 87  ASN   A O   
1821 C  CB  . ASN   A 87  ? 0.2419 0.2211 0.1431 -0.0073 0.0361  -0.0182 87  ASN   A CB  
1822 C  CG  . ASN   A 87  ? 0.2507 0.2314 0.1523 -0.0012 0.0442  -0.0128 87  ASN   A CG  
1823 O  OD1 . ASN   A 87  ? 0.2667 0.2271 0.1588 0.0142  0.0401  -0.0009 87  ASN   A OD1 
1824 N  ND2 . ASN   A 87  ? 0.2533 0.2562 0.1620 -0.0013 0.0399  -0.0042 87  ASN   A ND2 
1831 N  N   . LEU   A 88  ? 0.2034 0.2233 0.1557 -0.0328 0.0257  0.0101  88  LEU   A N   
1832 C  CA  . LEU   A 88  ? 0.1882 0.2202 0.1760 -0.0379 0.0186  0.0254  88  LEU   A CA  
1833 C  C   . LEU   A 88  ? 0.1886 0.2232 0.1641 -0.0388 0.0185  0.0329  88  LEU   A C   
1834 O  O   . LEU   A 88  ? 0.1962 0.2298 0.1942 -0.0418 0.0198  0.0419  88  LEU   A O   
1835 C  CB  . LEU   A 88  ? 0.1929 0.2257 0.1864 -0.0450 -0.0128 0.0375  88  LEU   A CB  
1836 C  CG  . LEU   A 88  ? 0.2080 0.2388 0.2092 -0.0400 -0.0241 0.0398  88  LEU   A CG  
1837 C  CD1 . LEU   A 88  ? 0.2224 0.2480 0.1983 -0.0356 -0.0236 0.0279  88  LEU   A CD1 
1838 C  CD2 . LEU   A 88  ? 0.2232 0.2528 0.2508 -0.0288 -0.0195 0.0323  88  LEU   A CD2 
1850 N  N   . ALA   A 89  ? 0.1912 0.2151 0.1471 -0.0362 0.0122  0.0120  89  ALA   A N   
1851 C  CA  . ALA   A 89  ? 0.1965 0.2112 0.1329 -0.0326 0.0063  0.0189  89  ALA   A CA  
1852 C  C   . ALA   A 89  ? 0.2031 0.2125 0.1339 -0.0278 -0.0122 0.0171  89  ALA   A C   
1853 O  O   . ALA   A 89  ? 0.1939 0.2097 0.1667 -0.0339 -0.0206 -0.0068 89  ALA   A O   
1854 C  CB  . ALA   A 89  ? 0.1922 0.2092 0.1194 -0.0336 0.0007  0.0160  89  ALA   A CB  
1860 N  N   . LYS   A 90  ? 0.2184 0.2252 0.1341 -0.0339 -0.0275 0.0253  90  LYS   A N   
1861 C  CA  . LYS   A 90  ? 0.2262 0.2369 0.1441 -0.0296 -0.0388 0.0241  90  LYS   A CA  
1862 C  C   . LYS   A 90  ? 0.2003 0.2171 0.1442 -0.0324 -0.0349 0.0171  90  LYS   A C   
1863 O  O   . LYS   A 90  ? 0.2028 0.2291 0.1692 -0.0353 -0.0396 0.0068  90  LYS   A O   
1864 C  CB  . LYS   A 90  ? 0.2546 0.2718 0.1819 -0.0220 -0.0478 0.0530  90  LYS   A CB  
1865 C  CG  . LYS   A 90  ? 0.2907 0.3070 0.2772 -0.0212 -0.0397 0.0632  90  LYS   A CG  
1866 C  CD  . LYS   A 90  ? 0.3307 0.3426 0.3791 -0.0250 -0.0180 0.0614  90  LYS   A CD  
1867 C  CE  . LYS   A 90  ? 0.3736 0.3808 0.4555 -0.0269 -0.0028 0.0585  90  LYS   A CE  
1868 N  NZ  . LYS   A 90  ? 0.3907 0.3970 0.5124 -0.0274 0.0018  0.0566  90  LYS   A NZ  
1882 N  N   . HIS   A 91  ? 0.1849 0.1904 0.1202 -0.0316 -0.0349 0.0216  91  HIS   A N   
1883 C  CA  . HIS   A 91  ? 0.1739 0.1748 0.1302 -0.0234 -0.0317 0.0164  91  HIS   A CA  
1884 C  C   . HIS   A 91  ? 0.1554 0.1644 0.1218 -0.0247 -0.0199 0.0182  91  HIS   A C   
1885 O  O   . HIS   A 91  ? 0.1512 0.1787 0.1283 -0.0298 -0.0116 0.0263  91  HIS   A O   
1886 C  CB  . HIS   A 91  ? 0.1898 0.1986 0.1770 -0.0013 -0.0395 0.0152  91  HIS   A CB  
1887 C  CG  . HIS   A 91  ? 0.2293 0.2462 0.2505 0.0173  -0.0662 0.0069  91  HIS   A CG  
1888 N  ND1 . HIS   A 91  ? 0.2388 0.2747 0.2929 0.0246  -0.0770 -0.0077 91  HIS   A ND1 
1889 C  CD2 . HIS   A 91  ? 0.2563 0.2663 0.2730 0.0245  -0.0793 0.0173  91  HIS   A CD2 
1890 C  CE1 . HIS   A 91  ? 0.2545 0.2855 0.2956 0.0278  -0.0816 0.0042  91  HIS   A CE1 
1891 N  NE2 . HIS   A 91  ? 0.2689 0.2841 0.2936 0.0303  -0.0848 0.0124  91  HIS   A NE2 
1899 N  N   . CYS   A 92  ? 0.1451 0.1548 0.1231 -0.0210 -0.0162 0.0188  92  CYS   A N   
1900 C  CA  . CYS   A 92  ? 0.1333 0.1482 0.1275 -0.0167 -0.0015 0.0188  92  CYS   A CA  
1901 C  C   . CYS   A 92  ? 0.1318 0.1431 0.1165 -0.0149 -0.0032 0.0175  92  CYS   A C   
1902 O  O   . CYS   A 92  ? 0.1282 0.1496 0.1398 -0.0176 -0.0057 0.0129  92  CYS   A O   
1903 C  CB  . CYS   A 92  ? 0.1326 0.1431 0.1402 -0.0081 -0.0049 0.0129  92  CYS   A CB  
1904 S  SG  . CYS   A 92  ? 0.1348 0.1375 0.1186 -0.0124 -0.0042 0.0107  92  CYS   A SG  
1910 N  N   . LEU   A 93  ? 0.1297 0.1311 0.1235 -0.0117 0.0000  0.0139  93  LEU   A N   
1911 C  CA  . LEU   A 93  ? 0.1212 0.1259 0.1308 -0.0081 0.0002  0.0124  93  LEU   A CA  
1912 C  C   . LEU   A 93  ? 0.1163 0.1161 0.1216 -0.0044 0.0023  0.0115  93  LEU   A C   
1913 O  O   . LEU   A 93  ? 0.1139 0.1266 0.1304 -0.0035 -0.0023 0.0100  93  LEU   A O   
1914 C  CB  . LEU   A 93  ? 0.1291 0.1292 0.1401 -0.0086 -0.0031 0.0285  93  LEU   A CB  
1915 C  CG  . LEU   A 93  ? 0.1331 0.1319 0.1367 -0.0045 0.0010  0.0227  93  LEU   A CG  
1916 C  CD1 . LEU   A 93  ? 0.1389 0.1376 0.1793 -0.0034 0.0081  0.0144  93  LEU   A CD1 
1917 C  CD2 . LEU   A 93  ? 0.1429 0.1342 0.1550 -0.0090 -0.0023 0.0170  93  LEU   A CD2 
1929 N  N   . HIS   A 94  ? 0.1105 0.1146 0.1294 -0.0033 0.0033  0.0162  94  HIS   A N   
1930 C  CA  . HIS   A 94  ? 0.1071 0.1142 0.1278 -0.0019 -0.0029 0.0191  94  HIS   A CA  
1931 C  C   . HIS   A 94  ? 0.1116 0.1147 0.1263 -0.0055 -0.0002 0.0129  94  HIS   A C   
1932 O  O   . HIS   A 94  ? 0.1134 0.1378 0.1666 -0.0002 0.0004  -0.0083 94  HIS   A O   
1933 C  CB  . HIS   A 94  ? 0.1094 0.1129 0.1327 -0.0027 0.0001  0.0148  94  HIS   A CB  
1934 C  CG  . HIS   A 94  ? 0.1156 0.1151 0.1285 -0.0048 -0.0043 0.0178  94  HIS   A CG  
1935 N  ND1 . HIS   A 94  ? 0.1143 0.1162 0.1348 -0.0061 -0.0026 0.0202  94  HIS   A ND1 
1936 C  CD2 . HIS   A 94  ? 0.1249 0.1270 0.1326 -0.0084 -0.0038 0.0120  94  HIS   A CD2 
1937 C  CE1 . HIS   A 94  ? 0.1226 0.1195 0.1360 -0.0098 -0.0151 0.0054  94  HIS   A CE1 
1938 N  NE2 . HIS   A 94  ? 0.1271 0.1232 0.1409 -0.0112 -0.0091 0.0065  94  HIS   A NE2 
1946 N  N   . VAL   A 95  ? 0.1084 0.1140 0.1178 -0.0022 0.0088  0.0111  95  VAL   A N   
1947 C  CA  . VAL   A 95  ? 0.1175 0.1118 0.1134 -0.0050 0.0093  0.0098  95  VAL   A CA  
1948 C  C   . VAL   A 95  ? 0.1182 0.1092 0.1094 -0.0079 0.0062  0.0071  95  VAL   A C   
1949 O  O   . VAL   A 95  ? 0.1210 0.1240 0.1312 0.0070  0.0082  0.0082  95  VAL   A O   
1950 C  CB  . VAL   A 95  ? 0.1215 0.1191 0.1329 -0.0059 0.0012  0.0064  95  VAL   A CB  
1951 C  CG1 . VAL   A 95  ? 0.1362 0.1233 0.1468 -0.0123 0.0067  -0.0003 95  VAL   A CG1 
1952 C  CG2 . VAL   A 95  ? 0.1173 0.1247 0.1427 -0.0168 0.0080  0.0198  95  VAL   A CG2 
1962 N  N   . VAL   A 96  ? 0.1201 0.1140 0.1120 0.0003  0.0043  0.0111  96  VAL   A N   
1963 C  CA  . VAL   A 96  ? 0.1286 0.1169 0.1235 0.0013  0.0117  0.0149  96  VAL   A CA  
1964 C  C   . VAL   A 96  ? 0.1325 0.1256 0.1207 -0.0012 0.0189  0.0133  96  VAL   A C   
1965 O  O   . VAL   A 96  ? 0.1414 0.1305 0.1439 -0.0028 0.0207  -0.0016 96  VAL   A O   
1966 C  CB  . VAL   A 96  ? 0.1333 0.1241 0.1250 -0.0034 0.0224  0.0134  96  VAL   A CB  
1967 C  CG1 . VAL   A 96  ? 0.1414 0.1333 0.1163 -0.0005 0.0161  0.0081  96  VAL   A CG1 
1968 C  CG2 . VAL   A 96  ? 0.1323 0.1293 0.1463 -0.0129 0.0216  0.0115  96  VAL   A CG2 
1978 N  N   A GLY   A 97  ? 0.1285 0.1297 0.1246 -0.0066 0.0130  0.0095  97  GLY   A N   
1979 N  N   B GLY   A 97  ? 0.1383 0.1300 0.1266 -0.0027 0.0121  0.0124  97  GLY   A N   
1980 C  CA  A GLY   A 97  ? 0.1364 0.1442 0.1202 -0.0080 0.0018  0.0097  97  GLY   A CA  
1981 C  CA  B GLY   A 97  ? 0.1473 0.1347 0.1305 -0.0021 0.0048  0.0137  97  GLY   A CA  
1982 C  C   A GLY   A 97  ? 0.1386 0.1590 0.1107 -0.0059 0.0056  0.0091  97  GLY   A C   
1983 C  C   B GLY   A 97  ? 0.1557 0.1397 0.1340 -0.0017 0.0003  0.0158  97  GLY   A C   
1984 O  O   A GLY   A 97  ? 0.1453 0.1591 0.1288 -0.0065 0.0079  0.0133  97  GLY   A O   
1985 O  O   B GLY   A 97  ? 0.1542 0.1399 0.1376 -0.0023 -0.0031 0.0216  97  GLY   A O   
1992 N  N   A PRO   A 98  ? 0.1451 0.1647 0.0996 -0.0042 0.0027  0.0085  98  PRO   A N   
1993 N  N   B PRO   A 98  ? 0.1672 0.1404 0.1327 -0.0017 -0.0029 0.0144  98  PRO   A N   
1994 C  CA  A PRO   A 98  ? 0.1605 0.1897 0.0997 -0.0100 0.0058  0.0067  98  PRO   A CA  
1995 C  CA  B PRO   A 98  ? 0.1807 0.1497 0.1345 -0.0027 -0.0018 0.0097  98  PRO   A CA  
1996 C  C   A PRO   A 98  ? 0.1581 0.1925 0.0985 -0.0216 -0.0019 0.0265  98  PRO   A C   
1997 C  C   B PRO   A 98  ? 0.1935 0.1553 0.1328 -0.0044 -0.0019 0.0140  98  PRO   A C   
1998 O  O   A PRO   A 98  ? 0.1504 0.1788 0.1371 -0.0123 0.0012  0.0269  98  PRO   A O   
1999 O  O   B PRO   A 98  ? 0.1907 0.1524 0.1419 -0.0016 0.0007  0.0108  98  PRO   A O   
2000 C  CB  A PRO   A 98  ? 0.1738 0.1984 0.0856 0.0022  -0.0051 -0.0044 98  PRO   A CB  
2001 C  CB  B PRO   A 98  ? 0.1806 0.1473 0.1304 -0.0005 -0.0073 0.0078  98  PRO   A CB  
2002 C  CG  A PRO   A 98  ? 0.1698 0.1893 0.1149 0.0027  -0.0023 -0.0119 98  PRO   A CG  
2003 C  CG  B PRO   A 98  ? 0.1767 0.1442 0.1332 -0.0024 -0.0072 0.0111  98  PRO   A CG  
2004 C  CD  A PRO   A 98  ? 0.1553 0.1698 0.1099 0.0035  0.0069  -0.0031 98  PRO   A CD  
2005 C  CD  B PRO   A 98  ? 0.1704 0.1390 0.1292 -0.0006 -0.0045 0.0145  98  PRO   A CD  
2020 N  N   A ASN   A 99  ? 0.1642 0.2099 0.1052 -0.0240 -0.0025 0.0355  99  ASN   A N   
2021 N  N   B ASN   A 99  ? 0.2081 0.1655 0.1290 -0.0028 -0.0047 0.0191  99  ASN   A N   
2022 C  CA  A ASN   A 99  ? 0.1824 0.2270 0.1140 -0.0234 -0.0084 0.0514  99  ASN   A CA  
2023 C  CA  B ASN   A 99  ? 0.2257 0.1810 0.1447 0.0002  -0.0129 0.0200  99  ASN   A CA  
2024 C  C   A ASN   A 99  ? 0.1909 0.2694 0.1103 -0.0334 -0.0035 0.0619  99  ASN   A C   
2025 C  C   B ASN   A 99  ? 0.2414 0.1996 0.1675 -0.0018 -0.0148 0.0112  99  ASN   A C   
2026 O  O   A ASN   A 99  ? 0.1982 0.2936 0.1212 -0.0245 -0.0093 0.0594  99  ASN   A O   
2027 O  O   B ASN   A 99  ? 0.2428 0.1902 0.1681 0.0015  -0.0130 0.0006  99  ASN   A O   
2028 C  CB  A ASN   A 99  ? 0.1859 0.2163 0.1277 -0.0207 -0.0194 0.0513  99  ASN   A CB  
2029 C  CB  B ASN   A 99  ? 0.2292 0.1823 0.1589 0.0038  -0.0164 0.0226  99  ASN   A CB  
2030 C  CG  A ASN   A 99  ? 0.1891 0.2067 0.1440 -0.0102 -0.0214 0.0352  99  ASN   A CG  
2031 C  CG  B ASN   A 99  ? 0.2314 0.1857 0.1680 0.0059  -0.0193 0.0233  99  ASN   A CG  
2032 O  OD1 A ASN   A 99  ? 0.1970 0.2173 0.1447 -0.0007 -0.0228 0.0216  99  ASN   A OD1 
2033 O  OD1 B ASN   A 99  ? 0.2359 0.1890 0.1593 0.0009  -0.0207 0.0257  99  ASN   A OD1 
2034 N  ND2 A ASN   A 99  ? 0.1922 0.2008 0.1642 -0.0051 -0.0253 0.0340  99  ASN   A ND2 
2035 N  ND2 B ASN   A 99  ? 0.2312 0.1887 0.1741 0.0141  -0.0239 0.0134  99  ASN   A ND2 
2048 N  N   A VAL   A 100 ? 0.2023 0.2890 0.1104 -0.0441 -0.0257 0.0539  100 VAL   A N   
2049 N  N   B VAL   A 100 ? 0.2542 0.2298 0.2033 -0.0087 -0.0163 0.0124  100 VAL   A N   
2050 C  CA  A VAL   A 100 ? 0.2259 0.3116 0.1376 -0.0527 -0.0386 0.0517  100 VAL   A CA  
2051 C  CA  B VAL   A 100 ? 0.2670 0.2609 0.2357 -0.0162 -0.0168 0.0168  100 VAL   A CA  
2052 C  C   A VAL   A 100 ? 0.2340 0.3276 0.1282 -0.0609 -0.0494 0.0742  100 VAL   A C   
2053 C  C   B VAL   A 100 ? 0.2828 0.2857 0.2530 -0.0224 -0.0155 0.0239  100 VAL   A C   
2054 O  O   A VAL   A 100 ? 0.2471 0.3413 0.1503 -0.0573 -0.0206 0.0679  100 VAL   A O   
2055 O  O   B VAL   A 100 ? 0.2841 0.2929 0.2495 -0.0265 -0.0161 0.0218  100 VAL   A O   
2056 C  CB  A VAL   A 100 ? 0.2449 0.3167 0.1800 -0.0570 -0.0399 0.0355  100 VAL   A CB  
2057 C  CB  B VAL   A 100 ? 0.2651 0.2655 0.2513 -0.0174 -0.0219 0.0158  100 VAL   A CB  
2058 C  CG1 A VAL   A 100 ? 0.2453 0.3235 0.2082 -0.0602 -0.0297 0.0349  100 VAL   A CG1 
2059 C  CG1 B VAL   A 100 ? 0.2661 0.2667 0.2599 -0.0164 -0.0242 0.0160  100 VAL   A CG1 
2060 C  CG2 A VAL   A 100 ? 0.2545 0.3171 0.1941 -0.0601 -0.0425 0.0190  100 VAL   A CG2 
2061 C  CG2 B VAL   A 100 ? 0.2639 0.2678 0.2607 -0.0182 -0.0249 0.0123  100 VAL   A CG2 
2080 N  N   A ASN   A 101 ? 0.2390 0.3312 0.1662 -0.0675 -0.0523 0.1093  101 ASN   A N   
2081 N  N   B ASN   A 101 ? 0.2959 0.2985 0.2685 -0.0241 -0.0157 0.0316  101 ASN   A N   
2082 C  CA  A ASN   A 101 ? 0.2669 0.3413 0.1931 -0.0712 -0.0478 0.1332  101 ASN   A CA  
2083 C  CA  B ASN   A 101 ? 0.3084 0.3091 0.2792 -0.0260 -0.0167 0.0398  101 ASN   A CA  
2084 C  C   A ASN   A 101 ? 0.2943 0.3749 0.2302 -0.0728 -0.0171 0.1577  101 ASN   A C   
2085 C  C   B ASN   A 101 ? 0.3203 0.3198 0.2887 -0.0251 -0.0072 0.0541  101 ASN   A C   
2086 O  O   A ASN   A 101 ? 0.3143 0.3836 0.2856 -0.0714 -0.0165 0.1478  101 ASN   A O   
2087 O  O   B ASN   A 101 ? 0.3220 0.3169 0.2770 -0.0254 -0.0040 0.0687  101 ASN   A O   
2088 C  CB  A ASN   A 101 ? 0.2735 0.3232 0.1932 -0.0718 -0.0671 0.1249  101 ASN   A CB  
2089 C  CB  B ASN   A 101 ? 0.3081 0.3071 0.2784 -0.0287 -0.0232 0.0308  101 ASN   A CB  
2090 C  CG  A ASN   A 101 ? 0.2788 0.3089 0.1833 -0.0743 -0.0764 0.0905  101 ASN   A CG  
2091 C  CG  B ASN   A 101 ? 0.3071 0.3039 0.2716 -0.0306 -0.0277 0.0209  101 ASN   A CG  
2092 O  OD1 A ASN   A 101 ? 0.2723 0.3136 0.1932 -0.0665 -0.0638 0.0515  101 ASN   A OD1 
2093 O  OD1 B ASN   A 101 ? 0.3040 0.3018 0.2662 -0.0298 -0.0306 0.0149  101 ASN   A OD1 
2094 N  ND2 A ASN   A 101 ? 0.2880 0.2932 0.1779 -0.0850 -0.0770 0.0895  101 ASN   A ND2 
2095 N  ND2 B ASN   A 101 ? 0.3090 0.3039 0.2704 -0.0321 -0.0289 0.0191  101 ASN   A ND2 
2108 N  N   A LYS   A 102 ? 0.2981 0.4032 0.2509 -0.0807 0.0005  0.1655  102 LYS   A N   
2109 N  N   B LYS   A 102 ? 0.3299 0.3319 0.3084 -0.0243 0.0007  0.0514  102 LYS   A N   
2110 C  CA  A LYS   A 102 ? 0.3118 0.4309 0.2618 -0.0838 -0.0006 0.1513  102 LYS   A CA  
2111 C  CA  B LYS   A 102 ? 0.3375 0.3424 0.3156 -0.0246 0.0068  0.0449  102 LYS   A CA  
2112 C  C   A LYS   A 102 ? 0.3237 0.4571 0.2410 -0.0751 0.0002  0.1323  102 LYS   A C   
2113 C  C   B LYS   A 102 ? 0.3371 0.3462 0.2987 -0.0248 0.0084  0.0444  102 LYS   A C   
2114 O  O   A LYS   A 102 ? 0.3270 0.4748 0.2346 -0.0740 0.0078  0.1220  102 LYS   A O   
2115 O  O   B LYS   A 102 ? 0.3385 0.3491 0.2971 -0.0256 0.0105  0.0433  102 LYS   A O   
2116 C  CB  A LYS   A 102 ? 0.3213 0.4347 0.3035 -0.0926 -0.0159 0.1373  102 LYS   A CB  
2117 C  CB  B LYS   A 102 ? 0.3443 0.3484 0.3393 -0.0274 0.0120  0.0363  102 LYS   A CB  
2118 C  CG  A LYS   A 102 ? 0.3340 0.4393 0.3408 -0.0968 -0.0367 0.1150  102 LYS   A CG  
2119 C  CG  B LYS   A 102 ? 0.3506 0.3533 0.3595 -0.0305 0.0155  0.0291  102 LYS   A CG  
2120 C  CD  A LYS   A 102 ? 0.3496 0.4467 0.3748 -0.0970 -0.0480 0.0858  102 LYS   A CD  
2121 C  CD  B LYS   A 102 ? 0.3562 0.3585 0.3784 -0.0321 0.0177  0.0200  102 LYS   A CD  
2122 C  CE  A LYS   A 102 ? 0.3648 0.4537 0.4070 -0.0929 -0.0556 0.0676  102 LYS   A CE  
2123 C  CE  B LYS   A 102 ? 0.3600 0.3633 0.3922 -0.0323 0.0179  0.0121  102 LYS   A CE  
2124 N  NZ  A LYS   A 102 ? 0.3725 0.4559 0.4182 -0.0928 -0.0611 0.0574  102 LYS   A NZ  
2125 N  NZ  B LYS   A 102 ? 0.3622 0.3663 0.4007 -0.0317 0.0180  0.0080  102 LYS   A NZ  
2152 N  N   A GLY   A 103 ? 0.3286 0.4648 0.2474 -0.0643 -0.0097 0.1034  103 GLY   A N   
2153 N  N   B GLY   A 103 ? 0.3346 0.3470 0.2926 -0.0226 0.0078  0.0385  103 GLY   A N   
2154 C  CA  A GLY   A 103 ? 0.3319 0.4656 0.2304 -0.0538 -0.0100 0.0801  103 GLY   A CA  
2155 C  CA  B GLY   A 103 ? 0.3315 0.3456 0.2808 -0.0206 0.0110  0.0325  103 GLY   A CA  
2156 C  C   A GLY   A 103 ? 0.3298 0.4659 0.2233 -0.0473 -0.0010 0.0575  103 GLY   A C   
2157 C  C   B GLY   A 103 ? 0.3297 0.3441 0.2739 -0.0185 0.0110  0.0226  103 GLY   A C   
2158 O  O   A GLY   A 103 ? 0.3402 0.4767 0.2454 -0.0401 -0.0049 0.0462  103 GLY   A O   
2159 O  O   B GLY   A 103 ? 0.3283 0.3454 0.2756 -0.0206 0.0139  0.0221  103 GLY   A O   
2166 N  N   A GLU   A 104 ? 0.3120 0.4503 0.1708 -0.0527 0.0072  0.0460  104 GLU   A N   
2167 N  N   B GLU   A 104 ? 0.3300 0.3414 0.2630 -0.0134 0.0074  0.0136  104 GLU   A N   
2168 C  CA  A GLU   A 104 ? 0.2902 0.4327 0.1524 -0.0622 0.0109  0.0330  104 GLU   A CA  
2169 C  CA  B GLU   A 104 ? 0.3288 0.3386 0.2555 -0.0091 0.0043  0.0044  104 GLU   A CA  
2170 C  C   A GLU   A 104 ? 0.2921 0.4424 0.1575 -0.0651 0.0173  0.0092  104 GLU   A C   
2171 C  C   B GLU   A 104 ? 0.3293 0.3414 0.2558 -0.0118 0.0042  -0.0038 104 GLU   A C   
2172 O  O   A GLU   A 104 ? 0.2840 0.4469 0.1782 -0.0684 0.0102  0.0073  104 GLU   A O   
2173 O  O   B GLU   A 104 ? 0.3282 0.3402 0.2524 -0.0120 0.0039  -0.0022 104 GLU   A O   
2174 C  CB  A GLU   A 104 ? 0.2635 0.4056 0.1290 -0.0693 0.0102  0.0506  104 GLU   A CB  
2175 C  CB  B GLU   A 104 ? 0.3264 0.3345 0.2532 -0.0022 0.0015  0.0075  104 GLU   A CB  
2176 C  CG  A GLU   A 104 ? 0.2448 0.3825 0.1429 -0.0723 -0.0013 0.0625  104 GLU   A CG  
2177 C  CG  B GLU   A 104 ? 0.3259 0.3322 0.2590 0.0045  -0.0005 0.0093  104 GLU   A CG  
2178 C  CD  A GLU   A 104 ? 0.2264 0.3598 0.1431 -0.0720 -0.0011 0.0788  104 GLU   A CD  
2179 C  CD  B GLU   A 104 ? 0.3256 0.3317 0.2638 0.0101  -0.0009 0.0100  104 GLU   A CD  
2180 O  OE1 A GLU   A 104 ? 0.2061 0.3423 0.1236 -0.0687 -0.0001 0.0732  104 GLU   A OE1 
2181 O  OE1 B GLU   A 104 ? 0.3245 0.3317 0.2653 0.0128  -0.0016 0.0127  104 GLU   A OE1 
2182 O  OE2 A GLU   A 104 ? 0.2366 0.3612 0.1560 -0.0740 -0.0002 0.0993  104 GLU   A OE2 
2183 O  OE2 B GLU   A 104 ? 0.3275 0.3326 0.2714 0.0112  -0.0008 0.0071  104 GLU   A OE2 
2196 N  N   A ASP   A 105 ? 0.3029 0.4464 0.1721 -0.0636 0.0293  -0.0149 105 ASP   A N   
2197 N  N   B ASP   A 105 ? 0.3297 0.3455 0.2654 -0.0153 0.0056  -0.0127 105 ASP   A N   
2198 C  CA  A ASP   A 105 ? 0.3065 0.4497 0.2206 -0.0569 0.0403  -0.0434 105 ASP   A CA  
2199 C  CA  B ASP   A 105 ? 0.3299 0.3498 0.2868 -0.0175 0.0063  -0.0205 105 ASP   A CA  
2200 C  C   A ASP   A 105 ? 0.2682 0.4269 0.1778 -0.0643 0.0283  -0.0645 105 ASP   A C   
2201 C  C   B ASP   A 105 ? 0.3199 0.3470 0.2747 -0.0228 0.0064  -0.0216 105 ASP   A C   
2202 O  O   A ASP   A 105 ? 0.2424 0.4115 0.1415 -0.0648 0.0209  -0.0888 105 ASP   A O   
2203 O  O   B ASP   A 105 ? 0.3162 0.3465 0.2673 -0.0223 0.0053  -0.0236 105 ASP   A O   
2204 C  CB  A ASP   A 105 ? 0.3401 0.4706 0.2978 -0.0421 0.0556  -0.0510 105 ASP   A CB  
2205 C  CB  B ASP   A 105 ? 0.3388 0.3561 0.3186 -0.0141 0.0066  -0.0268 105 ASP   A CB  
2206 C  CG  A ASP   A 105 ? 0.3677 0.4889 0.3698 -0.0278 0.0596  -0.0622 105 ASP   A CG  
2207 C  CG  B ASP   A 105 ? 0.3461 0.3615 0.3485 -0.0105 0.0037  -0.0331 105 ASP   A CG  
2208 O  OD1 A ASP   A 105 ? 0.3768 0.4952 0.3838 -0.0257 0.0587  -0.0732 105 ASP   A OD1 
2209 O  OD1 B ASP   A 105 ? 0.3460 0.3624 0.3528 -0.0102 0.0018  -0.0362 105 ASP   A OD1 
2210 O  OD2 A ASP   A 105 ? 0.3771 0.4975 0.4094 -0.0237 0.0611  -0.0588 105 ASP   A OD2 
2211 O  OD2 B ASP   A 105 ? 0.3527 0.3644 0.3634 -0.0098 0.0003  -0.0339 105 ASP   A OD2 
2220 N  N   A ILE   A 106 ? 0.2542 0.4231 0.2002 -0.0723 0.0022  -0.0645 106 ILE   A N   
2221 N  N   B ILE   A 106 ? 0.3138 0.3439 0.2742 -0.0283 0.0062  -0.0214 106 ILE   A N   
2222 C  CA  A ILE   A 106 ? 0.2312 0.4053 0.2220 -0.0811 -0.0165 -0.0768 106 ILE   A CA  
2223 C  CA  B ILE   A 106 ? 0.3062 0.3393 0.2758 -0.0333 0.0077  -0.0239 106 ILE   A CA  
2224 C  C   A ILE   A 106 ? 0.2157 0.3771 0.2239 -0.0949 -0.0132 -0.0944 106 ILE   A C   
2225 C  C   B ILE   A 106 ? 0.3002 0.3291 0.2775 -0.0393 0.0138  -0.0297 106 ILE   A C   
2226 O  O   A ILE   A 106 ? 0.1928 0.3618 0.2219 -0.0974 0.0043  -0.0967 106 ILE   A O   
2227 O  O   B ILE   A 106 ? 0.2982 0.3258 0.2731 -0.0378 0.0152  -0.0308 106 ILE   A O   
2228 C  CB  A ILE   A 106 ? 0.2354 0.4139 0.2660 -0.0682 -0.0306 -0.0539 106 ILE   A CB  
2229 C  CB  B ILE   A 106 ? 0.3053 0.3438 0.2863 -0.0314 0.0034  -0.0183 106 ILE   A CB  
2230 C  CG1 A ILE   A 106 ? 0.2321 0.4122 0.3017 -0.0512 -0.0326 -0.0328 106 ILE   A CG1 
2231 C  CG1 B ILE   A 106 ? 0.3029 0.3434 0.2944 -0.0286 0.0023  -0.0117 106 ILE   A CG1 
2232 C  CG2 A ILE   A 106 ? 0.2407 0.4186 0.2799 -0.0696 -0.0402 -0.0517 106 ILE   A CG2 
2233 C  CG2 B ILE   A 106 ? 0.3066 0.3465 0.2902 -0.0316 0.0001  -0.0175 106 ILE   A CG2 
2234 C  CD1 A ILE   A 106 ? 0.2348 0.4086 0.3178 -0.0355 -0.0246 -0.0186 106 ILE   A CD1 
2235 C  CD1 B ILE   A 106 ? 0.3021 0.3422 0.2973 -0.0260 0.0036  -0.0075 106 ILE   A CD1 
2258 N  N   A GLN   A 107 ? 0.2335 0.3646 0.2466 -0.0939 -0.0057 -0.1083 107 GLN   A N   
2259 N  N   B GLN   A 107 ? 0.2965 0.3214 0.2908 -0.0453 0.0207  -0.0348 107 GLN   A N   
2260 C  CA  A GLN   A 107 ? 0.2653 0.3491 0.3229 -0.0786 0.0230  -0.1023 107 GLN   A CA  
2261 C  CA  B GLN   A 107 ? 0.2911 0.3115 0.3090 -0.0493 0.0309  -0.0405 107 GLN   A CA  
2262 C  C   A GLN   A 107 ? 0.2416 0.2947 0.3061 -0.0682 0.0513  -0.0787 107 GLN   A C   
2263 C  C   B GLN   A 107 ? 0.2558 0.2810 0.2802 -0.0551 0.0456  -0.0506 107 GLN   A C   
2264 O  O   A GLN   A 107 ? 0.2442 0.2852 0.3564 -0.0605 0.0676  -0.0839 107 GLN   A O   
2265 O  O   B GLN   A 107 ? 0.2593 0.2814 0.2969 -0.0551 0.0492  -0.0541 107 GLN   A O   
2266 C  CB  A GLN   A 107 ? 0.3143 0.3839 0.4242 -0.0808 0.0158  -0.1016 107 GLN   A CB  
2267 C  CB  B GLN   A 107 ? 0.3182 0.3299 0.3586 -0.0488 0.0231  -0.0321 107 GLN   A CB  
2268 C  CG  A GLN   A 107 ? 0.3637 0.4169 0.5335 -0.0772 0.0089  -0.0883 107 GLN   A CG  
2269 C  CG  B GLN   A 107 ? 0.3412 0.3450 0.4086 -0.0476 0.0156  -0.0216 107 GLN   A CG  
2270 C  CD  A GLN   A 107 ? 0.4102 0.4433 0.6260 -0.0730 0.0043  -0.0762 107 GLN   A CD  
2271 C  CD  B GLN   A 107 ? 0.3595 0.3568 0.4521 -0.0449 0.0090  -0.0116 107 GLN   A CD  
2272 O  OE1 A GLN   A 107 ? 0.4240 0.4513 0.6633 -0.0726 0.0029  -0.0753 107 GLN   A OE1 
2273 O  OE1 B GLN   A 107 ? 0.3678 0.3619 0.4626 -0.0448 0.0077  -0.0071 107 GLN   A OE1 
2274 N  NE2 A GLN   A 107 ? 0.4162 0.4499 0.6576 -0.0715 0.0016  -0.0731 107 GLN   A NE2 
2275 N  NE2 B GLN   A 107 ? 0.3634 0.3601 0.4657 -0.0433 0.0059  -0.0082 107 GLN   A NE2 
2292 N  N   . LEU   A 108 ? 0.2166 0.2497 0.2386 -0.0604 0.0522  -0.0636 108 LEU   A N   
2293 C  CA  . LEU   A 108 ? 0.1863 0.1939 0.2097 -0.0240 0.0458  -0.0298 108 LEU   A CA  
2294 C  C   . LEU   A 108 ? 0.1589 0.1432 0.2067 -0.0083 0.0359  -0.0025 108 LEU   A C   
2295 O  O   . LEU   A 108 ? 0.1542 0.1457 0.2199 -0.0030 0.0364  0.0057  108 LEU   A O   
2296 C  CB  . LEU   A 108 ? 0.1874 0.2050 0.1841 -0.0290 0.0443  -0.0244 108 LEU   A CB  
2297 C  CG  . LEU   A 108 ? 0.2016 0.2303 0.2098 -0.0297 0.0537  -0.0229 108 LEU   A CG  
2298 C  CD1 . LEU   A 108 ? 0.2196 0.2378 0.2054 -0.0375 0.0649  -0.0152 108 LEU   A CD1 
2299 C  CD2 . LEU   A 108 ? 0.2080 0.2517 0.2626 -0.0215 0.0393  -0.0169 108 LEU   A CD2 
2312 N  N   . LEU   A 109 ? 0.1497 0.1415 0.2011 0.0008  0.0308  0.0103  109 LEU   A N   
2313 C  CA  . LEU   A 109 ? 0.1437 0.1326 0.1761 0.0006  0.0144  0.0144  109 LEU   A CA  
2314 C  C   . LEU   A 109 ? 0.1324 0.1319 0.1601 -0.0100 0.0167  0.0086  109 LEU   A C   
2315 O  O   . LEU   A 109 ? 0.1415 0.1279 0.1760 -0.0029 0.0025  0.0043  109 LEU   A O   
2316 C  CB  . LEU   A 109 ? 0.1490 0.1397 0.1898 0.0068  0.0044  0.0231  109 LEU   A CB  
2317 C  CG  . LEU   A 109 ? 0.1383 0.1477 0.1844 0.0102  0.0109  0.0330  109 LEU   A CG  
2318 C  CD1 . LEU   A 109 ? 0.1506 0.1421 0.2008 0.0034  0.0142  0.0104  109 LEU   A CD1 
2319 C  CD2 . LEU   A 109 ? 0.1412 0.1723 0.1988 0.0005  0.0085  0.0332  109 LEU   A CD2 
2331 N  N   . LYS   A 110 ? 0.1311 0.1305 0.1584 -0.0061 0.0044  0.0030  110 LYS   A N   
2332 C  CA  . LYS   A 110 ? 0.1321 0.1268 0.1683 -0.0046 -0.0007 0.0058  110 LYS   A CA  
2333 C  C   . LYS   A 110 ? 0.1348 0.1189 0.1590 -0.0079 0.0047  -0.0092 110 LYS   A C   
2334 O  O   . LYS   A 110 ? 0.1286 0.1213 0.1683 -0.0096 0.0099  -0.0074 110 LYS   A O   
2335 C  CB  . LYS   A 110 ? 0.1388 0.1312 0.1902 -0.0045 -0.0055 -0.0041 110 LYS   A CB  
2336 C  CG  . LYS   A 110 ? 0.1411 0.1256 0.1940 -0.0053 -0.0074 -0.0001 110 LYS   A CG  
2337 C  CD  . LYS   A 110 ? 0.1440 0.1314 0.2089 -0.0107 -0.0065 -0.0068 110 LYS   A CD  
2338 C  CE  . LYS   A 110 ? 0.1514 0.1385 0.2250 -0.0065 0.0131  -0.0104 110 LYS   A CE  
2339 N  NZ  . LYS   A 110 ? 0.1539 0.1431 0.2451 -0.0156 0.0214  -0.0096 110 LYS   A NZ  
2353 N  N   . SER   A 111 ? 0.1312 0.1242 0.1680 -0.0039 0.0030  -0.0005 111 SER   A N   
2354 C  CA  . SER   A 111 ? 0.1273 0.1298 0.1746 -0.0047 0.0104  0.0053  111 SER   A CA  
2355 C  C   . SER   A 111 ? 0.1241 0.1235 0.1681 -0.0071 0.0118  0.0066  111 SER   A C   
2356 O  O   . SER   A 111 ? 0.1367 0.1173 0.1838 -0.0043 0.0131  0.0080  111 SER   A O   
2357 C  CB  . SER   A 111 ? 0.1468 0.1451 0.1862 -0.0060 0.0168  -0.0085 111 SER   A CB  
2358 O  OG  . SER   A 111 ? 0.1896 0.1630 0.2071 0.0011  0.0240  -0.0157 111 SER   A OG  
2364 N  N   . ALA   A 112 ? 0.1278 0.1178 0.1797 -0.0031 0.0210  0.0062  112 ALA   A N   
2365 C  CA  . ALA   A 112 ? 0.1303 0.1143 0.1673 -0.0039 0.0190  -0.0042 112 ALA   A CA  
2366 C  C   . ALA   A 112 ? 0.1267 0.1131 0.1711 -0.0035 0.0159  -0.0013 112 ALA   A C   
2367 O  O   . ALA   A 112 ? 0.1281 0.1165 0.1713 -0.0134 0.0197  0.0059  112 ALA   A O   
2368 C  CB  . ALA   A 112 ? 0.1399 0.1191 0.1702 -0.0027 0.0212  -0.0042 112 ALA   A CB  
2374 N  N   . TYR   A 113 ? 0.1187 0.1189 0.1726 -0.0066 0.0144  0.0051  113 TYR   A N   
2375 C  CA  . TYR   A 113 ? 0.1155 0.1159 0.1721 -0.0059 0.0135  0.0143  113 TYR   A CA  
2376 C  C   . TYR   A 113 ? 0.1142 0.1176 0.1606 -0.0101 0.0138  0.0050  113 TYR   A C   
2377 O  O   . TYR   A 113 ? 0.1165 0.1182 0.1747 -0.0057 0.0149  0.0032  113 TYR   A O   
2378 C  CB  . TYR   A 113 ? 0.1185 0.1218 0.1718 -0.0050 0.0036  0.0178  113 TYR   A CB  
2379 C  CG  . TYR   A 113 ? 0.1197 0.1256 0.1622 -0.0118 0.0121  0.0163  113 TYR   A CG  
2380 C  CD1 . TYR   A 113 ? 0.1233 0.1316 0.1540 -0.0040 0.0135  0.0219  113 TYR   A CD1 
2381 C  CD2 . TYR   A 113 ? 0.1275 0.1299 0.1622 -0.0118 0.0032  0.0172  113 TYR   A CD2 
2382 C  CE1 . TYR   A 113 ? 0.1229 0.1381 0.1550 -0.0061 0.0103  0.0261  113 TYR   A CE1 
2383 C  CE2 . TYR   A 113 ? 0.1261 0.1313 0.1619 -0.0127 0.0018  0.0210  113 TYR   A CE2 
2384 C  CZ  . TYR   A 113 ? 0.1288 0.1330 0.1561 -0.0038 0.0078  0.0323  113 TYR   A CZ  
2385 O  OH  . TYR   A 113 ? 0.1205 0.1423 0.1731 0.0090  0.0107  0.0248  113 TYR   A OH  
2395 N  N   . GLU   A 114 ? 0.1186 0.1153 0.1633 -0.0083 0.0166  0.0078  114 GLU   A N   
2396 C  CA  . GLU   A 114 ? 0.1212 0.1111 0.1733 0.0015  0.0076  0.0138  114 GLU   A CA  
2397 C  C   . GLU   A 114 ? 0.1178 0.1173 0.1721 0.0010  0.0137  0.0113  114 GLU   A C   
2398 O  O   . GLU   A 114 ? 0.1274 0.1160 0.1776 -0.0016 0.0067  0.0062  114 GLU   A O   
2399 C  CB  . GLU   A 114 ? 0.1215 0.1127 0.1835 -0.0071 0.0056  0.0120  114 GLU   A CB  
2400 C  CG  . GLU   A 114 ? 0.1271 0.1163 0.1878 0.0012  0.0049  0.0058  114 GLU   A CG  
2401 C  CD  . GLU   A 114 ? 0.1322 0.1198 0.1902 -0.0052 0.0039  0.0030  114 GLU   A CD  
2402 O  OE1 . GLU   A 114 ? 0.1374 0.1214 0.1918 -0.0084 0.0146  -0.0058 114 GLU   A OE1 
2403 O  OE2 . GLU   A 114 ? 0.1559 0.1279 0.2032 -0.0117 0.0163  -0.0131 114 GLU   A OE2 
2410 N  N   . ASN   A 115 ? 0.1201 0.1177 0.1645 -0.0054 0.0130  0.0058  115 ASN   A N   
2411 C  CA  . ASN   A 115 ? 0.1209 0.1208 0.1728 -0.0067 0.0157  0.0141  115 ASN   A CA  
2412 C  C   . ASN   A 115 ? 0.1240 0.1179 0.1709 -0.0083 0.0072  0.0063  115 ASN   A C   
2413 O  O   . ASN   A 115 ? 0.1255 0.1285 0.1662 -0.0104 0.0123  0.0163  115 ASN   A O   
2414 C  CB  . ASN   A 115 ? 0.1336 0.1278 0.1715 -0.0124 0.0096  0.0104  115 ASN   A CB  
2415 C  CG  . ASN   A 115 ? 0.1306 0.1509 0.1700 -0.0191 0.0233  0.0147  115 ASN   A CG  
2416 O  OD1 . ASN   A 115 ? 0.1338 0.2436 0.2037 -0.0166 0.0294  0.0246  115 ASN   A OD1 
2417 N  ND2 . ASN   A 115 ? 0.1300 0.1308 0.1647 -0.0095 0.0317  0.0121  115 ASN   A ND2 
2424 N  N   . PHE   A 116 ? 0.1185 0.1226 0.1682 -0.0041 0.0136  0.0194  116 PHE   A N   
2425 C  CA  . PHE   A 116 ? 0.1165 0.1269 0.1610 -0.0040 0.0115  0.0120  116 PHE   A CA  
2426 C  C   . PHE   A 116 ? 0.1175 0.1321 0.1624 -0.0073 0.0199  0.0181  116 PHE   A C   
2427 O  O   . PHE   A 116 ? 0.1265 0.1396 0.1722 -0.0008 0.0099  0.0268  116 PHE   A O   
2428 C  CB  . PHE   A 116 ? 0.1206 0.1183 0.1734 -0.0056 0.0160  0.0157  116 PHE   A CB  
2429 C  CG  . PHE   A 116 ? 0.1211 0.1209 0.1632 -0.0099 0.0127  0.0112  116 PHE   A CG  
2430 C  CD1 . PHE   A 116 ? 0.1265 0.1201 0.1596 -0.0078 0.0106  0.0106  116 PHE   A CD1 
2431 C  CD2 . PHE   A 116 ? 0.1291 0.1283 0.1638 -0.0096 0.0170  0.0172  116 PHE   A CD2 
2432 C  CE1 . PHE   A 116 ? 0.1276 0.1191 0.1680 -0.0113 0.0129  0.0058  116 PHE   A CE1 
2433 C  CE2 . PHE   A 116 ? 0.1272 0.1264 0.1746 -0.0050 0.0149  0.0074  116 PHE   A CE2 
2434 C  CZ  . PHE   A 116 ? 0.1297 0.1133 0.1666 -0.0048 0.0078  0.0106  116 PHE   A CZ  
2444 N  N   . ASN   A 117 ? 0.1206 0.1245 0.1712 -0.0026 0.0110  0.0230  117 ASN   A N   
2445 C  CA  . ASN   A 117 ? 0.1229 0.1273 0.1774 -0.0078 0.0119  0.0238  117 ASN   A CA  
2446 C  C   . ASN   A 117 ? 0.1246 0.1318 0.1870 -0.0038 0.0151  0.0276  117 ASN   A C   
2447 O  O   . ASN   A 117 ? 0.1323 0.1398 0.2151 -0.0096 -0.0085 0.0427  117 ASN   A O   
2448 C  CB  . ASN   A 117 ? 0.1219 0.1331 0.1852 -0.0020 0.0056  0.0296  117 ASN   A CB  
2449 C  CG  . ASN   A 117 ? 0.1210 0.1303 0.1817 -0.0011 0.0108  0.0331  117 ASN   A CG  
2450 O  OD1 . ASN   A 117 ? 0.1236 0.1496 0.1945 -0.0122 0.0132  0.0234  117 ASN   A OD1 
2451 N  ND2 . ASN   A 117 ? 0.1164 0.1308 0.1873 -0.0014 0.0081  0.0286  117 ASN   A ND2 
2458 N  N   . GLN   A 118 ? 0.1204 0.1370 0.1980 -0.0054 -0.0034 0.0300  118 GLN   A N   
2459 C  CA  . GLN   A 118 ? 0.1268 0.1485 0.2003 -0.0037 -0.0072 0.0243  118 GLN   A CA  
2460 C  C   . GLN   A 118 ? 0.1294 0.1522 0.1874 -0.0099 -0.0058 0.0272  118 GLN   A C   
2461 O  O   . GLN   A 118 ? 0.1292 0.1852 0.2152 -0.0007 -0.0122 0.0076  118 GLN   A O   
2462 C  CB  . GLN   A 118 ? 0.1225 0.1508 0.2040 -0.0038 0.0025  0.0266  118 GLN   A CB  
2463 C  CG  . GLN   A 118 ? 0.1230 0.1482 0.1949 -0.0055 0.0095  0.0258  118 GLN   A CG  
2464 C  CD  . GLN   A 118 ? 0.1247 0.1497 0.2085 0.0032  0.0084  0.0211  118 GLN   A CD  
2465 O  OE1 . GLN   A 118 ? 0.1244 0.1650 0.2301 0.0106  0.0026  0.0162  118 GLN   A OE1 
2466 N  NE2 . GLN   A 118 ? 0.1318 0.1454 0.2106 0.0014  0.0026  0.0190  118 GLN   A NE2 
2475 N  N   . HIS   A 119 ? 0.1351 0.1469 0.1740 -0.0063 -0.0014 0.0295  119 HIS   A N   
2476 C  CA  . HIS   A 119 ? 0.1396 0.1547 0.1767 -0.0079 -0.0055 0.0309  119 HIS   A CA  
2477 C  C   . HIS   A 119 ? 0.1502 0.1633 0.1679 -0.0093 0.0042  0.0285  119 HIS   A C   
2478 O  O   . HIS   A 119 ? 0.1546 0.1697 0.1775 -0.0273 -0.0027 0.0352  119 HIS   A O   
2479 C  CB  . HIS   A 119 ? 0.1437 0.1494 0.1943 -0.0065 0.0152  0.0348  119 HIS   A CB  
2480 C  CG  . HIS   A 119 ? 0.1513 0.1539 0.2430 -0.0012 0.0110  0.0394  119 HIS   A CG  
2481 N  ND1 . HIS   A 119 ? 0.1614 0.1769 0.2952 -0.0152 0.0085  0.0369  119 HIS   A ND1 
2482 C  CD2 . HIS   A 119 ? 0.1577 0.1602 0.2584 0.0086  0.0310  0.0541  119 HIS   A CD2 
2483 C  CE1 . HIS   A 119 ? 0.1592 0.1721 0.3092 -0.0197 0.0277  0.0520  119 HIS   A CE1 
2484 N  NE2 . HIS   A 119 ? 0.1693 0.1641 0.2984 -0.0011 0.0431  0.0611  119 HIS   A NE2 
2492 N  N   . GLU   A 120 ? 0.1595 0.1889 0.1756 -0.0081 -0.0077 0.0534  120 GLU   A N   
2493 C  CA  . GLU   A 120 ? 0.1872 0.2233 0.1995 0.0049  -0.0078 0.0988  120 GLU   A CA  
2494 C  C   . GLU   A 120 ? 0.1641 0.2048 0.1804 -0.0075 -0.0074 0.0879  120 GLU   A C   
2495 O  O   . GLU   A 120 ? 0.1608 0.1947 0.1910 -0.0197 -0.0050 0.0800  120 GLU   A O   
2496 C  CB  . GLU   A 120 ? 0.2746 0.3047 0.2574 0.0263  -0.0117 0.1502  120 GLU   A CB  
2497 C  CG  . GLU   A 120 ? 0.3844 0.4022 0.3958 0.0377  -0.0094 0.1440  120 GLU   A CG  
2498 C  CD  . GLU   A 120 ? 0.5033 0.5015 0.5384 0.0414  0.0022  0.1190  120 GLU   A CD  
2499 O  OE1 . GLU   A 120 ? 0.5221 0.5103 0.5676 0.0427  0.0044  0.1110  120 GLU   A OE1 
2500 O  OE2 . GLU   A 120 ? 0.5510 0.5510 0.6040 0.0411  0.0080  0.1096  120 GLU   A OE2 
2507 N  N   . VAL   A 121 ? 0.1572 0.2048 0.1548 -0.0075 -0.0024 0.0675  121 VAL   A N   
2508 C  CA  . VAL   A 121 ? 0.1667 0.2077 0.1468 -0.0150 0.0052  0.0633  121 VAL   A CA  
2509 C  C   . VAL   A 121 ? 0.1548 0.1868 0.1323 -0.0249 0.0008  0.0496  121 VAL   A C   
2510 O  O   . VAL   A 121 ? 0.1557 0.1926 0.1540 -0.0308 -0.0131 0.0429  121 VAL   A O   
2511 C  CB  . VAL   A 121 ? 0.2057 0.2447 0.1806 -0.0010 0.0203  0.0700  121 VAL   A CB  
2512 C  CG1 . VAL   A 121 ? 0.2081 0.2605 0.1873 0.0075  0.0303  0.0729  121 VAL   A CG1 
2513 C  CG2 . VAL   A 121 ? 0.2288 0.2608 0.2250 -0.0067 0.0203  0.0522  121 VAL   A CG2 
2523 N  N   . LEU   A 122 ? 0.1473 0.1614 0.1458 -0.0223 0.0004  0.0403  122 LEU   A N   
2524 C  CA  . LEU   A 122 ? 0.1484 0.1506 0.1429 -0.0206 0.0134  0.0347  122 LEU   A CA  
2525 C  C   . LEU   A 122 ? 0.1440 0.1496 0.1429 -0.0244 0.0039  0.0281  122 LEU   A C   
2526 O  O   . LEU   A 122 ? 0.1471 0.1564 0.1668 -0.0287 0.0009  0.0340  122 LEU   A O   
2527 C  CB  . LEU   A 122 ? 0.1645 0.1580 0.1724 -0.0062 0.0035  0.0415  122 LEU   A CB  
2528 C  CG  . LEU   A 122 ? 0.1651 0.1649 0.1620 -0.0110 0.0146  0.0386  122 LEU   A CG  
2529 C  CD1 . LEU   A 122 ? 0.1795 0.1618 0.1874 -0.0203 0.0200  0.0434  122 LEU   A CD1 
2530 C  CD2 . LEU   A 122 ? 0.1606 0.1577 0.1599 -0.0093 0.0226  0.0294  122 LEU   A CD2 
2542 N  N   A LEU   A 123 ? 0.1401 0.1487 0.1428 -0.0226 -0.0011 0.0243  123 LEU   A N   
2543 N  N   B LEU   A 123 ? 0.1434 0.1465 0.1373 -0.0232 0.0041  0.0263  123 LEU   A N   
2544 C  CA  A LEU   A 123 ? 0.1434 0.1480 0.1331 -0.0199 0.0041  0.0280  123 LEU   A CA  
2545 C  CA  B LEU   A 123 ? 0.1441 0.1440 0.1354 -0.0211 0.0055  0.0239  123 LEU   A CA  
2546 C  C   A LEU   A 123 ? 0.1344 0.1397 0.1165 -0.0199 0.0041  0.0260  123 LEU   A C   
2547 C  C   B LEU   A 123 ? 0.1388 0.1392 0.1191 -0.0184 0.0090  0.0237  123 LEU   A C   
2548 O  O   A LEU   A 123 ? 0.1284 0.1436 0.1347 -0.0216 0.0062  0.0237  123 LEU   A O   
2549 O  O   B LEU   A 123 ? 0.1372 0.1391 0.1185 -0.0155 0.0128  0.0200  123 LEU   A O   
2550 C  CB  A LEU   A 123 ? 0.1508 0.1592 0.1271 -0.0247 0.0176  0.0294  123 LEU   A CB  
2551 C  CB  B LEU   A 123 ? 0.1483 0.1459 0.1481 -0.0258 0.0063  0.0220  123 LEU   A CB  
2552 C  CG  A LEU   A 123 ? 0.1568 0.1728 0.1413 -0.0138 0.0125  0.0143  123 LEU   A CG  
2553 C  CG  B LEU   A 123 ? 0.1473 0.1430 0.1462 -0.0321 0.0093  0.0218  123 LEU   A CG  
2554 C  CD1 A LEU   A 123 ? 0.1576 0.1830 0.1628 -0.0006 0.0124  0.0016  123 LEU   A CD1 
2555 C  CD1 B LEU   A 123 ? 0.1473 0.1413 0.1498 -0.0348 0.0121  0.0243  123 LEU   A CD1 
2556 C  CD2 A LEU   A 123 ? 0.1687 0.1757 0.1544 -0.0119 0.0130  0.0104  123 LEU   A CD2 
2557 C  CD2 B LEU   A 123 ? 0.1494 0.1428 0.1485 -0.0320 0.0110  0.0188  123 LEU   A CD2 
2580 N  N   . ALA   A 124 ? 0.1350 0.1323 0.1159 -0.0179 0.0110  0.0250  124 ALA   A N   
2581 C  CA  . ALA   A 124 ? 0.1313 0.1322 0.1258 -0.0148 0.0065  0.0225  124 ALA   A CA  
2582 C  C   . ALA   A 124 ? 0.1270 0.1289 0.1188 -0.0131 0.0129  0.0219  124 ALA   A C   
2583 O  O   . ALA   A 124 ? 0.1228 0.1394 0.1498 -0.0110 0.0182  0.0287  124 ALA   A O   
2584 C  CB  . ALA   A 124 ? 0.1365 0.1338 0.1468 -0.0114 0.0053  0.0240  124 ALA   A CB  
2591 N  N   A PRO   A 125 ? 0.1181 0.1243 0.1339 -0.0103 0.0058  0.0251  125 PRO   A N   
2592 N  N   B PRO   A 125 ? 0.1309 0.1297 0.1166 -0.0130 0.0113  0.0161  125 PRO   A N   
2593 C  CA  A PRO   A 125 ? 0.1204 0.1229 0.1401 -0.0034 0.0050  0.0226  125 PRO   A CA  
2594 C  CA  B PRO   A 125 ? 0.1342 0.1296 0.1183 -0.0132 0.0121  0.0096  125 PRO   A CA  
2595 C  C   A PRO   A 125 ? 0.1165 0.1286 0.1315 -0.0067 0.0009  0.0270  125 PRO   A C   
2596 C  C   B PRO   A 125 ? 0.1333 0.1292 0.1211 -0.0144 0.0115  0.0120  125 PRO   A C   
2597 O  O   A PRO   A 125 ? 0.1239 0.1339 0.1468 0.0019  -0.0032 0.0179  125 PRO   A O   
2598 O  O   B PRO   A 125 ? 0.1356 0.1241 0.1243 -0.0200 0.0099  0.0157  125 PRO   A O   
2599 C  CB  A PRO   A 125 ? 0.1310 0.1228 0.1390 -0.0083 0.0126  0.0221  125 PRO   A CB  
2600 C  CB  B PRO   A 125 ? 0.1377 0.1307 0.1189 -0.0129 0.0156  0.0069  125 PRO   A CB  
2601 C  CG  A PRO   A 125 ? 0.1291 0.1157 0.1325 -0.0106 0.0126  0.0150  125 PRO   A CG  
2602 C  CG  B PRO   A 125 ? 0.1403 0.1318 0.1203 -0.0125 0.0084  0.0075  125 PRO   A CG  
2603 C  CD  A PRO   A 125 ? 0.1194 0.1212 0.1350 -0.0174 0.0094  0.0200  125 PRO   A CD  
2604 C  CD  B PRO   A 125 ? 0.1353 0.1336 0.1198 -0.0139 0.0103  0.0091  125 PRO   A CD  
2619 N  N   A LEU   A 126 ? 0.1148 0.1329 0.1366 0.0038  0.0074  0.0205  126 LEU   A N   
2620 N  N   B LEU   A 126 ? 0.1337 0.1297 0.1304 -0.0097 0.0118  0.0107  126 LEU   A N   
2621 C  CA  A LEU   A 126 ? 0.1214 0.1363 0.1485 -0.0040 0.0076  0.0191  126 LEU   A CA  
2622 C  CA  B LEU   A 126 ? 0.1266 0.1247 0.1265 -0.0092 0.0175  0.0074  126 LEU   A CA  
2623 C  C   A LEU   A 126 ? 0.1306 0.1334 0.1495 -0.0018 -0.0012 0.0193  126 LEU   A C   
2624 C  C   B LEU   A 126 ? 0.1251 0.1188 0.1242 -0.0022 0.0196  0.0096  126 LEU   A C   
2625 O  O   A LEU   A 126 ? 0.1445 0.1306 0.1711 -0.0020 0.0102  0.0147  126 LEU   A O   
2626 O  O   B LEU   A 126 ? 0.1307 0.1087 0.1349 -0.0057 0.0318  0.0191  126 LEU   A O   
2627 C  CB  A LEU   A 126 ? 0.1308 0.1421 0.1563 -0.0016 -0.0068 0.0162  126 LEU   A CB  
2628 C  CB  B LEU   A 126 ? 0.1237 0.1271 0.1317 -0.0130 0.0182  0.0020  126 LEU   A CB  
2629 C  CG  A LEU   A 126 ? 0.1315 0.1536 0.1813 -0.0053 0.0082  0.0166  126 LEU   A CG  
2630 C  CG  B LEU   A 126 ? 0.1142 0.1237 0.1321 -0.0127 0.0230  -0.0049 126 LEU   A CG  
2631 C  CD1 A LEU   A 126 ? 0.1413 0.1669 0.2153 -0.0062 0.0064  0.0217  126 LEU   A CD1 
2632 C  CD1 B LEU   A 126 ? 0.1158 0.1242 0.1418 -0.0162 0.0186  -0.0068 126 LEU   A CD1 
2633 C  CD2 A LEU   A 126 ? 0.1452 0.1464 0.1666 -0.0082 0.0172  0.0163  126 LEU   A CD2 
2634 C  CD2 B LEU   A 126 ? 0.1098 0.1266 0.1334 -0.0136 0.0235  -0.0102 126 LEU   A CD2 
2657 N  N   A LEU   A 127 ? 0.1348 0.1405 0.1443 0.0031  0.0060  0.0253  127 LEU   A N   
2658 N  N   B LEU   A 127 ? 0.1199 0.1257 0.1196 0.0060  0.0133  0.0157  127 LEU   A N   
2659 C  CA  A LEU   A 127 ? 0.1319 0.1463 0.1293 -0.0052 0.0006  0.0177  127 LEU   A CA  
2660 C  CA  B LEU   A 127 ? 0.1109 0.1343 0.1138 0.0074  0.0037  0.0211  127 LEU   A CA  
2661 C  C   A LEU   A 127 ? 0.1275 0.1324 0.1296 -0.0039 0.0028  0.0072  127 LEU   A C   
2662 C  C   B LEU   A 127 ? 0.1119 0.1252 0.1121 0.0074  0.0061  0.0213  127 LEU   A C   
2663 O  O   A LEU   A 127 ? 0.1339 0.1301 0.1492 -0.0157 -0.0000 0.0106  127 LEU   A O   
2664 O  O   B LEU   A 127 ? 0.1138 0.1247 0.1140 0.0079  0.0018  0.0291  127 LEU   A O   
2665 C  CB  A LEU   A 127 ? 0.1397 0.1589 0.1492 0.0034  0.0088  0.0229  127 LEU   A CB  
2666 C  CB  B LEU   A 127 ? 0.1010 0.1487 0.1132 0.0142  -0.0036 0.0268  127 LEU   A CB  
2667 C  CG  A LEU   A 127 ? 0.1507 0.1639 0.1694 0.0038  -0.0002 0.0236  127 LEU   A CG  
2668 C  CG  B LEU   A 127 ? 0.0934 0.1622 0.1066 0.0163  -0.0194 0.0331  127 LEU   A CG  
2669 C  CD1 A LEU   A 127 ? 0.1505 0.1571 0.1693 0.0026  0.0003  0.0159  127 LEU   A CD1 
2670 C  CD1 B LEU   A 127 ? 0.0914 0.1651 0.1199 0.0200  -0.0123 0.0344  127 LEU   A CD1 
2671 C  CD2 A LEU   A 127 ? 0.1686 0.1647 0.1829 0.0146  0.0008  0.0147  127 LEU   A CD2 
2672 C  CD2 B LEU   A 127 ? 0.0988 0.1738 0.1065 0.0166  -0.0328 0.0274  127 LEU   A CD2 
2695 N  N   A SER   A 128 ? 0.1329 0.1335 0.1289 -0.0112 -0.0034 0.0058  128 SER   A N   
2696 N  N   B SER   A 128 ? 0.1169 0.1227 0.1195 -0.0002 0.0027  0.0164  128 SER   A N   
2697 C  CA  A SER   A 128 ? 0.1426 0.1426 0.1217 -0.0089 -0.0042 0.0130  128 SER   A CA  
2698 C  CA  B SER   A 128 ? 0.1205 0.1229 0.1225 -0.0055 -0.0032 0.0135  128 SER   A CA  
2699 C  C   A SER   A 128 ? 0.1464 0.1389 0.1219 0.0030  -0.0104 0.0185  128 SER   A C   
2700 C  C   B SER   A 128 ? 0.1241 0.1199 0.1335 -0.0110 -0.0107 0.0121  128 SER   A C   
2701 O  O   A SER   A 128 ? 0.1653 0.1560 0.1470 0.0069  -0.0085 0.0117  128 SER   A O   
2702 O  O   B SER   A 128 ? 0.1213 0.1212 0.1358 -0.0144 -0.0165 0.0076  128 SER   A O   
2703 C  CB  A SER   A 128 ? 0.1413 0.1545 0.1312 -0.0101 0.0032  0.0119  128 SER   A CB  
2704 C  CB  B SER   A 128 ? 0.1193 0.1261 0.1250 -0.0017 -0.0031 0.0102  128 SER   A CB  
2705 O  OG  A SER   A 128 ? 0.1478 0.1602 0.1409 -0.0083 0.0127  0.0137  128 SER   A OG  
2706 O  OG  B SER   A 128 ? 0.1213 0.1275 0.1331 0.0011  0.0025  0.0091  128 SER   A OG  
2717 N  N   A ALA   A 129 ? 0.1379 0.1447 0.1496 0.0016  -0.0100 0.0295  129 ALA   A N   
2718 N  N   B ALA   A 129 ? 0.1296 0.1246 0.1471 -0.0114 -0.0119 0.0158  129 ALA   A N   
2719 C  CA  A ALA   A 129 ? 0.1355 0.1532 0.1747 0.0052  -0.0011 0.0291  129 ALA   A CA  
2720 C  CA  B ALA   A 129 ? 0.1346 0.1316 0.1576 -0.0092 -0.0082 0.0136  129 ALA   A CA  
2721 C  C   A ALA   A 129 ? 0.1407 0.1492 0.1511 0.0031  -0.0142 0.0177  129 ALA   A C   
2722 C  C   B ALA   A 129 ? 0.1390 0.1330 0.1569 -0.0080 -0.0013 0.0047  129 ALA   A C   
2723 O  O   A ALA   A 129 ? 0.1438 0.1589 0.1380 -0.0026 -0.0106 0.0244  129 ALA   A O   
2724 O  O   B ALA   A 129 ? 0.1366 0.1335 0.1593 -0.0079 0.0053  0.0038  129 ALA   A O   
2725 C  CB  A ALA   A 129 ? 0.1399 0.1697 0.2001 0.0065  0.0161  0.0463  129 ALA   A CB  
2726 C  CB  B ALA   A 129 ? 0.1361 0.1374 0.1581 -0.0092 -0.0085 0.0188  129 ALA   A CB  
2737 N  N   A GLY   A 130 ? 0.1420 0.1428 0.1718 -0.0008 -0.0151 0.0169  130 GLY   A N   
2738 N  N   B GLY   A 130 ? 0.1456 0.1357 0.1667 -0.0074 0.0039  0.0009  130 GLY   A N   
2739 C  CA  A GLY   A 130 ? 0.1611 0.1441 0.1679 0.0079  -0.0136 0.0080  130 GLY   A CA  
2740 C  CA  B GLY   A 130 ? 0.1556 0.1396 0.1641 -0.0024 0.0038  -0.0006 130 GLY   A CA  
2741 C  C   A GLY   A 130 ? 0.1690 0.1331 0.1477 0.0082  -0.0197 0.0054  130 GLY   A C   
2742 C  C   B GLY   A 130 ? 0.1614 0.1411 0.1596 -0.0002 0.0036  -0.0022 130 GLY   A C   
2743 O  O   A GLY   A 130 ? 0.1684 0.1293 0.1511 0.0041  -0.0127 0.0035  130 GLY   A O   
2744 O  O   B GLY   A 130 ? 0.1610 0.1378 0.1554 0.0004  0.0112  -0.0081 130 GLY   A O   
2751 N  N   A ILE   A 131 ? 0.1789 0.1310 0.1551 -0.0010 -0.0220 0.0087  131 ILE   A N   
2752 N  N   B ILE   A 131 ? 0.1681 0.1468 0.1687 -0.0028 -0.0095 0.0042  131 ILE   A N   
2753 C  CA  A ILE   A 131 ? 0.1914 0.1291 0.1368 -0.0074 -0.0256 0.0111  131 ILE   A CA  
2754 C  CA  B ILE   A 131 ? 0.1751 0.1518 0.1697 -0.0028 -0.0194 0.0081  131 ILE   A CA  
2755 C  C   A ILE   A 131 ? 0.1745 0.1320 0.1283 -0.0143 -0.0237 0.0224  131 ILE   A C   
2756 C  C   B ILE   A 131 ? 0.1725 0.1630 0.1676 -0.0027 -0.0198 0.0152  131 ILE   A C   
2757 O  O   A ILE   A 131 ? 0.1717 0.1313 0.1519 -0.0199 -0.0256 0.0201  131 ILE   A O   
2758 O  O   B ILE   A 131 ? 0.1729 0.1694 0.1708 -0.0048 -0.0240 0.0191  131 ILE   A O   
2759 C  CB  A ILE   A 131 ? 0.2171 0.1460 0.1535 -0.0209 -0.0290 -0.0001 131 ILE   A CB  
2760 C  CB  B ILE   A 131 ? 0.1834 0.1495 0.1681 -0.0073 -0.0315 0.0071  131 ILE   A CB  
2761 C  CG1 A ILE   A 131 ? 0.2295 0.1805 0.1422 -0.0334 -0.0411 0.0068  131 ILE   A CG1 
2762 C  CG1 B ILE   A 131 ? 0.1892 0.1589 0.1658 -0.0043 -0.0392 0.0058  131 ILE   A CG1 
2763 C  CG2 A ILE   A 131 ? 0.2295 0.1309 0.1974 -0.0137 -0.0093 -0.0147 131 ILE   A CG2 
2764 C  CG2 B ILE   A 131 ? 0.1850 0.1425 0.1750 -0.0121 -0.0279 0.0043  131 ILE   A CG2 
2765 C  CD1 A ILE   A 131 ? 0.2360 0.1963 0.1793 -0.0369 -0.0420 -0.0017 131 ILE   A CD1 
2766 C  CD1 B ILE   A 131 ? 0.1923 0.1635 0.1635 -0.0009 -0.0430 0.0105  131 ILE   A CD1 
2789 N  N   A PHE   A 132 ? 0.1646 0.1283 0.1187 -0.0080 -0.0131 0.0172  132 PHE   A N   
2790 N  N   B PHE   A 132 ? 0.1683 0.1658 0.1629 -0.0011 -0.0164 0.0138  132 PHE   A N   
2791 C  CA  A PHE   A 132 ? 0.1679 0.1341 0.1268 -0.0132 -0.0066 0.0154  132 PHE   A CA  
2792 C  CA  B PHE   A 132 ? 0.1702 0.1686 0.1614 -0.0012 -0.0097 0.0100  132 PHE   A CA  
2793 C  C   A PHE   A 132 ? 0.1753 0.1488 0.1355 -0.0136 -0.0098 0.0188  132 PHE   A C   
2794 C  C   B PHE   A 132 ? 0.1723 0.1700 0.1606 -0.0026 -0.0055 0.0128  132 PHE   A C   
2795 O  O   A PHE   A 132 ? 0.1806 0.1547 0.1426 -0.0165 -0.0093 0.0165  132 PHE   A O   
2796 O  O   B PHE   A 132 ? 0.1774 0.1724 0.1570 -0.0065 0.0007  0.0130  132 PHE   A O   
2797 C  CB  A PHE   A 132 ? 0.1619 0.1318 0.1256 -0.0085 -0.0082 0.0137  132 PHE   A CB  
2798 C  CB  B PHE   A 132 ? 0.1691 0.1711 0.1577 0.0021  -0.0087 0.0050  132 PHE   A CB  
2799 C  CG  A PHE   A 132 ? 0.1627 0.1283 0.1165 0.0017  -0.0088 0.0120  132 PHE   A CG  
2800 C  CG  B PHE   A 132 ? 0.1708 0.1745 0.1519 0.0081  -0.0089 -0.0023 132 PHE   A CG  
2801 C  CD1 A PHE   A 132 ? 0.1593 0.1311 0.1347 0.0066  -0.0119 0.0056  132 PHE   A CD1 
2802 C  CD1 B PHE   A 132 ? 0.1703 0.1781 0.1517 0.0125  -0.0082 0.0003  132 PHE   A CD1 
2803 C  CD2 A PHE   A 132 ? 0.1643 0.1334 0.1227 0.0016  -0.0041 0.0029  132 PHE   A CD2 
2804 C  CD2 B PHE   A 132 ? 0.1723 0.1749 0.1479 0.0095  -0.0082 -0.0081 132 PHE   A CD2 
2805 C  CE1 A PHE   A 132 ? 0.1610 0.1348 0.1373 -0.0017 -0.0175 -0.0025 132 PHE   A CE1 
2806 C  CE1 B PHE   A 132 ? 0.1698 0.1796 0.1428 0.0176  -0.0129 0.0003  132 PHE   A CE1 
2807 C  CE2 A PHE   A 132 ? 0.1588 0.1460 0.1430 0.0073  -0.0088 0.0049  132 PHE   A CE2 
2808 C  CE2 B PHE   A 132 ? 0.1702 0.1775 0.1516 0.0158  -0.0103 -0.0084 132 PHE   A CE2 
2809 C  CZ  A PHE   A 132 ? 0.1565 0.1479 0.1456 -0.0030 -0.0237 0.0057  132 PHE   A CZ  
2810 C  CZ  B PHE   A 132 ? 0.1681 0.1798 0.1421 0.0173  -0.0124 -0.0018 132 PHE   A CZ  
2829 N  N   A GLY   A 133 ? 0.1779 0.1571 0.1335 -0.0170 -0.0297 0.0190  133 GLY   A N   
2830 N  N   B GLY   A 133 ? 0.1708 0.1667 0.1623 -0.0031 -0.0113 0.0127  133 GLY   A N   
2831 C  CA  A GLY   A 133 ? 0.1828 0.1683 0.1435 -0.0175 -0.0314 0.0134  133 GLY   A CA  
2832 C  CA  B GLY   A 133 ? 0.1679 0.1640 0.1626 -0.0010 -0.0113 0.0093  133 GLY   A CA  
2833 C  C   A GLY   A 133 ? 0.1889 0.1782 0.1387 -0.0163 -0.0375 0.0058  133 GLY   A C   
2834 C  C   B GLY   A 133 ? 0.1659 0.1610 0.1603 0.0037  -0.0185 -0.0013 133 GLY   A C   
2835 O  O   A GLY   A 133 ? 0.2062 0.1964 0.1446 -0.0115 -0.0294 -0.0165 133 GLY   A O   
2836 O  O   B GLY   A 133 ? 0.1685 0.1583 0.1595 0.0082  -0.0220 -0.0187 133 GLY   A O   
2843 N  N   A ALA   A 134 ? 0.1863 0.1639 0.1348 -0.0236 -0.0257 0.0034  134 ALA   A N   
2844 N  N   B ALA   A 134 ? 0.1641 0.1578 0.1607 0.0025  -0.0172 -0.0030 134 ALA   A N   
2845 C  CA  A ALA   A 134 ? 0.1849 0.1671 0.1631 -0.0198 -0.0270 -0.0006 134 ALA   A CA  
2846 C  CA  B ALA   A 134 ? 0.1607 0.1559 0.1662 0.0036  -0.0194 -0.0070 134 ALA   A CA  
2847 C  C   A ALA   A 134 ? 0.1848 0.1698 0.1631 -0.0178 -0.0274 0.0053  134 ALA   A C   
2848 C  C   B ALA   A 134 ? 0.1592 0.1488 0.1593 0.0003  -0.0250 -0.0072 134 ALA   A C   
2849 O  O   A ALA   A 134 ? 0.1910 0.1817 0.1761 -0.0213 -0.0106 0.0046  134 ALA   A O   
2850 O  O   B ALA   A 134 ? 0.1593 0.1485 0.1628 -0.0041 -0.0210 -0.0112 134 ALA   A O   
2851 C  CB  A ALA   A 134 ? 0.1900 0.1651 0.1986 -0.0175 -0.0241 -0.0044 134 ALA   A CB  
2852 C  CB  B ALA   A 134 ? 0.1618 0.1586 0.1805 0.0068  -0.0181 -0.0079 134 ALA   A CB  
2863 N  N   A ASP   A 135 ? 0.1875 0.1721 0.1790 -0.0232 -0.0281 0.0109  135 ASP   A N   
2864 N  N   B ASP   A 135 ? 0.1629 0.1486 0.1605 -0.0059 -0.0307 -0.0008 135 ASP   A N   
2865 C  CA  A ASP   A 135 ? 0.1884 0.1833 0.2124 -0.0285 -0.0373 0.0182  135 ASP   A CA  
2866 C  CA  B ASP   A 135 ? 0.1630 0.1463 0.1650 -0.0104 -0.0314 0.0038  135 ASP   A CA  
2867 C  C   A ASP   A 135 ? 0.1746 0.1741 0.2109 -0.0216 -0.0291 0.0282  135 ASP   A C   
2868 C  C   B ASP   A 135 ? 0.1530 0.1375 0.1600 -0.0066 -0.0228 0.0026  135 ASP   A C   
2869 O  O   A ASP   A 135 ? 0.1727 0.1678 0.2140 -0.0153 -0.0258 0.0328  135 ASP   A O   
2870 O  O   B ASP   A 135 ? 0.1511 0.1346 0.1579 -0.0084 -0.0150 0.0056  135 ASP   A O   
2871 C  CB  A ASP   A 135 ? 0.2127 0.2128 0.2547 -0.0421 -0.0614 0.0064  135 ASP   A CB  
2872 C  CB  B ASP   A 135 ? 0.1703 0.1543 0.1683 -0.0166 -0.0416 0.0022  135 ASP   A CB  
2873 C  CG  A ASP   A 135 ? 0.2303 0.2377 0.2998 -0.0593 -0.0654 0.0048  135 ASP   A CG  
2874 C  CG  B ASP   A 135 ? 0.1729 0.1651 0.1821 -0.0189 -0.0439 0.0076  135 ASP   A CG  
2875 O  OD1 A ASP   A 135 ? 0.2253 0.2467 0.3009 -0.0633 -0.0683 0.0291  135 ASP   A OD1 
2876 O  OD1 B ASP   A 135 ? 0.1744 0.1656 0.1914 -0.0165 -0.0443 0.0150  135 ASP   A OD1 
2877 O  OD2 A ASP   A 135 ? 0.2577 0.2583 0.3440 -0.0622 -0.0476 -0.0038 135 ASP   A OD2 
2878 O  OD2 B ASP   A 135 ? 0.1745 0.1715 0.1974 -0.0233 -0.0477 0.0051  135 ASP   A OD2 
2887 N  N   A PRO   A 136 ? 0.1601 0.1682 0.2145 -0.0151 -0.0166 0.0334  136 PRO   A N   
2888 N  N   B PRO   A 136 ? 0.1453 0.1292 0.1581 0.0013  -0.0196 -0.0013 136 PRO   A N   
2889 C  CA  A PRO   A 136 ? 0.1482 0.1654 0.2225 -0.0187 -0.0042 0.0236  136 PRO   A CA  
2890 C  CA  B PRO   A 136 ? 0.1438 0.1335 0.1588 0.0008  -0.0105 -0.0113 136 PRO   A CA  
2891 C  C   A PRO   A 136 ? 0.1321 0.1602 0.2124 -0.0090 -0.0010 0.0153  136 PRO   A C   
2892 C  C   B PRO   A 136 ? 0.1383 0.1386 0.1513 0.0011  -0.0055 -0.0085 136 PRO   A C   
2893 O  O   A PRO   A 136 ? 0.1287 0.1628 0.1988 -0.0135 0.0018  0.0135  136 PRO   A O   
2894 O  O   B PRO   A 136 ? 0.1372 0.1347 0.1369 0.0073  0.0068  -0.0090 136 PRO   A O   
2895 C  CB  A PRO   A 136 ? 0.1666 0.1661 0.2462 -0.0136 -0.0047 0.0209  136 PRO   A CB  
2896 C  CB  B PRO   A 136 ? 0.1497 0.1315 0.1672 0.0030  -0.0136 -0.0147 136 PRO   A CB  
2897 C  CG  A PRO   A 136 ? 0.1769 0.1727 0.2534 -0.0103 -0.0125 0.0253  136 PRO   A CG  
2898 C  CG  B PRO   A 136 ? 0.1548 0.1271 0.1789 0.0056  -0.0198 -0.0125 136 PRO   A CG  
2899 C  CD  A PRO   A 136 ? 0.1724 0.1711 0.2325 -0.0101 -0.0128 0.0377  136 PRO   A CD  
2900 C  CD  B PRO   A 136 ? 0.1472 0.1233 0.1651 0.0056  -0.0214 0.0005  136 PRO   A CD  
2915 N  N   A ILE   A 137 ? 0.1323 0.1570 0.2144 -0.0056 -0.0131 0.0272  137 ILE   A N   
2916 N  N   B ILE   A 137 ? 0.1385 0.1404 0.1589 -0.0015 -0.0060 -0.0072 137 ILE   A N   
2917 C  CA  A ILE   A 137 ? 0.1389 0.1655 0.2165 -0.0117 -0.0154 0.0227  137 ILE   A CA  
2918 C  CA  B ILE   A 137 ? 0.1408 0.1451 0.1578 -0.0015 0.0010  -0.0113 137 ILE   A CA  
2919 C  C   A ILE   A 137 ? 0.1375 0.1641 0.2024 -0.0167 -0.0173 0.0235  137 ILE   A C   
2920 C  C   B ILE   A 137 ? 0.1398 0.1510 0.1631 -0.0060 0.0106  -0.0067 137 ILE   A C   
2921 O  O   A ILE   A 137 ? 0.1437 0.1640 0.2078 -0.0136 -0.0122 0.0243  137 ILE   A O   
2922 O  O   B ILE   A 137 ? 0.1349 0.1510 0.1613 -0.0053 0.0215  -0.0086 137 ILE   A O   
2923 C  CB  A ILE   A 137 ? 0.1441 0.1781 0.2498 -0.0151 -0.0268 0.0123  137 ILE   A CB  
2924 C  CB  B ILE   A 137 ? 0.1441 0.1445 0.1680 0.0039  -0.0083 -0.0147 137 ILE   A CB  
2925 C  CG1 A ILE   A 137 ? 0.1564 0.2040 0.2856 -0.0106 -0.0339 0.0073  137 ILE   A CG1 
2926 C  CG1 B ILE   A 137 ? 0.1491 0.1491 0.1833 0.0054  -0.0198 -0.0195 137 ILE   A CG1 
2927 C  CG2 A ILE   A 137 ? 0.1560 0.1794 0.2746 -0.0234 -0.0299 0.0063  137 ILE   A CG2 
2928 C  CG2 B ILE   A 137 ? 0.1475 0.1414 0.1713 0.0073  -0.0119 -0.0168 137 ILE   A CG2 
2929 C  CD1 A ILE   A 137 ? 0.1737 0.2206 0.3102 -0.0046 -0.0328 0.0062  137 ILE   A CD1 
2930 C  CD1 B ILE   A 137 ? 0.1537 0.1526 0.1935 0.0063  -0.0278 -0.0199 137 ILE   A CD1 
2953 N  N   A HIS   A 138 ? 0.1362 0.1775 0.1908 -0.0130 -0.0121 0.0241  138 HIS   A N   
2954 N  N   B HIS   A 138 ? 0.1432 0.1614 0.1665 -0.0080 0.0105  -0.0007 138 HIS   A N   
2955 C  CA  A HIS   A 138 ? 0.1422 0.1871 0.1836 -0.0137 -0.0076 0.0171  138 HIS   A CA  
2956 C  CA  B HIS   A 138 ? 0.1455 0.1657 0.1722 -0.0094 0.0073  0.0047  138 HIS   A CA  
2957 C  C   A HIS   A 138 ? 0.1327 0.1762 0.1801 -0.0101 -0.0092 0.0230  138 HIS   A C   
2958 C  C   B HIS   A 138 ? 0.1378 0.1644 0.1692 -0.0081 0.0054  0.0169  138 HIS   A C   
2959 O  O   A HIS   A 138 ? 0.1377 0.1766 0.1904 -0.0105 -0.0043 0.0193  138 HIS   A O   
2960 O  O   B HIS   A 138 ? 0.1392 0.1645 0.1707 -0.0088 0.0098  0.0148  138 HIS   A O   
2961 C  CB  A HIS   A 138 ? 0.1603 0.2094 0.1803 -0.0159 -0.0115 0.0091  138 HIS   A CB  
2962 C  CB  B HIS   A 138 ? 0.1474 0.1710 0.1794 -0.0090 0.0080  -0.0040 138 HIS   A CB  
2963 C  CG  A HIS   A 138 ? 0.1804 0.2245 0.1884 -0.0199 -0.0083 0.0014  138 HIS   A CG  
2964 C  CG  B HIS   A 138 ? 0.1507 0.1720 0.1899 -0.0119 0.0090  -0.0092 138 HIS   A CG  
2965 N  ND1 A HIS   A 138 ? 0.1938 0.2353 0.2147 -0.0195 -0.0119 -0.0060 138 HIS   A ND1 
2966 N  ND1 B HIS   A 138 ? 0.1554 0.1748 0.2037 -0.0112 0.0037  -0.0159 138 HIS   A ND1 
2967 C  CD2 A HIS   A 138 ? 0.1847 0.2351 0.1787 -0.0138 -0.0046 0.0010  138 HIS   A CD2 
2968 C  CD2 B HIS   A 138 ? 0.1502 0.1705 0.1895 -0.0105 0.0135  -0.0083 138 HIS   A CD2 
2969 C  CE1 A HIS   A 138 ? 0.1987 0.2419 0.2094 -0.0072 -0.0126 -0.0123 138 HIS   A CE1 
2970 C  CE1 B HIS   A 138 ? 0.1563 0.1738 0.2015 -0.0070 0.0040  -0.0172 138 HIS   A CE1 
2971 N  NE2 A HIS   A 138 ? 0.1943 0.2425 0.1817 -0.0066 -0.0030 -0.0099 138 HIS   A NE2 
2972 N  NE2 B HIS   A 138 ? 0.1553 0.1723 0.1967 -0.0074 0.0109  -0.0145 138 HIS   A NE2 
2987 N  N   . SER   A 139 ? 0.1305 0.1618 0.1713 -0.0062 -0.0046 0.0237  139 SER   A N   
2988 C  CA  . SER   A 139 ? 0.1275 0.1580 0.1681 -0.0077 -0.0021 0.0272  139 SER   A CA  
2989 C  C   . SER   A 139 ? 0.1229 0.1466 0.1743 -0.0118 0.0043  0.0209  139 SER   A C   
2990 O  O   . SER   A 139 ? 0.1211 0.1457 0.1850 -0.0099 0.0068  0.0251  139 SER   A O   
2991 C  CB  . SER   A 139 ? 0.1243 0.1600 0.1732 -0.0152 -0.0071 0.0306  139 SER   A CB  
2992 O  OG  . SER   A 139 ? 0.1334 0.1527 0.1860 -0.0185 -0.0079 0.0416  139 SER   A OG  
2999 N  N   . LEU   A 140 ? 0.1190 0.1493 0.1838 -0.0112 0.0030  0.0336  140 LEU   A N   
3000 C  CA  . LEU   A 140 ? 0.1169 0.1445 0.1772 -0.0128 0.0044  0.0333  140 LEU   A CA  
3001 C  C   . LEU   A 140 ? 0.1143 0.1536 0.1804 -0.0146 0.0011  0.0301  140 LEU   A C   
3002 O  O   . LEU   A 140 ? 0.1196 0.1548 0.1956 -0.0074 -0.0003 0.0339  140 LEU   A O   
3003 C  CB  . LEU   A 140 ? 0.1253 0.1599 0.1766 -0.0149 0.0026  0.0305  140 LEU   A CB  
3004 C  CG  . LEU   A 140 ? 0.1248 0.1760 0.1784 -0.0154 0.0086  0.0392  140 LEU   A CG  
3005 C  CD1 . LEU   A 140 ? 0.1307 0.1775 0.1737 -0.0133 0.0129  0.0355  140 LEU   A CD1 
3006 C  CD2 . LEU   A 140 ? 0.1298 0.1934 0.1819 -0.0184 0.0161  0.0423  140 LEU   A CD2 
3018 N  N   . ARG   A 141 ? 0.1224 0.1589 0.1913 -0.0101 0.0023  0.0237  141 ARG   A N   
3019 C  CA  . ARG   A 141 ? 0.1343 0.1729 0.2044 -0.0209 -0.0036 0.0083  141 ARG   A CA  
3020 C  C   . ARG   A 141 ? 0.1358 0.1547 0.1955 -0.0154 -0.0058 0.0135  141 ARG   A C   
3021 O  O   . ARG   A 141 ? 0.1361 0.1523 0.2023 -0.0156 0.0057  0.0088  141 ARG   A O   
3022 C  CB  . ARG   A 141 ? 0.1469 0.1972 0.2364 -0.0272 -0.0037 -0.0163 141 ARG   A CB  
3023 C  CG  . ARG   A 141 ? 0.1787 0.2372 0.2664 -0.0288 0.0150  -0.0205 141 ARG   A CG  
3024 C  CD  . ARG   A 141 ? 0.2077 0.2648 0.3031 -0.0432 0.0150  -0.0293 141 ARG   A CD  
3025 N  NE  . ARG   A 141 ? 0.1992 0.2895 0.3203 -0.0485 -0.0021 -0.0278 141 ARG   A NE  
3026 C  CZ  . ARG   A 141 ? 0.2039 0.3145 0.3342 -0.0604 0.0046  -0.0122 141 ARG   A CZ  
3027 N  NH1 . ARG   A 141 ? 0.1939 0.3208 0.3194 -0.0737 0.0370  -0.0234 141 ARG   A NH1 
3028 N  NH2 . ARG   A 141 ? 0.2112 0.3257 0.3561 -0.0527 -0.0126 0.0047  141 ARG   A NH2 
3042 N  N   . VAL   A 142 ? 0.1282 0.1488 0.1815 -0.0140 -0.0000 0.0073  142 VAL   A N   
3043 C  CA  . VAL   A 142 ? 0.1332 0.1448 0.1804 -0.0100 0.0126  0.0024  142 VAL   A CA  
3044 C  C   . VAL   A 142 ? 0.1151 0.1399 0.1810 -0.0143 0.0103  0.0094  142 VAL   A C   
3045 O  O   . VAL   A 142 ? 0.1230 0.1429 0.1868 -0.0036 0.0104  0.0098  142 VAL   A O   
3046 C  CB  . VAL   A 142 ? 0.1408 0.1521 0.1769 -0.0120 0.0130  0.0070  142 VAL   A CB  
3047 C  CG1 . VAL   A 142 ? 0.1396 0.1447 0.1900 -0.0176 0.0192  0.0065  142 VAL   A CG1 
3048 C  CG2 . VAL   A 142 ? 0.1542 0.1698 0.1958 -0.0020 0.0102  0.0149  142 VAL   A CG2 
3058 N  N   . CYS   A 143 ? 0.1195 0.1414 0.1756 -0.0126 0.0081  0.0132  143 CYS   A N   
3059 C  CA  . CYS   A 143 ? 0.1198 0.1386 0.1795 -0.0142 0.0079  0.0190  143 CYS   A CA  
3060 C  C   . CYS   A 143 ? 0.1181 0.1381 0.1881 -0.0119 0.0026  0.0233  143 CYS   A C   
3061 O  O   . CYS   A 143 ? 0.1190 0.1399 0.1868 -0.0059 0.0005  0.0239  143 CYS   A O   
3062 C  CB  . CYS   A 143 ? 0.1284 0.1399 0.1801 -0.0080 0.0097  0.0268  143 CYS   A CB  
3063 S  SG  . CYS   A 143 ? 0.1445 0.1496 0.1789 0.0011  0.0111  0.0191  143 CYS   A SG  
3069 N  N   . VAL   A 144 ? 0.1201 0.1447 0.2010 -0.0109 0.0119  0.0325  144 VAL   A N   
3070 C  CA  . VAL   A 144 ? 0.1265 0.1516 0.2336 -0.0157 0.0150  0.0307  144 VAL   A CA  
3071 C  C   . VAL   A 144 ? 0.1325 0.1436 0.2270 -0.0210 -0.0053 0.0262  144 VAL   A C   
3072 O  O   . VAL   A 144 ? 0.1491 0.1453 0.2256 -0.0094 -0.0076 0.0267  144 VAL   A O   
3073 C  CB  . VAL   A 144 ? 0.1514 0.1778 0.3031 -0.0057 0.0328  0.0445  144 VAL   A CB  
3074 C  CG1 . VAL   A 144 ? 0.1669 0.1988 0.3374 -0.0128 0.0234  0.0530  144 VAL   A CG1 
3075 C  CG2 . VAL   A 144 ? 0.1355 0.1841 0.3141 -0.0051 0.0445  0.0516  144 VAL   A CG2 
3085 N  N   . ASP   A 145 ? 0.1335 0.1396 0.2319 -0.0136 -0.0042 0.0222  145 ASP   A N   
3086 C  CA  . ASP   A 145 ? 0.1491 0.1420 0.2402 -0.0199 -0.0037 0.0103  145 ASP   A CA  
3087 C  C   . ASP   A 145 ? 0.1488 0.1349 0.2346 -0.0089 -0.0029 0.0010  145 ASP   A C   
3088 O  O   . ASP   A 145 ? 0.1637 0.1441 0.2885 -0.0134 -0.0063 -0.0250 145 ASP   A O   
3089 C  CB  . ASP   A 145 ? 0.1605 0.1723 0.2699 -0.0279 -0.0085 0.0047  145 ASP   A CB  
3090 C  CG  . ASP   A 145 ? 0.1733 0.2042 0.2979 -0.0476 -0.0296 0.0121  145 ASP   A CG  
3091 O  OD1 . ASP   A 145 ? 0.1692 0.2197 0.3031 -0.0547 -0.0197 0.0142  145 ASP   A OD1 
3092 O  OD2 . ASP   A 145 ? 0.1955 0.2254 0.3048 -0.0535 -0.0543 0.0190  145 ASP   A OD2 
3097 N  N   . THR   A 146 ? 0.1319 0.1304 0.2075 -0.0122 0.0033  0.0088  146 THR   A N   
3098 C  CA  . THR   A 146 ? 0.1286 0.1301 0.1939 -0.0058 0.0055  0.0013  146 THR   A CA  
3099 C  C   . THR   A 146 ? 0.1245 0.1286 0.1958 -0.0023 0.0114  0.0116  146 THR   A C   
3100 O  O   . THR   A 146 ? 0.1335 0.1434 0.2103 0.0033  0.0017  0.0133  146 THR   A O   
3101 C  CB  . THR   A 146 ? 0.1221 0.1337 0.1960 -0.0029 0.0059  0.0059  146 THR   A CB  
3102 O  OG1 . THR   A 146 ? 0.1268 0.1492 0.1962 -0.0021 0.0019  0.0033  146 THR   A OG1 
3103 C  CG2 . THR   A 146 ? 0.1289 0.1341 0.2079 -0.0043 0.0048  0.0059  146 THR   A CG2 
3111 N  N   . VAL   A 147 ? 0.1208 0.1344 0.1841 -0.0031 0.0088  0.0162  147 VAL   A N   
3112 C  CA  . VAL   A 147 ? 0.1214 0.1371 0.1817 -0.0100 0.0199  0.0248  147 VAL   A CA  
3113 C  C   . VAL   A 147 ? 0.1248 0.1302 0.1991 -0.0145 0.0166  0.0283  147 VAL   A C   
3114 O  O   . VAL   A 147 ? 0.1277 0.1383 0.2167 -0.0122 0.0105  0.0245  147 VAL   A O   
3115 C  CB  . VAL   A 147 ? 0.1366 0.1363 0.1770 -0.0096 0.0233  0.0263  147 VAL   A CB  
3116 C  CG1 . VAL   A 147 ? 0.1649 0.1445 0.1816 -0.0088 0.0259  0.0280  147 VAL   A CG1 
3117 C  CG2 . VAL   A 147 ? 0.1465 0.1349 0.1813 -0.0103 0.0159  0.0195  147 VAL   A CG2 
3127 N  N   . ARG   A 148 ? 0.1222 0.1364 0.2100 -0.0157 0.0190  0.0391  148 ARG   A N   
3128 C  CA  . ARG   A 148 ? 0.1313 0.1408 0.2088 -0.0111 0.0079  0.0505  148 ARG   A CA  
3129 C  C   . ARG   A 148 ? 0.1373 0.1430 0.2059 -0.0143 0.0112  0.0613  148 ARG   A C   
3130 O  O   . ARG   A 148 ? 0.1711 0.1545 0.2260 -0.0196 0.0185  0.0477  148 ARG   A O   
3131 C  CB  . ARG   A 148 ? 0.1338 0.1411 0.2253 -0.0099 0.0120  0.0427  148 ARG   A CB  
3132 C  CG  . ARG   A 148 ? 0.1493 0.1429 0.2570 -0.0088 0.0299  0.0325  148 ARG   A CG  
3133 C  CD  . ARG   A 148 ? 0.1668 0.1406 0.2697 -0.0081 0.0400  0.0446  148 ARG   A CD  
3134 N  NE  . ARG   A 148 ? 0.1594 0.1458 0.2624 0.0036  0.0482  0.0460  148 ARG   A NE  
3135 C  CZ  . ARG   A 148 ? 0.1594 0.1339 0.2557 0.0013  0.0446  0.0319  148 ARG   A CZ  
3136 N  NH1 . ARG   A 148 ? 0.1678 0.1403 0.2569 -0.0127 0.0383  0.0110  148 ARG   A NH1 
3137 N  NH2 . ARG   A 148 ? 0.1549 0.1505 0.2604 0.0097  0.0441  0.0367  148 ARG   A NH2 
3151 N  N   . THR   A 149 ? 0.1409 0.1527 0.2007 -0.0174 0.0013  0.0475  149 THR   A N   
3152 C  CA  . THR   A 149 ? 0.1428 0.1567 0.2009 -0.0158 0.0054  0.0515  149 THR   A CA  
3153 C  C   . THR   A 149 ? 0.1383 0.1540 0.1837 -0.0235 0.0085  0.0536  149 THR   A C   
3154 O  O   . THR   A 149 ? 0.1378 0.1665 0.2022 -0.0221 0.0059  0.0493  149 THR   A O   
3155 C  CB  . THR   A 149 ? 0.1466 0.1650 0.2014 -0.0168 0.0031  0.0450  149 THR   A CB  
3156 O  OG1 . THR   A 149 ? 0.1471 0.1575 0.2098 -0.0260 0.0043  0.0368  149 THR   A OG1 
3157 C  CG2 . THR   A 149 ? 0.1480 0.1754 0.2041 -0.0099 -0.0056 0.0401  149 THR   A CG2 
3165 N  N   . ASN   A 150 ? 0.1431 0.1581 0.1821 -0.0117 0.0046  0.0565  150 ASN   A N   
3166 C  CA  . ASN   A 150 ? 0.1602 0.1663 0.1862 -0.0129 0.0069  0.0464  150 ASN   A CA  
3167 C  C   . ASN   A 150 ? 0.1411 0.1568 0.1844 -0.0200 -0.0016 0.0435  150 ASN   A C   
3168 O  O   . ASN   A 150 ? 0.1509 0.1675 0.2098 -0.0169 -0.0191 0.0371  150 ASN   A O   
3169 C  CB  . ASN   A 150 ? 0.2058 0.1943 0.2094 -0.0185 0.0301  0.0632  150 ASN   A CB  
3170 C  CG  . ASN   A 150 ? 0.2583 0.2299 0.2774 -0.0146 0.0138  0.0697  150 ASN   A CG  
3171 O  OD1 . ASN   A 150 ? 0.2735 0.2348 0.3040 -0.0235 0.0166  0.0828  150 ASN   A OD1 
3172 N  ND2 . ASN   A 150 ? 0.2866 0.2534 0.3141 -0.0063 -0.0011 0.0777  150 ASN   A ND2 
3179 N  N   . VAL   A 151 ? 0.1389 0.1427 0.1820 -0.0194 0.0012  0.0403  151 VAL   A N   
3180 C  CA  . VAL   A 151 ? 0.1456 0.1422 0.1803 -0.0210 0.0010  0.0393  151 VAL   A CA  
3181 C  C   . VAL   A 151 ? 0.1389 0.1403 0.1797 -0.0299 0.0045  0.0453  151 VAL   A C   
3182 O  O   . VAL   A 151 ? 0.1471 0.1503 0.2080 -0.0237 0.0038  0.0345  151 VAL   A O   
3183 C  CB  . VAL   A 151 ? 0.1727 0.1624 0.1786 -0.0062 0.0031  0.0373  151 VAL   A CB  
3184 C  CG1 . VAL   A 151 ? 0.1699 0.1851 0.2050 -0.0113 0.0123  0.0403  151 VAL   A CG1 
3185 C  CG2 . VAL   A 151 ? 0.1796 0.1606 0.1801 -0.0049 0.0210  0.0359  151 VAL   A CG2 
3195 N  N   . TYR   A 152 ? 0.1358 0.1427 0.1783 -0.0270 0.0057  0.0377  152 TYR   A N   
3196 C  CA  . TYR   A 152 ? 0.1375 0.1512 0.1503 -0.0207 0.0080  0.0385  152 TYR   A CA  
3197 C  C   . TYR   A 152 ? 0.1332 0.1458 0.1481 -0.0201 0.0138  0.0344  152 TYR   A C   
3198 O  O   . TYR   A 152 ? 0.1410 0.1437 0.1590 -0.0230 0.0156  0.0284  152 TYR   A O   
3199 C  CB  . TYR   A 152 ? 0.1532 0.1633 0.1475 -0.0184 0.0148  0.0388  152 TYR   A CB  
3200 C  CG  . TYR   A 152 ? 0.1674 0.1828 0.1507 -0.0269 0.0160  0.0433  152 TYR   A CG  
3201 C  CD1 . TYR   A 152 ? 0.1821 0.2056 0.1755 -0.0167 0.0204  0.0541  152 TYR   A CD1 
3202 C  CD2 . TYR   A 152 ? 0.1759 0.1961 0.1510 -0.0418 0.0075  0.0397  152 TYR   A CD2 
3203 C  CE1 . TYR   A 152 ? 0.2127 0.2194 0.1929 -0.0134 0.0086  0.0630  152 TYR   A CE1 
3204 C  CE2 . TYR   A 152 ? 0.2027 0.2113 0.1723 -0.0443 0.0124  0.0476  152 TYR   A CE2 
3205 C  CZ  . TYR   A 152 ? 0.2273 0.2166 0.1724 -0.0294 0.0080  0.0737  152 TYR   A CZ  
3206 O  OH  . TYR   A 152 ? 0.2565 0.2373 0.2071 -0.0230 0.0109  0.0837  152 TYR   A OH  
3216 N  N   A LEU   A 153 ? 0.1270 0.1389 0.1643 -0.0274 0.0166  0.0448  153 LEU   A N   
3217 N  N   B LEU   A 153 ? 0.1324 0.1495 0.1388 -0.0162 0.0095  0.0342  153 LEU   A N   
3218 C  CA  A LEU   A 153 ? 0.1241 0.1359 0.1712 -0.0150 0.0185  0.0377  153 LEU   A CA  
3219 C  CA  B LEU   A 153 ? 0.1317 0.1510 0.1325 -0.0080 0.0075  0.0326  153 LEU   A CA  
3220 C  C   A LEU   A 153 ? 0.1279 0.1394 0.1761 -0.0104 0.0281  0.0312  153 LEU   A C   
3221 C  C   B LEU   A 153 ? 0.1336 0.1586 0.1331 -0.0079 0.0074  0.0330  153 LEU   A C   
3222 O  O   A LEU   A 153 ? 0.1337 0.1446 0.1845 -0.0162 0.0310  0.0228  153 LEU   A O   
3223 O  O   B LEU   A 153 ? 0.1317 0.1615 0.1354 -0.0088 0.0058  0.0330  153 LEU   A O   
3224 C  CB  A LEU   A 153 ? 0.1203 0.1343 0.1854 -0.0107 0.0123  0.0327  153 LEU   A CB  
3225 C  CB  B LEU   A 153 ? 0.1321 0.1473 0.1346 -0.0001 0.0039  0.0344  153 LEU   A CB  
3226 C  CG  A LEU   A 153 ? 0.1247 0.1422 0.1826 -0.0125 0.0165  0.0265  153 LEU   A CG  
3227 C  CG  B LEU   A 153 ? 0.1360 0.1450 0.1327 0.0056  -0.0036 0.0404  153 LEU   A CG  
3228 C  CD1 A LEU   A 153 ? 0.1373 0.1419 0.1890 -0.0114 0.0034  0.0264  153 LEU   A CD1 
3229 C  CD1 B LEU   A 153 ? 0.1391 0.1449 0.1383 0.0052  -0.0060 0.0421  153 LEU   A CD1 
3230 C  CD2 A LEU   A 153 ? 0.1322 0.1474 0.1844 -0.0169 0.0205  0.0087  153 LEU   A CD2 
3231 C  CD2 B LEU   A 153 ? 0.1394 0.1462 0.1388 0.0080  -0.0044 0.0345  153 LEU   A CD2 
3254 N  N   A ALA   A 154 ? 0.1270 0.1317 0.1761 -0.0061 0.0249  0.0389  154 ALA   A N   
3255 N  N   B ALA   A 154 ? 0.1393 0.1615 0.1388 -0.0092 0.0076  0.0334  154 ALA   A N   
3256 C  CA  A ALA   A 154 ? 0.1339 0.1339 0.1815 -0.0027 0.0287  0.0327  154 ALA   A CA  
3257 C  CA  B ALA   A 154 ? 0.1465 0.1661 0.1442 -0.0068 0.0064  0.0320  154 ALA   A CA  
3258 C  C   A ALA   A 154 ? 0.1297 0.1274 0.1762 0.0039  0.0210  0.0303  154 ALA   A C   
3259 C  C   B ALA   A 154 ? 0.1473 0.1677 0.1479 -0.0064 0.0072  0.0368  154 ALA   A C   
3260 O  O   A ALA   A 154 ? 0.1359 0.1456 0.1747 0.0009  0.0211  0.0344  154 ALA   A O   
3261 O  O   B ALA   A 154 ? 0.1455 0.1688 0.1415 -0.0067 0.0128  0.0415  154 ALA   A O   
3262 C  CB  A ALA   A 154 ? 0.1504 0.1379 0.1972 0.0013  0.0205  0.0233  154 ALA   A CB  
3263 C  CB  B ALA   A 154 ? 0.1535 0.1676 0.1482 -0.0040 -0.0001 0.0261  154 ALA   A CB  
3274 N  N   A VAL   A 155 ? 0.1125 0.1066 0.1452 0.0028  0.0271  0.0496  155 VAL   A N   
3275 N  N   B VAL   A 155 ? 0.1461 0.1652 0.1484 -0.0057 0.0049  0.0424  155 VAL   A N   
3276 C  CA  A VAL   A 155 ? 0.1327 0.1297 0.1903 0.0067  0.0216  0.0554  155 VAL   A CA  
3277 C  CA  B VAL   A 155 ? 0.1576 0.1762 0.1686 -0.0037 0.0016  0.0382  155 VAL   A CA  
3278 C  CA  T VAL   A 155 ? 0.1683 0.1600 0.1865 -0.0058 0.0279  0.0477  155 VAL   A CA  
3279 C  C   A VAL   A 155 ? 0.1430 0.1439 0.2256 0.0204  0.0220  0.0630  155 VAL   A C   
3280 C  C   B VAL   A 155 ? 0.1719 0.1859 0.1967 0.0032  0.0055  0.0340  155 VAL   A C   
3281 C  C   T VAL   A 155 ? 0.1722 0.1608 0.1843 0.0012  0.0298  0.0509  155 VAL   A C   
3282 O  O   A VAL   A 155 ? 0.1430 0.1509 0.2362 0.0274  0.0379  0.0504  155 VAL   A O   
3283 O  O   B VAL   A 155 ? 0.1687 0.1851 0.2103 0.0037  0.0175  0.0335  155 VAL   A O   
3284 O  O   T VAL   A 155 ? 0.1735 0.1651 0.1777 0.0039  0.0280  0.0493  155 VAL   A O   
3285 C  CB  A VAL   A 155 ? 0.1391 0.1441 0.1977 0.0070  0.0060  0.0483  155 VAL   A CB  
3286 C  CB  B VAL   A 155 ? 0.1539 0.1767 0.1623 -0.0082 -0.0056 0.0390  155 VAL   A CB  
3287 C  CB  T VAL   A 155 ? 0.1651 0.1638 0.1856 -0.0064 0.0207  0.0426  155 VAL   A CB  
3288 C  CG1 A VAL   A 155 ? 0.1469 0.1585 0.2095 0.0121  0.0088  0.0518  155 VAL   A CG1 
3289 C  CG1 B VAL   A 155 ? 0.1554 0.1792 0.1677 -0.0110 -0.0126 0.0348  155 VAL   A CG1 
3290 C  CG1 T VAL   A 155 ? 0.1688 0.1703 0.1899 -0.0046 0.0227  0.0481  155 VAL   A CG1 
3291 C  CG2 A VAL   A 155 ? 0.1515 0.1513 0.1980 0.0137  -0.0105 0.0455  155 VAL   A CG2 
3292 C  CG2 B VAL   A 155 ? 0.1496 0.1737 0.1550 -0.0161 0.0023  0.0438  155 VAL   A CG2 
3293 C  CG2 T VAL   A 155 ? 0.1667 0.1658 0.1840 -0.0023 0.0116  0.0377  155 VAL   A CG2 
3319 N  N   A PHE   A 156 ? 0.1638 0.1578 0.2523 0.0214  0.0158  0.0761  156 PHE   A N   
3320 N  N   B PHE   A 156 ? 0.1908 0.1966 0.2047 0.0096  0.0017  0.0285  156 PHE   A N   
3321 N  N   T PHE   A 156 ? 0.1816 0.1603 0.1860 0.0025  0.0344  0.0544  156 PHE   A N   
3322 C  CA  A PHE   A 156 ? 0.1922 0.1725 0.2838 0.0302  0.0110  0.0819  156 PHE   A CA  
3323 C  CA  B PHE   A 156 ? 0.2064 0.2107 0.2140 0.0171  -0.0016 0.0265  156 PHE   A CA  
3324 C  CA  T PHE   A 156 ? 0.1967 0.1627 0.1810 0.0105  0.0408  0.0547  156 PHE   A CA  
3325 C  C   A PHE   A 156 ? 0.1963 0.1783 0.2770 0.0420  0.0247  0.0912  156 PHE   A C   
3326 C  C   B PHE   A 156 ? 0.2201 0.2234 0.2304 0.0141  -0.0006 0.0337  156 PHE   A C   
3327 C  C   T PHE   A 156 ? 0.1979 0.1749 0.1844 0.0179  0.0534  0.0588  156 PHE   A C   
3328 O  O   A PHE   A 156 ? 0.2088 0.1831 0.2867 0.0314  0.0333  0.0838  156 PHE   A O   
3329 O  O   B PHE   A 156 ? 0.2227 0.2230 0.2333 0.0195  0.0003  0.0361  156 PHE   A O   
3330 O  O   T PHE   A 156 ? 0.2050 0.1743 0.1803 0.0205  0.0622  0.0517  156 PHE   A O   
3331 C  CB  A PHE   A 156 ? 0.2134 0.1868 0.3087 0.0240  0.0038  0.0809  156 PHE   A CB  
3332 C  CB  B PHE   A 156 ? 0.2101 0.2164 0.2206 0.0242  -0.0014 0.0164  156 PHE   A CB  
3333 C  CB  T PHE   A 156 ? 0.2042 0.1539 0.1648 0.0108  0.0367  0.0568  156 PHE   A CB  
3334 C  CG  A PHE   A 156 ? 0.2338 0.1959 0.3207 0.0266  -0.0001 0.0702  156 PHE   A CG  
3335 C  CG  B PHE   A 156 ? 0.2155 0.2246 0.2240 0.0308  0.0004  0.0083  156 PHE   A CG  
3336 C  CG  T PHE   A 156 ? 0.2109 0.1503 0.1548 0.0150  0.0244  0.0657  156 PHE   A CG  
3337 C  CD1 A PHE   A 156 ? 0.2413 0.2013 0.3230 0.0319  0.0112  0.0606  156 PHE   A CD1 
3338 C  CD1 B PHE   A 156 ? 0.2178 0.2315 0.2209 0.0307  -0.0016 0.0076  156 PHE   A CD1 
3339 C  CD1 T PHE   A 156 ? 0.2139 0.1560 0.1758 0.0173  0.0110  0.0528  156 PHE   A CD1 
3340 C  CD2 A PHE   A 156 ? 0.2445 0.2068 0.3268 0.0326  -0.0079 0.0706  156 PHE   A CD2 
3341 C  CD2 B PHE   A 156 ? 0.2193 0.2263 0.2212 0.0374  0.0047  0.0050  156 PHE   A CD2 
3342 C  CD2 T PHE   A 156 ? 0.2129 0.1497 0.1637 0.0232  0.0203  0.0731  156 PHE   A CD2 
3343 C  CE1 A PHE   A 156 ? 0.2510 0.2071 0.3327 0.0348  0.0145  0.0527  156 PHE   A CE1 
3344 C  CE1 B PHE   A 156 ? 0.2207 0.2321 0.2242 0.0337  -0.0038 0.0075  156 PHE   A CE1 
3345 C  CE1 T PHE   A 156 ? 0.2183 0.1588 0.1950 0.0184  0.0073  0.0427  156 PHE   A CE1 
3346 C  CE2 A PHE   A 156 ? 0.2549 0.2136 0.3308 0.0353  -0.0037 0.0574  156 PHE   A CE2 
3347 C  CE2 B PHE   A 156 ? 0.2227 0.2277 0.2227 0.0406  0.0038  0.0054  156 PHE   A CE2 
3348 C  CE2 T PHE   A 156 ? 0.2176 0.1529 0.1773 0.0220  0.0178  0.0683  156 PHE   A CE2 
3349 C  CZ  A PHE   A 156 ? 0.2561 0.2134 0.3330 0.0378  0.0096  0.0496  156 PHE   A CZ  
3350 C  CZ  B PHE   A 156 ? 0.2215 0.2300 0.2209 0.0388  0.0008  0.0058  156 PHE   A CZ  
3351 C  CZ  T PHE   A 156 ? 0.2182 0.1525 0.1941 0.0148  0.0134  0.0545  156 PHE   A CZ  
3379 N  N   A ASP   A 157 ? 0.1915 0.1864 0.2662 0.0541  0.0266  0.0991  157 ASP   A N   
3380 N  N   B ASP   A 157 ? 0.2297 0.2351 0.2342 0.0077  -0.0039 0.0354  157 ASP   A N   
3381 N  N   T ASP   A 157 ? 0.1877 0.1891 0.2042 0.0181  0.0474  0.0661  157 ASP   A N   
3382 C  CA  A ASP   A 157 ? 0.1995 0.2131 0.2657 0.0593  0.0302  0.1006  157 ASP   A CA  
3383 C  CA  B ASP   A 157 ? 0.2419 0.2505 0.2509 0.0051  -0.0053 0.0380  157 ASP   A CA  
3384 C  CA  T ASP   A 157 ? 0.1816 0.2074 0.2133 0.0206  0.0396  0.0711  157 ASP   A CA  
3385 C  C   A ASP   A 157 ? 0.1842 0.2290 0.2690 0.0634  0.0388  0.1042  157 ASP   A C   
3386 C  C   B ASP   A 157 ? 0.2416 0.2575 0.2608 0.0026  -0.0058 0.0360  157 ASP   A C   
3387 C  C   T ASP   A 157 ? 0.1852 0.2277 0.2232 0.0273  0.0381  0.0758  157 ASP   A C   
3388 O  O   A ASP   A 157 ? 0.1715 0.2216 0.2590 0.0603  0.0439  0.1084  157 ASP   A O   
3389 O  O   B ASP   A 157 ? 0.2419 0.2580 0.2564 0.0004  -0.0060 0.0331  157 ASP   A O   
3390 O  O   T ASP   A 157 ? 0.1737 0.2248 0.2177 0.0252  0.0416  0.0780  157 ASP   A O   
3391 C  CB  A ASP   A 157 ? 0.2212 0.2249 0.2792 0.0679  0.0201  0.0969  157 ASP   A CB  
3392 C  CB  B ASP   A 157 ? 0.2550 0.2593 0.2600 0.0040  -0.0062 0.0389  157 ASP   A CB  
3393 C  CB  T ASP   A 157 ? 0.1724 0.2046 0.2206 0.0217  0.0287  0.0717  157 ASP   A CB  
3394 C  CG  A ASP   A 157 ? 0.2406 0.2365 0.3035 0.0753  0.0167  0.0886  157 ASP   A CG  
3395 C  CG  B ASP   A 157 ? 0.2694 0.2686 0.2677 0.0023  -0.0063 0.0403  157 ASP   A CG  
3396 C  CG  T ASP   A 157 ? 0.1571 0.1935 0.2257 0.0271  0.0222  0.0720  157 ASP   A CG  
3397 O  OD1 A ASP   A 157 ? 0.2687 0.2499 0.3336 0.0733  0.0023  0.0751  157 ASP   A OD1 
3398 O  OD1 B ASP   A 157 ? 0.2695 0.2636 0.2578 0.0002  -0.0009 0.0508  157 ASP   A OD1 
3399 O  OD1 T ASP   A 157 ? 0.1505 0.1796 0.2440 0.0246  0.0201  0.0607  157 ASP   A OD1 
3400 O  OD2 A ASP   A 157 ? 0.2259 0.2305 0.3060 0.0748  0.0312  0.1015  157 ASP   A OD2 
3401 O  OD2 B ASP   A 157 ? 0.2798 0.2777 0.2849 0.0029  -0.0120 0.0330  157 ASP   A OD2 
3402 O  OD2 T ASP   A 157 ? 0.1424 0.1924 0.1979 0.0358  0.0201  0.0854  157 ASP   A OD2 
3415 N  N   A LYS   A 158 ? 0.1931 0.2550 0.2890 0.0657  0.0421  0.0977  158 LYS   A N   
3416 N  N   B LYS   A 158 ? 0.2404 0.2631 0.2692 0.0032  -0.0092 0.0380  158 LYS   A N   
3417 N  N   T LYS   A 158 ? 0.2039 0.2498 0.2440 0.0338  0.0335  0.0700  158 LYS   A N   
3418 C  CA  A LYS   A 158 ? 0.1922 0.2789 0.3104 0.0752  0.0488  0.0897  158 LYS   A CA  
3419 C  CA  B LYS   A 158 ? 0.2418 0.2718 0.2797 0.0009  -0.0079 0.0381  158 LYS   A CA  
3420 C  CA  T LYS   A 158 ? 0.2181 0.2705 0.2739 0.0432  0.0292  0.0596  158 LYS   A CA  
3421 C  C   A LYS   A 158 ? 0.1721 0.2861 0.2942 0.0787  0.0382  0.0978  158 LYS   A C   
3422 C  C   B LYS   A 158 ? 0.2264 0.2741 0.2628 0.0060  -0.0132 0.0475  158 LYS   A C   
3423 C  C   T LYS   A 158 ? 0.2161 0.2763 0.2690 0.0435  0.0208  0.0560  158 LYS   A C   
3424 O  O   A LYS   A 158 ? 0.1703 0.2960 0.2980 0.0681  0.0495  0.0938  158 LYS   A O   
3425 O  O   B LYS   A 158 ? 0.2195 0.2773 0.2541 0.0056  -0.0177 0.0520  158 LYS   A O   
3426 O  O   T LYS   A 158 ? 0.2167 0.2808 0.2719 0.0424  0.0211  0.0512  158 LYS   A O   
3427 C  CB  A LYS   A 158 ? 0.2149 0.2902 0.3440 0.0747  0.0735  0.0817  158 LYS   A CB  
3428 C  CB  B LYS   A 158 ? 0.2565 0.2784 0.3013 -0.0044 -0.0037 0.0269  158 LYS   A CB  
3429 C  CB  T LYS   A 158 ? 0.2364 0.2817 0.3089 0.0459  0.0398  0.0542  158 LYS   A CB  
3430 C  CG  A LYS   A 158 ? 0.2399 0.3030 0.3834 0.0713  0.0824  0.0809  158 LYS   A CG  
3431 C  CG  B LYS   A 158 ? 0.2667 0.2850 0.3199 -0.0099 0.0002  0.0199  158 LYS   A CG  
3432 C  CG  T LYS   A 158 ? 0.2552 0.2928 0.3455 0.0462  0.0436  0.0530  158 LYS   A CG  
3433 C  CD  A LYS   A 158 ? 0.2575 0.3149 0.4123 0.0640  0.0963  0.0848  158 LYS   A CD  
3434 C  CD  B LYS   A 158 ? 0.2734 0.2885 0.3342 -0.0140 0.0050  0.0174  158 LYS   A CD  
3435 C  CD  T LYS   A 158 ? 0.2699 0.3018 0.3782 0.0460  0.0477  0.0534  158 LYS   A CD  
3436 C  CE  A LYS   A 158 ? 0.2722 0.3243 0.4342 0.0554  0.1046  0.0919  158 LYS   A CE  
3437 C  CE  B LYS   A 158 ? 0.2774 0.2901 0.3460 -0.0151 0.0082  0.0148  158 LYS   A CE  
3438 C  CE  T LYS   A 158 ? 0.2818 0.3090 0.4028 0.0441  0.0491  0.0572  158 LYS   A CE  
3439 N  NZ  A LYS   A 158 ? 0.2809 0.3290 0.4467 0.0496  0.1059  0.0971  158 LYS   A NZ  
3440 N  NZ  B LYS   A 158 ? 0.2778 0.2903 0.3517 -0.0162 0.0068  0.0123  158 LYS   A NZ  
3441 N  NZ  T LYS   A 158 ? 0.2891 0.3130 0.4164 0.0436  0.0480  0.0601  158 LYS   A NZ  
3481 N  N   A ASN   A 159 ? 0.1693 0.2874 0.2936 0.0702  0.0173  0.0978  159 ASN   A N   
3482 N  N   B ASN   A 159 ? 0.2201 0.2731 0.2615 0.0127  -0.0129 0.0482  159 ASN   A N   
3483 N  N   T ASN   A 159 ? 0.2178 0.2778 0.2729 0.0357  0.0127  0.0522  159 ASN   A N   
3484 C  CA  A ASN   A 159 ? 0.1667 0.2879 0.2818 0.0569  0.0026  0.1068  159 ASN   A CA  
3485 C  CA  B ASN   A 159 ? 0.2149 0.2723 0.2561 0.0130  -0.0081 0.0435  159 ASN   A CA  
3486 C  CA  T ASN   A 159 ? 0.2213 0.2795 0.2702 0.0245  0.0094  0.0536  159 ASN   A CA  
3487 C  C   A ASN   A 159 ? 0.1458 0.2860 0.2689 0.0422  0.0105  0.1003  159 ASN   A C   
3488 C  C   B ASN   A 159 ? 0.2025 0.2643 0.2454 0.0126  -0.0040 0.0380  159 ASN   A C   
3489 C  C   T ASN   A 159 ? 0.2198 0.2803 0.2648 0.0159  0.0188  0.0473  159 ASN   A C   
3490 O  O   A ASN   A 159 ? 0.1245 0.2902 0.2560 0.0432  -0.0007 0.0879  159 ASN   A O   
3491 O  O   B ASN   A 159 ? 0.1946 0.2689 0.2462 0.0127  -0.0066 0.0361  159 ASN   A O   
3492 O  O   T ASN   A 159 ? 0.2177 0.2817 0.2576 0.0141  0.0182  0.0380  159 ASN   A O   
3493 C  CB  A ASN   A 159 ? 0.1849 0.2942 0.2973 0.0519  -0.0094 0.1169  159 ASN   A CB  
3494 C  CB  B ASN   A 159 ? 0.2202 0.2773 0.2621 0.0123  -0.0098 0.0420  159 ASN   A CB  
3495 C  CB  T ASN   A 159 ? 0.2273 0.2829 0.2843 0.0214  -0.0001 0.0608  159 ASN   A CB  
3496 C  CG  A ASN   A 159 ? 0.2018 0.3059 0.3276 0.0437  -0.0114 0.1062  159 ASN   A CG  
3497 C  CG  B ASN   A 159 ? 0.2234 0.2804 0.2674 0.0099  -0.0104 0.0321  159 ASN   A CG  
3498 C  CG  T ASN   A 159 ? 0.2336 0.2884 0.3040 0.0181  -0.0053 0.0597  159 ASN   A CG  
3499 O  OD1 A ASN   A 159 ? 0.2106 0.3155 0.3484 0.0413  -0.0063 0.0979  159 ASN   A OD1 
3500 O  OD1 B ASN   A 159 ? 0.2289 0.2848 0.2736 0.0089  -0.0107 0.0251  159 ASN   A OD1 
3501 O  OD1 T ASN   A 159 ? 0.2366 0.2939 0.3179 0.0176  -0.0023 0.0560  159 ASN   A OD1 
3502 N  ND2 A ASN   A 159 ? 0.2061 0.3091 0.3468 0.0381  -0.0114 0.0988  159 ASN   A ND2 
3503 N  ND2 B ASN   A 159 ? 0.2224 0.2797 0.2671 0.0096  -0.0102 0.0309  159 ASN   A ND2 
3504 N  ND2 T ASN   A 159 ? 0.2354 0.2904 0.3145 0.0157  -0.0086 0.0585  159 ASN   A ND2 
3523 N  N   A LEU   A 160 ? 0.1392 0.2703 0.2519 0.0337  0.0104  0.1143  160 LEU   A N   
3524 N  N   B LEU   A 160 ? 0.1948 0.2471 0.2253 0.0126  -0.0058 0.0355  160 LEU   A N   
3525 N  N   T LEU   A 160 ? 0.2166 0.2750 0.2585 0.0105  0.0206  0.0517  160 LEU   A N   
3526 C  CA  A LEU   A 160 ? 0.1371 0.2528 0.2343 0.0182  0.0188  0.1224  160 LEU   A CA  
3527 C  CA  B LEU   A 160 ? 0.1906 0.2298 0.2063 0.0079  -0.0020 0.0305  160 LEU   A CA  
3528 C  CA  T LEU   A 160 ? 0.2162 0.2682 0.2504 0.0020  0.0242  0.0539  160 LEU   A CA  
3529 C  C   A LEU   A 160 ? 0.1231 0.2432 0.2096 0.0082  0.0232  0.1215  160 LEU   A C   
3530 C  C   B LEU   A 160 ? 0.1778 0.2175 0.1850 0.0031  0.0021  0.0283  160 LEU   A C   
3531 O  O   A LEU   A 160 ? 0.1108 0.2479 0.2059 0.0045  0.0238  0.1190  160 LEU   A O   
3532 O  O   B LEU   A 160 ? 0.1693 0.2150 0.1759 0.0031  -0.0010 0.0263  160 LEU   A O   
3533 C  CB  A LEU   A 160 ? 0.1463 0.2472 0.2250 0.0093  0.0215  0.1239  160 LEU   A CB  
3534 C  CB  B LEU   A 160 ? 0.1962 0.2263 0.2045 0.0074  -0.0043 0.0314  160 LEU   A CB  
3535 C  CB  T LEU   A 160 ? 0.2145 0.2627 0.2399 -0.0066 0.0275  0.0529  160 LEU   A CB  
3536 C  CG  A LEU   A 160 ? 0.1541 0.2488 0.2385 -0.0016 0.0206  0.0965  160 LEU   A CG  
3537 C  CG  B LEU   A 160 ? 0.2017 0.2255 0.2085 0.0074  -0.0104 0.0277  160 LEU   A CG  
3538 C  CG  T LEU   A 160 ? 0.2138 0.2604 0.2372 -0.0151 0.0304  0.0429  160 LEU   A CG  
3539 C  CD1 A LEU   A 160 ? 0.1650 0.2559 0.2569 -0.0075 0.0207  0.0792  160 LEU   A CD1 
3540 C  CD1 B LEU   A 160 ? 0.2034 0.2243 0.2116 0.0016  -0.0107 0.0261  160 LEU   A CD1 
3541 C  CD1 T LEU   A 160 ? 0.2163 0.2625 0.2422 -0.0171 0.0305  0.0350  160 LEU   A CD1 
3542 C  CD2 A LEU   A 160 ? 0.1556 0.2473 0.2499 -0.0051 0.0228  0.0777  160 LEU   A CD2 
3543 C  CD2 B LEU   A 160 ? 0.2042 0.2263 0.2069 0.0108  -0.0135 0.0250  160 LEU   A CD2 
3544 C  CD2 T LEU   A 160 ? 0.2127 0.2580 0.2363 -0.0191 0.0333  0.0377  160 LEU   A CD2 
3577 N  N   A TYR   A 161 ? 0.1328 0.2310 0.2335 0.0062  0.0221  0.1112  161 TYR   A N   
3578 N  N   B TYR   A 161 ? 0.1771 0.2093 0.1819 0.0030  0.0057  0.0316  161 TYR   A N   
3579 C  CA  A TYR   A 161 ? 0.1359 0.2241 0.2274 0.0051  0.0199  0.0931  161 TYR   A CA  
3580 C  CA  B TYR   A 161 ? 0.1736 0.2043 0.1773 0.0037  0.0123  0.0314  161 TYR   A CA  
3581 C  C   A TYR   A 161 ? 0.1360 0.2411 0.2244 0.0043  0.0182  0.0809  161 TYR   A C   
3582 C  C   B TYR   A 161 ? 0.1729 0.2194 0.1863 0.0017  0.0165  0.0291  161 TYR   A C   
3583 O  O   A TYR   A 161 ? 0.1319 0.2418 0.2073 -0.0030 0.0247  0.0670  161 TYR   A O   
3584 O  O   B TYR   A 161 ? 0.1711 0.2180 0.1856 -0.0023 0.0235  0.0190  161 TYR   A O   
3585 C  CB  A TYR   A 161 ? 0.1456 0.2104 0.2377 0.0041  0.0298  0.0741  161 TYR   A CB  
3586 C  CB  B TYR   A 161 ? 0.1726 0.1885 0.1678 0.0071  0.0161  0.0344  161 TYR   A CB  
3587 C  CG  A TYR   A 161 ? 0.1439 0.2002 0.2384 0.0047  0.0243  0.0555  161 TYR   A CG  
3588 C  CG  B TYR   A 161 ? 0.1678 0.1730 0.1655 0.0114  0.0163  0.0385  161 TYR   A CG  
3589 C  CD1 A TYR   A 161 ? 0.1463 0.1923 0.2455 0.0057  0.0271  0.0434  161 TYR   A CD1 
3590 C  CD1 B TYR   A 161 ? 0.1694 0.1706 0.1682 0.0113  0.0179  0.0406  161 TYR   A CD1 
3591 C  CD2 A TYR   A 161 ? 0.1459 0.2014 0.2386 0.0051  0.0141  0.0429  161 TYR   A CD2 
3592 C  CD2 B TYR   A 161 ? 0.1654 0.1617 0.1658 0.0127  0.0132  0.0385  161 TYR   A CD2 
3593 C  CE1 A TYR   A 161 ? 0.1465 0.1861 0.2433 0.0067  0.0223  0.0441  161 TYR   A CE1 
3594 C  CE1 B TYR   A 161 ? 0.1703 0.1701 0.1730 0.0117  0.0155  0.0421  161 TYR   A CE1 
3595 C  CE2 A TYR   A 161 ? 0.1493 0.1931 0.2381 -0.0007 0.0207  0.0464  161 TYR   A CE2 
3596 C  CE2 B TYR   A 161 ? 0.1663 0.1637 0.1715 0.0139  0.0083  0.0384  161 TYR   A CE2 
3597 C  CZ  A TYR   A 161 ? 0.1601 0.1833 0.2405 -0.0019 0.0163  0.0516  161 TYR   A CZ  
3598 C  CZ  B TYR   A 161 ? 0.1746 0.1709 0.1799 0.0132  0.0104  0.0403  161 TYR   A CZ  
3599 O  OH  A TYR   A 161 ? 0.1762 0.1821 0.2463 -0.0031 0.0086  0.0640  161 TYR   A OH  
3600 O  OH  B TYR   A 161 ? 0.1867 0.1788 0.1979 0.0121  0.0086  0.0408  161 TYR   A OH  
3619 N  N   A ASP   A 162 ? 0.1391 0.2629 0.2248 0.0018  0.0286  0.0855  162 ASP   A N   
3620 N  N   B ASP   A 162 ? 0.1722 0.2371 0.1900 0.0062  0.0194  0.0376  162 ASP   A N   
3621 C  CA  A ASP   A 162 ? 0.1358 0.2966 0.2355 -0.0068 0.0373  0.0663  162 ASP   A CA  
3622 C  CA  B ASP   A 162 ? 0.1750 0.2540 0.2055 0.0135  0.0135  0.0331  162 ASP   A CA  
3623 C  C   A ASP   A 162 ? 0.1229 0.3053 0.2402 -0.0178 0.0410  0.0572  162 ASP   A C   
3624 C  C   B ASP   A 162 ? 0.1770 0.2584 0.2158 0.0163  0.0080  0.0308  162 ASP   A C   
3625 O  O   A ASP   A 162 ? 0.1285 0.3129 0.2644 -0.0141 0.0286  0.0446  162 ASP   A O   
3626 O  O   B ASP   A 162 ? 0.1787 0.2608 0.2215 0.0174  0.0045  0.0268  162 ASP   A O   
3627 C  CB  A ASP   A 162 ? 0.1442 0.3190 0.2546 -0.0023 0.0371  0.0500  162 ASP   A CB  
3628 C  CB  B ASP   A 162 ? 0.1746 0.2639 0.2187 0.0186  0.0067  0.0292  162 ASP   A CB  
3629 C  CG  A ASP   A 162 ? 0.1563 0.3452 0.2763 0.0068  0.0414  0.0396  162 ASP   A CG  
3630 C  CG  B ASP   A 162 ? 0.1732 0.2721 0.2274 0.0245  -0.0052 0.0323  162 ASP   A CG  
3631 O  OD1 A ASP   A 162 ? 0.1706 0.3536 0.2830 -0.0027 0.0403  0.0460  162 ASP   A OD1 
3632 O  OD1 B ASP   A 162 ? 0.1719 0.2726 0.2301 0.0269  -0.0037 0.0403  162 ASP   A OD1 
3633 O  OD2 A ASP   A 162 ? 0.1718 0.3598 0.3056 0.0258  0.0336  0.0272  162 ASP   A OD2 
3634 O  OD2 B ASP   A 162 ? 0.1739 0.2773 0.2288 0.0302  -0.0193 0.0292  162 ASP   A OD2 
3643 N  N   A LYS   A 163 ? 0.1342 0.3170 0.2399 -0.0077 0.0237  0.0393  163 LYS   A N   
3644 N  N   B LYS   A 163 ? 0.1799 0.2609 0.2201 0.0198  0.0039  0.0293  163 LYS   A N   
3645 C  CA  A LYS   A 163 ? 0.1450 0.3273 0.2439 -0.0047 -0.0031 0.0329  163 LYS   A CA  
3646 C  CA  B LYS   A 163 ? 0.1843 0.2625 0.2242 0.0211  0.0014  0.0268  163 LYS   A CA  
3647 C  C   A LYS   A 163 ? 0.1412 0.3172 0.2314 -0.0115 0.0097  0.0407  163 LYS   A C   
3648 C  C   B LYS   A 163 ? 0.1761 0.2578 0.2094 0.0230  0.0052  0.0323  163 LYS   A C   
3649 O  O   A LYS   A 163 ? 0.1302 0.3140 0.2241 -0.0113 0.0118  0.0223  163 LYS   A O   
3650 O  O   B LYS   A 163 ? 0.1732 0.2638 0.2062 0.0224  0.0019  0.0386  163 LYS   A O   
3651 C  CB  A LYS   A 163 ? 0.1771 0.3478 0.2804 0.0142  -0.0247 0.0301  163 LYS   A CB  
3652 C  CB  B LYS   A 163 ? 0.2018 0.2704 0.2535 0.0207  -0.0023 0.0153  163 LYS   A CB  
3653 C  CG  A LYS   A 163 ? 0.2150 0.3661 0.3354 0.0134  -0.0245 0.0275  163 LYS   A CG  
3654 C  CG  B LYS   A 163 ? 0.2190 0.2773 0.2849 0.0186  -0.0018 0.0059  163 LYS   A CG  
3655 C  CD  A LYS   A 163 ? 0.2552 0.3806 0.3993 0.0115  -0.0205 0.0218  163 LYS   A CD  
3656 C  CD  B LYS   A 163 ? 0.2323 0.2825 0.3130 0.0167  -0.0025 -0.0003 163 LYS   A CD  
3657 C  CE  A LYS   A 163 ? 0.2850 0.3893 0.4457 0.0100  -0.0116 0.0231  163 LYS   A CE  
3658 C  CE  B LYS   A 163 ? 0.2405 0.2853 0.3350 0.0167  -0.0034 -0.0065 163 LYS   A CE  
3659 N  NZ  A LYS   A 163 ? 0.3037 0.3948 0.4714 0.0080  -0.0085 0.0298  163 LYS   A NZ  
3660 N  NZ  B LYS   A 163 ? 0.2451 0.2872 0.3478 0.0165  -0.0049 -0.0093 163 LYS   A NZ  
3687 N  N   A LEU   A 164 ? 0.1259 0.2988 0.2019 -0.0230 0.0159  0.0563  164 LEU   A N   
3688 N  N   B LEU   A 164 ? 0.1689 0.2461 0.1964 0.0195  0.0114  0.0299  164 LEU   A N   
3689 C  CA  A LEU   A 164 ? 0.1368 0.2825 0.1883 -0.0335 0.0217  0.0561  164 LEU   A CA  
3690 C  CA  B LEU   A 164 ? 0.1677 0.2346 0.1923 0.0153  0.0162  0.0259  164 LEU   A CA  
3691 C  C   A LEU   A 164 ? 0.1547 0.2816 0.1798 -0.0350 0.0149  0.0452  164 LEU   A C   
3692 C  C   B LEU   A 164 ? 0.1731 0.2356 0.2022 0.0085  0.0171  0.0232  164 LEU   A C   
3693 O  O   A LEU   A 164 ? 0.1531 0.2864 0.1674 -0.0431 0.0342  0.0390  164 LEU   A O   
3694 O  O   B LEU   A 164 ? 0.1688 0.2396 0.2030 0.0054  0.0222  0.0230  164 LEU   A O   
3695 C  CB  A LEU   A 164 ? 0.1321 0.2670 0.1914 -0.0349 0.0249  0.0507  164 LEU   A CB  
3696 C  CB  B LEU   A 164 ? 0.1662 0.2227 0.1804 0.0175  0.0206  0.0219  164 LEU   A CB  
3697 C  CG  A LEU   A 164 ? 0.1399 0.2578 0.1910 -0.0290 0.0176  0.0410  164 LEU   A CG  
3698 C  CG  B LEU   A 164 ? 0.1679 0.2136 0.1780 0.0205  0.0209  0.0177  164 LEU   A CG  
3699 C  CD1 A LEU   A 164 ? 0.1255 0.2529 0.1863 -0.0220 0.0107  0.0405  164 LEU   A CD1 
3700 C  CD1 B LEU   A 164 ? 0.1673 0.2115 0.1814 0.0222  0.0240  0.0118  164 LEU   A CD1 
3701 C  CD2 A LEU   A 164 ? 0.1582 0.2564 0.2009 -0.0308 0.0283  0.0320  164 LEU   A CD2 
3702 C  CD2 B LEU   A 164 ? 0.1687 0.2094 0.1749 0.0191  0.0232  0.0184  164 LEU   A CD2 
3725 N  N   A VAL   A 165 ? 0.1442 0.2708 0.1767 -0.0403 0.0142  0.0480  165 VAL   A N   
3726 N  N   B VAL   A 165 ? 0.1765 0.2324 0.2124 0.0031  0.0131  0.0253  165 VAL   A N   
3727 C  CA  A VAL   A 165 ? 0.1507 0.2650 0.1710 -0.0348 0.0214  0.0486  165 VAL   A CA  
3728 C  CA  B VAL   A 165 ? 0.1823 0.2319 0.2215 0.0002  0.0085  0.0267  165 VAL   A CA  
3729 C  C   A VAL   A 165 ? 0.1425 0.2763 0.1673 -0.0249 0.0284  0.0461  165 VAL   A C   
3730 C  C   B VAL   A 165 ? 0.1786 0.2299 0.2201 -0.0033 0.0095  0.0274  165 VAL   A C   
3731 O  O   A VAL   A 165 ? 0.1358 0.2760 0.1548 -0.0271 0.0390  0.0349  165 VAL   A O   
3732 O  O   B VAL   A 165 ? 0.1847 0.2303 0.2171 -0.0047 0.0147  0.0307  165 VAL   A O   
3733 C  CB  A VAL   A 165 ? 0.1681 0.2473 0.1682 -0.0376 0.0161  0.0474  165 VAL   A CB  
3734 C  CB  B VAL   A 165 ? 0.1896 0.2352 0.2296 0.0020  0.0039  0.0259  165 VAL   A CB  
3735 C  CG1 A VAL   A 165 ? 0.1743 0.2397 0.1789 -0.0374 0.0346  0.0372  165 VAL   A CG1 
3736 C  CG1 B VAL   A 165 ? 0.1958 0.2382 0.2347 0.0034  0.0060  0.0252  165 VAL   A CG1 
3737 C  CG2 A VAL   A 165 ? 0.1791 0.2438 0.1661 -0.0352 -0.0006 0.0622  165 VAL   A CG2 
3738 C  CG2 B VAL   A 165 ? 0.1905 0.2350 0.2334 0.0026  0.0010  0.0260  165 VAL   A CG2 
3757 N  N   A SER   A 166 ? 0.1316 0.2862 0.1952 -0.0196 0.0290  0.0363  166 SER   A N   
3758 N  N   B SER   A 166 ? 0.1650 0.2294 0.2206 -0.0067 0.0098  0.0256  166 SER   A N   
3759 C  CA  A SER   A 166 ? 0.1307 0.2966 0.2195 -0.0183 0.0284  0.0196  166 SER   A CA  
3760 C  CA  B SER   A 166 ? 0.1530 0.2301 0.2088 -0.0115 0.0105  0.0244  166 SER   A CA  
3761 C  C   A SER   A 166 ? 0.1367 0.3056 0.2385 -0.0129 0.0116  0.0158  166 SER   A C   
3762 C  C   B SER   A 166 ? 0.1555 0.2308 0.2117 -0.0117 0.0050  0.0179  166 SER   A C   
3763 O  O   A SER   A 166 ? 0.1491 0.3170 0.2812 -0.0177 0.0220  -0.0128 166 SER   A O   
3764 O  O   B SER   A 166 ? 0.1571 0.2358 0.2131 -0.0053 -0.0017 0.0187  166 SER   A O   
3765 C  CB  A SER   A 166 ? 0.1449 0.2984 0.2471 -0.0125 0.0126  0.0130  166 SER   A CB  
3766 C  CB  B SER   A 166 ? 0.1433 0.2308 0.2083 -0.0124 0.0104  0.0314  166 SER   A CB  
3767 O  OG  A SER   A 166 ? 0.1655 0.3029 0.2753 -0.0098 0.0136  0.0251  166 SER   A OG  
3768 O  OG  B SER   A 166 ? 0.1373 0.2327 0.2046 -0.0132 0.0106  0.0411  166 SER   A OG  
3779 N  N   A SER   A 167 ? 0.1429 0.2996 0.1896 0.0102  -0.0054 0.0460  167 SER   A N   
3780 N  N   B SER   A 167 ? 0.1597 0.2282 0.2193 -0.0145 0.0093  0.0182  167 SER   A N   
3781 C  CA  A SER   A 167 ? 0.1700 0.2980 0.2049 0.0149  -0.0087 0.0410  167 SER   A CA  
3782 C  CA  B SER   A 167 ? 0.1671 0.2266 0.2180 -0.0115 0.0111  0.0173  167 SER   A CA  
3783 C  C   A SER   A 167 ? 0.1760 0.2949 0.2141 0.0230  0.0027  0.0342  167 SER   A C   
3784 C  C   B SER   A 167 ? 0.1668 0.2307 0.2107 -0.0034 0.0144  0.0177  167 SER   A C   
3785 O  O   A SER   A 167 ? 0.1955 0.3063 0.2270 0.0297  -0.0148 0.0281  167 SER   A O   
3786 O  O   B SER   A 167 ? 0.1750 0.2374 0.2155 0.0030  0.0097  0.0122  167 SER   A O   
3787 C  CB  A SER   A 167 ? 0.1784 0.2985 0.2040 0.0137  0.0026  0.0440  167 SER   A CB  
3788 C  CB  B SER   A 167 ? 0.1748 0.2234 0.2316 -0.0112 0.0115  0.0130  167 SER   A CB  
3789 O  OG  A SER   A 167 ? 0.1758 0.2971 0.2160 0.0095  0.0251  0.0530  167 SER   A OG  
3790 O  OG  B SER   A 167 ? 0.1806 0.2228 0.2486 -0.0101 0.0106  0.0104  167 SER   A OG  
3801 N  N   A PHE   A 168 ? 0.1608 0.2819 0.2035 0.0240  0.0132  0.0355  168 PHE   A N   
3802 N  N   B PHE   A 168 ? 0.1595 0.2259 0.2027 -0.0028 0.0155  0.0238  168 PHE   A N   
3803 C  CA  A PHE   A 168 ? 0.1576 0.2804 0.2190 0.0174  0.0181  0.0422  168 PHE   A CA  
3804 C  CA  B PHE   A 168 ? 0.1629 0.2250 0.2009 -0.0037 0.0201  0.0246  168 PHE   A CA  
3805 C  C   A PHE   A 168 ? 0.1625 0.2951 0.2419 0.0128  0.0499  0.0240  168 PHE   A C   
3806 C  C   B PHE   A 168 ? 0.1631 0.2287 0.2000 -0.0033 0.0328  0.0198  168 PHE   A C   
3807 O  O   A PHE   A 168 ? 0.1744 0.3069 0.2865 -0.0011 0.0600  0.0322  168 PHE   A O   
3808 O  O   B PHE   A 168 ? 0.1472 0.2287 0.1846 -0.0025 0.0445  0.0209  168 PHE   A O   
3809 C  CB  A PHE   A 168 ? 0.1593 0.2687 0.2011 0.0096  0.0058  0.0483  168 PHE   A CB  
3810 C  CB  B PHE   A 168 ? 0.1707 0.2209 0.2004 -0.0093 0.0124  0.0273  168 PHE   A CB  
3811 C  CG  A PHE   A 168 ? 0.1512 0.2623 0.1909 -0.0002 -0.0036 0.0556  168 PHE   A CG  
3812 C  CG  B PHE   A 168 ? 0.1777 0.2165 0.2066 -0.0131 0.0088  0.0332  168 PHE   A CG  
3813 C  CD1 A PHE   A 168 ? 0.1536 0.2643 0.1992 -0.0075 -0.0035 0.0651  168 PHE   A CD1 
3814 C  CD1 B PHE   A 168 ? 0.1819 0.2155 0.2162 -0.0154 0.0105  0.0337  168 PHE   A CD1 
3815 C  CD2 A PHE   A 168 ? 0.1512 0.2602 0.1951 -0.0066 0.0105  0.0515  168 PHE   A CD2 
3816 C  CD2 B PHE   A 168 ? 0.1846 0.2151 0.2097 -0.0099 0.0018  0.0377  168 PHE   A CD2 
3817 C  CE1 A PHE   A 168 ? 0.1416 0.2597 0.1876 -0.0095 0.0041  0.0676  168 PHE   A CE1 
3818 C  CE1 B PHE   A 168 ? 0.1843 0.2155 0.2156 -0.0146 0.0093  0.0320  168 PHE   A CE1 
3819 C  CE2 A PHE   A 168 ? 0.1591 0.2531 0.1975 -0.0081 0.0144  0.0630  168 PHE   A CE2 
3820 C  CE2 B PHE   A 168 ? 0.1903 0.2169 0.2134 -0.0076 0.0005  0.0366  168 PHE   A CE2 
3821 C  CZ  A PHE   A 168 ? 0.1521 0.2524 0.1971 -0.0101 0.0084  0.0688  168 PHE   A CZ  
3822 C  CZ  B PHE   A 168 ? 0.1918 0.2176 0.2180 -0.0100 0.0053  0.0331  168 PHE   A CZ  
3841 N  N   A LEU   A 169 ? 0.1934 0.2956 0.2748 0.0034  0.0498  0.0008  169 LEU   A N   
3842 N  N   B LEU   A 169 ? 0.1823 0.2360 0.2168 -0.0017 0.0264  0.0192  169 LEU   A N   
3843 C  CA  A LEU   A 169 ? 0.2334 0.3049 0.3398 0.0052  0.0305  -0.0100 169 LEU   A CA  
3844 C  CA  B LEU   A 169 ? 0.2079 0.2464 0.2464 -0.0034 0.0168  0.0098  169 LEU   A CA  
3845 C  C   A LEU   A 169 ? 0.2285 0.2999 0.3662 -0.0003 0.0380  0.0088  169 LEU   A C   
3846 C  C   B LEU   A 169 ? 0.2241 0.2533 0.2588 0.0010  0.0068  0.0068  169 LEU   A C   
3847 O  O   A LEU   A 169 ? 0.2297 0.3038 0.3737 0.0038  0.0312  0.0064  169 LEU   A O   
3848 O  O   B LEU   A 169 ? 0.2305 0.2519 0.2636 -0.0019 0.0045  0.0070  169 LEU   A O   
3849 C  CB  A LEU   A 169 ? 0.2695 0.3217 0.3575 0.0045  0.0163  -0.0297 169 LEU   A CB  
3850 C  CB  B LEU   A 169 ? 0.2191 0.2516 0.2609 -0.0074 0.0190  0.0040  169 LEU   A CB  
3851 C  CG  A LEU   A 169 ? 0.3014 0.3377 0.3757 -0.0007 0.0034  -0.0517 169 LEU   A CG  
3852 C  CG  B LEU   A 169 ? 0.2311 0.2583 0.2736 -0.0108 0.0118  0.0005  169 LEU   A CG  
3853 C  CD1 A LEU   A 169 ? 0.3113 0.3413 0.3803 -0.0034 -0.0053 -0.0578 169 LEU   A CD1 
3854 C  CD1 B LEU   A 169 ? 0.2375 0.2621 0.2809 -0.0119 0.0057  -0.0010 169 LEU   A CD1 
3855 C  CD2 A LEU   A 169 ? 0.3092 0.3476 0.3784 -0.0044 0.0036  -0.0572 169 LEU   A CD2 
3856 C  CD2 B LEU   A 169 ? 0.2343 0.2596 0.2772 -0.0105 0.0148  -0.0021 169 LEU   A CD2 
3857 O  OXT A LEU   A 169 ? 0.2114 0.2983 0.3667 -0.0082 0.0531  0.0207  169 LEU   A OXT 
3858 O  OXT B LEU   A 169 ? 0.2340 0.2603 0.2700 0.0043  -0.0015 0.0036  169 LEU   A OXT 
3881 N  N   A SER   B 1   ? 0.3829 0.3539 0.3674 -0.1052 -0.0637 0.0446  1   SER   B N   
3882 N  N   B SER   B 1   ? 0.3577 0.3513 0.3589 -0.0388 -0.0292 0.0175  1   SER   B N   
3883 C  CA  A SER   B 1   ? 0.3708 0.3541 0.3742 -0.1137 -0.0619 0.0389  1   SER   B CA  
3884 C  CA  B SER   B 1   ? 0.3544 0.3510 0.3623 -0.0401 -0.0274 0.0158  1   SER   B CA  
3885 C  C   A SER   B 1   ? 0.3386 0.3521 0.3384 -0.1199 -0.0708 0.0576  1   SER   B C   
3886 C  C   B SER   B 1   ? 0.3435 0.3485 0.3461 -0.0403 -0.0301 0.0221  1   SER   B C   
3887 O  O   A SER   B 1   ? 0.3453 0.3536 0.3020 -0.1135 -0.0671 0.0606  1   SER   B O   
3888 O  O   B SER   B 1   ? 0.3453 0.3490 0.3354 -0.0393 -0.0317 0.0220  1   SER   B O   
3889 C  CB  A SER   B 1   ? 0.3858 0.3538 0.3898 -0.1141 -0.0520 0.0213  1   SER   B CB  
3890 C  CB  B SER   B 1   ? 0.3598 0.3519 0.3658 -0.0403 -0.0227 0.0090  1   SER   B CB  
3891 O  OG  A SER   B 1   ? 0.3990 0.3619 0.4408 -0.1119 -0.0514 0.0180  1   SER   B OG  
3892 O  OG  B SER   B 1   ? 0.3643 0.3546 0.3845 -0.0405 -0.0220 0.0065  1   SER   B OG  
3907 N  N   A MET   B 2   ? 0.3056 0.3483 0.3343 -0.1231 -0.0788 0.0927  2   MET   B N   
3908 N  N   B MET   B 2   ? 0.3311 0.3450 0.3411 -0.0397 -0.0303 0.0328  2   MET   B N   
3909 C  CA  A MET   B 2   ? 0.2820 0.3498 0.3501 -0.1046 -0.0847 0.1131  2   MET   B CA  
3910 C  CA  B MET   B 2   ? 0.3184 0.3406 0.3391 -0.0349 -0.0295 0.0406  2   MET   B CA  
3911 C  C   A MET   B 2   ? 0.2429 0.3262 0.3145 -0.0860 -0.0985 0.1400  2   MET   B C   
3912 C  C   B MET   B 2   ? 0.2951 0.3219 0.3061 -0.0347 -0.0283 0.0468  2   MET   B C   
3913 O  O   A MET   B 2   ? 0.2366 0.3373 0.3136 -0.0729 -0.1074 0.1405  2   MET   B O   
3914 O  O   B MET   B 2   ? 0.2973 0.3259 0.3053 -0.0322 -0.0237 0.0439  2   MET   B O   
3915 C  CB  A MET   B 2   ? 0.3150 0.3869 0.4416 -0.0820 -0.0644 0.0834  2   MET   B CB  
3916 C  CB  B MET   B 2   ? 0.3302 0.3556 0.3776 -0.0273 -0.0288 0.0386  2   MET   B CB  
3917 C  CG  A MET   B 2   ? 0.3460 0.4192 0.5150 -0.0576 -0.0428 0.0649  2   MET   B CG  
3918 C  CG  B MET   B 2   ? 0.3408 0.3695 0.4095 -0.0196 -0.0275 0.0407  2   MET   B CG  
3919 S  SD  A MET   B 2   ? 0.3754 0.4487 0.5915 -0.0370 -0.0284 0.0523  2   MET   B SD  
3920 S  SD  B MET   B 2   ? 0.3503 0.3823 0.4400 -0.0128 -0.0278 0.0440  2   MET   B SD  
3921 C  CE  A MET   B 2   ? 0.3816 0.4556 0.5944 -0.0327 -0.0252 0.0531  2   MET   B CE  
3922 C  CE  B MET   B 2   ? 0.3525 0.3854 0.4449 -0.0119 -0.0272 0.0403  2   MET   B CE  
3941 N  N   A VAL   B 3   ? 0.2179 0.2884 0.2952 -0.0870 -0.0889 0.1506  3   VAL   B N   
3942 N  N   B VAL   B 3   ? 0.2689 0.2975 0.2750 -0.0383 -0.0308 0.0542  3   VAL   B N   
3943 C  CA  A VAL   B 3   ? 0.2116 0.2548 0.2899 -0.0739 -0.0774 0.1324  3   VAL   B CA  
3944 C  CA  B VAL   B 3   ? 0.2441 0.2727 0.2501 -0.0398 -0.0329 0.0579  3   VAL   B CA  
3945 C  C   A VAL   B 3   ? 0.1956 0.2417 0.2547 -0.0616 -0.0710 0.1148  3   VAL   B C   
3946 C  C   B VAL   B 3   ? 0.2155 0.2513 0.2241 -0.0440 -0.0427 0.0710  3   VAL   B C   
3947 O  O   A VAL   B 3   ? 0.1928 0.2456 0.2690 -0.0624 -0.0739 0.1165  3   VAL   B O   
3948 O  O   B VAL   B 3   ? 0.2146 0.2554 0.2124 -0.0359 -0.0414 0.0663  3   VAL   B O   
3949 C  CB  A VAL   B 3   ? 0.2306 0.2509 0.3313 -0.0725 -0.0669 0.1148  3   VAL   B CB  
3950 C  CB  B VAL   B 3   ? 0.2492 0.2710 0.2583 -0.0380 -0.0262 0.0496  3   VAL   B CB  
3951 C  CG1 A VAL   B 3   ? 0.2415 0.2450 0.3505 -0.0754 -0.0648 0.1098  3   VAL   B CG1 
3952 C  CG1 B VAL   B 3   ? 0.2521 0.2700 0.2638 -0.0383 -0.0238 0.0462  3   VAL   B CG1 
3953 C  CG2 A VAL   B 3   ? 0.2358 0.2594 0.3494 -0.0627 -0.0606 0.1150  3   VAL   B CG2 
3954 C  CG2 B VAL   B 3   ? 0.2511 0.2723 0.2618 -0.0355 -0.0249 0.0490  3   VAL   B CG2 
3973 N  N   . ASN   B 4   ? 0.1894 0.2244 0.2224 -0.0567 -0.0568 0.0853  4   ASN   B N   
3974 C  CA  . ASN   B 4   ? 0.1849 0.2172 0.2039 -0.0602 -0.0448 0.0427  4   ASN   B CA  
3975 C  C   . ASN   B 4   ? 0.1927 0.2311 0.1888 -0.0627 -0.0355 0.0291  4   ASN   B C   
3976 O  O   . ASN   B 4   ? 0.1974 0.2374 0.2068 -0.0563 -0.0272 0.0125  4   ASN   B O   
3977 C  CB  . ASN   B 4   ? 0.1831 0.2116 0.1827 -0.0475 -0.0552 0.0345  4   ASN   B CB  
3978 C  CG  . ASN   B 4   ? 0.1800 0.1964 0.1705 -0.0450 -0.0523 0.0284  4   ASN   B CG  
3979 O  OD1 . ASN   B 4   ? 0.1843 0.1773 0.1752 -0.0467 -0.0507 0.0261  4   ASN   B OD1 
3980 N  ND2 . ASN   B 4   ? 0.1962 0.2020 0.1797 -0.0233 -0.0373 0.0242  4   ASN   B ND2 
3988 N  N   . SER   B 5   ? 0.2086 0.2499 0.2005 -0.0632 -0.0188 0.0317  5   SER   B N   
3989 C  CA  . SER   B 5   ? 0.2378 0.2867 0.2350 -0.0551 0.0038  0.0325  5   SER   B CA  
3990 C  C   . SER   B 5   ? 0.2589 0.2922 0.2586 -0.0714 0.0313  0.0296  5   SER   B C   
3991 O  O   . SER   B 5   ? 0.2753 0.2916 0.3287 -0.0678 0.0643  0.0281  5   SER   B O   
3992 C  CB  . SER   B 5   ? 0.2504 0.3140 0.2684 -0.0475 0.0182  0.0458  5   SER   B CB  
3993 O  OG  . SER   B 5   ? 0.2717 0.3341 0.3185 -0.0350 0.0212  0.0498  5   SER   B OG  
3999 N  N   . PHE   B 6   ? 0.2756 0.3078 0.2351 -0.0727 0.0376  0.0323  6   PHE   B N   
4000 C  CA  . PHE   B 6   ? 0.2833 0.3093 0.2029 -0.0879 0.0418  0.0141  6   PHE   B CA  
4001 C  C   . PHE   B 6   ? 0.3344 0.3439 0.2304 -0.0963 0.0688  -0.0102 6   PHE   B C   
4002 O  O   . PHE   B 6   ? 0.3485 0.3738 0.2707 -0.0896 0.0549  -0.0264 6   PHE   B O   
4003 C  CB  . PHE   B 6   ? 0.2516 0.2831 0.1754 -0.0767 0.0167  0.0104  6   PHE   B CB  
4004 C  CG  . PHE   B 6   ? 0.2170 0.2494 0.1629 -0.0730 -0.0007 0.0131  6   PHE   B CG  
4005 C  CD1 . PHE   B 6   ? 0.2183 0.2259 0.1466 -0.0651 -0.0172 0.0095  6   PHE   B CD1 
4006 C  CD2 . PHE   B 6   ? 0.1965 0.2463 0.1653 -0.0615 0.0022  0.0367  6   PHE   B CD2 
4007 C  CE1 . PHE   B 6   ? 0.2117 0.2040 0.1580 -0.0602 -0.0202 0.0065  6   PHE   B CE1 
4008 C  CE2 . PHE   B 6   ? 0.1956 0.2320 0.1881 -0.0536 -0.0002 0.0319  6   PHE   B CE2 
4009 C  CZ  . PHE   B 6   ? 0.1988 0.2127 0.1719 -0.0531 -0.0114 0.0089  6   PHE   B CZ  
4019 N  N   . SER   B 7   ? 0.3690 0.3331 0.2503 -0.1153 0.0989  -0.0361 7   SER   B N   
4020 C  CA  . SER   B 7   ? 0.3975 0.3428 0.3036 -0.1142 0.1210  -0.0475 7   SER   B CA  
4021 C  C   . SER   B 7   ? 0.3951 0.3220 0.2838 -0.1157 0.1332  -0.0611 7   SER   B C   
4022 O  O   . SER   B 7   ? 0.3990 0.3220 0.3142 -0.1112 0.1315  -0.0642 7   SER   B O   
4023 C  CB  . SER   B 7   ? 0.4172 0.3749 0.3725 -0.1105 0.1329  -0.0419 7   SER   B CB  
4024 O  OG  . SER   B 7   ? 0.4275 0.3890 0.4196 -0.1086 0.1354  -0.0316 7   SER   B OG  
4030 N  N   . GLY   B 8   ? 0.3920 0.3113 0.2905 -0.1078 0.1396  -0.0667 8   GLY   B N   
4031 C  CA  . GLY   B 8   ? 0.3767 0.2940 0.2936 -0.1008 0.1389  -0.0712 8   GLY   B CA  
4032 C  C   . GLY   B 8   ? 0.3526 0.2673 0.2878 -0.0947 0.1306  -0.0698 8   GLY   B C   
4033 O  O   . GLY   B 8   ? 0.3609 0.2709 0.3239 -0.0862 0.1323  -0.0743 8   GLY   B O   
4037 N  N   . TYR   B 9   ? 0.3313 0.2431 0.2666 -0.0828 0.1043  -0.0777 9   TYR   B N   
4038 C  CA  . TYR   B 9   ? 0.3095 0.2163 0.2340 -0.0679 0.0805  -0.0630 9   TYR   B CA  
4039 C  C   . TYR   B 9   ? 0.3065 0.2137 0.2181 -0.0676 0.0549  -0.0480 9   TYR   B C   
4040 O  O   . TYR   B 9   ? 0.3236 0.2374 0.2567 -0.0731 0.0551  -0.0365 9   TYR   B O   
4041 C  CB  . TYR   B 9   ? 0.2963 0.1928 0.2350 -0.0576 0.0735  -0.0546 9   TYR   B CB  
4042 C  CG  . TYR   B 9   ? 0.2848 0.1745 0.2360 -0.0620 0.0667  -0.0566 9   TYR   B CG  
4043 C  CD1 . TYR   B 9   ? 0.2885 0.1746 0.2590 -0.0783 0.0709  -0.0475 9   TYR   B CD1 
4044 C  CD2 . TYR   B 9   ? 0.2710 0.1697 0.2291 -0.0528 0.0597  -0.0602 9   TYR   B CD2 
4045 C  CE1 . TYR   B 9   ? 0.2861 0.1842 0.2618 -0.0828 0.0752  -0.0552 9   TYR   B CE1 
4046 C  CE2 . TYR   B 9   ? 0.2744 0.1740 0.2394 -0.0531 0.0591  -0.0593 9   TYR   B CE2 
4047 C  CZ  . TYR   B 9   ? 0.2787 0.1887 0.2526 -0.0712 0.0689  -0.0657 9   TYR   B CZ  
4048 O  OH  . TYR   B 9   ? 0.2759 0.2038 0.2670 -0.0830 0.0684  -0.0811 9   TYR   B OH  
4058 N  N   . LEU   B 10  ? 0.2870 0.1891 0.2010 -0.0642 0.0299  -0.0442 10  LEU   B N   
4059 C  CA  . LEU   B 10  ? 0.2839 0.1901 0.2060 -0.0699 -0.0066 -0.0370 10  LEU   B CA  
4060 C  C   . LEU   B 10  ? 0.2629 0.1921 0.2031 -0.0666 -0.0263 -0.0293 10  LEU   B C   
4061 O  O   . LEU   B 10  ? 0.2461 0.1924 0.2106 -0.0547 -0.0195 -0.0230 10  LEU   B O   
4062 C  CB  . LEU   B 10  ? 0.3036 0.1884 0.2294 -0.0739 -0.0255 -0.0182 10  LEU   B CB  
4063 C  CG  . LEU   B 10  ? 0.3266 0.1948 0.2600 -0.0704 -0.0519 -0.0106 10  LEU   B CG  
4064 C  CD1 . LEU   B 10  ? 0.3441 0.2104 0.2834 -0.0659 -0.0471 -0.0105 10  LEU   B CD1 
4065 C  CD2 . LEU   B 10  ? 0.3382 0.1991 0.2992 -0.0683 -0.0525 0.0044  10  LEU   B CD2 
4077 N  N   . LYS   B 11  ? 0.2783 0.2168 0.2018 -0.0597 -0.0352 -0.0256 11  LYS   B N   
4078 C  CA  . LYS   B 11  ? 0.2973 0.2413 0.2431 -0.0492 -0.0489 -0.0368 11  LYS   B CA  
4079 C  C   . LYS   B 11  ? 0.2806 0.2192 0.2493 -0.0679 -0.0415 -0.0473 11  LYS   B C   
4080 O  O   . LYS   B 11  ? 0.2950 0.2350 0.2823 -0.0865 -0.0356 -0.0781 11  LYS   B O   
4081 C  CB  . LYS   B 11  ? 0.3311 0.2942 0.3102 -0.0223 -0.0603 -0.0316 11  LYS   B CB  
4082 C  CG  . LYS   B 11  ? 0.3630 0.3302 0.3811 -0.0064 -0.0622 -0.0267 11  LYS   B CG  
4083 C  CD  . LYS   B 11  ? 0.3893 0.3527 0.4437 0.0009  -0.0610 -0.0262 11  LYS   B CD  
4084 C  CE  . LYS   B 11  ? 0.4085 0.3657 0.4892 0.0018  -0.0632 -0.0296 11  LYS   B CE  
4085 N  NZ  . LYS   B 11  ? 0.4189 0.3728 0.5120 0.0006  -0.0679 -0.0308 11  LYS   B NZ  
4099 N  N   . LEU   B 12  ? 0.2451 0.1905 0.2349 -0.0602 -0.0384 -0.0398 12  LEU   B N   
4100 C  CA  . LEU   B 12  ? 0.2285 0.1760 0.2583 -0.0509 -0.0302 -0.0350 12  LEU   B CA  
4101 C  C   . LEU   B 12  ? 0.2134 0.1769 0.2666 -0.0530 -0.0435 -0.0277 12  LEU   B C   
4102 O  O   . LEU   B 12  ? 0.2085 0.1778 0.2851 -0.0587 -0.0513 -0.0237 12  LEU   B O   
4103 C  CB  . LEU   B 12  ? 0.2268 0.1573 0.2580 -0.0412 -0.0231 -0.0384 12  LEU   B CB  
4104 C  CG  . LEU   B 12  ? 0.2227 0.1545 0.2605 -0.0443 -0.0129 -0.0302 12  LEU   B CG  
4105 C  CD1 . LEU   B 12  ? 0.2385 0.1574 0.2572 -0.0282 -0.0113 -0.0154 12  LEU   B CD1 
4106 C  CD2 . LEU   B 12  ? 0.2254 0.1565 0.2744 -0.0425 -0.0043 -0.0377 12  LEU   B CD2 
4118 N  N   . THR   B 13  ? 0.2069 0.1809 0.2746 -0.0518 -0.0512 -0.0390 13  THR   B N   
4119 C  CA  . THR   B 13  ? 0.2040 0.1901 0.2711 -0.0593 -0.0614 -0.0245 13  THR   B CA  
4120 C  C   . THR   B 13  ? 0.2457 0.2115 0.2854 -0.0705 -0.0710 -0.0209 13  THR   B C   
4121 O  O   . THR   B 13  ? 0.2588 0.2091 0.3002 -0.0718 -0.0359 -0.0214 13  THR   B O   
4122 C  CB  . THR   B 13  ? 0.1864 0.1881 0.2701 -0.0511 -0.0514 -0.0160 13  THR   B CB  
4123 O  OG1 . THR   B 13  ? 0.1777 0.1815 0.2813 -0.0396 -0.0388 -0.0171 13  THR   B OG1 
4124 C  CG2 . THR   B 13  ? 0.1900 0.1955 0.2795 -0.0434 -0.0371 -0.0140 13  THR   B CG2 
4132 N  N   A ASP   B 14  ? 0.2649 0.2256 0.2913 -0.0769 -0.1048 -0.0133 14  ASP   B N   
4133 N  N   B ASP   B 14  ? 0.2561 0.2217 0.3000 -0.0682 -0.0749 -0.0150 14  ASP   B N   
4134 C  CA  A ASP   B 14  ? 0.2793 0.2416 0.3192 -0.0797 -0.1100 0.0078  14  ASP   B CA  
4135 C  CA  B ASP   B 14  ? 0.2657 0.2308 0.3157 -0.0658 -0.0707 -0.0073 14  ASP   B CA  
4136 C  C   A ASP   B 14  ? 0.2668 0.2223 0.2853 -0.0786 -0.0886 0.0102  14  ASP   B C   
4137 C  C   B ASP   B 14  ? 0.2504 0.2141 0.2813 -0.0656 -0.0735 -0.0039 14  ASP   B C   
4138 O  O   A ASP   B 14  ? 0.2959 0.2368 0.2878 -0.0813 -0.0849 0.0199  14  ASP   B O   
4139 O  O   B ASP   B 14  ? 0.2586 0.2168 0.2765 -0.0666 -0.0762 -0.0067 14  ASP   B O   
4140 C  CB  A ASP   B 14  ? 0.3051 0.2782 0.3955 -0.0765 -0.1242 0.0091  14  ASP   B CB  
4141 C  CB  B ASP   B 14  ? 0.2891 0.2556 0.3636 -0.0616 -0.0632 -0.0061 14  ASP   B CB  
4142 C  CG  A ASP   B 14  ? 0.3367 0.3115 0.4674 -0.0689 -0.1153 -0.0027 14  ASP   B CG  
4143 C  CG  B ASP   B 14  ? 0.3109 0.2772 0.4073 -0.0566 -0.0547 -0.0080 14  ASP   B CG  
4144 O  OD1 A ASP   B 14  ? 0.3530 0.3221 0.4813 -0.0673 -0.1141 -0.0159 14  ASP   B OD1 
4145 O  OD1 B ASP   B 14  ? 0.3200 0.2871 0.4173 -0.0554 -0.0522 -0.0106 14  ASP   B OD1 
4146 O  OD2 A ASP   B 14  ? 0.3425 0.3255 0.5001 -0.0664 -0.1082 0.0005  14  ASP   B OD2 
4147 O  OD2 B ASP   B 14  ? 0.3174 0.2842 0.4218 -0.0561 -0.0522 -0.0069 14  ASP   B OD2 
4156 N  N   . ASN   B 15  ? 0.2272 0.1950 0.2569 -0.0607 -0.0765 0.0049  15  ASN   B N   
4157 C  CA  . ASN   B 15  ? 0.1803 0.1675 0.2342 -0.0381 -0.0539 0.0013  15  ASN   B CA  
4158 C  C   . ASN   B 15  ? 0.1610 0.1521 0.2126 -0.0274 -0.0398 -0.0020 15  ASN   B C   
4159 O  O   . ASN   B 15  ? 0.1627 0.1471 0.2373 -0.0272 -0.0424 -0.0181 15  ASN   B O   
4160 C  CB  . ASN   B 15  ? 0.1697 0.1624 0.2471 -0.0185 -0.0500 0.0053  15  ASN   B CB  
4161 C  CG  . ASN   B 15  ? 0.1580 0.1574 0.2483 -0.0223 -0.0255 0.0076  15  ASN   B CG  
4162 O  OD1 . ASN   B 15  ? 0.1630 0.1859 0.2790 -0.0430 -0.0335 0.0152  15  ASN   B OD1 
4163 N  ND2 . ASN   B 15  ? 0.1613 0.1360 0.2532 -0.0108 0.0008  -0.0046 15  ASN   B ND2 
4171 N  N   . VAL   B 16  ? 0.1668 0.1457 0.2121 -0.0324 -0.0458 -0.0013 16  VAL   B N   
4172 C  CA  . VAL   B 16  ? 0.1680 0.1494 0.2073 -0.0274 -0.0361 -0.0222 16  VAL   B CA  
4173 C  C   . VAL   B 16  ? 0.1617 0.1569 0.2094 -0.0343 -0.0329 -0.0199 16  VAL   B C   
4174 O  O   . VAL   B 16  ? 0.1646 0.1712 0.2277 -0.0331 -0.0300 -0.0303 16  VAL   B O   
4175 C  CB  . VAL   B 16  ? 0.1731 0.1439 0.2147 -0.0149 -0.0206 -0.0188 16  VAL   B CB  
4176 C  CG1 . VAL   B 16  ? 0.1818 0.1363 0.2121 -0.0034 -0.0180 -0.0146 16  VAL   B CG1 
4177 C  CG2 . VAL   B 16  ? 0.1685 0.1525 0.2310 -0.0093 -0.0156 -0.0147 16  VAL   B CG2 
4187 N  N   . TYR   B 17  ? 0.1697 0.1616 0.1991 -0.0264 -0.0279 -0.0285 17  TYR   B N   
4188 C  CA  . TYR   B 17  ? 0.1746 0.1725 0.1936 -0.0377 -0.0251 -0.0074 17  TYR   B CA  
4189 C  C   . TYR   B 17  ? 0.1692 0.1522 0.1974 -0.0374 -0.0151 -0.0101 17  TYR   B C   
4190 O  O   . TYR   B 17  ? 0.1682 0.1575 0.1992 -0.0308 -0.0245 -0.0300 17  TYR   B O   
4191 C  CB  . TYR   B 17  ? 0.2063 0.2159 0.2157 -0.0189 -0.0264 0.0263  17  TYR   B CB  
4192 C  CG  . TYR   B 17  ? 0.2397 0.2670 0.2596 -0.0110 -0.0455 0.0358  17  TYR   B CG  
4193 C  CD1 . TYR   B 17  ? 0.2569 0.2825 0.2811 -0.0084 -0.0611 0.0485  17  TYR   B CD1 
4194 C  CD2 . TYR   B 17  ? 0.2638 0.2958 0.2903 -0.0041 -0.0549 0.0335  17  TYR   B CD2 
4195 C  CE1 . TYR   B 17  ? 0.2756 0.3034 0.2974 -0.0010 -0.0751 0.0402  17  TYR   B CE1 
4196 C  CE2 . TYR   B 17  ? 0.2798 0.3122 0.3162 0.0048  -0.0698 0.0387  17  TYR   B CE2 
4197 C  CZ  . TYR   B 17  ? 0.2897 0.3207 0.3192 0.0061  -0.0790 0.0428  17  TYR   B CZ  
4198 O  OH  . TYR   B 17  ? 0.3084 0.3364 0.3381 0.0099  -0.0822 0.0502  17  TYR   B OH  
4208 N  N   . ILE   B 18  ? 0.1775 0.1503 0.1970 -0.0334 -0.0107 -0.0255 18  ILE   B N   
4209 C  CA  . ILE   B 18  ? 0.1816 0.1460 0.1974 -0.0349 -0.0088 -0.0283 18  ILE   B CA  
4210 C  C   . ILE   B 18  ? 0.1926 0.1492 0.1936 -0.0427 -0.0063 -0.0345 18  ILE   B C   
4211 O  O   . ILE   B 18  ? 0.2127 0.1639 0.2051 -0.0357 0.0038  -0.0379 18  ILE   B O   
4212 C  CB  . ILE   B 18  ? 0.1876 0.1495 0.2037 -0.0406 -0.0077 -0.0186 18  ILE   B CB  
4213 C  CG1 . ILE   B 18  ? 0.1932 0.1483 0.2122 -0.0403 -0.0066 -0.0104 18  ILE   B CG1 
4214 C  CG2 . ILE   B 18  ? 0.1898 0.1557 0.2058 -0.0456 -0.0141 -0.0170 18  ILE   B CG2 
4215 C  CD1 . ILE   B 18  ? 0.2031 0.1789 0.2277 -0.0398 -0.0229 0.0093  18  ILE   B CD1 
4227 N  N   . LYS   B 19  ? 0.1953 0.1528 0.2093 -0.0239 0.0260  -0.0441 19  LYS   B N   
4228 C  CA  . LYS   B 19  ? 0.2031 0.1555 0.2280 -0.0260 0.0312  -0.0476 19  LYS   B CA  
4229 C  C   . LYS   B 19  ? 0.1870 0.1567 0.2367 -0.0228 0.0345  -0.0504 19  LYS   B C   
4230 O  O   . LYS   B 19  ? 0.1847 0.1582 0.2085 -0.0151 0.0191  -0.0415 19  LYS   B O   
4231 C  CB  . LYS   B 19  ? 0.2276 0.1765 0.2423 -0.0330 0.0455  -0.0357 19  LYS   B CB  
4232 C  CG  . LYS   B 19  ? 0.2554 0.2010 0.2634 -0.0431 0.0557  -0.0388 19  LYS   B CG  
4233 C  CD  . LYS   B 19  ? 0.2798 0.2293 0.2733 -0.0542 0.0612  -0.0372 19  LYS   B CD  
4234 C  CE  . LYS   B 19  ? 0.3021 0.2553 0.3036 -0.0553 0.0582  -0.0383 19  LYS   B CE  
4235 N  NZ  . LYS   B 19  ? 0.3116 0.2702 0.3115 -0.0619 0.0619  -0.0336 19  LYS   B NZ  
4249 N  N   . ASN   B 20  ? 0.1878 0.1634 0.2721 -0.0176 0.0414  -0.0609 20  ASN   B N   
4250 C  CA  . ASN   B 20  ? 0.1869 0.1758 0.2915 -0.0140 0.0430  -0.0777 20  ASN   B CA  
4251 C  C   . ASN   B 20  ? 0.1852 0.1946 0.2940 -0.0187 0.0535  -0.0861 20  ASN   B C   
4252 O  O   . ASN   B 20  ? 0.2017 0.2308 0.3102 -0.0353 0.0507  -0.0853 20  ASN   B O   
4253 C  CB  . ASN   B 20  ? 0.2135 0.1797 0.3222 0.0064  0.0345  -0.0760 20  ASN   B CB  
4254 C  CG  . ASN   B 20  ? 0.2406 0.1909 0.3428 0.0351  0.0348  -0.0823 20  ASN   B CG  
4255 O  OD1 . ASN   B 20  ? 0.2740 0.2218 0.3712 0.0498  0.0350  -0.0832 20  ASN   B OD1 
4256 N  ND2 . ASN   B 20  ? 0.2292 0.1902 0.3347 0.0365  0.0231  -0.0808 20  ASN   B ND2 
4263 N  N   . ALA   B 21  ? 0.1854 0.1805 0.2890 -0.0253 0.0538  -0.0704 21  ALA   B N   
4264 C  CA  . ALA   B 21  ? 0.1953 0.1886 0.2948 -0.0325 0.0352  -0.0538 21  ALA   B CA  
4265 C  C   . ALA   B 21  ? 0.1934 0.1638 0.2806 -0.0221 0.0375  -0.0394 21  ALA   B C   
4266 O  O   . ALA   B 21  ? 0.1959 0.1517 0.2875 -0.0258 0.0383  -0.0325 21  ALA   B O   
4267 C  CB  . ALA   B 21  ? 0.2108 0.2165 0.3012 -0.0415 0.0332  -0.0422 21  ALA   B CB  
4273 N  N   . ASP   B 22  ? 0.1807 0.1558 0.2704 -0.0211 0.0310  -0.0322 22  ASP   B N   
4274 C  CA  . ASP   B 22  ? 0.1800 0.1460 0.2640 -0.0127 0.0222  -0.0210 22  ASP   B CA  
4275 C  C   . ASP   B 22  ? 0.1740 0.1425 0.2245 -0.0129 0.0134  -0.0100 22  ASP   B C   
4276 O  O   . ASP   B 22  ? 0.1751 0.1467 0.2288 -0.0099 0.0073  -0.0073 22  ASP   B O   
4277 C  CB  . ASP   B 22  ? 0.1880 0.1554 0.3042 -0.0086 0.0218  -0.0058 22  ASP   B CB  
4278 C  CG  . ASP   B 22  ? 0.1895 0.1749 0.3457 -0.0029 -0.0013 -0.0032 22  ASP   B CG  
4279 O  OD1 . ASP   B 22  ? 0.2024 0.1684 0.3432 -0.0001 -0.0150 -0.0049 22  ASP   B OD1 
4280 O  OD2 . ASP   B 22  ? 0.1967 0.2049 0.3998 0.0086  -0.0214 -0.0156 22  ASP   B OD2 
4285 N  N   . ILE   B 23  ? 0.1723 0.1366 0.2016 -0.0123 0.0070  0.0126  23  ILE   B N   
4286 C  CA  . ILE   B 23  ? 0.1642 0.1366 0.1763 -0.0099 -0.0012 0.0085  23  ILE   B CA  
4287 C  C   . ILE   B 23  ? 0.1562 0.1356 0.1770 -0.0090 -0.0124 0.0003  23  ILE   B C   
4288 O  O   . ILE   B 23  ? 0.1516 0.1399 0.1699 -0.0087 -0.0082 0.0059  23  ILE   B O   
4289 C  CB  . ILE   B 23  ? 0.1634 0.1449 0.1913 -0.0185 -0.0033 0.0112  23  ILE   B CB  
4290 C  CG1 . ILE   B 23  ? 0.1677 0.1579 0.1989 -0.0120 0.0099  0.0216  23  ILE   B CG1 
4291 C  CG2 . ILE   B 23  ? 0.1733 0.1692 0.1998 -0.0167 -0.0036 0.0035  23  ILE   B CG2 
4292 C  CD1 . ILE   B 23  ? 0.1725 0.1679 0.2064 -0.0085 0.0095  0.0111  23  ILE   B CD1 
4304 N  N   . VAL   B 24  ? 0.1603 0.1378 0.1856 -0.0086 -0.0080 0.0020  24  VAL   B N   
4305 C  CA  . VAL   B 24  ? 0.1556 0.1442 0.2060 -0.0051 -0.0199 0.0009  24  VAL   B CA  
4306 C  C   . VAL   B 24  ? 0.1570 0.1488 0.2201 -0.0126 -0.0087 0.0020  24  VAL   B C   
4307 O  O   . VAL   B 24  ? 0.1540 0.1565 0.2263 -0.0190 -0.0035 0.0113  24  VAL   B O   
4308 C  CB  . VAL   B 24  ? 0.1686 0.1623 0.2083 0.0003  -0.0248 0.0007  24  VAL   B CB  
4309 C  CG1 . VAL   B 24  ? 0.1682 0.1730 0.2265 -0.0037 -0.0270 0.0018  24  VAL   B CG1 
4310 C  CG2 . VAL   B 24  ? 0.1806 0.1893 0.2248 0.0080  -0.0197 -0.0067 24  VAL   B CG2 
4320 N  N   . GLU   B 25  ? 0.1815 0.1580 0.2215 -0.0131 -0.0002 0.0028  25  GLU   B N   
4321 C  CA  . GLU   B 25  ? 0.1930 0.1865 0.2425 0.0007  0.0085  -0.0043 25  GLU   B CA  
4322 C  C   . GLU   B 25  ? 0.1820 0.1810 0.2070 -0.0092 0.0116  -0.0026 25  GLU   B C   
4323 O  O   . GLU   B 25  ? 0.1869 0.1926 0.2219 -0.0068 0.0196  0.0032  25  GLU   B O   
4324 C  CB  . GLU   B 25  ? 0.2407 0.2351 0.3127 0.0301  0.0136  -0.0085 25  GLU   B CB  
4325 C  CG  . GLU   B 25  ? 0.2921 0.2990 0.4203 0.0447  0.0106  -0.0122 25  GLU   B CG  
4326 C  CD  . GLU   B 25  ? 0.3326 0.3593 0.5154 0.0482  0.0058  -0.0147 25  GLU   B CD  
4327 O  OE1 . GLU   B 25  ? 0.3650 0.3918 0.5418 0.0539  0.0075  -0.0119 25  GLU   B OE1 
4328 O  OE2 . GLU   B 25  ? 0.3661 0.3835 0.5457 0.0478  0.0016  -0.0217 25  GLU   B OE2 
4335 N  N   . GLU   B 26  ? 0.1799 0.1719 0.1917 -0.0299 0.0017  -0.0018 26  GLU   B N   
4336 C  CA  . GLU   B 26  ? 0.1779 0.1839 0.1923 -0.0367 -0.0104 0.0030  26  GLU   B CA  
4337 C  C   . GLU   B 26  ? 0.1601 0.1833 0.1793 -0.0246 0.0010  0.0120  26  GLU   B C   
4338 O  O   . GLU   B 26  ? 0.1767 0.2046 0.1815 -0.0227 0.0009  0.0186  26  GLU   B O   
4339 C  CB  . GLU   B 26  ? 0.2084 0.2045 0.2153 -0.0476 -0.0109 0.0140  26  GLU   B CB  
4340 C  CG  . GLU   B 26  ? 0.2486 0.2372 0.2816 -0.0505 0.0014  -0.0132 26  GLU   B CG  
4341 C  CD  . GLU   B 26  ? 0.2708 0.2593 0.2853 -0.0668 0.0200  -0.0506 26  GLU   B CD  
4342 O  OE1 . GLU   B 26  ? 0.2895 0.2436 0.2920 -0.0732 0.0643  -0.0550 26  GLU   B OE1 
4343 O  OE2 . GLU   B 26  ? 0.2724 0.2976 0.3386 -0.0615 0.0170  -0.0353 26  GLU   B OE2 
4350 N  N   . ALA   B 27  ? 0.1466 0.1611 0.1790 -0.0224 0.0081  0.0162  27  ALA   B N   
4351 C  CA  . ALA   B 27  ? 0.1472 0.1586 0.1920 -0.0180 -0.0021 0.0292  27  ALA   B CA  
4352 C  C   . ALA   B 27  ? 0.1553 0.1708 0.2169 -0.0138 0.0089  0.0386  27  ALA   B C   
4353 O  O   . ALA   B 27  ? 0.1632 0.1773 0.2255 -0.0027 0.0153  0.0468  27  ALA   B O   
4354 C  CB  . ALA   B 27  ? 0.1595 0.1470 0.1950 -0.0193 -0.0029 0.0221  27  ALA   B CB  
4360 N  N   . LYS   B 28  ? 0.1508 0.1925 0.2542 -0.0205 0.0158  0.0610  28  LYS   B N   
4361 C  CA  . LYS   B 28  ? 0.1685 0.2316 0.2791 -0.0102 0.0494  0.0829  28  LYS   B CA  
4362 C  C   . LYS   B 28  ? 0.1892 0.2507 0.2650 -0.0016 0.0634  0.0730  28  LYS   B C   
4363 O  O   . LYS   B 28  ? 0.2174 0.2569 0.2747 -0.0075 0.0636  0.0670  28  LYS   B O   
4364 C  CB  . LYS   B 28  ? 0.1903 0.2682 0.3428 -0.0003 0.0769  0.1019  28  LYS   B CB  
4365 C  CG  . LYS   B 28  ? 0.2218 0.3143 0.3790 0.0089  0.0921  0.1165  28  LYS   B CG  
4366 C  CD  . LYS   B 28  ? 0.2835 0.3731 0.4397 0.0143  0.1091  0.1158  28  LYS   B CD  
4367 C  CE  . LYS   B 28  ? 0.3419 0.4228 0.4893 0.0178  0.1111  0.1185  28  LYS   B CE  
4368 N  NZ  . LYS   B 28  ? 0.3727 0.4443 0.5120 0.0206  0.1081  0.1215  28  LYS   B NZ  
4382 N  N   . LYS   B 29  ? 0.2039 0.2750 0.2649 0.0214  0.0723  0.0652  29  LYS   B N   
4383 C  CA  . LYS   B 29  ? 0.2488 0.3099 0.2953 0.0227  0.0677  0.0640  29  LYS   B CA  
4384 C  C   . LYS   B 29  ? 0.2415 0.3108 0.2580 0.0224  0.0509  0.0739  29  LYS   B C   
4385 O  O   . LYS   B 29  ? 0.2583 0.3299 0.2673 0.0270  0.0506  0.0759  29  LYS   B O   
4386 C  CB  . LYS   B 29  ? 0.3096 0.3498 0.3865 0.0189  0.0669  0.0515  29  LYS   B CB  
4387 C  CG  . LYS   B 29  ? 0.3615 0.3834 0.4770 0.0145  0.0679  0.0468  29  LYS   B CG  
4388 C  CD  . LYS   B 29  ? 0.4051 0.4065 0.5478 0.0090  0.0746  0.0426  29  LYS   B CD  
4389 C  CE  . LYS   B 29  ? 0.4468 0.4212 0.5958 0.0052  0.0810  0.0386  29  LYS   B CE  
4390 N  NZ  . LYS   B 29  ? 0.4619 0.4283 0.6275 0.0033  0.0832  0.0345  29  LYS   B NZ  
4404 N  N   . VAL   B 30  ? 0.2118 0.2906 0.2400 0.0109  0.0396  0.0739  30  VAL   B N   
4405 C  CA  . VAL   B 30  ? 0.1958 0.2816 0.2711 -0.0061 0.0094  0.0746  30  VAL   B CA  
4406 C  C   . VAL   B 30  ? 0.1753 0.2772 0.2728 -0.0089 0.0147  0.0979  30  VAL   B C   
4407 O  O   . VAL   B 30  ? 0.1915 0.2952 0.2755 0.0024  0.0125  0.1151  30  VAL   B O   
4408 C  CB  . VAL   B 30  ? 0.1993 0.2761 0.2958 -0.0204 -0.0191 0.0696  30  VAL   B CB  
4409 C  CG1 . VAL   B 30  ? 0.2027 0.2794 0.2871 -0.0236 -0.0137 0.0653  30  VAL   B CG1 
4410 C  CG2 . VAL   B 30  ? 0.2097 0.2780 0.3162 -0.0285 -0.0295 0.0562  30  VAL   B CG2 
4420 N  N   . LYS   B 31  ? 0.1634 0.2390 0.3056 -0.0253 0.0087  0.1047  31  LYS   B N   
4421 C  CA  . LYS   B 31  ? 0.1522 0.2302 0.3421 -0.0371 0.0033  0.1068  31  LYS   B CA  
4422 C  C   . LYS   B 31  ? 0.1490 0.1953 0.2954 -0.0320 -0.0206 0.0904  31  LYS   B C   
4423 O  O   . LYS   B 31  ? 0.1609 0.2087 0.3065 -0.0237 -0.0164 0.1050  31  LYS   B O   
4424 C  CB  . LYS   B 31  ? 0.1768 0.2738 0.4022 -0.0371 0.0327  0.1241  31  LYS   B CB  
4425 C  CG  . LYS   B 31  ? 0.2146 0.3231 0.4438 -0.0315 0.0451  0.1196  31  LYS   B CG  
4426 C  CD  . LYS   B 31  ? 0.2617 0.3744 0.4823 -0.0236 0.0426  0.1037  31  LYS   B CD  
4427 C  CE  . LYS   B 31  ? 0.3050 0.4098 0.5188 -0.0205 0.0312  0.0893  31  LYS   B CE  
4428 N  NZ  . LYS   B 31  ? 0.3297 0.4351 0.5266 -0.0153 0.0201  0.0811  31  LYS   B NZ  
4442 N  N   . PRO   B 32  ? 0.1637 0.1563 0.2236 -0.0300 -0.0378 0.0517  32  PRO   B N   
4443 C  CA  . PRO   B 32  ? 0.1714 0.1510 0.1779 -0.0345 -0.0372 0.0321  32  PRO   B CA  
4444 C  C   . PRO   B 32  ? 0.1825 0.1410 0.1758 -0.0369 -0.0472 0.0318  32  PRO   B C   
4445 O  O   . PRO   B 32  ? 0.1944 0.1456 0.2104 -0.0385 -0.0681 0.0269  32  PRO   B O   
4446 C  CB  . PRO   B 32  ? 0.1849 0.1483 0.1715 -0.0371 -0.0312 0.0190  32  PRO   B CB  
4447 C  CG  . PRO   B 32  ? 0.2016 0.1392 0.1870 -0.0318 -0.0457 0.0225  32  PRO   B CG  
4448 C  CD  . PRO   B 32  ? 0.1892 0.1432 0.2101 -0.0282 -0.0540 0.0285  32  PRO   B CD  
4456 N  N   . THR   B 33  ? 0.1842 0.1332 0.1803 -0.0316 -0.0478 0.0215  33  THR   B N   
4457 C  CA  . THR   B 33  ? 0.1879 0.1413 0.1775 -0.0346 -0.0432 0.0295  33  THR   B CA  
4458 C  C   . THR   B 33  ? 0.1888 0.1291 0.1679 -0.0337 -0.0458 0.0211  33  THR   B C   
4459 O  O   . THR   B 33  ? 0.2108 0.1319 0.1856 -0.0426 -0.0537 0.0192  33  THR   B O   
4460 C  CB  . THR   B 33  ? 0.1977 0.1490 0.1826 -0.0179 -0.0512 0.0266  33  THR   B CB  
4461 O  OG1 . THR   B 33  ? 0.1895 0.1545 0.1881 -0.0189 -0.0503 0.0297  33  THR   B OG1 
4462 C  CG2 . THR   B 33  ? 0.2213 0.1542 0.1928 -0.0080 -0.0492 0.0306  33  THR   B CG2 
4470 N  N   . VAL   B 34  ? 0.1797 0.1272 0.1550 -0.0322 -0.0357 0.0150  34  VAL   B N   
4471 C  CA  . VAL   B 34  ? 0.1639 0.1268 0.1461 -0.0250 -0.0259 0.0046  34  VAL   B CA  
4472 C  C   . VAL   B 34  ? 0.1484 0.1208 0.1389 -0.0249 -0.0135 0.0053  34  VAL   B C   
4473 O  O   . VAL   B 34  ? 0.1646 0.1224 0.1453 -0.0235 -0.0294 0.0025  34  VAL   B O   
4474 C  CB  . VAL   B 34  ? 0.1671 0.1322 0.1802 -0.0119 -0.0283 0.0020  34  VAL   B CB  
4475 C  CG1 . VAL   B 34  ? 0.1630 0.1457 0.1819 -0.0076 -0.0165 -0.0014 34  VAL   B CG1 
4476 C  CG2 . VAL   B 34  ? 0.1729 0.1359 0.2071 -0.0125 -0.0304 0.0071  34  VAL   B CG2 
4486 N  N   . VAL   B 35  ? 0.1389 0.1193 0.1359 -0.0249 -0.0116 0.0052  35  VAL   B N   
4487 C  CA  . VAL   B 35  ? 0.1353 0.1178 0.1307 -0.0205 -0.0093 0.0050  35  VAL   B CA  
4488 C  C   . VAL   B 35  ? 0.1271 0.1128 0.1284 -0.0155 -0.0101 0.0058  35  VAL   B C   
4489 O  O   . VAL   B 35  ? 0.1339 0.1169 0.1407 -0.0171 -0.0028 -0.0007 35  VAL   B O   
4490 C  CB  . VAL   B 35  ? 0.1350 0.1368 0.1372 -0.0219 0.0009  0.0020  35  VAL   B CB  
4491 C  CG1 . VAL   B 35  ? 0.1268 0.1481 0.1611 -0.0213 0.0031  0.0050  35  VAL   B CG1 
4492 C  CG2 . VAL   B 35  ? 0.1417 0.1356 0.1532 -0.0127 -0.0003 -0.0012 35  VAL   B CG2 
4502 N  N   . VAL   B 36  ? 0.1292 0.1159 0.1243 -0.0151 -0.0125 0.0056  36  VAL   B N   
4503 C  CA  . VAL   B 36  ? 0.1281 0.1110 0.1239 -0.0135 -0.0032 0.0010  36  VAL   B CA  
4504 C  C   . VAL   B 36  ? 0.1201 0.1128 0.1199 -0.0124 -0.0025 0.0038  36  VAL   B C   
4505 O  O   . VAL   B 36  ? 0.1287 0.1244 0.1453 -0.0098 0.0000  -0.0036 36  VAL   B O   
4506 C  CB  . VAL   B 36  ? 0.1241 0.1190 0.1381 -0.0139 -0.0015 -0.0015 36  VAL   B CB  
4507 C  CG1 . VAL   B 36  ? 0.1246 0.1266 0.1449 -0.0169 0.0007  0.0016  36  VAL   B CG1 
4508 C  CG2 . VAL   B 36  ? 0.1290 0.1248 0.1416 -0.0130 -0.0097 0.0022  36  VAL   B CG2 
4518 N  N   . ASN   B 37  ? 0.1222 0.1190 0.1268 -0.0004 -0.0014 0.0049  37  ASN   B N   
4519 C  CA  . ASN   B 37  ? 0.1214 0.1216 0.1388 0.0012  -0.0098 0.0063  37  ASN   B CA  
4520 C  C   . ASN   B 37  ? 0.1205 0.1237 0.1307 0.0017  -0.0105 0.0019  37  ASN   B C   
4521 O  O   . ASN   B 37  ? 0.1300 0.1306 0.1409 -0.0004 -0.0017 0.0069  37  ASN   B O   
4522 C  CB  . ASN   B 37  ? 0.1256 0.1244 0.1305 -0.0008 -0.0087 0.0039  37  ASN   B CB  
4523 C  CG  . ASN   B 37  ? 0.1297 0.1251 0.1347 -0.0013 -0.0076 0.0033  37  ASN   B CG  
4524 O  OD1 . ASN   B 37  ? 0.1401 0.1306 0.1458 0.0067  -0.0122 -0.0007 37  ASN   B OD1 
4525 N  ND2 . ASN   B 37  ? 0.1332 0.1232 0.1418 0.0004  -0.0168 0.0055  37  ASN   B ND2 
4532 N  N   . ALA   B 38  ? 0.1349 0.1215 0.1266 0.0059  0.0029  0.0040  38  ALA   B N   
4533 C  CA  . ALA   B 38  ? 0.1447 0.1257 0.1342 -0.0020 -0.0025 0.0108  38  ALA   B CA  
4534 C  C   . ALA   B 38  ? 0.1410 0.1209 0.1389 -0.0035 0.0036  0.0120  38  ALA   B C   
4535 O  O   . ALA   B 38  ? 0.1486 0.1326 0.1471 0.0057  -0.0019 0.0069  38  ALA   B O   
4536 C  CB  . ALA   B 38  ? 0.1680 0.1290 0.1523 -0.0078 0.0124  0.0065  38  ALA   B CB  
4542 N  N   . ALA   B 39  ? 0.1369 0.1234 0.1406 0.0058  -0.0055 0.0032  39  ALA   B N   
4543 C  CA  . ALA   B 39  ? 0.1455 0.1295 0.1406 0.0001  -0.0037 0.0065  39  ALA   B CA  
4544 C  C   . ALA   B 39  ? 0.1509 0.1374 0.1256 0.0080  -0.0025 0.0014  39  ALA   B C   
4545 O  O   . ALA   B 39  ? 0.1510 0.1446 0.1522 -0.0015 0.0031  0.0070  39  ALA   B O   
4546 C  CB  . ALA   B 39  ? 0.1459 0.1329 0.1552 -0.0035 0.0000  -0.0001 39  ALA   B CB  
4552 N  N   . ASN   B 40  ? 0.1545 0.1565 0.1303 -0.0019 0.0028  -0.0046 40  ASN   B N   
4553 C  CA  . ASN   B 40  ? 0.1623 0.1636 0.1350 0.0009  -0.0059 -0.0043 40  ASN   B CA  
4554 C  C   . ASN   B 40  ? 0.1636 0.1677 0.1244 0.0091  -0.0083 0.0024  40  ASN   B C   
4555 O  O   . ASN   B 40  ? 0.1595 0.1601 0.1332 0.0109  -0.0077 0.0035  40  ASN   B O   
4556 C  CB  . ASN   B 40  ? 0.1755 0.1655 0.1653 0.0082  -0.0122 0.0112  40  ASN   B CB  
4557 C  CG  . ASN   B 40  ? 0.1746 0.1708 0.2007 0.0025  -0.0264 0.0132  40  ASN   B CG  
4558 O  OD1 . ASN   B 40  ? 0.1718 0.1674 0.2717 0.0016  -0.0358 0.0199  40  ASN   B OD1 
4559 N  ND2 . ASN   B 40  ? 0.1753 0.1705 0.1958 0.0011  -0.0145 0.0060  40  ASN   B ND2 
4566 N  N   . VAL   B 41  ? 0.1710 0.1728 0.1247 0.0104  0.0024  -0.0002 41  VAL   B N   
4567 C  CA  . VAL   B 41  ? 0.1812 0.1849 0.1338 0.0080  0.0055  -0.0114 41  VAL   B CA  
4568 C  C   . VAL   B 41  ? 0.1780 0.1801 0.1354 0.0155  -0.0014 -0.0147 41  VAL   B C   
4569 O  O   . VAL   B 41  ? 0.1799 0.1746 0.1407 0.0148  -0.0076 -0.0147 41  VAL   B O   
4570 C  CB  . VAL   B 41  ? 0.1941 0.2000 0.1521 -0.0053 0.0282  -0.0193 41  VAL   B CB  
4571 C  CG1 . VAL   B 41  ? 0.1907 0.2079 0.1808 -0.0088 0.0340  -0.0150 41  VAL   B CG1 
4572 C  CG2 . VAL   B 41  ? 0.2074 0.2198 0.1614 -0.0151 0.0272  -0.0255 41  VAL   B CG2 
4582 N  N   . TYR   B 42  ? 0.1788 0.1833 0.1406 0.0169  -0.0161 -0.0033 42  TYR   B N   
4583 C  CA  . TYR   B 42  ? 0.1836 0.1911 0.1495 0.0153  -0.0228 -0.0126 42  TYR   B CA  
4584 C  C   . TYR   B 42  ? 0.1701 0.1686 0.1536 0.0175  -0.0198 -0.0102 42  TYR   B C   
4585 O  O   . TYR   B 42  ? 0.1690 0.1769 0.1795 0.0126  -0.0184 -0.0167 42  TYR   B O   
4586 C  CB  . TYR   B 42  ? 0.2082 0.2182 0.1648 0.0078  -0.0277 0.0028  42  TYR   B CB  
4587 C  CG  . TYR   B 42  ? 0.2098 0.2372 0.1649 -0.0028 -0.0270 0.0129  42  TYR   B CG  
4588 C  CD1 . TYR   B 42  ? 0.2060 0.2370 0.1358 -0.0088 -0.0122 0.0088  42  TYR   B CD1 
4589 C  CD2 . TYR   B 42  ? 0.2257 0.2534 0.2110 -0.0038 -0.0067 0.0221  42  TYR   B CD2 
4590 C  CE1 . TYR   B 42  ? 0.2209 0.2543 0.1435 -0.0013 0.0003  0.0143  42  TYR   B CE1 
4591 C  CE2 . TYR   B 42  ? 0.2295 0.2650 0.2026 0.0030  0.0145  0.0353  42  TYR   B CE2 
4592 C  CZ  . TYR   B 42  ? 0.2391 0.2783 0.1867 0.0178  0.0209  0.0241  42  TYR   B CZ  
4593 O  OH  . TYR   B 42  ? 0.2704 0.3021 0.2324 0.0400  0.0274  0.0327  42  TYR   B OH  
4603 N  N   . LEU   B 43  ? 0.1617 0.1491 0.1405 0.0099  -0.0166 -0.0107 43  LEU   B N   
4604 C  CA  . LEU   B 43  ? 0.1624 0.1516 0.1309 0.0065  -0.0159 -0.0041 43  LEU   B CA  
4605 C  C   . LEU   B 43  ? 0.1659 0.1539 0.1368 0.0049  -0.0094 -0.0003 43  LEU   B C   
4606 O  O   . LEU   B 43  ? 0.1577 0.1561 0.1623 0.0058  -0.0162 0.0061  43  LEU   B O   
4607 C  CB  . LEU   B 43  ? 0.1582 0.1466 0.1499 -0.0007 -0.0197 -0.0111 43  LEU   B CB  
4608 C  CG  . LEU   B 43  ? 0.1625 0.1400 0.1536 0.0037  -0.0231 -0.0083 43  LEU   B CG  
4609 C  CD1 . LEU   B 43  ? 0.1675 0.1500 0.1925 0.0021  -0.0391 -0.0102 43  LEU   B CD1 
4610 C  CD2 . LEU   B 43  ? 0.1588 0.1461 0.1728 -0.0042 -0.0256 -0.0083 43  LEU   B CD2 
4622 N  N   . LYS   B 44  ? 0.1623 0.1510 0.1438 0.0089  -0.0107 -0.0066 44  LYS   B N   
4623 C  CA  . LYS   B 44  ? 0.1732 0.1635 0.1472 0.0091  -0.0102 0.0067  44  LYS   B CA  
4624 C  C   . LYS   B 44  ? 0.1630 0.1589 0.1406 0.0115  -0.0089 0.0004  44  LYS   B C   
4625 O  O   . LYS   B 44  ? 0.1803 0.1562 0.1732 -0.0001 -0.0078 0.0016  44  LYS   B O   
4626 C  CB  . LYS   B 44  ? 0.1983 0.1856 0.1672 0.0137  -0.0224 0.0038  44  LYS   B CB  
4627 C  CG  . LYS   B 44  ? 0.2371 0.2128 0.1973 0.0137  -0.0525 0.0069  44  LYS   B CG  
4628 C  CD  . LYS   B 44  ? 0.2726 0.2332 0.2521 0.0024  -0.0665 0.0039  44  LYS   B CD  
4629 C  CE  . LYS   B 44  ? 0.3050 0.2564 0.2998 -0.0045 -0.0711 0.0198  44  LYS   B CE  
4630 N  NZ  . LYS   B 44  ? 0.3187 0.2651 0.3278 -0.0016 -0.0808 0.0376  44  LYS   B NZ  
4644 N  N   . HIS   B 45  ? 0.1555 0.1568 0.1378 0.0082  -0.0107 0.0078  45  HIS   B N   
4645 C  CA  . HIS   B 45  ? 0.1569 0.1521 0.1397 0.0100  -0.0062 -0.0024 45  HIS   B CA  
4646 C  C   . HIS   B 45  ? 0.1772 0.1666 0.1869 0.0175  -0.0126 -0.0083 45  HIS   B C   
4647 O  O   . HIS   B 45  ? 0.1873 0.1980 0.2362 0.0406  0.0036  -0.0004 45  HIS   B O   
4648 C  CB  . HIS   B 45  ? 0.1508 0.1547 0.1442 0.0034  -0.0079 -0.0098 45  HIS   B CB  
4649 C  CG  . HIS   B 45  ? 0.1505 0.1515 0.1479 -0.0014 -0.0068 -0.0043 45  HIS   B CG  
4650 N  ND1 . HIS   B 45  ? 0.1522 0.1472 0.1558 -0.0001 -0.0121 -0.0070 45  HIS   B ND1 
4651 C  CD2 . HIS   B 45  ? 0.1615 0.1543 0.1623 -0.0109 -0.0090 -0.0032 45  HIS   B CD2 
4652 C  CE1 . HIS   B 45  ? 0.1645 0.1390 0.1396 -0.0040 -0.0240 -0.0074 45  HIS   B CE1 
4653 N  NE2 . HIS   B 45  ? 0.1673 0.1441 0.1495 -0.0004 -0.0155 -0.0088 45  HIS   B NE2 
4661 N  N   . GLY   B 46  ? 0.1943 0.1635 0.2075 0.0155  -0.0285 0.0043  46  GLY   B N   
4662 C  CA  . GLY   B 46  ? 0.2104 0.1801 0.2385 0.0136  -0.0457 0.0104  46  GLY   B CA  
4663 C  C   . GLY   B 46  ? 0.2038 0.1984 0.2829 0.0246  -0.0401 0.0111  46  GLY   B C   
4664 O  O   . GLY   B 46  ? 0.2089 0.2245 0.3702 0.0274  -0.0210 -0.0186 46  GLY   B O   
4668 N  N   . GLY   B 47  ? 0.1990 0.2046 0.2613 0.0101  -0.0191 0.0005  47  GLY   B N   
4669 C  CA  . GLY   B 47  ? 0.1875 0.1764 0.2247 0.0011  -0.0193 -0.0025 47  GLY   B CA  
4670 C  C   . GLY   B 47  ? 0.1681 0.1536 0.1851 0.0021  -0.0052 0.0019  47  GLY   B C   
4671 O  O   . GLY   B 47  ? 0.1787 0.1418 0.1925 0.0016  -0.0055 0.0115  47  GLY   B O   
4675 N  N   . GLY   B 48  ? 0.1532 0.1482 0.1826 -0.0023 -0.0103 0.0137  48  GLY   B N   
4676 C  CA  . GLY   B 48  ? 0.1477 0.1426 0.1850 -0.0046 -0.0034 0.0096  48  GLY   B CA  
4677 C  C   . GLY   B 48  ? 0.1452 0.1394 0.1796 -0.0008 0.0043  0.0118  48  GLY   B C   
4678 O  O   . GLY   B 48  ? 0.1423 0.1437 0.2007 0.0015  -0.0030 0.0016  48  GLY   B O   
4682 N  N   . VAL   B 49  ? 0.1472 0.1440 0.1615 0.0099  0.0020  0.0085  49  VAL   B N   
4683 C  CA  . VAL   B 49  ? 0.1499 0.1541 0.1510 0.0069  -0.0096 -0.0011 49  VAL   B CA  
4684 C  C   . VAL   B 49  ? 0.1423 0.1466 0.1436 0.0090  -0.0064 0.0086  49  VAL   B C   
4685 O  O   . VAL   B 49  ? 0.1483 0.1433 0.1554 0.0029  0.0007  0.0070  49  VAL   B O   
4686 C  CB  . VAL   B 49  ? 0.1512 0.1687 0.1790 0.0000  -0.0244 -0.0006 49  VAL   B CB  
4687 C  CG1 . VAL   B 49  ? 0.1521 0.1738 0.1695 0.0077  -0.0317 0.0050  49  VAL   B CG1 
4688 C  CG2 . VAL   B 49  ? 0.1637 0.1814 0.2087 -0.0091 -0.0368 -0.0052 49  VAL   B CG2 
4698 N  N   . ALA   B 50  ? 0.1348 0.1364 0.1435 0.0029  -0.0052 0.0064  50  ALA   B N   
4699 C  CA  . ALA   B 50  ? 0.1364 0.1297 0.1432 0.0054  -0.0083 0.0071  50  ALA   B CA  
4700 C  C   . ALA   B 50  ? 0.1407 0.1356 0.1446 0.0063  -0.0009 0.0037  50  ALA   B C   
4701 O  O   . ALA   B 50  ? 0.1435 0.1349 0.1496 0.0042  0.0002  -0.0002 50  ALA   B O   
4702 C  CB  . ALA   B 50  ? 0.1442 0.1300 0.1540 0.0005  -0.0025 0.0075  50  ALA   B CB  
4708 N  N   . GLY   B 51  ? 0.1389 0.1445 0.1658 0.0086  -0.0105 0.0066  51  GLY   B N   
4709 C  CA  . GLY   B 51  ? 0.1428 0.1495 0.1774 0.0188  -0.0122 0.0070  51  GLY   B CA  
4710 C  C   . GLY   B 51  ? 0.1434 0.1421 0.1695 0.0187  -0.0073 0.0072  51  GLY   B C   
4711 O  O   . GLY   B 51  ? 0.1435 0.1541 0.1855 0.0079  -0.0111 -0.0001 51  GLY   B O   
4715 N  N   . ALA   B 52  ? 0.1434 0.1398 0.1680 0.0153  -0.0048 0.0072  52  ALA   B N   
4716 C  CA  . ALA   B 52  ? 0.1523 0.1458 0.1733 0.0162  0.0002  0.0022  52  ALA   B CA  
4717 C  C   . ALA   B 52  ? 0.1376 0.1414 0.1540 0.0067  0.0017  0.0046  52  ALA   B C   
4718 O  O   . ALA   B 52  ? 0.1385 0.1466 0.1780 0.0088  0.0052  0.0007  52  ALA   B O   
4719 C  CB  . ALA   B 52  ? 0.1694 0.1494 0.1746 0.0068  0.0103  0.0013  52  ALA   B CB  
4725 N  N   . LEU   B 53  ? 0.1334 0.1395 0.1496 0.0128  0.0025  0.0037  53  LEU   B N   
4726 C  CA  . LEU   B 53  ? 0.1347 0.1475 0.1368 0.0105  -0.0057 0.0026  53  LEU   B CA  
4727 C  C   . LEU   B 53  ? 0.1386 0.1434 0.1398 0.0096  0.0065  0.0039  53  LEU   B C   
4728 O  O   . LEU   B 53  ? 0.1466 0.1488 0.1567 0.0005  0.0061  0.0149  53  LEU   B O   
4729 C  CB  . LEU   B 53  ? 0.1355 0.1554 0.1588 0.0055  -0.0043 0.0119  53  LEU   B CB  
4730 C  CG  . LEU   B 53  ? 0.1351 0.1714 0.1631 0.0044  -0.0034 0.0147  53  LEU   B CG  
4731 C  CD1 . LEU   B 53  ? 0.1429 0.1920 0.1871 0.0112  -0.0014 -0.0025 53  LEU   B CD1 
4732 C  CD2 . LEU   B 53  ? 0.1515 0.1985 0.1940 -0.0104 -0.0148 -0.0127 53  LEU   B CD2 
4744 N  N   . ASN   B 54  ? 0.1391 0.1318 0.1400 0.0064  -0.0004 0.0047  54  ASN   B N   
4745 C  CA  . ASN   B 54  ? 0.1455 0.1463 0.1602 0.0026  -0.0058 -0.0002 54  ASN   B CA  
4746 C  C   . ASN   B 54  ? 0.1410 0.1494 0.1750 0.0032  0.0042  0.0021  54  ASN   B C   
4747 O  O   . ASN   B 54  ? 0.1364 0.1516 0.1894 -0.0058 0.0034  0.0060  54  ASN   B O   
4748 C  CB  . ASN   B 54  ? 0.1465 0.1537 0.1695 0.0048  0.0020  0.0001  54  ASN   B CB  
4749 C  CG  . ASN   B 54  ? 0.1445 0.1634 0.1727 0.0059  -0.0085 0.0039  54  ASN   B CG  
4750 O  OD1 . ASN   B 54  ? 0.1423 0.1604 0.1761 0.0006  -0.0122 -0.0091 54  ASN   B OD1 
4751 N  ND2 . ASN   B 54  ? 0.1586 0.1848 0.2012 -0.0014 -0.0315 0.0140  54  ASN   B ND2 
4758 N  N   . LYS   B 55  ? 0.1375 0.1533 0.1884 0.0087  -0.0004 0.0020  55  LYS   B N   
4759 C  CA  . LYS   B 55  ? 0.1453 0.1649 0.1984 0.0159  -0.0036 0.0049  55  LYS   B CA  
4760 C  C   . LYS   B 55  ? 0.1420 0.1582 0.2038 0.0146  0.0046  -0.0023 55  LYS   B C   
4761 O  O   . LYS   B 55  ? 0.1327 0.1733 0.2225 0.0089  0.0101  0.0012  55  LYS   B O   
4762 C  CB  . LYS   B 55  ? 0.1560 0.1792 0.2444 0.0313  0.0059  0.0167  55  LYS   B CB  
4763 C  CG  . LYS   B 55  ? 0.1976 0.2123 0.3274 0.0394  0.0259  0.0278  55  LYS   B CG  
4764 C  CD  . LYS   B 55  ? 0.2347 0.2368 0.4017 0.0501  0.0433  0.0422  55  LYS   B CD  
4765 C  CE  . LYS   B 55  ? 0.2619 0.2649 0.4726 0.0495  0.0562  0.0499  55  LYS   B CE  
4766 N  NZ  . LYS   B 55  ? 0.2704 0.2814 0.5040 0.0460  0.0444  0.0613  55  LYS   B NZ  
4780 N  N   . ALA   B 56  ? 0.1380 0.1654 0.1806 0.0069  0.0042  -0.0079 56  ALA   B N   
4781 C  CA  . ALA   B 56  ? 0.1525 0.1810 0.1732 0.0012  0.0056  -0.0082 56  ALA   B CA  
4782 C  C   . ALA   B 56  ? 0.1522 0.1776 0.1811 -0.0002 0.0153  0.0014  56  ALA   B C   
4783 O  O   . ALA   B 56  ? 0.1649 0.1932 0.2013 0.0065  0.0308  0.0026  56  ALA   B O   
4784 C  CB  . ALA   B 56  ? 0.1641 0.1998 0.1789 -0.0100 0.0040  -0.0077 56  ALA   B CB  
4790 N  N   . THR   B 57  ? 0.1483 0.1667 0.1889 0.0005  0.0141  0.0086  57  THR   B N   
4791 C  CA  . THR   B 57  ? 0.1486 0.1675 0.1945 -0.0014 0.0184  0.0131  57  THR   B CA  
4792 C  C   . THR   B 57  ? 0.1531 0.1786 0.2204 0.0004  0.0196  0.0029  57  THR   B C   
4793 O  O   . THR   B 57  ? 0.1559 0.1785 0.2271 -0.0180 0.0133  0.0045  57  THR   B O   
4794 C  CB  . THR   B 57  ? 0.1567 0.1534 0.1684 -0.0006 0.0185  0.0139  57  THR   B CB  
4795 O  OG1 . THR   B 57  ? 0.1551 0.1467 0.1829 -0.0022 0.0172  0.0003  57  THR   B OG1 
4796 C  CG2 . THR   B 57  ? 0.1505 0.1614 0.1658 -0.0027 0.0142  0.0059  57  THR   B CG2 
4804 N  N   . ASN   B 58  ? 0.1344 0.2000 0.2353 -0.0118 0.0051  -0.0083 58  ASN   B N   
4805 C  CA  . ASN   B 58  ? 0.1642 0.2466 0.2719 -0.0284 0.0337  0.0018  58  ASN   B CA  
4806 C  C   . ASN   B 58  ? 0.1415 0.2182 0.2212 -0.0196 -0.0003 -0.0001 58  ASN   B C   
4807 O  O   . ASN   B 58  ? 0.1484 0.2254 0.2398 -0.0207 0.0076  -0.0117 58  ASN   B O   
4808 C  CB  . ASN   B 58  ? 0.2809 0.3438 0.4115 -0.0409 0.0686  0.0178  58  ASN   B CB  
4809 C  CG  . ASN   B 58  ? 0.4182 0.4449 0.5660 -0.0444 0.0840  0.0359  58  ASN   B CG  
4810 O  OD1 . ASN   B 58  ? 0.4580 0.4694 0.6162 -0.0471 0.0894  0.0406  58  ASN   B OD1 
4811 N  ND2 . ASN   B 58  ? 0.4699 0.4807 0.6155 -0.0444 0.0900  0.0402  58  ASN   B ND2 
4818 N  N   . ASN   B 59  ? 0.1426 0.2021 0.2039 -0.0109 -0.0036 0.0071  59  ASN   B N   
4819 C  CA  . ASN   B 59  ? 0.1424 0.1983 0.2038 -0.0139 -0.0114 0.0150  59  ASN   B CA  
4820 C  C   . ASN   B 59  ? 0.1406 0.1889 0.1953 -0.0162 -0.0087 -0.0007 59  ASN   B C   
4821 O  O   . ASN   B 59  ? 0.1444 0.1877 0.1907 -0.0132 -0.0124 -0.0055 59  ASN   B O   
4822 C  CB  . ASN   B 59  ? 0.1525 0.2156 0.2186 -0.0078 -0.0258 0.0131  59  ASN   B CB  
4823 C  CG  . ASN   B 59  ? 0.1679 0.2289 0.2384 -0.0021 -0.0420 0.0087  59  ASN   B CG  
4824 O  OD1 . ASN   B 59  ? 0.1723 0.2361 0.2375 -0.0006 -0.0233 0.0231  59  ASN   B OD1 
4825 N  ND2 . ASN   B 59  ? 0.1831 0.2391 0.2511 -0.0099 -0.0434 0.0068  59  ASN   B ND2 
4832 N  N   . ALA   B 60  ? 0.1406 0.1769 0.1923 -0.0134 -0.0001 -0.0001 60  ALA   B N   
4833 C  CA  . ALA   B 60  ? 0.1521 0.1683 0.2027 -0.0179 -0.0017 0.0034  60  ALA   B CA  
4834 C  C   . ALA   B 60  ? 0.1498 0.1567 0.1833 -0.0137 -0.0053 0.0009  60  ALA   B C   
4835 O  O   . ALA   B 60  ? 0.1524 0.1543 0.1953 -0.0184 0.0048  -0.0068 60  ALA   B O   
4836 C  CB  . ALA   B 60  ? 0.1633 0.1643 0.2217 -0.0144 0.0045  0.0105  60  ALA   B CB  
4842 N  N   . MET   B 61  ? 0.1436 0.1466 0.1792 -0.0103 -0.0015 0.0025  61  MET   B N   
4843 C  CA  . MET   B 61  ? 0.1388 0.1430 0.1744 -0.0088 -0.0046 0.0051  61  MET   B CA  
4844 C  C   . MET   B 61  ? 0.1465 0.1441 0.1662 -0.0117 -0.0052 0.0053  61  MET   B C   
4845 O  O   . MET   B 61  ? 0.1478 0.1434 0.1520 -0.0014 -0.0053 -0.0103 61  MET   B O   
4846 C  CB  . MET   B 61  ? 0.1371 0.1430 0.1750 -0.0039 -0.0058 -0.0009 61  MET   B CB  
4847 C  CG  . MET   B 61  ? 0.1358 0.1427 0.1616 -0.0022 -0.0040 -0.0041 61  MET   B CG  
4848 S  SD  . MET   B 61  ? 0.1349 0.1439 0.1855 -0.0038 -0.0056 -0.0072 61  MET   B SD  
4849 C  CE  . MET   B 61  ? 0.1409 0.1582 0.2043 0.0072  -0.0006 -0.0163 61  MET   B CE  
4859 N  N   . GLN   B 62  ? 0.1420 0.1517 0.1668 -0.0051 -0.0166 -0.0001 62  GLN   B N   
4860 C  CA  . GLN   B 62  ? 0.1453 0.1545 0.1744 -0.0015 -0.0151 -0.0032 62  GLN   B CA  
4861 C  C   . GLN   B 62  ? 0.1477 0.1605 0.1751 -0.0031 -0.0209 -0.0082 62  GLN   B C   
4862 O  O   . GLN   B 62  ? 0.1581 0.1618 0.1753 -0.0041 -0.0253 -0.0132 62  GLN   B O   
4863 C  CB  . GLN   B 62  ? 0.1504 0.1583 0.1733 0.0028  -0.0137 0.0037  62  GLN   B CB  
4864 C  CG  . GLN   B 62  ? 0.1547 0.1664 0.1737 0.0044  -0.0207 -0.0012 62  GLN   B CG  
4865 C  CD  . GLN   B 62  ? 0.1535 0.1621 0.1567 0.0031  -0.0259 0.0076  62  GLN   B CD  
4866 O  OE1 . GLN   B 62  ? 0.1543 0.1588 0.1776 0.0023  -0.0243 -0.0079 62  GLN   B OE1 
4867 N  NE2 . GLN   B 62  ? 0.1530 0.1634 0.1732 -0.0037 -0.0189 -0.0055 62  GLN   B NE2 
4876 N  N   . VAL   B 63  ? 0.1477 0.1652 0.1910 -0.0081 -0.0244 -0.0123 63  VAL   B N   
4877 C  CA  . VAL   B 63  ? 0.1599 0.1600 0.2141 -0.0151 -0.0285 -0.0128 63  VAL   B CA  
4878 C  C   . VAL   B 63  ? 0.1596 0.1498 0.1994 -0.0206 -0.0325 -0.0183 63  VAL   B C   
4879 O  O   . VAL   B 63  ? 0.1672 0.1534 0.2088 -0.0152 -0.0431 -0.0169 63  VAL   B O   
4880 C  CB  . VAL   B 63  ? 0.1584 0.1769 0.2537 -0.0202 -0.0240 -0.0125 63  VAL   B CB  
4881 C  CG1 . VAL   B 63  ? 0.1680 0.1799 0.2644 -0.0330 -0.0170 -0.0167 63  VAL   B CG1 
4882 C  CG2 . VAL   B 63  ? 0.1533 0.1935 0.2686 -0.0161 -0.0287 -0.0127 63  VAL   B CG2 
4892 N  N   . GLU   B 64  ? 0.1586 0.1421 0.1932 -0.0125 -0.0178 -0.0130 64  GLU   B N   
4893 C  CA  . GLU   B 64  ? 0.1625 0.1390 0.1737 -0.0100 -0.0236 -0.0078 64  GLU   B CA  
4894 C  C   . GLU   B 64  ? 0.1537 0.1404 0.1666 -0.0030 -0.0262 -0.0133 64  GLU   B C   
4895 O  O   . GLU   B 64  ? 0.1616 0.1494 0.1758 -0.0084 -0.0247 -0.0182 64  GLU   B O   
4896 C  CB  . GLU   B 64  ? 0.1619 0.1496 0.1722 -0.0157 -0.0206 -0.0044 64  GLU   B CB  
4897 C  CG  . GLU   B 64  ? 0.1639 0.1541 0.1743 -0.0248 -0.0266 -0.0152 64  GLU   B CG  
4898 C  CD  . GLU   B 64  ? 0.1675 0.1693 0.1812 -0.0309 -0.0236 -0.0089 64  GLU   B CD  
4899 O  OE1 . GLU   B 64  ? 0.1667 0.1844 0.1949 -0.0329 -0.0202 -0.0278 64  GLU   B OE1 
4900 O  OE2 . GLU   B 64  ? 0.1784 0.1785 0.1831 -0.0341 -0.0394 -0.0093 64  GLU   B OE2 
4907 N  N   . SER   B 65  ? 0.1500 0.1363 0.1598 -0.0089 -0.0165 -0.0155 65  SER   B N   
4908 C  CA  . SER   B 65  ? 0.1532 0.1352 0.1701 -0.0008 -0.0158 -0.0128 65  SER   B CA  
4909 C  C   . SER   B 65  ? 0.1550 0.1422 0.1652 -0.0029 -0.0215 -0.0165 65  SER   B C   
4910 O  O   . SER   B 65  ? 0.1610 0.1520 0.1647 -0.0056 -0.0168 -0.0280 65  SER   B O   
4911 C  CB  . SER   B 65  ? 0.1549 0.1399 0.1701 -0.0117 -0.0114 -0.0117 65  SER   B CB  
4912 O  OG  . SER   B 65  ? 0.1574 0.1395 0.1709 -0.0098 -0.0118 -0.0189 65  SER   B OG  
4918 N  N   . ASP   B 66  ? 0.1658 0.1530 0.1670 0.0003  -0.0220 -0.0165 66  ASP   B N   
4919 C  CA  . ASP   B 66  ? 0.1735 0.1595 0.1553 0.0027  -0.0279 -0.0123 66  ASP   B CA  
4920 C  C   . ASP   B 66  ? 0.1774 0.1629 0.1504 -0.0014 -0.0222 -0.0136 66  ASP   B C   
4921 O  O   . ASP   B 66  ? 0.1830 0.1663 0.1636 0.0031  -0.0257 -0.0173 66  ASP   B O   
4922 C  CB  . ASP   B 66  ? 0.1872 0.1763 0.1738 0.0096  -0.0416 -0.0123 66  ASP   B CB  
4923 C  CG  . ASP   B 66  ? 0.2158 0.1940 0.2065 0.0209  -0.0613 0.0002  66  ASP   B CG  
4924 O  OD1 . ASP   B 66  ? 0.2396 0.1863 0.2153 0.0136  -0.0602 0.0032  66  ASP   B OD1 
4925 O  OD2 . ASP   B 66  ? 0.2308 0.2167 0.2665 0.0397  -0.0531 0.0004  66  ASP   B OD2 
4930 N  N   . ASP   B 67  ? 0.1730 0.1557 0.1508 -0.0051 -0.0259 -0.0189 67  ASP   B N   
4931 C  CA  . ASP   B 67  ? 0.1874 0.1526 0.1766 -0.0080 -0.0271 -0.0121 67  ASP   B CA  
4932 C  C   . ASP   B 67  ? 0.1795 0.1512 0.1848 -0.0003 -0.0260 -0.0196 67  ASP   B C   
4933 O  O   . ASP   B 67  ? 0.1848 0.1567 0.1941 0.0009  -0.0158 -0.0238 67  ASP   B O   
4934 C  CB  . ASP   B 67  ? 0.2136 0.1576 0.1913 -0.0191 -0.0383 -0.0074 67  ASP   B CB  
4935 C  CG  . ASP   B 67  ? 0.2532 0.1684 0.1965 -0.0125 -0.0669 -0.0093 67  ASP   B CG  
4936 O  OD1 . ASP   B 67  ? 0.2745 0.1732 0.1999 -0.0168 -0.0617 -0.0045 67  ASP   B OD1 
4937 O  OD2 . ASP   B 67  ? 0.2675 0.1749 0.2190 -0.0007 -0.0774 -0.0044 67  ASP   B OD2 
4942 N  N   . TYR   B 68  ? 0.1692 0.1518 0.1752 -0.0014 -0.0336 -0.0262 68  TYR   B N   
4943 C  CA  . TYR   B 68  ? 0.1686 0.1651 0.1833 0.0045  -0.0367 -0.0386 68  TYR   B CA  
4944 C  C   . TYR   B 68  ? 0.1600 0.1690 0.1764 0.0010  -0.0361 -0.0391 68  TYR   B C   
4945 O  O   . TYR   B 68  ? 0.1692 0.1732 0.1903 0.0074  -0.0293 -0.0545 68  TYR   B O   
4946 C  CB  . TYR   B 68  ? 0.1740 0.1854 0.1948 0.0104  -0.0360 -0.0435 68  TYR   B CB  
4947 C  CG  . TYR   B 68  ? 0.1838 0.2046 0.2129 0.0135  -0.0351 -0.0628 68  TYR   B CG  
4948 C  CD1 . TYR   B 68  ? 0.1851 0.2068 0.2402 -0.0040 -0.0301 -0.0721 68  TYR   B CD1 
4949 C  CD2 . TYR   B 68  ? 0.1882 0.2233 0.2314 0.0229  -0.0476 -0.0657 68  TYR   B CD2 
4950 C  CE1 . TYR   B 68  ? 0.1923 0.2230 0.2709 -0.0004 -0.0332 -0.0714 68  TYR   B CE1 
4951 C  CE2 . TYR   B 68  ? 0.1903 0.2281 0.2500 0.0166  -0.0388 -0.0834 68  TYR   B CE2 
4952 C  CZ  . TYR   B 68  ? 0.1879 0.2288 0.2716 0.0033  -0.0429 -0.0826 68  TYR   B CZ  
4953 O  OH  . TYR   B 68  ? 0.1835 0.2523 0.3033 0.0040  -0.0382 -0.0713 68  TYR   B OH  
4963 N  N   . ILE   B 69  ? 0.1646 0.1591 0.1833 0.0038  -0.0290 -0.0329 69  ILE   B N   
4964 C  CA  . ILE   B 69  ? 0.1724 0.1620 0.1968 0.0031  -0.0191 -0.0371 69  ILE   B CA  
4965 C  C   . ILE   B 69  ? 0.1714 0.1611 0.1886 0.0079  -0.0353 -0.0369 69  ILE   B C   
4966 O  O   . ILE   B 69  ? 0.1768 0.1726 0.1810 0.0095  -0.0169 -0.0341 69  ILE   B O   
4967 C  CB  . ILE   B 69  ? 0.1833 0.1696 0.2102 -0.0043 0.0065  -0.0352 69  ILE   B CB  
4968 C  CG1 . ILE   B 69  ? 0.1807 0.1733 0.2146 -0.0086 0.0093  -0.0351 69  ILE   B CG1 
4969 C  CG2 . ILE   B 69  ? 0.2003 0.1749 0.2190 -0.0049 0.0089  -0.0299 69  ILE   B CG2 
4970 C  CD1 . ILE   B 69  ? 0.1748 0.1802 0.2310 -0.0156 0.0171  -0.0354 69  ILE   B CD1 
4982 N  N   . ALA   B 70  ? 0.1694 0.1602 0.1940 0.0099  -0.0412 -0.0322 70  ALA   B N   
4983 C  CA  . ALA   B 70  ? 0.1749 0.1633 0.1767 0.0048  -0.0409 -0.0282 70  ALA   B CA  
4984 C  C   . ALA   B 70  ? 0.1781 0.1606 0.1826 0.0010  -0.0454 -0.0381 70  ALA   B C   
4985 O  O   . ALA   B 70  ? 0.1842 0.1656 0.1921 0.0075  -0.0393 -0.0393 70  ALA   B O   
4986 C  CB  . ALA   B 70  ? 0.1779 0.1783 0.1853 -0.0013 -0.0384 -0.0257 70  ALA   B CB  
4992 N  N   . THR   B 71  ? 0.1860 0.1636 0.1934 0.0057  -0.0513 -0.0394 71  THR   B N   
4993 C  CA  . THR   B 71  ? 0.1981 0.1685 0.2133 0.0111  -0.0651 -0.0413 71  THR   B CA  
4994 C  C   . THR   B 71  ? 0.1936 0.1757 0.2308 0.0260  -0.0592 -0.0568 71  THR   B C   
4995 O  O   . THR   B 71  ? 0.2070 0.1819 0.2698 0.0325  -0.0545 -0.0678 71  THR   B O   
4996 C  CB  . THR   B 71  ? 0.2256 0.1890 0.2345 0.0018  -0.0750 -0.0148 71  THR   B CB  
4997 O  OG1 . THR   B 71  ? 0.2424 0.2118 0.2652 -0.0179 -0.0694 0.0098  71  THR   B OG1 
4998 C  CG2 . THR   B 71  ? 0.2430 0.1818 0.2544 0.0069  -0.0666 -0.0056 71  THR   B CG2 
5006 N  N   . ASN   B 72  ? 0.1782 0.1811 0.2255 0.0190  -0.0571 -0.0659 72  ASN   B N   
5007 C  CA  . ASN   B 72  ? 0.1814 0.1975 0.2237 0.0181  -0.0404 -0.0748 72  ASN   B CA  
5008 C  C   . ASN   B 72  ? 0.1837 0.2067 0.2328 0.0049  -0.0224 -0.0751 72  ASN   B C   
5009 O  O   . ASN   B 72  ? 0.1856 0.2228 0.2626 0.0077  -0.0113 -0.0785 72  ASN   B O   
5010 C  CB  . ASN   B 72  ? 0.1916 0.2125 0.2316 0.0158  -0.0516 -0.0618 72  ASN   B CB  
5011 C  CG  . ASN   B 72  ? 0.2086 0.2240 0.2425 0.0316  -0.0591 -0.0429 72  ASN   B CG  
5012 O  OD1 . ASN   B 72  ? 0.2277 0.2357 0.2478 0.0216  -0.0493 -0.0463 72  ASN   B OD1 
5013 N  ND2 . ASN   B 72  ? 0.2173 0.2316 0.2743 0.0461  -0.0524 -0.0130 72  ASN   B ND2 
5020 N  N   . GLY   B 73  ? 0.1893 0.2016 0.2134 -0.0005 -0.0310 -0.0682 73  GLY   B N   
5021 C  CA  . GLY   B 73  ? 0.1832 0.2071 0.1883 -0.0030 -0.0244 -0.0535 73  GLY   B CA  
5022 C  C   . GLY   B 73  ? 0.1769 0.2068 0.1533 0.0062  -0.0184 -0.0474 73  GLY   B C   
5023 O  O   . GLY   B 73  ? 0.1692 0.1925 0.1744 0.0065  -0.0210 -0.0365 73  GLY   B O   
5027 N  N   . PRO   B 74  ? 0.1789 0.2165 0.1399 0.0031  -0.0255 -0.0400 74  PRO   B N   
5028 C  CA  . PRO   B 74  ? 0.1715 0.2155 0.1327 0.0099  -0.0200 -0.0260 74  PRO   B CA  
5029 C  C   . PRO   B 74  ? 0.1591 0.2012 0.1477 0.0102  -0.0152 -0.0185 74  PRO   B C   
5030 O  O   . PRO   B 74  ? 0.1609 0.1979 0.1839 0.0113  -0.0126 -0.0308 74  PRO   B O   
5031 C  CB  . PRO   B 74  ? 0.1877 0.2314 0.1429 0.0075  -0.0212 -0.0233 74  PRO   B CB  
5032 C  CG  . PRO   B 74  ? 0.2079 0.2435 0.1775 0.0052  -0.0175 -0.0201 74  PRO   B CG  
5033 C  CD  . PRO   B 74  ? 0.2058 0.2330 0.1588 0.0071  -0.0160 -0.0355 74  PRO   B CD  
5041 N  N   . LEU   B 75  ? 0.1568 0.1895 0.1309 0.0122  -0.0165 -0.0186 75  LEU   B N   
5042 C  CA  . LEU   B 75  ? 0.1594 0.1875 0.1260 0.0037  -0.0177 -0.0044 75  LEU   B CA  
5043 C  C   . LEU   B 75  ? 0.1635 0.1955 0.1289 0.0044  -0.0041 -0.0083 75  LEU   B C   
5044 O  O   . LEU   B 75  ? 0.1794 0.2057 0.1450 -0.0045 -0.0037 -0.0030 75  LEU   B O   
5045 C  CB  . LEU   B 75  ? 0.1736 0.1947 0.1215 -0.0081 -0.0177 0.0110  75  LEU   B CB  
5046 C  CG  . LEU   B 75  ? 0.2023 0.2072 0.1450 -0.0311 -0.0119 0.0079  75  LEU   B CG  
5047 C  CD1 . LEU   B 75  ? 0.2345 0.2208 0.1627 -0.0362 0.0082  -0.0015 75  LEU   B CD1 
5048 C  CD2 . LEU   B 75  ? 0.2308 0.2293 0.2192 -0.0238 0.0031  0.0131  75  LEU   B CD2 
5060 N  N   . LYS   B 76  ? 0.1616 0.2175 0.1675 0.0059  -0.0004 0.0031  76  LYS   B N   
5061 C  CA  . LYS   B 76  ? 0.1780 0.2254 0.1902 -0.0028 0.0192  -0.0001 76  LYS   B CA  
5062 C  C   . LYS   B 76  ? 0.1660 0.2101 0.1631 0.0078  0.0128  0.0189  76  LYS   B C   
5063 O  O   . LYS   B 76  ? 0.1628 0.1933 0.1609 0.0006  0.0037  0.0193  76  LYS   B O   
5064 C  CB  . LYS   B 76  ? 0.1974 0.2366 0.2559 -0.0123 0.0409  -0.0365 76  LYS   B CB  
5065 C  CG  . LYS   B 76  ? 0.2091 0.2575 0.3093 -0.0018 0.0344  -0.0477 76  LYS   B CG  
5066 C  CD  . LYS   B 76  ? 0.2080 0.2675 0.3489 0.0039  0.0159  -0.0632 76  LYS   B CD  
5067 C  CE  . LYS   B 76  ? 0.2081 0.2834 0.4031 0.0069  0.0032  -0.0747 76  LYS   B CE  
5068 N  NZ  . LYS   B 76  ? 0.2067 0.2913 0.4139 0.0056  -0.0167 -0.0948 76  LYS   B NZ  
5082 N  N   . VAL   B 77  ? 0.1754 0.2180 0.1548 0.0147  0.0096  0.0221  77  VAL   B N   
5083 C  CA  . VAL   B 77  ? 0.1769 0.2028 0.1685 0.0181  0.0172  0.0482  77  VAL   B CA  
5084 C  C   . VAL   B 77  ? 0.1626 0.1810 0.1646 0.0180  0.0221  0.0352  77  VAL   B C   
5085 O  O   . VAL   B 77  ? 0.1660 0.1779 0.1716 0.0278  0.0265  0.0278  77  VAL   B O   
5086 C  CB  . VAL   B 77  ? 0.1851 0.2141 0.2059 0.0201  0.0298  0.0607  77  VAL   B CB  
5087 C  CG1 . VAL   B 77  ? 0.1965 0.2106 0.2350 0.0134  0.0369  0.0787  77  VAL   B CG1 
5088 C  CG2 . VAL   B 77  ? 0.1956 0.2315 0.2364 0.0175  0.0061  0.0658  77  VAL   B CG2 
5098 N  N   . GLY   B 78  ? 0.1581 0.1711 0.1590 0.0089  0.0196  0.0270  78  GLY   B N   
5099 C  CA  . GLY   B 78  ? 0.1552 0.1677 0.1609 0.0117  0.0264  0.0136  78  GLY   B CA  
5100 C  C   . GLY   B 78  ? 0.1483 0.1560 0.1566 0.0102  0.0201  0.0180  78  GLY   B C   
5101 O  O   . GLY   B 78  ? 0.1572 0.1545 0.1743 0.0153  0.0160  0.0194  78  GLY   B O   
5105 N  N   . GLY   B 79  ? 0.1442 0.1630 0.1537 0.0062  0.0190  0.0171  79  GLY   B N   
5106 C  CA  . GLY   B 79  ? 0.1465 0.1554 0.1500 0.0070  0.0118  0.0143  79  GLY   B CA  
5107 C  C   . GLY   B 79  ? 0.1358 0.1455 0.1522 0.0078  0.0116  0.0066  79  GLY   B C   
5108 O  O   . GLY   B 79  ? 0.1436 0.1435 0.1699 0.0118  0.0174  0.0151  79  GLY   B O   
5112 N  N   . SER   B 80  ? 0.1366 0.1400 0.1585 0.0071  0.0155  0.0019  80  SER   B N   
5113 C  CA  . SER   B 80  ? 0.1299 0.1392 0.1627 0.0037  -0.0006 0.0069  80  SER   B CA  
5114 C  C   . SER   B 80  ? 0.1364 0.1328 0.1619 0.0104  -0.0062 0.0035  80  SER   B C   
5115 O  O   . SER   B 80  ? 0.1508 0.1344 0.1880 0.0112  0.0018  0.0011  80  SER   B O   
5116 C  CB  . SER   B 80  ? 0.1337 0.1397 0.1633 -0.0052 -0.0013 0.0075  80  SER   B CB  
5117 O  OG  . SER   B 80  ? 0.1431 0.1553 0.1903 -0.0049 -0.0121 0.0078  80  SER   B OG  
5123 N  N   . CYS   B 81  ? 0.1360 0.1233 0.1623 0.0027  -0.0069 -0.0019 81  CYS   B N   
5124 C  CA  . CYS   B 81  ? 0.1389 0.1189 0.1678 0.0044  -0.0085 -0.0059 81  CYS   B CA  
5125 C  C   . CYS   B 81  ? 0.1367 0.1209 0.1383 0.0023  -0.0133 -0.0047 81  CYS   B C   
5126 O  O   . CYS   B 81  ? 0.1568 0.1260 0.1481 0.0083  -0.0021 -0.0065 81  CYS   B O   
5127 C  CB  . CYS   B 81  ? 0.1531 0.1315 0.1663 0.0031  -0.0134 -0.0095 81  CYS   B CB  
5128 S  SG  . CYS   B 81  ? 0.1543 0.1522 0.1670 -0.0040 -0.0252 -0.0116 81  CYS   B SG  
5134 N  N   . VAL   B 82  ? 0.1424 0.1194 0.1532 -0.0007 -0.0129 -0.0043 82  VAL   B N   
5135 C  CA  . VAL   B 82  ? 0.1475 0.1243 0.1498 -0.0081 -0.0130 0.0035  82  VAL   B CA  
5136 C  C   . VAL   B 82  ? 0.1516 0.1138 0.1654 -0.0034 -0.0025 -0.0026 82  VAL   B C   
5137 O  O   . VAL   B 82  ? 0.1605 0.1209 0.1866 -0.0057 -0.0069 -0.0145 82  VAL   B O   
5138 C  CB  . VAL   B 82  ? 0.1528 0.1416 0.1683 -0.0039 -0.0115 0.0018  82  VAL   B CB  
5139 C  CG1 . VAL   B 82  ? 0.1740 0.1691 0.1774 0.0030  -0.0087 0.0116  82  VAL   B CG1 
5140 C  CG2 . VAL   B 82  ? 0.1588 0.1507 0.1805 -0.0060 -0.0267 0.0142  82  VAL   B CG2 
5150 N  N   . LEU   B 83  ? 0.1408 0.1168 0.1607 -0.0123 -0.0196 -0.0120 83  LEU   B N   
5151 C  CA  . LEU   B 83  ? 0.1459 0.1228 0.1539 -0.0113 -0.0157 -0.0018 83  LEU   B CA  
5152 C  C   . LEU   B 83  ? 0.1448 0.1209 0.1588 -0.0173 -0.0130 0.0016  83  LEU   B C   
5153 O  O   . LEU   B 83  ? 0.1431 0.1312 0.1484 -0.0248 -0.0132 0.0011  83  LEU   B O   
5154 C  CB  . LEU   B 83  ? 0.1534 0.1353 0.1447 -0.0143 -0.0201 -0.0078 83  LEU   B CB  
5155 C  CG  . LEU   B 83  ? 0.1715 0.1551 0.1553 -0.0183 -0.0093 -0.0064 83  LEU   B CG  
5156 C  CD1 . LEU   B 83  ? 0.1838 0.1615 0.1713 -0.0061 -0.0142 -0.0061 83  LEU   B CD1 
5157 C  CD2 . LEU   B 83  ? 0.1885 0.1587 0.1662 -0.0115 -0.0143 -0.0254 83  LEU   B CD2 
5169 N  N   . SER   B 84  ? 0.1486 0.1320 0.1746 -0.0219 -0.0165 0.0063  84  SER   B N   
5170 C  CA  . SER   B 84  ? 0.1476 0.1515 0.1610 -0.0233 -0.0165 0.0161  84  SER   B CA  
5171 C  C   . SER   B 84  ? 0.1396 0.1701 0.1282 -0.0176 -0.0153 0.0180  84  SER   B C   
5172 O  O   . SER   B 84  ? 0.1444 0.1540 0.1305 -0.0181 -0.0114 0.0033  84  SER   B O   
5173 C  CB  . SER   B 84  ? 0.1667 0.1556 0.2033 -0.0265 0.0062  0.0168  84  SER   B CB  
5174 O  OG  . SER   B 84  ? 0.1646 0.1677 0.2512 -0.0325 0.0093  0.0211  84  SER   B OG  
5180 N  N   . GLY   B 85  ? 0.1434 0.1877 0.1452 -0.0201 -0.0140 0.0237  85  GLY   B N   
5181 C  CA  . GLY   B 85  ? 0.1404 0.1944 0.1532 -0.0349 -0.0034 -0.0017 85  GLY   B CA  
5182 C  C   . GLY   B 85  ? 0.1423 0.1792 0.1390 -0.0401 -0.0013 0.0101  85  GLY   B C   
5183 O  O   . GLY   B 85  ? 0.1508 0.1797 0.1469 -0.0462 0.0119  -0.0074 85  GLY   B O   
5187 N  N   . HIS   B 86  ? 0.1452 0.1638 0.1583 -0.0286 -0.0158 0.0200  86  HIS   B N   
5188 C  CA  . HIS   B 86  ? 0.1453 0.1619 0.1675 -0.0302 -0.0153 0.0215  86  HIS   B CA  
5189 C  C   . HIS   B 86  ? 0.1463 0.1748 0.1606 -0.0385 -0.0080 0.0392  86  HIS   B C   
5190 O  O   . HIS   B 86  ? 0.1561 0.1895 0.1741 -0.0362 0.0038  0.0369  86  HIS   B O   
5191 C  CB  . HIS   B 86  ? 0.1489 0.1624 0.1702 -0.0196 -0.0199 0.0104  86  HIS   B CB  
5192 C  CG  . HIS   B 86  ? 0.1552 0.1710 0.1571 -0.0106 -0.0228 0.0158  86  HIS   B CG  
5193 N  ND1 . HIS   B 86  ? 0.1685 0.1917 0.1805 -0.0215 -0.0250 -0.0063 86  HIS   B ND1 
5194 C  CD2 . HIS   B 86  ? 0.1546 0.1709 0.1699 -0.0103 -0.0240 0.0113  86  HIS   B CD2 
5195 C  CE1 . HIS   B 86  ? 0.1741 0.1883 0.1803 -0.0153 -0.0148 -0.0173 86  HIS   B CE1 
5196 N  NE2 . HIS   B 86  ? 0.1667 0.1788 0.1647 -0.0028 -0.0165 -0.0030 86  HIS   B NE2 
5204 N  N   . ASN   B 87  ? 0.1469 0.1781 0.1718 -0.0320 -0.0052 0.0289  87  ASN   B N   
5205 C  CA  . ASN   B 87  ? 0.1513 0.1964 0.1625 -0.0332 0.0114  0.0188  87  ASN   B CA  
5206 C  C   . ASN   B 87  ? 0.1649 0.1838 0.1492 -0.0262 0.0223  0.0159  87  ASN   B C   
5207 O  O   . ASN   B 87  ? 0.1880 0.1946 0.1862 -0.0232 0.0419  0.0135  87  ASN   B O   
5208 C  CB  . ASN   B 87  ? 0.1513 0.2331 0.1958 -0.0263 0.0184  0.0173  87  ASN   B CB  
5209 C  CG  . ASN   B 87  ? 0.1598 0.2561 0.2051 0.0112  0.0252  0.0323  87  ASN   B CG  
5210 O  OD1 . ASN   B 87  ? 0.1553 0.2467 0.1889 0.0095  0.0397  0.0486  87  ASN   B OD1 
5211 N  ND2 . ASN   B 87  ? 0.1891 0.2699 0.2443 0.0178  0.0271  0.0312  87  ASN   B ND2 
5218 N  N   . LEU   B 88  ? 0.1543 0.1686 0.1426 -0.0330 0.0178  0.0112  88  LEU   B N   
5219 C  CA  . LEU   B 88  ? 0.1624 0.1628 0.1435 -0.0314 0.0026  0.0017  88  LEU   B CA  
5220 C  C   . LEU   B 88  ? 0.1649 0.1520 0.1464 -0.0374 0.0017  0.0049  88  LEU   B C   
5221 O  O   . LEU   B 88  ? 0.1898 0.1599 0.1724 -0.0263 -0.0271 -0.0042 88  LEU   B O   
5222 C  CB  . LEU   B 88  ? 0.1757 0.1683 0.1592 -0.0373 -0.0075 0.0185  88  LEU   B CB  
5223 C  CG  . LEU   B 88  ? 0.2180 0.1967 0.1750 -0.0341 -0.0249 0.0317  88  LEU   B CG  
5224 C  CD1 . LEU   B 88  ? 0.2303 0.2250 0.1973 -0.0460 -0.0247 0.0402  88  LEU   B CD1 
5225 C  CD2 . LEU   B 88  ? 0.2569 0.2238 0.2296 0.0041  -0.0447 0.0124  88  LEU   B CD2 
5237 N  N   . ALA   B 89  ? 0.1535 0.1486 0.1406 -0.0355 0.0143  0.0049  89  ALA   B N   
5238 C  CA  . ALA   B 89  ? 0.1498 0.1419 0.1292 -0.0334 -0.0035 0.0136  89  ALA   B CA  
5239 C  C   . ALA   B 89  ? 0.1594 0.1470 0.1380 -0.0374 0.0144  0.0033  89  ALA   B C   
5240 O  O   . ALA   B 89  ? 0.1455 0.1571 0.1711 -0.0358 0.0145  -0.0219 89  ALA   B O   
5241 C  CB  . ALA   B 89  ? 0.1425 0.1452 0.1473 -0.0365 0.0008  0.0228  89  ALA   B CB  
5247 N  N   . LYS   B 90  ? 0.1926 0.1374 0.1473 -0.0425 -0.0084 0.0074  90  LYS   B N   
5248 C  CA  . LYS   B 90  ? 0.2055 0.1374 0.1437 -0.0413 -0.0108 0.0085  90  LYS   B CA  
5249 C  C   . LYS   B 90  ? 0.1908 0.1334 0.1477 -0.0446 -0.0084 0.0012  90  LYS   B C   
5250 O  O   . LYS   B 90  ? 0.2040 0.1517 0.1672 -0.0609 -0.0048 0.0027  90  LYS   B O   
5251 C  CB  . LYS   B 90  ? 0.2271 0.1376 0.1741 -0.0360 -0.0020 0.0184  90  LYS   B CB  
5252 C  CG  . LYS   B 90  ? 0.2325 0.1584 0.1788 -0.0211 0.0216  0.0076  90  LYS   B CG  
5253 C  CD  . LYS   B 90  ? 0.2633 0.1889 0.2315 -0.0120 0.0464  -0.0128 90  LYS   B CD  
5254 C  CE  . LYS   B 90  ? 0.2778 0.2035 0.2870 -0.0208 0.0632  -0.0222 90  LYS   B CE  
5255 N  NZ  . LYS   B 90  ? 0.2858 0.1973 0.2795 -0.0340 0.0822  -0.0164 90  LYS   B NZ  
5269 N  N   . HIS   B 91  ? 0.1664 0.1219 0.1318 -0.0309 -0.0167 0.0084  91  HIS   B N   
5270 C  CA  . HIS   B 91  ? 0.1539 0.1267 0.1410 -0.0219 -0.0157 0.0025  91  HIS   B CA  
5271 C  C   . HIS   B 91  ? 0.1443 0.1275 0.1288 -0.0268 0.0001  0.0036  91  HIS   B C   
5272 O  O   . HIS   B 91  ? 0.1561 0.1311 0.1295 -0.0267 -0.0182 0.0008  91  HIS   B O   
5273 C  CB  . HIS   B 91  ? 0.1726 0.1316 0.1732 -0.0112 -0.0111 0.0127  91  HIS   B CB  
5274 C  CG  . HIS   B 91  ? 0.2142 0.1438 0.2444 0.0073  0.0218  0.0258  91  HIS   B CG  
5275 N  ND1 . HIS   B 91  ? 0.2469 0.1502 0.3076 0.0060  0.0263  0.0185  91  HIS   B ND1 
5276 C  CD2 . HIS   B 91  ? 0.2275 0.1721 0.2914 0.0235  0.0125  0.0591  91  HIS   B CD2 
5277 C  CE1 . HIS   B 91  ? 0.2539 0.1660 0.3222 0.0216  0.0251  0.0242  91  HIS   B CE1 
5278 N  NE2 . HIS   B 91  ? 0.2403 0.1796 0.3211 0.0374  0.0263  0.0610  91  HIS   B NE2 
5286 N  N   . CYS   B 92  ? 0.1371 0.1242 0.1276 -0.0241 -0.0105 0.0037  92  CYS   B N   
5287 C  CA  . CYS   B 92  ? 0.1362 0.1210 0.1285 -0.0185 -0.0035 0.0024  92  CYS   B CA  
5288 C  C   . CYS   B 92  ? 0.1303 0.1152 0.1239 -0.0141 -0.0046 0.0009  92  CYS   B C   
5289 O  O   . CYS   B 92  ? 0.1355 0.1231 0.1495 -0.0163 -0.0035 -0.0006 92  CYS   B O   
5290 C  CB  . CYS   B 92  ? 0.1373 0.1315 0.1325 -0.0144 -0.0020 0.0029  92  CYS   B CB  
5291 S  SG  . CYS   B 92  ? 0.1375 0.1315 0.1280 -0.0120 -0.0100 0.0042  92  CYS   B SG  
5297 N  N   . LEU   B 93  ? 0.1267 0.1189 0.1319 -0.0151 -0.0067 -0.0019 93  LEU   B N   
5298 C  CA  . LEU   B 93  ? 0.1273 0.1212 0.1356 -0.0050 -0.0044 0.0036  93  LEU   B CA  
5299 C  C   . LEU   B 93  ? 0.1197 0.1182 0.1239 -0.0026 -0.0041 0.0072  93  LEU   B C   
5300 O  O   . LEU   B 93  ? 0.1265 0.1178 0.1458 -0.0059 -0.0050 0.0024  93  LEU   B O   
5301 C  CB  . LEU   B 93  ? 0.1328 0.1201 0.1457 -0.0039 -0.0049 0.0003  93  LEU   B CB  
5302 C  CG  . LEU   B 93  ? 0.1274 0.1288 0.1579 -0.0045 -0.0036 0.0086  93  LEU   B CG  
5303 C  CD1 . LEU   B 93  ? 0.1315 0.1423 0.1561 -0.0002 -0.0046 -0.0026 93  LEU   B CD1 
5304 C  CD2 . LEU   B 93  ? 0.1290 0.1346 0.1725 -0.0052 -0.0076 -0.0011 93  LEU   B CD2 
5316 N  N   . HIS   B 94  ? 0.1259 0.1144 0.1256 -0.0068 -0.0133 0.0052  94  HIS   B N   
5317 C  CA  . HIS   B 94  ? 0.1279 0.1116 0.1281 0.0008  -0.0023 0.0037  94  HIS   B CA  
5318 C  C   . HIS   B 94  ? 0.1278 0.1165 0.1336 0.0018  0.0004  0.0076  94  HIS   B C   
5319 O  O   . HIS   B 94  ? 0.1326 0.1259 0.1754 -0.0068 0.0174  -0.0036 94  HIS   B O   
5320 C  CB  . HIS   B 94  ? 0.1269 0.1251 0.1274 -0.0016 -0.0055 0.0016  94  HIS   B CB  
5321 C  CG  . HIS   B 94  ? 0.1319 0.1205 0.1336 -0.0055 -0.0176 0.0031  94  HIS   B CG  
5322 N  ND1 . HIS   B 94  ? 0.1326 0.1260 0.1376 -0.0067 -0.0210 -0.0000 94  HIS   B ND1 
5323 C  CD2 . HIS   B 94  ? 0.1386 0.1238 0.1395 -0.0015 -0.0129 0.0061  94  HIS   B CD2 
5324 C  CE1 . HIS   B 94  ? 0.1393 0.1257 0.1347 -0.0129 -0.0203 0.0079  94  HIS   B CE1 
5325 N  NE2 . HIS   B 94  ? 0.1348 0.1300 0.1424 -0.0161 -0.0134 0.0060  94  HIS   B NE2 
5333 N  N   . VAL   B 95  ? 0.1200 0.1158 0.1487 -0.0002 0.0012  0.0065  95  VAL   B N   
5334 C  CA  . VAL   B 95  ? 0.1218 0.1253 0.1475 -0.0006 0.0018  0.0149  95  VAL   B CA  
5335 C  C   . VAL   B 95  ? 0.1294 0.1245 0.1458 -0.0011 0.0098  0.0031  95  VAL   B C   
5336 O  O   . VAL   B 95  ? 0.1336 0.1243 0.1623 0.0046  0.0092  0.0096  95  VAL   B O   
5337 C  CB  . VAL   B 95  ? 0.1268 0.1202 0.1410 -0.0039 -0.0023 0.0027  95  VAL   B CB  
5338 C  CG1 . VAL   B 95  ? 0.1355 0.1430 0.1657 -0.0119 -0.0063 0.0125  95  VAL   B CG1 
5339 C  CG2 . VAL   B 95  ? 0.1364 0.1198 0.1434 0.0029  -0.0065 -0.0024 95  VAL   B CG2 
5349 N  N   . VAL   B 96  ? 0.1369 0.1289 0.1496 0.0085  0.0056  0.0095  96  VAL   B N   
5350 C  CA  . VAL   B 96  ? 0.1428 0.1400 0.1368 0.0103  0.0011  0.0164  96  VAL   B CA  
5351 C  C   . VAL   B 96  ? 0.1428 0.1470 0.1482 0.0062  0.0103  0.0140  96  VAL   B C   
5352 O  O   . VAL   B 96  ? 0.1462 0.1514 0.1684 0.0018  0.0172  0.0006  96  VAL   B O   
5353 C  CB  . VAL   B 96  ? 0.1497 0.1600 0.1369 0.0128  0.0083  0.0078  96  VAL   B CB  
5354 C  CG1 . VAL   B 96  ? 0.1519 0.1744 0.1578 0.0160  0.0080  0.0078  96  VAL   B CG1 
5355 C  CG2 . VAL   B 96  ? 0.1569 0.1679 0.1587 0.0074  0.0094  0.0027  96  VAL   B CG2 
5365 N  N   . GLY   B 97  ? 0.1476 0.1458 0.1455 0.0035  0.0071  0.0202  97  GLY   B N   
5366 C  CA  . GLY   B 97  ? 0.1638 0.1504 0.1465 0.0032  0.0100  0.0219  97  GLY   B CA  
5367 C  C   . GLY   B 97  ? 0.1829 0.1592 0.1592 0.0132  0.0086  0.0199  97  GLY   B C   
5368 O  O   . GLY   B 97  ? 0.1949 0.1680 0.1617 0.0058  0.0052  0.0116  97  GLY   B O   
5372 N  N   . PRO   B 98  ? 0.1932 0.1610 0.1737 0.0107  0.0283  0.0317  98  PRO   B N   
5373 C  CA  . PRO   B 98  ? 0.2022 0.1735 0.1798 0.0192  0.0380  0.0277  98  PRO   B CA  
5374 C  C   . PRO   B 98  ? 0.2114 0.1770 0.1522 0.0289  0.0371  0.0474  98  PRO   B C   
5375 O  O   . PRO   B 98  ? 0.2039 0.1723 0.1757 0.0238  0.0376  0.0400  98  PRO   B O   
5376 C  CB  . PRO   B 98  ? 0.1934 0.1782 0.1968 0.0148  0.0467  0.0308  98  PRO   B CB  
5377 C  CG  . PRO   B 98  ? 0.1896 0.1743 0.1994 0.0101  0.0389  0.0489  98  PRO   B CG  
5378 C  CD  . PRO   B 98  ? 0.1798 0.1657 0.1862 0.0142  0.0332  0.0384  98  PRO   B CD  
5386 N  N   . ASN   B 99  ? 0.2212 0.1944 0.1696 0.0438  0.0333  0.0230  99  ASN   B N   
5387 C  CA  . ASN   B 99  ? 0.2429 0.2054 0.1638 0.0531  0.0315  0.0444  99  ASN   B CA  
5388 C  C   . ASN   B 99  ? 0.2736 0.2395 0.1998 0.0511  0.0504  0.0748  99  ASN   B C   
5389 O  O   . ASN   B 99  ? 0.2868 0.2426 0.2071 0.0505  0.0417  0.0797  99  ASN   B O   
5390 C  CB  . ASN   B 99  ? 0.2535 0.1995 0.1665 0.0536  0.0198  0.0429  99  ASN   B CB  
5391 C  CG  . ASN   B 99  ? 0.2609 0.2084 0.1976 0.0468  0.0104  0.0422  99  ASN   B CG  
5392 O  OD1 . ASN   B 99  ? 0.2641 0.2113 0.2218 0.0487  0.0105  0.0460  99  ASN   B OD1 
5393 N  ND2 . ASN   B 99  ? 0.2633 0.2093 0.2131 0.0490  -0.0163 0.0330  99  ASN   B ND2 
5400 N  N   A VAL   B 100 ? 0.2904 0.2509 0.2395 0.0396  0.0571  0.0982  100 VAL   B N   
5401 N  N   B VAL   B 100 ? 0.2980 0.2558 0.2440 0.0447  0.0428  0.0842  100 VAL   B N   
5402 C  CA  A VAL   B 100 ? 0.3224 0.2710 0.2972 0.0296  0.0614  0.1144  100 VAL   B CA  
5403 C  CA  B VAL   B 100 ? 0.3272 0.2742 0.2869 0.0389  0.0352  0.0915  100 VAL   B CA  
5404 C  C   A VAL   B 100 ? 0.3477 0.2794 0.2819 0.0385  0.0551  0.1314  100 VAL   B C   
5405 C  C   B VAL   B 100 ? 0.3489 0.2820 0.2863 0.0434  0.0344  0.1140  100 VAL   B C   
5406 O  O   A VAL   B 100 ? 0.3572 0.2919 0.2844 0.0366  0.0625  0.1261  100 VAL   B O   
5407 O  O   B VAL   B 100 ? 0.3540 0.2880 0.2869 0.0427  0.0342  0.1109  100 VAL   B O   
5408 C  CB  A VAL   B 100 ? 0.3335 0.2892 0.3701 0.0104  0.0612  0.1159  100 VAL   B CB  
5409 C  CB  B VAL   B 100 ? 0.3355 0.2857 0.3246 0.0292  0.0277  0.0785  100 VAL   B CB  
5410 C  CG1 A VAL   B 100 ? 0.3406 0.2975 0.4034 0.0109  0.0609  0.1105  100 VAL   B CG1 
5411 C  CG1 B VAL   B 100 ? 0.3386 0.2892 0.3412 0.0275  0.0254  0.0727  100 VAL   B CG1 
5412 C  CG2 A VAL   B 100 ? 0.3341 0.2930 0.3917 -0.0014 0.0647  0.1257  100 VAL   B CG2 
5413 C  CG2 B VAL   B 100 ? 0.3382 0.2900 0.3390 0.0249  0.0257  0.0752  100 VAL   B CG2 
5432 N  N   . ASN   B 101 ? 0.3644 0.2848 0.2888 0.0492  0.0338  0.1351  101 ASN   B N   
5433 C  CA  . ASN   B 101 ? 0.4034 0.3044 0.3057 0.0593  0.0120  0.1428  101 ASN   B CA  
5434 C  C   . ASN   B 101 ? 0.4462 0.3450 0.3108 0.0640  -0.0006 0.1534  101 ASN   B C   
5435 O  O   . ASN   B 101 ? 0.4526 0.3586 0.3345 0.0718  0.0018  0.1275  101 ASN   B O   
5436 C  CB  . ASN   B 101 ? 0.4022 0.2886 0.3245 0.0543  0.0142  0.1277  101 ASN   B CB  
5437 C  CG  . ASN   B 101 ? 0.4030 0.2733 0.3390 0.0532  0.0174  0.1239  101 ASN   B CG  
5438 O  OD1 . ASN   B 101 ? 0.4073 0.2702 0.3607 0.0429  0.0360  0.1186  101 ASN   B OD1 
5439 N  ND2 . ASN   B 101 ? 0.4008 0.2715 0.3314 0.0554  0.0122  0.1105  101 ASN   B ND2 
5447 N  N   . LYS   B 102 ? 0.4802 0.3796 0.3346 0.0531  0.0030  0.1525  102 LYS   B N   
5448 C  CA  . LYS   B 102 ? 0.5134 0.4245 0.3654 0.0364  0.0134  0.1204  102 LYS   B CA  
5449 C  C   . LYS   B 102 ? 0.5073 0.4246 0.3441 0.0342  0.0217  0.1244  102 LYS   B C   
5450 O  O   . LYS   B 102 ? 0.5179 0.4327 0.3597 0.0356  0.0101  0.1159  102 LYS   B O   
5451 C  CB  . LYS   B 102 ? 0.5485 0.4667 0.4433 0.0225  0.0224  0.0734  102 LYS   B CB  
5452 C  CG  . LYS   B 102 ? 0.5785 0.5035 0.5153 0.0108  0.0326  0.0311  102 LYS   B CG  
5453 C  CD  . LYS   B 102 ? 0.6030 0.5319 0.5881 0.0030  0.0437  -0.0034 102 LYS   B CD  
5454 C  CE  . LYS   B 102 ? 0.6200 0.5505 0.6422 -0.0029 0.0506  -0.0282 102 LYS   B CE  
5455 N  NZ  . LYS   B 102 ? 0.6293 0.5602 0.6733 -0.0052 0.0522  -0.0410 102 LYS   B NZ  
5469 N  N   . GLY   B 103 ? 0.4859 0.4127 0.3319 0.0295  0.0417  0.1242  103 GLY   B N   
5470 C  CA  . GLY   B 103 ? 0.4620 0.4015 0.3399 0.0281  0.0573  0.0994  103 GLY   B CA  
5471 C  C   . GLY   B 103 ? 0.4340 0.3861 0.3300 0.0255  0.0726  0.0776  103 GLY   B C   
5472 O  O   . GLY   B 103 ? 0.4390 0.3956 0.3335 0.0254  0.0779  0.0766  103 GLY   B O   
5476 N  N   A GLU   B 104 ? 0.4134 0.3670 0.3158 0.0268  0.0931  0.0671  104 GLU   B N   
5477 N  N   B GLU   B 104 ? 0.4178 0.3773 0.3364 0.0211  0.0600  0.0602  104 GLU   B N   
5478 C  CA  A GLU   B 104 ? 0.3906 0.3485 0.2944 0.0300  0.1042  0.0522  104 GLU   B CA  
5479 C  CA  B GLU   B 104 ? 0.3995 0.3670 0.3333 0.0167  0.0473  0.0400  104 GLU   B CA  
5480 C  C   A GLU   B 104 ? 0.3954 0.3513 0.3084 0.0122  0.1405  0.0549  104 GLU   B C   
5481 C  C   B GLU   B 104 ? 0.3939 0.3649 0.3450 0.0110  0.0503  0.0309  104 GLU   B C   
5482 O  O   A GLU   B 104 ? 0.3998 0.3590 0.3329 0.0053  0.1392  0.0498  104 GLU   B O   
5483 O  O   B GLU   B 104 ? 0.3958 0.3674 0.3505 0.0097  0.0502  0.0279  104 GLU   B O   
5484 C  CB  A GLU   B 104 ? 0.3687 0.3263 0.2858 0.0490  0.0627  0.0259  104 GLU   B CB  
5485 C  CB  B GLU   B 104 ? 0.3884 0.3582 0.3222 0.0173  0.0302  0.0259  104 GLU   B CB  
5486 C  CG  A GLU   B 104 ? 0.3501 0.3102 0.2706 0.0648  0.0215  -0.0026 104 GLU   B CG  
5487 C  CG  B GLU   B 104 ? 0.3799 0.3517 0.3105 0.0174  0.0137  0.0111  104 GLU   B CG  
5488 C  CD  A GLU   B 104 ? 0.3338 0.2916 0.2489 0.0806  -0.0146 -0.0171 104 GLU   B CD  
5489 C  CD  B GLU   B 104 ? 0.3746 0.3464 0.2999 0.0172  -0.0002 0.0008  104 GLU   B CD  
5490 O  OE1 A GLU   B 104 ? 0.3158 0.2753 0.2109 0.0957  -0.0077 -0.0180 104 GLU   B OE1 
5491 O  OE1 B GLU   B 104 ? 0.3712 0.3424 0.2902 0.0170  -0.0006 0.0000  104 GLU   B OE1 
5492 O  OE2 A GLU   B 104 ? 0.3360 0.2947 0.2512 0.0754  -0.0466 -0.0322 104 GLU   B OE2 
5493 O  OE2 B GLU   B 104 ? 0.3744 0.3470 0.2986 0.0167  -0.0100 -0.0064 104 GLU   B OE2 
5506 N  N   A ASP   B 105 ? 0.3919 0.3464 0.2951 0.0013  0.1675  0.0608  105 ASP   B N   
5507 N  N   B ASP   B 105 ? 0.3855 0.3600 0.3441 0.0066  0.0515  0.0249  105 ASP   B N   
5508 C  CA  A ASP   B 105 ? 0.3928 0.3454 0.3122 -0.0090 0.1852  0.0489  105 ASP   B CA  
5509 C  CA  B ASP   B 105 ? 0.3788 0.3560 0.3517 0.0024  0.0508  0.0167  105 ASP   B CA  
5510 C  C   A ASP   B 105 ? 0.3785 0.3182 0.2875 -0.0221 0.1828  0.0479  105 ASP   B C   
5511 C  C   B ASP   B 105 ? 0.3717 0.3496 0.3361 -0.0005 0.0496  0.0117  105 ASP   B C   
5512 O  O   A ASP   B 105 ? 0.3638 0.3112 0.2773 -0.0231 0.1752  0.0482  105 ASP   B O   
5513 O  O   B ASP   B 105 ? 0.3710 0.3485 0.3256 -0.0005 0.0506  0.0118  105 ASP   B O   
5514 C  CB  A ASP   B 105 ? 0.4122 0.3715 0.3885 -0.0001 0.1828  0.0226  105 ASP   B CB  
5515 C  CB  B ASP   B 105 ? 0.3799 0.3591 0.3747 0.0023  0.0509  0.0129  105 ASP   B CB  
5516 C  CG  A ASP   B 105 ? 0.4279 0.3931 0.4570 0.0037  0.1907  0.0072  105 ASP   B CG  
5517 C  CG  B ASP   B 105 ? 0.3817 0.3620 0.4002 0.0009  0.0534  0.0119  105 ASP   B CG  
5518 O  OD1 A ASP   B 105 ? 0.4273 0.3965 0.4597 -0.0035 0.2076  0.0109  105 ASP   B OD1 
5519 O  OD1 B ASP   B 105 ? 0.3816 0.3634 0.4027 -0.0018 0.0554  0.0126  105 ASP   B OD1 
5520 O  OD2 A ASP   B 105 ? 0.4366 0.4053 0.4913 0.0116  0.1838  -0.0049 105 ASP   B OD2 
5521 O  OD2 B ASP   B 105 ? 0.3814 0.3626 0.4071 0.0012  0.0544  0.0120  105 ASP   B OD2 
5530 N  N   A ILE   B 106 ? 0.3710 0.2959 0.2955 -0.0302 0.1750  0.0473  106 ILE   B N   
5531 N  N   B ILE   B 106 ? 0.3644 0.3436 0.3271 -0.0020 0.0458  0.0085  106 ILE   B N   
5532 C  CA  A ILE   B 106 ? 0.3513 0.2682 0.3148 -0.0440 0.1741  0.0417  106 ILE   B CA  
5533 C  CA  B ILE   B 106 ? 0.3546 0.3369 0.3260 -0.0035 0.0437  0.0052  106 ILE   B CA  
5534 C  C   A ILE   B 106 ? 0.3195 0.2551 0.3174 -0.0355 0.1695  0.0187  106 ILE   B C   
5535 C  C   B ILE   B 106 ? 0.3412 0.3328 0.3232 -0.0013 0.0442  0.0004  106 ILE   B C   
5536 O  O   A ILE   B 106 ? 0.3063 0.2241 0.3182 -0.0341 0.1640  0.0035  106 ILE   B O   
5537 O  O   B ILE   B 106 ? 0.3387 0.3289 0.3169 -0.0022 0.0406  -0.0026 106 ILE   B O   
5538 C  CB  A ILE   B 106 ? 0.3709 0.2632 0.3474 -0.0556 0.1571  0.0477  106 ILE   B CB  
5539 C  CB  B ILE   B 106 ? 0.3582 0.3351 0.3308 -0.0066 0.0413  0.0062  106 ILE   B CB  
5540 C  CG1 A ILE   B 106 ? 0.3802 0.2650 0.3488 -0.0448 0.1460  0.0423  106 ILE   B CG1 
5541 C  CG1 B ILE   B 106 ? 0.3583 0.3328 0.3314 -0.0061 0.0392  0.0063  106 ILE   B CG1 
5542 C  CG2 A ILE   B 106 ? 0.3773 0.2641 0.3703 -0.0697 0.1539  0.0554  106 ILE   B CG2 
5543 C  CG2 B ILE   B 106 ? 0.3605 0.3366 0.3358 -0.0085 0.0416  0.0068  106 ILE   B CG2 
5544 C  CD1 A ILE   B 106 ? 0.3838 0.2678 0.3377 -0.0353 0.1450  0.0420  106 ILE   B CD1 
5545 C  CD1 B ILE   B 106 ? 0.3579 0.3315 0.3304 -0.0049 0.0384  0.0068  106 ILE   B CD1 
5568 N  N   A GLN   B 107 ? 0.3061 0.2775 0.3328 -0.0318 0.1605  0.0203  107 GLN   B N   
5569 N  N   B GLN   B 107 ? 0.3303 0.3324 0.3306 0.0010  0.0484  -0.0003 107 GLN   B N   
5570 C  CA  A GLN   B 107 ? 0.2929 0.2995 0.3442 -0.0271 0.1466  0.0193  107 GLN   B CA  
5571 C  CA  B GLN   B 107 ? 0.3185 0.3295 0.3389 0.0036  0.0530  0.0015  107 GLN   B CA  
5572 C  C   A GLN   B 107 ? 0.2622 0.2796 0.3097 -0.0171 0.1131  0.0083  107 GLN   B C   
5573 C  C   B GLN   B 107 ? 0.2830 0.2993 0.3019 0.0067  0.0671  0.0020  107 GLN   B C   
5574 O  O   A GLN   B 107 ? 0.2552 0.2794 0.3368 -0.0183 0.0865  -0.0113 107 GLN   B O   
5575 O  O   B GLN   B 107 ? 0.2839 0.3023 0.3042 0.0075  0.0583  -0.0049 107 GLN   B O   
5576 C  CB  A GLN   B 107 ? 0.3315 0.3433 0.4216 -0.0237 0.1216  0.0222  107 GLN   B CB  
5577 C  CB  B GLN   B 107 ? 0.3426 0.3549 0.3937 0.0038  0.0405  0.0030  107 GLN   B CB  
5578 C  CG  A GLN   B 107 ? 0.3698 0.3829 0.5001 -0.0150 0.0806  0.0221  107 GLN   B CG  
5579 C  CG  B GLN   B 107 ? 0.3628 0.3757 0.4443 0.0047  0.0267  0.0046  107 GLN   B CG  
5580 C  CD  A GLN   B 107 ? 0.3967 0.4127 0.5658 -0.0112 0.0529  0.0228  107 GLN   B CD  
5581 C  CD  B GLN   B 107 ? 0.3768 0.3903 0.4891 0.0045  0.0172  0.0055  107 GLN   B CD  
5582 O  OE1 A GLN   B 107 ? 0.4060 0.4256 0.5883 -0.0141 0.0487  0.0193  107 GLN   B OE1 
5583 O  OE1 B GLN   B 107 ? 0.3813 0.3950 0.5030 0.0030  0.0158  0.0048  107 GLN   B OE1 
5584 N  NE2 A GLN   B 107 ? 0.4061 0.4204 0.5852 -0.0040 0.0409  0.0278  107 GLN   B NE2 
5585 N  NE2 B GLN   B 107 ? 0.3827 0.3959 0.5033 0.0062  0.0134  0.0071  107 GLN   B NE2 
5602 N  N   . LEU   B 108 ? 0.2452 0.2648 0.2720 0.0112  0.0872  0.0078  108 LEU   B N   
5603 C  CA  . LEU   B 108 ? 0.2216 0.2320 0.2304 0.0285  0.0651  0.0208  108 LEU   B CA  
5604 C  C   . LEU   B 108 ? 0.1872 0.1913 0.2239 0.0246  0.0418  0.0312  108 LEU   B C   
5605 O  O   . LEU   B 108 ? 0.1860 0.1792 0.2193 0.0240  0.0334  0.0281  108 LEU   B O   
5606 C  CB  . LEU   B 108 ? 0.2391 0.2527 0.2205 0.0260  0.0693  0.0265  108 LEU   B CB  
5607 C  CG  . LEU   B 108 ? 0.2582 0.2840 0.2295 0.0264  0.0614  0.0064  108 LEU   B CG  
5608 C  CD1 . LEU   B 108 ? 0.2668 0.2955 0.2201 0.0175  0.0663  0.0093  108 LEU   B CD1 
5609 C  CD2 . LEU   B 108 ? 0.2720 0.3000 0.2529 0.0348  0.0471  -0.0062 108 LEU   B CD2 
5622 N  N   . LEU   B 109 ? 0.1736 0.1700 0.2228 0.0147  0.0341  0.0275  109 LEU   B N   
5623 C  CA  . LEU   B 109 ? 0.1541 0.1439 0.2321 0.0075  0.0291  0.0348  109 LEU   B CA  
5624 C  C   . LEU   B 109 ? 0.1409 0.1320 0.2336 0.0042  0.0272  0.0247  109 LEU   B C   
5625 O  O   . LEU   B 109 ? 0.1415 0.1320 0.2234 0.0036  0.0267  0.0335  109 LEU   B O   
5626 C  CB  . LEU   B 109 ? 0.1609 0.1371 0.2323 0.0069  0.0244  0.0384  109 LEU   B CB  
5627 C  CG  . LEU   B 109 ? 0.1617 0.1329 0.2381 0.0092  0.0184  0.0248  109 LEU   B CG  
5628 C  CD1 . LEU   B 109 ? 0.1590 0.1424 0.2235 0.0120  0.0305  0.0239  109 LEU   B CD1 
5629 C  CD2 . LEU   B 109 ? 0.1720 0.1421 0.2602 0.0091  0.0154  0.0281  109 LEU   B CD2 
5641 N  N   . LYS   B 110 ? 0.1398 0.1321 0.2268 -0.0027 0.0280  0.0237  110 LYS   B N   
5642 C  CA  . LYS   B 110 ? 0.1366 0.1304 0.2247 -0.0021 0.0246  0.0124  110 LYS   B CA  
5643 C  C   . LYS   B 110 ? 0.1320 0.1321 0.2095 -0.0032 0.0259  0.0066  110 LYS   B C   
5644 O  O   . LYS   B 110 ? 0.1307 0.1351 0.2105 -0.0066 0.0210  0.0008  110 LYS   B O   
5645 C  CB  . LYS   B 110 ? 0.1400 0.1281 0.2469 -0.0032 0.0279  0.0095  110 LYS   B CB  
5646 C  CG  . LYS   B 110 ? 0.1395 0.1298 0.2554 -0.0092 0.0164  0.0080  110 LYS   B CG  
5647 C  CD  . LYS   B 110 ? 0.1446 0.1352 0.2539 -0.0111 0.0167  0.0105  110 LYS   B CD  
5648 C  CE  . LYS   B 110 ? 0.1446 0.1443 0.2770 -0.0056 0.0133  0.0066  110 LYS   B CE  
5649 N  NZ  . LYS   B 110 ? 0.1437 0.1554 0.2703 0.0018  0.0038  -0.0008 110 LYS   B NZ  
5663 N  N   . SER   B 111 ? 0.1413 0.1308 0.2266 -0.0012 0.0287  0.0172  111 SER   B N   
5664 C  CA  . SER   B 111 ? 0.1493 0.1325 0.2117 0.0011  0.0258  0.0205  111 SER   B CA  
5665 C  C   . SER   B 111 ? 0.1419 0.1266 0.1995 -0.0006 0.0135  0.0105  111 SER   B C   
5666 O  O   . SER   B 111 ? 0.1332 0.1312 0.2013 -0.0014 0.0113  0.0133  111 SER   B O   
5667 C  CB  . SER   B 111 ? 0.1638 0.1514 0.2199 0.0046  0.0418  0.0249  111 SER   B CB  
5668 O  OG  . SER   B 111 ? 0.1751 0.1917 0.2223 0.0075  0.0446  0.0254  111 SER   B OG  
5674 N  N   . ALA   B 112 ? 0.1323 0.1291 0.1972 0.0040  0.0171  0.0181  112 ALA   B N   
5675 C  CA  . ALA   B 112 ? 0.1306 0.1349 0.1848 0.0025  0.0079  0.0102  112 ALA   B CA  
5676 C  C   . ALA   B 112 ? 0.1224 0.1291 0.1809 0.0006  0.0087  0.0043  112 ALA   B C   
5677 O  O   . ALA   B 112 ? 0.1235 0.1317 0.1933 -0.0066 0.0089  0.0033  112 ALA   B O   
5678 C  CB  . ALA   B 112 ? 0.1350 0.1436 0.1915 0.0062  0.0082  0.0115  112 ALA   B CB  
5684 N  N   . TYR   B 113 ? 0.1246 0.1233 0.1945 -0.0017 0.0126  0.0112  113 TYR   B N   
5685 C  CA  . TYR   B 113 ? 0.1205 0.1176 0.1875 -0.0032 0.0139  0.0022  113 TYR   B CA  
5686 C  C   . TYR   B 113 ? 0.1182 0.1118 0.1865 -0.0068 0.0115  0.0054  113 TYR   B C   
5687 O  O   . TYR   B 113 ? 0.1206 0.1163 0.1786 -0.0059 0.0038  -0.0043 113 TYR   B O   
5688 C  CB  . TYR   B 113 ? 0.1283 0.1191 0.1962 -0.0053 0.0180  0.0113  113 TYR   B CB  
5689 C  CG  . TYR   B 113 ? 0.1260 0.1178 0.2121 -0.0042 0.0129  0.0143  113 TYR   B CG  
5690 C  CD1 . TYR   B 113 ? 0.1337 0.1221 0.2204 -0.0085 0.0166  0.0151  113 TYR   B CD1 
5691 C  CD2 . TYR   B 113 ? 0.1341 0.1234 0.2112 -0.0037 0.0089  0.0083  113 TYR   B CD2 
5692 C  CE1 . TYR   B 113 ? 0.1358 0.1248 0.2132 -0.0018 0.0223  0.0102  113 TYR   B CE1 
5693 C  CE2 . TYR   B 113 ? 0.1397 0.1150 0.2166 0.0001  0.0101  0.0150  113 TYR   B CE2 
5694 C  CZ  . TYR   B 113 ? 0.1319 0.1181 0.2258 0.0048  0.0097  0.0058  113 TYR   B CZ  
5695 O  OH  . TYR   B 113 ? 0.1393 0.1183 0.2564 0.0075  0.0228  0.0091  113 TYR   B OH  
5705 N  N   . GLU   B 114 ? 0.1182 0.1130 0.1966 -0.0040 0.0122  0.0114  114 GLU   B N   
5706 C  CA  . GLU   B 114 ? 0.1159 0.1128 0.2001 0.0024  0.0034  0.0038  114 GLU   B CA  
5707 C  C   . GLU   B 114 ? 0.1189 0.1161 0.1925 -0.0014 0.0074  0.0007  114 GLU   B C   
5708 O  O   . GLU   B 114 ? 0.1182 0.1165 0.1998 -0.0002 0.0046  0.0061  114 GLU   B O   
5709 C  CB  . GLU   B 114 ? 0.1213 0.1152 0.2047 -0.0015 0.0106  0.0085  114 GLU   B CB  
5710 C  CG  . GLU   B 114 ? 0.1258 0.1181 0.1963 -0.0022 0.0072  0.0094  114 GLU   B CG  
5711 C  CD  . GLU   B 114 ? 0.1209 0.1256 0.2074 -0.0053 0.0081  0.0045  114 GLU   B CD  
5712 O  OE1 . GLU   B 114 ? 0.1233 0.1418 0.1998 -0.0091 0.0191  0.0077  114 GLU   B OE1 
5713 O  OE2 . GLU   B 114 ? 0.1223 0.1417 0.2234 -0.0166 0.0148  0.0094  114 GLU   B OE2 
5720 N  N   . ASN   B 115 ? 0.1245 0.1110 0.1896 -0.0043 0.0042  0.0052  115 ASN   B N   
5721 C  CA  . ASN   B 115 ? 0.1235 0.1168 0.1657 -0.0071 0.0006  0.0068  115 ASN   B CA  
5722 C  C   . ASN   B 115 ? 0.1194 0.1159 0.1624 -0.0092 -0.0027 -0.0016 115 ASN   B C   
5723 O  O   . ASN   B 115 ? 0.1323 0.1145 0.1721 -0.0127 0.0019  0.0019  115 ASN   B O   
5724 C  CB  . ASN   B 115 ? 0.1321 0.1289 0.1657 -0.0117 0.0009  0.0042  115 ASN   B CB  
5725 C  CG  . ASN   B 115 ? 0.1442 0.1332 0.1713 0.0014  -0.0013 0.0025  115 ASN   B CG  
5726 O  OD1 . ASN   B 115 ? 0.1781 0.1446 0.1952 -0.0029 0.0131  -0.0101 115 ASN   B OD1 
5727 N  ND2 . ASN   B 115 ? 0.1415 0.1416 0.1673 -0.0018 0.0033  -0.0023 115 ASN   B ND2 
5734 N  N   . PHE   B 116 ? 0.1222 0.1154 0.1529 -0.0053 0.0027  -0.0009 116 PHE   B N   
5735 C  CA  . PHE   B 116 ? 0.1259 0.1178 0.1665 -0.0091 -0.0047 -0.0036 116 PHE   B CA  
5736 C  C   . PHE   B 116 ? 0.1250 0.1098 0.1654 -0.0104 0.0009  0.0018  116 PHE   B C   
5737 O  O   . PHE   B 116 ? 0.1285 0.1176 0.1692 -0.0020 -0.0015 0.0031  116 PHE   B O   
5738 C  CB  . PHE   B 116 ? 0.1219 0.1162 0.1666 -0.0064 -0.0095 0.0030  116 PHE   B CB  
5739 C  CG  . PHE   B 116 ? 0.1184 0.1149 0.1667 -0.0104 -0.0021 0.0018  116 PHE   B CG  
5740 C  CD1 . PHE   B 116 ? 0.1269 0.1198 0.1849 -0.0059 0.0053  0.0049  116 PHE   B CD1 
5741 C  CD2 . PHE   B 116 ? 0.1258 0.1238 0.1691 -0.0045 0.0027  -0.0034 116 PHE   B CD2 
5742 C  CE1 . PHE   B 116 ? 0.1256 0.1250 0.1849 -0.0090 -0.0042 0.0064  116 PHE   B CE1 
5743 C  CE2 . PHE   B 116 ? 0.1268 0.1189 0.1687 -0.0019 0.0039  -0.0033 116 PHE   B CE2 
5744 C  CZ  . PHE   B 116 ? 0.1227 0.1258 0.1787 -0.0090 -0.0057 0.0038  116 PHE   B CZ  
5754 N  N   . ASN   B 117 ? 0.1215 0.1157 0.1790 -0.0041 -0.0025 0.0037  117 ASN   B N   
5755 C  CA  . ASN   B 117 ? 0.1311 0.1187 0.1765 -0.0022 -0.0007 0.0042  117 ASN   B CA  
5756 C  C   . ASN   B 117 ? 0.1296 0.1129 0.1908 0.0012  -0.0039 -0.0011 117 ASN   B C   
5757 O  O   . ASN   B 117 ? 0.1404 0.1222 0.2252 -0.0028 -0.0238 0.0099  117 ASN   B O   
5758 C  CB  . ASN   B 117 ? 0.1307 0.1181 0.1779 -0.0015 -0.0044 0.0000  117 ASN   B CB  
5759 C  CG  . ASN   B 117 ? 0.1238 0.1183 0.1936 0.0035  0.0035  -0.0066 117 ASN   B CG  
5760 O  OD1 . ASN   B 117 ? 0.1470 0.1206 0.2018 -0.0101 0.0071  -0.0051 117 ASN   B OD1 
5761 N  ND2 . ASN   B 117 ? 0.1267 0.1220 0.1950 0.0023  0.0052  -0.0026 117 ASN   B ND2 
5768 N  N   . GLN   B 118 ? 0.1343 0.1101 0.1787 -0.0085 -0.0088 -0.0018 118 GLN   B N   
5769 C  CA  . GLN   B 118 ? 0.1355 0.1194 0.1923 -0.0011 -0.0071 -0.0012 118 GLN   B CA  
5770 C  C   . GLN   B 118 ? 0.1402 0.1166 0.1999 -0.0010 -0.0088 -0.0038 118 GLN   B C   
5771 O  O   . GLN   B 118 ? 0.1569 0.1131 0.2286 -0.0078 0.0049  -0.0000 118 GLN   B O   
5772 C  CB  . GLN   B 118 ? 0.1431 0.1207 0.2002 0.0004  -0.0154 -0.0019 118 GLN   B CB  
5773 C  CG  . GLN   B 118 ? 0.1531 0.1214 0.1895 0.0048  -0.0021 -0.0116 118 GLN   B CG  
5774 C  CD  . GLN   B 118 ? 0.1550 0.1177 0.1982 0.0009  -0.0034 -0.0174 118 GLN   B CD  
5775 O  OE1 . GLN   B 118 ? 0.1624 0.1174 0.2225 0.0050  0.0061  0.0014  118 GLN   B OE1 
5776 N  NE2 . GLN   B 118 ? 0.1578 0.1177 0.2031 0.0031  -0.0053 0.0015  118 GLN   B NE2 
5785 N  N   . HIS   B 119 ? 0.1382 0.1190 0.1725 -0.0085 -0.0052 0.0042  119 HIS   B N   
5786 C  CA  . HIS   B 119 ? 0.1483 0.1306 0.1700 -0.0014 -0.0142 0.0079  119 HIS   B CA  
5787 C  C   . HIS   B 119 ? 0.1501 0.1323 0.1612 -0.0046 -0.0232 0.0067  119 HIS   B C   
5788 O  O   . HIS   B 119 ? 0.1555 0.1285 0.1782 -0.0229 -0.0187 0.0120  119 HIS   B O   
5789 C  CB  . HIS   B 119 ? 0.1507 0.1368 0.1784 0.0024  -0.0204 -0.0019 119 HIS   B CB  
5790 C  CG  . HIS   B 119 ? 0.1538 0.1656 0.1831 0.0102  -0.0334 -0.0152 119 HIS   B CG  
5791 N  ND1 . HIS   B 119 ? 0.1677 0.1840 0.2077 0.0055  -0.0434 -0.0361 119 HIS   B ND1 
5792 C  CD2 . HIS   B 119 ? 0.1707 0.1853 0.1899 0.0356  -0.0374 -0.0167 119 HIS   B CD2 
5793 C  CE1 . HIS   B 119 ? 0.1859 0.2000 0.2179 0.0183  -0.0440 -0.0452 119 HIS   B CE1 
5794 N  NE2 . HIS   B 119 ? 0.1871 0.2093 0.2074 0.0319  -0.0397 -0.0366 119 HIS   B NE2 
5802 N  N   . GLU   B 120 ? 0.1671 0.1360 0.1597 -0.0107 -0.0344 0.0124  120 GLU   B N   
5803 C  CA  . GLU   B 120 ? 0.1980 0.1534 0.1753 -0.0038 -0.0445 0.0277  120 GLU   B CA  
5804 C  C   . GLU   B 120 ? 0.1743 0.1380 0.1665 -0.0113 -0.0327 0.0234  120 GLU   B C   
5805 O  O   . GLU   B 120 ? 0.1680 0.1455 0.1709 -0.0126 -0.0304 0.0064  120 GLU   B O   
5806 C  CB  . GLU   B 120 ? 0.2683 0.1978 0.2483 0.0211  -0.0773 0.0528  120 GLU   B CB  
5807 C  CG  . GLU   B 120 ? 0.3383 0.2830 0.3577 0.0323  -0.1012 0.0761  120 GLU   B CG  
5808 C  CD  . GLU   B 120 ? 0.4027 0.3681 0.4740 0.0328  -0.1033 0.0806  120 GLU   B CD  
5809 O  OE1 . GLU   B 120 ? 0.4300 0.4016 0.5125 0.0292  -0.1018 0.0883  120 GLU   B OE1 
5810 O  OE2 . GLU   B 120 ? 0.4218 0.4090 0.5284 0.0320  -0.0999 0.0732  120 GLU   B OE2 
5817 N  N   . VAL   B 121 ? 0.1674 0.1302 0.1628 -0.0181 -0.0173 0.0153  121 VAL   B N   
5818 C  CA  . VAL   B 121 ? 0.1640 0.1441 0.1483 -0.0191 -0.0201 0.0067  121 VAL   B CA  
5819 C  C   . VAL   B 121 ? 0.1536 0.1367 0.1465 -0.0252 -0.0167 0.0084  121 VAL   B C   
5820 O  O   . VAL   B 121 ? 0.1576 0.1316 0.1750 -0.0286 -0.0199 0.0018  121 VAL   B O   
5821 C  CB  . VAL   B 121 ? 0.1846 0.1788 0.1646 -0.0087 -0.0185 0.0120  121 VAL   B CB  
5822 C  CG1 . VAL   B 121 ? 0.1867 0.1920 0.1901 -0.0190 -0.0130 0.0125  121 VAL   B CG1 
5823 C  CG2 . VAL   B 121 ? 0.2094 0.1983 0.1643 0.0024  -0.0116 -0.0015 121 VAL   B CG2 
5833 N  N   . LEU   B 122 ? 0.1442 0.1310 0.1416 -0.0165 -0.0168 0.0063  122 LEU   B N   
5834 C  CA  . LEU   B 122 ? 0.1357 0.1383 0.1308 -0.0188 -0.0165 0.0058  122 LEU   B CA  
5835 C  C   . LEU   B 122 ? 0.1392 0.1268 0.1376 -0.0237 -0.0149 0.0024  122 LEU   B C   
5836 O  O   . LEU   B 122 ? 0.1466 0.1245 0.1740 -0.0289 -0.0243 0.0016  122 LEU   B O   
5837 C  CB  . LEU   B 122 ? 0.1627 0.1427 0.1662 -0.0053 -0.0215 0.0094  122 LEU   B CB  
5838 C  CG  . LEU   B 122 ? 0.1516 0.1465 0.1691 -0.0155 -0.0084 0.0077  122 LEU   B CG  
5839 C  CD1 . LEU   B 122 ? 0.1523 0.1734 0.1810 -0.0208 -0.0125 0.0009  122 LEU   B CD1 
5840 C  CD2 . LEU   B 122 ? 0.1559 0.1531 0.1505 -0.0115 -0.0083 -0.0031 122 LEU   B CD2 
5852 N  N   . LEU   B 123 ? 0.1404 0.1194 0.1382 -0.0193 -0.0091 0.0026  123 LEU   B N   
5853 C  CA  . LEU   B 123 ? 0.1436 0.1203 0.1474 -0.0235 -0.0170 -0.0037 123 LEU   B CA  
5854 C  C   . LEU   B 123 ? 0.1342 0.1177 0.1427 -0.0304 -0.0166 -0.0004 123 LEU   B C   
5855 O  O   . LEU   B 123 ? 0.1434 0.1210 0.1478 -0.0327 -0.0185 0.0051  123 LEU   B O   
5856 C  CB  . LEU   B 123 ? 0.1459 0.1225 0.1481 -0.0247 -0.0072 -0.0055 123 LEU   B CB  
5857 C  CG  . LEU   B 123 ? 0.1440 0.1309 0.1625 -0.0162 -0.0046 0.0070  123 LEU   B CG  
5858 C  CD1 . LEU   B 123 ? 0.1545 0.1356 0.1746 -0.0168 0.0042  -0.0066 123 LEU   B CD1 
5859 C  CD2 . LEU   B 123 ? 0.1473 0.1369 0.1826 -0.0127 -0.0039 0.0217  123 LEU   B CD2 
5871 N  N   . ALA   B 124 ? 0.1294 0.1212 0.1422 -0.0224 -0.0058 -0.0020 124 ALA   B N   
5872 C  CA  . ALA   B 124 ? 0.1253 0.1223 0.1525 -0.0126 -0.0054 -0.0069 124 ALA   B CA  
5873 C  C   . ALA   B 124 ? 0.1250 0.1174 0.1476 -0.0145 -0.0050 -0.0055 124 ALA   B C   
5874 O  O   . ALA   B 124 ? 0.1344 0.1193 0.1608 -0.0120 -0.0074 -0.0007 124 ALA   B O   
5875 C  CB  . ALA   B 124 ? 0.1380 0.1239 0.1587 -0.0066 -0.0003 -0.0052 124 ALA   B CB  
5881 N  N   . PRO   B 125 ? 0.1322 0.1217 0.1452 -0.0155 -0.0128 0.0084  125 PRO   B N   
5882 C  CA  . PRO   B 125 ? 0.1442 0.1226 0.1526 -0.0138 -0.0126 0.0160  125 PRO   B CA  
5883 C  C   . PRO   B 125 ? 0.1382 0.1149 0.1770 -0.0152 -0.0086 0.0058  125 PRO   B C   
5884 O  O   . PRO   B 125 ? 0.1405 0.1154 0.1909 -0.0094 0.0017  0.0101  125 PRO   B O   
5885 C  CB  . PRO   B 125 ? 0.1482 0.1422 0.1713 -0.0202 -0.0144 0.0276  125 PRO   B CB  
5886 C  CG  . PRO   B 125 ? 0.1515 0.1469 0.1613 -0.0321 -0.0136 0.0155  125 PRO   B CG  
5887 C  CD  . PRO   B 125 ? 0.1440 0.1338 0.1456 -0.0281 -0.0072 0.0058  125 PRO   B CD  
5895 N  N   . LEU   B 126 ? 0.1396 0.1130 0.2016 -0.0143 0.0052  0.0127  126 LEU   B N   
5896 C  CA  . LEU   B 126 ? 0.1465 0.1208 0.2048 -0.0139 0.0216  0.0151  126 LEU   B CA  
5897 C  C   . LEU   B 126 ? 0.1406 0.1282 0.2092 0.0022  0.0216  0.0220  126 LEU   B C   
5898 O  O   . LEU   B 126 ? 0.1636 0.1562 0.2293 0.0149  -0.0045 -0.0029 126 LEU   B O   
5899 C  CB  . LEU   B 126 ? 0.1632 0.1270 0.2336 -0.0152 0.0254  0.0086  126 LEU   B CB  
5900 C  CG  . LEU   B 126 ? 0.1843 0.1313 0.2479 -0.0243 0.0255  -0.0099 126 LEU   B CG  
5901 C  CD1 . LEU   B 126 ? 0.2000 0.1416 0.2994 -0.0234 0.0216  -0.0214 126 LEU   B CD1 
5902 C  CD2 . LEU   B 126 ? 0.1836 0.1481 0.2374 -0.0312 0.0195  -0.0107 126 LEU   B CD2 
5914 N  N   . LEU   B 127 ? 0.1398 0.1215 0.2229 0.0000  0.0246  0.0140  127 LEU   B N   
5915 C  CA  . LEU   B 127 ? 0.1401 0.1313 0.2205 -0.0075 0.0279  0.0198  127 LEU   B CA  
5916 C  C   . LEU   B 127 ? 0.1362 0.1264 0.2156 -0.0010 0.0252  0.0185  127 LEU   B C   
5917 O  O   . LEU   B 127 ? 0.1423 0.1303 0.2262 -0.0142 0.0125  0.0175  127 LEU   B O   
5918 C  CB  . LEU   B 127 ? 0.1525 0.1323 0.2276 -0.0029 0.0297  0.0243  127 LEU   B CB  
5919 C  CG  . LEU   B 127 ? 0.1645 0.1306 0.2295 -0.0012 0.0296  0.0185  127 LEU   B CG  
5920 C  CD1 . LEU   B 127 ? 0.1646 0.1296 0.2342 0.0074  0.0115  0.0115  127 LEU   B CD1 
5921 C  CD2 . LEU   B 127 ? 0.1717 0.1351 0.2451 -0.0102 0.0251  0.0318  127 LEU   B CD2 
5933 N  N   . SER   B 128 ? 0.1414 0.1257 0.2135 -0.0005 0.0064  0.0110  128 SER   B N   
5934 C  CA  . SER   B 128 ? 0.1535 0.1336 0.2079 0.0045  -0.0025 0.0250  128 SER   B CA  
5935 C  C   . SER   B 128 ? 0.1671 0.1357 0.2369 0.0069  -0.0177 0.0194  128 SER   B C   
5936 O  O   . SER   B 128 ? 0.1822 0.1363 0.2668 0.0046  -0.0160 0.0330  128 SER   B O   
5937 C  CB  . SER   B 128 ? 0.1652 0.1403 0.2126 0.0055  0.0024  0.0317  128 SER   B CB  
5938 O  OG  . SER   B 128 ? 0.1737 0.1522 0.2145 0.0123  0.0149  0.0349  128 SER   B OG  
5944 N  N   . ALA   B 129 ? 0.1793 0.1439 0.2618 0.0237  -0.0154 0.0029  129 ALA   B N   
5945 C  CA  . ALA   B 129 ? 0.1957 0.1515 0.2752 0.0288  -0.0134 -0.0048 129 ALA   B CA  
5946 C  C   . ALA   B 129 ? 0.1822 0.1418 0.2618 0.0212  0.0038  0.0034  129 ALA   B C   
5947 O  O   . ALA   B 129 ? 0.1678 0.1458 0.2643 0.0178  0.0024  0.0105  129 ALA   B O   
5948 C  CB  . ALA   B 129 ? 0.2179 0.1751 0.3136 0.0368  -0.0063 -0.0102 129 ALA   B CB  
5954 N  N   . GLY   B 130 ? 0.1798 0.1408 0.2566 0.0245  0.0119  0.0014  130 GLY   B N   
5955 C  CA  . GLY   B 130 ? 0.1798 0.1540 0.2706 0.0238  0.0269  0.0011  130 GLY   B CA  
5956 C  C   . GLY   B 130 ? 0.1826 0.1559 0.2696 0.0176  0.0159  0.0104  130 GLY   B C   
5957 O  O   . GLY   B 130 ? 0.1998 0.1657 0.2735 0.0154  0.0111  0.0182  130 GLY   B O   
5961 N  N   . ILE   B 131 ? 0.1753 0.1658 0.2637 0.0326  0.0150  0.0084  131 ILE   B N   
5962 C  CA  . ILE   B 131 ? 0.1900 0.1810 0.2620 0.0305  -0.0008 0.0184  131 ILE   B CA  
5963 C  C   . ILE   B 131 ? 0.2039 0.1728 0.2243 0.0185  0.0017  0.0197  131 ILE   B C   
5964 O  O   . ILE   B 131 ? 0.2338 0.1918 0.2371 0.0182  -0.0136 0.0192  131 ILE   B O   
5965 C  CB  . ILE   B 131 ? 0.1873 0.2178 0.2963 0.0279  -0.0115 0.0295  131 ILE   B CB  
5966 C  CG1 . ILE   B 131 ? 0.1910 0.2429 0.3106 -0.0006 -0.0003 0.0295  131 ILE   B CG1 
5967 C  CG2 . ILE   B 131 ? 0.1847 0.2365 0.3187 0.0386  -0.0110 0.0259  131 ILE   B CG2 
5968 C  CD1 . ILE   B 131 ? 0.2017 0.2639 0.3237 -0.0190 -0.0055 0.0335  131 ILE   B CD1 
5980 N  N   . PHE   B 132 ? 0.1857 0.1530 0.2230 0.0109  0.0148  0.0251  132 PHE   B N   
5981 C  CA  . PHE   B 132 ? 0.1968 0.1574 0.2206 0.0060  0.0278  0.0147  132 PHE   B CA  
5982 C  C   . PHE   B 132 ? 0.2173 0.1725 0.2440 0.0091  0.0357  0.0137  132 PHE   B C   
5983 O  O   . PHE   B 132 ? 0.2366 0.1916 0.2728 0.0080  0.0527  0.0158  132 PHE   B O   
5984 C  CB  . PHE   B 132 ? 0.1823 0.1580 0.1970 0.0138  0.0297  0.0173  132 PHE   B CB  
5985 C  CG  . PHE   B 132 ? 0.1811 0.1615 0.1908 0.0156  0.0290  0.0234  132 PHE   B CG  
5986 C  CD1 . PHE   B 132 ? 0.1904 0.1623 0.2253 0.0105  0.0280  0.0219  132 PHE   B CD1 
5987 C  CD2 . PHE   B 132 ? 0.1822 0.1671 0.1717 0.0221  0.0207  0.0294  132 PHE   B CD2 
5988 C  CE1 . PHE   B 132 ? 0.1985 0.1673 0.2408 0.0075  0.0209  0.0223  132 PHE   B CE1 
5989 C  CE2 . PHE   B 132 ? 0.1923 0.1681 0.1801 0.0199  0.0162  0.0191  132 PHE   B CE2 
5990 C  CZ  . PHE   B 132 ? 0.1990 0.1653 0.2194 0.0106  0.0068  0.0270  132 PHE   B CZ  
6000 N  N   . GLY   B 133 ? 0.2165 0.1634 0.2461 0.0052  0.0300  0.0397  133 GLY   B N   
6001 C  CA  . GLY   B 133 ? 0.2255 0.1767 0.2482 -0.0149 0.0277  0.0462  133 GLY   B CA  
6002 C  C   . GLY   B 133 ? 0.2304 0.1854 0.2524 -0.0259 0.0350  0.0461  133 GLY   B C   
6003 O  O   . GLY   B 133 ? 0.2501 0.1968 0.3026 -0.0388 0.0361  0.0586  133 GLY   B O   
6007 N  N   . ALA   B 134 ? 0.2115 0.1830 0.2395 -0.0221 0.0342  0.0280  134 ALA   B N   
6008 C  CA  . ALA   B 134 ? 0.2030 0.1800 0.2445 -0.0135 0.0393  0.0169  134 ALA   B CA  
6009 C  C   . ALA   B 134 ? 0.2138 0.1719 0.2570 -0.0079 0.0401  0.0265  134 ALA   B C   
6010 O  O   . ALA   B 134 ? 0.2200 0.1904 0.2751 0.0056  0.0351  0.0177  134 ALA   B O   
6011 C  CB  . ALA   B 134 ? 0.1980 0.1829 0.2678 -0.0041 0.0273  0.0082  134 ALA   B CB  
6017 N  N   . ASP   B 135 ? 0.2259 0.1659 0.2587 -0.0165 0.0228  0.0328  135 ASP   B N   
6018 C  CA  . ASP   B 135 ? 0.2424 0.1575 0.2776 -0.0159 0.0033  0.0323  135 ASP   B CA  
6019 C  C   . ASP   B 135 ? 0.2275 0.1448 0.2636 -0.0029 0.0044  0.0280  135 ASP   B C   
6020 O  O   . ASP   B 135 ? 0.2181 0.1392 0.2677 -0.0054 0.0052  0.0244  135 ASP   B O   
6021 C  CB  . ASP   B 135 ? 0.2694 0.1698 0.3053 -0.0410 0.0033  0.0348  135 ASP   B CB  
6022 C  CG  . ASP   B 135 ? 0.2966 0.1680 0.3456 -0.0630 0.0033  0.0251  135 ASP   B CG  
6023 O  OD1 . ASP   B 135 ? 0.3044 0.1528 0.3360 -0.0460 -0.0002 0.0290  135 ASP   B OD1 
6024 O  OD2 . ASP   B 135 ? 0.3190 0.2050 0.3965 -0.0731 -0.0020 0.0052  135 ASP   B OD2 
6029 N  N   . PRO   B 136 ? 0.2181 0.1465 0.2748 0.0176  -0.0093 0.0269  136 PRO   B N   
6030 C  CA  . PRO   B 136 ? 0.1983 0.1397 0.2687 0.0131  -0.0119 0.0126  136 PRO   B CA  
6031 C  C   . PRO   B 136 ? 0.1780 0.1297 0.2845 0.0122  -0.0101 0.0085  136 PRO   B C   
6032 O  O   . PRO   B 136 ? 0.1620 0.1304 0.2717 0.0082  -0.0000 0.0152  136 PRO   B O   
6033 C  CB  . PRO   B 136 ? 0.2047 0.1592 0.2778 0.0292  -0.0190 0.0001  136 PRO   B CB  
6034 C  CG  . PRO   B 136 ? 0.2239 0.1668 0.2982 0.0329  -0.0111 -0.0013 136 PRO   B CG  
6035 C  CD  . PRO   B 136 ? 0.2254 0.1595 0.2852 0.0354  -0.0049 0.0116  136 PRO   B CD  
6043 N  N   . ILE   B 137 ? 0.1853 0.1272 0.2884 0.0147  -0.0132 0.0070  137 ILE   B N   
6044 C  CA  . ILE   B 137 ? 0.1925 0.1235 0.2996 -0.0035 -0.0065 0.0029  137 ILE   B CA  
6045 C  C   . ILE   B 137 ? 0.1807 0.1294 0.2904 -0.0096 0.0089  0.0168  137 ILE   B C   
6046 O  O   . ILE   B 137 ? 0.1721 0.1309 0.2764 -0.0125 0.0097  0.0110  137 ILE   B O   
6047 C  CB  . ILE   B 137 ? 0.2233 0.1314 0.3390 -0.0084 -0.0083 0.0023  137 ILE   B CB  
6048 C  CG1 . ILE   B 137 ? 0.2578 0.1480 0.3832 0.0021  0.0019  -0.0048 137 ILE   B CG1 
6049 C  CG2 . ILE   B 137 ? 0.2260 0.1354 0.3493 -0.0307 -0.0111 0.0060  137 ILE   B CG2 
6050 C  CD1 . ILE   B 137 ? 0.2790 0.1743 0.4164 0.0154  0.0043  -0.0002 137 ILE   B CD1 
6062 N  N   . HIS   B 138 ? 0.1848 0.1296 0.2953 -0.0079 0.0148  0.0185  138 HIS   B N   
6063 C  CA  . HIS   B 138 ? 0.1951 0.1376 0.2853 -0.0024 0.0286  0.0183  138 HIS   B CA  
6064 C  C   . HIS   B 138 ? 0.1795 0.1346 0.2703 -0.0074 0.0280  0.0246  138 HIS   B C   
6065 O  O   . HIS   B 138 ? 0.1681 0.1438 0.2878 -0.0012 0.0330  0.0352  138 HIS   B O   
6066 C  CB  . HIS   B 138 ? 0.2230 0.1495 0.2898 -0.0035 0.0421  0.0053  138 HIS   B CB  
6067 C  CG  . HIS   B 138 ? 0.2460 0.1647 0.2826 -0.0121 0.0582  0.0283  138 HIS   B CG  
6068 N  ND1 . HIS   B 138 ? 0.2559 0.1848 0.3103 -0.0066 0.0680  0.0183  138 HIS   B ND1 
6069 C  CD2 . HIS   B 138 ? 0.2608 0.1761 0.2830 -0.0134 0.0625  0.0269  138 HIS   B CD2 
6070 C  CE1 . HIS   B 138 ? 0.2630 0.1857 0.2994 -0.0086 0.0761  0.0160  138 HIS   B CE1 
6071 N  NE2 . HIS   B 138 ? 0.2683 0.1757 0.2855 -0.0028 0.0734  0.0104  138 HIS   B NE2 
6079 N  N   . SER   B 139 ? 0.1748 0.1219 0.2677 -0.0008 0.0244  0.0106  139 SER   B N   
6080 C  CA  . SER   B 139 ? 0.1695 0.1201 0.2538 -0.0053 0.0242  0.0003  139 SER   B CA  
6081 C  C   . SER   B 139 ? 0.1453 0.1133 0.2487 -0.0036 0.0174  0.0036  139 SER   B C   
6082 O  O   . SER   B 139 ? 0.1446 0.1157 0.2409 -0.0004 0.0076  0.0124  139 SER   B O   
6083 C  CB  . SER   B 139 ? 0.1780 0.1218 0.2570 0.0004  0.0123  0.0024  139 SER   B CB  
6084 O  OG  . SER   B 139 ? 0.1825 0.1219 0.2540 0.0030  -0.0014 0.0124  139 SER   B OG  
6090 N  N   . LEU   B 140 ? 0.1443 0.1109 0.2445 -0.0086 0.0153  0.0016  140 LEU   B N   
6091 C  CA  . LEU   B 140 ? 0.1432 0.1135 0.2447 -0.0017 0.0116  0.0024  140 LEU   B CA  
6092 C  C   . LEU   B 140 ? 0.1438 0.1162 0.2551 -0.0046 0.0042  -0.0042 140 LEU   B C   
6093 O  O   . LEU   B 140 ? 0.1426 0.1205 0.2606 -0.0028 0.0032  0.0069  140 LEU   B O   
6094 C  CB  . LEU   B 140 ? 0.1404 0.1142 0.2521 -0.0095 0.0142  -0.0090 140 LEU   B CB  
6095 C  CG  . LEU   B 140 ? 0.1535 0.1163 0.2495 -0.0097 0.0063  0.0037  140 LEU   B CG  
6096 C  CD1 . LEU   B 140 ? 0.1616 0.1267 0.2716 -0.0158 0.0090  0.0037  140 LEU   B CD1 
6097 C  CD2 . LEU   B 140 ? 0.1757 0.1281 0.2593 -0.0116 0.0069  -0.0075 140 LEU   B CD2 
6109 N  N   . ARG   B 141 ? 0.1353 0.1165 0.2664 -0.0116 0.0106  -0.0042 141 ARG   B N   
6110 C  CA  . ARG   B 141 ? 0.1382 0.1199 0.2996 -0.0156 0.0273  -0.0044 141 ARG   B CA  
6111 C  C   . ARG   B 141 ? 0.1356 0.1153 0.2859 -0.0134 0.0174  -0.0006 141 ARG   B C   
6112 O  O   . ARG   B 141 ? 0.1434 0.1215 0.2733 -0.0105 0.0070  -0.0123 141 ARG   B O   
6113 C  CB  . ARG   B 141 ? 0.1573 0.1293 0.3247 -0.0182 0.0390  -0.0047 141 ARG   B CB  
6114 C  CG  . ARG   B 141 ? 0.1871 0.1520 0.3400 -0.0222 0.0365  -0.0052 141 ARG   B CG  
6115 C  CD  . ARG   B 141 ? 0.2255 0.1740 0.3377 -0.0164 0.0208  -0.0177 141 ARG   B CD  
6116 N  NE  . ARG   B 141 ? 0.2479 0.1729 0.3308 -0.0295 0.0267  -0.0232 141 ARG   B NE  
6117 C  CZ  . ARG   B 141 ? 0.2612 0.1546 0.3160 -0.0243 0.0350  -0.0294 141 ARG   B CZ  
6118 N  NH1 . ARG   B 141 ? 0.2681 0.1483 0.3114 -0.0232 0.0306  -0.0262 141 ARG   B NH1 
6119 N  NH2 . ARG   B 141 ? 0.2693 0.1656 0.3237 -0.0118 0.0242  -0.0164 141 ARG   B NH2 
6133 N  N   . VAL   B 142 ? 0.1348 0.1157 0.2715 -0.0105 0.0174  -0.0012 142 VAL   B N   
6134 C  CA  . VAL   B 142 ? 0.1307 0.1194 0.2688 -0.0042 0.0180  -0.0022 142 VAL   B CA  
6135 C  C   . VAL   B 142 ? 0.1328 0.1175 0.2606 -0.0030 0.0140  -0.0032 142 VAL   B C   
6136 O  O   . VAL   B 142 ? 0.1395 0.1175 0.2657 -0.0004 0.0172  -0.0003 142 VAL   B O   
6137 C  CB  . VAL   B 142 ? 0.1445 0.1275 0.2728 -0.0006 0.0263  0.0108  142 VAL   B CB  
6138 C  CG1 . VAL   B 142 ? 0.1484 0.1228 0.2687 0.0059  0.0248  0.0029  142 VAL   B CG1 
6139 C  CG2 . VAL   B 142 ? 0.1655 0.1359 0.2817 -0.0026 0.0211  0.0098  142 VAL   B CG2 
6149 N  N   . CYS   B 143 ? 0.1302 0.1171 0.2498 -0.0022 0.0116  0.0034  143 CYS   B N   
6150 C  CA  . CYS   B 143 ? 0.1228 0.1143 0.2503 -0.0104 0.0067  0.0002  143 CYS   B CA  
6151 C  C   . CYS   B 143 ? 0.1191 0.1176 0.2484 -0.0077 0.0083  -0.0043 143 CYS   B C   
6152 O  O   . CYS   B 143 ? 0.1290 0.1212 0.2471 -0.0063 0.0018  -0.0031 143 CYS   B O   
6153 C  CB  . CYS   B 143 ? 0.1330 0.1226 0.2476 -0.0080 0.0024  -0.0054 143 CYS   B CB  
6154 S  SG  . CYS   B 143 ? 0.1348 0.1384 0.2476 -0.0059 0.0075  0.0019  143 CYS   B SG  
6160 N  N   . VAL   B 144 ? 0.1290 0.1208 0.2566 -0.0099 0.0087  -0.0116 144 VAL   B N   
6161 C  CA  . VAL   B 144 ? 0.1361 0.1265 0.2764 -0.0124 -0.0061 -0.0198 144 VAL   B CA  
6162 C  C   . VAL   B 144 ? 0.1359 0.1299 0.2761 -0.0125 -0.0098 -0.0073 144 VAL   B C   
6163 O  O   . VAL   B 144 ? 0.1454 0.1478 0.2898 -0.0023 -0.0045 0.0133  144 VAL   B O   
6164 C  CB  . VAL   B 144 ? 0.1613 0.1406 0.3256 -0.0128 -0.0188 -0.0298 144 VAL   B CB  
6165 C  CG1 . VAL   B 144 ? 0.1838 0.1772 0.3453 -0.0043 -0.0309 -0.0244 144 VAL   B CG1 
6166 C  CG2 . VAL   B 144 ? 0.1783 0.1411 0.3246 -0.0018 -0.0334 -0.0379 144 VAL   B CG2 
6176 N  N   . ASP   B 145 ? 0.1347 0.1215 0.2959 -0.0097 -0.0016 -0.0201 145 ASP   B N   
6177 C  CA  . ASP   B 145 ? 0.1365 0.1288 0.3133 -0.0069 0.0125  -0.0146 145 ASP   B CA  
6178 C  C   . ASP   B 145 ? 0.1309 0.1298 0.2976 -0.0076 0.0168  -0.0156 145 ASP   B C   
6179 O  O   . ASP   B 145 ? 0.1336 0.1476 0.3575 -0.0149 0.0191  -0.0314 145 ASP   B O   
6180 C  CB  . ASP   B 145 ? 0.1470 0.1392 0.3545 -0.0156 0.0284  -0.0145 145 ASP   B CB  
6181 C  CG  . ASP   B 145 ? 0.1626 0.1389 0.4115 -0.0273 0.0361  -0.0100 145 ASP   B CG  
6182 O  OD1 . ASP   B 145 ? 0.1664 0.1429 0.4183 -0.0260 -0.0013 -0.0227 145 ASP   B OD1 
6183 O  OD2 . ASP   B 145 ? 0.1946 0.1419 0.4593 -0.0324 0.0607  0.0013  145 ASP   B OD2 
6188 N  N   . THR   B 146 ? 0.1271 0.1225 0.2528 -0.0104 0.0039  -0.0007 146 THR   B N   
6189 C  CA  . THR   B 146 ? 0.1356 0.1191 0.2310 -0.0084 0.0069  -0.0002 146 THR   B CA  
6190 C  C   . THR   B 146 ? 0.1309 0.1182 0.2263 -0.0051 0.0053  -0.0017 146 THR   B C   
6191 O  O   . THR   B 146 ? 0.1358 0.1187 0.2333 -0.0062 0.0006  -0.0005 146 THR   B O   
6192 C  CB  . THR   B 146 ? 0.1395 0.1168 0.2354 -0.0032 0.0184  -0.0019 146 THR   B CB  
6193 O  OG1 . THR   B 146 ? 0.1438 0.1181 0.2419 -0.0078 0.0252  0.0044  146 THR   B OG1 
6194 C  CG2 . THR   B 146 ? 0.1498 0.1231 0.2348 -0.0051 0.0170  0.0000  146 THR   B CG2 
6202 N  N   . VAL   B 147 ? 0.1344 0.1220 0.2238 -0.0063 0.0106  -0.0026 147 VAL   B N   
6203 C  CA  . VAL   B 147 ? 0.1343 0.1189 0.2116 -0.0115 0.0020  -0.0052 147 VAL   B CA  
6204 C  C   . VAL   B 147 ? 0.1276 0.1193 0.2236 -0.0168 -0.0062 -0.0070 147 VAL   B C   
6205 O  O   . VAL   B 147 ? 0.1405 0.1286 0.2406 -0.0183 -0.0285 -0.0131 147 VAL   B O   
6206 C  CB  . VAL   B 147 ? 0.1385 0.1293 0.1978 -0.0087 -0.0058 -0.0049 147 VAL   B CB  
6207 C  CG1 . VAL   B 147 ? 0.1364 0.1435 0.1867 -0.0100 0.0021  0.0006  147 VAL   B CG1 
6208 C  CG2 . VAL   B 147 ? 0.1435 0.1262 0.2071 -0.0144 0.0021  -0.0013 147 VAL   B CG2 
6218 N  N   . ARG   B 148 ? 0.1351 0.1202 0.2155 -0.0094 -0.0107 -0.0108 148 ARG   B N   
6219 C  CA  . ARG   B 148 ? 0.1369 0.1358 0.2045 -0.0090 -0.0203 -0.0120 148 ARG   B CA  
6220 C  C   . ARG   B 148 ? 0.1429 0.1436 0.1900 -0.0093 -0.0244 -0.0055 148 ARG   B C   
6221 O  O   . ARG   B 148 ? 0.1556 0.1718 0.2042 -0.0244 -0.0344 -0.0037 148 ARG   B O   
6222 C  CB  . ARG   B 148 ? 0.1395 0.1401 0.2096 -0.0085 -0.0252 -0.0182 148 ARG   B CB  
6223 C  CG  . ARG   B 148 ? 0.1401 0.1533 0.2304 -0.0108 -0.0237 -0.0323 148 ARG   B CG  
6224 C  CD  . ARG   B 148 ? 0.1425 0.1653 0.2437 0.0052  -0.0270 -0.0383 148 ARG   B CD  
6225 N  NE  . ARG   B 148 ? 0.1536 0.1688 0.2308 0.0191  -0.0254 -0.0277 148 ARG   B NE  
6226 C  CZ  . ARG   B 148 ? 0.1455 0.1566 0.2054 0.0140  -0.0138 -0.0197 148 ARG   B CZ  
6227 N  NH1 . ARG   B 148 ? 0.1357 0.1631 0.2110 -0.0047 -0.0001 -0.0181 148 ARG   B NH1 
6228 N  NH2 . ARG   B 148 ? 0.1690 0.1400 0.2032 0.0159  -0.0187 -0.0110 148 ARG   B NH2 
6242 N  N   . THR   B 149 ? 0.1466 0.1309 0.1943 -0.0113 -0.0262 -0.0053 149 THR   B N   
6243 C  CA  . THR   B 149 ? 0.1496 0.1376 0.1899 -0.0121 -0.0213 0.0051  149 THR   B CA  
6244 C  C   . THR   B 149 ? 0.1492 0.1354 0.1772 -0.0144 -0.0313 0.0033  149 THR   B C   
6245 O  O   . THR   B 149 ? 0.1537 0.1356 0.1979 -0.0203 -0.0169 0.0050  149 THR   B O   
6246 C  CB  . THR   B 149 ? 0.1492 0.1351 0.1944 -0.0181 -0.0235 -0.0005 149 THR   B CB  
6247 O  OG1 . THR   B 149 ? 0.1533 0.1397 0.1817 -0.0219 -0.0239 -0.0015 149 THR   B OG1 
6248 C  CG2 . THR   B 149 ? 0.1520 0.1383 0.2217 -0.0092 -0.0209 0.0012  149 THR   B CG2 
6256 N  N   . ASN   B 150 ? 0.1575 0.1341 0.1753 -0.0154 -0.0308 -0.0007 150 ASN   B N   
6257 C  CA  . ASN   B 150 ? 0.1622 0.1456 0.1761 -0.0208 -0.0257 -0.0074 150 ASN   B CA  
6258 C  C   . ASN   B 150 ? 0.1560 0.1397 0.1734 -0.0157 -0.0229 -0.0016 150 ASN   B C   
6259 O  O   . ASN   B 150 ? 0.1593 0.1417 0.1939 -0.0265 -0.0351 -0.0041 150 ASN   B O   
6260 C  CB  . ASN   B 150 ? 0.1807 0.1765 0.1789 -0.0194 -0.0280 0.0005  150 ASN   B CB  
6261 C  CG  . ASN   B 150 ? 0.2088 0.2219 0.2160 -0.0173 -0.0360 0.0173  150 ASN   B CG  
6262 O  OD1 . ASN   B 150 ? 0.2179 0.2348 0.2313 -0.0275 -0.0505 0.0083  150 ASN   B OD1 
6263 N  ND2 . ASN   B 150 ? 0.2189 0.2443 0.2503 -0.0045 -0.0387 0.0561  150 ASN   B ND2 
6270 N  N   . VAL   B 151 ? 0.1440 0.1392 0.1736 -0.0156 -0.0197 -0.0029 151 VAL   B N   
6271 C  CA  . VAL   B 151 ? 0.1473 0.1428 0.1693 -0.0197 -0.0153 -0.0062 151 VAL   B CA  
6272 C  C   . VAL   B 151 ? 0.1477 0.1374 0.1684 -0.0267 -0.0230 -0.0064 151 VAL   B C   
6273 O  O   . VAL   B 151 ? 0.1518 0.1408 0.1960 -0.0249 -0.0187 -0.0100 151 VAL   B O   
6274 C  CB  . VAL   B 151 ? 0.1659 0.1526 0.1852 -0.0077 -0.0142 -0.0068 151 VAL   B CB  
6275 C  CG1 . VAL   B 151 ? 0.1738 0.1534 0.2082 -0.0179 -0.0115 -0.0114 151 VAL   B CG1 
6276 C  CG2 . VAL   B 151 ? 0.1772 0.1694 0.1772 0.0025  -0.0132 0.0103  151 VAL   B CG2 
6286 N  N   . TYR   B 152 ? 0.1436 0.1272 0.1628 -0.0212 -0.0152 -0.0075 152 TYR   B N   
6287 C  CA  . TYR   B 152 ? 0.1501 0.1437 0.1499 -0.0268 -0.0127 -0.0110 152 TYR   B CA  
6288 C  C   . TYR   B 152 ? 0.1456 0.1284 0.1503 -0.0243 -0.0078 -0.0110 152 TYR   B C   
6289 O  O   . TYR   B 152 ? 0.1497 0.1285 0.1630 -0.0254 -0.0135 -0.0047 152 TYR   B O   
6290 C  CB  . TYR   B 152 ? 0.1633 0.1553 0.1587 -0.0241 -0.0116 0.0027  152 TYR   B CB  
6291 C  CG  . TYR   B 152 ? 0.1755 0.1595 0.1676 -0.0341 -0.0109 0.0013  152 TYR   B CG  
6292 C  CD1 . TYR   B 152 ? 0.1859 0.1708 0.1672 -0.0295 -0.0203 0.0004  152 TYR   B CD1 
6293 C  CD2 . TYR   B 152 ? 0.1951 0.1808 0.1666 -0.0324 -0.0094 -0.0080 152 TYR   B CD2 
6294 C  CE1 . TYR   B 152 ? 0.2041 0.1896 0.1762 -0.0264 -0.0238 0.0160  152 TYR   B CE1 
6295 C  CE2 . TYR   B 152 ? 0.2047 0.1995 0.1719 -0.0344 -0.0135 -0.0117 152 TYR   B CE2 
6296 C  CZ  . TYR   B 152 ? 0.2127 0.2133 0.1632 -0.0324 -0.0348 0.0141  152 TYR   B CZ  
6297 O  OH  . TYR   B 152 ? 0.2398 0.2483 0.1813 -0.0256 -0.0423 0.0133  152 TYR   B OH  
6307 N  N   . LEU   B 153 ? 0.1414 0.1237 0.1634 -0.0279 -0.0142 -0.0087 153 LEU   B N   
6308 C  CA  . LEU   B 153 ? 0.1479 0.1225 0.1606 -0.0193 -0.0080 -0.0080 153 LEU   B CA  
6309 C  C   . LEU   B 153 ? 0.1479 0.1202 0.1633 -0.0238 -0.0017 -0.0180 153 LEU   B C   
6310 O  O   . LEU   B 153 ? 0.1564 0.1433 0.1832 -0.0143 -0.0108 -0.0321 153 LEU   B O   
6311 C  CB  . LEU   B 153 ? 0.1490 0.1156 0.1774 -0.0212 -0.0024 -0.0083 153 LEU   B CB  
6312 C  CG  . LEU   B 153 ? 0.1434 0.1312 0.2086 -0.0239 -0.0058 -0.0063 153 LEU   B CG  
6313 C  CD1 . LEU   B 153 ? 0.1512 0.1432 0.2232 -0.0239 0.0035  0.0023  153 LEU   B CD1 
6314 C  CD2 . LEU   B 153 ? 0.1446 0.1435 0.2109 -0.0271 0.0118  0.0005  153 LEU   B CD2 
6326 N  N   . ALA   B 154 ? 0.1430 0.1228 0.1766 -0.0107 -0.0123 -0.0123 154 ALA   B N   
6327 C  CA  . ALA   B 154 ? 0.1550 0.1323 0.2061 0.0008  -0.0132 -0.0191 154 ALA   B CA  
6328 C  C   . ALA   B 154 ? 0.1656 0.1378 0.2170 0.0021  -0.0251 -0.0218 154 ALA   B C   
6329 O  O   . ALA   B 154 ? 0.1955 0.1369 0.2194 0.0030  -0.0105 -0.0069 154 ALA   B O   
6330 C  CB  . ALA   B 154 ? 0.1510 0.1473 0.2222 -0.0042 -0.0126 -0.0340 154 ALA   B CB  
6336 N  N   . VAL   B 155 ? 0.1360 0.1287 0.2249 -0.0013 -0.0035 -0.0156 155 VAL   B N   
6337 C  CA  . VAL   B 155 ? 0.1295 0.1268 0.2303 0.0009  -0.0105 -0.0112 155 VAL   B CA  
6338 C  C   . VAL   B 155 ? 0.1361 0.1257 0.2267 -0.0045 -0.0115 -0.0178 155 VAL   B C   
6339 O  O   . VAL   B 155 ? 0.1535 0.1450 0.2676 0.0067  -0.0125 -0.0346 155 VAL   B O   
6340 C  CB  . VAL   B 155 ? 0.1382 0.1409 0.2707 -0.0038 -0.0164 -0.0005 155 VAL   B CB  
6341 C  CG1 . VAL   B 155 ? 0.1425 0.1344 0.2537 -0.0123 -0.0129 -0.0099 155 VAL   B CG1 
6342 C  CG2 . VAL   B 155 ? 0.1314 0.1525 0.2993 -0.0062 -0.0103 0.0297  155 VAL   B CG2 
6352 N  N   . PHE   B 156 ? 0.1278 0.1351 0.2422 0.0035  -0.0092 -0.0143 156 PHE   B N   
6353 C  CA  . PHE   B 156 ? 0.1328 0.1423 0.2802 0.0034  -0.0066 -0.0162 156 PHE   B CA  
6354 C  C   . PHE   B 156 ? 0.1320 0.1493 0.3088 0.0102  -0.0151 -0.0414 156 PHE   B C   
6355 O  O   . PHE   B 156 ? 0.1589 0.1711 0.3444 0.0208  -0.0050 -0.0454 156 PHE   B O   
6356 C  CB  . PHE   B 156 ? 0.1403 0.1409 0.2813 -0.0004 -0.0099 -0.0077 156 PHE   B CB  
6357 C  CG  . PHE   B 156 ? 0.1372 0.1528 0.2864 -0.0010 -0.0095 0.0128  156 PHE   B CG  
6358 C  CD1 . PHE   B 156 ? 0.1438 0.1789 0.3221 0.0028  -0.0052 0.0445  156 PHE   B CD1 
6359 C  CD2 . PHE   B 156 ? 0.1433 0.1662 0.2861 0.0051  -0.0156 0.0179  156 PHE   B CD2 
6360 C  CE1 . PHE   B 156 ? 0.1475 0.1935 0.3325 0.0027  -0.0109 0.0460  156 PHE   B CE1 
6361 C  CE2 . PHE   B 156 ? 0.1548 0.1867 0.3105 0.0101  -0.0189 0.0214  156 PHE   B CE2 
6362 C  CZ  . PHE   B 156 ? 0.1457 0.1962 0.3329 0.0130  -0.0250 0.0315  156 PHE   B CZ  
6372 N  N   . ASP   B 157 ? 0.1321 0.1416 0.3289 0.0103  -0.0232 -0.0244 157 ASP   B N   
6373 C  CA  . ASP   B 157 ? 0.1396 0.1509 0.3613 0.0071  -0.0275 -0.0286 157 ASP   B CA  
6374 C  C   . ASP   B 157 ? 0.1454 0.1472 0.3699 0.0096  -0.0218 -0.0422 157 ASP   B C   
6375 O  O   . ASP   B 157 ? 0.1378 0.1482 0.3625 0.0052  -0.0236 -0.0363 157 ASP   B O   
6376 C  CB  . ASP   B 157 ? 0.1668 0.1771 0.3728 0.0035  -0.0461 -0.0171 157 ASP   B CB  
6377 C  CG  . ASP   B 157 ? 0.2031 0.1919 0.3921 0.0029  -0.0304 -0.0170 157 ASP   B CG  
6378 O  OD1 . ASP   B 157 ? 0.2094 0.1805 0.4090 0.0133  -0.0213 -0.0165 157 ASP   B OD1 
6379 O  OD2 . ASP   B 157 ? 0.2310 0.2150 0.4177 -0.0007 -0.0122 -0.0122 157 ASP   B OD2 
6384 N  N   . LYS   B 158 ? 0.1504 0.1704 0.3803 0.0121  -0.0080 -0.0694 158 LYS   B N   
6385 C  CA  . LYS   B 158 ? 0.1642 0.1904 0.3893 0.0072  -0.0040 -0.0903 158 LYS   B CA  
6386 C  C   . LYS   B 158 ? 0.1636 0.1741 0.3963 0.0055  -0.0106 -0.0875 158 LYS   B C   
6387 O  O   . LYS   B 158 ? 0.1679 0.1737 0.3976 -0.0026 -0.0134 -0.0912 158 LYS   B O   
6388 C  CB  . LYS   B 158 ? 0.1904 0.2329 0.3837 0.0058  0.0116  -0.1154 158 LYS   B CB  
6389 C  CG  . LYS   B 158 ? 0.2312 0.2834 0.3939 0.0071  0.0202  -0.1235 158 LYS   B CG  
6390 C  CD  . LYS   B 158 ? 0.2646 0.3294 0.4069 0.0066  0.0269  -0.1193 158 LYS   B CD  
6391 C  CE  . LYS   B 158 ? 0.2870 0.3734 0.4269 0.0109  0.0250  -0.1083 158 LYS   B CE  
6392 N  NZ  . LYS   B 158 ? 0.2975 0.3910 0.4346 0.0113  0.0271  -0.1017 158 LYS   B NZ  
6406 N  N   . ASN   B 159 ? 0.1673 0.1648 0.4094 0.0057  -0.0219 -0.0675 159 ASN   B N   
6407 C  CA  . ASN   B 159 ? 0.1771 0.1560 0.4231 0.0178  -0.0338 -0.0533 159 ASN   B CA  
6408 C  C   . ASN   B 159 ? 0.1630 0.1439 0.4207 0.0115  -0.0433 -0.0444 159 ASN   B C   
6409 O  O   . ASN   B 159 ? 0.1712 0.1404 0.4380 -0.0071 -0.0457 -0.0399 159 ASN   B O   
6410 C  CB  . ASN   B 159 ? 0.2010 0.1685 0.4406 0.0243  -0.0341 -0.0455 159 ASN   B CB  
6411 C  CG  . ASN   B 159 ? 0.2312 0.1885 0.4686 0.0241  -0.0418 -0.0607 159 ASN   B CG  
6412 O  OD1 . ASN   B 159 ? 0.2480 0.1976 0.4630 0.0311  -0.0415 -0.0692 159 ASN   B OD1 
6413 N  ND2 . ASN   B 159 ? 0.2352 0.2013 0.4775 0.0285  -0.0475 -0.0551 159 ASN   B ND2 
6420 N  N   . LEU   B 160 ? 0.1487 0.1416 0.4010 0.0055  -0.0419 -0.0429 160 LEU   B N   
6421 C  CA  . LEU   B 160 ? 0.1510 0.1465 0.3637 0.0093  -0.0368 -0.0215 160 LEU   B CA  
6422 C  C   . LEU   B 160 ? 0.1484 0.1367 0.3503 0.0030  -0.0255 -0.0296 160 LEU   B C   
6423 O  O   . LEU   B 160 ? 0.1367 0.1395 0.3358 0.0000  -0.0331 -0.0206 160 LEU   B O   
6424 C  CB  . LEU   B 160 ? 0.1506 0.1552 0.3400 0.0047  -0.0331 -0.0129 160 LEU   B CB  
6425 C  CG  . LEU   B 160 ? 0.1527 0.1661 0.3103 0.0073  -0.0338 -0.0020 160 LEU   B CG  
6426 C  CD1 . LEU   B 160 ? 0.1675 0.1832 0.3073 -0.0035 -0.0171 -0.0029 160 LEU   B CD1 
6427 C  CD2 . LEU   B 160 ? 0.1586 0.1726 0.3013 0.0205  -0.0402 -0.0112 160 LEU   B CD2 
6439 N  N   . TYR   B 161 ? 0.1443 0.1437 0.3428 -0.0032 -0.0038 -0.0410 161 TYR   B N   
6440 C  CA  . TYR   B 161 ? 0.1511 0.1413 0.3275 -0.0099 0.0124  -0.0433 161 TYR   B CA  
6441 C  C   . TYR   B 161 ? 0.1549 0.1400 0.3252 -0.0118 0.0111  -0.0404 161 TYR   B C   
6442 O  O   . TYR   B 161 ? 0.1562 0.1406 0.3138 -0.0172 0.0026  -0.0362 161 TYR   B O   
6443 C  CB  . TYR   B 161 ? 0.1677 0.1517 0.3240 -0.0179 0.0291  -0.0484 161 TYR   B CB  
6444 C  CG  . TYR   B 161 ? 0.1916 0.1568 0.3173 -0.0246 0.0395  -0.0620 161 TYR   B CG  
6445 C  CD1 . TYR   B 161 ? 0.1972 0.1538 0.3164 -0.0400 0.0417  -0.0594 161 TYR   B CD1 
6446 C  CD2 . TYR   B 161 ? 0.2164 0.1676 0.3058 -0.0276 0.0336  -0.0670 161 TYR   B CD2 
6447 C  CE1 . TYR   B 161 ? 0.2189 0.1746 0.3196 -0.0423 0.0427  -0.0529 161 TYR   B CE1 
6448 C  CE2 . TYR   B 161 ? 0.2331 0.1827 0.3120 -0.0346 0.0358  -0.0656 161 TYR   B CE2 
6449 C  CZ  . TYR   B 161 ? 0.2331 0.1885 0.3153 -0.0474 0.0338  -0.0533 161 TYR   B CZ  
6450 O  OH  . TYR   B 161 ? 0.2602 0.2129 0.3367 -0.0468 0.0330  -0.0465 161 TYR   B OH  
6460 N  N   . ASP   B 162 ? 0.1604 0.1371 0.3411 -0.0082 0.0009  -0.0553 162 ASP   B N   
6461 C  CA  . ASP   B 162 ? 0.1719 0.1474 0.3429 -0.0050 -0.0026 -0.0560 162 ASP   B CA  
6462 C  C   . ASP   B 162 ? 0.1683 0.1415 0.3302 -0.0081 -0.0067 -0.0408 162 ASP   B C   
6463 O  O   . ASP   B 162 ? 0.1737 0.1441 0.3299 -0.0134 -0.0214 -0.0364 162 ASP   B O   
6464 C  CB  . ASP   B 162 ? 0.1884 0.1677 0.3620 -0.0025 -0.0059 -0.0772 162 ASP   B CB  
6465 C  CG  . ASP   B 162 ? 0.1922 0.1979 0.3823 0.0059  -0.0062 -0.0880 162 ASP   B CG  
6466 O  OD1 . ASP   B 162 ? 0.1979 0.2187 0.3756 -0.0009 0.0186  -0.0860 162 ASP   B OD1 
6467 O  OD2 . ASP   B 162 ? 0.2050 0.2159 0.4113 0.0246  -0.0100 -0.0897 162 ASP   B OD2 
6472 N  N   A LYS   B 163 ? 0.1612 0.1228 0.3198 -0.0103 -0.0212 -0.0300 163 LYS   B N   
6473 N  N   B LYS   B 163 ? 0.1767 0.1579 0.3199 -0.0087 -0.0108 -0.0282 163 LYS   B N   
6474 C  CA  A LYS   B 163 ? 0.1725 0.1303 0.3250 -0.0176 -0.0176 -0.0120 163 LYS   B CA  
6475 C  CA  B LYS   B 163 ? 0.1904 0.1778 0.3202 -0.0104 -0.0119 -0.0150 163 LYS   B CA  
6476 C  C   A LYS   B 163 ? 0.1447 0.1248 0.3140 -0.0173 -0.0226 -0.0047 163 LYS   B C   
6477 C  C   B LYS   B 163 ? 0.1633 0.1546 0.3020 -0.0120 -0.0173 -0.0066 163 LYS   B C   
6478 O  O   A LYS   B 163 ? 0.1400 0.1380 0.3462 -0.0195 -0.0213 -0.0064 163 LYS   B O   
6479 O  O   B LYS   B 163 ? 0.1652 0.1593 0.3038 -0.0121 -0.0163 -0.0023 163 LYS   B O   
6480 C  CB  A LYS   B 163 ? 0.2173 0.1586 0.3530 -0.0169 -0.0091 0.0029  163 LYS   B CB  
6481 C  CB  B LYS   B 163 ? 0.2313 0.2208 0.3455 -0.0099 -0.0094 -0.0089 163 LYS   B CB  
6482 C  CG  A LYS   B 163 ? 0.2827 0.2252 0.3936 -0.0218 -0.0039 0.0088  163 LYS   B CG  
6483 C  CG  B LYS   B 163 ? 0.2728 0.2641 0.3812 -0.0106 -0.0073 -0.0046 163 LYS   B CG  
6484 C  CD  A LYS   B 163 ? 0.3513 0.2767 0.4445 -0.0313 -0.0034 0.0026  163 LYS   B CD  
6485 C  CD  B LYS   B 163 ? 0.3081 0.3001 0.4215 -0.0124 -0.0055 -0.0035 163 LYS   B CD  
6486 C  CE  A LYS   B 163 ? 0.4047 0.3305 0.4758 -0.0349 0.0019  0.0017  163 LYS   B CE  
6487 C  CE  B LYS   B 163 ? 0.3418 0.3367 0.4530 -0.0135 -0.0029 -0.0025 163 LYS   B CE  
6488 N  NZ  A LYS   B 163 ? 0.4370 0.3540 0.5016 -0.0354 0.0024  -0.0025 163 LYS   B NZ  
6489 N  NZ  B LYS   B 163 ? 0.3526 0.3481 0.4743 -0.0138 -0.0025 -0.0029 163 LYS   B NZ  
6516 N  N   . LEU   B 164 ? 0.1381 0.1330 0.2970 -0.0142 -0.0231 -0.0051 164 LEU   B N   
6517 C  CA  . LEU   B 164 ? 0.1390 0.1301 0.2762 -0.0124 -0.0240 -0.0038 164 LEU   B CA  
6518 C  C   . LEU   B 164 ? 0.1455 0.1283 0.2790 -0.0172 -0.0293 0.0003  164 LEU   B C   
6519 O  O   . LEU   B 164 ? 0.1456 0.1506 0.2990 -0.0154 -0.0300 -0.0030 164 LEU   B O   
6520 C  CB  . LEU   B 164 ? 0.1395 0.1266 0.2607 -0.0153 -0.0202 -0.0026 164 LEU   B CB  
6521 C  CG  . LEU   B 164 ? 0.1483 0.1423 0.2660 -0.0117 -0.0063 0.0005  164 LEU   B CG  
6522 C  CD1 . LEU   B 164 ? 0.1513 0.1408 0.2600 -0.0154 -0.0164 -0.0102 164 LEU   B CD1 
6523 C  CD2 . LEU   B 164 ? 0.1625 0.1770 0.2741 -0.0110 0.0036  -0.0102 164 LEU   B CD2 
6536 N  N   . VAL   B 165 ? 0.1720 0.1374 0.3037 -0.0247 -0.0349 -0.0131 165 VAL   B N   
6537 C  CA  . VAL   B 165 ? 0.2100 0.1513 0.3016 -0.0303 -0.0562 -0.0123 165 VAL   B CA  
6538 C  C   . VAL   B 165 ? 0.2368 0.1613 0.3294 -0.0380 -0.0835 -0.0098 165 VAL   B C   
6539 O  O   . VAL   B 165 ? 0.2551 0.1750 0.3381 -0.0408 -0.0898 -0.0061 165 VAL   B O   
6540 C  CB  . VAL   B 165 ? 0.2314 0.1741 0.3006 -0.0168 -0.0249 -0.0164 165 VAL   B CB  
6541 C  CG1 . VAL   B 165 ? 0.2470 0.1849 0.3215 -0.0195 -0.0149 -0.0080 165 VAL   B CG1 
6542 C  CG2 . VAL   B 165 ? 0.2273 0.1805 0.2862 -0.0141 -0.0135 -0.0127 165 VAL   B CG2 
6552 N  N   . SER   B 166 ? 0.2447 0.1517 0.3610 -0.0377 -0.0857 -0.0277 166 SER   B N   
6553 C  CA  . SER   B 166 ? 0.2402 0.1555 0.4067 -0.0367 -0.0739 -0.0374 166 SER   B CA  
6554 C  C   . SER   B 166 ? 0.2234 0.1667 0.4246 -0.0398 -0.0765 -0.0130 166 SER   B C   
6555 O  O   . SER   B 166 ? 0.2260 0.1866 0.4559 -0.0523 -0.0864 -0.0359 166 SER   B O   
6556 C  CB  . SER   B 166 ? 0.2415 0.1620 0.4272 -0.0255 -0.0688 -0.0460 166 SER   B CB  
6557 O  OG  . SER   B 166 ? 0.2294 0.1550 0.4394 -0.0231 -0.0711 -0.0253 166 SER   B OG  
6563 N  N   . SER   B 167 ? 0.2043 0.1579 0.3963 -0.0415 -0.0790 0.0277  167 SER   B N   
6564 C  CA  . SER   B 167 ? 0.1953 0.1620 0.3863 -0.0372 -0.0503 0.0229  167 SER   B CA  
6565 C  C   . SER   B 167 ? 0.1897 0.1699 0.3692 -0.0456 -0.0427 0.0408  167 SER   B C   
6566 O  O   . SER   B 167 ? 0.1880 0.1797 0.3666 -0.0463 -0.0380 0.0392  167 SER   B O   
6567 C  CB  . SER   B 167 ? 0.1833 0.1685 0.3841 -0.0317 -0.0168 0.0117  167 SER   B CB  
6568 O  OG  . SER   B 167 ? 0.1727 0.1772 0.3736 -0.0206 -0.0030 0.0122  167 SER   B OG  
6574 N  N   . PHE   B 168 ? 0.1865 0.1662 0.3528 -0.0433 -0.0352 0.0500  168 PHE   B N   
6575 C  CA  . PHE   B 168 ? 0.1925 0.1627 0.3223 -0.0461 -0.0344 0.0307  168 PHE   B CA  
6576 C  C   . PHE   B 168 ? 0.1700 0.1497 0.2843 -0.0242 -0.0098 0.0153  168 PHE   B C   
6577 O  O   . PHE   B 168 ? 0.1897 0.1473 0.2900 -0.0006 -0.0105 -0.0056 168 PHE   B O   
6578 C  CB  . PHE   B 168 ? 0.2105 0.1682 0.3288 -0.0547 -0.0464 0.0451  168 PHE   B CB  
6579 C  CG  . PHE   B 168 ? 0.2323 0.1615 0.3183 -0.0548 -0.0478 0.0221  168 PHE   B CG  
6580 C  CD1 . PHE   B 168 ? 0.2586 0.1648 0.3214 -0.0486 -0.0507 0.0213  168 PHE   B CD1 
6581 C  CD2 . PHE   B 168 ? 0.2224 0.1589 0.3076 -0.0493 -0.0492 0.0242  168 PHE   B CD2 
6582 C  CE1 . PHE   B 168 ? 0.2705 0.1750 0.3142 -0.0361 -0.0464 0.0222  168 PHE   B CE1 
6583 C  CE2 . PHE   B 168 ? 0.2458 0.1655 0.3067 -0.0345 -0.0546 0.0228  168 PHE   B CE2 
6584 C  CZ  . PHE   B 168 ? 0.2596 0.1622 0.3043 -0.0245 -0.0563 0.0283  168 PHE   B CZ  
6594 N  N   . LEU   B 169 ? 0.1729 0.1634 0.2736 -0.0070 0.0064  0.0011  169 LEU   B N   
6595 C  CA  . LEU   B 169 ? 0.1909 0.1968 0.2989 -0.0109 0.0042  -0.0277 169 LEU   B CA  
6596 C  C   . LEU   B 169 ? 0.2147 0.2209 0.3478 0.0032  -0.0007 -0.0551 169 LEU   B C   
6597 O  O   . LEU   B 169 ? 0.2380 0.2439 0.3975 0.0012  -0.0039 -0.0786 169 LEU   B O   
6598 C  CB  . LEU   B 169 ? 0.2121 0.2362 0.3098 -0.0183 0.0030  -0.0064 169 LEU   B CB  
6599 C  CG  . LEU   B 169 ? 0.2506 0.2727 0.3473 -0.0095 0.0048  0.0011  169 LEU   B CG  
6600 C  CD1 . LEU   B 169 ? 0.2649 0.2952 0.3504 -0.0078 0.0011  0.0131  169 LEU   B CD1 
6601 C  CD2 . LEU   B 169 ? 0.2446 0.2778 0.3496 0.0033  0.0209  -0.0118 169 LEU   B CD2 
6602 O  OXT . LEU   B 169 ? 0.2306 0.2364 0.3490 0.0303  -0.0007 -0.0503 169 LEU   B OXT 
6614 C  C1  T TFA   C .   ? 0.1310 0.1542 0.1371 -0.0068 0.0148  0.0203  201 TFA   A C1  
6615 C  C2  T TFA   C .   ? 0.1608 0.1841 0.1750 -0.0155 0.0100  0.0046  201 TFA   A C2  
6616 O  O   T TFA   C .   ? 0.1028 0.1353 0.1270 -0.0069 0.0213  0.0319  201 TFA   A O   
6617 F  F1  T TFA   C .   ? 0.1713 0.1938 0.1926 -0.0133 0.0031  0.0048  201 TFA   A F1  
6618 F  F2  T TFA   C .   ? 0.1696 0.1909 0.1795 -0.0161 0.0100  0.0117  201 TFA   A F2  
6619 F  F3  T TFA   C .   ? 0.1750 0.1992 0.1965 -0.0269 0.0228  -0.0164 201 TFA   A F3  
6620 O  OXT T TFA   C .   ? 0.1340 0.1546 0.1516 0.0092  0.0161  0.0247  201 TFA   A OXT 
6621 S  S   B DMS   D .   ? 0.2930 0.3271 0.3293 -0.0053 0.0416  0.0147  202 DMS   A S   
6622 O  O   B DMS   D .   ? 0.2945 0.3295 0.3288 -0.0057 0.0400  0.0145  202 DMS   A O   
6623 C  C1  B DMS   D .   ? 0.2939 0.3273 0.3337 -0.0053 0.0380  0.0094  202 DMS   A C1  
6624 C  C2  B DMS   D .   ? 0.2946 0.3295 0.3361 -0.0034 0.0416  0.0112  202 DMS   A C2  
6631 N  N2  B A1A8X E .   ? 0.1622 0.1760 0.1322 0.0011  0.0111  0.0284  203 A1A8X A N2  
6632 C  C3  B A1A8X E .   ? 0.1854 0.1808 0.1542 -0.0066 -0.0060 0.0121  203 A1A8X A C3  
6633 C  C6  B A1A8X E .   ? 0.1650 0.1736 0.1423 0.0072  0.0036  0.0142  203 A1A8X A C6  
6634 C  C9  B A1A8X E .   ? 0.1502 0.1736 0.1281 0.0038  0.0033  0.0162  203 A1A8X A C9  
6635 C  C1  B A1A8X E .   ? 0.1784 0.1658 0.1543 -0.0041 -0.0024 0.0227  203 A1A8X A C1  
6636 C  C10 B A1A8X E .   ? 0.1399 0.1749 0.1309 0.0019  0.0043  0.0156  203 A1A8X A C10 
6637 C  C11 B A1A8X E .   ? 0.1222 0.1735 0.1312 -0.0026 -0.0033 0.0196  203 A1A8X A C11 
6638 C  C2  B A1A8X E .   ? 0.1815 0.1769 0.1502 -0.0071 -0.0028 0.0205  203 A1A8X A C2  
6639 C  C4  B A1A8X E .   ? 0.1853 0.1786 0.1602 -0.0011 -0.0025 0.0011  203 A1A8X A C4  
6640 C  C5  B A1A8X E .   ? 0.1804 0.1715 0.1546 0.0031  0.0023  0.0077  203 A1A8X A C5  
6641 C  C7  B A1A8X E .   ? 0.1538 0.1764 0.1033 0.0063  0.0181  0.0409  203 A1A8X A C7  
6642 C  C8  B A1A8X E .   ? 0.1423 0.1793 0.1277 0.0051  0.0010  0.0185  203 A1A8X A C8  
6643 N  N1  B A1A8X E .   ? 0.1757 0.1741 0.1548 0.0091  0.0045  0.0001  203 A1A8X A N1  
6644 N  N3  B A1A8X E .   ? 0.1508 0.1831 0.1236 0.0087  0.0071  0.0249  203 A1A8X A N3  
6645 N  N4  B A1A8X E .   ? 0.1229 0.1782 0.1256 0.0003  -0.0050 0.0166  203 A1A8X A N4  
6646 O  O1  B A1A8X E .   ? 0.1753 0.1551 0.1523 -0.0071 -0.0105 0.0371  203 A1A8X A O1  
6661 CL CL  B CL    F .   ? 0.2067 0.1464 0.3233 -0.0293 -0.0144 -0.0102 204 CL    A CL  
6662 O  O   . HOH   G .   ? 0.2687 0.4987 0.6154 0.0823  0.0875  0.0868  301 HOH   A O   
6663 O  O   . HOH   G .   ? 0.3842 0.7347 0.4647 -0.1227 0.0200  0.0816  302 HOH   A O   
6664 O  O   A HOH   G .   ? 0.3271 0.2147 0.3231 -0.0181 0.0297  0.0431  303 HOH   A O   
6665 O  O   B HOH   G .   ? 0.3890 0.5443 0.3433 0.0550  -0.0120 0.0311  304 HOH   A O   
6666 O  O   . HOH   G .   ? 0.6269 0.4878 0.3287 0.2414  -0.1187 0.0364  305 HOH   A O   
6667 O  O   . HOH   G .   ? 0.2620 0.3281 0.3181 -0.0278 0.0848  -0.0337 306 HOH   A O   
6668 O  O   . HOH   G .   ? 0.2793 0.6586 0.5334 -0.0323 -0.0677 0.1807  307 HOH   A O   
6669 O  O   . HOH   G .   ? 0.6728 0.5349 0.4120 -0.0534 0.0651  0.1759  308 HOH   A O   
6670 O  O   . HOH   G .   ? 0.4395 0.3540 0.5060 -0.0603 0.1350  -0.0788 309 HOH   A O   
6671 O  O   . HOH   G .   ? 0.5547 0.3446 0.4902 -0.0751 0.1668  0.0807  310 HOH   A O   
6672 O  O   . HOH   G .   ? 0.1733 0.1670 0.2030 0.0181  -0.0205 0.0205  311 HOH   A O   
6673 O  O   . HOH   G .   ? 0.3004 0.3053 0.1862 -0.0433 0.0429  0.0485  312 HOH   A O   
6674 O  O   . HOH   G .   ? 0.2782 0.2655 0.4218 -0.0293 -0.1130 0.1104  313 HOH   A O   
6675 O  O   . HOH   G .   ? 0.2207 0.2327 0.4598 0.0102  -0.0419 -0.0817 314 HOH   A O   
6676 O  O   . HOH   G .   ? 0.1839 0.3427 0.4268 -0.0264 0.0369  -0.1270 315 HOH   A O   
6677 O  O   . HOH   G .   ? 0.1698 0.1332 0.1597 -0.0168 0.0109  -0.0028 316 HOH   A O   
6678 O  O   . HOH   G .   ? 0.2617 0.5012 0.3437 0.0262  -0.0696 0.0532  317 HOH   A O   
6679 O  O   . HOH   G .   ? 0.2447 0.3531 0.4692 -0.0245 0.0898  0.1851  318 HOH   A O   
6680 O  O   . HOH   G .   ? 0.1996 0.1862 0.3550 -0.0433 0.0044  -0.0186 319 HOH   A O   
6681 O  O   . HOH   G .   ? 0.6692 0.5168 0.3657 -0.0241 -0.0885 0.1355  320 HOH   A O   
6682 O  O   . HOH   G .   ? 0.5016 0.4055 0.4706 0.0769  0.0864  -0.1257 321 HOH   A O   
6683 O  O   . HOH   G .   ? 0.3239 0.4542 0.2837 -0.0401 0.0666  0.0253  322 HOH   A O   
6684 O  O   . HOH   G .   ? 0.2956 0.3509 0.4166 -0.0556 0.1464  -0.0227 323 HOH   A O   
6685 O  O   . HOH   G .   ? 0.3358 0.2963 0.2631 -0.1143 0.0201  0.0612  324 HOH   A O   
6686 O  O   . HOH   G .   ? 0.3974 0.3200 0.3734 -0.0655 0.1704  0.0227  325 HOH   A O   
6687 O  O   . HOH   G .   ? 0.1599 0.4263 0.3070 0.0650  -0.0010 0.0466  326 HOH   A O   
6688 O  O   . HOH   G .   ? 0.3915 0.4025 0.3162 0.1644  -0.0859 -0.1245 327 HOH   A O   
6689 O  O   . HOH   G .   ? 0.8126 0.6559 0.7341 -0.0903 0.0922  -0.0432 328 HOH   A O   
6690 O  O   . HOH   G .   ? 0.1502 0.1462 0.2296 -0.0222 0.0078  0.0015  329 HOH   A O   
6691 O  O   . HOH   G .   ? 0.5561 0.3582 0.2883 -0.0737 -0.0741 -0.0393 330 HOH   A O   
6692 O  O   . HOH   G .   ? 0.5563 0.5997 0.4191 -0.1299 -0.1117 -0.0845 331 HOH   A O   
6693 O  O   . HOH   G .   ? 0.2400 0.2346 0.2579 0.0319  0.0275  0.0418  332 HOH   A O   
6694 O  O   B HOH   G .   ? 0.2436 0.2130 0.3412 -0.0168 0.1415  -0.0579 333 HOH   A O   
6695 O  O   . HOH   G .   ? 0.3023 0.6032 0.4417 0.0704  -0.0094 0.1787  334 HOH   A O   
6696 O  O   . HOH   G .   ? 0.2031 0.1632 0.1414 -0.0049 0.0184  0.0115  335 HOH   A O   
6697 O  O   . HOH   G .   ? 0.5303 0.5329 0.2976 -0.0932 0.1777  0.0872  336 HOH   A O   
6698 O  O   . HOH   G .   ? 0.4888 0.2108 0.4923 0.0403  -0.1364 0.0955  337 HOH   A O   
6699 O  O   . HOH   G .   ? 0.1470 0.3948 0.2441 0.0058  0.0273  0.0570  338 HOH   A O   
6700 O  O   . HOH   G .   ? 0.2748 0.3333 0.3375 -0.1101 0.0900  -0.0225 339 HOH   A O   
6701 O  O   . HOH   G .   ? 0.4827 0.3970 0.4142 -0.1812 -0.0914 0.1969  340 HOH   A O   
6702 O  O   . HOH   G .   ? 0.3494 0.4496 0.3896 0.2005  0.0509  0.0187  341 HOH   A O   
6703 O  O   . HOH   G .   ? 0.5180 0.1902 0.5190 0.0572  -0.0116 0.0072  342 HOH   A O   
6704 O  O   . HOH   G .   ? 0.2163 0.4653 0.3867 0.0037  -0.0501 0.1639  343 HOH   A O   
6705 O  O   A HOH   G .   ? 0.2263 0.2304 0.2508 -0.0472 0.0498  0.0449  344 HOH   A O   
6706 O  O   . HOH   G .   ? 0.2386 0.3905 0.3457 0.0962  -0.0517 -0.0059 345 HOH   A O   
6707 O  O   . HOH   G .   ? 0.3778 0.3444 0.3723 -0.0358 -0.0035 -0.0823 346 HOH   A O   
6708 O  O   . HOH   G .   ? 0.2677 0.3878 0.3461 -0.0922 -0.0611 -0.0446 347 HOH   A O   
6709 O  O   . HOH   G .   ? 0.6189 0.4044 0.5923 0.0043  -0.0860 0.0485  348 HOH   A O   
6710 O  O   . HOH   G .   ? 0.4446 0.4577 0.5986 0.1118  0.1542  -0.0733 349 HOH   A O   
6711 O  O   . HOH   G .   ? 0.1915 0.2137 0.3124 -0.0005 -0.0365 0.0365  350 HOH   A O   
6712 O  O   . HOH   G .   ? 0.1919 0.1974 0.3699 0.0161  0.0860  -0.0169 351 HOH   A O   
6713 O  O   . HOH   G .   ? 0.3085 0.3838 0.2135 -0.1142 -0.0150 -0.0670 352 HOH   A O   
6714 O  O   . HOH   G .   ? 0.3159 0.3176 0.2169 0.0081  -0.0784 0.0253  353 HOH   A O   
6715 O  O   . HOH   G .   ? 0.5958 0.4346 0.3850 -0.0791 0.1187  0.1728  354 HOH   A O   
6716 O  O   . HOH   G .   ? 0.5480 0.4701 0.4978 0.0688  0.2060  -0.0837 355 HOH   A O   
6717 O  O   . HOH   G .   ? 0.2399 0.2030 0.2350 -0.0237 -0.0014 -0.0061 356 HOH   A O   
6718 O  O   B HOH   G .   ? 0.1918 0.2580 0.1803 0.1198  0.0300  0.0718  357 HOH   A O   
6719 O  O   . HOH   G .   ? 0.1421 0.2221 0.2195 0.0071  -0.0097 0.0503  358 HOH   A O   
6720 O  O   . HOH   G .   ? 0.1994 0.1668 0.2331 0.0198  -0.0325 -0.0001 359 HOH   A O   
6721 O  O   A HOH   G .   ? 0.1526 0.2043 0.1926 0.0423  0.0317  0.0459  360 HOH   A O   
6722 O  O   B HOH   G .   ? 0.2705 0.2928 0.2902 -0.0171 0.0067  -0.0885 361 HOH   A O   
6723 O  O   . HOH   G .   ? 0.6078 0.4082 0.3017 -0.0424 -0.0044 0.1618  362 HOH   A O   
6724 O  O   . HOH   G .   ? 0.2956 0.3214 0.4779 -0.0576 -0.1038 -0.0803 363 HOH   A O   
6725 O  O   . HOH   G .   ? 0.3468 0.2770 0.3365 -0.0883 -0.0095 -0.0182 364 HOH   A O   
6726 O  O   . HOH   G .   ? 0.2093 0.1652 0.2178 -0.0140 -0.0369 0.0041  365 HOH   A O   
6727 O  O   . HOH   G .   ? 0.5003 0.3043 0.4255 -0.1849 0.1943  -0.0837 366 HOH   A O   
6728 O  O   . HOH   G .   ? 0.2455 0.3970 0.3283 -0.0290 0.0666  -0.0072 367 HOH   A O   
6729 O  O   . HOH   G .   ? 0.1300 0.1265 0.1350 -0.0050 0.0131  0.0078  368 HOH   A O   
6730 O  O   A HOH   G .   ? 0.2185 0.2706 0.2104 0.0401  0.0172  0.0208  369 HOH   A O   
6731 O  O   . HOH   G .   ? 0.1458 0.1888 0.2607 0.0074  -0.0143 0.0132  370 HOH   A O   
6732 O  O   . HOH   G .   ? 0.3949 0.2079 0.2302 0.1155  0.0529  0.0160  371 HOH   A O   
6733 O  O   . HOH   G .   ? 0.2980 0.2329 0.4917 -0.0582 -0.0380 0.0395  372 HOH   A O   
6734 O  O   A HOH   G .   ? 0.3374 0.1607 0.1868 0.0175  0.0125  0.0164  373 HOH   A O   
6735 O  O   B HOH   G .   ? 0.2154 0.3236 0.3201 0.0545  0.0124  0.0362  374 HOH   A O   
6736 O  O   . HOH   G .   ? 0.1401 0.1471 0.1501 -0.0051 -0.0130 -0.0043 375 HOH   A O   
6737 O  O   . HOH   G .   ? 0.3704 0.2517 0.4738 -0.1254 0.0519  0.0526  376 HOH   A O   
6738 O  O   . HOH   G .   ? 0.1953 0.1836 0.2383 -0.0372 0.0061  0.0428  377 HOH   A O   
6739 O  O   . HOH   G .   ? 0.1475 0.1301 0.2333 -0.0089 0.0182  -0.0020 378 HOH   A O   
6740 O  O   . HOH   G .   ? 0.1867 0.2509 0.3383 0.0146  0.0708  -0.0723 379 HOH   A O   
6741 O  O   . HOH   G .   ? 0.2485 0.3788 0.2826 0.0295  0.0654  0.1580  380 HOH   A O   
6742 O  O   . HOH   G .   ? 0.2572 0.2069 0.1636 -0.0649 0.0082  0.0354  381 HOH   A O   
6743 O  O   . HOH   G .   ? 0.3684 0.6689 0.4421 -0.0776 -0.1505 0.0837  382 HOH   A O   
6744 O  O   . HOH   G .   ? 0.2907 0.2774 0.2156 0.0297  0.0791  0.0129  383 HOH   A O   
6745 O  O   . HOH   G .   ? 0.1965 0.2198 0.2155 -0.0213 -0.0425 0.0394  384 HOH   A O   
6746 O  O   . HOH   G .   ? 0.1730 0.2187 0.1678 -0.0114 0.0008  0.0541  385 HOH   A O   
6747 O  O   . HOH   G .   ? 0.1858 0.1875 0.1583 0.0068  0.0059  0.0052  386 HOH   A O   
6748 O  O   . HOH   G .   ? 0.1596 0.1655 0.2246 -0.0165 0.0120  0.0367  387 HOH   A O   
6749 O  O   T HOH   G .   ? 0.1019 0.1122 0.2525 -0.0136 0.0339  0.0361  388 HOH   A O   
6750 O  O   . HOH   G .   ? 0.3196 0.3142 0.2347 -0.0197 -0.0485 0.0233  389 HOH   A O   
6751 O  O   A HOH   G .   ? 0.1351 0.1614 0.2633 0.0088  -0.0358 -0.0653 390 HOH   A O   
6752 O  O   . HOH   G .   ? 0.1803 0.1906 0.3850 0.0372  0.1039  0.1013  391 HOH   A O   
6753 O  O   . HOH   G .   ? 0.5548 0.5248 0.5803 -0.0609 0.0018  0.1425  392 HOH   A O   
6754 O  O   . HOH   G .   ? 0.1459 0.1870 0.1901 0.0296  -0.0341 -0.0548 393 HOH   A O   
6755 O  O   . HOH   G .   ? 0.3482 0.5671 0.5543 0.1193  0.0940  0.1222  394 HOH   A O   
6756 O  O   . HOH   G .   ? 0.2436 0.3446 0.2970 -0.0482 -0.0158 0.0613  395 HOH   A O   
6757 O  O   . HOH   G .   ? 0.3268 0.2477 0.3118 -0.0164 -0.0344 0.0909  396 HOH   A O   
6758 O  O   . HOH   G .   ? 0.2972 0.5852 0.3829 0.0866  0.0454  -0.1123 397 HOH   A O   
6759 O  O   . HOH   G .   ? 0.3761 0.5939 0.4219 -0.0985 0.0167  0.1521  398 HOH   A O   
6760 O  O   A HOH   G .   ? 0.2949 0.2204 0.2369 0.0726  0.0612  0.0508  399 HOH   A O   
6761 O  O   . HOH   G .   ? 0.1869 0.2131 0.2568 -0.0183 -0.0171 0.0858  400 HOH   A O   
6762 O  O   . HOH   G .   ? 0.2352 0.3971 0.3493 -0.0331 0.0907  -0.0825 401 HOH   A O   
6763 O  O   B HOH   G .   ? 0.2844 0.1432 0.4003 -0.0165 0.0310  0.0941  402 HOH   A O   
6764 O  O   A HOH   G .   ? 0.2065 0.1785 0.3339 -0.0208 0.0586  0.0050  403 HOH   A O   
6765 O  O   . HOH   G .   ? 0.2857 0.2517 0.2177 -0.0762 -0.0799 0.0297  404 HOH   A O   
6766 O  O   . HOH   G .   ? 0.1859 0.2612 0.3745 -0.0097 -0.0246 0.0220  405 HOH   A O   
6767 O  O   . HOH   G .   ? 0.1270 0.1399 0.1754 -0.0005 -0.0195 0.0052  406 HOH   A O   
6768 O  O   . HOH   G .   ? 0.2303 0.2709 0.3129 -0.0033 -0.0154 -0.0615 407 HOH   A O   
6769 O  O   . HOH   G .   ? 0.5609 0.2731 0.4699 0.0848  -0.0222 -0.0380 408 HOH   A O   
6770 O  O   B HOH   G .   ? 0.2837 0.2446 0.3209 0.0012  0.0822  -0.0127 409 HOH   A O   
6771 O  O   A HOH   G .   ? 0.2093 0.1922 0.2447 0.0167  0.0039  0.0641  410 HOH   A O   
6772 O  O   . HOH   G .   ? 0.5236 0.3863 0.1724 -0.0376 0.0696  0.0526  411 HOH   A O   
6773 O  O   . HOH   G .   ? 0.5303 0.3106 0.3158 -0.1327 0.0546  0.0969  412 HOH   A O   
6774 O  O   . HOH   G .   ? 0.2389 0.1683 0.2549 0.0039  0.0090  0.0208  413 HOH   A O   
6775 O  O   . HOH   G .   ? 0.2078 0.1655 0.2934 0.0033  -0.0357 0.0092  414 HOH   A O   
6776 O  O   . HOH   G .   ? 0.6346 0.5155 0.3829 0.1662  -0.0575 -0.0246 415 HOH   A O   
6777 O  O   . HOH   G .   ? 0.8028 0.3270 0.5479 -0.0170 -0.1329 0.0889  416 HOH   A O   
6778 O  O   . HOH   G .   ? 0.1498 0.1574 0.2927 0.0023  0.0052  0.0258  417 HOH   A O   
6779 O  O   B HOH   G .   ? 0.2991 0.2910 0.2664 0.0598  0.0243  0.0799  418 HOH   A O   
6780 O  O   . HOH   G .   ? 0.4660 0.6437 0.3668 -0.0840 -0.0237 0.1803  419 HOH   A O   
6781 O  O   . HOH   G .   ? 0.2537 0.2050 0.2421 -0.0592 -0.0027 0.0569  420 HOH   A O   
6782 O  O   . HOH   G .   ? 0.2026 0.2879 0.2565 -0.0101 -0.0603 0.0472  421 HOH   A O   
6783 O  O   B HOH   G .   ? 0.1480 0.3019 0.2406 -0.0300 -0.0599 -0.0870 422 HOH   A O   
6784 O  O   . HOH   G .   ? 0.6089 0.3862 0.5323 0.0235  0.0897  0.1511  423 HOH   A O   
6785 O  O   . HOH   G .   ? 0.3296 0.3492 0.6694 -0.0108 0.0911  -0.0236 424 HOH   A O   
6786 O  O   . HOH   G .   ? 0.5435 0.6517 0.6045 0.0533  0.0512  -0.0074 425 HOH   A O   
6787 O  O   . HOH   G .   ? 0.1557 0.1927 0.2652 -0.0104 0.0058  0.0393  426 HOH   A O   
6788 O  O   . HOH   G .   ? 0.2814 0.6029 0.1749 -0.0218 0.0464  0.0068  427 HOH   A O   
6789 O  O   B HOH   G .   ? 0.1236 0.1148 0.2329 -0.0122 0.0307  0.0163  428 HOH   A O   
6790 O  O   . HOH   G .   ? 0.2159 0.4407 0.2556 0.1565  -0.0167 0.0066  429 HOH   A O   
6791 O  O   . HOH   G .   ? 0.3288 0.1300 0.2106 0.0079  -0.0431 0.0074  430 HOH   A O   
6792 O  O   . HOH   G .   ? 0.4073 0.2189 0.5269 -0.0787 -0.2089 0.1137  431 HOH   A O   
6793 O  O   . HOH   G .   ? 0.6385 0.4125 0.5212 0.1778  -0.0849 0.1639  432 HOH   A O   
6794 O  O   A HOH   G .   ? 0.1524 0.2464 0.2936 -0.0264 0.0714  0.0416  433 HOH   A O   
6795 O  O   . HOH   G .   ? 0.4591 0.3299 0.4255 0.1362  0.0110  -0.0267 434 HOH   A O   
6796 O  O   A HOH   G .   ? 0.1545 0.1463 0.1766 0.0062  -0.0266 0.0011  435 HOH   A O   
6797 O  O   . HOH   G .   ? 0.5750 0.5732 0.6260 -0.1387 -0.0991 -0.0877 436 HOH   A O   
6798 O  O   . HOH   G .   ? 0.5107 0.4635 0.3541 -0.0286 -0.1373 0.0420  437 HOH   A O   
6799 O  O   . HOH   G .   ? 0.5875 0.7031 0.4033 0.0737  0.2626  -0.0795 438 HOH   A O   
6800 O  O   A HOH   G .   ? 0.1653 0.1728 0.2073 0.0317  -0.0317 0.0140  439 HOH   A O   
6801 O  O   . HOH   G .   ? 0.1815 0.1695 0.1688 0.0017  -0.0078 -0.0220 440 HOH   A O   
6802 O  O   . HOH   G .   ? 0.3717 0.2693 0.1775 -0.0734 0.0398  0.0627  441 HOH   A O   
6803 O  O   . HOH   G .   ? 0.1835 0.2195 0.5377 -0.0286 -0.0915 0.0519  442 HOH   A O   
6804 O  O   . HOH   G .   ? 0.5813 0.5475 0.6534 -0.1357 0.0341  -0.1202 443 HOH   A O   
6805 O  O   . HOH   G .   ? 0.2616 0.1527 0.2680 0.0037  0.0074  0.0093  444 HOH   A O   
6806 O  O   . HOH   G .   ? 0.5446 0.6586 0.5499 -0.0818 0.0102  0.0357  445 HOH   A O   
6807 O  O   . HOH   G .   ? 0.6417 0.6426 0.5468 0.1287  -0.1302 -0.0220 446 HOH   A O   
6808 O  O   . HOH   G .   ? 0.8173 0.8966 0.7175 0.0495  0.0105  -0.0323 447 HOH   A O   
6809 O  O   B HOH   G .   ? 0.3558 0.2233 0.2944 -0.0751 0.0324  0.0989  448 HOH   A O   
6810 O  O   A HOH   G .   ? 0.1966 0.1664 0.2118 -0.0079 -0.0182 0.0100  449 HOH   A O   
6811 O  O   . HOH   G .   ? 0.4478 0.3527 0.6469 -0.0446 0.0429  -0.1250 450 HOH   A O   
6812 O  O   . HOH   G .   ? 0.3995 0.3211 0.3312 0.2003  -0.0747 -0.0490 451 HOH   A O   
6813 O  O   . HOH   G .   ? 0.2470 0.3467 0.5077 -0.0089 0.0810  -0.1581 452 HOH   A O   
6814 O  O   . HOH   G .   ? 0.4417 0.4447 0.4697 -0.1107 -0.0881 -0.1122 453 HOH   A O   
6815 O  O   . HOH   G .   ? 0.5486 0.6882 0.3719 0.1699  -0.0484 0.1889  454 HOH   A O   
6816 O  O   . HOH   G .   ? 0.2209 0.2027 0.2639 0.0061  0.0263  0.0217  455 HOH   A O   
6817 O  O   . HOH   G .   ? 0.2077 0.2622 0.2536 -0.0005 -0.0178 -0.0423 456 HOH   A O   
6818 O  O   A HOH   G .   ? 0.5149 0.3187 0.3300 0.1832  0.1393  0.1362  457 HOH   A O   
6819 O  O   . HOH   G .   ? 0.6678 0.5523 0.7112 0.0745  -0.1291 0.1705  458 HOH   A O   
6820 O  O   . HOH   G .   ? 0.5636 0.3224 0.4110 -0.0213 0.0114  0.0417  459 HOH   A O   
6821 O  O   . HOH   G .   ? 0.4193 0.4326 0.4214 0.0705  -0.0451 0.0220  460 HOH   A O   
6822 O  O   . HOH   G .   ? 0.3019 0.3570 0.3672 0.1055  -0.0401 0.0757  461 HOH   A O   
6823 O  O   . HOH   G .   ? 0.4212 0.3705 0.4734 -0.0081 0.0379  0.0796  462 HOH   A O   
6824 O  O   . HOH   G .   ? 0.5905 0.5811 0.4633 -0.0952 0.0807  0.0755  463 HOH   A O   
6825 O  O   . HOH   G .   ? 0.6623 0.7244 0.4716 0.1093  -0.1156 -0.0211 464 HOH   A O   
6826 O  O   . HOH   G .   ? 0.2860 0.4697 0.5523 -0.1324 0.0706  -0.1713 465 HOH   A O   
6827 O  O   . HOH   G .   ? 0.2711 0.2710 0.3362 -0.0595 0.0309  -0.0612 466 HOH   A O   
6828 O  O   . HOH   G .   ? 0.3705 0.4514 0.4523 0.0488  -0.0489 0.1476  467 HOH   A O   
6829 O  O   . HOH   G .   ? 0.3107 0.4325 0.3798 -0.0760 -0.0347 0.0056  468 HOH   A O   
6830 O  O   . HOH   G .   ? 0.2558 0.2845 0.3542 -0.0912 0.0679  -0.0480 469 HOH   A O   
6831 O  O   . HOH   G .   ? 0.4353 0.5519 0.3627 -0.1079 -0.0735 0.1875  470 HOH   A O   
6832 O  O   . HOH   G .   ? 0.6171 0.3342 0.7314 0.0719  0.0889  0.2077  471 HOH   A O   
6833 O  O   . HOH   G .   ? 0.2612 0.4039 0.5311 0.0563  0.0248  -0.1829 472 HOH   A O   
6834 O  O   A HOH   G .   ? 0.2803 0.2933 0.5086 0.0869  -0.1748 -0.0974 473 HOH   A O   
6835 O  O   B HOH   G .   ? 0.4383 0.2343 0.2593 0.1206  0.0464  0.0978  474 HOH   A O   
6836 O  O   . HOH   G .   ? 0.2570 0.1671 0.2607 0.0196  -0.0878 -0.0178 475 HOH   A O   
6837 O  O   . HOH   G .   ? 0.3478 0.2297 0.3505 0.0256  0.0784  0.0014  476 HOH   A O   
6838 O  O   B HOH   G .   ? 0.1670 0.2577 0.2303 -0.0197 0.0182  -0.0538 477 HOH   A O   
6839 O  O   . HOH   G .   ? 0.5705 0.5006 0.4501 0.0273  0.1191  0.0565  478 HOH   A O   
6840 O  O   . HOH   G .   ? 0.3985 0.5032 0.3381 0.0332  -0.0352 -0.0668 479 HOH   A O   
6841 O  O   . HOH   G .   ? 0.6486 0.5844 0.6425 0.1376  0.2240  0.1839  480 HOH   A O   
6842 O  O   . HOH   G .   ? 0.4805 0.5300 0.5072 0.0775  -0.1103 -0.1115 481 HOH   A O   
6843 O  O   . HOH   G .   ? 0.3987 0.4042 0.5047 -0.1899 -0.0350 -0.0053 482 HOH   A O   
6844 O  O   . HOH   G .   ? 0.4257 0.4875 0.3226 -0.0309 -0.0583 -0.0527 483 HOH   A O   
6845 O  O   . HOH   G .   ? 0.5655 0.5680 0.5113 -0.1602 -0.1013 0.0204  484 HOH   A O   
6846 O  O   . HOH   G .   ? 0.4032 0.4920 0.2726 0.0066  0.0158  0.0249  485 HOH   A O   
6847 O  O   . HOH   G .   ? 0.7050 0.5614 0.6543 -0.0675 0.0756  -0.0891 486 HOH   A O   
6848 O  O   . HOH   G .   ? 0.5381 0.4138 0.3928 -0.0135 0.0375  -0.1299 487 HOH   A O   
6849 O  O   . HOH   G .   ? 0.4585 0.2659 0.3367 -0.0917 -0.1177 0.0723  488 HOH   A O   
6850 O  O   . HOH   G .   ? 0.2847 0.4427 0.3261 -0.0276 -0.0224 -0.0905 489 HOH   A O   
6851 O  O   . HOH   G .   ? 0.7583 0.3891 0.3042 -0.0325 -0.0920 -0.0009 490 HOH   A O   
6852 O  O   . HOH   G .   ? 0.2345 0.2246 0.2559 0.0132  -0.0027 0.0048  491 HOH   A O   
6853 O  O   . HOH   G .   ? 0.2755 0.4969 0.3381 0.1131  0.1019  0.2208  492 HOH   A O   
6854 O  O   . HOH   G .   ? 0.2706 0.4263 0.4596 0.0244  0.1287  0.1336  493 HOH   A O   
6855 O  O   . HOH   G .   ? 0.5934 0.6217 0.4496 -0.0554 0.1640  0.1116  494 HOH   A O   
6856 O  O   . HOH   G .   ? 0.5128 0.5378 0.5813 0.0377  -0.1141 0.0509  495 HOH   A O   
6857 O  O   B HOH   G .   ? 0.2076 0.4270 0.2710 0.0122  -0.0827 0.0345  496 HOH   A O   
6858 O  O   . HOH   G .   ? 0.6381 0.4895 0.4927 -0.0688 -0.0970 -0.0976 497 HOH   A O   
6859 O  O   . HOH   G .   ? 0.2431 0.2526 0.7129 -0.0081 -0.1261 0.0339  498 HOH   A O   
6860 O  O   . HOH   G .   ? 0.5388 0.5635 0.6250 0.1016  0.1324  -0.1167 499 HOH   A O   
6861 O  O   . HOH   G .   ? 0.4568 0.3672 0.2842 -0.0949 0.1674  -0.0691 500 HOH   A O   
6862 O  O   . HOH   G .   ? 0.4629 0.3178 0.4539 -0.0255 0.2203  0.0283  501 HOH   A O   
6863 O  O   . HOH   G .   ? 0.5632 0.3855 0.3992 -0.0362 0.1067  -0.0278 502 HOH   A O   
6864 O  O   . HOH   G .   ? 0.4641 0.2993 0.4793 -0.1096 0.1124  0.0609  503 HOH   A O   
6865 O  O   . HOH   G .   ? 0.2904 0.2133 0.5425 0.0036  0.0366  0.0976  504 HOH   A O   
6866 O  O   . HOH   G .   ? 0.2635 0.3929 0.4783 0.0387  0.0999  -0.0544 505 HOH   A O   
6867 O  O   . HOH   G .   ? 0.3922 0.7911 0.5769 -0.0928 -0.0611 0.2531  506 HOH   A O   
6868 O  O   . HOH   G .   ? 0.2363 0.3790 0.3367 0.0790  -0.0317 0.0620  507 HOH   A O   
6869 O  O   . HOH   G .   ? 0.6028 0.2776 0.4817 -0.0556 0.0867  0.1038  508 HOH   A O   
6870 O  O   B HOH   G .   ? 0.3313 0.3290 0.2961 0.0021  0.0510  0.0936  509 HOH   A O   
6871 O  O   . HOH   G .   ? 0.4717 0.2800 0.4442 -0.1556 -0.0281 0.0636  510 HOH   A O   
6872 O  O   . HOH   G .   ? 0.2641 0.4338 0.3776 0.0459  -0.0176 0.0333  511 HOH   A O   
6873 O  O   . HOH   G .   ? 0.5627 0.7198 0.5092 -0.0443 -0.1219 0.0566  512 HOH   A O   
6874 O  O   . HOH   G .   ? 0.5931 0.5913 0.4274 0.0700  -0.1371 -0.0136 513 HOH   A O   
6875 O  O   . HOH   G .   ? 0.7784 0.5092 0.6011 0.0179  0.0421  0.0314  514 HOH   A O   
6876 O  O   . HOH   G .   ? 0.4853 0.5424 0.4324 -0.0641 -0.0391 -0.1332 515 HOH   A O   
6877 O  O   . HOH   G .   ? 0.2862 0.2336 0.4630 0.0135  0.0199  0.0813  516 HOH   A O   
6878 O  O   . HOH   G .   ? 0.4757 0.6251 0.5130 0.2805  0.0156  0.1020  517 HOH   A O   
6879 O  O   T HOH   G .   ? 0.1352 0.1384 0.1633 -0.0143 -0.0054 0.0173  518 HOH   A O   
6880 O  O   A HOH   G .   ? 0.3702 0.7184 0.4794 0.1393  0.1933  -0.0017 519 HOH   A O   
6881 O  O   . HOH   G .   ? 0.2639 0.7171 0.3541 0.0257  0.0351  -0.0406 520 HOH   A O   
6882 O  O   B HOH   G .   ? 0.3576 0.3327 0.3267 0.0551  -0.0381 -0.0028 521 HOH   A O   
6883 O  O   B HOH   G .   ? 0.2428 0.2672 0.2416 -0.0603 0.0292  -0.0398 522 HOH   A O   
6884 O  O   . HOH   G .   ? 0.4684 0.4738 0.4479 0.1435  -0.0416 0.1298  523 HOH   A O   
6885 O  O   . HOH   G .   ? 0.4627 0.6548 0.5419 -0.0568 -0.0704 0.0608  524 HOH   A O   
6886 O  O   . HOH   G .   ? 0.4079 0.4582 0.4971 -0.0432 -0.1026 0.2739  525 HOH   A O   
6887 O  O   . HOH   H .   ? 0.2273 0.2173 0.3170 0.0132  0.0667  0.0484  201 HOH   B O   
6888 O  O   . HOH   H .   ? 0.4928 0.3172 0.3642 -0.0317 -0.0142 -0.1187 202 HOH   B O   
6889 O  O   . HOH   H .   ? 0.5886 0.5763 0.5799 0.1882  0.0111  0.0410  203 HOH   B O   
6890 O  O   . HOH   H .   ? 0.4872 0.4718 0.2570 0.0108  0.0321  -0.1172 204 HOH   B O   
6891 O  O   . HOH   H .   ? 0.3297 0.7177 0.3571 0.0906  0.0095  0.2270  205 HOH   B O   
6892 O  O   . HOH   H .   ? 0.7235 0.4074 0.4666 0.0870  0.1352  -0.0170 206 HOH   B O   
6893 O  O   . HOH   H .   ? 0.5208 0.5645 0.3917 0.2688  -0.1280 -0.0463 207 HOH   B O   
6894 O  O   . HOH   H .   ? 0.3556 0.3539 0.6432 -0.0424 0.0256  -0.0649 208 HOH   B O   
6895 O  O   . HOH   H .   ? 0.3073 0.5334 0.5122 -0.0296 0.1735  -0.1759 209 HOH   B O   
6896 O  O   . HOH   H .   ? 0.3460 0.4060 0.4962 -0.0884 0.0117  -0.1273 210 HOH   B O   
6897 O  O   . HOH   H .   ? 0.5707 0.2949 0.4215 -0.1655 0.0542  0.0205  211 HOH   B O   
6898 O  O   . HOH   H .   ? 0.4495 0.3786 0.3923 -0.0012 -0.1153 0.0631  212 HOH   B O   
6899 O  O   . HOH   H .   ? 0.4185 0.4373 0.6300 -0.0607 -0.1471 -0.0987 213 HOH   B O   
6900 O  O   . HOH   H .   ? 0.2770 0.2692 0.6361 0.0541  -0.1041 0.0618  214 HOH   B O   
6901 O  O   . HOH   H .   ? 0.4401 0.5588 0.3912 0.2760  -0.0512 0.0083  215 HOH   B O   
6902 O  O   . HOH   H .   ? 0.1618 0.1842 0.2789 -0.0177 0.0008  0.0053  216 HOH   B O   
6903 O  O   . HOH   H .   ? 0.1986 0.2688 0.2880 0.0308  0.0093  -0.0582 217 HOH   B O   
6904 O  O   . HOH   H .   ? 0.4383 0.2056 0.3485 -0.0131 -0.1211 0.0225  218 HOH   B O   
6905 O  O   . HOH   H .   ? 0.4602 0.4155 0.5861 0.0529  -0.1012 0.2529  219 HOH   B O   
6906 O  O   . HOH   H .   ? 0.4069 0.4803 0.4320 0.0681  0.0717  -0.1291 220 HOH   B O   
6907 O  O   . HOH   H .   ? 0.2996 0.2024 0.5586 0.0110  0.1908  0.0781  221 HOH   B O   
6908 O  O   . HOH   H .   ? 0.3278 0.5194 0.5172 0.2187  0.0341  -0.0521 222 HOH   B O   
6909 O  O   . HOH   H .   ? 0.3765 0.4194 0.5191 -0.1557 -0.0124 0.1012  223 HOH   B O   
6910 O  O   . HOH   H .   ? 0.2456 0.1777 0.2869 -0.0311 0.1171  -0.0136 224 HOH   B O   
6911 O  O   . HOH   H .   ? 0.1719 0.2068 0.3202 -0.0169 0.0098  -0.0046 225 HOH   B O   
6912 O  O   . HOH   H .   ? 0.4056 0.6262 0.3709 0.2088  0.0084  -0.0706 226 HOH   B O   
6913 O  O   . HOH   H .   ? 0.2114 0.2126 0.4205 -0.0286 -0.0108 -0.0626 227 HOH   B O   
6914 O  O   . HOH   H .   ? 0.5887 0.6124 0.3551 0.0517  -0.0646 0.0139  228 HOH   B O   
6915 O  O   . HOH   H .   ? 0.7269 0.4507 0.5004 0.1933  -0.0618 -0.1050 229 HOH   B O   
6916 O  O   . HOH   H .   ? 0.3583 0.3208 0.2466 0.0321  0.0538  0.0348  230 HOH   B O   
6917 O  O   . HOH   H .   ? 0.3175 0.2061 0.4404 0.0012  0.1454  0.0300  231 HOH   B O   
6918 O  O   . HOH   H .   ? 0.2762 0.3772 0.3548 -0.1053 0.0127  -0.0034 232 HOH   B O   
6919 O  O   . HOH   H .   ? 0.3453 0.4661 0.4833 0.1136  -0.0876 0.0465  233 HOH   B O   
6920 O  O   . HOH   H .   ? 0.1975 0.2414 0.3039 -0.0531 0.0124  -0.0246 234 HOH   B O   
6921 O  O   . HOH   H .   ? 0.3574 0.1737 0.2139 0.0097  -0.0775 -0.0128 235 HOH   B O   
6922 O  O   . HOH   H .   ? 0.2947 0.2541 0.3015 0.0511  0.0074  -0.0945 236 HOH   B O   
6923 O  O   . HOH   H .   ? 0.3610 0.2856 0.5712 0.0035  0.0563  -0.0151 237 HOH   B O   
6924 O  O   . HOH   H .   ? 0.2047 0.1306 0.3460 0.0104  -0.0584 -0.0126 238 HOH   B O   
6925 O  O   . HOH   H .   ? 0.1398 0.1439 0.1607 -0.0153 -0.0057 -0.0022 239 HOH   B O   
6926 O  O   . HOH   H .   ? 0.2062 0.3910 0.2486 -0.0618 -0.0150 0.0560  240 HOH   B O   
6927 O  O   . HOH   H .   ? 0.2282 0.3488 0.3063 -0.0396 -0.0574 -0.0341 241 HOH   B O   
6928 O  O   . HOH   H .   ? 0.3400 0.4058 0.3987 0.0892  -0.1009 -0.1840 242 HOH   B O   
6929 O  O   . HOH   H .   ? 0.2971 0.2484 0.3195 -0.0081 0.0089  -0.0684 243 HOH   B O   
6930 O  O   . HOH   H .   ? 0.5391 0.2907 0.3972 -0.2153 -0.0204 0.0103  244 HOH   B O   
6931 O  O   . HOH   H .   ? 0.1577 0.1376 0.2846 -0.0074 0.0100  -0.0073 245 HOH   B O   
6932 O  O   . HOH   H .   ? 0.2090 0.1958 0.2093 -0.0238 -0.0326 0.0112  246 HOH   B O   
6933 O  O   . HOH   H .   ? 0.1427 0.1288 0.1673 0.0002  -0.0064 0.0112  247 HOH   B O   
6934 O  O   . HOH   H .   ? 0.3121 0.4724 0.5255 0.0268  0.0066  -0.1184 248 HOH   B O   
6935 O  O   . HOH   H .   ? 0.3239 0.5064 0.3830 -0.0186 -0.1006 0.1251  249 HOH   B O   
6936 O  O   . HOH   H .   ? 0.2790 0.2260 0.2986 0.0886  0.0859  0.0254  250 HOH   B O   
6937 O  O   . HOH   H .   ? 0.3881 0.2524 0.3962 0.0886  -0.0434 -0.0696 251 HOH   B O   
6938 O  O   . HOH   H .   ? 0.3077 0.4592 0.2061 0.0184  0.0691  0.0037  252 HOH   B O   
6939 O  O   . HOH   H .   ? 0.4343 0.3525 0.3632 -0.0960 0.0664  -0.1085 253 HOH   B O   
6940 O  O   . HOH   H .   ? 0.1996 0.1469 0.2182 -0.0229 -0.0319 0.0248  254 HOH   B O   
6941 O  O   . HOH   H .   ? 0.6039 0.3772 0.2387 -0.0143 0.0232  -0.0174 255 HOH   B O   
6942 O  O   . HOH   H .   ? 0.3178 0.1772 0.6100 -0.0203 -0.1363 -0.0332 256 HOH   B O   
6943 O  O   . HOH   H .   ? 0.2417 0.2141 0.2581 0.0707  -0.0827 -0.0691 257 HOH   B O   
6944 O  O   . HOH   H .   ? 0.2146 0.3290 0.2365 -0.0652 0.0224  0.0478  258 HOH   B O   
6945 O  O   . HOH   H .   ? 0.3072 0.4494 0.2950 -0.1320 -0.0266 -0.0780 259 HOH   B O   
6946 O  O   . HOH   H .   ? 0.1603 0.1636 0.2924 -0.0243 -0.0157 0.0030  260 HOH   B O   
6947 O  O   . HOH   H .   ? 0.1355 0.1630 0.2059 -0.0046 0.0063  0.0105  261 HOH   B O   
6948 O  O   . HOH   H .   ? 0.2365 0.2111 0.1984 0.0087  -0.0091 0.0112  262 HOH   B O   
6949 O  O   . HOH   H .   ? 0.1734 0.2659 0.2773 0.0399  0.0347  0.0981  263 HOH   B O   
6950 O  O   . HOH   H .   ? 0.2460 0.1796 0.3437 0.0064  -0.0720 -0.0325 264 HOH   B O   
6951 O  O   . HOH   H .   ? 0.2576 0.1954 0.2888 -0.0624 0.0145  -0.0161 265 HOH   B O   
6952 O  O   . HOH   H .   ? 0.2400 0.5070 0.5519 0.1422  -0.0812 -0.1106 266 HOH   B O   
6953 O  O   . HOH   H .   ? 0.1778 0.1771 0.1727 -0.0413 -0.0375 0.0078  267 HOH   B O   
6954 O  O   . HOH   H .   ? 0.4554 0.5282 0.4737 0.0345  -0.1306 0.0029  268 HOH   B O   
6955 O  O   . HOH   H .   ? 0.1940 0.3977 0.4699 -0.0190 -0.0302 -0.1692 269 HOH   B O   
6956 O  O   . HOH   H .   ? 0.2332 0.2075 0.2081 0.0122  -0.0102 -0.0033 270 HOH   B O   
6957 O  O   . HOH   H .   ? 0.2042 0.1466 0.2294 -0.0244 -0.0191 0.0122  271 HOH   B O   
6958 O  O   . HOH   H .   ? 0.2521 0.4200 0.3505 0.0414  0.1082  0.0354  272 HOH   B O   
6959 O  O   . HOH   H .   ? 0.2332 0.2894 0.2458 -0.0303 -0.0763 0.0157  273 HOH   B O   
6960 O  O   . HOH   H .   ? 0.1758 0.1371 0.3783 -0.0062 -0.0249 -0.0110 274 HOH   B O   
6961 O  O   . HOH   H .   ? 0.2280 0.2485 0.2342 -0.0379 -0.0613 -0.0224 275 HOH   B O   
6962 O  O   . HOH   H .   ? 0.3771 0.3660 0.4756 0.0042  -0.1253 -0.0849 276 HOH   B O   
6963 O  O   . HOH   H .   ? 0.2672 0.2017 0.5214 0.0165  0.0528  0.0384  277 HOH   B O   
6964 O  O   . HOH   H .   ? 0.2589 0.4129 0.2274 0.1574  -0.0386 -0.0509 278 HOH   B O   
6965 O  O   . HOH   H .   ? 0.1593 0.1497 0.1856 0.0010  0.0126  0.0021  279 HOH   B O   
6966 O  O   . HOH   H .   ? 0.4452 0.3658 0.2862 0.0438  -0.0102 -0.0985 280 HOH   B O   
6967 O  O   . HOH   H .   ? 0.1568 0.1485 0.3593 -0.0131 0.0090  -0.0080 281 HOH   B O   
6968 O  O   . HOH   H .   ? 0.2746 0.5003 0.4857 -0.1204 -0.1338 0.1216  282 HOH   B O   
6969 O  O   . HOH   H .   ? 0.4467 0.3388 0.4633 -0.1112 -0.0120 0.1369  283 HOH   B O   
6970 O  O   . HOH   H .   ? 0.3076 0.4458 0.5755 -0.0685 0.0736  -0.0182 284 HOH   B O   
6971 O  O   . HOH   H .   ? 0.3322 0.3872 0.4514 0.1079  -0.0789 -0.1207 285 HOH   B O   
6972 O  O   . HOH   H .   ? 0.1615 0.2056 0.1650 -0.0177 -0.0237 0.0075  286 HOH   B O   
6973 O  O   . HOH   H .   ? 0.2981 0.6407 0.7230 0.1550  -0.0520 -0.1096 287 HOH   B O   
6974 O  O   . HOH   H .   ? 0.5384 0.6352 0.2714 -0.0011 -0.0403 0.0763  288 HOH   B O   
6975 O  O   . HOH   H .   ? 0.2295 0.2649 0.2973 0.0080  -0.0734 0.0205  289 HOH   B O   
6976 O  O   . HOH   H .   ? 0.2473 0.6872 0.2487 0.0607  -0.0238 -0.0349 290 HOH   B O   
6977 O  O   . HOH   H .   ? 0.2559 0.3735 0.3361 -0.0828 0.0704  -0.1566 291 HOH   B O   
6978 O  O   . HOH   H .   ? 0.3742 0.2201 0.4134 -0.0899 -0.2122 0.0865  292 HOH   B O   
6979 O  O   . HOH   H .   ? 0.1671 0.1949 0.2827 0.0262  -0.0104 0.0107  293 HOH   B O   
6980 O  O   . HOH   H .   ? 0.5044 0.4503 0.2573 0.1299  -0.0368 -0.0228 294 HOH   B O   
6981 O  O   . HOH   H .   ? 0.1681 0.3209 0.4991 0.0319  -0.0063 -0.1306 295 HOH   B O   
6982 O  O   . HOH   H .   ? 0.5069 0.3676 0.2389 0.1397  -0.0903 0.0312  296 HOH   B O   
6983 O  O   . HOH   H .   ? 0.2119 0.1617 0.2608 -0.0195 -0.0262 -0.0043 297 HOH   B O   
6984 O  O   . HOH   H .   ? 0.3587 0.2855 0.2175 0.0523  -0.0795 -0.0259 298 HOH   B O   
6985 O  O   . HOH   H .   ? 0.1723 0.1588 0.2501 0.0077  0.0019  0.0163  299 HOH   B O   
6986 O  O   . HOH   H .   ? 0.3067 0.2862 0.2955 -0.0119 0.0068  -0.1315 300 HOH   B O   
6987 O  O   . HOH   H .   ? 0.3399 0.6818 0.3298 0.1398  -0.0917 0.0991  301 HOH   B O   
6988 O  O   . HOH   H .   ? 0.6156 0.5914 0.5654 0.2859  0.0028  -0.0229 302 HOH   B O   
6989 O  O   . HOH   H .   ? 0.5805 0.3742 0.3177 0.2584  0.1090  0.0819  303 HOH   B O   
6990 O  O   . HOH   H .   ? 0.4274 0.4853 0.2371 0.0233  0.0741  0.0660  304 HOH   B O   
6991 O  O   . HOH   H .   ? 0.3340 0.3684 0.3856 -0.1334 0.1307  -0.0580 305 HOH   B O   
6992 O  O   . HOH   H .   ? 0.3055 0.2944 0.5374 -0.0339 -0.1099 0.1244  306 HOH   B O   
6993 O  O   . HOH   H .   ? 0.2011 0.1556 0.3394 0.0312  -0.0933 -0.0004 307 HOH   B O   
6994 O  O   . HOH   H .   ? 0.1985 0.2677 0.6381 0.0344  -0.0465 -0.1052 308 HOH   B O   
6995 O  O   . HOH   H .   ? 0.2782 0.2787 0.3761 -0.0476 0.1143  -0.0885 309 HOH   B O   
6996 O  O   . HOH   H .   ? 0.1548 0.1466 0.3000 0.0104  0.0027  -0.0055 310 HOH   B O   
6997 O  O   . HOH   H .   ? 0.3476 0.1841 0.3505 0.0715  0.1199  0.0523  311 HOH   B O   
6998 O  O   . HOH   H .   ? 0.2431 0.1429 0.2600 -0.0148 -0.0178 0.0304  312 HOH   B O   
6999 O  O   . HOH   H .   ? 0.4307 0.3896 0.5957 0.0701  -0.0294 0.0378  313 HOH   B O   
7000 O  O   . HOH   H .   ? 0.5371 0.2933 0.2342 -0.1983 0.0911  -0.0253 314 HOH   B O   
7001 O  O   . HOH   H .   ? 0.4173 0.2511 0.2756 0.1686  0.1062  0.0396  315 HOH   B O   
7002 O  O   . HOH   H .   ? 0.2244 0.2932 0.5070 -0.0356 -0.0358 0.0063  316 HOH   B O   
7003 O  O   . HOH   H .   ? 0.5079 0.2259 0.3846 0.0431  0.0505  0.0668  317 HOH   B O   
7004 O  O   . HOH   H .   ? 0.1579 0.1881 0.2855 -0.0254 -0.0081 0.0046  318 HOH   B O   
7005 O  O   . HOH   H .   ? 0.6298 0.4421 0.5163 0.1033  0.0829  -0.0019 319 HOH   B O   
7006 O  O   . HOH   H .   ? 0.1559 0.1608 0.2889 -0.0143 -0.0111 -0.0114 320 HOH   B O   
7007 O  O   . HOH   H .   ? 0.2698 0.3206 0.4682 -0.0599 -0.1562 0.1214  321 HOH   B O   
7008 O  O   . HOH   H .   ? 0.2147 0.2067 0.1951 -0.0101 0.0228  0.0197  322 HOH   B O   
7009 O  O   . HOH   H .   ? 0.4304 0.4388 0.2765 0.0367  -0.0503 -0.0731 323 HOH   B O   
7010 O  O   . HOH   H .   ? 0.4144 0.3249 0.4968 0.1079  0.1981  0.1627  324 HOH   B O   
7011 O  O   . HOH   H .   ? 0.1674 0.2829 0.2370 -0.0129 -0.0189 0.0724  325 HOH   B O   
7012 O  O   . HOH   H .   ? 0.3464 0.4498 0.7045 -0.0348 -0.1000 0.2230  326 HOH   B O   
7013 O  O   . HOH   H .   ? 0.5927 0.5124 0.5873 0.1047  -0.0974 0.2247  327 HOH   B O   
7014 O  O   . HOH   H .   ? 0.5512 0.5176 0.5563 -0.0948 -0.0089 0.1316  328 HOH   B O   
7015 O  O   . HOH   H .   ? 0.1874 0.1904 0.2946 0.0307  0.0284  0.0103  329 HOH   B O   
7016 O  O   . HOH   H .   ? 0.2775 0.2266 0.2422 0.0194  -0.0280 0.0337  330 HOH   B O   
7017 O  O   . HOH   H .   ? 0.1790 0.2650 0.3031 0.0228  -0.0037 -0.0600 331 HOH   B O   
7018 O  O   . HOH   H .   ? 0.2227 0.5980 0.5209 -0.0660 0.0004  0.0060  332 HOH   B O   
7019 O  O   . HOH   H .   ? 0.2559 0.2033 0.4849 -0.0051 0.0004  0.0229  333 HOH   B O   
7020 O  O   . HOH   H .   ? 0.8016 0.2060 0.3227 0.0240  -0.0798 0.0080  334 HOH   B O   
7021 O  O   . HOH   H .   ? 0.2199 0.2311 0.5322 -0.0484 0.0065  0.1380  335 HOH   B O   
7022 O  O   . HOH   H .   ? 0.5745 0.3464 0.3530 -0.0141 0.1046  0.1102  336 HOH   B O   
7023 O  O   . HOH   H .   ? 0.5412 0.4688 0.5967 -0.0513 -0.0446 -0.1151 337 HOH   B O   
7024 O  O   . HOH   H .   ? 0.5190 0.3507 0.4404 0.0251  0.0689  -0.1499 338 HOH   B O   
7025 O  O   . HOH   H .   ? 0.4856 0.3281 0.3231 0.0177  -0.1234 -0.0539 339 HOH   B O   
7026 O  O   . HOH   H .   ? 0.1706 0.1457 0.2314 0.0079  -0.0175 0.0049  340 HOH   B O   
7027 O  O   . HOH   H .   ? 0.1976 0.5485 0.6398 -0.0144 -0.0481 -0.0085 341 HOH   B O   
7028 O  O   . HOH   H .   ? 0.4658 0.5505 0.3541 -0.0284 -0.1066 0.0474  342 HOH   B O   
7029 O  O   . HOH   H .   ? 0.4473 0.6934 0.3821 -0.0025 -0.0424 0.1640  343 HOH   B O   
7030 O  O   . HOH   H .   ? 0.3986 0.6459 0.3719 -0.0665 -0.0936 -0.0920 344 HOH   B O   
7031 O  O   . HOH   H .   ? 0.6645 0.6319 0.3101 -0.0265 -0.0690 0.1104  345 HOH   B O   
7032 O  O   . HOH   H .   ? 0.2187 0.1843 0.2927 -0.0061 0.0597  0.0025  346 HOH   B O   
7033 O  O   . HOH   H .   ? 0.2620 0.6401 0.3045 0.1810  -0.0539 -0.1317 347 HOH   B O   
7034 O  O   . HOH   H .   ? 0.4063 0.4786 0.4917 0.0093  -0.0689 0.0642  348 HOH   B O   
7035 O  O   . HOH   H .   ? 0.2080 0.4595 0.5179 0.0136  0.0635  0.0198  349 HOH   B O   
7036 O  O   . HOH   H .   ? 0.2887 0.2263 0.4906 -0.0218 -0.0977 -0.0531 350 HOH   B O   
7037 O  O   . HOH   H .   ? 0.4347 0.5838 0.6335 0.0277  0.0157  -0.0621 351 HOH   B O   
7038 O  O   . HOH   H .   ? 0.4736 0.5779 0.4898 -0.1233 0.0235  0.1216  352 HOH   B O   
7039 O  O   . HOH   H .   ? 0.3502 0.2427 0.3540 -0.0758 0.0165  -0.0965 353 HOH   B O   
7040 O  O   . HOH   H .   ? 0.2911 0.1911 0.4066 0.0398  -0.1247 -0.0554 354 HOH   B O   
7041 O  O   . HOH   H .   ? 0.3656 0.2697 0.3927 -0.0977 0.0314  -0.0721 355 HOH   B O   
7042 O  O   . HOH   H .   ? 0.3673 0.4233 0.4700 -0.1511 -0.0072 -0.0294 356 HOH   B O   
7043 O  O   . HOH   H .   ? 0.5778 0.3442 0.4188 0.0376  0.1437  -0.0531 357 HOH   B O   
7044 O  O   . HOH   H .   ? 0.4059 0.3531 0.5752 -0.1026 0.1160  0.1142  358 HOH   B O   
7045 O  O   . HOH   H .   ? 0.4999 0.5098 0.5236 -0.0759 -0.0108 0.0413  359 HOH   B O   
7046 O  O   . HOH   H .   ? 0.4579 0.3445 0.4697 -0.0059 -0.1444 -0.0285 360 HOH   B O   
7047 O  O   . HOH   H .   ? 0.4380 0.5370 0.5362 0.1668  -0.1190 0.1629  361 HOH   B O   
7048 O  O   . HOH   H .   ? 0.4718 0.4241 0.6722 -0.0115 0.0884  0.0748  362 HOH   B O   
7049 O  O   . HOH   H .   ? 0.3831 0.6127 0.2960 0.1672  0.0063  0.0240  363 HOH   B O   
7050 O  O   . HOH   H .   ? 0.2210 0.3743 0.6494 -0.0709 -0.0785 -0.0844 364 HOH   B O   
7051 O  O   . HOH   H .   ? 0.5328 0.3054 0.5454 -0.1516 0.0072  0.0226  365 HOH   B O   
7052 O  O   . HOH   H .   ? 0.5675 0.4897 0.4484 0.1401  0.0950  0.1029  366 HOH   B O   
7053 O  O   . HOH   H .   ? 0.5438 0.3843 0.5068 0.1130  -0.1359 0.0208  367 HOH   B O   
7054 O  O   . HOH   H .   ? 0.5754 0.5700 0.3583 0.1460  -0.1533 0.0746  368 HOH   B O   
7055 O  O   . HOH   H .   ? 0.4960 0.5234 0.4307 -0.0631 -0.0505 -0.1053 369 HOH   B O   
7056 O  O   . HOH   H .   ? 0.6083 0.2215 0.4153 -0.0060 0.0133  0.0809  370 HOH   B O   
7057 O  O   . HOH   H .   ? 0.7623 0.6962 0.4973 0.2446  -0.1293 0.1104  371 HOH   B O   
7058 O  O   . HOH   H .   ? 0.4502 0.5881 0.5715 0.2455  0.0904  0.1177  372 HOH   B O   
7059 O  O   . HOH   H .   ? 0.5657 0.4093 0.3288 -0.0802 -0.1095 -0.0782 373 HOH   B O   
7060 O  O   . HOH   H .   ? 0.4446 0.3608 0.4751 0.1028  -0.1434 -0.0893 374 HOH   B O   
7061 O  O   . HOH   H .   ? 0.4536 0.4700 0.4815 -0.0930 -0.0727 0.0593  375 HOH   B O   
7062 O  O   . HOH   H .   ? 0.2376 0.4620 0.4385 0.0117  -0.0463 -0.1074 376 HOH   B O   
7063 O  O   . HOH   H .   ? 0.4481 0.6750 0.5583 0.1555  0.0734  0.2694  377 HOH   B O   
7064 O  O   . HOH   H .   ? 0.7554 0.3920 0.5169 -0.1026 -0.0735 -0.0186 378 HOH   B O   
7065 O  O   . HOH   H .   ? 0.5276 0.7202 0.4397 -0.1343 0.0369  -0.1378 379 HOH   B O   
7066 O  O   . HOH   H .   ? 0.3354 0.4055 0.2105 0.0411  0.0325  -0.0077 380 HOH   B O   
7067 O  O   . HOH   H .   ? 0.3063 0.2459 0.3491 0.0180  0.0141  0.0508  381 HOH   B O   
7068 O  O   . HOH   H .   ? 0.3323 0.4308 0.5050 0.1043  -0.0196 0.0383  382 HOH   B O   
7069 O  O   . HOH   H .   ? 0.5563 0.6699 0.6431 0.0188  0.1735  0.1145  383 HOH   B O   
7070 O  O   . HOH   H .   ? 0.5012 0.8005 0.6032 0.0480  0.2401  0.0708  384 HOH   B O   
7071 O  O   . HOH   H .   ? 0.6461 0.4420 0.4646 0.1302  0.1076  -0.0593 385 HOH   B O   
7072 O  O   . HOH   H .   ? 0.2429 0.4114 0.4165 -0.0705 -0.0974 -0.0340 386 HOH   B O   
7073 O  O   . HOH   H .   ? 0.5747 0.4543 0.5317 -0.0730 0.0513  -0.0396 387 HOH   B O   
7074 O  O   . HOH   H .   ? 0.5598 0.4627 0.4078 0.0189  -0.1180 -0.0553 388 HOH   B O   
7075 O  O   . HOH   H .   ? 0.4869 0.3547 0.3157 0.0134  0.0445  -0.0138 389 HOH   B O   
7076 O  O   . HOH   H .   ? 0.7028 0.5974 0.4795 0.1460  -0.0238 0.0396  390 HOH   B O   
7077 O  O   . HOH   H .   ? 0.3691 0.2197 0.3353 0.0701  -0.0195 -0.0048 391 HOH   B O   
7078 O  O   . HOH   H .   ? 0.5176 0.3759 0.3934 0.0259  0.0342  0.0534  392 HOH   B O   
7079 O  O   . HOH   H .   ? 0.4012 0.2270 0.5305 -0.0336 0.0715  0.0610  393 HOH   B O   
7080 O  O   . HOH   H .   ? 0.2584 0.4009 0.6470 -0.1236 -0.0526 0.0058  394 HOH   B O   
7081 O  O   . HOH   H .   ? 0.4273 0.4198 0.4327 0.0263  0.0937  0.1036  395 HOH   B O   
7082 O  O   . HOH   H .   ? 0.4519 0.5732 0.3492 0.1471  -0.0051 -0.0845 396 HOH   B O   
7083 O  O   . HOH   H .   ? 0.2195 0.2886 0.5561 -0.0683 -0.1043 0.0480  397 HOH   B O   
7084 O  O   . HOH   H .   ? 0.3101 0.3676 0.4187 0.0449  0.0235  -0.0717 398 HOH   B O   
7085 O  O   . HOH   H .   ? 0.5340 0.4302 0.3040 -0.2246 -0.0498 0.1228  399 HOH   B O   
7086 O  O   . HOH   H .   ? 0.5699 0.6547 0.6926 0.1488  -0.1081 0.1561  400 HOH   B O   
7087 O  O   . HOH   H .   ? 0.5707 0.6410 0.3905 0.1764  -0.0322 -0.0212 401 HOH   B O   
# 
